LOCUS       WP_284331825             550 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase [Dyella
            flagellata].
ACCESSION   WP_284331825
VERSION     WP_284331825.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..550
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=60940
     Region          1..550
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 msldariliv dddensrfml rkrlkqlgfq hvteardgda gldqarrlpp dimlldvmmp
       61 gidgvtvlrm mrddeqlrdi svlmvsahdt lsmaaqciel gaedylakpv lmpllraria
      121 avlerrrlrn vehaflarfd eqtglpnraa lleriesamm sgrpltlvav tcnnhanial
      181 gmderqaaal lselashvrs cweqvdtiar vaenmlgwli pgvqadqqlv levqavlgmt
      241 ahasmhglta siatwpvagm ladatellrl amneaaridp lgeervtlad palrtrtraa
      301 laiheqleeg largelelyy qpifsvqadp rlvgaeallr wnhpqrgvla pgefleaieq
      361 tplmnridaw vmeqaianlv awdrelpsnf rlhvnatars lasgrlmeil tthlsepvrr
      421 hlalelterl yvsdmpscvs mlqslralgi hvalddfgtg fsslshvsll pcdtmkidrs
      481 fvsgvyaneq mrrllesmvs maqslgltvi vegvehdgel avlremgcpf vqgyllgapr
      541 peidflrhlh
//
LOCUS       WP_284331943             101 aa            linear   BCT 25-DEC-2024
DEFINITION  FmdB family zinc ribbon protein [Dyella flagellata].
ACCESSION   WP_284331943
VERSION     WP_284331943.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..101
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10533
     Region          1..73
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 mpiyefqcna cghrfdrlqk lsdpdpancp dcgqpqvqrq lsapqfrlag ggwyetdfkk
       61 dgdkkrnlag dggtaasspe pssspspapa papaptatst t
//
LOCUS       WP_284331858             701 aa            linear   BCT 25-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Dyella flagellata].
ACCESSION   WP_284331858
VERSION     WP_284331858.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Shan,L., Mathews,I.I. and Khosla,C.
  TITLE     Structural and mechanistic analysis of two prolyl endopeptidases:
            role of interdomain dynamics in catalysis and specificity
  JOURNAL   Proc Natl Acad Sci U S A 102 (10), 3599-3604 (2005)
   PUBMED   15738423
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Polgar,L.
  TITLE     The prolyl oligopeptidase family
  JOURNAL   Cell Mol Life Sci 59 (2), 349-362 (2002)
   PUBMED   11915948
REFERENCE   3  (residues 1 to 701)
  AUTHORS   Polgar,L.
  TITLE     A potential processing enzyme in prokaryotes: oligopeptidase B, a
            new type of serine peptidase
  JOURNAL   Proteins 28 (3), 375-379 (1997)
   PUBMED   9223183
REFERENCE   4  (residues 1 to 701)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 701)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..701
                     /product="prolyl oligopeptidase family serine peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=75319
     Region          25..697
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 msvllrclpa ltllaslaay agesvkppas ptrpdasslh gitvndpyrw lensqdpavq
       61 awikaqndht eavlaampdg kamtervrql aitsttrssp llaggtlfym qetppqpqpq
      121 lmaqawpdgk arvlvdlnas ggntaitgyw pspsgrylay gtaeggselt tlhvldvssg
      181 kslddalpya gggttpqdva wdadergfvy vrfpppaaga evkqfdaalv hhalgkaaag
      241 devvfghdys kvaeyrlrts pgakqlavla nigdggpaev ylragsqwkk vlgyeanvrn
      301 aawvgqrllv tsfadaprgk llaidaqgkv stllpqrega lqdvapiang flvtrswgpd
      361 wwaeqydwqg nfvrrlplpq hditvagiaa eqgrnhalvt yggwtlparw adydansgnl
      421 htvfevkpaa dygkvevrri dgvskdgtki pvtllamrgv vpngqrptil ysyggydipi
      481 tphfigpela wlerggvlaf anirggneyg qdwhaqgqml hkqnvfddfh aaalalfkah
      541 wsdrahlgil gasnggllmg aslvqhpqdy ravvamvgiy dvirhetnft ngaynvsefg
      601 tvsdpaqfka tlaysplqnv qphtaypavl mttgandprv apwqsrkfta alqdatasdq
      661 pillltrmna ghgigapfsq rvgdtaimlt ffaqelglpa r
//
LOCUS       WP_284332033             617 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF885 domain-containing protein [Dyella flagellata].
ACCESSION   WP_284332033
VERSION     WP_284332033.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..617
                     /product="DUF885 domain-containing protein"
                     /calculated_mol_wt=69033
     Region          28..606
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
ORIGIN      
        1 myvspcwgse kvrprfrklv qtvaraitlc glvtfslval paratpapps anskalqqll
       61 aaeweyqlke apetattigd yryndrwtdy spahaaaqrt vlqdfldrfq qlglsglseq
      121 eqlsqkmmir qlqdeltsir lknyempldq ingvhlqlae fvsavpfdst qhyqgylkrl
      181 halpnaidql iaasrlglad klvqpkylle kvatqadeia apagianvfg qpaahfptsm
      241 paaeqqrlrk aildavdqev rpayrklarf vandyaphgr tqegiwalpd gderyrfaih
      301 aqtttdlspa qihqigldev ariegqmlki arslgyqdla slraavaknp klyatsreqi
      361 ldryrgyiag mqpelpklfg rlpasklevv pteayreqna pfaeyrqgtp dgsrpgqvvv
      421 dtgdyakral ytiedtayhe gipghhlqia iaqtlplppf rqqaqynayv egwalyaerl
      481 agemgfyrdp ysryghlvee llradrlvld tgvhylhwnr qqmlaffrah paedeasiqa
      541 evdryvawpa qalgyklgql kflalraraq relgakfdlr afhdemlggg ampldlldar
      601 tdawiatakk tgmaaap
//
LOCUS       WP_284332038             373 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Dyella flagellata].
ACCESSION   WP_284332038
VERSION     WP_284332038.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..373
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40088
     Region          8..368
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mghwlgvksy dliivgagii gtacadyasr eglrvaiiep gpigggataa amghlvamdd
       61 dpaelalany slalwedftg ieqieysrcg tlwvasneae yahipakiar laavgvqaer
      121 idsdqlyrle palqrgltgg mrvpreavvy ppgmarhlln racargaaly pqrataitsh
      181 gvqledrtgl agsvlvatgc alpqllpqlp mrsrkghlvi tdrypgvihh qllelgyads
      241 ahgdadssva fnvqprptgq iligssreyg sdtsevsmsm vrrmlersfr ylpalrqlna
      301 lriwtgfrpv svdglpylgr vperpnvwva agheglgitt slgsarlvid qwlgrttain
      361 arpydparva twa
//
LOCUS       WP_284332073             330 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Dyella flagellata].
ACCESSION   WP_284332073
VERSION     WP_284332073.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..330
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35878
     Region          21..316
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mttetlapaa pmtvqiihar tqalrqqvah afigqgevfd qvlmallagg hvliegvpgl
       61 gktllvrala aamscsfgri qftpdlmptd vtghaiydvk aerfqirrgp vfanlllade
      121 inrapaktqa alleamqegq atiegrrfpl pkpfmvvatq npieqegtyp lpeaqldrfl
      181 ikvlinypsl edeksmvekv lsgkvaadld vsrvqqvmtq eellamqqgv ahmhmdpavt
      241 dyavriarat rewpavlgga gprgglalar larahaamdg rdfvtpddvr tvalpalrhr
      301 lmlapealve rqrpddvira llhkvaaprq
//
LOCUS       WP_284332125             285 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Dyella flagellata].
ACCESSION   WP_284332125
VERSION     WP_284332125.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..285
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31050
     Region          4..281
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mpdlpltvwi viagvlglil gsflnvvilr lpaqldafwr reahdvlgle apteslppgi
       61 vresshcphc khplaaydni plfgwlllrg rcrychapis iqyplvellt galsaiviwk
      121 fgptwaglag liltwalvtl sgidfrtqll pdqitlpllw vglllslmhl fveppasilg
      181 aaigylslws vywlfklltg kegmgfgdfk llaalgawmg pmallpvill ssligalvgg
      241 tlialrkhgr evpmpfgpfi amagwvwfva geqlwhaylg ltgmr
//
LOCUS       WP_284332180            1005 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Dyella
            flagellata].
ACCESSION   WP_284332180
VERSION     WP_284332180.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 1005)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 1005)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..1005
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=109233
     Region          55..904
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mfannmgcre atrgttapac rkkylalqlt mvlaglpfmg yanaqstsas ssdadqttak
       61 kpvslqavtv tgsnirsvdv enaqpvvtis sqeiqkqgfa tvgqllqnvs smsppdlsrs
      121 apgdlgpnqg gafidlrglg amrtlvlvdg qrigaahggy tninviptav vdhidilatg
      181 asavygsdai agvvniitkk nfngiqldty ngeymphsdg rqtqssvtlg kstdkfgvvl
      241 slsyqnqspv wandrpfsay pytsqhpyyg lssydsqpqi rnapasfagg grlvlnpggd
      301 pmnpadyhpf tlathgpdgd vvnpndqtyn pdadrrnmvl tadktknlyl dthykitdni
      361 tfkfnygyna dyeyaksntp lfysgmgang nfpsllsqys yynpvygvkd lsiaqritqd
      421 syrsynnpkn hrygfgvdgl fslgshefnw dvymydskis gvnvrtgyfn linvanglgp
      481 sflqngtvvc gtpdnvvagc vpinplatlt pqmlnyigin svehygseer awaadfggdl
      541 lelpggeltf stgvqhrdes gydspdsfay agystdggvg pnrggydlne ayaeinapll
      601 kdlpgaqsls ldvstryshy snfgsttnss fkltwkpind vlvrasygtg fraptvndly
      661 qgrypagtft dpcdavygps aygqstlvaq rclsgyggip gvpanfrqtd nngapitgps
      721 gsgympstnw tggnpklrpe tsyngdlglv yspswlpgfd atvdwwtyni rnlitgisnd
      781 qliadcyqys itsacgqfqr daatgqiinm lnletnagwm kesgydfsah yrfpetrfgn
      841 fklgmngtyl tafnmlptvg snivymagnt qnfysawrlr gnvsldwswh dfgaswtary
      901 fspykancaf dpslgvtafp ctlpnyyapg vgvmpqtqip svtfndvqvy wnapwnatis
      961 lgandifnrv spnvyggyss gdtpfdfnss ydlgrfvymr yqqrf
//
LOCUS       WP_284332207             185 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Dyella flagellata].
ACCESSION   WP_284332207
VERSION     WP_284332207.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..185
                     /product="YybH family protein"
                     /calculated_mol_wt=20294
     Region          70..172
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mmalqlkwmg gialvfvagm laghlldsft hamlptassm dntdangnad lsgidelhkl
       61 dvrvtlmnsa kalqqewadg avrilqdarv dvgkpaiyas dvqsiaaepg saivsyepdi
      121 rdvrvagdwa fewgyfdagf rqgkdkpiss mhgkllrvlr rengqwkffr vmvmwkedgk
      181 aeapq
//
LOCUS       WP_284332201             242 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor [Dyella
            flagellata].
ACCESSION   WP_284332201
VERSION     WP_284332201.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 242)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..242
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=27107
     Region          1..239
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 miaddeapar eklerwiaeq admavvgsae dglsaaqcie llrpqvafld vqmpalsglq
       61 vaaqlepssa plivfvtafd ehavkafdln aidyllkpyd qerfartvqr vrerlhahes
      121 gatavamgra rtpscerllv pdrerlqlid aasiewlead dnyvhvhtia rtyllrrtlq
      181 dllsqlgdqr fvrihkstav nlgsigsltp lfkgdyeihl hngrilrlsr ryrealfarm
      241 gl
//
LOCUS       WP_284332214             281 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfotransferase family protein [Dyella flagellata].
ACCESSION   WP_284332214
VERSION     WP_284332214.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..281
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=31701
     Region          16..216
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mpatpdasnp srkfhfisgl prsgttllaa ilnqnprfra gmtspladim gvvmaeassk
       61 ndfsfdvsde qrvallrglv enfysvqtda gvvfdtsrlw csrmqllntl fpgvkviacv
      121 rqlawvldsm erlvqrqpvs vskvfrfdtn ttvysrveal tdprgmvgfa yqatkdafyg
      181 qyaqkhllml tyeslvsdpv aamrsvyrfl depwfehdfd hieyhaeefd arvgmpglhs
      241 vrpkvasier qpvlpreifg rfaneafwmd pknnvnhvpi v
//
LOCUS       WP_284332218             301 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor [Dyella
            flagellata].
ACCESSION   WP_284332218
VERSION     WP_284332218.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..301
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=32607
     Region          <178..299
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mkqrhfdlla iagvfvaysi tirfalqadv rgsllggvan tipvvifgam vrriilrrli
       61 gkpaalqlla hlplcvafsa lsygllmvll gllfdgrgfs gflvkpfsis gtawqslenv
      121 ttyaliaamt ylqaqyrrhn mvpsapaeaa lvpeqlalag nlgmraapdy aavpvtpale
      181 eppkepddsr anadlsryfv rigdelrpid ldsvvsigga ddyaevrtls gkhlvrmtla
      241 eftksldpak yarvhrswiv nvhriaraep agggrlllhm etgqvistsr tgarllrdrv
      301 i
//
LOCUS       WP_284332243             358 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Dyella flagellata].
ACCESSION   WP_284332243
VERSION     WP_284332243.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..358
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=37434
     Region          13..342
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 maaspyspll grlgirlpiv qapmagvssp amaaavsncg glgslgvgam tapqarqaih
       61 qfrelsqgpl nvnvfvhrpa qahpqkesaw lqrldsqfgr anaqppanlr evytsflvdd
      121 dmlamlveek pqvvsfhfgv prpdqlaalh eagivllgsa tntqeakale tagvdaivaq
      181 gyeagghrgv fepddedsrl gtfaltrllv rtlgipviaa ggimdgagia avmklgavaa
      241 qlgtafiatd esladqafre rlfsdaahht vmtrvisgrp arslandfth wgatvpdnav
      301 pdypitydag kalnaagkaa gltgygaqwa gqgaplaral pthalmrele helelalh
//
LOCUS       WP_284332362             220 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Dyella flagellata].
ACCESSION   WP_284332362
VERSION     WP_284332362.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..220
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24299
     Region          5..207
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 msalrqlgtt qqrllrqllm aneggtvesl ceqlrishna vrqhlsalia rqyvertqsr
       61 psggrptacy rltesghalf prnygtiava llaqmheqlg dsatesmlre lghrlgsqev
      121 apppgtptke ivdglaqkld algyeataar hgeewqieaf ncvfhalakq ypqvckfdla
      181 ymeaaggrri hhmecivrgg hvcrfrlgal rrekggdeee
//
LOCUS       WP_284332387             543 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Dyella flagellata].
ACCESSION   WP_284332387
VERSION     WP_284332387.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..543
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=60006
     Region          141..>363
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mrsrllllga llgaglttav htyarqespa vsthrffhvq lgdkqtqpvs grlllfvepa
       61 aaakaesqdg kitqvdadpl hptqtsiaaq evdrlvpgqt vdidvdaqty peawsklpag
      121 dyvvqavldv hhnynylgrd agdlvsdvvp vhwpdagtap ikldatvpar dpwalpdsvp
      181 aplrnaakav heqaqpidfv spslsqfwgr dihmygyvll ppgynaasgk rfptvyfthg
      241 ftsnkdrmlr fmaymqagms sgqmppmiwv fldqssatgt hefadsvnng pwgqaltael
      301 ipyleskyhm dgnangrfln ghssggwatl wlqtrypkif ggtwstspdp sdfhdftgpd
      361 lyapqanvyh kpdgtpwplv rdkgkvlgtf qqfaqmervl gpyggqmasf dwvfsprgkd
      421 grpepmfdrd tgdvdpavva ywhdhydiay rlksnwpvlk pdldgkihly vgtadtfyld
      481 gaahrlkavl dglgahaefr fipdrthfdl yqvgddrfgl fkdiswamya varpqaapkp
      541 kln
//
LOCUS       WP_284332389             317 aa            linear   BCT 25-DEC-2024
DEFINITION  TolB family protein [Dyella flagellata].
ACCESSION   WP_284332389
VERSION     WP_284332389.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..317
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=34259
     Region          38..173
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 mirkplsrmv avglfsaacs sfaadvsvqq pqvfapgvis gpageacpaf tpdgntvyfd
       61 vgsmilvshr ehdvwtkpei asfsgqwgdh dpamapdgsy lvfvsnrpva gagkptpgfg
      121 hlwrvdrkgd gwgtpvhlpe tvnasdrtya psiaadgsly yihpdeqgvm hvyasafvhg
      181 tyqastrvav gdpaaathdp aiapdqsfmv fnmsdaakkg dmgdfyiafr qgdhwgkaid
      241 lgeaingkpg rwsqwgahig pdhrtlyyts drqtrlsfpl theqakaale rmeswdnggd
      301 niwyvslgpw ldaprar
//
LOCUS       WP_284332401             459 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Dyella
            flagellata].
ACCESSION   WP_284332401
VERSION     WP_284332401.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..459
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=50603
     Region          16..401
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msptssfvse prsrrrdthr liwrwhfyag lfclpfvlwl aitgtiylfk pqlepwlerh
       61 yanvthlpaq apsaqvaaal havpgsvlna yvlpesseaa trvllgrgse lirvfvdpst
      121 lqvlnvvgen drfmrvvfyl hgelllgrgg silvelaasw tilmllsgly lwwprnarla
      181 gvlyprlrhg srvfwrdlha vtglwislla lflllsglpw tttwggtlrs lrhalvantt
      241 ppdwttgsas eraqirlant psssehagmn mpgmamddps mavdyapidr lapvvaaqrl
      301 appvliapps qktphwtars dtdnrprrse lildentgav lqrttfmqkp lldriigygi
      361 aihegvlfap lnqvlgvfta lglitlcssa tvmwwrrrpa gvlgappatg sgyrhvligl
      421 lvllglllpl fglsmllvvl ieqgflqrsk raraflgls
//
LOCUS       WP_284332804             904 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Dyella flagellata].
ACCESSION   WP_284332804
VERSION     WP_284332804.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 904)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..904
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..904
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=98232
     Region          30..446
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          499..903
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mmsspfktla wslllglgla gasvparada paaskavand gnvlrttldn gmrvvivret
       61 lspmvttqit ylaggyqtpv glpgtahale hmmfrdsqgm tgaqlnemtg kmgadnnaft
      121 tndatqyyfv apsnyldlll hiestrmnga llnqpdwqre rgaieqevsr disqpeflaf
      181 qkaehilyag tgyaddplgt rpsfdkttaq dlqkfykdwy apnnallviv gdvdpqqtla
      241 kvqqlfgkir kgnvpahqpl klqpvkpeti asttpqgtga vqfmyrmpgm mekkdnaaaq
      301 vlldvltnar sslaqlavqg kvlstsaqmq pfsyggvgvl evafpkggna sqaqadldgv
      361 inellkngvp adlieaskqs eiaqaefnkn savtlasaws qaiawmglns peeaeeqirq
      421 vtvddvnria rqylkpderv tvvltpnpng qrppdsngfg gsesfnsnek ldaplpawaa
      481 qklsklempr wtlapvqmql dngirlivqp snisktvtvm ghvdnnpklq epagkegvar
      541 llgslfdygs ttldrnafhk alddisaten ggtdfgvaal sehfdramql ladnelhpal
      601 pqqgftvqqe tlaralagem qspqykmmka lragllpagd pdlrlptpdt igalslqdvk
      661 dyhaktyrpd lttivvvgdv tpelakatve ryfgtwkaqg tkpdviskpv tvnpagyavi
      721 dnsyasqdqv lmgqmldltm hnpdryalql gnnvlggngf asrlmtdirv khgyaygags
      781 gmhfdrsrsi ffvqygsdpd kvapvntlir qnlgqmqttp ikqdelenar qyeirsipvg
      841 vssissitrs lldwawhgep ldqpmvaakh yltltpaqvq aafkkylkpe nlmqvvqgpp
      901 pakh
//
LOCUS       WP_284332778             308 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Dyella flagellata].
ACCESSION   WP_284332778
VERSION     WP_284332778.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 308)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 308)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   7  (residues 1 to 308)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18827174
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..308
                     /product="ArsR/SmtB family transcription factor"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33755
     Region          6..76
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(11..12,16..18,31..33,42..45,47..48,51..52,54..55,
                     61..63,68..70)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Region          140..267
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mdlatassvl rlladptrvr llallereel tvaelaavlh laqprvsthl aklkeaelvr
       61 drragvsayy ransegderq halirslres iddallreda arlsavlaqr anehgwadtv
      121 agdmerhysp grtwetltrs llqlletgdv ldiasgdgvt aellaphara ivcvdaserv
      181 veaaakrlaa fgnvevrqgd mhalplqadr fdlvlmlhal tyseqpakav aeaarvlrpg
      241 grllavtlgk hdhravvepf dhrnlgfnes dlgqlatqak lqvlncnrls rerkaphfev
      301 isllarks
//
LOCUS       WP_284332875             478 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Dyella flagellata].
ACCESSION   WP_284332875
VERSION     WP_284332875.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..478
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=52399
     Region          214..440
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mnprfalagl cgllfgglls iaspgqfama matafvlpvi lrqpylglal faftatfmpy
       61 stvelgvrit lseallamac lgtlwqlcmh rlhwswgpte kavlllmvfs alpfavgqlt
      121 ihtddnglvn warwllnlst iflvplllad aerrerlivv llagslalll lslteflrhq
      181 stqdmisllt rmhyahtdav rsiftvehar latpwvhpnl tggalvlfvp lglsfalvre
      241 gwkrwlgsav allggvalll sssrgamlsl aavliwmacl rvpatrqill aaavigvvlv
      301 lfypplhari atmfsagnas tqvrmdeyrr fpeavarypl gigfkadppv pgsgllgisn
      361 lwlnyvyklg llgmlmycav iwrwwrecrp rgaidklgpa ngiwlgslag ivaalltglf
      421 dhyysftvvl valfwlmlgi nlqaarelyg vrraqrnpsl lpftarlpan etshlplh
//
LOCUS       WP_284332913             759 aa            linear   BCT 25-DEC-2024
DEFINITION  RCC1 domain-containing protein [Dyella flagellata].
ACCESSION   WP_284332913
VERSION     WP_284332913.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Hadjebi,O., Casas-Terradellas,E., Garcia-Gonzalo,F.R. and Rosa,J.L.
  TITLE     The RCC1 superfamily: from genes, to function, to disease
  JOURNAL   Biochim Biophys Acta 1783 (8), 1467-1479 (2008)
   PUBMED   18442486
REFERENCE   2  (residues 1 to 759)
  AUTHORS   Renault,L., Nassar,N., Vetter,I., Becker,J., Klebe,C., Roth,M. and
            Wittinghofer,A.
  TITLE     The 1.7 A crystal structure of the regulator of chromosome
            condensation (RCC1) reveals a seven-bladed propeller
  JOURNAL   Nature 392 (6671), 97-101 (1998)
   PUBMED   9510255
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..759
                     /product="RCC1 domain-containing protein"
                     /GO_function="GO:0003682 - chromatin binding [Evidence
                     IEA]"
                     /GO_function="GO:0005085 - guanyl-nucleotide exchange
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=80872
     Region          28..366
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
ORIGIN      
        1 mlavaacaah alprdsdnis qlvfsykhrc alrnngsvdc vsespylges rggdgeityr
       61 pvqmvprgat rltagefaic aivddaldcw kdvpatgkkl appqqiiash vtdiavgddh
      121 acavangaal cwgsdsagkv ghheddyhng tvqtkpwpvi asgvtrvaag gdvscavaqa
      181 alwcwgytgl asdanskalw dgdhpplrvf ergvttvaag shhvcaivsg tlwcwgdnth
      241 gqvgigisvd haqhspsfqt agvagtfmdg dqtchrqwtq ltctvehpvk vidhgvtavf
      301 asanetcaqa ngslqcwgan wqgqlgiapa kkdvlkatva iagevnfval dstrvcavmq
      361 ggvlsctlpc kkdvntcpdh pgfvaddpnd msgvemrggv wrgtignaev mvclqaeqpf
      421 sqssyyylrh gfsipldfad nsgailneas sngrefdysk ptavwtlqpa agrrmdgiwk
      481 tadgsrtlpi hlvrvmsldt gngascdstv pndpsrlafn aprvasqkls itqmpgglrr
      541 igaldghvsm telpasvpna dnfnhamraw laeeiagyyd calsnggsad fnesydisfl
      601 sppwlvares ysvycggahp sggtagysiw nletgktvdp wdflkdskwd yvkevdhcdn
      661 anncsrrppp klneiltarf nednagtgdc sdsldsgisp gyllhmdkng lifstdfphv
      721 iqacdedial pwktvapflt plgktvmqsl thkapqhgh
//
LOCUS       WP_284332936             226 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF2076 domain-containing protein [Dyella flagellata].
ACCESSION   WP_284332936
VERSION     WP_284332936.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007341
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..226
                     /product="DUF2076 domain-containing protein"
                     /calculated_mol_wt=23353
     Region          1..223
                     /region_name="COG3416"
                     /note="Uncharacterized conserved protein, DUF2076 domain
                     [Function unknown]"
                     /db_xref="CDD:442642"
ORIGIN      
        1 mtpqeqllld dflqrlaavt gvnkdaqada lihqrlanqp davyllvqrc llqqhaldaa
       61 kaqiaqlqsq magqqgggsf lggqpqqssw ganpppfpqq qaapaqaptw rerlfgssap
      121 aapapqqggg ssflanaatt aagvaggmfl fdgiesllgg hhgggmfggg fgggqpevie
      181 nvtennffdn gsnnnlpsgg dqdfasndfd danfdgnsvd ddnswt
//
LOCUS       WP_284332947             173 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Dyella flagellata].
ACCESSION   WP_284332947
VERSION     WP_284332947.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 173)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 173)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 173)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007114
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..173
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17789
     Region          <87..170
                     /region_name="CytC5"
                     /note="Cytochrome c5 [Energy production and conversion];
                     COG3245"
                     /db_xref="CDD:442476"
ORIGIN      
        1 msksdqsflr qfslliaglg vltlvlifta wtiyehepke tdpnaaqqls tslapngavy
       61 agntgraaml aaqeaaakaa aaqvayggst dgktiydnlc hschtagvag apvlgnkamw
      121 apriaegvdt lvkhaidgyh gpdgntmpak ggnpsltdaq vqaavkwivd qak
//
LOCUS       WP_284333166             287 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB family protein [Dyella flagellata].
ACCESSION   WP_284333166
VERSION     WP_284333166.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01352.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..287
                     /product="TonB family protein"
                     /GO_function="GO:0015291 - secondary active transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=30813
     Region          <130..262
                     /region_name="tolA_full"
                     /note="TolA protein; TIGR02794"
                     /db_xref="CDD:274303"
     Region          200..264
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mnavarrpgd nkigatfvfs llvhglllfg igvsyvatrp alptldvtlv nvanseapdk
       61 adflaqannk gggesdkaqr psqpysgllp lpsqgtaprp vtaatpspqq atdqrmlttt
      121 gqagfsvnsd sakdardtte aaadearlaq eaaqlaaevr qqsqayakrp hkkfisantk
      181 eyayaaymrg wvdriervgn lnypqqardq hlhgdviltv glnrdgsins idvtqssgys
      241 iidkaaiaiv klcapfpplp pdskekvdil yitrtwqfqp gdvlktr
//
LOCUS       WP_284333209             465 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Dyella flagellata].
ACCESSION   WP_284333209
VERSION     WP_284333209.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..465
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49561
     Region          121..454
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrfaryalss llvlvligsa fvaskrealh iaaasvsqsl caaafvsqvd pdrvfaqeqr
       61 pllgsiawaa sytvdrarqn vrsrvlglfq arseyraglg ctlvfgddpa pkavavdvhs
      121 vpdtfgpqvv tpvdpalraa lelafaepdp ahprltkavv vlhdghliae ryapgygpqt
      181 piwghsitks vmqaligilv rqgqlhpdqa apiaawaspt dprhaitvdq llrmdsglpf
      241 detegpvnpa thmwfreadt aayaarmpla hapgtawgys nlsyallskl vgeasggtaa
      301 daekfvrdel faplgmnhsv ietdvsgsll gsgfmygsar dfarfgqlyl ddgvvdgkri
      361 lpegwatyah sqtldtgyga gfwtnlvnqg svpvwdapwg mpqlpkdmfy argafgqyvi
      421 ivpsehlvvv rmglsvqggs tgigdatari iaalhrtgsa alair
//
LOCUS       WP_284333337             295 aa            linear   BCT 25-DEC-2024
DEFINITION  amidohydrolase family protein [Dyella flagellata].
ACCESSION   WP_284333337
VERSION     WP_284333337.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..295
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32959
     Region          3..277
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 miivdahqhy wqparadygw laqapatlqr aflprdlraq ratagvqysv lvqaapteae
       61 trylfelaqe dpavagvvgw vdmeasdvda ridalirdgr gllrglrpma qdladpdwla
      121 rpsldrafdc iqdcglsfda lvdmrqlpal lrrlrrhpql nvvldhagkp aigdgrfdqw
      181 tswidelsqh pllqcklsgl ltllgepvhe daiepyvadl fahfgpqrlm wgsdwplltt
      241 radyahwlhv amtlteryaq gsqaevfaan avrfyalnid lpnqgtshdl thdan
//
LOCUS       WP_284333474             288 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Dyella flagellata].
ACCESSION   WP_284333474
VERSION     WP_284333474.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..288
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32348
     Region          8..286
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mrdthvkela ellqlerled nlfrgqsrdi gtrfvfggqv lgqalsaaqq tvdpsreahs
       61 lhayflragd idapivysve rardggsfss rrvvaiqhgq pilngaisfq vperglehqs
      121 smpevpeped vepmhrvppd elarlpvklq rwlgsdgpfe frqvwprdel hpakrppiqh
      181 iwfrltapve espdlhrall ayasdfhlig tstlphgisy ltpnlqmasl dhalwfhrpf
      241 kvdewllysf dsptaqgarg largqifsrd grlvastaqe glirlrge
//
LOCUS       WP_284333478             498 aa            linear   BCT 25-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Dyella
            flagellata].
ACCESSION   WP_284333478
VERSION     WP_284333478.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     BTLCP proteins: a novel family of bacterial transglutaminase-like
            cysteine proteinases
  JOURNAL   Trends Biochem Sci 29 (8), 392-395 (2004)
   PUBMED   15288868
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..498
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=54354
     Region          277..444
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mrsriaplll vpmlclassl akaaedaapp dttwmtvlln grkigheeiq rertgdtvtt
       61 tqtlvmsier nhkmvpyinv srsvetaage pigfvmsstl satetrvegk rlpdgrlela
      121 nttggqtrqs vtawpagavl vegqrqamra aiahpgtdyr llmynqasql amdlsvtvig
      181 nervqlvdhv etlshqretl kgpqgiqsvd lwldargnir kgsvsllgkp ldmvacseac
      241 aeaptqslnm mdsalvdspr litpemssdf lsyrvhvadr aitrpfidtd eqsvvdlghg
      301 ewqinvyvge ldaqgpptpa dtqpnawlqs dapeikrlas laaggghdks himgnlnafv
      361 nryisqggld igyasaleva rdrrgdcaey avllaamara eniparvvvg mlyakrydsk
      421 qrvfvphawv tawvhgrwrs fdptierfdt ghialdisdg npwhfdraan efgsiridav
      481 qtfsellnsp pvsitvgw
//
LOCUS       WP_284333507             146 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Dyella flagellata].
ACCESSION   WP_284333507
VERSION     WP_284333507.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..146
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=15800
     Region          <53..126
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 msttrtwryy lggfalllvf dtivqlsfkl tgahafppaa stawvlrils qpwiylalig
       61 yvgnfftwmn llrhapigpa faashldvvs vmlasawlfh ealtpmrllg agvimlgiic
      121 laaaesrlpr eyaaeagnaf aiegsd
//
LOCUS       WP_284333510             162 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Dyella flagellata].
ACCESSION   WP_284333510
VERSION     WP_284333510.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 162)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 162)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..162
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18555
     Region          8..157
                     /region_name="NUDIX_MutT_Nudt1"
                     /note="MutT homolog-1 and similar proteins; cd18886"
                     /db_xref="CDD:467596"
ORIGIN      
        1 mpytpivatl gyvlspdrrk vlmihrnarp ddqhlgkyng lggkmepged iaacmrreir
       61 eeagiecesm hlrgtlnwpg fgkqgedwlg fifvidsfsg epgthnpegs lewieierim
      121 elpmwegdrh flplvfdrdp rpfhgvmpyk dgrmqswaft rl
//
LOCUS       WP_284333647             393 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Dyella flagellata].
ACCESSION   WP_284333647
VERSION     WP_284333647.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..393
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=43283
     Region          1..360
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 msahgkklaw iqalrgiaal mvvmvhdrga lageggagrt vanallpmam gvdlfflisg
       61 flmvlitrdf dgskayawaf takriariwp lyamvtllai gvdhpglhgl vdrsvllpyl
      121 egllfvphnp aashlyfqma vgvawtlcfe cyfylvfalc mlfgrwrygv magwfaltli
      181 aipvlrggyn lgvatqplva wsryanlavn pivwefvfgm lagwlylsrf tirynaviys
      241 svmlsmvvll lgwhrigmvn ffgpagwgap ltllffgavl lakkgglvap awcvwlgeis
      301 yslylvhvyv felvermavr iptssemiga vlfvarpiaa vmaawmvfry veapasarvr
      361 ecllriswgr hagkhsppwp dtessvrrvs ggp
//
LOCUS       WP_284333614             123 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Dyella flagellata].
ACCESSION   WP_284333614
VERSION     WP_284333614.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 123)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 123)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..123
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13372
     Region          16..104
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msilprtnas arsagtkfpq lrkavpvfaa lgdetrlrli vllctggals itqltagtei
       61 trqavtkhlk vladaglvrd lrsgrerlwe lessrleear rsldviagqw dqallrlkaa
      121 lek
//
LOCUS       WP_284333638             310 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Dyella flagellata].
ACCESSION   WP_284333638
VERSION     WP_284333638.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..310
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33992
     Region          36..270
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msimqtvlrs phfkvvshvc qrprvdcgtv iggeparfif trrgsfmlha gsrswfarpg
       61 qavlvakgve yhashpdaes cncctdvlis demldmlgvr tdpgqpcraf ghdlrfqkth
      121 vevlrgllrg gdaddaeevl ldtlgylies hesrapaadd ikvlrqvarv eaaivgraee
      181 nlgvdelakv agcspfhlcr ifractgqsl rqfrmqqrlg salgrlgdge rdlaalacdm
      241 gfnshshmtd afrlvlgmsp sevrddmrqs dlrvlrerlr dtlggsssrh vgvsknpfak
      301 skeialltpe
//
LOCUS       WP_284333649             383 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Dyella flagellata].
ACCESSION   WP_284333649
VERSION     WP_284333649.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..383
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41708
     Region          35..377
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrnttwigca lmlactatqs sttahsvrsd npihsaldra vdqaaqgyfr nschvglsvv
       61 vreggssyfy nygstsrskp qlptehsiye lasvtktfta tlaaqavsek rldldsdfqa
      121 ylpdrytnlt wqgkpitllt llthrsgmpr dipdtdaifa ennpatrpsh mlalfqgfgr
      181 dqflsalhdv klrsepstke aysnagflvi glgleqvygk pfetlvreri tqplgmtstg
      241 favtavdrak lvsgydrvgr smpyhpqnag aawglyaspq dmanylrlql dtrdpairvs
      301 hqplvgaagd geamawylgq dngqpmiwhg ggsfgmssqm vlyprqhqgf vllandtceg
      361 tesalkgiaq sihrqidsia psp
//
LOCUS       WP_284333656             701 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase [Dyella
            flagellata].
ACCESSION   WP_284333656
VERSION     WP_284333656.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 701)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 701)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..701
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=75843
     Region          8..686
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mpstynpllv vislmvatla sytaldlasr isllkpsasr hawlaggaaa mgvgiwsmhf
       61 igmlafslpi plgydpaitg cslliaifvs wfalnavtra rlgsreiaag gvlmglgiac
      121 mhytgmaalr mhpgidydpa lftasiaiai gastaalwia htlshvgqrh viskragaal
      181 vmgiaitgmh ytgmaaadfv pgsvcgaang vdarwlatsi tlftfailiv tlmlsrfdvr
      241 talltgsvtq lndqivrmah hdaltdlpnr ralvqrietv idsakraeqs failfmdidg
      301 fktindslgh sagdevlqaf srrlqqcvre gdtvarlggd efvilmenlv spddaqdaaq
      361 iildrmgrgh wsdeqpiqav psvgialfpr dgetadallk nadaamyeak ragratwrff
      421 easmhgaalr tlhiqnalrv alheegfslr fqpkycgstn elvgaealir ldhpelgmla
      481 paefiptaer sgqivqigqw vmretcrqir rwqtaglpav kvavnlsprq iaqadlvdtm
      541 irivrseqvs cdqiifeite avamqdapkt aemiqafqha gfeiaiddfg tgysslayle
      601 rfrvkqlkid rffthgldaq ghesraivsa iialahsldm evvaegvetp sqlselrvma
      661 cdqiqgyllg kpltaeafav lleqhrvres idakpcprpa a
//
LOCUS       WP_284333715             392 aa            linear   BCT 25-DEC-2024
DEFINITION  thiolase family protein [Dyella flagellata].
ACCESSION   WP_284333715
VERSION     WP_284333715.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 392)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..392
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40133
     Region          1..391
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 msdiviaaak rtaigsflgq ftgvpsptlg atairavleq sgiaakdvse vimgcvlpan
       61 lgqaparqaa lnaglppatg cttinkvcgs gmkaimlghd likagsasvv vaggmesmtn
      121 aphmvnargg irygegkmid hmawdgltnp ydgkamgvfg elcadkyhfs reeqdafaie
      181 svkrsqaaqa sgafadeiva vtvagrkgdv qvdtdeqpsr sdigkvptlk pafrkdngti
      241 taassssisd gaaalvllsa ddakargvkp larivahath sqepewftta pvgaiskvld
      301 kagwkvddvd lfevneafav vamapmrelg vahdklnvng gacalghpig asgarivvtl
      361 lnalktrglr rgvaalcigg geatalaver ld
//
LOCUS       WP_284333778             108 aa            linear   BCT 25-DEC-2024
DEFINITION  HesB/IscA family protein [Dyella flagellata].
ACCESSION   WP_284333778
VERSION     WP_284333778.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Lu,H.M., Li,J.D., Zhang,Y.D., Lu,X.L., Xu,C., Huang,Y. and
            Gribskov,M.
  TITLE     The Evolution History of Fe-S Cluster A-Type Assembly Protein
            Reveals Multiple Gene Duplication Events and Essential Protein
            Motifs
  JOURNAL   Genome Biol Evol 12 (3), 160-173 (2020)
   PUBMED   32108236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..108
                     /product="HesB/IscA family protein"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=11382
     Region          2..107
                     /region_name="IscA"
                     /note="Fe-S cluster assembly iron-binding protein IscA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0316"
                     /db_xref="CDD:440085"
ORIGIN      
        1 mtisitpsaq qrmrqflaqa psaagvrfgv krtgcsgfay vvdlaqqvge edqtfqiegv
       61 pvivdakslp lvegteidfq rqglnasfvf hnpnatgecg cgesftvg
//
LOCUS       WP_284333789             419 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Dyella flagellata].
ACCESSION   WP_284333789
VERSION     WP_284333789.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..419
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45210
     Region          5..416
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mnasrsdvli lgggviglac alhllkggar vrvleqgtpg cgsshgncgt itpshaapmt
       61 mpgtlgvalr sllradaply lnprldgprl rwlmgfarrc twrdferaaq araailqrsy
      121 rllaelvrse rldcefveeg llyvyrssaq maddehhhaq lldrlgiavq rlrggeveai
      181 epslkagvqg gmfhpgdarl rpdryaaela rlvrerggii etgakieria tdgkgivsva
      241 talgdftgdr vvlalgawsp llgkqlglrl pmqpgkgysl tytrpaqapr halvlreakv
      301 cvttwnsgfr lgstmefsgy aeginrtrid alrrgaaecl repegpqlqe ewwgwrpmsv
      361 deipiigpsa rwsnlhlatg hgmlgvsmsa atgelvaaqm lgaapaidpa pyapsrfhl
//
LOCUS       WP_284333898             428 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Dyella flagellata].
ACCESSION   WP_284333898
VERSION     WP_284333898.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 428)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 428)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..428
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=47356
     Region          117..426
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mqsrrklrfr llisfalfgf glsalfamas lyvrakvenq lvnaslqsdv nqavesthad
       61 pskpvgsrli dawmfsdrti yraplgwqnl asgvydmhdv dkdgrprhyk lavsrkysli
      121 gfisydisre dlgkrqlvas lvasvilfsl lslaigmwls rkvlkpvtel arrlrdfrkt
      181 graeplapyf addevgelal aldeystrlt amverdrefn sdvshelrtp lavissttel
      241 lqgspdltdk lrerlkrier asrqatelie allllsraer rgptrgeitd vakvaadvie
      301 sqrpqirdkp ieveltqsdp vtvnapasvl svaltnlign aikytlegrv tvqvekgrie
      361 vidtgpgikp edaerlfqrg vrgegaggsg aglglaivrr lcelygwdvs irprtdanga
      421 iasivfer
//
LOCUS       WP_284333922             331 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Dyella flagellata].
ACCESSION   WP_284333922
VERSION     WP_284333922.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..331
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36327
     Region          18..318
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mdmphapapg hlqtaffrlr delreqiigq prlidcllia lladghllve gapglaktta
       61 vkalatrida dfhrvqftpd llpadltgtd vfrpqsatfe fergplfhni vladeinrap
      121 akvqsallea maerqitvgr ntwrlpdlfm vmatqnpieq egtfalpeaq ldrfvmhvti
      181 gypdaaaela ilrlareqaa kpahapvala psvsqedvfv arqavlgvhv apaleqyltq
      241 lvlatrdagq ygpelkrwia wgaspratia ldrcarahaw lagrdfalpe dvhaiahevl
      301 rhrvllsyea eaegirsdkv inrlldlvpl p
//
LOCUS       WP_284334309             463 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Dyella flagellata].
ACCESSION   WP_284334309
VERSION     WP_284334309.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..463
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=50861
     Region          4..451
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mkpstpqvll addqpdvrea lrlllksegi asvgvadpaq aieavrrhef acalidcnys
       61 rdttsgeegl alleqlrqha pdlpvvamta wgnvaltvea mrrgaadfie kpwdntrlln
      121 vlrtqialge aarrerrlea enallrgnae ddfigesqam qrvlglvarv apsdanvlvl
      181 gengtgkgvi arrlhalsar atkpfvkvnm ggisetvfes emfghvrgay tdakserigr
      241 feladsgtlf ldevgnipas qqpkllrvle egeferlgss rtqsvdlrli satnadlhte
      301 vvegrfrkdl lyrlntleir lpplrervad ilplarrfla rnakrygrdg lrlassaera
      361 letwrwpgnv relqhlmera allaehdqvs asslsfgapp dggqdieglt leqaeawlvq
      421 ralerhngnl qhaadalgit rqalyrrldk halrdeagds gga
//
LOCUS       WP_284334435             631 aa            linear   BCT 25-DEC-2024
DEFINITION  polysaccharide biosynthesis protein [Dyella flagellata].
ACCESSION   WP_284334435
VERSION     WP_284334435.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 631)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 631)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18500220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..631
                     /product="polysaccharide biosynthesis protein"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=69861
     Region          127..244
                     /region_name="FlaA1"
                     /note="NDP-sugar epimerase, includes UDP-GlcNAc-inverting
                     4,6-dehydratase FlaA1 and capsular polysaccharide
                     biosynthesis protein EpsC [Cell wall/membrane/envelope
                     biogenesis, Posttranslational modification, protein
                     turnover, chaperones]; COG1086"
                     /db_xref="CDD:440703"
     Region          287..570
                     /region_name="Polysacc_synt_2"
                     /note="Polysaccharide biosynthesis protein; pfam02719"
                     /db_xref="CDD:426938"
     Site            order(291,293..296,316..317,343..345,366..368,370,385,408,
                     424,447..450,453..454)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(317,319,323,327,341..344,347,350,368..371,374,378,
                     381,384,454..455,460)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187548"
     Site            order(370,410..412,420,448..449,455..457,460..461,
                     472..474,478,480,515,542,545)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(386,410,420,424)
                     /site_type="active"
                     /db_xref="CDD:187548"
ORIGIN      
        1 mslrkwvgtv hpraavvlhd llitalawwv akelryaldp kliitfepye fpivlmvqgl
       61 vyawtglykg vwrfaslpdl wnilraaivg tvaigvalfl ygrldgvprs vlllypfvls
      121 lflgtprlay rfwkdsrvdl fmsaktqrvl ivgadsagea lardlhrdsr ymvvgfvddr
      181 rslrgaring kpvlgsleql pevakesavq mllialpgas arqmrqvvel cdrtglpyrt
      241 vpkledvvag raqfnqikev siedllgrda veldwtkire tltgrrvlvt ggggsigsel
      301 crqvarlgvh altivescey nlyqisqelr aaypelllns vlvdcgdava mrrlfaeskp
      361 qvvfhaaayk hvpmlqgqlr tavrnnvlat ravadlsset gvecfvlist dkavnptsvm
      421 gackriaeiw cqnlnahsnt hfitvrfgnv ldsagsvvpl frqqiqaggp vtvthpeisr
      481 yfmtipeatq lilqaaaigq ggeifaldmg epvkirdlae qmirlagkkp gteipivytg
      541 lrsgeklfee lfhplenysa tthnkiflaq hrpvswellq aqmvkateav rlfnedelrq
      601 cvssllpsfs wsdaaqagnv iplrrndige k
//
LOCUS       WP_284334443             429 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Dyella flagellata].
ACCESSION   WP_284334443
VERSION     WP_284334443.1
KEYWORDS    RefSeq.
SOURCE      Dyella flagellata
  ORGANISM  Dyella flagellata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Dyella flagellata"
                     /db_xref="taxon:1867833"
     Protein         1..429
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=48112
     Region          27..400
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mkqasvpsyy ratatpyepy aplqgraear vaiigggfag lntalglaer gvrdivvler
       61 eqvgfgasgr nggfvfggys lgeealhrqq gderakrifd lttaavqrir ervtrysmac
      121 dmvdqgviwa nwfrdpnvlr krqrllaeqy gvdwdwlpqe elrervrser yydglyerna
      181 lhlhplnyai glaaaavqqg vricensdvw rlrregghwl istpqgelqa ehvvlacggy
      241 laglrrqidr avlpiatyvm vteplgdrld eclqtraavy dtrfafdyyr plpdtrllwg
      301 grisirnrsa aavqrvltrd llrvfptlkg vridyawsgl msyarhqmpq vgtagdglww
      361 aqafgghgla ptcaagella aaiadgdegw rqfadyglar aykpfgllaa qasywwqefn
      421 dwfktsleg
//
LOCUS       WP_284334542             331 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Comamonas halotolerans].
ACCESSION   WP_284334542
VERSION     WP_284334542.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..331
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34479
     Region          22..329
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mnlkktsrwa vaaawavtil gsatpamala epfpekpvtf vvpfppggpt damartlgva
       61 ltqalgqsvi venragaggn igadavarak pdgytimfgt sgplainksi yskigydpak
      121 sfapiirvgy lpnvlvvhpn vkantvqeli aldkarpgsl nyassgngas shlagvlfnq
      181 eaqttfqhvp ykgtgpalnd llagqvdmsf tdiltampyv qsgklkmvgv atakrsqamp
      241 dvptiaeqgl pgydvsvffg vvapagtpte rinvlnqafr kalssekvrs tfasqglepa
      301 pdltpeglgr fipeevakwq avvhasgarl d
//
LOCUS       WP_284334634             101 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Comamonas
            halotolerans].
ACCESSION   WP_284334634
VERSION     WP_284334634.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..101
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11343
     Region          5..97
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msskenaain qlleklerry alrvlwalrd ghpqtfrllq dsvggitpnt lntrikelre
       61 eglmehgndg ytvtpsgqdl lkrlsdlqaf atrwaaarpk k
//
LOCUS       WP_284334641             353 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Comamonas halotolerans].
ACCESSION   WP_284334641
VERSION     WP_284334641.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..353
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35885
     Region          37..350
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mnalgqwfva grlkpqaali agvlllalal lwgsargaya ispgqlwrvl cdsllgsaqp
       61 gaehlvfmni rlprlllgav agaglglaga lmqglfrnpl adpgligvss gaalaaasai
      121 vlgpvvfpal aftlgswtla asafaggvlv tvliyslgqs qggtriglml lagiavnala
      181 gaglgflshv ssdeqlrnvq lwlmgslgha rwatvylvaa vvllcmglaq alarplnala
      241 lgesqaqllg vaverskrqa vvltalvvgt vtsatgvigf iglvaphwvr lvagpdhrvv
      301 lpcsallgaa lvlaadavsr tivqpaempl gvltaligvp lfllmlrqfr skl
//
LOCUS       WP_284334799             330 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Comamonas halotolerans].
ACCESSION   WP_284334799
VERSION     WP_284334799.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..330
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=35077
     Region          3..327
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mstlnrrqll afgisapvlg igslaqaqaa wpnkiiklmv afpaggptdt aarivgqkls
       61 erlgqqviie nkpgasgsia tasfikspad gynlsmfgmp sllaplmykn nlynvtkdfi
      121 pvatvydlpm aivinpqvlp gintlpelir hiqnsklpmd ftssgtgsfg hlameqlkdl
      181 gkfdlmhvpy rgsspavadl lggqigimfa dvvaalphiq agklkalals spkakamlpn
      241 vptiseqgfp nfdfdswggl iaplntpqai vdrlaqetks iissdkelqq kllnagaiaa
      301 fqdgkqmhar lvadyarwsh ivntkgisan
//
LOCUS       WP_284334982             237 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Escherichia coli].
ACCESSION   WP_284334982
VERSION     WP_284334982.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..237
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=26102
     Region          6..231
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 msakkkpltq eqledarrlk aiyekkknel glsqesvadk mgmgqsgvga lfnginalna
       61 ynaallakil nvsveefsps iareiyemye avsmqpslrs eyeypvfshl qagmfspelr
      121 tftkvdaerw vsttkkasds afwlevegns mtaptgskps fpdgmlilvd peqavepgdf
      181 ciarlggdef tfkklirdsg hvflqplnpq ypmipcnesc svvgkviasq wpeetfg
//
LOCUS       WP_284335116             471 aa            linear   BCT 25-DEC-2024
DEFINITION  cytochrome b [Comamonas halotolerans].
ACCESSION   WP_284335116
VERSION     WP_284335116.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Tolkatchev,D., Yu,L. and Yu,C.A.
  TITLE     Potential induced redox reactions in mitochondrial and bacterial
            cytochrome b-c1 complexes
  JOURNAL   J Biol Chem 271 (21), 12356-12363 (1996)
   PUBMED   8647838
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Howell,N.
  TITLE     Evolutionary conservation of protein regions in the protonmotive
            cytochrome b and their possible roles in redox catalysis
  JOURNAL   J Mol Evol 29 (2), 157-169 (1989)
   PUBMED   2509716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..471
                     /product="cytochrome b"
                     /GO_function="GO:0008121 - ubiquinol-cytochrome-c
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=52776
     Region          17..463
                     /region_name="QcrB/PetB"
                     /note="Cytochrome b subunit of the bc complex [Energy
                     production and conversion]; COG1290"
                     /db_xref="CDD:440901"
ORIGIN      
        1 mahefkdidp naptgakvtn wfenrfptaf saykvhmsey yapknfnfwy ifgslallvl
       61 viqivtgifl vmhykpdaek afasveyimr dvpwgwliry mhstgasaff vvvylhmfrg
      121 llygsyrkpr elvwifgcai flalmaeafm gyllpwgqms ywgaqvivnl faavpfvgpd
      181 lallirgdyv vgdatlnrff sfhviavplv llglvvahll alhdvgsnnp dgveikapna
      241 pkdangnpld gipfhpyytv hdifgvavfl flfsavvffa pefggyfley nnfipadplk
      301 tplhiapvwy ftpfysmlra itsemmyali acvvlaalfg vfksklaglf klvivgaaav
      361 vvalmmaida kfwgvvvmgg avvilfalpw ldmspvksir yrpswhkymy avfvvnflil
      421 gylgvqppsp igervsqvgt lfyfgffllm pwwsqlgtpk avpdrvtfkp h
//
LOCUS       WP_284335341             863 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Comamonas
            halotolerans].
ACCESSION   WP_284335341
VERSION     WP_284335341.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..863
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         <1..863
                     /product="beta strand repeat-containing protein"
     Region          <8..858
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 tvdttapsit lslavdtgtt gdgitsdgtv nvtglelgmg weystdgggs wvpgtgtsfe
       61 llagnypsgn vlvrqtdqag nqseialage vsvqtllaan daaeielggr vsqeqtpitn
      121 snlqviglld ngattngvpi tiaegstgdv vievsqdall svadafniei ydetgtriyv
      181 atagnnplvg dalgldilgv tgdgtvtasv tglapgdyti vvrkgesalg tlldadgngv
      241 sleelgeggv vlgaenqalv ltavetalng psspsglgtv vrgllegvlg ltteigagel
      301 vdvltsgldr lgltssldtv lgavadalln ntltliqsts vtvkvtengf anagepvqgn
      361 vidpdtttqg esgedsaipg stvtevensn gdsvaagqsi tglygtlvia adgsytytpn
      421 gdpaavgqte tfvytisdgt nssqanlvft idgsrvtndt aqagieydyv ttagpsvtda
      481 lsygwilgal giviptpgss ltgdsftvsa dtlqnvtlnv dvgglvglgv ggtlfvevnn
      541 ggvwstvksy dvgqligllg lggttsvvas dlaageyrtr vdlsipvgva gsisvdtvse
      601 ivhlnqfevs qvfpaegnll endilisgqt lqindagtyv dvvagtaqtv ngtygtltln
      661 adgsftyepl tagnltspvt dvfeyqlvnp ngqidqgqle vtvepsgagv isafsamamm
      721 psaseivgts gddvlygtaf ddiliggagd dvltgnggsd iyqweeinas afdggngmdt
      781 iedfmvgvvg tdanadvidl sqllgtvsep vgnyvdvtss ngdtvisidr dgsggaydfv
      841 qlatltgvtt dlesllanqq iiv
//
LOCUS       WP_284335455             118 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA recognition motif domain-containing protein [Comamonas
            halotolerans].
ACCESSION   WP_284335455
VERSION     WP_284335455.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Muto,Y. and Yokoyama,S.
  TITLE     Structural insight into RNA recognition motifs: versatile molecular
            Lego building blocks for biological systems
  JOURNAL   Wiley Interdiscip Rev RNA 3 (2), 229-246 (2012)
   PUBMED   22278943
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Clery,A., Blatter,M. and Allain,F.H.
  TITLE     RNA recognition motifs: boring? Not quite
  JOURNAL   Curr Opin Struct Biol 18 (3), 290-298 (2008)
   PUBMED   18515081
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Maris,C., Dominguez,C. and Allain,F.H.
  TITLE     The RNA recognition motif, a plastic RNA-binding platform to
            regulate post-transcriptional gene expression
  JOURNAL   FEBS J 272 (9), 2118-2131 (2005)
   PUBMED   15853797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..118
                     /product="RNA recognition motif domain-containing protein"
                     /GO_function="GO:0003729 - mRNA binding [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=12293
     Region          2..86
                     /region_name="RRM"
                     /note="RNA recognition motif (RRM) domain [Translation,
                     ribosomal structure and biogenesis]; COG0724"
                     /db_xref="CDD:440488"
ORIGIN      
        1 mttklyvgnl aysvrdndlq qqfssfgnvi saqvmmergs drskgfgfve mstadeaeaa
       61 iegmheqtmg grnltvniar preeggssyr snsggggyrg ngggyggngg gygggnry
//
LOCUS       WP_284335458             414 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Comamonas halotolerans].
ACCESSION   WP_284335458
VERSION     WP_284335458.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..414
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=46692
     Region          1..404
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mltdahcrna scppdrkqar ftdagglylq vspsgskrwf ykyrvdgkek qlalgsypsv
       61 gltaarkard aakvqraegs dpiaarklek lkgglerght fkavalewha kqtegwsagh
      121 aertlrqler dlfpwlgeqp mssiepmell svlqkveerg aletadralm larqvwrywl
      181 ptasntqrdi teglksrltp yrgknfaaiv epqrfgellr amhaykggpl vrtalllapl
      241 lyqrpgnlrm mewaeldlda glwtipskkm krskqekeng ephvvpmptq avellrdlqp
      301 itgqgryvfp gqrdhdrpls dnsvrsalyg lgfgteqswh gfrasartml vdqldldpla
      361 ieanlahavk dangrsynrt kylakrfdlv qqwadyldkl rrggdvielh qras
//
LOCUS       WP_284335472             198 aa            linear   BCT 25-DEC-2024
DEFINITION  IMPACT family protein [Comamonas halotolerans].
ACCESSION   WP_284335472
VERSION     WP_284335472.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Park,F., Gajiwala,K., Eroshkina,G., Furlong,E., He,D.,
            Batiyenko,Y., Romero,R., Christopher,J., Badger,J., Hendle,J.,
            Lin,J., Peat,T. and Buchanan,S.
  TITLE     Crystal structure of YIGZ, a conserved hypothetical protein from
            Escherichia coli k12 with a novel fold
  JOURNAL   Proteins 55 (3), 775-777 (2004)
   PUBMED   15103642
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Okamura,K., Hagiwara-Takeuchi,Y., Li,T., Vu,T.H., Hirai,M.,
            Hattori,M., Sakaki,Y., Hoffman,A.R. and Ito,T.
  TITLE     Comparative genome analysis of the mouse imprinted gene impact and
            its nonimprinted human homolog IMPACT: toward the structural basis
            for species-specific imprinting
  JOURNAL   Genome Res 10 (12), 1878-1889 (2000)
   PUBMED   11116084
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..198
                     /product="IMPACT family protein"
                     /calculated_mol_wt=21482
     Region          3..193
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 msqtiaspvh helvikksrf lccvqpmqdr asaqavvdtl wqehpgaahv cwallaggqs
       61 aavddgepsg tagrpmlevl rhqelegvla tvvryfggvk lgagglvray tdcvaqallk
      121 aekitlqrma tlqcrlpyam egwlrrelel agaallqvqh qasvqmqwsi seaqsaplva
      181 rineggqgri dwlkfwsd
//
LOCUS       WP_284335492             306 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Comamonas halotolerans].
ACCESSION   WP_284335492
VERSION     WP_284335492.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..306
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=33861
     Region          <2..291
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 malfpsdghd antlcnlaqd amaaakkagr nrcmyyerls flngkmegcl arelptaiaq
       61 eqlllhfqpk iclqdrtivg lealvrwqhp qqgliypgdf iaqaealghi qvlgdwvvqa
      121 ccrqiaawrl qgirivpiaf nvsplqlrdv dfprristwl qhygiqaqei eveitesclv
      181 dssgaaqqvl rqlqemgiri amddfgtgys slsqiralpi qtikldksfa kelcsnqkag
      241 vlvtsiitla hnlklqvvae gvekmdqfvf lktagcdvvq gyflsrplpa qcaresllkr
      301 tlepag
//
LOCUS       WP_284335800             450 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Comamonas
            halotolerans].
ACCESSION   WP_284335800
VERSION     WP_284335800.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..450
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47406
     Region          1..449
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mqqltewlqd lnglvwgvpm ivlilgtgfy lqlrlgfmpl rnigygfrmi wksrsvddka
       61 hgdispyaal mtalsatvgt gniagvatai avggpgavfw mwmtalvgma tkyaevvvav
      121 kyreknangq wvggpmyaik nglspkwrwl atafalfggl ggfgigamvq angissaieg
      181 afgletwitg lviaaltaav vlggikriga vaeklvpsmc vvyilcvlwv lasfyeqipa
      241 afalifeqaf nptaavggfa gstvlmairm gvargifsne aglgtagiaq aagkskdpvf
      301 sgivgmmgtf idtiivctmt glaivvsgvw nsgasgails tqsfeaampg igkyflavsl
      361 alfafttilg wayygekcwn ylvgpvcekp frilwvlgvf vgavvtldva wlvadtlnal
      421 maipnlisll llspviaklt kdyfeakkra
//
LOCUS       WP_284335840              66 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Comamonas
            halotolerans].
ACCESSION   WP_284335840
VERSION     WP_284335840.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 66)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..>66
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          17..64
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
ORIGIN      
        1 mrlrrhdpds raqlafrfka mylslgmdlp acakylhite rtlhnwlsgk hdipfatykl
       61 lrllny
//
LOCUS       WP_284335968             139 aa            linear   BCT 25-DEC-2024
DEFINITION  MerR family transcriptional regulator [Comamonas halotolerans].
ACCESSION   WP_284335968
VERSION     WP_284335968.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..139
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15876
     Region          11..131
                     /region_name="HTH_GnyR"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     regulatory protein GnyR; cd04776"
                     /db_xref="CDD:133403"
     Site            order(12..14,28,47..49)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133403"
     Site            order(60,63,67..68,77,98,102,108,112,115..116)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133403"
ORIGIN      
        1 mskttsapvs ysisdlaref dlttrairfy edmgllqptr kgtggrtrvy sardrtrlrl
       61 ilrgkrlgls lveakevidl ydsprdthvq ltrflevlgk hrqqmeerme dlqatleevr
      121 aqekeartll rkigkakaa
//
LOCUS       WP_284335993             558 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Comamonas
            halotolerans].
ACCESSION   WP_284335993
VERSION     WP_284335993.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..558
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=61168
     Region          9..414
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mrvdgkpegl rqsmswlhtw sglllgwlly avfftgtlsy fvdevsdwmr pelhvsvpqa
       61 dtaekamagm qklapdassw slhlpnerqt aveatwrpqg appgregmqr ayldaatgev
      121 lpvretrggs flyrfhfely amprvwgrwi vgiatlvmfv ailsgiithk kifkdfftfr
      181 prkgqrswld ahnatavlal pfhivitfsg llllmtmlmp wganavyegq pqrfnaerrg
      241 mqmvsapqaa arapregrge ragyedaapm aeiapmfaqa qaqlkgaavg siivqnpntr
      301 ramvelraeg adsltsgrga gqrvqfdgit gamkeapsvr epsstvavmn slvsvhlgrf
      361 adpavrwllf lsgvvgtvmv atgmvlwvvk rlpernklgf ipkghrlvev lnvaaiagls
      421 vavvgyfwan rllpvglsdr saaeihvfft lwllsllhal vrpharawle qmvvaamafv
      481 clpllnvwtg gagllqtmth sqwsvagfdg mmlalavvhg svayklwqrl rqpavpaarv
      541 rqgvaasrta lqapkehl
//
LOCUS       WP_284336159             399 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Comamonas halotolerans].
ACCESSION   WP_284336159
VERSION     WP_284336159.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..399
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42944
     Region          4..394
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mavserprpl dgitvvsleh avaapfctrq ladlgarvik verpgsgdfa rgydqrvngq
       61 sshftwinrs keslaldvkq pqakaallel lktadvlvqn lapgaaarmg lsyealkdsn
      121 pklivcdisg ygadgpyrdk kaydlliqse agflsvtgtp dtpsksgisv adiaagmyay
      181 tnimsalllr aktgqgshid vsmleamsew mgyplyyafd gapppprtga shasiypygp
      241 fragdgktvm lglqnerewk ifcdavlqqp dvatdarfds narrnanrea lqalitqtfa
      301 altasqvvqr leeagianar vnemadlwah pqlqarqrwr tvetpkgevp allppgvnsa
      361 fdyrmeavps vgqhnasila slgwseaqiq alqspatst
//
LOCUS       WP_284336211             303 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Comamonas halotolerans].
ACCESSION   WP_284336211
VERSION     WP_284336211.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 303)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 303)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14398448
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..303
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33492
     Region          42..146
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          218..295
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mnkidalpva aagtnphrna rtlaqiplld phlyrphaqr pvrskmreld kdtlimphth
       61 vwaqlvlstg gvvklslada tyiipphrav wvppgiphat tmvetarlyt vyflpeahgg
      121 gpqarwmdda awqecrvmea sallralvve mdassdhapp lsteqlerev hlsalvshei
      181 rhapviqlgv rlpqdkrlkh lceavlqdpt rhetleqwal dtgaslrtva rlfrqelgct
      241 ftqwrqqvvl akavtmaarr lpiayiaael gytpsafsal vrrtvgmtaa tflgqqhnas
      301 ttt
//
LOCUS       WP_284336265             186 aa            linear   BCT 25-DEC-2024
DEFINITION  KdsC family phosphatase [Comamonas halotolerans].
ACCESSION   WP_284336265
VERSION     WP_284336265.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..186
                     /product="KdsC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=20216
     Region          16..184
                     /region_name="KdsC"
                     /note="3-deoxy-D-manno-octulosonate 8-phosphate
                     phosphatase KdsC and related HAD superfamily phosphatases
                     [Cell wall/membrane/envelope biogenesis, General function
                     prediction only]; COG1778"
                     /db_xref="CDD:441384"
ORIGIN      
        1 mpkpytspam yyepelllka qsirvvffdv dgvltdgglh fteqgetikr fntldghgik
       61 llqkadiapa vvtgrdsapl rlrlaqlgvq hvvygtedkv paaqrilnsl glnwnqaamm
      121 gddwpdlpvm rrcalacapi nahpenlaia dfvttvaggq gavrqlcdll lvasgryrgm
      181 letyqq
//
LOCUS       WP_284336268             114 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA recognition motif domain-containing protein [Comamonas
            halotolerans].
ACCESSION   WP_284336268
VERSION     WP_284336268.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Muto,Y. and Yokoyama,S.
  TITLE     Structural insight into RNA recognition motifs: versatile molecular
            Lego building blocks for biological systems
  JOURNAL   Wiley Interdiscip Rev RNA 3 (2), 229-246 (2012)
   PUBMED   22278943
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Clery,A., Blatter,M. and Allain,F.H.
  TITLE     RNA recognition motifs: boring? Not quite
  JOURNAL   Curr Opin Struct Biol 18 (3), 290-298 (2008)
   PUBMED   18515081
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Maris,C., Dominguez,C. and Allain,F.H.
  TITLE     The RNA recognition motif, a plastic RNA-binding platform to
            regulate post-transcriptional gene expression
  JOURNAL   FEBS J 272 (9), 2118-2131 (2005)
   PUBMED   15853797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..114
                     /product="RNA recognition motif domain-containing protein"
                     /GO_function="GO:0003729 - mRNA binding [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=11782
     Region          2..86
                     /region_name="RRM"
                     /note="RNA recognition motif (RRM) domain [Translation,
                     ribosomal structure and biogenesis]; COG0724"
                     /db_xref="CDD:440488"
ORIGIN      
        1 mgnklyvgnl pyafrdndle qafsefgavq sakvmmerdt grskgfgfve mgsdaeaqaa
       61 iqglhgqnyg grdlvvnear pmeprpprsg gfgggrgngg gfggggfggg rnsy
//
LOCUS       WP_284336337             322 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Comamonas halotolerans].
ACCESSION   WP_284336337
VERSION     WP_284336337.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..322
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33695
     Region          1..319
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mqrrhflsav aaaaavsvsg mtmaqdtrpl rivvpfpagg stdmvprnmq dvlgkllgqp
       61 viienkagag gsigmaevar sndgltfgia tlsthgvnpa vytklpynai edfvgvteiv
      121 kapgvivinp klipaknfae lvaylkanpg kvsyatpgng tighmwgaqf ikstgvdmlh
      181 ipyrgagpai ndvlggqvpv yfdqvasslp hikggklrai avswserldv lpdvptykev
      241 ghpelndpsw fglvapkstp aetvarvqka vaealkdpav kkrmdaqgmy vsgtssadft
      301 qqiasevakm ktvaasanis vn
//
LOCUS       WP_284336353             499 aa            linear   BCT 25-DEC-2024
DEFINITION  rhomboid family protein [Comamonas halotolerans].
ACCESSION   WP_284336353
VERSION     WP_284336353.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Koonin,E.V., Makarova,K.S., Rogozin,I.B., Davidovic,L.,
            Letellier,M.C. and Pellegrini,L.
  TITLE     The rhomboids: a nearly ubiquitous family of intramembrane serine
            proteases that probably evolved by multiple ancient horizontal gene
            transfers
  JOURNAL   Genome Biol 4 (3), R19 (2003)
   PUBMED   12620104
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10483871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..499
                     /product="rhomboid family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=56605
     Region          138..307
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
     Region          273..>488
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
ORIGIN      
        1 mflaiplenk pswssppwmt vllivincvi fwgwqtpdee sverasqhya qtvlptielp
       61 lflehlqkqs ahahvrkrns meaikelyeh kaydllytlm wqervfresl leglvittsh
      121 pdyaqwqear aaftplelse sfterwsiny aptaglqpvq aftstflhgs tghllgnmvf
      181 lflfgftlei algsftylaf yvlggtaasl falmfyagmg gyglgasgai salmamyavm
      241 yrmrrirffy mllfyfnyat wpalimlpvw mgvellqhll gdkqvaymah fggllagall
      301 mwaymrlhvv qapisaqala ktsrhqlada varaqrytda lefdraalaw rkaahlapsd
      361 pdtlrawfes arhhpdredf haaarrifkl pattdserql qlssyrtyrq rarpgmrmsa
      421 etmhglarnf vrigalpeae tlcqslcklt dhpqlpdtli llvngmvrag rvqeakswlp
      481 tlqqlapket ttqwlaqqd
//
LOCUS       WP_284336441             328 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Comamonas halotolerans].
ACCESSION   WP_284336441
VERSION     WP_284336441.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..328
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34716
     Region          28..324
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mksvynrgrr avlgalaaaa cavlggnawa gsdwpqktvk vlvpytaggp vdtvtrvlme
       61 nvakslgqti iienrpgant qvatgqlars padgytfgii paayttnqvl akklpykpgd
      121 fvavshmvni plflfasasn pannvaefve warkekpsya stgpgstghl lgamfamnak
      181 fegthvgyng saqvmpdlms glvayifdpa tggmphvkag klkvlgvslp qrctcapdvp
      241 tmaesgypem vqgswlglma pkgtpqpvvq rmsdeiakam rnpdftrrle tmgfdavgsk
      301 paefqslidq dikayesiar kanisldh
//
LOCUS       WP_284336486            1108 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl-CoA carboxylase family protein [Comamonas halotolerans].
ACCESSION   WP_284336486
VERSION     WP_284336486.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 1108)
  AUTHORS   Wang,Y., Yu,W., Li,S., Guo,D., He,J. and Wang,Y.
  TITLE     Acetyl-CoA Carboxylases and Diseases
  JOURNAL   Front Oncol 12, 836058 (2022)
   PUBMED   35359351
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1108)
  AUTHORS   Brownsey,R.W., Boone,A.N., Elliott,J.E., Kulpa,J.E. and Lee,W.M.
  TITLE     Regulation of acetyl-CoA carboxylase
  JOURNAL   Biochem Soc Trans 34 (Pt 2), 223-227 (2006)
   PUBMED   16545081
REFERENCE   3  (residues 1 to 1108)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
REFERENCE   4  (residues 1 to 1108)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20212453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1108
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..1108
                     /product="acetyl-CoA carboxylase family protein"
                     /EC_number="6.3.4.14"
                     /EC_number="6.4.1.2"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=118461
     Region          4..463
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          510..572
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(529,538..540,547)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            539
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
     Region          594..1091
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mklfqkilva nrgeiavrii raardlgigc vaiyssddaq slhrvladea vslngtgpaa
       61 yldtaviiaa aqslqcdaih pgygflsera dfakacqdag irfvgptveq lalfgdkgsa
      121 lilarecgvp vmpatrggat qeevagffaa qgdagivika vgggggrgmr vvksqaeipe
      181 lyarcrseak safgldsvya erlvsrarhi evqiagdghh vvalgerdct lqrrfqkvve
      241 iapspilpah mresilraaq rmaekvayqg lgtfeflvee nedgllqnfv fieanprlqv
      301 ehtiteqvtg vdlvtlqirl asghslqqag idpqnpprvk gcaiqvrima estdasglar
      361 pahgtlerfv ppsgpdvrid thaysgyapa pafdtllakl ivssndskfs tvvqrlrrsl
      421 aefrivgvas nlhllqalvq redfaqqknh trylesilae lieqaqvlaq qqaqkaaiie
      481 gatpiqavaq vqprqpracl eenrvgsyvp lsgrvvevav tvgdtvqkgq siavidamkm
      541 ehsiaadchg qvvevraveg ayvtegdilv viepgdglaa tqsqavaidl dfvrpdlqav
      601 ldrhaflydd arpeavakrr srgqrtaren ladlcdensf vefgalviaa qasrrskedl
      661 iantpadgii tglgningte fgyerslsav maydatvlag tqgkrnhikt drlveraknd
      721 elpfimfaeg gggrpgdvdf pfisglyqps faalaelsge vpllgivsgr cfagnaaflg
      781 vcdviiadks anigmagpam ieggglgiyq peevgpasvq ysngvidilv eneaeavlta
      841 khylsmfqgt vrewvapnpl alrhivpenr lrvydsrqvi egiadtgsvl mlragfgngi
      901 htalarvegq pvgiiannpl hlggaidata adkaarfmkl cdihglpiis lidtpgfmvg
      961 peeeakaqvr hvsrmfltaa klrvailaia lrkgyglgam amaggsfrsa sctvswptge
     1021 fgpmglegsi qlgfkkelas vpegperqal ydqlvaraye rghainvast aeidavidpa
     1081 etrtwirqgi asarrrgsrp rrsfvdaw
//
LOCUS       WP_284336589             116 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Comamonas halotolerans].
ACCESSION   WP_284336589
VERSION     WP_284336589.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 116)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 116)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 116)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..116
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12123
     Region          4..91
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mnedqvikal aalahsvrls vfralvvaga egrtpsalse qlgvpstals fhlkelvnag
       61 lvcqervsrn lfyraaydem naligylten ccagadcgqt gavchpkaik sttkgs
//
LOCUS       WP_284336596             195 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Comamonas halotolerans].
ACCESSION   WP_284336596
VERSION     WP_284336596.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..195
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21772
     Region          20..124
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mqidfdapyl etdpwgyrnr wyeqrrrnli aavlpqydlg svlevgcang liaqqladra
       61 kdwlgvdvss kavelanqtl agnphikvrq aniaqhwpsg kfdtylicdv gyylspqale
      121 fmahniassa hsstvmlaah wrhpfdqvvt ptqqvhqilg hasclqplar ytdedlllev
      181 wtgngqsiar tegfi
//
LOCUS       WP_284336605             305 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Comamonas halotolerans].
ACCESSION   WP_284336605
VERSION     WP_284336605.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 305)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..305
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33179
     Region          1..281
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mnlhkirsll nqlntvvvgk kqqvqdcvtc llagghllie dvpgvgkttl ahalahgfgl
       61 kfsrvqftsd lmpsdltgvs vydrssesfv fhpgpvfaqv lladeinras pktqsallea
      121 meekqvsieg hthklpdpff viatqnpheq lgtyplpesq ldrflmrisl gypdrtaelq
      181 llrhhghriq aealsaqitp qelaalqqav lnihaadpll hyvqdlleas rngqwfvqgl
      241 spragialir aakanalvhg rdyvapddvq aifvptmahr lhavagagrg tveqtramlq
      301 avaip
//
LOCUS       WP_284336768             425 aa            linear   BCT 25-DEC-2024
DEFINITION  M20 family metallopeptidase [Comamonas halotolerans].
ACCESSION   WP_284336768
VERSION     WP_284336768.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Turner,A.J.
  TITLE     Exploring the structure and function of zinc metallopeptidases: old
            enzymes and new discoveries
  JOURNAL   Biochem Soc Trans 31 (Pt 3), 723-727 (2003)
   PUBMED   12773192
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10119591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..425
                     /product="M20 family metallopeptidase"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45963
     Region          19..422
                     /region_name="M20_like"
                     /note="M20 Zn-peptidases include exopeptidases; cd02697"
                     /db_xref="CDD:349869"
ORIGIN      
        1 mnqdrqatya aldawidqhf deqvqflqal vqvptdtppg nnaphaerta dliqafgfaa
       61 ekhvvpeqev kdygmqsitn livrrqygaq gdggktialn ahgdvvppge gwskdpygae
      121 iedgkmygra tavsksdfst ftyavralea vakptkgsie lhftydeefg gelgpgwllk
      181 qgltkpdlmv aagfsyevvt ahngclqmev tvhgkmahaa vphtgvdalq aavaimsgly
      241 aenvkyqkvl skvpgikhpy vnigrieggt ntnvipgkvv lkldrrmipe enpaeveasi
      301 raviataves fnaergykgd davrvdikrl llanamtpla gnqplvdaiq thgelifgek
      361 paavgtplyt dvrlyvergi pgviygagpr svleshakrs derleledlr ratkvvarsl
      421 adwma
//
LOCUS       WP_284336780             324 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Comamonas halotolerans].
ACCESSION   WP_284336780
VERSION     WP_284336780.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..324
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34149
     Region          18..322
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mlrrtvlaat atlavtaglp glaqakdawp tktitlvqpy apggtsdmla rivalelekr
       61 idasvivesk pgangniata fvsrakpdgg tflvgssspv vispslyksv pynpktdltp
      121 ittiakapfl lvtgatsgin svdelvkqik adklnfgsag agspqhmiae mfhmqvkaks
      181 phipykgsap liialmanev qygidnpvpl kpqidggklk alaitskhas pkfpgvkslh
      241 elgytdfeve pwygmigskg lpkelaermn qyvrdilaqd nvkkkisdlg aeayglstae
      301 ftslidadik kwgeavkvsg atad
//
LOCUS       WP_284336796             326 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Comamonas halotolerans].
ACCESSION   WP_284336796
VERSION     WP_284336796.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..326
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33995
     Region          1..323
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mkkrtliqaa vmavtsltlg gnalaqefpp kkpitmvvgf apggaadaaa rtiaktlgen
       61 igqsvivenr ggaggniahg qvangpadgs milfgsigpl aiaphlmkln ydplkslapl
      121 sggvnfpnll vvhkgagikn lkefvakaka epnkldfast gagsashlag ellnqragiq
      181 tvhvpykggg pamqdllger vtsyfaappt ampqveagrl ipiattgltr paympniptv
      241 aeagypgfea lnwyafvapg ktptaildrw nteivkalkd psvnkmltey gltpqpttrq
      301 eladfikkey dqwgkvvkeg nlqggn
//
LOCUS       WP_284336797             369 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Comamonas halotolerans].
ACCESSION   WP_284336797
VERSION     WP_284336797.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..369
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=42466
     Region          9..349
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 maasvfklry npaldglrgv aiilvilsha haplfngaff gvdlffvlsg flitslllqe
       61 fqtngqldyw rfyrrrffrl mpplalflat yclvaphiwp elddiysdal vsllyladyg
      121 iaffdspdtl lhmwslsvee hfyliwppll vwllrkvtpg rvwapllglw vlstlwralw
      181 vfqeqefyev ffrfdtrasg llagallaal mvekpqwier lqslrsytmw lvlavpllme
      241 lewsnmhall wgitvvecat ivlllavqsp kglvyemlta ptllrlgkls ygiylwhypv
      301 vrylradysw pvavagtlvi saalsalsfy tierwamryr dgrapaakaq rpqrerqeph
      361 lqqasnhsf
//
LOCUS       WP_284336798             640 aa            linear   BCT 25-DEC-2024
DEFINITION  B12-binding domain-containing radical SAM protein [Comamonas
            halotolerans].
ACCESSION   WP_284336798
VERSION     WP_284336798.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   2  (residues 1 to 640)
  AUTHORS   Banerjee,R. and Ragsdale,S.W.
  TITLE     The many faces of vitamin B12: catalysis by cobalamin-dependent
            enzymes
  JOURNAL   Annu Rev Biochem 72, 209-247 (2003)
   PUBMED   14527323
REFERENCE   3  (residues 1 to 640)
  AUTHORS   Ludwig,M.L. and Matthews,R.G.
  TITLE     Structure-based perspectives on B12-dependent enzymes
  JOURNAL   Annu Rev Biochem 66, 269-313 (1997)
   PUBMED   9242908
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..640
                     /product="B12-binding domain-containing radical SAM
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0031419 - cobalamin binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=71090
     Region          205..564
                     /region_name="YgiQ"
                     /note="Radical SAM superfamily enzyme YgiQ, UPF0313 family
                     [General function prediction only]; COG1032"
                     /db_xref="CDD:440655"
ORIGIN      
        1 mtapaprvls lippmtqlnt pypsapyltg flrtrgidav qedlalalvl kllsreglaq
       61 iielvqaqfd adpdrlfspa vqsfmgqrdr ylatvnrvia flqgkdstls hrivsrtwlp
      121 egprfdaleh ymddgsgdpv gwafgalgqq drakhyatly lndladvird aadarfefvr
      181 yaeslsgnqp tfdplaqala aaptlvdeal aeltrkaiwr hrptvvllst pfpgsvyaaf
      241 riaqtikaef pyiklvlggg fvntelrdla eprvfdyfdf vtldagerpl lallehlrge
      301 rgrsrlvrtf vrndegavqy inmmesdiaf aevgtptwdg lpihdylsll dmlnpmhrmw
      361 sdgrwnklti ahgcywkkcs fcdvsldyig ryegasatel anridaivae tgqtgfhfvd
      421 eaappkalka lskeliergt eiswwgnirf ektfspelae lmaesgciav sgglevasdr
      481 llnlmkkgvs veqvarvtka ltdagilvha ylmygfptqt vqdtvdaley vrqlfengci
      541 qsgffhrfac tvhspvgqnp aeygvtlpem pkatfarndi pfidptgvdh dklgvalkka
      601 iynfmhgvgv eedvrnwfdf kvpkptvprn kiakalaakh
//
LOCUS       WP_284336903             217 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Comamonas halotolerans].
ACCESSION   WP_284336903
VERSION     WP_284336903.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 217)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 217)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..217
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23377
     Region          11..105
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          122..206
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mikawtsvfa mfvacatssa faqtlqgdlk agegkvamci gchgisgyqa sfpevhkvpm
       61 isgqsaayit aaldayrkgd rrhptmrava eslsdqdiad lsayydahnp arkelqphdp
      121 paqvaaliek gacfschgqn fgkpidasyp kvagqhadyl fvalksykti enakigrsng
      181 imapiaqqfs nqelrllany iskldgdlkt ipqahfr
//
LOCUS       WP_284336904             280 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Comamonas halotolerans].
ACCESSION   WP_284336904
VERSION     WP_284336904.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 280)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..280
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31939
     Region          2..262
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mkfqgsdnyv atqdlmlavn aaiklqrpll vkgepgtgkt mlaeevaaal dmpllqwhik
       61 sttkaqqgly eydavsrlrd sqlgdertkn ienyivkgvl wqaftadrpv allideidka
      121 diefpndllr eidrmefycy etremvhakh rplvfitsnn ekelpdaflr rcffhyikfp
      181 dadtmrqiva vhfptlkgdl lsaalktfyd vrnlpglkkk pstselidwl kllvaedipl
      241 ealqspdqkv svpplvgall kneqdmslfe klvfmnqrnr
//
LOCUS       WP_284336929             329 aa            linear   BCT 25-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Comamonas halotolerans].
ACCESSION   WP_284336929
VERSION     WP_284336929.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..329
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36300
     Region          26..305
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mnapltlspr qlllqrlqda qaatphisit pqsahigali agvdlrqals aqevhtirsa
       61 llqwkvvffr dqhlsheqhv afsrqfgelt ighpvfghvd gypqlysiak hrranshgge
      121 perrpwtgwh tdvtaavnpp agsilrgvti ppyggdtqwt nlvaayeals eplkaflqtl
      181 rgehrfspps gsdasaeyle likkntlvse hplitrhpet gekvlfispg flktisglrt
      241 resrvllell wehavrsdft vrfkwepgsi afwdnratah vapqdifale fdrqlyrstl
      301 vgsipvgadg rdsialqgdp vlaahsaaf
//
LOCUS       WP_284336948             269 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Comamonas
            halotolerans].
ACCESSION   WP_284336948
VERSION     WP_284336948.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..269
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29975
     Region          35..247
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mglmagswra irrftqmlwh aikgvhlarn gfnqldaqaq qraverware fleaagialr
       61 iegqpvahgp vllvanhqsw ldiptlhaar hcrfiskaei srwplvgala raagtlfvqr
      121 nsrrdtqrtv lamaqalehg diltvfpegt vgpgrellpf hgnmlqaaid vdvavqpvam
      181 tfvdqrtgai syvpceaypd epmlrslwrt igtehlmavv hygvpekang rdrrqwandl
      241 raqvqalrwn aasepeleqd lpleqatvr
//
LOCUS       WP_284336982             483 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Comamonas
            halotolerans].
ACCESSION   WP_284336982
VERSION     WP_284336982.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..483
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=52947
     Region          4..462
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mgtspasilv vddepdlrtl yeltllregh rvetaatlae arahlricqf dvlivdmrlp
       61 dglgmellre qreqhrqert ivitaygsae navealrfga fdyltkpvdl kqfrsvvasa
      121 icseagssgi pvpmpssigg aqarvvnaav alerlvgnsa vmqqvrqriq kvsqsmapvm
      181 itgesgtgke lvaralhacs hrahapwiav ncgaipehll eaeffgarkg aytgatadre
      241 gffsaarggt lfldeigelp lsmqakllra iqercirplg stqeepvdvr ivsathrnla
      301 advqagrfrq dlyyrlnvid ipipplrerr edlpdlcavl lqriagdsls svppiaphvl
      361 eqlqkmplyg nvrelenllh rfialnedva pssgedapas aapnaeqlpl delpedlqaw
      421 ldqqermilm ralqhygnnr taaaarlgis lrqiryriar lniplspeeq eassdnalhd
      481 ahl
//
LOCUS       WP_284337032             899 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Comamonas halotolerans].
ACCESSION   WP_284337032
VERSION     WP_284337032.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 899)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 899)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..899
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..899
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=99148
     Region          14..899
                     /region_name="PRK10490"
                     /note="sensor protein KdpD; Provisional"
                     /db_xref="CDD:236701"
ORIGIN      
        1 maattspsln paerpdpdal vaqlqaehvq asrgklriyf gsnagvgkty amlaaaqrer
       61 qsgrsiligl vethgraete lqlyglellp rcrlayqgkt lmefdldgal trhpdvllld
      121 elahsnavga rhpkrwqdvq elleagidvw ttlnvqhles lndvvsgivg iqvhetvpdh
      181 ifddadeviv vdlppeelik rlkagkiypl eqaerasrnf frlgnllalr elalrrtadr
      241 vdedmrdyrr eraiediwpa rerllvgvng rtgddalvrq varlarrlea vwtvvyvdap
      301 drqhrqrpar etvlktltla erlgadtati pgsnvaqalv dfaqernash lvlarvqqrw
      361 nrwlpwrras lpeqiallnp gldvlvlsvn sarkehltpm qvnadngwnw kgysgvtlac
      421 faaatlaell levfepanvv mlflllvvls slrwgrgpga waallsvllf dfyfvpprns
      481 fsindtqyif tfclmlgval icgqlmarlr hearvaaere rrsgalarla rdlsaaltqe
      541 qiteialstm sgvfdaqagl llpdskeqln iargsegpid isvarwcmeh gqiagsgtdt
      601 laaapamymp liapvrvrgv lalqlhspkr lhipeersll dacasqiala lervhfvdva
      661 qqtklamege rmrntllsai shdlrtplts ilgaaqaalp haqsrdtydm liqirkqala
      721 mqqlvenlla marlqqggvh lrrewiplde vigsalrqmq drlsahivtt nlppdlplly
      781 idptlmervl vnlldnaaky tppqtvihia ariegaecvl svqdsglglp khispeqlfe
      841 pftrgetest vtgiglgltl aqrivqahgg qlgceaaple tgsvfsirlp vatqptisd
//
LOCUS       WP_284337094             415 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Comamonas halotolerans].
ACCESSION   WP_284337094
VERSION     WP_284337094.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..415
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44833
     Region          1..414
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mniaivgagi tgistalela rdghhvtvye qmnaaaedas fapsgwlsps aaqslaapga
       61 gmdlqqmqng ngllqassmi gsatwrwmrq wkkheknaae hgnhafsqal halsnysasl
      121 rwqdcadtdm aaerksgslv flrtpqevef wnaqldllqa qgtsiqlasp qqaqtlepgl
      181 gqeiawlkal hfpeaesinp rlwtqfmrmq aqeigvrfvt gtsiqrlhhq ptgveiagqm
      241 kpydavvlct ganqhllstl glqlplmpia gysitapvrd slhapraaim dwsqqaiisr
      301 mgqriritag lemaspadap hhkptlermy rllndwfpgg aqlssaqvqv wrgvrgylpd
      361 glpalgnsgh agiwvnlahg shgaslasgc araladmllq rapaidmqaf splrf
//
LOCUS       WP_284337115             346 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Comamonas halotolerans].
ACCESSION   WP_284337115
VERSION     WP_284337115.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..346
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=35879
     Region          49..340
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mtaslhsalt srrtwlrwsl aasasavatp wglhaahaaa plltlpavpg kavtiivggp
       61 aggatdgvar viaqalshsl arevivdnkp gaggtigskl vsqskndgyt lllgqiapnv
      121 lsplmqnprp ydpitgftpi gqigntasvl vvpangpqtl kkalriwkqk gsfsyastgv
      181 gsgahllghl massleiegl hvpyrgspfa lqdltggrvd affvtagalg sylesgklia
      241 latasrarsh fyaqlptlre aghstvsneg wfglfaaaqt padiastlhq hlnaalqtae
      301 vkqqlqslvv diapsaspeq yadfirqeva hwsqvlarmg sslqat
//
LOCUS       WP_284337142             326 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Comamonas halotolerans].
ACCESSION   WP_284337142
VERSION     WP_284337142.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..326
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34168
     Region          1..324
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mnmnrkqfgr valaaglals gwnvvaakdn ypskpinmvv pasaggttdl aarmtaqalg
       61 pvlgqtivve nkgggngnia aaqakraead gynllmqysg fhvisphlgk sswalsdfvp
      121 vanvlsapqi vvvrgdlpvn tmqelvayak anpmklnyas sgngslqhvt gvqleqaagi
      181 qmvhvpykgt gpalqdllgg qvdltfgtap pfmahiqagk lkvlavtgke rlpslskvpt
      241 taetglpavn atswfalfap aktpqdivsk leadvrnmls dpafqkkald qgatadfkds
      301 kalgamvrqd wemwakvvke aniqad
//
LOCUS       WP_284337215             195 aa            linear   BCT 25-DEC-2024
DEFINITION  OmpW/AlkL family protein [Comamonas halotolerans].
ACCESSION   WP_284337215
VERSION     WP_284337215.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006882
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..195
                     /product="OmpW/AlkL family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21096
     Region          2..195
                     /region_name="OmpW"
                     /note="Outer membrane protein OmpW [Cell
                     wall/membrane/envelope biogenesis]; COG3047"
                     /db_xref="CDD:442281"
ORIGIN      
        1 mkktllavaa lcamtsgaam aqqqdgkwqv rvravnvdlk sagsnglsvk dktipevdis
       61 yfftpnfaae liltypqkhd vrlkgvgkig tvkelpptll aqyhftnfga fkpyvgagvn
      121 ytrfssvdld vpgadikrss wggalqvgfd yaldknwsin fdvkkvymdt kenglglgkv
      181 kldpvlvgvg vgyrf
//
LOCUS       WP_284337272             546 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Comamonas halotolerans].
ACCESSION   WP_284337272
VERSION     WP_284337272.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 546)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 546)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 546)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 546)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 546)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..546
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59992
     Region          1..540
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 msavdhtapa lrwrgfafal pialltiipl lavvwmavtp qpdiwqhlwk yvlprvlgnt
       61 lllmllvsvv vlavgvplaw ltvmcdfpgr rffswalvlp laipayvlaf vqmglfeyag
      121 pvqsflrevm gssrwfpdir gslwglvmvl vmafypyvyl mtrsafltqg hrsmeaaqal
      181 glspvaaffk valplarpwi gaglalvlme vladfgaiav fnfdtfttal ykswfdlhni
      241 gaaaqlaail vlvvlllvaa eqrsrsaqrf hvsnpqqhrv vlkggrgwaa sllcllvfsa
      301 afavpmvqiv wwslevwedv lnsdywgyaw ntlslalita aiasvfalll swirrrhsdg
      361 ltgwtvrlav lgyavpgvvl avgvfvpiaw ldeklmalve pwgietlgil kgslagmlla
      421 laarflavay natdaamqri trsqeeacas lglspwqtlr rlhlpllrtg llsaflmvvv
      481 dvmkempitl mmrqfgwdtl avrvfqltse smwqeaalpa laivlvgllp villvlqtek
      541 tpssag
//
LOCUS       WP_284337274             189 aa            linear   BCT 25-DEC-2024
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Comamonas halotolerans].
ACCESSION   WP_284337274
VERSION     WP_284337274.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..189
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20628
     Region          9..174
                     /region_name="YdeN"
                     /note="Predicted esterase of the alpha/beta hydrolase fold
                     [General function prediction only]; COG3545"
                     /db_xref="CDD:442766"
ORIGIN      
        1 msssapriii vpgwrnsgae hwqslwaqll pnverveqdd wltpkradwv qtlervilar
       61 pepaivvahs lgcittahlg geaaariqsa llvapadper rahladfapv pyqplpyrsv
      121 lvastndpyc pirlagayar swgsefvrlp naghiniesg hghwplgwal lqslvedmaw
      181 gkgkqmvaa
//
LOCUS       WP_284337283             289 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Comamonas
            halotolerans].
ACCESSION   WP_284337283
VERSION     WP_284337283.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..289
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30514
     Region          2..287
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mrsklfvpas rpelfakala sdadalsfdl edavaeprke eardmlkafl espeakatsk
       61 tlivrvnamd tvhfaadvaa vvrpglhlvn lpkpdspdav vqaaaciada glanglselp
      121 glllnietpq slrmaatlar ahpavvglql glgdlfepyg vhrrepsalq qalftvrmaa
      181 aeanvfaydg afadihdseg fraeaelsrr lgfigkscih psqialansv yqptkteiah
      241 aqrvlqaaek aeasstgafv vdgkmidrpf vlraqaiias arasglltg
//
LOCUS       WP_284337316             336 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Comamonas halotolerans].
ACCESSION   WP_284337316
VERSION     WP_284337316.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..336
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34350
     Region          34..328
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mskgaqrscw laallllata illmlgasvg stgwesvwrm qsdavalqiv wdirlprtsg
       61 awlagallgl agavaqglfr npladpyllg sasgaalgga vamvlsgtaa mgmewmqrlg
      121 mtgmafagaa favlltllma qgvqnslrll lagvvvgvvl gavrdmlemr ypdilqpmka
      181 fglgstafig wascsllava wavcavaawg lsrvldgltl gestaaslgl plapmragli
      241 avmalatgta vaqtgliafv glaaphlvrs mvsvgharsi vlsslmggvv lltadilarw
      301 vmapeelpvg vltallggsy llwlmhrgha arqarg
//
LOCUS       WP_284337361             368 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Comamonas halotolerans].
ACCESSION   WP_284337361
VERSION     WP_284337361.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..368
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41013
     Region          1..351
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mntrnttldq vkavaclviv chhlafygpm admlrpvlpg llqwldeygr mavqvflvlg
       61 gyfaaaalap qgvgkhpqfw palnkrfvrl slpysaallm aivvnetvrg lgfqhesvsd
      121 tptwssviah llllhsiadf esisagvwyv aidfqlyvlc llwlwlckqq trwtgwgqag
      181 ialataaslw vwnldpdldv wflyflgayg lgmmawwath sedraqrtlw ivaiatfgii
      241 alsvawrdri alalisalvl aiagnlrwpe slrhaqiapl twigqrsysi flihfpmsll
      301 vnaevhsqwp nsvaansigm lvavllsiaa gavlyewter asatwqrlrr whlgvlstgl
      361 malwlqqi
//
LOCUS       WP_284337397             193 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II [Comamonas halotolerans].
ACCESSION   WP_284337397
VERSION     WP_284337397.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..193
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=20666
     Region          3..192
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 mkllmidnyd sftynivqyf gelgadvtvv rndeitldev ialvadqgie rvvispgpss
       61 paeagisvaa iqhfagklpv lgvclghqsi gaafggdiir agqqmhgkts vistdqkgvf
      121 aglpvqftvn ryhslvidkk tlpecleita tsedgeiqgv rhkslavegv qfhpesilte
      181 hghamlknfl dqk
//
LOCUS       WP_284337457             311 aa            linear   BCT 25-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Comamonas halotolerans].
ACCESSION   WP_284337457
VERSION     WP_284337457.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..311
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34573
     Region          28..309
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 msvafaveap avvsrtsvva drvadtaafr iiplqgsvge lgaevvgldl sqplsavdfd
       61 rlqqahwkhh vlvfrdlrit paqqvafsrl wgplqihvlr qfqlpghpei lqvsnirdsk
      121 ghpeglgdag qmwhsdlsyk evpslgsllh aqelpceggd tlfadqhaay dalplalkqq
      181 laglqaehsy llhynanspw rpkltqsqid evkpavhpvv tthpgngrka lfvsehftsr
      241 ivglpedesr dllqqlfahs vqpqfvyrhh wqphdmvfwd nrsvlhlaag tpehlrrkly
      301 rttvegskpq a
//
LOCUS       WP_284337473             122 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Comamonas
            halotolerans].
ACCESSION   WP_284337473
VERSION     WP_284337473.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..122
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13323
     Region          8..104
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mkrlnsksgc avevtlsvmg gtwkpvvlfh llhgkkrfse lnrliggitq rmltlqlrel
       61 eeagivlrtv haevpprvdy eltplghslq pvlvamrdwg teyasgrgqd eslseqcavg
      121 sa
//
LOCUS       WP_284337510             550 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Comamonas halotolerans].
ACCESSION   WP_284337510
VERSION     WP_284337510.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..550
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=62332
     Region          <26..539
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mrrfvnasse sviffrhgri fyanpaaial tgyqldqlld rsvlhllphv lrasaqnmle
       61 hgtisaqetr llrhngqeqd veititlqpe eggdlgvmvl rditerkrae aemhflafhd
      121 pltrqlnrqg lmrqlqqtle ratqfnhrca vlyvdldrfk dvndsmghda gdkllveaar
      181 rlrskvhpdd ivarlgadef vvvlasplta cqpecilrei qflmnkpyal vkglanlpas
      241 igislypedg nsaeelmlna saamemaknl gqgnhqyysa lmhmrpskwl tqdrllreai
      301 ekdlglvlhy qplwdlsrdc legfealvrw qhpergllpp sefisfaesr glislldrwv
      361 mraackqlre wrnaglppvv vsvnmsaief nqvnllaevq qvltdtgidp qsleieltet
      421 tlmkhsehvl stltslqklg irlsiddfgt gysslaylkr ypldklkidr afvkdtpqdq
      481 dyvslvtaii qmarslnlrt vaegvetkeq wdllkqlgce liqgyylsrp mtaedalrwq
      541 qhhcqtpapq
//
LOCUS       WP_284337531             395 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfotransferase family protein [Comamonas halotolerans].
ACCESSION   WP_284337531
VERSION     WP_284337531.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..395
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=45060
     Region          92..344
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mnassisqal dvdellqaar eraagldyfg ddnyrqalev ltkslnteak lsttgivlmr
       61 erlvsqlanr livedyfqrf peiakmeidd plvivglprt gttmlqrtla vdsrfysaaw
      121 wetrypapla geslkepvqr isqakaevaq mveaipqils ihpldamlcd eefmlmehsf
      181 lcamdayadv psyttwldqq dlrpvytllk kmlqflqwqk aqrgeapsqr wllkapqhlh
      241 tidillsvfp kakvmlthre paqtipsmss maytlwqiys dspdaksagk qwntrmargi
      301 rhtmkvrdsg nearfmdihf adtvskpmev lervyefael pftdkaraaa qqwinnngre
      361 krsshdysle vfglseqqmq adyasyrarh lkaad
//
LOCUS       WP_284337625             351 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Comamonas halotolerans].
ACCESSION   WP_284337625
VERSION     WP_284337625.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..351
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=37534
     Region          24..349
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mgdfsrdfva caidcltdsh hperrlwltq aacllaasav psafadtaas yptkpvrivv
       61 pfapggatdv larvtgngla aqlkqpviie nrpggaglig gdvvakatpd ghnlylgtts
      121 tmlsmqflfk kmpfdpqtnf apvsricwap ivlvvnselp vhtvnqlvey irankgrlsy
      181 gsygigshah lafvtldkla nggmthiayk geapmtqelv ggslkmgmgs tlslkqhies
      241 gklralaftg ahrvpalqdi ptfeeagfkq ealrisgwlg vvatggtppe ivqkigqafr
      301 saltqrdvna rvltagfvpl sddtpqkfak nwieemaiwk rllheadvqp n
//
LOCUS       WP_284337812             354 aa            linear   BCT 25-DEC-2024
DEFINITION  MraY family glycosyltransferase [Comamonas halotolerans].
ACCESSION   WP_284337812
VERSION     WP_284337812.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Anderson,M.S., Eveland,S.S. and Price,N.P.
  TITLE     Conserved cytoplasmic motifs that distinguish sub-groups of the
            polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase
            family
  JOURNAL   FEMS Microbiol Lett 191 (2), 169-175 (2000)
   PUBMED   11024259
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Lehrman,M.A.
  TITLE     A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P
            transferases
  JOURNAL   Glycobiology 4 (6), 768-771 (1994)
   PUBMED   7734839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10161037
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..354
                     /product="MraY family glycosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=38240
     Region          30..226
                     /region_name="GT_MraY_like"
                     /note="This subfamily is composed of uncharacterized
                     bacterial glycosyltransferases in the MraY-like family.
                     This family contains both eukaryotic and prokaryotic
                     UDP-D-N-acetylhexosamine:polyprenol phosphate
                     D-N-acetylhexosamine-1-phosphate transferases, which...;
                     cd06912"
                     /db_xref="CDD:133467"
     Site            88..89
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133467"
     Site            209..212
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133467"
ORIGIN      
        1 mafvtsfltc lvlvltkrwh gafttdtttg lqkfhtaptp riagigivag vlagffassh
       61 gvaaaekrai lntillagmp aflfglledv tkkvsvktrl latmasgvlg wgitgtslth
      121 vdiwgidwll sftlisvvft afavggvana iniidgfngl tagtaiimla afgfiarqvg
      181 diplaftcli iagavagffi vnwpsgkifl gdggayflgf mlawiavllp ernaavspwt
      241 sllicsypii evgfsfirkt mregyhpsqp dgvhlhmlan krwakkvfsr fskpiqnglt
      301 spflwvyaav pcvlaiftyq nkwlavgsff isvlcylafy sklaffhwvp shrd
//
LOCUS       WP_284337832             185 aa            linear   BCT 25-DEC-2024
DEFINITION  D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase
            [Comamonas halotolerans].
ACCESSION   WP_284337832
VERSION     WP_284337832.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 185)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..185
                     /product="D-glycero-alpha-D-manno-heptose-1,7-bisphosphate
                     7-phosphatase"
                     /EC_number="3.1.3.83"
                     /GO_function="GO:0034200 - D-glycero-beta-D-manno-heptose
                     1,7-bisphosphate 7-phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19851
     Region          1..172
                     /region_name="HisB1/GmhB"
                     /note="Histidinol phosphatase/D-glycero-mannoheptose
                     bisphosphatephosphatase, HAD superfamily [Amino acid
                     transport and metabolism]; COG0241"
                     /db_xref="CDD:440011"
ORIGIN      
        1 mklaildrig tlniegedsi valkdwvlqe gvldavaqln rggwhvtlat nqpglgrgsf
       61 dlndlnaihl rmqrelaavg arieavffcp htpeegcscr kpapgllqqi aarygaepde
      121 iwvvgqdtkh leageaigah vvwlqlgeta plngvfqdvp ryvswkalad alapdvqtpp
      181 aaprp
//
LOCUS       WP_284337862             329 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Comamonas halotolerans].
ACCESSION   WP_284337862
VERSION     WP_284337862.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..329
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34243
     Region          21..326
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mlrrtlista vvalasvaat stawaaggaw pqlkpitliv pfsaggnvdf qsrligqkls
       61 erlgqtvvid napgaggvlg vskaiaakpd gytlvmgfdg pvsvaqlvnk avkydaekdl
      121 mpiglvsvap vvlmarpglp aqnmqelidl akaqpgkity gssgvgtvlh lamemvqera
      181 gvkmvhvpyr ggaqitndvm ggqvdtgymv ttsatplvnq gklhalgvts aqridsiakv
      241 ptfsethvlk gleintwtgl fapkgtptav vqrlatelga vlqqpevqqr lkdggatpgq
      301 itlgdfaqfl kkekasyaai vqsakieqe
//
LOCUS       WP_284337863             305 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Comamonas halotolerans].
ACCESSION   WP_284337863
VERSION     WP_284337863.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..305
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31643
     Region          1..291
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 msaprsssfv pvlallgsia flctgtswak helfptigaq gttalrigfs amlmslfwrp
       61 wnaqlirsdw rsitlyggtl gvmclffyms lrtlpfgiav aieftgpltv aiwssrrsld
      121 ylwialamtg lglllplghd lhtldpvgia waalggtgwg cyiifgkrmg hlpisvsapl
      181 gaamaalvva pvgiahagsa llspsvlltg lgvalvssai pislelfalk hlpknvfgtm
      241 tsmepavaal lallllgevl sftqcvaial imsasigcai taqarrikpv piasgsegks
      301 vaggv
//
LOCUS       WP_284338023             753 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Comamonas halotolerans].
ACCESSION   WP_284338023
VERSION     WP_284338023.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 753)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 753)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..753
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=82768
     Region          42..752
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mrsvtslppt tgedgalptg lkpsganvev phllaatagn ipdqldalrr arafaepllv
       61 geelssgent lahadataai lqgiggseam qaacylvyas mhlnkplevl tkafgpnfae
      121 lavettklmh fqqqarggda svrvddpatq tetvrkmllg fsrdvrvvll rlasrlqtlr
      181 wyaaskrpvs psmayealhv faplanrlgi wqikweledl sfrflepdty rtiaklldek
      241 raerevymeq lrsrlesglr aysisatvsg rpkhiysivk kmrgkslnfd qlfdiralrv
      301 vvpnvkdcyt alswvhenft aiesefddyi akpkpngyqs lhtvvrdeqg kaieiqirtq
      361 amhdhaengv aahwaykeag tkgyagvsat geydakiavl rqllawgqdl senpnhrglf
      421 ddriyvltpd aavielpqga tpvdfaysvh tnlghrcrga rvdgnmvpln tplqsgqtve
      481 ittvkegrps rdwlnpelgy lvsnrakakv rawfnaqamn etvtrgreav ekllqregkt
      541 aiklddlavq lgfksadalf evvgkdeysl rnievvlrpa epaepeediq smvrkprann
      601 aaqkggvlvv gvdslmtqla kcckpappdd iggfvtrgkg vsvhrtdcsn fremaarnee
      661 rvidvtwglp kaakhtavyp vdvsveatdr qgllrdisdv fakektnvig vqtqsvkgta
      721 wmtftvevsd sgrlnkvlgi vagiagvrsa rrr
//
LOCUS       WP_284338037             481 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Comamonas halotolerans].
ACCESSION   WP_284338037
VERSION     WP_284338037.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 481)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 481)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..481
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52996
     Region          135..468
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mnkasqslvq rlarslitav lavwllstal vawyvdrqiq dnfdvelies ahrqlypall
       61 elqiiqpphs aaaalqpltg gdpqvmgelp gsnhseplll qlrhrdgqvl lrtqatpasp
      121 favplkagfy dtpdfrvfsl ydeqyqvwlq ladpleerse tsqrtvtglv ivllvmlpvm
      181 awlitavarr elrfvgdlqk qisarngrnl qalevhampq elrtvgegvn qllerlseal
      241 nverslasna ahelrtplae vrlrlhtave qaqqhdgstt qtqeaavpla evkaalqsle
      301 ilshrterll qlsraeggdr ahfarvnlve laaqvaqtfw qqnqaqkrld litpdahdav
      361 wvwgdidsla ivlrnlidna lrhsdgwvtl evlaapqaal vvrdsgagls akqiqliqqr
      421 harldtqhig yglgmsivkt iadkhgaqlv ftspppgmpt gleaglrfqd aandgdelre
      481 v
//
LOCUS       WP_284338072              88 aa            linear   BCT 25-DEC-2024
DEFINITION  BolA family protein [Comamonas halotolerans].
ACCESSION   WP_284338072
VERSION     WP_284338072.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..88
                     /product="BolA family protein"
                     /calculated_mol_wt=9366
     Region          6..86
                     /region_name="BolA"
                     /note="DNA-binding global transcriptional regulator BolA,
                     affects cell shape, cell division and biofilm formation
                     [Transcription, Signal transduction mechanisms]; COG0271"
                     /db_xref="CDD:440041"
ORIGIN      
        1 mtetitaaai eqalrdklap sqlevidesa ahaghagang tgfgthfrvr iaapvfegkr
       61 rvaqhrlvyd alqhfidqgl halaievl
//
LOCUS       WP_284338162             158 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF2269 family protein [Comamonas halotolerans].
ACCESSION   WP_284338162
VERSION     WP_284338162.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..158
                     /product="DUF2269 family protein"
                     /calculated_mol_wt=17279
     Region          2..156
                     /region_name="COG5528"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:444279"
ORIGIN      
        1 mntylllktv hiissvllvg tglgsafymf fanrsgsiaa qavvsklvvr adwwfttpci
       61 ivqpatglam mylagwplst swlalsigly vlagacwlpv vwlqirmahl aeqahtqgaa
      121 lpclflryqr mweslgypaf aamagtyflm vnkpslwg
//
LOCUS       WP_284338140             660 aa            linear   BCT 25-DEC-2024
DEFINITION  GumC family protein [Comamonas halotolerans].
ACCESSION   WP_284338140
VERSION     WP_284338140.1
KEYWORDS    RefSeq.
SOURCE      Comamonas halotolerans
  ORGANISM  Comamonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 660)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Comamonas halotolerans"
                     /db_xref="taxon:3041496"
     Protein         1..660
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=74371
     Region          9..659
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 midirslrdl lrlffifqre frwavlvtvm vavlgafllp aryesnarll vkpdrqsttl
       61 pieaqnrqtl vapstqrdpi vdeeklltgr pivhqvaqry laeiaaqqpt gfwktvkhhv
      121 kravgatlng vrsvlqvlgi vepqtdeqrl arkleksfqa sheagsavie mrfvwddpvv
      181 aqkvlntwve vylaerarvl grtslhgfyq gemdktahri rslkeqlqeg lqdidsisak
      241 arlenltnqi drltdarvta qnertglasl aggarqqirn qpaevvtdre islnptqldl
      301 krqlnalqve rtrllrtytd eappvrlieq dirnvealvk qekerlersq nlapnalvsn
      361 arqqlmdael rqqqlaaqig dydrelqalr kerdrvlrde pelnrlqlel etaeksyaly
      421 aenlekarid haldssqisn iaqieeatln aarvfpkslm illaafpaai gvgllviyic
      481 ylldqrihdg ariqqrfgvp lwasipdsdg vdrhaliasv yrlygllple rirsegvala
      541 ltsarsgegv nfimdqlepl lkengfvvrr ggdasaapge lvlldvsall snqdaflvlr
      601 radlivlvvq artstvpmve nalsllltaf kkvdgiilnr rrfevparlm nilqrwrsvq
//
LOCUS       WP_284338267             162 aa            linear   BCT 25-DEC-2024
DEFINITION  SRPBCC family protein [Devosia nitrariae].
ACCESSION   WP_284338267
VERSION     WP_284338267.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..162
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=18691
     Region          12..151
                     /region_name="SRPBCC_CalC_Aha1-like"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of Micromonospora echinospora CalC, human Aha1, and
                     related proteins; cd07814"
                     /db_xref="CDD:176856"
     Site            order(13,15,17,26..28,30..31,36,50,58,60,62,64,73,75..76,
                     78,81,87,89..90,104..105,107,109,119,121,123,125,130..138,
                     140..142,145)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mrqrtddlrd dellitrvfe apvavvwrlw sepehwfrws gpqgftvtdl dhdfrvggqw
       61 rtgmksaayg rsvshgqfle ivpherivms faweegsget tqttititfe eedgrtvqhf
      121 hqtpfssrdy rdshvmgwns qfnkeaeyae alargvqlaq ls
//
LOCUS       WP_284338370             564 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Devosia nitrariae].
ACCESSION   WP_284338370
VERSION     WP_284338370.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..564
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=60522
     Region          1..559
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mapllaienl siaymlgdgr saeaisdfsl rlergriagi vgqsgagkst igkailgllg
       61 enaritsgti tldgtvitrf segefaairg krigyiyqnp mtalnpvlsi geqmieaiea
      121 ntarrgeaar tyalellksa evshaeerls kyphqlsggl cqrivfaiai aaqpdliiad
      181 epttaldvtv qkavlatlkr laceqqiaiv lithdmgvvf qmcdevsvlc rgrlvehgst
      241 aqvigaprer ytkdlmaaip svdlkrdrfd vldsfantpg rrrgiaflks giaaarggea
      301 lltvnglskt fdtrgrraas ggfralddvg fevfagetlg ivgesgsgks tigrailgli
      361 epdagagiaf qgrpiadmrs rrdrialsrs lqcifqdpys slnprmsagt nitygivaqg
      421 lisrahakvl aedllevvgl prqaagrmph afsggerqri giaralafrp elifcdepts
      481 aldvtvqaei lnlmkelqet lgltlvfvsh dlavvrqmcd rvivmragrl veegradqvl
      541 typretytre llaamprial egar
//
LOCUS       WP_284338388             420 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Devosia nitrariae].
ACCESSION   WP_284338388
VERSION     WP_284338388.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..420
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45716
     Region          1..404
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtvrqttldn gmvvltddmp hlesaslgvw vragarserk sehgvshlle hmafkgtasr
       61 salniaesie nvggdlnaat siehtgyfar vlkddvvlaa diladilqns vfdenelere
      121 khvieqeiga ardnpddhvf dlfqaaafpd qpigrtilgt vdsvseftpd virkymrrny
      181 vgdhmtmaaa gnvdhdelvr vagerfsdlk pngapapqra eykggeerlv sdheqahivl
      241 gfegraynsd gfyaaqilas ilgggmssrl fqevrekrgl cysvyafhwa fadsgvfgva
      301 aatgedevgd lvpvvveelr ratqtitdee vvrvrnqira gllmslesps aragqiarqq
      361 ilwgrpiplq etverigrit aqrvkdiaeq ifstgdisla gigpisglpd assigktlkr
//
LOCUS       WP_284338399             117 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Devosia nitrariae].
ACCESSION   WP_284338399
VERSION     WP_284338399.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 117)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 117)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 117)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 117)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..117
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12499
     Region          2..91
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdiddataal salaqptrls afrllvraep egvaagdlar rldvpqntls shlavlaqag
       61 lvagerqsrs iiyradfprf revmlfllsd ccnghpevca pvldtlshic qpgeevc
//
LOCUS       WP_284338433             112 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Devosia
            nitrariae].
ACCESSION   WP_284338433
VERSION     WP_284338433.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..112
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12426
     Region          13..111
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mvsgpepdak mlhcpalvti rliagkwktr ilwalrpgpv afnalqrqlp gisakmlieh
       61 lrqletdglv irtgarrgkv etvtyaysdy grtlipvldr lgdwglahee rn
//
LOCUS       WP_284338665             300 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Devosia
            nitrariae].
ACCESSION   WP_284338665
VERSION     WP_284338665.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..300
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31799
     Region          62..272
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mletvesria vstwslhktl gvtfphdlds dgvgpreesy gpgsarlidl palvkshwie
       61 rlevcsfhlp srdagylaef rdalasagva lqtmlieagd lsnpvtagrd gkwisgwvet
      121 aialgaehar iiagkqkpsr ealdlaadgl taiadrysea pirlftenwf dllatpelvn
      181 glldrtegkv glngdfgnws gpgkyddlas ifsraelcha kagftdgvld addygqciha
      241 aesagytgpy tlifdaqapd ewagiaiera flldrlaeag tglgptpaas vhptgsapar
//
LOCUS       WP_284338633             133 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Devosia nitrariae].
ACCESSION   WP_284338633
VERSION     WP_284338633.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 133)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 133)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 133)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..133
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13650
     Region          30..107
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 magypglnis rdiemkldel qalaafaals qetrlsmvrs lvvageqglp agvvgdavga
       61 ssssasfhls hleraglvts rrearsiiya anfdalsglv eflmrdccqg hpdvvagatk
      121 aaadccapde qag
//
LOCUS       WP_284338713             205 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Devosia nitrariae].
ACCESSION   WP_284338713
VERSION     WP_284338713.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..205
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23548
     Region          8..196
                     /region_name="HAD_sEH-N_like"
                     /note="N-terminal lipase phosphatase domain of human
                     soluble epoxide hydrolase, Escherichia coli YihX/HAD4
                     alpha-D-glucose 1-phosphate phosphatase, and related
                     domains, may be inactive; cd02603"
                     /db_xref="CDD:319790"
     Site            order(10..14,110..111,143,167..168,171..172)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            138
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mteplipvfd lggvfvdwnp mylfrklfpt eeeaawfhen ictsawnlef dageiysegv
       61 aklitrfpry wreiqaydlr wketfngfid gtvaihdelv daeiptfait nfswekwvtc
      121 lgewpflekf dgvivsgleg lvkpdvriyr lfceryglap escvfvddne snviaarnfg
      181 meaihfvspe dlrarligyg lplka
//
LOCUS       WP_284338738             476 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Devosia nitrariae].
ACCESSION   WP_284338738
VERSION     WP_284338738.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..476
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=50704
     Region          14..139
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
     Region          <130..463
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mvtaggsatl tqgrlllvdr dassarvlaa tlaeclvsap emtavgggrq aaetlragdf
       61 dvvladlasl adlaeateda varlvklarg almvalsdga svsaavaamq agahdyvakp
      121 ingpalatri gelaerhgkt raiaiearpq agvtgfagfv gassamqfvy eqieriapss
      181 apvfitgesg tgkevaaeal hargpraeka fiavncaaip rdlmeselfg vvrgaytgah
      241 edrkgaaela dggtlfldei gemdlslqsk llrflqtgmm srvgesgtrk idarvicatn
      301 rnpmqmiadk tfredlfyrl hvlpihlppl rqrpadimal arhfletfar eerkqfsgfs
      361 aeaaaamlar dwpgnvrqlq nltrrlvvmf dggqidaeml raadiesrea vietapvpre
      421 rrpvlpmwqq eqriiedaia sfngnislaa aaleispsti yrkrqswaem gtagaa
//
LOCUS       WP_284338885             229 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Devosia nitrariae].
ACCESSION   WP_284338885
VERSION     WP_284338885.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 229)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..229
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25349
     Region          20..>221
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msraerllal lellrrhrrp vsgpalarel gisirtlyrd ldslraqgaa idgapglgyv
       61 lqpgfvlppl mltsdeidal clgldwvhdr adpglaasaa nlrakieavl ppekartmms
      121 stslagppah plpdavdlga vraairdhhv ieivyrgetg qstnrriwpf migyfdsvrl
      181 igawcelrgg irhfrtdrig pvhftreryp arrqelmrqw rvedgltgd
//
LOCUS       WP_284338940             570 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Devosia
            nitrariae].
ACCESSION   WP_284338940
VERSION     WP_284338940.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 570)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 570)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..570
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=62658
     Region          16..551
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mavmteaslp ialdgarkvr gnltqtrirw mifaifigfs lvggrlvqlg mvetdtrieg
       61 qtrdviqasr ppildrngle mavdirvpsl faeprriidv deaaealltv lpdldpqwlr
      121 qrlsgdkgfv wvereltpai qervmrlgip gidfiteskr fypgmneash ilgsvnidnq
      181 giagierhmd genvallqel glargnalap vqlsvdmrvq hvvysellda ltryqaiaaa
      241 gvvmdvntge ivamaslpdf dpnepatalv kdsfnrvtsg ifepgsifkt vtmaaaldsg
      301 avnitdqfda rfgirfgryt iddfhgkhri lslpevfkys snigtirvmq amgkenyraf
      361 ltrmgfdqrv pfelpemrlp svpkefsevg aatasfghgl svsplhmvta ysafvnggny
      421 vpptlykrai eeaqplyrqv lqprvseyir yllrlnaids ggsgsrmnkl algfrvggkt
      481 gtaekvvdgr yssskvtnff gsafpldnpr yamiimvdep krenpqsgtt agwnagevtg
      541 riikriapml giqpdfrpev daalvppvlr
//
LOCUS       WP_284339117             382 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Devosia nitrariae].
ACCESSION   WP_284339117
VERSION     WP_284339117.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..382
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42132
     Region          7..225
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mksreklisv vipaynaerf lertlrsaaa qtyspieiiv iddgstdttr dialrfaead
       61 arvkvinvan ggvararnig iersrgdyva fldaddlwhp tkialqvatl eaaddpswaa
      121 cytlfrsidt ddftqrpgps ryrsgyilaq llfakfvgng ssllvrrsaa lavggfdpsy
      181 adagiggsed ldfelrlaar yriaavpqfl vgyrryvgnm sssqlrmsra vvetvrrcla
      241 anpdlpkaag ryalatthnw aggfnlwreg gaalslahkm tafrndpllt afriyhwlgr
      301 rwhavtaava prapagprky ldvspldgle lrpsryhelr lrqlaridae rerrlfsskp
      361 ststvtrpee qvnssepaas ms
//
LOCUS       WP_284339127             288 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Devosia
            nitrariae].
ACCESSION   WP_284339127
VERSION     WP_284339127.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..288
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31692
     Region          1..255
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mpfginllcl tdfvedahlg aieriraagy dgvevcvlrg dpdhyawlar eldrlelrrt
       61 ttsiipspda dptsadagtr srgikhldwa ldcavalsae svggpfhapi ghftgtgpta
      121 eewargaeah rrmaeraarh gmilslepln rfethflntm eqsrkyvdlv ghpafkimyd
      181 tfhanieerd qaraietlgd gmgvlhisen drgipgkghi dfrqvfqaar ktgfdgwvvl
      241 eafgaglpai aaatrvwrpl fpdhetlfre glkfmregwa eaakeaaa
//
LOCUS       WP_284339168             106 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Devosia nitrariae].
ACCESSION   WP_284339168
VERSION     WP_284339168.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..106
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11929
     Region          3..86
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mhlsdtfaal gnhtrlaive rllregelpa gelvvegems apamshhfkv lrdagivvqr
       61 vdaqrrlysv rpeamrvign wtmtyrefwe qsldrlgaai dkeqgr
//
LOCUS       WP_284339175             277 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Devosia nitrariae].
ACCESSION   WP_284339175
VERSION     WP_284339175.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..277
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28823
     Region          34..277
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 msiftitvrs aavalalsag gvlaaetvvd lpseikgtla lpesgatgqa vvmlhgfgss
       61 rdevgglfal qaedlaaegi aslridfrgy gesggdmadt tlegliddaa aardilagve
      121 gvdparigvi gysfgaavam lepdpfasvv vwgqmgdlqa efheflgqdf ydtaanegva
      181 svdlgwrtis lkqaffdsla rhdlaerfag ydgpfltiag dgdpavsyfd qylglaegra
      241 eslivpgadh mlgvftdepe igrqvigktt awlretl
//
LOCUS       WP_284339233             225 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Devosia nitrariae].
ACCESSION   WP_284339233
VERSION     WP_284339233.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..225
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23892
     Region          1..169
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 magvlldmdg tlldteviyl sstmaamnsl gypdameich amigipgpec eamllsrygp
       61 qfsisgfnre fvihrdrlle qglplkpgas elidaladaq ipravvtsss rktaerhltl
      121 agirsriemv vtrddvsrgk papdlyllaa erlslapqsc laiedstpgi saahaagiaa
      181 imvpdilqpt adtrqmcaav lpdlmavlal lrtqgflpgr vlqad
//
LOCUS       WP_284339239              78 aa            linear   BCT 25-DEC-2024
DEFINITION  GGDEF domain-containing protein, partial [Devosia nitrariae].
ACCESSION   WP_284339239
VERSION     WP_284339239.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 78)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 78)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 78)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         <1..78
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
     Region          <1..76
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 avllrgcdla dakrvgeaia sdicaipiql agrphvvsas igivslspgm dadtalvsad
       61 aacyaakntg rsrivvge
//
LOCUS       WP_284339300             174 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Devosia nitrariae].
ACCESSION   WP_284339300
VERSION     WP_284339300.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 174)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 174)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..174
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18383
     Region          <24..140
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mhrnafrlac aaalatlsaf atqadeaqva rgkylvnlgg chdchtpgyf lgqpdmsryl
       61 ggsdvgfeip glgmflgpnl tpdeatglgg wsdeevatal ttgkrpddrv lapimpyhay
      121 sqltdedvqa iveflrsipa vshevpgpfg pgetvptfim rtlppgetaa rapr
//
LOCUS       WP_284339364             325 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Devosia nitrariae].
ACCESSION   WP_284339364
VERSION     WP_284339364.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..325
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34313
     Region          19..309
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mkrilvtaas lacallampl aahaqyperd irvvvpwgag ggtdaiarkl tqiaedeigg
       61 tmyveniegg vsatgisqvm raptdgytig vltydsvvti pwqgllpsyd lenlklvarv
      121 tsepdalvid adagydtleq llaaakedpe gvrvavqnlg grthlallql qqlsdtqfqv
      181 isypggagpq keailsgeav gavtslgdfa nllqdgtvkg laefssapnp typdvplakd
      241 hgvdleigsf ivlavpagtp ddivaqiesa yqaayesqef qdwvsnvgvt pswlgtsevt
      301 qwaeetqqtl feemdalveq giltk
//
LOCUS       WP_284339373             296 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_284339373
VERSION     WP_284339373.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..296
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          <1..275
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 gqndafrypq gvkldqensr iflpklgwmr yrnsrqvtgv vknvtvsqsc gkwyisiqte
       61 sevstpvhps asmigldagv aklatlsdgt vfgpvnsfqk nqktlarlqr qlsrkvkfsn
      121 nwqkqkrkiq rlhsrianir rdylhkvttt vsknhamivi edlkvsnmsk saagtvsqpg
      181 rnvraksgln rsildqgwye mrrqleykql wrggqvlavp paytsqrcac cghtakenrl
      241 sqskfrcqvc gytanadvng arnilaagha vlacgemvqs grslkqepte miqata
//
LOCUS       WP_284339371             218 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Devosia nitrariae].
ACCESSION   WP_284339371
VERSION     WP_284339371.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..218
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24018
     Region          <12..204
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msvcdpilqq wrycrtasad atvlpdgcrd liirvtpdgr sslelcaldd rtrkvhltag
       61 ecliglrlrp gasvpasvlr qlrmefatgd dhermqmrll daihthvrln eepiaailet
      121 tsvraaarql gvsprtlhry lvsatgraps fwfdlararr alaglatqad lasiaflsgy
      181 adqahmtrsf rhrfghtpgr frknealmrl aahpglsg
//
LOCUS       WP_284339471             125 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Devosia nitrariae].
ACCESSION   WP_284339471
VERSION     WP_284339471.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..125
                     /product="YybH family protein"
                     /calculated_mol_wt=13762
     Region          7..120
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mftverpeaf netwarafnt reldhllaly edeailadat rtvrgkaeia fflgeflkvp
       61 gtlsgrnnfc lqlgdlallr adwvlrdpdg nqimsgssae iirrqpdgnw lyaidhaaga
      121 slpav
//
LOCUS       WP_284339472             124 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Devosia
            nitrariae].
ACCESSION   WP_284339472
VERSION     WP_284339472.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..124
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13730
     Region          17..104
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mlhwaqnyaf eepvarpatd cpvedwlafl ghrwnacilw hlsagakrys elarclpgvt
       61 pkvlterlea ledrglvtrs pqstfprsvi yalspegrrv veiigllepl aksshtprrv
      121 atgg
//
LOCUS       WP_284339490             787 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Devosia nitrariae].
ACCESSION   WP_284339490
VERSION     WP_284339490.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 787)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 787)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 787)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 787)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..787
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..787
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=83587
     Region          115..772
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mavwrtagsq iartavvalv iaavaaganf glfapldqal aqfrfagnsr ppsgevlfve
       61 idaasleaig vwpwprrvhg evldalmemg aaevvfdidf stasnsadda lfeaalarag
      121 gyaflaafqq fladgtlivn eplkrfarha savsvnvdgd gtgltrsipt vlagpdlpsi
      181 plalvptfgg egarifidys idlmqvprip vhrllagavd pslvagrqvv igagaielrd
      241 ffrvprfgvl pgplvqigav etakagrnls vpgawpalal agvagllyla fgarlslgrl
      301 amvavaasla ielaawaalg qaallvetlp fhatagalvl lalfeerarr wfesreqqar
      361 lawlaehdvv sgarsrhafl adldrqlave paaslmlvhl grleavnasl ghevadavaa
      421 qvvkrlgslf kilpariggd vfalnlpsgl ddahrsllpa rlrvmlgqpf evaghqvvis
      481 ptcgfsetsp gtpvgaaell rqaevaltta rqrhtgsavf apaqaqriad rrrldlalrr
      541 aldenqfhll fqpqmdlksg amvgvealvr wqspelglvs padfipvaee tgvivalgdw
      601 vmreacrqaa ewastvnisv nvssiqfrlg nvvgtvkral aesglaperl dieitesvfi
      661 dndetmrgtl eslralgvti alddfgtgys slsylsklpv drikidqafi rtlpdphnea
      721 ivesivlmar rlektvvaeg veteeqrayl agigvelvqg ylfgrpglpe aiglveraer
      781 stiavsa
//
LOCUS       WP_284339569             252 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Devosia nitrariae].
ACCESSION   WP_284339569
VERSION     WP_284339569.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..252
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27640
     Region          34..142
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 maqniyddaa ffegysqfpr sreglagape wpalrailpp vrgkrvldlg sgfgafcrwa
       61 veegaievtg vdlsrkmiaa ardrgpglpi hyieadletf epeadtydlv ysslavhyla
      121 dfgafcrkvr ralspdgrlv fsmehpifaa raepewmtda sgervfalrd yaregervtn
      181 wvvdgivkyh rkistvimtl lasgfaidam dewspdqval aanpaltdei vrpmllliaa
      241 rpvapatidp gp
//
LOCUS       WP_284339618             219 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Devosia nitrariae].
ACCESSION   WP_284339618
VERSION     WP_284339618.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..219
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=23397
     Region          <22..207
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mqanaltdrl nseaavarhl nallardprl ravneragpf pprsaprgfv glakiicgqq
       61 lsvasanaiw srfealpgal dpqtylglde stvratgfsa gkyrtvrvia eavvsgeldf
      121 tlveglaaee avayltahkg igpwtaeiyl mfcaghpdvf pagdlalqka vghafgldas
      181 psvkqlvsma ldwsphrata allfwryyaa irdregiil
//
LOCUS       WP_284339657             144 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Devosia nitrariae].
ACCESSION   WP_284339657
VERSION     WP_284339657.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..144
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15897
     Region          48..143
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 msdpfiemse aepelvdeie rkllaairss qkqalnssft lgmrdesgvl iaglaastay
       61 gwllikliwv deghrdkglg rrlmaeaeae girrgchgaw ldtsmpdsag fyvrlgyetf
      121 gtlenaagdv vpghrrwfmr krlv
//
LOCUS       WP_284339664             307 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Devosia nitrariae].
ACCESSION   WP_284339664
VERSION     WP_284339664.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..307
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33326
     Region          1..276
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
ORIGIN      
        1 mspsdlyiip fddwvnflvr dwlvpnfrpf fralqvpitl vlnwlddffa fvpmpittiv
       61 fallafkfag rwmalftivg fifidmidlw setmttlsmi itsvlfcaii gipvgilaar
      121 ndvvwkvtrp ildimqtips fvylvpivml fgvgmapgii atiifalppi irltnlgirn
      181 vradlieaae afgstawqml tevqfplalr timaglnqtl mlalsmvvia aligagglgl
      241 vvntglgrld vggataggvg ivilaiildr itqglgeqna vetvslratl aslfrlrpma
      301 detkkag
//
LOCUS       WP_284339763             455 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Devosia nitrariae].
ACCESSION   WP_284339763
VERSION     WP_284339763.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..455
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=48319
     Region          62..449
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mglvlalafg wpviaqtepq dqtsgqmspp veqgaqatgn gapaqetsag tadptadpdp
       61 epataeeaqa tleeiersit lsreradelr qeiadmegdr trqnaaliaa aqrvklaeie
      121 iddievrlde livselevrg rldgadteia nvlaalaris rspppalivd psdalgsarg
      181 allisallpq lqdkamaita dltrlteika kaqeeeqllr anfavleeeq lriatlilar
      241 krgveirneq laeeereala laeratslkd lieslsaran aagtpaedvp amseeairva
      301 lanaartepa vpfaqargwl arpangvtvv dygandgfgg iaqgvsittr aeaqvvapad
      361 gwvlykgpyl nygqivilnt gqnytallag letvtvdigq fvlmgepvgt mgsrtigrtv
      421 ttsagnsqpt lyielrrdne pidptgwwan eaqtt
//
LOCUS       WP_284339826             155 aa            linear   BCT 25-DEC-2024
DEFINITION  SRPBCC family protein [Devosia nitrariae].
ACCESSION   WP_284339826
VERSION     WP_284339826.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..155
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=17844
     Region          10..153
                     /region_name="SRPBCC_CalC_Aha1-like"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of Micromonospora echinospora CalC, human Aha1, and
                     related proteins; cd07814"
                     /db_xref="CDD:176856"
     Site            order(10,12,21..23,25..26,35,51,59,61,63,65,73,75..76,78,
                     81,87,89..90,103..104,106,108,120,122,124,132..140,
                     142..144,147)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mtsekieakv thhfrasper vydamtdpek arlwqeawmv qaglkgpivr femdvreggs
       61 ffysdmrdge eakhwgtflv lhrptkiqht wfvdeseedq lslvtiiiep apdgqgstvt
      121 lyhemnaewe eylerteqgw mkmllavegl leaeg
//
LOCUS       WP_284339828             116 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Devosia nitrariae].
ACCESSION   WP_284339828
VERSION     WP_284339828.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 116)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 116)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 116)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..116
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13131
     Region          7..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mraienpqld htlialadpt rrailrrlae gearvtdlaa pfaislnsvs khikllerae
       61 lverrregre hilrfrpepl taaqawiesq qtywtgrlra ldalltaegg kerede
//
LOCUS       WP_284339942             330 aa            linear   BCT 25-DEC-2024
DEFINITION  thioredoxin family protein [Devosia nitrariae].
ACCESSION   WP_284339942
VERSION     WP_284339942.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..330
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=34620
     Region          36..141
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
     Region          171..228
                     /region_name="TPR_19"
                     /note="Tetratricopeptide repeat; pfam14559"
                     /db_xref="CDD:434038"
     Region          192..219
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          240..329
                     /region_name="TPR_20"
                     /note="Tetratricopeptide repeat; pfam14561"
                     /db_xref="CDD:434039"
     Region          260..291
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          296..328
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
ORIGIN      
        1 mkgykepnda kakalsmtit lngspsqatq ppgdlvkdss drafkadvid asveapvlvd
       61 fwapwcgpcr qltpalekvv aekagkirlv kinidenpav agqlgiqsip avfafaggrp
      121 vdgfmgalpe sevrrfadrv iaaapapqps agsleeqiaa alaaadeals endlgraaqi
      181 fgmvlqqdpt hapaliglsr vylaagetdq aqatfdmipe darsgddyaa laaslkllte
      241 aaglsgaesl eariaanpdd hqarfdlavv lnsqgdrvga aealvglmkr drswnedgar
      301 kkllelfeaw gpkdpatikg rrllsaalfs
//
LOCUS       WP_284339947             117 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Devosia nitrariae].
ACCESSION   WP_284339947
VERSION     WP_284339947.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 117)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 117)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 117)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 117)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..117
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13237
     Region          2..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mteserldat ftaladptrr ailarlmesd asvmelaepf amsqpaiskh lkmleragli
       61 srgrdaqrrp chiegealke atgwleqyrn vwegnfrrld alledlqstr grpkrdn
//
LOCUS       WP_284339957             210 aa            linear   BCT 25-DEC-2024
DEFINITION  LolA family protein [Devosia nitrariae].
ACCESSION   WP_284339957
VERSION     WP_284339957.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Tajima,T., Yokota,N., Matsuyama,S. and Tokuda,H.
  TITLE     Genetic analyses of the in vivo function of LolA, a periplasmic
            chaperone involved in the outer membrane localization of
            Escherichia coli lipoproteins
  JOURNAL   FEBS Lett 439 (1-2), 51-54 (1998)
   PUBMED   9849875
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..210
                     /product="LolA family protein"
                     /calculated_mol_wt=23348
     Region          1..199
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mirrdalllg vsalfalaap glaqtvplta eeaqlirdis ahntairtma grflqidsng
       61 griegtffle rpdkvrfryn ppsreeivsv grgfyvlnra drtyyaypqd tiplrqflgd
      121 tidlfqanmv giaqsdgylt vtiidetvag tvevslvfdt etldlaqwsl vepngteltf
      181 slydveknve iprsffyida tytpidpanr
//
LOCUS       WP_284339994             807 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-glucosidase [Devosia nitrariae].
ACCESSION   WP_284339994
VERSION     WP_284339994.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 807)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 807)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 807)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 807)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 807)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12807938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..807
                     /product="beta-glucosidase"
                     /EC_number="3.2.1.21"
                     /GO_function="GO:0008422 - beta-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0030245 - cellulose catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=86433
     Region          1..>327
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          53..790
                     /region_name="PRK15098"
                     /note="beta-glucosidase BglX"
                     /db_xref="CDD:185053"
ORIGIN      
        1 mtleeqvsil sgedfwsvpa vprlgvgklr vtdgpngarg ggsliggvks asfpvgialg
       61 atwsvalvge igaaladevk skgahmllap tvnihrsvtn grnfecysed piltaelasa
      121 yvtglqgqwi aatikhfagn eseierttis seiderslre iylvaferav kvagtwgvms
      181 synklngtyt sehnwllttv lrnewgydgi vmsdwfgshs taetvnagld lempgrtrdr
      241 gdklvaavre gtvkaptvre ralnmlrlmd rtgaltdtrp faeraddrpe hrslirraga
      301 eaavllknnn vlpltgagki avigpnaria qimgggsaql nahyrvspwe glvaalgeaq
      361 lthapgctnh rfepllkgqf kveyfanetl sgepahvgeq edaqafwige vaegkvdplq
      421 fsarltgsyt akesgehrvg vhsagfakvy vdgrlvadaw tnwtkgrtff eegcdevvgv
      481 vvleagrsye itiefatkdf atlglaafav gigfplgdka iaeaarvaae aeiaivfigr
      541 ngewdtegsd lsgivlpgrq nelvaavaga nprtivvlqt ggpvempwld dvaavlqawy
      601 pgqeagnaia dvltgaaepg grlpqtfpvk wtdnptnsqd vevypgldgk vryeegvfvg
      661 yrhydkhgia plfpfgygls ytsfalsdla vddgqfeadg svtvsvtlan tgerpgvcvv
      721 qlyvtddias ldrphkelka fakaslkpge srrldlrlda rafafystsa rhwlveagdf
      781 tlrvgtssad lplsakvsrs ttlmlpv
//
LOCUS       WP_284340043             224 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Devosia nitrariae].
ACCESSION   WP_284340043
VERSION     WP_284340043.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 224)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..224
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=23949
     Region          <1..209
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 makksvaatp gsvlviglgr fggavadslv rlghevlaid edaaivqswa trlthvvqad
       61 ttnvdtlkrl gvgeferavv aigtdieasl mtvlalselr vpdiwakalg dkhgrllert
      121 gahhviypea amgervahlv tgqmidfief ddgfaivktr apkeslnrtl aesalrskyg
      181 vtvvgvkrpr tdftyarpet viqpgdlliv sgatnlverf aale
//
LOCUS       WP_284340068             391 aa            linear   BCT 25-DEC-2024
DEFINITION  lipid II:glycine glycyltransferase FemX [Devosia nitrariae].
ACCESSION   WP_284340068
VERSION     WP_284340068.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Rohrer,S. and Berger-Bachi,B.
  TITLE     FemABX peptidyl transferases: a link between branched-chain cell
            wall peptide formation and beta-lactam resistance in gram-positive
            cocci
  JOURNAL   Antimicrob Agents Chemother 47 (3), 837-846 (2003)
   PUBMED   12604510
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Hegde,S.S. and Shrader,T.E.
  TITLE     FemABX family members are novel nonribosomal peptidyltransferases
            and important pathogen-specific drug targets
  JOURNAL   J Biol Chem 276 (10), 6998-7003 (2001)
   PUBMED   11083873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006395
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..391
                     /product="lipid II:glycine glycyltransferase FemX"
                     /EC_number="2.3.2.-"
                     /calculated_mol_wt=43266
     Region          27..330
                     /region_name="FmhB"
                     /note="Lipid II:glycine glycyltransferase (Peptidoglycan
                     interpeptide bridge formation enzyme) [Cell
                     wall/membrane/envelope biogenesis]; COG2348"
                     /db_xref="CDD:441916"
ORIGIN      
        1 msaieeqtsp alpavaakda asalgltvei asgsawdaav adfdevcqeq lhafsatrwp
       61 gtvqepvlfr qggelvggal mmiqplplrl gaiavskwgp mlkdagrada eaihagmiel
      121 liadyararg mmlsvlpraa leadnrrhry lvergfrrgs ellypsryiv nlrlddaglr
      181 ksfaqkwryh lnksekegla fehadvarmd efhalysamt drkqfsdhsa ydtvdtlmtm
      241 kppnlrpelf fvrhesgiva gaiiftagdr avylygatsd ralplragyf lhwhvirwlr
      301 dntranwydl ggtdgyqglh qfkkgmvgea gvirpvppva nyadnpmall vgegafaard
      361 ayhqvqrtih awrnpkarpd qprsaengea r
//
LOCUS       WP_284340082             394 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Devosia nitrariae].
ACCESSION   WP_284340082
VERSION     WP_284340082.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616068
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..394
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=43017
     Region          159..295
                     /region_name="Methyltransf_32"
                     /note="Methyltransferase domain; pfam13679"
                     /db_xref="CDD:379330"
ORIGIN      
        1 mtpvaeerta afldtlgeaf rdgslirlkl ggyhgsdeal ksaegrkval kggdklsivw
       61 ryktrditkn ygvdeavall rawladdfrs arlsttgfdl sferngdkvr lkretvegra
      121 tasgahdrak drpvvaekpw lnalgltdtq gnvlnaaqdk frqinrmvei fapliqaipk
      181 erltrivdmg agkgyltfal ydhlatalgl evemvgvevr kslvelcngi aaengfsrlr
      241 fvegsildyd aagasavial hacdtatdda isrgiaagae liavapcchk qirremeagk
      301 aaddldfllr hgvflerqae mvtdglralm lelssyrtrv fefvpdahtp knvlivaqkd
      361 rragrdreav lgkiaatkar fgigrhqlet llgl
//
LOCUS       WP_284340102             366 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Devosia nitrariae].
ACCESSION   WP_284340102
VERSION     WP_284340102.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 366)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..366
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37382
     Region          43..361
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 maqaslitqg ilergrpegd rtglgqlavf llalllaivm vvsmttgasg asawrvlaha
       61 fgfvplegte avrdqvvvln irlprmilgv ligaglavsg lvmqglfrnp ladpglvgvs
      121 sgaglgavgi ivlgttmlap ltallgiyal qiasfiggli ttfilyrvat rsgqtaiatm
      181 llagiaigal agavtgvlvy maddnqlrdl tfwglgslsg snwtkvmssg piilaaliga
      241 gflakglnam tlgeataahl glsvqpfkrw aivivaaatg asvavsggig fvgivvphll
      301 rlvigpdhry llpasallga sfllladavs rtivapaelp igivtafvgg pfflwillrr
      361 rsqlaw
//
LOCUS       WP_284340160             329 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel beta subunit family protein [Devosia nitrariae].
ACCESSION   WP_284340160
VERSION     WP_284340160.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442711
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..329
                     /product="potassium channel beta subunit family protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:0008076 - voltage-gated potassium
                     channel complex [Evidence IEA]"
                     /GO_function="GO:0015459 - potassium channel regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36830
     Region          1..318
                     /region_name="AKR_AKR6C1_2"
                     /note="AKR6C family of aldo-keto reductase (AKR); cd19143"
                     /db_xref="CDD:381369"
     Site            order(19..21,27,49,54,82,122,152..153,178,207..212,216,
                     218,226..228,268,285..289,293,296..297)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381369"
     Site            order(49,54,82,122)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381369"
ORIGIN      
        1 meyrrlgksg lkvsefslgs wvtfgkqvdq kdamdimtla ydeginffdn aegyergvse
       61 tlmgealkkl awgrdtyavs skvfwggdkp tqrglsrkhv tdachaalkr lqvdyldlyf
      121 chrpdvdtpv eetvwamhnl itqgkilywg tsewnaqqlt eayavarslg isppvmeqpq
      181 ynlfvrqkve gdylplydlm glgttiwspl asgvltgkyn dgipadsrln lpgyewlkkq
      241 weseegkakl ekvkqlaala seiglpihhl allwclvtpn vstvilgask ksqlednlsa
      301 leskdkltpd vlerieqimg nkpegpkrf
//
LOCUS       WP_284340240             429 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Devosia nitrariae].
ACCESSION   WP_284340240
VERSION     WP_284340240.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..429
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=46399
     Region          175..408
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 magtsgafap laatragqlg ravlrartas lldsvvafwi faggiilfep slyefafilv
       61 lvlavaagms iysstmplla ltvifagfam igafqvrytg ltqaflfvav tvflfltscf
      121 lanyvgeaph rrmavirray iaigvvsagv gtlaylglvp naefflrfdr akgmfkdpnv
      181 fgpflilpam fllrdvffgh rrallfaaaa flvvmvgvfv sfsraawghf aasgllvfgl
      241 sffleahard kvrmiilalv glmviliala glvsipevga lfeqrasatq eydtgetgrf
      301 grqgyafela lahpwglgpt efenlliseq phntyvtvlq aygwgggicy yllvlatlwr
      361 gisglrdpak rallipviav yiplaiqsgl idtdhwrhyf lvvgliwgit vnanpkgrmg
      421 alertgatf
//
LOCUS       WP_284340262             252 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Devosia
            nitrariae].
ACCESSION   WP_284340262
VERSION     WP_284340262.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..252
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27917
     Region          4..250
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 maypiayqly ssrnfpplaa qfpilkqmgy daiepwlpay eadpalfrrq lddaglacyg
       61 fhmplsglvd eperfidial tlgatlmipp yipveerett safwqrlgek largaqkaqp
      121 hdlkvawhnh dfeylalpdg srpidhilet ggdtvwfeid cgwitragad paaeltrygd
      181 riaaiqtkdt appgtaaddg wtatgdgiid wetlvplfkq taadhivaeh dnpsdwqrfa
      241 grsieklral gl
//
LOCUS       WP_284340303              77 aa            linear   BCT 25-DEC-2024
DEFINITION  GGDEF domain-containing protein, partial [Devosia nitrariae].
ACCESSION   WP_284340303
VERSION     WP_284340303.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 77)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 77)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 77)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         <1..77
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
     Region          <1..77
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 avllrgcdla dakrvgeaia sdicaipiql agrphvvsas igivslspgm dadtalvsad
       61 aacyaakntg rsrivva
//
LOCUS       WP_284340399             402 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Devosia nitrariae].
ACCESSION   WP_284340399
VERSION     WP_284340399.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 402)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 402)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 402)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..402
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=43297
     Region          56..390
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mkilgfpwti rtrltllyag afllagvali afiylflgqv leqqfmirta pgappleetp
       61 galdqtrrvv dimirrarvd tlqtmliasg vfvavltiaa giigwlvagq alqplrnitl
      121 tarrvadrsl herialagpn deikdladtl damlerldra fdsqrrfvan ashelrtplt
      181 itrtlieval meakanasvr qlgttllavn erherlidgl ltlagseega agrhpldlce
      241 vaahvvneqv tiadkvgvrl dadvrpapml gdgfllerlv qnlvenaiqy nlaeggwvri
      301 atgmedgqat lrvensgpqv psyeiaslfe pfrrlksser laepgrrait rgaglglsiv
      361 rsvarthgge veavartegg lavtvrlpaa gdvgddvisp gt
//
LOCUS       WP_284340393             223 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Devosia nitrariae].
ACCESSION   WP_284340393
VERSION     WP_284340393.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..223
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23501
     Region          10..213
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mqwsprspge rvlmalkmhg avsaailgrm lgttgeaarq qlarlaedgl vaatseargv
       61 grptqywslt aagearfpdt haaltvqlla ivredlgeea ldriiavrea rtatayraam
      121 egtaslrdrv aalaklraqe gymadwweea dgtlmlvenh cpicaaaiac qgfcraelev
      181 fqsvlgpdaa vsrsehivag arrcayvvrs aaaltapgav taa
//
LOCUS       WP_284340483             337 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Devosia nitrariae].
ACCESSION   WP_284340483
VERSION     WP_284340483.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..337
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=35475
     Region          10..326
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mfstritraf gldtpivnag mamiarpala aavsnagglg tigcdinppe vlramvretq
       61 iytgrpfgvd ligdfvtdah igvlieekvr laiffwtlpn qeqvdrlksa giaiwmqvgg
      121 vaeaeaaval gvdalivqgs eagghnrsea stmvlfprlr raypdlplia sggiaegstm
      181 aaalalgada vwcgtrflas reahahdlfk kavveadvgd trittiygpe wpdqamraiv
      241 ndglqraegr eaeaigeaqg vmvgttllng eripvprysa ilptrefegd ieqvcltagq
      301 ssgniddlpt ageivarmdr eataaidrvs sllgepa
//
LOCUS       WP_284340518             834 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-mannosidase [Devosia nitrariae].
ACCESSION   WP_284340518
VERSION     WP_284340518.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 834)
  AUTHORS   Nascimento,A.S., Muniz,J.R., Aparicio,R., Golubev,A.M. and
            Polikarpov,I.
  TITLE     Insights into the structure and function of fungal
            beta-mannosidases from glycoside hydrolase family 2 based on
            multiple crystal structures of the Trichoderma harzianum enzyme
  JOURNAL   FEBS J 281 (18), 4165-4178 (2014)
   PUBMED   24975648
REFERENCE   4  (residues 1 to 834)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 834)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14312040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..834
                     /product="beta-mannosidase"
                     /EC_number="3.2.1.25"
                     /GO_function="GO:0004567 - beta-mannosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005537 - D-mannose binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=94154
     Region          24..>641
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          754..831
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; pfam17753"
                     /db_xref="CDD:465483"
ORIGIN      
        1 mtysaldlsg tfdlsspekd vrtsialpgd vhtallaaei ipdpyfgene kavmwvnrtp
       61 wtversftas aadidayltl tlseidciat vrlngeaild adnafvrydi dvtgkvrege
      121 nhlkiefavt rdiararaea hpfpipftkn yqtnglegvh mnfvrkaach agwdwgiclm
      181 ptgvygtmsl rksrlarqes vevaqahgkn sveltiktrl fafahgevel qheidgqtit
      241 dkvvvtkgen vfthnvtige prlwwpagqg eqplyelvts legevtrrki glrklewvve
      301 pdeidhtfkc ringrditmm ganwipadai psritpavvr dllesakaan mnmlriwggg
      361 qyepdffyel cdelglllwh dfmfacmsyp sdrkfldsvr neitqqvrrl shhasialwc
      421 gdnevigsls wypetraape ryvanydrln smlgnivede dpdrrfwpss psmgyldfsd
      481 gwhadtrgdt hywdvwhsak sfeayrtvnp rfasefgfqs ftsmnivetf aeekdrnpss
      541 pvmenhqrnd ggnariletm cryfrfpknf eqmvflsqvq qglaiktaie hwrstkprcm
      601 gtlfwqindi wpvaswssld yggqwkllhy makrfylpvn vvavpreaev rtnsrglave
      661 smpteivlka vndtaekqei ylevqavrig ggartlfegk akigpdaake veaikarkle
      721 adeflffswt dedgnllgen dyfpkpykay elarptitta wsqvgetpvl tletdkpalf
      781 vtatvdvpgy fsdnavtllp grktvltftp rlgtrvsade larslkvsgl sqtf
//
LOCUS       WP_284340565             509 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Devosia nitrariae].
ACCESSION   WP_284340565
VERSION     WP_284340565.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 509)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 509)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 509)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..509
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55661
     Region          153..486
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mpsrpaihtn dvraqmgrdv rrniqktvld arqrltsssg trasfdyelm qaytgsriga
       61 alplsaivvi lavvasfwvp fvftavwagm vllsllaval mcrrfqhtea akfnaehwtt
      121 nfvaaetvyg itwsliplfg lltqadalav vtfamvlvsi asnavatrtl tpatvmstlp
      181 atltvsinlv smggtlnytl gaivlcaeif fvylarqlha selerishqa ekdsliaele
      241 eaqhmsdear rhaeqaniak sqflatmshe lrtplnaiig fsevlksell gphhvpqyke
      301 yagdihgsgq hllnlinell dlsrieagky elneevvsli diaedcrrmm elrakakgid
      361 ltfsygknlp klwgderair qvvlnllsna ikftpqggkv tlvinrsadg gqlisvkdng
      421 pgipeeeiet vlssfgqgsl aqktaeqgag lglpivqkim dlhqgrfdlf skvrfgtevi
      481 asfprarvmd alapvverrn rlqifseag
//
LOCUS       WP_284340595             107 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Devosia nitrariae].
ACCESSION   WP_284340595
VERSION     WP_284340595.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 107)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 107)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 107)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..107
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11510
     Region          2..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mqdddlaaam ralghpvrls ilrilaaqqq qdqcccthvt eclplaqstv sqhikvllea
       61 gliecrpkgt rncylprydr leaigagygg llagltaklr pnetepa
//
LOCUS       WP_284340712             309 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Devosia nitrariae].
ACCESSION   WP_284340712
VERSION     WP_284340712.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 309)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 309)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 309)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..309
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35034
     Region          10..309
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mrlrlsdyfq tlsedlrrdw qlylllapmm iwflvflykp mhglqiafkd fsifrgieas
       61 pwvgfehfga lfadamfira fwntitisfl glifafpvpi llalmfnevq nalakrwaqt
      121 ivylphfisv vivagivinf lspstgivnt vlgwfgiapi yfltqpewfr pvfigssiwk
      181 eagfdsivyl aaiagvsptl yesarvdgas rwqmvwritl pcilptiiim liirignlve
      241 vgfeyiilly rpstyqtadv vstfiyrtgl qgtqydlata aglfnaviaf vlvytanris
      301 rkvsstslw
//
LOCUS       WP_284340796             139 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Devosia nitrariae].
ACCESSION   WP_284340796
VERSION     WP_284340796.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..139
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15259
     Region          3..139
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mlvhsrqvei efgdcdpagi vyypnyfrmf dastahlfea alrmkkiawt rhyqivgipm
       61 vdtgakfvkp srfgdvvtie srvtefrrss fsvahqlyna gdlaieahev rvwaaadpan
      121 pggiksaaip etviaafsa
//
LOCUS       WP_284340818             319 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Devosia
            nitrariae].
ACCESSION   WP_284340818
VERSION     WP_284340818.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..319
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35758
     Region          27..286
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mpirnsillg tlgryadrfh eyqksrslae rleiakripr thgvepvypq dlghhgehvq
       61 tvkdsglais avnvnlkged ifrngsftnp daairrrsvd ylktamdmaa dfgadmlsvc
      121 plidgwdyaf qveydkqwqw laecfreata yrpdvrisie ykayevrnri vlpnmgrtlh
      181 fcdvvgadnl gvtmdvghal iagetpaaei ciahaagrlf yihfndndrg adwdmlpasv
      241 nfwetlealy yvrklgwdgw aaydvftrsg dnaeavaatf eimenldkli drigfdtlkg
      301 lsqegipara fnsmigall
//
LOCUS       WP_284340869             115 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Devosia nitrariae].
ACCESSION   WP_284340869
VERSION     WP_284340869.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..115
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12874
     Region          3..88
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 maldqlsatf aalsdptrra ilarllegea svaelaepfq mttravskhi gvleaaglvt
       61 rgrdaqrrps riraeplvdv dmwlqgyrrl wisrfqqlde rlaklqmegr tgdre
//
LOCUS       WP_284340989             437 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Devosia nitrariae].
ACCESSION   WP_284340989
VERSION     WP_284340989.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 437)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..437
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47990
     Region          28..432
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(143,145,284,286,319..321,365)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mhryvvrgfv taaavvatta lasaqdvelv qwqtnlrppd iegitaltnr fmelhpdiri
       61 qiestpwdth pqkilaafna gsglpdvgri gnlaqaaavg yvqpldeyid qawrdsifdv
      121 awadaefsvd gqqpahiwgv pkmlatevwf ynktmfdaag ldpesapqsv eefkdiacql
      181 tldtdgdgrv dqwgvnltag aeggpvrqyt maahsfggrl vegsyvdsqi gdeitwnseg
      241 tvegfnwlks mydegcspps tisdtvrdva nnfragrvam afmgpwelel tkqtfeengw
      301 efglmrfpeg pggrgefayv galgmfsqtq hpeevieylk fytsaeglal ymhvngmipa
      361 nkealadpfy sedpyyatll etinsadlpa pkwlglrgag tlmdtiwtpl yqrmlageis
      421 vedgvkemhd slaasiq
//
LOCUS       WP_284341006             788 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Devosia nitrariae].
ACCESSION   WP_284341006
VERSION     WP_284341006.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 788)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..788
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..788
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=84709
     Region          1..351
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
     Region          368..776
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mpgaldhlwv vdlsdtlagq ycarlfadfg atvvlveppa gspvrrlapf seqgdslqff
       61 hlntgkrsvv idratgegss rfeallatad vvvlppngda aaverlnpac vvvvpsnfgs
      121 dgpradwqgp elvlqalsgm mhnngaagre plygtgnraa lasgvgayvg altalyarkt
      181 tnrgqvvrvd aaetaaamcf pyvmqyiyng tvrqrteqai qagqvlcrdg wvciwiynfr
      241 whalvnalgl pelehdprfa dpgdrrvnwd alfailqtrv admmaedlve ilqraqviaa
      301 kayrpselig srhlaarnyw eeingrtalg ppfrlsavpr tlsrgapepg eagdlaappa
      361 rrspparpaa dmplsdirii elttawagpm sgrvlayfga ecihveapnr vnswrlnkdr
      421 pnpvnfpdgq pgarwydrsf lfnsqnvnkl scilnlktee gratlrrlva vadvvvcnfr
      481 pgtlkklgld yesltaikpd iivaelpafg adgpmsgyaa lgptmemaag msamigypgg
      541 qpevtgpsyl dpiggfnaaa ailtaliyrq rtgqgqyvev pqveaamqli gaeilkaget
      601 gidpapsgnr vphavphdaf ptrghdqwva iaaldeaqwr nlckvmnrpd liedprfasv
      661 drrldnqdal tiivsdwtrs qdkheiadal qaagvpaapv qtpkdlaedp ylahrgffte
      721 lehpdagrhp hpglpidlsa tpgaqvraap pfgghnrhvl egilglsvde iatieagpam
      781 atrplega
//
LOCUS       WP_284341009             145 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Devosia nitrariae].
ACCESSION   WP_284341009
VERSION     WP_284341009.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..145
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16312
     Region          11..145
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mdrrpagrrq dyrwfsvitl rwndidvfgh annaqfyeff dttvvrflhe grglgiakgg
       61 tsmvvaengc rflkeivftd rlemglrver igtssvrygl aafvndedaa aadghfvhvf
      121 ldpvskrpap lsakvrehle tilvq
//
LOCUS       WP_284341029             627 aa            linear   BCT 25-DEC-2024
DEFINITION  ABCB family ABC transporter ATP-binding protein/permease [Devosia
            nitrariae].
ACCESSION   WP_284341029
VERSION     WP_284341029.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 627)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..627
                     /product="ABCB family ABC transporter ATP-binding
                     protein/permease"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69314
     Region          1..609
                     /region_name="ATM1"
                     /note="ABC-type transport system involved in Fe-S cluster
                     assembly, permease and ATPase components
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5265"
                     /db_xref="CDD:444078"
ORIGIN      
        1 mesrptvsae eggllstvrn lwgymwpaar pdlklrvvla igallvskaa ttlipfaykg
       61 vidsldgttp enavvlgiav pivlviafgi gnivdagfqq lrdvlfasvg qhavrklayr
      121 tfqhmhrlsl rfhlsrrtgg lsrviergtk gietivrftm lntaptlvef vivaivfivm
      181 fgvsylgvlv atiwaylyft ikasnwriai rrdmnesdtd anskaidsll nfetvkyfan
      241 eemeaerfdr smaryersai riwtslgfln fgqaaifwgg livisvmavn gvmsgtltlg
      301 dfvllntflm qiyrplnfig fvyreirqgl tdieemfkll dqnpeiedkp garpitisgp
      361 vvrfedvhfh ydpdrqilrg idfevpagkt vavvgpsgag kstisrllyr fydvtggsit
      421 idgqdvrevt qaslraaigm vpqdtvlfnd tiaynirygr pdatedevre aarmaqvagf
      481 ierlpkgyet evgerglkls ggekqrvaia rtilkspail ildeatsald tkterdiqsa
      541 ldavsanrtt vviahrlstv inadeilvlr dgqiaergrh eellalggly aqmwsrqrea
      601 seaeeqlrra aeedpdgfik rgaaaae
//
LOCUS       WP_284341032             112 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Devosia nitrariae].
ACCESSION   WP_284341032
VERSION     WP_284341032.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 112)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 112)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 112)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..112
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12652
     Region          3..88
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mgqhsqsldg ifqaladptr ravlkrlgeg sasitdlarp fdmalpsfmk hirflegsgl
       61 irtrkegrvr tcsinrqqfr aieawlteqh aiwegrtdrl erfvtaqake ks
//
LOCUS       WP_284341052             416 aa            linear   BCT 25-DEC-2024
DEFINITION  cytochrome b [Devosia nitrariae].
ACCESSION   WP_284341052
VERSION     WP_284341052.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Tolkatchev,D., Yu,L. and Yu,C.A.
  TITLE     Potential induced redox reactions in mitochondrial and bacterial
            cytochrome b-c1 complexes
  JOURNAL   J Biol Chem 271 (21), 12356-12363 (1996)
   PUBMED   8647838
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Howell,N.
  TITLE     Evolutionary conservation of protein regions in the protonmotive
            cytochrome b and their possible roles in redox catalysis
  JOURNAL   J Mol Evol 29 (2), 157-169 (1989)
   PUBMED   2509716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..416
                     /product="cytochrome b"
                     /GO_function="GO:0008121 - ubiquinol-cytochrome-c
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=47015
     Region          5..403
                     /region_name="QcrB/PetB"
                     /note="Cytochrome b subunit of the bc complex [Energy
                     production and conversion]; COG1290"
                     /db_xref="CDD:440901"
ORIGIN      
        1 msehstynpa ngvekwlddr lpvvrftkeh lmdfptpknl nywwtfgail amclgvqivt
       61 giilamhytp nvemafdsve hirrnvnagr elqavhsvga smfffavyvh ifrglyfgsy
      121 kapreilwil gvtifilmma tafmgyvlpw gqmsfwgatv itnifsaipi vgdpilqllr
      181 ggfavdnptl nrffslhyll pfiiaalvvl hiwalhvpgn nnpigvevks srdtvpfhpy
      241 ytmkdafamv vflipfawfv ffapdilghp dnyiqansqv tpthivpewy llpfytilra
      301 idfnvlfids klggviamgg allillvlpw ldrspvrsgn frpmfrwfyw lfvlnfitlt
      361 ylgaqpaegt yvliakicva yyfayfiiil pvlarievpk plpasisesv lgkana
//
LOCUS       WP_284341064             297 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Devosia nitrariae].
ACCESSION   WP_284341064
VERSION     WP_284341064.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..297
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32855
     Region          2..269
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mttlahisdi hlaplprvrp rdlagkritg ylnwkltrks vlsgeslktl idhlqtqnad
       61 fiavtgdmvn lalteeitra rewlktlgpa dricvspgnh dayvhgalek alnhwgdyit
      121 getlekntrf pfvrrvgdva viacssavpt apflavgefg rdqaarlagi lkvtreagyf
      181 rvvmihhppn velqhpsfgl rghklfrdiv eregcelvlh ghthrssihs ihgpegevpv
      241 igvaaasaaq ggrlddpary nlfriernga gwactmrefg fqrlgndivm rlqmriy
//
LOCUS       WP_284341119             533 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Devosia
            nitrariae].
ACCESSION   WP_284341119
VERSION     WP_284341119.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..533
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55698
     Region          20..516
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mkrllagata ltmmtsaaya dftlnilhin dfhsrfdpit gtdsncdaet daagecfggi
       61 arlkaiidtr rdeistgggn slllsagdnf qgslyyttyk skvvsdffnq mgfdvvatgn
      121 hefddgpeef ltfieaaqfp iiggnfdvsr spelrgking sivvevgger igiigatted
      181 tpeiaasgpd iefyevaqyv rgaaealeaa ginkiillsh igynedmava aavpgvdviv
      241 gghshtllsn taegaagpyp tmvtnpagie vavvqanqyg kylgdltvtw dddgnvvsae
      301 gepylidasv egnadfasql aelsgpieet maevigtate aiegsrevcr amecsmgnlv
      361 adamldrvad qgvtiaiqng gglrasidag eitmgevltv lpfsntlatv eisggaviea
      421 lengvsdven gagrfpqvag lkysfdlsqp pgsrisdvev meggawapid eeatygvvtn
      481 nfmrgggdgy epfanggnpy dfgppleqvl adyiaeagge ytpytdgrit ave
//
LOCUS       WP_284341236             280 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Devosia
            nitrariae].
ACCESSION   WP_284341236
VERSION     WP_284341236.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..280
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30988
     Region          2..271
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkiavtgasg gigraivaea errghgivgi draehpdvaa ndkrrfilag menyetlvda
       61 lagcdavihm aaipspgrhp dhvvhnnnvv gsynilqaaa engikricqa ssvnaighsy
      121 srkprydyfp idekhpnyse dpyslskwic eqqadsfvrr ypdmviasmr fhfvcddksi
      181 alrylgphsd atkhlwaytr rdaaadacll slqapftghe vfyivapdtt sdtpsrelaa
      241 qhlpevpled gwnahrsffd sskaermlgw khgnvdprrl
//
LOCUS       WP_284341248             659 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Devosia nitrariae].
ACCESSION   WP_284341248
VERSION     WP_284341248.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13939702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..659
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=70014
     Region          <107..>209
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     Region          198..510
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
     Region          472..655
                     /region_name="DUF3520"
                     /note="Domain of unknown function (DUF3520); pfam12034"
                     /db_xref="CDD:432277"
ORIGIN      
        1 mnnepfaalg kldvpapdag akaralaagt aafevareeq akkmqraakg kswrerlksi
       61 vptfqgnwim dmrlpvataa mallllplgy qlltttsmtp ttipqqaaap tapepvetre
      121 ealadadtae mpvsapamta nraktavtaq sgaaapaqdi eaipspapma pslmatgvia
      181 pspaeasgda ftrfneqpvk avaeapvstf svdvdtasys yvrrmleegq vpqpdavrie
      241 eminyfpygy peadsaeapf aptvalyptp wnpatrllhi gikgyeppat edkpsnlvfl
      301 idtsgsmdsp dklpllkraf rllveqltdn dtisivtyag sagvalepts arekakilsa
      361 ldslwsggst agaegielay rlaeeakveg ginrvilatd gdfnvgisdp deledyikak
      421 rdsgvflsvl gfgtgnlgdd tmqslaqngn gqasyisnfr eaqkvlveei ggtletiakd
      481 vkiqvefnpa liseyrlvgy etralnredf nndkvdagdi gaghtvtaiy evtptgsega
      541 lidplrygsa etttsgasne yaflrmrykl pdgdvsqlie tpvtaevtye tmdevpadmr
      601 faaavaafgq klrgsdyagd mswqairsla qsgrgaddag yraefvglvd laaslkpdr
//
LOCUS       WP_284341313             119 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Devosia nitrariae].
ACCESSION   WP_284341313
VERSION     WP_284341313.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..119
                     /product="YybH family protein"
                     /calculated_mol_wt=12548
     Region          20..117
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mqrtgpalsp gnlsrlllta lnnadveaiv slytenavlv lpdgetargh geirsfyakl
       61 crdrpqfppg kqsaplingr valtstvlan gtvtaevaaq qedgtwlwai dhpfigpat
//
LOCUS       WP_284341448             247 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Devosia nitrariae].
ACCESSION   WP_284341448
VERSION     WP_284341448.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..247
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27366
     Region          33..239
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mqprlvretl asrrepayid vmiiddsdia lkpfeavifd mdgtildtes vfrtivfevc
       61 eelgfemtdn vhlsmvgssh ektnqlliea ygvsfpyalf dekcrfsmrn rihdvpvkag
      121 areilselre rgiptavats srrahvdlhl tkagligmfd aivtrddvin pkpnpepylt
      181 aaarlgiepv eclaledsys gvraahaagm qtvmvpdlvh pseeiralgi aimeslhhvr
      241 raafpvr
//
LOCUS       WP_284341602             138 aa            linear   BCT 25-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Devosia nitrariae].
ACCESSION   WP_284341602
VERSION     WP_284341602.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..138
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=13845
     Region          3..135
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mktireldls darkllegar aleigvpmci aiadsagnll afermdggki tsiviaidka
       61 ftaaaarkat heygeasqpg spayginsai ggrlmivggg lpvqvdgevv gavgvssgtp
      121 lqdravaqaa ldhfsaag
//
LOCUS       WP_284341609             499 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Devosia nitrariae].
ACCESSION   WP_284341609
VERSION     WP_284341609.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 499)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 499)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..499
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=53799
     Region          8..490
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mpnppaplfr yqpillalgf allvgvagis mwlvqqtrsd aeqaihalei keqlaslqgl
       61 vwraeshqrs lllsgepsyg rafrddaeav rlalseleaa sagsadpers sllarlstai
      121 daelaslegd aargrltvpa alpaetnant aqalspteev raliaqllqq eqhlltgemq
      181 asnertrlll iaslagatii avlaagsiam vhrstaqlla aqgalrqtne sleetvarrt
      241 aelrqaneei qnfayvvshd lraplvnimg ftgeleairk dllerrhvgv aghdatsape
      301 dqlgrdfdea lhfiktsigr mdrliksilk ltregrrefr lepidmtgsv rsiadglgyq
      361 ahavgasiei eelpplvgdr laieqifgnl ldnalkylrq dvpgrivvsg lttasgliye
      421 vrdngrgiea kdqarifeif rrsgaqdqpg egiglthvrt lvsrlggtit vqsqpgqgsi
      481 frvtlpsrqp assgepvhe
//
LOCUS       WP_284341628             402 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Devosia nitrariae].
ACCESSION   WP_284341628
VERSION     WP_284341628.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 402)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 402)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..402
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42093
     Region          5..396
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mntasaawrt lailvvavil pmttwfsata vlpqlteywa lssdmrtwmt ngvqlgfvvg
       61 alslslvslp diaplrllma iaaalagvan lgllvapspe wavgcriltg valagvyppa
      121 lklvatwfqr grglamgali ggltfgsavp hllralsqgv swsyvvvgss vltfigaiif
      181 llraregpyp fsravfdprq igrvlrnrgv alanlgyfgh mwelyamwgw flafagagfg
      241 ggmlsasqls llvfaviatg vlgcllggvl adrigrtatt almmitsgac alliglvftg
      301 pfwlfvvval iwgisvigds aqfsamttev gdsdlvgtal afqlgigfal tmvsltlvpi
      361 iadavgwrwa flvlvpgpll gtaamlvlrv lpesariaqg rr
//
LOCUS       WP_284341773             417 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Devosia nitrariae].
ACCESSION   WP_284341773
VERSION     WP_284341773.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 417)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..417
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45138
     Region          31..411
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(137,139,267,269,301..303,344)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrrsktlava lplvaaglta mmtttafaqn lsmwvresaa dpgqlmvdlw nqtheaqiel
       61 taipdnqlvt klatsvragd apdlisfdli ympdfmragf ladltdqlss dpnyethvea
      121 ykdiatyedr iygvgftpdv silvwnkelf reagldpdvp pktiyeihem atqigalgdd
      181 tygfyfagsc pgcnifvtsp lmvaggahil prngedaale geavrvvlde yrmmweegli
      241 pesaevdage nfvsaftagn igiagsggfl lslmerqfpe fdygvgllpg leegqvsafv
      301 ggdvvaiptg ganeevaref vtwvlsdeaq leglaknail ttrtdladne yfagnekvqk
      361 taealavgyv pwvfhfadmv nsdsspwinm lqqaifdgdv dgaieearar mlqiase
//
LOCUS       WP_284341792             127 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Devosia nitrariae].
ACCESSION   WP_284341792
VERSION     WP_284341792.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 127)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007442
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..127
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13435
     Region          17..116
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
ORIGIN      
        1 mltmlapfss haqeltgdpa ngetvfrkcm schrvgpdar nmvgpalngv vgrqagsvad
       61 fnysdamkns gitwdaasld eflaaprevv qgtkmvfpgl pdaqdrtdvi aylaqfdeeg
      121 nmtapaq
//
LOCUS       WP_284341823             161 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Devosia
            nitrariae].
ACCESSION   WP_284341823
VERSION     WP_284341823.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..161
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17124
     Region          2..90
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mdqrsgcpin lsvevlgdrw slvvlrdiif gnfrtyseih gnslegiatn ilaarlkhlt
       61 qegfltaaad pghkqrtiys ltdkaialvp alaalgawga rylpaspdla aranaldagg
      121 pqmwadlvde lrhlhlgapa prrsvlaeln aayghvverg g
//
LOCUS       WP_284341915             423 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Devosia nitrariae].
ACCESSION   WP_284341915
VERSION     WP_284341915.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 423)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..423
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45968
     Region          29..412
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(132,134,261,263,299..301,343)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mkrsspfaal vlvavsgqvl aqetvlryms wdpaqleieg paieefetah nvtvetqalp
       61 pddywprlsa laaagdlpdv famssgfvae waeagnlanl geqmegvdln ayygaaieag
      121 mvdgepyafp qnwvapvlyy nkdafdaagv dypsddwtwd dflnaakalt idengdgepe
      181 qwgyyfygry ahtdgwifrn ggrlinaeet aleptqeavn aleflvglvs ehtvapqpqs
      241 legvrqqdvf plgmaamwvd gtwnidntrq vagdsfawgi apipmgpdat petavtyawa
      301 dmmsiaetse qkdlawqfiq hmvgegrtpa dfpggkvpay kaiaeteswl eeglqpdnkg
      361 lilelgaqpt ytgfsknwsa wrgyaaagsg gmngeidevl ngrksldeai dafvaygndv
      421 lsr
//
LOCUS       WP_284341921             110 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Devosia nitrariae].
ACCESSION   WP_284341921
VERSION     WP_284341921.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 110)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 110)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..110
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12446
     Region          2..83
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdvftaladp trrrmlellv gsakpagafa eafpdvrqpt lshhlkvlrq aglvqveada
       61 qrriyslrte plreigdwla rnrlywrnel dalenhldtm peagepsner
//
LOCUS       WP_284342094             648 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Devosia nitrariae].
ACCESSION   WP_284342094
VERSION     WP_284342094.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..648
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72051
     Region          1..472
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mylsdvsikn frvltdfrvr lnpsinlivg ennsgksalv davryalsvn sgewiriqdr
       61 dfsrgatsfs iqlkfedita rqaaafvehl thetipgted rrsvlylnyq aeqtthlirg
      121 arqirtelrs ganaegpsve reardflatt ylrplrdada elmggrgsrl aqilgssdrf
      181 geaavienll ttivaanaai iendgvsatr erieeqlrrl dfrtkplspl isimggtdle
      241 qldaterkqm frailerlql lidsqeryqg lgysnllfma aelllleqeq hdfpllliee
      301 peahlhpqlq mkflralreg fggqnsslqs iltthspnla skaplenvii maegkafslr
      361 kdetrldaqn yvhlekfldv tksnlffakg vmivegdgen illstfadll gtpfedfgvs
      421 vvnvgsiafa pfarifqrag mddpansaaw lgtrvvclrd ldlwpepari segniygflq
      481 tklgnqqywe shyadnaqgr lnwvesrksl sgqnvrvevs dhwtfeyall raglaaevyq
      541 alkgtlegyd elpadpelra vaiykdiatq sgaktklaya lssvlmeefg piitpapene
      601 mpeqadarrq adqaqtaerr avfraalpvy ivraidyvtg heapaaaa
//
LOCUS       WP_284342097             464 aa            linear   BCT 25-DEC-2024
DEFINITION  B12-binding domain-containing radical SAM protein [Devosia
            nitrariae].
ACCESSION   WP_284342097
VERSION     WP_284342097.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Banerjee,R. and Ragsdale,S.W.
  TITLE     The many faces of vitamin B12: catalysis by cobalamin-dependent
            enzymes
  JOURNAL   Annu Rev Biochem 72, 209-247 (2003)
   PUBMED   14527323
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Ludwig,M.L. and Matthews,R.G.
  TITLE     Structure-based perspectives on B12-dependent enzymes
  JOURNAL   Annu Rev Biochem 66, 269-313 (1997)
   PUBMED   9242908
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..464
                     /product="B12-binding domain-containing radical SAM
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0031419 - cobalamin binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=50817
     Region          32..356
                     /region_name="YgiQ"
                     /note="Radical SAM superfamily enzyme YgiQ, UPF0313 family
                     [General function prediction only]; COG1032"
                     /db_xref="CDD:440655"
ORIGIN      
        1 mersdvipfv sagllapkkr dhqlarrqly lnygalslat mldlggrntl lihgdhetpe
       61 illerlasmg afptrhpvml sipsfyslpw aqafcrlvka tdpgarlvvg grwvvgpdva
      121 wlrtklpeah vlvpglgepv irsllttdpd lrrlaaptpa ftlnhllvad hlrfqpsiea
      181 srgcgmgckf ceerdiplek lrepeeiars malvrdqygg sdihpymqas mfvpnprwsa
      241 rlaaavqelg ldigwrtesr vdallpesia hlaraglkvl dlgletaspt qilamkkann
      301 peryltkasa llqacrdngv makvnvllya getqntlaet tqwldahasc iagvsvgpvi
      361 aygppatadi lldewsraga rpvdatsaie tgitrmhlsd efdaeaaela slqvsrrfms
      421 mdayftlksf syyprdynra dfdrdvtesa gerlpfavdp apvv
//
LOCUS       WP_284342266             494 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Devosia nitrariae].
ACCESSION   WP_284342266
VERSION     WP_284342266.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..494
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=52972
     Region          1..484
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mtrvlivddd pvqlrltaev anragfravt ttggaealsi lrsdrsmgav ildlvmpevd
       61 gmavmeamar eglttpviiq tatasletvv tamrqgaady fvkpvaperl vvslrnaikl
      121 dtleaavrae harrsgtlsf sdmiaeapam artvslcaka akstipvmie getgvgkelv
      181 arviqggger agkpfiavnc galppnlves tlfghkkgaf tgaiadqpgk faeanggtif
      241 ldevgdlppe aqvkllrvlq egeiepvgas rpervnvrvi satnrrllnl tkagefredl
      301 yyrlnvfpiy vpplrerred iaalvdhfia rfaaeagkri tgiapgaldl lmrydwpgnv
      361 rqlentvyra vvltdgttle tadfpqiiaq lggreaalms ldavpvpaap vhvddapprr
      421 rqaevetsaq drfldengev atvaeieral iafaitqhgg rmarvaralg igrstlyrkl
      481 heygltdsid sdaa
//
LOCUS       WP_284342267             143 aa            linear   BCT 25-DEC-2024
DEFINITION  SRPBCC family protein [Devosia nitrariae].
ACCESSION   WP_284342267
VERSION     WP_284342267.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..143
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=16146
     Region          10..141
                     /region_name="SRPBCC_CalC_Aha1-like"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of Micromonospora echinospora CalC, human Aha1, and
                     related proteins; cd07814"
                     /db_xref="CDD:176856"
     Site            order(11,13,15,24..26,28..29,34,40,48,50,52,54,60,62..63,
                     65,68,74,76..77,92..93,95,97,107,109,111,113,120..128,
                     130..132,135)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mneapsglrt vvverqipyp aekiwraltq phlmeewlmk ndfkpdvghh fnlrgdwggv
       61 ldcevldiep ertlsytwnf ahedpayglt svvtftltpt dagthlrveq sgfrpeqtqa
      121 fggahagwke flgkleqvva ree
//
LOCUS       WP_284342292             577 aa            linear   BCT 25-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Devosia nitrariae].
ACCESSION   WP_284342292
VERSION     WP_284342292.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..577
                     /product="long-chain-fatty-acid--CoA ligase"
                     /EC_number="6.2.1.3"
                     /GO_function="GO:0004467 - long-chain fatty acid-CoA
                     ligase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=62858
     Region          42..563
                     /region_name="FC-FACS_FadD_like"
                     /note="Prokaryotic long-chain fatty acid CoA synthetases
                     similar to Escherichia coli FadD; cd05936"
                     /db_xref="CDD:341259"
     Site            order(224,227..232,234..235)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(227,344..345,366..371,450,462,465,476,556)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(227,269..270,317,319..320,323,344..345,366..371,450,
                     462,465,473..476,537)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(269,319..320,323,344,473..475,531,537)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mdkkadanrt sqplrpwidh ypegidwdvd idirpvheqv ldacaktpsa ialdflgatt
       61 tfgaladait afagalqsef gvtkgtrval llpntpfypv ayyavlragg tvvncnplyt
      121 vdelahmadn agadlmitld lkmifekaet lvetgrigsl ivchfpdalp lakkvlfsla
      181 krkdlvdtrr sriagrvahy rqlvarkltp epvtidphtd iavqqytggt tgipkgallt
      241 hanvaanmsq idkwgcdlfy pptkvvavlp ffhifamtvc mnvplcngaq vvmlprfelk
      301 aladliartr anilptvptl ltalaradni tsndlsslev avsggaalpn evreafakks
      361 kallaegygl teaspvvcca alrvpskpms iglplpatdi rfvdidsgrv lgigedgelq
      421 vkgpqvmlgy ynnreatedv fmdgwlrtgd vghmdedgyv flvdrikdmi icsgfkvypr
      481 vieealaehp avdevnvigv pdqyrgeapv afvklktdea aseseiksfl aerlnkiemp
      541 reiifkqalp ktligklskk elredyaqmk aknreqa
//
LOCUS       WP_284342303             754 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Devosia nitrariae].
ACCESSION   WP_284342303
VERSION     WP_284342303.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 754)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 754)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 754)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..754
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=82625
     Region          94..751
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 manggqkeqa eakaawevrr qaavkalail dtpptpefea lvdivgqtlg vpicgislid
       61 drrqwfkalr glglkqmpre hafcnrlies gaplvisdla aesassshpl vaggprlrfy
      121 agapltledg lvvgaicvfd taprvfekke aealsrlagi aegllrqfes aeklarlsre
      181 aeahlrlved qrrqlfqqhr vlsqasvmar igawerdlat gayrwsegmy rlhevgedfv
      241 vdeeavfsfy prserrriag viararkant syrldaqivt gkgnrrwvri sseaemidgv
      301 pvrrfgimrd itdekeaadr iasmaerdal tglynraflq tridglaetv pgrrhaflll
      361 dldgfkdind thghaagdec lrrvsrrigr aagrgalvar iggdefailv eesqgrdara
      421 larhvrkaiq vplrwqgqaf qlsasigiay wpgtgpirsd alfadadlal ydakgagknc
      481 davyrvelka eatqrfaivr disralkrgn lelyyqpkvr ladgahrgfe allrwvredg
      541 svvaagafgp alkdpglsve ighfvlrsgl eqaaewqrqg lafgsvainl gasqfrhrnl
      601 artilehias lglppgsiev evtedvflsr aagyapeicr dlkqggvtia fddfgtgfas
      661 lthlrefpvd vlkidrsfis rlgtdastts ivhavidlah nldlqtvaeg vetegqaqfl
      721 ravgcewaqg ylyarpmdar svpaylgaae rlra
//
LOCUS       WP_284342342             326 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Devosia
            nitrariae].
ACCESSION   WP_284342342
VERSION     WP_284342342.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..326
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=35778
     Region          2..315
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkllvtgatg kvgrnflgaf lsrdefrawd vvalchnrtl eatprvrvif gsqadeavvr
       61 tamegvthvl hmaavkespd laigvavkgm fllleearrs ptlrqfmlis gdcavghifh
      121 rypapiteas prmaypgcya ltkvleevmi eqyqiqygln gtvlrapwvm ekddfryals
      181 fgpgqfggpa wstlisaeee vglaekgavp llldaagapl krnfvhvddl vgailaaldn
      241 raaegalfni smnepvdyak vaeylagtrg lepaairtpf hsnwldnska rlllgwqpht
      301 dfealveraw ayerdpgdpr kiwypg
//
LOCUS       WP_284342481             250 aa            linear   BCT 25-DEC-2024
DEFINITION  endonuclease III domain-containing protein [Devosia nitrariae].
ACCESSION   WP_284342481
VERSION     WP_284342481.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Kuo,C.F., McRee,D.E., Fisher,C.L., O'Handley,S.F., Cunningham,R.P.
            and Tainer,J.A.
  TITLE     Atomic structure of the DNA repair [4Fe-4S] enzyme endonuclease III
  JOURNAL   Science 258 (5081), 434-440 (1992)
   PUBMED   1411536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..250
                     /product="endonuclease III domain-containing protein"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=27460
     Region          17..228
                     /region_name="Nth"
                     /note="Endonuclease III [Replication, recombination and
                     repair]; COG0177"
                     /db_xref="CDD:439947"
ORIGIN      
        1 mqltlpfvme nrlarahell saafgpvaat rrmdpvsqmv famlsgrtrd giaksafegl
       61 ansfptwepv armragdlla rigqttfpek kafyvpsalq aimrrrqrld ldflgnrpve
      121 aaqtwleslp gigpkastav lnfstlhrrv lcvdtthyrv amrfglvppg tphklasrll
      181 nqlvpdqwsa ddtethhilm qflgrvfcta grprcapcpl rlmcptanss avaplsafsp
      241 qafhpdrqgg
//
LOCUS       WP_284342505             102 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Devosia nitrariae].
ACCESSION   WP_284342505
VERSION     WP_284342505.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 102)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 102)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 102)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..102
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11549
     Region          3..96
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mnadqldhif raladptrrr iidrlreqpd qslfqicaas vaedgkaisr qavtqhldml
       61 eksglirvtw sgrtkihsld lkplreavei wlarhlqegn gr
//
LOCUS       WP_284342507             139 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Devosia nitrariae].
ACCESSION   WP_284342507
VERSION     WP_284342507.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..139
                     /product="YybH family protein"
                     /calculated_mol_wt=15627
     Region          3..123
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mfdevkalld grseairmkd idrlmsfysp dvvyfdtvpp lqyvgtavlr drflhwfdgw
       61 kgsigqeird lkisasgdva vaymlvrasg alknglever wvrvtsccqr sddkwltahe
      121 hvsfpidfas gravmdlvp
//
LOCUS       WP_284342549             115 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Devosia nitrariae].
ACCESSION   WP_284342549
VERSION     WP_284342549.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..115
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12774
     Region          2..87
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mqpdqvsltl saiadptrra ilmrlmdgea svkelaapfe msipaickhl kvlegaglis
       61 rgrkaqlrpc rleaqplrea yswieefskf wdtnlnrldg llerlqsadp aakkn
//
LOCUS       WP_284342560             816 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Devosia nitrariae].
ACCESSION   WP_284342560
VERSION     WP_284342560.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 816)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..816
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=89313
     Region          2..815
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 melvfgdyrl kirereligp aghvalsara fdllrallde peglldkdal faaawpgmiv
       61 edntlqvhms alrkalgtgy ittvhgrgyk yvgprphapg vpepapehns gnierylgdc
      121 iereaeasai arlleqhrlv sivgsggvgk ttvatavats reaaggvwli dlasldsgaf
      181 idsaliqtla ipyrsetqvl qlvaehlrra qavllfdnce hvqaeaaqii akllaevpal
      241 rvlatsqvpl gvagerifkl lpfaladgad eglpaagqfl rhciemsget lsrddypviq
      301 rlcrrldgva lalkmaaaga stigleavde qierqlagle adwnttlprh rsllaslrws
      361 ydllpedvrg tlralgvfng sfslagalav agesaeahig elvrrslvar dtanrgryrl
      421 ldstrrfalq elaaageesl ardrhaafvt rlfassielw etmpdtiwea tfrpdgdnlr
      481 aalawtkakp nsagyvelva ettrfflqeq lgaeglatie salpsapdas aqaqarlgla
      541 laevarvnaa dikgrqgies algwlrdndr glryfealvm ltwittfsrd rsealplvke
      601 lgdvlhrmpv sktkawalva lgthmwlsgd reaglarcqa gsamhietgn lrgrfrslmn
      661 fteivhkegd trlalelaqs vlpdvrqyat rfhlsnqlgn iaaylfwvge ieeaerahle
      721 sapvmwpdgs ywhlcvlqna aechywrgdh isaslllgiv dkrveawpdg rqateqiqrd
      781 rlrerlaeal gegeyrrlre qganldleda rqlaam
//
LOCUS       WP_284342623             249 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Devosia nitrariae].
ACCESSION   WP_284342623
VERSION     WP_284342623.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..249
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27729
     Region          9..248
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          167..244
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mepqaycihr afeaagprlf rldrhyfvya legslrlead grrwtlppar galieadhpv
       61 risvparfis asvlfdsamf kpsqplavfd vsplarelvr ecrqwgrdde dqtpharqmf
      121 ralasvigql artpspcvlp vptsremmra lamiedapad qpdfaviara tgqsprtlar
      181 rfasemrmtg retlqririi haveilalgn asitdvalqv gytslsafna afrqvmgmtp
      241 sqyrmayrg
//
LOCUS       WP_284342733            1111 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Devosia nitrariae].
ACCESSION   WP_284342733
VERSION     WP_284342733.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 1111)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 1111)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1111
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..1111
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=121623
     Region          618..901
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
ORIGIN      
        1 mgaffksgcg kaaaglavga avvlsvqpap vfglerarlf vtqeegygrl vlgfpdrdkl
       61 ppyylrmdng vlsiefedev svvmpdvevt lpdyisiarv dpdlngvrfa lrgdfnfnsi
      121 eagerlfvdl lplswrglpp slpqeiidel aerarlaaie aerqrkardv aelnpaaevr
      181 igrnptflrl qfnwnvdtta ayeqvedear iafewpvdvd lmdlaldlpv eiasvesett
      241 pdgavvslkl aegieprffq nssreflldv dlagvslpki gvedlaaeag daqaaeaaea
      301 svesaasmpr amsaepvtpf vtvvgttari vfpfeeevpa avfrrgdtlw mlfdtdvait
      361 apedrsnlgg iagafevtpa gdaqvvrial sgerlatlgs egrawvlslg dlvlaptepv
      421 gfarrlglsd lyemtadmar pvrvhefrdp qvgdvlkivt ayppargvtr tfdyvdfdal
      481 rsihglvlrp ehegvgvrle gglavvsaeq gltvssldqv rretffgsaa rregfidltr
      541 ltqgdpaafa qrrkmlmaqa aegegrardi arlelaqfyv anrfahealg vlrmvgvdfe
      601 ardvlrkirm tqaiantlag rpqeaitilq spllatdvda llwraiarvd asdfkggrqd
      661 aqvaepvlds yptwvkarfr laavraavet gdagmakrlf eaidfaelnl eqtslyhlle
      721 grlaelegrp edamdmygqv iaadirptra eaiyrtlqll dgadnldagk aaetlaaeam
      781 lwrggpleae mqkmltdlyy regayrqgfe tvrqamaast esaainamrd eaqrvfadlf
      841 lngradtlap vdalglyydf rqltppgarg demirnlarr lirvdllgqa aellqyqlen
      901 rlrgvarsqi aadlavvyla drrpqdalrv ltgtrlpdis ttlarqrrvl earalievgr
      961 helaldmird msgrdidlmr ieanwkagry evaagmleai yspetgpltq aermsivkaa
     1021 vgfvladdrl gvsrlrskfg erlvttpewa mfdyvtsaiq ptslefrqva revaaidgln
     1081 aflasyrqvy esegalapaq asqaqasvas r
//
LOCUS       WP_284342617             113 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Devosia nitrariae].
ACCESSION   WP_284342617
VERSION     WP_284342617.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 113)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 113)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 113)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..113
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12642
     Region          8..81
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(12..13,17..19,32..34,43..46,48..49,52..53,55..56,
                     62..64,69..71)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 maraattsdv fnaiaepqrr eilvllrage rpvtelaqal gmtqpgaskh lrvlrkvglv
       61 rdrkagkqrl ygldarqlra vhewtggfeg fwnesfdrld ayvqglkqar qke
//
LOCUS       WP_284342757             550 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Devosia nitrariae].
ACCESSION   WP_284342757
VERSION     WP_284342757.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..550
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=57563
     Region          <2..202
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mrilqslvla avaalgfllp svaaeraiiv ldgsgsmwaq idgtaritia retlndvlqs
       61 lpddlelgfm tyghrekgnc tdiellvppa pgmgeaigaa aadinpkgmt plsdavrmaa
      121 eelryteera tvilitdgle tcevdpcdlg felesagidf tthvvgfgls ddegrqvacl
      181 aentggtylp andadaltsa ltltvaevve pepepepape pepvalefnl speavmaegg
      241 epivrsgtaw nvyearadgs rgegvtygyg npfetslepg dyiiaikege vemeqavtva
      301 aeevarprfi lnaatvtlra yaaeggpvae gaalnlyypg gdtygygeet fivpagevta
      361 takvgqgevs etftiaaget ierdlvagvg rvvvnaayve gmkveagglg vnvfkasasi
      421 dgsreevgyg fgpdtgydlp pgdyvavvkm ddataevaft vetgksvevv gvleagvvai
      481 taagtdrlni ysgkadiqgn rkefgysyde eyqqtlpagk yvvvahfpdd vekevpftva
      541 agdrvdvtve
//
LOCUS       WP_284343041             226 aa            linear   BCT 25-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Devosia nitrariae].
ACCESSION   WP_284343041
VERSION     WP_284343041.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Niehaus,T.D., Elbadawi-Sidhu,M., de Crecy-Lagard,V., Fiehn,O. and
            Hanson,A.D.
  TITLE     Discovery of a widespread prokaryotic 5-oxoprolinase that was
            hiding in plain sight
  JOURNAL   J Biol Chem 292 (39), 16360-16367 (2017)
   PUBMED   28830929
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Fan,C., Li,Z., Yin,H. and Xiang,S.
  TITLE     Structure and function of allophanate hydrolase
  JOURNAL   J Biol Chem 288 (29), 21422-21432 (2013)
   PUBMED   23754281
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Wang,L., Grau,R., Perego,M. and Hoch,J.A.
  TITLE     A novel histidine kinase inhibitor regulating development in
            Bacillus subtilis
  JOURNAL   Genes Dev 11 (19), 2569-2579 (1997)
   PUBMED   9334321
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005226
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..226
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=23670
     Region          9..224
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 mfaadgsdpa akplvlplge sallvrfgst lsqaantaal rfarilelrp iagvvevvpn
       61 lvsvllryep qrigfhhlag eigllltaav ddvgaearnh ivkvafggea gpdlpdvaer
      121 lglsagafva ahnasrlrvl atgfapgfvy cgfhperlhv prraevrprv aagsvlfaag
      181 qtaiaatdip tgwhvightq lrnfdalrdp ptllqagdti efeatt
//
LOCUS       WP_284342917             264 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Devosia nitrariae].
ACCESSION   WP_284342917
VERSION     WP_284342917.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..264
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=29796
     Region          20..259
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 maitpsdwfd ttparapade dvlnvdvtgy egpldllldl arrqkvdlaa vsilalaeqy
       61 lafietvrsr rievaadylv maawlaylks rlmvpqapsd depsgemlaa llqfrlkrle
      121 amrnaasqlm hrprlglrvy argepepmvv nrrsiweasl ydllkayatq rergiatdya
      181 pvqrtvwslq eareilerli gesmdwvpld tyladylasp qeratvrass fsaslelvrq
      241 gqvelrqsna fgplfvrrrr tgeq
//
LOCUS       WP_284343135             373 aa            linear   BCT 25-DEC-2024
DEFINITION  two-component system sensor histidine kinase NtrB [Devosia
            nitrariae].
ACCESSION   WP_284343135
VERSION     WP_284343135.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 373)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 373)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..373
                     /product="two-component system sensor histidine kinase
                     NtrB"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009399 - nitrogen fixation [Evidence
                     IEA]"
                     /calculated_mol_wt=40606
     Region          12..362
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 mkvkvdpqas tavlqalpqp iivcsedgsi tfvnyaaeaf fgaslsvlar qkledliafg
       61 spiislvetv aqrrapmtey rvrvgssrfg deriadvfas plsesdgrva lliqertmad
      121 kidrqmvsrg aarsvtglas mlaheiknpl sgirgaaqll eqsvppeeip larlireetd
      181 rivdlidrve vfgderpler epinihvvld rvkllakngv argitfseey dpslppvygn
      241 rdqliqifln lvknaseale rtqkpeikfs tafrpgiris vtgvserisl pleiiiedng
      301 pgvppdilpf lfdpfvttkt ngsglglalv akivgdhggv idcdsrpgrt rfrillpvan
      361 payiapseev mak
//
LOCUS       WP_284343199             248 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Devosia
            nitrariae].
ACCESSION   WP_284343199
VERSION     WP_284343199.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..248
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27624
     Region          1..247
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mdlsfqlysa rnfpplddfl gklaalgytq vegfgglysd pagldqmlrk hgltmptghf
       61 gpdqlkdkda tlkiaetigv ktifcphinr elfgnsdakw tefaetlagf aetykaegyg
      121 fgwhnhhfef wkteagstpm eiiletgasl ewemdvawva kggedprawm drygeritav
      181 hvkdiapege nadedgwadv ghgtmdwdnl indvkaktka ayfvaehdnp sdaerfarrs
      241 ietakawk
//
LOCUS       WP_284343236             154 aa            linear   BCT 25-DEC-2024
DEFINITION  YcbK family protein [Devosia nitrariae].
ACCESSION   WP_284343236
VERSION     WP_284343236.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..154
                     /product="YcbK family protein"
                     /calculated_mol_wt=16759
     Region          3..147
                     /region_name="YcbK"
                     /note="Uncharacterized conserved protein YcbK, DUF882
                     family [Function unknown]; COG3108"
                     /db_xref="CDD:442342"
ORIGIN      
        1 mrmlltaltf alalggcvpl amfadgssss yrglrsdwgt yvssrevnal clspklrlai
       61 wdfegrfgrk vvmssgyrds hhnaqaggas dsyhtkcmaa dfhipgvpke eliafamrng
      121 yvgglgcypg rkfihidvrd rprgytrpvt fsgc
//
LOCUS       WP_284343263             372 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Devosia nitrariae].
ACCESSION   WP_284343263
VERSION     WP_284343263.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..372
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=42104
     Region          102..363
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mtailpngrt rtlgnpatgq havlrlnnfn vlseamqrgt vgfaaaymng diesddltal
       61 frfflqnrdm fekanpgmfr raahdlhyhl srrntlegsk qniaehydlg ndfygqwldp
      121 smtyssavft sgdqsleeaq lakyrrvadm agitegstvl eigcgwggfa etvarhykaq
      181 lrgitlsaeq lkfglerlrs qgldtfaelv fedyrhtkgq fdhiasiemi eavgednwpg
      241 yfqtlydrlk pggtaaiqai tineadfegy ksgpdfiqry ifpggmlltk tvmkefgdkv
      301 glvlenaehf rlsyaktlal wrerflerwp miaplgydeh fkrkwvyyls yceagftegs
      361 idvgiyqyrk pa
//
LOCUS       WP_284343269             377 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Devosia nitrariae].
ACCESSION   WP_284343269
VERSION     WP_284343269.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..377
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39917
     Region          5..373
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mdiaaridha vaaaledkrv vgsvvivkrd getlhrraag lanretgrtm qpdaifrlss
       61 ltkpivattv lamaergllr lsdpvtrylp dfrpkladgs apditlqhli thtaglgpmp
      121 plfedertdp eflavgldrw hlslernlar lmrvplqfap gvgwaysagi dvlgavaatl
      181 vggtlgdava tyvtgplgmg dtrfsvtdvs rlaapyadgp egpvlmgdph evanprggit
      241 tyypglildp kayhaggggm agtaddfmtl lemlrtggga ilspqmlaeg aadqlaadvh
      301 qspgwkfgyf gavlvdpvla espqsvgtyr wggiyghswf idpaeelsvv amtntglegs
      361 dgrfpidirn avygrnh
//
LOCUS       WP_284343277             218 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-L-isoaspartate O-methyltransferase family protein [Devosia
            nitrariae].
ACCESSION   WP_284343277
VERSION     WP_284343277.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Edwin,R.K., Challa,N., Sharma,R., Satyamoorthy,K., Parsa,K. and
            Misra,P.
  TITLE     PIMT/TGS1: An evolving metabolic molecular switch with conserved
            methyl transferase activity
  JOURNAL   Drug Discov Today 27 (8), 2386-2393 (2022)
   PUBMED   35462043
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Furuchi,T., Sakurako,K., Katane,M., Sekine,M. and Homma,H.
  TITLE     The role of protein L-isoaspartyl/D-aspartyl O-methyltransferase
            (PIMT) in intracellular signal transduction
  JOURNAL   Chem Biodivers 7 (6), 1337-1348 (2010)
   PUBMED   20564550
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Kagan,R.M., McFadden,H.J., McFadden,P.N., O'Connor,C. and Clarke,S.
  TITLE     Molecular phylogenetics of a protein repair methyltransferase
  JOURNAL   Comp Biochem Physiol B Biochem Mol Biol 117 (3), 379-385 (1997)
   PUBMED   9253175
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..218
                     /product="protein-L-isoaspartate O-methyltransferase
                     family protein"
                     /EC_number="2.1.1.77"
                     /GO_function="GO:0004719 - protein-L-isoaspartate
                     (D-aspartate) O-methyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0030091 - protein repair [Evidence IEA]"
                     /GO_process="GO:0036211 - protein modification process
                     [Evidence IEA]"
                     /calculated_mol_wt=23085
     Region          13..207
                     /region_name="Pcm"
                     /note="Protein-L-isoaspartate O-methyltransferase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2518"
                     /db_xref="CDD:442008"
ORIGIN      
        1 mvdfeharra mvdsqlrttn vtdrrilaam griprenfvp earrpiayid eshgfgalap
       61 grflpapspf aklvqlaeig pgdhildvga gtgystavla algaevvgve reaklveqar
      121 anlaslgian akvvegahdr apkgrfdviv legavtsvpe afftslgedg rlvalvqtgv
      181 tavahlfvka gktvtsraef nanlppleap rpredfvf
//
LOCUS       WP_284343335             715 aa            linear   BCT 25-DEC-2024
DEFINITION  GumC family protein [Devosia nitrariae].
ACCESSION   WP_284343335
VERSION     WP_284343335.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 715)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 715)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..715
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=77419
     Region          3..715
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mheqefnlrs flgtvrrqag lilavlvvvv gassvailsl tpiyrattlv lvdpseknll
       61 nptngsssaa sdnarvesev siaqaetive evldrlklae dpayqpqpgl reriatllri
      121 appeeyttee rrihavgalq naitverqgl tylitisana ntpekaaria ntmadvyira
      181 qlqskingvl sgrniledrv tetraglvka erafndfiis sartiaeqsg rtdidqlrve
      241 ledvvaqreq ageeltvlet alasqdwaqv vqnldngtlr elerqrqqiq qqlsdivdgs
      301 eqaealrael vgvidglsaq anaqleqlra evaanralet dlqlqlrssi ltsdlppevl
      361 atmyelqqna eiartqyqqm lvrlrdieaq aylqladsrv vseatpptsa sfpntrflig
      421 laaivgtiag livafvreql iggvtsteql ggvsgfhait siplqrrlgr sedgkpirsi
      481 aelvakqpys tlaeavrrvm isvdqalrri rgnepsgeaa iilvtsanag egkttaavtl
      541 artyaisgrk tllidadlrr psvhrelglt andnlanyla snasgdtfrd lvhadtlssa
      601 efllgsnlig saagqvvsge rfgkllssaa hqydivivdt ppvgaivdal ylsqhvdviv
      661 nvvrfgttsq revratirel leakqdttei vavlnaepqs raearrrfgg yyaqa
//
LOCUS       WP_284343344             455 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Devosia nitrariae].
ACCESSION   WP_284343344
VERSION     WP_284343344.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..455
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=48345
     Region          1..444
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrvaiigtgy vglvsgacla hkghivqcvd idhrkidmin srrppiheag ledvlasvvp
       61 erlsatadla aavngadltm iavgtpfngs eidltyieka awqigealat kdeyhvvvvk
      121 stvvpgttet vvlpileras gkkagidfgv gmnpeflkeg eaiadfmnpd rvviggidda
      181 sidrqaelys pfpgvdivrt tpstaemvky tsnallatli sfsneignts aalgvdamev
      241 mkgvhldkrf spilpdgqrv rpgmlsylap gcgfggscfp kdvksiiahg qrlgqpmrll
      301 eavasvnadq psqminmleg rfrelrglkv avlgmafkpg tddvrespai avtrtlidkg
      361 vqvvgydpia rsaaqailpe vvefeenlaa avadadaili mtawaelral pamladmdtp
      421 pvlidgrrli dksavrdyla iglpttrefs pvepa
//
LOCUS       WP_284343410             240 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfotransferase family protein [Devosia nitrariae].
ACCESSION   WP_284343410
VERSION     WP_284343410.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..240
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=27794
     Region          49..203
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mslvtiigrg hggtraisht lyasgvymgq tlnasgdlvp peamyeacri faryvdwtgg
       61 lewdfsrals aeipaefrql iekylaavlt skaehrgwki pettlvypwi qrmfpearyv
      121 fwirdprdsi lathktddma dfgidyprsd dvlrrraisw kyqydlvqat pkpahwlevr
      181 fedfvddqea tlerlerflg ydlariivrp davgrwrsrp gkdvsfdffe palkayrydi
//
LOCUS       WP_284343544             241 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Devosia nitrariae].
ACCESSION   WP_284343544
VERSION     WP_284343544.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 241)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..241
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27474
     Region          1..>220
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mdkterlfav mdamrrhrrp vtaaqlaeeq nvsvrtlyrd vqtliglgap idgeagvgym
       61 lrpgffmppl mftpeeleal vlgarwveaq pddglvsaar nalgkiatas pedlrdriad
      121 tglwpvmmrg paapkpmlae irramrseka vhiaytdesg reserdiwpv qlayyegkqi
      181 iaawcclrqa frnfrtdriv slfptenryg krrtvlarew evewqrqhpd wamepdvrpt
      241 h
//
LOCUS       WP_284343567             209 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Devosia nitrariae].
ACCESSION   WP_284343567
VERSION     WP_284343567.1
KEYWORDS    RefSeq.
SOURCE      Devosia nitrariae
  ORGANISM  Devosia nitrariae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Devosia nitrariae"
                     /db_xref="taxon:2071872"
     Protein         1..209
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=23136
     Region          2..207
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 miplptslly rtldqsqtaa lladivavir aaplyrpvmp rsgkpfsvlm tncgplgwvs
       61 dregyryqaq hpvtggpwpp ippmllalwd eladyphepq aclvnyygqs trmglhqdrd
      121 eedfsapvls vslgdtarfr lggtdrkdpt qsfllrsgdv mllagdrrla yhgvdrvltg
      181 ssrlleahpd lfpdggrinl tmrrvtkpr
//
LOCUS       WP_284343702             529 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Dyella mobilis].
ACCESSION   WP_284343702
VERSION     WP_284343702.1
KEYWORDS    RefSeq.
SOURCE      Dyella mobilis
  ORGANISM  Dyella mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Dyella mobilis"
                     /db_xref="taxon:1849582"
     Protein         <1..529
                     /product="beta strand repeat-containing protein"
     Region          <6..>509
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 sgltgtvtgf vngqtlanat tgtasfttga tatsnvgnya idgngltand gnytftqaag
       61 nataltvspa tltitannds ktydglayag ghgvtysgfv ngetssvlgg tlgytgdsqg
      121 ainaggytit pdgltagnya itykngnltv dqatleisss nvsktydggl saigtavvsg
      181 gtlfgsdtls ggnfaftdkn vgtgkhvtvn gvtvsdgngg rnyavtyvdn tsstitarsi
      241 tvdatgtnrv ydgttadavk lastgilagd tvifsgtgaf adknvgtgka vsvsgiaasg
      301 adagnysfnt tanttadisp lsitvdatgt nrvydgttvd avnlassgil tgdtvafrgt
      361 gafadknvgt skavsvsgit atgidagnys fntsatttad itpatltyra dtahfkigqm
      421 pgdlsgvvtg lvggdtldaa tdgtlawqtp atatspagay aidgsglsah nyvfvqassn
      481 atalqvidgs aprlvvstva glqqsddsgk prapyapdvh ivnggvrlp
//
LOCUS       WP_284343816             973 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Dyella mobilis].
ACCESSION   WP_284343816
VERSION     WP_284343816.1
KEYWORDS    RefSeq.
SOURCE      Dyella mobilis
  ORGANISM  Dyella mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..973
                     /organism="Dyella mobilis"
                     /db_xref="taxon:1849582"
     Protein         1..>973
                     /product="beta strand repeat-containing protein"
     Region          <44..941
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mntsngkqhi srhpnglqvf rrkllpasmm sllglfaygn dawagghvsv nttptggsiv
       61 ggngtilqng alttiqqnsq llsinwqsfn vganasvlfk qpsftsvaln rildqnasqi
      121 fghinsngqv flinthgiif grtsqlnvgg lmastldltp tdflsnhfnl dahggsagiv
      181 nhgtidaasg svslvggqvv ndgliianyg hinldgadra vldfdgdgli diqitgalqk
      241 rlnadeaavt nkgklqadgg tvvlqasaak dlftnlvnnt gvvsaggist hggkvqlias
      301 ggnavtsgti dvsgaqggsv qvlsdqnvsv tgninasgtn gggsirvggg fhggegltta
      361 ntayvgpsat lnadatqtgn ggsvvvwgnq gndfegsita rggalggngg qvetsahngl
      421 nadgdvnasa ahgttgswll dpynvtiggs nsgystings gtveysanan ssnikastig
      481 aalnngtdvf vytnnaggsq ngditvsrgi tangqgslyl qasgsifvnn nisgdnfgda
      541 lnvylwanys gtggataysr gtcasstgcv vqigngagit tnggnldiet nggvslaags
      601 gggssistgg gnvtigtssn pvnslsvtgg ssiatfggni dvetggqasv dstsyidttn
      661 tvgalgnlai nagaginaag altisgtttl nggagaisay dsgngnnnlv gtvsitnegn
      721 navivsndsg vlnlgkvsvg tstlslsgvg iaqssgttis qasgtnpvts eavtliggsa
      781 aitlnnandf vggitasnsg asngitlnng snamtlagvt agggllatst ggidlagtit
      841 tgtgqnyqga vtltadssla sntggaivfn stvdgaqnls itnggtttfn gtvgstvalq
      901 slnvlgggkt vldanvttag tqsygtlalg nsvilastsa gvtfngtvdn atsttqealt
      961 inaagpvafd gav
//
LOCUS       WP_284343805             318 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Dyella mobilis].
ACCESSION   WP_284343805
VERSION     WP_284343805.1
KEYWORDS    RefSeq.
SOURCE      Dyella mobilis
  ORGANISM  Dyella mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Dyella mobilis"
                     /db_xref="taxon:1849582"
     Protein         1..318
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=35162
     Region          <12..231
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 malshvavrs nvfhwaileg kaeadptial rgtikrvkhk hhaaitdsmk igqllrdidg
       61 ftgqpvthaa lklaplvfvr agelrgaews eldlegavwh ipgarmkmkl dhlvplsiqa
      121 vailrdlqll tgqgryvfps lrgasrhmse navniglrsv gydgdtmtgh gfcamassrl
      181 nemgwderai ecqlahaepn evkgaynyaa kyldirkdmm qawadylhal kvvnskpnsm
      241 kdeqqtdvit pskahhvked sskpgvaqne psrvvsipar gmpidqqnit nnteaqaepv
      301 rvvslermlp rnkpwlrk
//
LOCUS       WP_284343817             236 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Dyella mobilis].
ACCESSION   WP_284343817
VERSION     WP_284343817.1
KEYWORDS    RefSeq.
SOURCE      Dyella mobilis
  ORGANISM  Dyella mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Dyella mobilis"
                     /db_xref="taxon:1849582"
     Protein         1..236
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=25660
     Region          5..236
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mtlhyssvgh tdtgkvrghn edailvredv glwvvadglg ghsagdyass liverlgglp
       61 rngsvfdfve siedalvqvn adlrnaarer nvdvigstvv vlvhdkefml cgwvgdsrgy
      121 cfeegrlrqi trdhvhghkn ddtrlgqspp agsgvltrai gaeetlfvdw vvagnrpgma
      181 fllctdgink elsdaeldee yrthsdpqil larlfelslg rsardnisav ivrlqd
//
LOCUS       WP_284344234             329 aa            linear   BCT 25-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase, partial [Escherichia
            coli].
ACCESSION   WP_284344234
VERSION     WP_284344234.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10594375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..329
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
     Region          12..148
                     /region_name="SIR2_2"
                     /note="SIR2-like domain; pfam13289"
                     /db_xref="CDD:433090"
ORIGIN      
        1 iqdffkentf kvittnydkl aeklagenrt ctitpglpip kyncevkvyh vhgsidspsd
       61 mvvtsedyfr fingnsyfsn klstvlhent ivilgyslsd anlkaiiney kvfsrdnvms
      121 sniflisrgk llqpikdyyf scfgirvidk tevsdffrkl nkkipeakki kdklrhsiks
      181 vikngreyki eflkledsfy hiississsg yswndekvln vfcdiidkki dltkesgawe
      241 qyehlakwli yfgslfevkg tnfekkyiha vehsmtymnk pyetgyswra ylawktkwps
      301 ltasnrslik skmeeiplqq ihdiiskfi
//
LOCUS       WP_284344734             176 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_284344734
VERSION     WP_284344734.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>176
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          1..>175
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 yipygkmasw lvewknatet qwlkdspsqp lqqslkdler ayknffrkra afprfkkrgq
       61 ndafrypqgv kldqensrif lpklgwmryr nsrqvtgvvk nvtvsqscgk wyisiqtese
      121 vstpahpsas mvgldagvak latlsdgtvf epvnsfqknq ktlarlqrql srkvkf
//
LOCUS       WP_284344779            1504 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Escherichia coli].
ACCESSION   WP_284344779
VERSION     WP_284344779.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 1504)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1504)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1504)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1504)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1504
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..1504
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=166246
     Region          192..1496
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mgtglanadd slpssnyapp aggtffllad ssfssseeak vrleapgrdy rryqmeeygg
       61 vdvrlyripd pmaflrqqkn lhrivvqpqy lgdglnntlt wlwdnwygks rrvmqrtfss
      121 qsrqnvtqal pelqlgnaii kpsryvqnnq fsplkkyplv kqfryplwqa kpfepqqgvk
      181 legassnfis pqpgniyipl gqqepglylv eamvggyrat tvvfvsdtva lskvsgkell
      241 vwtagkkqge akpgseilwt dglgvmtrgv tddsgtlqlq hispersyil gkdaeggvfv
      301 senffyesei yntrlyiftd rplyragdrv dvkvigrefh dplhsspivs apaklsvlda
      361 ngsllqtvnv tldarnggqg sfrlpenava ggyelrlayr nqvysssfrv anyikphfei
      421 glalakkefk tgeavsgklq llypdgepvk narvqlslra qqlsmvgndl ryagrfpvsl
      481 egsetvsdas ghvalnlpaa dkpsrylltv sasdgaayrv tttkeilier glahyslsta
      541 aqysnsgesv vfryaaless kqvpvtyewl rledrtshsg elpsggksft vnfakpgnyn
      601 ltlrdkdgli laglshavsg kgstahtgtv divadktlyq pgetakmlit fpepideall
      661 tlerdrveqq sllshpanwl tlqrlndtqy earvpvsnsf apnitfsvly trngqysfqn
      721 agikvavpql dirvktdkth yqpgelvnve ltsslkgkpv saqltvgvvd emiyalqpei
      781 apnigkffyp lgrnnvrtss slsfisydqa lssepvapga tnrserrvkm lerprreevd
      841 taawmpsltt dkqgkayftf lmpdsltrwr itargmngdg lvgqgraylr seknlymkws
      901 mptvyrvgdk paaglfifsq qdnepvalvt kfagaemrqt ltlhkganyi sltqniqqsg
      961 llsaelqqng qvqdsistkl sfvdnswpve qqknvmlggg dnalmlpeqa snirlqsset
     1021 pqeifrnnld alvdepwggv intgsrlipl slawrsladh qsaaandirq miqdnhlrlm
     1081 qlagpgarft wwgedgngda fltawawyad wqasqaigvt qqpeywqhml dsyaeqadnm
     1141 pllhralvla waqemnlpck tllkgldeai arrgtktedf seedtrdind slildtpesp
     1201 ladavanvlt mtllkkaqlk stvmpqvqqy awdkaansnq plahtvvlln sggdatqtaa
     1261 ilsgltaeqs tieralamnw lakymatmpp vvlpapagaw akhkltggge dwrwvgqgvp
     1321 dilsfgdels pqnvqvrwre paktaqqsni pvtverqlyr lipgeeemsf tlqpvtsnei
     1381 dsdalyldei tltseqdavl rygqvevplp pgadverttw gisvnkpnaa kqqgqlleka
     1441 rnemgelaym vpvkeltgtv tfrhllrfsq kgqfvlppar yvrsyapaqq svaagsewtg
     1501 mqvk
//
LOCUS       WP_284344868             476 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Escherichia coli].
ACCESSION   WP_284344868
VERSION     WP_284344868.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..476
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51522
     Region          1..448
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mpdffsfins vlwgsvmiyl lfgagcwftf rtgfvqfryi rqfgkslkns ihpqpgglts
       61 fqslctslaa rvgsgnlagv alaitaggpg avfwmwvaaf igmatsfaec slaqlykerd
      121 angqfrggpa wymarglgmr wmgvlfavfl liaygiifsg iqanavaral sfsfdfpplv
      181 tgiilavfal laitrglhgv arlmqgfvpl maiiwvltsl vicvmnigql phviwsifes
      241 afgwqeaagg aagytlsqai tngfqrsmfs neagmgstpn aaaaaaswpp hpaaqgivqm
      301 igifidtlvi ctasamlill agngttympl egiqliqkam rvlmgswgae fvtlvvilfa
      361 fssivanyiy aennlfflrl nnpkaiwclr ictfatvigg tllslplmwq ladiimacma
      421 itnltailll spvvhtiasd ylrqrklgvr pvfdpfrypd igrqlspdaw ddvsqe
//
LOCUS       WP_284345187             262 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Escherichia
            coli].
ACCESSION   WP_284345187
VERSION     WP_284345187.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..262
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29759
     Region          1..262
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mkigtqnqaf fpenilekfr yikemgfdgf eidgkllvnn ieevkaaike tglpvttacg
       61 gydgwigdfi eerrlnglkq ierilealae vggkgivvpa awgmftfrlp pmtsprsldg
      121 drkmvsdslr vleqvaartg tvvyleplnr yqdhmintla darryivend lkhvqiigdf
      181 yhmnieednl aqalhdnrdl lghvhiadnh ryqpgsgtld fhalfeqlra dnyqgyvvye
      241 griraedpaq eyrdslawlr tc
//
LOCUS       WP_284345263             498 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Escherichia coli].
ACCESSION   WP_284345263
VERSION     WP_284345263.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..498
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55430
     Region          21..457
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mqgtkirlla ggllmmatag yvqadalqpd pawqqgtlsn glqwqvlttp qrpsdrveir
       61 llvntgslae stqqsgysha iprialtqsg gldaaqarsl wqqgidpkrp mppvivsydt
      121 tlfnlslpnn rndllkeals ylanatgklt itpetinhal qsqdmvatwp adtkegwwry
      181 rlkgstllgh dpadplkqpv eaekikdfyq kwytpdamtl lvvgnvdars vvdqinktfg
      241 elkgkretpa pvptfsplra eavsimtdav rqdrlsimwd tpwqpiresa allrywradl
      301 arealfwhvq qalsasnskd iglgfdcrvl ylraqcaini espndklnsn lnlvarelak
      361 vrdkglpeee fnalvaqkkl elqklfaaya radtdilmgq rmrslqnqvv diapeqyqkl
      421 rqdflnsltv emlnqdlrqq lsndmalill qpkgepefnm kalqavwdqi mapstaaatt
      481 svatddvhpe vtdippaq
//
LOCUS       WP_284345389             190 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_284345389
VERSION     WP_284345389.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>190
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          <1..>182
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 raafprfkkr gqndafrypq gvkldqensr iflpklgwmr yrnsrqvtgv vknvtvsqsc
       61 gkwyisiqte sevstpvhps asmvgldagv aklatlsdgt vfepvnsfqk nqktlarlqr
      121 qlsrkvkfsn nwqkqkrkiq rlhsrianir rdylhkvttt vsknhamivi edlkvsnmsk
      181 saagtvsqpg
//
LOCUS       WP_284345621             328 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Escherichia coli].
ACCESSION   WP_284345621
VERSION     WP_284345621.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..328
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36308
     Region          <2..325
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mseliataas sinaftlakr vaafnvpvli qgetgagkec vakyihtvaf genenapyig
       61 vncaailenm leatlfgydk gaftgaiasv pgkmelanng tllldeigdm plalqakilr
      121 vlqeqqverl gsnrqiklnf rliactnknl eqevaagrfr edlyyrlavi pitmpplrer
      181 lndiiplaes fikkystvlv knitlsestr ramlnyrwpg nvrqlenaiq rgmilnrdgv
      241 iypdalglse ndvadrselq wpaqptahia etsdlgqhgr saqyqyiadl mrkyqgnrsk
      301 iadllgitpr alryrlasmr khgievfs
//
LOCUS       WP_284345662              69 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Escherichia coli].
ACCESSION   WP_284345662
VERSION     WP_284345662.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 69)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..69
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=7910
     Region          22..68
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mktitylsdi gcleihgasl ekerqkitsi srsqawkler egkfpprkti gkkscgwlls
       61 dllwwisqy
//
LOCUS       WP_284346564              62 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Escherichia coli].
ACCESSION   WP_284346564
VERSION     WP_284346564.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 62)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 62)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 62)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..62
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..62
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=7026
     Region          4..62
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mrkmtqkeva dligvspmtl nrwlrsgkfp eccrvingyr qpgtfdratv eawikenvkd
       61 an
//
LOCUS       WP_284346976             471 aa            linear   BCT 25-DEC-2024
DEFINITION  type I polyketide synthase, partial [Frankia sp. Cppng1_Ct_nod].
ACCESSION   WP_284346976
VERSION     WP_284346976.1
KEYWORDS    RefSeq.
SOURCE      Frankia sp. Cppng1_Ct_nod
  ORGANISM  Frankia sp. Cppng1_Ct_nod
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Frankia.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12098227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Frankia sp. Cppng1_Ct_nod"
                     /db_xref="taxon:2897162"
     Protein         1..>471
                     /product="type I polyketide synthase"
                     /EC_number="2.3.1.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
     Region          4..31
                     /region_name="Docking"
                     /note="Erythronolide synthase docking domain; pfam08990"
                     /db_xref="CDD:462650"
     Region          33..>469
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
ORIGIN      
        1 mavstdeiva alraslrene rmrrrlhele avdpiaivgm acrypggast peelwrlvse
       61 grdaisgfpt drgwnlaaly dpdperpgts yvreggflyd aaefdaeffg vsprealamd
      121 pqqrlllets weaieragid rkwlrgsrtg vfigftnqdy lamhdapegf egyllagnta
      181 sflsgriayv fglagpaiti dtacssslva lhlgvralrs gecslalvgg asvmsrpgef
      241 lefsrqrgls pdgrckayge aadgtgwgeg vgvlllerls darragrrvl avvrgsavnq
      301 dgasngltap ngraqqrvir ealaagnlsv ddvdvveghg tgtrlgdpie vqavlatygr
      361 rdsgrvflgs lksnightqa aagvggvmkm vlalrngtip atlhadnltp avdwssgave
      421 vavearpwvr agrprragvs sfgasgtnah viieeapeve nregrdsdsg t
//
LOCUS       WP_284347328              77 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator, partial [Escherichia
            coli].
ACCESSION   WP_284347328
VERSION     WP_284347328.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>77
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          4..>29
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 makvsiseaa rltgksrttl hrlikagels tcrgernakm letsellrvf gafapvpveq
       61 rgeqvsgqrd tvtsdhn
//
LOCUS       WP_284347348             140 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase, partial [Escherichia coli].
ACCESSION   WP_284347348
VERSION     WP_284347348.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>140
                     /product="DNA-methyltransferase"
     Region          12..>133
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mantvkissc elinadclef iqtlpensvd livtdppyfk vkpegwdnqw kgdddylkwl
       61 dqclaqfwrv lkpagslylf cghrlasdie immrerfnvl nhiiwakpsg rwngcnkesl
      121 rayfpateri lfaehyqgpy
//
LOCUS       WP_284347519            2722 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Rhodovastum atsumiense].
ACCESSION   WP_284347519
VERSION     WP_284347519.1
KEYWORDS    RefSeq.
SOURCE      Rhodovastum atsumiense
  ORGANISM  Rhodovastum atsumiense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Rhodovastum.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2722
                     /organism="Rhodovastum atsumiense"
                     /db_xref="taxon:504468"
     Protein         1..2722
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=267814
     Region          <15..913
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          566..2224
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mtdissttdi stlttdeiaa lttsqiaslt ttqvvglttd qipalsntqi galtatqaav
       61 letedlaalt tdqvpglata alaalttrqi gtlttaqvva lttaqartft taqvaaltsa
      121 qagalelddl aalttttlva lttaavaalt tdqvpaltta qaraltttqi ralttaqlva
      181 itndqagvlt sgqtavltss qaaaleasdl avlttaalvt lttaaiaalt tdqvpaltta
      241 qaralttaqv aaltpaqaga lglddlaalt taqmvvlgta avaalttdqv palttaqara
      301 lttaqvralt tdqvvaitnd qarvltsdqa aaltsaqaaa lepgdlatlt ttslvaitta
      361 avaalttdqv pafttaqara lttaqvralt tdqvvaitnd qagvltsgqt avlttaqaaa
      421 lepgdiaalt taalvaltta gvaalttdqi palttaqaka lttaqvaalt saqagaleld
      481 dlaalttaqm vvlgtaavaa lttdqvpalt taqaraltta qvralttdqv vaitndqarv
      541 ltsdqaaalt saqaaalepg dlaaltttsl vaittaavaa lttdqvptlt taqaraltta
      601 qvralttnqv vaitndqagv ltsgqtavlt tsqaaalepg dlaalttsav vtlttaavaa
      661 lttdqvpalt taqaraltta qvaaltpaqa gvlelddlaa lttaqmvvlg taavaalttd
      721 qipalttaqa ralttaqiaa lttdqvvait ndqaraltsg qtavlttaqa aaleaddvaa
      781 lttaalvalt taaiaalttd qvpalttaqa ralttaqvaa ltpaqaatle addltaltta
      841 qlvtlttaav aalttdqvpv lttlqaralt taqvaalttd qvvaltgdqt raltstqaaa
      901 ltsaqaaale iddlvvlttt alvalttaai aalttdqvpa lttaqaralt ttqtvalgta
      961 qvaaltpvqa valttaqvva lttaqvaale tddlaaltii qvaaletgdl avlttdqvia
     1021 lttaqvqalt taqaraltta qaaaletddl aalstaalaa lttaavatlt tdqvpaltta
     1081 qarafttaqi aalttpqaaa lttsqaialt taqvvaltta avaalttdqv salttaqart
     1141 lttaqiaalt tdqvvaltta qaqalttaqa qtltttqaaa letddltalt taalatlsta
     1201 avaalttgqv palttaqart lttaqiaalt tpqaaaltta qaialttaqv valttaavaa
     1261 lttdqvpalt taqtraltta qfgalttdqv valttaqatm ltsaqaaalt saqaaaletd
     1321 dlaaltstal valttaavaa lttgqvpalt tgqagtltta qvaaltsaqv valttdqarv
     1381 ltstqaaalt saqaaaletd dlaaltttal valttaavaa lttdqvpalt saqvttlats
     1441 qiralttaqv valttdqarv ltstqaakla taqiaaleta dlaalttaav valgtagaaa
     1501 lttdqvpalt tdqtralata qiaalttaqi valttdqapa lstaqaaalt taqaqaleta
     1561 dlaslttaal aalttagtta lttdqvpalt taqiaalttg qaaglttaqv valttdqlpa
     1621 lsttqaralt tlqvpalepa dlatlttnal aalstaavav lttdqvpalt taqvpaltsa
     1681 qvgalttaqi talttaqvpv lttaqvtllt taqaaafttl qvpvlttaqa kaftttqlra
     1741 lttaqiialt tdqipaltta qiaalttaqa aalesqdlaa lttagltalt taaiaalttd
     1801 qvialttaqa ralttaqara lttaqlgale tddlaaltta gvaalttsqt salttdqipv
     1861 lttaqvaalt asqiitlttg qiialttaqa aaltsaqaat ltsdqaatle tadfaalata
     1921 aiavittaav aalttnqlpa lttaqakalt vaqlrvlstd qlgaletedl aalttagvaa
     1981 latsqtialt tnqipaltsa qvaalttaqi ralttdqvpa lttiqaaalt taqaaalttg
     2041 qvlaletgdl aalipaalaa fttaaiatlt tdqvpaltta qaralviaqv qalgtaqaaa
     2101 latvdlaals taqvaaltsa avaalttdqv palttsqvaa lntaqiralt tdqvpaltta
     2161 qaralttaqa aalttaqaat leagdlaalt ttalaaltsa avatlttdqv pilttaqvaa
     2221 lttaqmralt sdqlpalttd qakilttaqv aalttgqvps lgtddlaalt ttalaaltsa
     2281 avatlttdqv palttaqara lttaqmraft saqavaleta dlvalttaqv aalttaavaa
     2341 lttdqvpalt taqaraltta qvraftsaqa valetadlva lttaqvaalt tdaaaalttd
     2401 qvpalatvqv aalttaqmra lttgqvsalt taqaraltta qaatlttdqv palataniaa
     2461 lstagvvaft taaiaalttd qvpalttaqa ralttsqmra lttaqipalt taqapvltta
     2521 qittlttaqa aaletddlaa lttsavaalt taqipalttd qvpalttaqa ralttnqvra
     2581 lataqiaalt tdqarafatt qiaaltttqv palesedvaa lgtiqimait taalavlttn
     2641 qvvalqsaqv aalttaqvra ltslqagalt teelsgfttl qvgaltttal aaipeldrah
     2701 gfragqlavm saeqlralfd vs
//
LOCUS       WP_284347524             397 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase, partial [Rhodovastum
            atsumiense].
ACCESSION   WP_284347524
VERSION     WP_284347524.1
KEYWORDS    RefSeq.
SOURCE      Rhodovastum atsumiense
  ORGANISM  Rhodovastum atsumiense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Rhodovastum.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Rhodovastum atsumiense"
                     /db_xref="taxon:504468"
     Protein         1..>397
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
     Region          1..125
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mkptpaydiv ntellslvpr qarrvvdvgc mlgslgrevr rrspgvefig ididpeyaav
       61 aaqhctrafa cdieaiepgq wgslfpsdcw ifgdclehly dpwrllrevr rridpdgcll
      121 vclpnaqhws vqwrlasglf ryensglmdr thirwftrtt gfemfhatgw qvetglsrnm
      181 paieqqegil aalrgliaag ggdpetavqd avpfqyifrc vpgpladdtp eaarsrpkaa
      241 rlmtpssage veqaatavhl yhiaysaatl aaepgydiln nfenprpdwr eywpirkfll
      301 netldehafy gffsprfhak tglshaqvrt fvqahanrad vmlfspqpdm gafflnvfeq
      361 aelfdpglid afsaflaein rpvqlrqllm dsrhvvf
//
LOCUS       WP_284347731             128 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Paraferrimonas sedimenticola].
ACCESSION   WP_284347731
VERSION     WP_284347731.1
KEYWORDS    RefSeq.
SOURCE      Paraferrimonas sedimenticola
  ORGANISM  Paraferrimonas sedimenticola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Ferrimonadaceae; Paraferrimonas.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Paraferrimonas sedimenticola"
                     /db_xref="taxon:375674"
     Protein         1..128
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14717
     Region          2..111
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mpfqdcdpmn vvwhgnyfry leegrtalld tidfgymtmk qegfmfpvvd trmkyissar
       61 fedeliihak ldewenrlki syriinsrdg ttcvkahtth cavgiadgqm ryaspqclin
      121 rvnakvsl
//
LOCUS       WP_284347732             370 aa            linear   BCT 25-DEC-2024
DEFINITION  OmpW/AlkL family protein [Acinetobacter baumannii].
ACCESSION   WP_284347732
VERSION     WP_284347732.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006882
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..370
                     /product="OmpW/AlkL family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40015
     Region          <132..370
                     /region_name="OmpW"
                     /note="Outer membrane protein OmpW [Cell
                     wall/membrane/envelope biogenesis]; COG3047"
                     /db_xref="CDD:442281"
ORIGIN      
        1 mkiklskivi asslliftnm syaegvkrfs vsagwlhvmp qgkanpfnin tsvkngtvak
       61 vgsisptsfl nsvdpnatev dvggepfnqk eflelalndd flkgllldee gnikpevage
      121 atiqgleqwh qndaglevdd tdtlglmfny ylndnvslqf iggippkvdi kgqgeilapl
      181 sgvalsphel vkilfpygit lgqavpitnl gnkpkaasvr awtpaieaqy qfgksgvnkf
      241 rpylgvglmy ahfndiklnd eirsdlisag hmiqnvldgk agaaldrkes sgnmvvkvda
      301 ddaiapifta gftydfndsw ytvasvsyak lnnrtkidvi nqntgarlih gstkvdidpi
      361 itylgvgyrf
//
LOCUS       WP_284347814             333 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA carboxylase subunit beta, partial [Streptomyces sp. A
            4/2].
ACCESSION   WP_284347814
VERSION     WP_284347814.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. A 4/2
  ORGANISM  Streptomyces sp. A 4/2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces sp. A 4/2"
                     /db_xref="taxon:2934314"
     Protein         <1..333
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
     Region          <1..330
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 fmvretsqmf itgpdvvrav tgeeitqngl ggadvhaets gvahfaydde etciaevryl
       61 ismlpsnnre nppshpsedp adrrsevlld lvpadgnrpy dmhkvieelv ddgdyleihe
      121 rwarniical armdgqvvgi vanqpqslag vldieaseka arfvqmcdaf nipiitlldv
      181 pgflpgvdqe hggiirhgak llyaycnatv prislilrka yggayivmds qsigadltya
      241 wptneiavmg aegaanvifr kqiaeaedpd amrarmvkey kaelmhpyya aerglvddvi
      301 dpaetrevli aslamlrtkh adlpsrkhgn ppq
//
LOCUS       WP_284347825             315 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Sneathiella chinensis].
ACCESSION   WP_284347825
VERSION     WP_284347825.1
KEYWORDS    RefSeq.
SOURCE      Sneathiella chinensis
  ORGANISM  Sneathiella chinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sneathiellales; Sneathiellaceae; Sneathiella.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 315)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Sneathiella chinensis"
                     /db_xref="taxon:349750"
     Protein         1..315
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36063
     Region          17..302
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtvidkdpas aiadiqkrfe aagyicdrhi atsiylsnkl dkpilvegpp gvgktelaka
       61 taelmdadli rlqcyeglde skalyewkyg kqllytqilk eklgdileda tglgesmdkl
      121 hrfgdqffsd qflearpllq alqsekqtvl lideidksdh efeaylleil sdyqitipei
      181 gtvrakkkpi vfltsnnsre mgdalkrrcl hlyipfpdqd rereiirarv pelddrlrnq
      241 ivsfvqqlrt qdlkklpavs etidwartll llhadtldie mvrntlnlll kfeddienmd
      301 revpkmvtva ikesr
//
LOCUS       WP_284347851             409 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Sneathiella chinensis].
ACCESSION   WP_284347851
VERSION     WP_284347851.1
KEYWORDS    RefSeq.
SOURCE      Sneathiella chinensis
  ORGANISM  Sneathiella chinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sneathiellales; Sneathiellaceae; Sneathiella.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466432
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Sneathiella chinensis"
                     /db_xref="taxon:349750"
     Protein         1..409
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=46482
     Region          12..390
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 mtapadnngt faeniihfar tlrraglpvg pgrvieaira vecagierrd dfywtlhavf
       61 vnrhdqwplf dqafhifwrn pdilkrmmdm mlptnyldtg pgdanqiskr lsqalapsea
      121 pdrpdeeqtq eidihaelta sesellqskd fesmsgeele aakkamqtlr lpirecpirr
      181 tkpspmgrvd mrrtlraaqr sggdiiplrh kaparrhppl vilcdisgsm tqysrmllhf
      241 mhaltndrdr vhtfvfgtrl tnitrymrfr dvddaldavs ekvedwsggt rigstvaefn
      301 kfwsrrvlgq gavvlfisdg ldrdtgdgls tqmerlhksc rqliwlnpll ryegfepkar
      361 girailphvd ifrtvhnlqs lqelseilsr pdaaspfpss sfqerketa
//
LOCUS       WP_284347853             262 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Sneathiella chinensis].
ACCESSION   WP_284347853
VERSION     WP_284347853.1
KEYWORDS    RefSeq.
SOURCE      Sneathiella chinensis
  ORGANISM  Sneathiella chinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sneathiellales; Sneathiellaceae; Sneathiella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Sneathiella chinensis"
                     /db_xref="taxon:349750"
     Protein         1..262
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=26629
     Region          1..261
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mysfdyerps gidnaaaavg eddrflaggq sllpalklrl aqvdklvdlg giadlkgitv
       61 tdsevvigsm tthaavassa evqkaipala slaahigdaq vrnrgtlggs ianndpaady
      121 paalvglgat vhtnkrtlpa etffvdlmet aledgelitk vsfpipkkag yakfpnpasr
      181 falvgvfvaq tgsgarvavt gagpcvfrqs dmeaalagtf assavtgvkt datglnadih
      241 assdyrahlv svmagravda as
//
LOCUS       WP_284347906             478 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Sneathiella
            chinensis].
ACCESSION   WP_284347906
VERSION     WP_284347906.1
KEYWORDS    RefSeq.
SOURCE      Sneathiella chinensis
  ORGANISM  Sneathiella chinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sneathiellales; Sneathiellaceae; Sneathiella.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Sneathiella chinensis"
                     /db_xref="taxon:349750"
     Protein         1..478
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=52169
     Region          19..469
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mrfpetgnta saraglitaa ltlfmlfsgg vaqaaspdee larlkkameq sserqenlsa
       61 rldllsseir sikekavsva tkltrldrdl idteqrladi rdienqtlaa lnqqhdnlge
      121 tlsallqlsr qpegtlignp eglinslrts vllksavpel kreadqlsqq letlaslrdq
      181 hleekknflh lkesrqseqe tlnalfkskd eaqsslrqqs trearkqeql rqeardfeal
      241 ilrleeekkq rlaaerqria keiarqeklq qeaaarqrae aeaeakrrad aaknrqtggq
      301 svasiptpvp srkaeaprqe tpagkrvspa easkslaalg sgrpfskvkg slplpvggri
      361 vssfgnkrsa nkkngiviet rndavvvspy dgqiafagpf rhygllliid hgegyhtlla
      421 glgsiegavg qlvlagepvg qmnsgndenp tlymelrdkg tpvnpvpwlm agsrkvsg
//
LOCUS       WP_284348004             332 aa            linear   BCT 25-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Roseisolibacter agri].
ACCESSION   WP_284348004
VERSION     WP_284348004.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..332
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=34359
     Region          3..324
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(9..10,12,56..58,86,114..115,118..119,121..122,125,
                     129,131,139,141,143,145..151,153..157,175..176,180..181,
                     280..281,288,294..300,302..305,307)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(57,87..89,112,251,298,301)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240626"
     Site            order(88..89,116,165..169,188..190,193,221..223,227..228,
                     249..251,275..276,298,300..301)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 mrpvvavtrr lpapvearlt salttavdar lnaddrplda dgladalata davlctvtdr
       61 idaavfaeaa rrapdgrpra gllanfgvgv nhidleaara hgvavtntpg vltddtadva
      121 ialmlmaarr lgegerelra grwsgwrpth llgtsltgat lgivgfgrig qavarrahhg
      181 fgmpvrylnp sardaeaaav gatrcgtlae llttsdvvsl hcpatpatrh lidaaalaha
      241 rpgailvnta rgdvvdadal adalragrla aagldvyege prvppallal envvllphlg
      301 satvrtrram gdraldnlea flagrtppdr vi
//
LOCUS       WP_284348092             269 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Roseisolibacter agri].
ACCESSION   WP_284348092
VERSION     WP_284348092.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..269
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27547
     Region          41..252
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <172..252
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mlvlvvhnda lrslagkaaa rlaspplvld aspdarvdag ralvaalrds rdphggllvh
       61 dfapdaeasa rwldavggaw paltvlallg spagaalhql vghprrfaca dvvlgreita
      121 palgdrlaea tralgqaatv ralatgwpld alllglarha famtgdgpsw ptldallrta
      181 gvsrgtfvrh aaaagfrppl rflqllrvlg vaaavrgget aasaaarfgy gsadtlrrhf
      241 agltgltprd arhvdaddli armraagga
//
LOCUS       WP_284348081             993 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Roseisolibacter agri].
ACCESSION   WP_284348081
VERSION     WP_284348081.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 993)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 993)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 993)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 993)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..993
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..993
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=107903
     Region          41..992
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msvsrwrtaa llaapllvta pigarlaaqq ptgqaatqva vrgrvlvaet gepvvganvv
       61 argtnpvigt qtnergefsl rlpsaqytlv vsrigfaqdt ialagrtdve lrlrrnalsl
      121 sevvvvgygt qrrsditgsv tsitperlen kpnasveqal qgalpgvqvt tssagaegnv
      181 nvqirgrnsi sastnplvvv dgipyngslt dinpsdigsi evlkdasata iygargsngv
      241 ilitskrgts gkpqvaysgy tgrseyanip rlmtaqefad fkcvrinngq ncntalttte
      301 qrnlaagvnt pwvdlathsg sqqqhdfnvr ggsddtkyyl ggsllkidgv arndlldrat
      361 vranldqrls kwlsvgtntq vsqidrsgrg asfenaffan plispyeadg ttlavvpwpe
      421 dpvtnnalep llavdddltr rlftsnflql tvprvqglsf rvnagldlas sktgtywgrn
      481 tqtgravqgl atvsntlrnd wtlenilryq rgfgahnldf tglysrqgsd ldvngvrgqg
      541 fpndvlgyrs tvpllsvptv svtdydlvsq mgranygydd rylltftvrr dgysgfgsnn
      601 kygvftstal gwnaaneaff pwketvntlk vrlsygqngn qairpyrtls qlddrsylng
      661 dvaapgyipt tlgnpdlkwe tttsrnvgvd lglwndrvra tidaysastr dlllaraiss
      721 vhgittitqn igrtankgie lqlgttnidr ggfqwqteln isanrnrivd lygdkqddiv
      781 ngwfigrpid vnygyqfagi wqtgddians aqptakpgdv kiadlngdkk idpldrtfig
      841 slqpdyiagl antfrykrls lnaylntvqg vtrsnillgt nqvfsdvrrn tvyrqywtaa
      901 npintypans ntsnplsvpf yedasfvrlr dlslqydvpt tlagrigart lrvyvngrnl
      961 wtstkwtgld pelsnqrsip lerivtggln vgf
//
LOCUS       WP_284348165            1060 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Roseisolibacter agri].
ACCESSION   WP_284348165
VERSION     WP_284348165.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=113630
     Region          28..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkwakglcsl aalaapvavh aqvqtgritg tvtiapggqp laganvlvvg tevrgstgpd
       61 grftlgnvpa gshqlrvqri gyapvtqtvv vtpgqaavan atlqpqavql aeivsigygt
      121 qsrrdvtgsv atvttealdk apvatidqvl qgtapgvqvt tassepggal sirirgtssi
      181 tgsaeplyvv dgfpiendie gssagnggrt rttppnplst lnpsdiesis ilkdaastai
      241 ygargangvv iittrqgrgt kpqfgletyv gaakvaktyd llnaqqymdy antfaanast
      301 pytpfpdsvk arilaagtdt dwqdeifrta gvrnlqlsvr gattaasptr ynlsggvfdq
      361 qgvvvgsglr rlssrlnlnq afgsrvelgg sftasqarsk aipssgqqna gagaisgalq
      421 yvpilpvrra dgtysyintd lnafatqlda pqtpnpvsla revkdslsdt rllgnvfgqv
      481 dileglrfrt tfgadnanrw rytyyprttl rgeqsrgeai rassnttswl nentltyqre
      541 fggihdinvl ggysrqhtdv dgenmnntnf vsditgyydi gagtqeggpg issrrtaqal
      601 eswlsrvnys lldrylftlt yradgnsrfa egkkwgafps aavawrasse pwlrgidqld
      661 elkfrasygl agnpsirpyq slsrlndqgy sfggtpyagy ypvavgnpdl twettrqldl
      721 gvdvgfldrf tvtadyyrkr tsdlllqisl pletgfesal anrgsvenrg fefgidaqif
      781 nakdrgafsw ranlnyatnr nevldlggpd rifadlittd ynlpgsmiqk gkpigvfygf
      841 rslgiirdsa qaatvtyknf nnsafragdm lvqdldgdgv itlndrtdig dptpkftlgl
      901 tntfgwkgle ltgllqgsyg gkvlnvnrir tessprvnvs rerfldawtp tnqdakypri
      961 genpnqvgtn nftsnlledg sylrlrtltl sygiprsllr ganvtgarvy vtgtnlftis
     1021 dytgfdpdvs gqsvgntnrg idigayplar tvtaglnfsy
//
LOCUS       WP_284348221             165 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Roseisolibacter agri].
ACCESSION   WP_284348221
VERSION     WP_284348221.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..165
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17720
     Region          28..164
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mtrmlrhllv asllalpaav raqesglpvg taapaaavrt lagqptdlar yiggrptvie
       61 fwatwcpnck qlepqlqria rtygsrvrlv avavsvsqtp qraqlyarky rlpmemlwdg
      121 dgkatdayev patsyvvivd gtgkiaytgq gggqnleaal kklvr
//
LOCUS       WP_284348296             287 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Roseisolibacter
            agri].
ACCESSION   WP_284348296
VERSION     WP_284348296.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..287
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31038
     Region          40..278
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mahpsptrra flhtsacaaa glalgapsrv raqpattaav rlgvasyslr kfpraraiem
       61 vralgtpyvn vksvhadyal saaelaaarr efeaaglqlv gggtitfahd tdddvrryfd
      121 yaralglpli vatcdpailp rverfatryd vrvaihnhgp edrhypapad alrhvrtmdp
      181 rmglcidvgh tartgadvvq aiadagprll dmhakdlrdl tardsqcivg egripfpeif
      241 rqlqamryag vvnleyeida adplpgmqrs faymrgvlag laphgrk
//
LOCUS       WP_284348353             272 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Roseisolibacter agri].
ACCESSION   WP_284348353
VERSION     WP_284348353.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 272)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 272)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..272
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=29585
     Region          9..264
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 msaasnvvra ivvddeplar aglrallaed pevevvaeca ngreavdalr ahapdlvlld
       61 vqmpgldgfg vvreigvdrm pvvvfatafd qyalrafear aldyllkpft derfrevlar
      121 akeqvrqrrv gargaqlaaq laallasggv peapatpptp aaparvavrl gnrtafvrld
      181 dvdwveaady yvrlhvagts hllresmdem earldprrfv rvhrsaivnv arvrelrsaa
      241 agrhevvlrd gtrlplsrsr relvaralae ag
//
LOCUS       WP_284348441             275 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Roseisolibacter
            agri].
ACCESSION   WP_284348441
VERSION     WP_284348441.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..275
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30373
     Region          43..243
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mqrlvtawvw tlwvlivlvg fpiiclvfac tapfdkgrya pgrvfrffgs lgarlnpwwh
       61 fhttgvridd prrpyvvvsn hesyadifll cylpwemkwl akktifnipv mgwimrmagd
      121 vplvrgnras aigalarcrd rlarrasvmv fpegsrsntd ellsfkdgaf alavesqvpl
      181 lpiavagtrn amakhsfrvq rataacrvlp pidttglsss dvpalrehvr tlidgarrel
      241 laelraghrl palapapepa plplaaslpm asear
//
LOCUS       WP_284348495             695 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Roseisolibacter agri].
ACCESSION   WP_284348495
VERSION     WP_284348495.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 695)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 695)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..695
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=76325
     Region          13..684
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 msierapgpf gerpeesada qvarltrrle rerrarveae avaerglrdl yerqreivll
       61 gaisaeanra tsveavlrfa leqlcahtgw pvahvllpap pddaaaepgv aalvtsgiwh
      121 craatpyapf veatarrrfa hgeglpgril asgtplwite iaederfprw reaaaaglra
      181 gfglpvlvge qvgavleffs eatvppdgpl lelaahvglq lgrvlerkra eerlvhdafh
      241 daltglpnra lfrerlelav krarrhtdyr favlfldldr fklvndslgh hvgdrlieea
      301 srrlarclrh dallplaagt rspgedtlar lggdeftvll ddiredsdaf rvaerlqavl
      361 qepfvldghe ivtsasigvv tngridgads vdallrnada amyrakangr araelfdttm
      421 haqamarlrl eselrraler defrlvyqpi ialasgdvag fealvrwqhp trglvspmef
      481 ipvaeecgli lplgdwvlrt acrqlrawqa tfpaaarmtm svniaprqfa qpdllervrr
      541 vlvetdleas clkleiteta amgnaartqe vlqalhalgv rlsiddfgtg ysslsylrrf
      601 plqtlkidrs fidgmdreqe sreivrgiiv lattlgmdvv aegaetqeqv ahlrelscgf
      661 gqgyffqrpa deatitglla amapevapea agaas
//
LOCUS       WP_284348525             103 aa            linear   BCT 25-DEC-2024
DEFINITION  (2Fe-2S) ferredoxin domain-containing protein [Roseisolibacter
            agri].
ACCESSION   WP_284348525
VERSION     WP_284348525.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790154
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..103
                     /product="(2Fe-2S) ferredoxin domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=11096
     Region          1..97
                     /region_name="COG3411"
                     /note="2Fe-2S ferredoxin [Energy production and
                     conversion]"
                     /db_xref="CDD:442637"
ORIGIN      
        1 msqyerhvfv cdgkrcgrdg sedvrdalke cvsraglkkr vrinragclg qcghgpmvvv
       61 ypegvwyagv daaggrrige ehliggrvvs alryvappgd nkr
//
LOCUS       WP_284348664             192 aa            linear   BCT 25-DEC-2024
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Roseisolibacter agri].
ACCESSION   WP_284348664
VERSION     WP_284348664.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..192
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20380
     Region          5..181
                     /region_name="YdeN"
                     /note="Predicted esterase of the alpha/beta hydrolase fold
                     [General function prediction only]; COG3545"
                     /db_xref="CDD:442766"
ORIGIN      
        1 mittlilpgl ydsgpehwqs hwervdpsch rvvqadwetp rcgdwvatld aaigahatph
       61 ggpvtlvahs aacamvahwa rdaapaqrar vrgallvaps dpegprypag ptgfapmpmr
      121 plpfpsivva spddeyvtpa tarayadawg sryvelppcg hvnsasglgm wptgyallee
      181 lralptrvha ta
//
LOCUS       WP_284348666             138 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Roseisolibacter agri].
ACCESSION   WP_284348666
VERSION     WP_284348666.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..138
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14933
     Region          8..135
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mtaprdttpr vhrtavqmrf adtdalghvn ngsfvlyaet arleflgalg gavqslilah
       61 laidfrrqvt fgqtvvvdtw verigqtsvt ilhairadda vaaevrsvvv sfdyaaqrpr
      121 pwtdaqraal dayraigg
//
LOCUS       WP_284348841              89 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Roseisolibacter agri].
ACCESSION   WP_284348841
VERSION     WP_284348841.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..89
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9401
     Region          16..>84
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mshsplasvp sigavtcpvs eaqahgllda elsgaeagav rrhlegcarc rahvtrlshl
       61 lvalrrqrlr qerapaslha rvralarae
//
LOCUS       WP_284348902             416 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Roseisolibacter agri].
ACCESSION   WP_284348902
VERSION     WP_284348902.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..416
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46342
     Region          15..409
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mlapsdtntt sfdvnglqvi lrrvtsnevv aanlyllggt rqvsaqqagl epflleaser
       61 gtvaypreql rekmarlgsl igvdpdhdwt tfalrsttat fdstwaifad rllrpaldsg
      121 evellrgqll ngvrqrrdsp daqleylads lafaghpygi apsgteaslr ritiadlrky
      181 rqeqmvtsrm llvvvgdvdr arierlvatt lgtlpkgsyt wtppapptaq pagvaverre
      241 lptnyllgyf pgpsaaspdy yplriatavl sgrffaeirs krnlsyavha pfvdravatg
      301 gvyvttvdpr ttlalmreel rnlqegwitp rgldqlrqqf iteyfldnet nadqanflar
      361 aqlyrgdwrr aarfveelra vtpddvrrva rqylhdlrla yigdpgklde slvkvf
//
LOCUS       WP_284349023             410 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA desaturase [Roseisolibacter agri].
ACCESSION   WP_284349023
VERSION     WP_284349023.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Los,D.A. and Murata,N.
  TITLE     Structure and expression of fatty acid desaturases
  JOURNAL   Biochim Biophys Acta 1394 (1), 3-15 (1998)
   PUBMED   9767077
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..410
                     /product="acyl-CoA desaturase"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0006636 - unsaturated fatty acid
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=46524
     Region          14..287
                     /region_name="OLE1"
                     /note="Fatty-acid desaturase [Lipid transport and
                     metabolism]; COG1398"
                     /db_xref="CDD:441008"
     Region          274..>352
                     /region_name="PRK13428"
                     /note="F0F1 ATP synthase subunit delta; Provisional"
                     /db_xref="CDD:184048"
ORIGIN      
        1 mqhapspdar hehapshthd ephddiihps plafilvhva cigafwsgvp asalllclal
       61 yvvrmfgvta gyhryfshrs fktgrvmqfv lafiaqstaq rgilwwaakh rhhhrhsdte
      121 hdvhsprhmg fwyshvgwif taqhdttdfd sipdltkype lmwlerhpyl paatlaiacf
      181 alggwpalfv gffwstvlly hgtffinsla hvhgkqryvt gddsrnnwwl avitlgegwh
      241 nnhhayqrst rqgfrwyeyd ptfyilkams wlglvwelge ppadvvrner qlgraviekv
      301 srhlaesfha paiaarlqes revlehalad arhaaqhard eavakltarl aelhlphvpt
      361 ldelreaarq kyasspsmet ivlrarerll eaiarellap slagpaplpa
//
LOCUS       WP_284349037             254 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Roseisolibacter agri].
ACCESSION   WP_284349037
VERSION     WP_284349037.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..254
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=27673
     Region          4..246
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mseplrvlvv ddeaparrkl arllsampdv alageaetga eaverigalt pdlvlldvqm
       61 pvldgfgvva avgvgamppv vfvtahdeha lrafevrald yllkpvtaer lreaidrvrs
      121 rprtpaaeae raarlqalda ppapvlrhll vqdaqgarll svedvelara ernyvalhta
      181 tgtfrvrgti gelaarldpa rflrvnrsdv vrldairelq pwshgdyriv lrdgsallws
      241 rrfraeqaga felg
//
LOCUS       WP_284349131             235 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Roseisolibacter agri].
ACCESSION   WP_284349131
VERSION     WP_284349131.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..235
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25464
     Region          25..235
                     /region_name="Nnt1"
                     /note="Protein N-terminal and lysine N-methylase,
                     NNT1/EFM7 family [Posttranslational modification, protein
                     turnover, chaperones]; COG3897"
                     /db_xref="CDD:443104"
ORIGIN      
        1 mtatmpatsp dpertlrtta gdfplreyrl hvaerewavl htdavlsaad eshflgggqq
       61 qrpygvvlwp aaialahdvg aradafrgar vlelgagtgl pgivaaslga rvtqtdrnel
      121 amsvcrrnva rngladaieh rladwtawdd atrydwilgs dilyaprmhe hvrrildtnl
      181 apggrvllsd pfrraslpll eameadgwai slgkwrvged aaarpigvye ltrgg
//
LOCUS       WP_284349180             387 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Roseisolibacter agri].
ACCESSION   WP_284349180
VERSION     WP_284349180.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..387
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41473
     Region          59..372
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mpirlrrprp arlrvvvarl llagalgtsl gcasrasvva papasvaara vypgasweri
       61 aapeslgwsr agldsvrarl atmpstgfva vvggrvlmey gdvqavsyla svrksvlsml
      121 fgryvadgtv rldrtladlg iddvggltpq erratvrdll tarsgvyhaa snagddlasa
      181 pprgsqapgt yflysnwdfn algtafekmt grdiydaldt dlarpigmqd wdraaqrksg
      241 dttrsvhlay hinlstrdma rlgylmlreg swagrqlvpr dwvrestrat tpvsrmnpas
      301 hragpfgygy lwwvwdgpha tgayrgaytg lgavgqhisv lpaldlvvah ktrpgegrsv
      361 shaqyrelld llvrarcgna gggsagc
//
LOCUS       WP_284349183             376 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Roseisolibacter agri].
ACCESSION   WP_284349183
VERSION     WP_284349183.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 376)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..376
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41532
     Region          <8..376
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mtapfdptla rsaallegiv qlasegilsv daeerihlfn rgaeeifgyr adevlgrple
       61 lliperyrgr hhaehlphfa gahetsrrmg errevygrrk sgeefpaevs iskvdvdgrr
      121 mynavvrdvt errrteaalr argealarsn aeleqfayva shdlqeplrm vasytqllar
      181 ryqgkldaqa dtyirfavdg aqrmqvlihd llalsrvgtq erphrpvdta kvltgvlrwl
      241 gsaleesggt vevegalptv lgdagqleql fqnlvanalk frkagvpprv viraaraagg
      301 amweftvrdn gigfepqfae qiftvfqrlh trteypgtgv glaicrkive rhggtiraeg
      361 tpgegaafhf tlpdap
//
LOCUS       WP_284349278             140 aa            linear   BCT 25-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Roseisolibacter agri].
ACCESSION   WP_284349278
VERSION     WP_284349278.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..140
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=14311
     Region          7..140
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mskpqtspap ltledarrii aagerkaddi gqpmniavad aggnliahvr mdgawmgsid
       61 isikkawtsr afdistkela tltqsggdff glhasndgrv mifaggvplk rdgvvvgavg
      121 vsggsgkqdh evaeaaakal
//
LOCUS       WP_284349351             901 aa            linear   BCT 25-DEC-2024
DEFINITION  CHAT domain-containing tetratricopeptide repeat protein
            [Roseisolibacter agri].
ACCESSION   WP_284349351
VERSION     WP_284349351.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 901)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 901)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   3  (residues 1 to 901)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Classification of the caspase-hemoglobinase fold: detection of new
            families and implications for the origin of the eukaryotic separins
  JOURNAL   Proteins 46 (4), 355-367 (2002)
   PUBMED   11835511
REFERENCE   4  (residues 1 to 901)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20684228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..901
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..901
                     /product="CHAT domain-containing tetratricopeptide repeat
                     protein"
                     /GO_function="GO:0004197 - cysteine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=95319
     Region          119..191
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
     Region          119..146
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          159..187
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          169..900
                     /region_name="COG4995"
                     /note="Uncharacterized conserved protein, contains CHAT
                     domain [Function unknown]"
                     /db_xref="CDD:444019"
     Region          201..227
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          242..267
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(243..244,247..248,250,280,283..284,287..288,
                     290..291,320,323..324,327..328,331)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          278..308
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          319..345
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          359..387
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          632..900
                     /region_name="CHAT"
                     /note="CHAT domain; pfam12770"
                     /db_xref="CDD:432771"
ORIGIN      
        1 mtaratlvta lvalalgmag dpaasmaqat taslsdsarr ldslamalrq pplpanrrra
       61 velwtdaaal yrqlgdrare gamlrnaalr htsadtaaty lhaalglarq agdragegra
      121 lfhlganafa rgqfdsagal lpraaqiare vgerwserav vfhamgwmlw qlsdldaada
      181 slrdalalvr rvgdrraesa algdignvfa qrgrhdstfa yfqaaldvvr aigdkggeal
      241 wlynlgalhe elgrpdsalv ylrsslalar gagrthmtaa slngignvlr dlgrpdsalv
      301 alreaeqvar thqhpdvlae ilrnlgkqeq lqhrwdaara rfqeahdlyr gvgrapgvas
      361 tlaaiaelhe avgrldsari aydeglalar asqkpateae ilrnlgalha rvgdrqalar
      421 avahfdsaaa irgallvrvg tdasrvsfae tgtglferwa lawlarapei geresalaal
      481 avaergraqa llellrrgeg aeavrrrlgt ersdtpgadl vregeriaat aratgapvla
      541 llstpdtlvg wlvlpsgevt varqsigrds igqlvtavra algvdeggar alravepstr
      601 rvgrrataai grltgftlpv eltrrlstag dlvivasgpl alvpfaalpl gpageplgvr
      661 havryapsia tlgvmqasag giaarrdaig salvvgnplm psvrsstgrt lrlpalpaae
      721 rearwvadml raspltgrda teravrdrla aspvvhlath gfafsaears ldsfvafapd
      781 sasdglltvg evlgdasrlt aelvvlsacq tgmgnlqqae gtvglqrafl argarsvlvs
      841 lwsvsddate llmrrfyshw lrdadapgka ealrraqrdv ratprfrapr ywaafqlvga
      901 s
//
LOCUS       WP_284349409             260 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Roseisolibacter agri].
ACCESSION   WP_284349409
VERSION     WP_284349409.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..260
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28936
     Region          9..207
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 madttsgrrl sfviparnee aligevveai lvsiaravgv trdalwlpdt pfevvvaddg
       61 sedataaivg ryaagagvrl vacvgrtcar arnagaaatt grilcfvdad tivpadavar
      121 ilqlheregr clvlyrlasr epgvrawlww tfwglarhlp laraksmpaf mscdrahfes
      181 ygpfdeswvi aeewplteaa yryhperfly drtltartss rrmelqpfgy lrtflkwvlv
      241 vlspwartda ydhirheagd
//
LOCUS       WP_284349544             751 aa            linear   BCT 25-DEC-2024
DEFINITION  RCC1 domain-containing protein [Roseisolibacter agri].
ACCESSION   WP_284349544
VERSION     WP_284349544.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 751)
  AUTHORS   Hadjebi,O., Casas-Terradellas,E., Garcia-Gonzalo,F.R. and Rosa,J.L.
  TITLE     The RCC1 superfamily: from genes, to function, to disease
  JOURNAL   Biochim Biophys Acta 1783 (8), 1467-1479 (2008)
   PUBMED   18442486
REFERENCE   2  (residues 1 to 751)
  AUTHORS   Renault,L., Nassar,N., Vetter,I., Becker,J., Klebe,C., Roth,M. and
            Wittinghofer,A.
  TITLE     The 1.7 A crystal structure of the regulator of chromosome
            condensation (RCC1) reveals a seven-bladed propeller
  JOURNAL   Nature 392 (6671), 97-101 (1998)
   PUBMED   9510255
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..751
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..751
                     /product="RCC1 domain-containing protein"
                     /GO_function="GO:0003682 - chromatin binding [Evidence
                     IEA]"
                     /GO_function="GO:0005085 - guanyl-nucleotide exchange
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=78695
     Region          86..389
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
ORIGIN      
        1 mirfrgpvra rqltsrasea spvvpalela rrtvvalaia sgvvgchdei aplgpaqvad
       61 apnalvvstp hsfrwlatnv sgfvpcgirs dgavecwgam raylapvhvp tsgtftqvvs
      121 vvspliynvr nldpygnyft ystadrvkvc alrsdgvvkc wayfddpsfs eperehrasv
      181 grfvqvevag yndfgvcglr sdgvvqcsgh plnqngtfim dwgnappera psvpgeqftq
      241 fsmshdftcg lrsdgvvecw grntggaapp erlaapgrfy vqvttgdsft cglrddgave
      301 cwgssgsvvt errpvdgryi qvtagghaca lrtdgvvecw grnesgqapa erattngrrf
      361 vqvmasggst cavrddgive cwgynadgqa patktasgsw trreypvatf gapasvtvga
      421 sfdigfknay vpgapgetef tyrldcgdga gygaaskvna iscptsalgq rtvrgqvidr
      481 agdateytaq vsvqmqrqtv tlgyvaprtv hpgetylfta tassglpatv litaasapyc
      541 sisgsgatrp vtflaegect vvahqggtel vepafphsva ftvvrrpqti tlgslpgtvi
      601 vgarlvltat gggsgnpvtf tsltpatcat sgpsgatlai tgpgwcrvqa dqagtpaylp
      661 atpvlaelsa mtpehattml hasvieyghq eiaapllaav galrrgstae acrqldvfir
      721 vvearrtkfi rtsladawia eatrirealg c
//
LOCUS       WP_284349548             377 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Roseisolibacter agri].
ACCESSION   WP_284349548
VERSION     WP_284349548.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..377
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42255
     Region          91..341
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mptrpaplrr varaaalaal taaplaaqse tgapapqvvr mdsariaaly vsnrhedhpp
       61 adyarqmaqk rrtdsvyaar sanvmefrki tyrsrvdgmt ipaylfaplq krgakghaam
      121 iwvhggvhgd wgtsmfpfvr eavqrgyvii tpdyrgstgh geahhkaidy ggkevddvis
      181 avdflktlpy vdqdrlgmmg wshggfitah tlfrdahefk agaaivpvtn litrlsyrgp
      241 gyarsfstqk elqglpheql eeyvrrspvy haeklkvpml vhvatndrdv yyiedvqmvh
      301 tlrslkpdla etkiyvdpap wgssvghafs rrvdpvtler vdspeqidsw nrtwtffdwt
      361 lrpyedrskp appvrtr
//
LOCUS       WP_284349571             447 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Roseisolibacter agri].
ACCESSION   WP_284349571
VERSION     WP_284349571.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..447
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46970
     Region          50..431
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mplrlprqva pralsivlaa iasaacadat lgaqslprat pgdvglsaea lariapamra
       61 ytdsgklggm lvavarhgrl ayletfgtad vrtgaplasd avfrmysmtk pvtavavlql
      121 vergtlgldd pvaryipafa eaavyaggga ahptttpavr pitirqllmh tsgmayglgv
      181 lapdsianar glfvasrtva gfadtvarip lafqpgarwr ygpglevlgr vveivdgrpf
      241 eryldeeift plgmrstamr ltpalrarla gyyergpdgr lrttrgmvpq dllepaarfa
      301 cggcglvsta gdylrfaqml lndgtldgvr ilrpesaael rrdalppalg pipagnfgpg
      361 tgfglgvavq rdraspenps apgtfgwsga antyfwvdpa ngvigmvltq hhppfsypll
      421 retkqlvyaa lvapdstapa tpprrpr
//
LOCUS       WP_284349600             464 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Roseisolibacter agri].
ACCESSION   WP_284349600
VERSION     WP_284349600.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..464
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48520
     Region          31..369
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mlrslrlaac ilalpslatv lgaqpsrari varldsiaga pvargdvagl tvvvrrggdt
       61 llargyghvd laravpmtvd rvfpiasltk qvaaaavlrl vergvvgldd dvrrhvpdap
      121 tqgrritvrq llthtaglpd fadrpdpdst rardvrpmet larvrglpld fapgtqlrys
      181 ntgylllgml lerhagvsfa ehvtrtllrp agaatagycg vragatapvs ghrrtreglr
      241 vverplhpsv ahaaggthlc asaldlaawn dalhrgrvla pasyaamttg alvrgagadt
      301 lrarygfgla lstlagrrar hhggdvggya sylaylpdds lsivlllnte gpvrhvalae
      361 qliaaalgpa aperetpvra spatldalag aygdgpaafa rsgdglafvw dggppepmrq
      421 vaplaftnga srftfvvrpg appavwadlt yvvarwtrrg aagr
//
LOCUS       WP_284349661             210 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Roseisolibacter agri].
ACCESSION   WP_284349661
VERSION     WP_284349661.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 210)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..210
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23117
     Region          31..195
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mlltvldgql aaalvraegr pgerlrerwt lpwepgaaee sltdaaerla rdvmgtaphy
       61 leqigafgdg rrhpgpasls vayvglvpag aslpgdtdgd ffpvndlpal aprqramvda
      121 avahvqqrvg qapvafrllp ptftlselqe lyellldrrl hkasfrrslq aariveptde
      181 wrsegrgrpa qlfryaprrr rsaprgvrfe
//
LOCUS       WP_284349689             536 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Roseisolibacter agri].
ACCESSION   WP_284349689
VERSION     WP_284349689.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 536)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 536)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 536)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..536
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55530
     Region          27..519
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          287..519
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 msrtpaggtl rqwlawlavl aaltvgmlsv rdrldkahva lgfllvvlga saaagralgl
       61 tvaaaafvaf nlfflppyht pviadpldwl vllaflvtsi vaaqllyran atadaalrra
      121 aevdrlatlg aetlsapdad aalraivavi rttvgvdace vfrrgqvdeg ptgglvgwvv
      181 rhgrsaaels dgtvrmapgg ggpaattagv dyvvhgpesl pgwrgarppd tgdvralllp
      241 lvvreqtvgv lriassagvs lsaeaarllv alayyaalgv ervrlvetae raeaerrves
      301 lrsallmavs hdlrtpltti kgiahevatg asparaaiie aeadrlnalv gdlldlsriq
      361 agavspnvav ntadelvgaa lqraagalge ravvvdlppd ellagrfdft qalrvlvnll
      421 enaakyapad tpvtvrarrd gawlvlavld egpgvpeser erifepfyrp pgtppdvrgt
      481 glglsiargl aaaqqgtvry eprtgggsaf vfalpatdav lpedddsddg epasag
//
LOCUS       WP_284349702             494 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Roseisolibacter agri].
ACCESSION   WP_284349702
VERSION     WP_284349702.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 494)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..494
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=53909
     Region          17..484
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 msdiapaefr gdlpieefrr yaaqlidwia eylahperfp vvprvrpgdv aaqlppappa
       61 rgesladvla dvervivpgt thwnhpgffa yfsisssipg ilgellaaal dvnamlwktg
      121 paateleqva ldwlrqlmgl gpgwfgvvnd tasistllal aaareakpal airargmagr
      181 adlptlrvyc sahahssvdk aaitlglghe nvvkigvdda frmrvdlleq amerdraagm
      241 lplcvvatig ttsttsidpv geiaelcrse dvwlhvdgay ggiaavvpel hdlmdgvhla
      301 dslvvnphkw lftpvdcsaf ytrqpevlkr afslvpeylv treqdevvnl mdygvqlgrr
      361 fralklwmvi rafgaeglae rirwhvqlaq efagwvrdep gwelcaphpl slvcfrhapp
      421 gtseaereal narvmhevna sgeaflshtk lgdryvlrla ignirtdrrh varawellra
      481 atakspaagp gars
//
LOCUS       WP_284349887             379 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Roseisolibacter agri].
ACCESSION   WP_284349887
VERSION     WP_284349887.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..379
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41964
     Region          95..366
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mleirrrhag rtvlaaaava lwaapaaaqe gnepggrrpr qvvpmdsara amlyvsnrhe
       61 dhpqadfeaq lktkartdsi faarskgvmq yrkttykspv dgmeipvylf splqtrgarg
      121 haalvwvhgg vhgnwdqnyl pfiieatqkg yvvaapeyrg stgygaahyn aidyggkevd
      181 dvlgaydflk aqsyvdpdrv gvmgwshggf itahlmfrge tpfqsgaaiv pvtnllfrls
      241 fkgpgyqrsf stqkelqglp feqraayvkr spyygvdslk kpilvhiasn dedvnfeear
      301 plvdaliark pqlaetkiyw nptpgpvsvg htfsrrvnrq tllrddspeq idswnrtwaf
      361 fertlkpggg tasgmpvrk
//
LOCUS       WP_284349976             144 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Roseisolibacter agri].
ACCESSION   WP_284349976
VERSION     WP_284349976.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 144)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007442
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..144
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14794
     Region          35..124
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
ORIGIN      
        1 mrvraclaaa llapvvalag creggvtprp avsggdaerg rrmvaaygcg gchavpdvpg
       61 avgrvgpslh alaarsylag tirndpetlv rwiqdpqalr pgtampdlnv gprdardiaa
      121 flytdhaggl gpphllpkrw lgah
//
LOCUS       WP_284350065             361 aa            linear   BCT 25-DEC-2024
DEFINITION  SPL family radical SAM protein [Roseisolibacter agri].
ACCESSION   WP_284350065
VERSION     WP_284350065.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Berteau,O. and Benjdia,A.
  TITLE     DNA Repair by the Radical SAM Enzyme Spore Photoproduct Lyase: From
            Biochemistry to Structural Investigations
  JOURNAL   Photochem Photobiol 93 (1), 67-77 (2017)
   PUBMED   28027411
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Frey,P.A., Hegeman,A.D. and Ruzicka,F.J.
  TITLE     The Radical SAM Superfamily
  JOURNAL   Crit Rev Biochem Mol Biol 43 (1), 63-88 (2008)
   PUBMED   18307109
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Sofia,H.J., Chen,G., Hetzler,B.G., Reyes-Spindola,J.F. and
            Miller,N.E.
  TITLE     Radical SAM, a novel protein superfamily linking unresolved steps
            in familiar biosynthetic pathways with radical mechanisms:
            functional characterization using new analysis and information
            visualization methods
  JOURNAL   Nucleic Acids Res 29 (5), 1097-1106 (2001)
   PUBMED   11222759
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18546879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..361
                     /product="SPL family radical SAM protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=39107
     Region          40..334
                     /region_name="SplB"
                     /note="DNA repair photolyase [Replication, recombination
                     and repair]; COG1533"
                     /db_xref="CDD:441142"
ORIGIN      
        1 mrhapdddtp rlalddapap rrmlpvldaa lgvqkdivyr evasrsvlng pestgigcws
       61 lnpyvgcafg caycyaryah rytmeraggg pdeaplppwl aferrilvkr eapallrral
      121 agrsariarl lsgdetlivg satdpyqpae rrfrvtrgvl evlaehpglr vviitksplv
      181 ardvdvlarl arhatlsvhv slitldrala rrvepraptp esrlravaql aaagvdvgin
      241 cmpvlpgitd rprdlaalvr aaadagastv aagalrlqpa ardrylpwla aefpalaary
      301 ratyarghym gdayrqglhd yvvrlcerhg lrvreysrdg aararsaara gasgvqltld
      361 l
//
LOCUS       WP_284350094             263 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Roseisolibacter agri].
ACCESSION   WP_284350094
VERSION     WP_284350094.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..263
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25930
     Region          191..263
                     /region_name="GerE"
                     /note="Spore transcriptional regulator GerE (stand-alone
                     HTH domain) [Cell cycle control, cell division, chromosome
                     partitioning, Transcription]; COG5905"
                     /db_xref="CDD:444607"
ORIGIN      
        1 mptvrvvila gspvvragle sllgerpglv vvgagavgae segveaafdr vaewdadvvl
       61 wvldagmrep vasllrragv vpaappagdd gdgaeflpsg aperegaaap avvllvdrgd
      121 pgpsalaalr agaravlpad vgaatlalvt esaaaglttl padaahalla appeagdarv
      181 rvagaarvat pdgaparapa lsarerevla llaeglpnkv igprlgiseh tvkahvaaif
      241 eklgtgtrae avvtaarlgl lll
//
LOCUS       WP_284350117             743 aa            linear   BCT 25-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Roseisolibacter
            agri].
ACCESSION   WP_284350117
VERSION     WP_284350117.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Shan,L., Mathews,I.I. and Khosla,C.
  TITLE     Structural and mechanistic analysis of two prolyl endopeptidases:
            role of interdomain dynamics in catalysis and specificity
  JOURNAL   Proc Natl Acad Sci U S A 102 (10), 3599-3604 (2005)
   PUBMED   15738423
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Polgar,L.
  TITLE     The prolyl oligopeptidase family
  JOURNAL   Cell Mol Life Sci 59 (2), 349-362 (2002)
   PUBMED   11915948
REFERENCE   3  (residues 1 to 743)
  AUTHORS   Polgar,L.
  TITLE     A potential processing enzyme in prokaryotes: oligopeptidase B, a
            new type of serine peptidase
  JOURNAL   Proteins 28 (3), 375-379 (1997)
   PUBMED   9223183
REFERENCE   4  (residues 1 to 743)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 743)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..743
                     /product="prolyl oligopeptidase family serine peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=80807
     Region          42..732
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mahlpralaa vaslaalalt adalsaqtpa apaanapasp strvqyprtk avdhvddyhg
       61 triadpyrwl edldgadtks wieaqngltf gylnglpgrd likqrltemw nyprvslpyr
      121 qggrlwftkn tglqrqspyy tatgaakgaa eratlildpn eiskdgstsl slfspdptgt
      181 yvayglsagg adwrtvkvkr vadgkdlddt vdwlrysgvs wtedgkgfyy trypeppkaa
      241 gktlsnasrd pkvyyhalgt pqskdveifs fakeptwgvg agvsedgrwl fayvnrgtdp
      301 enhlyvadlk npkapdvkaa lkpidttlea sftpigvvgt tayvhtnlga pkyrlvaidl
      361 tkparaswkt iipetehtle gvslvggklf aqyladvksq vsihdlsgkk tgdlplpgig
      421 tlaglsgred epelffgfts ylvpgsvyry dvstgaveqf fkpnvpfdas ryetkqvffp
      481 skdgtripmf vthrkgiald gtnptmlyay ggfnvnqvpa fsasvatwle lggvyavpnl
      541 rgggeygeaw hqagkldkkq nvfddfigaa eylirekyts pqklairggs nggllvgavm
      601 tqrpdlygva lpavgvmdml ryhkfsagvf wvpeygsadd pkqfetlkqy splhnlkpga
      661 cypatlttta dhddrvvpsh sfkwasalqa aqgcdnpvli rieaqgshgy rpldkaiaeq
      721 adiwafaakn lgldvkferk nam
//
LOCUS       WP_284350167             127 aa            linear   BCT 25-DEC-2024
DEFINITION  bleomycin resistance protein [Roseisolibacter agri].
ACCESSION   WP_284350167
VERSION     WP_284350167.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..127
                     /product="bleomycin resistance protein"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=13984
     Region          10..120
                     /region_name="BLMA_like"
                     /note="Bleomycin binding protein (BLMA) and similar
                     proteins; cd08349"
                     /db_xref="CDD:319937"
     Site            order(10,40,47..49,51,70..75,80..81,84,118)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319937"
     Site            order(32..33,40,51,53..54,72,100,107,109,113..115,117)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:319937"
ORIGIN      
        1 maqllesrcv lavrdlaast rfwidvlgfr rdfgdgtdgw sflsrdnfrv mlgecpdapp
       61 asdigdhsyv aylvvddvda lhaelserlp epaaapvsep wglrefgirt pdghrlrfge
      121 pvvvqdd
//
LOCUS       WP_284350188             602 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Roseisolibacter agri].
ACCESSION   WP_284350188
VERSION     WP_284350188.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 602)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 602)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 602)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 602)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 602)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..602
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=66139
     Region          107..587
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          354..590
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mspparrgpl ararrrvaav lasrrrdllf vaaiattvll vgvamlsirn rwqderaamq
       61 ralveemsdv ggmmmegfha qrqameltlm apvhglvsap gdppfgldrf arytaehlag
      121 memqgdprhg vfrialdepw ptaaslqatg alrdpalasa ilahlaarrd slraplamis
      181 hkrltfrgep vgllfarert tdgrvravlg vtyspahwya higrslyekt allppsfygv
      241 dwtsvqwatr dregrprrdt fgrtdkrhnr ilnirvtqrn gnvvfrtpga tgdptheryh
      301 sfaipydgpr vdvwmsrahg drlvtaavpi gaeqwliagi avlgamfvaa tilelrrqha
      361 laeerrnfva avshelrtpl ahmvllsetm lgpaaqtseq rrrwlhvihr esmrlarlvd
      421 nvllhargeh helplerrwv dacdvvdevv ghmgaaaaar gaqlcgvtpa rcsvyvdpda
      481 lrqillnlld naikygpdgq tvtvtlnapt vadpvlrltv ddqgrgvpar drrrvwspfv
      541 rledragstg gsglglsvvr dlarrhggrv eildapggga rllltlpqdd vaddaplrla
      601 sg
//
LOCUS       WP_284350286             404 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Roseisolibacter agri].
ACCESSION   WP_284350286
VERSION     WP_284350286.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..404
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43163
     Region          24..392
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 msdtprvfak vtsdnrarma qsiglypyfa piqesttsea rigdrwkvml gsnnylglth
       61 hpkvleactq alhrygsgat gsrllngtld lhetlearla afyrkpaalv fttgyqtslg
      121 aiaalmgrdd ilyldkldha civdaaqlal gdtvryphgd laqlarqlek apegagklia
      181 tdgvfsmegs iadlpgltkl akqhgaallv ddahalgvlg edgagtarhf glddevdlim
      241 atfskslasv ggvlvgpedv lhwvrhhara liftaamppa svagtlaald vlqaeperrt
      301 rlwantrrma eqlraigldp gpaqtpilpv tvgdvfetar vwralfdddv fvhlvippav
      361 panscrirls mtaehtdaqi drvveafara vrthaprala gags
//
LOCUS       WP_284350291             329 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Roseisolibacter
            agri].
ACCESSION   WP_284350291
VERSION     WP_284350291.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..329
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=34132
     Region          4..325
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mlalvtgasg fvgshlvdal ladgwrvrrl arpasppaad arvethvaal ddaaaiarsg
       61 aladvdvvfh vagvtrahsa arfhagnvap tvalldalaa ahgaslprgv lvssqaaagp
      121 atardrprte ddppapvgay gaskhaaera vaahaagatw avvrpcavyg prdrdflavf
      181 rhaargvalf pgtrdawlsl vhvhdlaral lragtvpaaa grtyfvagde avswpavyea
      241 aaraagtrvr wardvprwal alggaagdaw salsgrdtla greklrlaap rwwlcsaara
      301 rselgwradl pleagmqatr awyraagwl
//
LOCUS       WP_284350304             464 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Roseisolibacter agri].
ACCESSION   WP_284350304
VERSION     WP_284350304.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..464
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49894
     Region          29..444
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtnptlaarr spldapprpe paaprpyhfp rferrtldng mrllvapvhk lpvvsvvavv
       61 dagatcdpqg reglaqlaah altegttsld avalaqrver lgasldagad wdgalvsltt
      121 ltrhvdeafa lfadvltrpv fpereierlk aeriaelmhl ateprglade afaravyapd
      181 sryahpeggs rtsvpaltrd dvaafhaary rpsattlvva gditldaaea larrtlgdwt
      241 geaapraaad draaaterrt hlvakadaqq selrvghvgv prshpdyfpl vvmnailggl
      301 fnsrvnlnlr erhgytygah sgfdwrvqag pfvvasavqs estaaaarev lseidrirte
      361 pvapeelsla tsyldgvfpi ryettaaiag alanltlygl pddyfdayrg riravtaadv
      421 qrvaaehlhp drlqllvagd pealraplea lefgplllte peeg
//
LOCUS       WP_284350340             119 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Roseisolibacter agri].
ACCESSION   WP_284350340
VERSION     WP_284350340.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 119)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 119)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..119
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13027
     Region          11..91
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mqlsqsrpgs ldalfhalad ptrralverl trgpasvsal aepmamslpa vlqhlqvlea
       61 sglvctekvg rvrtcrlepq alrtaeswit errtlwerrl drlgeylara sddpapgrg
//
LOCUS       WP_284350364             170 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Roseisolibacter agri].
ACCESSION   WP_284350364
VERSION     WP_284350364.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..170
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17709
     Region          83..150
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mttrvraaaa adrdaivalv prlrafgaap lrppealdra eretlerala anapdaallv
       61 aeveglgvag vayahgatdy ftgephahlg ilavaeaaeg rgvgrallea vdawaraqgh
      121 ryvtlnvfat nararavyer agyaqdtlry ykelaphapp appasdashg
//
LOCUS       WP_284350387             619 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF885 domain-containing protein [Roseisolibacter agri].
ACCESSION   WP_284350387
VERSION     WP_284350387.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..619
                     /product="DUF885 domain-containing protein"
                     /calculated_mol_wt=66737
     Region          37..614
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
ORIGIN      
        1 mhddraradg alnrreviaa laaaaalpll sacgggatpt pvasgdaaar alldevaenl
       61 lrlspeqats lgidtgaraa lrsalgdrsa egqrriaaql ktdlervral dtsglshatr
      121 tsvevvrsay atalegfalp ygditvggwr ntpyvvvqnv gayldvprfl dtdhrvesap
      181 daeaylarlt ayarqldgel grvqaaraag lvppaflldk airqmtlsvq garaggtlvd
      241 slvrrtakip gdwagrarti vvqeiapale rqlaelqaqr rvatdapgia arphgaefyr
      301 walkasttts mspdeihelg rsevarlhaq mepilkeigl tggsvgarmq alakdpryqf
      361 aegdagraei lafiherlaw iraqmprafh tvvnpnmevk rlppeeepga paayggagsi
      421 dgkipgrmwi nlrttalhsr ysladltfhe aipghvwqge ythdmplirq mlafnayseg
      481 walyaeqlad elgayatdhv grlgylqsla fracrlvvdt gihakgwtra qgvqyfvdvn
      541 gsnplevase vdrycswpgq acgykvghse ivrqrerata algakfdlra fddavvrggn
      601 vpldvlarnv deyvrtasr
//
LOCUS       WP_284350480             258 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Roseisolibacter agri].
ACCESSION   WP_284350480
VERSION     WP_284350480.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..258
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=27253
     Region          95..254
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mpprsaprpa tralprgaal latlatvval aacrasgeer aaaaapasag attatttata
       61 ggeaatgeal atpadstamr aaadrgrilg dstakvwvlm vsdfqcpyck mwhdqsfeal
      121 rreyvatgkv rmaylhypld qheqavpsae aamcasvqrk fweyqsalfg tvarwgqagd
      181 qsavydslaq gqgldmtrfr actkshvmra iveadrdrma ragvrstpsf fvgqqgiaga
      241 qpvgvfreai eaelkkar
//
LOCUS       WP_284350694             168 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Roseisolibacter agri].
ACCESSION   WP_284350694
VERSION     WP_284350694.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..168
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18360
     Region          26..152
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mtvrapdsdd apaaappgss dagrdtfart levaesdlde qahvnnvvyv qwvqdtatah
       61 wlalttpedr aqvgwvctrh eidylapall gdavvvrtrv ghakglifer htdvrrvddd
      121 rvlarsrtlw cpvdpttgrp rrvpphlral fsigeparev tdgdapar
//
LOCUS       WP_284350758             326 aa            linear   BCT 25-DEC-2024
DEFINITION  ParB/RepB/Spo0J family partition protein [Roseisolibacter agri].
ACCESSION   WP_284350758
VERSION     WP_284350758.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..326
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34414
     Region          86..284
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mrrgridpsq laaayavdes elavlkqwap qatevivrap vasihaspfq pkgrpsarav
       61 aavaaalaqs gapsvlieea gardlarlda earalvelva didehgvetp levrrvgdgf
      121 ellsghrrla aanlagladv pvvdrgaipd haaaaivyrr nllrkdftaw qeavsfsaiq
      181 rnrreaglpd svravaralg sshgragdll siarafspel lsslgagdpe laeealarlt
      241 frtlrevatl pnaddrlaaa revtglgvaa vertprsvce hvprrgggft ltvrtsperm
      301 svdearatla vleemaakvr nrlgtg
//
LOCUS       WP_284350871             258 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Roseisolibacter
            agri].
ACCESSION   WP_284350871
VERSION     WP_284350871.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..258
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27683
     Region          42..237
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mrtllaapal liltlvcggi vlvaqllgip dgpgtiyeka prwwakgmll asgtkvvihg
       61 eermrtgepr ifvsnhiswy dvlvlvaylp rysfvakaei fkvplfggaa ravgtipier
      121 enrkaafqsy eeaaarmkgg rnvvvfpegt rgpeyalrpf kkgpfvlaia agapivptli
      181 hgtievlprg sfwlragrvd vhllepvpta glaydqrdel arrvydrlaa aqqslygias
      241 palpgaaaps dtpvvrag
//
LOCUS       WP_284351038             387 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Roseisolibacter agri].
ACCESSION   WP_284351038
VERSION     WP_284351038.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..387
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42523
     Region          <163..386
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mrrrapvvlv vvgivllvaw nvvytqrvlt rirdaerrqt iilqrvfraq adsnpavaaa
       61 alqdvifqlq qsgvpmvqls adgkamggmn lpwgsdftdp ripayitqla kqntpvqdpe
      121 tgtvvyfgys dlveglrvip llqagllgal llagvyalvv rgraerehvw agmaresahq
      181 lgtplsslsg widllddevt eqgrhakpmm ksavdsmkad lerlervahr ferigrepkr
      241 ddvdvavlvd rivayfkrrv ptrsaavtvr ahrprdpvvv kgdavllewv lealtknavd
      301 alagrggkid vmverrddgt vrlrvaddgp gippklrrri fdagfstker gwgiglslar
      361 riveenhggr ialvpsdrga tfdvils
//
LOCUS       WP_284351063             145 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Roseisolibacter agri].
ACCESSION   WP_284351063
VERSION     WP_284351063.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..145
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15965
     Region          4..137
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 msrvhtselr vryaetdqmg vvyhanylaw cevgrtdwir aagmsyrdme aqgvglavsd
       61 lqmrfhaaat yddvvrvetr ctevrsrtvt feylvtradt garlvsattr liaidrqgrt
      121 mampaavrel leraaadgsa seasa
//
LOCUS       WP_284351168             491 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Roseisolibacter agri].
ACCESSION   WP_284351168
VERSION     WP_284351168.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..491
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53437
     Region          57..466
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mssplpprar wprtrrplaa lapaalalta lvalpgaara qagaasarva apriphtkft
       61 lpngltvvth edhsapvatv svhykvgskh ekpgrtgfah lfehimfegs qnvpegsfdk
      121 ylesagannn gttdndrtly yesmpsnale talwlesdrl gfllptldqk kldgqrdivk
      181 nerrlrvdnq pfgsrfevvs aaiypaghpy swpvigsmrd lsdatlddvk dffrtyytpn
      241 ntvlvvagdi dpakvrqqvt ryfgdiprgp altrpkiapv tlaaekrlvl edskarlpqi
      301 aftwpsvgir snddapltal srvltqdrts rltkllvydr qlatnvgafq gsnedvgeft
      361 invtprpgas lteierlvds vvtglvaapp taaeverykn ffavstitgl qsvfgkattl
      421 geselyfgdp ehfrkdltda lavtpadvhr varqylskgr ivlsmvpagq ltlvskpdlp
      481 yvnvtpkpav q
//
LOCUS       WP_284351181             272 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Roseisolibacter agri].
ACCESSION   WP_284351181
VERSION     WP_284351181.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..272
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28547
     Region          1..217
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mqhvpgtlgg frglraelli alkkaphplt akeladrfgl tpnalrrhld sleaeelvrh
       61 rrevrgvgap vhaygltaag ealfpqayap vlaavleavr etagpagvrq vlarqwaglv
      121 egagdrlael plperaqlva elrssqgyma eavplgdgda virehhcair dvaaqfpeic
      181 eaehelmerl lgvpvertgh mlhgcttcey tvrasapvgd ggpgpaapra delapvavpa
      241 appaladaav rstthlptct cashraapqe qa
//
LOCUS       WP_284351200             213 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Roseisolibacter agri].
ACCESSION   WP_284351200
VERSION     WP_284351200.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..213
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23049
     Region          62..172
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 msaapiptaa apaasakcaa ectraaelga vlfrnrgwlp vpffvvplvv pgtqtaaswi
       61 agaalvaage avrlagvaaa gtvtrrrsra vqrlvtygif gwmrnplyvg nflawlgvvv
      121 asgvfwflpv aallfaleys livryeegvl esffgreyld ykartprwfp rppaepesgp
      181 hhwgeawrse vstllqyvvf agvlvakqmw lar
//
LOCUS       WP_284351260             581 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Roseisolibacter agri].
ACCESSION   WP_284351260
VERSION     WP_284351260.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..581
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=63043
     Region          330..563
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mgpwrlpplr wptllllasv alttvgvvea nrairshrav aehalrdyag faawsyqqhl
       61 reslgaatqe llgavnhgeg mhtsprvpda relahyipmd aqcgchrprh gpspavffgw
      121 klgtdtlglg vnshadpmeg wevdrplayp asadrrtpft aeerawindt ltrhirrggd
      181 vgrfplviar ldsvprvlvy tlmptawgdt lvygaeysrg afagmlrrvm ndrgllpeaf
      241 trgraatevv hlqvddatga tlfasapvrd wtlddstrlp pgvgslrvra qiqpalagtl
      301 vigglprsrl pflvgllsva aalslvavgq irregelarm rgdfvdsish elrtplaqmr
      361 lyletlrlgr ftteaqrars ldnveretmr lgqlvervlr fsrlgrdddg arapvdvgde
      421 vtrivgefap laaarraqla vdaarvpvlr lrpsalrhll lnlldnavky gpvgqtvrvr
      481 lrhadgalrl evtdegsgvp aneresvwkp yqrgrtvght agsgiglavv rdvaaqhggr
      541 afieatpdgr gatfvvvlpv dpadavestv ashtapepvh g
//
LOCUS       WP_284351348             483 aa            linear   BCT 25-DEC-2024
DEFINITION  MBL fold metallo-hydrolase [Roseisolibacter agri].
ACCESSION   WP_284351348
VERSION     WP_284351348.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..483
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51062
     Region          2..197
                     /region_name="POD-like_MBL-fold"
                     /note="ETHE1 (PDO type I), persulfide dioxygenase A (PDOA,
                     PDO type II) and related proteins; MBL-fold
                     metallo-hydrolase domain; cd07724"
                     /db_xref="CDD:293810"
     Site            order(56,60,120,145,148,152..154,197)
                     /site_type="active"
                     /db_xref="CDD:293810"
     Region          274..>306
                     /region_name="RHOD"
                     /note="Rhodanese Homology Domain (RHOD); an alpha beta
                     fold domain found duplicated in the rhodanese protein. The
                     cysteine containing enzymatically active version of the
                     domain is also found in the Cdc25 class of protein
                     phosphatases and a variety of proteins...; cl00125"
                     /db_xref="CDD:444705"
     Region          370..473
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mffqrfydtg laqasyligc qrtgeavvvd pnrdvqpyld aaareklrit hvtethihad
       61 fvsgarelaa rtgarlllsg eggddwqyaf aasdgatllr dgdafmvgnv rleamhtpgh
      121 tpehlsfvvt dtpagagpwg iltgdfvfvg dvgrpdllek aaghagtmea gartlfrslq
      181 rfralpdhlq vwpghgagsa cgkalgaips stvgyekign wgvattdese fvrmvldgqp
      241 eppryfaqmk rinrdgprvl galpdavrlp adalgallrr geivvdtrpn alyaqghvpg
      301 tiniplggsf ttwagwllpy drdayllvdd atqsaaaatr alaligldrv agvlgadaia
      361 qwaasgqplg titqrtpaev aamvergeat vidvrgraew eaghlpdvpn ipvgfltehl
      421 dalptdrpvv lhcqggsrsa iaasvlharg ltnvvnmsgg ygawrqaglp vvhedaelap
      481 apa
//
LOCUS       WP_284351376            1211 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease/M1 family aminopeptidase [Roseisolibacter
            agri].
ACCESSION   WP_284351376
VERSION     WP_284351376.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 1211)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1211)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 1211)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   4  (residues 1 to 1211)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   5  (residues 1 to 1211)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
REFERENCE   6  (residues 1 to 1211)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17580737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1211
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..1211
                     /product="ABC transporter permease/M1 family
                     aminopeptidase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=131722
     Region          4..204
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
     Region          632..>1118
                     /region_name="PepN"
                     /note="Aminopeptidase N, contains DUF3458 domain [Amino
                     acid transport and metabolism]; COG0308"
                     /db_xref="CDD:440077"
ORIGIN      
        1 msklwsilrf evayqlrrvs twlyfavllg ltyqfateay idsarrggfh fnspfvvaav
       61 tllgsvmvll vaaatagdag ardvqtrmha lvysapldra sylggrflga flvsaivllg
      121 vpagvllaal vpgpeaallg pfrpavyvga yvqlalpnaf iatavafala tlgrrpglsy
      181 lgavllffvt mlawqlvavg lgrwelgrll dplaltamse lsrswtaaek naravtlega
      241 lltnrllwlg vacgllalth lrfrfahpga rswrraapda gtsaapddaa amleaarrap
      301 iaaprvrrtf draaqtrqlr rvtresfaei vtgwgglgla altvllvlai qsmtqhlgvp
      361 llpttghltt yigdtgeivw miiplliayy agelvwrerd aglheiadaa pvpewiaalg
      421 rflglalvla alqllmmgaa mlvqarmgyh dfelglyari llglqlgdyl lfallaiamh
      481 vivdqkyvgh tlvllayalt tfatslgidq pmlvyrsdpg wsysdlrgfg ptlapvlwfr
      541 lywaawalll avatrllwvr gterglaarl qlarrrftrp vgvttlaats lvvavggylf
      601 yntavlraps tgddavrrsv ayerlygrfe gapqpqlasv rlrvelhpte gaadidgsyr
      661 lvnasgvaid tvhvatatrv gtgelrfdra atralvddtl ghrvyvlaap lppgdslrmd
      721 ftvrhrprgf asggidlavt pkatyvaqse wlpaigyqpe ralsgagerr aqglpprpsv
      781 raledeaarr dmagaeritv davvgtdagq vavapgalrr twtergrryf hyatdvpirn
      841 elaiysaaya vdearwsapa gtsaqpvalq vlhhpahtrn varmlrsmra tldyqtarfg
      901 pypygqlrlv eragrsmslh aspidmwfqe gfaimnpddd prdidfayav vahevahqww
      961 gnqlmpavvq gaplltesla wysalgvveq tygrahldrl lammresyls praragqpll
     1021 rtydrlivsr kgpfamfaar eyvgearvdg alrrlverfg dgaaplptsl dlyhelraat
     1081 pdslhpllad lfernaywql aterataepm aggawrvtmd vkarkvvvds lgietelpmd
     1141 dlveigvqaa grdgepgapl yrrlhrvrgg tqrivvtvpa rparagldpr hllidvgpgd
     1201 nvsdvttgar p
//
LOCUS       WP_284351591             435 aa            linear   BCT 25-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Roseisolibacter agri].
ACCESSION   WP_284351591
VERSION     WP_284351591.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..435
                     /product="metal-dependent hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44717
     Region          31..>93
                     /region_name="NagA"
                     /note="N-acetylglucosamine-6-phosphate deacetylase
                     [Carbohydrate transport and metabolism]; COG1820"
                     /db_xref="CDD:441425"
     Region          73..410
                     /region_name="Met_dep_hydrolase_A"
                     /note="Metallo-dependent hydrolases, subgroup A is part of
                     the superfamily of metallo-dependent hydrolases, a large
                     group of proteins that show conservation in their
                     3-dimensional fold (TIM barrel) and in details of their
                     active site. The vast majority of the...; cd01299"
                     /db_xref="CDD:238624"
     Site            order(91,93,255,275,343)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mlrrplaatl llaaaplaaq tpaapapaat vlraarlfdg tgstlvrngv vvvrgdriva
       61 agaadrvtvp adarvidlgd atllpglida hvhltgeidg nfdravkdlp amealfgaan
      121 aqktlmagft tvrdvgagdf tnvaldrats lgiipgprii aaghsigitg ghcdvtgyap
      181 gileqgpedg vadgpdaalr atryqikhga kvikicatag vlsfeesvga qqlteaemra
      241 iveeagrhgl kvaahahgte gikaairagv asiehgsild deavrmmker gtylvptlhl
      301 seaialdklp apirakaesv lpnmrtsfer avragvkiaf gtdaaviphg tngrefgtmv
      361 kfgmtpadal raatsgaadl lgrrdlgala agkladvvav pgdplqdvrv mervsfvmkn
      421 gvvyrapagt qtvsr
//
LOCUS       WP_284351639             349 aa            linear   BCT 25-DEC-2024
DEFINITION  Gfo/Idh/MocA family oxidoreductase [Roseisolibacter agri].
ACCESSION   WP_284351639
VERSION     WP_284351639.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..349
                     /product="Gfo/Idh/MocA family oxidoreductase"
                     /calculated_mol_wt=36970
     Region          6..229
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
     Region          <162..324
                     /region_name="GFO_IDH_MocA_C"
                     /note="Oxidoreductase family, C-terminal alpha/beta
                     domain; cl21649"
                     /db_xref="CDD:451345"
ORIGIN      
        1 madngrtpri gvvgagalgy hhvrilrdlp garfagfheq saerraqvas elgvpafesl
       61 dalidacdal tvvvptpahy avaraalerg khlliekpit atldeadell alaerngavv
      121 qtghverfnr avraalpyvd aprfiesdrl apfsmrgadv avvldlmihd idlvrtlvgs
      181 hvsevratgv gvltptvdia narlafesga vanitasrvs rerlrkirif qqsgylsldl
      241 aagngeffrm rrdvdlakva asvastagap agpldlalfv ervpldapeg eplrlefesf
      301 vaairgeapp tvtgadgrea ldvalrivse iertlpalrg vaaqpavas
//
LOCUS       WP_284351670             209 aa            linear   BCT 25-DEC-2024
DEFINITION  KdsC family phosphatase [Roseisolibacter agri].
ACCESSION   WP_284351670
VERSION     WP_284351670.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..209
                     /product="KdsC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=22169
     Region          22..194
                     /region_name="KdsC"
                     /note="3-deoxy-D-manno-octulosonate 8-phosphate
                     phosphatase KdsC and related HAD superfamily phosphatases
                     [Cell wall/membrane/envelope biogenesis, General function
                     prediction only]; COG1778"
                     /db_xref="CDD:441384"
ORIGIN      
        1 msatisasag rthdaaptld aaramrvkwv gldvdgvltd ggiylgdvag ermefkrydi
       61 qdglgilmmr magikvaivt grvsdsvrlr aaelsvddlv qdpkarklpa lkriagergi
      121 gldemaflgd dlpdvgvlre vglpvavgna tedarraash girlsrrggh gavrefaevl
      181 lrargqweev teryvavcsa dvepavglp
//
LOCUS       WP_284351676             191 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II [Roseisolibacter agri].
ACCESSION   WP_284351676
VERSION     WP_284351676.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..191
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=20805
     Region          2..190
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 milvidnyds ftynlvqylg dlgvepvvrr ndaigveeig alrpraivls pgpctpseag
       61 itvpvvrrwg geipilgvcl ghqaigeayg grvvrarrvm hgktstirhg gtelfeglpd
      121 plpvmryhsl vveseslpes levvaraedd pteihalrhr thpvwgvqfh pesilttggr
      181 ellanflrla p
//
LOCUS       WP_284351689             177 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Roseisolibacter agri].
ACCESSION   WP_284351689
VERSION     WP_284351689.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..177
                     /product="YceD family protein"
                     /calculated_mol_wt=18965
     Region          1..164
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mlsfdirsle skaeavdgel pptdpvwveg dplpqgpirv tgrlsaagag rfyfsgrmag
       61 tatgecrrcl tdvtsevdid ahlifaeeel daegeesday pfdpserlld lrpaireewl
      121 laapafplcr edcrglcpqc gadlnedpqh thaasdprwd alrdatggaa gdppiss
//
LOCUS       WP_284351754             194 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Roseisolibacter agri].
ACCESSION   WP_284351754
VERSION     WP_284351754.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..194
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21473
     Region          41..142
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mskkpwsiqr lrvplgfvva alylwgatrs pwlswrslal gaavaviglv irawaaghiv
       61 kndrlattgp yahtrnplyf gsfllaagca lavhwallva vavfwlavya pvikrerafv
      121 sarfpdayae werhvpsfvp rvtpwrgggs aasgdappfd lklylfhrew qaalgflgvm
      181 awlaywtwrr qtgg
//
LOCUS       WP_284351756             692 aa            linear   BCT 25-DEC-2024
DEFINITION  RecQ family ATP-dependent DNA helicase [Roseisolibacter agri].
ACCESSION   WP_284351756
VERSION     WP_284351756.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Larsen,N.B. and Hickson,I.D.
  TITLE     RecQ Helicases: Conserved Guardians of Genomic Integrity
  JOURNAL   Adv Exp Med Biol 767, 161-184 (2013)
   PUBMED   23161011
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Rezazadeh,S.
  TITLE     RecQ helicases; at the crossroad of genome replication, repair, and
            recombination
  JOURNAL   Mol Biol Rep 39 (4), 4527-4543 (2012)
   PUBMED   21947842
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 692)
  AUTHORS   Bernstein,K.A., Gangloff,S. and Rothstein,R.
  TITLE     The RecQ DNA helicases in DNA repair
  JOURNAL   Annu Rev Genet 44, 393-417 (2010)
   PUBMED   21047263
REFERENCE   5  (residues 1 to 692)
  AUTHORS   Chu,W.K. and Hickson,I.D.
  TITLE     RecQ helicases: multifunctional genome caretakers
  JOURNAL   Nat Rev Cancer 9 (9), 644-654 (2009)
   PUBMED   19657341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..692
                     /product="RecQ family ATP-dependent DNA helicase"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0043138 - 3'-5' DNA helicase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=75380
     Region          9..680
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
ORIGIN      
        1 msqqvttptl ddarallrar fgypefrpgq eravravleg rdtlvilptg ggkslcyqvp
       61 alllpgltvv vsplislmkd qvdaltargl paafinstlt taqaqerftr aargelklly
      121 vaperfdfgn tadrlremgv allavdeahc isewghdfrp sylrmrrvre algdpvtial
      181 tatatpevrr diaaqlglhe petvitgfdr tnlhyhvvpv kgdrekdaal advlarndgq
      241 aivyastrks vervtevltr akiptvayha glddahrhev qdsfmnedvr aivatnafgm
      301 gidkpnvrlv vhhampgsle ayyqeagrag rdglpsevfl lhsfpdrfth effikgaype
      361 rqlveqvfer lrrdadrsgl vqygaedlav alpgkvsare vesalrvmsq adlirteses
      421 psrvhvrlla tpdrikrelg sdpmalellr alwriagkql esgaivdlda lppgmgggqg
      481 alpvlealqa rqfvvverag ggtrltdprr aladapidwn glerrrrael skvdamqrya
      541 yhtgcrrhfv lryfgdpaar nqcsgcdncl gikhtvtapa lptavpkpgg grsrarsggg
      601 asapapsqem vlgpeeaalf aalkavrgel araeqvpayv vfpdrtlael avrrprtlsa
      661 mgevrgvgpa klekygarfl talreaegte aa
//
LOCUS       WP_284351819             423 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Roseisolibacter agri].
ACCESSION   WP_284351819
VERSION     WP_284351819.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..423
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45802
     Region          2..421
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mspasafaev gprrttldng ltvlsehipg vrsvafgafv lagsiherre tmgvshlleh
       61 mvfkgtptrs akqlsleiet lggsldaytt reytsyqarv laehldiaad vigdlvfrpl
      121 lrdddlkler nvileeigmm edtpddlvfe lhnalmwgeh pygysilgtr etvgaldtga
      181 lralharayh pgrvvvaasg lvdhdalvda lvrtgwgalt pgdatplath vptasapaya
      241 hhtdkeltqt hvvfgapmpk hadprryals lvsmvlgggm ssrlfqrvre elglayavht
      301 fqsfhhdvgm qgvyvasape tarkaadair gelarlvdeg lpadelaaar rqlkgqvtls
      361 mesvtnrmyr aagqvlydep frpldevlar idaideaevl avsreffape ihtvlslgpk
      421 avg
//
LOCUS       WP_284351923             274 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Roseisolibacter agri].
ACCESSION   WP_284351923
VERSION     WP_284351923.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..274
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30528
     Region          28..154
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 msranplkdl sehfafganw adyargvdde risharqale rllgdavrgr sfldvgcgsg
       61 ihslaalqlg aarvlatdld plsvattrrm lrdhapaesd wsarqisvfd ldpdalgtfd
      121 vvyswgvlhh tgamfeaias aarlvapggl lclalyrrtl lcplwraekr lytrrsprtq
      181 rlmsglykra fqlgmrltgr dpqrheaeyr grrgmsldhd ihdwmggypy esigpvalrr
      241 fveplgfevv qqwarpggig lfgsgcdehl frrl
//
LOCUS       WP_284351926             370 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Roseisolibacter
            agri].
ACCESSION   WP_284351926
VERSION     WP_284351926.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..370
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39717
     Region          15..367
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mrvpfldlqa phhelraeid aaiadvldrg wfirgqllea feaefaqycg vrhtvglsng
       61 ldalhlvlra wdvgpgdevi vpshtfvatw lavtfagatp vpvevdpaty tidpdaiaha
      121 vtprtkavip vhlygqpadm tgvmavaerh glrvledaaq ahgardqgrr agalghaaaf
      181 sfypgknlga igdaggittd daaladrvrr lanygssrky vheeagfnar ldevqaavlr
      241 vklrrldewn arraqvaary aaaladgpva lpqvrqgaep vwhlfvvrsa ardrlaahle
      301 ahgvqtlvhy ptpphrqaay aalapaitda dpwplatrla nevlslpmgp hlaerdvdhv
      361 aaalrsfdgp
//
LOCUS       WP_284351966             620 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Roseisolibacter agri].
ACCESSION   WP_284351966
VERSION     WP_284351966.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 620)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 620)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..620
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..620
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=64259
     Site            order(8..9,12..13,15,44,47..48,51..52,54..55,98,101..102,
                     105..106,109)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          8..32
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <14..126
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          42..72
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          97..120
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          470..>612
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Site            order(495,498..499,502..503,505,529,532..533,536..537,
                     539..540,573,576..577,580..581,584)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          495..522
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          527..567
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          572..600
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msalakikkq aaqlehdrqy dkalalytrl ldaspeadde idvalynrag dvalragdtp
       61 ravtyyeral dlyaaggfln naialgakil rqaperaath ytlgvlhakk gfrsdarqhf
      121 ltyaermqrg gqggevarsl adyvvlcdga adaraglaah latggarpad qsaklqelld
      181 qalraaglgd eataefetpr aggasrnaaa adlvfldlda aaieeaaaah eapldllssv
      241 dfsepaaaea pawadapsid ldlsapaatg aplaslpgel pplapsmval dggrgdgdwa
      301 haaesplaid vdvpvgvpaf adadlasidl esavvehave apvglglell dvepldveap
      361 dtpdespvaw sdasvdlpll vddfaadvaa apaveqaaeq aeepllelea hdlvspvaqv
      421 aapapapepa paaavvpdsd gldlgawlrd sepakstrli aptmpttgde eadfqatlqa
      481 fkagiarsle dadfdahydl gvaykemgll eeaigefqka arapgrplra mealascfle
      541 rgepdlvlst lapvagtlsg dapatseapq qvalcyllga asqevgrvdd arawylrvla
      601 tdyafrdaat rlaslspptr
//
LOCUS       WP_284352032             431 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Roseisolibacter agri].
ACCESSION   WP_284352032
VERSION     WP_284352032.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..431
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45194
     Region          53..398
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msrarvtmta lllaaganva gaqpaatrvs kdapaapgal sdaatraavl aavrgvmeka
       61 iadsafpggv avvgdatggy vmhgagridw apdapapnaa tiwdmasltk vvattsamlq
      121 lvaerkvald apvqrylpdw kgprketvtv rhllthssgm pswrplykea tnaaeamalv
      181 mqtqldtlpg arylysdlna illgeivrrv sgqpldqyla krvfgplgmr dtrylppkse
      241 lariaptefd pwrqrkvhge vhdenaymlg gvsghaglfs taadlsrlar aylnggtldg
      301 trvfdaatia eftrvqdtti srraigwetp tggnsagqyl srrafghtgf tgtslwidpa
      361 rgvyvilltn rvnptrqntr iggvrtalan aavramggsp vfgsstssap spapatpaaa
      421 tprpaalptp p
//
LOCUS       WP_284352046             152 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Roseisolibacter agri].
ACCESSION   WP_284352046
VERSION     WP_284352046.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..152
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=16508
     Region          1..139
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mgmsaqvsgg svkaepnvtp lvdvmlvlli ifmviiptlt sglnaeppqg vnlkkhpeed
       61 gdqllgidrn gqyylnrnpi rnetlgaqik qiydarevdk ilyiradrql eyskvldasd
      121 ivskngvrvv gyiseqtpgt egqsidekkg gn
//
LOCUS       WP_284352082             386 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Roseisolibacter agri].
ACCESSION   WP_284352082
VERSION     WP_284352082.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..386
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40801
     Region          26..361
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrplrflsla vavvasaapr aahaqpavpd svaafvdrla realtanpag gmtvgivsdt
       61 glvwtrsygm adaargrrat astvyrigsi tkqftalmll qlaeagtvrl sdpvnrylpv
      121 idsvrrlpph appvtlvqla tmrgglaqep dslerflvgg vdewervlaa alrhtayvda
      181 pgarweysni gyaalgaala vaarrsyvah vrdailrplg mthtgfvlds agraelavgy
      241 sfehgpmdsv tprrelagrg ykvpngglfs tvgdlarflv ftmgkgpeav lpratlarqf
      301 galawatpdl tagyglgfhv mrrgslvaig hpgsvagyla tayfdpathv gvivlrnvdd
      361 pkfdilaftm svlekattga pparrp
//
LOCUS       WP_284352122             452 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Roseisolibacter agri].
ACCESSION   WP_284352122
VERSION     WP_284352122.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..452
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47915
     Region          23..451
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mtdslapevl vlgagvagla aarvlvdagr rvlvleardr iggrvltqrr edlatpielg
       61 aefvhgtpae lwavldaarl rvvdaaedhv tfdggrleer edfggalgav lgaldqearg
      121 pdrsfaefld arfadaahad arrlaasyve gfhaapiddv gvhglaraeg aasgndqafr
      181 vvdgydrvaa wlhegagapp rvrlrtvahr vrwsaghvrv eahgpdarse svfdaaaciv
      241 tlpvgvlasr pdadgavafe ppldakrdal arigaghvtr vvlrfrrrfw eereyvpala
      301 ddvdplqlsf vhapeqpvpv wwtqralrtp llvawiggpr gaamaaldre alterciasl
      361 attlgrdpad vraelvdvht hdwsddpfar gaysyarvgg adagaalarp lddtlffage
      421 ataaggntgt vhgallsgqr aarevlaalg rr
//
LOCUS       WP_284352167            1005 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Roseisolibacter agri].
ACCESSION   WP_284352167
VERSION     WP_284352167.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..1005
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=96661
     Region          <19..>1000
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mssfgllral assplrrral aiaavagvaf asactsattg dvgggslarv qlsdsvlrlr
       61 vgaegalaar vldasgqels grklfwsvrd saiatvsqsg vvtgrapgst lvsanvegrs
      121 gvatvivsar pvsvvrvept tlqlvagata plqvraldev ggevagsiva wtssdttvar
      181 vasngvvtaa apgiavitai vdgrsavvav svspvavanv sltaardtlv vgastqltlv
      241 trdaggalit nrpttwasdr pnvasvsstg evlavspgta tieatvegrs arvaliivpr
      301 paaalvispd astifvgatl rlltlvtdas gnvltnrpig ysssdpsvas vdtagvvtar
      361 vpgnvtitat segkrgtatv rvlavpvatv tiapeapavr vgdvvtltat praedgtalt
      421 gravtwssga pgiasvsang evrglasgta lilarvegas gtvtvrvdra paasvtvspa
      481 tasivvgdsa glgatvrdas gallgdrlvt wssasnaiat vsntgvvkgv aagtttvrat
      541 vdgvsgsatv titapapapa avasvlvtpp sasvaagatv qlsttvrdan gnaltgrtit
      601 wstsnpaias vstsgvvtgv aagaatitat segrsgtaai tvtgtagggt gviavasvav
      661 spstlsvvag gtgqlsatar dasgnaltgr titwstsnpa vatvstagvv tavaagsati
      721 satsegqtgs aavtvtaapp ptpapvvsva vspstlalqt gatgqlsatp rdasgnaltg
      781 rtitwstsna svatvssagv vtavgpgsat itatsegrtg saavtvtapp papvasvavs
      841 pstlslltga tgqlsatprd atgtaltgrt vtwassntav atvsstgvvt avapgsatvt
      901 atsegrsgsa avtvtapppa vasvrvtpdn sriepgqrvt lsaepldaqg rviqttlavt
      961 wtssnplvav vsssgqvtgl trgdatitat iggrsgsalv rvrpd
//
LOCUS       WP_284352191             371 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Roseisolibacter agri].
ACCESSION   WP_284352191
VERSION     WP_284352191.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..371
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40387
     Region          28..357
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mlaallahqw patfddlara vpaygdeara ldarlrmfer dkdelrafgv pietvpgeeq
       61 pgyrlrkadf ylpylavada vggsgaargr ttsaapqrid rwgyqslrvl afepeelgai
      121 aaaatraral gdpalaehag havrklafdl pldtgagedv allppraasd pavldalgqa
      181 llarktvtfq yramerdett trtvepwglf flgghwylaa rdpargdgta glrnfrvsri
      241 sevsshgkrp qspdfevpas frlrdharar qpwelgdgee evavvefrae tgatlpalrl
      301 gepvdgagia rrrfrvrrre afvrwlltfa gearpvappa lvdayreqlq rtwrvhggas
      361 srgagvtgda p
//
LOCUS       WP_284352192             357 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Roseisolibacter agri].
ACCESSION   WP_284352192
VERSION     WP_284352192.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..357
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38399
     Region          28..340
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mipphnppap rtgprtedrr rtpdtaaaql rrildlvphv adgephpiae laqhagvder
       61 trlrdlqsls srfdapggfv dglsifvete taevhtnhfl rpmgltvpel ralelglavl
      121 aaerpaegqr aidgararlr ealgtrataa aldvstagpa apldaagtat lavlrearln
      181 ghkvqlayrk aevsdaseri vapyalvvas gawylvarce tsdalrvfri drvvsavala
      241 epftvpesfd vravfregra fvtdappetl vvrygprvar wvaeregrpl dddgsltleh
      301 pladinwavr hllqygpdve vlgpdsvrqa lvervdamla sldepwsspg ttpagat
//
LOCUS       WP_284352230             464 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Roseisolibacter agri].
ACCESSION   WP_284352230
VERSION     WP_284352230.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..464
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48310
     Region          24..366
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mpprslrlaa tlalavappv halhaqppaa srdaqrsleq avdsivraag sipiegiava
       61 vtrgdavvle kaygvadrar nakatpatif evgsitkqlt aaavvrlaeq rklglddsig
      121 ahlpaladra rgvtlrhlls htsglsrawt vadltapssp rtvvdslaar avefapgery
      181 aynnngyill glvvekasgm pyadyvrtaf lqplglrstm pcdaapaarr aagyahatrg
      241 piaatvapsh hatvtysagl lcstagdlar wqralatgrv vsaeswkama tpvtlasgrp
      301 aryglgveig avdgqrylah ggatpgflge taylpdsalg vtvltngvya gsivtrlvqt
      361 varqalglaq psiadlpmta aerarfagtf dlgpvklevy eqgdhlraqp pgqvaarllh
      421 qgdgvfvaeh dpalrfrfqv egeragtlvi eqggramppa krss
//
LOCUS       WP_284352238             385 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Roseisolibacter agri].
ACCESSION   WP_284352238
VERSION     WP_284352238.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..385
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40605
     Region          34..350
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mqhalalaci tvgascrpri ppalgaeplg dvqttvllig dagdpgrhar agaepvlral
       61 araaseradr ttvvflgdnv yddgvppeeg spgharaesi lrrqltaedg ippvvrrifv
      121 pgnhdwndhg rrrdprgadr vraqrdvlrr ldgsgaatls ppascpgpev hdvgprlrlv
      181 aldsewwlqp gggagactes gvphdsassv dalraatata gdrhvvvvah hplltggehg
      241 ghctrwlslc sikrlfsggn wqdtpsrana rmrqaitaal rdrpallyaa ghdhtlqvlr
      301 gtggsapaar ylavsgagiy gnqsqvkcld eslaairapg fmrldvradg sarltvltvd
      361 rdgnaterar vwltrddsst tpcgr
//
LOCUS       WP_284352354             341 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Roseisolibacter agri].
ACCESSION   WP_284352354
VERSION     WP_284352354.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..341
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36804
     Region          34..330
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mssappsvat apqatgddva llrelaaarr aladqiarrv vgqhevvdhl ltallaggha
       61 llvgvpglak tllvqtvaqa ldlqfsrvqf tpdlmpsdit gteileedha tgrrvfrfvn
      121 gpifgnmvla deinrappkt qaallqamqe havtaagtth rlpepffvla tqnpieqegt
      181 yplpeaqldr fmlelkvgyp sreeeerivt attganearv epvlsaerlg amqrlvrrlp
      241 apptvvqyav qlvrgtrpde aeasaamkky vgwgagpras qalvlaakar aamdgrpmpd
      301 lddvravalp vlrhrivlnf qaeadgmtve klldlrerst r
//
LOCUS       WP_284352385             571 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Roseisolibacter agri].
ACCESSION   WP_284352385
VERSION     WP_284352385.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 571)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 571)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 571)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 571)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..571
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=62683
     Region          93..571
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          338..571
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mrrargwwvr rwrvwvasla vvatltavga aalqqwiawr tedalvqral vrsaaysari
       61 fddgiqrqlg dlplhalspv lgapawgtsa eplplaaler hlrttpmwqt lqrdsvlaig
      121 vvdyragqgr risvrrvgrv adsvdaaaai aqvmtgseqw rglnttgmsf rgpgarlynv
      181 lwawqkdard rpvalvllvt dahlrlrtat svvfryvpll ppldeadtsp eraraswsep
      241 ngrddtrtfn hryiavrlre yagqrrvffa spnwndawva ssplrgehps lfgalmveav
      301 vnpelrayfp esrasrsaqt mlggilalaa ilalasvasl rrrqelaqar elfvssishe
      361 lrtpltqirl ftesllndra rspeqagrwl rvidrearrl gdlvdnallh arglrhdvhl
      421 arvpvaledp laamveatrp fatsrdarva vdvppgvrvl gderalrhvl qnlvdnalky
      481 gpagqtvrvt aafdapgtvd vavddegpgv aiadrrriwe pfvrlahddg atgtglglsv
      541 vhtlvcagrg rvrvedapgg garfvvrlpl a
//
LOCUS       WP_284352483             282 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Roseisolibacter agri].
ACCESSION   WP_284352483
VERSION     WP_284352483.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..282
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=29748
     Region          4..277
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mlephwslav laflfgsaig sflnvcivrw pegesvvrpr srcprcgrpv qalenvpils
       61 wlvlrgkcrg cglpisplyp aiealvglgw laayftygpt ldalrvavfg tvllgiaatd
      121 arrylipdgf tvflllwvla tsliargaga atlfaspyea ligactgaga iaiigwlgel
      181 afkkeamgfg dvtmmaavga algperallt vivgafvgav asvsvivpaa wvlhrrrlvq
      241 gdadaafelp pvpfgvflap aalltllwgd rmiawyfatv lq
//
LOCUS       WP_284352596             807 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Roseisolibacter agri].
ACCESSION   WP_284352596
VERSION     WP_284352596.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 807)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 807)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 807)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 807)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..807
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=83146
     Region          26..806
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtrrsaaant ttadasgags vtmaattcel rvggmdcasc aasveralks legvqdvrvd
       61 vvggkvrvgy aegtlargdl arairrvgyt vedtndrvsr raaflvdglc caaearqled
      121 rlgnlpgvtt lefdvmrhrl ivegtitape vqraiqdlgm taraegeqaa pasfwrrrgr
      181 lvmtaasggg valglaatla glpagvelal lgaatiaggw fvvprgvraa mhraldmnvl
      241 msiaaigawl igepeeaaat lflfavaell eshsmdrarn aikalmdhsp aeatvrrdga
      301 evrvpatdvq agetvvvrpg eklpvdgevt ggrssvnqap itgesmpvdk apgaevfags
      361 lngqgvlevr stkpasdttl ariihaveea qasrgpsqtf vdrfaraytp lvvlvavlvg
      421 vvppafgwgt sdawvyrala llvvacpcal vistpvtivs glagaarggv likggahlet
      481 agtatvvcld ktgtltegrp avtdvvpfgd aapgaqafdg ilrlalgver hsehplarav
      541 ldagaargla apesvdfeal vgrgarahvg savvylgner lleerrlltp pvraafarla
      601 aegktavava verheaglrt gevlgvlgla drlrpnarta ldalraagvr rlvmltgdsh
      661 gtaravaaav gadevhaell pddkvrvvre legrgervvf vgdgvndapa laaasvgvam
      721 gaagtdvale tadvalmadd letlpfamrl srktlgivkq niafslavka vflvlavggw
      781 atlwmavaad mggslvvvan glrarrl
//
LOCUS       WP_284352644             459 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Roseisolibacter
            agri].
ACCESSION   WP_284352644
VERSION     WP_284352644.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..459
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=50314
     Region          24..424
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mfayalepsl mfagrsfald arcaqqrlly aeirrsrwvw nravalarrl rriavaakaa
       61 grpvpavcrt sypalcrrlt vwrrrrpwla agsvvpqqqt lktyvqaean alagrarwpv
      121 fkkrrdplgl ryplphatls dttltlakvp ggirlrrssp dlgalrhvtv ahdgvrwtvs
      181 vcyaaapvpv pehprmaala sgddsaavgl dfgvvstwtr tvgaegqaav qiarrspaqr
      241 rrtarlgrqr srrrkgsrgw wrsvraeqrl qrrvatqrre qvrqlaqdlv rdhavvgfee
      301 lhlrsmtarp rdrsgvrngr aakaalnrrm legafratvq atrwaarktg avvattpapy
      361 tsqtcaacgh tasenresqa gfrcqrcgha ahadgnaahv vrqrvlvalg lrpavgceta
      421 gpsppdgrrr kplgepgaar alagnlepae rpvafarag
//
LOCUS       WP_284352746             477 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Roseisolibacter
            agri].
ACCESSION   WP_284352746
VERSION     WP_284352746.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..477
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=51871
     Region          61..477
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mfkrvagrla lwglllalal laligvlsvt rgtpveyvia rgdpagppap adtlfvrtve
       61 lyagtslhpg nrvqvlengd gtypllwrdl rtcqravtvq myfaqpgaia dtmaqvltec
      121 arkkarvlll ldgfgaqtla ekwveklkaa gveiawlrql rwytlhkaae rsharvvvvd
      181 grvgytggfg ladywlgagr kpdewretnv rfegpavaql qaafgstwae atgelltgda
      241 ffppvsfkpv adgdsvspvg vqrpvlrsgp graasaerpp padapvvara vaegtvragl
      301 lhavpstgst qaerflalti agarrtlyit nayfvpdddf rrllaaaakr gvdvrimttg
      361 prtdvqttrf agrfryeell ragvkvyeyq panmhaktms vdgvwgsvgs mnfdnrslaf
      421 ndettllvhd savvagmdrm fledlrhsre mtvaemakrp wwikardgga atlqrvl
//
LOCUS       WP_284352754             437 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Roseisolibacter
            agri].
ACCESSION   WP_284352754
VERSION     WP_284352754.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..437
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=46499
     Region          1..435
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mlsvlvvddd dtiretlvdf fdslghvtrg artategrqv aaahspdval vdlrlpdadg
       61 lrlmealrad hpevavillt ghgdvatavr amregaadfl ekpidlaald aavrraaeha
      121 rlarevavlr areagalwte tapaaerapv pdldrlvela arnddapvlv igetgtgkgy
      181 varqihersp rraqpwvein caslsatfve selfghekga ftdarqakrg lvevagrgtl
      241 fldevaelap evqpkllkai eerafrrlgg tatltsdarl ivatnvplad avargrfrad
      301 lyyrlqvlti alpplrtrrd eipalaaall prgarlaesa raalqaydwp gnirelknal
      361 wrasiladga pitpahlglt psngaavapl ddpvtladae rraiaaalaa tggnraqaaa
      421 rlgiarstlq eklkrgg
//
LOCUS       WP_284352795             303 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Roseisolibacter agri].
ACCESSION   WP_284352795
VERSION     WP_284352795.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..303
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32050
     Region          53..298
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mrraagaaiv avlvsaacad aqprvpardp vtldlpardt anpmalvelh fpsggarlng
       61 llylapgkgp hptvvllhgy pgnernldla qamrraglnv lffhyrgawg sggefsfdna
      121 qadvaaalrf lrdsvnatrh ridrrrlalv ghsmggwlal rgaaadptva caaglefwdv
      181 gregvamrkd saaraeflay ttditapgap lraaggaaal vkamldrgde walaasapal
      241 rarpvllldn tantshapla dalrkagnar vathvwptdh sfsdrrvgla rtvidwlrtd
      301 crl
//
LOCUS       WP_284352834             310 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Roseisolibacter agri].
ACCESSION   WP_284352834
VERSION     WP_284352834.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..310
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32710
     Region          16..310
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 msaergapra erslirsvll ivnpaarqaa areadaceaf vragvactva rtaraghaae
       61 lavareavda vftlggdgta mevvgalahg dtpvgilpgg tgnlmartlg vplgvrdava
      121 sllhgdvari dlgvveaegq aprrfafaag vgidarmiee tparwkrrlg vlayaltaar
      181 aliardrftv rividgveel rrdaaavmiv nfgavlgdlf hfgpgiradd grldlclfsp
      241 esvgdavrvs wrllrkdfrd drcvvyraar efrietvpqr aaqadgellg rtplvarvep
      301 laatllvpas
//
LOCUS       WP_284352873             506 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Roseisolibacter
            agri].
ACCESSION   WP_284352873
VERSION     WP_284352873.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..506
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=55363
     Region          15..491
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mtdpadradd pdrkqqlril ivdddrtlre gcanvlqldg hqvvtfarge daieaaqrqh
       61 fdialvdlym tpvsgmdvlr aigsadretl vvvmtgnptv asslealrag awdylpkpfs
      121 ashlqvlvgr aahaaragss tvtvretrsl hsspaaaapa aaavaeeddi ligespafrq
      181 aiamakrvaa tdasvmifge sgtgkeliaq yihrhsrrtn rklvpvncaa ipgallesem
      241 fghkkgsftg adrdkpglle manggtffld elgempmplq akllrvlqdg vvrrvgsekq
      301 davvdvrfvs atnrdpreav qsgllredlf yrlcvvpirl palrqrpedi allarhflqr
      361 fwsrhrkagt plpvlteesi aflqtrpwkg nvrelqnvme hvtvvaepgr pispddipiy
      421 edapmeqggt aglpatifne sfhtakeqlv thfereyltr ltaraagnms kaarlasidr
      481 ttlyrllekh nirrddagaa latfgd
//
LOCUS       WP_284352874             811 aa            linear   BCT 25-DEC-2024
DEFINITION  GumC family protein [Roseisolibacter agri].
ACCESSION   WP_284352874
VERSION     WP_284352874.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 811)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 811)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 811)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..811
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=87764
     Region          36..788
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 msaslppalp sghgsalepy ahphtppvvy rgdagegdqs gggeigrvls alnrfkwlvl
       61 avlavgsagg vmatrlltpe yqvqstillt gaqggsssrg plrddallda qgwqdllrsy
      121 siadsvvmql alylepkkaa dsvvfrgfql nrarfypgqy tleisgpryt lrdnigvine
      181 tgvvgdsigr kaagflwrpt kavlgddrti efrvrtpret svgilqrlnv elaqgsnlil
      241 lglsgtpqqk paetlnawge qfvriaadlk tarlsqfvri ltaqraeaeq rlrnaemalt
      301 qfrvntvalp seglamkpgl sgiamrepvf dqyfkdrydl qtvqrdraql daaaakvtpt
      361 etpieallai psvasdpgam tlreslnela kkqaqyrtlk eqftdsmrvv kdalygiqll
      421 qsttipqqla ayraelakre atmqstiaka tselqgipsr siqqeayrrd ldnatqlyas
      481 lqarsadael seksaipdvr ildqavmple ptkntaprii lmaiagslgl gvglaflldr
      541 ldrrfryptq atrdlalqil gvvpvveqgr rasaekvanv veafrslrmn vryacmpsqk
      601 vtlaitspgp gdgkslvasn lalsfaeggw rtvlvdadlr rgflnetfel patpglieyl
      661 egtsplddvl nathhanltv iaggtrhrra pellatprmq elvatlarsf daiiidtppl
      721 gagtdayaia tattnvaivl rggttdvkma kakmetldrl pvsvigailn gvqtddgiyq
      781 yysydphytl aavedreape eaevarigdg r
//
LOCUS       WP_284352905             414 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Roseisolibacter agri].
ACCESSION   WP_284352905
VERSION     WP_284352905.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..414
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=43979
     Region          56..383
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mlltllwvgt vtralplmsg sgaweraaat geralalarg rgsdpaaara ydaheqelrr
       61 slelarrysf vapragrvll atgvigvall ivgtsrvagh lsrqlsrpld qlvrwtalvq
      121 agqplpdepe prgapefrtl rqrmrtmsre laegrarale aeraeafret arrvahelkn
      181 pltpirfave rlrrdatpaq aeavevlaae tarleamars faqfgrlpdg paadvdlgdl
      241 arwavatsvp eqlegrveva ddvplvhghy dalaralnnv llnaveacap ggrvtvrvqr
      301 arcpavpgda velavhdtgv giapellari wdpyvtqkah gtglglaiar qtvqahggiv
      361 davsavgrgt evrfilpvgg agatpgrlps adprhdapar daavppplat rtia
//
LOCUS       WP_284352909             456 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Roseisolibacter
            agri].
ACCESSION   WP_284352909
VERSION     WP_284352909.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..456
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=49088
     Region          1..454
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mpsvlivdde anirrmvgal lategydvrd aadgnagvas alahepdval ldlmmpgldg
       61 lgalerlrea ypdlpvvmms gragladavr atklgaftfl ekpltpegvl lalasalelr
      121 qarraaralr edlglggemv gaspamlkvr eliarvgpsd arvlitgesg tgkelaaaai
      181 hvasarrerp firvncaaip rdlvesemfg hergaftgat errigrfela htgtlfmdev
      241 gdlgaeaqak llraieakei ervgggkpir vdvrivaatn kdlaravtdg afredllfrl
      301 nvipihlppl rerpddvpll vrhfsalyra rtgrpapawt dealallvrh rwpgnvrela
      361 niverlailh agepvteshv rqvlavdrgt psdgvpvtlp dpsdlgasln daldgyertl
      421 ivralavaqg nvaeaarrlq tdrpnlyrrm krlgiq
//
LOCUS       WP_284352949             297 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Roseisolibacter agri].
ACCESSION   WP_284352949
VERSION     WP_284352949.1
KEYWORDS    RefSeq.
SOURCE      Roseisolibacter agri
  ORGANISM  Roseisolibacter agri
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Roseisolibacter.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Roseisolibacter agri"
                     /db_xref="taxon:2014610"
     Protein         1..297
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30878
     Region          9..289
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mpaaaagcrt iavpdpesat pipivvlypa dapahptrlg pytldvamda pvaagtyplv
       61 lvshgsggsh layrdlaahl aragfvaalv ehpgnsrndn srvdteanla arprhlrlvv
      121 dhltadvavg phlapdavai vghsmggyta laaaggrpta fpretadgms revpvprdpr
      181 vralvllapa tpwfmapgal rdvrvpilml taehdphtpe ghavivkrgl ppetplthrv
      241 vpnaghfsfl gpfppamtha gfapsqdppg fdraafhael hgevegflrg vfgsatl
//
LOCUS       WP_284353111             496 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Pseudomonas putida].
ACCESSION   WP_284353111
VERSION     WP_284353111.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..496
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52365
     Region          58..473
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 msdrraprpt llatgirala latvlaapal adnaakadts aarpantlqs laeldgkaps
       61 rrqlniqhws taegarvlfv earelpmfdl rvtfaagssq dagtpgvaal tnamlnegva
      121 gkdvtaiaeg feglgadfgn gsyrdmavas lrslstkdkr epalklftev agkptfpeda
      181 lkriknqmla gfeyekqnpg kiagkalfgn lygdhpyahp sdgtadsing itlaqlrafh
      241 akaytagnav ialvgdlsrs eaeaiaaqvs aglpkgpala apaqpaepkp glthidfpsk
      301 qthlmlaelg idrqdpdwpa lslgnqilgg gafgtrlmse vrekrgltyg vysvfspmqv
      361 rgpfminlqt raelsegtlk lvqgiladyl kqgptqqeld dakrelagsf plsnasnasi
      421 vgqlgaigfy nlpltwledf mqqsqaltve qvkaamnkhl sadklvivta gpkvpqkplp
      481 aptdkpseqp lgvpeh
//
LOCUS       WP_284353112             451 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Pseudomonas putida].
ACCESSION   WP_284353112
VERSION     WP_284353112.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..451
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49945
     Region          16..449
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mnalarraag llfgtlclpl aafaadvqpt hefildnglk vvvredhrap vvvsqiwykv
       61 gssyetpgqt glshalehmm fkgsakvgpg easrilrdlg adenaftsdd ytayyqvlar
      121 drlpvalele adrlaslrlp adefsreiev ikeerrlrtd dqpnskafel framaypasg
      181 yhtptigwma dlermkveel rhwyeswyap nnatlvvvgd vtadevkgla qkyfgsipkr
      241 avppaklple laepgqrqlt lhvrtqlpsl iygfnvpglp takdprtvha lrlisalldg
      301 gysarmparl ergqelvaga sssynaftrg dslflisatp nvqkqktlad vekgiwqlle
      361 elkttppsae elervraqvi aglvydrdsi ssqattigql etvglswkli dseldelkrv
      421 tpqdiqdaar tyftrerlsv ahvlpeesah e
//
LOCUS       WP_284353208             262 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudomonas putida].
ACCESSION   WP_284353208
VERSION     WP_284353208.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..262
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29355
     Region          28..242
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mplvarlfci lllaclspla lgerlrlvsd dwapyiyqhn gqprgidyev tsevfkrlgv
       61 evewqflpwk rclamieqgl adgildifqn earhpylvya peplsqvefv lfqararrhp
      121 vtglddlagl tvgtspgyay gaafneatqf rreaaptqea nfgklllgri dlaitdrkvg
      181 hyllrqlgle qqveelplli nhqaqylglv rkpgrealal afaeelqrfk qepafaaish
      241 rytgdignil naveqqesst ar
//
LOCUS       WP_284353226             245 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudomonas putida].
ACCESSION   WP_284353226
VERSION     WP_284353226.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..245
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27159
     Region          28..245
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mrpllcvlgl lammlatpaa ghdklrlvad swppftdasm pggglatsiv ttalaragya
       61 stfeeapwar allgvsegry dvlinawqnd ararigqfss ayltnrirll qrkgeafhyk
      121 gqsdlypysi avvrdyaysp efdgdtrlhk vpvrsfssav rmlaagrvnl avedeyvary
      181 nlqrepqevr dgvmlveppl gentlhilvs lkhpehkriv erfeqaiaam kadgsyarlm
      241 rqhgf
//
LOCUS       WP_284353501             355 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Pseudomonas putida].
ACCESSION   WP_284353501
VERSION     WP_284353501.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..355
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=40108
     Region          51..>312
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 melpffydfs edeqefllaa algnrgvvvk rlngvcgdif vmdqgesvnp ryvcakvprk
       61 letvpavean krfvqelalq lrfshhtfvh wcfdlrevlg apvalfrywd gdlldymsgq
      121 seirqlslia yccsglihcy srglachqdl kpanifvrdf ekvinglrni diyqvamiad
      181 fglanaflkt pavfegsrpy mapeqwgrtq lsektdvfal giilyellts gvhpvgvrtd
      241 dvwpsakpgh stkwtrskew qkwiargcll htevnltsdi islvqrtlsv dpderpsmmg
      301 lrdeilslik arceishfql sgvighfdgn askgdladew pylanawarf qkrfg
//
LOCUS       WP_284353676             269 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Pseudomonas putida].
ACCESSION   WP_284353676
VERSION     WP_284353676.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..269
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28958
     Region          <80..267
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          186..267
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mprshaalwr npalahvesr rachsracyk ahshptfsig avdagnshft gaadgqerlt
       61 pgtlvfvpah rvhacnpapg qawsyqmlhv daewltqlrl esglsgagag eparicrepq
      121 vyrqfcelng llfsrasnge keaaliaflg dldvstqptl saapaleana lggllrrieg
      181 qdpshlslea larqaglgry qlirafraat gftphaylln arinrgrqll gegaalaeva
      241 yqlgfadqsh fqrvfkahvg vtpgqyrgr
//
LOCUS       WP_284353687             331 aa            linear   BCT 25-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Pseudomonas putida].
ACCESSION   WP_284353687
VERSION     WP_284353687.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Rengstl,B., Oster,U., Stengel,A. and Nickelsen,J.
  TITLE     An intermediate membrane subfraction in cyanobacteria is involved
            in an assembly network for Photosystem II biogenesis
  JOURNAL   J Biol Chem 286 (24), 21944-21951 (2011)
   PUBMED   21531723
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Komenda,J., Nickelsen,J., Tichy,M., Prasil,O., Eichacker,L.A. and
            Nixon,P.J.
  TITLE     The cyanobacterial homologue of HCF136/YCF48 is a component of an
            early photosystem II assembly complex and is important for both the
            efficient assembly and repair of photosystem II in Synechocystis
            sp. PCC 6803
  JOURNAL   J Biol Chem 283 (33), 22390-22399 (2008)
   PUBMED   18550538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..331
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=34777
     Region          52..249
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          143..320
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
ORIGIN      
        1 msvfkrcsvv mlalaalhga ahaapftdvl dvpampsala assalrdvtl agqrlvavgp
       61 rghilysddq gahwqqaqvp vsadlnavsf atpelgwavg hdgvvlhsrd ggvhwqkqld
      121 grvlaeqlpa aatdnalldv wfsdarngya vgvfnlllrt ldggehwqpw ldhsdnpqgl
      181 hltslaavgd dlfitgeqgl llkwdgerfs rvetpyagtl fgavgkpgvl lvyglcghvy
      241 rstdggqqwq pvntgintsf taagidrdgq lwlasqagdl llsrddgasf spvpqnargp
      301 vaalasdtgn glvlvgergv rnqagnptlh p
//
LOCUS       WP_284353712             348 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Pseudomonas putida].
ACCESSION   WP_284353712
VERSION     WP_284353712.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..348
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36986
     Region          21..332
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mtlprcmlal allgsllaha eaapwvaglh hmtladpvdn rpmqalafyp avgkthssri
       61 dgypidvaee apvamgqfpl lvlshgntgs plalhylats larqgfvvva vvhpgdnard
      121 hsrlgtlsnl ygrplqvsaa igaarddall gpylnegkvg vigysagget alilsgarpd
      181 ldrlrqycle rpndtdackt hgiliadrse lapqadqrvg avmlmaplsl lfgrhalagv
      241 qvpaliysgd sdqlvavdrn aealarklpv tpdyrllaga ghfvfmahcd aeqyarmpal
      301 ckdaegvdrr hihhsleret aaffsqalga pqvgersaea gatrqqqr
//
LOCUS       WP_284353820             460 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudomonas putida].
ACCESSION   WP_284353820
VERSION     WP_284353820.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..460
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=50467
     Region          30..412
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 msakyqlsql pnkplwfapg psrerldgst qadvvivgag ytglwtayyl lksdpslrvv
       61 llekhevgfg asgrnggwas aifpislhrv eqlyshnaal hlqaamndtv deigrvlale
      121 gvdadyakqg flslarskpq rdraraaves sarfglpdqw rvldaaeaqa rvgaqgtlgg
      181 lytehcalih pgklvrglar lvegmgakiy eqsavnqmap gvvqtahgsv raemtvrate
      241 aftsqqpghs rfviplyslv lateplpsdl laklnldhrm afndmrhlrv ygqvtaegrl
      301 vfggrgapyn wgsrmsaedd lvdsihgkiy dtlleffpvl rdarithrwg galgvsrdwc
      361 ptvsidrnkr mawagnyvgd gvatsnlagr llrnfilerd edintlplvn hrspswerep
      421 lrwfginsgl aaaslsdiee rfthkpsrta mllekltgah
//
LOCUS       WP_284353823            1288 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Pseudomonas
            putida].
ACCESSION   WP_284353823
VERSION     WP_284353823.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..1288
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..>1288
                     /product="beta strand repeat-containing protein"
     Region          2..1288
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 matisgndga ntlsgtsrad tlnglggndt lngndgndil dggtgndlli ggggndsyrf
       61 gggygndvid nsggqandld siqlvnlnas qirltrvgnd lvltllasge tltvsqhfld
      121 anhaidriqf adrttwnasa iqanlyylpv tptagadvln gnpdndvlqg lggndtlfgn
      181 ggndlldggs gadrmeggig ndtyvvddqg davveaansg ddtvqasidy tlsanverlt
      241 qlgtgnlkgt gntlantlig nsgnntldgg dgadnlqgga gndtllggag ndslaggdgn
      301 dvldggagtd slaggtgddl yliaqagdsi seaggegsdt vrasiaytlg anlenleltg
      361 tgnlagtgnv ldnrltgnsg rntlngglgn dwlagrqgnd tyvyglnggn dlvdnsggla
      421 advdtlqltg lnpadvrflr sgndlvmlvs snlqtltiks fylgadfeid rvqfangtvw
      481 tkatllanvq agatngpdvl fgsngddliq alggndeira lggndtlegg tgddamygga
      541 gddlyqvdsa gdqvnevage gsdtvrasis ytlgsnvenl tltgsanldg vgnasnnqlq
      601 gnagnnqlsg gagddsldgg vgddtlrged gndtllgggg vdflwggagd drlivgngqv
      661 gtfllgeagn dtfdarslsn gsganliggt gndtylvdgt gdlsisddng lgqfnvvqfs
      721 anispgdlhf vrpadrfnds gnmliefpng hrlfigsmgl aypqdsgegf gvqafrfadg
      781 tewnraeilh ragwyfgttq ndsivgsagh dylngsagdd qlngvagndy vngwvgndav
      841 aggdgndlvd gnegndvvsg gagddqlygg ydddilsgds gndvyhyflg rgadivdnrs
      901 aevadhdvif ledvqpaqvt vtrvvndlll tlnasdsitv veyflggeaq vgeirfangt
      961 vwslatvlam frsppsstdd svtthedtpl vlqasdfgny sdpqntplva vkitslpvlg
     1021 slqynngsaw vavaqdqvis kadldtgklq fvpvpngngn gyvsigfkvg dgtdfsidan
     1081 tlsvdvtpvn daptgvvais gnatetqtlt avntladldg laaisyqwql sadgssnwtd
     1141 iagttsttlv lsnallgqhv rvlanytdgg gtvesvasva taavaqlvnl fegdannnvl
     1201 dgtgfsdilr gfagadvlng yagedvlegg dgddtitagd gddtltggng adtlrgdnga
     1261 dtlnggadgs fdqlfggdgd dqltlayg
//
LOCUS       WP_284353884             279 aa            linear   BCT 25-DEC-2024
DEFINITION  polysaccharide deacetylase family protein [Pseudomonas putida].
ACCESSION   WP_284353884
VERSION     WP_284353884.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..279
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31184
     Region          18..271
                     /region_name="CE4_HpPgdA_like"
                     /note="Catalytic domain of Helicobacter pylori
                     peptidoglycan deacetylase (HpPgdA) and similar proteins;
                     cd10938"
                     /db_xref="CDD:200563"
     Site            order(24,26,99,103,232)
                     /site_type="active"
                     /db_xref="CDD:200563"
     Site            order(32..33,42..43,45..47,49..50,54,58,77,80..82,
                     101..102,104..105,108..109,112..113,116..117,120,140..141,
                     143,161..167,184..186,191..193,195..197,211..212,215..216,
                     219,238..240,242..243,246)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:200563"
ORIGIN      
        1 mktdyqarqh wpqhkstavs ltfdvdaeag ylgespsfar rltslsegrf gvtrgvpril
       61 ellrrhgiaa tffvpgytae qhpklvetll qagheighhg hmhlrsdkvs eqeqvdemer
      121 glealaraga pkpagyrsss weltpdtfal llrhgfvyds scmgddrpyv etcngasile
      181 lpvhwslddy pmfgwgidng gnfshprmlf dtwlaeyesa rrdarhtsft mhpevigraa
      241 rfeqlerlve rmvsdgdvwf arldavaahv apqlvkgga
//
LOCUS       WP_284354012             317 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Pseudomonas
            putida].
ACCESSION   WP_284354012
VERSION     WP_284354012.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..317
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=34633
     Region          2..316
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mnvlltggtg ffgkallrhw maaantgaai pvvtvlsrap dgflerypef adqdwlrlhr
       61 gdildpaslp eggdfshvlh aaadstagpq lsplqrytqi vdgtrnlley aarqriprfl
      121 mtssggvygp qpqgleqipe dyhglpdple pahaysvakr caehlcilyq qqfglevvia
      181 rcfafvgrdl prdvhfaign firdalespa irvsgdgtpv rsymdqrdla hwldvmlrqg
      241 ragsaynvgs deavtiaela hqvrdvlspq kpvhiaaaqa tpgsfrnryv pcidkarsel
      301 glqlrhglqq sikdaai
//
LOCUS       WP_284354070             255 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Pseudomonas putida].
ACCESSION   WP_284354070
VERSION     WP_284354070.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..255
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27455
     Region          6..251
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          166..249
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtagpilslr hyrdsliahs hehpqlvfgl rgrlefevqg qgagidrqgl ivvpsgahht
       61 casnagsdcl vldvpgehwl heqlgehada srrlldspaa lalndrqqql vdwlaaspme
      121 dpliarqgaa lllaslnpta aasvaasrrl pyaafdthie qhaayplqvs dlarlaglss
      181 arlharftae cgmtpmdyir qrrllkarrl vtqtllpmge iaaqvgyssq safsaamlra
      241 fgctplalrr epgdn
//
LOCUS       WP_284354164             111 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Pseudomonas putida].
ACCESSION   WP_284354164
VERSION     WP_284354164.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 111)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 111)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 111)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..111
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12281
     Region          26..104
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mainetpvim svmraykhpn pedlilerll yalsdpvrle ivrhlagvae ascgeldggr
       61 pkssmshhfr vlrdaglvht rnvgtthmns lrsdilderf pgllgcilqq r
//
LOCUS       WP_284354238             645 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Pseudomonas putida].
ACCESSION   WP_284354238
VERSION     WP_284354238.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..645
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72295
     Region          53..618
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mtigsthnhp adlaiepssp mqpwaarfpn ppdlcfdyrr lveqqggvac aaqpehrici
       61 vgagvtglta arellrcgft ritlieqsqr vggrhltvvn negnykqpst pfemgamrmp
      121 lfnrtgeppk dgcslmayya klfklrlsdf pnpgtpwvna tgiylregql egegtpellv
      181 wrnpegdtpp ptatlqkvye kwhrfarqfa eriamvygtq cwastwqavv eryhllsfrd
      241 lvhlpmltaw npanpgdfgg lgmsseesai fysigigdgs wgafydvccl yplrtaifgf
      301 sshlqlvhgr vdqdgvpyaa pyleasnvpd srglmfkgpa yiglaamdes llfldtgmng
      361 tslydhllqq dnglltdtsv rslqkleagr irvgycwhcs dpanqslqyd dfdsvilttp
      421 swlietnirl dgfsrqilpq sivdawkhah wetsckvyap lkkryldrks alpqilvtds
      481 fvhdvyayry ndrypddcil lsytweddat kltaftdeel ankcveeldr illrcsnvge
      541 aispyidtrn iriqrwitdr nalgcaklyr agtyydavgl mkynrdfsas sglylagesf
      601 svdagwtepc lrtaldavin lcnrttavfn ggftlehyph yqvgk
//
LOCUS       WP_284354255             754 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pseudomonas putida].
ACCESSION   WP_284354255
VERSION     WP_284354255.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 754)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 754)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 754)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..754
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=82749
     Region          42..717
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mewlglqlfa dlpatgrivi dcrhepfqvl layfvacaac fatldmaerq shspeptahr
       61 qwnmlgaccl aggiwamhfi smlafqapve vhydvsltil sllialavaw lamhslertq
      121 mrthhvvqst vliglgiilm hfvgmaamet gavqhyqtgl llasaaiall tslaalclar
      181 ylrkgsgtln qamkycasll iaggivathf tamsamtlvi padtalrlps gdnslqlalg
      241 igfitllisg asisaaladk klqskehdlr rvsmllsqld qaraslqqaa hydaltnlvn
      301 rrgfnqvfae rlaehlases rlavmfldid hfkrindslg hdagdellkv ianhikaatr
      361 sqdlvarfgg defcivtsln nrdearhlaq rimqrmkepi dlggrrmvmt tsigisifpd
      421 dgtcaeellk hadlalyqsk dngrnslnff ndslkaqasi alqleeelrl alleehglcv
      481 hyqpifdlrs gqvaklealv rwqhpqhgll gperfigiae angliidldl wvlrhactdl
      541 ahlqrygygd fkvtvncsav tlshdelpne vekalfhagl aprqlelevt enalmgdiqr
      601 tvnllkrvra lgvalsiddf gtgysslayl krlpldvlki drtflqdvpg sqkdreivqa
      661 iiimahtlhl qvvsegveta eqqafldahg cdylqgyllg rpaplaelrp llerlqrqng
      721 vlnpcygkaq pvspdlfagn pgyragasia rrgh
//
LOCUS       WP_284354291             315 aa            linear   BCT 25-DEC-2024
DEFINITION  flagellar protein MotY [Pseudomonas putida].
ACCESSION   WP_284354291
VERSION     WP_284354291.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16063479
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..315
                     /product="flagellar protein MotY"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0097588 - archaeal or bacterial-type
                     flagellum-dependent cell motility [Evidence IEA]"
                     /calculated_mol_wt=33959
     Region          22..165
                     /region_name="MotY_N"
                     /note="MotY N-terminal domain; pfam18393"
                     /db_xref="CDD:465741"
     Region          176..273
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(181..182,216..217,220,224..225,228,270)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mrqrylallt lfaslpagal tfqtrmenia wkvegdpfec rltqpiegfg sgefvrrage
       61 qpvfqlrsds nalgtgtasl laaaapwqpg rgdinlgsvr lartgvlfss sqgqasrlin
      121 glldgrstvv rsysgeagrp mevrvlpvsf akaysdyqac agkllamnyd qvrqtqvgfp
      181 gggielegaa karldlildy mkadptvnhi eldghsdnsg nrltnrdlsr rramavadyf
      241 kahgvpeeqi tvrfhgeryp laknnnaanr arnrrvniel drvaavekpv qktdeqaaaa
      301 apaspapaap eakap
//
LOCUS       WP_284354309             137 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Pseudomonas putida].
ACCESSION   WP_284354309
VERSION     WP_284354309.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 137)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..137
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=14666
     Region          6..128
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 mpniiriaaa llidpqgrtl lvrkrgteaf mqpggkidag esplqalvre lqeelglnis
       61 pdqavhlgqf sapaanepgf evqaelfrvd saalvtpaae ieevvwlaad qspvlqlapl
      121 trdlilplyr qavsvpr
//
LOCUS       WP_284354502             339 aa            linear   BCT 25-DEC-2024
DEFINITION  Leu/Phe/Val dehydrogenase [Pseudomonas putida].
ACCESSION   WP_284354502
VERSION     WP_284354502.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Brunhuber,N.M. and Blanchard,J.S.
  TITLE     The biochemistry and enzymology of amino acid dehydrogenases
  JOURNAL   Crit Rev Biochem Mol Biol 29 (6), 415-467 (1994)
   PUBMED   7705101
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10500541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..339
                     /product="Leu/Phe/Val dehydrogenase"
                     /EC_number="1.4.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35654
     Region          23..130
                     /region_name="ELFV_dehydrog_N"
                     /note="Glu/Leu/Phe/Val dehydrogenase, dimerization domain;
                     pfam02812"
                     /db_xref="CDD:460706"
     Region          140..338
                     /region_name="NAD_bind_Leu_Phe_Val_DH"
                     /note="NAD(P) binding domain of leucine dehydrogenase,
                     phenylalanine dehydrogenase, and valine dehydrogenase;
                     cd01075"
                     /db_xref="CDD:133444"
     Site            order(174,176..178,197..198,202,231..232,253,255)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133444"
     Site            285
                     /site_type="active"
                     /note="Phe binding site [active]"
                     /db_xref="CDD:133444"
ORIGIN      
        1 mfalmqstrt qslhlfndpp tglkavvaih seqlgpamgg crylpyadde samtdairla
       61 qgmsykaala glplgggkav imrnphvenr aalfeafgrf idtlngrfii avdsgtstld
      121 mdciaqstlh vtsttasgdp sphaamgvfa girattsfrl gsddlrglrv avqglgnvgf
      181 alaeqlhavg aellvsdldp grvrlameqf dakpvtndal istpcdifap cgvgpvlngq
      241 svmqlrcaav agaannqltt lqvadqlesr gilyapdyvi naggliyval thrgedlgti
      301 tahlaripsr ltevfghaqa ekrsparvaq mlaerllyg
//
LOCUS       WP_284354517             582 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Pseudomonas
            putida].
ACCESSION   WP_284354517
VERSION     WP_284354517.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 582)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..582
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=63158
     Region          2..552
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mklegalypw rfrvviglla imvgaicwri idlqvvdrdf lkgqgdarsl rhipipahrg
       61 litdrngepl avstpvttlw anpkemqask drwpqlaaal gqnpqqlver ltaqaskefi
      121 ylvrgltpeq gqhvldlkvp gvygleefrr fypagdvtah mvgftdlddh gregvelayd
      181 ewlagvpgkr qvikdrrgrl ikdiqvtkna kagktlalsi dlrlqylatr elrnaiaeqd
      241 akagslvimd vktgevlamv nqptynpnnr rsmfpaamrn raiidvfepg stvkpismsa
      301 alqsgrwkpt dkvevypgsl qigrytikdv srsegpildl tgilinssnv gmskiafdig
      361 geaiyrvmsq vglgqytglg fpgervgnlp nhrewrkaet atlsygygls vtalqlvhay
      421 aalandgkmv plsiikvdka peavqaipke taetvqgmlq qvieaprgvf raqvpfyhva
      481 gksgtarkat vgskgytena yrslfagfgp msdpryaivv videpgkggy fgglvsapvf
      541 skvmsgtlrl mnvppdnlpp ptpaapavqs qvnaadakgg rg
//
LOCUS       WP_284354605             271 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Pseudomonas
            putida].
ACCESSION   WP_284354605
VERSION     WP_284354605.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..271
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29548
     Region          6..268
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtdrifslaa ltvlelsppd mveaaaragy shvglrlvpa teqeqhfplv adanlrrqtq
       61 arlrdtgikv ldleilrlkp etcvadfeai lavgaelggt ellvagndpd earlterfaa
      121 lcelavgygi hphlefmpwt dvrdlrqamr vvanadrang cvlvdafhfn rsrsslgdla
      181 elapqrmrya qlcdvagpvp admdeilrqa rnerrfpgdg dadlvsllrv lpssvplsle
      241 iptrqlleqg isgeqrarma lekakavlaa v
//
LOCUS       WP_284354623             410 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Pseudomonas putida].
ACCESSION   WP_284354623
VERSION     WP_284354623.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..410
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43829
     Region          1..403
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 msqalplagi rvidyshfla gpyvgrclaa lgaevikver pgsgdagrqh aftldgqqsg
       61 yflqlnmgkq gvsvnmkdpr gkafmqrlad sadvfienyr pgaldklglg yaelsvrnpr
      121 lvycsisayg htgpdahrag fgliaeaksg imqmvgvpge appllrislg dmytgihava
      181 ainaallgrv ssgrgqhidm alydtlvsmh eyavqcytls dgtvlpeqtg hdmptstlyg
      241 vfraadgdlv iaaqvddawq rfaamleang gpagfgsdnr yhdlngrnah rqailavvrd
      301 wvgarsvaev lalldavdip sakvqridev ladpqiqarn mvieqlhpry gtlrlpnlpf
      361 rfsgcdttih qvapdlgqhn aevaaalgfs peeitamqad gvlfthgdar
//
LOCUS       WP_284354795             386 aa            linear   BCT 25-DEC-2024
DEFINITION  two-component system sensor histidine kinase NtrB [Pseudomonas
            putida].
ACCESSION   WP_284354795
VERSION     WP_284354795.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 386)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..386
                     /product="two-component system sensor histidine kinase
                     NtrB"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009399 - nitrogen fixation [Evidence
                     IEA]"
                     /calculated_mol_wt=42192
     Region          15..382
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 mvsadcldhp vmpahryeql vqsvvdyaiy mldpsghvvs wnagaqrikg yradevigkh
       61 fslfftpqdc aegrperllr qaleqgvaqd egwrvrkdgt qfwalaaldv irddqgqiig
      121 lakvtrditd rresamqlda vraqlfqaqk lealgqltgg lahdfnnmlt iilssarlal
      181 atqdparaqr mlqhildagq rgteltqqll sfarhrqldv arvapadlva atrgllehal
      241 pgsidlqvql qadlpmievd agqlqmvlln llfnardaia gegriglaae vvelagevdg
      301 lrgsfvrfvv edsgegiapd vlprifepff ttkpfgkgtg lglsqvygfa rqsggaiyvv
      361 sepghgtsmq lylptyqdrt nsqldr
//
LOCUS       WP_284354816             253 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfite exporter TauE/SafE family protein [Pseudomonas putida].
ACCESSION   WP_284354816
VERSION     WP_284354816.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..253
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26253
     Region          1..252
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mmdiavlsvf afaaglidaa vggggliqip alfnvlptaq paallgsnkl asvcgtafaa
       61 rsfirkvtld wglivpaals afvmsfagaa tvslvppsmm rpavlvlivl maiytfckkd
      121 fgtlhkpari grkeqclavl iggaigfydg lfgpgtgsfl iflfirffal dflhasasak
      181 vvniatnlaa lvffvptgnv lyaialpmav cnilgaltgt wlavrkgagf vralflvllc
      241 vliaklswdl lag
//
LOCUS       WP_284354841             275 aa            linear   BCT 25-DEC-2024
DEFINITION  PhnE/PtxC family ABC transporter permease [Pseudomonas putida].
ACCESSION   WP_284354841
VERSION     WP_284354841.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..275
                     /product="PhnE/PtxC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29394
     Region          26..264
                     /region_name="PhnE"
                     /note="ABC-type phosphate/phosphonate transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG3639"
                     /db_xref="CDD:442856"
ORIGIN      
        1 mlkadtrdpa vlprlllall avavlwpgiq lselnpgvll qaenqqqias ftsafwppah
       61 dsdflgllye atlqtlavat agmvlallla ipagllasra lslraasrgg rvgfwsrllr
      121 lpvrgllifl rsvpeivwal lfvravglgp tagvlaiait ysgmlgkvya eifesvdqrp
      181 ahallqagsg rltaffygil pnaapevvsy tvyrwecavr asvvmgfvga gglgqqidls
      241 mrmfagaqva smlltflvlv mladllsrll rwrla
//
LOCUS       WP_284354931             426 aa            linear   BCT 25-DEC-2024
DEFINITION  CynX/NimT family MFS transporter [Pseudomonas putida].
ACCESSION   WP_284354931
VERSION     WP_284354931.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..426
                     /product="CynX/NimT family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44549
     Region          55..415
                     /region_name="MFS_NIMT_CynX_like"
                     /note="2-nitroimidazole and cyanate transporters and
                     similar proteins of the Major Facilitator Superfamily of
                     transporters; cd17339"
                     /db_xref="CDD:340897"
     Site            order(55,58..59,62,94,143..144,146..148,151,170,173..174,
                     177,246,249..250,253..255,258,285,289,338..339,343,347,
                     364,367..368,371..372,375)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340897"
ORIGIN      
        1 maesitrntp pnerdldell idaeaddeqv qqqpvklrrp wllllglvlv alnlrpalss
       61 mapvlgqvse glglnasqag llttlpvlcl glfaplapvl arrfgservi lgilvtlalg
      121 ivvrsafgpi gvflgslmag asigiigvll pgivkrdfpk hagtltgvyt malclgaama
      181 agatvplaqh fegswalglg fwmlpallam lvwlpqarqg hglhkvayrv rglwrdplaw
      241 qvtlymglqs slayivfgwl psiligrgls pteaglvlsg svivqlvssl sapwlatrgk
      301 dqrlaivlvm lltlvglfgc lyapisglwg wavvlglgqg gtfalaltli vlrskdahva
      361 anlssmaqgv gytlasmgpf avglvhdltg gwaalgwifa vlgigaivfg lgagralhvq
      421 vdsekv
//
LOCUS       WP_284354890             468 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudomonas putida].
ACCESSION   WP_284354890
VERSION     WP_284354890.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..468
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=52233
     Region          29..409
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mqplrtlslw mdqldeplca rpalrenlda dvciigagyt glwtayylkr qapqlniavi
       61 daniagfgas grnggwlmgn llgedrllat lspqqrrasi dllhgipdev hsvlqregie
      121 cdyrkggvly caarypeqer slraylddly rqgmteddyr wlrpeqldaq lrvsnafgai
      181 ysphtatiqp aklvrglara vealgvpiye ntpaidwqpg evrtplarir cqwvvpaveg
      241 yaaslpplgk hqlpvqsllv ateplpestw eqiglsqgqa fsessrqvty gqrtadnrlv
      301 fgarggyrfg grlrenfnld eheielrryl fselfpqlkh vrithswggn lgmarrfrph
      361 mlcdrqrgia laggyggegv gatnlggrtl aalilnqhne mtaqpwvldn rpvsslaswp
      421 pepcrwlgyn aiiqsfvhed rtlanpasap wrrrlassla dfmegfmh
//
LOCUS       WP_284354948             471 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudomonas putida].
ACCESSION   WP_284354948
VERSION     WP_284354948.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..471
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=51212
     Region          53..470
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mgmtrrkfli gggvvaiagg agiltplltr egrlipgkpr fgyvegtegv lpkqadvvvv
       61 gagilglmta inlverglsv vvvekgeiag eqscrfygqv mtykmpdatf qlhhlakqrw
      121 remnakvgad tsyrtqgrve vpfdeedldg vrkwidvktr evgadipfkt riiqgseleq
      181 rlrgassrwt vagfeedsgs ldaerasfvm aeyakkvgvr iythcaargl etqagaisdv
      241 vtekgairas rvivaggaws rlfmqnlgvd vptlpayqsq qiisaaprap ggnvalpgni
      301 yfreqadgty atsprvvvap vvkesfmygy kylpllaipd fpvhislnkq lidsfiqpth
      361 wkldevspfe knrlmtaapd lpelnaslek lkvefpafsd aklidqwsga maiapdenpi
      421 isqvneypgl vlntatgwgm tespvssels adlllgkapv ldpkpfslyr f
//
LOCUS       WP_284354982             345 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudomonas putida].
ACCESSION   WP_284354982
VERSION     WP_284354982.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..345
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35678
     Region          7..344
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 magkaphviv igagilgasi awhlsgrarv tvlevksapa kgvtghsygw vgtgsripse
       61 qpasfaleqh allefpllea llgplpvaaq galiwlddqq qtcsmlaeqq aagvnmvavg
      121 reavhqlqpg lvdvpemalw apddfavepd vltcrllsaa qdkgavvrgd trvlavemrg
      181 ervigvrttq gvvgadivvl anamgaqala splginlpiy eeaavllrfe aagvalrhll
      241 cadalelrpg lggglvsaad lpldgeagla elgrdsvrai sdlfglqgdi vlqsikavar
      301 pktrdgtplr tflpkvegly aavahpgvil apllgrlvse dilgl
//
LOCUS       WP_284354992             691 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Pseudomonas putida].
ACCESSION   WP_284354992
VERSION     WP_284354992.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..691
                     /product="PhoX family protein"
                     /calculated_mol_wt=74176
     Region          22..684
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 msrdtgdnld rnqsgnlpma nvmdaylsrr svmrgslgaa iamiagtglt gcfdgggsdh
       61 ddpvteppvt eppvtepevp klalgfqsip gsrtdacvva agysayvlap wgtpinsngn
      121 pwksdgsnts tdqanamgmh hdgmhffpin gssedgllai nfeyidtaal hpagpttdvn
      181 gkrpveevrk einahgagvv rlqkvsgrwq vvdndplnrr fttasrmeit gplrgtdhvk
      241 tkystagthc rgtnnncgng ytpwgtyltc eenwpgifvn kntrpedqrr igvgtssgqy
      301 kwetaagdst evadefarfd vtvkgasatd dyrneastyg yiveidpyns stlatkrtal
      361 grfrhegcap glpvagkplv wymgddsnne ylykwvstav wdaadanpad rlatgakyld
      421 qgklyvarfn adgtgvwlll dvatattggs tlgalygdlp giilntrgag davgatpmdr
      481 pewttvnpln gdvyltltnn sartpekvda anprgpnrhg hiirwhdsdd qlsftwdifv
      541 fganaagtad inrsglteln qfaspdgmsf dsrgvlwfet dngestltdy tndqllavip
      601 sdlvdasgkq vpvnaqnqvn lrrffvgpne cevtgitftp dnktlfvniq hpgnwpytdk
      661 atdatpagat vrprastvvi qrndggeigt a
//
LOCUS       WP_284355019             399 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Pseudomonas putida].
ACCESSION   WP_284355019
VERSION     WP_284355019.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..399
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43219
     Region          2..399
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mstpskplag lkvvelgtli agpfasrica efgadvikve spdggdplrk wrklyegtsl
       61 wwfvqarnkq sltlnlkhpe grevlkklla eadilienfr pgvleklglg wdvlhalnpr
      121 lvmvrlsgfg qtgpmkdqpg fgavgesmgg lryitgfddr ppvrtgisig dsiaalwgvi
      181 galmalrhre vnggqgqvvd valyeaifam mesmvpefdv fgfirertgn impgitpssi
      241 htsadgkhvq igangdaifk rfmqaigrad laddpalasn dgrdlrrdel ygvidrwans
      301 lpleqlmqvl ttaevpasri ysaedmfndp qylaremflq aklpdgkpfr mpgivpklsd
      361 tpgstewvgp algehteall trlgydaaai aglreagav
//
LOCUS       WP_284355225             337 aa            linear   BCT 25-DEC-2024
DEFINITION  MraY family glycosyltransferase [Pseudomonas putida].
ACCESSION   WP_284355225
VERSION     WP_284355225.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Anderson,M.S., Eveland,S.S. and Price,N.P.
  TITLE     Conserved cytoplasmic motifs that distinguish sub-groups of the
            polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase
            family
  JOURNAL   FEMS Microbiol Lett 191 (2), 169-175 (2000)
   PUBMED   11024259
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Lehrman,M.A.
  TITLE     A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P
            transferases
  JOURNAL   Glycobiology 4 (6), 768-771 (1994)
   PUBMED   7734839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10160628
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..337
                     /product="MraY family glycosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=35705
     Region          30..286
                     /region_name="GT_WbpL_WbcO_like"
                     /note="The members of this subfamily catalyze the
                     formation of a phosphodiester bond between a
                     membrane-associated undecaprenyl-phosphate (Und-P)
                     molecule and N-acetylhexosamine 1-phosphate, which is
                     usually donated by a soluble UDP-N-acetylhexosamine
                     precursor; cd06854"
                     /db_xref="CDD:133464"
     Site            91..92
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133464"
     Site            208..211
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133464"
     Site            order(257,268..271)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:133464"
ORIGIN      
        1 mmllwalpav lllsllmtag lrryalarsv idvpnarssh tvptprgggv aivltfllai
       61 aglmlsgagd sralvalggg galiaiigfm ddhghiparw rllghfiaaa wmlawmgglp
      121 pltlfgwqvd lgwlggvlaa vylvwllnly nfmdgidgia sieaitvclg aaslyslagl
      181 gshavlpmll aaavagflfw nfppakifmg dagsgflgiv lgglslqaaw vapemlwcwl
      241 illgvfivda tytlvrrllr gdkvyeahrs hayqfasrkf gkhlpvtlav aglnlcwllp
      301 iafcvarlgl dgavgvvlay iplvllavrf rageied
//
LOCUS       WP_284355297             192 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Pseudomonas putida].
ACCESSION   WP_284355297
VERSION     WP_284355297.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..192
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=20837
     Region          3..192
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mlplllasss ayrrellarl rlpftwaspd ideqrqdgep avelvrrlar qkaealadsh
       61 pghliigsdq vavlgeqvlg kphtferace qllecsgqqv sfltglalln sttgqcqvdc
      121 vpftvtmrel srerveryva aeqpldcags fkaeglgvsl fqsthgcdat sliglplirl
      181 vdmltkegiv ip
//
LOCUS       WP_284355323             299 aa            linear   BCT 25-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Pseudomonas putida].
ACCESSION   WP_284355323
VERSION     WP_284355323.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..299
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33503
     Region          17..298
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 msaalnalst idsaqpqvfe irpfsgavga eiigldlakp vsaedftrih rahldhhvlv
       61 frdqrispeq qiafsrrfge lqihvlkqfl ltghpeiliv sniiengqni glgdagkfwh
      121 sdlsykelps lgsmlhaqel pseggdtlfa dmhkawdgvp dalrkvvegr saahsytary
      181 aetkfegnwr ptltaeqlaq vkevihpvvr thpengrkal fvsegfttri vglpddesrd
      241 vlqqlyaisv leqniyrhqw qphdlvfwdn rslihlatgc paqlrrklyr ttiqgdapf
//
LOCUS       WP_284355458             896 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pseudomonas putida].
ACCESSION   WP_284355458
VERSION     WP_284355458.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 896)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 896)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 896)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 896)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..896
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..896
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=100680
     Region          222..892
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mksqpdaasr vaaevvtplp vpsrlgmlrf erlneatwam lyldpacerq fglhagdlca
       61 lvdapyaslm epearyqlhd eiqlqltqrg yyrvrytlht psaslrllev geaykqhnrq
      121 llrgylsvld dqqddtgead asdlesrnnr lqlalqlnqr aqqeqlehle rvrgqqdlil
      181 rlarqrysag nslleaaqli trsaceiykv dsasiwhldd qrlepitawy rdaqehrqpe
      241 aidasrfpdy ldalhasrai dahnaghdpr tralaqslrp enkamldasi rvdgqvvgvl
      301 cleqtgqpra wqsdeiafag eladqfaqvi tnhnrrtaas alhlfqrave qsasafllvn
      361 rdgrveyvnp sftaitqyst devqgrhlge lpalenlsel lfdspsslam gnswqgefks
      421 rrknlepywg qlsiskvygd nrelthyigi yedvtqtkla qqrierlayt dnltnlgnrp
      481 afirsldecf ardgesamcl llvdidnfkr indslghqtg dkllvslarr lrnsldtsgi
      541 larfasnefa vllddtsled gqgvaqqllr tldkpmfvdn qlinvtasvg layaplhgad
      601 paslmknagl alhkakangk hqvqvftevl naeasyklfv ennlrraltq nelevfyqpk
      661 iclrsgrllg leallrwnhp ergmirpdqf isvaeetgli ipigkwvvrq scrmsqqlre
      721 agrgnlhvai nlspkqfsdp dlvasistil keealpphll elelteglll easedthrql
      781 delkalgltl amddfgtgys slsylkkfpi dilkidrsfi neipdnqddm eitsavvama
      841 hnlklkvvae gietpeqlaf lrrhrcdvgq gylfdrpipg relaerlkry prgpla
//
LOCUS       WP_284355538             318 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Pseudomonas putida].
ACCESSION   WP_284355538
VERSION     WP_284355538.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..318
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=33773
     Region          11..308
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mslpasleqh lrlpvvaapm flisnpklvl accangvvgs fpalnqrdsa gfkawleeie
       61 aglaqlqapa pyavnlivhp tnprlqadla lcvehrvpiv itslgavkev vdavhryggm
      121 vfhdvttrrh aekaaeagvd gliavaagag ghagtwspfa laaeirqffd ktlllagcln
      181 hgheilaaql lgadlaymgt rfiattesqa qddykqmlld ahaadiihtp avsgipasfl
      241 rpsleqagyd mnaikgghep gklkpiddea kawktvwsag qgvggiddlp sasvlierlh
      301 neylealqrc qalrartl
//
LOCUS       WP_284355612             470 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Pseudomonas putida].
ACCESSION   WP_284355612
VERSION     WP_284355612.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..470
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50037
     Region          2..464
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mtsaansapl iekhtigyvp pqdrhgkvrd lftlwfggni aplpivtgal gvqlfhlnlv
       61 wgiiailvgh lvggvlmalh saqgpqmgip qmiqsraqfg tlgallvvvi agvmyigffa
      121 snivlagksl hgvvdavpvp vgivigalgs giigiigyrf ihvlnrigtw vlgigivvgf
      181 gyifthvqsd dfltrggfnl agwlatvsla alwqiafapy vsdysrylps dvkvsstfwt
      241 tylgsalgss lsfifgavav laipagmdtm eavklatgtl gpimlvlfll svishnalnl
      301 ygavlsiitl vqtfayrwip taksravlsl ivlsaccvva vfasadfigh fvdmvlvllv
      361 vlvpwtainl idfyaihkgd ydiqsifqvd ggiygrynpq aliayavgiv vqipfmntpl
      421 yvgpisehin gadlswlvgl aitsplygwl asrdsayrrr qtsaklamgh
//
LOCUS       WP_284355568             710 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Pseudomonas putida].
ACCESSION   WP_284355568
VERSION     WP_284355568.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 710)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 710)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..710
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=78419
     Region          60..710
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 manmsvvpas isvlgllvvp avhaaaqtea pgslalpata vtsayeqqsy kasesrsamk
       61 idaplrdipq tvnvvpesvi kdqgaqsmqd vlknvpgigl sngdgqrdqv tirgfsaigd
      121 myidgvrdda lyfrdlsnie rvevikgpaa vlygrgssgg linsiskkps ftpkrevgms
      181 fdsegkrrtq fdtgwadpqs nqayrvtgaf edsdtfrddg yidrkaiaps ayfrlsddle
      241 lnlgatylyd krlidfgipa lgnrpvdvdr dkrfgsgdad qdyarsevfs ltasldyrin
      301 dnftltntsr yyrydldrnn tladssptrf vtapngellv klnrgnvard eygvfnqtel
      361 kqqaqlagmq hnllygvevg fqdkyqrvls qnnvalvpvy rdalvpvpeh aanlsskgtn
      421 fqqttglylq dmielnehwk alvgvrydif gqeyddgrvq nvdldrtdkt wspraglvyq
      481 pdaiqsyyvs vsrsyqpsge vfavsptnqh lepeettnye igakwdllds rlsltaavfr
      541 lertnmktad panpnltvla geqrtdgfea tvsgqltdkw qiyagyayld aeitksnskt
      601 ngvanegqtp tltprnsanv wlvrtltpaw rvaaganyvd erytaldnvv vmpgyttfda
      661 allysvpqwd aalrlknvfd rdyyasahgs vdlvtpgapr tleasfnyrf
//
LOCUS       WP_284355659             258 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudomonas putida].
ACCESSION   WP_284355659
VERSION     WP_284355659.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..258
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29577
     Region          23..242
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mtrrawgmal allsvqagaa qtvrycdypv yppiswsdgh qvrglapmvv relfarmgyd
       61 vqtvvlgnwk rclmdaaagr vdvvlaynsd qrdqrmrfsl epvvreevav fynrkrpvqf
      121 qqledlagyr ggllygesyg aefdrfvary qniervsssq qnfgklirgr idyviqerrt
      181 gqlfiehlpg aqdirvlpra lsvdylrvav srqsplnqhm deidaqlrrm neageiarwl
      241 eqsevtyrdm inlpanar
//
LOCUS       WP_284355695             273 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Pseudomonas putida].
ACCESSION   WP_284355695
VERSION     WP_284355695.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..273
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31403
     Region          7..272
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mtserntdie irllieaiyl kysydfrnys gasikrrilh alrqfdcltv salqervlhd
       61 pgmfmqllqy ltipvsemfr dpghflalrn evvpllrtwp sikvwiagcs tgeevysmai
      121 llreegller tiiyatdinp hsldkakqgi ysmqsmrdya enyriaggrr dfseyytaay
      181 gnaimdstlr dnvtfadhsl atdsvfsetq lvscrnvliy fnkelqdral glfheslchr
      241 gflvlgskes vdfsaygdrf eplvkperiy rks
//
LOCUS       WP_284355786             397 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Pseudomonas
            putida].
ACCESSION   WP_284355786
VERSION     WP_284355786.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..397
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=44026
     Region          11..383
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 makspkksks rlwflvhswl alpiwffvli vcftgmlavv sqeivwlanp dvraskpdgd
       61 aerlsfqqvl damhkaepdm aveslvqpdg shfalladvt ypdgtsptly vnpytgviqg
      121 kspdfnfeaf tralhgwwlv pftngfswgw ylvsilglpm laslvtglvv ykkfwkgffk
      181 pvrtghgsri fwgdlhrlag vwsiwfiavi sitgtwfliq allsdnhiti ssrpiapvia
      241 redvpqtpdg tpapridlde aariaglaip gleitfislp atayshvsmg grgwyplmfq
      301 saavnpytrn vdsqfllsdr stlefitesm rplhtgdfgg lpikliwfff gliltlmvfs
      361 glliwtkrta qataaalkrg drapraarsq tpletqs
//
LOCUS       WP_284355858             265 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Pseudomonas putida].
ACCESSION   WP_284355858
VERSION     WP_284355858.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..265
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28604
     Region          1..265
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mnfnqlldav ranpdavsip pswaqgraaf gglmaamvye amrlkltddr pvrslaisfv
       61 apaaadvpir fdvevlregk avstllgrav qdgqvvtlvq gnfgagrpsv vdvpalpgme
      121 mkaledaape lpyikgitpe fmrhvalrwa vgglpfsgnq srrmggwvrl rdvaeeqvne
      181 ahllalvdaw ppslmpflkq paagstltwt iefiqptakv stldwcrycv etehardgyg
      241 haaaalwtae gellalsrqt vtvfa
//
LOCUS       WP_284355832             378 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudomonas putida].
ACCESSION   WP_284355832
VERSION     WP_284355832.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..378
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40477
     Region          4..374
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtptydtlii gagiagaslg yrlagqqrvl lleresqpgy hstgrsaamf meaygtpqiq
       61 altrasrafy etppqgfceh plleprgcly vasleqrell ehthaqnlan gtevslldrd
      121 aalalvpslr setlagavle pgamdldvha lhqgflrgyr aaggelrcna eliqawyldn
      181 lwqveladgs rlqarqlvna agawadrvae qcgvariglq pcrrsaftfp gpadqdfarw
      241 pavigvdesf yfkpdagqll gspanadpve pqdaapeeld valgiyniea mttlairrps
      301 htwaglrsfv adgdlvigfd ahapaffwla aqggygiqsa agasrlaadl llgqplcssl
      361 vsqgvaperl sparfqqp
//
LOCUS       WP_284355968             338 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Pseudomonas putida].
ACCESSION   WP_284355968
VERSION     WP_284355968.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..338
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34111
     Region          24..335
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mirllpciav alaallaall agtaigetnl spsvvgqvla nhlwqagypv dpidagivwn
       61 yrltrtlvaa acgaglatcg vilqallrnp laepyllgls agastgavlv gllglgslal
      121 smsagafiga laafalvlvl araagpssnn aqvilagiag sqlfnaltaf litksataeq
      181 argilfwlmg nlsgvrwpsv wlavpvalfg lvvcllhrra ldaftfgads aaslgipvrr
      241 tqllliscaa lvtavmvsiv gaigfvglvi phalrlllgp ghsrllpasa lggalfliaa
      301 dvlsrtlivg qvipvgvvta ligapvfali lvsrrgrs
//
LOCUS       WP_284356138             188 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Pseudomonas putida].
ACCESSION   WP_284356138
VERSION     WP_284356138.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..188
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=21005
     Region          <20..181
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mawlptllkg rprlrqdlcw qqrqarpael wlvivdasas trrhqalaqt kgllaalfdq
       61 ayrqrarlal ltasgrtpqw qrhglkasaa lqpwlqalga gggtpliaal eqarhwlkar
      121 qrahpaeavr cliftdgrlq hwnavepmpc atllvdmela pvrlgraqrl aeqlqadyqh
      181 lqqfnvlg
//
LOCUS       WP_284356207             439 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Pseudomonas putida].
ACCESSION   WP_284356207
VERSION     WP_284356207.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..439
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=48332
     Region          7..425
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mtlnnleidt lvvgagqagv amsehlnklg vphlvlernr iaeawrtgrw dslvangpvw
       61 hdrfpglafn ldadafagke qvadyfeqyv rkynlpvrtg ievkrvvrns drpgftietn
      121 egviranrvv aatgpfqkpv ipaiapkdsn mhqihsaayy npeqlpegav lvvgagssgv
      181 qiaeelmrag rqvylsvgah drpprayrnr dfcwwlgvlg ewdaeiakpg rehvtiavsg
      241 argghtvdfr alahqgmtlv gltqsfengv arfqdnlven inrgdenyla lldaadayie
      301 rngldlpeep eartrladpa cmssplreld laqagvtsii watgygvdfs wlqvdtfdan
      361 gkpqhqrgva repgvyflgl pwlsrrgssf iwgvwhdakh vaghiatqrt ytayrdrdqr
      421 eadaqqantl snvstlgah
//
LOCUS       WP_284356337             103 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Pseudomonas putida group].
ACCESSION   WP_284356337
VERSION     WP_284356337.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida group
  ORGANISM  Pseudomonas putida group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Pseudomonas putida group"
                     /db_xref="taxon:136845"
     Protein         1..103
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11209
     Region          38..96
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
ORIGIN      
        1 mrdiesiaka ieadageplp dlrqalkeak agagrittpe qilvrqarer cgltqasfae
       61 riatpvatlr dweqgrfvpp ggvlcllrli lkhpelsqel tki
//
LOCUS       WP_284356529             403 aa            linear   BCT 25-DEC-2024
DEFINITION  nitrate/nitrite transporter [Pseudomonas putida].
ACCESSION   WP_284356529
VERSION     WP_284356529.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 403)
  AUTHORS   Yan,H., Huang,W., Yan,C., Gong,X., Jiang,S., Zhao,Y., Wang,J. and
            Shi,Y.
  TITLE     Structure and mechanism of a nitrate transporter
  JOURNAL   Cell Rep 3 (3), 716-723 (2013)
   PUBMED   23523348
REFERENCE   6  (residues 1 to 403)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..403
                     /product="nitrate/nitrite transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42133
     Region          14..379
                     /region_name="MFS_NRT2_like"
                     /note="Plant Nitrate transporter NRT2 family and Bacterial
                     Nitrate/Nitrite transporters of the Major Facilitator
                     Superfamily; cd17341"
                     /db_xref="CDD:340899"
     Site            order(24..25,28..29,32,64,116..117,119..121,124,142,
                     145..146,149,218,221..222,225..227,230,258,262,312..313,
                     317,321,336,339..340,343..344,347)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340899"
ORIGIN      
        1 mstsfwksgh vptlfaafly fdlsfmvwyl lgplavqiaa dlqlsaqqrg lmvampilag
       61 ailrfamgvl vdrlspktag ligqviviva laaawhlgvh syeqalllgv flgfagasfa
      121 vslplasqwy ppqhqgkamg iagagnsgtv faallapala agfgwsnvfg faliplslal
      181 vvfallarna pqrpkpkama dylkalgdrd swwfmffysv tfggfiglas alpgyfsdqy
      241 glspvtagyy taacvfagsl mrplggamad rfggirtllg mysvaaicia avgfnlpsaa
      301 aalalfvsam lglgagngav fqlvpqrfrq eigvmtglig maggiggfll aaglgtikqh
      361 tgdyqlglwl faslgllawf glhgvkqrwr ttwgsaavta arv
//
LOCUS       WP_284356611             715 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Pseudomonas
            putida].
ACCESSION   WP_284356611
VERSION     WP_284356611.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 715)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 715)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 715)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..715
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80530
     Region          21..691
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mpvsiliqgr tvfpgtppyp rlliltallg gpavaddlfi dstdlpqvlt atrlkqspaa
       61 vpgsmtvlds elirasgard ipellrlvpg mmigygagnq ptanyhgsnv ndarrmqvli
      121 dgrsvyragl atvdwsdipl amedieriev frgpntvsyg analmavvni ltrnpadshg
      181 trlkvtrgqd gindfyashg fgwdggdmrl slsgqqddgf denqfgqnyr dsrrltrfnl
      241 sashnlavdq tlewqlaake gsnqrpytyq pvfaryeagd nadvnakdya gslrwtkdfs
      301 aehslyiqgs aqhfdrqqvw racdalqsfs peltqlwqmn pdfaekvarg iatgvplstn
      361 dpalkgllqk vqqqwerggm qqvcgdvdqs tretrydlei qdtlsltdsl rllsgmnyry
      421 dradsqtyfn gslddqtwrl fgqlewrade hwilqggtmf edsrlsgssl tprvavnyli
      481 tprhglravy seavrspdmf ennvnwsytv knlspnafgl qngeyfvktr gpgnleqerm
      541 rsrelgyngf fsdidlsmdv klfydeitgm iseplknnqy iasnankarf sgseaqldwr
      601 ptlrdrlrlt yayvdawasn pddrrlsahn sgsagwmrew gagwssalfy ygddalnqyr
      661 yerldlrlak rfrvhgsnle laalwqqrld depttaiqnr ydsrhrlsvs aeldf
//
LOCUS       WP_284356721             237 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Pseudomonas putida].
ACCESSION   WP_284356721
VERSION     WP_284356721.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 237)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 237)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..237
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25399
     Region          4..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mnaassisqi aslmadpkrs amlwalidgt prlanelaim tgltsssaca hlsllssagl
       61 lrheargrkr yfrlatpqvg aavealasvq lestrgerak apvsplpmsm rrarrcgdhl
      121 ggelaselyh rlvvagwleg sgrqlmvsde graqlalvgv yidalapheq rgcvicrcte
      181 wndqgphlgg glgqalfrlf lqsgwmreae dtralhisal giqqinriar vatlqvg
//
LOCUS       WP_284356783             219 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Pseudomonas putida].
ACCESSION   WP_284356783
VERSION     WP_284356783.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..219
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24030
     Region          46..218
                     /region_name="Nnt1"
                     /note="Protein N-terminal and lysine N-methylase,
                     NNT1/EFM7 family [Posttranslational modification, protein
                     turnover, chaperones]; COG3897"
                     /db_xref="CDD:443104"
ORIGIN      
        1 mpplalqqal sgligearlv vselpgcdlk lwlideqnmd rafsseetrr ileeppywsf
       61 cwasglamar ylaerpewva gkrvldfgag sgiagiaaar agalevvacd ldplaldacr
      121 anaalngvel gysndffaed drfdlilvad vlydranlpl ldafldrgrq alvadsrvrd
      181 fshplyqqlg vlealtlpdl aephefrrvs lyhasrdtl
//
LOCUS       WP_284356740            1633 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Pseudomonas putida].
ACCESSION   WP_284356740
VERSION     WP_284356740.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 1633)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1633)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1633)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1633)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1633
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..1633
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=178332
     Region          56..1632
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mfnkglllac alallsacds stpgtpapae kpvatapaea paakredpav lakhyegrel
       61 tlldvsevql dgaatlsisf sapldakqdf atkvhlvdtv kgkldgawel sdnqmelrlr
      121 hlepqrklvl tvdkgllavn gkqldsesit qletrdmqpt igfasrgsll ptrlaeglpv
      181 ialnvdkvdv effrvkpeml stflaswgrn sslyyyqske tldmaelvys grfdlnparn
      241 tretvllpia gikplqdpgv ylavmrasgt ydysqpatlf tlsdigvsah ryrdridvfa
      301 qaleggkaln gvnleihdek gkllaqastd gkghaqlpit pkadtliatq gvnttllrln
      361 taaldlaefd itgpqanplq lfifgprdly rpgeavllng llrdqdgkpv kaqpvsvevr
      421 rpdeqvsrkf vweadsngly qyqlqlatea ptgrwqllld lgggrkqvye flvedflper
      481 lalelkgsst plspeedari evngrylyga paagnrlsgq ayvrplrkav palpgyqfgs
      541 vtetelnqdl eldevtldqa gkavvdiesr waearsplql tvqaslqesg grpitrrleq
      601 piwpaerlpg lrglfdgeet dsdgpvefef lvadrdgnkl aandlkvrli rerrdyywny
      661 sqsdgwsyay nekfltqnee tvsvkagsta klsfqvewgp yrvevedpqt glvsserfwa
      721 gyraqdnaeg gavrpdqvkl aldkpsyadg atakvtvtpp aagsgylmie ssdgplwwqe
      781 idvpaegktf dvqldkawar hdlyisalvi rpgerkanat pkrsvgvlhl pldraerkla
      841 vslqapekmr pkqpltvkvk aanadgsvpk qvhvllsavd vgilnitdfk tpdpfaslfg
      901 rkaygadqld iygqlieagq grlaslafgg daamakggkr pnttvtivar qslpvtlddk
      961 gegeatvdip dfngelrlma qawteehfgm aegktvvaap liaelsaprf laggdrtrla
     1021 ldlanlsgra qqlnveitte gqlslvasav qnvalaegqr stlmipvqae gglgqgkvhv
     1081 rvtglqlpne pttaferewt lgvrpaypam lkhyrvalke qpwtlpdadl aafepaglea
     1141 slalssrppl nlaeqirale aypygcleqt tsglypslya dadslkrlgi kgepadvrkr
     1201 kiemgiehll gmqryngsfg lwssdseeey wltayvtdfl lrardqgygv paealkkase
     1261 rllrylqern lievdysena dhtrfavqay aalvlsrsqq aplgalrglf erradarsgl
     1321 plvqlavald kmgdkpraeq alqaglgisr gkgwmadygs alrdqalila llqesnlass
     1381 qvdqrlfals delaanrwls tqernalfla grgllgkpeg kwqarldsag evrefnnaea
     1441 gmklegplla splsvrnegs etlyqqltls gyprqapaag gngmqirrey lgmngqpldl
     1501 hnlrsgdlvl vhlalkaedr vpdalvvdll paglelenqn laqsaasldn assavkewre
     1561 smqnasvvhq eyrddryvaa lkldsygtth llylaravtp gtyrvpppqv esmyrpnlqa
     1621 vgdgqgemtv kap
//
LOCUS       WP_284356805             261 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfite exporter TauE/SafE family protein [Pseudomonas putida].
ACCESSION   WP_284356805
VERSION     WP_284356805.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..261
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27725
     Region          13..261
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mellgafwae hwllailmlg aiafvagfvd siagggglfl vpgfllvgmp pqvalgqekl
       61 vstlgtlaai rnflanskmv wqvalvgvpf sllgaylgah livsisqetv gkiilalipf
      121 gilifltpkd rqveerelss rmlytvvplt claigfydgf fgpgtgsmfi iafhyllrmd
      181 lvsssanskt fnfasnigal vafviagkvv yllalplvac nilgnhlgsa lalrkgndvv
      241 rkvlvfsmlc lftslgvkyl a
//
LOCUS       WP_284356965             261 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Pseudomonas
            putida].
ACCESSION   WP_284356965
VERSION     WP_284356965.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..261
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28878
     Region          35..238
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mvqatmsilq airvflfyll lgtssllwcs lsffiapfls fpkrytfinv ywcrcalflv
       61 rtilgidyki tgaenvpaep cvilsnhqst wetfflsqyf splsqvlkre llyvpffgwa
      121 mamlrpiain rdnpkealrq vaskgdellk qktwvlifpe gtrvpfgtvg kfsrggtala
      181 vnaglpvlpi ahnagkfwpk tgwgkragti evvigepmya ngsgpraiae lndraaawne
      241 atqramgslp paaekpqeqt a
//
LOCUS       WP_284356928             481 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Pseudomonas putida].
ACCESSION   WP_284356928
VERSION     WP_284356928.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..481
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=54013
     Region          36..447
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mlvvenakpn nppsppiiip aqkngrsyyt ivshdkttdd ffnawsyqlr kkkskntnka
       61 yteyngvlls yvhhiafqhg eltapllsea iehyesflvf gtesdvpmvr raaralgnrn
      121 lsgssvgval aalnsfvdas erfrlgmiel eqrgyiasks lsgfslaqtv riespqkvrt
      181 aikenswlag claggarrik rkglsaiskp sdlahtdmyg gdefafpidk caelirsatc
      241 srdrmlwsll aacgarvsea qtmlnididp sleehlsrvr iidpdtrrnv likylseeei
      301 nglphkgrah pqtfliepfa smfwialeey kadlrkqnym apithdfllr nlqtgapmtn
      361 syqtlyerfr daakkitgrq ygfhslrhmy gyylvnhcpn plpgsnkkyg lpletvqklm
      421 gharlkttrr yarqdahllq atlaaanmar ltggpktvie ariafhneei trlkqlslea
      481 k
//
LOCUS       WP_284356974             430 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Pseudomonas
            putida].
ACCESSION   WP_284356974
VERSION     WP_284356974.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..430
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=47107
     Region          1..430
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mpethplila lvsylehdal paivldtdyn ilaanaayrr qfgrhdqapl gekchkvshh
       61 yavpcdqage hcpmrkawds kvpervlhvh htprgpehvd velrpildeq grvvafverl
      121 tsitlasaqp qeqglvgrap afkaalaslq raapaqipvl lqgesgsgke lfaravhmgs
      181 prangplvvv dctglteslf eselfgyekg aftganqrki glaeaahggt lfldeigevp
      241 lamqvkllrl iesgsfrpvg slrtvhsdfr lvsathkplk qmvaqgsfre dlyyrisgfp
      301 irlpalrerv edlpllaqsl lqrmagkptp rlsddalqql glhpfpgnir elrnilerar
      361 lfaddglirp ehlpedigpv gatatggrrn nlaelaqale qfkgsrsela shlgmsertl
      421 yrrlkalgln
//
LOCUS       WP_284357029             185 aa            linear   BCT 25-DEC-2024
DEFINITION  chorismate--pyruvate lyase family protein [Pseudomonas putida].
ACCESSION   WP_284357029
VERSION     WP_284357029.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Meganathan,R.
  TITLE     Ubiquinone biosynthesis in microorganisms
  JOURNAL   FEMS Microbiol Lett 203 (2), 131-139 (2001)
   PUBMED   11583838
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Siebert,M., Severin,K. and Heide,L.
  TITLE     Formation of 4-hydroxybenzoate in Escherichia coli:
            characterization of the ubiC gene and its encoded enzyme chorismate
            pyruvate-lyase
  JOURNAL   Microbiology (Reading) 140 (Pt 4), 897-904 (1994)
   PUBMED   8012607
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Nichols,B.P. and Green,J.M.
  TITLE     Cloning and sequencing of Escherichia coli ubiC and purification of
            chorismate lyase
  JOURNAL   J Bacteriol 174 (16), 5309-5316 (1992)
   PUBMED   1644758
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..185
                     /product="chorismate--pyruvate lyase family protein"
                     /EC_number="4.1.3.40"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0008813 - chorismate lyase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006744 - ubiquinone biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=20671
     Region          5..175
                     /region_name="UbiC"
                     /note="4-hydroxybenzoate synthetase (chorismate-pyruvate
                     lyase) [Coenzyme transport and metabolism]; COG3161"
                     /db_xref="CDD:442395"
ORIGIN      
        1 msyespqaaa vawlpysqla tgidqltldw lfdegsltrr ltrlsndhfs vtplfegwqp
       61 lrddecqalg iatgaegwvr evylrghgqp wvfarsvasr salerggldl etlgsrslge
      121 llfcdqafir hpievcsypq awlpteaahd alwgrrsrfe rggldllvae vflpalwqaa
      181 keenr
//
LOCUS       WP_284357225             791 aa            linear   BCT 25-DEC-2024
DEFINITION  efflux RND transporter permease subunit [Pseudomonas putida].
ACCESSION   WP_284357225
VERSION     WP_284357225.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Sandhu,P. and Akhter,Y.
  TITLE     Evolution of structural fitness and multifunctional aspects of
            mycobacterial RND family transporters
  JOURNAL   Arch Microbiol 200 (1), 19-31 (2018)
   PUBMED   28951954
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Hand,N.J., Klein,R., Laskewitz,A. and Pohlschroder,M.
  TITLE     Archaeal and bacterial SecD and SecF homologs exhibit striking
            structural and functional conservation
  JOURNAL   J Bacteriol 188 (4), 1251-1259 (2006)
   PUBMED   16452406
REFERENCE   3  (residues 1 to 791)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
REFERENCE   4  (residues 1 to 791)
  AUTHORS   Arkowitz,R.A. and Wickner,W.
  TITLE     SecD and SecF are required for the proton electrochemical gradient
            stimulation of preprotein translocation
  JOURNAL   EMBO J 13 (4), 954-963 (1994)
   PUBMED   8112309
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..791
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86749
     Region          12..774
                     /region_name="MMPL"
                     /note="Predicted exporter protein, RND superfamily
                     [General function prediction only]; COG1033"
                     /db_xref="CDD:440656"
ORIGIN      
        1 mhphhqdkat llerlifnnr pvvialcvlv siflfwqatq irpstsfekm iplqhpfieq
       61 mmehrndlan lgntvrisve avngdifdkd ymetlrqvhd evfyipgvdr aglkslwsps
      121 vrwsevteeg fsggevipnt yngsqdsldt lrdnvlksgq vgrlvgnnfk ssivdvplle
      181 sypdpqdpgr qvkldyqqfs hlleekirdk fqaqnpnvki hivgfakkvg dlidglvmva
      241 mffgvalait wvllywftwc irstiavlit tlvavvwqlg lmhavgfgld pysmlvpfli
      301 faigishgvq kingialqss dadnaltaar rtfrqlflpg miailadavg fitlliidig
      361 virelaigas igvavivftn lillpvaisy vgiskkaier skkdatrehp fwrllsnfas
      421 akvapvsvtl alvafagglw ysqnlkigdl dqgapelrpd srynqdnsfi isnystssdv
      481 lvimvktppe qcsvhstmap idelmwtmqn tpgvqsaisl vtvskqvikg mnegslkwes
      541 lsrnpdilnn siaradglyn gdcslapvlv flndhkaetl ervtaaakaf adshnkeglq
      601 fllaagnagi eaatneviks aeltililvy icvavmclit frsfaatlci vlplvltsvl
      661 gnalmaymgi gvkvatlpvv algvgigvdy giyiysrles flraglplqe ayyqtlrstg
      721 kavlftglcl aigvctwifs aikfqadmgl mltfmllwnm fgalwllpal arflikpekm
      781 vgkeggsifa h
//
LOCUS       WP_284357205             572 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Pseudomonas putida].
ACCESSION   WP_284357205
VERSION     WP_284357205.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..572
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=62554
     Region          1..275
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
     Region          353..>455
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Site            order(382..383,385,404,407..408,411..412,414..415,438,
                     441..442,445..446,449)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          402..432
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mielwpqwlr plwllavpll gwllyklwhr rkragrwqmi lppafhgvll gggsgstskl
       61 pwvalglawa lvilallgps wqrveenrqr padplville ltpqmlaeds ppnrleqarr
      121 kildllehrr dsqtalvvya gsahtlvpls ddlattrnll eaidpsimpq agqradlavq
      181 kglallaqsg lgqgrlllig sslsaperqg isqalgrqgp sllmlgigsr egapvrqang
      241 eflkdnqggi llprldsasl kgfisgtggr yrhariddld lrglglfdnp rtarndgqtl
      301 qldswadqgy wlliplllla acagrrgwlf clplllalpq psqafefndl wlrpdqqgqr
      361 lleqnrpasa arhfqdpqwr gmalyqagdy agaaeafsqg dtapahynrg nalahsgele
      421 aaldayeqal erqpdlqaal dnqalvqqml qqrdakaeeq ppssdaqgtp gsetegnsss
      481 asspaqgtpg ndehasaeqp gesssnsqaa pgnqaggdds viqppqrpvs tsldaeqrqa
      541 leqwlreipd npaellrrkf wyeqqlhqet qr
//
LOCUS       WP_284357234             555 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pseudomonas putida].
ACCESSION   WP_284357234
VERSION     WP_284357234.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 555)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..555
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=61807
     Region          8..543
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mstpveplrl llladepewa allhacmpal sgsavlltap nwdavdslfs hdrqavvlat
       61 palqpvpgrc dlptillldh epevapsavs dwlvrdqlna dtlrrslrhv rergvlvatl
      121 qrlaeqdplt gianrqgfqa lltarlaene grglalghld ldnfrhvnda lghqsgdrli
      181 lqvvsrlqnq leagdqlarl gsdefallid trrdanraew iaeriieala epywidgesl
      241 llgcslglah araqsgadpl mwhahiamrq akgsqgctfh vfnerinrna rsladlesel
      301 rralrrdele lhyqprldla dgrivgleal vrwrhaergl lppsefvpla eqsglivplg
      361 ywvisralrd mqalcergle plhmavnlsf rqfqdsqlla tlsrlilehg vdarwlefel
      421 tetavmrrne vvrqtmdalg rlgvrfsldd fgtgfssfvh lnslpitllk vdrsfvaeme
      481 mreenrklvh aminlahnln levvaegves eaqlallrgf gcdqvqgflv skplpvgeli
      541 dfllkvpgrq ldavr
//
LOCUS       WP_284357282             695 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pseudomonas putida].
ACCESSION   WP_284357282
VERSION     WP_284357282.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 695)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 695)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..695
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=74768
     Region          18..689
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mltgsysssl vlislcvail asytaldltg riatakgraa ylwmgggala mgigvwsmhf
       61 igmlafslpi dlgydlglta fslliavlss gfalwlvsqp slpglqlgfg alimgagiac
      121 mhytgmaalr mlpgidydpa lfgaslliav gasaaalwia frlrmhtpyv rqirgvaavv
      181 mgfaivgmhy tgmaaanfpe gsfcgalggg lqgdslvylv littlavlav alltsvldar
      241 leartaelar sltlanqelt qlalhdtltd lpnrtlladr ieqaiakvae qggcfalmfi
      301 dldgfkpvnd afghhigdll lkavasrlrg hlhsqdtlar iggdefvllv elqepddamd
      361 vavkqvnlvs rpfrvaehdl qlsaslgivl ypgngqdqhe llrnadaamy haksagkngy
      421 sffdasmnsn arqqlqllqd lrqaleqrqf rlhyqpkfda qaclpigaea llrwehpqhg
      481 lllpdrfigl aektgliipi gewvldeacr qmrhwldqgh egwrmavnls aiqfchaglv
      541 esvaralqqn glpancltle itettamhda dasltvlqrl sdmgvdlsid dfgtgysslm
      601 ylkrlpanel kidrgfvrdl ehdsddaaiv saivalgqal glrivaegve tdkqqdfltr
      661 lgcdslqgyl lgqpvpaeqf mgklqalrqq daaag
//
LOCUS       WP_284357357            2161 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Tritonibacter mobilis].
ACCESSION   WP_284357357
VERSION     WP_284357357.1
KEYWORDS    RefSeq.
SOURCE      Tritonibacter mobilis
  ORGANISM  Tritonibacter mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Tritonibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2161
                     /organism="Tritonibacter mobilis"
                     /db_xref="taxon:379347"
     Protein         1..2161
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=207209
     Region          15..1720
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mtgdvtvgtn gtlttsgdvq gtiandsitt vtdgsvadle ntgnatvsgg vvadldnsgs
       61 gdltigaggt vttlsnssta snagevgtlt nsggtftntg nvtgtssvtg gtldndggtl
      121 tgdvtvgtng tlttsgdvqg tiandgittv tdgsvahldn agnatvsgge vtdldntgnv
      181 tvsggevadl dntgnatvsg gvvadldnsg sgdltigagg tvttlsnsst asnagevgtl
      241 tnsggtftnt gtvsgsttit dgtvtnnggs fggdvtiegg anatlsletd taingnvvnn
      301 gtieangsgs isldvtgghs ltntgtlngg thglditade iylsetsivg tgvnligdtt
      361 negvltldtd lvgdlttidg sqsdivgdva gngndvnveg gslgvadgva ftgigaltne
      421 sditvgtgat leaetidned ggsislggna tlsgtgntln nggiitvgdg gtvqdagdin
      481 neatgtitft gsgtlnadtd ndgdgltnsg tistadggnd tltlgdgtdd tftnaaggml
      541 aigdsdivtg sgttmvnsgv agsnatitlg tgsslsvasl tngahgeitn agtistsgga
      601 lmneadavlt ntatgtiqng vqsagtfsnv gqvngavevt ggattntgvf ggttsvsgga
      661 lnndggtltg avditggavt nsgtfadttt vtdgslnndg gtltgavtvg adgdlttsgi
      721 vtgtltnagt ttvtdgsvad ldntgnatvs ggvvadldns gsgdltigsg gtvttlsnag
      781 tasnagevgt ltntggtftn tgnvtgtssv tggtldndgg tltgdvtvgt ngtlttsgtv
      841 gdvtnagttn vtggtvasva gsgtanvsgg tvavltsnsg tvnvsggtvn dlngngssvi
      901 tisggtvddl agagtfnvqs ggtvtemtvn ngsatnagtv gsvgvngngt lansvggqvt
      961 gtvsltgtss ltnsgtigga ittsgttnit naatgvmqgt vgvgadaslt tsgtisgtvs
     1021 nagtttvegg tvadldnsgt vtvndgvvad ldnstagqlt igadgevtvl tnagtasnag
     1081 evgtltnsdg tftntgtvtg tstitggdlv nsgtlggnvs vasgaelsts gtingtvsns
     1141 gvttvtsgtv agldnsgtat vtggsvsdfd nsgtatisdg vvadldnggs gqltieadge
     1201 vtvlanagta snageigtlt ntdgtltntg tvtgvstvsg gtvensgtlt gnvdvaaagt
     1261 lntngtvggt idndgtvtvg ggtvaglnnt ntatvndgvv aaltnsgtgq lvintngsvt
     1321 alsnagtasn agtvgaltns dgtftntgsv tgdatisggs vtnsntiagt tvlsggsldn
     1381 sgtlggavtn natlvstgti ngdltnqgna tanlsgtvsg aittqdsasv tvngdldsvt
     1441 sithggsgtf ainsgtttla gagtvtnsgs ftltsatlda tgdavfantg fanlsvgagg
     1501 nldmdlnndg tvqiadggsv ggtlqngsgg svnldgavgg nlsnagtldl sgsvagtlgn
     1561 tgmlmvdgas tvtgtltnag smfvndtlah gnltnsasgp awsdtmlvtd avlrvsgsga
     1621 ltsgtltnss siglsdgati tsavinsgti iadgsvtgag dfthqtgail dlgddtgddv
     1681 fmiagdavln gtielditle geelvgdqiq vagavsgnat fnfnltdada vdllgtvnvl
     1741 sygsgqldsy svnglpnsga avfalvnntd adayqlqsga npavgglatg laltqsligs
     1801 vvnrptspfv tglavpgdep cgfgtwsrat ggratasgss etalgtynse ltanyhgmqi
     1861 gadyscfgga fngwdlsfgg vagynggttt qpvyffdant gqvntdvlts tnrtsfsqsy
     1921 gsayiaasrs fansgrvlfa dvqvrgdkta fdldnsvnaa aldavrtltg datltaedls
     1981 fgvkdqsyds kgvtigasag lsiplneakd lrlvptlgfs lanietdtly fsngeleied
     2041 iesrvgfagl tlaktkiaps gtaafnyfat atvyhdfgsp avsnfylyes gttdrsgdvl
     2101 sssssnlgty gelslgmnft kilqpgsamp grqldtsvrl dsrfsdklds wgltaqfriq
     2161 f
//
LOCUS       WP_284357382             305 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Elizabethkingia anophelis].
ACCESSION   WP_284357382
VERSION     WP_284357382.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..305
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35083
     Region          44..294
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mkrrkflakv plaasalmlg gtatnllaat qkdkninlkk kllltvahit dvhlpadpkv
       61 merfvkclke vktkkvdffl ntgdsimavd rdnstrqevy dqwnawdsci keiadydmys
      121 cvgnhdiwwa ggksdemygv syaakrlkmp nryysakkgk whfimldgnn sgvtldpeqm
      181 nwlkqeleni pqgeyvlims hypiltvtgt feggqhkdhv alkdlfykhk dkvkgclsgh
      241 qhlldrawyn dvyyfcngam sgfwwgegdk rsakpfyyqe tppgyailkf yddgtfeney
      301 ivhhy
//
LOCUS       WP_284357453             482 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Elizabethkingia anophelis].
ACCESSION   WP_284357453
VERSION     WP_284357453.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 482)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003416
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..482
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55611
     Region          <131..>236
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
     Region          280..442
                     /region_name="DUF3526"
                     /note="Domain of unknown function (DUF3526); pfam12040"
                     /db_xref="CDD:432281"
ORIGIN      
        1 mrkniirlis kqvwkqslqn kgilfllvll sclfvfaayt gwrnysvqek irtehqqevr
       61 qqweskpdkh phrmahygyl ifrpryplsf fdsglerytg nsvfleahkq ntanfseagf
      121 ssgmlrfgei siamvlqilv plfifflgfs cisaerennt lkillsqgvk wkelltgkil
      181 gllslvslly fpviivfvml wlslagfkvs idevtrlvwi ilsyfgyffi islvcvlvsa
      241 tsktskssli klisiwllfi vimpraaqaf gsythpapsk idfdtqvese likagdshnp
      301 ddihykgikd sllktykvat veelpfnysg yimtegekls agiynkywne qlniyekqnn
      361 istylsfinp flairnlsma ltgsdfnsyv syqkqveeyr yklaqlmnkl qmenisnkkq
      421 gatdkpytis kdhwkempdf syrfigqkdl frneisails liiwgagllf lihfmskkik
      481 iy
//
LOCUS       WP_284357475             421 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Elizabethkingia anophelis].
ACCESSION   WP_284357475
VERSION     WP_284357475.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..421
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46271
     Region          7..419
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtqnkgkali igagiaglss ayyllkkgwq veileqndls nncsygnagm ivpshftpla
       61 apgvvtqglr wmfnskspfy vkpslsskli swglqflrhs nqkhvdasas airdlnlass
      121 klynelakte dfnfelnqng ilmlyktekv aeeetelahi akelgldvdv ldwkgiqdle
      181 pninldvigg vnykcdghld prklmtqmis ylknngvtfy tqhrvsgfet seskinavia
      241 sgkkftadqy imtggsflpe laqkagikiq lmpgkgysfm ytpensaykl ehaalllear
      301 vavtpmsgqi rfggtmelak hqhkinmnrv egivasipky mpdfqvtlpk eseiwygyrp
      361 capdglpylg assklknlii aggggmmgls lgpvfgrtvs eiangeklsv didifrperf
      421 n
//
LOCUS       WP_284357479             607 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Elizabethkingia anophelis].
ACCESSION   WP_284357479
VERSION     WP_284357479.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 607)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..607
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=69616
     Region          42..574
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mkkvfvsscl isftlcmaqe kiidtvyvfd nqmnrvrnfh hvtkltssdl eknatnlsev
       61 lrfqspvyik engrgavssp sfrgttaqqt afvwnginin ssflgqgdin ntgllgydql
      121 dikpgggsvv ygsgaiggsi hlnntldfnk glkgslysea gsyetfntil rtsysnekls
      181 vkfsgnyais kndyeveekn yinrngnyyn ttfnfglsyk lnynnkiswq sqlfdssqhy
      241 pvffetttpt kyktqnirsl iaweynkkni nnnlrlayte enfqyyania epkssggsgk
      301 nyiikndfny flndklnini isefqqnkge gylsgikdvs rnifslagli ryfpfkklsf
      361 etgvkkdfie disspllfsf sgkwnalkfy niktsfsknf rypsfndlyw qpggninlkp
      421 etaiqldmnh efkindfslv ispfyikikd mirwlptang ywapintdnv esygsevqid
      481 yrkkitenhn inaqlgysft ksvnsdtqkq lmyvplhkff snigyeykfm klyvqgmwng
      541 ktyttsdesn nealksyfvl nagisaillk hysvgfkinn itntvyettl yyplpmrnys
      601 ffvninf
//
LOCUS       WP_284357560             957 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Elizabethkingia anophelis].
ACCESSION   WP_284357560
VERSION     WP_284357560.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 957)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..957
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..957
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=109023
     Region          674..927
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mklkfilssv lvagsvctya qkkpldhsvy dgwqsigsrk isndgkwvgy svdpqegnsk
       61 lylsspksks slefprgskl sftsdskfal fsikpffkdi kavkdkklkk dklakdtlgi
      121 vnlftqkvek ipnvqsfksp ekggawmayl menmkdktat pdakdddadd kkdddantkp
      181 sdlilvnllt gkkttyenvv ryqfsengkq lifvtqkped kdkdkkdnkk pekkdksapv
      241 kyalqtvnwv dvekgtvnkl tegegnfsql tfdelgnrla figtlsaknd lvkdyqlyyf
      301 aqnakntivn nqhanlpkgw vvsenrapif skngkqlyfg iapkpiakdt tliandhavv
      361 dvwnykddyi qttqlknmsr dlkksfgavf qtdkpdvfrr lgdndtdtir linegdapyv
      421 lgysnkgsri qsqwegsdrr iyylinnltg nttevvkeln gnavasplgr yvvyfdrdkg
      481 nwysynvvtk vttqlnknls vsftdeefdm pdkpyaygia swtdndesvi ikdrydlwef
      541 flngkkaprn itnsygrthk itfdtynldk dikslsrkkp myisafnnvt kadgiyetsi
      601 vsgkdpkevy mgdiwgfktl mkaknteeyi ftkesyvksp nlfvtsdfke qtqlsdtnpq
      661 qaqynwgtde lvnwttpkgy qstgvlfkpe nfdpnkkypm ivyfyeklse nlnryvapap
      721 tpsrlnisyf vsngylvftp disynedghp grfaveyins gveylkknpw vdgkhigiqg
      781 qswggyqvth litqtdmyaa awagapvanm tsayggirwg sgmnrqfqye ksqsrigksl
      841 weardlyien splfhfdkvn tpvvvmandk dgavpwyqgi emftalrrlg kpvwmlnyng
      901 ddhnlikrqn rkdiqireqq ffdyylkgak apawmtkgip atmkgkdwgf dltddkp
//
LOCUS       WP_284357604             145 aa            linear   BCT 25-DEC-2024
DEFINITION  bleomycin resistance protein [Elizabethkingia anophelis].
ACCESSION   WP_284357604
VERSION     WP_284357604.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..145
                     /product="bleomycin resistance protein"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=16781
     Region          13..136
                     /region_name="BLMA_like"
                     /note="Bleomycin binding protein (BLMA) and similar
                     proteins; cd08349"
                     /db_xref="CDD:319937"
     Site            order(13..15,45,52..54,56,79..84,89..90,93,134)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319937"
     Site            order(37..38,45,56,58..59,81,116,123,125,129..131,133)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:319937"
ORIGIN      
        1 msndktikfn rlipellvss ieaskvfyve qlgftieyer reddfalisy egsqfmleqd
       61 hatawitgel gsirgrginf qievdcldtv iakietndlp yfrkskeqsy rintieegvk
      121 elliqdpdgy llrfqqylge rdile
//
LOCUS       WP_284357724             349 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Elizabethkingia anophelis].
ACCESSION   WP_284357724
VERSION     WP_284357724.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..349
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40593
     Region          5..328
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mekldyiivg dgyaamffah qllksgktfk lfsegnkaas hisagvcnpv vlkrynkiwn
       61 deaqmdylpv ifneieeylh knyliqenvv rvfhdegeyk lwlkkasqdk fegyldsdiq
      121 klssvenpfg agrvnnscrl dvrnffsdff sflekkkvlv kerfdyneln vdqnayqnyn
      181 fnkivfaegt gikdnpyfge ipvkpnkghr fslhlekdte afvikkkhfl frfsgdeyyy
      241 ggtydrdset heieekavee lkkgleevyk ydykidevst afratvadrr piigrheihd
      301 nlyifnglga rgvlngsyfs kllfdfielg tlfheevnvk rfsqigkls
//
LOCUS       WP_284357795             971 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Elizabethkingia anophelis].
ACCESSION   WP_284357795
VERSION     WP_284357795.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 971)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..971
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..971
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=110898
     Region          45..496
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          556..950
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mrkivstlsl vllmnmmnaq dfkiqtlkdn kgytyetvnn dpdhvrvytl knglkvflak
       61 ntdapriqty ipvrtgsnnd padntglahy lehmvfkgts klgtkdwtke kaliqqisdl
      121 yeahkaekdp akkreiykki davsqeasky aianeydkat ssigatgtna htwldetvyk
      181 nnipnnelek wfkiekerfs elvlrlfhte leavyeeynr aqdndgrlvn yelmsalfpk
      241 hpngqqttig taehlknpsm vainkyfdty yvpnnmavvl vgdldfdkti eladkyfgtf
      301 qykelpmkkm vseepmtkiv ektvkspttp rlqmawrtds ygsneshlae itaqilsnsg
      361 eaglldtnvn qqqkalrava ynsplktygy ftmvivpkeg qsmqdakqll lqqidlikkg
      421 efpdwmipsi iedmklsrmr qletadglat nlydtyikgr swdqelnein eyskitkadi
      481 vkfandffkd nyvvvykekg vndklvrven pgitpiqlnk daqspflkei isekvsdiap
      541 vfvdfkkeik etavkgvkls yiqnktndia qmnyifnfgt dndkelglal nvleylgtdk
      601 yspeqlkaef ykigisynlq igadrinvsl sgpeknigkg lalvnhwiqn vkpdqeiynk
      661 tvktilegre iakkdkarim aalsnyakfg kdsrfrdvis kerltsikae eitnkiksla
      721 kypyelffyg kdlgafekev sgyvqkaslk ypaakvypel ptggqvyftn ydmvqmemsk
      781 igrgeeikpa nfgkinvfne yfgrglssiv fqeiresrsl aysayvnyay pdelkkhdyv
      841 ttyigtqank lpqavsamne lmaelpqiqv qfdnakgsal kqiasnritk rniyfnylrm
      901 kklgidydir kdiynevkdl tlpqlsnfyn tevkpvnynt aiigkkenld mnainklgtf
      961 wevsleeifg y
//
LOCUS       WP_284357828             469 aa            linear   BCT 25-DEC-2024
DEFINITION  MBL fold metallo-hydrolase [Elizabethkingia anophelis].
ACCESSION   WP_284357828
VERSION     WP_284357828.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..469
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51640
     Region          2..184
                     /region_name="POD-like_MBL-fold"
                     /note="ETHE1 (PDO type I), persulfide dioxygenase A (PDOA,
                     PDO type II) and related proteins; MBL-fold
                     metallo-hydrolase domain; cd07724"
                     /db_xref="CDD:293810"
     Site            order(54,58,110,133,136,140..142,184)
                     /site_type="active"
                     /db_xref="CDD:293810"
     Region          255..357
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
     Region          358..448
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mkveqiytgc laqgayyivs qgesviidpl revrpyldkl qqdnaklkyi lethfhadfv
       61 sghvdlsdkt gasivygpta kpefeaiiak deevfeigdi kikvlhtpgh tmesscylli
      121 dekgketalf sgdtlflgdv grpdlaqkgk dltqedlagm lydslmnkii plsdeitvyp
      181 ahgagsacgk nmqketvdtl gnqkktnyal nqpdkasfik evtdgltppp gyfamnvamn
      241 kkgyesfdqv lehglkplsa eafeamadet galildtrpa sefhkgfipq svnigvkgdf
      301 apwvgamivd vnqplllvtd egseeevitr lsrvgfdnvv gylkgglsaw qsagketdsv
      361 eritpeefaq rytedskiid vrkegeyaae hiaeaysrpl ayintwikdi dpkehfflhc
      421 aggyrsmiaa silqargyrn fteveggfgk ikltevpttd fvcqsktmk
//
LOCUS       WP_284357971             376 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Elizabethkingia anophelis].
ACCESSION   WP_284357971
VERSION     WP_284357971.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..376
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=42397
     Region          7..375
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 msnatfsdsk khyeildglr giaaimvvml hileifaggd htklminhgy lavdffflls
       61 gfviahaydd rwnnmtigqf fkrrlirlhp liiagmtlgg iffyfsessv lfpivgetpv
      121 wklilvmlig ytlipvplsl dihgwgemhp lngpawslfy eyvgnilyal flrktsttvl
      181 silvllsgaf layytisspq gdiiggwslt geqltigftr llypflagll lhrifkpmsl
      241 kngfllcsil livvlampri gekehlwmng tyesiviifi fplilflgas gniqgkvatk
      301 vcnflgdisy plyithfpvl yvyyawvvnn kvtldqawpv gigilissiv vawlllkyyd
      361 ipvrkwltqk ymnpkh
//
LOCUS       WP_284358021             602 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF885 domain-containing protein [Elizabethkingia anophelis].
ACCESSION   WP_284358021
VERSION     WP_284358021.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..602
                     /product="DUF885 domain-containing protein"
                     /calculated_mol_wt=69030
     Region          1..602
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
ORIGIN      
        1 mkklikigml asmgltlaai scqkkdsvkn eatesrenek ltqladkyye aylrhsplda
       61 tyqgdirynd llpdnisakv iaeeinfynn tikelskiny ealddqhkvi fdvldnqlkt
      121 kvesyvyhpe yipfsqfegl pltmpllgsg kgsqpfktvk dydnwlkrid qfpawmatae
      181 qnfrtgmknk mvlpkklvvk mipqlsaaei ttiefnknif ygpvkefpkd ftteqrqkyt
      241 klfqeaikdk iipayshmak flkeeylpna rdtdgynalp ngkdiyayyv ktwtttnktp
      301 deihktglqe varireemek vkaqvgykgt leeflvhvkn dpktmpykts keildgfqgi
      361 ltkitpklkt mfnvtpktpf eirqtekfre atasaeymqg tpdgkrpgif yipipdprkf
      421 nvtsgmeslf lheaipghhy qislqqentk lpkfmrfgwl gaygegwaly ceslgpefgl
      481 ytdpyqklgs lsdemmravr lvvdtgihtg qmtreqaiky flsnvaydea gataeierym
      541 aipgqalsyk tgalkirelr tryekqlgtk fnlasfhdev lsqgclplsv lerkmdlwsk
      601 kq
//
LOCUS       WP_284357978             246 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Elizabethkingia anophelis].
ACCESSION   WP_284357978
VERSION     WP_284357978.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 246)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 246)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 246)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..246
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28475
     Region          1..241
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mrvyvledee nirnyilsil keipeivvvg yadqvqtalv eipklephli ladirlkdti
       61 sfrlfdtldi ekykvifita fshysiqaln lgaigyllkp iaddelkaai qkvivkneay
      121 lvhqcqlqla nsyiekpkev eklvlknrdy lqiircddiv ycegdkgytt fflnnepgvl
      181 vskvlkeyet llstanfirc hqsylvnmny vtryfkegyl qlrtgvkipv strkkddvlr
      241 yleqll
//
LOCUS       WP_284358056             414 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Elizabethkingia anophelis].
ACCESSION   WP_284358056
VERSION     WP_284358056.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..414
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46842
     Region          1..410
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mtkseyqeal ewlfvqmpny qtdgikaykp gldniirlce yfgnpqkelk mihiggtngk
       61 gstsnmlasv lqeegykigl ynsphlihft erikvngkna ndefvynfiq klknlpeeik
      121 psffefttim afeyfrqqkv dyaiievglg grldatniil piltaitnia ldhtnilgnt
      181 keeiarekag iikagipvvs gdenpsvrni iqqktnelna kfidatslnp eldsdlkgay
      241 qknnirvvla lveelrlqni siskessekg llhvhkntnf igrwfefskn plticdtghn
      301 qagleyvfnq lktysqskhi vlgfvndkni ddvipllpkn ekfyfvkpsi hrgrnpqeye
      361 dlikkenlny qifndvqsgy laakenctad eiifiggsnf vvgdfleknl avhe
//
LOCUS       WP_284358049             214 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Elizabethkingia anophelis].
ACCESSION   WP_284358049
VERSION     WP_284358049.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..214
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=23980
     Region          75..198
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
     Region          108..148
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          153..186
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkklflatal lltgfiafaq sayekvmtdk igkivqcktn ddftalsndf srigdkeksq
       61 wlpyyyaals viqggrvlmr dqktdgldvs gdaalnyisk aeslspnnae lfllkkmahg
      121 ikmmvdpmsr ymtegqeaqk algeaikldp nnpriyilqa edlyftpeqy ggdkkkaket
      181 flkakelfkt nkpktaidpn wgeseadyfl sqmk
//
LOCUS       WP_284358194            1419 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Dyella nitratireducens].
ACCESSION   WP_284358194
VERSION     WP_284358194.1
KEYWORDS    RefSeq.
SOURCE      Dyella nitratireducens
  ORGANISM  Dyella nitratireducens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1419
                     /organism="Dyella nitratireducens"
                     /db_xref="taxon:1849580"
     Protein         1..1419
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=141075
     Region          <3..1315
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 msnptinvsa fqaatggnqq lmdlipilnn sptlvglint ftanannklv igtnnqdpvn
       61 tsgsgstati sssffanfdp ttinvaqndg vneaeaigve ighevahtvs qggqytqnpt
      121 slsqgesadl naegvasvas ynvanefnqw ntaqygagfd vqaandnsgl qnvlngvtig
      181 sypslaaaqv aaaanwmstq npssatslty kqyiddsvav qlcngsssti nsaglnnsli
      241 twpsvtpnnf vvtpdangdg gwslsaqgiq tsngtfslsg ssspsqvtkc vfnqttpsgq
      301 qsaylfgqga qddisnatvs aapasqvait gnannvtsgs gtttdvqgng ntvtamggti
      361 ndtagdsgnt fdgdqtiina ggsfsgtvdg ignsiylvsn tssdltlgga sqsvfstgnq
      421 islmgsdaga tvtgvntisl esanqsltld tsgdtvntsa gdtgemlngs gfrlnggagq
      481 fmgtvsgsnd tfnldassns slaltgtget vtsagntial dgadssgtva gantvdmngt
      541 nqsltlsssg dtiavaaddt dtingsgani sagtdafvna fgsdntvkgt tgdgmgvtgs
      601 gntidagsde lvwingtngt adtvvgsaia tgdtmangqg sgiwvannaq vnvegsdnsi
      661 ggasgdsigv ngggntvdag sdelvwlnat ngtadtvigs diatgdtman gqdsgiwvan
      721 ntqvnvtgss ntiagtsgds igvngggntv dagadelvwl natngtadtv vgsdiatgdt
      781 langqdsgiw vanntqvnvt gssdtiagts gdsiginggs ntvdagadel vwlnatngta
      841 dtvvgsdiat gdtlangqds giwvanntqv nvtgssdtia gtsgdsigin gggntvdaga
      901 delvwlnatn gtadtvigsd iatgdtlang qdsgiwvann tqvnvtgsgd tvagttgdsi
      961 gvtgggntid agsdelvwvn gtggnadtvi gsniangdam angqdsgiwv tdnaqvdidg
     1021 sgnaigmgsg dvlslngsdk ndffsgsddt lhadsqddft idgsddtvtg sddqvslsgq
     1081 gdlidishat vdvsgddgvt idgsddkivg nsgddftitg tddtvdasda sitfdgtntg
     1141 dyvsgssdtg snwddptgsg gysdpgtgyy gygmtkwknk npsaaqiaka ehsdsvyega
     1201 kwvdktitws fasagngysd aiansaeqas vaqafqawak asglnfdeva agskadievg
     1261 fsdlnpastn qigltkysse agvltganva ledpnqaalt snasgqltya ntdatfeqvv
     1321 lheighalgl tdtdvagsim namlgtdnqa isatdatnvq klyantsssn aelsqvhqlv
     1381 qamstfdage qgidlnpmae lylqkehllv gslsharav
//
LOCUS       WP_284358334             414 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Candidatus Phycosocius spiralis].
ACCESSION   WP_284358334
VERSION     WP_284358334.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..414
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=46416
     Region          143..408
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 msdqilpdti pvthaiarrl rgvplafkma amamtkiveg qilvtlpdgr illfqgykpg
       61 ksatlhikdf gfirrvaaqg digfaeglma gewdtpdlav llevfssnld lmpklllggp
      121 lwmvinkfrh kflkrntksg skrnilahyd lgnsfyarwl dpsmtyssav ykdagedlts
      181 aqmnkyrala eqvnlkpghk vleigcgwgg faefaareyg ahvtgltisk eqhnyaverl
      241 draglshltd iqltdyrdiq gefdavvsie mfeavgeeyw ptyfdkvnsv lkpggkaglq
      301 iitideslfd vyrtradfiq ryvfpggmlp tvprlkqeia raglvwqsta afgisyadtl
      361 aawarsflae wiqikdlgfd erfrqlwrfy layceagfrt gridvghfsm vkpt
//
LOCUS       WP_284358379             369 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Candidatus Phycosocius
            spiralis].
ACCESSION   WP_284358379
VERSION     WP_284358379.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18602699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..369
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=42162
     Region          29..134
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
     Region          <63..111
                     /region_name="Methyltransf_11"
                     /note="Methyltransferase domain; pfam08241"
                     /db_xref="CDD:462406"
     Region          <201..>341
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
ORIGIN      
        1 mttlaheeqk qfclsvkqkf pdffrdkwvl digsfdingn nqylftqcgy lgldllpgkn
       61 vdlvstghel qlpdatfdvi istecfehdq yyaktitniv rmlkpgglfl ftcattgrpe
      121 hgtrrttped apftgafgdw gdyyknleea diravcdieq ffscfefssq hkthdlyfwg
      181 vkhgvlpsrd dysfhlpeap lqrtyealrr ledeaaatas alheerthrg eaearclilq
      241 dratwsegrl setetrlset etrlsstemr lsetemrlsa tethltaten rlseaqaqaa
      301 ralheertqr vetevrltat etrlsevqaq amfaeeerrr iigsnswrit rplraaarlv
      361 rgqttgfrk
//
LOCUS       WP_284358440             390 aa            linear   BCT 25-DEC-2024
DEFINITION  two-component system sensor histidine kinase NtrB [Candidatus
            Phycosocius spiralis].
ACCESSION   WP_284358440
VERSION     WP_284358440.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 390)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 390)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..390
                     /product="two-component system sensor histidine kinase
                     NtrB"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009399 - nitrogen fixation [Evidence
                     IEA]"
                     /calculated_mol_wt=41743
     Region          32..384
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 meslnttkvs vgfdasqika rqtvdregqi aaafldalpl palgvkdgte iilangaaqd
       61 lflksirsik tngilglfsq dspihdller arvtsspvsa rdmklggagf gdfmcditas
      121 psedgsfvav vlrprgrgrd lsermqdmag arsmaalgrt lahevknpla girgaaqlll
      181 rdadpgelel vnliveetdr vrrlidrmes fgadppiefa svnvhaaler vaalaengfa
      241 rdhvvkrlfd pslpealgde dqliqvflnl aknaaeatht hqggaeiila tayrhgvrir
      301 tasgetrdlp leiafydngr gvsddvkdcl fepfvstkps sgglglplvq kivnahggvv
      361 dfesepgrtv frvrlpvstq ragpltahyp
//
LOCUS       WP_284358517             466 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Candidatus
            Phycosocius spiralis].
ACCESSION   WP_284358517
VERSION     WP_284358517.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..466
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=50619
     Region          24..392
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mstsqpipig qqagskstns ekfarlyrml wrwhfyaglf cipfiillsi tgslylfkpq
       61 ieaaldrpyt qltfegasap vsqqvnvala qiegsrlksy rlpdgprdaa qvlvthkgvd
      121 tlvyvhpssl avlkavpked rfmaiirnih gellmgdkgs lvvelaaswa ivmvvtglyl
      181 wwprtakgvm gvlvprlrag pqvfwrdmha vtglwvsffa lfilltglpw tnvwgggfdq
      241 vrawskteak skdwtnsrsg erqasmaafe hgghfapyyl atiddiaaea raerlmppve
      301 iapptaknpn wtarstapdr isqvsltyha qdgalvgrqa fadkavldqa vgigiaaheg
      361 qlfgplnqam glltalglit lsasafilwr rrapegglga pppipdskig aglgllifvf
      421 glflpvlgas ivliavlerl vlaripsvsr flglvpnrpv qsktfp
//
LOCUS       WP_284358587             403 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Candidatus Phycosocius spiralis].
ACCESSION   WP_284358587
VERSION     WP_284358587.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..403
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42698
     Region          26..389
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 miepigglaa sfvsflvvlg vvvfvhefgh yqvarwfkvk iesfsigfgp elcawtskag
       61 vrwriaalpl ggyvkfegdk dvssqsvssp tfkdgiadrn sglfhaqpvh vraavtaagp
      121 lfnfgfsiav faiffaifge mvqrpiishv lpdgaaaaag mkagdevvai ngrkiddfvd
      181 lqtaimvsgg kemaldirra dgavhirvtp kiverqtpfg dketqgllgi etrftretve
      241 krsynpiqal vrggeqtani iatqfnfila vlrggmsagh ingplgifqi agkvtensva
      301 eagpqasaaq vaesvgiglv rlaavlsvav gfmnllplpv ldgghlvfya aeavrgkpip
      361 ekvqaisfqi glacilslfv fatfqdlers glfnllkgfv aag
//
LOCUS       WP_284358724             610 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF885 domain-containing protein [Candidatus Phycosocius spiralis].
ACCESSION   WP_284358724
VERSION     WP_284358724.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..610
                     /product="DUF885 domain-containing protein"
                     /calculated_mol_wt=65956
     Region          8..604
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
ORIGIN      
        1 mqitrrdall gaasvcagsf lwgcsqskad npalkalidt itttmlkdsp eiassltvpe
       61 alaggpykar vsdasadaei krnqwvagwl kdlgaidqts lnptdkithq vvtsaltysa
      121 aaapmgygsa gygspnpylv sqltgsyvgm pdfldsqhvv ktkddaqawl srvegfagqm
      181 gqevtrvkad vakgvvppdf iidrtlgqlr tfmrtpakds vlvaglvrka keagldaagl
      241 geactklvie kvlpayqaqi dlfeglrgqa ksdagvwklp egeayyqaal gywtttkmtp
      301 nevhelgrdl vgsygsqmda glkqlgmtqg svgermaalg kdpkylypnn eagktqllad
      361 lnvqmanlkk rlpevfatla kadcevkrvp ayteagapgg yyqqpapdgs rpgayyinlr
      421 dtaarpkwsl ptltyheaqp ghhlqislaq eaqglpflrs kmlwfgayge gwalyaeqla
      481 delglyegdi agrlgyaqsa afraarlvvd tglhakkwsk eqavdymmea tgdtrdsivt
      541 everycvwpg qassymvgkt niirlrtdak tklgdkfdlk afhdqillrg pmpldvldqv
      601 ivdwqngika
//
LOCUS       WP_284358704             928 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_284358704
VERSION     WP_284358704.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 928)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 928)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 928)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 928)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..928
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..928
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=103014
     Region          28..927
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvnykvfta slffmgvcvy sqkkdtllke nkidevivvg ygkstksrmt dnvakisaes
       61 ikevpnanfq nalvgkaagv qisqtngkle agfnvnirgs asisagtgpl yvidgipmin
      121 rdestneapv nplvtlsase iesveilkda ssaaiygsrg sngvvlittk tgkkgkprls
      181 fnisqgfssp tnkvrflnak eyvellleag rnvndedfvi rrfnrysnnt dwrngaidtd
      241 wqkyifrqgs vrdadfsvsg gndnynymft asnndskgii rgndlgrnta rlnisakvtd
      301 klklgmnlgf srtsidrvan dnafvtpmqa vaqapispaf idgepfagtp yanflledky
      361 anyntlikrl tgklsaeyki lknltfnsdl gydyynqkek nyrgrkvpqm atdgyaynsy
      421 vdtenlvftn ylsynlkfgs nnistvagte ynknrrefgs vtgirfpsdd fqninsagei
      481 tegkgeasey tffsyfarvn ydykgkyllk gsirrdgssr fgqanrygvf pafsagwvis
      541 kenflsesnt isllklrasw gktgnaeigd faardqwqat kykqlpgiep fqpanpdltw
      601 ekstqtdigl dfglfsnris geidlynkkt ngllfqqnip ytsgyasiyr nigdmsnkgf
      661 eivlntqnfr kenftwntsf niasndnkit alpdnnadqi igntilrvge rsasfyltey
      721 agvdpangda lyykntlkpd gmldktttnq ysqanrivag tftplwiggl tntleyknfd
      781 lsftlygefg asmynsggkf mstagswfdn qtadqmnrwq ksgditnvpq arlgeengtq
      841 estrylekrd fvrlrnlslg ytlnkdlmks lgvsklriyv sainlltftk ysgydpeala
      901 dtgrggggat fysappartf tfglnvnf
//
LOCUS       WP_284358739             365 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide)
            pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
            [Candidatus Phycosocius spiralis].
ACCESSION   WP_284358739
VERSION     WP_284358739.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Davies,G.J., Gloster,T.M. and Henrissat,B.
  TITLE     Recent structural insights into the expanding world of
            carbohydrate-active enzymes
  JOURNAL   Curr Opin Struct Biol 15 (6), 637-645 (2005)
   PUBMED   16263268
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   4  (residues 1 to 365)
  AUTHORS   van Heijenoort,J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit
  JOURNAL   Nat Prod Rep 18 (5), 503-519 (2001)
   PUBMED   11699883
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Ha,S., Gross,B. and Walker,S.
  TITLE     E. Coli MurG: a paradigm for a superfamily of glycosyltransferases
  JOURNAL   Curr Drug Targets Infect Disord 1 (2), 201-213 (2001)
   PUBMED   12455415
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..365
                     /product="UDP-N-acetylglucosamine--N-acetylmuramyl-
                     (pentapeptide) pyrophosphoryl-undecaprenol
                     N-acetylglucosamine transferase"
                     /EC_number="2.4.1.227"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0050511 -
                     undecaprenyldiphospho-muramoylpentapeptide
                     beta-N-acetylglucosaminyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051991 -
                     UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-
                     glutamyl-meso-2,
                     6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol
                     4-beta-N-acetylglucosaminlytransferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0030259 - lipid glycosylation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=38075
     Region          1..359
                     /region_name="MurG"
                     /note="UDP-N-acetylglucosamine:LPS N-acetylglucosamine
                     transferase [Cell wall/membrane/envelope biogenesis];
                     COG0707"
                     /db_xref="CDD:440471"
ORIGIN      
        1 mgplviiaag gtgghmfpar afgdaivarg gqvalitdpr gkrytegfpa kdililpvtn
       61 adegglrgki dagfavmksl slvrpfmkdl hpdaiigfgg yptfpvlass gkvpvlvheq
      121 navlgrvnrl fqgkavaias gfaqleglde pdkhvvvgnp vrqaivnarl ggypdlssgd
      181 lrilvtggsq garilgavvp eaiaalpehi rarlfvshqv reeqcdgard iyvqagvgce
      241 vwpffkdmad rlakchlvig ragastvset avvgrpailv plpgatndhq tfnakalasv
      301 gaadiiqeqa ftaskltdll gnrltapdel qkrakaaksv gqpdaaeala dlvyraisqn
      361 qlava
//
LOCUS       WP_284358851             391 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Pseudomonas putida].
ACCESSION   WP_284358851
VERSION     WP_284358851.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..391
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=43175
     Region          160..349
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mlyqknwarv wlglglvwfl aaialapsnk iyqqglvlfl wlptlvlaws arevlvqack
       61 rqpalwmsll lllawsglsl vwssaedpgr eikrlvyilv flmafpllaq lglarirqll
      121 llgsallava alvsvihfyg vlgmpwrarl qgigeishpi lgayvvgaav lfmlyepprq
      181 rglqllwlva laclgafaml sqsrgallal vltvimaplw frdrhsrvfs ilavfatgva
      241 fyvvydliak rgssyrpeif havvdmiaah pwtglglgta ydvsavgkhf dhthnmfthv
      301 avemglpgml lwvmvwlftl geiirargtl fgkvllgfwv ystlamqfda asltgtprae
      361 wfiswlpvgl ammlpwgrae ndacgkisgs t
//
LOCUS       WP_284358871             107 aa            linear   BCT 25-DEC-2024
DEFINITION  BolA family protein [Candidatus Phycosocius spiralis].
ACCESSION   WP_284358871
VERSION     WP_284358871.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..107
                     /product="BolA family protein"
                     /calculated_mol_wt=11391
     Region          3..98
                     /region_name="BolA"
                     /note="DNA-binding global transcriptional regulator BolA,
                     affects cell shape, cell division and biofilm formation
                     [Transcription, Signal transduction mechanisms]; COG0271"
                     /db_xref="CDD:440041"
ORIGIN      
        1 mgpiqlqmrk klidafaplf leitdesarh ashigaklha akqggasvvs gethfsihmi
       61 saafegqslv arqraiyqvl aeelsgpvha lslkaeppld nwpvqas
//
LOCUS       WP_284358894             148 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Pseudomonas putida].
ACCESSION   WP_284358894
VERSION     WP_284358894.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 148)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 148)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008128
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..148
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16230
     Region          1..146
                     /region_name="CytC556"
                     /note="Cytochrome c556 [Energy production and conversion];
                     COG3909"
                     /db_xref="CDD:443115"
ORIGIN      
        1 mlnrltvvll aalalsgcdr vdpnsplgkr kvifkdmlkt sedlggmlrg rlpfdglkfa
       61 dgalkldsls hqpwqhfpqv rdggdsaara evwelqarfh dlarqlesvt gelvdvsrsq
      121 pldaaqlkap mdkveaacka chtefrnh
//
LOCUS       WP_284358910             262 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudomonas putida].
ACCESSION   WP_284358910
VERSION     WP_284358910.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..262
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29545
     Region          28..242
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mplvarlfwi lllaclspla lgerlrlvsd dwapyiyqhd gqprgidyev ttevlkrlgv
       61 evewqflpwk rclamieqgl adgildifqs etrrpylvya peplsevefv lfqararrha
      121 varpedltgl tvgtspgyay gaafnqathf rreaaptqea nfgklllgri dlaitdrvvg
      181 hylirqlgme qqveelplvi nrqaqylglv rkpgretlal afaeelqrfk qepafaaish
      241 rytgdignil naveqqesst ar
//
LOCUS       WP_284359258             391 aa            linear   BCT 25-DEC-2024
DEFINITION  thioredoxin family protein [Elizabethkingia anophelis].
ACCESSION   WP_284359258
VERSION     WP_284359258.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..391
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44592
     Region          1..130
                     /region_name="SoxW"
                     /note="Thioredoxin-related protein SoxW [Posttranslational
                     modification, protein turnover, chaperones]; COG2143"
                     /db_xref="CDD:441746"
ORIGIN      
        1 mkklistlfl flgllafsqa gikfddgnfs sllakakken klifldayas wcgpcklmak
       61 niftlqsvgd yynshfvnak mdmekgegve lakkynvkay ptylfingdg evvhrvlgyv
      121 eekpfiqfak daedpkrnig alkarfekgd adpeflrnla mltiyedanf sgkvtkkyfe
      181 vksdkafsqe diqlllsglm ntedpryeif knkkeeivki lpaaqyeafd knikmntiik
      241 kaynpdtktl nteyfltete kafgkeqaek mlvrvkasya lknkdyatye kltleqykdf
      301 skananelns aawnffenvk dkkslqtail waqesvkkde syantdtlan lynkvrdkkn
      361 aklwaeksve lakksgedat etqklldslk k
//
LOCUS       WP_284359400             251 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Candidatus
            Phycosocius spiralis].
ACCESSION   WP_284359400
VERSION     WP_284359400.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..251
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27539
     Region          30..232
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 milirsllls vwialsvliv gtlgvpyvla frlggahvmt vwarvaafga rwicgikfev
       61 rgienmpngp vmiaskhqsm fdtiapilft rfpvyvlkqe llslpifgwy crkagliavd
      121 rsghmsalra mvahakerfe egrpliifpe gtrqpiglpp kykpgvaaiy mllgvpcvpm
      181 alnsgvawpa kgilryggtv vfeflpmipp glkreifmel leskietatq alvdefhgqg
      241 lvrkvakets v
//
LOCUS       WP_284359398             303 aa            linear   BCT 25-DEC-2024
DEFINITION  cell division protein FtsX [Candidatus Phycosocius spiralis].
ACCESSION   WP_284359398
VERSION     WP_284359398.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..303
                     /product="cell division protein FtsX"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=32433
     Region          29..279
                     /region_name="FtsX"
                     /note="Cell division protein FtsX [Cell cycle control,
                     cell division, chromosome partitioning]; COG2177"
                     /db_xref="CDD:441780"
ORIGIN      
        1 minalkllwv rfthesqsal lptdsrqvrp ltivvaimca lgclaglgas agfraastwt
       61 sdlksamsii vqsprgdedl eraalivgri egvtrsetms rerakellrn ygtdlsttld
      121 alpvprliev gvmsgqttvk ediekeltaa gfkivvddhs rftgeilrts tmvrilamma
      181 llslvvaala tiafaaraal etrreavhil hlvgakdafv arevqkrflr lgfvaglwga
      241 naagiiallg ltvfafgasd ftsgsplvsw tdlwillvap fitafasawa aevaaratlr
      301 dlv
//
LOCUS       WP_284359445             269 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Candidatus Phycosocius
            spiralis].
ACCESSION   WP_284359445
VERSION     WP_284359445.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..269
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28985
     Region          5..262
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 middvssthn sliklaksld rkktrsetgl flaegarhvg egldqgwqle allfsgaaet
       61 rlavqalaqk aldvgarvar vtdrvleava krdnaqsvig lfqqrlssls slmdapfiia
      121 lerirdpgnl gtimrtldci ggggivllee scdpfsveav rasmgsvfst pisksdfasf
      181 nmwrkdfgfk lvgtslkgsq rhtdtdfgtk tvllmgneqs glpdswaqac dglvrlpmsg
      241 radslnlaia tavtayeiwr qkdffgard
//
LOCUS       WP_284359497             258 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Candidatus Phycosocius spiralis].
ACCESSION   WP_284359497
VERSION     WP_284359497.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 258)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19108954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..258
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28182
     Region          10..207
                     /region_name="NUDIX_AcylCoAdiphos_Nudt19"
                     /note="Nucleoside diphosphate-linked moiety X)) motif 19;
                     cd18870"
                     /db_xref="CDD:467582"
ORIGIN      
        1 mtgaqdplyp astlllvrdv adglevlmve rhanigfagg alvwpggkve vadfeegwld
       61 hadgldglsp deraariaai retfeetgvl lahldgalig pkvqdlklmr hkidrdaslf
      121 lplvrdqglr ltgnnltpfa rwipppalhk rfdtrfylar vpadqigcqd gteavellwi
      181 kpkaalqela egkrkiifpt vrnlellals pttdraltda aarpqgivqp iiedgvlkir
      241 ddlgypvtqe rlesalrg
//
LOCUS       WP_284359513             403 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Candidatus Phycosocius
            spiralis].
ACCESSION   WP_284359513
VERSION     WP_284359513.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..403
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43668
     Region          6..403
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 msksspeatg plkglrviel gvllagpfcg qllgdlgaev ikieppdqgd pmrdwgpikp
       61 kgqglwfpiv arnkkcivan mrkpegqqil kdlvadadfv lenfrpgtme kwgigydtls
      121 ainpgiimir vsgygqtgps shkagyasvg eamgglryvm geadrmpsra gisigdtlaa
      181 tfatigalaa lehrrktgrg qmvdaaiyes cfammeslip dfqfgnyire ragsilpkia
      241 psniypasdg mliiaanqdt vwcrlaelmg rpelahdpry athiargehq geldelisaw
      301 trtqtsqsle diceqggvpc griyrapeml qdehfaarqa iievehpvlg gfkmqnvfpk
      361 lsetpgnvrw tgpdmgahtl evlqnilgyd dtkiealkav nai
//
LOCUS       WP_284359686             193 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Candidatus Phycosocius spiralis].
ACCESSION   WP_284359686
VERSION     WP_284359686.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..193
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=20593
     Region          1..187
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mkfilasasp rrqellarig ivpdaidpad ldetplpget gralalrlak ekaqavasrh
       61 ptalvlaadt vvcvgrrllp kaetrqqale cltllsgrnh kvitaigvql gakaasrave
      121 trlhfkrlsa lelsgylesg qwmgkaggyg iqglagafct tlrgswesvm glplyetvcl
      181 vegfgyrrri etg
//
LOCUS       WP_284359720             354 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Elizabethkingia
            anophelis].
ACCESSION   WP_284359720
VERSION     WP_284359720.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..354
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40696
     Region          6..345
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mknvfdilen yikkikfngn imiaerrkil ytgsfgntyh peekpelsrs svfelasvsk
       61 pftafamlkv mdvyhlslht dvkyflpdfp yegisvfqll nhtsglpdym elfeefwdkt
      121 iiadnsdvlg llialrpkvy fnpgerwdys ntgyvilavi lekitgfsfp evlkkyifrp
      181 ldmkntmvyn rrkkpqlipd yafgissdpe tgklklpdti kgeeyvyyld giqgdgtvns
      241 tlddlliwnn aileqylvde kyldlmfept vnndgqvfpy glgweldekk ngekqvyhtg
      301 gwpgyftyns lylnsgisvi llcnkpdsed venemlqkle daafgkkspr tlys
//
LOCUS       WP_284359745             142 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Candidatus Phycosocius spiralis].
ACCESSION   WP_284359745
VERSION     WP_284359745.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10021508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..142
                     /product="ExbD/TolR family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=15639
     Region          17..138
                     /region_name="tolR"
                     /note="TolR protein; TIGR02801"
                     /db_xref="CDD:274306"
ORIGIN      
        1 mtsrrglsrh grrprrlmge invtpfvdvm lvlliifmia aplltvgvpv dlpkteaknl
       61 pteteplsvt ilangqvylq demiaydqlm pkltalagqg ydrrifiraa ekapygivmq
      121 vmarintagy knlglvtdtv eq
//
LOCUS       WP_284359814             141 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Pseudomonas putida].
ACCESSION   WP_284359814
VERSION     WP_284359814.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..141
                     /product="YybH family protein"
                     /calculated_mol_wt=15742
     Region          2..125
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mstaaeteir qligrwmqav rdrdipnita pyaddivafd aiqalqfkgk aaytahwemc
       61 igmctgpmvf elaeltvhaa gdlalahwln rcgpgddesq cgfmratvgy rrkgdqwqvi
      121 hehwsapfdm etqkalfdlk p
//
LOCUS       WP_284359888             415 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudomonas putida].
ACCESSION   WP_284359888
VERSION     WP_284359888.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..415
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45061
     Region          6..415
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mvenpeadia vvgagivgva calqlarqgr rvllvdrqap ghgasygnag hlateqvfpi
       61 adlsilkrlp rmlldpmgpl rldwkylpta mpwftrllln lrpapfqrsv agirtlnegs
      121 lgawqrllgs igrsdlfqed gsllvfekpe srqalealrt rmqqqavpvd vwsaetvrea
      181 apqlspsllg glffprtghf idpyrvvcel feaakasgvr fvqaqvdggq lhsagvslas
      241 dqgtlnarqv liscgahsak ltaaltgkrv pldtergyhl mlpgehqrlp favtslerkf
      301 imtpmaeglr lagtvefagl eappsmqraw qlhrlskglf rqdlsvegat pwmgfrpslp
      361 dslpvidrvc dgrvllafgh qhlgltqaav taewvgrlae qvggpgtaay rldrf
//
LOCUS       WP_284359913             545 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Candidatus Phycosocius spiralis].
ACCESSION   WP_284359913
VERSION     WP_284359913.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 545)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 545)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 545)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..545
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=59072
     Region          35..545
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          300..545
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mpsrhcmglg iaikkpkhna tesfgktqrr hrrggiagii fianfagili lvlgsllfne
       61 lrsgltkarm ealraqgsti asviaeaaip pdalpaldem rarailrqlt repgarlrlf
      121 drelrpiads svlddtvevr qlpplgpaap dvvdvadrav anarvfiqga sddphkalir
      181 eistalqgqv vqserfdeng rrvvsvtvpi qriravvgvl tlessdvsei vdaerralyp
      241 filsailvta lsatllawsi avplrrlaaa addvrrgraq algadklrqr pdeigdlada
      301 laamtqtlqd rinanesfaa dvaheiknpl aairnaaell pratseeska klesiilsda
      361 rrvdrlvtdi anasrldael arasqkkfam admiddmgrv yasiahahqv kiivqhtdet
      421 drllvsaree aisrvltnll dnalsfspaq aniylrgtre hekvcvqved egpgipqeal
      481 qsvfkrfyth rptsvgeegq aafgkhsglg laiarqiaes hggilwvenr tegqgarfvl
      541 elpaa
//
LOCUS       WP_284359916             468 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Elizabethkingia
            anophelis].
ACCESSION   WP_284359916
VERSION     WP_284359916.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..468
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55040
     Region          <358..468
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mdmvinkfgk nifsilliif vviniacqkn nkektsvena mglqkendsi hatinvefid
       61 tgvfalntli nqrsfsinip ssksikkksk qlslvkpsvf esyrlvknki vvkryfvfke
      121 dtlsfkfcrd cinsysgnak nnilnilind nnvfavqtpn niinyieeqr knyeknvrev
      181 qkmantynna eqgfiidylt lyfynkifni dfskvndpkt ieqldfyyke ifdniklldk
      241 lntilnknil ynllrftsfk nknpdllecl hfldsklyqt ealdgflldy mesfynnlsd
      301 kdlitikkyi rkrslknifd rktkkisenv fssklqdvns nealfqevll vkateslvli
      361 dlwatwcvpc lnempawnks eqkykgkikf vkisidnnfe kwynflsskn dhnfnyiitn
      421 snhpfikefk istiprymll nknheiisdd ftrpsdsrfs eqiekylq
//
LOCUS       WP_284359951             424 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Candidatus Phycosocius spiralis].
ACCESSION   WP_284359951
VERSION     WP_284359951.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..424
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44304
     Region          1..390
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 msdttlhhls ngvrllmdpi sglastsvgv wvkvgaraet laengsahll ehlvfkgagg
       61 rdaralaeda egqgvylnaa tgyertgffa rclaedagfa lsltadlvlk phlraedlel
      121 ekhvilqeig eafddpedrc gvlhqqaafp dhalgrpilg deaslagidh aaiaafrart
      181 yapsqmivav sgafeasaiq dqveqafggl apftapalap vslggqalse vrdaeqihlt
      241 fslpgpnlgs qqaiaarvmc eilgggmasr lfqdlretrg lvysveafsd lyedggricv
      301 sagctpnvge evarrsaqhl vdlaqkgpse kelkralril easmmmaaes pparcevavs
      361 qtllygrpla lfevasrirs vttehvqava tsaivggqag fgaaaaigpt lglgaaevfa
      421 asfr
//
LOCUS       WP_284359940             499 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Candidatus
            Phycosocius spiralis].
ACCESSION   WP_284359940
VERSION     WP_284359940.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..499
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=54038
     Region          1..489
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 msktvlivdd dpsqrrllqa averqgfatr saedgaqaia qaldpavdvv lldlimpgvs
       61 gmealaairt krddlpiivl tasggidtvv kamqagasdf fvkpasperv lvsirnalkv
      121 gelsgevkrl kkkatgtftf idmvagafam rqvirlgqra aasnipvlil gesgvgkevi
      181 araihgeser sgrpiitvnc gaipenlves ilfghekgaf tgaherhlgk fqeaaggtlf
      241 ldevgelpld mqvkllralq egevdpigsk rpikldvrmi aatnkdlakl vaegrfredl
      301 yyrlnvfpid vpplrdrmed iqdlvkhfvt rinaeegkcv lgisphalmm lqkfdwpgnv
      361 rqlenavfra vvlsdgdflq pedfphiqma lphfpvqsge ndapktsqga pigldlanmp
      421 akgdglaaal dhtssvaifd paghlrtleq ierdliecai dlyaghmtev arrlgigrst
      481 lyrklkeydl vehitqaag
//
LOCUS       WP_284360008             438 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Candidatus Phycosocius
            spiralis].
ACCESSION   WP_284360008
VERSION     WP_284360008.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..438
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47716
     Region          40..398
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mhlptspsrh vhaeasarst wyhasaprrf algetlnnti sadvvvvgag ytgmsaaldl
       61 aqaglkvvvl eadevgagas grngglacsg wrhdqiwlee rmgqadaral wtlaedakad
      121 lfsrmqtlni dadwmagqif aahtprlmqa ldydadhmar vygfeapqrl nqeevehalg
      181 skayfggwrd tsaghlhplk llyglsdaal aegatlyehs lvieigtqgl krfartsegk
      241 vlanhvllcg dgymdgidqr vetrvlpigs fivateplae dseilpnkes amdtrfvvny
      301 wrrtqdnrii fgggekytps wptdvgtfvr rnlikiypsl eriklthawg galgitptrl
      361 pflhqlapgl isasgysgqg vvlapffgri laacvlgqsg yqdvlsrvpv pqfpggrllr
      421 wpllaaamsw yalrdklp
//
LOCUS       WP_284360106             869 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit
            [Pseudomonas].
ACCESSION   WP_284360106
VERSION     WP_284360106.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 869)
  AUTHORS   Sandhu,P. and Akhter,Y.
  TITLE     Evolution of structural fitness and multifunctional aspects of
            mycobacterial RND family transporters
  JOURNAL   Arch Microbiol 200 (1), 19-31 (2018)
   PUBMED   28951954
REFERENCE   2  (residues 1 to 869)
  AUTHORS   Hand,N.J., Klein,R., Laskewitz,A. and Pohlschroder,M.
  TITLE     Archaeal and bacterial SecD and SecF homologs exhibit striking
            structural and functional conservation
  JOURNAL   J Bacteriol 188 (4), 1251-1259 (2006)
   PUBMED   16452406
REFERENCE   3  (residues 1 to 869)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
REFERENCE   4  (residues 1 to 869)
  AUTHORS   Arkowitz,R.A. and Wickner,W.
  TITLE     SecD and SecF are required for the proton electrochemical gradient
            stimulation of preprotein translocation
  JOURNAL   EMBO J 13 (4), 954-963 (1994)
   PUBMED   8112309
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..869
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..869
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=96135
     Region          1..838
                     /region_name="MMPL"
                     /note="Predicted exporter protein, RND superfamily
                     [General function prediction only]; COG1033"
                     /db_xref="CDD:440656"
ORIGIN      
        1 merylnfver yaraivfvlv aitayftytl galmsdtnpy llkdthpark tiidlqreft
       61 gtydsvmval nnpesvfntt slnaqfelsq airqlmland edrvelqriv glhsgdpdaq
      121 gllvqilaeg fsqndyaaak alrdhgiarh wdshdlqfls flaerlnpiq emasmadlen
      181 islsadgelw ihktlhaldm dpikveaqim gneqmvggvv sadkkvamvv aelgtkqdda
      241 qaqlrayhqv reiiakyqaa hpeftdevfi agmpifiaaq qeiidhdlam lfpivfllvt
      301 sllvfffrkp lgvvlplfni lfctiwtlgl mallrvpmdl ltsvlpvflf ticcadaihv
      361 maeyyeqlns gksfreanre tqrlmvtpvv lttvttiatf listtnnivs irnfgvfmsi
      421 gltaaliisl llipawisiw gkdavprkvq lkaslishyl vvfcawlirw rkpvllvilp
      481 llammtvftf kvdiedsgia yfkkdspvrt sdafinragv agtspgwiaf dtktprgalt
      541 tetvqflerl dqfikaqpnv sytysvatyi krmnlvlndm npaflrvpqa veqvtvvddd
      601 gkpetfdvdg nslieqhimm fengggtdlq nvlnadyska vtlftmtssv agdyqamldk
      661 ldawlainkp anlqvthagt pyiwtgvlqe itqgqvlsfs lallavtlmm mfwlksvrlg
      721 ilgmltlltt svtvygsmyl ldielnigtt lvtflvvgvv dyavhllsri kmlvqkgiei
      781 deailaamqg vgrstvvnvv ifsmgfvall fsaykpvidl gvlvilalss sgfmtillvt
      841 lispwffasi vpqpavqege qprggavpg
//
LOCUS       WP_284360121             198 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Candidatus Phycosocius spiralis].
ACCESSION   WP_284360121
VERSION     WP_284360121.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..198
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22035
     Region          93..179
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mnqnqiftma aadvwtatqs dgpalamfcq lnpeydlflt gempkvalwv eefltsqppa
       61 lfhwtqthkl iarthqhpdt iaavldvted miapgvghis lfqvatalqg sgfahvlyqa
      121 ledwlasrgm dvlrlgvleg nprgmafwtr qgylktrerv gtapsgkthq syvmykplkp
      181 ltldayrqrv prddpksp
//
LOCUS       WP_284360135             242 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: DUF899 domain-containing protein [Pseudomonas].
ACCESSION   WP_284360135
VERSION     WP_284360135.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..242
                     /product="DUF899 domain-containing protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=27449
     Region          6..233
                     /region_name="COG4312"
                     /note="Predicted dithiol-disulfide oxidoreductase, DUF899
                     family [General function prediction only]"
                     /db_xref="CDD:443453"
ORIGIN      
        1 mstsesrhpv vsrsqwlaar qqlwlhekaf thhrdaltaa rralpwvkve hdyqfqgpeg
       61 glsladlfag rsqlllyhfm fvegwsegcp gcsfladhfd ganlhlahhd vslvavsrap
      121 yaefqafrrr mgwqfpwyss hgsgfnedfg vsvgsagerq ynyepyegse selpglsafy
      181 readgsvyht ystyargldi lvntynfldi aplgrnesgt mdwvrhhdry egqsdqphcc
      241 hn
//
LOCUS       WP_284360464             266 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Candidatus Phycosocius
            spiralis].
ACCESSION   WP_284360464
VERSION     WP_284360464.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..266
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=29495
     Region          20..263
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 magvdvleaa laqvheasla fsvdldgyeg plhvllrlar dqkvdlrrls ilklaeqyle
       61 fvatarssri dlaadylvma awlaylksrl llpkkerpqg eepvediaah lawrlarlda
      121 mrasadalyq rpqqgldfft rgapeetavt eiplweatil dllhayamqr vrgfetkhev
      181 kawpvyside arkrleelip rakdwqalgt fapsatafak npptaasrya sllaaslelt
      241 kqgrlsvrql dhdaplyvka gaevgl
//
LOCUS       WP_284360396             326 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Candidatus Phycosocius
            spiralis].
ACCESSION   WP_284360396
VERSION     WP_284360396.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..326
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=34505
     Region          9..313
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 msipqilsrl ripvigaplf iisnpdlvia qckagvvgsf palnarpapv ldewldkitt
       61 elaewdaknp drpaapfavn qivhktndrl mhdveacvkf kvpvvitslg aredvnqaiq
      121 syggitlhdi innrfakkav ekgatgliav sagagghagt lspfalvqei rewfdgplci
      181 sgsianggav laaqamgadf ayigsafiat leanadqayk qmivdssaed iiysnlftgv
      241 hgnylvpsvv aagldpsnlp esdpsvmnfg sggtqakkaw rdiwgcgqgi gvikeistag
      301 qlverlaqey eaahqriqan wvhaaw
//
LOCUS       WP_284360568             360 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [Pseudomonas].
ACCESSION   WP_284360568
VERSION     WP_284360568.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..360
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39672
     Region          34..357
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mlkglllvlc lalataeaeg wpdpawqndp atfdwqavda yafpprtapd rsgirtdall
       61 iirdgrilhe rytapttaat ahltwsvsks vlatlmgvaq gegrfqledp vtrfypamrg
      121 hpgirmadll hwasgldwqe dyeyaplkss vvamlytrgr edmaayttar gasaspgqry
      181 lyssgdsnll aaalrgmlda gqypdypwha lftplgidsa vwerdragty vgssylylsa
      241 rdlarigllm qrdgrwqgrq llpkawvafn rtafdhaepv pgeatpgghw wlnqplagaa
      301 rpwpsapddt yaalghwgqa lyvlpaqklv vvryaddrdg syqhdellkr vlaamaregt
//
LOCUS       WP_284360572             385 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: phospholipase D-like domain-containing protein
            [Pseudomonas].
ACCESSION   WP_284360572
VERSION     WP_284360572.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..385
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=44523
     Region          6..376
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mpgpvfpwrd gnqfellidg peffprmlea ivgaefqvdl elylveagac aeavvevleq
       61 aarrgvrvrc lfddygslaf nsalrqrlle agvylrlynr lrwkrglrnl yrdhrklllv
      121 derwavvggt gvtdefwkpg datsewhevm vqiqgpvvtd wqllfdrqws annrrtawrp
      181 aegfglprlp klpahgqgmg rvayadarqh qdilhslvra lnsgkqrvwl atpyflptws
      241 vrrslrraas kgldvrlllt gprtdhpsvr yaghryyprl lragvrifey qpcflhlkma
      301 vvddwvsvgs cnfdhwnlrf nleanieald ppltaavvas ferdfalsqe vdldhwharp
      361 lwrrvkqriw gwidrlvvnv ldrrd
//
LOCUS       WP_284360686             230 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Candidatus Phycosocius spiralis].
ACCESSION   WP_284360686
VERSION     WP_284360686.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 230)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 230)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007442
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..230
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23201
     Region          78..175
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
ORIGIN      
        1 msnnnlwfnm vagavlatgl gimglrtvgd mvyandqtav gypvevadaa aagpaaesgp
       61 ellpdwgtvl adptqtaalv eqgdklhkvc aschnvepgs anktgpslyg ifgrtagtha
      121 gfaysdamka ygkawdfdgl ynflkapkty ikgtamsyag mskssdrval vaylhslaps
      181 paplpapdpt rdpaqvaaaa aaapateaap daaaaptdaa qapevapapk
//
LOCUS       WP_284360698             205 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Candidatus Phycosocius spiralis].
ACCESSION   WP_284360698
VERSION     WP_284360698.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..205
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=21816
     Region          8..203
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mrsqlhsgfg yyagfldraa qeailatlep llasapfyrp smpktgkpls vqmtnlgslg
       61 wvsdqagyry qathpvtglp wpaipqalld iwaavsgyap lpqaclvnly qqgakmglhr
      121 deneedrdap vvsislgdsa ifrlggpers gpttslklts gdvvvlggss rhfyhgidrv
      181 lagssslvqg ggrinltmrv vrrpg
//
LOCUS       WP_284360718             301 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: class II glutamine amidotransferase [Pseudomonas].
ACCESSION   WP_284360718
VERSION     WP_284360718.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Zalkin,H. and Smith,J.L.
  TITLE     Enzymes utilizing glutamine as an amide donor
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 72, 87-144 (1998)
   PUBMED   9559052
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Zalkin,H.
  TITLE     The amidotransferases
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 66, 203-309 (1993)
   PUBMED   8430515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..301
                     /product="class II glutamine amidotransferase"
                     /EC_number="2.4.2.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006541 - glutamine metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32261
     Region          2..296
                     /region_name="GlxB"
                     /note="Glutamine amidotransferases class-II
                     (Gn-AT)_GlxB-type. GlxB is a glutamine
                     amidotransferase-like protein of unknown function found in
                     bacteria and archaea. GlxB has a structural fold similar
                     to that of other class II glutamine amidotransferases...;
                     cd01907"
                     /db_xref="CDD:238888"
     Site            order(2,150..151,176..177,201)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238888"
ORIGIN      
        1 mcgivglylk kpeleaqlgk lfepmleamt drgpdsagfa iygdevadgw vkltlqaadi
       61 nypwttlmgq leghlgcsld wfqnasaavl kvhtdeaaar aalaalapdv rimsagqsie
      121 ilkgmglpae issryglagm kgshiightr matesavtme gshpfstgad lclvhngsls
      181 nhfrlrqelk regisfetdn dtevaagylt wrlqqgdsla qaldgaledl dgfftfaigt
      241 rngfavirdp iackpavlae tedyvamase yqalaglpgi ehakvwepap atlyvweres
      301 a
//
LOCUS       WP_284360733             420 aa            linear   BCT 25-DEC-2024
DEFINITION  cytochrome b [Maritalea porphyrae].
ACCESSION   WP_284360733
VERSION     WP_284360733.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Tolkatchev,D., Yu,L. and Yu,C.A.
  TITLE     Potential induced redox reactions in mitochondrial and bacterial
            cytochrome b-c1 complexes
  JOURNAL   J Biol Chem 271 (21), 12356-12363 (1996)
   PUBMED   8647838
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Howell,N.
  TITLE     Evolutionary conservation of protein regions in the protonmotive
            cytochrome b and their possible roles in redox catalysis
  JOURNAL   J Mol Evol 29 (2), 157-169 (1989)
   PUBMED   2509716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..420
                     /product="cytochrome b"
                     /GO_function="GO:0008121 - ubiquinol-cytochrome-c
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=47657
     Region          5..403
                     /region_name="QcrB/PetB"
                     /note="Cytochrome b subunit of the bc complex [Energy
                     production and conversion]; COG1290"
                     /db_xref="CDD:440901"
ORIGIN      
        1 mahqsnykpn sgfekwmder lpiirlgyds fvdfpspknl nywwtfgail aiflviqivt
       61 givlamsytp hvdlafnsve hirrdvnwgr yiqaahanga sffffavyvh ifrglyygsy
      121 kaprevlwil gvtifllmma tafmgyvlpw gqmsfwaatv itnffsaipv vgdtiktllv
      181 ggfavdnptl nrffslhyll pfmiagvvgl hiwalhvpgn nnptgvevks kadtvpfhpy
      241 ltmkdlfavm vimipfawfv ffapdilghp dnyipanplv tpphivpewy flpfyailra
      301 idfnvgpids klggvimmfg sivvwffvpw ldrskvrsga frpmfkwfyw vwvisfiglt
      361 ylgaqpaegv ylffaklcta yyflyflvil pflprvevtk plpasisesv lsksasqaae
//
LOCUS       WP_284360867             385 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Maritalea porphyrae].
ACCESSION   WP_284360867
VERSION     WP_284360867.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..385
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=41156
     Region          10..385
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mvdkqkrgnq hittrivqan gvidpqtggv vppiqssttf arnadysqis pdhlyarddn
       61 dlvrlgedvl tkaegadagl lfpsgmaaia avmrtvpngg tiiiqsqiyw gttkwvrdfc
      121 arrkialhei ecsetaaiea aidahkpnlv fvetpsnpwl ritdieavak acggvdatlv
      181 vdstaaspvl snplafgadi vmhsatksin ghsdvlagfl atadaqseiw qaiamdrhda
      241 gavigsfeaw llirgmrtlp lrmermsena mkiaefldgh aqveavlypg lkthpahala
      301 tkqmpngfgs llsfqvkgda ktalevcskl etfkratslg gveslvehrh siegdatgvp
      361 enlirlsvgi ehiddligdl nqals
//
LOCUS       WP_284360878             276 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Pseudomonas
            putida].
ACCESSION   WP_284360878
VERSION     WP_284360878.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..276
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28478
     Region          4..218
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtglgvahlt alqlaparlv rearhagfsa vglrlhpvma galaypvaag sqamrelrav
       61 lagegvrvtd iefvsltaqt rvadyqplla agaelgavsl tvsgddedva rltgnfaalc
      121 emarghglrv dlefmrwrpv atlqqacavv tgagqansgv lvdalhlfrs ggqvadigav
      181 dphllravql cdapmlapae aliipeareg rllpgegqlp latllaalpg dveisvevpc
      241 aglpaeqrlq aaaqvthgwl hgrrpvspav qvaghc
//
LOCUS       WP_284360914             386 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Candidatus
            Phycosocius spiralis].
ACCESSION   WP_284360914
VERSION     WP_284360914.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..386
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42524
     Region          1..382
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mkrlfalfms llsfvtalpv hgqssaeqel krleaervrr ehhygslved anrlasdaea
       61 lrkklvaaad yrdrlereve akesrliqlr hqekdlsari kasqsaledv viallamerd
      121 rpptlavqpk nvaesarvai lmgeiapilq srarqaasqi anlrtvresi lmqnisyrds
      181 ntrlmiarqt igglikerqi mqariladad tertriieiv rrsndlrelv lrlggsvpgl
      241 qatspaevnq edggfaramg siaypafgqi vvsygatles ggrsegitir tklgaqvsap
      301 ydgeiefvgp frsygrvmil nvgggyhlvl agmantyadv gqhvlagepi gemtsdtrlm
      361 pdlymevrqq stplnpnlwv krpdgt
//
LOCUS       WP_284360927             454 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase 5 family protein [Candidatus Phycosocius
            spiralis].
ACCESSION   WP_284360927
VERSION     WP_284360927.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Sharma,K., Dhillon,A. and Goyal,A.
  TITLE     Insights into Structure and Reaction Mechanism of &#946;-Mannanases
  JOURNAL   Curr Protein Pept Sci 19 (1), 34-47 (2018)
   PUBMED   27739373
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Ketudat Cairns,J.R. and Esen,A.
  TITLE     beta-Glucosidases
  JOURNAL   Cell Mol Life Sci 67 (20), 3389-3405 (2010)
   PUBMED   20490603
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467628
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..454
                     /product="glycoside hydrolase 5 family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49988
     Region          46..448
                     /region_name="COG3934"
                     /note="Endo-1,4-beta-mannosidase [Carbohydrate transport
                     and metabolism]"
                     /db_xref="CDD:443135"
ORIGIN      
        1 minrrglslg lggfalggat sviaaeqskp gsaqnfitvd gqrfiregkp yyfvganlwy
       61 aayaacpdpk ignpgrleke ldtlaslgvn nvrilassel splknslnpa iqnpdgslne
      121 vllqgldhsl nllaqrkmva vlyltnfwew sggmgtyeaw tnggkfvemn dpahpwpafp
      181 dyvsqfylnk kalalyeayv rslvgrintv tgkayvddpt imawqlcnep rpggtkavid
      241 qrmpayiewi nrsarliktl dphhlvcvgh egpigctdnl aetfnvgyaq laqasadidy
      301 ttahiwpqnw swsnvkdlag tfpnvetrtk ayirdsvgia nrlgkplvie efgfprdags
      361 fdagtpttwr drfydligaa llesharkge iaglnfwawg gqaralhddk rmrpgetayl
      421 gdpphepqgw ysvfdndtst lakiktlsyq vskl
//
LOCUS       WP_284361054             352 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Maritalea
            porphyrae].
ACCESSION   WP_284361054
VERSION     WP_284361054.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..352
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39530
     Region          8..323
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mktikgpalf laqfagddap fnnwnditkw aadcgylgvq vpswdnrlid leraatsksy
       61 ceelqgvare ngveitelst hlqgqlvavh paydkgfdgf apaqvhnnpe arqiwavdqv
      121 kkaltasknl gisqhvsfsg alawpylypw pqrpaglvee afdelakrwl pilnhaedcg
      181 vdicyeihpg edlhdgitfe mflervnnhq rcnmlfdpsh fvlqcldyld hidiykdrik
      241 mfhvkdaefn pngrqgvysg yqswvdragr frslgdgqvd fgaifskmaa nnfdgwavve
      301 wecclkhped garegaqfvk dqiirvtera fddfadggtd raanramlgi te
//
LOCUS       WP_284361058             158 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Maritalea porphyrae].
ACCESSION   WP_284361058
VERSION     WP_284361058.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 158)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 158)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..158
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17628
     Region          <38..144
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mkkqyiaigl vavvaigava wgtigntqpe lpegalfpyy drqvvaegke iyqqncasch
       61 gdelqgepnw rtpkdsgkmp apphdetght whhkdevlfa itkfgiarls nnpnyqtdmp
      121 vyeeilsdde ivaalayiks rwpesiqkrh delnaikq
//
LOCUS       WP_284361062             301 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Maritalea porphyrae].
ACCESSION   WP_284361062
VERSION     WP_284361062.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..301
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32210
     Region          70..293
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mrkivvqlva gaaaiaavst iaivawpiga qvelqelegn agrgaylarm sgciachtdt
       61 enggaplagg lslptdfgtf yspnltmsak fgmgewtidq fakalrqgvs psgepyypaf
      121 pfpfyaklsd qdvadlwtaf ktvpaveias kdhemkfpfs fraglklwra afvdfekfqe
      181 dtsksaawnr gkyivegpah cgachtprnf agarqveqrl hganklpdgg kspaitkeel
      241 lekgwtvegl ayalktgiky dgdvfggsmv evvrdgtsfl spkdlsaiat yllgdqnaad
      301 k
//
LOCUS       WP_284361066             136 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Maritalea porphyrae].
ACCESSION   WP_284361066
VERSION     WP_284361066.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 136)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 136)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10440481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..136
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14734
     Region          48..130
                     /region_name="Cytochrom_C"
                     /note="Cytochrome c; pfam00034"
                     /db_xref="CDD:459641"
ORIGIN      
        1 manrtaiivv llvfglfgvv ildrtkpept gesmievvpi vvseeimegk qtfdencaac
       61 hgknaagrqg iapplihriy kpshhadiaf klaaqvgvrs hhwpfgdmpp vpsvneddmv
      121 svitylrklq vangie
//
LOCUS       WP_284361084             192 aa            linear   BCT 25-DEC-2024
DEFINITION  SoxW family protein [Maritalea porphyrae].
ACCESSION   WP_284361084
VERSION     WP_284361084.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Bagchi,A. and Ghosh,T.C.
  TITLE     Structural insight into the interactions of SoxV, SoxW and SoxS in
            the process of transport of reductants during sulfur oxidation by
            the novel global sulfur oxidation reaction cycle
  JOURNAL   Biophys Chem 119 (1), 7-13 (2006)
   PUBMED   16183190
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   6  (residues 1 to 192)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   7  (residues 1 to 192)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..192
                     /product="SoxW family protein"
                     /calculated_mol_wt=21576
     Region          39..170
                     /region_name="SoxW"
                     /note="SoxW family; SoxW is a bacterial periplasmic TRX,
                     containing a redox active CXXC motif, encoded by a genetic
                     locus (sox operon) involved in thiosulfate oxidation.
                     Sulfur bacteria oxidize sulfur compounds to provide
                     reducing equivalents for carbon dioxide...; cd02951"
                     /db_xref="CDD:239249"
     Site            order(63,66)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239249"
ORIGIN      
        1 mlriiltmaf alittvasag tigedglhkq dwfaltfrdi aedietaaad gkrlalvfeq
       61 rgciycakmh eellsdpeva dylqehfliv qynmfgdeev tdldgdvlte ktaarkwgyv
      121 ftptivflpa evpansisvs kaavatmpga fgkwtflnmf kwvfdrgyeg dehfqkyhar
      181 iieqlraegr lk
//
LOCUS       WP_284361144             312 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Maritalea porphyrae].
ACCESSION   WP_284361144
VERSION     WP_284361144.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..312
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=35599
     Region          4..293
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mqpktvrdaa svwilrceld elekstirsy kgqlkhhilp llgdkelkal trrtvrefld
       61 amlakstrsm takvltslrs llseavdrew idynfakdik lrknnrlafq pvfpskadlr
      121 allensvekd kpfwttaiyt gmrlselrgl rwdnvnfetg iisitqrade nfkigrpksr
      181 aserkipmap sviyqlerwk qmcpkghlnl vfpngkgnie ssanihsrkw qplmksacll
      241 nsegkprfni halrhgaasl fleqgwpikk vqsilghssi smtmdtyghl medvandvgl
      301 fvklerdllt ks
//
LOCUS       WP_284361146             534 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Candidatus Phycosocius spiralis].
ACCESSION   WP_284361146
VERSION     WP_284361146.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 534)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 534)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 534)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..534
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55763
     Region          25..529
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mitsdgldlq dtdasytgat lgyttlvrrq hsrvkgwvll afvmaipglp vlfalaaacq
       61 psasfshivd wlltdmvwtt vklavistcg acmigvvaaw lvtaydfwgr gllswtlalp
      121 lampayvaay awgdltgsrg fyvavlvyit tlypyvylaa rsafeaqsvc aleaarllga
      181 gpltrffkia lplarpaiga gaalmgleia adfgaadhlg lstlttgifk awfsfgdlaa
      241 aarlaallll gviilvcler anrsgrvggg asswrslvrv klkgvwhgfa slgciallsf
      301 alivpighli llaianglpe rsllqpiast aflcilgasa tlitaslsaf laqngkrvka
      361 cvhvaslagy atpgavtalg ilaaltfggh hfvaalsgpv aifgltyayv arfsaaglep
      421 isaglerctr smleaaatlg annwqrflrl eaplavpsvf aaaliiavei akelpattll
      481 rpfgidtlav rahayaader lgaaawpala ivglaliptv wfshrlsksr agqk
//
LOCUS       WP_284361224             138 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Maritalea porphyrae].
ACCESSION   WP_284361224
VERSION     WP_284361224.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..138
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15806
     Region          1..137
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 maafqydqpv mfrhcdpaki vfypryfemv ntvietwfer eanypfltmf ddantgvpta
       61 aietrfhaps rmgdmlnwtl qvtrlggtsv sfdidahckd qkrvsvvttl vhvdgqtgkp
      121 kswpqavrdn ihnfmert
//
LOCUS       WP_284361369             297 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Maritalea
            porphyrae].
ACCESSION   WP_284361369
VERSION     WP_284361369.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 297)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..297
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=32974
     Region          2..294
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrilftggsg kagkhavayl ldrghrvlnv drvpldmpgv dnriaditda gqvydvmfsy
       61 agfdelepgt gvpkfdavvh faavprlllt sdnecyrvnt igtynvidaa lkagvrkvif
      121 assettygvc fadgerkpey ipvdedhpvv pedsyamskv anevtarsfq rrsgadiygl
      181 rinnviephe yeenfpayla dasirrrnif ayidardlgq mverclqtdg lgfelfnvsn
      241 ddhsvapttq elidefyqgv pqkaqmgthe tfysnakakk llgfapqhsw rdyisae
//
LOCUS       WP_284361358             246 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Maritalea porphyrae].
ACCESSION   WP_284361358
VERSION     WP_284361358.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..246
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27691
     Region          23..97
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          <160..244
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mydpkgnskd ksvqavqfve aeppehlrgi vhrflalktn gslpedyrfh alpdacaylv
       61 fdqlsptiag atklraesee fnlgkefhfv nirfmpgvwq edreplrygl lnqpykgalp
      121 indtaqklvg cpfekqqstl isfvqtlved nivapnptte kifqnldeit svadmaeatn
      181 isarqlqril kkstgftphd flkilrlqqs lngadtwsya dqshfihsfr katgytpgkf
      241 akkfdv
//
LOCUS       WP_284361432             282 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Candidatus Phycosocius spiralis].
ACCESSION   WP_284361432
VERSION     WP_284361432.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..282
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32125
     Region          2..233
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mrfegsknyv atddlkiavn aaiklerpll ikgepgtgkt vlaievakal glpllewhik
       61 sttkavqgly eydavtrlrd sqlgdervkd vknyikkgkm weafehqgrc vllideidka
      121 diefpndllq eldrmefhvy etgetikain rpiviitsnn ekelpdaflr rcffhyikfp
      181 dedtmqaivd vhfpgikkrl iatalasfyd mrkvpglkkk pstselldwl kllvtddidl
      241 daikqkdpnk lipplhgall kneqdvalfe rlaflarrea rt
//
LOCUS       WP_284361461              67 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Candidatus Phycosocius
            spiralis].
ACCESSION   WP_284361461
VERSION     WP_284361461.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 67)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..67
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=7502
     Region          1..57
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mntdtlltve daaahlkisk htlnrwrvtg egppfikygp rlvrylvsal dawaldrlya
       61 ntsqygr
//
LOCUS       WP_284361465             394 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Maritalea porphyrae].
ACCESSION   WP_284361465
VERSION     WP_284361465.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..394
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=43440
     Region          16..377
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 manfakpiah ktlnnaekpq nrdqtldifr aaavlmvvlf hyttrlpsev fgavpyavvp
       61 fefgwigvyf ffiisgfcif ftlekaksig sflakrfsri ypaflaaavl lfaldqvfgl
      121 pllpefsyre tapsivdlvg nlvllggife wvngsfwsit vevqfyvmia imalvfkqge
      181 klarlfsyaa lalgtawllv elassdiatm gklatmlqkt liapfmpffa vgvvgvqlkr
      241 speafaglfw qlaalcfviv vvtsaegdat llsassvstg livvgligif caycvgwrlp
      301 hmpflsngla higllsfswy llhenlgfll lealnpalpy wlsviiamgm tyaaaamfsk
      361 lfewrfrkta eawfmaalrl ftarlpkkmg esli
//
LOCUS       WP_284361497             778 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Candidatus
            Phycosocius spiralis].
ACCESSION   WP_284361497
VERSION     WP_284361497.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 778)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 778)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 778)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..778
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84888
     Region          16..715
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mmhqsvfkah grllavllas talpsmalaq vntasdtpkp ttetvvvtae rnrapatnva
       61 qelaiygtdv qvisgatieq sgainfaeav qflvkgvnvg yspdegeyti rldgggdrdt
      121 lvtldgvply drgpvleniw gattidnhiv enievfrggn slyfgsnggi gvvnvvtkkp
      181 dgtvkgdfgv sygafntrel wgnysfpida egnhslmvyg sllatdgpri ydpnlftdnv
      241 alsggiqeyp lnknnigvky lwkinestef ranaiytesw fqdafpsges yspntlrypi
      301 idaslthkag dkllieasay ysnpllwnae lypvvcriaa gcpianqata agvgtrtvpr
      361 gawtgavepa fahgfgttnq fksgfveigg tvratykfne ylevvggvqy vsykddsdar
      421 favpnndtat tgvfvdvhpt lpfspktgis lavrtdfsda fdsktiwkfg ikhpfmdnfy
      481 vranggtsys lpqtnelfin nprpptavne tgfttignpd llpeetetfn taigythefg
      541 qsvlfmelgg fktevtnris ttsgrpiivt npitglqtpv dtffnnnfvn eiqgwtaevd
      601 lkigeqwafn vgytnqdsal ssgsrgglql netpewfata slnwtsedkr lkvqllpriq
      661 gdewstggpa iagttkaagp dgkgadtgvp ryrtnfgnyt vvnasityla genmqhrfmf
      721 rvvnlldedy aerwgfgnnf ygaafnrgey tntddryfyg ypfegkprsf yvtyatkf
//
LOCUS       WP_284361510             108 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Maritalea porphyrae].
ACCESSION   WP_284361510
VERSION     WP_284361510.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..108
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11803
     Region          25..100
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(29..30,32,35,38..39,42..43,46,76,95..96,98..100,
                     102..104)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(30..31,35..37,50..52,61..64,66..67,70..71,73..74,
                     80..82,87..89)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(50,53,95)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mslnsseint apsfstdlyy sageassllk aiahegrlmi lcrlsereas vseledllea
       61 rqaavsqqla rlrqeglvqt rrdgkaiyys ladervrdii savhgtfs
//
LOCUS       WP_284361569             192 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Candidatus Phycosocius spiralis].
ACCESSION   WP_284361569
VERSION     WP_284361569.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..192
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=21409
     Region          14..115
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
     Region          38..68
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          73..96
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mretcddqtm eeligllqan deraldklds lvrefstdpr lpfmkasllv stgnpiqahy
       61 wfnkalelap dfaiarfqfg lfqltsgepa qaletwgrld llpdghylra fvdglrclir
      121 ddfngarrhl tigmaanden gplnndmall mrqldslehs sqnlsspddt sdeevsqtsl
      181 llqqlgiygl pn
//
LOCUS       WP_284361609             116 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Maritalea porphyrae].
ACCESSION   WP_284361609
VERSION     WP_284361609.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 116)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 116)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 116)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..116
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12232
     Region          4..96
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 maqnetdfte aaqafaamgs eprlevlmcl vragdagllv gdiqdrtnip astlnhhlkf
       61 ltaagivtqe kqgrtiinra qfdalealas filkqccidv ptnvgqsssv sqnega
//
LOCUS       WP_284361627             350 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Maritalea
            porphyrae].
ACCESSION   WP_284361627
VERSION     WP_284361627.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..350
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=39071
     Region          20..316
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mplsvgnitm hlgpqniggp ddleaaiief ieaatkslyi svqeldhkpi adaivaaklr
       61 giqvhmvmeq dylkeshppa adslgelevn rellmrilrh gidakadynp sifhqkfivr
      121 dgeavltgst nftttgvrkn lnhivvvkdk lvareytref rsirkgifgk rsldrsrkpl
      181 edhyvgdvrv kplfapdhmp emefikhmnk ardridfaif tfskssgidd amvlsqlagv
      241 svrgvldrra anqkwaakdt lknggitlfq nktgtgvrkv hhklmtiddq ltivgsfnyt
      301 gpanltnden imvlgdldet dpakrdaqsq lalyarneiv riiehqseei
//
LOCUS       WP_284361686             656 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Candidatus
            Phycosocius spiralis].
ACCESSION   WP_284361686
VERSION     WP_284361686.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..656
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=70350
     Region          40..623
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mrrvsrlval wvlaatcvyg pgaqakivdy sstinpslks vaetetiivt atrtplpatk
       61 igasvtvltn qaivraqsas vvdllrdvpg vgfsrnggig gvtsvrlrga eadqtvvlid
      121 gvkvndpssp gggynfanll vgdidrievl rgpqstlygs qamggviqii trrgdvpfag
      181 sltlergdla syhalasvrg tvdaltyaan fghfetkgis aavagserdd fqsdqangrl
      241 syqltpslev egrtfwtksd agndgfpapl fvladtpera kteelvvyag anlnlldgrs
      301 rtrlglsqsq iereslnatl tpattfigkg tnqtlelqst ldvtpqfqlv gggeieeahl
      361 rtaipsrtnp npiplrastd lgalyiqaqa sptswlttsf garwthsdrf gdalnaratl
      421 vasfnegntl vragasngfk aptpfqlysn fgnpalgpee agslelgveq alfsrrlkgt
      481 itlfdrdttn qidfiscfrn pidmcanrpn gtydniartk aegleaslea mptdrlslsi
      541 gystlnarnk versanfnrr larrpeetsf ltigydfpfg ldvsatvsri gesfddaans
      601 rplkgyevvt lrvsqklgdh wsvigrvena gdeiyqttfg ygsprqqswi glrasf
//
LOCUS       WP_284361708             114 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsB family cell division protein [Candidatus Phycosocius
            spiralis].
ACCESSION   WP_284361708
VERSION     WP_284361708.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius spiralis
  ORGANISM  Candidatus Phycosocius spiralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Candidatus Phycosocius spiralis"
                     /db_xref="taxon:2815099"
     Protein         1..114
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=12780
     Region          9..99
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 maflkgiris tylfagvlvy favhffvgqq gvlswhgyvk radvlleerd vlinrrrele
       61 rrlaryqpgr vdsdyveera iaqlglagph dimirlskpa irsgatasvq tpnp
//
LOCUS       WP_284361752              68 aa            linear   BCT 25-DEC-2024
DEFINITION  tautomerase family protein [Maritalea porphyrae].
ACCESSION   WP_284361752
VERSION     WP_284361752.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..68
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=7481
     Region          2..54
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mpyvnikvtd egvtreqkak likgvtdllv dvlnkdpktt hividevple nwgfdaiptd
       61 vhrakqsa
//
LOCUS       WP_284361767             209 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Maritalea porphyrae].
ACCESSION   WP_284361767
VERSION     WP_284361767.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..209
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23526
     Region          20..143
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mpqqssfwnr qatrydkais dhdqryemrl tqitqllhrd anvldfgcas geialdiaar
       61 vnsiegidpa semiriatek ankrginnas flatdifdar lepesfdavl afnvlhlvhd
      121 hdevihriks llkpggmlfv etpclgeftw wkrqlilaas alrlapfihv ykfgepnael
      181 ehrsfkilga qnepdqdcra fiaaqkpae
//
LOCUS       WP_284361809             211 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Maritalea porphyrae].
ACCESSION   WP_284361809
VERSION     WP_284361809.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..211
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24204
     Region          4..90
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mrhgkiaryl vdqfsevlav dpskrmielg qslqngnakn lrwleglaet tplkgkfdli
       61 taalsvhwmd heklfvrlae hvspnhlfav iegddaynpp wrtseisfle kwvpavtgkq
      121 fveghrefmt ryqhhvhlie eieiisepft qsiddfiacq hsrdtfaisk lgqrleefdn
      181 elkeilqpha ddnsiltfkt kstltlsklk i
//
LOCUS       WP_284361828             320 aa            linear   BCT 25-DEC-2024
DEFINITION  FecR family protein [Pseudomonas putida].
ACCESSION   WP_284361828
VERSION     WP_284361828.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20752687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..320
                     /product="FecR family protein"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0016989 - sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35491
     Region          22..62
                     /region_name="DUF4880"
                     /note="Domain of unknown function (DUF4880); pfam16220"
                     /db_xref="CDD:435227"
     Region          67..320
                     /region_name="FecR"
                     /note="Periplasmic ferric-dicitrate binding protein FecR,
                     regulates iron transport [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG3712"
                     /db_xref="CDD:442926"
ORIGIN      
        1 mtdspaprps pagpsarara mdealdwlvr lqcadaadtq afeawlsaap enaeayveae
       61 alwngmplhq aatqmhqqqr rswrgrlrsh wkplataavl lvglftvgnl ptrlqadhlt
      121 vvgerqrlql edgakvllnt nsafasdrre grqvarllqg eayfqipega llpleveagp
      181 lraqvrdtdf avryldgeaq vrvqrgdvdl qgardqrirl sagdsisvgp qgfgqrqrad
      241 mqkdlawvdg rlvfencpls qvlaevrryy pgwiinrnaq ledvavtgny rldqpletlr
      301 alahitsaql heypplviln
//
LOCUS       WP_284361899             468 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudomonas putida].
ACCESSION   WP_284361899
VERSION     WP_284361899.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..468
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=52231
     Region          30..409
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mqplrtlslw mdqleeplca rpalredlav dvciigagyt glwtayylkr qapqlsiavi
       61 daniagfgas grnggwlmgn llgedrllat lspqqrrasi dllhgipdev qgvlqregid
      121 cdyrkggvly caarypeqer slraylddly rqgmteedyr wlrpeqlenq lrvsnafgai
      181 ysphtatiqp aklvrglara vealgvpiye ntpaidwqpg dvrtplarir cqwmvpaveg
      241 yaaslpplgk hqlpvqslli ateplpestw eqiglsqgqa fsessrqvty gqrtadnrlv
      301 fgarggyrfg grlrenfnlq eheielrryl fselfpqlkh vrithswggn lgmarrfhph
      361 mlcdrqrgia laggyggegv gatnlggrtl aalilnqhne ltaqpwvldn rpvsslaswp
      421 pepcrwlgyn aiiqsfvhed rtlanpasap wrrrlassla dfmegfmh
//
LOCUS       WP_284362032             115 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Maritalea
            porphyrae].
ACCESSION   WP_284362032
VERSION     WP_284362032.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..115
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12547
     Region          19..109
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mvdiprpgqp vrgsktgapi malfdllgrn wsmgivwvls eigpctfrel qahcesispa
       61 alnmrlkelq vacfvervad gyvltplgke lyedlvplga lakkwgeell sqpnk
//
LOCUS       WP_284362034             404 aa            linear   BCT 25-DEC-2024
DEFINITION  MDR family MFS transporter [Maritalea porphyrae].
ACCESSION   WP_284362034
VERSION     WP_284362034.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023665
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..404
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44399
     Region          12..390
                     /region_name="MFS_MdtH_MDR_like"
                     /note="Multidrug resistance protein MdtH and similar
                     multidrug resistance (MDR) transporters of the Major
                     Facilitator Superfamily; cd17329"
                     /db_xref="CDD:340887"
     Site            order(22..23,26..27,30,63,113..114,116..118,121,142,
                     145..146,149,223,226..227,230..232,235,264,268,319..320,
                     324,328,344,347..348,351,354)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mfaavrhfnk tiwliifatf asrfvlfmvw pflaillyqk fglnefqigm flagsaavgv
       61 ffgfyvgfls divgrrkiil iglvlnivam fvlgisdqlw wifagtvlqs fgrgmvespg
      121 ralmtdmved revkdmalhm ryfflnigaa tgpllgtfvg atgqqstfli vsalyvvyfl
      181 iaaivfrier plkrtkagta lrfvdalhvl rkdrafmlfv aatlishiay gqidaglvqy
      241 lrqenvvdla tlyatlifin gatiivfqfa flkllehvrp llramggvvl faagflgfaf
      301 aptdpgywlf gamfilslge tilfptlnii tdrmapdhlk gsyvgaasla smgfvsapiv
      361 ggfflhqfgg ftlwlsmaal alvvaslygl aarirpasrp lkid
//
LOCUS       WP_284362047             691 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Pseudomonas putida].
ACCESSION   WP_284362047
VERSION     WP_284362047.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 691)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 691)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 691)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 691)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..691
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=76547
     Region          56..691
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mlvpcrlspl tlglsllfsa elasaatttl pessvtadse rekdnprike vstatrtstp
       61 vryvpqaidt vktanvldyg nntlgkaleg ipnvssgadt rfdsvrirgf easndfyldg
      121 irddsqyird lhniervevl kgpaavlygr gsqggivnrv skapeqgrrs sieaqagsed
      181 lrslyadlsa dpsdtvslrl nmgnqdnnsf regidgsrql fatsvswqit pdlnwlvqye
      241 ysrynrtpdr gipgvngrpa dvsrgttygd qrdyiddraq slrsrlnyql netwqlrhtl
      301 glfkldsefd ntyvtgynas tnvltrqrwq qdlntrnlfn nleaegdfdt lglehklllg
      361 lefgnqkrdp vlytagsqpl pglgkpgsnq qhngtlalss nnhtvvdsrg lylqdqirln
      421 dqwqilagvr fdqfdvettn kdgvrepqds nstsprlgvv ytpwrdhsfy aswsktfspv
      481 gggligitpd apgngndakp eetrqkeigv ksdwldqrlt ttlaiyelel ynrrtrdpen
      541 pnnillsglq rsrgieltat gnivgnwyvr ggiglqdaii vkdnngqegn rindvakrna
      601 slfvtwkpel gwyaetgvtl vgeryadnqn ttvlpgygrw dalagyrthd wdvraalsni
      661 adktyyssat saaqiqvgdp rslvvtgsys f
//
LOCUS       WP_284362055             468 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Pseudomonas putida].
ACCESSION   WP_284362055
VERSION     WP_284362055.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..468
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=50934
     Region          9..450
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mttetlidsq aqvilvdddp hlrqalsqtl dlaglkvval adaqglaeri eadwpgvvvs
       61 dirmpgidgl qlleqlhgrd selpvllitg hgdvplavqa mragaydfle kpfatdalld
      121 svrralalrr lvldnrslrl alsdrqqlat rlvghspsml rlreqigala gtradvlilg
      181 etgagkevva ralhdlssrr dgpfvainag alaesvvese lfghepgaft gaqkrrigkf
      241 efanggtlfl deiesmsldv qvkllrmlqe rvverlggnq lipldiriia atkedlrqsa
      301 dqgrfradly yrlnvaplri pplrergddi lvlfqhfada asqrhglpph tlqpaqravl
      361 lrhpwpgnvr elqnaaerfa lglelaldgq appataaaap vlsgnlseqv eqfersliaa
      421 elaqphssmr slaealgipr ktlhdklrkh slsfdggsgg hddqedhr
//
LOCUS       WP_284362094             126 aa            linear   BCT 25-DEC-2024
DEFINITION  VOC family protein [Maritalea porphyrae].
ACCESSION   WP_284362094
VERSION     WP_284362094.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..126
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14205
     Region          3..122
                     /region_name="PhnB"
                     /note="Zn-dependent glyoxalase, PhnB family [Energy
                     production and conversion]; COG2764"
                     /db_xref="CDD:442048"
ORIGIN      
        1 mnrlfpnlmv qdmeqtltfy qnlgfsvlsk mpeespvwal veldgikimf qskpsltaef
       61 pqladqqsgg altlwintpn vkkyferasi qckllkplgv tdyngatefv lrdpdgfilh
      121 fsdlem
//
LOCUS       WP_284362159             530 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Maritalea porphyrae].
ACCESSION   WP_284362159
VERSION     WP_284362159.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..530
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=58315
     Region          <78..506
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 msklaaffrg dpsispiclt lfqtagatvl asflavlafk tvgvhyagvw yqlgvtlvva
       61 sfvapiflyp tyrtsanlqk anaiiaeqat tdhltglpnm lalsselaql laqgdrhqpf
      121 avhfldidrf kqvndslghd vgneliaatg qriqewvgda gfvarfggde fvviqyhtsn
      181 emaatqfgre lrvhlakryn lsdhevnvtt sigtalsplh gegqdqllka adlalykake
      241 tghsscvfep rfaseasnrr riegilrdti ahgtlkpryh sivhaqnplq iagfealcri
      301 elpdgevlnp eqfipvaest glildigaym lqqacfecan whpdlfvsvn vspvqlirsd
      361 flttvqealn dsglppyrle leitesvlin dvehirttle rvralgvqia lddfgagycg
      421 lhylrqieid kikidksiid daetveisrn ilngvsliak qmditlvaeg vddiskaefl
      481 cqgervhqfq gylfskpvsa adarrmqkil pqqstpdnvi qlpvrkkdsv
//
LOCUS       WP_284362221             195 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Maritalea porphyrae].
ACCESSION   WP_284362221
VERSION     WP_284362221.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 195)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..195
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21366
     Region          19..108
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 msnapfqdvt qkfvlsepaq lralgaptsr lvfqgllqlg qgsikevaal igktphalyh
       61 hmdklvavgl vlengerrsg arieklyrpv ahlletdpsn rdrdyleava dnaaagyrqa
      121 erelrralls geahigtdkk nalalqfsvp lnaqqrqdlv hriealvedf tsgldmdeng
      181 qhylvtlgls pepnk
//
LOCUS       WP_284362252             227 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Maritalea porphyrae].
ACCESSION   WP_284362252
VERSION     WP_284362252.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..227
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23522
     Region          75..223
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 msqdphneae kkapnkwnmg vivgvvvaia tavwvsnggg gqngsagtgg ftpspaiata
       61 ldeaaagela afratakgeg ypeikfvadt gesvgfdhfn gkvtlvnfwa twcgpcraem
      121 paldalhaky qdqgfqvati nldvgedgld kakafmeevg lknlplhadp tfeafevlkt
      181 rgtalglpat lligpdghew gvlagpaewn sedahaliea alalvns
//
LOCUS       WP_284362291             289 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Maritalea porphyrae].
ACCESSION   WP_284362291
VERSION     WP_284362291.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 289)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..289
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31259
     Region          1..276
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
ORIGIN      
        1 mfpelfntrp lriwiddgln wvvkhwgdaf eaaaypllvm lntierfllm mpwwliiall
       61 aglaygatrk vtlpivvvig lvfmglmelw edsvktmalm isatvtaivf sipmgivmar
      121 sslvrkivtp ildlmqtmps fvyliptvmi fgpgkipall ativyaappl vrltdlgirq
      181 vepnvleaaq afgasprqrl fgvqiplalp tilaginqtt mmalamvvia smigagglgy
      241 qvlqgigrle vsrgvfaglg ivvlaiifdr itqaygkqlq aqiglsgar
//
LOCUS       WP_284362394             477 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Maritalea porphyrae].
ACCESSION   WP_284362394
VERSION     WP_284362394.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..477
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=53758
     Region          2..469
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mskktivwfr qdlrvadnpa lneaaergdv lpilivdetd qdmalrgtar avwlhhslla
       61 ldkklgghlq vfagdpeqil lavaaengad avfwnrcytp hriiadkqik qflserdlaa
      121 rsfngsllwe pwqvlkkdkt pykvftpfyk kgclsaqapr atvaapsdis fvgeasdqsm
      181 idglellprh dwaakmmadw qpgeqgarea waqfadnglm gykngrnfpa kanvsrlsph
      241 lafgeisphq iwaalehqpq nedvahfrse lawrefsayl lyhfptlpfe nfnskfdqmp
      301 wqidqtalek wqrgqtgipi vdagmrelwq tgymhnrvrm ivasfltknl gvdwregakw
      361 fehclvdady annraswqwv agsgadaapy frvfnpvlqa ekfdplgayi rtfvpeiael
      421 pnkflgkpfe apaqvladag lelgiayphp ivdlkqsrnr alaayqtmrg qdmvepa
//
LOCUS       WP_284362560             361 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Maritalea porphyrae].
ACCESSION   WP_284362560
VERSION     WP_284362560.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..361
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40241
     Region          40..297
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 midrhqmekc vyvlpnfapp niaetlksia esdhaflpad iygqggacee vatrlkkmfd
       61 kpaarfcvkg miaqmavlra vteftgnnrv vvhrashldy demeaveilh piqflragnh
      121 hhpftvddld algekpaavc velplrrasy rlmpfaelqk istwchvhdv hlhidgarif
      181 gaaaaygkkf seiamlcdsi yvsfykelkg lggcgivgsk almdavevwv trmggelpfq
      241 fpyaisalmg mdkhlgeiph yvaaartiam linqipdvtt spevphtsgf qvhikgdrkk
      301 iekalkhmie yeriwiaggv metafdhvyg fdveigesam alaperwafy iekltqlmre
      361 d
//
LOCUS       WP_284362603             881 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Maritalea porphyrae].
ACCESSION   WP_284362603
VERSION     WP_284362603.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..881
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..881
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=95353
     Region          27..183
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <381..878
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 msvhtssale khqdaqtaia vkiplrligi lclvsvafii falmswsvnd pslsyassea
       61 vnnwlgypga vvadimlqff glggilyiip paiwslslvr kkvplgfglr vlmwacalfl
      121 tcgvlafips ptswplptgl ggiiglgfsa vasfvvgpev lqaagwlfav ilatpalvsf
      181 wmavragarf gletqdanav attdqksdep ktliqwigak ltamftillg aithvifsth
      241 vsikkswaar kaekqqaeeq pwrqgehepa lhnphpaqaq qhqrrieprf egpnapspdq
      301 anwaegptdq ypddyvdvdp aeyaqpyaap ehenpaptqp aapsaasakp sprvaapapr
      361 papgrrmvae aqqsflgndt felpelsyma eppttktare hlpevleena rllegvledf
      421 gvrgdiinvr pgpvvtlyel epapgikssr vigladdiar smsaisarva vvpgrnaigi
      481 elpnktretv ylremlgsad fekvkgklpl clgktiggep viadlarmph lliagttgsg
      541 ksvavntfil sllyrwtpeq crlimidpkm lelsiydgip hlltpvvtdp akavtalkwa
      601 vremedrykk mskigvrnid gfnqkvaesk kkgeiitrtv qtgfdketge aifeseefdl
      661 eplpfivviv demadlmmva gkdiegaiqr laqmaraagi hlimatqrps vdvitgtika
      721 nfptrisfqv tskidsrtil geqgaeqllg mgdmlymagg grtkrlhgpf vadaevetvv
      781 nhlkaqgspe ylesvteese edagvgnsnl gnsgdelydk avnivlsdrk astsyiqrrl
      841 sigynraatl iermeqegvi spanhagkre vlvggdeeap f
//
LOCUS       WP_284362604             186 aa            linear   BCT 25-DEC-2024
DEFINITION  LolA family protein [Maritalea porphyrae].
ACCESSION   WP_284362604
VERSION     WP_284362604.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Tajima,T., Yokota,N., Matsuyama,S. and Tokuda,H.
  TITLE     Genetic analyses of the in vivo function of LolA, a periplasmic
            chaperone involved in the outer membrane localization of
            Escherichia coli lipoproteins
  JOURNAL   FEBS Lett 439 (1-2), 51-54 (1998)
   PUBMED   9849875
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..186
                     /product="LolA family protein"
                     /calculated_mol_wt=21003
     Region          18..180
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 matasssler plteeeiqii tdisqhhsgv eqmagrflql dsggnrsegi fylkrpnkir
       61 fkyappsyee visvgkgfyv inrkeqskfa ypqsrvplrq flsdeidlfs anitdvikte
      121 emiavgvsde tpagpvsvtm ifnletkeie qwtltepngn evtfsiydtt teidipkayf
      181 ylpdyk
//
LOCUS       WP_284362670             714 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Maritalea porphyrae].
ACCESSION   WP_284362670
VERSION     WP_284362670.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 714)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 714)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 714)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..714
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=78375
     Region          <195..704
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mqkthkrnwi islglfaigv atigasvysa qkvmddllrk davsngmswa qhvadttdgl
       61 navvsgyapa sdvegvlgrl aavgdiyqfa fisphgelif ktgsyhppae ageaahhahs
      121 hdpapqlgad vehvqhdnht thaasasntp tshdhgahah dhaapqepqa hgehdhaaay
      181 pgsstqphlq hstklmigdg etdpihfaev nhpvtvngei qyvirlrldq terfeiyqaa
      241 vstlsiilas ivllavgipa llalrsrkqa eladqqvhfl arhdpltgll nrssfldqle
      301 haaqtrrgin eqiglfiidl dgfkgindgf ghdvgdellr qladslkfqg edldaiarlg
      361 gdefaafvsf dpdevdlhdl anhtlasltg iyevnghdvv ttasigvalc pddaelpael
      421 mqkadialyn vktngrngya ffergmekrm kkrrnmeall rqarhdqafe lhfqplfdqk
      481 sraliafetl vrmrdekgef vppdvfipva edmgmmeelg efilreatkt amnwpdqvgl
      541 avnlspkqfe sgkllsivss alvrsglkpe rleleitesl lmsnsqrnlr qlellkeigv
      601 siamddfgtg ysslgylwkf pfdkikidks flggmenvde kanqivstii alghtlemcv
      661 taegveteaq aeflnahkcd qlqgfllgrp mpkeeidrfi legknkkael qivs
//
LOCUS       WP_284362711             252 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Maritalea porphyrae].
ACCESSION   WP_284362711
VERSION     WP_284362711.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..252
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27908
     Region          45..162
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mnnqnelsri nrvawetsaf eawvkkygep eaaasqiasn pehtarrilp hlqnpkdlli
       61 anplgshgrl atalsllgak akvfdisssn akygtalaka agasveyvvg dfvercedyh
      121 ncfdatvmel gilhyfhslp efvsalvqit kpngiiilvd fhpftkkllr fgedrievgg
      181 dyfstvaera ptpyeevlgy klppclvrrw klsdilsafl vpelgivsfs eepaweseki
      241 pgiftlvvkr hk
//
LOCUS       WP_284362725             268 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Maritalea
            porphyrae].
ACCESSION   WP_284362725
VERSION     WP_284362725.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..268
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29790
     Region          26..261
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 miwrivfffl itlpvllvla liqwlvlafk fknwnfvpil ahklvcfnlg vkvrqigkpa
       61 sdkptllvsn hiswmdipai gsivpisfva kaevgrwpiv gflarlqkti fvdrqkktdt
      121 grvanemger msdgravvlf aegtsdvglh vlpfrsalvg gtqramendh ieemyiqpmv
      181 iaythlnglp isaaerskia wigdmgiedn ildilsvgak tttimfgepi tikrgddrkl
      241 atkqaeekvr emlvannrqm plppahkg
//
LOCUS       WP_284362873             439 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Pseudomonas].
ACCESSION   WP_284362873
VERSION     WP_284362873.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..439
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47984
     Region          34..401
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 myrntstpad dngcgwfhls pprqpraahq grsearwvvl gagftglaaa rqlalhhpdd
       61 evilvdaqev gfgasgrnsg faidlphdig aadyigdlpt armnlklnlr aqailrelin
      121 qhgidcqirp dgkyqaaved kglavleayr sgleklgqpy qmidardlpe hfgttfyrka
      181 lytpgtqllq paalakglad slpgnvtlhe rttithieqg rrinlkhang eivadqlllt
      241 nnafasyfgf lpgrllpift yasmtrplte deqarlggkn twgiipadpf gstlrrtpdq
      301 rllvrnsfsf nadgranprh iaragrqhrd sferrfpmls gmafeytwgg smclsrnhls
      361 hfgtlapnvh aalccnglgi trgtatgtll adwlsgehde lidfllgsag pnrnppepll
      421 tagvnlnlhw gqrragles
//
LOCUS       WP_284362911             355 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: aromatic ring-hydroxylating oxygenase subunit alpha
            [Pseudomonas].
ACCESSION   WP_284362911
VERSION     WP_284362911.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..355
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39423
     Region          4..345
                     /region_name="PobA"
                     /note="Chlorophyllide a oxygenase/letal leaf spot protein
                     [Coenzyme transport and metabolism]; COG5749"
                     /db_xref="CDD:444459"
ORIGIN      
        1 mypkntwyva ctpdeiaakp lgrqicgeki vfyraqenkv aavedfcphr gaplslgyve
       61 dgnlvcgyhg lvmgcdgktv smpgqrvrgf pcnktfaave rygfiwvwpg dqaqadpali
      121 phlewavnde wayggglfhi gcdyrlmidn lmdlthetyv hassigqkei deappvttvt
      181 gdevvtsrhm enimappfwr malrgnglad dvpvdrwqic rftppshvli evgvahagkg
      241 gyhaeaqhka ssivvdfitp etdtsiwyfw gmarnfaahd qtltdnireg qgkifsedle
      301 mlerqqqnll aypernllkl nidaggvqsr kvleriiake rapqpqliat satpa
//
LOCUS       WP_284362921             261 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudomonas putida].
ACCESSION   WP_284362921
VERSION     WP_284362921.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..261
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29805
     Region          26..245
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mthrarrawg malallsvpa gaaqtvrycd ypvyppmsws dghqvrglap tvvrelfarm
       61 gydvqtvvlg nwkrclmdaa agrvdvvlay nsdqrdqrmh fstepveree vavfynrkrp
      121 vqfqqledla gyrggllyge sygaefdrfv arhqniervs ssqqnfgkli rgridyviqe
      181 rrtgqlfieh lpgaqdirvl psalsvdylr vavsrqspls qhmdeidaql rrmnqageit
      241 rwleqsevty rdminlpada r
//
LOCUS       WP_284363242             499 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: purine-cytosine permease family protein
            [Pseudomonas].
ACCESSION   WP_284363242
VERSION     WP_284363242.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..499
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52388
     Region          4..464
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mshstgietn gveqipddqr daspldlfrl ifggantfat avlgsfpvlf glsfqagvwa
       61 illgvgvgal ilapmglfga lngtnnavss gahfgvhgri vgsflsllta vaffslsvws
      121 sgdalvggak rlaglpetdl tlgltyglfa vlvlvvcifg frfmlwvnki avwassllfl
      181 lgivafagpf dasyagsvnh gqagfwaafv gaailamsnp vsfgaflgdw sryipraipk
      241 trimlaviaa qgatlipflf glctatlvat qapdyiaann yvggllavap swfflpvcli
      301 aviggmstgt talygtgldm ssvfprllsr agatlligvl aigfifigrf tfnlvqsvst
      361 favliitcts pwmvimilgl itrrgfyhad dlqvftrgqr gghywflhgw nwrgmgawlp
      421 saavglcfvn lpgqfvgplg dlgggidlsl pvtlglagvm yllllnlfpe pagvygprgp
      481 rwvrckstah tpvttaema
//
LOCUS       WP_284363302             217 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Pseudomonas putida].
ACCESSION   WP_284363302
VERSION     WP_284363302.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..217
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24444
     Region          1..216
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 malaifdlde tlihgdcasl wseqmarlgw vdgkdflrrd relmeaygkg hlqmedymaf
       61 slepiagrtl eevehlvepw vedviepiif gdacrciaeh rqrgdrilii sasgthlvgp
      121 iaarlgvdey laieleavng vytgkthgvl tyregkitrl lewldqeqen legasfysds
      181 rndlplllkv dhphvvnpda vlrehaqtng wpilswt
//
LOCUS       WP_284363354             447 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Maritalea porphyrae].
ACCESSION   WP_284363354
VERSION     WP_284363354.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..447
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=48749
     Region          21..440
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 msanlqtvvl vdddldllee iaenlelagn nvetysdpvv aknsiekdln ivvisdvrmp
       61 kmdghallda vreidpdipf imitghgqva qataamkaga ydflekpidp nqlaavvgra
      121 lekrslhlqn kklkallnsd qleaqiigns epakqlrqqv atlaslevdl iikgetgsgk
      181 dlvarclhen sarkphpfva vncgalpanl vdsaffgher gaftgadtsh igyfeaadgg
      241 tlfldelesm pmpfqaillr vletrevtrl ggakskklnf rvvaavkgel salvaaqrlr
      301 adlmyrlnva sielaplkqr kpdiellfcr faeaaaafhn rpmptisdql rrkllayewp
      361 gnirelknta erfviglpla fanngdgnti satgleeaid afekqkieea lkqtagaige
      421 aaslldiprk klylrmrkyg iskhfss
//
LOCUS       WP_284363357             580 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Maritalea porphyrae].
ACCESSION   WP_284363357
VERSION     WP_284363357.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 580)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 580)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 580)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 580)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..580
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=62332
     Region          30..565
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mdtttqdagg kpgikrsltd rifpslsgta laaifiatll fgflilpvak viyvafldpn
       61 sgaltlqnfg dffssslfre sffnsfyvsa msvvlasvfa lplayitsrf efsgamliqs
      121 lgfiplimpp fvgaiamqll fgrngsinll laqyginipf meglngvilv qsvhyfpfil
      181 inlstslrni drsmeesaqn lgahglrlfr rvvfplaapg ylagaslvfi kvfddlgtpl
      241 llnvnnmlap qaylrissig isdpmgyvis filvafsvfs lwasfllmrg kdyattqkgg
      301 gglsrrklst renigaygiv iailllvlsp hialgllafg tiwsysplpd gytlenfntm
      361 fgqsgqyikn tliyagaaaf ldivlataia yivlrtkivg rkwldymata alavpgvvlg
      421 igylrtfndf evpfvgkpla swwviivval mirrlpyalr actaalqqvs qsleeaaenl
      481 gatrsrtirk vviplmsggi lagfvtsfat aavelsatim lvssdsdapl aygiylfmqt
      541 psgrgagaal gilavvivaa gtmlaqciid rerkartgeh
//
LOCUS       WP_284363391             201 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Pseudomonas putida].
ACCESSION   WP_284363391
VERSION     WP_284363391.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..201
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22641
     Region          31..132
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mtswkafydr tdkrapsvll nraldlasdl rprlaidlgc gtgneawqli qagwqvlaid
       61 kepeaivrtm nkcsmddarq ldarvadfey ltelppsnli haglslpfch psrfpylwsq
      121 ickslptggv faghffgkkh swasqkrmsf hsaddieama agfqvillre tessmiidse
      181 lvnwhridvi lrkdhphtns y
//
LOCUS       WP_284363631             314 aa            linear   BCT 25-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Maritalea porphyrae].
ACCESSION   WP_284363631
VERSION     WP_284363631.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Kutner,J., Shabalin,I.G., Matelska,D., Handing,K.B.,
            Gasiorowska,O., Sroka,P., Gorna,M.W., Ginalski,K., Wozniak,K. and
            Minor,W.
  TITLE     Structural, Biochemical, and Evolutionary Characterizations of
            Glyoxylate/Hydroxypyruvate Reductases Show Their Division into Two
            Distinct Subfamilies
  JOURNAL   Biochemistry 57 (6), 963-977 (2018)
   PUBMED   29309127
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10187381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..314
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=34811
     Region          1..312
                     /region_name="GDH_like_2"
                     /note="Putative glycerate dehydrogenase and related
                     proteins of the D-specific 2-hydroxy dehydrogenase family;
                     cd12164"
                     /db_xref="CDD:240641"
     Site            order(47,66..68,92,229,277)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:240641"
     Site            order(67..68,86,92,96,140..144,162..165,167,194..196,
                     200..201,227..229,253..254,277,279..280,312)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240641"
     Site            order(95,97..99,101..102,105..106,109,111,114..115,
                     117..118,122..123,125,128,131,155,251,255,258..260,262,
                     266..267,269,272,274..276,278..279,283)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240641"
ORIGIN      
        1 mtmlmhlsdv serewadafq kalpnhkivt redkfdlkei kylyvwkpea dafdglvnle
       61 vifslgagvd givkhpklpq gvpvvrfvdd eltqcmtdyv vanvamhhrq atrykrdqtq
      121 rqwdqyyper astinvgimg lgqlgadaae klnylgynva gwarsaknia gieeftgaet
      181 fdaflnrtdi lvcllpltpd ttdilcmnnf kklrrghlpg gpcivnaarg ghqneddivt
      241 alldgtlgaa sldvfkvepl pstsalwsfd ncyitphiaa isgldagvrl vteqitrfeq
      301 sgelkhvvdt krgy
//
LOCUS       WP_284363676             475 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Maritalea porphyrae].
ACCESSION   WP_284363676
VERSION     WP_284363676.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..475
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52147
     Region          <242..473
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 maisqnqpyq rarfglsvkl itmiiamimi vevviylpsv anfrirwldd riqvagvaar
       61 vietvpdamd ltpdminnll ksaqaealvv rmddksqlie rldmpmpiav vdadtrqrds
      121 lpliigaldv iingsnrtmr iigvpsgstd lavevlmsea glrqemlays rnifwlsllv
      181 avataaaiff flnrllvrpi grmtqnmiaf rktpedanri ivpsnrtdev giaerelamm
      241 eqdifsmlrq kqhladlgla vakinhdlrn tlsaaqllsd qvatledpqv qrlaprlvtt
      301 ldrainfaqs vldygrqkti ppkfmhvdlr alidesaida gvrshpsief endvpddvvi
      361 nvdpdqisrv fvnimknare aleshtkadg gkkvyvkrie gsncnqilig dngpglppra
      421 kenlfvafdg sgraggtglg lviakeiaea hggkltyleg eqgtvfsvel plasn
//
LOCUS       WP_284363692             443 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Maritalea
            porphyrae].
ACCESSION   WP_284363692
VERSION     WP_284363692.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..443
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=48372
     Region          11..434
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 maralfsqli lrsllvcgmf sasivgpvwa qfvdpqtaed artelerveq tinisterid
       61 slrkeiadme gdrsqqtaal iasaqrvkla eievtaiser maelraeens ikatldlens
      121 eigtlltalq iigrnpppal ivepnnatks araalllssi lpqlsnrada irieldalld
      181 ikqqveaeet elrenlnilr eeklriavli earkegvera sqaldaeqre aellasraks
      241 lnqllkvlee evqsvteane aarqsdetpr fdvgvqlene aiqlaladtn rtqpafpfel
      301 gkghlvpptn gvsviefgnn dgfggisqgt fivtraeaqv vapadgwvly qgpylnygqi
      361 vilnvgqnyn illaglaqtn velgqfvlmg epvgimgkrt isqtiatsag nsrptlyiel
      421 rqegepmdps dwwattrntt qng
//
LOCUS       WP_284363896             382 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Maritalea porphyrae].
ACCESSION   WP_284363896
VERSION     WP_284363896.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..382
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=43056
     Region          34..151
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mssksalssa qvkaldsagi einhyhssmf qgenihqawi ddcarylqci fgdkiagktv
       61 vdygfgrgnw slafrqlgae hvisieasqn aaenfkryvk dheiqnisvq lgntddqelh
      121 ieadivflyg ilhhvkhper llgsarhwlk deqsqilaya ydagsmreml vsacrkllgt
      181 ekpepswela lhplarhrav ddlvapivsf wtpkqlvdva ndaglkpigq ekdfsnfqnk
      241 slapefdpyi lllkanaaqe etiepianah qyideykvig ealdlvvqha paqskpniai
      301 gifnswfaga qpasfedklf ylwrylchai ntmpqdlvfa stsdeletll fltrrmshkk
      361 sdelmrncem lkdkitnnsf ri
//
LOCUS       WP_284363836             116 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Maritalea
            porphyrae].
ACCESSION   WP_284363836
VERSION     WP_284363836.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..116
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=13059
     Region          1..93
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 miavifevwp epehkgayld iaaqlkfele qidgfisver fqsltdegkv lslsffkdev
       61 avkawrnlps hraaqkagre qlfagyrlri asvvrdyskl ereqapldsv avhaqs
//
LOCUS       WP_284363937             405 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Maritalea porphyrae].
ACCESSION   WP_284363937
VERSION     WP_284363937.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 405)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..405
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42881
     Region          47..387
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(135,137,261,263,292..294,334)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mklakillgs avvlgslaga syaedqrihi ilcgddtwgg evnaahmaaw easnpgfktd
       61 ieyvpwgqcq dkattlaasg nppaiaymgs rtlkqlaqne limshdltee elasyaapil
      121 gtvtadgkiw glprafstka lyynkdlfea agldpnsppk twdelysaaa aikektdadg
      181 iglaaasfdn tmhqfmnyvy tnggevinad gdivfnspnn vetmefygkl asvsqpgpva
      241 ydrgklvplf neakigmyis gpwgrsqtgd avnwgvaplp vgpngtpgtl litdsyavfk
      301 gsgveeaals lakfmtstdn qmefeiaagl tplrpdhpev aklreadptw gafldaiatg
      361 gpepfvtdyv glqdvineai qsvvlgeasa adavaqaaed leeyk
//
LOCUS       WP_284363965             277 aa            linear   BCT 25-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Maritalea porphyrae].
ACCESSION   WP_284363965
VERSION     WP_284363965.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Pereira,J. and Lupas,A.N.
  TITLE     The VCBS superfamily forms a third supercluster of beta-propellers
            that includes tachylectin and integrins
  JOURNAL   Bioinformatics 36 (24), 5618-5622 (2021)
   PUBMED   33416871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..277
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=30536
     Region          95..161
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          150..218
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mrllfilsla mllpafvsga maqpyppikn syvavgqkqi arawlseptt ryqhfvlgdr
       61 feasrlvvql angqqfshel pasfvfedrh vrladlnndg adelvvvmss islgaalavf
      121 nadqsglhll attphiglpy rwlnpagiad fdgdgnleia lvqkphltkr lefwrldger
      181 lvrvgsangf snhrngsrnq rmsaaydinn dgvvdllips anrteiiavt lvpeikqlrr
      241 wqlpspadgd felqvdkaph qvvlklesgd nfvialq
//
LOCUS       WP_284364154             319 aa            linear   BCT 25-DEC-2024
DEFINITION  flagellar protein MotY [Pseudomonas putida].
ACCESSION   WP_284364154
VERSION     WP_284364154.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16063479
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..319
                     /product="flagellar protein MotY"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0097588 - archaeal or bacterial-type
                     flagellum-dependent cell motility [Evidence IEA]"
                     /calculated_mol_wt=34324
     Region          22..166
                     /region_name="MotY_N"
                     /note="MotY N-terminal domain; pfam18393"
                     /db_xref="CDD:465741"
     Region          176..280
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(181..182,216..217,220,224..225,228,270,274)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mrqryltllt lfaslpagal tfqtrmenia wkvegdqfec rliqpiegfg sgefvrrage
       61 qpvfqlrsds nvlgagtasl laaaapwqpg rgdinlgsvr martgvlfss sqgqasrlin
      121 glldgrstvv rnytgeagrp mevrvlpvsf akaysdyqvc askllpmnyd qvrqtqvgfp
      181 gggtdldasa rarldvildy mkadptvnhi elnghsdnsg nrltnrdlsr rralavadyf
      241 kahglaeeqi tvrfhgeqyp lvknnsaanr arnrrvniel drvsvvekpv ekpaepaapa
      301 apapaaaspa aaapgakap
//
LOCUS       WP_284364170             420 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Maritalea porphyrae].
ACCESSION   WP_284364170
VERSION     WP_284364170.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..420
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45744
     Region          1..404
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mpvrsttldn gmtvithsmp slesasvgvw akagsrcete qehgishlle hmafkgtetr
       61 ssrqiaeeie tvggdvnaat sventgyfsr ilkedvglaa dilsdilqns lfsaeelqre
      121 khvivqeiga shdapddyvy dlfqgaayqd qpigrsilgt vesvesftpe airaymerty
      181 vgdsmvmaaa gnvnhdqlvd iaakkfdglk atgapdpvea nyvggdirlq rdheqahvli
      241 gvegrayhsd gfyasqilas ilgggmssrl fqevrekrgl cysiysfhwa fadsgifgvs
      301 aatgdddlae lipvvldelk natlnitede vvrvrnqira gllmslerps sragqlarqq
      361 llwgrpiple etverinnid agrvmevaeq lfngakpvva gigpmsnlae ydriesqlkf
//
LOCUS       WP_284364062             310 aa            linear   BCT 25-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Pseudomonas putida].
ACCESSION   WP_284364062
VERSION     WP_284364062.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Kutner,J., Shabalin,I.G., Matelska,D., Handing,K.B.,
            Gasiorowska,O., Sroka,P., Gorna,M.W., Ginalski,K., Wozniak,K. and
            Minor,W.
  TITLE     Structural, Biochemical, and Evolutionary Characterizations of
            Glyoxylate/Hydroxypyruvate Reductases Show Their Division into Two
            Distinct Subfamilies
  JOURNAL   Biochemistry 57 (6), 963-977 (2018)
   PUBMED   29309127
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10187381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..310
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=33113
     Region          5..306
                     /region_name="GDH_like_2"
                     /note="Putative glycerate dehydrogenase and related
                     proteins of the D-specific 2-hydroxy dehydrogenase family;
                     cd12164"
                     /db_xref="CDD:240641"
     Site            order(48,67..69,93,225,273)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:240641"
     Site            order(68..69,87,93,97,141..145,163..166,168,195..197,
                     201..202,223..225,249..250,273,275..276)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240641"
     Site            order(96,98..100,102..103,106..107,110,112,115..116,
                     118..119,123..124,126,129,132,156,247,251,254..256,258,
                     262..263,265,268,270..272,274..275,279)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240641"
ORIGIN      
        1 maslvllcqn paltdwlaal ftehaphlnv lrpedagarh aevavcwfpp qgslgrlpnl
       61 rlvhsigsgt dhlaqdssrd aslpvcrvvd pdhtqgmsey vhwgvlhfhr gfdrviagna
      121 sqhwqrpvqr kagdfrvgvm glgaigapva qrlaaagydv rgwartprqv dgvntfagpa
      181 slqgflagld vlvnllplta sthgvlnhav frhmaegsal incgrgqhln phdlrqalas
      241 gqlrgalldv feqeplpads plwhtpgvwv tphmasaasd lciarqvadn vsrlsaglgl
      301 nnlvdpelgy
//
LOCUS       WP_284364342             501 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Maritalea porphyrae].
ACCESSION   WP_284364342
VERSION     WP_284364342.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..501
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55080
     Region          266..499
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mnktttksss afswlfsatt isivmlvfaf acgltsalmw ersnsswqth ldkafnggia
       61 lfgtvselrs qpsrevqsdi fefeivqptk vpesnvtqlr fsvpnssvye tsltlhppsa
      121 avtssadrva vrifspqfqy svsnlpatnd glafqfgels rgiarlcsda tmfveidsdn
      181 wlsirapsiw scssrpadlr lpalllaalt lgilfsvang fsqmlenlas dirkaatsgs
      241 ieeipergan evknltsavn affaserqrl eqralllsgi shdlgtpatr lklrtalidd
      301 qilrekldrd idqmtdmidg vlsytrhemd teaprkismr slveaivddy qdlgkpvtle
      361 apdkinldrl gnvfsqtsen tqilirdhqr vlckcrpnai rraltnlien alkygeeaqv
      421 alhatadhft ivvsdrgsht sfeqpeklle pfvrgenakl lkgaglglti tnsvvknhgg
      481 tlsfsqgqng levvmdlprw i
//
LOCUS       WP_284364648             403 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Maritalea porphyrae].
ACCESSION   WP_284364648
VERSION     WP_284364648.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..403
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43344
     Region          7..376
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mnfeknvdtv iigggnvgaa iahhladlgk tdvcvlergt isnlqgstgh apglvvrnny
       61 stvmsewady stklytslpd ggshmelvgs ieasrheknt pvfeaklaaa ksrgfkakll
      121 asnevgemlp yvdagklals llvegdgvvd akstvqsllk naeskgiavh entevlsitt
      181 hnsrvtavet tggriacntv vlavgiwgav flekmgvklp lvpvqhpyly tkaapvlgep
      241 tsaavrpmfr dmdnlfylre hgnqfgygwy nhaplgaemq dnraaelpyv eqvfdsklpf
      301 dllpvlrtlp vidqlngvfs mtpdggpllg eidevvglfl aeavwvthag gvgrsaaqml
      361 tgntltqdvs kfdanrfssy daqriyadal slynniyhwp ltv
//
LOCUS       WP_284364722             639 aa            linear   BCT 25-DEC-2024
DEFINITION  ABCB family ABC transporter ATP-binding protein/permease [Maritalea
            porphyrae].
ACCESSION   WP_284364722
VERSION     WP_284364722.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 639)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..639
                     /product="ABCB family ABC transporter ATP-binding
                     protein/permease"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=71141
     Region          18..618
                     /region_name="ATM1"
                     /note="ABC-type transport system involved in Fe-S cluster
                     assembly, permease and ATPase components
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5265"
                     /db_xref="CDD:444078"
ORIGIN      
        1 mavaptgrtv skkqtvnade gspfatiknl wpymwpsdrp dlkarvmlal lallaamgaa
       61 tmapyfysqv idsleigdgi eqakmfgltl aiafaiaygl gqiteslfmq lrdvlfasvg
      121 qhavrqlahr tfvhlhalsl ryhlqrrtgg lsrviergtk gietivrftm lntaptlvqf
      181 viistifvwr fglpylavlv ltvvgyiyft vkasnwrigi rrkmndsdte anskaidsll
      241 nfetvkyfgn eemearrfde smavyegaai rmwtslgfln fgqavifwig mivisimsvn
      301 svlagditvg dfvlinmymm qiyrplnfig fvyreirqgl tdienmfell dkdaeikdkp
      361 dakplevsgp vlkfndvkfh ydpdreilkg vsfevpagkt iavvgpsgag kstisrliyr
      421 fydaiegsve idgqdvrdvt qkslrasvgm vpqdtvlfnd tiaynirygr peatdeevre
      481 aaklaqisdf idglpqgfdt pvgerglkls ggekqrvaia rtilksppil ildeatsald
      541 tqtereiqsa ldhvsqnrtt lviahrlstv inadeiivlr ageiaergnh eallaldgly
      601 aqmwnrqrev deageklrla retdtegfli kqseqdpvk
//
LOCUS       WP_284364725             429 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Pseudomonas].
ACCESSION   WP_284364725
VERSION     WP_284364725.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..429
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47249
     Region          31..396
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mfkqsaqhva syytqtypan iplrptlqgt hdtdvliiga gfsglhtalr ltqagkrvtl
       61 leasrvawaa sgrnggqall gwscdmpple kalgvertrr lwasmcwaad emrelpqrhg
      121 fdidyrqgsl wtavlprrvk mleealhdae hkwgydalrl igrdelpqwi dspryqaaly
      181 dakgahlnpl klaqglasti easgghiyeq sqvlsyqqdg ngytarteng evrcqvlvla
      241 cnayidrldr glsrrllpvg syqvatapld adfaqsllpr nscvidnqfv pdyfrltpdh
      301 rllfgggcty lggipkdvas atrpylervf pqlagvaidy awgghidcsi qrtpdvgreg
      361 qrywlqgfsg hgvlptlaaa ravsdailgd edllalyqgi dngrfpggdl laapleaaak
      421 awyrmrdrv
//
LOCUS       WP_284364739             769 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Maritalea porphyrae].
ACCESSION   WP_284364739
VERSION     WP_284364739.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 769)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 769)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 769)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 769)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..769
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=85193
     Region          94..763
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mfgrllktiq serqlsavir ahlvdglfhp fasfvtgvii gvaitalmwi ftddivirdl
       61 ssglaiiail rlcvgllylr rnrpigiees nkweiaffvg aaafalclgl ltlfalirvp
      121 dievhlilti tcagygssia arnagrplla vgqlylttip mwiglivqtq ytslvssfgw
      181 cglflftigi sditlamrkt iidalehkqr naelaasfre qaerfdaalt nmshglcmfd
      241 qdkklvvwne kvadiigadq slfttgtsmd siiaafhpdd hskivdqtkd nvhsewseta
      301 klsdgrfvaa strtmengnv vivfadvtek ekaearirnl awvdqltglm nrvslhelfv
      361 eklenlnvss elavhyidld hfksvndtlg hpigdmllrq vadricdvcl degevarmag
      421 deflviqtls pqarsprdla qqivdalhqp fnvnshfiqi gasvgiviap kdgndadlll
      481 kradmalyaa kkagrnkfay fepqmdqrlq qmraleldik qaleknqfkl afqpivdaed
      541 qsvasfeclv rwthptngkm mpakfipaae etgqimeigr wvtkeaikta aawpvrkqis
      601 vnfsavqfqd srfadflrrq lkrynfpadl leleitetaf ivdmenslkq lqqlkdlgvk
      661 islddfgtgy sslsqlqrfs fnkikidgsf vrdletnpss aavatavaei gkalditvva
      721 ecvetqeqld flrsvgvtri qgyftgrpmd aeaaeallik eapavgevg
//
LOCUS       WP_284364809             384 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Pseudomonas putida].
ACCESSION   WP_284364809
VERSION     WP_284364809.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..384
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43359
     Region          76..383
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mikvvalptk nilnsnrdts cpdskkminl ahrrdylrqi lraagkplst advhaklvaw
       61 vgrhgdaadd qrdkttirdl kaleelnyvq sqtdpedkrg llwsavgrsh slvlspsdam
      121 slwavfqhae rfglqsatde lkglrdytel mmqdgsvrkl nftkritsgt rftqlqpgky
      181 kaqhlkqiqm aildnealev wyrprnadgv ecvyqlkplg lshqdsniyl sayvteeqwl
      241 gnapahdepr gkyssngpnt lcalmlhrit kvepgkriid dpegydihad eaqtdlvtih
      301 spaqktrlrl sqnlynrlae npldknqkll pdgnkwlltc kvrdtqglrl flmanaadie
      361 vleplalrah ihemlalalk tyeq
//
LOCUS       WP_284364868             308 aa            linear   BCT 25-DEC-2024
DEFINITION  FecR family protein [Pseudomonas putida].
ACCESSION   WP_284364868
VERSION     WP_284364868.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20752687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..308
                     /product="FecR family protein"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0016989 - sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34562
     Region          13..54
                     /region_name="DUF4880"
                     /note="Domain of unknown function (DUF4880); pfam16220"
                     /db_xref="CDD:435227"
     Region          73..308
                     /region_name="FecR"
                     /note="Periplasmic ferric-dicitrate binding protein FecR,
                     regulates iron transport [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG3712"
                     /db_xref="CDD:442926"
ORIGIN      
        1 mpakqlqqpd pqqealewfs llrqpgcdet qrqafaawcq vpenahayae letfwqqlqp
       61 pparprprhv tvrrshlgkw lalvflvglg aatylywpll qrlaselhtd vgerrstrla
      121 dgttlnldsa samnidlrgr trqlhlvqgq vylevvldgr amevdvgnar iqvfgtrlqv
      181 arhaghdelv vlsgkamvtq ggeqrmvsag ervtfndtri dpvqkadlkt adswrngrlk
      241 atdmplgqvl erlasyqgqr vwmvdeqiah rrvsgdfnld rpgeslqsla aaqhlqlqgv
      301 lghwlmvh
//
LOCUS       WP_284364938            1633 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Pseudomonas putida].
ACCESSION   WP_284364938
VERSION     WP_284364938.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 1633)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1633)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1633)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1633)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1633
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..1633
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=178613
     Region          22..1632
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mfnkglllac alallsacds stpdkpapve kpvatapvet qapkredpav lakryegrel
       61 svldvsevql dgaatlsisf sapldakqdf atkvhlvdtv kgkldgawel sdnqmelrlr
      121 hlepqrklvl tvdkgllavn gkqldsesvt qletrdmqpt igfasrgsll ptrlaeglpv
      181 ialnvdkvdv effrvkpeml stflaswgrn sslyyyqske tldmaelvys grfdlnparn
      241 tretvllpia gikplqdpgv ylavmrasgt ydysqpatlf tlsdigvsah ryrdridvfa
      301 qaleggkald gvnleihdek gkllaqastd gkghaqlpit pkadtliatq gvhttllrln
      361 taaldlaefd itgpqanplq ffifgprdly rpgetvllng llrdqdgkpv kaqpvsvevr
      421 rpdeqvsrkf vweadsngly qyqlqlanea ptgrwqllld lgggrkqvye flvedflper
      481 lalelkgsst plspeedari qvngrylyga paagnrlsgq ayvrplreav palpgyqfgs
      541 vtetelnqdl eldevtldqa gkavvdiesr waearsplql tvqaslqesg grpitrrleq
      601 piwpaerlpg lrglfdgeet dsdgpvefef lvadrdgnkl aandlkvrli rerrdyywny
      661 sqsdgwsyay nekfltqnee tvsvkagsta klsfqvewgp yrvevedpqt glvsserfwa
      721 gyraqdnaeg gavrpdqvkl aldkpsyadg atakvtvtpp aagsgylmie ssdgplwwqe
      781 ievpaegktf dvqldkawar hdlyisalvi rpgerkanat pkrsvgvlhl pldraerkla
      841 vslqapekmr pkqpltvkvk aanadgsvpk qvhvllsavd vgilnitdfk tpdpfaslfg
      901 rkaygadqld iygqlieagq grlaslafgg daamakggkr pnttvtivaq qslpvtlddk
      961 gegqatvdip dfngelrlma qawteehfgm aegktvvaap liaelsaprf laggdrtsla
     1021 ldlanlsgra qqlnveitte gqlslatnav qtvalaegqr stlmipvqaq gglgqgkvhv
     1081 rvtglqlpne pttaferewt lgvrpaypam lkhyrvalkd qpwtlpeadl aafepaglea
     1141 slalssrppl nlaeqirale aypygcleqt tsglypslya dadslkrlgi kgepadvrkr
     1201 kiemgiehll gmqryngsfg lwssdseeey wltayvtdfl lrardqgygv paealkkase
     1261 rllrylqern lievdysena dhtrfavqay aalvlsrsqq aplgalrglf erradarsgl
     1321 plvqlavald kmgdkpraeq alqaglgisr gkgwmadygs alrdqalila llqesnlass
     1381 qvdqrlfals delaanrwls tqernalfla grgllgkpeg kwqarldsag evrefnnaea
     1441 gmklegplla splsvqnegs etlyqqltls gyprqapaag gngmqirrey lgmngqpldl
     1501 hnlrsgdlvl vhlalkaedr vpdalvvdll paglelenqn laqsaasldn assavkewre
     1561 smqnasvvhq eyrddryvaa lkldsygnth llylaravtp gtyrvpppqv esmyrpnlqa
     1621 vgdgqgemtv kar
//
LOCUS       WP_284365135             266 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [Pseudomonas].
ACCESSION   WP_284365135
VERSION     WP_284365135.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469162
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..266
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=27087
     Region          <166..262
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          166..192
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(168..169,172..173,175,199,202..203,206..207,
                     209..210,237,240..241,244..245,248)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          197..227
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          236..262
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrcdvnkwlf pavtalavlq gcssvprgni pvvdsstrvs nservtanrs aggyntgtaq
       61 aqtlpedsgv tvmipqgaga sgiqtfpaan gaapistspi tpgpitsgpv ssapmttnpn
      121 piadepfdia amnstpasss aptgiprsta agglsadeql dgpvlalltt aqtqqgsgdf
      181 ngaasslera qriaprepqv lyrlaqvrls qgdaaqaeql arraltyang rpslqaelwn
      241 tiaqarekqg dsagaalarq karvns
//
LOCUS       WP_284365152             472 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Pseudomonas putida].
ACCESSION   WP_284365152
VERSION     WP_284365152.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..472
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=52161
     Region          5..330
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(7..8,11..12,44,47,101..102,154)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(99,102,176..182,211,237..242,271,297..301,303)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mlwacillpq laldtvlrer ddpdtplvll ggptqrrvlq avspaaaalg lragqtltaa
       61 raladgftcv eadprrieqv qqllaawayr fsaqvslhyp ralllevgss lqlfgpwplf
      121 earlrqelad lglrqrivla snpvaarmla nahdglavgd adatraallg mpitriglpa
      181 daaeafarmg lrqlghvlcl prdtlakrfa pqvqlhldql lglrnlglaf yqppdrfetr
      241 lelnfdvesh qallfplrrm lndlaaflag rdcgvqrfcl hlehaegpdt lltvgllaae
      301 rdaamlfelt rgrleplrip apvrnvwlva edlptfvpqh qalfdpraqq aqpweqlrer
      361 lrarlgdeav kglsaaadhr pecawqlteq gaqgsmpvap gtrpgwllpa pmaldtasyq
      421 vhgqaeries gwwdggdvrr dyyrietrdg lrgwayrdlg qagplwlqgw fa
//
LOCUS       WP_284365190             116 aa            linear   BCT 25-DEC-2024
DEFINITION  HesB/IscA family protein [Maritalea porphyrae].
ACCESSION   WP_284365190
VERSION     WP_284365190.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Lu,H.M., Li,J.D., Zhang,Y.D., Lu,X.L., Xu,C., Huang,Y. and
            Gribskov,M.
  TITLE     The Evolution History of Fe-S Cluster A-Type Assembly Protein
            Reveals Multiple Gene Duplication Events and Essential Protein
            Motifs
  JOURNAL   Genome Biol Evol 12 (3), 160-173 (2020)
   PUBMED   32108236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..116
                     /product="HesB/IscA family protein"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=12072
     Region          11..116
                     /region_name="IscA"
                     /note="Fe-S cluster assembly iron-binding protein IscA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0316"
                     /db_xref="CDD:440085"
ORIGIN      
        1 msdvatapek vsvtdaalar ieailskqkp gtvlrvavsg ggcsgfqyey nlvqeepsed
       61 dlvlgndkak vlidslslef mqgaeidfvn dligqsfqin npnavascgc gtsfsv
//
LOCUS       WP_284365247             147 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Pseudomonas
            putida].
ACCESSION   WP_284365247
VERSION     WP_284365247.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..147
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16131
     Region          3..104
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mldennaqcp varalevlgd rwalmilrda fdglrrfsef qknlglakni lasrlkllve
       61 sgllmtqpas dgsaykeyvl tekglsvfpv vvglrqwgel ylfeagears elvegvtgqa
      121 letlqvravd grvlgaedcl rrvvrhg
//
LOCUS       WP_284365291             288 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: prepilin peptidase [Pseudomonas].
ACCESSION   WP_284365291
VERSION     WP_284365291.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..288
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31786
     Region          11..286
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mtlwtllaeq payfltlatv lgllvgsfln vlvyrlpiml erqwqreaqe vlglplaqhe
       61 rfdlclpasr cphcahqira wenipvlsyl alrgrcsack trispryplv eiasallslv
      121 vawrfgasae allalpltwc llalslidad hqllpdvlvl pmlwlglivn afglyvplad
      181 alwgavagyl slwtvywvfk lvtgkegmgy gdfklmalig awggwqvlpl tlllssvvga
      241 lvglcllrlr ryamgtaipf gpylaiagwi avlwgdeiya symqllgy
//
LOCUS       WP_284365297             347 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Pseudomonas putida].
ACCESSION   WP_284365297
VERSION     WP_284365297.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..347
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=39332
     Region          7..342
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 marttapltd tacrsakptd rpyklfdgdg lyllvypngr kgwrfryvkp dgregltsfg
       61 nypviglada rqkrletkrm laegidpias kqqdkaeavv rghtferval dwhkemsvkw
      121 apghsrtvls rlkthvfpll garaivdldt fdlmqpleai kkrgtidval rvqnylqsim
      181 reakrlrlit vnpaydlegf isaprvthrp alplsrlpel mdrieqykgr tltrltvmls
      241 lhmfvrssel rfarwsefdl krgiweipdt rhaldgvpys trgtkmagdi hlvplspqav
      301 alleqiyait gyfdlvftsd alswkpmsen tvnsalrnmg ydtkgmd
//
LOCUS       WP_284365335             558 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Maritalea porphyrae].
ACCESSION   WP_284365335
VERSION     WP_284365335.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20358183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..558
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=59978
     Region          108..349
                     /region_name="SBP_bac_11"
                     /note="Bacterial extracellular solute-binding protein;
                     pfam13531"
                     /db_xref="CDD:463911"
     Region          <380..531
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mntmaksflg talvagvltl sacggapiet teaaheniak lvkeqikpsr qenrvranie
       61 ltptnllsll pnideypiti aandsatvea veiftsseks grgtdglynd laerfnrqnn
      121 kisngkfakv airkmpsglg aqfiladkhv pdafspsnkl wgkmiesqgv vadeinpvta
      181 pntagivvrk skldlvttdg kldlqkllte vtsgefsmgy tnpyqsstgl nflmmvlhsf
      241 aqgdevefls pdvasafeaf qlgvpfvaqn tlqmrdaavg sgvldalvme hqtwvnvtgm
      301 adyefvpfgv rhdsplyalp qadeaerevl aafnqfiean kneiskfgfg nnadytasyd
      361 iedgsliqqa qklwkdkksg gkpiaamfva dvsgsmdgsr lkelkqalvd ssdliaasna
      421 iglisyndsv nidlpvrqfn lqqkslfiga veslvaggat atnngvivaa nellnfaaan
      481 pdhklvifvl sdgetnegle fatvketlry aripihsiay elssdhlkem aglveaayie
      541 ssvgsasyri gnllnsem
//
LOCUS       WP_284365340             618 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Maritalea porphyrae].
ACCESSION   WP_284365340
VERSION     WP_284365340.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 618)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..618
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=68684
     Region          22..614
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 maqtatltqn ysdgvfktan tvvhnlakan pdrvairqkr ygiwneyswa dvdrltrela
       61 aaliemgvkr gskvgilsen rcewvlaqfa iqaagatvvg myptspsfei hhlvdasdte
      121 flfiedqeqf dkivelegkt prlkklmvfd pkglhdeefl glqsfsdlae igrsaieqha
      181 keiearitdt kaedtalmvf tsgstgapka akishgnyfa agklidnffg ghvlqgsnil
      241 sylplchiae qdmtvvnala anhimnfges lrtitldlrd aapdlffgvp riwekmqagl
      301 mvhiktahpi qtwisemalr saerlshtpr skwtiwqrav nqfwdvlvyr hlrsflglgr
      361 vkiaitaaap isldlltffr gigvniceiw gmtettgaac mqpdwgesdg rvgffpegve
      421 akladdgell vkggivfkgy yrnpeatsst lvdgwlhtgd iaashpdgsf sivdrkkdvm
      481 itaagknltp slientmkas pyikecivia drrpypvglv qidfetmrvw aekagitytt
      541 frslaenpav vrlindevhr lnerlarveq ikkvrlltke ldhddgevta tlkvrrakin
      601 etyaeviesl yeeqavsa
//
LOCUS       WP_284365397             105 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsB family cell division protein [Maritalea porphyrae].
ACCESSION   WP_284365397
VERSION     WP_284365397.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..105
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=11737
     Region          11..100
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 mptrlkrpkl rnklaiaavl iafqgylgyh liegkfgias qarfsqqvie lqdqrdalar
       61 rievaqnrns llaadrldpd llterarhll gwgnpsdtiv pthnk
//
LOCUS       WP_284365683             311 aa            linear   BCT 25-DEC-2024
DEFINITION  GDP-L-fucose synthase family protein [Maritalea porphyrae].
ACCESSION   WP_284365683
VERSION     WP_284365683.1
KEYWORDS    RefSeq.
SOURCE      Maritalea porphyrae
  ORGANISM  Maritalea porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Maritalea.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Maritalea porphyrae"
                     /db_xref="taxon:880732"
     Protein         1..311
                     /product="GDP-L-fucose synthase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34758
     Region          6..305
                     /region_name="GDP_FS_SDR_e"
                     /note="GDP-fucose synthetase, extended (e) SDRs; cd05239"
                     /db_xref="CDD:187550"
     Site            order(11,13..16,37,40..43,63..65,67,87,106..108,137,141,
                     164..165,167)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187550"
     Site            order(84,108,137,141)
                     /site_type="active"
                     /db_xref="CDD:187550"
     Site            order(108,137,166,185,202,210)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187550"
ORIGIN      
        1 mdfddkifva ghrgmvgsai fraltkagyq nvitrtrqel pldnsneves ffaverpkyv
       61 flaaakvggi qanklyggdf irenlqievn iidaayrhgv ekflflgssc iypkfaeqpi
      121 qetslltgel eetnlpyava kiagtvmcda yreqfgfnaf tvmppnvygi gdnfhpensh
      181 vvaglmqrfh kakvnclpev vawgtgsplr eliycddlae gciylmqnyd dggminvgts
      241 deytirqite lvadvvgyeg kiawdkskpd gtprkimnne kisqlgwkak tefrtglemm
      301 yawymqecev g
//
LOCUS       WP_284366974              92 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Bacillus safensis].
ACCESSION   WP_284366974
VERSION     WP_284366974.1
KEYWORDS    RefSeq.
SOURCE      Bacillus safensis
  ORGANISM  Bacillus safensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 92)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 92)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 92)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Bacillus safensis"
                     /db_xref="taxon:561879"
     Protein         1..92
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=10311
     Region          1..91
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mknhsnlqqa vkiykalgep trlkitcllv netnlccsdi girlesiags tlshhlkqlt
       61 dcgllsthke gtyvyyildr elirkyapyv mt
//
LOCUS       WP_284369012             395 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Algimonas porphyrae].
ACCESSION   WP_284369012
VERSION     WP_284369012.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..395
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=45637
     Region          1..395
                     /region_name="CoxE2"
                     /note="Uncharacterized CoxE-like protein, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3825"
                     /db_xref="CDD:443037"
ORIGIN      
        1 mfhhffselr rasvpvsire yltllegvdk gvandsldgf yylsrtalvk derdldkfdq
       61 vfshvfrgid yigdifgqde haipedwlrk maelhlspee maeiealgdf dkimealker
      121 ldnqdkrheg gnrnigtagr spfgaygynp egvrigqkdg rhgkavkvwd krqfknldgd
      181 keigtrnikv alrrlrkfar egaaeeldlp gtirgtarqg wldirmrper rnavkvltff
      241 diggsmdahv kqvedlfsaa ksefkrlehf yfhnmlyeqv wrdnrrrmse ttptwdilht
      301 fpsdhrvviv gdaamspyev amrggsvehw neeagavwlk riadvyphlv winptqekyw
      361 efsqstqmiq eiiggermfp mtlngledam relar
//
LOCUS       WP_284369040             444 aa            linear   BCT 25-DEC-2024
DEFINITION  spinster family MFS transporter [Algimonas porphyrae].
ACCESSION   WP_284369040
VERSION     WP_284369040.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..444
                     /product="spinster family MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006869 - lipid transport [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48001
     Region          27..423
                     /region_name="MFS_spinster_like"
                     /note="Protein spinster and spinster homologs of the Major
                     Facilitator Superfamily of transporters; cd17328"
                     /db_xref="CDD:340886"
     Site            order(29..30,33..34,37,70,120..121,123..125,128,148,
                     151..152,155,238,241..242,245..247,250,280,287,338..339,
                     343,347,367,370..371,374..375,378)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340886"
ORIGIN      
        1 mtdpqpprqp rsryrtyvll lltlvygfnf idrqivgila pwiqadlelt ntqmglligl
       61 afaifytvmg ipiafiadrv nrkgllaial atwsgftalt glaqnflhig larigvgvge
      121 aggsppshsi isdlygkeer agalgvyslg iplgimsayf itvalmgadp savdwrrifi
      181 ilgvsgilla vivmftirep krgameaaps tdipkvpfsq alktllsips wwwmsfgiaf
      241 asfaayalsg fqtkylglle pdmtgarlre illwlgvmng lfyasgtflg arfvdkqakk
      301 svsaygwvpa lsilialpig llslwvpsin mhlvllapfq fllgvylgps faiaqtlapv
      361 hiramstalf ffilnmialg ggptvagfli dvfasdtvsq leatryalmt vfgsfilavi
      421 sfmmvrrtlp kdwadaearn stas
//
LOCUS       WP_284369134             372 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Algimonas porphyrae].
ACCESSION   WP_284369134
VERSION     WP_284369134.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..372
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=42175
     Region          15..356
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mdisrkrfgr pvsirdghdn fftplrllfa llvvighaya vgkgspdaep qlflsytfsy
       61 mavnlffits gflvtksmly rgdptlftas rliriypali vhvlfvvfiv gtfmsdlplw
      121 aylshpdvls qpirvlsffn tdmilpgvfa dngepyasap lwtlrfemlc yigtvlaftl
      181 glmrrkwmll aqfvvpsiiw ivgqqsgtfe hlpaslenmi rfaiayglgt aiyayrdrit
      241 vslwmipala llcwlirdie avevtmnlml aafvmwaafl haprfdalkr lpdmsyglyi
      301 yhwvilqtam alwpglsvia lfaialpitl glawlswiwi ekpalarkgp fsdwlrfgre
      361 pkpfdrnavl id
//
LOCUS       WP_284369145             104 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsB family cell division protein [Algimonas porphyrae].
ACCESSION   WP_284369145
VERSION     WP_284369145.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..104
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=11472
     Region          28..104
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 mrlprptlpd mkrrapvaal lmlylylgfh afsgsqgivr waensakaer learlaalqa
       61 krdalqadvd llastsldld tldiearrtl fvakpgeiti wldp
//
LOCUS       WP_284369155             217 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Algimonas porphyrae].
ACCESSION   WP_284369155
VERSION     WP_284369155.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..217
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24333
     Region          1..213
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mtrlaifdld ytltrqgtwg rfvlrsmkar plglppllla agwtqlrykr gavpriavkt
       61 ammrrsmvgr treelsdvad aliaddmqng lnlrvldalr ahqqagdivl iasaavdllv
      121 erycealgah gqvstrmawt qddrladhfa sdncygtqkm drikgllter nllpshvtay
      181 sdsradapml efadkaiiva pkrktrdyaq rmnfeiw
//
LOCUS       WP_284369206             650 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Algimonas porphyrae].
ACCESSION   WP_284369206
VERSION     WP_284369206.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..650
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..650
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=72765
     Region          400..643
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mrkfllscva aigvvgtslm atpslaakpy pleywaapsf msnlevspdg kyvafrkats
       61 qkgdfiieif etsnmdkkpv rvgaesmdlr nfswvgdaem vvsfrgqvsd kikgfnqgaf
      121 ksklalysve sgdfkelnad dfslslanpl vnepdhvlvq yvsfsegqaf rapayyrynl
      181 krgtrnlvlk gnsdlrgyrf dvdgnprfav dvsdpmkatf lyrpvggsgw tpyyeqsids
      241 peafdyaglv qgddnliyvi ahngedrtsl wkynlsekkf eekvyqhpnv dlrftarhsn
      301 pytnpgevtg vryftdnfht ewfnaeeaai irqfeevipn ahfvritsrs rdgnvlviqn
      361 igpkdpgtfy lfnrgqfskv gssngllkpe glsdveyvkw tardgktitg hvtkpegagp
      421 fplivmphgg pfisetilfd pwaqmfanng ymvlqpqyrg stnyglefyk agfieegegg
      481 kamqddkddg vkyliekgwv dpdrvamfgw syggyaalia asrgddlyqc aiagaavadn
      541 tqqvnyyrdr irgwqeveqi gfwdgsvnpi dladqvdmpl milhgtidqr vplrhaekyi
      601 nalesagkef tyveledadh fldtlnydhm tkaypaminf lkkdcgpggl
//
LOCUS       WP_284369264             263 aa            linear   BCT 25-DEC-2024
DEFINITION  glutaredoxin family protein [Algimonas porphyrae].
ACCESSION   WP_284369264
VERSION     WP_284369264.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Shelton,M.D., Chock,P.B. and Mieyal,J.J.
  TITLE     Glutaredoxin: role in reversible protein s-glutathionylation and
            regulation of redox signal transduction and protein translocation
  JOURNAL   Antioxid Redox Signal 7 (3-4), 348-366 (2005)
   PUBMED   15706083
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Fernandes,A.P. and Holmgren,A.
  TITLE     Glutaredoxins: glutathione-dependent redox enzymes with functions
            far beyond a simple thioredoxin backup system
  JOURNAL   Antioxid Redox Signal 6 (1), 63-74 (2004)
   PUBMED   14713336
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002164
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..263
                     /product="glutaredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28491
     Region          34..90
                     /region_name="GrxC"
                     /note="Glutaredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG0695"
                     /db_xref="CDD:440459"
ORIGIN      
        1 mdnlvlgdey ssnpvsaatg ktavlyrmvm pghtcpfglk aksllerkgf tvddrhittr
       61 eqqdaikaef dvkttpqtfi egeriggytd lkkhfglkvl ekgettytpi iaifamtalm
      121 atamgigrpg ptlmgwvvdf ialsmcvlai qklrdlegfs sgflgydlla krwvpyayiy
      181 pfaeafagim mltngygwvg apvalfigai gawsvfkavy iekrelkcac vgggsnvplg
      241 avsltenvmm vamgvwmlak lit
//
LOCUS       WP_284369212             552 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Algimonas porphyrae].
ACCESSION   WP_284369212
VERSION     WP_284369212.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 552)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 552)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 552)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 552)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..552
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59244
     Region          14..545
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 msvlrlnppi qlsprrlvyr lsiyaiaalv alplvtvlfa lfagesgvws rlwattlpvy
       61 vanslllmal tgliatligv gtgwcvamlt fpgrrwiswl lilplaapay ivayvyvell
      121 dyfgplqsal rsltgweqgd yafpplrtlp gaalilglcl ypyvyllara sfgqqsatqw
      181 qaarslganp fqafrrvalp marpaiiggl alvlmetlad fgvadyfgip tfstgifrsw
      241 laagdrpaam klaavmllci ftlilmeass rkgrvsargr tmgqagrltl grragwmvtl
      301 lclcpvilgf aipvvsllhn visvpdarpa gdfmtyagnt viigitvvil slllagclay
      361 anrrltgrfs qavirfstlg yalpgallav gllipiggvd ravtrfatth lgwdggllls
      421 gtiivlvfal lirfltvsyn alsagfnqip psmdaaarsl gaspaavmrr ihlpllrpsl
      481 lagglivfvd tlrelpatli lrpfnfdtla triywlasde riveastaam lvilcglipv
      541 ilinrtfenq gg
//
LOCUS       WP_284369272             348 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Algimonas porphyrae].
ACCESSION   WP_284369272
VERSION     WP_284369272.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..348
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=38668
     Region          20..348
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mvstlatepl tkadplfgkn hftlirwvla gfvalghfwl tttgyepfri hqwtggymav
       61 ngffvlsgll imkslatrnd lksytasrll rifpalivim lafglifapi fsrpgglpnl
      121 vsaetwsyvl rvlvmgdpqg apgsifagnl eedfngplwt iryemaayil aavaftigla
      181 krlsttlmmw tgataiylll phiidtsslp asilpffrls scfllgmvlw hwpaarrppw
      241 wsiamvfglf lafgagpige flatlsltgl mlrlglpdqt fdpllrlpdy sygiyiwhyp
      301 liqavlffip dlgpiqimvi stplfvlvag lswhliekps lrlkrris
//
LOCUS       WP_284369366             343 aa            linear   BCT 25-DEC-2024
DEFINITION  MDR family NADP-dependent oxidoreductase [Algimonas porphyrae].
ACCESSION   WP_284369366
VERSION     WP_284369366.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..343
                     /product="MDR family NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=37052
     Region          1..341
                     /region_name="CurA"
                     /note="NADPH-dependent curcumin reductase CurA [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG2130"
                     /db_xref="CDD:441733"
ORIGIN      
        1 mtrpsrrqaw gvaqrpvgkp kpddflfkee piraieagev lletlylgia pvmrmymmda
       61 akagivtgea pldigdtihg rgvarvlesr hpdyavgdvv qgqlgwqthk isamtagerf
      121 lrvtehdlsy alavrilsmt gltaytsyry rcdpkpgetl lvsgaaggvg hmivqlakad
      181 glcviglagg pekcaivrgl gadavidykn edvgvaidsh apdgldiyyd nvggeilmaa
      241 ldrlamgarv llcgsiseyg raesfgltny trlrraeadm rgyfvynhlh rfdetvctls
      301 smiragtlkp lvdeligfdk mpealigvyd gknvgtrcvr vta
//
LOCUS       WP_284369389             165 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Sulfitobacter pacificus].
ACCESSION   WP_284369389
VERSION     WP_284369389.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 165)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007442
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..165
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17062
     Region          67..164
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
ORIGIN      
        1 mfdtmtltki aaglcgawli lllgkwagee lyhadahgep syvievasag tdepaeeidl
       61 valmasadad kgskvfrkct achkvdgtdg vgphlngvvd rdiaavggfg ysgalggleg
      121 nwtiealmgf lespknyapg ttmgfaglkk padradviay lsslq
//
LOCUS       WP_284369675             413 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Algimonas porphyrae].
ACCESSION   WP_284369675
VERSION     WP_284369675.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..413
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=44050
     Region          164..401
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mlasltnraa tvwllfwisf favyihmggl afsglvillg aagwlvwavn yrnvgwpskd
       61 lalalmafla ffvwlaisgs wsgygsgtai rlggqivmmm alpvllltrs pairefvshi
      121 imamalggva vlaldvasgy gintfldpvg pgqdlnmrqg daeknigrgh vvyaiftpll
      181 lglfatrlpr kpalaaaigl lallfvgtml nrlavapliv igalllvaig wrsprwgvrl
      241 slgtavasvl laplvgvfar lagegvmarv pmswdhrlrm wdyslsriae aplfgqglda
      301 srtmqegftt rigvdipfvs lhphnlglqt wmeagavgav llsialaaly rplrrlsggs
      361 rwraaalsgt vmgaaiasai tvgawqywww gliglaamlv vlipedaydt pha
//
LOCUS       WP_284369737             586 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Algimonas porphyrae].
ACCESSION   WP_284369737
VERSION     WP_284369737.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..586
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=65558
     Region          37..544
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 msdahksgir ptrrsalall glggasacap nvervlsnae gasgtfehgi asgdpmatsv
       61 ilwtrvtpad dvtpvpviwe idtdpdfplp lsgqlearaa rdftvkveat dllpgrvyyy
      121 rfrtaddmsa vgrtktlpng speslrfavv scsnyehgyf nvydqiahqq rlsggdryda
      181 llhlgdyyye ygadtydapd kpagrvhepa heiidltdyr trhaqyrrdp nlqsatelmp
      241 miaiwddhet sndswrggaq nhdategswe drkaaalray yewmpvrepv agrareafyr
      301 sfqfgdlltl vaietrltar eepliveeyk deivadadaf kadilndpsr smlgaeqqdy
      361 ivdtfaksks dgvawrmlan qvilgrimtp dftpyvteea ttaiekdwpg ihdfltlsky
      421 dlpfypdswd gypharerfy daldkvgvnd llvvtgdahe fwandltred gtkmgtefvt
      481 ssvssktlia ylgdataqhn llltreneda ryynalhngf mdvelgrksg tvtmyavdtv
      541 nnrdygtfra arftirprtv dgkdtlrmgr prglnipqra lfmglg
//
LOCUS       WP_284369823             388 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Algimonas porphyrae].
ACCESSION   WP_284369823
VERSION     WP_284369823.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..388
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41926
     Region          1..388
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 msslplhgik vvefshmvmg paagmmladl gadvikvepi ggdktrrlrg agagyfpmyn
       61 rnkrsicvdl kspqgrdavl tlidgadvfi enfrpgaldk lgfgwdalsa rndrliycse
      121 kgfldgpyeh rtaldevtqm mgglaymtgp pgrplragss vidvtggmfg amgvmaalye
      181 reqsgrgkrv taslfettvf lvgqhmaqma vtgqpaapmp artsawaiyq lfdtkdgeqv
      241 fvgvvsdgqw ktlcnafgle hlladpdlae nrdrvihkdr flpeieaafk sltkselmdr
      301 iehlglpfap igrpedmfdd phlnasggll nmemedgtma klpalpvaln gervglrhsp
      361 pkagehtdtv fndlgldlat lrkqgvig
//
LOCUS       WP_284369857             321 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Algimonas porphyrae].
ACCESSION   WP_284369857
VERSION     WP_284369857.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   8  (residues 1 to 321)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18445993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..321
                     /product="ArsR/SmtB family transcription factor"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35759
     Region          2..73
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
     Region          141..273
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mdrvarilkl lghpdrlriv allsrgeltv selvsvlels qprvtqyirs leeagiidrl
       61 regswtfsrl rpecdgqspl lssvlsalpq ddpvlqadls rlgsvrarra qqseqffadv
      121 annrgqlshe ylpqsrteav lldaigdrhf damvdlgtgs grmlallaeh vsrgtgvdls
      181 pdmlrvarht lseprfghll vqqsdltqte lpdrsadlvt lhqvlhhldr padalreaar
      241 llradgvlli vdfaehdrde frdryahrrl gfsadeilta leplgfrnsv chrvdsgead
      301 rpdllvwqav rvcsaemela s
//
LOCUS       WP_284369887             108 aa            linear   BCT 25-DEC-2024
DEFINITION  YegP family protein [Algimonas porphyrae].
ACCESSION   WP_284369887
VERSION     WP_284369887.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..108
                     /product="YegP family protein"
                     /calculated_mol_wt=12077
     Region          2..>46
                     /region_name="YegP"
                     /note="Uncharacterized conserved protein YegP, UPF0339
                     family [Function unknown]; COG3422"
                     /db_xref="CDD:442648"
     Region          61..>98
                     /region_name="YegP"
                     /note="Uncharacterized conserved protein YegP, UPF0339
                     family [Function unknown]; COG3422"
                     /db_xref="CDD:442648"
ORIGIN      
        1 madtwefyed kagehrwrct asngniigaa tegykakrdc eanaerhgyn gnpnslgakd
       61 kwefyedkag ehrwrrtasn gepvgrsteg ykakrdcean atrmgwtg
//
LOCUS       WP_284369890             316 aa            linear   BCT 25-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Sulfitobacter pacificus].
ACCESSION   WP_284369890
VERSION     WP_284369890.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..316
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=33624
     Region          3..309
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(8..9,11,51..53,73,101..102,105..106,108..109,112,
                     116,118,126,128,130,132..138,140..144,162..163,167..168,
                     265..266,273,279..285,287..290,292)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(52,74..76,99,236,283,286)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240626"
     Site            order(75..76,103,152..156,175..177,180,206..208,212..213,
                     234..236,260..261,283,285..286)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 mtkllitrpl pqlvqdaakg afdvtvrtet tpltvaertt alrdfdavlp tlgdqfpaka
       61 fvekpraril anfgvgfnhi dadaaraagl evtntpgavt datadiamtl mlmtcrrage
      121 germvragnw pgwhptqllg mhvsgktlgv vgmgrigkai akraaagfgm kvvfynrsev
      181 ndlpfeatql eslhavmqaa dvvvlavpat pqthhmidaa alavmtpdsy liniargdvm
      241 devalitalq ekriagagld vyefepkvpa alialenvtl lphlgtsaqe vreqmglmav
      301 enliaffdgk pvpnpv
//
LOCUS       WP_284369927             375 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Algimonas porphyrae].
ACCESSION   WP_284369927
VERSION     WP_284369927.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..375
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40017
     Region          8..369
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mtdmsqrrqg altdlkviec aqliagpfcg qlladhgaqv ikveqpgvgd pmrtwgrdgf
       61 plsweilarn kesvflnlrd adgqtalkal vaeadilien frpgtmekwg lsyetlsain
      121 palimvrvsg ygqtgpyakr agyaavgeam gglralmgdp drkparagis lgdslagmfa
      181 tigaltalhh rdrtgegqvv dasiyesvla lteatipeha iegftrqrsg sylpgiapsn
      241 iydcadgqvv iganqdtvfa rlaeamgape lasdprygdh vargenqiel daritdwtsq
      301 rsadavqaim ddhgvpcskl yraadmltdp hyaareavvt vqsdrygqvp mpgvfpklsk
      361 tpgavrhsgk gtpdl
//
LOCUS       WP_284370174             492 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Sulfitobacter pacificus].
ACCESSION   WP_284370174
VERSION     WP_284370174.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..492
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=54696
     Region          10..338
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(13..14,17..18,49,52,106..107,159)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(104,107,179..185,214,240..245,274,300..304,306)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mfdgsqrrvv slwfprlasd rvlrgcpleg pfaltlkqsn anrlyclnae aahqglhqgm
       61 shsdarafcp dlqtapadll qdqrflqilr rwatrycpwv glegrdglml disgsahlfg
      121 geegmlndmr krlmraglsa qvgladtrga awalahhgeg vappgemlpa lqslpvaalr
      181 lgeqtttala rlglrqigdl aiaprapltr rfgpdvmmrl dqalgrhpee itpladpphy
      241 gvrmtlpepi glvsdvmaga qrlltrlcat ltaqemgarv feitlrrvdr dtqtvelrla
      301 rplrdphril plferglagv dagfgidqlr leatqveplp arqithvstr dkgqlddlit
      361 rigtriglen iqrflpadsh ipersfivap aaysdpasgw asanprplcl ippepiagtg
      421 pqpperfrwr rmslttgrat gperiapeww leddnwrsgl rdywrietle grrlwlfytp
      481 qnpgwfvqge fa
//
LOCUS       WP_284370209             387 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Algimonas porphyrae].
ACCESSION   WP_284370209
VERSION     WP_284370209.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..387
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42246
     Region          1..387
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mthlplsgir iiaveqygag pygtqllsdl gaevikienp gtggdvsrfv sphrigdtds
       61 qffqtfnrnk kslsldlkda dgrkqfeslv ktadavsnnl rgdlpaklgi dyatlsainp
      121 kivcahlsay grdnsreawp gydylmqaea gfcsvtgepd gppvrfglsm vdfmtgsmma
      181 tglvsavlga hrtgqgcdid vslfdtalhq vsypatwyln eghvvtrepr gahpaivpsq
      241 lmeagdgwim fccqtqkfwe rvaerlghpe wvedprflkv edrranralv qdtmeavlkt
      301 ntvahwmeqf ggyvpaapvy diaqafenpy vaevemtyet ehpgmppkpg ekvgtirlms
      361 spykvngnrl kggiapelga dthdllg
//
LOCUS       WP_284370224             277 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Algimonas porphyrae].
ACCESSION   WP_284370224
VERSION     WP_284370224.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..277
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29520
     Region          6..271
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mktfpsfdgk vcvvtgaasg igravaiala asgarlaltd insdeldktv emigganqhk
       61 vdvmdmadaq aiaayapdve aalgpadyvf niaglsrfgd frntpaesfe kvmdvnfygm
      121 vrmskafleq liktkgglvn vssiygiigv pgqahycask fgirgfseal slemldygvt
      181 vtsvhpggvk tnvvrngevd slahigttkd slienfdkna artsaedaat iildgterkk
      241 llvlvggdat fvqrltrlfp vryrnfvmkr qaritgr
//
LOCUS       WP_284370250             301 aa            linear   BCT 25-DEC-2024
DEFINITION  cell division protein FtsX [Sulfitobacter pacificus].
ACCESSION   WP_284370250
VERSION     WP_284370250.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 301)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..301
                     /product="cell division protein FtsX"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=31343
     Region          47..284
                     /region_name="FtsX"
                     /note="Cell division protein FtsX [Cell cycle control,
                     cell division, chromosome partitioning]; COG2177"
                     /db_xref="CDD:441780"
ORIGIN      
        1 mkfdlatlra liagdhhadr vvppsgftaq ltvfaaaama flavfalals laagrlaerw
       61 geelarsati rivapldqrv aqtdaalril ettkgvasar alsdaeqqal lapwfgadla
      121 ldslpvprli eviedsdgmd paglrlrlaa evpgavlddh srwraplvqa asrlrllgwv
      181 sialittava amitlaanaa laanaqviav lrlvgatdey ialafirrft lralsgaagg
      241 aalgmlavll lpsasetggf ltglgfkgah wlwpicipil agivafaatr aaarrtlrel
      301 a
//
LOCUS       WP_284370281             554 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Algimonas
            porphyrae].
ACCESSION   WP_284370281
VERSION     WP_284370281.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 554)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 554)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..554
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=60012
     Region          26..532
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 msrvklsrqs avrladvnhm avsegririr islviflami cvvlvrladv alfspdahlr
       61 erpaaildmr adltdrngvi lattlssfsl yaepsriwnp aetaaalasi rpdlnvarvt
      121 kqlasdrafv wvdrglspke rqaifdlghp glgfrtepkr vypnaplaah ligwtdidla
      181 gaagaerafd krlgadnape lalsidarvq havteelkas ivhfsalsga aivmdiqtge
      241 liafvsapdf nsnafgaasp eqrfnhasms tydlgsvfkp ltiamvledk latrdemfdv
      301 hkpykvlnkf irddhpssvp lnldfvlaes snrgtamlaq rigaerqqyw lrqlglldrv
      361 pfelaesarp qiqknwgema tvtvsyghgl svsplalvaa igaalndgvy vaptilkrha
      421 thrpetrrvf ssavsqdlae mmrltvtdgt grkanisgfg vmgktgtaek pmrggydtdr
      481 lvtsfvaafp hsspryamiv tldepkaveg thgyatagwn aaptagaiie rigpmlpgar
      541 dvpqfaanqm eafq
//
LOCUS       WP_284370301             282 aa            linear   BCT 25-DEC-2024
DEFINITION  urea carboxylase-associated family protein [Sulfitobacter
            pacificus].
ACCESSION   WP_284370301
VERSION     WP_284370301.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10558624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..282
                     /product="urea carboxylase-associated family protein"
                     /calculated_mol_wt=31077
     Region          49..228
                     /region_name="DUF1989"
                     /note="Domain of unknown function (DUF1989); pfam09347"
                     /db_xref="CDD:430546"
ORIGIN      
        1 mtentpsdae arraiqpvic ypvetlpqpd malyaqarae lrktdevlvp prdastftvp
       61 aghffrissv eaaqvgdlnl wnakdlsekf ysgktralhg thittgqqmw ssfphlrpmt
      121 titrdtldwy gidafggsvh dvigtrcdpy thhllkggqy hhcchsnltr alaahldvpl
      181 aeaephvhdv lnvfmctgft rdtgqyfmka spvrpgdyle ffaeidllga lsacpggdcs
      241 aehssdvarc ypllvevfap eldvlkarad nhvngydrth gl
//
LOCUS       WP_284370355             387 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Sulfitobacter
            pacificus].
ACCESSION   WP_284370355
VERSION     WP_284370355.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..387
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42326
     Region          81..364
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrrfgkwlgr fllvlvlval avglwkreei trllavnslf sedkivhnfs nmdaaflntp
       61 vnrgagptse ltygdeyapp aavetwiker svtalvvlkd gqiayenyfl gtqpddlris
      121 wsvaksylsa lvgilleega iasiddpvtk yaprlkgtay dgttlrnvln masgvtfded
      181 yldknsdinr mgrilalggk mddftaelte tfaapgagwk yvsidthvvg mvvrgatgkp
      241 iaellsekvv aplglehspy yltdgvgtaf vlgglnlttr dyarfgqmfl qegmwqgqqi
      301 vpaqwvrast ipsaptadge igygyqwwip vgaapgeyma rgiygqyiyi dtarnvviat
      361 naadrkfrea gvsqqninif reiaqgl
//
LOCUS       WP_284370448             121 aa            linear   BCT 25-DEC-2024
DEFINITION  6-pyruvoyl trahydropterin synthase family protein [Algimonas
            porphyrae].
ACCESSION   WP_284370448
VERSION     WP_284370448.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Phillips,G., Grochowski,L.L., Bonnett,S., Xu,H., Bailly,M.,
            Blaby-Haas,C., El Yacoubi,B., Iwata-Reuyl,D., White,R.H. and de
            Crecy-Lagard,V.
  TITLE     Functional promiscuity of the COG0720 family
  JOURNAL   ACS Chem Biol 7 (1), 197-209 (2012)
   PUBMED   21999246
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Colloc'h,N., Poupon,A. and Mornon,J.P.
  TITLE     Sequence and structural features of the T-fold, an original
            tunnelling building unit
  JOURNAL   Proteins 39 (2), 142-154 (2000)
   PUBMED   10737935
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..121
                     /product="6-pyruvoyl trahydropterin synthase family
                     protein"
                     /EC_number="4.1.2.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13641
     Region          3..107
                     /region_name="QueD"
                     /note="6-pyruvoyl-tetrahydropterin synthase [Coenzyme
                     transport and metabolism]; COG0720"
                     /db_xref="CDD:440484"
ORIGIN      
        1 mlfeiekdfq feaahyfvhd dandlfkrvh ghsfrgtvtv rgnaqdekgw vrdlwkieqi
       61 vkdvvspldh allndvegle qpaleqiaaw iferlgpklp glhcvevgrp scgerariva
      121 p
//
LOCUS       WP_284370509             467 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Algimonas porphyrae].
ACCESSION   WP_284370509
VERSION     WP_284370509.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..467
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50466
     Region          27..464
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mtcdltrrht liglaassll mpacqpssrk ldadvivlga glsglytaml ledsgftvrv
       61 iealprvggr mftldhgdgy tegggqqiga syarvldvaa elgvplyaet grgpatshyl
      121 ndawqlgsvd ipvfpepfrn tppgsvlfrl lartpgfdrp dgwldpapel disaaqfltq
      181 ngfsqaaqgl idralnandl ssysmlnlhr twqlyqqsag mgatqyvegg sqrlpeamaa
      241 slnqpvltdh pvteialeag rgtvrtsrgs ftgahivctl pfpalrrirl sgfdtplplt
      301 eaidglaytq imqvhmrakt dywttddlap slwtdtdler vfadsgrdgs lsgfqrgwvn
      361 gtgvahwmhd tasaqqryvq rlaelrpasq gqldplalid wttnnpfagg ayyhwqpgqa
      421 arfgrdmgrp igplrfageh lgllhtgmea amesaertal diiegnt
//
LOCUS       WP_284370527             523 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA synthetase [Algimonas porphyrae].
ACCESSION   WP_284370527
VERSION     WP_284370527.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..523
                     /product="acyl-CoA synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016405 - CoA-ligase activity [Evidence
                     IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0032787 - monocarboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=57156
     Region          19..507
                     /region_name="FACL_FadD13-like"
                     /note="fatty acyl-CoA synthetase, including FadD13;
                     cd17631"
                     /db_xref="CDD:341286"
     Site            order(172,175..180,182..183)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341286"
     Site            order(175,292..293,313..318,398,410,413,424,504)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341286"
     Site            order(175,215..216,265,267..268,271,292..293,313..318,398,
                     410,413,421..424,485)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341286"
     Site            order(215,267..268,271,292,421..423,479,485)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341286"
ORIGIN      
        1 mtqkaysdfn qvidwieyha atkpdaramv dlasqrvfty admhervara agmlkdrgia
       61 pgdrvaflcl nttdvmelif acwrvgavcl alnfrltppe liyilndsea slvlvdepfa
      121 gvakasveac psvkcwihtt gvgkdsdyea glaqaspvyd fhpqtyseqa llmyssgttg
      181 hpkgviithg mieftnagam rvgdarpdrv slnnmplfhi gglgvtalpc lwiggccvim
      241 rifdvdatlk aiddpdlsva vlfmvpaayn amrlhpdidk idfsrieial gggetvpepl
      301 shfwlekglv iqegygmtet caagttlrke diphrigsag rplshsrirv vdengqevpr
      361 gqtgeilfkg asvtpgywrn peanaasftd dgwfrsgdig rmdadgyvyi edrvkdmyis
      421 ggenvypaei esvifempqf selavigvph ekwgetgcvv gvleqdqsct lddvlahlqg
      481 rlaryklpgh lhivtelprg gsgkvlkyql rksvpdmlrq sas
//
LOCUS       WP_284370572             420 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Sulfitobacter pacificus].
ACCESSION   WP_284370572
VERSION     WP_284370572.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..420
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45611
     Region          5..409
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mslnehrlsn gfrivtehmp glasasigvw vaaggrhetp qqngiahfle hmafkgtakr
       61 tslqiaeaie dvggyinayt srevtayyvr vlendvalgl dviadilrnp vldpneieve
      121 rgvilqeigq aldtpddvif dwlqeqaypg qalgrtilgp servsnfsrt dlqgfikdhy
      181 gpeqmilsaa gavdhdeivq laeklfgdmp akplfqmdta sfkggevrqn kqleqahfal
      241 gfespgyrad diyvaqiyas algggmssrl fqeirenrgl cytifaqaga hadtgmmtiy
      301 agtsaeqlpe lagitidemk raasdmspae vararaqmka gllmglesps nraerlarli
      361 qiwdrvpslk etiekidavt tgdvrdlaqr maadapaala lygpvekapg lgtlqerraa
//
LOCUS       WP_284370636             402 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal-phosphate-dependent aminotransferase family protein
            [Sulfitobacter pacificus].
ACCESSION   WP_284370636
VERSION     WP_284370636.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Koper,K., Han,S.W., Kothadia,R., Salamon,H., Yoshikuni,Y. and
            Maeda,H.A.
  TITLE     Multisubstrate specificity shaped the complex evolution of the
            aminotransferase family across the tree of life
  JOURNAL   Proc Natl Acad Sci U S A 121 (26), e2405524121 (2024)
   PUBMED   38885378
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Koper,K., Han,S.W., Pastor,D.C., Yoshikuni,Y. and Maeda,H.A.
  TITLE     Evolutionary origin and functional diversification of
            aminotransferases
  JOURNAL   J Biol Chem 298 (8), 102122 (2022)
   PUBMED   35697072
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..402
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43198
     Region          13..401
                     /region_name="PucG"
                     /note="Archaeal aspartate aminotransferase or a related
                     aminotransferase, includes purine catabolism protein PucG
                     [Amino acid transport and metabolism, Nucleotide transport
                     and metabolism]; COG0075"
                     /db_xref="CDD:439845"
ORIGIN      
        1 msrsptlahg raylaipgps vmpdavlqam hraapniyag elvemmpsla adlkrvartr
       61 hqvamytgng haaweaslan ilqpgdkvlv patgrfgigw getakglgae vetidfgkqs
      121 pmdmtrieev lradkshnik avlavhvdts tsirndisal rqtldavghp allmadcias
      181 lgcdrfemde wgvdimvtgc qkglmvppgm sfvffndkae aaraklprvs wywdwtprah
      241 aeeffqyhag tapthhlygl rtaldmihae gienvwarhs tlaravwaac evwgttgsfa
      301 mnvtdpayrs navtslrlqs pdatalrdwv eqqlgltlgi glgmatpgdp awhgffrlgh
      361 mghvngqmim gmlggieagm ralnidhgtg aldaaaevig gg
//
LOCUS       WP_284370842             185 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Sulfitobacter pacificus].
ACCESSION   WP_284370842
VERSION     WP_284370842.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469162
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..185
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=20412
     Region          62..178
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Site            order(66,69..70,73..74,76,100,103..104,107..108,110..111,
                     134,137..138,141..142,145)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          66..93
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          98..128
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          133..161
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrnlpvnlkr hlaalgafvl lcstgfagtv apevfdrlkn aneidaprva keielewsks
       61 gsaamdlllr rgrealsdgq yplaiehlta ltdhapdfae gfharaeayf ranlygpald
      121 dlettlalnp lhyeamfglg vilqefgdlr raaqlyrkvl aiypshensr ealsrlkrdg
      181 igrel
//
LOCUS       WP_284371035             456 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Algimonas porphyrae].
ACCESSION   WP_284371035
VERSION     WP_284371035.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..456
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=50780
     Region          181..414
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mmsatyqtgy ahtqlqqrny alfgllrgae salwvliilf fsgaiigltf asaealdqgd
       61 spfarmlwyp iyaivagfml lqlpktlrli arnpliiicv lwlgltflws idpgvslrrs
      121 ialmmttlag lvfaarydwg emlqrigvav lilclitlvv alanptrgim qeihpgawrg
      181 pwaeknylgg imakgfavsl cafamrpgrf wvwiptgmlc flimllstsk tallaamgcf
      241 alflivrvfr rfpflrvpvi wavivgtagl vllltvgfew alsligkdpt ltgrtdiwil
      301 lgraieqkfw lgygygvfwq dplgpsyetr tvlqwdvpta hngwldswls ggvviialfg
      361 slllatviks ltriktggve tywlvlsvff filfslsesa ilqqndiswf lfvattaklw
      421 andpawwrrg srgeklgsva rvgihrpshn rytlsl
//
LOCUS       WP_284371101             616 aa            linear   BCT 25-DEC-2024
DEFINITION  ABCB family ABC transporter ATP-binding protein/permease
            [Sulfitobacter pacificus].
ACCESSION   WP_284371101
VERSION     WP_284371101.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 616)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..616
                     /product="ABCB family ABC transporter ATP-binding
                     protein/permease"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67557
     Region          20..616
                     /region_name="ATM1"
                     /note="ABC-type transport system involved in Fe-S cluster
                     assembly, permease and ATPase components
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5265"
                     /db_xref="CDD:444078"
ORIGIN      
        1 mpsdtsqaap qatskpplqp pdidaeerqs gflvlrkvap ylwpadmpwv krrvlwamaa
       61 lfisklvsvi tplfyrdavd alagegvpmv aigaigltva ygmarlmtvg fqqlrdavfa
      121 rvgqralrml aletfehihr lsmryhitrk tgglsriier gvkgvefllr fllfnigpli
      181 lellmigavl tylfdwtyll vvavtialyv wftfaitewr vrqrrqmnaa dtdanqkavd
      241 sllnyetvky fgaegreaar ydramagyee aaiktslsla flnfgqslii taglvavmvm
      301 aaigvqngtl svgdfvmvna ymvqitvpln flgtvyreir qalvdmgqmf glleqpaeis
      361 dkkdaaelqv tggqvtlenv hfgydpdrai lkgvtleakp getvaivgst gsgkstigrl
      421 lfrfydvgsg alkidgqdlr dvtqlslhra igvvpqdtvl fndtigynig ygregatqaq
      481 ieaaardaqi hdfivglpdg ydttvgergl klsggekqrv giartllkdp pillldeats
      541 aldsetehei qdalnragqg rtvltiahrl stiaeadriv vlekgeiveq gthddllaqd
      601 gryaqlwhrq qsedqa
//
LOCUS       WP_284371139             232 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF1223 domain-containing protein [Sulfitobacter pacificus].
ACCESSION   WP_284371139
VERSION     WP_284371139.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 232)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..232
                     /product="DUF1223 domain-containing protein"
                     /calculated_mol_wt=24941
     Region          1..232
                     /region_name="COG5429"
                     /note="Uncharacterized conserved protein, DUF1223 domain
                     [Function unknown]"
                     /db_xref="CDD:444181"
ORIGIN      
        1 mkqilpaffa amltsalpvv aqdmpvvvel ytsqgcsscp padailhela arddvialal
       61 hvdywdyigw kdpfgdpaha arqrayaaag nrrsiytpem ivggttdivg akpmklakai
      121 aehasqpeqv emalsrsdde lriqaraigk vrgtltvhml rytpihttri krgenrgktl
      181 enanivegwt vlgtwdgkap lslktaiagd kpavvilqea nagpivaaar lr
//
LOCUS       WP_284371157             237 aa            linear   BCT 25-DEC-2024
DEFINITION  heme-dependent oxidative N-demethylase family protein
            [Sulfitobacter pacificus].
ACCESSION   WP_284371157
VERSION     WP_284371157.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Ortmayer,M., Lafite,P., Menon,B.R., Tralau,T., Fisher,K.,
            Denkhaus,L., Scrutton,N.S., Rigby,S.E., Munro,A.W., Hay,S. and
            Leys,D.
  TITLE     An oxidative N-demethylase reveals PAS transition from ubiquitous
            sensor to enzyme
  JOURNAL   Nature 539 (7630), 593-597 (2016)
   PUBMED   27851736
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10571292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..237
                     /product="heme-dependent oxidative N-demethylase family
                     protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=26293
     Region          28..234
                     /region_name="DUF3445"
                     /note="Protein of unknown function (DUF3445); pfam11927"
                     /db_xref="CDD:463399"
ORIGIN      
        1 mavilqnalp demlqpqalp gvspcaaddw lrvdeayaaq mayratlmae kpdavlwmsp
       61 aalpaaqevl qealgilppl gfdvqrdhvi cpdgrcvvld gddplhtlgh lvqqdicvle
      121 krgaehvlta aivcfpanwr ladkvdrpls aihdpvaeyd adltrrvqrm fngvragrpl
      181 wrfnrlsyvd adlhqpfrka sgdiekftrs erqcilrlpr teavvftiht hvvpkig
//
LOCUS       WP_284371235             493 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Algimonas porphyrae].
ACCESSION   WP_284371235
VERSION     WP_284371235.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..493
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54535
     Region          10..297
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mtirtrnihl sdanwaaali gtllvfrivm lmlsasglhg deaqywawsl dpdfgyyskp
       61 pliawiiwvs tsifghaewa irlaspflht gtailtylta srlfgsragl iacalyilmp
      121 gvalsaslis tdaallffva lfihswirlr ertdwrwvim lgvalslglm akyamiyvlp
      181 afglallfda rsrasllglk gavaaivaaa iitpnliwnq qhsfatlqht tdnanmgdgv
      241 qlnplelief vvgqlgvfgp itfilllial wrlrldrtsf rlwlavlvlt plsviclqal
      301 lsrananwaa aayaaapvll aawaihsqqt lrwvmaglav nlllsivppl vltspaltdr
      361 lgfanavkrq rgwpetveri teqfaagdyd avavdnrlmf yaltyydmeg taplfmwrye
      421 prlnnhaemt rplpeddrsv llisyyptya dyfardfeql trlgeieidl gggksralia
      481 yaaqgykgpv ard
//
LOCUS       WP_284371251              68 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Sulfitobacter
            pacificus].
ACCESSION   WP_284371251
VERSION     WP_284371251.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 68)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..68
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=7509
     Region          5..64
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mddlsfpktg fvrlaqilap ngpipvskst wwagvkegrf pqpqklgprt tvwkvedira
       61 lfeddqdg
//
LOCUS       WP_284371258             476 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Sulfitobacter pacificus].
ACCESSION   WP_284371258
VERSION     WP_284371258.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 476)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..476
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=51432
     Region          5..467
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mdwedfrtrg kdaadwaady haglrerpvr aqtkpgdiia qlppsapeqp etidailndl
       61 ehkimpgmth wqhprffayf panaapvsvl aesyvtaiaa qcmlwqtspa ateletrtcd
      121 wmrqavglpd gfsgviqdsa statlcavlt mreraldwag nraglsgqpr lriyasgevh
      181 tsidraiwia gigeanlvri pvtgpsramd vtalqaaita draaghlpag iitcvggtgv
      241 gatdniaavm diaeseglyt hvdaawagaa micpefqdiw agvaradsvv lnphkwlgaq
      301 fdctthflrd ptslvrtlai qpeylksdga dggiinysew svplgrrfra lklwfllrah
      361 gldglrgmir nhvkwakgla gllaetadfe ivtepmlslf sfryapdgva dldalnqqlv
      421 nainadgriy ltqtrvdgdl virfqagsws ctaediataf dviielapkv aaqmsa
//
LOCUS       WP_284371286             751 aa            linear   BCT 25-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Algimonas
            porphyrae].
ACCESSION   WP_284371286
VERSION     WP_284371286.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 751)
  AUTHORS   Shan,L., Mathews,I.I. and Khosla,C.
  TITLE     Structural and mechanistic analysis of two prolyl endopeptidases:
            role of interdomain dynamics in catalysis and specificity
  JOURNAL   Proc Natl Acad Sci U S A 102 (10), 3599-3604 (2005)
   PUBMED   15738423
REFERENCE   2  (residues 1 to 751)
  AUTHORS   Polgar,L.
  TITLE     The prolyl oligopeptidase family
  JOURNAL   Cell Mol Life Sci 59 (2), 349-362 (2002)
   PUBMED   11915948
REFERENCE   3  (residues 1 to 751)
  AUTHORS   Polgar,L.
  TITLE     A potential processing enzyme in prokaryotes: oligopeptidase B, a
            new type of serine peptidase
  JOURNAL   Proteins 28 (3), 375-379 (1997)
   PUBMED   9223183
REFERENCE   4  (residues 1 to 751)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 751)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..751
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..751
                     /product="prolyl oligopeptidase family serine peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=82213
     Region          44..746
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 msprnttrnf ltatamalvl aacsnadeas vtettdtaat dmatsdmssp etpstdaaty
       61 vpvayetdgq rdadhlwlee vegeaaldqv kawnevtlne lmadpryetl yndalsilqs
      121 kdripyvsyr ggaahnfwqd etnvrgvwrk ttmdsylsgn tawetvldfd alaeaedknw
      181 vykgnnclsp dytlciinls dggkdavvrr efntetgefv vdgfvtpesk gtmdwvdent
      241 mvvavdfgeg tmtdsgypst ariwtrgtpl aesveigrgn qtdvgywpgv felsdgrrei
      301 vvsqsetfyd tnyfwfprna dgtvgdavpf pipsksnlga efkgqvmlsl nedwrgfnsg
      361 dlvsfaiddf mddgeiadln lvyspdakss lggygvtkdk vllakttdvk gsvlafdwdg
      421 etwtsepial pengaagvga tnpkesiafl saedfltpdt lytidtsada ltpvaakslp
      481 dwfdasnmvs eqkfatsadg tqvpyfivrs kdtamngenp tllygyggfe islnpsysat
      541 rgklwlengg vyvlanirgg geygpnwhqa glkterqriy ddfiavaedl ietgvtspdh
      601 lgieggsngg lltgvmttqr pdlfnaaiia vplldmqrfh kllagaswmg eygnpddave
      661 gaflrqispy hnirededyp evflitstkd drvhpghark famrmqdqgh dfhyyenidg
      721 ghsaaanlke takrlalqhv yllqkladda s
//
LOCUS       WP_284371341             385 aa            linear   BCT 25-DEC-2024
DEFINITION  FliM/FliN family flagellar motor switch protein [Sulfitobacter
            pacificus].
ACCESSION   WP_284371341
VERSION     WP_284371341.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13389420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..385
                     /product="FliM/FliN family flagellar motor switch protein"
                     /calculated_mol_wt=41028
     Region          130..290
                     /region_name="FliN"
                     /note="Flagellar motor switch/type III secretory pathway
                     protein FliN [Cell motility, Intracellular trafficking,
                     secretion, and vesicular transport]; COG1886"
                     /db_xref="CDD:441490"
     Region          229..290
                     /region_name="FliMN_C"
                     /note="Type III flagellar switch regulator (C-ring) FliN
                     C-term; pfam01052"
                     /db_xref="CDD:460043"
ORIGIN      
        1 mdttlhrkaq agraehqara mslakalrlt lakvaedkfe msmaalslrn qtcpgekidq
       61 hlsetdllml fdgpggrraa vmmdpalvga liqqqtmgkv lavndsadrp mtptdaaiaa
      121 pfldallqra apvpedpddq klisgfrfga wvedarvlam sldapdyqli hidvdisggi
      181 rqgrimmcmp lgqevesaak pgdspaedkp dldppqrvtl setvmkltvd lrislakmrm
      241 plrdlgklav gdvldlgaad fskvrvqtla graigrgtlg qldgvravqv aatsdvtqnl
      301 qrrasdrdhm nlpdisgpaa eadephgmpd lpelpdlpdl tggegegata padslpdlpd
      361 lpdmsdlpdf deapdlpelp elnvg
//
LOCUS       WP_284371350             269 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Algimonas porphyrae].
ACCESSION   WP_284371350
VERSION     WP_284371350.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..269
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29794
     Region          98..209
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 msdfscplcs gssyvileae adwlvrakra dderrmigai vagdpdlsfg givrceacgl
       61 atvrtppapd algrfysayy asasygtkrd kkirraakrv rrlqrqirsd grrfldvgan
      121 lgyavegarq qgfdatgiei dgeavaraqa dfprnryiet tveafaaqgq rfdlvycsev
      181 iehaldiraf atalmdlvap ggvlfvttpa dghratpdpl vswvqvkppe hlhwfakshl
      241 lslfdrpdfv prfwfnhkpg hklvlrrda
//
LOCUS       WP_284371357             706 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Algimonas porphyrae].
ACCESSION   WP_284371357
VERSION     WP_284371357.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 706)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 706)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..706
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77778
     Region          48..702
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mrksalilst ilanaglvap afaddgpfdd eviatgtyls idkinavktp tpiidipqsl
       61 tiitaetird qsfqsigdit ryspgvnisq geghrdaiii rgnqttadff qdgvrddvqy
      121 yrplynlqqv eilrganall fgrggvggiv nrvtktadst dsfttldasi dtfgaaygav
      181 dynqplsdrv glrvngfves lnnhrdffdg drfginptlg ielgpqtald lsyeyldddr
      241 vvdrgvpsvn vatgpdvple gfdntffgsp dqnfttlqah ilrgradhqf ndmlrgnvtl
      301 qyadydkvyq nlyaseevvl tngifpqvel dgyrdttdrn nfvaqanlvg efdtgpight
      361 vlvgveyasq htdnarldnv faqnnddqlf ipfsdplnip afgftdpard rksnvyvlsa
      421 yaqnqidltd qfkvvlgarf dsfdidvtdi qnnaqftrkd eeitprigai fkpvdnmsfy
      481 asysetftpr sgdqfltldl dtastrpqft enleagakwd vrpdlsvtaa ifqldregft
      541 sidpnnqqql itidgasvkg lelqligqlt qawsinagys yldgevedls faggvvgagg
      601 ldgneprqtp thtlsvwnny qlndrlglgl gatyqdsyfv rednsvevpd fvrvdaalfy
      661 dvsddlrlql nvenlfdtdy fpdahsndni stgapinarf tvmsrf
//
LOCUS       WP_284371365             266 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Algimonas
            porphyrae].
ACCESSION   WP_284371365
VERSION     WP_284371365.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..266
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29492
     Region          31..240
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mvrstlfnlf fyaatalyal vgvvlslvpg rallmgglrr ytkvirwgmr viagitvdvs
       61 ghervphdgp viiaakhqsy gdgiimfhqf ddlsfvtgdh lekfwlikvi lakmnavvve
      121 scggpatrar maetsrvvre qgrriliype ghlsqvgshh pykkgvwhlq qefdcpvvpv
      181 atnlgqrwnq sdwikhpgha kvefldpipp glgkdefmai lqdrietrsi amldhedpga
      241 lnpddigtvq lnpvaqarad rqkanp
//
LOCUS       WP_284371418             394 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Algimonas porphyrae].
ACCESSION   WP_284371418
VERSION     WP_284371418.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..394
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42048
     Region          31..389
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mklflkillg fillialaig ilwfaakqsn kpgppadplt slddaglkaa idgiaaerkl
       61 vgmaakvmvg gdviaqavtg wrtkdeqtal qlddlyhmgs igksmsatai arlveagams
      121 wddtlgsrls dmemdaawad vtlsqlltht asiprgpisg minqvsepvr laevrremaa
      181 tllsepprva pgsafaysne gfmlaslmae eatgehweti irtqlaapls mdrlgfgapt
      241 gedtaevpwg hrklgpakia adpseaadnp pwmaaagtmh mglddllsya qahldagqss
      301 qailspatfe rlhtpdmndy aygwvvqsrd lgdgpepviw hngsntmwya llvllpdrna
      361 aitlvtndgs qlsltqrrfd afameiaeai strg
//
LOCUS       WP_284371470             489 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Algimonas
            porphyrae].
ACCESSION   WP_284371470
VERSION     WP_284371470.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..489
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51668
     Region          1..474
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mesliqwvnn qvwgwpmlgl llltgafltv glrfisiyki pyafkqlfrk rgantddgdv
       61 spfaalmtal sstigtgnia gvaaaiaigg pgavfwmwvt avlgtatkfs egvlavryre
      121 idsngnrvgg pmyyiknglg skwmplallf sffgmfaswg tgnsiqansv advlnaeynl
      181 spwitavfla ggaaavilgg ikrigsvask vvpfmagayi llgllvvimn isavpgafst
      241 ifkgafglqe agtgisiglm vlamqkgvar gifsneagqg sapiahaaaq nndpvnqgti
      301 amlgtvidtl fvctitalvi ltsgvvspec lagpenyqql mtgmqpagcd tgapltssaf
      361 aaqygemgrh lipialtifa fttilgwsyy gercaafmfs ekailpyrii yiavvffsaa
      421 aialedqign ivnlfwlmad tltglmaapn lialiflspv vfkltrdyfd rdkeatdgli
      481 dqddlprgs
//
LOCUS       WP_284371484             229 aa            linear   BCT 25-DEC-2024
DEFINITION  LolA family protein [Algimonas porphyrae].
ACCESSION   WP_284371484
VERSION     WP_284371484.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Tajima,T., Yokota,N., Matsuyama,S. and Tokuda,H.
  TITLE     Genetic analyses of the in vivo function of LolA, a periplasmic
            chaperone involved in the outer membrane localization of
            Escherichia coli lipoproteins
  JOURNAL   FEBS Lett 439 (1-2), 51-54 (1998)
   PUBMED   9849875
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..229
                     /product="LolA family protein"
                     /calculated_mol_wt=25170
     Region          41..215
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mksihtlsaa alialavpaf staqdayapq prvqnasttn lpafthpqsv pqdlarvdgg
       61 lnatgsfqgr ftqygadgsv stgtvhlqrp grvrfeydap npllivsdgv tlvqqdrale
      121 tfdrvplsat plnyflkenv nlardtevig fqklpnqwrv tsrdgsgema gaitlvfdpq
      181 slalmewvia defggtttvr lselqynqal dprlfilrdq redrrdrrr
//
LOCUS       WP_284371591             120 aa            linear   BCT 25-DEC-2024
DEFINITION  HesB/IscA family protein [Sulfitobacter pacificus].
ACCESSION   WP_284371591
VERSION     WP_284371591.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Lu,H.M., Li,J.D., Zhang,Y.D., Lu,X.L., Xu,C., Huang,Y. and
            Gribskov,M.
  TITLE     The Evolution History of Fe-S Cluster A-Type Assembly Protein
            Reveals Multiple Gene Duplication Events and Essential Protein
            Motifs
  JOURNAL   Genome Biol Evol 12 (3), 160-173 (2020)
   PUBMED   32108236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..120
                     /product="HesB/IscA family protein"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=12605
     Region          9..110
                     /region_name="IscA"
                     /note="Fe-S cluster assembly iron-binding protein IscA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0316"
                     /db_xref="CDD:440085"
ORIGIN      
        1 mfgipgkqav titpkaaaqi tklmgsagha glrigikkgg cagmeytmey vdeadpndev
       61 vnqdgacvmi apmaqmflfg teidyetsll esgfkfnnpn vteacgcges ikfddslsvk
//
LOCUS       WP_284371649             262 aa            linear   BCT 25-DEC-2024
DEFINITION  OmpW/AlkL family protein [Algimonas porphyrae].
ACCESSION   WP_284371649
VERSION     WP_284371649.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006882
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..262
                     /product="OmpW/AlkL family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28511
     Region          54..262
                     /region_name="OmpW"
                     /note="Outer membrane protein OmpW [Cell
                     wall/membrane/envelope biogenesis]; COG3047"
                     /db_xref="CDD:442281"
ORIGIN      
        1 mkddpaaset erfrvahhiy dlrnvgqdpr qnketimltp slprqdflks silkttmlcg
       61 liaapfmvap talagsvddp wlvrvrglsv mpdeagttvp lggtvsienq ivpeldisyf
      121 ftenfaveai favtphdvsv ensllgdvdl gdvwllpptv taqyhfnprg kvrpyvgagi
      181 nytaffnads gpvantieys defgwalnag vdipvndiwf anidvkklfl etdvvanagg
      241 livtsdvqid pwivgvgfgr rf
//
LOCUS       WP_284371690             215 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Algimonas porphyrae].
ACCESSION   WP_284371690
VERSION     WP_284371690.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..215
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=22990
     Region          11..214
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mttrnppafp pgfahyplyf spdqqaelid tvkagvaqap ffqptmprtg aplsvvmsnf
       61 gplgwvtdkd dgyryqadhp ktggpwpdlp rllkdlwhdv tdwpglpeac linwyrasan
      121 dgkgakmglh vdndehamga pvvsvslgdp alfriggear ggktaglklf sgdvvvlagk
      181 arrsyhgisk vdygqsalvp hggrinltmr vvgac
//
LOCUS       WP_284371698             279 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Sulfitobacter pacificus].
ACCESSION   WP_284371698
VERSION     WP_284371698.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 279)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..279
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31625
     Region          2..235
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mkfqgtadyv atddltiavn aavtlerpll vkgepgtgkt elakqvsaal glrmiewnik
       61 sttraqqgly eydavsrlrd sqlgeervhd vanyirkgkl weafeadekv vllideidka
      121 diefpndllq eldkmeffvy etgemvkaan rpiviitsnn ekelpdaflr rcffhyiqfp
      181 dmetlkkive vhhpdikesl lttaltqfye irdqqglkkk pstsevldwl klllaedmda
      241 adlkkdgtsa lpklhgallk neqdvhlfer lafmarggr
//
LOCUS       WP_284371728             275 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Sulfitobacter pacificus].
ACCESSION   WP_284371728
VERSION     WP_284371728.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..275
                     /product="metallophosphoesterase family protein"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28924
     Region          16..239
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mrgirhldlg alegpvlvfg gpysnaqama alirvaqarg ipaaqmicsg dvvaycgapa
       61 rtvaqiralg cavvagncei qlgsdapdcg cgfedgsacd llsagwygfa adileeadka
      121 wmaslpdvvs frhqgaryav ihggmtdvar fiwpssstev faqewaaver avgpvdhiia
      181 ghagvpfvkf iprgrwinag vigmpahdgq qgtrfailed gevwienlpy daqgaaedmt
      241 raglpqgyrd gllsgywpse dvlpeslrvt psarg
//
LOCUS       WP_284371937             698 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein [Algimonas
            porphyrae].
ACCESSION   WP_284371937
VERSION     WP_284371937.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 698)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 698)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 698)
  AUTHORS   Porat,A., Cho,S.H. and Beckwith,J.
  TITLE     The unusual transmembrane electron transporter DsbD and its
            homologues: a bacterial family of disulfide reductases
  JOURNAL   Res Microbiol 155 (8), 617-622 (2004)
   PUBMED   15380548
REFERENCE   4  (residues 1 to 698)
  AUTHORS   Kimball,R.A., Martin,L. and Saier,M.H. Jr.
  TITLE     Reversing transmembrane electron flow: the DsbD and DsbB protein
            families
  JOURNAL   J Mol Microbiol Biotechnol 5 (3), 133-149 (2003)
   PUBMED   12766342
REFERENCE   5  (residues 1 to 698)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   6  (residues 1 to 698)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   7  (residues 1 to 698)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   8  (residues 1 to 698)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   9  (residues 1 to 698)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12109673
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..698
                     /product="protein-disulfide reductase DsbD family protein"
                     /EC_number="1.8.-.-"
                     /EC_number="1.8.1.8"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=73642
     Region          43..154
                     /region_name="DsbC"
                     /note="Disulphide bond corrector protein DsbC; pfam11412"
                     /db_xref="CDD:463273"
     Region          304..696
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 mrtvfltllm wlsaatsafa ttslpvdtgk veasllsshy tvapgqtfqi alkttldekw
       61 htywrnpgds gepvqiswvl pdvlsageiv wplpypiptg piinygfega plfpvdftva
      121 dnapigsvle iqadvyylvc kdicipeegt lrlilqvsge aelndanaae iaeainrapa
      181 aidirvsmqa ddgalslqfa dlpstvadgn fadayffpyd ntllahsdpq tvtigsdglq
      241 idttasfgwg egfdtpqqgl lsfdldgert grivtvstga plaigldasr papdgagsig
      301 lisaligafi gglilnlmpc vfpvislkal slaksahaer siarreaway algvfatfal
      361 lviallivka tgaalgwgfq lqnpvvvgli alllfavgln ligaydiagg syqgagatla
      421 grggltgsff tgalavlvat pctaplmasa igyalaqpaf itfivfmala agfaapfvll
      481 ayapgllmkl pkpgpwmvrl revlafpmfa aaiwlvwvvg nqagidglvl vlmamlsfal
      541 avwliqrrgi wkllgvaaiv lavalpftar tvpasasgaa sinlatdvws pdrvaelrad
      601 gravfvdfta dwcvtckvne rlvlktntvk qafidtdtaf liadwtnrnd aiareleayg
      661 ragvplylyy pagdnsvrae vlpqilttdl vvktlkgs
//
LOCUS       WP_284371988             275 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Sulfitobacter pacificus].
ACCESSION   WP_284371988
VERSION     WP_284371988.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..275
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=28707
     Region          3..275
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mpyvrpsdle talslasqpn qgviaggtdv fpasqqgqrf qnlldltavr elagitlses
       61 girigaaarw rdvidadlpa afdglkqaar qvgsvqiqns atvagnlcna spaadgvppl
      121 ltldasveva saargirrlp ldafilgvrq talqpdeimt aimvptppen agssfeklgs
      181 rtylvisiam vaalvfkdag gritfariav gacspvaqrl rrlevscigk rpeeisvtad
      241 hladltpidd vrgsaayrld avaelcqrav kgaar
//
LOCUS       WP_284372113             402 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Sulfitobacter pacificus].
ACCESSION   WP_284372113
VERSION     WP_284372113.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..402
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42025
     Region          2..402
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 mkrvvitgag tinalghsvp atlqamrdgv cgigqlafrd verlqiqigg qvrgfeaegr
       61 ynrqqmslyd rftqftlaaa keaiaqsglt fsgelaaksg vvlgtagggv stwddnyrav
      121 yeegknrvhp fvvpklmnna aashvsmewn lkgpsftvst acassnhama qafsmvrsgm
      181 spamitggse smlcfggvka weglrvmsrd acrpfsanrn gmvqgegagi fvfeeydhar
      241 argadilcev vgfamssdas divmpskaga aramagaled agvsreevgy inahgtgtaa
      301 ndktecaava dvfgphadql misstksmhg hliggtgave llacimalrd gviaptigye
      361 epdpecaldv vpneareaki svalsnafaf ggmnavialr ki
//
LOCUS       WP_284372126             147 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF4870 family protein [Algimonas porphyrae].
ACCESSION   WP_284372126
VERSION     WP_284372126.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007819
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..147
                     /product="DUF4870 family protein"
                     /calculated_mol_wt=16678
     Region          35..138
                     /region_name="COG3671"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:442888"
ORIGIN      
        1 mptedpspsg hwdeveavqr yerelreqed qqtlkpqrgq dnanliyily lvnmavpflg
       61 ivgvimaysa rdhaepdlqs hydnqirifw itvigyiisv vlmlvfigvl lallvfiwki
      121 vrvatamsll srglpvrnve sfsftsd
//
LOCUS       WP_284372158             111 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Sulfitobacter pacificus].
ACCESSION   WP_284372158
VERSION     WP_284372158.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..111
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11995
     Region          4..108
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mpahyiwlff ailtetlgtt alqasqqftr fwpalavvvf yglsfycmsf alrampvgiv
       61 yaiwsglgiv liagigfvlf gqkldmpall glaliisgil iihlfsasnt h
//
LOCUS       WP_284372194              82 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Algimonas porphyrae].
ACCESSION   WP_284372194
VERSION     WP_284372194.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 82)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..82
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8975
     Region          2..70
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 maiqvnldrv lldrkmslte ladrvgitla nlsilktgka ravrfstlda lcrelecqpa
       61 dilewvpegd tppipefsvg kr
//
LOCUS       WP_284372212             395 aa            linear   BCT 25-DEC-2024
DEFINITION  thiolase family protein [Algimonas porphyrae].
ACCESSION   WP_284372212
VERSION     WP_284372212.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 395)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..395
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40846
     Region          6..394
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mnqssdpvvi vgiartpmga fmgslssvta pelgsaaima amneagvead aveqaimgcv
       61 lpagqgqapa rqaalgaglp rsteattvnk mcgsgmqaai mahdaikags vdiavaggme
      121 smsnapyllp karegmrmgn qqvidsmmhd gltdayagga mgvfadeiat eyqftreqqd
      181 ayaiesvrra kaaqgeggfd reltpvtvkt rkgdivvdtd egpgkampek ipnlrpaftk
      241 dgtvtaanas sindgaaamv lmrrsqaeag ghkvlaeivs haahahepak fttapvhamk
      301 kalekaswev ddvdlweine afavvpmiam qemgidhdrv nvngggcvlg hpigasgari
      361 matligemer rdaktgvasl cigggeatav clrrd
//
LOCUS       WP_284372247             444 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Sulfitobacter
            pacificus].
ACCESSION   WP_284372247
VERSION     WP_284372247.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..444
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=48918
     Region          3..437
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 maqamkiaiv ddeqdmrqsi sqwlalsgyd tetfgsaeda lktlgpdypg ivisdikmpg
       61 mdgmqflkkl mgsdsalpvi mitghgdvpm aveamrvgaf dflekpfnpd rmselakkat
      121 narrlvmdnr alrrelsdgg qlmkkligqs pvmerlredi ldlgqadghv lidgetgtgk
      181 tlvahalhav gsragkkfvl vscgaleeem lskrlfgpmq pedaqlpaie earggtlvle
      241 dvealsetlq arllsvineq gtpaetriva isnlqeagrt sedalrsdlf yrlaalritv
      301 pplrqrgedi ltlftrlseq fseeygcdtp qvsaqeaaql lqapwpgnvr qlinvaerav
      361 lqsrrgsgti asllmsdhee mqpvmttegk plkeyveafe rmlidntmrr hkgsissvme
      421 elclprrtln ekmakyglqr sdyl
//
LOCUS       WP_284372406             216 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Sulfitobacter
            pacificus].
ACCESSION   WP_284372406
VERSION     WP_284372406.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..216
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=22841
     Region          4..205
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mggaavkdag riirtdldva egaawlaqqd arfaqalaqt gplplrlkpd gfnglleiii
       61 sqqvsvasan airarmlaag lnteaavlda geeglrgagl srpkiryali laaaeldyag
      121 lhaladrdvm erltaitgig pwsaeiyamf cmgradifpa gdlalqvaaq glfdlparpg
      181 aeelarmaev wtpwrsvaar alfayyrilk nreglg
//
LOCUS       WP_284372495             302 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Sulfitobacter pacificus].
ACCESSION   WP_284372495
VERSION     WP_284372495.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..302
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33232
     Region          4..276
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtemtsidav qkmlgdqgyi cgrdlgtvvf lslrlgrplf legeagvgkt eiakalaagl
       61 nrklirlqcy egldassavy ewnfpaqmva iraaeaagga dtealtadlf sdkylierpl
      121 leamrpdeng apillideld rtdapfeafl lealsdfqvt ipemgtinap eppiviltsn
      181 rtrevhdalk rrclyhwvdy pdfdremeil qarapeaaek lsrevvafvq llrtedlfkk
      241 pgvaetidwa kcllaldvin lspeviadtl gailkyqddi aklqgseakr ildqakasle
      301 pv
//
LOCUS       WP_284372560             454 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Algimonas porphyrae].
ACCESSION   WP_284372560
VERSION     WP_284372560.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 454)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 454)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..454
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48328
     Region          130..440
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mgsifgqsit tlertlrida hldvrtrara riiyatglif ilvqiinvis mhavtggwtg
       61 qqaipliasv falamtamlr ftksatffgl gygiacliai ggsamissvp nypppginta
      121 llpvlcgvsa liafigtrwt allyiaasfg viaallnvtl gygadaamti iawdratqal
      181 iglilvgpic iviahllftn lehldravkr araaesarag flammsheir tplngimgms
      241 dmlaeadipd tekryaklvq vsanslmeii nevldmakle dgtvtiaqdp fspaemlqdv
      301 cdlfsikaah kglwlgtktn gmpefligda phlrqilsnl vgnalkftae ggvqigarlv
      361 svqsgvaitq ffvqdtgvgi peseqahife rfsqtssakm tkekgtglgl sicrelteim
      421 ggtlqlhsvp gqgttfhftl afpmtdaape rlla
//
LOCUS       WP_284372563             462 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Algimonas porphyrae].
ACCESSION   WP_284372563
VERSION     WP_284372563.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 462)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..462
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=49624
     Region          152..440
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mwghintlil glidwmdlpe dmpaanrira rlfciaslsf ilvalfnffg lswafgistp
       61 hhlvsffmas sggifllllr rfkdpialsw gfaiastlgg wlsayidyaa ateitgigla
      121 yspymvailv ivcllgnrqv aifyaglcvm tligfyamtv algfdvgllt qnrlslvlrs
      181 sailltlaim apvsqmiyrt lddvedardr araaeetrsg flatmsheir tplngilgms
      241 dmlakadipd tekryaklvq vsanglmeii nevldmakle dgtvkiaqdp fspaeviqdv
      301 cdlfavraae kdlwigsevg glpgqligda phlrqimsnl vgnalkftpe ggvragaklv
      361 svqsgtamiq ffvqdtgvgi aaeeqtnifd rfsqtssakt tkekgtglgl sicreltekm
      421 ggtlalhsqv gqgttfhftl alpltakqtq ataeplgvqs ga
//
LOCUS       WP_284372659             397 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Sulfitobacter
            pacificus].
ACCESSION   WP_284372659
VERSION     WP_284372659.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..397
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42518
     Region          15..388
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 msevfkgsft qqepipedgi eaavdvmrsg rlhryntaeg elsqtalleq efaaqvgaky
       61 clavasggya matalravgv kpgdkvltna ftlapvpgai aavggvpvfv gvtdqlvidl
      121 ddlaaqagqa dvlllshmrg hladmealma lcddagvivi edcahtmgas wrgvpsgtqg
      181 kvgcyscqty khvnsgeggl fvtddpevaa ravilsgsym myekhlagpp aeayaqirye
      241 tpnisgrmdn lraailrpql rkldaqrvrw neryfaietg lrdtpgltvi erpadevimg
      301 ssiqfllqgw satnveavla rclkrgvelk wfggaepvgf tsrydswryv dapampksdv
      361 vlagivdmrv pltfsledca liariikaev savyqgs
//
LOCUS       WP_284372734              85 aa            linear   BCT 25-DEC-2024
DEFINITION  BolA family protein [Sulfitobacter pacificus].
ACCESSION   WP_284372734
VERSION     WP_284372734.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..85
                     /product="BolA family protein"
                     /calculated_mol_wt=9176
     Region          1..83
                     /region_name="BolA"
                     /note="DNA-binding global transcriptional regulator BolA,
                     affects cell shape, cell division and biofilm formation
                     [Transcription, Signal transduction mechanisms]; COG0271"
                     /db_xref="CDD:440041"
ORIGIN      
        1 msktqeiear lraalsprel dvvddseshr ghagfqegge shfnvrirae afaglsriar
       61 hravhgaigp elmgrihala ldldv
//
LOCUS       WP_284372767             219 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-L-isoaspartate O-methyltransferase family protein
            [Algimonas porphyrae].
ACCESSION   WP_284372767
VERSION     WP_284372767.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Edwin,R.K., Challa,N., Sharma,R., Satyamoorthy,K., Parsa,K. and
            Misra,P.
  TITLE     PIMT/TGS1: An evolving metabolic molecular switch with conserved
            methyl transferase activity
  JOURNAL   Drug Discov Today 27 (8), 2386-2393 (2022)
   PUBMED   35462043
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Furuchi,T., Sakurako,K., Katane,M., Sekine,M. and Homma,H.
  TITLE     The role of protein L-isoaspartyl/D-aspartyl O-methyltransferase
            (PIMT) in intracellular signal transduction
  JOURNAL   Chem Biodivers 7 (6), 1337-1348 (2010)
   PUBMED   20564550
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Kagan,R.M., McFadden,H.J., McFadden,P.N., O'Connor,C. and Clarke,S.
  TITLE     Molecular phylogenetics of a protein repair methyltransferase
  JOURNAL   Comp Biochem Physiol B Biochem Mol Biol 117 (3), 379-385 (1997)
   PUBMED   9253175
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..219
                     /product="protein-L-isoaspartate O-methyltransferase
                     family protein"
                     /EC_number="2.1.1.77"
                     /GO_function="GO:0004719 - protein-L-isoaspartate
                     (D-aspartate) O-methyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0030091 - protein repair [Evidence IEA]"
                     /GO_process="GO:0036211 - protein modification process
                     [Evidence IEA]"
                     /calculated_mol_wt=23359
     Region          15..211
                     /region_name="Pcm"
                     /note="Protein-L-isoaspartate O-methyltransferase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2518"
                     /db_xref="CDD:442008"
ORIGIN      
        1 mpqfdfdaar etmvesqirt advtdldlla afrrtprekf vpanrmalay gdavvdygdg
       61 rsllrprdfa klvqaadika nevvldlgca rgystailaq iaetvvglet dedrvtratd
      121 lltdigvlna avvqgdlkrg aaehgpfdvi ivngavsavp qawfgqlang grlavimrdg
      181 pigratlytk sgdavgdrvv fdanapmlsg fevepsfvf
//
LOCUS       WP_284372769             559 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Algimonas porphyrae].
ACCESSION   WP_284372769
VERSION     WP_284372769.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..559
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=59269
     Region          22..364
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mltlkhmiap icltallacs pavtepvpgd ddfasealsl lrdaypedgp gaaaivtkdn
       61 etlfidghgl adlaegrpiq antvfryasi tkqfaaatlm llaedgrvdl dapignylpd
      121 ypepgraiav rhllnhtsgi psytgipgwm aetntarayt tdemvavfed lpadfapgdq
      181 faynnsayll lgavieavtg qswsdavkdr itkplgidti esgllegeid rmatgytagn
      241 aasqrihmsv phaagaligd vqgladwana fhdgevvsae syaamtrptv tndgedvpyg
      301 yglsfaelrg hptighsggi fgfstdsvyi psedifvavl ansdnpatsp gmmtvklaal
      361 aldapfplfe tmdidlagle pvlgvykset vtrtlfvrdd ilytlregga espvysagnn
      421 rffygpasls wfeienpsdg pvrmvfhssd slepdtlswt gpvpdmitvs pdiletylgt
      481 ytlsipmiat iaaqdegldn gitiqltgqp pfslqpssdt efavpsvgav vrfapddags
      541 mtmeilqggq titgemtde
//
LOCUS       WP_284372867             471 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Algimonas porphyrae].
ACCESSION   WP_284372867
VERSION     WP_284372867.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..471
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50316
     Region          52..468
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtsnltasar giapllfglt llsgcetvpp avavpeltat seaatneaac hvtapvpspa
       61 idktfsadmd rlmthmidrg iapgaviain rngetiftqa ygyadletgk pmttdslfri
      121 ysmtkpvtti aalqlvdrgl ialddpisdh lpdfakirva tdetgtnvra psraptvrdl
      181 mrhttgltyr tgakadpiaa yyaelgipag pgvsdvptng mdpvigndgf isrivqaplk
      241 hdpgqgftyg nstdvlgalv akvsgqplse ymqdnifdpl gmedshfrit pdrigdftsa
      301 yivppqapsg spidynlpid elqpqtpyrl dpydsslyak apdfefggag lvsdaddyla
      361 ftqalidaep rlvsetlwqe atrdqlsaea rasaaflgkr gfglgfavrd aetlvapvfp
      421 qcglfwagaa styfwideet dttgvfmtqv fesdvrsyfg eilariyaeg g
//
LOCUS       WP_284372886             249 aa            linear   BCT 25-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Sulfitobacter pacificus].
ACCESSION   WP_284372886
VERSION     WP_284372886.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Pereira,J. and Lupas,A.N.
  TITLE     The VCBS superfamily forms a third supercluster of beta-propellers
            that includes tachylectin and integrins
  JOURNAL   Bioinformatics 36 (24), 5618-5622 (2021)
   PUBMED   33416871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..249
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=27224
     Region          90..157
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mrgglvawll wlmaaplcaq vitsaeynep ttryahgvlg davewgnmtv tvrretsqpg
       61 avfqtwttqs yhlrlpevlv yedtaprlad ldgdgrpeii vveshrdkga rlavyglkdd
      121 gvpallawts figqrnrwma pvgvadfdgd gtidiavvdr phlarrlfvm rygigkmksf
      181 ailepvtnhr igddyisggv rncgagpemi lldagwtqil tvrwgdggfq arvlapyegr
      241 esvaqalac
//
LOCUS       WP_284372939             433 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Sulfitobacter
            pacificus].
ACCESSION   WP_284372939
VERSION     WP_284372939.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 433)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..433
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46497
     Region          25..421
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(133,135,261,263,297..299,343)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mslrnalgaa tavslitasg afaetltiat vnngdmirmq gltadftekt ghevewvtle
       61 envlrqrvtt dittkggsfd imtigmyetp iwgkngwlip lddlsadyna adilpamsgg
      121 lsydgtlyas pfygessmvm yrtdlmeaag mempkaptwe firdaaaamt drekeingic
      181 lrgkagwgeg gafitamsns fgarwfdmdw npqfdteawa ntvnffkdmm dasgpagyat
      241 ngfnenlslf nqgkcgmwid atvaasfvtg kdstvadhvg falapdnglg krsnwlwawa
      301 laipagtqke aaakefiewa tgtgyielva anegwanvpp gartslyenp eyqkvpfaqm
      361 tldsilsadp nnstveespy vgvqfaaipe fagiatdvsq efsaayagqq tveealakaq
      421 altndameaa gyk
//
LOCUS       WP_284373029             251 aa            linear   BCT 25-DEC-2024
DEFINITION  lipase family alpha/beta hydrolase [Algimonas porphyrae].
ACCESSION   WP_284373029
VERSION     WP_284373029.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18498059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..251
                     /product="lipase family alpha/beta hydrolase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27635
     Region          39..139
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
     Region          <105..>189
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mstsmaakap slfwtltegr sllelnsfya lrplmkrlpk gdghpviafp gfvasdrstr
       61 pmrnllrdlg ystygwglgr nlrfnpqred emasllhsvh qrygrkvsli gwslggvfar
      121 eiakanpeav rnvitlgspi sgdmdhtnat rlyeylngap svemkarmsq lseappvptt
      181 siysktdgiv swkgslqkpg gqtenirvpa shcglgvnpl vmylladrlq htpsswtpfe
      241 adgakrflfr s
//
LOCUS       WP_284373038             248 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Sulfitobacter pacificus].
ACCESSION   WP_284373038
VERSION     WP_284373038.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10786099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..248
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27775
     Region          1..78
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
     Region          110..240
                     /region_name="SRPBCC"
                     /note="START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC)
                     ligand-binding domain superfamily; cl14643"
                     /db_xref="CDD:472699"
     Site            order(111,113,115,124..126,128..129,144,151,153,155,157,
                     171,173,179,195..196,198,200,209,211,213,215,220..223,
                     225..226,229..231,234)
                     /site_type="active"
                     /note="hydrophobic ligand binding site [active]"
                     /db_xref="CDD:176902"
ORIGIN      
        1 mdavfkalad parrtlldal rqkdgqslqe ltellemtrf gvmkhlgvle saglvvtrkk
       61 grfkyhylna vtlqqtidrw iepmrakpva ravldlkstl ernhlmtkpd fmmqtfirct
      121 qdalwdalsd pasmaayhfm cervegeave ggaltwilpd gnkmltqrpt kvvpktriea
      181 efephffgpd apgsrmafii epqgdicklt iehydvpegq qgvgegwarl aaslkswlet
      241 gtalkmam
//
LOCUS       WP_284373090             136 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Sulfitobacter pacificus].
ACCESSION   WP_284373090
VERSION     WP_284373090.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 136)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 136)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10440481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..136
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13959
     Region          29..109
                     /region_name="Cytochrom_C"
                     /note="Cytochrome c; pfam00034"
                     /db_xref="CDD:459641"
ORIGIN      
        1 mhitylslaa gaavavlaac apvsmpepae graffaqnct schgtsgrgd gplsgdlkpk
       61 ptdltllars nggtfptasa lsyiwgdpld nhlirvmpef gpamaddlvp vevdgvltpt
      121 pralagllgy lesiqr
//
LOCUS       WP_284373167             378 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Algimonas porphyrae].
ACCESSION   WP_284373167
VERSION     WP_284373167.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..378
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40553
     Region          3..377
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 masppsapls gyrivelagi gpcpyagmll admgaevilv nrpgfavptv hdrgktsiai
       61 dlrqpdgvav lldlversda lieglrpgvv erlgigpdac harnaklvyg rmtgwgqtgp
      121 waktaghdln yiaitgalaa mgregepppp plniigdygg gtlflvmgvl aallqaertg
      181 rgdvidaami dgtnslmglf htlaglgqwt perdtnlldg gmpfyrcyat sdgkfmavgc
      241 iepqffaefl rlleidpgdf gdqmdkreha kqharlealf kthtrdhwaa rfdgsdacvt
      301 pvldyteapd hpqnrarggl erhghyvhpr papvfgghyd vpdpvlpvin ggrdavtrll
      361 gynadrvstl iqtkilse
//
LOCUS       WP_284373200             429 aa            linear   BCT 25-DEC-2024
DEFINITION  cytochrome b [Algimonas porphyrae].
ACCESSION   WP_284373200
VERSION     WP_284373200.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Tolkatchev,D., Yu,L. and Yu,C.A.
  TITLE     Potential induced redox reactions in mitochondrial and bacterial
            cytochrome b-c1 complexes
  JOURNAL   J Biol Chem 271 (21), 12356-12363 (1996)
   PUBMED   8647838
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Howell,N.
  TITLE     Evolutionary conservation of protein regions in the protonmotive
            cytochrome b and their possible roles in redox catalysis
  JOURNAL   J Mol Evol 29 (2), 157-169 (1989)
   PUBMED   2509716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..429
                     /product="cytochrome b"
                     /GO_function="GO:0008121 - ubiquinol-cytochrome-c
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=48316
     Region          5..405
                     /region_name="QcrB/PetB"
                     /note="Cytochrome b subunit of the bc complex [Energy
                     production and conversion]; COG1290"
                     /db_xref="CDD:440901"
ORIGIN      
        1 msghstyepk gsiarwmdqr lpvvrmgadf mamptprnln ywwtfggilt lclviqivtg
       61 vilgmhyvah vdhafdsvqr irrdvpygwl mqsthavgas mfflavymhm frglyygsyk
      121 apreilwiig cliylvmmat aflgytlpwg qmsfwgatvi tgffgavpiv geglqqwllg
      181 gyavenatln rfyslhyllp fiiaalvglh vwalhvtgsn npigvsekvk tdtlpfhpyf
      241 tvkdmfaivv flmifgfflf ylpdalghad nyipadplnt pahivpewyf lpfyailrav
      301 pdklagillm lgailvlfvl pwldtsrvrs mrfrplarpf fflflffcfv lgwcgagvpd
      361 dyaikigdgg ltfyrlgqis tlyyfayfli ilpilglied pkerpasitq silsetskpq
      421 petalapae
//
LOCUS       WP_284373265             259 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Algimonas porphyrae].
ACCESSION   WP_284373265
VERSION     WP_284373265.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..259
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28192
     Region          3..259
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mrttfsdliq ntdpqverlp dswkqgrtay ggltaalmlv raqariddlp plrsalinft
       61 gpvseppwie ttllrrgrnv ttmesngavd gktvctgtfs fgaardshlh vdlpapdtpd
      121 peacelflgg dspfipaftr nfetrliags rpmsggtskr lrcwarhade asrtgeaall
      181 cladilppaa ltvmqqigpv ssmswicnil rdpetddgwy qveaeltaal dgyssqvmri
      241 wnrrgdlive gmqsiaifa
//
LOCUS       WP_284373315             404 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Algimonas porphyrae].
ACCESSION   WP_284373315
VERSION     WP_284373315.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..404
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=42952
     Region          <125..368
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
     Region          <164..>229
                     /region_name="metallo-dependent_hydrolases"
                     /note="Superfamily of metallo-dependent hydrolases (also
                     called amidohydrolase superfamily) is a large group of
                     proteins that show conservation in their 3-dimensional
                     fold (TIM barrel) and in details of their active site. The
                     vast majority of the members have a...; cl00281"
                     /db_xref="CDD:469705"
ORIGIN      
        1 mirqwlsqtr tdyrssdkgn vasmtavaal lllgaigaai dytrmgtlks qlqnavdsgv
       61 laaasfdses ddarrlhger vaeanianlt giptditlni dksglvigtg emtyqpvmmh
      121 mfgfdtlpvt alseamaegg vvdaeivlvl dysssmnsky vamrtaavnl vrdlsasdda
      181 eiefglvpfa eevfmtldgq yavggvrgvp wvgctisrrw pfvvsdktpn gsarskwgag
      241 gtdcgqyvpr slvvqpltdn haaviaqlla mrphrgtnts lgaeigyqli spnppfaase
      301 fsggkqkfiv mlsdgeqtrp sygpgdrltm dqaasnlqsi cdaaasngvt vitvlydtss
      361 trarsamrnc asspdlfmea tsgnisdrfa migemvksdi rlsr
//
LOCUS       WP_284373341             189 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Algimonas porphyrae].
ACCESSION   WP_284373341
VERSION     WP_284373341.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..189
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20548
     Region          58..189
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mftltnairl milagllava ltlvkacqap egalerfgvd sltkltvldn pplqsgatfq
       61 tptgtmtled vrgkvvlvnv watwcapcvv empsldeler mrggedfavv pisldrtmee
      121 ietfyarmel saipiihdpn ysvnaqldlp glptsilydr sgrevarlpg eaewvsteal
      181 alidyliaq
//
LOCUS       WP_284373459             230 aa            linear   BCT 25-DEC-2024
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Sulfitobacter
            pacificus].
ACCESSION   WP_284373459
VERSION     WP_284373459.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439579
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..230
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25941
     Region          6..218
                     /region_name="PssA"
                     /note="Phosphatidylserine synthase [Lipid transport and
                     metabolism]; COG1183"
                     /db_xref="CDD:440796"
ORIGIN      
        1 msiqtrallv hlftatgavf amlamlaavd gkwdmmflwl vvaffvdgid gplarrydvk
       61 tnapqfdgvl ldliidylty vfipafalfk sglmdgwsgw vmiiivtfas amyfcdtrmk
      121 tkdnsfwgfp gcfnmlvlvl falsppwwvc liivtilsvt mflpvkfvhp vrterwrivt
      181 lpmalawvff agwaawvdfh peswahfglv ltsiylcvag avqqltepkd
//
LOCUS       WP_284373633             133 aa            linear   BCT 25-DEC-2024
DEFINITION  MerR family transcriptional regulator [Sulfitobacter pacificus].
ACCESSION   WP_284373633
VERSION     WP_284373633.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 133)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..133
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15721
     Region          6..123
                     /region_name="HTH_GnyR"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     regulatory protein GnyR; cd04776"
                     /db_xref="CDD:133403"
     Site            order(7..9,23,39..41)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133403"
     Site            order(52,55,59..60,69,90,94,100,104,107..108)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133403"
ORIGIN      
        1 mtsdlmtirq mcdtfdvtpr tlrfyeakel lfpiregqkr lftkrdrarl klilrgkrfg
       61 fsleeirqll dlyhrgdqqr tqitraldia rerltemlaq redldaaind lkeqlkwgek
      121 mmtslnqtps mae
//
LOCUS       WP_284373645             280 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Algimonas porphyrae].
ACCESSION   WP_284373645
VERSION     WP_284373645.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 280)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..280
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31936
     Region          2..225
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mrfegtkdyv atqdlmmavn aaitlerpll ikgepgtgkt vlaheiakgl napllewnik
       61 sttkaqqgly eydavarlrd sqlgddrvhd isnyikrgki weafesaqrp illideidka
      121 diefpndllh eldkmsfhvy etgetisasq rpiivitsnn ekdlpdaflr rcffhyiqfp
      181 deetmadiva vhfpdlkprl lsaalkrffe vrampglkkk pstselldwl klllvedidp
      241 etlretdksk lipplhgall kneqdvhlfe rlafltrres
//
LOCUS       WP_284373703             655 aa            linear   BCT 25-DEC-2024
DEFINITION  GumC family protein [Algimonas porphyrae].
ACCESSION   WP_284373703
VERSION     WP_284373703.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..655
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=72201
     Region          42..>499
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
     Region          <510..>651
                     /region_name="PTZ00395"
                     /note="Sec24-related protein; Provisional"
                     /db_xref="CDD:185594"
ORIGIN      
        1 malfrrgkek srtpdaasay spapvraadl tvgdyanglp nirigemias ffrqmvwvfp
       61 laligavgaf hltkdmkrty tgegtvmvql gdeyvyqpva gtnaqsslmq tpdtitlnev
      121 almkndrvid dviaqikdsp gglrafapki atdmarhseg ttayrqeymk lrrmmnmsyh
      181 vstrpkssvv dmsfkhedpd lavstlnrlm dsymtyrrti fvdgtgdvia erradteqrl
      241 rqvdreiaaf ldknqisdft seqagartrt edlraalngl raqivesers lasvedqlra
      301 tpdtinlyid drasnriaqa elelkqllak ylpnsdpvrq kqleidelrs ltagqgdrit
      361 ggrrvgpnpv yqalltqrnt vqatanslre keitmqqqln sadgklrrma gieprlnall
      421 reretltlrl ttylgkeqea llnqqqaeaa senvkvisks tfpikgrnms algfvgataa
      481 wvftllmfal frvfadprly avpatttrnp qtgpyasrnl anegfspmsa nyhsadyhna
      541 gyavpqsghp tsgqpeawqp paqpyapdpy aydagqpmpa apypasaqly egqfhqpapv
      601 qqayvdpaya ypdpnayagq dpyagqdtyt atdpyaahgp dgtipanpyl tgtrg
//
LOCUS       WP_284373724             680 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Algimonas porphyrae].
ACCESSION   WP_284373724
VERSION     WP_284373724.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 680)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..680
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=76191
     Region          415..667
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mrvgsrtakv grrvlaaltl clitltatvs ahaqsvtdfa gatyfehvsl spngnlysmv
       61 rfnrdgssea riydrrtlqr vggltipegm sftwvewasd ttilasvstq lrvegrkihl
      121 ptarifshdi rdrrkpvilf eneerilntn irlnrvvdmm pddpdhivmg awrngdfdlf
      181 rvnvetgeae riakgrdmtl swftdvtgrp slrfdcatnt crkinlytpe dgadpsdtrt
      241 rwkllrsfvq nnseddkfmd lqplgptanp deffvldgrd eqprravrvy nirtnefvet
      301 lfeddrhdvs halidpksra ymgaqiwrdt ieyvlvdatl qdhldtlngy fegdwnvsfs
      361 kiadngsaal vyasasdepg ayyiydfkak dtkriarknr slhnaleaet evldipvrdg
      421 ttltgyltvp gknskgrlim mihggpeqrd vldydrdvqf lasrgyavar vnfrgssgyg
      481 rafasagyrq wggvmhtdvi datlwlqkrq diagsetcim gysygayaal lagalqpqly
      541 tcivagggps dlnqflkder kthgrnspql aywekaiger kadkdllasi spinlvdrye
      601 dpvllihaty dntveidhsk dlekalnksg rsvellelyg ghthgtwprs srvaylkkle
      661 affathlaps asdpakadap
//
LOCUS       WP_284373812             395 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Algimonas porphyrae].
ACCESSION   WP_284373812
VERSION     WP_284373812.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..395
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43056
     Region          61..389
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrgsslicli afvvgfspsa naqtdntlfp lpaqsdtvaw ptqgwpvgep lsvvqsvrln
       61 avldpvftte igdglgetra iviirggeii yeryrpgfna etrhiswsva ksitsalvgr
      121 avqsgliasi ddpmpgpfaa ddprsdiswr hwlqmldgld yveleatgls dsdviqmnyg
      181 pgrfdsmaya ranfppahip gehwnystlg fhvigralqs llpgtcldpd edprlcnadp
      241 tvmsdwidtv lfrplgmngv eeydaagtlq ggsqfylsar dyakfgllhl rdglwdgeml
      301 lpvgwvdfvr rnpgtsdnng ygggfwpale npdnpetvft ppydafyagg regqliwivp
      361 srdlifvrvg impdssenwn alfklaqdag aavmp
//
LOCUS       WP_284373954             451 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Sulfitobacter pacificus].
ACCESSION   WP_284373954
VERSION     WP_284373954.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 451)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..451
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48229
     Region          122..447
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mtrlrhiwrs mplrlaillv alfatvslls laasyavtqs sfeetiradl qqdlagfraa
       61 psaravaqlv eaesraadpg rlilsyvard griygngaia qdeggfhifs lnperaefeg
      121 eylsltnply ggvitiarsr aeivalrgvf vnillisllp tvlialsggl ilarrskrhv
      181 evvgaaldkm tsgdlgarvq igprwsddlv riggklnqma aaqeaqmgal rdvtsdiahd
      241 lrtplqrval yvqdlsdrva ddpesavlag kvqgevdgmt hvfhallqla qveagspkar
      301 fetvdltqvc rkvvelfeds avasghdlsl dlvaeplslq gdrallgqmv snlienalrh
      361 tpsgteitvs lrgqegavvl qvadtgpgip adergkvlqr lyrldrsrqt pghglglslv
      421 qavaglhgaq lslqnnapgl rvdvrfptkv g
//
LOCUS       WP_284374059             464 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Sulfitobacter pacificus].
ACCESSION   WP_284374059
VERSION     WP_284374059.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 464)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..464
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50504
     Region          131..457
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mvhslsgrll ilttvfvmia eilifvpsia rfredymlnr leraqiasla lladdmldpe
       61 lesellrnae vfnvvlrrde arqlvlstnm pqavsetfdl rdatamtlir dalrrmfspr
      121 neivrvigap vreaglliev tmetaplrma midygtrilv lsavisvita vllflalral
      181 llkpikgvvg hmqryaqape darriiepsa sitelreaem almtlqtdlt qalkqkerla
      241 qlgsavskis hdlrnimtsa qlftdriems edpvvkrmap klvgsitrav hlcestlafg
      301 raeepgptlt malletlied avegeklasg dqpiryvtdv pagmmvrada eqlyrvisnl
      361 vrnarqalmg igqggeitvq agesdsawqi dvsdtgpglp akaqehlftp fqggarkggs
      421 glglaiaael vkghggqlil aetdasgtrf riilpkgdgt lnil
//
LOCUS       WP_284374061             472 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Sulfitobacter
            pacificus].
ACCESSION   WP_284374061
VERSION     WP_284374061.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 472)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..472
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49968
     Region          4..450
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mnriktdvli igagsgglsv aagaaqmgad vvlleghkmg gdclnygcvp skaliasgka
       61 aygqqhsaqy gvadaagtvd yaaakdhvad viaqiapvds qerfegfgin virefgrfis
      121 adevqagdtv ikarriviat gssplvppip gldkvpyetn etlfelrekp ahlliigggp
      181 igmemaqahi rmgcavtvie gakalgkddp elatvvldsl rdegvvieed alaaeirgka
      241 gaieveakdg rifkgshllm avgrkantdk ldlekagiep tksgikvddg lrstnrkvya
      301 igdvagglqf thvagyhagv iirsmlfglp skaktahipw atytdpelaq vglteaqake
      361 qhgsklevvr fhythndrai aerktkgfik lmvvkgrpvg asivgyqage linlwalala
      421 nkmkmsqiaa mvapyptige inkraagayf sprlfesdlv kqvvgfvqry lp
//
LOCUS       WP_284374064             163 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Algimonas porphyrae].
ACCESSION   WP_284374064
VERSION     WP_284374064.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..163
                     /product="YybH family protein"
                     /calculated_mol_wt=17175
     Region          31..161
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mnyksivaia ilaftpitac gelsdnppsv dtdavaedvr qsvdgmvaaf lrrdvegate
       61 sfaddyvgmf hgqpnvvgka aevevtkaqm tdpalgltls nvavdvakaa dmaiftatya
      121 ydftdpetmt pttetgnwvl iykrqadgtm kvttgivtdt pps
//
LOCUS       WP_284374069             133 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Algimonas porphyrae].
ACCESSION   WP_284374069
VERSION     WP_284374069.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..133
                     /product="YybH family protein"
                     /calculated_mol_wt=14712
     Region          1..127
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mttsqsgega lhrryveain sndvdhilal lsddvvfqap gepeligkda irewgnsffe
       61 afdahwdkte lsfersgdla isryiysary tgrddnavme etgkgtciyr rgedgswrla
      121 idswstneag aeg
//
LOCUS       WP_284374101             194 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Algimonas porphyrae].
ACCESSION   WP_284374101
VERSION     WP_284374101.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 194)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..194
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20781
     Region          119..191
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mkivplaead ldctarltlg rlnvlaypef ynglglegea ldrlsadmfd vsegelsdti
       61 vaisdedtlc gylsalpsdd fraaasrtaf avlkgvardq rkpvmahmqa igagqdalpa
      121 nthylariav spdwqgkgia aelmdifeaq gggcdhvlhv aadnarairf yekrgyetes
      181 gsdstllmrr rass
//
LOCUS       WP_284374142             389 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Algimonas porphyrae].
ACCESSION   WP_284374142
VERSION     WP_284374142.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..389
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=43307
     Region          <194..379
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mndapdlimn wrsammvmvv lplllcglil llrrvearaa rplglflilg glsmgpqiig
       61 fagayqiwpw ltfcplffvd lwlgpllvih ahnlmrggpl gwrrwlllpg llqtayytga
      121 fllpgdglfd tpakwafnda fhlpyiipme sllgiglfgf sivliwrgrg ryltfldqtq
      181 saardfdpvw lrnlivamsi gltiyaglei lslavalsyp atfpallllt svltwvglda
      241 awrltapfpk mdiaapaprm tvsdnhalpd dlsarvrsai idqrwylepr ltisdvarrl
      301 gtnesyvsra lnqslgdsfn rfvnraridh akalletgeg silsmamdsg fnskatfnrv
      361 fktfthetpt qfrnrrrasd lqseasqsp
//
LOCUS       WP_284374172             516 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Sulfitobacter
            pacificus].
ACCESSION   WP_284374172
VERSION     WP_284374172.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..516
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=54051
     Region          57..509
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mkrflatglt atalslptla aaqeavsfeq kvndvfagst gwfvnlifms lpgtnfpwiv
       61 lwlvvaasif tiyfgfvqfk afghaislvk gdysdpndag evshfqaltt alsgtvglgn
      121 iagvavavgi ggpgatfwmv lagllgmask ftectlgvky rneypdgtvs ggpmyymtkg
      181 fkerglpggk vlavifaift iggalgggnm fqanqahaqi tnitgdfsgl itgvifagvv
      241 favivggiks iasvtekvvp fmgvmyvlaa lvilimnadq igwafgqifa gaftglgvag
      301 gfvgaliqgf kraafsneag vgsaaiahsa vktkepvteg vvsllepfid tvvictmtal
      361 vitisgvlvm dpatgnfvln eagtaiktvd gssgvsltss afaagfswfp yvlalavilf
      421 afstmiswsy yglkawtylf gegkttelvf klifcffiiv gaaaqlgavi dfsdamifam
      481 avvnitalyf lmpivkremn syfdrlksga ivrhkh
//
LOCUS       WP_284374189             289 aa            linear   BCT 25-DEC-2024
DEFINITION  inositol monophosphatase family protein [Sulfitobacter pacificus].
ACCESSION   WP_284374189
VERSION     WP_284374189.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..289
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=31130
     Region          25..283
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 msdtlpaplp kavslaqqqh ivniirraak aeimprfral sagdiraksh ahdlvtaadt
       61 aaeqmitral qiafpealiv geeaaadtpe llgeianaql afiidpidgt wnyahgmavf
      121 gviiavtrfg rpafgviydp vnddwviadd espammdaaa tsprplkasm gkplnaligy
      181 vplhifpkeh qaklavaltg farthplgcs aheyrmiaqg hadflltasl hpwdhaagal
      241 iceragayve mldggpynad rhsghlmvap drttwnrlkk vfaflleqp
//
LOCUS       WP_284374333             399 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Sulfitobacter
            pacificus].
ACCESSION   WP_284374333
VERSION     WP_284374333.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..399
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=44318
     Region          133..392
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mddiiielaa tgtfaiavfg avfclmqsre frvsasfaaf latvainnip dafrrlieae
       61 pssldamidv avwpssffla plfwiyvftl tsssqqqpqn rlrhfvlpgl avvltvlvll
      121 sppdvqails adepkmdtgw smavvlgfgl lqlavypqia vylfliwrrl mafrqrlrdv
      181 yasteehelr wiyvicgfya lfwlaqtvll lvvidaadta vppvfinias lagltvvaat
      241 vlwglrqrpp lvpdddqntp eptkgqspsk yeksalsaea shrlgrklra smevdhlhrd
      301 pnlslwalar higaspnyvs qtlneeiges ffdfvngyri aeaknllttt dqsiltityd
      361 vgfnarssfy nafkritgqt psyfrknmsr paglddisa
//
LOCUS       WP_284374335             336 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Sulfitobacter
            pacificus].
ACCESSION   WP_284374335
VERSION     WP_284374335.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..336
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35626
     Region          8..335
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mnrrkfnsvg latilahlpr ltlaetavsq rhgyqvaain nglltarhng mahsqsavdd
       61 etlfqvgscs ktatalavmt lvrdgrvdld mpvnryltrw qlpgprgava tiaelmshta
      121 gttvhgfagy gptgklptln diltgrgvan sdpilaqrri fgrfrysggg tmvlqslied
      181 itgtdfatyt tnevlrpvga shatfaitpt rpfaygsyen gqaveggymr hpesaaaglw
      241 atasdlanlf hgvlqalagt rhaiipmala ermvtpvcrk vglgvfvsag ptishegrnf
      301 gfdsivaadl ntgqvraavt nrngaiesyt eqllah
//
LOCUS       WP_284374382             457 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Algimonas porphyrae].
ACCESSION   WP_284374382
VERSION     WP_284374382.1
KEYWORDS    RefSeq.
SOURCE      Algimonas porphyrae
  ORGANISM  Algimonas porphyrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Algimonas porphyrae"
                     /db_xref="taxon:1128113"
     Protein         1..457
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=49640
     Region          <11..190
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mpetnksteq imvvldasgs mwgrvdgrtk isvvrdayad lmktwdeadv esglilyghr
       61 rkgdcsdiel isrpgqtdsh slgrtvakln pkgktpigas vrqaaeelky teqkatvill
      121 sdgietcgvd pcqlgrdlea lgvdftthvi gfdlggeate qlqclarntg grflqarnts
      181 dlkeafeqva disrplslqg lvaetgeaap gmmwtitrkd gvivveqrte tstlsmaela
      241 dgqlpdgdyt vtgraknysg stnftlptek pviyvrlfpd vpytrlrveg dilsgdeftv
      301 awegiggped iisivprgad wgqaistvrv rtgnpvslka ppnageydll ylnsdvelnr
      361 idermpvtvl eslyalnaag aiqagqsftv nwrgpalegd miaigprtsg rddyfsmtwi
      421 esdgpvslta pdmpgdyelr yygdgyvvqf vqpvrvq
//
LOCUS       WP_284374451             644 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Sulfitobacter pacificus].
ACCESSION   WP_284374451
VERSION     WP_284374451.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 644)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 644)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 644)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 644)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 644)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13370558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..644
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=70138
     Region          135..461
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
     Region          320..455
                     /region_name="AAA"
                     /note="ATPase family associated with various cellular
                     activities (AAA); pfam00004"
                     /db_xref="CDD:459627"
ORIGIN      
        1 msqtsdamel reediaghvt vaqallegfd haprigkpav aaaperssgi gtrrrfrstt
       61 pglvtqrrva agavsligrv egadgddalm splqatvlhg lrraiaiala vaenvaeqsg
      121 lgdlkranle gslpaarkge fdellaaeal vtlyvfgnat ayllsahlpe vavevgevee
      181 vlldngqtam hgalweldrd iaahgrddah vvatvaafae slmekvalra qtaprlegfk
      241 aaswrveadd ftvsgfspaa kakstkltmt fkkpnevvgn hiakyqamkl akmlmaydfd
      301 rrlnpfaelg gfiftfmgdg apgtgkttli qmmaglisey cnnagypfry qnlstdnids
      361 yqgksgqnak afinniidps vigfgtiddi dqlagkrgdr qssagqleit avlmesfaga
      421 ntvvrgnctf gmfsnypenv ddalrqraga rflvdgpqtr edyvdilyll mgknhdiplg
      481 ehqvfeaqai kkavaasfeg hlkpheagll tvyetvqaei galdtinklg tylkaiqead
      541 prftgraikn itdavkvram dfelpdewme epelflfkgy dekkamieem rqeitvemvv
      601 qeinryadse fryadksdem aienavrdmq rmeaakkryl ggeg
//
LOCUS       WP_284374463             633 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Sulfitobacter pacificus].
ACCESSION   WP_284374463
VERSION     WP_284374463.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13939702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..633
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=66785
     Region          181..477
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
     Region          456..630
                     /region_name="DUF3520"
                     /note="Domain of unknown function (DUF3520); pfam12034"
                     /db_xref="CDD:432277"
ORIGIN      
        1 msddlddlks lmnaatprpd ttrksenial aqknfadlqg srdgarltsd rpetglisgv
       61 knmlstltsr agltastaiv avglvmlspl gesllptkpd aafvpsapqe epavvmekat
      121 aptssplves apmiaadmat esmggapapa mmaspansrm imdlpvvrpe sstenfansd
      181 anpvqvttqn pvstfsidvd tasysvirns ltngqlppkd avrveeminy fpydyaaptg
      241 ndafqptvtl tptpwnadtq llqigiqgal pdladrppln lvflidtsgs meqpnklpll
      301 kqsfrlmlgq lrpedqiaiv tyagsagevl aptaasersk ilnaldnlga ggstagqagl
      361 qqayataaam seegdvnrii latdgdfnvg lndpealkdy iadkrdsgty lsvlgfgrgn
      421 lddatmqala qngngqaayi dtlseaqkvl vdqlggalfp iaddvkiqve fnpatvseyr
      481 ligyetralk redfnndkvd agdigaghqv taiyevtpkg saaerndplr ydtpvvtena
      541 sdelaflrlr ykapgsdtsa lvetpvqasv tgeagfatai agfgqllrdg tytgswtyad
      601 aiklasetkg ddpfgyraea vqlmrlaesl saq
//
LOCUS       WP_284374467             272 aa            linear   BCT 25-DEC-2024
DEFINITION  trypsin-like serine peptidase [Sulfitobacter pacificus].
ACCESSION   WP_284374467
VERSION     WP_284374467.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..272
                     /product="trypsin-like serine peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=28657
     Region          42..241
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mrvfaqitav alcalmfgga aeadstklrk lgtkndalaw qsvgrldlgr ngyctgtlia
       61 pdmvltaahc vyqngqlvaa qditfraglt ngdaaakrtv sqieahvgyd ptagfdgnni
      121 rhdlalvrla epipshqlap frvfsgampk gsvsvvsygr grsdalsrqn qcqvlgmqer
      181 lvvmdcdvtf gssgapvfth lngrgqiasv isgigargdk kvafgmalpq lisdlkrqmr
      241 ankarpgaki rrvtvgtrkt ssgakfvran gs
//
LOCUS       WP_284374486             245 aa            linear   BCT 25-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Sulfitobacter pacificus].
ACCESSION   WP_284374486
VERSION     WP_284374486.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Niehaus,T.D., Elbadawi-Sidhu,M., de Crecy-Lagard,V., Fiehn,O. and
            Hanson,A.D.
  TITLE     Discovery of a widespread prokaryotic 5-oxoprolinase that was
            hiding in plain sight
  JOURNAL   J Biol Chem 292 (39), 16360-16367 (2017)
   PUBMED   28830929
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Fan,C., Li,Z., Yin,H. and Xiang,S.
  TITLE     Structure and function of allophanate hydrolase
  JOURNAL   J Biol Chem 288 (29), 21422-21432 (2013)
   PUBMED   23754281
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Wang,L., Grau,R., Perego,M. and Hoch,J.A.
  TITLE     A novel histidine kinase inhibitor regulating development in
            Bacillus subtilis
  JOURNAL   Genes Dev 11 (19), 2569-2579 (1997)
   PUBMED   9334321
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005226
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..245
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=26187
     Region          1..230
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 msdwpkirtv glsgvlvtfa gemsepanra alafraavdg adwpevsets tslvstflev
       61 dlastspqdv terleellks rdwfaaalpa grtlwqvptl ygtelapqle eaaevagvdp
      121 dqaiaeisas rvrvltigfa pgqpymgels dtwniprqqg ltksvpsgal viairqlivf
      181 tnaaptgwrh igqtafrtfr pdaempftla pgdeltfpai sraeyeaila kdtsglggat
      241 revlt
//
LOCUS       WP_284374492             415 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Sulfitobacter pacificus].
ACCESSION   WP_284374492
VERSION     WP_284374492.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..415
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43995
     Region          1..410
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtrhvaviga givgvstaiw lrragidvtv idrgapgsgt shgnagvlaa camvpvtspg
       61 litkapgmll npdfplfmrw gylpkllpwl rkyvahanda dtrriaqglt pivgdaveqh
      121 kslcddlglg dwvsesdycf ayanraafea esytwalrke agftpmlieg qevrdyepal
      181 gpdlgfmaim knhgfirspg gyvqalaqaf egmggtilqa evkdfdlsgg avsavhttqg
      241 tvhctevvla tgvwskpmma klglnvples ergyhivfed atggparptm vasgkfvatp
      301 meqgvrcagi vefggleara skaplaflrr haakafpnlk aksevewlgh rpatsdslpl
      361 igqvgdtkvy tafghhhigl tggpktgrlv agliagaqvn tdlapyhpqr fstkt
//
LOCUS       WP_284374625             145 aa            linear   BCT 25-DEC-2024
DEFINITION  VOC family protein [Sulfitobacter pacificus].
ACCESSION   WP_284374625
VERSION     WP_284374625.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..145
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15615
     Region          22..133
                     /region_name="PhnB"
                     /note="Zn-dependent glyoxalase, PhnB family [Energy
                     production and conversion]; COG2764"
                     /db_xref="CDD:442048"
ORIGIN      
        1 mdyetigaed fgaslrgigl nllvrdvaae iafletvfgm ksfqptadfa imtygeqvfq
       61 ihadgtyhan pllgllpenp prgagieirl ydtdpetaca kaevaggtil qaptdkphgl
      121 reayilceng yawvpsrike kskge
//
LOCUS       WP_284374671             200 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Sulfitobacter pacificus].
ACCESSION   WP_284374671
VERSION     WP_284374671.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..200
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=22014
     Region          1..199
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mtkltlrgfv ihkglldlpa qhalvkavrg vvrsaplfrp dtpqgkqmsv rmtaagkygw
       61 ysdragyryv snhpngaswp aipsqileiw dqvtgldrqp ecclinyyvp darmgmhqdk
      121 deadfqwpvl svslgddalf rignvtrggk tesvwlqsgd vvvmggearl ayhgvdrlra
      181 gssrllpkgg rvnltlrvve
//
LOCUS       WP_284374846             355 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Sulfitobacter pacificus].
ACCESSION   WP_284374846
VERSION     WP_284374846.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..355
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36173
     Region          39..350
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mfaalsrvpp rldrvqlarm ahlwlvmllv lvslaalatg asgtslwsal aklaqgqalt
       61 rteavvlwdi rvprllmgil vgaalamsga vmqglfrnpl adpglvgvsa gaglgaiiai
      121 vlggllpasv alffgtyllp vaaflggwgs tlvlyrvatr ggrtsvatml lagialaala
      181 gaasgllvya addnqlrdlt fwglgslaga swfkvmvaap liliacgmal tlgaglngla
      241 lgeatahhig ipvqrlknta iltvaaatga avavsggigf igivvphllr lwtgpdhrgl
      301 lfnsallgai lllladiisr vivapaelpi givtatlgap vflwillrrr glmdl
//
LOCUS       WP_284374890             238 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Sulfitobacter
            pacificus].
ACCESSION   WP_284374890
VERSION     WP_284374890.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 238)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..238
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26920
     Region          1..>220
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtrthrlfql mttlrrlpap vratqladem stslrtvyrd idalrglgav idgeagfgyt
       61 liedaalppl gfeddeleal vlglrdvtvi gdpalakaak talakitarv pprqahrlqh
      121 aildarrfvr pdppridvad lraatweeet vrfaytdgag vattrevdpl glvyfqdtnm
      181 lmawchlrrd frvfrldrmd elmrtgqsfr prrvpllrey teilraeala raerraer
//
LOCUS       WP_284374941             345 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Amylibacter marinus].
ACCESSION   WP_284374941
VERSION     WP_284374941.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..345
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38044
     Region          10..342
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mryqtpisil lsfmiaapaa iaqdyqtgmk elvilekdgt rhlngflwyp ttevenpvpa
       61 hgnvvwepis vipdapltte thplvllshg mfgnarnqaw lasaltkqgy ivaaidhpgt
      121 stfnrnadqr rslwrrpqdi srtldylldq pafksvidpa rihmaghslg gftavalagg
      181 rfdpdhfdgf cadnpadlvc tifdrwnvak sntdraamqv dlrddriksi avfdlggtqt
      241 fspeslgqis tpmivygapq disgldldve sralvtslsq divqyhepeg lahfdflgvc
      301 taaaldilke eepddifvce egrqerraah qmivenvahf fedqs
//
LOCUS       WP_284375144             374 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Sulfitobacter pacificus].
ACCESSION   WP_284375144
VERSION     WP_284375144.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..374
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40337
     Region          6..374
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mgngnagpla glkvvemarv lagpwagqtl sdlgcevikv espagddtrq wgppfvtrde
       61 dvsasyfhst nrgkasvtid frtdagqaql kellrdadiv ienfktggla kygldyeslr
      121 eefpqliycs itgfghtgpy ahragydfii qgmsglmsit gepdrqpqks gmaitdvftg
      181 iyattailaa vhqrsqtgrg qhidmalldc avaimgnqam nymttgiapt rmgnahpnlt
      241 pyevfetsdg hiiiatgndg qfqrlcrllg lddmatapey aknadrvanr pemnrriega
      301 tsqrtrddll aaceahnvpa gpinnlddvm vdpqvvargm qieldgvpgl rspfrfsdae
      361 lalhrpapkl gedn
//
LOCUS       WP_284375154             290 aa            linear   BCT 25-DEC-2024
DEFINITION  dimethyl sulfoxide reductase anchor subunit family protein
            [Amylibacter marinus].
ACCESSION   WP_284375154
VERSION     WP_284375154.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..290
                     /product="dimethyl sulfoxide reductase anchor subunit
                     family protein"
                     /calculated_mol_wt=31014
     Region          1..286
                     /region_name="DmsC"
                     /note="DMSO reductase anchor subunit DmsC [Energy
                     production and conversion]; COG3302"
                     /db_xref="CDD:442531"
ORIGIN      
        1 mhpapsvilf talsglgfgm laslglgnpd vtglsafiff alafaltigg llasvfhlgn
       61 pknaikafsq wrsswlsreg ilsvlalsim giyaigaifl gvrwhvlgat gailsvatvf
      121 ttsmiytqlk siprwnhwnt pvlflsltia ggalmtgqvr caiaaliiag viqivtwymg
      181 drrfaarast igtatglgdi gqvrmfepph tgtnyllsem vyvvgrkhgq klrvialglm
      241 vvlpvillcl sqdhftgaia vishligvfv srwlffaqae hvvglyygqr
//
LOCUS       WP_284375211             390 aa            linear   BCT 25-DEC-2024
DEFINITION  thiolase family protein [Sulfitobacter pacificus].
ACCESSION   WP_284375211
VERSION     WP_284375211.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 390)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..390
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40079
     Region          1..390
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mknvviagaa rtpmggfqga feglsasalg ghaikaaldn aktetvqevl mgcvlpagqg
       61 qaparqagfa aglgeevpat tlnkmcgsgm kaamigfdqi alghtdvmva ggmesmtnap
      121 yvlpkmrgga rlghgavvdh mfldgleday dkgrlmgtfa edcaetfqft rekqdeyala
      181 slsraleaqs ngafadeias vemktrkgsv tvttdeqpan arpdkipqlk pafreggtvt
      241 aansssisdg aaalvlased aanaqglnir arilghasha qapglfttap vpaaqkllaq
      301 igwskedvdl wevneafavv pmafmhemgl dhaivnvngg acalghpiga sgarimvtll
      361 nalekrglkr giaaiciggg egtaiaierv
//
LOCUS       WP_284375200             201 aa            linear   BCT 25-DEC-2024
DEFINITION  LolA family protein [Sulfitobacter pacificus].
ACCESSION   WP_284375200
VERSION     WP_284375200.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Tajima,T., Yokota,N., Matsuyama,S. and Tokuda,H.
  TITLE     Genetic analyses of the in vivo function of LolA, a periplasmic
            chaperone involved in the outer membrane localization of
            Escherichia coli lipoproteins
  JOURNAL   FEBS Lett 439 (1-2), 51-54 (1998)
   PUBMED   9849875
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..201
                     /product="LolA family protein"
                     /calculated_mol_wt=21232
     Region          1..191
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mrilstavls iglalalpla aaaqklplnd isaylnklqt akgeftqind dgsistgtiy
       61 ikrpgkvrfe ynppetalvv agsntvvifd kksnqpaesy plartplsii larnvdlgka
      121 nmvtghsfdg tatvvkaqdp enpqygniql kftgnpvelr qwvindgngs qttvvlgdlq
      181 kggnlpnslf nvgspgstan r
//
LOCUS       WP_284375216             218 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-L-isoaspartate O-methyltransferase family protein
            [Amylibacter marinus].
ACCESSION   WP_284375216
VERSION     WP_284375216.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Edwin,R.K., Challa,N., Sharma,R., Satyamoorthy,K., Parsa,K. and
            Misra,P.
  TITLE     PIMT/TGS1: An evolving metabolic molecular switch with conserved
            methyl transferase activity
  JOURNAL   Drug Discov Today 27 (8), 2386-2393 (2022)
   PUBMED   35462043
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Furuchi,T., Sakurako,K., Katane,M., Sekine,M. and Homma,H.
  TITLE     The role of protein L-isoaspartyl/D-aspartyl O-methyltransferase
            (PIMT) in intracellular signal transduction
  JOURNAL   Chem Biodivers 7 (6), 1337-1348 (2010)
   PUBMED   20564550
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Kagan,R.M., McFadden,H.J., McFadden,P.N., O'Connor,C. and Clarke,S.
  TITLE     Molecular phylogenetics of a protein repair methyltransferase
  JOURNAL   Comp Biochem Physiol B Biochem Mol Biol 117 (3), 379-385 (1997)
   PUBMED   9253175
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..218
                     /product="protein-L-isoaspartate O-methyltransferase
                     family protein"
                     /EC_number="2.1.1.77"
                     /GO_function="GO:0004719 - protein-L-isoaspartate
                     (D-aspartate) O-methyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0030091 - protein repair [Evidence IEA]"
                     /GO_process="GO:0036211 - protein modification process
                     [Evidence IEA]"
                     /calculated_mol_wt=23032
     Region          13..209
                     /region_name="Pcm"
                     /note="Protein-L-isoaspartate O-methyltransferase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2518"
                     /db_xref="CDD:442008"
ORIGIN      
        1 mndftsarta mvdcqvrpsd vtkypiinal lniarekyvp tdkisiayvg dhvalgnsry
       61 lldartfakm ldavnvrgde lvldiacglg ystaviadla eavvgvedna eladaasetl
      121 sqqgvdnaiv vsaplstgaa khgpydvvvl qgaievfpes lvqqlkdggr vaaifvdgam
      181 gqcrigiksg dtinwkrdfd atapilggfe rtiefnla
//
LOCUS       WP_284375329             646 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Amylibacter marinus].
ACCESSION   WP_284375329
VERSION     WP_284375329.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 646)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 646)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 646)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13370558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..646
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=70824
     Region          161..463
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
     Region          322..457
                     /region_name="AAA"
                     /note="ATPase family associated with various cellular
                     activities (AAA); pfam00004"
                     /db_xref="CDD:459627"
ORIGIN      
        1 msnsagllei keeqisakys aamglldgfd htprlakaad idggaekssg igtrrrfrst
       61 tpglvtrsta rpegvhianr vmasddddpl tsplqatvlh glrralatai vvsdqfseqt
      121 glealladnl agnlpkskqs efsellsasa lislhvfanm aqfllsnvaq agdvaeigev
      181 eeiltdnpql alsgalweld qdlalfasde arllpvilay lekmmekval raantprldv
      241 fenlafrvea ddfessgfaa saratssklt mtfkkphevv gnhiakyqam klskmlmayd
      301 ferklnpfad lggfiftfmg dgkpgtgktt liqmmaglin dycqnagyaf ryenlstdsi
      361 dsyqgksaqn aknfiknvld pnvigfgtid didqlagkrg drqssagqle itavlmesfa
      421 gantvvrgnc tfgmfsnype nvddalrqra garflvdgpq tredyidilh llmgknhnip
      481 vgdhelfsaq qikkavaasy dshskpheag llnvfdrvhs evgaldtiak mgaylkaiqq
      541 adarftgrai knitdavkvr amdfelpdew mentelflar dydtkrnmia elaqpitvem
      601 viqeinryad sefryadksd evaienmvrd ygrqeeakkr ylegkg
//
LOCUS       WP_284375492             195 aa            linear   BCT 25-DEC-2024
DEFINITION  HD domain-containing protein [Sulfitobacter pacificus].
ACCESSION   WP_284375492
VERSION     WP_284375492.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..195
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21590
     Region          8..171
                     /region_name="YfbR"
                     /note="5'-deoxynucleotidase YfbR and related HD
                     superfamily hydrolases [Nucleotide transport and
                     metabolism, General function prediction only]; COG1896"
                     /db_xref="CDD:441500"
ORIGIN      
        1 mgtrldqqia flneadklks tiratelcdn sryensaehs whltlyamvl adqagpdvdi
       61 tlvikmlilh dlveidagdn pifgdldhaa ieaqeqaaad rifgllpedl rvsfraiwde
      121 feaaespsaq faksldrfqp pmqnlqsggg swidfdvteq qihnrvgski aigapalwdy
      181 akariatffa erstk
//
LOCUS       WP_284375370             415 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Amylibacter marinus].
ACCESSION   WP_284375370
VERSION     WP_284375370.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..415
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44010
     Region          1..>413
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mtilqiasll ivlagafgtv nylffklpss igilvvalla svavmamdwf lpalgmeaqi
       61 savvkeiefs dallegmlgl llfagalhvk lgdlreqawv vllmatlgva istvfvgigf
      121 hfilgvpili alvfgslisp tdpvavlgvl reanlrksle tkiageslfn dgvgyvvflv
      181 lvgiafpsgd hhgsglagaa tlffqeavgg avlgailgyl vfqimkridd yalevllslg
      241 lafggyqlav ylhmsgpima vvaglfigdv gmkygmteet rhyldkfwel ideilnailf
      301 lligievfai afdanavlag llsivlalia rfaavavpif llkpfrsfps dvipimtwgg
      361 ikggisvala lslpdnewkp liltatyvvv lfsiiiqglt iaplarklgr epdll
//
LOCUS       WP_284375847             231 aa            linear   BCT 25-DEC-2024
DEFINITION  corrinoid protein [Amylibacter marinus].
ACCESSION   WP_284375847
VERSION     WP_284375847.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10114609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..231
                     /product="corrinoid protein"
                     /calculated_mol_wt=25069
     Region          20..220
                     /region_name="corrinoid_protein_B12-BD"
                     /note="B12 binding domain of corrinoid proteins. A family
                     of small methanogenic corrinoid proteins that bind
                     methyl-Co(III) 5-hydroxybenzimidazolylcobamide as a
                     cofactor. They play a role on the methanogenesis from
                     trimethylamine, dimethylamine or...; cd02070"
                     /db_xref="CDD:239021"
     Site            order(111..117,120,157..159,161..163,192,208,211,214)
                     /site_type="other"
                     /note="B12 binding site [chemical binding]"
                     /db_xref="CDD:239021"
     Site            114
                     /site_type="other"
                     /note="cobalt ligand [ion binding]"
                     /db_xref="CDD:239021"
ORIGIN      
        1 mseeeiilse lsdedlnlqm qddlydgmke eieegvnifl ergwqpydil tkvlvegmri
       61 vgidfrdgil fvpevllaan amkggmailk pllaetgapr lgnmvigtvk gdihdigknl
      121 vtmmmegagf evkdlginnd adayiseles gqydilgmsa lltttmpymk vvidtlvekg
      181 trddyvvlvg gaplneefgn aigadaycrd aavavetake fmakrhnqla g
//
LOCUS       WP_284376028             141 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Sulfitobacter pacificus].
ACCESSION   WP_284376028
VERSION     WP_284376028.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 141)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 141)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10440481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..141
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14880
     Region          52..135
                     /region_name="Cytochrom_C"
                     /note="Cytochrome c; pfam00034"
                     /db_xref="CDD:459641"
ORIGIN      
        1 mksiavffaf valiagawyv tldngrdage talpegalaa vtlpssfseq eeigarayea
       61 scavchgtna sgkvgvappl vhkiyepshh gdmafvlaaq ngvrahhwkf gnmppveglt
      121 raevlnivay vralqrengi h
//
LOCUS       WP_284376162             111 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Amylibacter marinus].
ACCESSION   WP_284376162
VERSION     WP_284376162.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..111
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11767
     Region          6..107
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mqahtlylcv aiiaetiatt llkssngftk lwpsigalvg faitlyllal tlrympvgvv
       61 yaiwsgagiv litiagiiff kqhldfagyl gialivtgvv vlqafskisl h
//
LOCUS       WP_284376426             475 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Amylibacter marinus].
ACCESSION   WP_284376426
VERSION     WP_284376426.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 475)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..475
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=50784
     Region          13..468
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mttgdldpkn wdefraraha llddsldkms tadqgrvwtp lpnqlkaqie qplprgggdv
       61 dqilrailpy gvgnthprff gwvhgagaps gvladiiaaa mnvnaggrnh vapvvekqvi
      121 nwcadvmgfg etasglivsg tslatvvalk tardqanala sirgvpqgrl vgytsnqahs
      181 cikrafdllg lgtdslrlvp cndafemdtd aliaqieadv aaghqpflva gtagavnmga
      241 iddletiadi aaehklwfhv dgafgaagrl gtaaadrltg iaradslafd fhkwfqvnye
      301 aglvlirnda ahrasfsdra eylrgtergl aggafwavdy gpelsrgfra lkvwahlveh
      361 gfdalgatid rnialagalr arivaherlq pmaptplnin cfrytsdrvd mdilnteivi
      421 alqesgvavp sttvlngeta irvnitnhrt qesdldvlie avveqgarle kvldr
//
LOCUS       WP_284376591             400 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Amylibacter marinus].
ACCESSION   WP_284376591
VERSION     WP_284376591.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..400
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44061
     Region          8..387
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 messaqnkty dvvivggaim gssvawflth npdfngsilv iecdptyefa stshtnscmr
       61 qqfstpvnvk isqycaefiq qfpeiardsr ipklsvqnfg ylylantpef athlqnnqmm
      121 qaqlgagtrt ldqealrray pfmnvediic anynnlnegy fdgnalfqww krlaiaggae
      181 yicnkvvgit tapdrasvqh ialnsgetis cgtlinaagp raaqlaqmag lnlpvephkr
      241 htyvfaaenp lgevlpltid pngmhvrsdg dyymagctpd idpavayddf aedhdlwmdk
      301 lwpslanrip eferikvmhs wvghyavntf drnaiigadt tvknmfying fsghglqqap
      361 amgralseli tyggfqtldl galgpqrlld graknetali
//
LOCUS       WP_284376619             240 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF1223 domain-containing protein [Amylibacter marinus].
ACCESSION   WP_284376619
VERSION     WP_284376619.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..240
                     /product="DUF1223 domain-containing protein"
                     /calculated_mol_wt=25898
     Region          22..236
                     /region_name="COG5429"
                     /note="Uncharacterized conserved protein, DUF1223 domain
                     [Function unknown]"
                     /db_xref="CDD:444181"
ORIGIN      
        1 mnffktlasa avlatataaq addtmivvel ftsqgcsscp padeilrkls khddvialsm
       61 hvdywdylgw kdqfaiakfg erqarynaqi ikrsrrvtpq mifngvaeva ggsgrsvsri
      121 nqavkalrnq heaadvswtq kgntikvsla snagelgrav lnlveyspme tvkikrgena
      181 grtisyvntv ksftrvgnwd gksnstvsfd lpktgdyali vqgynagpvf aarklagsgs
//
LOCUS       WP_284376771             186 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Amylibacter marinus].
ACCESSION   WP_284376771
VERSION     WP_284376771.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..186
                     /product="YceD family protein"
                     /calculated_mol_wt=20333
     Region          15..185
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 msknpkppaa qtdsviilae lsqnrprrfa lrlddaqtaq iqndltlrrl skvtlegeit
       61 segrtdwalt asvgasvvqa cvisnddikt rldigisrry lhdfeaydae ftteeelnae
      121 ieplpaeidl idliresisl niddfpring tsletslsap kgvtpltdea vkpfaalasl
      181 kdklks
//
LOCUS       WP_284376847             267 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Sulfitobacter
            pacificus].
ACCESSION   WP_284376847
VERSION     WP_284376847.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..267
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=29004
     Region          9..248
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mnrndyftfe tgqgsdvgck rkvnedsyla rpeyglwvva dgmgghaagd fasqtivhel
       61 nsiglavsad dlvarfdqrl trandviraq aaklesgmig atvaallvhq tqfdciwsgd
      121 srlyllrdgq liqqtrdhte aralldagsi taeeaanwpr knvithavgv sekpicervt
      181 gelqlgdlfl icsdgltehi adaeiaevll ryppqeacaq lieetvrrga rdnvtviamr
      241 csdapppaed emlydldnss ldtgsil
//
LOCUS       WP_284376857            1896 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Sulfitobacter pacificus].
ACCESSION   WP_284376857
VERSION     WP_284376857.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter pacificus
  ORGANISM  Sulfitobacter pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1896
                     /organism="Sulfitobacter pacificus"
                     /db_xref="taxon:1499314"
     Protein         1..1896
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=182787
     Region          40..1729
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 maavtvsgtg tfdvdggtsg avvisggtld asggtlasld vnggtahsis gsaavtgatt
       61 idnatltqsg gslntvtvgv sgtydvqadv sinalagaea savvdvnsnt ltiagsgnts
      121 fdgtlsggas gvlsntgggt ltlggdnssy aggfdisggs tiagdvnafg dgtgaitlns
      181 gtldvtasst vanaitvgan ggtvgatagt vatltgditr ngtltfgdgt lagggqvivn
      241 stgfsgtgst vvsenlelvl gspqsialln ngiavngtvd lngqnpstsn ltgagvitsn
      301 aanatftfng pttfngsfvd gttgimsidv nvggpntlql nsgsstysga ttitsgtlqv
      361 sgggaigdas avtvsagaif dvdasetvgs itgagsitva dthvltsaqt dlsatplitt
      421 fdgvisgmgg ltvgtptatg tltltnvnty mgpttvdggt lrlanantlv dtgavivngt
      481 ldlmttdeti gslagngsgi vsingntltv agtgagtttd fdgviqgagg qlvvnngpdt
      541 lrlggvntft ggttvnggtl amsatgslgd vtlnggafns agtvtgtati aggimtvtgg
      601 tvvaanndsg vlnitggtvs tvnsaattsn agtvttavvt agtftnnggg svgtatvsgg
      661 sfatsgsvtg sltnnggavs vtggavasls nnsgtatits gsvssmsnsa tasnsglvge
      721 ltqgsgtftn agnistanls ggsftttgtv gslnnagats eiqggtvsaa sntggsltis
      781 ggsvgslsss asttnagsvg eanisgstfv ntgivsgstt isgggvtnng smasvslsgg
      841 sitnaagtlg gvtnaggavn itggsageii netgtlsvan ggqtgavtns atavnlgtva
      901 slnnlegtfe nggtitgltt vaggivsntg smgdvatngg sftssagsis sitnnggsve
      961 lsggtvgavt neagtltlgl dagavtnsat lvlsgsatsl tntggtttvs gtvsgpttls
     1021 ggsltntgal nggvtvsagn ldstgvitga ldaaggtisl sgrldgalva gngdvtitgp
     1081 ltgvdsitnd gsgalviaag tttvdsgglv nnagsltvdg vlgggavlln tgtlnigetg
     1141 nvgmgitnng ilqadgaitg dltnsagrta niagsmtgni inaadgevnl agtqtgvien
     1201 rgdvtvtgtn vggvinyeql tvadegtvdg difntailel ngevtgdvin ngsassseir
     1261 lrvgdgavin lnggvsgdla nasdlnlrgr vdgtltntgl ttlqegvstv edfvndtqfi
     1321 adigtltygs ftnngvaair nagilsggvf tnageltlrd ggriaagtvv nnatlllpgg
     1381 gligadvinn atltavgnnq aggtltnsas geilmangst advitvsgda nlngrvtadl
     1441 nlspdrqgvd qinvgghlsg nvqvdfndms eefgtldggl tvfsygtldd gftfdqtglp
     1501 agraliygfq ndpeqnaivv qsganpavag iasgltltqs lintvvnrps spfvaglaae
     1561 dddpcgfgsw argvggvada tgqtstsigs feselsasyg glqvgfdysc fdsryagfdl
     1621 sfggiigana gslsqpvfkf dptsisldrs qqvsvndtdf nqtyagayig asrgrlfgdi
     1681 qlrfdrtafd lkntafiesa angglddlgv adqeydssst tisgsvgyaf plseasglvf
     1741 vpavgvshsr tsvdnlrfdg gtpdivgddg flviddivst vgfvsatlsr skvlpsgtaa
     1801 lnmfgtityy hdfgddttsr yfaldanglp egepltttss nlgayaelsl gvnytkllqp
     1861 gapggarqfd aslridgrfs ggldsygitg qmrfqf
//
LOCUS       WP_284377119             559 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Amylibacter marinus].
ACCESSION   WP_284377119
VERSION     WP_284377119.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..559
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=61260
     Region          184..557
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 maenekelqs idgwvgnpdl ivsagdnnhs gafrifrsfn lvrrifltsf iatglfligv
       61 lfitqpqnkt lnllrgyieq qadlqksvie yalrvmpear aadmntsllq ameglpqnss
      121 aglvlysdvl dkigekaarp fqnasqvsea egamsgtpel lrmlievmqg drlpiddvme
      181 peefntvllt llsqgnqkvq savlrgddtv lgvarsisfd gqevgyivlt tprgllssil
      241 sartrgifaf fglslfvsfc favvlarsit dplndlaraa eigktaelgq edarkvlipd
      301 lagrhdvvgr laaamgdmtq alysrietne sfaadvahei knplasmrsa vetlrvardd
      361 tgrrklldil emdvqrldrl vsdisnasrl daelvkeete afdlgkmlsn ivefhriean
      421 kngvdlfweg ptrpimfegl eerlaqvfvn lvtnaasfcv endairvwar vrgnrilavv
      481 edtgpgiped sledifrrfy sqrptddfgt hsglglaisk qiieahggti waenirsgqe
      541 ggqsevlgar fvvglpafl
//
LOCUS       WP_284377396             484 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Litoribrevibacter
            albus].
ACCESSION   WP_284377396
VERSION     WP_284377396.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 484)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..484
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=53318
     Region          9..481
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mtnnfikqts aklllvdder afcelcalwl eqagyqvvsc gdgqqaelef lkaeasgdgf
       61 dlvihdlalp ptfkpedgla ylkryhntpv vvltghdert lalkaielga edfiakpvdp
      121 dflkiivqrt vekhrlmkqv qdleaelksn qgpndelglv gvsqgthair elitriaptq
      181 vpvfiqgpsg tgkeiianai hglsgrsdqa fisvhcgaip aelleselfg ykkgaftgad
      241 kdrkgllama dkgtlfldei gemplamqvk llrvlqegsf ypvgsrdlvt idvrlvsatn
      301 rdlplavqqg efrddlyyri kgltittqrl derredippl lrafldryne qhntqltlsp
      361 evlhwfnhtd wpgnvrelkn tlesaaaisl gqqitlqela lirsdlmqee alnpgssfss
      421 sngdafaqna dlskpleeqv saleiqliqa amaandnnkt rsaqqlgitr qglinkinry
      481 glgl
//
LOCUS       WP_284377074             556 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Amylibacter marinus].
ACCESSION   WP_284377074
VERSION     WP_284377074.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 556)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..556
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=61167
     Region          20..>219
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 maqtdpnppm vymtkgamgl valfavlilg lcfwhninwd efhflsipfd margqvekpl
       61 qtfhahlfsw lthlpfseig mviagrivaf gclmgtlyfi yriasifapk pyailgglay
      121 vtsgfvighg asfradpfaa fllmgalyll fchplrarpl lvagfaaals vmitiksllf
      181 ipafvgaliw rgtsrdavlr ivlagvaavf mllamflwhk sqlnipsnis gaeatqkvlk
      241 nasgrtifga gflpakpylk vwliysivpl laalaalrag tgagrekwvl ltlclplgsv
      301 lfygnaypyf mpfitppmmv aaavglrrld grrfalggvt glmalggitq avltsqetqs
      361 aqrqtiaavh qlftepvpyi drngmitsfp kvgvfmsswg menyrkagqp ifqkaleqet
      421 plflidntry lqaalegdar ianccgffpk daqtlrqnfl pfwgdiyvlg krlqmakglh
      481 evtiyhagpy ildsqtpvfi dgqrieqgmq valsagihrv etshphqmrl rwagvvpdal
      541 ppppeteiyh lfwgir
//
LOCUS       WP_284377400             141 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Litoribrevibacter albus].
ACCESSION   WP_284377400
VERSION     WP_284377400.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..141
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=15425
     Region          <19..134
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mnvvrvsree vsklsfftsw vaagfpspad dyaerslsid ellikhpsat ylvrahgdsm
       61 irsgifdqdi lvvdrslear dgdiviaacn geltckyldl aarclvaanp kfpsipicde
      121 qdlliegvvt ssirlhracm r
//
LOCUS       WP_284377433             117 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator
            [Litoribrevibacter albus].
ACCESSION   WP_284377433
VERSION     WP_284377433.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 117)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..117
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13370
     Region          11..110
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mkhsdydcnl gcpveatlnt iggkwkgvil yhllakthrf nelrrlmpdv tqrmltkqlr
       61 eleadnliir tvypeippkv eysmsayget lvpvihalre wgirhlegle skerega
//
LOCUS       WP_284377499             246 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Litoribrevibacter albus].
ACCESSION   WP_284377499
VERSION     WP_284377499.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..246
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=26753
     Region          28..245
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mkagirkllt llcllgmstf sfaetlkvvl ydggspplff ekgdsntgiy vdllnaigkq
       61 sgiqfqfdyl ptkramalfe qgqvhvepgi npvwrsgsav pgeftiafak aedvvifneg
      121 klksvsgpqd lsgmkvgtik gffypgymda fgsgsihrqd slnedklmlk lvnnridtaf
      181 irkeaaqyri ktdaslksiq igsvigsadi mfrvhpskaa vipaineait elkangtvet
      241 iyaqyr
//
LOCUS       WP_284377519             465 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Litoribrevibacter
            albus].
ACCESSION   WP_284377519
VERSION     WP_284377519.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..465
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51309
     Region          1..461
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mnsrilived esalaqmlsm hfedeghevf hasclreare lvplhqpdli lmdqglpdgk
       61 gydllkelqe hntpatmvmm taehdlelai aaikagafdf vhkpiktdel nhtvnraleh
      121 qklarqvevl ssvsnealte prllgksqam ldvskeialv agsnarvlit gesgtgkelv
      181 araihhhsqc pgpfmainca alvdnllese lfghergaft gatdrkpgkf elaengtlfl
      241 deigemalpl qakllrvlqe gtferlggsq qlrsnarvia atnrnlpnei dagnfredly
      301 yrlnamqiql pplreraedi ptlvegller icrsegkpnl tttpeamall khyhwpgnir
      361 elqnvltqav irarsnfige qelciskdah ygvqsingft hsdnasthss nnanealstl
      421 adleakhiqy vldytgghkg ksakildisr paldrkieky gltvk
//
LOCUS       WP_284377543             769 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Litoribrevibacter albus].
ACCESSION   WP_284377543
VERSION     WP_284377543.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 769)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 769)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..769
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=83614
     Region          7..722
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mglksnisrr rfiqtavaat gaaalplsgl tgcsnsdsss ssstpsyfpq svmsgdprpn
       61 svilwtrvnd asvsgditla levasasdfn easlvlaqef taeadhdhcl kvrvinldaa
      121 tqyyyrftyv kngkanrtnt grtktaptag sdtdlkfayv scqdyngryy ntylplleqd
      181 ldfivhmgdy iyettgasfq ssegrsiqft dldgainlgd dgyaaqslsn yrqlykeyrs
      241 dsvlqklhel fpliaiwddh eysddswrnn gtyfdagkse estfrkqnse qawfefmpid
      301 heaaidetal naggtldiss dqlypntriy rdfqfganls lfltdyrsnr pdhiipedaf
      361 pgalamtqaq iiatldastg gngaaahaal fgsntfayin iddaaysttr aylrlimgsq
      421 yrdtyeargi saedagknya qlaneavtgn lsafyinaal taardsgala vpdsafisda
      481 dmtaaekgva fvhfgkqgly sdlgsryfvn kdlfdlyagf raaldggasq naygdaqttw
      541 lgtqlatngg twnvmgssvs fspllldlrd nsdnknrnfl dfsaipslfq nrfylnvdhw
      601 dgfpnakqnl innvfagnnv isiagdihst yvtdhgngsf dittssvtsg tfgsymdeav
      661 sglieglggn vediaplmsn ldflvpnsan addvsstlaf arlrehgvai vdvtadnfqv
      721 tmlnvptsen gneyiseswy nrsadfianl rthvisidea trtltppas
//
LOCUS       WP_284377566             279 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Litoribrevibacter albus].
ACCESSION   WP_284377566
VERSION     WP_284377566.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..279
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31492
     Region          70..165
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 maeidpaavn eyfnnvqpsi mgpymmdgfg fpntageyrf keelkivdrl laerdhvhdl
       61 stnpqtktva ldlgsgvgfw aeafaerfsq veavegsasl feelqarcts ldnvrahyan
      121 vldfqpespf dlafsggllm ylndqdvtsl lqklktqasp sgvvlcrest vrgesvtkqg
      181 eysviyrsle hyqqlfedsg fvvrtiqpnd pyilmqtgce likkwkqrip eraqmlplig
      241 ratylslrlt npwvtkipra lkvdfpvlen hffllepsr
//
LOCUS       WP_284377741             521 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Litoribrevibacter
            albus].
ACCESSION   WP_284377741
VERSION     WP_284377741.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..521
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=58952
     Region          5..519
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mttpineyvq ryelilrsmn egvygldrqg vatfinpaae rltgwsaeet igkpihsyhh
       61 htkpdgspyp qiecpifkta qtgvehkigy elfwrkdgss fpveysstpi fqdgelvgav
      121 vvfqdiserk laeqklqiaf dqvktltekl eaenrylkde iedelelqel igdspafrmi
      181 qtqieqvakt datvliqges gtgkemiaha iyqashrknr tmvkvncgai ptnlveself
      241 ghekgaftga ikrhigrfel anggtlflde vgelpldvqv kllrvlqege fervggttpv
      301 pvdvrviaat nrdlrkmvde gsfrtdlyyr lnvfpmvipp lrdrkedlpa lirhrlnkle
      361 kqlgkqlfgv sdqtlqrfss yrwpgnirel nnlleraaiv thspwlevtg feptgfeptg
      421 fegrefeptg feqrdyepte dshqrhtyid gpfdsalnkq ysssasstlp vltmaeaerq
      481 hilevlertn wvisgkqgaa dlldlppstl rsrmkklriv r
//
LOCUS       WP_284377761             701 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Litoribrevibacter albus].
ACCESSION   WP_284377761
VERSION     WP_284377761.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 701)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 701)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..701
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=79390
     Region          51..692
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mdaiiitedh slshqiklwc epncvsleqf stssfssnei tceclakrep dliivdlrds
       61 flqtsgdela nirtlvases phlymlyiid evdpeywlna heydyrvvmp apigkleakl
      121 nsiltnyrvm helksqvllm etlfdrsrdg iaisdkngnl litnhqlnsl fgyknhgldg
      181 knvsellpkp ynehfrqyls kfsstieeyk qghkfveege gldihgkiip velsitelpg
      241 lnemrylavi rdirqksadk ralskasqyd altqlpgrel linrltkrin qwdinkisqs
      301 pylllidinr fktfneslgh kvgdqllinl irrirfnlse qdtlyrvasd efaivlkpgi
      361 tendidcltg qilddlakpf fmgtlelymt vcfgvakanq dtdsaesllq canqallqak
      421 qsntpisyyr akentsstyr lelesslfka ldnedfelyy qpqvcvrngh isgaeallrw
      481 sdakhgaisp mefipiledt glidrvgswv iekacafwkf wqdegliqpe qklsvnvspy
      541 qfrntgllvs vksaleesgl spndlileit estlladden nlailnslks lgvtialddf
      601 gtgfsslsyl trfpidylkv drsflmnimd stndahlvta iinmaqslem kviaegvdsi
      661 eklnflklkg cdnyqgfyfs rpvsgnefir linhishmea c
//
LOCUS       WP_284377839             232 aa            linear   BCT 25-DEC-2024
DEFINITION  OmpW/AlkL family protein [Litoribrevibacter albus].
ACCESSION   WP_284377839
VERSION     WP_284377839.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006882
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..232
                     /product="OmpW/AlkL family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24735
     Region          25..231
                     /region_name="OmpW"
                     /note="Outer membrane protein OmpW [Cell
                     wall/membrane/envelope biogenesis]; COG3047"
                     /db_xref="CDD:442281"
ORIGIN      
        1 mkmnklssai laatltltga tatyaheagd iivragfanv dpkdattndi devsalgans
       61 niaadgdtql glnfvymlsd nigvellaat pfehdiqvsl antgtaldgt hnvgstkhlp
      121 ptlslqyylf dkdasfrpyv gaginytwff desdgtnfdd ldlddsigla fqagvdvmlt
      181 dnllfnasvy hididteatv kldqslplgg eelhadvdid pmvymvslgy kl
//
LOCUS       WP_284377832             196 aa            linear   BCT 25-DEC-2024
DEFINITION  LolA family protein [Amylibacter marinus].
ACCESSION   WP_284377832
VERSION     WP_284377832.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Tajima,T., Yokota,N., Matsuyama,S. and Tokuda,H.
  TITLE     Genetic analyses of the in vivo function of LolA, a periplasmic
            chaperone involved in the outer membrane localization of
            Escherichia coli lipoproteins
  JOURNAL   FEBS Lett 439 (1-2), 51-54 (1998)
   PUBMED   9849875
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..196
                     /product="LolA family protein"
                     /calculated_mol_wt=21510
     Region          1..196
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mnkrdfikas lvglaafcat pasaeqlpls alsdyfnsle saqtaftqin sngsqttgtv
       61 yikrpgrmrf eyngtnaplv lasagsiavy dgkskgkpki yplrrsplnl ilaknvnlet
      121 sgmvvkqtyd grftsiiard pkepnlgqiq lvftdnpiql rqwivtdqsr nrttvkldal
      181 ntstehsnkl fritkp
//
LOCUS       WP_284378118             230 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Amylibacter marinus].
ACCESSION   WP_284378118
VERSION     WP_284378118.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..230
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24936
     Region          163..229
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 madphqplfe aidatwpaaq ylshegwlir rgagggkrvs aatlqsddaq idaaisaqts
       61 mgqaplfmir ptdnaldcal aqrgfeivdp vvllakslgt trptahscyp qctpemqaiw
      121 aaggidqpri dvmqraagpk cftyltegav afsalhqgic mthavevapd arrqglgrri
      181 mqdiecwaqt mgaqrlmvls vrenrgamal yqslnmrqis ayhyrrapap
//
LOCUS       WP_284378145             708 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pseudomonas putida].
ACCESSION   WP_284378145
VERSION     WP_284378145.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 708)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 708)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..708
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=78402
     Region          31..699
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mdgahphpqp ldgnsvllvv ddypenlism rallarqdwq vltansgmea lsallehdvd
       61 lvlldvqmpe mdgfevarlm rgsqrtrltp iifltaneqs eaavlkgyas gavdymfkpf
      121 dpqilkpkvq alldqqrnrr mlqrltrele aarafnasil enaaegilvv daqgvisfan
      181 paisrllsap vqqlqgahll dlvqltsasl wnesdfyqay lerrifrvhd aqlrtlggel
      241 vpvalscapl padqqamvvt vldmsavrsl hqqleyqavt dpltgllnrr gfyqaaegal
      301 lrnersdkaq almymdldgf krindslghd agdrvlhwva eqlkdclgse allarmggde
      361 ftalfdslpy peqagryaer llerisishq vegldvslgv sigiatypdc ganvegllra
      421 adaamyaakq agrqqyrfyd qelngrarsr lmledsvraa veqqdftlvy qpqvgfndgr
      481 lrgfeallrw qhpsvgdvpp glfiplleea rlinrlaswi yrqgaaqrqa wyqrfpadlv
      541 lgislsraqf ampsladelh rviqlyqldp aqlevevaet slmynidaav kqihrlrelg
      601 vrvalddfga gdcslrmlrd lpidtlkldr hlvarlpdsa vdaalvrsvi slcadyritv
      661 iaegvetpaq aawlkangce yvqgflvayp mtatdasafp aifswpgp
//
LOCUS       WP_284378205             391 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudomonas putida].
ACCESSION   WP_284378205
VERSION     WP_284378205.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..391
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41888
     Region          5..313
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mpsaistdvl ivgagvaglw lnarlrrlgy stvlverasl ggeqtiksqg iihggtkyal
       61 hgaltgasea iadmprrwre alsgsgeldl tstrllsdah ylwspgtlag nltsffaska
      121 vrgrvdqvkg eqlppalqdr afkgkvyrla elvidvpsll anlaelagds llageriepl
      181 regddliglr vderdiraqr ivlsagagte dllhalglsq pamqtrplhm vmakganlkp
      241 lyahclgggp kprvtvtthp aadgqwvwyl ggdlaeadgv arepaaqiaa aqkeiasllp
      301 wvdqsqvrwa tlrvdraepa qsglvrpdna fladqqrllv gwptklalap dfsdrvishl
      361 erdgirpqvq adladlprpp lavpaweqll p
//
LOCUS       WP_284378294             398 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Litoribrevibacter albus].
ACCESSION   WP_284378294
VERSION     WP_284378294.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..398
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=43155
     Region          1..394
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mdviilgggv agvstaialk qngfnvrvfe rhkvastiga gvviwpnaay vleqlgvlnq
       61 ieevsgrpka mrrvsstgep lgamnlelin sqmgyesfsi lrrdlqevli skleslgvei
      121 eygksvvdic nsgvdkatvc lvdptgvkes vsadviigae grmasqtrty vlgdnqpvyq
      181 gfinwigvye snsseldtpl fdssildywg vgerfgivpv gpnkaywagg iaskdigtrn
      241 pehykdelts ifsewpepvr kviegtpvsr inkvyvhdhd paekwhknnv imigdaahap
      301 lptsgqgacq aledaiylaq clrdhqhdis safeqftasr fqkttsiima arglasslfn
      361 pdpqfcharn esskqsdfta aargmaqlwg qglpltvn
//
LOCUS       WP_284378428             260 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Litoribrevibacter albus].
ACCESSION   WP_284378428
VERSION     WP_284378428.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..260
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29700
     Region          27..256
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mtrfiglvfs lvlsliswcv caepvtvkvg gysfppfvni pddpnqnvng ltidliealn
       61 qlqntyqfvf vsttpkgryr hfnngridal ffeskkwgws dypveesdsy lnggevyiar
      121 kvagrdqsyf dsikdkrlma ilgyhygfan fnsdeiflre nfniyltssh rnsiralfsg
      181 tgiadiavvt ksylhqflae npeykdkili sdrldqvynh tilirkehal kvsdvnqylk
      241 tlseqgklqa iwskygihqp
//
LOCUS       WP_284378439             160 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Litoribrevibacter albus].
ACCESSION   WP_284378439
VERSION     WP_284378439.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..160
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18022
     Region          20..160
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mkiiktmwal cllfgmnlas agqqasdfal rsvadgnirl seyygdvvml nfwatwcgpc
       61 kqelpileql qkkfkragft vlainvdtpd vdvsgylkef nlsypvllde shsvvkeyni
      121 rampgsvfls rdgevrhvhl gyqegdqqky eqiieallke
//
LOCUS       WP_284378651             258 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Litoribrevibacter albus].
ACCESSION   WP_284378651
VERSION     WP_284378651.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..258
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=30137
     Region          36..236
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mrylavtlll llhsdpnfae nsfprveivc eewkdytnkd gsglywdilk aiyqpkgiel
       61 nlqtvpwkra krlvstrkkd vlvaeyylpq sdyvfpqihf avedpvvalf dpsliqwkki
      121 eslsparlaw vrgydfsdyl nfpielievn ntqqglkmls agrievlldy eqgvkeaakq
      181 ehmdisqfql eqalpgkkly lafakndhtp rlielyeqgm ksiylsgele rlykkwhqsq
      241 kylwfkdsik nqitptek
//
LOCUS       WP_284378670             248 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Litoribrevibacter albus].
ACCESSION   WP_284378670
VERSION     WP_284378670.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..248
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28786
     Region          27..247
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mfgrfiffli fslsievsan etdtnwvivt gsdfppytdl dypeggllik lfhivmeelp
       61 gnyeikwlpw rrgyletieg tyvgtfpyvh tperarhlly seaiigveer ffsranesrd
      121 fnnienykni vtckpvgynl naiqpfvdkg hislrwadnl dtcflqlsqg rvdlvdmdky
      181 vgfasikkag lkpmnfkmhe rilltqsmhl lvskkhprgk efldafnkal ltvreskvyr
      241 dllneylr
//
LOCUS       WP_284378770             270 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Litoribrevibacter albus].
ACCESSION   WP_284378770
VERSION     WP_284378770.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..270
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=30167
     Region          34..237
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mrssffacli llfsyplsaq aestllists nvmpwgieks dapnegllve fakafgdssg
       61 iryknrlkpy prvindirlg hadlavlfes peseriaysl gevtsvdvia vsksshrqiw
      121 slsdldgerv ayvrgskygh qfdqhkgfkk vpvnnmnqgl kmlmqnhvdv vvstdqsiyy
      181 gidslgiqsk wlkkllvist atanlylskq safvhkkdel savvkkmkag gilnhifygr
      241 dyissqelnr qetwhvpsls seyelitaiq
//
LOCUS       WP_284378776             690 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Litoribrevibacter albus].
ACCESSION   WP_284378776
VERSION     WP_284378776.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 690)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 690)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..690
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77965
     Region          49..649
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mhtelckpwt fvvllitcvg mvnpaegngv hashdatedf eslldlpiee lmqveitgas
       61 ltpksvitap ssvtvfdrer iqelgvdklh elinyipgfq sylssswshs ypisvrgrri
      121 ssgtseilll idgqrinnpr tggsgvvlpt fplsqierve firgpgasiy gsnammgvin
      181 iitrkeanev qvgygtyerk tadlalskri gnldvsvlah hdsddgedyt vlsnnkrlpv
      241 amkdqksykd iivnvqlndt rfnlqyydln stgyfaegst pnqdnvrdgd lltlqltqgf
      301 ewfsvksdit ieyqtsdati hgqveeagvf nfisnppsnd plmsdvqfnn vegyrafwln
      361 dwqvsdtqsv qfgseyrylh ipsaytlsnf diaalaiqdf piessdtlsi rtevqedtdr
      421 difgvfgqyq lelgdatqlt lgarydnyas igselspris lihalnnnhs lkllygqafr
      481 apsenelflv nnpvmignpd lesetvttwe aiwlaqwert flsfgyfknq fkdsimltqi
      541 lnnriqfqnv hlddthgvef elhhhlnnqw sartalmhlf nnaeqsfrea rtmgsvtiny
      601 asnqwsssls svyhgtretq lraatertql dsywlmngkl ayqwndqwty dlqvknlldk
      661 eydtpnshva mnnpvpnrgr eflasltfqf
//
LOCUS       WP_284378830             253 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Litoribrevibacter albus].
ACCESSION   WP_284378830
VERSION     WP_284378830.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..253
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29045
     Region          26..252
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 manflrlfls savgvsitln afakdldvaf gqnrppfifq esgkwkglev divqealsyk
       61 ghsirssahm vnrrleiava qmdydaaagv qyiddgtfys nsfvtyinya isragegvvi
      121 nsiqdltkyk paawqnayrn lgsefvkyyg pesdgdylkd ymefgnqeaq naffwagran
      181 viivdkfifl wyrkqlanqy ntgvdlvfhk ifpketsyqv nfrdknlrdd fneglqflre
      241 sgryqqlfdq yiq
//
LOCUS       WP_284379049             444 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Litoribrevibacter albus].
ACCESSION   WP_284379049
VERSION     WP_284379049.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469162
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..444
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=51599
     Region          48..165
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          75..99
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(76..77,80..81,83,106,109..110,113..114,116..117,140,
                     145..146,149..150,153)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          104..134
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          139..165
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mfrvqclllt fflslnlnas dlsafksemm kqvdiynays tqpeieklfv egkasvanqk
       61 lktlvpdhek tkydyfvlgn mlfqndfeas ynymlkaeqr dpdnplisfe raihehrlgn
      121 yakaldyylr yqksgaskvn vipdaylthv ylmlgqadka leswkgvnfr rthtavekam
      181 ytifskvnqe sdrqeliski rlgeplrlcd lhsldsnwei dwwnhtpkks yleydqklae
      241 sildpasalf kyvqlcqsgs kisdqqyvde lnklgffsel pesseliyes lrraistkht
      301 tpdaflktfe dkliafseky pldrkyfdvl aflysssgnk eklkaidrhg wkvlklekya
      361 qsylasldpg sdeymtalde slrdfpfsig lniyrlsiek qrtrdafiqf aaaqfanvkn
      421 nwagpyrlnd ymtnlkyele kldk
//
LOCUS       WP_284379055             262 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Litoribrevibacter albus].
ACCESSION   WP_284379055
VERSION     WP_284379055.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..262
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29428
     Region          34..258
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 msrhvlsvit lfflvffsfa ssaspstgik rstlkvgise tdyypfyfee ggkitgaaae
       61 ivsalaeqlr yeltfkrfpw krvqhnlasg kidmvmlyfk tperakdvfy vevphihess
      121 slitlksrdi afngdinqls sykfgnvngy whgeaysnhp tlvkrafsst telltvlkrg
      181 gidiavgnkp vltqlantmg lsdqfkflep kidyapdyia fskaspnapk lveefsdalk
      241 kflkspeykq ilkkygfdlk ak
//
LOCUS       WP_284379088             144 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Litoribrevibacter albus].
ACCESSION   WP_284379088
VERSION     WP_284379088.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..144
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=15690
     Region          9..144
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 miqasssvsd nevpsleltp lidivfiviv fllitanapl lklpvqipea tenpsadvis
       61 eetlvitvas denrwalged tyeewnelks almarmqsqq salnplsisi atdnsataes
      121 lvkvmsflne hqlknvqilm qqpn
//
LOCUS       WP_284379178             362 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Amylibacter marinus].
ACCESSION   WP_284379178
VERSION     WP_284379178.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..362
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38699
     Region          12..360
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mnfidlaaqq drlrekidag iaavlahgqy ingpevqele erladftgas hciscangtd
       61 alqvalmavg vgygdhvitp afsyiataet vavlgakpiy vdidpitfai dpalieaait
      121 pktkaiipvs lygqcpnmda ineiaarhni pviedaaqsf gathkskrsa nlttigctsf
      181 fpskplgcyg dggaiftsdp dlavvlrqia rhgqdrryhh irvgvnsrld tlqaaillpk
      241 leilddelka rqkaadyyta gfaghngitt pdiapentsa waqytlrvnn rdqvqdalks
      301 agiptaihyp lplnqqpava ddtatlphgn laatqvislp mhpyistsdq drvietliqa
      361 ah
//
LOCUS       WP_284379249             560 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Litoribrevibacter albus].
ACCESSION   WP_284379249
VERSION     WP_284379249.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..560
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=61115
     Region          19..387
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mkknntvnkp sstlsgdsae qkrvlvvgag pvglamaasl kqhdiqcdvv eqndgptels
       61 kaigihaitl elantlnlsh dfnkagkahk varlnsggkt vlsinfdkve sefsqvlalp
      121 qcstealllk rlkefggdvn wgvalesida lddgrckvql cqngerteti ydwvlgcdgt
      181 hslvreqmgv dfaggeydka fllgdvkidw dspqkddlqf flsgkgyllm vplpdgmhrm
      241 icqtsndfid dgqggrrqva ledlqaivde kgpggitvhs pqwltcapfy hrmassaikg
      301 nmallgdalh lysplggqgl ntgfqdvfnl awklayhlkg yadrslvesy aferlqvaqr
      361 vqdvtaktts fitgtapwlc farthllpwy gkrasvqdtl pwlysglkqc yldsplngns
      421 qhnalipgqr lphiqvktsd gseqaisslv hgtefslllv shqgqvlpdn ngieqaisvc
      481 eqlpvnlisl nqplaeaanl aikslglkrw iskkeqlwcl vrpdghvait agikdfhtie
      541 tylksvfqns eintatriaa
//
LOCUS       WP_284379254             325 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Pseudomonas putida].
ACCESSION   WP_284379254
VERSION     WP_284379254.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..325
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=36427
     Region          59..322
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 matieqrpng awrtkirrkg yptlsatfdt kaeaqrwaae iegdmsrarf vdmreaestt
       61 leealdrysr evtstkkgak qemtriakwk khklakkgla airssdmaay rddelkegks
      121 tatvkldlav ishlftvaik dwgieglsnp varlrmpkga ksrdrrptaq elkdvikaag
      181 dihaempaii giavetamrr selltlrren vkakhviled tkngtrrlvp lsvrarnlle
      241 slparldgkv fslvphsvsq yftracraan vedlhfhdlr hegtsrlfek glsmmevsti
      301 tghkslsmlk rythlcpdtl adklg
//
LOCUS       WP_284379474             301 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family oxidoreductase [Litoribrevibacter albus].
ACCESSION   WP_284379474
VERSION     WP_284379474.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Blankenfeldt,W., Kerr,I.D., Giraud,M.F., McMiken,H.J., Leonard,G.,
            Whitfield,C., Messner,P., Graninger,M. and Naismith,J.H.
  TITLE     Variation on a theme of SDR. dTDP-6-deoxy-L- lyxo-4-hexulose
            reductase (RmlD) shows a new Mg2+-dependent dimerization mode
  JOURNAL   Structure 10 (6), 773-786 (2002)
   PUBMED   12057193
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437758
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..301
                     /product="SDR family oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009226 - nucleotide-sugar biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0019305 - dTDP-rhamnose biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=33673
     Region          2..290
                     /region_name="RfbD"
                     /note="dTDP-4-dehydrorhamnose reductase [Cell
                     wall/membrane/envelope biogenesis]; COG1091"
                     /db_xref="CDD:440708"
ORIGIN      
        1 mklmvvgses qvgselvtll etqgidfvaf dsdeqlfidq rdiaqliqeh qpdflinstl
       61 ypfvdraeae iercrlknle ipralakacs tvdipmlhlt spylfdgdkv gpytekdvpn
      121 pvnlygeihq tseeavsail ekhiilrlgl vfssgednfv grvldhggqd ermevigqql
      181 acptsacsaa evilaickql sceinvwgiy hycdveavtr refleaviee aerhpelnar
      241 hveqvsssqh kgsakrpmna vlncqkllyt fgikqrswrv elakvvvkla drrlknsepa
      301 n
//
LOCUS       WP_284379490             570 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Pseudomonas putida].
ACCESSION   WP_284379490
VERSION     WP_284379490.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..570
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=61534
     Region          1..539
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msdktltveg lnvafddgsv vrdlsftlpp grcvalvges gsgksvsarc lvglagarak
       61 vsarrlsfag hdlldlserq wravrgkdig fvlqdalvsl dplrpvgkei levlqthgyg
      121 drhtrtarvh ellervgvpd velrarqrpg qlsgglrqra liasalaldp alviadeptt
      181 aldatvqaqi levfqqikar gaslliishd lavvaqlade vvvlrhgdvv eqgpmqqvls
      241 qprhpytral laavpaehpr gsrlspervg vrsqpwarsh sdvllegrgl gkrylgpdgl
      301 vrqvvqgvdf tlragrtlgi vgesgsgktt varialgllq pdegevlyrg qpwnrpanav
      361 seavrrplrg eisviyqdpl gsfdprwsva qilddalqva gieaparpar iavllnqvrl
      421 paalaqrrpl qlsggqrqrv aiaraiasep kviicdepvs aldvsvqaqv ldlladlqde
      481 lglaylfish dlgvirhvsd dvlvmrhgqv veqapveqlf dnpahaytrr llgavprlpg
      541 sgaelvvppl dlvheafdlf detrlwkiai
//
LOCUS       WP_284379557             502 aa            linear   BCT 25-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Pseudomonas putida].
ACCESSION   WP_284379557
VERSION     WP_284379557.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..502
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=53880
     Region          23..501
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mdnkvkaylq afgvseatqr flskpqrmfi ggawleasdg vsaeviepst egvlaripmg
       61 tredldravr aaraqfdggp wsqlkplere rlihrladli eanadelaqi esidmgksva
      121 qaravdiqgt vdtlryfagw askihgrtve pslpgnylay trkeavgvvg aivpwnfplq
      181 tmawklgaal atgctvvvkp aeltslsalr faelvqasgi pdgvlnivtg rgsvvgeams
      241 shpgidklsf tgstpvgtsv gkvamdqmkr ltlelggksp vivfadadie vaaeavangv
      301 ffnsgqvcda gtrvyversv ypqflealar ytatlkiapg ldpdcfispm vsrqqqqrvl
      361 eyialgkaeg aqvyyggepv egpgffvqpt ifancnndmr vvreeifgpv lvtapfdtqe
      421 qalelandse fglaaaiysn dlgkvhglip rlragtvyvn ahstldpsmp fggykqsgyg
      481 kdmgaeqlef lletkavwit lp
//
LOCUS       WP_284379574             394 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Amylibacter marinus].
ACCESSION   WP_284379574
VERSION     WP_284379574.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..394
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=43002
     Region          1..375
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mkiailgcgi gglaaaifaq ragfnvslfd qfdqpqpvgs glviqpigqh vldrigvldd
       61 aiargakgyh mlghdarski kvldvsygpm grdmfglgih raalfdillg alkssgaevi
      121 nnhrvasstl vedarylhfh ngaeigpfdl vidatgagsp isplrakplk ysaiwgtvdw
      181 pdstclnqnm lqqryrrask migilpigli pndptpkaal fysmpragyg awrdaplrdw
      241 qsearalwpa ldpfisqits hdqmtfaqys hgtlrrpfat rlvhigdaah raspqlgqga
      301 nmalvdadtl itclqnhspp halaayarar rwhietyqal swlftpmyqs dsrllpllrd
      361 rilaplstrq parglltrlv tgtliaptfg lrsr
//
LOCUS       WP_284379576             142 aa            linear   BCT 25-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Amylibacter marinus].
ACCESSION   WP_284379576
VERSION     WP_284379576.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Schwartz,C.J., Giel,J.L., Patschkowski,T., Luther,C., Ruzicka,F.J.,
            Beinert,H. and Kiley,P.J.
  TITLE     IscR, an Fe-S cluster-containing transcription factor, represses
            expression of Escherichia coli genes encoding Fe-S cluster assembly
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 98 (26), 14895-14900 (2001)
   PUBMED   11742080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..142
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=14998
     Region          2..135
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mqlskftdyg lrvlmhlaac hplrvsvtqi aasfdisehh vakvasalvk ggfvisgrgr
       61 tgglvlatpa dhinigavvr hltgdvpvae cfakdgadca afaqcglrgp lqraqqafye
      121 vldnytlkqv vkdqklmaal la
//
LOCUS       WP_284379577             277 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Litoribrevibacter albus].
ACCESSION   WP_284379577
VERSION     WP_284379577.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..277
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=31974
     Region          56..259
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mgfykpvlas ltlalvsgvl iaspvtgnsa ssqhtlyvsa idwcpqicpt tpdkpgylve
       61 middlfrese fqldfeyvpw sraiyrvktg qtdallspsk eeapdlryhl eplsyqthcf
      121 wklkdsdwhf kglesltskp fviyrdhsyv sffasgkvpi nsdhyfeisy deryipraiq
      181 lleakrantf iftvnsvify qqmqkrqplv vdecikrdel wfalspkpsh kidaiqahld
      241 tslgsykkte ryrallnkyn vilpalyner phtendr
//
LOCUS       WP_284379645             292 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Litoribrevibacter albus].
ACCESSION   WP_284379645
VERSION     WP_284379645.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..292
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=34092
     Region          20..289
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 msskdeadrg nglqntmfgq fddqsyeqwr alieqrtglq ladhlrtylq gglnrrmklh
       61 nihdyeqyle yvtnerngik ewselidtlt vqetqffrhl dsysfietyl kelvdssert
      121 rsiemwsvgc ssgeesysla mlaekvltes ehmasygvig tdislsaiss aklriykark
      181 adwipdhyhh cfdrldntik ikqriadrvc farvnildld rvpirdmdii fcqnlliylr
      241 kwrrkevvnr lserlkvggi lvlglgevtd wshpklrqvd srdvlaferf ka
//
LOCUS       WP_284379700             139 aa            linear   BCT 25-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Amylibacter marinus].
ACCESSION   WP_284379700
VERSION     WP_284379700.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Schwartz,C.J., Giel,J.L., Patschkowski,T., Luther,C., Ruzicka,F.J.,
            Beinert,H. and Kiley,P.J.
  TITLE     IscR, an Fe-S cluster-containing transcription factor, represses
            expression of Escherichia coli genes encoding Fe-S cluster assembly
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 98 (26), 14895-14900 (2001)
   PUBMED   11742080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..139
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=14902
     Region          2..131
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mkrnsrlsla lhtlghmavn prkmrtsaei aehagtnpvv vrrvlgklrq agllisekgh
       61 aggwqlarep qeitladiyl aldesliatg rteepsrcsv ehalhqkvas vmadieksli
      121 erlasttiae vggaesghl
//
LOCUS       WP_284379756             717 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Pseudomonas
            putida].
ACCESSION   WP_284379756
VERSION     WP_284379756.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 717)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 717)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 717)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..717
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81252
     Region          22..653
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mpvsiliqgr fvfpgtppyp rlliltallg gpamaddlfi dntdlpqvlt atrlkqspaa
       61 vpgsmtvlds elirasgard ipellrlvpg mmvgynagnq ptvnyhgsnv ndarrmqvli
      121 dgrsvyragl atvdwsdipl amedieriev frgpntvsyg analmavvni ltrnpadshg
      181 trlkmtrgqd gindfyashg fgweggdmrl slsgqqddgf denqfgqdyr dsrrltrftl
      241 nashnlahdq tlewqlaake gsnqrpytyk pvfgdyqags dadvnakdya gsmrwtkdfs
      301 sehslyiqgs aqhfdrqqvw racdalqsfs pdltqlwqmn pdfaekvvya lrsgeqvstg
      361 dpvlnelltk vkqqwakdgr qqvcgdvdqs tretrydlei qdtlsltdsl rllsgmnyry
      421 dradsqtyfn gsiddqtwrl fgqlewrade hwilqggamf edsrlsgssl tprvavnyli
      481 tprhglravy seavrspdmf ennvnwsytv knltptpnaf klqngeyfvk trgpgdldqe
      541 rmrsrelgyn gyfsdidlnm dvklfydeit gmiseplknn qyiasnanka rfsgseaqld
      601 wrptlrdrlr ltyayvdawa snpndrrlsa rnsgsagwmr ewgdgwssal fyygddalnq
      661 yryerldlrl akrfrvhgsn lelaalwqqr lddepttaiq nrfdsrhrls vsaelef
//
LOCUS       WP_284379801             346 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Amylibacter marinus].
ACCESSION   WP_284379801
VERSION     WP_284379801.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..346
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=37286
     Region          6..343
                     /region_name="Tdh"
                     /note="Threonine dehydrogenase or related Zn-dependent
                     dehydrogenase [Amino acid transport and metabolism,
                     General function prediction only]; COG1063"
                     /db_xref="CDD:440683"
ORIGIN      
        1 mnnetmraay yrgdktfvve qanktapkag evtlriaycg icgtdmhvyh gnmdarvgln
       61 rivghemsgi ieavgegven vqlgqkvvvr pldhcgdcpa cnegyehvch nlkflgldtd
      121 gamqeywtvp ahtlhilpdd lrldhaalie pvavachdvr lselkdgedv vvigggpigi
      181 lvamvardlg gkvtisevne nrlaiaqklg fdtinplkad laseintktn gkgaevvfev
      241 sgsqpgvdam ttvaatrgri vmvaihaskp tidmfqffwr elrllgarvy epqdyekaik
      301 viksggvdad tvitdispla diqaafedld rnptamksli kvgela
//
LOCUS       WP_284379848             239 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Amylibacter marinus].
ACCESSION   WP_284379848
VERSION     WP_284379848.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..239
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27202
     Region          1..>224
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mnirlrhdai vrslrrngtt tidqlaeevg asrrtilrdi stlrdegfvv hsdvgrgggl
       61 qldpqsvqtk arltvpevfa llisvaamra egnlpfsdla daglakieks lpsdkvrdlr
      121 afldclhvgs lsshqdlsdv tridadllpv fettflnhqy irfdyrdakn rksqrqvepq
      181 amlilpplwy lvawdptrkd frhfrmdris nptaivdqnf rrrhvpfedd vcpyselvr
//
LOCUS       WP_284379916             356 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Litoribrevibacter
            albus].
ACCESSION   WP_284379916
VERSION     WP_284379916.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..356
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=40078
     Region          59..299
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 measvlykeh tpkelvsqts iktnsfqiqe llqhlqiqfq nsnatatnkt edcpsdvtaf
       61 mvffshwvkh rfdnitvrga eninpnrnhi fisnhrdill dpvlvnhali sqnhsaarci
      121 igsnltedps maalmklagc levprgnlpl kqkfvtlkrl sqhiqhslph hnvwiaqreg
      181 rakegfdqtn pavlkmltma kekgqsqtef ltqqsiipva isyqwdpsdt hkaletylkg
      241 lsgseystat rtdtmehlid sldrcqgeve irfgtplvas dniddvaqhi ddhvhnhykl
      301 fdshhaahhi inktvipehl taaakqlkar asqlpaaaqr kliqsyansy qqvhvr
//
LOCUS       WP_284379940             255 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudomonas putida].
ACCESSION   WP_284379940
VERSION     WP_284379940.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..255
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28766
     Region          22..243
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mrrllallll wstysqaeqp vlrfsvaesw smplvriesd qpvegllydl mqalakevgv
       61 rpeyhvmarl rlqeamnsgd idvrcyvstq wfndrpgdfv wsipllhqrd llvgragdsi
      121 plppeqlpaq aigtvlgyty stlqplldqg rlhredsrsq llvlqklqag ryrhavsnql
      181 slqwfnqglp aeqqlqalav ledqdlgcmv rndpaiptqg llralvrmkq sgeierivqr
      241 yggmanqepm svarp
//
LOCUS       WP_284380089             252 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Litoribrevibacter albus].
ACCESSION   WP_284380089
VERSION     WP_284380089.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..252
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28592
     Region          27..240
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mlraliafll sfyaaflhse evtinivgae fppyytkhsd nhgiigeviq kslentdfkp
       61 rfkikpfara lieaksgkad iiaglyktte reqffhytda iinakivlyt ltsnpikthn
      121 lndliskrig mirhssthed lsnnlnitev nsyqqgldml lrehldfmvg nelviqhlln
      181 gsrysnqaqn ikyippeisq entfiatsrn slyeaklfkq lnqgiealkq sgklqkiiqn
      241 nlknlstskn qp
//
LOCUS       WP_284380156             451 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Pseudomonas putida].
ACCESSION   WP_284380156
VERSION     WP_284380156.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..451
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=48976
     Region          1..437
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 maikvllved drvlrqalgd tleiggfayr avgsaeealg vvleeafslv vsdvnmpgmd
       61 ghqllaqlrr qqpqlpvllm tahaaverav eamrqgavdy lvkpfepkal lslverhaag
      121 rvaeeegpva cepasrqlle laarvarsds tvlisgesgt gkevlaryih qqspraaqpf
      181 vaincaaipd nmleatlfgh ekgaftgaia aqagkfeqae ggtllldeis empmalqakl
      241 lrvlqereve rvggrkpisl dirvlattnr dlagevaagr fredlyyrls vfplawrplr
      301 erpgdilqla erllarhvak mkhapvrlsp qaraclqaha wpgnvreldn alqralilqq
      361 ggvieaadfc lagaiplsag iepspevaae agglgddmrr heyqmiidtl raergrrkea
      421 aerlgisprt lryklaqmrd agfdveaslf g
//
LOCUS       WP_284380194             309 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Litoribrevibacter albus].
ACCESSION   WP_284380194
VERSION     WP_284380194.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..309
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=34966
     Region          84..300
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mkpvgfqvvl csllvtlggv pavvlgspps slqpeptpvs yqvlaahggt svpqaqtqtq
       61 tqtqtqtqtq kssaqtklvh isageyppwi setlkdngfi aqvirdsfel egysveftff
      121 pwkrnydqar rgkydatayw ytseerkkdf yysdplsvea thffyhkskp lknwetledl
      181 qgfnvgatdg ytyteefwal aksgklnvet tvkdklnlak llhqridvfp vekhlafsil
      241 qkefkahvih midyhpkplm ettghllfpk alktspellq rfnrglaelk asgrhdeifd
      301 stlfektqn
//
LOCUS       WP_284380223             215 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Litoribrevibacter albus].
ACCESSION   WP_284380223
VERSION     WP_284380223.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..215
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24374
     Region          32..144
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 madkykyigp lydflstiyg gesihnckra mlceehvkpg dkiliagagh gkdairaaem
       61 gadvtvvdls ktmleklqka fdkhpkdlkv nvvhadilkf eeydkydmvi anfflnvfyk
      121 dtmltfmdhl ikltkqggkf vvgdfafpkg nvisraiqkg ywyiaaiify fasdnaihei
      181 ynypelmker gldiadarhf rylgmncyts vlgvk
//
LOCUS       WP_284380238             627 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Amylibacter marinus].
ACCESSION   WP_284380238
VERSION     WP_284380238.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..627
                     /product="PhoX family protein"
                     /calculated_mol_wt=67766
     Region          26..622
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 msdknlvdlt wddfdevrdp rpneaqfdqv vdnaisrrgl lagaltfgsg aavfgtglft
       61 gaktagatea lkfgfrpidi atdhevhvpe gfetqvmvrw gdplwseaeg aytdtngvpv
      121 emsdkvfgen tdgmelfvvd gkeliavnse yvnpkinlpa eaegyprtaq evellknlqg
      181 vtvmevakga qgyavvvdsp ynrrithete mvlagplagd dlvkthadpk gmtvkgtmnn
      241 cgsgktlwgt yltceenfng yfgatgaqpv gqgyqrygig gegrygyekf darydisqep
      301 nephrhgfvt eidpanpnsv pvkrsalgrf khenaemvha kdgrvvvylg ddergeflyk
      361 yvskntwaeg qdpsglldeg tlfaakfndd lsgewlpltp dttgmsiaei lcftrmaasa
      421 agattmdrpe wvaanplkae aycaltnnkn rgvkpnaggd dtatnavnpr etnhygqivr
      481 wtpadenhaa sefvwdlyvm agnptlynnd yagssninag nmfnspdgma fssdgllwiq
      541 tdgdyknegd fagmgnnqml vgdpdsgeia rfmtvpngae vtglcwsadk tvafvgiqhp
      601 ggswpdgagk prssvvsvwr kdgyafg
//
LOCUS       WP_284380242              70 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Amylibacter marinus].
ACCESSION   WP_284380242
VERSION     WP_284380242.1
KEYWORDS    RefSeq.
SOURCE      Amylibacter marinus
  ORGANISM  Amylibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Amylibacter.
REFERENCE   1  (residues 1 to 70)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 70)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 70)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Amylibacter marinus"
                     /db_xref="taxon:1475483"
     Protein         1..70
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7514
     Region          3..64
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 meitvrldvm lalrkmksrd laaqigiteq nlsllksgkv kgirfetlak icaalecqpg
       61 dlleatlsae
//
LOCUS       WP_284380544             360 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Pseudomonas putida].
ACCESSION   WP_284380544
VERSION     WP_284380544.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..360
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39777
     Region          11..357
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mlkglllffc mamapakaev wpdpdwhndp apldwqavda yafparatae rsgirtdall
       61 iirdgrilhe ryapptsaat ahltwsisks vlatllgvaq gegrfqlqdp vtrfypamqa
      121 hpgvrmadll hwasgldwqe dyeyaplkss vvamlytrgr edmaaytaar etvaspgqrf
      181 lyssgdsnll aaalrgmlda sqypdypwha lftplgidsa vwerdragty vgssylylsa
      241 rdlarigllm qregrwqdrq llprpwvafn rtpfaaaeav pgeanpgghw wlnqplagaa
      301 rpwpsapadt yaalghwgqa lyvlpaqklv ivryaddrdd syqhdemlkl ilvalagkga
//
LOCUS       WP_284380972             373 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Pseudomonas
            putida].
ACCESSION   WP_284380972
VERSION     WP_284380972.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..373
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42274
     Region          18..367
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
ORIGIN      
        1 mndfkrlpad fcanadeaft ipanfytqaa vfehekeaif arswicvghr sevaennayi
       61 trevigesii vvrgrdsvlr afynvcphrg hqllsgsgka knvitcpyha wtfkldgela
      121 harncdnvvn fdkenstlvq lrveeyagfi finmdmdags vedqlpglqa rmreacavid
      181 dlhlaarfvs dtpanwksiv dnylecyhca pahpgfsdsv dvgqyshslh gnwtlqygla
      241 kpseqsfkfd envkdpsfag fwawpctmfn vppganfmtv iyefpvdaet tlqhydiyfl
      301 nkdiseeqqk lidwyrevfr pedlrlvesv qkglksrgyr gqgrimadrq rsgmsehgia
      361 hfhnliavah ldd
//
LOCUS       WP_284380860             696 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pseudomonas putida].
ACCESSION   WP_284380860
VERSION     WP_284380860.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 696)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 696)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 696)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..696
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=74873
     Region          18..690
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mltgsysssl vlislcvail asytaldltg riatakgraa clwmgggala mgigvwsmhf
       61 igmlafslpi dlgydlalta fslliavlss gfalwlvsqp slpglqlgfg alimgagiac
      121 mhytgmaalr mlpgidydpt lfgaslliav gasaaalwia frlrahtpyv rqirglaavv
      181 mgfaivgmhy tgmaaanfpe gsfcgalagg glqgdglvyl vlittlavla valltsvlda
      241 rleartaela rsltlanqel tqlalhdtlt dlpnrtllad rieqaiakva eqggcfalmf
      301 idldgfkpvn dafghhvgdl llkavatrlr ghlhsqdtla riggdefvll velrepndam
      361 dvavkqvnlv srpfrvaehd lqltaslgiv lypgngqdqh ellrnadaam yhaksagkng
      421 ysffdvsmns narqqlqllq dlrqaleqrq frlhyqpkfd aqacqpigae allrwehpqq
      481 glllpdrfig laektgliip igewvlieac rqmrewldqg yqgwrmavnl saiqfchagl
      541 vesvaralqq nnlpancltl eitettamhd adasltvlqq lsdmgvdlsi ddfgtgyssl
      601 mylkrlpane lkidrgfvre leqdsddaai vsaivalgqa lglrivaegv etdkqqdflt
      661 rlgcdslqgy llgqpvpaeq fmgklqamhq estaag
//
LOCUS       WP_284381139             440 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Pseudomonas putida].
ACCESSION   WP_284381139
VERSION     WP_284381139.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..440
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=50054
     Region          7..413
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 marttapltd tacrsakptd rpyklfdgdg lyllvypngr kgwrfryvkp dgregltsfg
       61 nypviglada rqkrletkrm laegidpias kqqakaeaav rghtferval dwhkemsvkw
      121 apghsrtvls rlkthvfpll garaivdldt fdlmqpleai kkrgtidval rvqnylqsim
      181 reakrlrlit vnpaydlegf isaprithrp alplsrlpel mdrienykgr tltrltvmls
      241 lhvfvrssel rfarwsefdl krgiweipdt rpaldgvsys trgtkmagdi hlvplspqav
      301 tlleqihait gyfdlvftsd arswkpmsen tvnsalrnmg ydtkteicgh gfrsmacsal
      361 vesglwseta ierqmshrer nnvraayihk aefleerrmi mswwsrylea nrqehisphe
      421 fanqtgsnvs slrarrgave
//
LOCUS       WP_284381153             447 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pseudomonas putida].
ACCESSION   WP_284381153
VERSION     WP_284381153.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 447)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 447)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..447
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48278
     Region          135..447
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mdglkghlrh slqlrlsaal availlvatl tgifsylsay dealafqdns lrqvaalhtr
       61 qgltfhysaa mpatpeddee triviqflad gasavhgdds rlplpipasv adglstvdvg
      121 hepfrvwvgk datgarfvva qeigsrnrda rnsawrallp failfpilll vvadlirklf
      181 kpvatlaasl dnrgdqdlrp iddlalasei rpfvqainrl lgrvsrtleg qkrfvadaah
      241 elrtpltals lqvegleaep mpaaiqaqvq qlrngigrsr klveqmlala aaqlaeplpg
      301 nvsvhsacrr vledlmplas rkqldigveg edtslplrnv elrvviknlv enainhappg
      361 gqvdvrilst hqavevvvsd dgpgiapeew srvfdpfyrg qghqvpgsgl glsivqtlvq
      421 rsggqievgf tnaasrsgws vrlrwpl
//
LOCUS       WP_284381163             449 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Pseudomonas putida].
ACCESSION   WP_284381163
VERSION     WP_284381163.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..449
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=48596
     Region          1..447
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 marilivddd aafrdslaem lqdlghavlq aettdaglhr lrtedvdaai vdlrlpgedg
       61 lvflrraari sqvpcimlta yasggntiea mslgafdhlt kpvtraalle tleralrraa
      121 htpdrpqaag asaaarepvd etelvsssea mrqvfkrigl aansdatali lgetgtgkel
      181 varalhrnsg rasgpfvavn caaipadlme selfghvkga ftgavndrtg rfreadggtl
      241 fldeigdmpl atqakilrvl qereitpvga nrvqpvnvri ivathrdlps avkegrfred
      301 lwyrlqvvpl wlpplrerlg dvlllaehfl rllggdspkr lsaaaarlll ahpwpgnvre
      361 lrnameraai lshgpvidve higlqpaaal tpgldidweg pmaqavarle remivralaa
      421 tagnraeaar rlglsrqqly rklaefnld
//
LOCUS       WP_284381190             551 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Litoribrevibacter albus].
ACCESSION   WP_284381190
VERSION     WP_284381190.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..551
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=63188
     Region          18..462
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mnsqlstetl dqktqnktaq vkeidvviag agfgglcmai qlreedndnf vllekkhdig
       61 gtwrdnsypg cacdvqshmy sysfapkddw skryapwnei qkyildtadk ynirpfcrfn
      121 qevtsavfde esgrwtvktt sgdvylcrhf ilasgplhvp qipkikglen fkgrvfhsaq
      181 wdhdydleck nvvsigtggs aiqycpeiap kvkklhvfqr tpawvlprdd rkylgvekta
      241 fklipgwrrl hrfrlywtne srvwpmfnps vakslsqiak awirfqvkdk alarkltpdy
      301 tigckrilis nkyypmfnrd nvelvtegik evkensivtq dgqerpidci ilgtgfvvdp
      361 riymkdfelk glggrelnnd wkdhteayyg tsitgypnlw mlvgpntglg hnsiifmiea
      421 qvkyilncmk aieqresdym dvkpeaqeiy nvelqklmkd tvwssgcqsw yqqadgrntt
      481 lwpkstwkfw letlnvkknd ynfirlandq igvdysadaq aentetadaa tkkparkkrt
      541 skksatepsa v
//
LOCUS       WP_284381244             580 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Bacillus
            safensis].
ACCESSION   WP_284381244
VERSION     WP_284381244.1
KEYWORDS    RefSeq.
SOURCE      Bacillus safensis
  ORGANISM  Bacillus safensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 580)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Bacillus safensis"
                     /db_xref="taxon:561879"
     Protein         1..580
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=65801
     Region          28..557
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mrkkrriqwt gaiifilllg llmrlaeiql fftesfskld inliqesvkq rteevvisdg
       61 rgefldrngq alltkeqpav ilfpflqydl prlqqtasil emeedelkkq ltetkkplil
      121 kdditkkklk dindmkysgv ygvymkekdk krlalhtlgf tsenpellrk rypdkkelsi
      181 rteigtfgle stfdefllpe qdtkllyhvd grgnplfgmd vkytaeahsf yplqvqttid
      241 edmqaemekv lkdqgvekgg avlldiesss vlamastpnv tsknrhearn ymltaiapgs
      301 vfktavlaaa ieknldqpqt mydcrknlyg epegkqevln ltdsfsqscn ytfaalaekl
      361 iqtddqiiek taaklglidr agwegdvyhk hhfkqfdree tgsvwgdkrd khvkkaiaqt
      421 aigqknvktt plqianmmaa iarggerkev kiaekvlyqn gttmlsfqnk rheggsidry
      481 taqklqkflr qvvtsdkgtg rrfqdlpfdv agksgtaqtg nqdkkgnply hkwfagyfpv
      541 ekpkyalvvv hldetsgrak tndafydivk kvneiekkqt
//
LOCUS       WP_284381248             453 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC1 kinase family protein [Litoribrevibacter albus].
ACCESSION   WP_284381248
VERSION     WP_284381248.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..453
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0004672 - protein kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=51315
     Region          13..437
                     /region_name="AarF"
                     /note="Predicted protein kinase regulating ubiquinone
                     biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport
                     and metabolism, Signal transduction mechanisms]; COG0661"
                     /db_xref="CDD:440425"
ORIGIN      
        1 msehdqghqk kgkwishrkr atklagmtas ivgkyasnri rssfqkshrt evakselyre
       61 igkqvvstlg elkgaamkvg qmlsqmqhlf pqefteelaa lqnqapsmdy svierqiile
      121 lgdypdnifa efskkpiasa sigqvhkatt hdgqevvmki qypgvekack sdlkhlrrll
      181 kfggllkvdp saleavfeel setlireldy leearqlkrf gefhqsdsnv cipsvideys
      241 tkcilttsle qglsikevpk qlpqdiinql gntlfhfiar qvfefnafhs dphpgnfafk
      301 sdgtlivydf gsvspisamh kqaflnclss ainrdydqln qallelnvrs qsnrripdef
      361 yklwtdifmt pfettdgfdf grsnvhkkvl kewksvlpyw sdfqpsadtv finrviggiy
      421 lmlvemgcqc qfrpalddfi qraelqqaea cps
//
LOCUS       WP_284381277             487 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Litoribrevibacter albus].
ACCESSION   WP_284381277
VERSION     WP_284381277.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..487
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54472
     Region          8..487
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mskiqagsls ssqiqsdfhq lgtsfftelk psgisnpnwv alsnstanll kldqsnvkse
       61 dlkvlsgnsv lqgsnplsmi ysghqfgvyn pqlgdgrgil lgeikgegdd lydlhlkgag
      121 ltpysrmgdg ravlrssire flcseamaal nipttralsl vkgddqiire rvepsamvcr
      181 vakshirfgs feyfyytgqk qqlqellnyt ilryfpllsi dedgyvafyr qvlertakmv
      241 akwqavgfch gvmntdnmsi lgetfdygpf gfmeafnpah vcnhsdhsgr yafnqqpnis
      301 ywncaclgqa lsnllpeaai kqilneypsm fgnyylaemr sklgfqeede rdaslvqell
      361 aalhqnqmdy tnffrglsga dfmaltdcse dssdslsqwl gkyqsrlede kycpqvrmvt
      421 akasnpkyil rnylaqiaid kaekndfsev nvlldilsrp yeeqfenday aqntpewgcg
      481 lqvscss
//
LOCUS       WP_284381288             138 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Litoribrevibacter albus].
ACCESSION   WP_284381288
VERSION     WP_284381288.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..138
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=15064
     Region          1..138
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mnfrtkkred vsvdltplid vvfllliffm vsttftketh leidlpessa eaemseqvel
       61 ieivvnssgg ysvngnslin nqldtlkrai qkesngntkl pmvvtadasv aheyvvramd
      121 aagqlgftkl sittkqaq
//
LOCUS       WP_284381390             445 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Pseudomonas putida].
ACCESSION   WP_284381390
VERSION     WP_284381390.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..445
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=48749
     Region          1..437
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mkvtvfgtgy vgltqavcla qvghsvlcmd vdaervasln eghcpifepg lapmleknla
       61 cgrlrfttda saaanyarlq fiavgtppqa dgsadlkhvf avvdsileha dgpkvivnks
      121 tapvgtvqri kariaqavad tsrfhvisnp eflkegsavd dcmrperiii ggaepaevel
      181 lrelylpfsr nreklmvmda rsaeltkyaa ncmlatkisf ineianlaeh lgadiemvrr
      241 gigsdprigy dfiyagcgfg gscfpkdlqa lrrsaeaegf epqllraves vneqqkgrlf
      301 skiqrhyprg lrgkvfalwg lsfkpntndi reassrvlle alwaagarvq ahdpqameei
      361 qrhygprvdl qlvpckedal rgadalvivt ewqdyrvlnl dkvpqqladr vvfdgrnlfe
      421 pehmaaaglt yygigrgqvq pacpy
//
LOCUS       WP_284381394             506 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Pseudomonas putida].
ACCESSION   WP_284381394
VERSION     WP_284381394.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..506
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56935
     Region          24..377
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mprfktlrae rlalialavl lvgagigwrq pmnvdeerfl gvalemlqsg nwfiphraae
       61 iygdkpplfm wtvalfshlt gspkvalylp gllsaatitw vlhdlgqrlw hrrigviaal
      121 lflatyqsys ilrtgqidsf lclwvalgfy gmvrhlllgp awgwfylaca amglgiiskg
      181 vgfvpalmll pyawavrqrw hgvvampaqg wrwslgllwl lagcavwllp llvsiahggg
      241 eaelaylkei llrqtasrya nawdhrepfw yffvmvipky wlplvlalpw lvpawrrqlq
      301 krdgrfllll gwvalvllff slssgkrkly ifpalpglvl aiapllpwll krwlqrrpaw
      361 rraftgvala wfalwfargf veplkegrnp hetlmseaar atggadlvlv dwreghwlfa
      421 rqpivhfgft gqskadaaay wlrhnptafa lipaselgrc faadkarrlg etsraewyvv
      481 gadadngqcq atapshvyhf awagsp
//
LOCUS       WP_284381403             295 aa            linear   BCT 25-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Pseudomonas putida].
ACCESSION   WP_284381403
VERSION     WP_284381403.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Niehaus,T.D., Elbadawi-Sidhu,M., de Crecy-Lagard,V., Fiehn,O. and
            Hanson,A.D.
  TITLE     Discovery of a widespread prokaryotic 5-oxoprolinase that was
            hiding in plain sight
  JOURNAL   J Biol Chem 292 (39), 16360-16367 (2017)
   PUBMED   28830929
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Fan,C., Li,Z., Yin,H. and Xiang,S.
  TITLE     Structure and function of allophanate hydrolase
  JOURNAL   J Biol Chem 288 (29), 21422-21432 (2013)
   PUBMED   23754281
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Wang,L., Grau,R., Perego,M. and Hoch,J.A.
  TITLE     A novel histidine kinase inhibitor regulating development in
            Bacillus subtilis
  JOURNAL   Genes Dev 11 (19), 2569-2579 (1997)
   PUBMED   9334321
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005226
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..295
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=32908
     Region          7..260
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 maeplvttpi rysfgadehl faevsesmsl eaffkgmavt raverlaldg vldvclanas
       61 fqirfdpdri apqallaavr gaeaqavaer slqtriieip vlyndpwthe tlmrfrdrhq
      121 dpgstdleya arvngladve afiaahsgap wfvsmvgfva glpfmfqmve rerqlqvpky
      181 lrprtdtpkl tlghggcfgc iysvrgaggy qmfgvtpapi ydpqqtlnyl kehmvffrpg
      241 divqfkpidr rtydqavanv eegrfdlrir pvefsldafl adpvgypqtl qevla
//
LOCUS       WP_284381436             255 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Litoribrevibacter albus].
ACCESSION   WP_284381436
VERSION     WP_284381436.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..255
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28731
     Region          28..249
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mflrnivisl sllsavsgha sapdqeliiv rgdenyppye ytennqltgf hielvkqaak
       61 eiqitpvfks vpwkralsmi edgtadaitf itkttvrerf slfleenrls ksysgfialt
      121 ghhlskrydg tlasiedlni gvqlgfkygn afdnasnirk ielssadkly stlyakridl
      181 aivsqnefle hqslgkaqgi eflkpafsef tnylaftkak dmsglalrfa nafkrfrqtk
      241 ayralvkkyh ipenq
//
LOCUS       WP_284381465             241 aa            linear   BCT 25-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Litoribrevibacter
            albus].
ACCESSION   WP_284381465
VERSION     WP_284381465.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..241
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27836
     Region          2..238
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mntlyitgag vsaesgiptf rgedgfwtig srnytpmema trqmythnpv eflswyyhrf
       61 atyrhhdpnd vhywladknl itqnidgldg kagnqdyiai hgrldqmtlf hqqgddvdth
      121 ttpwdnvdes dlehsllelf nidkghqqpe inkslkpyvl lfdeyytely riseaqqrml
      181 eadrmvfmgt sfsvnitqma leiaitqgip ieivdpnpve ipyqktsyhr mkasdfikte
      241 d
//
LOCUS       WP_284381535             352 aa            linear   BCT 25-DEC-2024
DEFINITION  saccharopine dehydrogenase family protein [Litoribrevibacter
            albus].
ACCESSION   WP_284381535
VERSION     WP_284381535.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..352
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37634
     Region          2..349
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 msvliygayg ysgqlisqea kqqgldvvla grdeaalset ahklklphlt fslkdkqalh
       61 lalskvslvi hcagpfssta kpmieaciat kthylditge vevfeyahss dvdqrateag
      121 iivcpgvgfd viptdcvasa lkaalpdash ltlafqggsa ispgtaktmv eslgkgvmir
      181 rngrikeatl keksinfgsg dktcmgiswg dvstayhstg ipnvevyvpa sskviqkmkl
      241 lrfgrwifkp kfiqrliqsq ieskvtgpda nvrsanpati ygearnewgk tvqarlktln
      301 gyevtkygav hlakhiltsd pvkrgsttps lllgaslise lpgsspitlf eh
//
LOCUS       WP_284381575             260 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Pseudomonas putida].
ACCESSION   WP_284381575
VERSION     WP_284381575.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..260
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27805
     Region          5..256
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mvpdtalitg asggiglela rlhaarrgdv vlvarsrdkl esikqelqtr ygvkvyvive
       61 dladpgaadr viaatealgl sidvlinnag fgghgkfver diaadlammq vnmgalttlt
      121 hhylkamvlr rrgrilniss tasfipgplq avyyatkayv tsftqaiaee vreygvtata
      181 lcpgavatgf vtagdlqgvd awknaktaqs vaqcgyeame rgelvafneg klrvmldwiv
      241 pllprklvlk msrkamekas
//
LOCUS       WP_284381680             374 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Litoribrevibacter
            albus].
ACCESSION   WP_284381680
VERSION     WP_284381680.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..374
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=42789
     Region          13..366
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mnptstslct pprllvdgss fypeildtlk qatksilien ylvedgelwg svsetlleaa
       61 dagvkvfcif dafgslglhn dfdrlslhpn isiklfnpih iglgfhnlrr thvklfivde
      121 kiaytggagi tdsfyqpsra lspwsevmvk vedqsipelc siftwkfnav gnkprslfip
      181 lkgpnyifqk rmvgwlyahh fsthwikraf ykklssanrr iwinsayffp trktirflvk
      241 kaqqgvdvrl llpgvtdvvf mkylargryk kllaagvtih elndrflhsk viliddwatl
      301 gsfnldvfsf rfnhelnfas tdscfvsdie gfflsklqsa ieikphewtn rqllskller
      361 ityrvahffv klik
//
LOCUS       WP_284381699             467 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Pseudomonas putida].
ACCESSION   WP_284381699
VERSION     WP_284381699.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..467
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52611
     Region          29..422
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mrclmfvcll icslpsfald rsrvegyllp nglqvilkng yerdhvairl vvgvglddfn
       61 ceqkelphll ehllfsgide tgeggleerl qslggewnay tssadttfvi eaparnqrki
      121 ldlllavihd tridakalat akriieredg ghyghlqrwl drqdighpas dqlatelglk
      181 cpersnlddm tleqvntlrd rwyaannmtl ivvggldrll paylertfge lpatepeerr
      241 tlesigqqae qrrnltrgwl gdsvklhwlf vepvldndhq atldllshyl dwalydqlrl
      301 rnglsygpsa kresfgdtgl lslnadlere didqavevmq klfdhlrkeg ldpdtferik
      361 yasvakesws tqgnsalady ywgalndysd grfanpvrkl rqvslaqana alkqllkedg
      421 yvriekpllg ydelyglvav llglilaagl lrwrrhgpek pggatre
//
LOCUS       WP_284381747             359 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Pseudomonas putida].
ACCESSION   WP_284381747
VERSION     WP_284381747.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..359
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=38845
     Region          1..324
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 marpgfrlav fatllallvv llgaytrlth aglgcpdwpg cygfisvpks eaqlahaelh
       61 fpehpveaak gwaemvhryf agtlamvial lavqalrrha rdgqpyrlpm lllgvvlaqa
      121 afgmwtvtlk lwpqvvtahl lggfttlsll fllslrlsra faplpklpls lrriaalall
      181 vvigqivlgg wvsanyaava cidlptchgq wwpaadfsng fhltqhvgpn ylggqldsda
      241 rtaihishrl gallvtcvll mlswklhrcg lpglarlvll alvvqvglgi snvllhlpla
      301 vavahnagga llllsmvlvn yrirvvdkvr vgighgwrlr pvagvgishh mrndswrrf
//
LOCUS       WP_284381813             358 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein [Litoribrevibacter albus].
ACCESSION   WP_284381813
VERSION     WP_284381813.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..358
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39983
     Region          10..351
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mpssphihai pvniitgflg vgkttailhl lkhkpanerw avlvnefgev gidgailkaq
       61 qadrqtsegn sdllikeipg gcmccvnglp tqvglnalla qnpdrlliep tglghpneii
      121 qmltgdnykt vvelqntitl vdpskiriek yqthdiyrtq lavadylvat kgdlydgpyq
      181 tdfdewvrel khqgrirpdc qtkwtsfgri dlewldghss adqsdhhdhd hdhdhdhdhd
      241 hdhghvldna slavpddqlf irkentgsgh vscgwifrqe ltfdamklqa lffglqvdrv
      301 kgvfkisenq sliinseqgm vtlketnvsh dsrievitse pmnwdqiese lilaaeai
//
LOCUS       WP_284381846             667 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Litoribrevibacter albus].
ACCESSION   WP_284381846
VERSION     WP_284381846.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 667)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 667)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13939702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..667
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=73358
     Region          203..516
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
     Region          478..664
                     /region_name="DUF3520"
                     /note="Domain of unknown function (DUF3520); pfam12034"
                     /db_xref="CDD:432277"
ORIGIN      
        1 mtiynpntek altvkhkplp wtislimlgs ltmgsltigs msgcalneap esgngtsasq
       61 ttrddldstq psltveaedv eagdvetdet drsvaqveyq qerlerames kpvapkvkva
      121 rqkaeklsgd mavsqgyqga apsaypaatm stattmsiaa mpnasmstmp apgfvppdlp
      181 esypgmmdee dlqnenyadl einsiksvae qpvstfsidv dtgsysnvrr ilnqgvlppk
      241 navrveemvn yfdyhypqpd qskapfsvnt elakapwsdd hlllrvglqg fepakehrpq
      301 anlvflldvs gsmsspdklp llkksllmlt nqltdkdkvs ivvyagasgv vleptagnek
      361 fkieqalqql qaggstngqq giqlayrlae qsfvkdginr vllatdgdfn vgmsdvealk
      421 glierkrkng islttlgfgr gnyndhlmeq ladvgngnya yidtlheark vlveelsstl
      481 mtiakdvkiq vefnpqwvae yrligyenrm laredfnndk vdsgeigagh kvtaiyelal
      541 vdsqgqrlep lryqsndmrn dtkvknspel aflklrykqp sedkshlieq pivlnkevna
      601 fasasqdfrf aavvagfgqk lrnnkylqgf eyqdminfaq kakgddpfgy rnefiqlvrl
      661 adslsne
//
LOCUS       WP_284381894             323 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein [Pseudomonas putida].
ACCESSION   WP_284381894
VERSION     WP_284381894.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..323
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35637
     Region          5..323
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mlqnipthvi agplgagktt lirhllaqrp anerwavlin efglvgldaa llsrdedgia
       61 igevaggclc cvngmpfqvg lgrllrksrp drlfiepsgl ghplqllaql qqapwagvlt
      121 iqpllmvvda qsmvrnerlp eaqqqafdas esvvfnksev vdeyakflin nifyekkifw
      181 tvqgklplsd lpalpkgsvd sssvdnmivd nlvdppaalw aepgqpicla qqggggwsig
      241 wrwhpgqqfy pqrlqaflra wpwrrakgvi hsvegwqsfn glngdmptwq psdwrrdtri
      301 elifdqpqsq palqaglsec rvs
//
LOCUS       WP_284382015             339 aa            linear   BCT 25-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Litoribrevibacter albus].
ACCESSION   WP_284382015
VERSION     WP_284382015.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..339
                     /product="Glu/Leu/Phe/Val family dehydrogenase"
                     /EC_number="1.4.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016639 - oxidoreductase activity, acting
                     on the CH-NH2 group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36853
     Region          1..336
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mfelmrehql pelhffqqdr lnaivaihst elgpalggcr fvpysdtasa aldaarlaqg
       61 msykaalagv pfgggksvil ypegefdrea lfeafgsvve qlngryitam dsgthvedmd
      121 iirrttshva shseigdpsp htargvfhgi kmileeelni pldkatvaiq glgnvgyalm
      181 ekliehdvtm ivsdinqert rramkeygvf vapvsellte pcdvlapcgl ggvitpelvp
      241 rlnckaiags annqllnles gellhrreil yapdfvinsg gliyasgsyn qlpknqienn
      301 lenltstltk vfseshkqnk psdqvavtma keiianhsk
//
LOCUS       WP_284382033             519 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Litoribrevibacter albus].
ACCESSION   WP_284382033
VERSION     WP_284382033.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..519
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57044
     Region          1..474
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mtdfdvivig agnagltaav aaqrggartl llerhnipgg catsfvrgdy efevalhqls
       61 gmgtddkpfi lrqifqklgi mdrlevvqeh slyrivmpge fdvtlpasvk glievlsnef
      121 peeadgiaky mklcetlcle afmmmpramr andenmlkas cpnyvkyglk stkdvldeff
      181 qseklkaiia aywcyigmpt kdipfmdmav miysyaaykp chikggsqai ssallesfme
      241 aggevrfncg akkiltenda vtavvtenge tfscssvisn sspihtfnel ldtdhppiqa
      301 aqdmksrrlg tsafvlyigl dcspqdigvn aassfiidsc deevahknmq smtppihtml
      361 tcynfedpsf apegkttlsl lclqygepwe sippedyakt kyefadhlid haervfpgir
      421 dnieelevgt pltmmrylnt pggaiygfqq ntqdgqlfre rmnaidglml agcwngmggf
      481 qptymigest graavkkikk kqaqqqasea vlnteaega
//
LOCUS       WP_284382112             278 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Litoribrevibacter albus].
ACCESSION   WP_284382112
VERSION     WP_284382112.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..278
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32001
     Region          13..278
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 msisgsirfe kndfdqfrqf lenesgivlg dnkqylvasr lrkimqeadl hdlkdllskv
       61 kfngrlkerv idamttnetl wfrdkhpyri lkeiifpefv sqkksslriw saacssgqep
      121 ysmsmmvdey nrtnpgkrvn qaqilatdls seileqakrg syeklalarg ldadlqkryf
      181 tenpdaswtv nrdiksrvdf rslnllssya slgkfdiifc rnvliyfsae qkqdiltrlg
      241 rqlnpngylv igatesltgl nhiyemiqcr pgliyklk
//
LOCUS       WP_284382134             179 aa            linear   BCT 25-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Pseudomonas putida].
ACCESSION   WP_284382134
VERSION     WP_284382134.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Schwartz,C.J., Giel,J.L., Patschkowski,T., Luther,C., Ruzicka,F.J.,
            Beinert,H. and Kiley,P.J.
  TITLE     IscR, an Fe-S cluster-containing transcription factor, represses
            expression of Escherichia coli genes encoding Fe-S cluster assembly
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 98 (26), 14895-14900 (2001)
   PUBMED   11742080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..179
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=19378
     Region          5..154
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mslysagvey gihcllflvd ergdsressv rdlaelqgvp qeylakvftk laraglvaat
       61 egvrggfrla rpsdeitvld ivnaidgpkk ifdcrevrer cslfegappg wategtcaih
      121 avmlgaqkrm eealaqqtil dlarrfgrka paefgqkvsa wmgerregkg agdipvsqv
//
LOCUS       WP_284382147            1119 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Litoribrevibacter albus].
ACCESSION   WP_284382147
VERSION     WP_284382147.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 1119)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 1119)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1119
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..1119
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=127801
     Region          73..>268
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          77..101
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          106..134
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          139..167
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(140,143..144,147..148,150,217,220..221,224..225,
                     227..228,251,254..255,258..259,262)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          173..198
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          215..245
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          617..844
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          765..790
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          795..826
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkplirilpi kekkrellti gditalesll gsmsveltkl ypvflndvml evslkqhglq
       61 vlieqasqip drqlasytrg alytlagspt dalhalassl eskegdplsc iyaarscvqk
      121 gllkeaaqly eaagdyrlpe swlelakvyn slgyyprahe cfekafevfn ddetllsliv
      181 flrdrlrmee qfrssyqqrl lilldvsmse lqdreaellg mkadvayirg ddqeaeslyr
      241 ealnldpnnl saevnlsycl lrqskfeegw alnsnrtava snavlqyegl sllpkwegqc
      301 lknktmlvls eqgvgdqilf vryllllqsr fvlkdivciv epriaslfef sdfgkvrfvs
      361 vdstklnaqg fdyysylgdl prnlgagtda tlfkseqyiy ahrtrvheyr dkyfklfgnk
      421 kkigitwkss srlsgdrknl elasmaplfe lenvqwiclq ygdvsedlyk lntafetniy
      481 vdetvdltnn lalsavqima ldlvvtvsna tahlcgalgv dcllltsksp mwywggdgek
      541 svfypsisiy rqkehnqwle vvervkktis enytsvtskn tisdvelhka ftagkyqqii
      601 erlsgepvas ltfaqkllla nsflkegfpt evtrvldycs ieekhseetl llyakvgiyk
      661 kqfaqaetil nsivqnertv nwylvyidlf lsqeihnpsv ehawktllki sssdqdldal
      721 vvyfsevvkk igqeqyfnvv kfnmlkqmle dfdrsfgkrn pvvncflkae mynlegqpek
      781 aiayyekaik ikpelkqrft ntlgycflrv gefkkgfqlv eerlmldkrl trsdsltyey
      841 eklkhkhlnk skgkvllits eqglgdqllg lqfvrklqty fkgkvvlkvd skllpvvket
      901 fsdllyvgsd ldqlpenils qidyqlpias isalipeife nytpvdqiik anpervqfyr
      961 nkykerfgdk kligvswrsa sptwkgrkdm nlddfkplls aediqcisiq ysdvkseidd
     1021 fnaangvslf ldesfdatnd lkelfcqiaa ldavvtisnv nahfagglni pvhllvkkmc
     1081 lwhwhantsq smwypsmtih rerefnewgq vmaelvnel
//
LOCUS       WP_284382162             488 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Litoribrevibacter
            albus].
ACCESSION   WP_284382162
VERSION     WP_284382162.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..488
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=54816
     Region          12..484
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mwrevnvlvv dnneerrtql giilnflgee fyltseddwl nvansisadd qavtapdvis
       61 ivgqvsdkea lltgikewdq svpvisveea esapveiqte slqrmcvgvl twpttynklm
      121 dqihrsqiyr eqfdlrrgqq qrrevqlfrs lvgtsraiqq vremmaqvad kdasvlitgp
      181 sgtgkevvar nlhhnsprkd kpfvpvncga ipaellesel fghekgaftg aissrsgrfe
      241 laeggtlfld eigdmplnmq vkllrvlqer tyervggtkm mktdvriiaa thkdlesmie
      301 sgdfredlyy rlnvfpiemp plkeriedip lllneliarl enekrgsirf nsaaimslcr
      361 hewpgnvrel anlvermaim hpygvvgvqe lpnkfrhidg feedetvhfp vevpassssn
      421 vmdpdapall pvngidlkdy lgrlekslis qalddsngvv araaeklslr rttlvekmrk
      481 lglskdki
//
LOCUS       WP_284382187             377 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudomonas putida].
ACCESSION   WP_284382187
VERSION     WP_284382187.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..377
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39890
     Region          4..366
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mklievdaii vgggivgssa altlaragqq vallerdfcg shssgvnygg vrrqgrslaq
       61 lplsmrahai wgqlrawigi dgeyarsghl klarsetdfd alkayarrtq afdlrlqlle
      121 rhelrqrfpw vgdiavgasy cpedghanpr lvspafaqaa rrngaqvheq skvlevghdg
      181 hrfsvhtsng qcfkapwlln cagawsaqla eqfgepvplt aahpamlvte plplfmtast
      241 gvegggiyar qvargncvlg ggrgfaltpt tarpgqaavl dilrsately palagaqair
      301 twsgtegylp ddepvlgpsl sqpgllhgfg fagagfqigp aagealaqci lhgapalsla
      361 afsikrfqpn hhkehls
//
LOCUS       WP_284382181             269 aa            linear   BCT 25-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Pseudomonas putida].
ACCESSION   WP_284382181
VERSION     WP_284382181.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Bagautdinov,B. and Kunishima,N.
  TITLE     Crystal structures of shikimate dehydrogenase AroE from Thermus
            thermophilus HB8 and its cofactor and substrate complexes: insights
            into the enzymatic mechanism
  JOURNAL   J Mol Biol 373 (2), 424-438 (2007)
   PUBMED   17825835
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..269
                     /product="shikimate dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27633
     Region          4..254
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 mirgstelva ivgspiaqvk spenfntwfa nnncnlamlp idlqeaalet fagtlrgwkn
       61 lrgcvvtvpy kqalasrldg lseraaalgs vnvirrerdg rllgdnvdga gflgaarkhg
      121 fepagkralv vgcggvgsai ayalgeagia sitlsdpsta rmgavcellg nafptveiat
      181 rvdglegfdl lvnaspvgmg gsaelplpaa llatlqaetl vadvvtspei tpllnrarqv
      241 gcavqtgpem afaqlghlga fmgvtplei
//
LOCUS       WP_284382414             699 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Pseudomonas putida].
ACCESSION   WP_284382414
VERSION     WP_284382414.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 699)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 699)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..699
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77374
     Region          56..699
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mlvpcrlspl tlglsllfsa glasaatttl pelsvtadse rekdnprvke vstatrtstp
       61 vryvpqaidt vkaanvldyg sntlgkaleg ipnvssgadt rfdsvrirgf easndfyldg
      121 irddsqyird lhniervevl kgpaavlygr gsqggivnrv skapepgrrs tieaqagsed
      181 lrslyadlsa dpsdtvslrl nmgnqdnnsf rdgidgsrql fapsiswqvt pdlnwlvqye
      241 ysrynrtpdr gipgvngrpa dvsrsttygd tqrdyiddra qslrsrlnyq lnetwqlrht
      301 lglftldsef dntyvtgyna snntvtrqrw qqdlntrnlf nnleaegdfd tlglehklll
      361 glefgnqkrd pllyttlpvk eggqavpgld lgnpdrsqqh ngpmtvfsdn htvvdsrgly
      421 lqdqirlndq wqvlagvrfd qfevettnkd grsepqdsns tsprlgvvyt pwrdhsfyas
      481 wsktfspvgg gligitpgak gngndakpee trqkeigvks dwldqrlttt laiyelelyn
      541 rrtrdphnpa nillsglqrs rgieltatgn ivgnwyvrgg iglqdativk dnnaqegnri
      601 ndvakrngsl fvtwkpelgw yaetgltlvg eryadnqntt vlpgygrwda lagyrthdwd
      661 vraalsniad ktyyssatsa aqiqvgdprs lvvtgsysf
//
LOCUS       WP_284382468             591 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Litoribrevibacter albus].
ACCESSION   WP_284382468
VERSION     WP_284382468.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..591
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=66369
     Region          125..381
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(259..260,263..264,266,290,293..294,297..298,
                     300..301,323,326..327,330..331,334)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          259..283
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          262..556
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          288..318
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          323..350
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          354..384
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          426..452
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(428..429,432..433,435,459,462..463,466..467,469,471,
                     494,497..498,501..502,505)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          457..488
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          493..521
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          527..554
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrhllwsaii llsgcatftn tstsdqtdqa ptqeaqsqtp eeyptrpfqt etlynllvae
       61 iagqrsqydl alsyyldeak ntqdpyvaar asriaqylne plaaaeaadi wrendkqnih
      121 ahltaanswl kqhevdksit alkdalalte sisleqiylt gkelpkelqq plidglsrii
      181 sehpnhirlh ftkalllsdy grdqealeam itlkksgemt pphyimlakl ysragqneat
      241 vntleegwdk ytgdktlgll ygqaladnqq tddaldilns ltqthpsdde ilisaalina
      301 elgqykaaed lflaatqtkq rdnawyflgq lheqqhhtdq aieayksvqe gknlisavtr
      361 tatllkdsqs lasarqylre lhssqpnkip rliqieaelv reasnldeal alyneaiele
      421 ptdgnllygr amvhdlkgni egmesdlkti liqdpnnait lnalgytlad ktdrleeaqs
      481 yierayilnp ndpaiidslg wiyfklrdye kaevlllkay qmfkdqevaa hlgevlwvqn
      541 kkdqalkiwi dglrhnpngp tlletlkrfn invnhknpqe saedaspanq q
//
LOCUS       WP_284382556             261 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Litoribrevibacter albus].
ACCESSION   WP_284382556
VERSION     WP_284382556.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..261
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29439
     Region          44..258
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 maslvnqlhr qfslrvtalv glllcsylsf agsgasvstv slgtgdwppl ispeakgfgp
       61 isqivvesfe qvgiapsirf wpwsraienl negnvdasya writderlek yffsepvydt
      121 gnvffyrkgy pfdwetledl kaykiagvqd yaysnelvea eaagdlkldr vvdekqlvfl
      181 llagridafp ashvvgkeli rkyapeqekd iaihpqwisk nplylitlkt kqgqqmlerf
      241 nqgltqlkes grydaiynhf q
//
LOCUS       WP_284382621             248 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Litoribrevibacter albus].
ACCESSION   WP_284382621
VERSION     WP_284382621.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..248
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27489
     Region          2..238
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mkfddikklh qkkyrqqfgh ylvegehlil elqkavaqsg idlhtiqlfv tekyqdwssp
       61 fekrvvsskq mtllsdtksp qgiiacvplp esapaadqsv sdqskserci ylhevqdpgn
      121 lgtilrtlaw fggfrlllsp nsvdpynskv vrssmgaifh vpmelevsld dlaerfdrfa
      181 yldmngeiik seafadfpcy lfgneargvp realtalnat aftipgngai eslnlasavn
      241 msvfqlsv
//
LOCUS       WP_284382289             291 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudomonas putida].
ACCESSION   WP_284382289
VERSION     WP_284382289.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..291
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=32700
     Region          34..282
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mrllamlfsg lllwcaavqa qvrsydaiia agelkvavyk dfapysfqdh gqprgvdvel
       61 aqalatalgv rlqlvwappg ekldddlrdy iwrgsplrhq qladlmmrvp ydhayaqrrn
      121 evgelenaqv vmfgpyqeer wqvaydrrrl psvasvavfq qhpigvevds vpsfyltsvf
      181 ngmlsakthh ypnvqqafga mqagqvdavm amrgevdwql hqatdpqlal aenaypnlgk
      241 qaweigmavh esnrqlayav eealealird grmkaiyasy glryqvpemy q
//
LOCUS       WP_284382647             132 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Litoribrevibacter albus].
ACCESSION   WP_284382647
VERSION     WP_284382647.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..132
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15307
     Region          2..128
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mhiyrtqvtd qdldhnhhvn nvvyiqwmqn aaedhgqtag iielsdkdng twfvrehniv
       61 ykqpampgde vmietwieni kgfqslrkye ikrtsdqvll asaytnwvyv dkdqgkpkki
      121 paefknmfnc pa
//
LOCUS       WP_284382659             270 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Litoribrevibacter
            albus].
ACCESSION   WP_284382659
VERSION     WP_284382659.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 270)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..270
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29530
     Region          1..253
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mssvvwitgc asglgkhlve afylrgyrvv atdinsgalt rhalterwpd dsvmcapldv
       61 tsaeqwsall sdvlekwgqi dyllnvagyl kpgyahqqsl deidrhldin vkglmygcql
      121 vgqqmtkqks ghiiniasta alasvpglnl ysaskfavra fslairhelk pygvnvsvic
      181 pdaiqtpmlt lqetyeeaam tfsgnkvlkv ediellifdr vipkapaeam ipfsrgvlak
      241 lgnlfpgltd rlvvflqekg kkaqrssyks
//
LOCUS       WP_284382720             345 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Litoribrevibacter albus].
ACCESSION   WP_284382720
VERSION     WP_284382720.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..345
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=36634
     Region          9..333
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mktritellg iehpvvlpgm swisvpelva avsnagglgi lasgplsrqe trdairrire
       61 ltdkpfgigv tlmmpgaeen akialeeevp vinfslgkgd wlvegakkyg gkviatvvte
      121 khalaaqksg vdalmvtghe aaahggsvts lclvpaiadl vdipviavgg fgdgrgllaa
      181 lalgaegvam gsrfatsles plhnrvkdtv vtkrvedtiy sknfdglyar vmktpmaeka
      241 tkrpmnfima alksfkaakm vdmplwklml gmlaqfdkir mlslfgaate kleaatidgd
      301 lekgvqfigq sqgvindves vqvlmdriin daknlsielt ktvvd
//
LOCUS       WP_284382812             264 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Litoribrevibacter albus].
ACCESSION   WP_284382812
VERSION     WP_284382812.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..264
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29950
     Region          43..263
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mknishiqtl vglwllmivs iiqpcysqsl sipspqskrl qlvtleyppy eysednqvkg
       61 vavnlvsdvf ktmghdisie ilpwarains iklgqadaif tafhtkeraa fadyskevli
      121 hqeislfale kspltfhgdl ttigqyqigv irkmsygkkf dqavidniiq ytqstssleq
      181 niekllsgri dfvvsnklga ldtlnkmnkr alirvlsppl estpsyiafs kqrnlthird
      241 afdrhlkqlk qtgryqeiid eyfq
//
LOCUS       WP_284382851             651 aa            linear   BCT 25-DEC-2024
DEFINITION  IucA/IucC family protein [Litoribrevibacter albus].
ACCESSION   WP_284382851
VERSION     WP_284382851.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..651
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73891
     Region          18..625
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mnrysestrp isfyfdpsln cffnallrew qdwhyrptad apfssecvys gssndsnsla
       61 psgwfqlqts dgllsipcmn ysttgrhhll apclinidgq lqtvdfqesv drvmrqssin
      121 svliqnnsqn csqdttqgmn asepksltdf irrahqsdtn lqqalayrea efdqlfgksl
      181 tfeqaesalf tghsihpcpk ardnfspedt layapefggh fqlqwyklht sclytretdg
      241 fdyqaliedl isqdpqaqaw qktlesdyvl ypchpfqhkv wqntarltdl isqgllvhlg
      301 qgtidwsatt svraiyskqs pwmlkfslsv kltnsirhlq peelvrgael crvlttppaq
      361 efeqrfadrf kilfeptaaa icdeagkpfe etivlwrenp fvegkdhnte vlatllqddp
      421 rsgqsrleqs lkqwqteysn attyanqate wfkryldvav kplliaqady gllfgahqqn
      481 ivltlsqgmp vkmyfrdcqg tgfsqlanql ytqylpdmaa dsanviedem airlfsyyli
      541 inatfnviss lsrsgeipes vfigqlqffl qdirtqgvkd tqcidyllns eelsakgnff
      601 vslkqlnent etdylamyhp mtnplkmsas eprpqrssae lihtdlatdi a
//
LOCUS       WP_284382917             572 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Pseudomonas putida].
ACCESSION   WP_284382917
VERSION     WP_284382917.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..572
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=62605
     Region          1..275
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
     Region          353..>442
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          402..432
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mielwpewlr plwllavpll gwllyklwhr rkragrwqmi lppafhgvll gggsgstskl
       61 pwvalglawv lvilallgps wqrveenrqr padplville ltpqmlaeds ppnrleqarr
      121 kildllehrr dsqtalvvya gsahtlvpls ddlatsrnll eaidpsimpk pgqradlavq
      181 kglallaqsg lgqgrlllig sslsaperqg iaqalgrqgp sllmlgigsr egapvrqang
      241 eylkddqggi llprldsasl kgfisgtggr yrhariddld lrglglfdnp ragrndgqtl
      301 qldswadqgy wlllplllla acagrrgwlf clplllalpq psqafefndl wlrpdqqgqr
      361 lleqnrpasa arqfqdpqwr gialyqagdy tgaaeafsqg dtaaahynrg nalarsgele
      421 aaldayeqal erqpdlqaal dnqalvqqll qqreakaeeq passdtqdtp gsetegnsss
      481 asnpaqgtpg ndeqasaeqp gegssnsqva pgnqagadds viqppqrpvs tsldaeqrqa
      541 leqwlreipd npaellrrkf wyeqqlhqet pr
//
LOCUS       WP_284382941             963 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Litoribrevibacter albus].
ACCESSION   WP_284382941
VERSION     WP_284382941.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 963)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 963)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 963)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 963)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..963
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..963
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=109354
     Region          <37..>170
                     /region_name="COG5373"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:444140"
     Region          331..963
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mqsttatvnd stlpdfrsge hqllkaqlkr laveskafyt lsllaslvvv itfwrhlpsw
       61 qtiswlalqc alplgqlafy sfiasnrqvs mrlkslftta gaalsglaws sifvaidpis
      121 tndqallfcl laslavyata afsayipafi sftiailmap fahlihnydl shsnlifvag
      181 lfsvflcysa vrinrstvva lkyradketl idnlthsmtq sdqlnqeliq evqqrvtael
      241 klkraheqle qtvdnrtqel qqtnhlleqe malhknttke llnsqnrlsk smevsqlglw
      301 ewdlendciy hshfhklfgs snttttqflk hlkshthped fraarkalie hmrgnteqyl
      361 vryrirqeng swlwfedsgq avewnekgra trilgtrrev tqvmehtekl rlgnivfqnt
      421 teaiaildrn fkfitvnnsf itmtgyelne vigktsveld dsvekletlk aigrelahnd
      481 lwqgeitdyr ksgsaypmwl kinlvrdssg lpshyiclls dltarkeidr klrylthydk
      541 ltglvnrdlf ldrlhtsmqh shrtetplal flinldrfkl indtfghgag dkvlrtaaer
      601 lsqvfsdadt vsrynsdefa iaieysddir tiqakakrai ellnqpvkva dkelilsasi
      661 gisltpthtk dmhtllnqae larnqakgmg gnvfylfeeh lndssaerlh lenelhnall
      721 knqfevfyqp kqnlkdncie saealirwnh pehglippvk fiplaeqtgl inkigefvlr
      781 tacqqarwws lkgfgdikvs vnlsaqqlka dgfmslltsi lketnleper lileitesll
      841 mddveatirq lqeirdlgvg lsiddfgtgy sslsylkrfp idilkidqsf ikeintnadd
      901 aaitkaiiam ahsldlrvia egveteesre flrdqncdli qgylvsrplt ndqmqrmlan
      961 faa
//
LOCUS       WP_284383022             666 aa            linear   BCT 25-DEC-2024
DEFINITION  IucA/IucC family protein [Litoribrevibacter albus].
ACCESSION   WP_284383022
VERSION     WP_284383022.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..666
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=75664
     Region          5..605
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mrqsarqiad hasfqafmns ylkevdpgvw hqanhwqqqt dqtlsatshq vlelklpsqh
       61 itlavgvsyr sqvgrhtlte vfqkplhqfd wqaldffsai lllikelyap apghpqsdqq
      121 rkkelellar liesqqvmtr yleqrlddpk lrnlnfidse qsilfghwlh ptpksrqgih
      181 dwqhqdyspe lcgefqlhyf svdralieqg silsqsaeai lqqiltqqst amdtlslpls
      241 edrllipthp lqaqwllhqd yiqqriasge iqdigplgak ftptssvrtl yseqldfmvk
      301 lsipvkvtns mrinmhhele agivvanllr tsqfshkypr fqtiddpayv svtlperees
      361 gfeliirenp fsrcqpnadq lsvislaalt qdgitedqps rlsqlihqla dnqqkeqqrp
      421 iaqvaaqwle hywqcaiepa irlydeygia leahqqnsll dvtdglpsry fyrdnqgfyl
      481 snahktalla mepqlantpe lfyddemiln rfsyylivnq lfsvinrlgi dqllpehqal
      541 elcvgwlail ekqltgqgkr lvesllsqrd iafkgnlltr ihdvdelqad qelavytkik
      601 npfraiafaq gvvtsetdsg qrlddqgtat aahtlhlnal isasergsat hfsdvsettg
      661 gqresa
//
LOCUS       WP_284383028             323 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein
            [Litoribrevibacter albus].
ACCESSION   WP_284383028
VERSION     WP_284383028.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..323
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36752
     Region          39..295
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 masahlqcry rpyrhrqcrq pdwpcsiskh gstgggarmk lsictisfrh qlvsidqlvn
       61 waranhfqgi elwgvhaknl aeqpsynkdw lagfglsasm isdylplqgp etaafqkvqq
      121 lcllakhwga tklrtfasnl gshqvteter qditrrmrdi cqwtaqhgit liveihpgtl
      181 adtmastlrl ledvnqpnlk infdvlhvwe sgadpveafq llkpeiehfh lknissadll
      241 svfsppnvys asgsreglvp lfegavdyqr fleyvmqqpd skfhhmdasl ewfgdqckqt
      301 lsqdryniqr leqqfdlpqr ivn
//
LOCUS       WP_284383096             325 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Litoribrevibacter albus].
ACCESSION   WP_284383096
VERSION     WP_284383096.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..325
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34348
     Region          38..145
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mnamtqwaar favaislsii sttasawcwf fcsddsdyak trypivlvhg mlgfdsvlgm
       61 dyfygvesal edkgarvypv qvtaldssea rgeellaqvq qilavtgask vnlighshgg
      121 ptaryvasvr pdlvasvtsv gsphkgsdva dlvqdisdgs qvvtvavsav vnglgslinl
      181 lsnnptdngq dslatlesln segaaafnaq ypegipssyc gegdyvasng vryyswsgts
      241 pytnvfdpad pflllasgaf alksgeandg lvgrcsshlg dvirdnysmn hldeingfvg
      301 ihhlfetdpv tvyeqqanrl knagl
//
LOCUS       WP_284383099             254 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Litoribrevibacter
            albus].
ACCESSION   WP_284383099
VERSION     WP_284383099.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..254
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28640
     Region          31..237
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mllalirsii fyiiifffsi aqntlgiiig lflpyelryr fiittwtssf iwllkvicgv
       61 ryeitgkhni pdqpclissn hqsswetffl qsictpqtqv ikrellwipf fgwaysllkp
      121 iainrgdkqn araqvleqgs qylnsgiwvl ifpegtrnpp kklgryarsg aalainagvp
      181 vlpiahnsgh fyinkefiky pgtiqvhigq pissegktae qltdevrawt erslqaiegv
      241 eqvsstfehp sitg
//
LOCUS       WP_284383114             274 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Litoribrevibacter albus].
ACCESSION   WP_284383114
VERSION     WP_284383114.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..274
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=31597
     Region          45..269
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mlvtlnqcvs elrvdlkahq eivlqlllai lilacsragf aepflivgtp eepfkmetse
       61 siqgidvdvi sevmaqlgve ydiqliasga riireaqqgr idmvlsfsfk eprtdylvyp
      121 eqsykdvswn ffyhednfgr fhydqlsdlk glkvgavnaw aytpefwhap fkieevskht
      181 llldmllhkr idlapmnlve tryrlkqrgl sntllylptp lisrpyfnaf vkfskhpmmk
      241 rvqagydqii rqmredgrin eiysaylgev ptre
//
LOCUS       WP_284383130             278 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Litoribrevibacter albus].
ACCESSION   WP_284383130
VERSION     WP_284383130.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..278
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=31309
     Region          <40..164
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
ORIGIN      
        1 msrrlplgrv latlmlslsl vsgvwalpke ieldrlmlgv etaiseqqwd kanarliaaq
       61 alddempavf yfyrgqvssq lgeyaeakqa leryleregk dgshyraslm llnqleekeq
      121 kqaqeqirsa satqlvlqda ahtdyieqlk tlylvespqe alelhintll snhryipgry
      181 rsdrkwmgsl yqiqthrgei avlekranpk ggyslnqsqv siygvnpyvg vscdsvgdqc
      241 wikhpetgkq wleleanska aesiaeafsh llrqmqgg
//
LOCUS       WP_284383137             233 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Pseudomonas putida].
ACCESSION   WP_284383137
VERSION     WP_284383137.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..233
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=24211
     Region          3..220
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mnplylasgs prrrelltqi gvpfsvvsap idetplpnes apayverlar akaaaglasl
       61 epsvqairgh arshrysadp vgagvpakap kgpavvlgad tavvldgril gkpenredal
      121 vmladlsgre hqvltavals dgqrvhslcv tskvrfrais adeaqrywas gepadkaggy
      181 aiqglgavfv tglsgsysav vglplcetae llgqfgiacw qspahtpevt nqr
//
LOCUS       WP_284383139             271 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Litoribrevibacter albus].
ACCESSION   WP_284383139
VERSION     WP_284383139.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..271
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=30476
     Region          52..269
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mkqriwssls lmlmvtltcp ssviadehiq spsqllfche neqafpwvmt vdgesqgldi
       61 elltqvsqkl nididyialp wkrclhhlel skvdgafaas ykqerlhmgr fpvtlkgnld
      121 anrrihtsgy slyipknsdl gwngetfinl tgeisiqngf sigdrltalg ipvvefqgpm
      181 anlikvkear vagtalqtdr adqilkqnpe ladaiekypi pisskpyylm lsfklvrshp
      241 dfvellwetl aevrdsteme avqadfyaqh n
//
LOCUS       WP_284383267             497 aa            linear   BCT 25-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Pseudomonas putida].
ACCESSION   WP_284383267
VERSION     WP_284383267.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 497)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..497
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=53142
     Region          16..497
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mlcelpilpa traflerklk mrigadwqda asgrtlsfhn patgevlgev paaeaedvdr
       61 avraarqafd dspwsrlrpr erqnllwrla dlmerdarql aeleclnngk saavaqvmdv
      121 qlaidflrym agwatkiegs tveasmplmp ndqfhgfvrr eavgvvgaiv awnfplllac
      181 wklgpalatg ctvvlkpade tplsvlklae lvdeagypag vfnvvtgtgl nagaalsrhp
      241 gvdkltftgs tevgkligka amdnmtrvtl elggksptiv mpdanlqeaa agaataiffn
      301 qgqvccagsr lyvhrkhfdn vvadiagian gmklgsgldp avqmgplisa kqqdrvtgyi
      361 elgrelgati acggegfgpg yfvkptvivd vdqrhrlvqe eifgpvlvam pfddidevig
      421 mandnpyglg asiwsndlaa vhrmipriks gsvwvnchsa ldpalpfggy kmsgvgremg
      481 aaaiehytel ksvlikl
//
LOCUS       WP_284383507             227 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase [Litoribrevibacter albus].
ACCESSION   WP_284383507
VERSION     WP_284383507.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..227
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=25067
     Region          82..214
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mtktsdttsl eltesdyqeq qkqrlsympw lyhtlkprlk awakpwqehl qnrlskletv
       61 rfgdecfiap saklfaepgr tieigdytti aadvfihgpa nfghhvainh nvsmdggssg
      121 itigdhsrva cqctffafnh gmapdllvre qavsskgini gedvwigant sivdgvrihd
      181 haiigmgavv tqdipeyava vgnparviad rrdkpdaqwd wvtnnar
//
LOCUS       WP_284383395             564 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Litoribrevibacter albus].
ACCESSION   WP_284383395
VERSION     WP_284383395.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 564)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 564)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 564)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 564)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..564
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=62827
     Region          37..564
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mdhsssktpe qlttgrafsf qrivdnsvvn wviqkrwwlm vlaialsvfm pvaviflswl
       61 npqpddwshl ldtvlselvl ntllltlgva fgvlvlgvsl awltamcqfp grklfdwalm
      121 lpfsvpayvm afcflglldy sgpiqtwirs hisaefdlpv rnlagvitvf ilafypyvym
      181 lartafmnqg rgqmdaarsl gcnsfqafwr vmlpmarpav aagmalaime tladfgavsv
      241 fnfdtfttai ykswyglfni yaaaqlasll lvfviaclwm eqrargrarf eqherqqkqq
      301 lytlsggqal latmfctlvl glafvlpvsq lvwwvvetql adldarfiql mwntlslgit
      361 aalitvvaam vmafaqrvek nskldqiarf stlgyalpgt vlavglmvwf swvdnnlisf
      421 vnqvfginig qlflgsvfal lvsytvrfla vaygpvnshl qavrvtihea aqslgasqrq
      481 vlwrvyvpml rpgllvaall vlvdvmkemp atllmrpfgw dtlavriyem tsegeweraa
      541 lpaltlvivg lapvivlmsk srrh
//
LOCUS       WP_284383550             108 aa            linear   BCT 25-DEC-2024
DEFINITION  glutaredoxin family protein [Litoribrevibacter albus].
ACCESSION   WP_284383550
VERSION     WP_284383550.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Shelton,M.D., Chock,P.B. and Mieyal,J.J.
  TITLE     Glutaredoxin: role in reversible protein s-glutathionylation and
            regulation of redox signal transduction and protein translocation
  JOURNAL   Antioxid Redox Signal 7 (3-4), 348-366 (2005)
   PUBMED   15706083
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Fernandes,A.P. and Holmgren,A.
  TITLE     Glutaredoxins: glutathione-dependent redox enzymes with functions
            far beyond a simple thioredoxin backup system
  JOURNAL   Antioxid Redox Signal 6 (1), 63-74 (2004)
   PUBMED   14713336
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002164
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..108
                     /product="glutaredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=12296
     Region          35..106
                     /region_name="GrxC"
                     /note="Glutaredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG0695"
                     /db_xref="CDD:440459"
ORIGIN      
        1 mlrlaflltm issagpifaq nnqeipdnht qqqnkvfift qtycpaciha kqymsehkie
       61 yveldietsp ealsaferik grgvplliin kqmsygfdpk finaqlyq
//
LOCUS       WP_284383658             326 aa            linear   BCT 25-DEC-2024
DEFINITION  YbgA family protein [Litoribrevibacter albus].
ACCESSION   WP_284383658
VERSION     WP_284383658.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007153
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..326
                     /product="YbgA family protein"
                     /calculated_mol_wt=37117
     Region          79..323
                     /region_name="YbgA"
                     /note="Uncharacterized conserved protein YbgA, DUF1722
                     family [Function unknown]; COG3272"
                     /db_xref="CDD:442503"
ORIGIN      
        1 mfspnisnng qlthkipvgi sqcllgdkvr fdgghkhskl cteqlgqyfd yvpscpelga
       61 glgvprrtlr mvgddqtqri vetkdnridv tdalanysaq rvkeldhlsg yifmqkspsc
      121 gvfrvkvyad ngyaqnssag ifanafkeqh plipveeegr lhdpvllenf lvrvfvyhhw
      181 rlfiqqglts kglinfhqri kyqlmahsvk gyketgklls dlksrpledi ahdyiqllmt
      241 hlekratkkt htntllhirg yfkgklsaie qqeltqvind yrlgivplvv pitllqhytr
      301 kigndyieqq lylqpyphnl glrngi
//
LOCUS       WP_284383661             928 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Bacillus safensis].
ACCESSION   WP_284383661
VERSION     WP_284383661.1
KEYWORDS    RefSeq.
SOURCE      Bacillus safensis
  ORGANISM  Bacillus safensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 928)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 928)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 928)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 928)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 928)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 928)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 928)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18767243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..928
                     /organism="Bacillus safensis"
                     /db_xref="taxon:561879"
     Protein         1..928
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=107895
     Region          1..928
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          1..198
                     /region_name="AAA_27"
                     /note="AAA domain; pfam13514"
                     /db_xref="CDD:433272"
ORIGIN      
        1 mkirslhian fgkfsnrtfh fsddgfqlvy glnesgkttl kafiesmlfg fsknkiykpk
       61 qgsfyggslt cldeelgvih ierssdrggq aqvflpngev kdeaflrtll kgtdrrlfqs
      121 iysfdvfglq nvqalnedqi gefllfsslf gsdaaskmds rllkqqeqlf kpngrkpeln
      181 qqldrlkelt gqlkqarlae grytekkweh seliesiaal qkemkqteeq iqqlnehirl
      241 ypmiekkmel kkelaryper vkrfraeteh eldkleshlh pkkaqmtalk qkldhlqtsl
      301 aqvqplhdkd tllemtrvid esshaerikn rlaeckaerd slkqkmdeaa aklkwqrsvk
      361 ldqiddslef ewelkeavsh yvrlmdrkaq lddrfdharh eleeaetalk glkeqqarsd
      421 ssveagetra kekqvhsraw lfpvmvifda afllvlfflt ewwvtflfag fsvfvffaiy
      481 pflkstqvkq gsgggtfdsf qvqaasaetl vrqkellyer iirqyedweq elepvqqqve
      541 ekkkqlglss elsflveafl ilkqlktnta gyeelsreid elagqqsnye qrvealssll
      601 qrkegtiqen isafqeilkd eakrekerqt ldvsiqhvkq qittlegeid yyekqmdalf
      661 rqveaeskkd yqilshlske yrerlshlqq lnqelhrsgc fdeeesivrk glrlleeeca
      721 eakqhlnniq snaanmekrl aeraveirqi easgtvselt hqlsaeqeha khlakkwaai
      781 qlvrsvirek lnehkekrlp allqtasrfi qpltndryea ilfspeddrl ivkrmdgrif
      841 rpeelsqatc eqvylairfa lalshqqecq lpfmmddsfv hfdhvrlgrv lelmneltry
      901 etqlfyftch qlmmqaaedg qitslave
//
LOCUS       WP_284383677             278 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Litoribrevibacter albus].
ACCESSION   WP_284383677
VERSION     WP_284383677.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..278
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=32208
     Region          34..274
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mklvrnliiv lfcwwcssvl adahglvnam ekrvtvatst hnppfnfdkp naklllqeil
       61 ppgqdserlq gysldilres fhemgytiel hvypwprafd evkkgnldil fptgfneert
      121 qffqyshepi nhvefliyvk psstlvwngl dsldglligv lrgwnygpkw qtrdrivkye
      181 ineilqgfym ldhghvdgla gyklnfdyal kqankkqrfk qlpvfdstde yavtaknhph
      241 gkqlltdfde gkrriiengt flritnkwqg teeahirk
//
LOCUS       WP_284383716              66 aa            linear   BCT 25-DEC-2024
DEFINITION  tautomerase family protein [Litoribrevibacter albus].
ACCESSION   WP_284383716
VERSION     WP_284383716.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..66
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=7182
     Region          2..60
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mpyvnikitd egvtpeqkqa liegatqllv dvlnknpktt fviieevntd nwgiggdtvt
       61 qlrkqs
//
LOCUS       WP_284383730             257 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Pseudomonas putida].
ACCESSION   WP_284383730
VERSION     WP_284383730.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 257)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 257)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 257)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14398449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..257
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28945
     Region          19..113
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          176..255
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mlkpqrdllv evdewtwevg sratdyptdw fiephshakh qliyaikglm ivesgnerwt
       61 vppsrgvwmp cgqvhaircv gdvkmrsvfv rtdaavqlpv qskaisispl lselikasvg
      121 ftapfaedsr earvmrlild eicvlptlpl klsqpadkrl qticstlher pddnatladw
      181 gqqlgvdekt iqrlfrketg mtfgqwrqqa rlmqaleria lgeriidvag tlgydspsaf
      241 asmfkrhfgi tpsqffk
//
LOCUS       WP_284383778             285 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Litoribrevibacter albus].
ACCESSION   WP_284383778
VERSION     WP_284383778.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..285
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31848
     Region          11..283
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mylnqfsgeq llafsvilgl lvgsflnvvi yrvpemlkrq wrsectvfle ldtpeasepk
       61 epfnlvkpns tcpkcghkik pwenipvlsy lflrgkcsnc ktpislrypa iealtgvltg
      121 lmvfqfganw tglfaiffiw mlialffidy deqllpdnit lpllwlglia nsqglfidls
      181 salygaifgy lslwsvywif klvtgkegmg ygdfkllgal gawcgwmmlp qiiiissvvg
      241 lcfglaqifr sgenkpfafg psliiagfia flwgadinqw ylgnl
//
LOCUS       WP_284384142             446 aa            linear   BCT 25-DEC-2024
DEFINITION  protoporphyrinogen/coproporphyrinogen oxidase [Litoribrevibacter
            albus].
ACCESSION   WP_284384142
VERSION     WP_284384142.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Pawelek,P.D., Cheah,J., Coulombe,R., Macheroux,P., Ghisla,S. and
            Vrielink,A.
  TITLE     The structure of L-amino acid oxidase reveals the substrate
            trajectory into an enantiomerically conserved active site
  JOURNAL   EMBO J 19 (16), 4204-4215 (2000)
   PUBMED   10944103
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440906
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..446
                     /product="protoporphyrinogen/coproporphyrinogen oxidase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006779 - porphyrin-containing compound
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=50070
     Region          6..>289
                     /region_name="HemY"
                     /note="Protoporphyrinogen oxidase HemY/PPOX [Coenzyme
                     transport and metabolism]; COG1232"
                     /db_xref="CDD:440845"
ORIGIN      
        1 mprslkvavv gagasgiata yylkqagysh itifekeeri ggkcltfkhg dhefdlgany
       61 itpyyhevlr iakeldlktq papqrksfdl ttgnflntlr ttlmgkslls fgaasakyly
      121 lafkyrkqin epgfteleac pelchpfgkw ldingmsilr qlflipvtif gygalddvpt
      181 pyvlkymdak nflllarvga glskewprhf ldgyqgflna iirseqldvr lnshivsikr
      241 tpnvvvglad gslhefdriv facpldkilp visdaseheq allsrikyrn yyvsacdvdg
      301 mldittdelq lppakplpai ghpwgivkfw kdsdvnlfft vgdgedkdkt qpqdalpavt
      361 pkmveanira dvkrmggvfq svvhqqlwtt ffphveaadf idgyyqqler qqgklntyyv
      421 gaimalelve pifnyskqlv dqhfss
//
LOCUS       WP_284384050             732 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Pseudomonas putida].
ACCESSION   WP_284384050
VERSION     WP_284384050.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 732)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 732)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 732)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..732
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=80732
     Region          1..525
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mylsalsirn frqfgdltpg ftlhfnegvt alvgendagk tavidairyv lqtrdsdflr
       61 leledfhvgs dgepatditm vctlaglttl elgafaeyvt fsrgegllhv hwsarrlamp
      121 tasrrwvdiq vrcgergegp aldigarqll ataylkplrd aeremspgrn srlsqvlssf
      181 pgidagepyv diappasaae atglsisgmg dymrelvrgh qaikvaqati neryleplsl
      241 agqplhshlg fgdtgsettk lkqilerlel glldkgsgna rgsyglgsnn llfmacelll
      301 lgkepdglpl llieepeahl hpqrqlrlme flerasqprp qqqnqtqqqd qtqqqdqtqq
      361 qdqtkqqdqt qqqdqtqqpd qtqaepahtr pvqviltths pnlsskiale nlvlihgqra
      421 fsmaqgrtrl saddyrflsr fldvtkaslf fakglliveg daeaillpal arllgrdlte
      481 hgvsivnvgg vglrryahim qradategvi qiptacitdm dvmpdcapai mgldphklna
      541 kgkparrqwr mlsdfgatei erepklaahr qkrtrgdgqn vktfvadhwt leydlavegl
      601 mdwvhraatl alhdekiner kltrqkvler atkalaalks qyltneerat evyrqvdsgs
      661 ksitaqhlvd llqsafdege ldqaslraal ppyvveaiey atrgrimpsa peqpatniae
      721 tplealqage la
//
LOCUS       WP_284384145             566 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Litoribrevibacter albus].
ACCESSION   WP_284384145
VERSION     WP_284384145.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..566
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=62681
     Region          32..534
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mvkeqastlv skvgrryrsn rvdalveask idhvvigsgi gglscaasla kmgrkvlvle
       61 qhytaggfth syerngfewd vgvhyvgqvg nrltgpgalf hwmsegrlaw dslgevydef
      121 iiggqtyrpp lgkgayrrfl eshfpnetna ikqychylfs verwlplffa gktssfpgaa
      181 sigrtvsklv pscyyqttae vfnqltdnve lkavwsaqwg dlglppgqss fflhclianh
      241 ymsggwyprg gsseiarsil ptieqaggsv mtyaevaril atdgavtgve madgyriacd
      301 svisncgwfn tqslldlpsa krfskpmeek vvessachic lylgfdvdis elgvpkgnrw
      361 lhhsadfdqa ltafeedsta dfpfvyvsss aardstwpvr hpgksvmelv svipktefsq
      421 wfgsqwgkrd tdyeerktyw serllavlyq qyphlkgkvs yyelstplst hhfmkyqdge
      481 iyglahtpqr ylqkglkpkt eiaglfltgq daltsgvvga amsgvfsaae vlgdtykrql
      541 wrgvkgmlpn aggwrsmirq kkapqs
//
LOCUS       WP_284384164             430 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Pseudomonas putida].
ACCESSION   WP_284384164
VERSION     WP_284384164.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..430
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46119
     Region          7..426
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 msetphvvvt gmsvltalge dpgslldnll aghsgirrws sfdrqiatkv ggslegfdpr
       61 prlcaladsl tdaprlrlrr asnrlpwsta lsvlmagraw qdaglfdlpa gddgetaiiv
      121 gghnigqnyy ynnfrqfeqd pdhidvqfgl agldtdhaav asevlgirgp gysvggacas
      181 galalraafn eirfgdaqrv vvlapvldys plelhalalm qavsqrsfnd hpeqasrpfd
      241 rrregfvpah ggaclvlera dlaqargaep lcevlavaar sdasrqpspq edgqtrtiqa
      301 alrearlqpd didficahat stplgdltea rsirrvfgah ldrlkvnapk smlghtcwsa
      361 plvelvaaia qmragqlhpt inlddpdpel dfdvcaagav ahpvryllkn afgfggnncv
      421 ailgrweprp
//
LOCUS       WP_284384158             515 aa            linear   BCT 25-DEC-2024
DEFINITION  WS/DGAT/MGAT family O-acyltransferase [Litoribrevibacter albus].
ACCESSION   WP_284384158
VERSION     WP_284384158.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Stoveken,T., Kalscheuer,R., Malkus,U., Reichelt,R. and
            Steinbuchel,A.
  TITLE     The wax ester synthase/acyl coenzyme A:diacylglycerol
            acyltransferase from Acinetobacter sp. strain ADP1:
            characterization of a novel type of acyltransferase
  JOURNAL   J Bacteriol 187 (4), 1369-1376 (2005)
   PUBMED   15687201
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Kalscheuer,R. and Steinbuchel,A.
  TITLE     A novel bifunctional wax ester synthase/acyl-CoA:diacylglycerol
            acyltransferase mediates wax ester and triacylglycerol biosynthesis
            in Acinetobacter calcoaceticus ADP1
  JOURNAL   J Biol Chem 278 (10), 8075-8082 (2003)
   PUBMED   12502715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496208
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..515
                     /product="WS/DGAT/MGAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0045017 - glycerolipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=57062
     Region          4..469
                     /region_name="acyl_WS_DGAT"
                     /note="acyltransferase, WS/DGAT/MGAT; TIGR02946"
                     /db_xref="CDD:274360"
ORIGIN      
        1 mqqlssldas fyfletehtp mhvgglylfd nsetgqdftf aqfrelilsr lhiarffrqr
       61 iievplkldn pywvddpdfh vdnhllhvpl gkpsnrkklv nmaaaefakp lerdkplwea
      121 ifvdgfdeee fgshrfavif klhhcaidni sgeemisall dvepnlsrse iarewrpeel
      181 ptetelllks ykkkasqmaq lgqlgqlare flsnltntml kkrlvessgn qpglfsapht
      241 pfngsiscrr vfghkaldms rikavrdavd gatvndvilt icsgalrhyl nfkrnlprks
      301 liafsplsvr srtihasfgn qmsatlvrlg thienpverl ltihksvsss kvynhaisad
      361 slteiipttt lalasrlysg lhladrhspi ynlsitnvpg pqrplylgsa klesqsnsap
      421 lfdglglviv alsyngvvdi avtstpevmp dmqimtdaig ialndlevai ekssvtsvds
      481 dptegrselp vvltksiwde vlekakgavg ldssq
//
LOCUS       WP_284384433             520 aa            linear   BCT 25-DEC-2024
DEFINITION  GumC family protein [Pseudomonas putida].
ACCESSION   WP_284384433
VERSION     WP_284384433.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..520
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=58159
     Region          6..>517
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mksdyelslr dyiaiikdrg lilgvsivvi laatvavavm vppiyqstgt ilvesqqisp
       61 elvstnntsf aderievirq rvmtrenllr iiakynlfpd krfsesdkid hmrsavvvet
      121 lttyvrgrge atvafnvsfe hkqpevakev adelvtlfln enlkqrtera nettefltqe
      181 anklgaelas lenqladfkq ahanalpehq tlrmnmlsrs elefrevdrd ykaaqeelry
      241 lelelsaana glatkagegp raasaeqpqd lpslkaeyaq llsrykeahp dvvavkrriq
      301 aleangnrta aastvgldva rvrakmsaaq eriaslaeqk reltrkmegy eaeileapqv
      361 erglvtlmrd hdnarkkyee irakemgaki tesleqenka erfvlleppl mpekpikpnr
      421 kkiaalglvl apagggalvm llemfnqrir gvgalenllg rrvlvalpyi dtkadvarrk
      481 rwrnwlilaa lalaaimvvl vhvfympldv lllkvmsrfa
//
LOCUS       WP_284384678             665 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Dyella flava].
ACCESSION   WP_284384678
VERSION     WP_284384678.1
KEYWORDS    RefSeq.
SOURCE      Dyella flava
  ORGANISM  Dyella flava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Dyella flava"
                     /db_xref="taxon:1920170"
     Protein         1..665
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=73142
     Region          400..649
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mithegaaad aapntaahgp ipignfirqp dfskvtispd grylaalvpl pdnpygnlig
       61 ivdaktakiv hvlrsasntl iadyfwasdd rivatlatqr ggldtplptg elfatnadgs
      121 dqvdlfgyra ggpqtgtlih ttekrnayae pisrypidkn kiliavndft heragsftea
      181 eildirngra vsqgnspvpn akliadhagq vrvayadnqf kgdmvwlras psdawtvlnd
      241 pgksgvefap igfnrdnskl yvrmahgdrp daielmdlan htftkvyqgq fadpgellpt
      301 adgldyyaii tndgeqklfy lnenspeaql skalaanfpg qlayfssftr dgkraivrvv
      361 sdrnpgdyyl fdldtrnary vfsampwida hqmrpmqpie lttrdglllh gfltvpagnk
      421 pfplivlphg gphwifdtwg fnsetqmfad rgyavlqiny rgsggygvnf vsrgfrqwgl
      481 smqddltdat ewaihqgyad aqriciygas yggyaaiega vrepdlykca vgysgvydlr
      541 vqlsnsdteq tdkgdaylkl algydqddll rrsplsgvnr ikadlllihg gedprapfkn
      601 fkeltkaldq dnkhyetlve pdeghgfflp qhreeayeki vsfidshigs sdmasdkqtq
      661 akasp
//
LOCUS       WP_284384691             195 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Dyella flava].
ACCESSION   WP_284384691
VERSION     WP_284384691.1
KEYWORDS    RefSeq.
SOURCE      Dyella flava
  ORGANISM  Dyella flava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Dyella flava"
                     /db_xref="taxon:1920170"
     Protein         1..195
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=20968
     Region          1..192
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mlylasqspr rrelleqvgv vfsvlnvdvl eqravgespq dyvhrvardk araglaqlsp
       61 hdrehaivlg sdtevvldgd vfgkprdadd aasmlhrlsg rthevisavw lvaaeleqgd
      121 icisrvrfak ldkaaitayv asgepfgkag ayaiqgrgag liehlegsys gvmglplfet
      181 srllknfhaa ipara
//
LOCUS       WP_284384927             752 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Pseudomonas putida].
ACCESSION   WP_284384927
VERSION     WP_284384927.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 752)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..752
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=82792
     Region          <13..318
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
     Region          <322..731
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 meplctthpg dedgvpgrsp amqalqallr rvaqsdrpvl ifgptgagke viaqqlhrls
       61 apgkpfidln cgaipeqlle selfgharga ftgavgermg hlqmagagtl fldeigelpl
      121 alqpkllrvl etgqyrplgs sesrhfrgrv vaathrdlkr lvaeerfred lyyrlsvfel
      181 elpglnerre dipdliehfc rqqrrplhfd aaalellcqr dwpgnvrelr nsidrigtla
      241 psplvdretl eqllappspa salavelaea llglegpdkl aavetllieh alnrcngnks
      301 aaaqllgvnr kvierrvrlr qdlrltvery laegrklidg adfrgalgpl qkglevaerv
      361 yegkdlwrlq felhrllgvs frsiegwlsi tslasyrdaq alaarqgqaq emasvsfglw
      421 ttllmglela earataqqml qqaqiaggea lrieahlama ntlfwlgdfe eslacltrgr
      481 lleddqaswp snqgldlvgl artfeglaaf elglfsqarq alarlqsrae qavdnpfnra
      541 valqgaawla avlgerdalg rqarelells arhefsfyrg vgmilrgyhq gisgeyeage
      601 qaiaegyqqh vlrnggllfh gfqawkrgev lllggraeac lelvdvaldl aqdhqerayl
      661 celmllrgra llalgddrea eatlrvalst altlgvvpar lhaalelarl lersergaqv
      721 qsilvralrg ldpqldyppa snvrswlarl ss
//
LOCUS       WP_284384937             165 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Pseudomonas
            putida].
ACCESSION   WP_284384937
VERSION     WP_284384937.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..165
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18917
     Region          4..109
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
     Region          109..>143
                     /region_name="KU"
                     /note="Ku-core domain; includes the central DNA-binding
                     beta-barrels, polypeptide rings, and the C-terminal arm of
                     Ku proteins. The Ku protein consists of two tightly
                     associated homologous subunits, Ku70 and Ku80, and was
                     originally identified as an autoantigen...; cl02666"
                     /db_xref="CDD:470650"
ORIGIN      
        1 mpmqdetsdt vcpvarsmds vgdkwtilvl relymgatrf eemqiqttat pqmltsrlka
       61 leanglvkrr pysekplrye yhltdkgwdf ypviyalraw gekwckhpde gvavhyvhra
      121 cghdvgvasv cphcgapver kdleamisnr flaeresrre afkrk
//
LOCUS       WP_284385164             549 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Pseudomonas putida].
ACCESSION   WP_284385164
VERSION     WP_284385164.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..549
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=59283
     Region          7..537
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msifeknqap lvdisglhvs fngvpvvhgv dlqlragqcl alvgesgsgk svtartlvgl
       61 tgtgahvqaq rlafagqdlr qfderawqrl rgehigfvmq dalgsldplr rvgaeieepl
      121 llhtnlaaeq rrlrvlellr qvgvpepevr arqypwqlsg glrqralias aiacqprlli
      181 adepttalda tvqaqildll ehlrerdnsl lmvshdlavv arladwvavm rhgvvveqgs
      241 veqilqdpqd pytqrllsaa ravhfkrpaa palalvedgv deqpvvlear glskafvgpd
      301 grlrqvldgv slqlragqtl gvvgesgsgk stlgrillgl erpeqgslql agqdwlalsa
      361 aqqrqarqgi qvvfqdpqas fdprytvlrv laealahagv pralqrteaa allervqlpv
      421 gsldrrplel sggqrqriai aralamkprv lvldepvsal dvsvqarila llaelkaeln
      481 laclfishdl gvveqvsdqv lvmqggrvve qgaaaqvlgq prqaytrall davphlpaar
      541 pswfariav
//
LOCUS       WP_284385162             570 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Pseudomonas putida].
ACCESSION   WP_284385162
VERSION     WP_284385162.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..570
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=61892
     Region          1..539
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msdktliveg lnvafdgasv vrdlsftlpp grclalvges gsgksvsarc lvglaggraq
       61 vsarrlsfgd hdlldlserq wravrgkdig fvlqdalvsl dplrpvgkei levlqthgyg
      121 drhtrparmh ellervgvpd vqlrarqrpg qlsgglrqra liasalaldp alviadeptt
      181 aldatvqaqi levfqqikar gaslliishd lavvaqlade vvvlrhgevv eqgpmqqvlr
      241 qprhaytqal laavpaehpr gsrlspervg lrseprarar sdvllegrgl gkrylgpdgl
      301 vrqvvqgvdf tlragrtlgi vgesgsgktt varialgllq pdegevlyrr qpwnrpanav
      361 seavrrplrr eisviyqdpl gsfdprwsva qifddalqva gieaparpar iavllnqvrl
      421 paelgqrrpl qlsggqrqrv aiaraiasep kviicdepvs aldvsvqaqv ldlladlqde
      481 lglaylfish dlgvirhvsd dvlvmrhgqv veqapveqlf dnpaheytqr llgavprlpg
      541 sgaelvvppl dleheafdll detrlwkiai
//
LOCUS       WP_284385388             266 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Pseudomonas putida].
ACCESSION   WP_284385388
VERSION     WP_284385388.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 266)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..266
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29428
     Region          83..260
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mrhclallvl flslplsaaq lhlelgattr ewssadlldh pqardisidq dvsykqpmry
       61 ravplaalld gvsasdhlqa valdgfaaem paapllqhgp aqawlaveep srpwpplgqg
      121 kpsagpfylv wtapqasgir peqwpfqist irklasvear fpallpdpkl paespvrrgf
      181 alfqqnclac hrlngagdaq vgpdlnvphn pteyfrpeyl rqlirdpqsl rqwpqakmpg
      241 faesvlsepe ldellaylrh marrrp
//
LOCUS       WP_284385438             431 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudomonas putida].
ACCESSION   WP_284385438
VERSION     WP_284385438.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..431
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47189
     Region          26..391
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mfsysnnyyt gtmrpapqrp alagetradv ciiggglagl svalellarg rsvvlleaar
       61 vawgasgrng gfvlqgwseg lsaierrcgk qtaaalfrls legvdivrdt iarhqlpgca
      121 attgklsvvr yddadnlqrt rdrmardfgf emeyldtptl rshlntdryy qglrdsygfh
      181 fhplnyclgl aelvelaggr vheqspmlrv areaghhrvt tahgavtcad vvyccggygg
      241 aefgrlrraf lpiatyvvlt ehlgerlndv vrttdavgdn rrasdyyriv egdrllwggh
      301 ittrnlqdeq rlgqlltrdi lsvypqlqgl kiakawsglm gyarhkmphi gplgpglwac
      361 tsfgghgmnt apvgarvvae avcgetdryr lfdayglqwn ggpfgpaaaq avytglklmd
      421 rfqearsqyn n
//
LOCUS       WP_284385476             142 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: LexA family protein [Pseudomonas].
ACCESSION   WP_284385476
VERSION     WP_284385476.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..142
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=15414
     Region          <5..138
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mitilgplkp sgaklplfsf rvpagfpspa adhlekrisl delldvraph iylvrvegds
       61 migagifpgd lvivdrsiea epghiviaav nceplckrla rdgsqvvlks ensrypsryl
      121 legeelqvwg vvtysvrshd ka
//
LOCUS       WP_284385543             497 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pseudomonas putida].
ACCESSION   WP_284385543
VERSION     WP_284385543.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 497)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 497)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 497)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..497
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55284
     Region          184..483
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mqmldnevpd karttasgva vplrefnllr wfsvisllii asvagglgyv strfvvrdsv
       61 erdamltaqf iqamaqaevr hsqlppgstm gelldprldq qhlqftpdla estrvefldh
      121 vehlpdilla nvyardrtiv wstnreligk riaadgdldr afrsrkavsa syhqadddre
      181 eqkfqrepry lfienyiplf dsqgeqvlam veiykepqdl vrriqrgyvl iwastlvgga
      241 lvyfglfwiv rraaqllhlq qdrlvasety valgemssav ahslrnplan irssaelaqe
      301 ianpaaqkni tdiisqvdrm srwvrdllvs lrptsddaea vdlvtaiedt hlafaqqier
      361 ngvrfcyegp gsqwvasqpl qltqilntlf snaleampeg gmlraqvsvq dgqraefvlt
      421 dtgkgmsqqq ermvfkpfyt tkqgglgvgl alvkrimerf ggsvslssre eegtrvsltf
      481 niaaggdhga qhpgsrg
//
LOCUS       WP_284385616             162 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudomonas putida].
ACCESSION   WP_284385616
VERSION     WP_284385616.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..162
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=17564
     Region          31..>129
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
     Region          <122..151
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
ORIGIN      
        1 mrstigvmla vlitplaqae lideiadrge lriavqvdns pyafkendhl ngfeidfgqa
       61 lakeldlrae fieapaaevl pgvetgkydi altpssespk ndgpldvslp fgekqlvipf
      121 qkdnpafesa vnnalqrlke sgrtaeleqk wfkgvpetad gq
//
LOCUS       WP_284385653             370 aa            linear   BCT 25-DEC-2024
DEFINITION  CdaR family transcriptional regulator [Bacillus safensis].
ACCESSION   WP_284385653
VERSION     WP_284385653.1
KEYWORDS    RefSeq.
SOURCE      Bacillus safensis
  ORGANISM  Bacillus safensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20544506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Bacillus safensis"
                     /db_xref="taxon:561879"
     Protein         1..370
                     /product="CdaR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=42090
     Region          4..132
                     /region_name="Diacid_rec"
                     /note="Putative sugar diacid recognition; pfam05651"
                     /db_xref="CDD:461704"
     Region          77..369
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mqfltselaq emvertmhil hkninvmnad gviigsgern rigqkhdgar lvltsgnsve
       61 idqetslrle gvkpginlpi cfheqvvgvi gitgepedir hhaelvkmaa elvleqsfll
      121 ervqwrhrle seivnqlvsy sdvgdhqlkn raawlgmdld krrmaivfqp vpssedavhk
      181 lmhaiqydkk addllgmtfc helillsqpi lvhrlkqvag hlqrtmqkav ggqvlvgigt
      241 vaddisqlpi sfqhardalr lgkaldpees myffesyqle slfmnagiae kksrwtdfye
      301 pltqeaelah tlriyieegg dlqrivdrlf ihrntlryrl dkiqeltgkd prhvkqliel
      361 ymaqlmnqls
//
LOCUS       WP_284385675            2382 aa            linear   BCT 25-DEC-2024
DEFINITION  amino acid adenylation domain-containing protein [Bacillus
            safensis].
ACCESSION   WP_284385675
VERSION     WP_284385675.1
KEYWORDS    RefSeq.
SOURCE      Bacillus safensis
  ORGANISM  Bacillus safensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 2382)
  AUTHORS   Konz,D. and Marahiel,M.A.
  TITLE     How do peptide synthetases generate structural diversity?
  JOURNAL   Chem Biol 6 (2), R39-R48 (1999)
   PUBMED   10021423
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01733.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2382
                     /organism="Bacillus safensis"
                     /db_xref="taxon:561879"
     Protein         1..2382
                     /product="amino acid adenylation domain-containing
                     protein"
                     /calculated_mol_wt=266379
     Region          6..>2106
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
     Region          2132..>2299
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 msiqsvdsfp ltgaqsgiwy aqqldpanpi fntaeyieik gpidpiqfea airktvlead
       61 slymqfvedt dgpkqwmtsk keipfqyvnl qnekqpldaa kawmkadlst pvslekdvlf
      121 revlfqladd rfiwyqrihh iaidgfafsl iarrvaevys alsngtpmpp qtfgslhdvv
      181 qeeltyqqsn ryeddqafwk nrfadqpevv slaelaprts dhfirktagy daekvskmkk
      241 naqafggtwh emilaasaly mhrmtgahdi vlglpvmmrl gscalqtpgm vmnlvplrlt
      301 ckpemtlsal vrqvsdelka irphqryrhe dmrrdfklig rnqrlfgpqi nimpfdydlm
      361 fdqsmgqahn lsagpvddis iniydradgn gfqidfdanp avykeqavda hqqrflqlle
      421 eitgleqdqt isqfnlllse ekenilkhwn dtkrelpres lrelfekqvs ktpqakalqf
      481 egitltyeel nqranqlahy lkkhdigpeq fvaialprsi nmvvsllavv ktgaaylpld
      541 pdypndrvay mledakpacl ltiketadgl nhphivqldd stvhqeiads phinpawseg
      601 sphhpayily tsgstgkpkg vvvtkrnvin filsmqdsfl ldqkdqllav ttiafdisgl
      661 emflpllhga aillakketi qepaklsdmi rshhvtimqa tptlwhalad eypdvitgmr
      721 vlvggealpa sllhtlqslq cditnlygpt ettiwstmen vtahrensgp aigkpiwnts
      781 iyildeglnp vpagsigely iagegvsrgy lgrydltaer fvadpfstkg trmyrtgdla
      841 rwredgsidy isradhqiki rgfrielgei etvmmqhqai khtsvivhed qpgqqllcay
      901 vvltdgsslh pselrqfaas llpdymvpsa vvvlpelplt pngkidrkal papnmslvss
      961 ertprtpqed mlcslfaetl glsqigidds ffdlgghsll aarllrrird tlgadlsmst
     1021 ifesprvael aqhidkakdi rpplqvedkp deiplsfaqk rlwflhcleg psptyniplv
     1081 iqltgtldqt aligaladit ekhetlrtif pnkngmprqv ilhpksvqpe lhvtassdqq
     1141 ienqlneair ysfqieeepa lraelftlda nrsvlllllh hidgdgwsla pltrdlaaay
     1201 eariqgksis lpaepvqyad yaiwqqkllg seketdslfa kqlsywkgal hdlpeelelp
     1261 ydfprpqegs fngatidfti epalhqnlle lakqhqvslf mvlqaslaal ltrlgagtdi
     1321 pigspiagrn ddalddivgl fvntlvlrtn tagnptfsel lkrvrnvdla ayehqdlpfe
     1381 rlveilnptr srsrnplfqv mlafqntpka emkltqldsn lyvkpvgsak fdltielaeq
     1441 rtetgsaagl tglfefstdv fkqstiraia drmkrfltev aerpqvsigq vnilsdkerh
     1501 tflpdkktfa qldqahslpa lfektaqqyp nrvavtdgkk qltyeelnnk anrlahllie
     1561 rgvgpeqfva lalprsidml vsllavhkag aayvpldpdy padrlaymiq dakpvcsitt
     1621 kadalhlpad cdlilldeke tsdqlltmpn hnpadidrie plsslhpayi iytsgstgkp
     1681 kgvviphqnv irlltstehw fhfdeedvwt mfhsyafdfs vweiwgplly ggrlvivpht
     1741 isrspeemlq llveegvtvl nqtpsafyql mqidkeqqtl gqalslryvi fggealelsr
     1801 ledwysrhsd ckpklvnmyg itettvhvty nelnrdmitk nsssligepi pdlhvyvlde
     1861 hlqpvppgtt gemyvagagl argylgrpdl tsdrfpadpy gapgtrmyrt gdlarwteeg
     1921 aldyigradh qikirgfrie lgeieavlar hdavaqvavm mrenqpgdkr lvayivttee
     1981 dhfdtealrh faaaslpdym vpaayvqida mpltangkld qkslpapqlh iqktdgrgpr
     2041 npkeeilchl feevldlpki siddrffdig ghsllavrli srirdalgvk lsigtlfeap
     2101 nvaslaekle tgsdenaldi llplrtnger yplfcvhpag glswcyagll ntlekdipiy
     2161 glqargiark ddyphtlddm aadyikhiqt iqpkgpyhll gwslggnvvq amatqlqqqg
     2221 eeialvamld aypnhflpik aapdeeeali allalggydp dtltgepltm ksavdilkkd
     2281 gsalaslsed airnlketyv nsvrllgeyq pktyqgdilf frstiipdwf tpidpeawap
     2341 yingtieqhd ihcrhkdmcq pkplaeigvi ldnalhrvkq kh
//
LOCUS       WP_284385697             430 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudomonas putida].
ACCESSION   WP_284385697
VERSION     WP_284385697.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..430
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46503
     Region          29..399
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mihsaqhaas yyaassaphp dhsflqgehs advcivgggy sglntaiela ergfsville
       61 arklgwgasg rnggqlirgv ghgleqflpv igeegvrslk lmgleavqiv rerverhaia
      121 cdltwgycdl ankpaellgf aedaeelrgl gyahelrlvg kddihsvvgt dcyvgglvdm
      181 gsghlhplnl algeaavasr lgvklfeqse vtridygpev qvhtaqgrvr aktlvlccna
      241 yhndlnrelg gkvlpagsyi iateplgeer ahsllpqnma vcdqrvaldy yrlsadqrll
      301 fggachysgr dpkdiaaymr pkmlkvfpql advridyqwg gmigiganrl pqvgrlasqp
      361 nvyyaqaysg hglnathlaa rllgeaisgq esgrfdlfak vphitfpggk hlrspllalg
      421 mlwhrlkeli
//
LOCUS       WP_284385775             322 aa            linear   BCT 25-DEC-2024
DEFINITION  YbgA family protein [Pseudomonas putida].
ACCESSION   WP_284385775
VERSION     WP_284385775.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007153
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..322
                     /product="YbgA family protein"
                     /calculated_mol_wt=36191
     Region          74..319
                     /region_name="YbgA"
                     /note="Uncharacterized conserved protein YbgA, DUF1722
                     family [Function unknown]; COG3272"
                     /db_xref="CDD:442503"
ORIGIN      
        1 mhdpsahskp riaisacltg hsvryngghk asdlcrmqle ehfdwlpvcp evaiglgvpr
       61 dpirlvgnpd rpevvgtrnp gmdltgplrs ygeqmaveld dicgyifmqk spscglervk
      121 vyqenghpal hggrgvyaqa fcarrpdlpv eeegrlhdpv lrenfisrvy ayadwqrlla
      181 eglsrgalvr fhsrykyllm annpqayrsl grmlgsmskd ddpqsigpry fsqlmqalrr
      241 casrgthcnv lqhlsgyfkd tltqqdkael qaiigqyqqg vvplivpltl lkhhlrkhpd
      301 pylqqqaylq phperlglrn av
//
LOCUS       WP_284385814             458 aa            linear   BCT 25-DEC-2024
DEFINITION  class II fumarate hydratase [Pseudomonas putida].
ACCESSION   WP_284385814
VERSION     WP_284385814.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Woods,S.A., Schwartzbach,S.D. and Guest,J.R.
  TITLE     Two biochemically distinct classes of fumarase in Escherichia coli
  JOURNAL   Biochim Biophys Acta 954 (1), 14-26 (1988)
   PUBMED   3282546
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..458
                     /product="class II fumarate hydratase"
                     /EC_number="4.2.1.2"
                     /GO_component="GO:0045239 - tricarboxylic acid cycle
                     heteromeric enzyme complex [Evidence IEA]"
                     /GO_function="GO:0004333 - fumarate hydratase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006099 - tricarboxylic acid cycle
                     [Evidence IEA]"
                     /GO_process="GO:0006106 - fumarate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48123
     Region          1..454
                     /region_name="FumC"
                     /note="Fumarate hydratase class II [Energy production and
                     conversion]; COG0114"
                     /db_xref="CDD:439884"
ORIGIN      
        1 msdtrierds mgelqvpaqa lygaqtqrav dnfpisgqrm paqfiralll akaaaakanv
       61 eleqlstaqg qaivtaveql lagdfiqhfp vdvfqtgsgt ssnmnanevi atlasrvlge
      121 avnandhvnc gqssndiipt tihvsaalal heqllpalah lvqvieaksa qvhqyvktgr
      181 thlmdampvr msqvldgwaa qingakahie atlpnlqala qggtavgtgi nahpqfaagf
      241 arqlssltqv eftpgqnlfa ligsqdtava lsgqlktaav almkiandlr wmnsgplagl
      301 geielqglqp gssimpgkvn pvipeatamv aaqvigndat iaiagqsgnf elnvmlpvia
      361 rnllesielm anvsrlladk aiasfkvnes klkealarnp ilvtalnpii gylkaaeiak
      421 taykqgrpii dvalehtnls rdqlealldp ekltaggi
//
LOCUS       WP_284385816             352 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-nucleoside phosphorylase [Gluconobacter frateurii].
ACCESSION   WP_284385816
VERSION     WP_284385816.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter frateurii
  ORGANISM  Gluconobacter frateurii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10534769
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Gluconobacter frateurii"
                     /db_xref="taxon:38308"
     Protein         1..352
                     /product="purine-nucleoside phosphorylase"
                     /EC_number="2.4.2.1"
                     /GO_function="GO:0001882 - nucleoside binding [Evidence
                     IEA]"
                     /GO_function="GO:0002060 - purine nucleobase binding
                     [Evidence IEA]"
                     /GO_function="GO:0004731 - purine-nucleoside phosphorylase
                     activity [Evidence IEA]"
                     /GO_function="GO:0042301 - phosphate ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_function="GO:0047975 - guanosine phosphorylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006139 - nucleobase-containing compound
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=38522
     Region          3..352
                     /region_name="NUP"
                     /note="Purine nucleoside permease [Nucleotide transport
                     and metabolism]; COG5042"
                     /db_xref="CDD:444049"
ORIGIN      
        1 mpwafslaci aplalagnha daadkpwdir avvlttyeig adtgdragef qpwiegehlt
       61 ekvpfplgih piytdpdhhl lvvvtgtpia pattsvmala tdprfdlrha ywmvdgisgf
      121 dpavasvgsv siadyvvgdi tryidkreap kewpygyfmi taqmpnqyal sggdapdgsi
      181 qhnnafqlnp slvhwaynlt qtitlsdppq leaqrklyks tdvaaghpav vtggdfgsdt
      241 fwhgkimtgf ardwvhlltq gkshfvssdm edsgilealt rlgqarrvds srvlilrsas
      301 nyteqprsmt avqsmnsgyd gekvaldngy rvgsriihel lqhweqfgsk tp
//
LOCUS       WP_284385860             387 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Pseudomonas putida].
ACCESSION   WP_284385860
VERSION     WP_284385860.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 387)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 387)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 387)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..387
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43961
     Region          1..387
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 miysygarny fsfkeglnas fqltakvpaf vsqgrkvatv lgikggnasg ktsilkclrf
       61 lswfiadsfa ndekdninld pyfdnknptd fyidfqidda kyryeltatr eavvrealyk
      121 klqrktlive rkgdaisyrs neysaldlie lktrasfvst ivkykiknlp ndferivsyf
      181 erfagnvtpl glipdsemfn resatsfyns vpeafefvkn firradlgiv dieihshdlp
      241 tgkkeyfpif ihkvgksngr aaltsydqss gtmalyrrla iywmvlkegg vlimdefdqn
      301 chpmllppll dlfinkesnp hgaqflftah nsdvidslgk yrtilvsked gesysyrlde
      361 ipgdlirndr sisalyregk lggipkl
//
LOCUS       WP_284385912             821 aa            linear   BCT 25-DEC-2024
DEFINITION  efflux RND transporter permease subunit [Pseudomonas putida].
ACCESSION   WP_284385912
VERSION     WP_284385912.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Sandhu,P. and Akhter,Y.
  TITLE     Evolution of structural fitness and multifunctional aspects of
            mycobacterial RND family transporters
  JOURNAL   Arch Microbiol 200 (1), 19-31 (2018)
   PUBMED   28951954
REFERENCE   2  (residues 1 to 821)
  AUTHORS   Hand,N.J., Klein,R., Laskewitz,A. and Pohlschroder,M.
  TITLE     Archaeal and bacterial SecD and SecF homologs exhibit striking
            structural and functional conservation
  JOURNAL   J Bacteriol 188 (4), 1251-1259 (2006)
   PUBMED   16452406
REFERENCE   3  (residues 1 to 821)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
REFERENCE   4  (residues 1 to 821)
  AUTHORS   Arkowitz,R.A. and Wickner,W.
  TITLE     SecD and SecF are required for the proton electrochemical gradient
            stimulation of preprotein translocation
  JOURNAL   EMBO J 13 (4), 954-963 (1994)
   PUBMED   8112309
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..821
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89620
     Region          26..792
                     /region_name="MMPL"
                     /note="Predicted exporter protein, RND superfamily
                     [General function prediction only]; COG1033"
                     /db_xref="CDD:440656"
ORIGIN      
        1 maatrqdtlp virnlddfdp rsgnclerlv fnhrlpfllc mllatlvlgy maltrlelrp
       61 sfdkmlpqsh pyiqnylenr pslrglgnav rvvventqgd ifdpgylqtl rhindelfls
      121 qgvdrawvks lwspavrwte vteegfqggp vmpdgyqgat adieqlrqni eranivgslv
      181 ardfkssmlv vplldqdsat gkgldyhafs qkleqlrsqy qasgqyrihv igfaklmgdl
      241 idgliqvmaf falavltsll iiycytrclr stllvvlcsl tavvwqlgiv awlgyaidpy
      301 silvpflifa igvshaaqkm ngilqdigrg thrqvaaryt frrlfvagvt alladavgfa
      361 vlmlidipvi qdlaitasig vavliftsll lmpvalsyvg vgrkaaeral hidaraaqhr
      421 gfgrlwdlld rfterkwaca allvalalga lgiwgslqlk igdldsgape lradsrynld
      481 nayitqhyal ssdtfavmvk tapegclqyq tlvladrlaw elqqlpgvqt tvslanavrq
      541 itagtyegnp rlnslqrnqd vlnyaaqqas vnapelfnnd cslmpviayl kdhradtlaq
      601 vaavaerfaq anssteqqfl laagsagiea atnvvvsean hrmlllvyla vtlfclftfr
      661 swratlvail plmltsvlce almvamgigv kvatlpvial gvgigvdyal yllsvqlhyq
      721 raglslaqay qkavaftgrv vglvgitlaa gvvgwawspi kfqadmglll tfmflwnmlg
      781 alvlipalsh fllrgqaapa paeaqatslp qtqetecsph v
//
LOCUS       WP_284385917             326 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Pseudomonas putida].
ACCESSION   WP_284385917
VERSION     WP_284385917.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..326
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34562
     Region          3..326
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(41..42,46,124,128,131,149,152..154,173..174,178,193,
                     217..218,239..243,264..267,314,316)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(136,232..233,246..251,259..266,269..270)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mskvvrfhqt ggpevlryed aevgepdpgq vrlrqvavgl nyadtyfrng typiplpngi
       61 gveaagvvea lgegvtqvav gdrvtytgfl ntlgaycter lipaaalikl pdtiafetaa
      121 amtmrgltsa yllrrlhdfk pgdsvllhaa aggvglivaq waqllglnvi gtvsteakae
      181 varahgcnhv inycaedvat rvreltdgvg vnvvfdsvgk ntfmgsldal krrglmvcvg
      241 tasgtippfd pqllaikgsl qltrpaladf iadpaekadl agelfdhvgs gririeinqh
      301 yalqdavqah rdlearkttg ssifvi
//
LOCUS       WP_284385913             331 aa            linear   BCT 25-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Pseudomonas putida].
ACCESSION   WP_284385913
VERSION     WP_284385913.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Rengstl,B., Oster,U., Stengel,A. and Nickelsen,J.
  TITLE     An intermediate membrane subfraction in cyanobacteria is involved
            in an assembly network for Photosystem II biogenesis
  JOURNAL   J Biol Chem 286 (24), 21944-21951 (2011)
   PUBMED   21531723
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Komenda,J., Nickelsen,J., Tichy,M., Prasil,O., Eichacker,L.A. and
            Nixon,P.J.
  TITLE     The cyanobacterial homologue of HCF136/YCF48 is a component of an
            early photosystem II assembly complex and is important for both the
            efficient assembly and repair of photosystem II in Synechocystis
            sp. PCC 6803
  JOURNAL   J Biol Chem 283 (33), 22390-22399 (2008)
   PUBMED   18550538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..331
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=34790
     Region          52..249
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          227..>316
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
ORIGIN      
        1 msvfkrcsvv vlawaalqga aqaapftdvl dlpampsalv assalrdvtl agqrlvavgp
       61 rghilysddh gthwqqaqvp vsadlnavsf atpelgwavg hdgvvlhsrd ggvhwqkqld
      121 gralaeqlpg tgsdnalldv wfgdarngya vgvfnlllrt vdggehwqhw ldhsdnpqgl
      181 hltslaavgd elyitgeqgl llkqdgerfs rvetpyagtl fgavgkpgvl lvyglrghay
      241 rstdggrqwq pvstgvntsl taagvdrdgq lwlasqagdl llsrddgasf spvpqsargp
      301 vtalatdtgn glvlvgergv rnqagnptlh p
//
LOCUS       WP_284385926             445 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Pseudomonas putida].
ACCESSION   WP_284385926
VERSION     WP_284385926.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..445
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=48799
     Region          1..437
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mkvtvfgtgy vgltqavcla qvghsvlcmd idaervasln aghcpifepg lapmmeknla
       61 ygrlrfttda seaanyarlq fiavgtppqa dgsadlkhvf avvdsileha dgpkvivnks
      121 tapvgtvhri kvriaqavad tsrfrvvsnp eflkegsavd dcmrperiii ggaepaevel
      181 lrelylpfsr nreklmvmda rsaeltkyaa ncmlatkisf ineianlaeh lgadiemvrr
      241 gigsdprigy dfiyagcgfg gscfpkdlqa lrrsaeaegf epqllraves vneqqkgrlf
      301 skiqrhyprg lqgkvfalwg lsfkpntndi reassrvlle alwaagarvq ahdpqameei
      361 qrhygpradl qlvpckddal rgadalvivt ewqdyrvlnl dkvpqqladr vvfdgrnvfe
      421 pehmaaaglt yygigrgqvq pacpy
//
LOCUS       WP_284385942             708 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Pseudomonas putida].
ACCESSION   WP_284385942
VERSION     WP_284385942.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 708)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 708)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..708
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=78526
     Region          57..708
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 msrifklhpl aaclavslpa laddldrqpl alpstaitdt ldsyaidlat ptqagsrlgl
       61 saletpasts sisakqiqqr nnftvqdavt rspgisyigs pgdggtglsa rgftghnsvm
      121 tlfdgarlyt gagtqtfpvd pwmveridvi rgpasvlyge gatgavvnvi pkkpfagevr
      181 nhlrlgygsw drqqlgldsg gslgerlsyr lalnqqtgng wvdrtpsrsl alsaalrfda
      241 sddlsftlah drgdaqpany ygtplidghy rsslrkknyn vqddvqhyvd ewtrlntdwa
      301 lndhlsasnq lyyiksrrhw rnaedyswdt rhqqllrgsy lqikhnqeqf gdrqaftldh
      361 rllglasktv vgaeynkvrf nvdsnapynd agsdyidpwq pqpgwfhsas plrpqtlstt
      421 htfalfaenr lqlsdrlslv tgvrrdqnhi vqeklttdsr sdrslqggnw raglvfavsd
      481 dlslygqyst sedgvnnlis lsanqmhydl tearqtevgl kqrfwegrge wtlaayhivk
      541 kkllvddpit hekqqagqqt sdgleatlel alahqwqvsa naaivraryd dfdemvgava
      601 qdragnhpan vprrtanlwl skgfgqrlea gigaryvder yadtantqsa pgytvvdadi
      661 gwqvlpdvrl glqlnnlfdr eyvqsafsgq qwlmgmprsy fatvdysf
//
LOCUS       WP_284385976             504 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Pseudomonas
            putida].
ACCESSION   WP_284385976
VERSION     WP_284385976.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..504
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=55145
     Region          3..374
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mknsftqsma wlhtwaglif gwllfaifvt gtlavfdkel dhwmqpeipa tevpqadaar
       61 raiaylqahe pqagnwgisl pserspglrv stgerrhgpv vqldprtgea ievrdsvggn
      121 fffrfhftld lprnwgifvv galalvmlaa lvtgivihkk ifkefftfrp nkgqrswldf
      181 hnasavlllp fhlmitytgl vifmliyipa gvdalfagdn rayfqaqgna rleqpgglar
      241 qpaalvdvap llaqaearlg pigglnirnp ntaaarieir pglgnriala kgqamvfdgv
      301 sgqllgdvve wraapltqrv maglhfaqfg gypmrwlyfv cglvsclmia sglvlfcvkr
      361 grkytsaeaa vrrwyrvaev cnvgfvsgll lacvgllwas rvlpvelaqr eswevraffg
      421 vwllallhag irpvrrawie qllltallci glgalgglgd amrlgvaaca lvlgvllgll
      481 vwrlwqaqwg tqkarsgrcm eaga
//
LOCUS       WP_284385994             347 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Pseudomonas putida].
ACCESSION   WP_284385994
VERSION     WP_284385994.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..347
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=38158
     Region          48..76
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(49,52..53,56..57,59,83,86..87,90..91,93..94,117,
                     120..121,124..125,128)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          58..302
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          81..111
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          116..144
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(173,176..177,180..181,183,207,210..211,214..215,
                     217..218,241,244..245,248..249,252)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          173..200
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          205..235
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..266
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          270..298
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mnrisllltm iavlsgcqst gsdlngvrsv ysggnsvlyq vqsqsnspdq amqmaamayq
       61 agdldqalyq ylrvlelape rydalvwvgr ihrergnnql aemaftevlg kapenpdalt
      121 emgllnlsmr kheqakamll kavavdqqrf tkdpantqtg aaalrvdsks plkaynglgv
      181 ladladnfae aqtyyrlael idprsalvqn slgysyymag qwadaelryk rgvsydgtyk
      241 plwrnyglll armgryeeav safeqvekra easndvgyvc lvegkldvae qffrsaiels
      301 pghypvawen lnrvqqirqi rqlggdvamp epiavgpavq vttasap
//
LOCUS       WP_284386028              73 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Bacillus
            safensis].
ACCESSION   WP_284386028
VERSION     WP_284386028.1
KEYWORDS    RefSeq.
SOURCE      Bacillus safensis
  ORGANISM  Bacillus safensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 73)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 73)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 73)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Bacillus safensis"
                     /db_xref="taxon:561879"
     Protein         1..>73
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          13..64
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(16,20,46)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(19,45)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(26..27,39,42,46..47)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mqnspynqrn lpeilrkvrk eagysqyqlg kliggrdqrn vsdiengyvr ptpelcinwf
       61 kacgayehid lvh
//
LOCUS       WP_284386076             136 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein, partial [Bacillus
            safensis].
ACCESSION   WP_284386076
VERSION     WP_284386076.1
KEYWORDS    RefSeq.
SOURCE      Bacillus safensis
  ORGANISM  Bacillus safensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Bacillus safensis"
                     /db_xref="taxon:561879"
     Protein         1..>136
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          35..>136
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrknqhvmyl sfllailwvs sfaggihaka visskaidqv ieeqmnfgri pgmsvvvvkk
       61 devvyqkgfg yadrkkkkqv tsrtffeigs tskaftalai velekqgklh lkdpvssyip
      121 gffptyngkp qrltve
//
LOCUS       WP_284386227             147 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Pseudomonas
            putida].
ACCESSION   WP_284386227
VERSION     WP_284386227.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..147
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16456
     Region          3..104
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mldenntqcp varalevlgd rwalmilrda fdglrrfsef qknlglakni lasrlrwlve
       61 sglltlqpas dgsaykeyvl tekgrsvfpv vvglrqwger flfeagelrs elvdgdtgqa
      121 letlqvrard grvlavgdcl rkvvrhr
//
LOCUS       WP_284386242             342 aa            linear   BCT 25-DEC-2024
DEFINITION  GGDEF domain-containing protein [Pseudomonas putida].
ACCESSION   WP_284386242
VERSION     WP_284386242.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 342)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 342)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..342
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38101
     Region          68..340
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mlaarfhaei csvlmaknip ttlpgtpppe aaqtllallh aqgevarlse reqlfsslld
       61 svnavlwafd wetrqvlyvs payerifgrp aslvladyne wrdsiypddl efaerslaqv
      121 llkgsvedre yrilnaegql rwlsdkcyin qqsdgdrvii vgiaeditek kqlegelqrl
      181 attdvltqss nrrhffecaq qafdnaredg tplafllldi ddfkrindsy ghqegdqvlq
      241 qiadsgkavl rrgdlfgrig geefaavfpg csaqvaeqia erlqrqiqrl sfshgeqtyg
      301 vtvsqgvtgl tdddaaldsl yaradaamyq akrqgknqiv rg
//
LOCUS       WP_284386294             339 aa            linear   BCT 25-DEC-2024
DEFINITION  Leu/Phe/Val dehydrogenase [Pseudomonas putida].
ACCESSION   WP_284386294
VERSION     WP_284386294.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Brunhuber,N.M. and Blanchard,J.S.
  TITLE     The biochemistry and enzymology of amino acid dehydrogenases
  JOURNAL   Crit Rev Biochem Mol Biol 29 (6), 415-467 (1994)
   PUBMED   7705101
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10500541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..339
                     /product="Leu/Phe/Val dehydrogenase"
                     /EC_number="1.4.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35492
     Region          23..130
                     /region_name="ELFV_dehydrog_N"
                     /note="Glu/Leu/Phe/Val dehydrogenase, dimerization domain;
                     pfam02812"
                     /db_xref="CDD:460706"
     Region          140..338
                     /region_name="NAD_bind_Leu_Phe_Val_DH"
                     /note="NAD(P) binding domain of leucine dehydrogenase,
                     phenylalanine dehydrogenase, and valine dehydrogenase;
                     cd01075"
                     /db_xref="CDD:133444"
     Site            order(174,176..178,197..198,202,231..232,253,255)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133444"
     Site            285
                     /site_type="active"
                     /note="Phe binding site [active]"
                     /db_xref="CDD:133444"
ORIGIN      
        1 mfalmqstrt qslhlftdpp tglkavvaih seqlgpamgg crylpyadde samtdairla
       61 qgmsykaala glplgggkav imrnphvenr aalfeafgrf idtlqgrfii avdsgtstld
      121 mdciaqstph vtsttasgdp sphaamgvfa girattsfrl gsddlqglrv avqglgnvgy
      181 alaeqlhaag adllvsdldp grvrlaveqf nahpvtndal istpcdifap cgvgpvlngq
      241 svmqlrcaav agaannqltt lqvadqlesr gilyapdyvi naggliyval thsgedlgti
      301 tahlaripsr ltevfghaqa ekrsparvaq mlaerllyg
//
LOCUS       WP_284386295             327 aa            linear   BCT 25-DEC-2024
DEFINITION  FecR family protein [Pseudomonas putida].
ACCESSION   WP_284386295
VERSION     WP_284386295.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20752687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..327
                     /product="FecR family protein"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0016989 - sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35142
     Region          13..54
                     /region_name="DUF4880"
                     /note="Domain of unknown function (DUF4880); pfam16220"
                     /db_xref="CDD:435227"
     Region          107..327
                     /region_name="FecR"
                     /note="Periplasmic ferric-dicitrate binding protein FecR,
                     regulates iron transport [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG3712"
                     /db_xref="CDD:442926"
ORIGIN      
        1 msrlppitea qsraalqwls rineqpaqae gaafkrwlla dpghreayaq aqllwqnsai
       61 paarlaaeeq aslqryldam arpparhpwl qraaalavaa clvlavgvag gwhpglwlqd
      121 lqadyssadq vrlvtladqs qvmldagsai avdfaqgerr vrllhgaaff qvthtgapfv
      181 veaaggevrv lgtqfevrkq gegaqvtvqs grvavspvpg aaareltanq qatyaggrvg
      241 dtltvasdnr lawrqgwlny yqvplaqvve dlgryypgri lllddelgqr kvsgsfpvaa
      301 pllaldslgk vmgfsrqtvl grltvir
//
LOCUS       WP_284386440             694 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Algimonas
            ampicilliniresistens].
ACCESSION   WP_284386440
VERSION     WP_284386440.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 694)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 694)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..694
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76433
     Region          50..646
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mgiglgardf tiiavvlast aapvfarqdv avpaeqaanl dsfapsfftq fqpntaldmv
       61 eripgftlrs gddergfgva dtnflingrr pstksqdaed ilsripagtv vrievldgas
      121 ldipglsgqv vnvvaravel sgrwrysarf eegtepqile gevvlsgrrg dlgfsvglkn
      181 rqftltedsv erffdssgal iedrtedvyl rnvapsanln ltwtptigrf aghvanlnas
      241 iekdnenngl reiftaidpt rtsgesfadi gedeiqieig gdyalplpia gldgtlklia
      301 lnqlddgesg vvfvsardgs iplrtkfsed fkegeligra eygfkagsgh dvqisveyay
      361 nflesattfq nsftapiide vrveedrfna ritdswqiss dlslqtsiga eysslqvvnp
      421 lsdarnffrp kgfaavsyrv sdrytlraka drsvgqldfd tfvstrnlvd nlltsgnaei
      481 kpsqstelsl efertddkll sgrirpylel iedpidrill snnaeapgnl dsatrygiea
      541 natllfdtlg vpglrleasg gigeseiddp ltgeqrqinf neeysyslfa rydipqsnia
      601 ltgrvnndes spfyrlddir tidvrrpfls lglihknvfg mqltisgtnl ldntviqerd
      661 rfltpdrrlg plirserfer qrgrrlsitl tdtf
//
LOCUS       WP_284386449             754 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pseudomonas putida].
ACCESSION   WP_284386449
VERSION     WP_284386449.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 754)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 754)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 754)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..754
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=82778
     Region          42..714
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mewlglqlfa dlpatgrivi dcqhepflvl layfvacaac fatldmaerq shsedptahr
       61 qwnmlgaccl aggiwamhfi smlafqapve vhydasltil sllialavaw lamhsldrsq
      121 mrahhylqsa vliglgiivm hfvgmaalet garqyyqsgl llasatiall tsltalylar
      181 yfrhgsgnlh qamkygasll maggivathf tamsamtlvi padtalrlps gdnslqlalg
      241 igfitllisa asissaladk klqskehdlr rvsvllsqld qaraslqqaa hydaltslvn
      301 rrgfnqvfae rlaehkvtes hlavmfldid hfkrindslg hdagdellkv iashikaatr
      361 nhdlvarlgg defcvvtsln nrdearhlaq rimqrmkepi nlggrrmvmt tsigisifpe
      421 dgttaeellk hadlalyqsk gngrnslnff ndslktqasi alqleeelrv alleehglcv
      481 hyqpifdmrs rqvaklealv rwrhpqhgll gpdrfvaiae angliidldl wvlrhacadm
      541 aylqrhghgn lkvtvncsav tlshdelpne vekalfhagl aprqlelevt enalmgdiqr
      601 tvnllkrvra lgvtlsiddf gtgysslayl krlpldvlki drsflqdvpg sqkdreivqa
      661 iivmahtlhl qvvsegveta eqlafleahg cdylqgyllg rpeplaelrs llerlqhqgg
      721 vfkpccdtaq pgspdlfagt pglragasiv rqgh
//
LOCUS       WP_284386451             610 aa            linear   BCT 25-DEC-2024
DEFINITION  ABCB family ABC transporter ATP-binding protein/permease [Algimonas
            ampicilliniresistens].
ACCESSION   WP_284386451
VERSION     WP_284386451.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 610)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..610
                     /product="ABCB family ABC transporter ATP-binding
                     protein/permease"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66909
     Region          24..604
                     /region_name="ATM1"
                     /note="ABC-type transport system involved in Fe-S cluster
                     assembly, permease and ATPase components
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5265"
                     /db_xref="CDD:444078"
ORIGIN      
        1 msppthpdav eteerglleq lsalrglvpy vlppgdlsak vrtalaiflv ivsqfilvga
       61 pfflgraqda vadaagrdea faqvglfiaf fvvgygalrl lstlfseare yvfapvaqqa
      121 qrkiatetfa hlhrlslryh lakrtgglsr iiergvraid flfrfllfni gptllqlvia
      181 gaafavayng wfaviaivvv vayvtftvmt tewrlkfrre mnkrdteswa ravdsllnye
      241 tvkyfdaerr evkrydvame ayakaairsr tslatvnigq sllmnagiva smvlaaafil
      301 ggdmstgdml titlvlnqly rplnilgfay reikqaltdl ermfqlleep pevidaeqat
      361 diknvrgqve fdavdfhyep dreilrglsf kaepgqtvav vgptgagkst lsrilyrfyd
      421 iaggsvridg rdirditqas lraaigmvpq dtvlfndtig yniayarpda sqaeieqaar
      481 daqihdfias lplgydtmvg erglklsgge kqrvaiartl lknpailild eatsaldsat
      541 evdiqaalgl asqgrttlvv ahrlstiqda dlilvmdqgq ivergthael lakaglyadl
      601 wtrqdttela
//
LOCUS       WP_284386543             345 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Algimonas
            ampicilliniresistens].
ACCESSION   WP_284386543
VERSION     WP_284386543.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..345
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38562
     Region          1..339
                     /region_name="PobA"
                     /note="Chlorophyllide a oxygenase/letal leaf spot protein
                     [Coenzyme transport and metabolism]; COG5749"
                     /db_xref="CDD:444459"
ORIGIN      
        1 msgfvhdiwy fagiksdlpa sglkrviiag epiclgrred gtyfairdic phraapfsag
       61 clkggtvecp yhgwrfdtdd grctdipalt adsivepdri rvrtfpiaqt ghilwvwfss
      121 dkrfqgeppf pppafpltet kpiiddgvkl nchvdhavig lmdpahgpyv hkqwwwrsea
      181 sihekakafe prergfamaa hspssnsaay kllggkpvte itfqlpgirt ehitvgdktv
      241 lsftavtped eghtrirqlf fsdhglfrll spvlargaka flrqdadmvd lqaqglrfdp
      301 nlmliedadt qakwyhqlkl awakaqesge pfvnpvkart lrwrs
//
LOCUS       WP_284386588             251 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Algimonas ampicilliniresistens].
ACCESSION   WP_284386588
VERSION     WP_284386588.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..251
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27509
     Region          46..251
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mgaqhinheg aklayhyveg rpeiggptmi wcgglksdmd gtkavflheq ceragrpfvr
       61 fdyfghgisd geftdgtvsr wasdvvamid rfgkngvvli gssmggwasl laaldrpdav
      121 kglvlinpap dftekmvwsg wddhkrtmli edgvvyepsd ygepyaysra liedgrarqi
      181 ldapidfngp ieilqgandd vvppaysrli vktvtservg ytlvkggdhs lsrphdlsrl
      241 wttletmlaq l
//
LOCUS       WP_284386647             115 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Algimonas
            ampicilliniresistens].
ACCESSION   WP_284386647
VERSION     WP_284386647.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..115
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12925
     Region          12..90
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mshdiqmsaq pifrgladpt rreivtllar esrsvseiag efpisrnaiv khlrvledsg
       61 lvvtetsgre rinhldphgl klafdwlsdf nqfwdaklld lktaveedvy dtpnp
//
LOCUS       WP_284386680             463 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Algimonas
            ampicilliniresistens].
ACCESSION   WP_284386680
VERSION     WP_284386680.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..463
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49903
     Region          60..460
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mktslkvtta alaisafsvi gcehtptagt dqqstvadas acqvsapyet aqfdnefetk
       61 idglmahmmd rgiapgavvq itqkgeivlk kaygfadled qkpmqtdslf riysmtkavt
      121 tiaalqlvdk gqleldapis rylpafadik vatdetgaat rppsraptir dlmrhttglt
      181 yrtgaktdpi aaiyaklgvp agpgvsdapt ngmdpvvgne mfaerismap lkhdpgqqft
      241 ygnstdvlga vvatvsgqsl sdyldenifi ptgmtdssfi idperqddft sayivpsqtp
      301 arssidyttp iddlkpqtpy rvdpyrdgiy tktpdfefgg agmvadaddy laftnaling
      361 sprlvspeiw aeasrdqlpa takaqdafld krgfglgfav resethdgtv fpqcglfwag
      421 aastyfwide etettgvlmt qvfegdvrsy fqellnavya kpq
//
LOCUS       WP_284386711             423 aa            linear   BCT 25-DEC-2024
DEFINITION  spinster family MFS transporter [Algimonas ampicilliniresistens].
ACCESSION   WP_284386711
VERSION     WP_284386711.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..423
                     /product="spinster family MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006869 - lipid transport [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44994
     Region          11..404
                     /region_name="MFS_spinster_like"
                     /note="Protein spinster and spinster homologs of the Major
                     Facilitator Superfamily of transporters; cd17328"
                     /db_xref="CDD:340886"
     Site            order(21..22,25..26,29,62,112..113,115..117,120,140,
                     143..144,147,225,228..229,232..234,237,269,321..322,326,
                     330,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340886"
ORIGIN      
        1 mkrsdnrwyl lavltlvyaf nhvdrqimvi lqepikqefg lsdtqlgmlt gflfaafyat
       61 lgipfaawad rgnrrniiti altiwsgmta lsgfaqnfwq lafarmgvgi geaggtppat
      121 smisdrfpah erafalgiyt tgislgilvg fmlggliaer ygwrvgffva gvpglllaat
      181 lmltvkepkr geadaivddg iapplsetlr fffsqkamvf mllggvltcv sanaflagvp
      241 lyfirvhsvp lgelgialgl llggvggvga ivigkicdrl sakdlrwrpw iialtsllal
      301 pfaaafllve tkaaayaiya ipsffgliya sisyaamqel apprmramas avmllcltli
      361 gigvgpvlvg vlsdafaael garsiarall wlltlnvasa gfyliaarny rgdvaraisl
      421 gaa
//
LOCUS       WP_284386741             598 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Algimonas ampicilliniresistens].
ACCESSION   WP_284386741
VERSION     WP_284386741.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475669
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..598
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=64352
     Region          138..270
                     /region_name="TolBN"
                     /note="TolB amino-terminal domain (function unknown)
                     [Signal transduction mechanisms]; COG5616"
                     /db_xref="CDD:444347"
     Region          318..572
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          324..365
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          370..399
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(413..414,416,440,443..444,447..448,450..451,474,
                     477..478,481..482,485)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          438..468
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          473..498
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          510..536
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mqkifdelrr rnifrvagvy gasswliiql giafetslnl pgwfdrlltt lvllgfpial
       61 ilawafeltp eglkrteigg psedgsrrag rklgialial isvviglitw riitsevqrq
      121 ndmssaassd gstatsvteq samdalrtia vmpfenladd erydyissgl sssirddlag
      181 nrllrvvars ssqavanesl galeiaerln vanvlegrve krgekllitv slvdartgft
      241 rwvetltydp ealidirnki tsvcaqtlsv dqrsqgrepg datvpeafte yfrgttllyq
      301 eatleslesa rrhletavql dpgfadahss lagvylilga vsadkglada midkseamar
      361 eaialapsda dthavlgeil msgrvdmvaa agpfdraqal glssgdglsr havflsatgr
      421 hdeaieqayr aktldplsas asetlglayy adrqfgsait ayrlalsqnp eryttrarlg
      481 lahiysgsve dgldwcskee nlmerlpcea aaavrkgese saekalgeli evfgdagayq
      541 qaemlaemgq tevaiatllk aeslgdtgla magydpaldn lrdderfqal lvrlglsd
//
LOCUS       WP_284386776             468 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Algimonas ampicilliniresistens].
ACCESSION   WP_284386776
VERSION     WP_284386776.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..468
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49555
     Region          15..410
                     /region_name="FucP"
                     /note="Fucose permease [Carbohydrate transport and
                     metabolism]; COG0738"
                     /db_xref="CDD:440501"
ORIGIN      
        1 mvtttatagv paginrnrlf wlsclslivt amtfairagi ltqlsdqfal tdtelgwvng
       61 maflgfplam vvfgflynvl gpklimilaf lghvlglvlt iyaggflgll istffigfan
      121 gsveaacnpm vadlykddkt kwlnrfhvwf pggivigavv syimtnmgig wqpqiaimlv
      181 ptaiygflif ttvfpdvdpd skslrldgks illisavfgl lvligtpntl ltsvpggiml
      241 plilvlalvy lltfvltgrh rdavllvalm gimsmtatse lgtqqwveri lgssgaqpml
      301 ilamvtgima vgrffagpli halnplgvll asavvttlgl fmmatmsggm vyvaaivfai
      361 gvcyfwptmi gvtaqyvprs galgmslvga agmfaltiwn pviggwidaa rktaedtglt
      421 gdaievaagq galsklllfp ivliaafavl yflrkriiat anpiaeev
//
LOCUS       WP_284386819             360 aa            linear   BCT 25-DEC-2024
DEFINITION  FecR family protein [Algimonas ampicilliniresistens].
ACCESSION   WP_284386819
VERSION     WP_284386819.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20752687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..360
                     /product="FecR family protein"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0016989 - sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39877
     Region          20..62
                     /region_name="DUF4880"
                     /note="Domain of unknown function (DUF4880); pfam16220"
                     /db_xref="CDD:435227"
     Region          75..353
                     /region_name="FecR"
                     /note="Periplasmic ferric-dicitrate binding protein FecR,
                     regulates iron transport [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG3712"
                     /db_xref="CDD:442926"
ORIGIN      
        1 msvheifger pdypphdadd qatywmtmlg sdrctpaqrr sfahwlddrs enrvafdnla
       61 aivdgaelva edpliralrr dalghglpkp fwirqrskls vaavgfaaal lmvafvqwgt
      121 spfetspsdv tytvesdsnl natllttqig eqltrqlddg stielntdse vryeladnqr
      181 siyllrgqav fdvahdpsrp fvvfagdrrv talgtlfevr mdsastrvtl legkvrvdei
      241 altdeidttk paksfelkpg erfvsvdevm stvpatviet dlswregrhs fkdaklsdiv
      301 aemnrytnrk ikladpsige lkatanfklg stlslastlg psfgltvkdd pnndhilvdw
//
LOCUS       WP_284386820             649 aa            linear   BCT 25-DEC-2024
DEFINITION  elongation factor G [Devosia yakushimensis].
ACCESSION   WP_284386820
VERSION     WP_284386820.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 649)
  AUTHORS   Margus,T., Remm,M. and Tenson,T.
  TITLE     Phylogenetic distribution of translational GTPases in bacteria
  JOURNAL   BMC Genomics 8, 15 (2007)
   PUBMED   17214893
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 649)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..649
                     /product="elongation factor G"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=68652
     Region          1..630
                     /region_name="PRK13351"
                     /note="elongation factor G-like protein; cl46912"
                     /db_xref="CDD:481252"
ORIGIN      
        1 mrtlnlgila hvdagktslt erllfaagvi pklgsvdagn tqtdtleler qrgitirsav
       61 vsfaigganv nlidtpghpd fiaevertlg vldaavvvvs avegvqaqtr vlvralqrlg
      121 vpfvfflnkv drlganyant ikalreqlpv rplamssvte agsksamvaa ldpaddpfra
      181 llrealaend ealledylla perltvqrmh qalagqvgrg llhpafagsa atgvglstlm
      241 eaietllpaq eadpdgpvag rifkiergwg gekqaylalt sgtialrhml dlpqgearit
      301 gikvfeagkl mpattlkagq igrisglgda vigdlvgaga ghdervhfap ptlearvlpc
      361 hkadnaalwt alsqlaeqdp linlrhdeea geifvslyge vqkeviqstl aldfglevvf
      421 lestvicver vlgmgeglde vfrggnpfva tvglrveprp agtgnsfvld vslglmptgf
      481 yraieetvhe vlrqgvsgwq vidchvtvtk agqkapmtta adfrqltplv laaalaeakt
      541 vvcepvsrfy ldlpasmvga mvtalaqaga vvtdtaides marlegtiaa amvhgmqqql
      601 pgltggagam ecvfdhyapi sgtvrtrlrs gpdpfhrvdy lialrrlpg
//
LOCUS       WP_284382730             103 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Litoribrevibacter albus].
ACCESSION   WP_284382730
VERSION     WP_284382730.1
KEYWORDS    RefSeq.
SOURCE      Litoribrevibacter albus
  ORGANISM  Litoribrevibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Litoribrevibacter.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 103)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 103)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 103)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Litoribrevibacter albus"
                     /db_xref="taxon:1473156"
     Protein         1..103
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10436
     Region          17..103
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mdiklilatl alatatsavq aadinagkak aavcaschga dghasiptyp nlagqnagyi
       61 eaallaykag qrtspqaaim ksmamplneq diknlaayys slk
//
LOCUS       WP_284386821             965 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Algimonas ampicilliniresistens].
ACCESSION   WP_284386821
VERSION     WP_284386821.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 965)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..965
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..965
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=106915
     Region          43..468
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          598..965
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mshtrlrlma ttaialmita cttsaqdqay datnatiqaq avsvdlpela pdpalvtgtl
       61 engiryailp nktppgraal rvrfdtgsfn evpgtgglah ylehmafngs knvpegemiq
      121 ilerlglsfg adtnastgvd rtiyklnlpn tddevldaaf mlmretaenl tldedaidre
      181 lgiilsekrt rdtsiyrawe aymgllangs damsrlpigt eetlraiqsd dfrayynahy
      241 hpektvvafv gdadpkviea riretfgewt gegdagdtli ptsatpeasr vvvyeedglp
      301 tqvrlvstqp yvkhedtpew rrertlrsla ygmmsyrmra laeqvdrpfv nasmgrhstf
      361 dltegpvfsa ytqpenwdra lrgldtelrr alqygfsqse ldaqlarlda svkaraegad
      421 trattsrtgg ltgalmstfd ndrvfthpsq dlarfeamre tltldavntk lrsewgdied
      481 lsvfiqtsda petpeaavrs vlldsrstpv skpdmsedkp fayedfgtpg kvvsdrvved
      541 vdarlidfen nvrltikttk fqddrvllkv tfgdgmlsap vrnegmrrma lgviqssgle
      601 ehepdelrri lagrlvasna ftaraaddkf sfttltvpdd mllqfqiyaa qlsaqafrer
      661 arlnyidklk awyprhdatm dgvyskhvlr rvyggdkrfg fenedqfyat eltkleawlr
      721 pqfeqgpvev tvigdidpev vieavaqtlg alptrsslds pdspsvaamr qvsfgaqgdg
      781 ptifrhkgdd nqaqlriywp andgkdplya rqlsvlravl rnrlvkdire geattyspga
      841 gshasttfdg fgyvlavltl kpedvdamad kvrdiandla sgnidqdefd ralkpiverl
      901 dstektngyw lnvlddaqsd glgltshrsr asdydamrve diqslaatvf daeraldiri
      961 lptee
//
LOCUS       WP_284386829             293 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Devosia yakushimensis].
ACCESSION   WP_284386829
VERSION     WP_284386829.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..293
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32958
     Region          7..238
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 madmsrpprv saiiivyngd rylgeaidsv lsqtfpdwel iiaddgsvdr sreiardyaa
       61 rhpehiraia hpdggnhgms atrnlgiaea rapligfldc ddiwlsgkla eqvdlldrhp
      121 daqmiygrtl iwhswqtgnv gddffydlgt tpdrliaapq lltlllenks qtpttcnalm
      181 rsaflrelgg fenrfrgmfe dqvffakall eapayvssrn waqyrqhkes fsaksagrgg
      241 dgrarlaflm wlagyvvrra pwqlgvlmqt arlvarecwa iarprrpawl rtr
//
LOCUS       WP_284386861             488 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Algimonas ampicilliniresistens].
ACCESSION   WP_284386861
VERSION     WP_284386861.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..488
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51523
     Region          96..485
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mtsdsnasrg vsqniglaag pmvaillflf frpdglsltg tataafaawm aiwwsteaip
       61 vavtaflplv lfplfgintm svtassyshp iiylflggfv ialaiersgl hvraalkvfr
      121 maglngkslv agfmaaaali smwisntstt lmllpiaasv tlvirdtmsd slskteisnf
      181 etsmllglay aatlggmatl vgtppntfmv gfmadsyqmd idflrwmivg vplalimlpl
      241 twlvltrfly pvnfratqqa rshidhlytg lgtmsvaerr tlylfialvl gwvlrkqiva
      301 vtgltgltds gvamaaavaa fiipsgktge glitwedmkr lpwgvlilfg gglalaggmt
      361 atgltlwlgk qlaplgeini avlvvcsall viflteltsn lattatilpv maaiavetgq
      421 dplvfvipvt laascafmlp vatppnaivf ssgrvsiprm mragfvlnii gvivlslval
      481 klvplvfg
//
LOCUS       WP_284386867             452 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Algimonas ampicilliniresistens].
ACCESSION   WP_284386867
VERSION     WP_284386867.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..452
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=49358
     Region          33..452
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 miskthgptl alqvlgivav allisltatq tqayvtmgll ctllgiqswl lfrsarrgqt
       61 eiarfadslr ygdfnqtfss ahltselsna fngaldsfrt lnvvrdaeka klralldeap
      121 nalitldsnd llsclniaar klfgqaseas ihidaisdre laqaikqmrs gerrlirsen
      181 nglthritlt analtvrgsd lkivairnid selgaaefea whdlvrvlth elmntvtpvn
      241 tmahtakelv delsvaqmpl nsepetheqw qdlrsavhai agrtlglkkf aesyrkiari
      301 papekrdvli gpflsrvaas mtdtldkvpl kiievtpqll srfdpnlieq alvnllanar
      361 datleagqtt piilsaedra dsllvlrvtd sangvrkdie griftpfftt krdgtgvgls
      421 lvrqialahg gyaryaprtp sgsvfevilp me
//
LOCUS       WP_284386943             482 aa            linear   BCT 25-DEC-2024
DEFINITION  leucyl aminopeptidase family protein [Devosia yakushimensis].
ACCESSION   WP_284386943
VERSION     WP_284386943.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Drinkwater,N., Malcolm,T.R. and McGowan,S.
  TITLE     M17 aminopeptidases diversify function by moderating their
            macromolecular assemblies and active site environment
  JOURNAL   Biochimie 166, 38-51 (2019)
   PUBMED   30654132
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Lowther,W.T. and Matthews,B.W.
  TITLE     Metalloaminopeptidases: common functional themes in disparate
            structural surroundings
  JOURNAL   Chem Rev 102 (12), 4581-4608 (2002)
   PUBMED   12475202
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415720
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..482
                     /product="leucyl aminopeptidase family protein"
                     /EC_number="3.4.11.-"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0030145 - manganese ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0019538 - protein metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50564
     Region          1..477
                     /region_name="PepB"
                     /note="Leucyl aminopeptidase [Amino acid transport and
                     metabolism]; COG0260"
                     /db_xref="CDD:440030"
ORIGIN      
        1 mnitfeasrg vgtgaaavei lhpetlaafv dassererla riltaedfag rtgqvvilla
       61 pagriedrli laglsseasv fdaqlagarl avkcldlpgd lalaypegld anlfaefvyg
      121 flartyrfdk yrsaprsgla nlkitgcsev vitqikslqv avetvhivrd lvnepgnalp
      181 plelaarieg lcaplgiave ildatklael ganlllavgq gsvnppcmvv lrmqgegtpi
      241 glagkgmtfd tggihikpva gmwemkndma gaatiaasma amarlgisrp lvaalglaen
      301 masgsatrpg dvvrslagpy veirntdceg rlvladclty lqqrfapgql idvatltyav
      361 qvglgpryag iygnsrpeid allqsaertg elvwpmpida gfhdelasdf adflnwpgvt
      421 ygnasiaaaf lekfvapatp wlhidiagpa yapkgnslsp aggtgfglrm lvdylaktrt
      481 fa
//
LOCUS       WP_284387036             440 aa            linear   BCT 25-DEC-2024
DEFINITION  site-specific DNA-methyltransferase [Algimonas
            ampicilliniresistens].
ACCESSION   WP_284387036
VERSION     WP_284387036.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..440
                     /product="site-specific DNA-methyltransferase"
                     /calculated_mol_wt=48442
     Region          13..100
                     /region_name="ParB_N_like_MT"
                     /note="ParB N-terminal-like domain, some attached to
                     C-terminal S-adenosylmethionine-dependent
                     methyltransferase; cd16403"
                     /db_xref="CDD:319260"
     Site            order(59,61..62,64..65)
                     /site_type="other"
                     /note="putative ParB Box II like motif [polypeptide
                     binding]"
                     /db_xref="CDD:319260"
     Region          171..415
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 msnlphpkie mvptdslipn prnarrhpdh qisklaltia tvgwlvpiii ddnnvivagh
       61 grllvalklg hrevpcirak fvteadkraf alaenripel sttdksilnd ellfvfedkq
      121 afestgysvg didfsvtvps qapeaeevsl pdpntyavsr vgdlwqigph riycgdarsv
      181 dswerllgdd radivfadpp ynvpidghvs gngknkhref vmgagemnqa eftsflriia
      241 rncvrfskng sihyiamdwr hcrelldaad gvytehkqiv vwvktnggqg afyrsqhefi
      301 fvfksgkakh innfklgetg ryrtnvveya gantfrkgrd edlaahstvk ptalvmdfll
      361 dcshagglvv dpclgsgttl laalhtgrrg agmeldplyc dtalqrlsva ngltpildgd
      421 grsfeeikte rlgmeathag
//
LOCUS       WP_284386959             106 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Algimonas
            ampicilliniresistens].
ACCESSION   WP_284386959
VERSION     WP_284386959.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..106
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11104
     Region          22..87
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(27..28,32..34,47..49,58..61,63..64,67..68,70..71,
                     77..79,84..86)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mtrpdisspe afeimserih eaahvlkama sdtrlkilca lsagelsvge laeltnrsss
       61 svsqhlaklr saglvtanrd aqtifysctg gvgkvvvdal cghyad
//
LOCUS       WP_284387085             703 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Devosia yakushimensis].
ACCESSION   WP_284387085
VERSION     WP_284387085.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 703)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13939702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..703
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=73814
     Region          223..537
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
     Region          495..678
                     /region_name="DUF3520"
                     /note="Domain of unknown function (DUF3520); pfam12034"
                     /db_xref="CDD:432277"
ORIGIN      
        1 msenmhdplt vlsqakapda radakkrals agmaafeaaq aqaaqksaea tkgnrkgqrl
       61 tsiisilkgn wimdmrlpig taaiallvlp lgyqlytsts mtpgvsapaq taannqpaea
      121 vapppaatpe ttmpvspdpl gaasqdaeip avqqaepavp gdelrmrqda apqfgnstim
      181 apsaapitvl pgavarnsdn ymlaapaeas gdqftsfeeq rlkvaaeepv stfsidvdta
      241 sysyvrrsle dgyvpepdav rveellnyfp ydyapatsad qpfqptmavf ptpwnpktql
      301 leigikgyvp pagedkpsnl vflidtsgsm depdklpllq rafgllvdql sgndtvsiva
      361 yagsagvvle ptkatdkaki laaldqlyag gstagaegie layklaeqak veggtnrvil
      421 atdgdfnvgi ddpekledfi kakrdsgvtl svlgfgmgnl ddatmqalaq ngngnasyis
      481 nfreaqkvlv eevgstlhmi akdvkiqvef npavvseyrl igyetralnr edfnndavda
      541 gdigaghtvt alyeitpvgs ggelvdplry ggdaaaaagg neeiaflkmr fkmpdsdvsq
      601 lieqavtpsv vyddisavsd darfaaavaa fgqklkgsdy vrgmswdair alaqsgkgad
      661 esgyraefiq llktaallkp dtapaadaee dacvaagead sac
//
LOCUS       WP_284387105             347 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Devosia yakushimensis].
ACCESSION   WP_284387105
VERSION     WP_284387105.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..347
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35091
     Region          40..343
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtalglpspv rqpiagrsnr vrslwllgla gllaalcals vttgsrdvgw adiaaaltgg
       61 qdnigqaavs lriprtllav lagsalglag avmqgvtrnp ladpgilgvn mgaslavvig
      121 vawfniasaq ayiwaaiiga gctagfvyti gslgrggatp lklalagvat siafaslvma
      181 vvlprndiag girswqiggv ggatferilp vlpflavgmv iallsarrln slalgdemaa
      241 glgervalar gvsalgaill cgattaicgp igflglivph lcrllvgady rwllpfsalg
      301 gaslllladi agriiarpae ldvgivtafv gapffiwvvm rqrirel
//
LOCUS       WP_284387149             273 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Devosia yakushimensis].
ACCESSION   WP_284387149
VERSION     WP_284387149.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..273
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29531
     Region          53..266
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mlryftlgla llmagsayaq ssgippeemd nsrrlagdai nvcfdvtslg rafdedvaka
       61 igdalflevn vvegfggfpl sgdgfldelt lamnntcdmf mgvsvsvnsp vsdafaltrp
      121 yatipfvfvv adpdwqklgd ipkdrklgta maslgemnyi twaqqqpeae rwvrypyanf
      181 dlmttrvldg tiagmvlwqp afarlqqerp datalrvian dpipnaevhv galvssrnsf
      241 lrnqvdqaid alvadgtiag fleqygytgh age
//
LOCUS       WP_284387219             616 aa            linear   BCT 25-DEC-2024
DEFINITION  autotransporter assembly complex protein TamA [Devosia
            yakushimensis].
ACCESSION   WP_284387219
VERSION     WP_284387219.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..616
                     /product="autotransporter assembly complex protein TamA"
                     /GO_component="GO:0097347 - TAM protein secretion complex
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=65970
     Region          28..616
                     /region_name="TamA"
                     /note="Outer membrane translocation and assembly module
                     TamA [Cell wall/membrane/envelope biogenesis]; COG0729"
                     /db_xref="CDD:440493"
ORIGIN      
        1 mapasafeif giklfesqsd adaeaviadp qpykvnlsvt etgapenavr nasaliades
       61 epasgavgll akargdykri iaalynegyy ggtvsiriag aeaanlppdt klpkpvdvai
      121 lvtpgplfhf nsvnivnqap ptsdpfdhve ppssrgfgsg eiaksstilr aeqlaleawr
      181 qqgyakavvv trdvvadhas ssvdvtitvn pgmkaafgev svsgtermdp efvrrqtglt
      241 vgeeydpdel alaqkrldrl evfqaarlea aqsispdgll pynlivqesa grrfgigaty
      301 stvdglgveg fhlwrnlfgq aerlrldarv asiawpldte efdymfggtf tkpgfltpdt
      361 dlvaaisaer tiyptymets anaklglthf fsdqitfegg avfersqfed dvfgtrdfmt
      421 agvyasatld frdnkvdpts gwylkadlep fyefnyenpa aqivvegrty fgfgeedpfv
      481 lagrfkagal vgpdlseipp dklffggggg svrgyafksi gvddglgnvt ggryllegsl
      541 earakvtsdi gvvgfldggy vaadtfpdle dlrlgagvgv ryytglgplr ldvavplnkr
      601 agdpdyaiyv gigqsf
//
LOCUS       WP_284387276             298 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Devosia yakushimensis].
ACCESSION   WP_284387276
VERSION     WP_284387276.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..298
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=31368
     Region          21..296
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mavlnrdggt lrtmdldglc dqaigifarh ghvldcriva geaveaelqr iagtagvdvm
       61 laaggdgtvs aaagiafatg mplavlpagt mnlfaralqm pleltaamea ladgeigavd
      121 iatandrafv hqfgvgvhar lvrirermvy rsrigkmlas lravvsaavr ppdfeaeiqt
      181 rhgrerrrvs giavsnnplg dghiphadrl dagvlgvyla apmstwalir lavdvllgrw
      241 rsspavseqe veqvtlsfpr rkrgaqavid gelirlapsv vlklhpgalk vllpkaga
//
LOCUS       WP_284387322             293 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Devosia yakushimensis].
ACCESSION   WP_284387322
VERSION     WP_284387322.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..293
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31602
     Region          17..293
                     /region_name="COG4132"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443307"
ORIGIN      
        1 mtdttlpppk pprripwdsl avfpfvifav mflflptlsl vgaaftdrag sftfdniagl
       61 ftdqilaayw isirisgasa ilgaliglai tlaiirgrlp aglrsavmtf sgvasnfagv
      121 plafafiatl grlglvtiil rtvfgfdlyr sgfnllsfwg ltltylyfqi plmmltiapa
      181 vdglkkewne aaqmlgasqw qfwryvglpi lwpsflgtls llfanafgai atawaltgsn
      241 lnivtvllyn qirgdalqnp glgaalalgm ivitslanvi ylvvaaraer wmk
//
LOCUS       WP_284387349             534 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Devosia
            yakushimensis].
ACCESSION   WP_284387349
VERSION     WP_284387349.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..534
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56194
     Region          23..517
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mkrlllgata ltlcagfsga ayadftlnil hindfhsrfd pitgtdsncd aetdaagecf
       61 ggiarlktii ddtrakyadg nslllsagdn fqgslyytty kskvvsdffn qmgfdvvatg
      121 nhefddgpee flkfieaakf piiggnfdvs rdenlrgkik gsfvievgge kigiigatte
      181 dtpdiaspgp dieftdviqy vrgasealda agvnkiills higytvdqqv aaalplvdvi
      241 vgghshtlls ntaegaagpy ptmvtnpdgv evpvvqanqy gkylgdiait wddngvvtka
      301 egepflidas vkgnedfaaq ladlagpiad ltgkvigsst aplegarevc ramecsmgnl
      361 ladaildrva dqgatiafqn gggirasida geitvgdvlt vlpfsntlat vqisggdvie
      421 alengvsdve ngagrfaqva glkysfdlre pagsrvsdvl vkdgenwvpi deeatytivt
      481 nnyvrgggdg yepfangenp ydfgppleev vadyiaklgg eytpytdgri teik
//
LOCUS       WP_284387400             149 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Algimonas ampicilliniresistens].
ACCESSION   WP_284387400
VERSION     WP_284387400.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..149
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15914
     Region          <5..144
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mmmvitvlsg lvlitaliql aridwathrl pniitlplia agllwafgta edfyphllga
       61 algygvfwav evlyrlirkr dglgrgdakl laaggawcga walpaivlia svsaliyilp
      121 kgeqrdtrip fgpflaigig avwlvqail
//
LOCUS       WP_284387434             110 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Devosia yakushimensis].
ACCESSION   WP_284387434
VERSION     WP_284387434.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..110
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11381
     Region          5..107
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mngavyllia ivgeviatsf lrasagftql gpsivvvvgy vitfyffsla lqtipvgigy
       61 aiwsgvgiil vsiiayfayg qtldlpalig iglilagvlv inlfsqssth
//
LOCUS       WP_284387457             296 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Devosia yakushimensis].
ACCESSION   WP_284387457
VERSION     WP_284387457.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..296
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32551
     Region          2..279
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mitlahisdi hlspmpdial rdlfgkrltg flnwkikrhg elnsetlasl vahmqaqnad
       61 ftavtgdltn laldieiera gkwlealgsp driavcpgnh dayvpgalee aqkqwgnylr
      121 getldgaafp fvrrvgelav iscssavptr pflaigrfee kqadrlsril kamgdagyfr
      181 tvlihhppna elqhpsfglk ghklfrqvia ehgaelilhg hthrssihsi pgknhevpvv
      241 gvaaasaaqg gtlddparyn lfrieksgeg wtctmreygf qrlgsdivmr lqmriy
//
LOCUS       WP_284387478             416 aa            linear   BCT 25-DEC-2024
DEFINITION  cytochrome b [Devosia yakushimensis].
ACCESSION   WP_284387478
VERSION     WP_284387478.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Tolkatchev,D., Yu,L. and Yu,C.A.
  TITLE     Potential induced redox reactions in mitochondrial and bacterial
            cytochrome b-c1 complexes
  JOURNAL   J Biol Chem 271 (21), 12356-12363 (1996)
   PUBMED   8647838
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Howell,N.
  TITLE     Evolutionary conservation of protein regions in the protonmotive
            cytochrome b and their possible roles in redox catalysis
  JOURNAL   J Mol Evol 29 (2), 157-169 (1989)
   PUBMED   2509716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..416
                     /product="cytochrome b"
                     /GO_function="GO:0008121 - ubiquinol-cytochrome-c
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=46704
     Region          5..403
                     /region_name="QcrB/PetB"
                     /note="Cytochrome b subunit of the bc complex [Energy
                     production and conversion]; COG1290"
                     /db_xref="CDD:440901"
ORIGIN      
        1 msehstyvpg naaekwlder lpvvrfakeh lmdfptpknl nywwtfgail vlclgvqivt
       61 giilamhytp nvalafdsve hirrdvnggr iiqavhsvga smffaalyih ifrglffgsy
      121 kapreilwil gvvifiltma tafmgyvlpw gqmsfwgatv itnifsaipv vgesllqllr
      181 ggfavgnptl nrffslhyll pfiiaavvvl hiwalhvpgn nnpigvevkd krdtvpfhpy
      241 ytmkdlfamv lfmipfawfv ffapdilghp dnyiqansqv tpshivpewy llpfytilra
      301 vdfnvlfins qlggviamgl smlalllvpw ldtgkvrsgs frpmfkwfya lfvldfiala
      361 ylgaqeaiep yttlakvctg yyflhffvil pvlsrievak plptsisesv lgkahs
//
LOCUS       WP_284387563             254 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Devosia yakushimensis].
ACCESSION   WP_284387563
VERSION     WP_284387563.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..254
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28110
     Region          30..246
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msdpsktdny rlwfiwsgeg elvapdgqti almpgvtvim rpdgiyqarh npanrlgvtf
       61 lnyaygdgda plpplwcwta dflfvdavtr kivqlhaael agmadngtrt amllraalde
      121 lalsarqmqq asaptsrldr dvielankvl empaefddis glagqvlrsr ahftrtfgri
      181 ygvsparfvk stkllkarnl lqtstmsige isaqlgyast qyftrqyksy fattpgedrr
      241 raqanngkkq eekk
//
LOCUS       WP_284387733             199 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Algimonas
            ampicilliniresistens].
ACCESSION   WP_284387733
VERSION     WP_284387733.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..199
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=21979
     Region          1..171
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mkavyqrhae lwhtqrsral yekpwldrfi dvlspngrvl dlgcgtgdpi agyfldqgfd
       61 ivgidyaasm ieiasaqfpk aqwqigdira lpqigtfdgi yswdsffhls ipeqrailpq
      121 lsklirqdga llltvgpreg evtgtiggea vyhaslspse yeqtlkacgf qsvtyksedp
      181 dcqgrsvlfa samfpdrnc
//
LOCUS       WP_284387826             561 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Devosia yakushimensis].
ACCESSION   WP_284387826
VERSION     WP_284387826.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..561
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=61116
     Region          4..549
                     /region_name="COG4425"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:443540"
ORIGIN      
        1 mkfaralawf nrfstggiml gllffalslt psliprnfvv qgiltgcvfa agygigvfle
       61 wlwtflelsl pndvwarrik qgitlacagl vvaflwfstg wqnsiravmg vepvesiqpl
      121 wvaaiaivpa tlligigtli vqgvrlvsam lrriiprrva fvggvlvvgl vaslfvngvv
      181 irwalytadr fyaefdtiag rddpaptdpl ksgsaaslip wdtigldarv yvesgptaee
      241 isamigrpae tplrvyvglr ssetvqeraa lalaemlrvg afdrsvlvli mpvgtgwvdp
      301 paidtleilh ggdvasvalq ysyltswlsl vvepdvgtsa aqalfsavyh ywtdlpketr
      361 pklylhglsl gayasqasgt lyeiladpfd galwagppfa satwrtttan rdpstpewlp
      421 rfedgsiirf tnqgnaldip gaqwgpirlv ylqypsdpiv ffepdafyrp pewiegkrap
      481 dvspllnwyp vvtflqlald malaqtapvg fghvyapqdy fdgwvavtdp pgwtaealaa
      541 lkarltrhgd raligagwfr d
//
LOCUS       WP_284387838             147 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Algimonas ampicilliniresistens].
ACCESSION   WP_284387838
VERSION     WP_284387838.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..147
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16525
     Region          15..145
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mtgtservqp dtrddyayvl elptrwndnd vyghinnavy yeyfdtvvnr wlidndllti
       61 gvsetiglvv etacgyfapl tfpepitagl raskvgsssv ryeiglfgtg dkaaarghfv
      121 hvyvdektrr pvkisdrmke tlreitr
//
LOCUS       WP_284387956             337 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Devosia yakushimensis].
ACCESSION   WP_284387956
VERSION     WP_284387956.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..337
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36153
     Region          21..323
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 msataanaqq adaeltrlle tliraraeig rvvlgqqdii edlligliag ghvllqgppg
       61 vgktllvrtl atatglsfar vqftpdlmpa ditgsmvlvp dtdgrnhlef qrgpiftqll
      121 ladeinratp rtqsalleam qertvsaagt smplpepffv latqnplemd gtyilpeaqi
      181 drfllqldvp lptsetlsai ldsttgtdea vaeqclsdqd iiaiqalvrs vpiaehvrra
      241 iadfaiatqp aganaiddvr rylrfglspr gaqalvlask ahallngrfn vsfedvkaml
      301 lattrhrihl nfegnadgvs leallqrlfd tsikgvl
//
LOCUS       WP_284388092             519 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA synthetase [Algimonas ampicilliniresistens].
ACCESSION   WP_284388092
VERSION     WP_284388092.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..519
                     /product="acyl-CoA synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016405 - CoA-ligase activity [Evidence
                     IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0032787 - monocarboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=56947
     Region          19..507
                     /region_name="FACL_FadD13-like"
                     /note="fatty acyl-CoA synthetase, including FadD13;
                     cd17631"
                     /db_xref="CDD:341286"
     Site            order(172,175..180,182..183)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341286"
     Site            order(175,292..293,313..318,398,410,413,424,504)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341286"
     Site            order(175,215..216,265,267..268,271,292..293,313..318,398,
                     410,413,421..424,485)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341286"
     Site            order(215,267..268,271,292,421..423,479,485)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341286"
ORIGIN      
        1 meqkahshst qvidwieyha stkpdaramv dlasgriysy gqmhervara agmlkahgik
       61 pgdrvaflcl nttdimelif gcwrigaicl alnfrltppe layilndsda slvlvddpfk
      121 avaeatkphc esvehwistd gvggdsdyeq glakanpvyd fypqsydeqc llmyssgttg
      181 hpkgviithg mieftnagam rvgdarpdrv slnnmplfhi gglqvtglps lwiggccvim
      241 rlfdvdatlk aidsadlnia vlfmvpaayn amrmhpkide idfsrieial gggetvpepl
      301 thfwltkglv iqegygmtet caagttlrke diphmigsag rplshsriki vdesdnevar
      361 geageilfkg asvtpgywrk peanerafte dgwfrsgdig rmddkgyvfi edrvkdmyis
      421 ggenvypaei egilyemphf aelsvigiph ekwgetgcvv avfkeghaca iedilahleg
      481 rlarykmpsc ihiiealprg gsgkvlkyql rktvpgela
//
LOCUS       WP_284387972             276 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Algimonas
            ampicilliniresistens].
ACCESSION   WP_284387972
VERSION     WP_284387972.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 276)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..276
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29984
     Region          7..270
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mktfqifndk vcvvtgaasg igramalnla asgarlalsd inedglretl emigpsnrhm
       61 adridmadad aiaayapkvd aqlgaadyvf niagltrvgd frstsaesye kvmdvnfygv
      121 vrmskafleq liqtkgglvn issifgivgw pgqshycask fgvrgftetl smemaehgvs
      181 vscvhpggiq tnvlrnaevd hiaapgltka mmdenfdent pttaeraaei ildgtakrdq
      241 riivgsdakf mqfwnrlfpt ryrkmvmkra qriatd
//
LOCUS       WP_284388098             148 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Algimonas ampicilliniresistens].
ACCESSION   WP_284388098
VERSION     WP_284388098.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10021508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..148
                     /product="ExbD/TolR family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=16007
     Region          26..144
                     /region_name="tolR"
                     /note="TolR protein; TIGR02801"
                     /db_xref="CDD:274306"
ORIGIN      
        1 mamtakrgvg rngsrrrhrr srvsseinvt plvdvmlvll ivfmvaapll svgvpidlpk
       61 tdakalpsqq epltitvdas gkvflqeeev liedliaklv avsdtgyder iylrgdensd
      121 ygavmkvmar inaagfsnln lvtdpisq
//
LOCUS       WP_284388139             127 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Devosia
            yakushimensis].
ACCESSION   WP_284388139
VERSION     WP_284388139.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..127
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14583
     Region          27..117
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mskqiykrsg ahlpdncrpg wdilftlgdk wtgpvlgtls rdgrqrfsdi ekalpalsqr
       61 mltltlrrle rdglvqreiy pavpprveye ltergrslll avkdfaswgf knhediersr
      121 qrfdaae
//
LOCUS       WP_284388251             413 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Devosia yakushimensis].
ACCESSION   WP_284388251
VERSION     WP_284388251.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..413
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=43911
     Region          9..389
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mtgagkaldi aicgagpagl atalymhrlg hrpvilerfd aprplgsgli lqptgqavlh
       61 dlglfeaica lgapldrlhg adarsgrvvl dvryhslpgi grglgihraa lfgvlhdavl
      121 eagisirtgq svqaladlpa grravlfegd qqsepfdlvi dclgggsplk phssgpgkar
      181 alpfgaiwgt vpwqgdgfep taltqryqra svmigvlpig ravpegpela affwslkpad
      241 yealrqkgfa awkeavlghw pevrphldav edfsamtlar yahhtmampv gealafvgds
      301 ahsaspqlgq ganmalldar alhlalrdhp ddldkalahy arlrrghvrl yqalsamftp
      361 fyqsdsrmlp mvrdlfvsal akippapqll aaivagalls pikklelekp pgf
//
LOCUS       WP_284388162             264 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Devosia yakushimensis].
ACCESSION   WP_284388162
VERSION     WP_284388162.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..264
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27513
     Region          5..228
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mpnrtpstal itgassgiga ayarrlaarg ydlvlvarra drletlavel tkefgievrp
       61 viadlathag taqvaeilas dtsidmlvnn agisrlgatm dlspaalddm valnitaltr
      121 lsraalpgfv arnrgtivni gsvlaframp iasvysgtks yvllftsglq eelkdtairv
      181 qavlpagvat eiydgtilpl dqippelvmq vdamvdaala gldsgelvtl psvsdlells
      241 rytsaqadlf sasqtgrpaa rygv
//
LOCUS       WP_284388282             395 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Algimonas ampicilliniresistens].
ACCESSION   WP_284388282
VERSION     WP_284388282.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..395
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=45607
     Region          1..395
                     /region_name="CoxE2"
                     /note="Uncharacterized CoxE-like protein, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3825"
                     /db_xref="CDD:443037"
ORIGIN      
        1 mfhhffselr rasvpvsire yltllegvdk gvanesldgf yflsrtalvk derdldkfdq
       61 vfshvfrgvd ylgdifgqde htipedwlrk maelhlspee maeiealgdf dkimdalker
      121 lenqekrheg gnrnigtagr spfgaygynp egvrigqkeg rhgkavkvwd krqfknldgd
      181 reigtrnikv alrrlrkfar egaaeeldlp gtisgtakqg wldirmrper rnaikvlaff
      241 diggsmdahv mqaedlfsaa ksefkrleyf yfhnclyeqv wkdnrrrmse vtptwdilhk
      301 fpsdhrvviv gdaamspyev amrggsvehw ndepgavwlk rlvdiyphlv winptqekyw
      361 efsqstkmiq evigedrmfp mtlsglesam relar
//
LOCUS       WP_284388319             390 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Devosia yakushimensis].
ACCESSION   WP_284388319
VERSION     WP_284388319.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616068
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..390
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=42948
     Region          156..291
                     /region_name="Methyltransf_32"
                     /note="Methyltransferase domain; pfam13679"
                     /db_xref="CDD:379330"
ORIGIN      
        1 mtdrieefls avksafagnt lvklklagyh ggeadlksid vkkivakgve kfsftfhykt
       61 rdiiknqiqp ealgnlrial kdefrsaqla ttefdlsfer ngdkirlkrt evagreapst
      121 dhnraknrpl aetnkpylha lgitgkdgvv rndaqdkfrq inkmveifap liqaikaekp
      181 rivdmgagkg yldfalydyl anvakrpaei vgvemrdklv edgnataaqs gfsglnfqpg
      241 tildsdatga davialhacd tatddaiykg iaagasliav apcchkqirr qmeagkpedk
      301 lsillrhgif merqaemvtd alralyleln gyrtkvfefv sdahtpknnl ivaekdgrvg
      361 rdrdailrqi setkamfgie rhylegllgl
//
LOCUS       WP_284388356             341 aa            linear   BCT 25-DEC-2024
DEFINITION  SufB/SufD family protein [Algimonas ampicilliniresistens].
ACCESSION   WP_284388356
VERSION     WP_284388356.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Hirabayashi,K., Yuda,E., Tanaka,N., Katayama,S., Iwasaki,K.,
            Matsumoto,T., Kurisu,G., Outten,F.W., Fukuyama,K., Takahashi,Y. and
            Wada,K.
  TITLE     Functional Dynamics Revealed by the Structure of the SufBCD
            Complex, a Novel ATP-binding Cassette (ABC) Protein That Serves as
            a Scaffold for Iron-Sulfur Cluster Biogenesis
  JOURNAL   J Biol Chem 290 (50), 29717-29731 (2015)
   PUBMED   26472926
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Sendra,M., Ollagnier de Choudens,S., Lascoux,D., Sanakis,Y. and
            Fontecave,M.
  TITLE     The SUF iron-sulfur cluster biosynthetic machinery: sulfur transfer
            from the SUFS-SUFE complex to SUFA
  JOURNAL   FEBS Lett 581 (7), 1362-1368 (2007)
   PUBMED   17350000
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Fontecave,M., Choudens,S.O., Py,B. and Barras,F.
  TITLE     Mechanisms of iron-sulfur cluster assembly: the SUF machinery
  JOURNAL   J Biol Inorg Chem 10 (7), 713-721 (2005)
   PUBMED   16211402
  REMARK    Erratum:[J Biol Inorg Chem. 2006 Jan;11(1):128]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..341
                     /product="SufB/SufD family protein"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=37205
     Region          <68..340
                     /region_name="SufB"
                     /note="Fe-S cluster assembly scaffold protein SufB
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0719"
                     /db_xref="CDD:440483"
ORIGIN      
        1 mtlmydvvah lphrgleawk wsdlkstvea rkpdglsgpm rpalstldgm iigetkpaeg
       61 sdpmtkmasi lsggatkitv pdgaqfdqpl vlrdlrqgna qivieigkga slsvvehhes
      121 dagfvnldlr ytvreggsls rtlisqdgnd vvryarahvt lwdgarfnqt lltfggaftr
      181 letrlacmga vevdmsgayl ldgsrhadit hyidfaapgs tvrdtvagvv tdksrgvfqg
      241 kfhvrrpaqq tdaemrhdal mlsdkakina kpeleiyadd vecahgntig qldeqslfym
      301 rqrgipegqa rallieafia arlgenedml alvrdwlesr s
//
LOCUS       WP_284388364             125 aa            linear   BCT 25-DEC-2024
DEFINITION  HesB/IscA family protein [Algimonas ampicilliniresistens].
ACCESSION   WP_284388364
VERSION     WP_284388364.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Lu,H.M., Li,J.D., Zhang,Y.D., Lu,X.L., Xu,C., Huang,Y. and
            Gribskov,M.
  TITLE     The Evolution History of Fe-S Cluster A-Type Assembly Protein
            Reveals Multiple Gene Duplication Events and Essential Protein
            Motifs
  JOURNAL   Genome Biol Evol 12 (3), 160-173 (2020)
   PUBMED   32108236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..125
                     /product="HesB/IscA family protein"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=13557
     Region          16..119
                     /region_name="IscA"
                     /note="Fe-S cluster assembly iron-binding protein IscA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0316"
                     /db_xref="CDD:440085"
ORIGIN      
        1 mtetltktrr prpklvtlsd aaaeqvreil dergegylrv gvknggcagm eymmdyvsep
       61 erfdevvedn gvkivvdaka vlfilgavid hettllhskf vfrnpnqtda cgcgesvtiv
      121 paaad
//
LOCUS       WP_284388366             388 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Algimonas ampicilliniresistens].
ACCESSION   WP_284388366
VERSION     WP_284388366.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..388
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=42532
     Region          17..374
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 maqrhhigia gcgigglaaa cflkrqghav tvfdqfdeps pvgsglviqp vgltcleklg
       61 lleivtgrgq aiyqmqgies asrrtvlrva ygpqggdryg laihraelft alytqalalg
      121 atiigsthvt asqldgeqrt ilsdkgdihg pfdlvidasg igsnlspirt kplpygalwg
      181 tvdwpddtrl ptdrlsqcyr rahhmlgvlp lghkqqtaif wsepqnslqd wvqgdldtwk
      241 tqtirlwpef apfvdqitsh admspafyrh gtlktpytdr mafigdaahq aspqlgqgan
      301 malldaials ealnrhpipe allryaaqrr rhvrfyqmis nlftpfyqsr nsvlpmirnn
      361 vfhpasqiwp lnrgltqlvs gslvstgi
//
LOCUS       WP_284388412             962 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Algimonas ampicilliniresistens].
ACCESSION   WP_284388412
VERSION     WP_284388412.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 962)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..962
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..962
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=104559
     Region          42..467
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          518..935
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 msirsllltt taaallmacg pqavdtdank vrvttettdg dkassftldy eaftldnglq
       61 vflqrdasdp ivavstviha gssrekpgrt gfahffehma fndsenvprg wnrgqipkwg
      121 gsrnggtwsd gtiyyetvpk dafdkilwid sdrlgymint vtpealerek qvvknekrqr
      181 ydnaaygytn eviraalype dhpynwttig alpdlqaatl ddvrefydlw yapnnatlai
      241 vgdidieetk ekvklwfgei prgrdipdpv pqpvtltetk nlwyednfak lpelrmtfpt
      301 vdgsnseqya lavlgemlgg srtsplyvei vdgaklapnv ssynsssela gtftvrvran
      361 agvdlddvka avetamarfe aegidelalk rvkagqetal yaslstalgk ansmarfnel
      421 qgdpayqvks aaairavtad qvmaayerhi kdkpyiltsf vpkgqaelvv agaeratvwi
      481 eevkadvase evsagdladf ektvtvhdrs epefgelpll kmpaiwtrtl andavvrgie
      541 tneiplvqfd itlpggrwae dpaqngrfal ladlmeegta tktpgeleqa igilgasinv
      601 sagsedltir attlarnfee tvalvqeilt eprwqtedfd rvksarltgi kgreanpqai
      661 aamafnsliy gnthplgrps ggsedsvsal elddlksahs dlltatprlh vagdidpdra
      721 aaglstlaea vaptgadrpa ydiptqdnag rvffidvpgs kqsvlrigal tpasshpdfn
      781 kiqftneklg ggiagdlaqm lriekgytyg agsfiprgtv erpftmstsv ranatqasle
      841 tirdmvlayg etfdevavea tqqkiikasa rafeslgakl gtlneisqyg lsdryveeeq
      901 aelvamtdad fkriateymd esnfvyvivg dratqlepvq afaaetgkge vveldifgqp
      961 ve
//
LOCUS       WP_284388441             399 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Algimonas
            ampicilliniresistens].
ACCESSION   WP_284388441
VERSION     WP_284388441.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..399
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44225
     Region          86..364
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msrivriili laaaliaiga alffakgddi krlatvntlf dadkivdnfs nmdraflthd
       61 ltvpirddwt veeaalpttv niagtervla evldeldtta lvivrngkii hesyyrdtgp
      121 ddrriswsva ksymsglygn aladgtigsl ddevtsyvpa lkgtayegas lrnilnmssg
      181 irydedyldq ssdinkmgrt valggslddy tttlkerqfe pgsdwqyvsm dthvaawalr
      241 natgrnlhdl weetyaplgf rqqpfylvdg kdtafalggl nlttrdyakf gqlflqggew
      301 ngqqlisrew veastahsap alsdrgvgyg yqwwvpmpad qdyfavgvyg qyiyidpktn
      361 iviaknaadr efmfpdevgt hsmnknielm rslasqlgq
//
LOCUS       WP_284388496             104 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Devosia yakushimensis].
ACCESSION   WP_284388496
VERSION     WP_284388496.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 104)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 104)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..104
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11855
     Region          4..85
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msetdifkvl adptrravfe rlataemtat elregfaisq pamsqhlavl reaglvserr
       61 egryvnyrie paglaplhgw larhrafwpq ridhlkdllk emdq
//
LOCUS       WP_284388927             427 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Devosia yakushimensis].
ACCESSION   WP_284388927
VERSION     WP_284388927.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..427
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=45573
     Region          146..396
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mtrllrrrgv igplvdidla aafsvlalsg lvlnalvgsl aamaflgfgg lllisdpqqs
       61 itliarwwfl lllpaycmls tlwsqypeit lrasiqlmit lsiavvmagr vkpttlvral
      121 fvvyavgvla svtighhpag apwlgifgsk nafaahiavf altslavvvd rhaglllrls
      181 alggllisgp lmilaqsaga immvvpciav mvlllltgrl tgnqklfmtl gvivagaafg
      241 lfilangqsl lseilegsgk dptltgrtdl wataftfiae rplqgigfra fwvagfapae
      301 qlwamflvps gagfnfhnty isnaveiglv gvalqafliy ggfllivlat ilrpnpqnaf
      361 lvglqmlvil rsfievevff efsvrsilvl vtfiygatgv lqemragrqp srpmprqvhi
      421 rplgvqp
//
LOCUS       WP_284388852             390 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Algimonas ampicilliniresistens].
ACCESSION   WP_284388852
VERSION     WP_284388852.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..390
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42450
     Region          8..384
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 mltdiiyifl aaltffgvis aliffhelgh ysvarffgir verfsigfgr aiyqrkaksg
       61 tnwmisripl ggyvkfagda gaasnpdaea leaikaeegd vsdifhfrpv wqralvvlag
      121 pvanfilavi lfaivvlwve tihpealigd veegspaaaa gvqsgdriva mdgrtirdwv
      181 dmsqhiqmrs ntpietvier gservevtvt prliedkdfi ggrmtrgqfg vsispdakie
      241 rrhyspvdal vfgskqvvft isstghyigr iftgkedgek lgsigriatm vgkstvdvak
      301 aerpvseklk afalrmlqlg aaisvalgfa nlipipmldg ghlvfyayea iagkplsqkk
      361 qelgfrlgma vllalfvvlt indigyfrsl
//
LOCUS       WP_284388984             197 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Algimonas ampicilliniresistens].
ACCESSION   WP_284388984
VERSION     WP_284388984.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..197
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22041
     Region          31..190
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 msdaieqrlr gaflptpidd dthritretq rvaavllpfv qrtsgwhliy tqrpetmpnh
       61 agqisfpggk aemgetvlna alreteeeig iqadrieilg rlpsfdaagh frvtpfagiv
      121 dpaaplvidp heveeafevp ltflmdpsnh vakqltfedq mhtvyympyt epdgtirniw
      181 gmtagmtrrv wnrafng
//
LOCUS       WP_284389009             644 aa            linear   BCT 25-DEC-2024
DEFINITION  S9 family peptidase [Algimonas ampicilliniresistens].
ACCESSION   WP_284389009
VERSION     WP_284389009.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18486225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..644
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=69725
     Region          71..227
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          207..375
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          392..644
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mkkllilgts llaltsmvgc astaeigeta savmeaitpa prysaeaffm ttsyglpnss
       61 gytfgpktgd ilitadetgv fnayrmdpdt gaktaltast tsavraltwf pnderllytq
      121 dgggdelnhv fvraedgttr dltpgenvka sfggwtddet gffimtnerd gksfdiyqyd
      181 addysrilly qndglqidav sgngryvamt knrtsadsdi ylvdlstada tpelitaheg
      241 nvahsaygfs rdnrtlyyat neggeftraa syniasgarg dayradwdvn yvgespsgry
      301 miaivnadas seltltdtnt geavvlndlp dgqlrnirfn adeseiafiv ngdrspsnih
      361 vadlssgnqk altsalnpei dadqlvdgev vrfasydgld ipgilyrpkg staatpapal
      421 vwvhggpggq srlgynpaiq hlvnhgyavy ainnrgssgy gktffhlddk khgdvdlkdv
      481 vaskdfladk hwidgdrvgi iggsyggymv aaalafepev fdvginifgv tnwvrtlesi
      541 ppwweafrea lydemgdpat davrhraisp lfhaenivkp llvvqgandp rvlqvesdel
      601 veavrkngvp veyvlfpdeg hgfakrenrv sasnayvefl dehl
//
LOCUS       WP_284389143             268 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Devosia yakushimensis].
ACCESSION   WP_284389143
VERSION     WP_284389143.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..268
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29110
     Region          35..138
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 malsnpgltf gtnpagyhda rppypeatwe vlrdraglap gidiveigpg tglatghlla
       61 heprrlvave pdrrladflr eglgdrrlqv iggsfeevel ppaafdlvac atafhwldag
      121 pallrvrdll rpggavalww nvfgdtsrld pfheatehlf agersnpsag qservphald
      181 vearlaelnd agfqtdspvf mhwtlnldaa gvrrlyetfs nvlvlplter halldglvdv
      241 aerqfggrve rnmttaiyta rpvgfqag
//
LOCUS       WP_284389187             172 aa            linear   BCT 25-DEC-2024
DEFINITION  SRPBCC family protein [Algimonas ampicilliniresistens].
ACCESSION   WP_284389187
VERSION     WP_284389187.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..172
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=18903
     Region          31..161
                     /region_name="SRPBCC_CalC_Aha1-like"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of Micromonospora echinospora CalC, human Aha1, and
                     related proteins; cd07814"
                     /db_xref="CDD:176856"
     Site            order(32,41..43,45..46,51,59,67,69,71,73,84,86..87,89,92,
                     98,100..101,117..118,120,122,133,135,137,139,148..156,
                     158..160)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mklihailgl gsvlstgtta naqlrpmiye eitvdanqad vfsdwttadg ieaffapqat
       61 ieakpggmye lcfsleapkg scgnddgril aiqpdemlsf twamppympe irphlttvqi
      121 lfepvdadtt rvrlfhtgfg igedwdqgrn yfvktwpavl elyrdskais gl
//
LOCUS       WP_284389219             328 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Devosia yakushimensis].
ACCESSION   WP_284389219
VERSION     WP_284389219.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 328)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..328
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36315
     Region          17..328
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mvarqeqqla atasngnvpv aesanrllps tanfgakvrq wwpyyammap giiffvlfhy
       61 lpiweakiaf eqvriippni wvgikhfqvl ftspvfwqvl vntliisgmk mafvfpvpii
      121 valmlnevrs gslrkfiqsa vylphflswv viagvfiaal spsngvvndi tgffggqpks
      181 ymtdtgairw vlvfsemwrs agwdsllyla aiiaidqaly daaemdganr wqkilyvtip
      241 givptiatlf ilnagmflsa dlnqvinfsn dvvrsqidiv dtyvyriglq tgeyslataa
      301 glfkavlgml lillahlfsk rltgkgvw
//
LOCUS       WP_284389275             104 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsB family cell division protein [Algimonas ampicilliniresistens].
ACCESSION   WP_284389275
VERSION     WP_284389275.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..104
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=11589
     Region          28..104
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 mlrakiklpd fkrrapaaal lilylylgfh alsgsqglvr wmehterakh lqvklaalea
       61 rreslqadvd llsadsldld aldiearrsl fvakpgeiti wldp
//
LOCUS       WP_284389297             402 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Algimonas ampicilliniresistens].
ACCESSION   WP_284389297
VERSION     WP_284389297.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..402
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=46107
     Region          112..371
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mrlldammrr fvttgrltii dhkgarhdyg pggepsatvr ltdpklyrrl flnpelyage
       61 aymdgtlive dggirgflev fahnrdglrk gpvrqrikrv qktfrrtmqr nkreassknv
      121 eahydlsndl yrlfldedmq yscaywpeyg mtleqaqlak krhiaaklrl ehghrvldig
      181 cgwggmamhl akehdvqvvg vtlsndqyal arerveaagl qdrveirlqd yrdckgpydr
      241 vvsvgmfehv gvghyaeffg qirdvltddg calvhsigrk ggpgttgkwi rkyifpggys
      301 palsetyaei ekaglwvtdm eilrlhyawt laewekrfqa nrdavvamkd erfarmwefy
      361 lvisefsfly gkhmnfqiql tkdvhalppt rnymmdgpgl ls
//
LOCUS       WP_284389437             173 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Devosia
            yakushimensis].
ACCESSION   WP_284389437
VERSION     WP_284389437.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..173
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19393
     Region          2..105
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mtrdhrsgcp inltlevlgd kwsllilrdm ifggkrhfre llrsqegias nilsqrlaml
       61 veeglltkad dashkqkaiy sltgpaielv pimaqlgswg rrhqpvsael siraqlleeg
      121 gptmwdqfmd elrtehlhtp srwpaptvrq tlqagyeevv arqqagqnpp per
//
LOCUS       WP_284389521             778 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase NtrY-like [Devosia yakushimensis].
ACCESSION   WP_284389521
VERSION     WP_284389521.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 778)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 778)
  AUTHORS   Machado,H.B., Yates,M.G., Funayama,S., Rigo,L.U., Steffens,M.B.,
            Souza,E.M. and Pedrosa,F.O.
  TITLE     The ntrBC genes of Azospirillum brasilense are part of a
            nifR3-like-ntrB-ntrC operon and are negatively regulated
  JOURNAL   Can J Microbiol 41 (8), 674-684 (1995)
   PUBMED   7553451
REFERENCE   4  (residues 1 to 778)
  AUTHORS   Pawlowski,K., Klosse,U. and de Bruijn,F.J.
  TITLE     Characterization of a novel Azorhizobium caulinodans ORS571
            two-component regulatory system, NtrY/NtrX, involved in nitrogen
            fixation and metabolism
  JOURNAL   Mol Gen Genet 231 (1), 124-138 (1991)
   PUBMED   1661370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20231976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..778
                     /product="sensor histidine kinase NtrY-like"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=85635
     Region          <139..313
                     /region_name="NtrY_N"
                     /note="NtrY N-terminal region; pfam19312"
                     /db_xref="CDD:437144"
     Region          307..750
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mtetatidsq paptrrsdaa hpsrvpffaa htnrplrvlg fvvvsasvlm ssisflilsg
       61 atniepsatv wtviwivtgi lvllmialvv teavlliqar sqrqpgssmq vrmvtmfaiv
      121 aaipaaivav vatfslnqgl dqwfsertra mvessrlvar symlehaqvl rddiiwvate
      181 leqargtfee drarferilt alavtrslpf tslihgdgdt lmraqinvqg ayprlpegit
      241 qgvvegvpsa iapgstnlvg sivklrgydd tflfvarpvd aevleymrlt deniteyrqy
      301 asnrlvfqit ftimyvglav vlllaalwig ialanrfvdp irnlmiassr vsrgdldvqv
      361 pvqegrgdlr dlsngfnqmt lqlksqredl ltasemnekr rqfteavveg vsagiigldp
      421 fgavtlvnar acemlgrdei glmgerieva mpqlapiler arsarrgqvr dqiqlgnetd
      481 rrtyqvqltr egsiaeskgy vltfdditdl esaqrtsawa dvarriahei knpltpiqls
      541 aerlrrrygs kleddrdvfd kcintivrqv gdigrmvdef safarmpeaa petadlsdti
      601 rqavflesvr lpemvihtdl pdepiyawfd srlisqsltn liknaveafe nvsvssdwip
      661 titvqgqieg nharinvsdn gkgwpsenrq rllepymttr ekgtglglai vakiieqhgg
      721 ivelvdaepd stgrvgacvt ftlplqsptk tsekgsadaa ptalsqqeep lisaavhk
//
LOCUS       WP_284389490             323 aa            linear   BCT 25-DEC-2024
DEFINITION  ribose-phosphate diphosphokinase [Devosia yakushimensis].
ACCESSION   WP_284389490
VERSION     WP_284389490.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Sinha,S.C. and Smith,J.L.
  TITLE     The PRT protein family
  JOURNAL   Curr Opin Struct Biol 11 (6), 733-739 (2001)
   PUBMED   11751055
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Becker,M.A., Smith,P.R., Taylor,W., Mustafi,R. and Switzer,R.L.
  TITLE     The genetic and functional basis of purine nucleotide
            feedback-resistant phosphoribosylpyrophosphate synthetase
            superactivity
  JOURNAL   J Clin Invest 96 (5), 2133-2141 (1995)
   PUBMED   7593598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..323
                     /product="ribose-phosphate diphosphokinase"
                     /EC_number="2.7.6.1"
                     /GO_component="GO:0002189 - ribose phosphate
                     diphosphokinase complex [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004749 - ribose phosphate
                     diphosphokinase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0006015 - 5-phosphoribose 1-diphosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009156 - ribonucleoside monophosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009165 - nucleotide biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34359
     Region          1..311
                     /region_name="PrsA"
                     /note="Phosphoribosylpyrophosphate synthetase [Nucleotide
                     transport and metabolism]; COG0462"
                     /db_xref="CDD:440230"
ORIGIN      
        1 mnqiavfags shpelakdic tqlgvplhpt lvkrfsndcl evqlqancre qdvfliqtls
       61 apvqdhlvel llmldaarga sasritavip hyayarsdkk daprisiggr lvadllttag
      121 adrvltmtlh spqvhgffsv pvdhlhalse laayfqrydl snavvvspdl gnaktaaafa
      181 krlgtpvaag akerisdtkv risaiigevr grdvivldde iasggsmiel lghlrangvr
      241 siriacthgi fggnglqrla aepdlaeivc tntlpiaper mvdkltvlsv apalaeamrr
      301 insgesvssl fhdavrseqa aae
//
LOCUS       WP_284389620             694 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein [Algimonas
            ampicilliniresistens].
ACCESSION   WP_284389620
VERSION     WP_284389620.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 694)
  AUTHORS   Porat,A., Cho,S.H. and Beckwith,J.
  TITLE     The unusual transmembrane electron transporter DsbD and its
            homologues: a bacterial family of disulfide reductases
  JOURNAL   Res Microbiol 155 (8), 617-622 (2004)
   PUBMED   15380548
REFERENCE   4  (residues 1 to 694)
  AUTHORS   Kimball,R.A., Martin,L. and Saier,M.H. Jr.
  TITLE     Reversing transmembrane electron flow: the DsbD and DsbB protein
            families
  JOURNAL   J Mol Microbiol Biotechnol 5 (3), 133-149 (2003)
   PUBMED   12766342
REFERENCE   5  (residues 1 to 694)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   6  (residues 1 to 694)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   7  (residues 1 to 694)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   8  (residues 1 to 694)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   9  (residues 1 to 694)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12109673
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..694
                     /product="protein-disulfide reductase DsbD family protein"
                     /EC_number="1.8.-.-"
                     /EC_number="1.8.1.8"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=73194
     Region          44..151
                     /region_name="DsbC"
                     /note="Disulphide bond corrector protein DsbC; pfam11412"
                     /db_xref="CDD:463273"
     Region          303..692
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 mralflslfl wliattsafa ttslsvdtgr veasllsshy tvtpgqtfqi alkteldenw
       61 htywrnpgds gepvqitwil pdalsaddiv wplpdtiptg piinygfega plfpvaftva
      121 enaaigsile ieaqvyylvc ydicipedgt lrivlqvset adlndenaaa iveaigqapr
      181 eiavraamqa dgaalsiqfs dlpegdfsda yffpydktll vhsdpqvvsv gpdgiqidts
      241 asfgwqdgfs gsqsgvlafd lngertgriv svapgpaiav gavagnlpgg sgpsgapigl
      301 lgaiigafig glilnlmpcv fpvislkals laksahsera varreawaya fgifatfail
      361 vvvllaikag gaelgwgfql qnpifvglma lllfavglnl vgvfeiaggt yqgtgaglag
      421 rgglsgsfft galavlvatp caapfmatav gyallsesaf vtmlvfaala agfaapfilf
      481 ayapgllskl pkpgpwmvrl reflsfpmfa asllfvwvvg nqagvdgmgl vllamlafal
      541 avwllqrkgi wrivgvatii laialpfaar tetatgsadi atdawsperv aelraegrpv
      601 fvdftadwcv tckvnerlvl ktdsvkqafa etntafliad wtnkndviar elesygragv
      661 plylyfpasd nsvrgqvlpq iltvdmllnt lkgt
//
LOCUS       WP_284389633             436 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pseudomonas putida].
ACCESSION   WP_284389633
VERSION     WP_284389633.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 436)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 436)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 436)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..436
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48705
     Region          106..422
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mefkqslaqr iiiafalmsa lvagafafgi vatvhlveer lissvlggdl qrllrmdsvs
       61 dwshrprpdq lfyfsggrdd felpkdlrhl drgfhevfrd qlsyhamvei vdgrryvllq
      121 dqsdfeerer vlfavvvvgf vlslvlavil gwlvarrvma pvirlarqvr hrdqllglap
      181 plapdyaade vgqlavafdd tlgrlrdalt rerlftsdvs helrtplmvl atscellmen
      241 pnldararsq vervaratee mrelvktflm laraqrdega vasqatlrev adeligvwrd
      301 tieqkgltly fdgrvsaspv lynatflqsv mgnlvrnaah ytdsgyirls leangfsved
      361 sgvgipeeqr eamfkpfvrg derrgeglgl glslvqricd dqgwrvtlts tlphgcrfqv
      421 dlssttgkgd lnamae
//
LOCUS       WP_284389656             228 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Devosia yakushimensis].
ACCESSION   WP_284389656
VERSION     WP_284389656.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 228)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 228)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..228
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25706
     Region          1..>221
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msraarlldl lqalrnrtvp vsgqdlaael gisirtfyrd iatlqaqgad iqgepglgyi
       61 lrpgftlppl mfsadeieal vlgsrwvaar ssdgrlsasa qqalskitav lpadlrdrve
      121 atnllvrrss nadridaaei rlairgeykl riryrslggd lstrtiwpfl igffedariv
      181 agwcelrqdy rhfridlien ierlaerypk rravmlrewr aiytgkhl
//
LOCUS       WP_284389803             226 aa            linear   BCT 25-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Devosia yakushimensis].
ACCESSION   WP_284389803
VERSION     WP_284389803.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Niehaus,T.D., Elbadawi-Sidhu,M., de Crecy-Lagard,V., Fiehn,O. and
            Hanson,A.D.
  TITLE     Discovery of a widespread prokaryotic 5-oxoprolinase that was
            hiding in plain sight
  JOURNAL   J Biol Chem 292 (39), 16360-16367 (2017)
   PUBMED   28830929
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Fan,C., Li,Z., Yin,H. and Xiang,S.
  TITLE     Structure and function of allophanate hydrolase
  JOURNAL   J Biol Chem 288 (29), 21422-21432 (2013)
   PUBMED   23754281
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Wang,L., Grau,R., Perego,M. and Hoch,J.A.
  TITLE     A novel histidine kinase inhibitor regulating development in
            Bacillus subtilis
  JOURNAL   Genes Dev 11 (19), 2569-2579 (1997)
   PUBMED   9334321
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005226
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..226
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=23685
     Region          12..224
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 maspasrell aspilqplgd aallirfatt ltdpanraai acaqtfvrdp vpgvvevvps
       61 lvsvllrydp rraalntlmg evrlrlfgls vedvappver siparfggaa gpdvdevaqm
      121 lgmapeafva ahnattlrvl atgfapgfvy cgfhpaelll prrsvvrssv pkgsilfaag
      181 qtaiaateip tgwhvightd fanfdatamp pttlipgdrl ifeali
//
LOCUS       WP_284389887             630 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF885 domain-containing protein [Algimonas ampicilliniresistens].
ACCESSION   WP_284389887
VERSION     WP_284389887.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..630
                     /product="DUF885 domain-containing protein"
                     /calculated_mol_wt=70787
     Region          1..617
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
ORIGIN      
        1 mskllrlsat talcslapls iasaqtleas sntevrsfsc pegrvsligd ttrcalsdsl
       61 drlitdfeaa elvnnpitag ekgdrdalrs lpdvsdaart adydrlqalk rrhtalrrsp
      121 efsgfnaaqr lnyemmdfll dqrqrlipfd ssripfvnds gffnemsyvs rqtqfnrakd
      181 fedyaarltq lpryfaqhrd nmqrgiddgf tasadilpgv idvvrslsqg patehplfap
      241 flnfpdtide tersrltelg taavnisvlp aysdllkffe evyapsarvd agvgsseegr
      301 dyyralvrnf ttldlspdev hdiglaevar irtemdtvie qsgfdgsfad fldflrtdpq
      361 fyaqseqell mraawlakri dgkmpeffgt lprlsygvmk vpdeiaknyt tgrywggspd
      421 agragfyvvn tydlamrply nlpaltaheg vpghhhqial aqeledipdf rkslyatafg
      481 egwglysekl aaemglyetp yerfgqltye mwracrlvvd tgmhwkgwsr eqaeacflen
      541 salsksnirt evdryiswpg qalaykigel kilelrsrak ealgedfdir afhdavleng
      601 svplsilerq idrfiaqsrr eanearatdd
//
LOCUS       WP_284389925             370 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Devosia yakushimensis].
ACCESSION   WP_284389925
VERSION     WP_284389925.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..370
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38904
     Region          4..365
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mglvervdaa idaalvqriv gcviiinkdg qeiyaraagl adreanvplr rdaifrlasv
       61 tkpivatavl rlvdlgligl ndrvtrylpw ftpanpdgsp adirirhlln htsglayerv
      121 padasgglsg pinsltetlt niarvplafa pgtgwaygts idvlggvlaa ingsnvedal
      181 gryvtgplgm vdthfhvtdp arlstayadg tppvrmgeph vildaeghgt tfspgrifnp
      241 aapqnggagm agttddimkm leayngrpgl lapetvalal tnqigdlprr ehdagkrfsf
      301 lgavladpva annpspqgtv dwggawghnw vvdpinriti avctnttfeg cngpfrddil
      361 ravyggkdlt
//
LOCUS       WP_284389926             373 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Devosia yakushimensis].
ACCESSION   WP_284389926
VERSION     WP_284389926.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..373
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39315
     Region          5..372
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msleqlvnaa vgkaldekri vgavllvrrn geliheaayg ladreagrpm qadaifrlss
       61 ltkpivatti lamvdagmig ldnavtdylp yftprledgs tptitirhll thtaglggdi
      121 plseaekqap dfdrwhlsld enmerlasmp llfapgtgwa yspaidvlga vagrlvggtl
      181 gdavekyvtg plrmvdtafh atdrarlaaa yadgadepvl mgdphsvpsp wggvttyspg
      241 rildakayha ggggmagtar dymtlletlr tgggavlkpe tvglglanqt pqlaqsvspg
      301 wqfgffgawl adpklaespa nvgtsrwggi yghtwfidpt aglsvvsmtn tglegcdray
      361 plevrdaiya glr
//
LOCUS       WP_284389936             218 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-L-isoaspartate O-methyltransferase family protein [Devosia
            yakushimensis].
ACCESSION   WP_284389936
VERSION     WP_284389936.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Edwin,R.K., Challa,N., Sharma,R., Satyamoorthy,K., Parsa,K. and
            Misra,P.
  TITLE     PIMT/TGS1: An evolving metabolic molecular switch with conserved
            methyl transferase activity
  JOURNAL   Drug Discov Today 27 (8), 2386-2393 (2022)
   PUBMED   35462043
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Furuchi,T., Sakurako,K., Katane,M., Sekine,M. and Homma,H.
  TITLE     The role of protein L-isoaspartyl/D-aspartyl O-methyltransferase
            (PIMT) in intracellular signal transduction
  JOURNAL   Chem Biodivers 7 (6), 1337-1348 (2010)
   PUBMED   20564550
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Kagan,R.M., McFadden,H.J., McFadden,P.N., O'Connor,C. and Clarke,S.
  TITLE     Molecular phylogenetics of a protein repair methyltransferase
  JOURNAL   Comp Biochem Physiol B Biochem Mol Biol 117 (3), 379-385 (1997)
   PUBMED   9253175
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..218
                     /product="protein-L-isoaspartate O-methyltransferase
                     family protein"
                     /EC_number="2.1.1.77"
                     /GO_function="GO:0004719 - protein-L-isoaspartate
                     (D-aspartate) O-methyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0030091 - protein repair [Evidence IEA]"
                     /GO_process="GO:0036211 - protein modification process
                     [Evidence IEA]"
                     /calculated_mol_wt=22878
     Region          13..207
                     /region_name="Pcm"
                     /note="Protein-L-isoaspartate O-methyltransferase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2518"
                     /db_xref="CDD:442008"
ORIGIN      
        1 mvdyerarrf mvdnqlrtsh itdrrilaem grlpreqflp eprrplayid dvqplgpags
       61 arfmpapatf akllqladia atdrvldlga gagystavia glcqavlgle edaqlaaaat
      121 gnlaalglan aamragtaad vagqrydvim vegavdsvpe alfalleedg rlvalvrggg
      181 vavahvfvks hgsvaaraef natlpplyag prpvefvf
//
LOCUS       WP_284389978             351 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Devosia
            yakushimensis].
ACCESSION   WP_284389978
VERSION     WP_284389978.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..351
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39018
     Region          8..323
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mrtikgpavf laqfagdkpp fnsfdaicgw aanygykgvq iptwvsslid lekaatskty
       61 adeltgtaak hglaitelst hlqgqlvaah pvydtmldgf apasvhnnpk arqewavqql
      121 hwaakasknl gltehatfsg alawpflypf pqrpaglvee afdelarrwt pilnafdeng
      181 vdvgyelhpg edlfdgvtfe mfldrvknhp ranilydpsh mvlqqldyle fidiyherik
      241 lfhvkdaefn ptgrqgvysg yqswinragr frslgdgqvd fasifskmaq ydfagwavle
      301 wecaikhped garegaefik nhiihvteha fddfasagtd aaanrkilgl s
//
LOCUS       WP_284389983             252 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Devosia
            yakushimensis].
ACCESSION   WP_284389983
VERSION     WP_284389983.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..252
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27849
     Region          4..251
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtelsfqlys arnypsleef lgklaalgyt qvegfgglyg nvadattlag nlkkhgltip
       61 tghfgpaqvq dtdttvktae ilgikriycp higaegrsed eskwlelaef lakaaetytk
      121 egygfgwhnh dfefkpttsg rtpmeiilet apkieweadv awivrgkadp iawfekygdr
      181 isavhvkdia pagentdedg wadvgygtlg wdnlinqvks ktkaqyfvae hdkpsdperf
      241 atrsiatakk wk
//
LOCUS       WP_284390094             375 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Devosia yakushimensis].
ACCESSION   WP_284390094
VERSION     WP_284390094.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..375
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41812
     Region          1..281
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; cl46764"
                     /db_xref="CDD:481104"
ORIGIN      
        1 mslragrley vetirglacl llvsfhvtga dvtdglgldq whplrivnda ldnsrmpifs
       61 fisgfvlsav ivslsqwqga itskvkrlll pmvtasiify vlraaagydq qpflsiffvq
      121 yahfwflqat fvltallltl sfllkgrsdl aaiilivffv pvfifaerwd pnimsmyqgc
      181 ylapffyagh lfayylrrra qegegditpw mtmalgvvla lllainiali lsliqvprpi
      241 ehihqiilgl gsalflfllk prsrillffg pytyaiflyh vtftgttrev iqkiwpsiap
      301 eliflpaflm gvfapilvek lalkndltal fllgidlkaq rrkaarrane etqaakgtwl
      361 ppsapgekis glsgp
//
LOCUS       WP_284390132             182 aa            linear   BCT 25-DEC-2024
DEFINITION  group I truncated hemoglobin [Algimonas ampicilliniresistens].
ACCESSION   WP_284390132
VERSION     WP_284390132.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Keppner,A., Maric,D., Correia,M., Koay,T.W., Orlando,I.M.C.,
            Vinogradov,S.N. and Hoogewijs,D.
  TITLE     Lessons from the post-genomic era: Globin diversity beyond oxygen
            binding and transport
  JOURNAL   Redox Biol 37, 101687 (2020)
   PUBMED   32863222
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Bustamante,J.P., Radusky,L., Boechi,L., Estrin,D.A., Ten Have,A.
            and Marti,M.A.
  TITLE     Evolutionary and Functional Relationships in the Truncated
            Hemoglobin Family
  JOURNAL   PLoS Comput Biol 12 (1), e1004701 (2016)
   PUBMED   26788940
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Wajcman,H., Kiger,L. and Marden,M.C.
  TITLE     Structure and function evolution in the superfamily of globins
  JOURNAL   C R Biol 332 (2-3), 273-282 (2009)
   PUBMED   19281958
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Vinogradov,S.N., Hoogewijs,D., Bailly,X., Arredondo-Peter,R.,
            Guertin,M., Gough,J., Dewilde,S., Moens,L. and Vanfleteren,J.R.
  TITLE     Three globin lineages belonging to two structural classes in
            genomes from the three kingdoms of life
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11385-11389 (2005)
   PUBMED   16061809
REFERENCE   5  (residues 1 to 182)
  AUTHORS   Wittenberg,J.B., Bolognesi,M., Wittenberg,B.A. and Guertin,M.
  TITLE     Truncated hemoglobins: a new family of hemoglobins widely
            distributed in bacteria, unicellular eukaryotes, and plants
  JOURNAL   J Biol Chem 277 (2), 871-874 (2002)
   PUBMED   11696555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..182
                     /product="group I truncated hemoglobin"
                     /GO_function="GO:0005344 - oxygen carrier activity
                     [Evidence IEA]"
                     /GO_function="GO:0019825 - oxygen binding [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19993
     Region          35..145
                     /region_name="TrHb1_N"
                     /note="truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 1 (N); cd00454"
                     /db_xref="CDD:381253"
     Site            order(37,42..43,46..47,50,80..81,84,113,116,120,123,134,
                     137)
                     /site_type="other"
                     /note="apolar tunnel"
                     /db_xref="CDD:381253"
     Site            order(51,60,63..64,67,71..72,75..76,78..80,82,90,92..95,
                     98..99,102,104,108..109,112,137,140,144)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381253"
     Site            order(53,56..57,115,118,122..124)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381253"
ORIGIN      
        1 mmkpaiqall lgasltlslt lplqasdktk stlyddlggk pvmdkviadm ldlaladprm
       61 apifvdsdme rlekliiiht chiadgpcdy dgqdmrrahd glgirtlhfn tlvenlqqam
      121 ddqdipfrtq nrflarlapm hddvterspv pprttkadsy svapitrmgp dqdpetpsea
      181 sp
//
LOCUS       WP_284390140             206 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Algimonas ampicilliniresistens].
ACCESSION   WP_284390140
VERSION     WP_284390140.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..206
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22583
     Region          125..203
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mvfdlptlpa kistgqrgea rlfaeitaka fakdpfnlwv fgkpnamrpt fhveaahtyl
       61 phglchrige qaaamwmlpk tlggrstdip mrampglimi llryggigav rraaaadram
      121 kankptephl ylftigvtpd aqgqgfghql lspllraadr aglpiyless npanhdfyag
      181 hgfethkivy arpdapplet mwrypq
//
LOCUS       WP_284390186             203 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Algimonas ampicilliniresistens].
ACCESSION   WP_284390186
VERSION     WP_284390186.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..203
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=21983
     Region          9..183
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 msaqleqnrl ilasgsairr dimigagldf evivkpidea aikdamlsdg arprevadal
       61 aeakalrvsr nelglvigad qvmvmdgalf dkpasigaar drliamrgqr helvgsvvva
      121 kdgapvwryv setklwmrdf sdefledylv regdlvtksv gayrfegpga qlfsrvegdf
      181 fsilglsllp llqylrdcga iaa
//
LOCUS       WP_284390159             228 aa            linear   BCT 25-DEC-2024
DEFINITION  LolA family protein [Algimonas ampicilliniresistens].
ACCESSION   WP_284390159
VERSION     WP_284390159.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Tajima,T., Yokota,N., Matsuyama,S. and Tokuda,H.
  TITLE     Genetic analyses of the in vivo function of LolA, a periplasmic
            chaperone involved in the outer membrane localization of
            Escherichia coli lipoproteins
  JOURNAL   FEBS Lett 439 (1-2), 51-54 (1998)
   PUBMED   9849875
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..228
                     /product="LolA family protein"
                     /calculated_mol_wt=25301
     Region          2..213
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mtritkalaa lllvstapfa vsaqigvapn pvlqpaaalp afthrqtvpq dlnqinasln
       61 ntgsfqgrft qygadgsvas grvtiqrpgr vrfeydapnp llivsdgvtl vqqdraletf
      121 drvplaatpl nyflkenvrl qddtevislq klpdqwrvts rdgsgemage itlvfdpgtl
      181 alrqwvitde fggqttvqls dlqynqrvdp rlfilrdere drrdrrrr
//
LOCUS       WP_284390255             758 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Devosia yakushimensis].
ACCESSION   WP_284390255
VERSION     WP_284390255.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 758)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 758)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 758)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 758)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 758)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..758
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..758
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=84311
     Region          1..733
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mmrqyelver vqaynpnade qllnkayvya mqkhgsqkra sgdpyfnhpl evaailtelk
       61 lddasiavgl lhdtiedtda traeidqlfg seigaivdgl tkierlnlvs reeaqaenlr
      121 klllaisqdv rvllvkladr lhnmrtlqym ppekrtriaq etmdiyapla grmgmqdmrn
      181 eledisfkil qpehynaite rlnemqaeyr etististel serlaaegia arvkarvksp
      241 ysifskierk sialeqlsdm igfrvivnsi eecyhtvgvv htkwkvvpgr fkdyisvpkh
      301 ndyqsihtti vgpgrqrael qirteemdri aefgiaahal ykdgasadmg rieiesqayg
      361 slrqtighlt qglstedfve ytklelfqdq vfcftprgrl ialprgatpi dfayalhtdi
      421 gdtcvgakin gailplvtql rsgdeveiir dqnhlppanw igiaatgkar aairravrha
      481 asqrafalge hvlkmmlere gvmlddseak alaealgsps krdlliavge gkigseplaa
      541 elarikglrk rrrkldlpva dtadgwfalr atdlfrfrvp ggqrsghrak aalaqldfhm
      601 pvtisgegvv pgdrlvgilq pdapmlvypi hsdalmnlhd sdvawvdvrw nlsgkedlyp
      661 tvismesvnr pgslaqissa iaacdaninn lvmrmispdf hqmifeievr dlaqltdvla
      721 tlkrspglss vqragmreas mistlewdgs vdrrnddd
//
LOCUS       WP_284390268             269 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Algimonas
            ampicilliniresistens].
ACCESSION   WP_284390268
VERSION     WP_284390268.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..269
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29439
     Region          111..209
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mtdfscplcd caqfgmlepe gdwlaraana dderaligki vegdeslafg givrcadcgl
       61 atvqtpptpd algrfysayy asasygtkrd kkikraakrv krvrrriksg gtrfldvgsn
      121 lgyavegarl qgfeatgiei dadavlqaqa dfpggrffvt tvedfaqrge qfdfvycsev
      181 iehavdirgf adalmdliap ggvlflttpa dghratpkpl vswvqvkppe hlhwlakehl
      241 lrlfgcdgft prfqfnpkpg hklvlnrdl
//
LOCUS       WP_284390290             274 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Algimonas
            ampicilliniresistens].
ACCESSION   WP_284390290
VERSION     WP_284390290.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..274
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30323
     Region          30..231
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mrstlfnlff ysvtalyali gvlfslvpgr allmgslrry tkvirwgmrv iagitvevtg
       61 hervpadgpv ilaakhqsyg dgvimfhqfd dlsfvtgdhl ekfwlikvil akmnavvves
      121 cggaatrarm aetsrvvreq grriliypeg hlsqvgthhp ykkgiwhlqe dfgcpvvpva
      181 tnlgqrwnqt dwikhpgrah veflepippg lgkdefmdll qarietrsie lldldnpgal
      241 npadigqval nsvaqarear kasqtdahnk enaa
//
LOCUS       WP_284390383             325 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Algimonas
            ampicilliniresistens].
ACCESSION   WP_284390383
VERSION     WP_284390383.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..325
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32271
     Region          22..322
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mirrisisfs lvglalvcli aalivgpasi smsdavagll gqadsattai mrevrlprai
       61 galivgaglg asgaalqgft rndlaapgll gfsacaalga vaalyfglnr filpaaiiga
      121 ligagvisvm arrqvgaagl ilagigigal ataltgllmn lapnpwalse lvywlmgtle
      181 nvdmaglsva vpltliglva liltgpalra lalgedtaas lgvsltrvqt sivigtalci
      241 gsgvalagai gfvglfvphi mrrvtgpdps klitssalag gvfllatdti arlsagpgtp
      301 lylgivtsli gvpfflylal rrtgs
//
LOCUS       WP_284390397             379 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Algimonas ampicilliniresistens].
ACCESSION   WP_284390397
VERSION     WP_284390397.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..379
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=43084
     Region          8..356
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mtgditlrsf rnnfdsirlf gavlviwgha fvllglpast slymsvhtlg vkiffvvsgy
       61 liaqswsydp nlfrfaarrc lrifpalilc viftalvigp afttmghqey fahlqygdyf
      121 wniflkpryv lplvfadnpy ahavngslwt lpvefvayfv aptlviisrl rwiglpliva
      181 fiaawmgldi wgrdvpidir nqhivwgsew laaaqlmtyf wigsavaiyr lerflrmdva
      241 ivtfvlfami pfdraglsyw pgiilipylt ltfaliapan nwfraitdrg dysyglylya
      301 fpvqqgiial fgatflrenf llfvfmslip tslfaiiswh lveksalqlk prrpkpvetv
      361 qdsddiqesd ldrtqtvga
//
LOCUS       WP_284390401             624 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Algimonas
            ampicilliniresistens].
ACCESSION   WP_284390401
VERSION     WP_284390401.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 624)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 624)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 624)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..624
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=66586
     Region          26..592
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mkrfilstal vavitgpalf pgqvwaqvqa dvdntdlfds deiivaaarl galstaevtv
       61 aasvltetei qargqqyvsd llrslpgiav sasgsrgtlt qirvrgsean hvlviidgve
      121 manpsdggfd lsglrtqdiv kievlrgeqs alygsdaiag vinivtrage treqwrasve
      181 ggsrstaqgq asaviplgra alsingtafr tdgfdisgln gekdgstsks lnlglnalqi
      241 ggvrfdakfg qsileadfdg gsplrntsdn lrvdtttarg dlrfetgaid hkvslshlet
      301 dtendgafgl sqsvgtrsqa swaaglsrdt dtvtlvaeye retytntpnf tdpngkaene
      361 tgalaaeyrr tfgatsltas grydandlfk davtwrlgaa htfawdgrlr gsigtgvknp
      421 tlielfgffp adnfignpdl epetsigani gyvqqignfe gsvdffysel qneidgfvfn
      481 gvstvrnler esirqgiele asytldrirl tgaatfldtd qadteeqrrp eftgsatltw
      541 datdqlslsa yldhtgsqld tdfstfklve ldsftlvgar aayalgdhvt lslrgenltd
      601 adyqelvgya spgravfagl aldf
//
LOCUS       WP_284390492             266 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Algimonas
            ampicilliniresistens].
ACCESSION   WP_284390492
VERSION     WP_284390492.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..266
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29806
     Region          19..142
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mdaltrteav stsvldvlea earfgwdevs pyvkpndrcl eigagsclls amaasrvasi
       61 taleplsqtf slsepildav grqglsnmsi erttlydfep eegfdfiwsl ntfehlddwr
      121 sgvlktlsll ktggraiilc pnynipyesh fgipilgstt atrrlfgrsi aryeaehrcd
      181 glwdslnfik asevgrfarv qgidltfdrs atirmfdrfa tdrhladrha ilgplvgfvq
      241 akglhriwra lpdrfhpyma ihidrr
//
LOCUS       WP_284390671             509 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Devosia yakushimensis].
ACCESSION   WP_284390671
VERSION     WP_284390671.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 509)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 509)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 509)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..509
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55218
     Region          151..486
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mplqsavida dvrsqmgrdg krtaqktvld arqrlmsssg trasydfell hdyaqsrisa
       61 alpmaaivvi lstvaslwvp vvfttlwaaa vllgllivvm vasrfrrsdp akfnatnwtt
      121 tfiagemiyg lswsllalft lvapaetltp vmfamvlvsv aanavttntl ppatlmstlp
      181 vtltvsanlv avggtlnytl aavavcgeif fvylarqlha seletithqa ekdslinele
      241 earqmsdear rhaeqaniak sqflatmshe lrtplnaiig fsevlksell gthqvpqyke
      301 yagdihasgq hllnlinell dlsrieagky dlneeavslv diaedcrrmm elrakskgie
      361 laynvgnnlp klwgderair qvvlnllsna ikftppngkv tlvvtrsgdg gqlvsvkdng
      421 pgipedeiat vlssfgqgsl aqktaeqgag lglpivqkim elhqgrfdlf sklrfgtevi
      481 atfprarvmd alapvvekrs rleiyseag
//
LOCUS       WP_284390699             617 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Devosia yakushimensis].
ACCESSION   WP_284390699
VERSION     WP_284390699.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 617)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 617)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..617
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=66929
     Region          6..597
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 minsvllavt qasapaplry gipcllivgc iarlamwwsk rhrdltseqa qslldsttyv
       61 aillptgfsa walalfphgn gfeqahvvfy maitsiccvf clsylraaat lsglcvlvpf
      121 fgyfilsgng vlivlalnll litlallvvv agnsrdfaal vasrsetarr qdeaqnlhea
      181 nerlarldgl tglpnrhsfh relqtrleaa aaagkrlsva rldldsfksv ndifghaagd
      241 rvlqevasra rafggfiarl dndqfgligd earsetylaa wgemlceair rpfvfaevsl
      301 hvtasaglam sqpddraetl fdradyvtsv akreargsav vfsdrhekei skvramehal
      361 htadldaeiy vlfqpqfdis ldrvtgyevl arwrspvlge vspadfipma ertgivpkit
      421 qavvrkalav idqlpppmrl svnlsahdig smtaiegiva ligqsgtpcr idfeitetav
      481 mgdmqqanaa llallalgsr ialddfgtgh sslthvqklp ldrikidrsf vavvtsdats
      541 raiikttidl crnlgvscvf egieteeqle allglggsvm qgylfgrpms qemmlerqss
      601 pqpgwqasrn rmfgaga
//
LOCUS       WP_284390705             553 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Devosia yakushimensis].
ACCESSION   WP_284390705
VERSION     WP_284390705.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 553)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 553)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 553)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..553
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=58991
     Region          215..543
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrsaeqsgag aegfgigqvq sdndrragra aapfslatrf klspitaava ltslvaaslf
       61 fvydcartld dvqrelkiig aavvadiaea apdtaqlale tsvqryatvt kaslvgeaga
      121 itpalfretl pagthgtlal evaqtpaltg matrgsiafa laglltllva frrrpagmpd
      181 llqrqnyqtl agaipmgvac wtrlgelivc ndryrdrlql tgaqvryhda vkrliargnm
      241 kligedehsr vlelhgedgs clliderpld dgafmtlvsd iterkrtdtl laaireeqrh
      301 larryheekl raeaashakt nflahlshdi rtplnhiigf aelmrhqtyg plgdaryady
      361 vnsikssgeh llasfatild laeleggrke lrsepvavda lldsvvqrfr gqaqragltf
      421 alrqgcgaiv sgdrlglqrm vgnivenair ftpargritl aafaatdgvv ieitdtgigm
      481 deerlaslsq pfalgdatft rdgvgpglgi siaraiaels ggrlaidssp slgttvaisl
      541 paqlanqmle vaa
//
LOCUS       WP_284390841             451 aa            linear   BCT 25-DEC-2024
DEFINITION  T6SS phospholipase effector Tle1-like catalytic domain-containing
            protein [Algimonas ampicilliniresistens].
ACCESSION   WP_284390841
VERSION     WP_284390841.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10561933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..451
                     /product="T6SS phospholipase effector Tle1-like catalytic
                     domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50839
     Region          21..325
                     /region_name="DUF2235"
                     /note="Uncharacterized alpha/beta hydrolase domain
                     (DUF2235); pfam09994"
                     /db_xref="CDD:462937"
ORIGIN      
        1 mpkdsaksks atmvkdtpgp kniiicldgt gneieenisn vlkiyltlrs iggqpvyysq
       61 gvgtlvevrp wsrmldwfrd kllgnlfgyg ldrrvqeayr fivrhyepgd hififgysrg
      121 aymarilagm ihavgvlkpn qdnlvgaaya aylakpkrrr ptysgenvpd lldkddgeee
      181 esegkaapae etqsakavtf rrvtqaytvp vhflglfdtv asvmapgfrl gspfpltlnp
      241 yphtflnesv rrvrhaisid errqffpvsl wpadqkhrts ryvpdekase qdleevwfsg
      301 ahgdvgggni rddsglsqip lnwmmkaaie ptelkndiva elklngrmlr yvtgeepyna
      361 hteylypead saaklhpsfs gwkgvfwylf elvptvwpkv irignhsrwl rlglgsrrkl
      421 ppeatlhesv yerikqrpdy rpsnietgkg a
//
LOCUS       WP_284390874             452 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydroorotase [Devosia yakushimensis].
ACCESSION   WP_284390874
VERSION     WP_284390874.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Gojkovic,Z., Rislund,L., Andersen,B., Sandrini,M.P., Cook,P.F.,
            Schnackerz,K.D. and Piskur,J.
  TITLE     Dihydropyrimidine amidohydrolases and dihydroorotases share the
            same origin and several enzymatic properties
  JOURNAL   Nucleic Acids Res 31 (6), 1683-1692 (2003)
   PUBMED   12626710
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10784973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..452
                     /product="dihydroorotase"
                     /EC_number="3.5.2.3"
                     /GO_function="GO:0004151 - dihydroorotase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006221 - pyrimidine nucleotide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=48579
     Region          6..447
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
ORIGIN      
        1 msdfdlvlsg tvvlpstiie ngyvavrdgk ivhvgegvap saherhelgk alilpgaida
       61 qthslsqkdq edfiwstrsa aaggvttivd mpydegnlvs saeavrkkva haspqarvdf
      121 alygtikpee gasrileqve agvaafkfst fgtdpvrfpr ippalleecf aaiaptglta
      181 gvhneddeav raamakvkal gitdyrahal srppltella slqiyetgaq tgcpahvvhc
      241 slgrgyeiar syrdqgfdat ieccihyltl deehdvarlg gkakinppir prveveklwe
      301 hvragnvtlv stdhvswsen rktnpdmlan asgvpglevm vplfikgale rdisltwaak
      361 lmaenparhf rlgskgalta gkdadiavlf drpkvydaae sghnvvgwsp yngielpwtv
      421 gltylrgrqv fdgvtvgepg vgrfvrpegl sl
//
LOCUS       WP_284390916             473 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Algimonas
            ampicilliniresistens].
ACCESSION   WP_284390916
VERSION     WP_284390916.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 473)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..473
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=53447
     Region          5..470
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mtalspsivw frddlrlgdh palnaaihrg gplillyire kdaarkpgga krvwlhhslq
       61 alksdiedrg galilrtgva advidalikd sgaravfwnr ryhepdrdrd aaikealter
      121 dvavesfkan llvepwevrt kagtpykvft pfwraakdgm evsdplpapk klecvdkvls
      181 aalddwsllp tqpdwgskml nhhtpgeaga iarltdfldg piedyaqgrd rpdkaltskl
      241 sphlahgeis prqiwdackd nevtsrkfls eigwrefsyt llfynpdlat enfadgyeam
      301 ewdhddqafe awtkgqtgyp fvdagmrqlw atgwmhnrvr mvvasflikh lmidwrdged
      361 wfwdcllead lasnaaswqw vagtgadaap yfrvfnpfgq gekfdpngdy vrqwvpelkd
      421 lpnkyiqqpw tapdkvlnaa gielgrdype pivdhkqare rvleayktar nsa
//
LOCUS       WP_284390969             289 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Devosia yakushimensis].
ACCESSION   WP_284390969
VERSION     WP_284390969.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 289)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..289
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31252
     Region          1..276
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
ORIGIN      
        1 mfpqlidtrp lrraiddgln wvvrnwgdgf etaaypllml lkaiedllia tpwwlivgll
       61 taiawlasrr wqlplivlvs llfigvmelw ndamttmalm laatitaivi sipvgvsmsr
      121 sprvrqvitp vldlmqtlps fvyliptvmi fgpgkipali ativyaappl vrltdlglrs
      181 vdpavmeasr afgtnprqrl fgvqiplalp tilaginqtt mmalsmvvia smigagglgy
      241 qvlqgigrle vsrglfaglg ivalaivfdr itqsfgkqlq griglaear
//
LOCUS       WP_284390992             411 aa            linear   BCT 25-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Devosia yakushimensis].
ACCESSION   WP_284390992
VERSION     WP_284390992.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..411
                     /product="metal-dependent hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43146
     Region          6..>67
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
     Region          47..389
                     /region_name="Met_dep_hydrolase_A"
                     /note="Metallo-dependent hydrolases, subgroup A is part of
                     the superfamily of metallo-dependent hydrolases, a large
                     group of proteins that show conservation in their
                     3-dimensional fold (TIM barrel) and in details of their
                     active site. The vast majority of the...; cd01299"
                     /db_xref="CDD:238624"
     Site            order(64,66,229,249,321)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mtnsylftgg rvldaeqgvl rdgldvlvtg nriaavgtsl tapsntteia lggrtimpgl
       61 idchvhvvae tldlwanmta psslaalraa rvmnealqrg fttlrdlgga dyglvravne
      121 glipgprlvi cgkgltttgg hadlrartdd rpgifsdrlg smglivdgvd nvraacrtmi
      181 keganfikvm anggvsspnd pihsiqysre eilamveead naglyvsahv ytdkailrcv
      241 elgvhslehc nliepetakl aaekgciavp tlvaydalal egealglgat efakievvrs
      301 gglrslevmr daglpmafgs dllgqlrkyh cmefeilakv ltpaeiirsa tiigaklcrl
      361 egeagiiapg asadllving nplsdigllq gdgahmsaim srgtfaknhl n
//
LOCUS       WP_284391046             283 aa            linear   BCT 25-DEC-2024
DEFINITION  amidohydrolase family protein [Devosia yakushimensis].
ACCESSION   WP_284391046
VERSION     WP_284391046.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..283
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30461
     Region          22..280
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 msdaplclpp kplgalprlp vgacdshfhv feagaplasp rsytpqilti adwqpyaeaa
       61 giargvlvqp svygldngvm lraiardpgr lrgvavvapd isagalreld aggvrgirin
      121 trnkagvale avaellgkvg plgwsvqfqv raeqladvaa lehgevplvl dhlafirfge
      181 adtgerldal rrlldrpnic tkisapyrlt aradyadvga aitaltashp hrllwgsdwp
      241 htelwdgmpd dgdllsayeh wlpdpqlrqq ifvdtpnslf fsr
//
LOCUS       WP_284391054             463 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Devosia yakushimensis].
ACCESSION   WP_284391054
VERSION     WP_284391054.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 463)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 463)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 463)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..463
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=49612
     Region          159..449
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mkptrtslar kltrrmirvq litlalffgl gvfptvvapv vdflgdaqpl dpratmvfah
       61 slvdvedkqi nfvatpelea vrrdypsmwl yvrnqsgasa tlgevppmyr qiedelwlle
      121 svevrttdps ygsllvrteq spvgtvrvmt gggptvgvag iikrvsgila laivfvlgla
      181 saitiprivr remrglsava dqaklidina rgtrlstdgl pdevqplvka vndglarldd
      241 syakrerfla dsahelrtpi ailqtriema epfpeqaqll vdaarlasla gqlldlqrmd
      301 lgdshfeple lgdmagnvvg dlaplaiaag yelslnapdd pvmvdgdsss lsraltnviq
      361 naiayggkkg eitvdvgrdg tisvsddgpg ipiserdrvf epfyrvkpaa hgaglglnlv
      421 eaivrrhhgh itiadapsgg aciiislpvl rqaakksepv pal
//
LOCUS       WP_284391093             346 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Devosia yakushimensis].
ACCESSION   WP_284391093
VERSION     WP_284391093.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..346
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35744
     Region          32..343
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msfisrkfgg qaglgllavf slvllalaig agvgigelpi pldttyfait nrlgwtavpl
       61 drihesviwd yrlsralvaa ccgaglalcg ailqsllrnp laepyvlgvs agastgavsi
      121 ivlglgagti tlsmgafags laaflfvvll asgarggadr tilagvaasq lfnaltsyiv
      181 stsanaqqar dvmfwllgsf ggvrwpefql vlvmvilgfg iclyyarald afafgddaas
      241 slgisvgrvr iilfattalm tativsmvgs igfvglvvph aarfivgplh mrllpacvav
      301 gaifmvladi vsrvilpqqv lpigvvtali gvpffsvily rarrta
//
LOCUS       WP_284391224             210 aa            linear   BCT 25-DEC-2024
DEFINITION  ParB/RepB/Spo0J family partition protein [Algimonas
            ampicilliniresistens].
ACCESSION   WP_284391224
VERSION     WP_284391224.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..210
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23436
     Region          32..>185
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mlctaqtqip rhapvdrfql lrgrlltgnr lrdvkalqds iirfgllspi vaidraghfi
       61 vvdgrkriaa irrlafedrl prslthipyl ltdemtaaer rvpilvsnrd lfaallsqfh
      121 dgasvtemad rfcisnqcvr dilslsrldp avraaffrrv infsqaraya alpdrraqva
      181 rlrelgpfat pkqileetsp aeaeadlvaa
//
LOCUS       WP_284391243             298 aa            linear   BCT 25-DEC-2024
DEFINITION  TolB family protein [Devosia yakushimensis].
ACCESSION   WP_284391243
VERSION     WP_284391243.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..298
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=32387
     Region          11..136
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          151..292
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 mrklaenqic qvwvhdtatg enqllfetsd llleapnwsl qgdalilngn gdlwrlplaa
       61 pkleaipltg lprmnndhvl dpdgehifvs tyddwqiyra plaggaavkv sgkegpanll
      121 hflhgvspdg rqlafvgvea kisgdkmtfi saeictigtd ghgfrqitsg gapadgpeys
      181 pdgqwlyfnt etfsghaqia rmrpdgseig rltdnetvdw fphlspdglk avylayppgt
      241 sghppdlwve lrlvvgerwl eaksvarlfg gqgtinvnsw spdstrfafv aypiddvs
//
LOCUS       WP_284391320             446 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Algimonas ampicilliniresistens].
ACCESSION   WP_284391320
VERSION     WP_284391320.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 446)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..446
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48033
     Region          119..432
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mnlpedlpse dqirvrlfci aslcftvaas infigltwal glfapqhmvs ffiacsgvmf
       61 mlllkrfkdp ialtwvfaim stmggwlsay idysaatett giglayspym vailvivcll
      121 gtrraaifya glciatligf ylatvalgfa paileqnrms vvirssaill tlgimvpvsq
      181 miystlqnle caveranrae narkqllatm shevrtplng iisvsdlldk rqhdettrsy
      241 ldiigisasn lltivneslg rarsehlgde ngnaiqinsq pfdprdliqq vcnlftanas
      301 qkglwvgtyg ldalpvsllg daphlrqvln nlvgnavkft hqggvrigar lvdahrpdhv
      361 vqffvqdtgv gieddakarv ferfgqsasg lttkadgtgl glaicndlvt amggtlemds
      421 nvgvgtafyf tlvlpdagrq attfaa
//
LOCUS       WP_284391372             220 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF1223 domain-containing protein [Algimonas ampicilliniresistens].
ACCESSION   WP_284391372
VERSION     WP_284391372.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 220)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..220
                     /product="DUF1223 domain-containing protein"
                     /calculated_mol_wt=23018
     Region          1..189
                     /region_name="COG5429"
                     /note="Uncharacterized conserved protein, DUF1223 domain
                     [Function unknown]"
                     /db_xref="CDD:444181"
ORIGIN      
        1 mkstllsvla itvcaapava attsqptsvv elftsqgcss cptanafiag ldadhpdvla
       61 lsygvtywdy lgwkdtfgdp aftarqrqyd qaldsgvytp mmvvggqaha prmpidtatr
      121 anvpasialv rqsgelcveg klpkgsklal igyepgiqav nvkkgenrgh tltlanvvtd
      181 ldyrewsgqm vcglhpkagl avlahdatta aiigaarfep
//
LOCUS       WP_284391504             294 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Devosia
            yakushimensis].
ACCESSION   WP_284391504
VERSION     WP_284391504.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..294
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32301
     Region          1..251
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mktlgihsfv wtggttqqel egamekshrl gygliefprl dpskfdvawl aqrlrdynlk
       61 vvvtmglpad sdissedlds vkrgeaalnd avavtrdlgg eklggiifsa hnkyrsmptk
      121 kgwdnsvaam arvaekakas gvsmnleivn rfesnllntt aqglayieat gsdnvflhld
      181 tfhmnieenn paaaiklagk klgyfhvgen yrgylgtgti dfpaifdalv aigyddyvtf
      241 esfstkvvde dlsitcgiwr dtwvdnveva rlakvfiesr ydealrkaei grta
//
LOCUS       WP_284391464             342 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Devosia yakushimensis].
ACCESSION   WP_284391464
VERSION     WP_284391464.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..342
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36005
     Region          27..335
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 masrrwtrta laftlflaal aisivvslcv grysvsalra leilgtaimq pgrvvetmde
       61 rivllvrapr viiaamsgaa latagvalqg vfrnplvspe vlgisqgaaf ggalaitmgi
      121 wgvplllavf vagflalilv gllaridgrt eiitvilsgm vigslfsafv sllqfiadpn
      181 sslpaivywl mgsfatatwd rvlvsapgll agmgllwalr frlnvlsldd searslgahp
      241 dlerwlvfal valivgcqva vsgivgwvgl viphaarliv gydhrrllpa tavlgaafmv
      301 tidtlartvt aaeiplgvlt aivgapvfaa llrrhyrere ak
//
LOCUS       WP_284391782             379 aa            linear   BCT 25-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Algimonas
            ampicilliniresistens].
ACCESSION   WP_284391782
VERSION     WP_284391782.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Pereira,J. and Lupas,A.N.
  TITLE     The VCBS superfamily forms a third supercluster of beta-propellers
            that includes tachylectin and integrins
  JOURNAL   Bioinformatics 36 (24), 5618-5622 (2021)
   PUBMED   33416871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..379
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=39100
     Region          60..123
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          112..172
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          161..221
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          210..270
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          308..366
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mtkqgyntqt vtpsallltv mliagsataq dapsapnfra hpflqfdagd grtadialad
       61 vdgdgdldal vangrhwaqq dfvflnagsg rflearrlgd glaasyahlv adfnadghpd
      121 ivtlgdqipa mlrlndgsgq fgaalrlant dghvrsgtvl dansdgqpdi aiatrrgadv
      181 illsdglgsf sapidlpgdg kgstglatgd fngdgrtdiv varrdgsasv vmmnrgdakf
      241 gavplngsvg dhrkavvgdf ngdatpdill vstdgdhkly tetnsdgfgg plsinrdgha
      301 tqamaaadln adgrldlieg ndgtnyilln rgdgtfaphp lsddtddtyg vsvadmngdn
      361 rsdiiiansg aanrvltqr
//
LOCUS       WP_284392061             417 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Algimonas ampicilliniresistens].
ACCESSION   WP_284392061
VERSION     WP_284392061.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..417
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=44945
     Region          175..402
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mtfrslidrv atgwlllwls ffavyihmgg lafaglvill gavgwvvwlt qrqeypaltr
       61 pglvclsafl ifflwlgvsg lwsgagpeta irlagqmalf asipillrtr teqtrdtlsh
      121 ilmamslggv avlaldvasg ygintlldpi gpgeslnkrq geaemnigrg hvvyalltpl
      181 lialfatrls rgwaiaaslg fvavlltgtl lnrlavapvl ligaaplfwm gfrsprwglr
      241 lslgaacasi llaplvgvis rlmgegvmas lpmswdhrlr mwdyslaris eapllgkgld
      301 ssrnmqdaft trigvdvpfv slhphnfglq twmeagalga vlltialltl yrplrrlvgv
      361 dpwrsaavsg tlmsatiasa vtvgawqyww wglvglgltl aalipsqhrl ntnrltd
//
LOCUS       WP_284392086             306 aa            linear   BCT 25-DEC-2024
DEFINITION  cell division protein FtsX [Algimonas ampicilliniresistens].
ACCESSION   WP_284392086
VERSION     WP_284392086.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..306
                     /product="cell division protein FtsX"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=32353
     Region          55..299
                     /region_name="FtsX"
                     /note="Cell division protein FtsX [Cell cycle control,
                     cell division, chromosome partitioning]; COG2177"
                     /db_xref="CDD:441780"
ORIGIN      
        1 mieatdisap tpakmaapqt llparpeqgr alltvlvvma flaalallfa rgadrlsdrw
       61 taqlsssstv qilimteaer faqmsaaqdi liralpndar mtslsraesa rllrpwlgdt
      121 glpddlpvpg viridsevrl paesletqfe aaglrtvidd hsrfsgqlkr tvgrlvlfgi
      181 vllgliglaa tavsmfatra glaaqrdiih vlvqagatdg fiarlfvtqa arrgfigagi
      241 gaamaavlwf lislgpargs vgwrgltdga ldgvalicla ilfalicass agwaamrqla
      301 yerrra
//
LOCUS       WP_284392106             138 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Devosia yakushimensis].
ACCESSION   WP_284392106
VERSION     WP_284392106.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..138
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15052
     Region          49..137
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mdfhitddat dpaiarigde ltafnradvg psdrraiavl lrdgdavtag lsgytawgwl
       61 ytqwlwidea hrgkgiagql lvaaeaealh rgchgayidt fspvalrtyr kagyeifgvl
      121 ndfpqgrtrs flmkalra
//
LOCUS       WP_284392112             335 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Devosia yakushimensis].
ACCESSION   WP_284392112
VERSION     WP_284392112.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..335
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36567
     Region          16..334
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mpplsalkfd rafapleaai aagripggvl gvieadgtkq vrhigkaqtv pterpmteht
       61 wfdlasltkv lfttpailal adagtidlda plttvlpdlr hynpdawerk itfrqclghq
      121 tpfpavepiy tygrdpdllr tfilqrewra gpsvysdinf illgfvlerl nkkwirelda
      181 gpgfawsanp qdaaatedcy wrhrvlvgev hddncsaleg aghaglfgtv hsvldfargl
      241 ldgtgasaqs ialmrqpvrg nrthgwekpy igwsggelcs petightgft gtglwidfaa
      301 grawtlltnr vhptrhfdsg ifalrravgd aingn
//
LOCUS       WP_284392183             277 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Devosia
            yakushimensis].
ACCESSION   WP_284392183
VERSION     WP_284392183.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..277
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30128
     Region          43..271
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtsiadriav stwslhrllg svyphdlttt aigpedqryg egeesllglp samanhgyhr
       61 lelvsfhlrs rdavylgelr dqlkvsgvtl qtllidagdi shpehgardt kwiaswieta
      121 nelgaqhari iagkqkptrd aldrsvkalt aladgnagss vrlvtenwfd llaepahvhy
      181 lldkldgrig lladmgnwtg pskyadlqsi fgraelchak agfidgdlde adyglciaaa
      241 eeagykgpyt lifdseipge whglaaerdf vttrlea
//
LOCUS       WP_284392224             444 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Algimonas ampicilliniresistens].
ACCESSION   WP_284392224
VERSION     WP_284392224.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..444
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46853
     Region          20..>437
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mlsifeiaal llvlsavlsw inraylklph tigllvmall asflliglha iapglqvyet
       61 itgaigqidf netlmkgmlg fllfagalhv dfaklrdakw siglmatfgv vlstfivgtg
      121 fwllaglfnv elpyiwalvf galisptdpv avlsilktvk mpksletkia geslfndgvg
      181 vvvftlilai atggataham mdttllagpi mattpgasig vldvvelfmv davgggvlgl
      241 iagwigyqmm eridepaiei lislalvagt yaiaqridil ghhlsgpiav vvaglmignk
      301 gaafamsdkt realfgfwem ideilnsvlf lliglellvl glspsfgiit liaiplvlla
      361 rlcavyvpmk algtfktftq gaipvltwgg vrggisvala lslpdneykp liltatygiv
      421 vfsiivqglt iknvvqrtvd pkll
//
LOCUS       WP_284392225             312 aa            linear   BCT 25-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Devosia yakushimensis].
ACCESSION   WP_284392225
VERSION     WP_284392225.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Kutner,J., Shabalin,I.G., Matelska,D., Handing,K.B.,
            Gasiorowska,O., Sroka,P., Gorna,M.W., Ginalski,K., Wozniak,K. and
            Minor,W.
  TITLE     Structural, Biochemical, and Evolutionary Characterizations of
            Glyoxylate/Hydroxypyruvate Reductases Show Their Division into Two
            Distinct Subfamilies
  JOURNAL   Biochemistry 57 (6), 963-977 (2018)
   PUBMED   29309127
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10187381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..312
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=34071
     Region          2..310
                     /region_name="GDH_like_2"
                     /note="Putative glycerate dehydrogenase and related
                     proteins of the D-specific 2-hydroxy dehydrogenase family;
                     cd12164"
                     /db_xref="CDD:240641"
     Site            order(46,65..67,90,227,275)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:240641"
     Site            order(66..67,84,90,94,138..142,160..163,165,192..194,
                     198..199,225..227,251..252,275,277..278,310)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240641"
     Site            order(93,95..97,99..100,103..104,107,109,112..113,
                     115..116,120..121,123,126,129,153,249,253,256..258,260,
                     264..265,267,270,272..274,276..277,281)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240641"
ORIGIN      
        1 mlllhlsdvd easwaeklra alapypvvrq sepfdpndir yifvwkpkpd afdgldrlka
       61 vlslgagvda llkhpklpnv pvvrfvdedl sqrmsdyvva hvtmhqrlys rfradqkarr
      121 wnqlyppass qtavgimgmg vlgqdaasrl kplgfalrsw srtakaiegv egfvgpdqld
      181 aflagtdilv nllpltpett gilnyetfgk lrhgrleggp aivnaarggh qreadivral
      241 adgtlgaasl dvfeteplpa esplwdienc yvtphiaais setagvayyt riiaeheagq
      301 plinvvdrar gy
//
LOCUS       WP_284392231             450 aa            linear   BCT 25-DEC-2024
DEFINITION  leucyl aminopeptidase family protein [Devosia yakushimensis].
ACCESSION   WP_284392231
VERSION     WP_284392231.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Drinkwater,N., Malcolm,T.R. and McGowan,S.
  TITLE     M17 aminopeptidases diversify function by moderating their
            macromolecular assemblies and active site environment
  JOURNAL   Biochimie 166, 38-51 (2019)
   PUBMED   30654132
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Lowther,W.T. and Matthews,B.W.
  TITLE     Metalloaminopeptidases: common functional themes in disparate
            structural surroundings
  JOURNAL   Chem Rev 102 (12), 4581-4608 (2002)
   PUBMED   12475202
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415720
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..450
                     /product="leucyl aminopeptidase family protein"
                     /EC_number="3.4.11.-"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0030145 - manganese ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0019538 - protein metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47071
     Region          7..447
                     /region_name="PepB"
                     /note="Leucyl aminopeptidase [Amino acid transport and
                     metabolism]; COG0260"
                     /db_xref="CDD:440030"
ORIGIN      
        1 msqvqslpvi vveegrldaa slapswhawa rangfagqrg rllalpgeag avegylfgsg
       61 epaarpalil glaganlpeg dyhlegtygd pvlaavgfrl gayrfaryrk tepaprlaap
      121 aaadaaeidr lveaavlard lvntpsndlg pdafeqvird fasargisvs aivgddllaa
      181 nfpmihavgr aaaqpprlld lswgresdpk vtlvgkgvtf dtggldikta tgmllmkkdm
      241 ggaanvlgla haivsaglav rlrvlipive naiagdafrp gdvltsrkgl tveigntdae
      301 grliladala ladeespdll idmatltgaa rvalgpdlpa lystddslar dlmaaglrad
      361 dplwqmplws pydsmmsski advnnagsgg fagsitaalf mrrfvsraka wvhldimawa
      421 pearpgrpqg gtdhgiravy gllkhrypai
//
LOCUS       WP_284392254             206 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Devosia yakushimensis].
ACCESSION   WP_284392254
VERSION     WP_284392254.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..206
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23784
     Region          8..196
                     /region_name="HAD_sEH-N_like"
                     /note="N-terminal lipase phosphatase domain of human
                     soluble epoxide hydrolase, Escherichia coli YihX/HAD4
                     alpha-D-glucose 1-phosphate phosphatase, and related
                     domains, may be inactive; cd02603"
                     /db_xref="CDD:319790"
     Site            order(10..14,110..111,143,167..168,171..172)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            138
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mtdapvpvfd lggvfvewnp mylfrklfes eedalwfhqn ictldwnlef dageiysegv
       61 aklitrfpky wreiqafdlr wketlggfiq gtidihdeli eqeiptfait nfswekwvsc
      121 lgewpflekf dgvivsgleg lvkpdprlyr vfceryglap escvfiddse pnivaarkyg
      181 mhgihfkdpv mlrkelialg lplkak
//
LOCUS       WP_284392287             310 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Algimonas
            ampicilliniresistens].
ACCESSION   WP_284392287
VERSION     WP_284392287.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..310
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33823
     Region          4..>113
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
     Region          6..271
                     /region_name="BcsA"
                     /note="Glycosyltransferase, catalytic subunit of cellulose
                     synthase and poly-beta-1,6-N-acetylglucosamine synthase
                     [Cell motility]; COG1215"
                     /db_xref="CDD:440828"
ORIGIN      
        1 mtlsapliti viptfkrpkd ltrllnsida dlgqrddtai ivadndvaet arkavetfaa
       61 etgrsvdyrv apepgvsnar nvgmsgvhsr yvlfldddme vvppylepil ktsrdlgtal
      121 tfapaiaalp agtemlerwl splfsrvveg dtrvieetlg tggclvdlkg vslpspifdp
      181 alnevggedd affahiiaqg gtvgwcantk awehvpphra tpsylwrrhf afgqtptrea
      241 adrglrgwpe igkwtligga qtlihgplyl lhrllkrpsr ighfgrlaqg lgkifwwdgl
      301 sprlygskar
//
LOCUS       WP_284392435             345 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Algimonas ampicilliniresistens].
ACCESSION   WP_284392435
VERSION     WP_284392435.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..345
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37224
     Region          11..>102
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mnfdfdhqqt rdafrlglqs avaatlcyii ikwmgsddaf lavlsavliv qpsigrtvsa
       61 gwerllatlv gsaiglvclf llpngygvav alaivmfvmn fiagfrsnwr ygvvaavala
      121 ladtsgdidv aqaraiaigi givvgigvsl ivwpesaakr aarhrrqalr aaadryewal
      181 kdeedsdrse aarqkfhqsl sscrtvagaa kstqkdrlha tieaiqelyn siifldrvds
      241 plsrfdesvi trddlikagr taiealseed hdgeaddafe qaidnvddsl sgrdlqdadt
      301 kgaasvafal reisrcidni rtalaseegp sltekvpskl keimp
//
LOCUS       WP_284392446             615 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF885 domain-containing protein [Algimonas ampicilliniresistens].
ACCESSION   WP_284392446
VERSION     WP_284392446.1
KEYWORDS    RefSeq.
SOURCE      Algimonas ampicilliniresistens
  ORGANISM  Algimonas ampicilliniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae; Algimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Algimonas ampicilliniresistens"
                     /db_xref="taxon:1298735"
     Protein         1..615
                     /product="DUF885 domain-containing protein"
                     /calculated_mol_wt=70163
     Region          35..613
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
ORIGIN      
        1 msylrplavt lallaacsqa dvpattstpt pqvdaapias dqsesdrvna wfarrfeeea
       61 lnrpeylaql grkqrqgewn detkaawlnr mdraqsdldf lteevdvatl dedatlshrl
      121 yvknaqdrle gmrwygysyp fnqmrgthsg iptfllnqhn idneaeaeay iarlagipek
      181 ldpviqrsae sfdrgiappk fvyahvlrdi snilsgapfe dsedlnlild dfkkkvdlld
      241 lpdntrerlf sdaieamdda vgpayrrlet elrrqqagas dddgawklpd gadyyayrlr
      301 rmtttdlsad eihdiglrev drihgemrei mksvrfegdl qdffefmrts eqfyysnddd
      361 gkarylreat siidvmegrl devflrkpka emevraveaf reqsagkafy srpaadgsrp
      421 gyyyanlynm armptyqmea layhegipgh hmqiaiaqel egvpnfrkfg gytpysegwg
      481 lyseylpkem gfyedpysdf grlamelwra crlvvdtglh hkrwtrqeai dylaentpnp
      541 qgdivnaier yivmpgqata ymigkikile lrerskaalg dafdirdfhe vvlssgavpl
      601 dvmeervnay ieaar
//
LOCUS       WP_284392497             114 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Devosia yakushimensis].
ACCESSION   WP_284392497
VERSION     WP_284392497.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 114)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 114)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..114
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12356
     Region          9..99
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msvsvtatpt dsqiaviaet yrllgdptrl rvllaclaqp iavgdiakav aaspslvshh
       61 lrllrgarlv rgtrrnkqvf yeaadehiar mladmieham eehvaseaed erdt
//
LOCUS       WP_284392572             227 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Devosia yakushimensis].
ACCESSION   WP_284392572
VERSION     WP_284392572.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..227
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24913
     Region          12..219
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mkpqsdilrl apfqaaifdm dgtlldteav fktivfevct elgfemtdav hmamvgsshe
       61 rtnqllieay gvafpytlfd ercrvsmrer thagvpvkqg arefltelrd rkipiavats
      121 srqphahthl gaaglldlfe tvvtrddvvn pkphpepylt aarrlgidpt qclaledsha
      181 gvraahaagm qtvmvpdlvh pndelralgi svlesldhvr laaftpr
//
LOCUS       WP_284392616             420 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Devosia yakushimensis].
ACCESSION   WP_284392616
VERSION     WP_284392616.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 420)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..420
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44885
     Region          25..416
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(129,131,272,274,306..308,346)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrlksilgal alatcltapa faesisvlve gggeqlqkai aekftaetgi evnfvvvpya
       61 gvferlsaei aagssnydva tldviwmarf aefvepldel ftdtvkadia palladaqfg
      121 gayigmpawa naeilfyrtd lfedaaeqaa fkakygyela ppktwqqfrd vsvfftrdtd
      181 adgvvdlygt dvkgvnpeew matvlqagsp givlddsgav iidnaqhkaa ldfyiashct
      241 dhatppvgva qidwpaaqnl fyqgktammr fwahayrltp edslvegkvg vapmiggeag
      301 vaavpgpwyn vipkssthkd aarqfvafai annalgieap lglaatnsay qsyvgkpgfe
      361 hfeplletla apatkgrpli aqwqeivdqa vtpmlqdals cnadtgellt qakaiiedil
//
LOCUS       WP_284392639             275 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Devosia
            yakushimensis].
ACCESSION   WP_284392639
VERSION     WP_284392639.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..275
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29867
     Region          23..275
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtttpsqrpl nkvsikwnmv eepgltitdk fllladlgfd gveldapndl pmdevlnaqr
       61 rsglaipgvv nsmhwkaplt dpdpatreis iaairtaldt araygastvl vvpgvvnagt
      121 syarafelaq aglggvldra eatgvslave nvwndfllsp leaarfvdgf dhprigwyfd
      181 vgnilrygrp ahwiealgqr ilkvdvkefs ldrmnslgpw kgfdvelgdg dcdwaavnta
      241 lraagysgwa sievpggdrh rlkelkerfd riaal
//
LOCUS       WP_284392752             402 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Devosia yakushimensis].
ACCESSION   WP_284392752
VERSION     WP_284392752.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..402
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=44829
     Region          28..396
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 maqgkralsa qqvaalsdng thrvdnqlyl qireqgtrsw vfrysrngkt hwiglgrasd
       61 vplsrakela vveraklvng gspieerrav keslrlerqv qsdvptfawc ageyieghra
      121 swknqkhidq westlrmyag pvigklpvdq vtvdhvykil kpiwltkpet asrlrgriek
      181 vlgwagakky ragenparwq ggelshllpa igkvqkiehh kavphaemrg lmadlrkles
      241 isakalilli lcasrtgeii garwneidld aatwiipaer mkagaehrva lsseavkllk
      301 smertsdlvf pgprgklsnm amlqclrgir gtgetvhgfr atfstwarde tdypreliea
      361 slahavgnav eqaynrsdyl akrrslmdaw aaylagkgqr pt
//
LOCUS       WP_284392906             599 aa            linear   BCT 25-DEC-2024
DEFINITION  fructose-specific PTS transporter subunit EIIC [Acidovorax sp.
            SUPP2825].
ACCESSION   WP_284392906
VERSION     WP_284392906.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01427.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..599
                     /product="fructose-specific PTS transporter subunit EIIC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022877 -
                     protein-N(PI)-phosphohistidine-fructose phosphotransferase
                     system transporter activity [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=59891
     Region          4..87
                     /region_name="PTS_IIB_fructose"
                     /note="subunit IIB of enzyme II (EII) of the
                     fructose-specific phosphoenolpyruvate:carbohydrate
                     phosphotransferase system (PTS). In this system, EII (also
                     referred to as FruAB) is a fructose-specific permease made
                     up of two proteins (FruA and FruB) each...; cd05569"
                     /db_xref="CDD:99911"
     Site            order(10..13,15..17)
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:99911"
     Site            order(10,12..13,16..17)
                     /site_type="active"
                     /db_xref="CDD:99911"
     Site            10
                     /site_type="phosphorylation"
                     /note="phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:99911"
     Region          135..597
                     /region_name="FrwC"
                     /note="Phosphotransferase system, fructose-specific IIC
                     component [Carbohydrate transport and metabolism];
                     COG1299"
                     /db_xref="CDD:440910"
ORIGIN      
        1 mahliaiaas qagpahsfmt gealraaaer lghhialsvr sslgaqggwt ddellradav
       61 iiaadmavdr sglpaarlhe ttpgavlada advvraalar agasggavaa pgvpspaaaa
      121 vpavaaadva rplrivaits cptgvahtfm aaealeqgaq alghtikvet qgsvgaqnal
      181 tadeiaqadl iviaadtqvd rarfagkrlh atgtkaaihd aaavfaqaaa qaavwgdapa
      241 agtaatpgaa pagaavrste rtgpykhlmt gvsfmlpfvv aggllialaf alggiyvydd
      301 ahqgtlgwtl fqigakagft lmlpalagyi afsiadrpgi apgmigglla gtvgagflga
      361 iaagfiagya vhwmnrairl prtldglkpv lllpllgtlv vgvlmmmvig kpmagvmaal
      421 tewlkglqtg savllgvilg ammafdmggp vnkaayvfst tliasgvanp maatmaagmv
      481 pplgialacw vfrsrfsaee reaskavavl glafitegai pfvardplrv ipacmagaav
      541 agglsmmwni glqaphggvf vlaipnavnh vvlyalaiaa gtgvtalalg vlkrrvava
//
LOCUS       WP_284392918             690 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Acidovorax sp. SUPP2825].
ACCESSION   WP_284392918
VERSION     WP_284392918.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 690)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 690)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..690
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=76630
     Region          21..690
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mpdtssradg psqdphcsss llrlladsvp allayfesst lrcvfanqgy aestghtvea
       61 ilgktvqeai gdsawasiqp qiqqvlrger vqytrkqrvr ggpprmievn liphlhpklg
      121 lmgafvlind ithhweaera vreseermrk fsqateeaiv fhreglvtdf nealtrlmgy
      181 slaevrgrrm ldfvseefrp vteayvregr eepyevtvlh rdgravpvei vgktmpwkgs
      241 dyriavlrdi tarrqaqere aflarhdalt qlpnratlme kltaviesaq rtpqaaavlf
      301 idmdhfktvn dslgheagdm llcevarrlv qgvrpvdiva rvggdefvvv lrdaqdrpsa
      361 lavadqllad vcavfhadgt plsvsvsigv smypddgdta aelvrradaa mqqakdsgra
      421 nrqayapgme tpstgvlqhe rllrdailhg afvlhyqpqv rlddgslvgf ealvrwrhpe
      481 rdlvgpidfi afaearglit pigrwvlvea crqmrawhde glpqvpvavn lsalefrqrd
      541 vageiagvlr qtglaprfle ieltesvlmh eadqvrrtld alkalgvrvs iddfgtgyss
      601 laylkrypid klkidrsfvs dtpaneddva ivtaivqmgr slqiqtvaeg vetaaqhdll
      661 rtlgchlaqg ylisppmdpr qtrewllkkr
//
LOCUS       WP_284392924             276 aa            linear   BCT 25-DEC-2024
DEFINITION  amidohydrolase family protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284392924
VERSION     WP_284392924.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..276
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29577
     Region          22..275
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mptdadraph pdawdgagac wdahvhvfda daptqpghyr pahhplerie gvaaahgvrh
       61 lvlvqpsvyg tdnavmlral aarpgrhrgv avvdaavpda lldrmhalgv rgvrfnrvsp
      121 vgngpeafra laprlrergw hvqwyagpeh laeiaalhag tgvacvldhl aglhaelpad
      181 daawnalaal aaqgawikls gwyrlraqap ygalqetirr vadlapgrlv wgsdwphtsf
      241 aadampaydl vwqpvvealg pdragtvrqn asrlya
//
LOCUS       WP_284392964             318 aa            linear   BCT 25-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284392964
VERSION     WP_284392964.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..318
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35006
     Region          16..286
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 msetspsrfd tsfgnlrirr vagslggevl glqlsgeldd atiadltaal vrhkvlffrg
       61 qthlddtahq afgarlgktv ahptvpsptg trifeldask gggradswht dvtfidafpk
      121 ygilrgvtip ayggdtvwan taaayarlpe dlqrladglw avhsndydyg aervvveeer
      181 lnhhrkvfvs svfeaehpvv hvhpvsgera lllghfvkki agfsstesar lfeilqnrvv
      241 rlentvrwqw qqddvaiwdn ratqhfaind ygtqarvvrr vtvhgepava vdgrrsrtrv
      301 rpeatndaqi dsvitata
//
LOCUS       WP_284393056             243 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Devosia yakushimensis].
ACCESSION   WP_284393056
VERSION     WP_284393056.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..243
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25440
     Region          10..>82
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mskpstppit deiltafadg vldepqfsrv aqaiendddl aarleqlveg aalakagfap
       61 llapvpaale knvraaiara ergatwqnwl eklrlspvga tafaaviall aipslylltl
      121 rgdngpaigt legpdiaial dslpsgesrt lpngmdvtai atfidaagtt crefettgaa
      181 nylavacrta qswqtrlaia ttqdngnyrp asgmelldsy lqsigagvpl ldqdelkalq
      241 rpd
//
LOCUS       WP_284393135             517 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Acidovorax sp. SUPP2825].
ACCESSION   WP_284393135
VERSION     WP_284393135.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..517
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=55026
     Region          47..>367
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
     Region          <137..>247
                     /region_name="IucD"
                     /note="Lysine/ornithine N-monooxygenase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3486"
                     /db_xref="CDD:442709"
ORIGIN      
        1 mtiatptdst lapapaglva learlrqdlq wlglparrwv pprlteagep vldvaivggg
       61 maglalgasl ahmgvqaplf drapegfegp wattarmetl rspkeltgpa lglpaltfra
      121 wfesqfglpa waaldkiprl qwmdylrwyr rvlgldvrnr qrvlavhpra dglvridlad
      181 danggaphhv larhavlatg rdglggpwvp dwaralpagr wahsadvwdg aalrglrvav
      241 vgggasamds aataleagaa rvdllvrrae lprvnkgkga gnpgmahgfw slpdewkwrf
      301 rhylnvqqvp pphgstlrvs rhanahfhlg agvhgasvrp dgalrletak gplaadfvvf
      361 ctgfrtdwal rpefaafapa vrlwqdrfvp pageddvela aspdlgplfe fqekapgacp
      421 gldrvhcfny ggalsqgaga gdipqisdga qrlarglaar lladdaalhy aamqryeepe
      481 ldgdewtpaa fpaygpegaa paasapalse sapevtr
//
LOCUS       WP_284393201             195 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Devosia yakushimensis].
ACCESSION   WP_284393201
VERSION     WP_284393201.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..195
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21106
     Region          26..135
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 madddtlrfy aenaatyvqr qrrigthlah flaalpagat ilelgsggge daahmlsqgf
       61 dihptdaspe laaeasrhig rpvrvmrfdq ldadaqfdgv wasasllhap daelagnlaq
      121 ifralkpggl fvasfkagsg egrdqfgryy nypnaetlla ryraaaawse lelteedggg
      181 ydnlptrwlw vaarr
//
LOCUS       WP_284393240             312 aa            linear   BCT 25-DEC-2024
DEFINITION  cell division protein FtsX [Devosia yakushimensis].
ACCESSION   WP_284393240
VERSION     WP_284393240.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..312
                     /product="cell division protein FtsX"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=32553
     Region          28..308
                     /region_name="FtsX"
                     /note="Cell division protein FtsX [Cell cycle control,
                     cell division, chromosome partitioning]; COG2177"
                     /db_xref="CDD:441780"
ORIGIN      
        1 miervaslfa llrrrrgaap ivpeksvagr tlllmitims flsavtlggv vlvqksaiaw
       61 sadvgrelti qirpvegevm esnlrtavsl aqttpgvasa raltleesqk llepwlgagl
      121 dlaaievprl vvvqladpvd adiegltrnl aaikgasldt haawrqqlnt magtivlsgl
      181 mvltligvat vlaiifatrg amatnreivd vlhyigasnr fiagefqgrf lsiglqggll
      241 gaaaallffg ligtaagnml sseagaqmgv lfgrfalgvd gmigilavip viaaltaits
      301 rmtvrrylae ts
//
LOCUS       WP_284393300             284 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: AAA family ATPase [unclassified Acidovorax].
ACCESSION   WP_284393300
VERSION     WP_284393300.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..284
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32351
     Region          2..266
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mkfqgsqsyv atqdlmlavn aaitlqrpll vkgepgtgkt mlaeevsrel gmpllqwhik
       61 sttkaqqgly eydavsrlrd sqlgdadsse rvkdirnyiv qgvlwqafta dqpvallide
      121 idkadiefpn dllreidrme fycyetreli rakhrplvfi tsnnekelpd aflrrcffhy
      181 ikfpeaetmr kivdvhfptl kaellavamk tfydvrglpg lkkkpstsel idwlkllvae
      241 diplealqsa dhkvavpplv gallkneqdv glfeklvfmn qrnr
//
LOCUS       WP_284393350             381 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ATP-binding protein [unclassified Acidovorax].
ACCESSION   WP_284393350
VERSION     WP_284393350.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 381)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 381)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10543770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..381
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40958
     Region          90..232
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
     Site            95..102
                     /site_type="other"
                     /note="Walker A motif"
                     /db_xref="CDD:99707"
     Site            order(96..103,168,215)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:99707"
     Site            164..169
                     /site_type="other"
                     /note="Walker B motif"
                     /db_xref="CDD:99707"
     Site            231
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:99707"
ORIGIN      
        1 maisrktppp geaatagvpl qrppseilha aelerlraqd tdprppgwsl glraarafil
       61 gdaalgiapk ivapvasier mlvtlatgrg lmlvgepgta ksllsellaa avsgvstlti
      121 qggasttedq ikygwnyall inegpspral vpaplyqgmq qgrivrfeei traplevqdc
      181 llgmlsdrvm avpelageha mlyaregfni iatantrdrg vnemsaalkr rfdfetvfpi
      241 ldfdrelslv qdasarllaq sgiphavpap vlellvstfr dlrgapadgq rgappdaamd
      301 rlsavmstae avnvahavgv rawflerreg spadlvdcia gtivkdnadd raklrryfeq
      361 kaakrtgghw rayyearhrl p
//
LOCUS       WP_284393386             338 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284393386
VERSION     WP_284393386.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..338
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34500
     Region          7..336
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mtfpafrrrt lmlalslaga lgtataqsap galatpgwps kplriivgfp pgsspdltar
       61 tfseplaqal ghpvivenkv gaggnigada vakatdghti glfingnlti akllnpavpy
      121 dpqkdlapls lvgtsplvlt apasqpdvpa hadaraflaa arqagsrwsy gtpgvgtvgh
      181 lgtellkara giapvhvpyp gypqvatgml ggqlqmallp palalsqert gklrligvts
      241 agrstlvpgv pslaeagvpd lnleiwnafa apatmpaavq arlsaliadi arspdvrakl
      301 fqqgwqvagt spqglanriq adtalmarvi rtqgirad
//
LOCUS       WP_284393647             140 aa            linear   BCT 25-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Devosia yakushimensis].
ACCESSION   WP_284393647
VERSION     WP_284393647.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..140
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=13803
     Region          3..137
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mltinrlsls dagpllegar araeaigvpm ciavtdesgn liafermdgg kitsitiaid
       61 kaftaaaark ptheygeaaq pgsaaygins aiagrllvva gglpivvdgv vvggigissg
      121 tpgqdrevae aaiaafgsgq
//
LOCUS       WP_284393504             494 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Devosia
            yakushimensis].
ACCESSION   WP_284393504
VERSION     WP_284393504.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..494
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=53353
     Region          1..484
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mtrvlvvddd pvqlrltaei anragfkplt atggeqalai lredrnigam ildlvmpdld
       61 gmgvmeamrr erlttpviiq tanasletvi samrqgaady fvkpvsperl vislrnamkl
      121 dtleaairae harrtgtfta admiakapam grvltlcaka akstipvlie getgvgkeli
      181 ariiqgsger agrpfvtvnc gaippnlves vlfghkkgaf tgaiadqpgk faeahngtlf
      241 ldeigelppd tqvkllralq dgeiepvgas rtekvnvrvi satnrrllnl aksgefredl
      301 yyrlnvfpiy vpplrermed apalvamfia rfsaeagkrv lglspaaldl ltaydwpgnv
      361 rqlenavyra ivlsdgafle tvdfpqivaq sagrdialsd ietvpvpaap vhidtaparq
      421 rayedfspap drfldasgei aalaeieraa ivfaiehhgg rmsrvaralk igrstlyrkl
      481 heyglaedli ndaa
//
LOCUS       WP_284393756             120 aa            linear   BCT 25-DEC-2024
DEFINITION  bleomycin resistance protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284393756
VERSION     WP_284393756.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..120
                     /product="bleomycin resistance protein"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=13273
     Region          15..118
                     /region_name="BLMA_like"
                     /note="Bleomycin binding protein (BLMA) and similar
                     proteins; cd08349"
                     /db_xref="CDD:319937"
     Site            order(15..17,45,52..54,56,70..74,79..80,83,116)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319937"
     Site            order(39..40,45,56,58..59,72,98,105,107,111..113,115)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:319937"
ORIGIN      
        1 msrqpaparl vhatvpvlas ldldesaafc adrlgfaprl rtgdyliaer dgcelhfwlc
       61 terhiaents cyvrgdtral hadfaargla vdppreqpwg mrelyvidph gnllkfgesl
//
LOCUS       WP_284393831             401 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284393831
VERSION     WP_284393831.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..401
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=42315
     Region          35..374
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mqdaqplydl aplarmvllg avialgplaw vwlrnrgtsr vrrlqaltvl tlfltfdlvl
       61 fgaftrltds glgcpdwpgc ygnvsplgah aeisaaqqam ptgpvthgka wvemihryla
      121 sgvgmliivl tvgawwqrsr aarhqgpppa lspwwptatl vwvclqgafg altvtmklfp
      181 aivtlhligg lvllallcvq avrethaarg vppvalgrgl rgllvattvl lavqivlggw
      241 vstnyavlac ttfptcqgsw wpdmafgqgf eiwrplgllq dgshitfagl taihyahrla
      301 ayavllalgl lawrlhraal lpaqarwiag lalmqfatgl snvvldwplv aavlhtggaa
      361 alvvvltwal aasravgvar plaaaagtpt taptgatris a
//
LOCUS       WP_284393833             444 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Acidovorax sp. SUPP2825].
ACCESSION   WP_284393833
VERSION     WP_284393833.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..444
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47327
     Region          21..441
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 maaraclafa galclahpaw allpiqhwte psgarvwlve spaipmvdvq vdfdagarrd
       61 paaqaglasa vaamsskgvr aqgdepamde nalgeawadl gasfeaaadr dglsfslrsl
      121 tepdlldraa rlaarqlaqp sfpqdiwqre rsrwaaalke aetrpgtaaa kafgsavygt
      181 hpygqrttpd tlgrieiadm qayhgryvet crarvsivga vtrpqaqalv atllsqmpar
      241 dpatcqplpp vpevqalaap vqqdipfasa qahvligqpg farrdpdfla llvgnhilgg
      301 ggftslltse vrekrglsys vysqfspgln tgvflvglqt rpdqaaeavk vsrdvlarfv
      361 aqgpteaqlk aakdnliggf alridsnrkl lanvvniawn dlpldylehw tdrvqaltaa
      421 dvraamarkl qpdrmvtvvv ggqp
//
LOCUS       WP_284393849             289 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Devosia
            yakushimensis].
ACCESSION   WP_284393849
VERSION     WP_284393849.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..289
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33066
     Region          5..284
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mslgiglqly svrnalaadp wgtlekiaet gfkrieaanh kaktdpgvgf gvdarelrqr
       61 lddlglsmig chinpldlsi lpraldyqtt lgnaqfgcdi effppndldh vkrrcdvfnq
      121 vgqlahergm rfyyhnhfqe fqridgdfvy shiientdps lvyfeidtyw myragqdpvr
      181 wmqqlgervv llhqkdfpae taqplnlydg vfspteeitm refedrkdpl cfteigtgil
      241 piqeiidtgt rlpnaeyiil eqdhtqlpel esvrlslerf kskfsnlap
//
LOCUS       WP_284393910             432 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Devosia yakushimensis].
ACCESSION   WP_284393910
VERSION     WP_284393910.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..432
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46191
     Region          27..430
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 msatnlrdda kpdrrprkia vtprysvigg givgvctala lmekgfstrl fearspgaga
       61 ssgnagiiai asiaptgvpg larrvprmll dplsplaidw rhfpqlapwl isllrnsspe
      121 rvaqitearh allsrsiaay ddilnatgts dlrrsqpklt afesddgfrt faagqsgrls
      181 rgirvdlisg degreiepal ganvkhvarf pdvhffsdpa avvrglvdhf vrlggvvvnd
      241 eilgfegpqs kptsligkqs nylcdqvvia agpwsgalak rlgvklpiea ergyhlmlgg
      301 akgfkhavnf heryvgltpm tnglritgma efaglhakpk mrrldavlkn irqavpgigg
      361 sellrwsgdr pslpdslpai grtvraanvl facghdhlgm tmapitgklv aqlaagerpd
      421 lnltpyspdr fk
//
LOCUS       WP_284394042             244 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF1223 domain-containing protein [Devosia yakushimensis].
ACCESSION   WP_284394042
VERSION     WP_284394042.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 244)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..244
                     /product="DUF1223 domain-containing protein"
                     /calculated_mol_wt=26089
     Region          4..243
                     /region_name="COG5429"
                     /note="Uncharacterized conserved protein, DUF1223 domain
                     [Function unknown]"
                     /db_xref="CDD:444181"
ORIGIN      
        1 misrsflapv lgivafavla lpagaekvrd rpkavvelft sqgcaqcppa dalltslaee
       61 gdvialayhv dywdyvgwed tfgkadysdr qrayakswgs sriytpqmvv ngdkgvvgsr
      121 rsevhgaldt aslpldvait kqgdmlkiav ppdanysdav vwlvtyldra dvaidkgena
      181 gktmvytqvv tgrqalgmwe ndtgadlklp lpemlaentg mavivqqenn glpgpilgaa
      241 afer
//
LOCUS       WP_284394128             310 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Devosia yakushimensis].
ACCESSION   WP_284394128
VERSION     WP_284394128.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..310
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32545
     Region          40..290
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrplaslvdl agfaagnpvt varctasgii edfvtgtwpd gravvasdrf ygaslakqlt
       61 gaaaailvrd grldpdqpvt rhlsdlppwa aditprhlah hlaglpaaga leaqasgdwt
      121 edfvstalaa lprlvtppgt syaysnlgyi llarlveria gepfaafvna rllaplgiag
      181 mafvrdipay pqvahmgpcl pltqgdgglw ttsrafalwl rqqnqdalgi agiveapgql
      241 angmtapygw glglrthhtq rllihggewt gavakavrcp argiavvama ancpfqtldr
      301 lvemvlneaw
//
LOCUS       WP_284394197             128 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Devosia
            yakushimensis].
ACCESSION   WP_284394197
VERSION     WP_284394197.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..128
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14300
     Region          20..107
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msalsashea eedrlvvkpg kwtlvvvmql rsetrrfsel rrgigdisqk tltitlrele
       61 rdgfvsrtif ptipprvdye ltalgqellq ladgwrqfaa rnrvaveaar hrfdlaagep
      121 airlvsss
//
LOCUS       WP_284394266             430 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Devosia yakushimensis].
ACCESSION   WP_284394266
VERSION     WP_284394266.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..430
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46036
     Region          1..427
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 msrtdailkr lsmlhpklid lslerlnrll ddlgrpdhhm ppvihvagtn gkgstiaylr
       61 amleaagksv hvytsphlvr fnerirlagk lvstrrlnav lerveqvnag qpityfevtt
      121 aaafvlfsei kadylllevg mggtydttnv vehplgiiit pvdldhmafl gntigkiave
      181 kanimkrgsp aviarqaeeg lasinrvaar lgvvpfvgge dfdafaqdgr liyqddkgll
      241 dlpppklign hqfenagvai aairhfglpv deaamaqglg dvvwparlsp vagklrdllg
      301 pgaelwldgg hnahgtrala raledmnrar paplvlimgm mntrspaavl apfegmaeri
      361 itltipgepn ahearyiaee askagfkasa artieaalks aattpnarvv isgslylagq
      421 vllkngtfpe
//
LOCUS       WP_284394407             464 aa            linear   BCT 25-DEC-2024
DEFINITION  class II fumarate hydratase [Acidovorax sp. SUPP2825].
ACCESSION   WP_284394407
VERSION     WP_284394407.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Woods,S.A., Schwartzbach,S.D. and Guest,J.R.
  TITLE     Two biochemically distinct classes of fumarase in Escherichia coli
  JOURNAL   Biochim Biophys Acta 954 (1), 14-26 (1988)
   PUBMED   3282546
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..464
                     /product="class II fumarate hydratase"
                     /EC_number="4.2.1.2"
                     /GO_component="GO:0045239 - tricarboxylic acid cycle
                     heteromeric enzyme complex [Evidence IEA]"
                     /GO_function="GO:0004333 - fumarate hydratase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006099 - tricarboxylic acid cycle
                     [Evidence IEA]"
                     /GO_process="GO:0006106 - fumarate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48948
     Region          4..462
                     /region_name="FumC"
                     /note="Fumarate hydratase class II [Energy production and
                     conversion]; COG0114"
                     /db_xref="CDD:439884"
ORIGIN      
        1 mgaatrtehd afgpveipad rlwgaqtqra lavfdigeer fpacllhtfg lqkqaaaran
       61 rrlgaldalr adaieaaaee lrtglldahf pltiwqtgsg tqtnmnanev lanranqrlg
      121 qppgtrspvh pndhvnasqs sndsfptvmh latalelrdr lvpalallqs rlqeratafa
      181 gvlkiarthl mdavpmtlgq gfdafarqvg hgidrlhatl prlcllaqgg taagtglnap
      241 pgfdvafcee asalaglaft pnpskfegmg ahdalvevsg alnvvaasla kiandlrllg
      301 sgprcglgel ripddgltss impgkrnpti aevvaqaawq vmgnhttitl agasghfeln
      361 vakpvliynl lqsirvlads arvfserlvq gieadtdrla anvdnallla talnpvlgyd
      421 rvaritream ergitpkaaa valgvltgde ydrrvnaram agrg
//
LOCUS       WP_284394537             373 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Devosia yakushimensis].
ACCESSION   WP_284394537
VERSION     WP_284394537.1
KEYWORDS    RefSeq.
SOURCE      Devosia yakushimensis
  ORGANISM  Devosia yakushimensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Devosia yakushimensis"
                     /db_xref="taxon:470028"
     Protein         1..373
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39496
     Region          15..366
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mnadivvigg givgsaiayg larrkvrvav ldgsdrdvra ananfglvwl qgkgtnmpay
       61 qrwtrksiql wpefsaelte atgidlqyec dggltitlge adfekrrati erlaeqlgdl
      121 epdchmidrr elesvlpgvr lgsevtgasy grsdghanpl rllaalhaet vrnggellgg
      181 cavqriqrda sgsflvdygs grvsaarvvi aaglgskela aqvgldiqir pqrgqilvte
      241 rvepflplpt sglrqtregt vmigatmdea gfdtsttaea aaalgakair rvpalaglnl
      301 vrqwaglril tpdrhpvyae skshpgayva vchsgvtlaa vhaadiahaf asgqlpasln
      361 vfhhsrfdvs kaa
//
LOCUS       WP_284394620             252 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [unclassified Acidovorax].
ACCESSION   WP_284394620
VERSION     WP_284394620.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..252
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26786
     Region          1..251
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mewiivslas llagfvdaiv gggglilvpa lfatfpnapp atllgtnksa siwgtgiatw
       61 qysrrvqmrw qamlpaaaag figafagawt vtvisadslr kllplillav llytlarkdl
      121 grhhtprfeg rietrlacai glvvgfydgf fgpgtgsffv flfvrllgyd flnasvsakl
      181 lnlatnvaai ilfaakghvw whfavplava nvvgsvigth malkhgtgfv rgifivvvsa
      241 lilktgydaf lr
//
LOCUS       WP_284394766             613 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Acidovorax sp. SUPP2825].
ACCESSION   WP_284394766
VERSION     WP_284394766.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 613)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 613)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..613
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=69522
     Region          2..407
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 malsdmavrn akpngkpytl sdidglclav sptggkawhy ryywvgkqkr mslgtypevg
       61 lrearalrdg arallakgin prsdrkqkrq avrladentf kavfdkwvih rslslkegrq
      121 ttisqikrvf dndvlptlgk tpiyeiqrpd llevvakier rkalsvaekv rtwlrqlfry
      181 alivvpglqq npafdldvva mpqppvrhnp flrmaelpam lqrlrryhgk lqtqlglrll
      241 mltgvrtgel rlatpdqfhl dqglwiippe vvkqlqlemr kegkrpadip pyivplsvqa
      301 meivrhmlak fkpaqkylfc hysdlkkris entlnaalkr mgytdqltgh girgtmstal
      361 heigypkvwi daqlshtdpd qvsaaynhae yveqrrhmmq dwadrldlfe qhqveagsmr
      421 ltlhlegvpd vlhershhda rvviaptpvr lvsstpqtap tvpdtvrrls aiagpreqsa
      481 lsdaqrqrne mvdifnaphv lsaaefakma gksrrwisye isnkkilals mgnlgqrvpd
      541 whfdplkhrl iqaalkhagd adpweiyrvl sqphdlldgl apvqavtpqn fheavmavcf
      601 tlkekapnaq wsa
//
LOCUS       WP_284394812             279 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Acidovorax sp. SUPP2825].
ACCESSION   WP_284394812
VERSION     WP_284394812.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 279)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 279)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..279
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=29901
     Region          10..279
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mnlppsrapr aliaedepll aaalrqelar awpdlqiaat vgdglaavqq aldlrpdvll
       61 fdirmpgqsg leaaaelada wpvdtpfpal vfvtaydqya vqafeaqavd yllkpvqper
      121 lrkavqklqa tlarqaapaa ldfeatlarl ralvalpgaa apgvagaaah papltviqas
      181 sgaqihlvpv advvvfeaad kyvrvltatq eylirtplke laaqldantf wqvhrgtlvr
      241 asgiasavrd esgrlhlrlr erpetlavsr lyahrfkam
//
LOCUS       WP_284394829             379 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Acidovorax sp.
            SUPP2825].
ACCESSION   WP_284394829
VERSION     WP_284394829.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..379
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42992
     Region          12..371
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
ORIGIN      
        1 msdlslqlqq aasqlpvssy fdealfqrel etifqrgpry vghqlsvpda gdyyalpqeg
       61 egralvrnaq ggvelisnvc rhrqavmlkg rgtlqghgkg haggnivcpl hrwtyspggq
      121 llgaphfaqd pclnlnnygl rewngllfed ngrdigadla gmgpraelsf dgfsldrvem
      181 hecnynwktf ievyledyhv gpfhpglgnf vtcedlswef qkhysvqtvg vastfgkpgs
      241 dvyrqwhdvl lryregklpe rgaiwltyyp himvewyphv ltvstlhpvs ptktmnmvef
      301 yypeeitafe refveaqqaa ymetciedde igermdagrr alyergdnev gpyqspmedg
      361 mqhfhewyra amgdavppr
//
LOCUS       WP_284394857             272 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family oxidoreductase [Dyella lipolytica].
ACCESSION   WP_284394857
VERSION     WP_284394857.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Persson,B. and Kallberg,Y.
  TITLE     Classification and nomenclature of the superfamily of short-chain
            dehydrogenases/reductases (SDRs)
  JOURNAL   Chem Biol Interact 202 (1-3), 111-115 (2013)
   PUBMED   23200746
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   6  (residues 1 to 272)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10793067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..272
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28629
     Region          1..271
                     /region_name="PRK08278"
                     /note="SDR family oxidoreductase"
                     /db_xref="CDD:181349"
     Site            order(13,15..16,18,37..39,97..99,147..149,164,168,
                     194..197)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187535"
     Site            order(121,149,164,168)
                     /site_type="active"
                     /db_xref="CDD:187535"
ORIGIN      
        1 msnlagktlf itgasrgigl aialraardg anvviaaksg vpnpklpgti htaaaeveaa
       61 ggkalalqvd ireeaevhaa vaqaverfgg idivvnnasa iwlagtegtp mkrydlmhqv
      121 ntrgtfmvtq aclphlkkag nphvlmmapp pnldpkwfap htaytiakyg mslcvlgmsa
      181 efaplgiavn alwprtviat aaiamidgvk peqcrrpeiv adaahallvq sarqctgrfa
      241 ideevlreag ihnfdayayq igapllpdlf ln
//
LOCUS       WP_284394881             219 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-L-isoaspartate O-methyltransferase family protein [Dyella
            lipolytica].
ACCESSION   WP_284394881
VERSION     WP_284394881.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Edwin,R.K., Challa,N., Sharma,R., Satyamoorthy,K., Parsa,K. and
            Misra,P.
  TITLE     PIMT/TGS1: An evolving metabolic molecular switch with conserved
            methyl transferase activity
  JOURNAL   Drug Discov Today 27 (8), 2386-2393 (2022)
   PUBMED   35462043
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Furuchi,T., Sakurako,K., Katane,M., Sekine,M. and Homma,H.
  TITLE     The role of protein L-isoaspartyl/D-aspartyl O-methyltransferase
            (PIMT) in intracellular signal transduction
  JOURNAL   Chem Biodivers 7 (6), 1337-1348 (2010)
   PUBMED   20564550
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Kagan,R.M., McFadden,H.J., McFadden,P.N., O'Connor,C. and Clarke,S.
  TITLE     Molecular phylogenetics of a protein repair methyltransferase
  JOURNAL   Comp Biochem Physiol B Biochem Mol Biol 117 (3), 379-385 (1997)
   PUBMED   9253175
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..219
                     /product="protein-L-isoaspartate O-methyltransferase
                     family protein"
                     /EC_number="2.1.1.77"
                     /GO_function="GO:0004719 - protein-L-isoaspartate
                     (D-aspartate) O-methyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0030091 - protein repair [Evidence IEA]"
                     /GO_process="GO:0036211 - protein modification process
                     [Evidence IEA]"
                     /calculated_mol_wt=23963
     Region          14..211
                     /region_name="Pcm"
                     /note="Protein-L-isoaspartate O-methyltransferase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2518"
                     /db_xref="CDD:442008"
ORIGIN      
        1 mamnfdqarq nmvenqvrpw evldgrvlsv lgsirredfv apahrqlafa dlclpighge
       61 vmmkpimegr vlqalelkpe dhvleigtgs gfltaclasl aghvtsvdlh adftaaagqr
      121 lqaaridnvq lvtgeavngw qpqgtfdalv vtgavyripd pflgwlkpgg rllvirgesp
      181 vqqvillthe gngryreesl fetdlpylan aepprqfvf
//
LOCUS       WP_284394893             422 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Dyella lipolytica].
ACCESSION   WP_284394893
VERSION     WP_284394893.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..422
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=45813
     Region          162..406
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mnastpvlkn llrspplpfw lvvallpfgr saelgtllcf igaafalrrd skaflqgsga
       61 rlllillacy igaallsapt amaprkswtt vlallryipl glyacyamrg eqrlqrfyaa
      121 aavviaiwvf dawmqmltgw slrghaeper isglfgaddp klgptlavls plalwvarqr
      181 wglrglivas vlvlgpvmls gsraawicyg lvallfawre tgspwrfiaa ctigavllla
      241 gggiawktst rfdarmqrtl talsgneqdl nqamtgrldi wrnsvamiaa hpltgvgvrd
      301 fryaysqyap sndhfvvaen cgegvgacha hqivleilte tgfiglmlwl agvamawraw
      361 rrvgavgrts afpvtvslav mlfplnthla fysawwgllf awllglwsaa lyastkepdd
      421 ga
//
LOCUS       WP_284394936             357 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Dyella lipolytica].
ACCESSION   WP_284394936
VERSION     WP_284394936.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..357
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38587
     Region          54..171
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
     Region          209..342
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 maavpnrehv gvtakeivvr vvalltlmll gvfsaslrae tgdqhaqaaa rglvgttapr
       61 lvlktidgqt idlaslygkk avylefwatw cvpcrqqmph lkqvyeqagp dlaviavdvg
      121 fddtvqdvrn yrrdmglkmp ivfddgsige afhlrvtpqh vvigrdgril figheanakl
      181 eaallaarts tassgtlaam pseephydvg drlpdlavpt lsgeafhlps qtgknqptvl
      241 vflspwcety lagsrpalaa scravreqva alsrdthvrw lgiasglwag kddllayqkd
      301 hhltmplald asgtlfrsfr vmhvptllvv daqgrivrri egvdpqlgge lkvlasr
//
LOCUS       WP_284395095             157 aa            linear   BCT 25-DEC-2024
DEFINITION  SixA phosphatase family protein [Dyella lipolytica].
ACCESSION   WP_284395095
VERSION     WP_284395095.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..157
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16578
     Region          4..157
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mhelillrha eaqpaspggd dairrlsgrg eqearaagaw lkshgvrvdr vlcspsertc
       61 atanlalasl arvptmqvat eiynatpgel lalldqhgda ntlmlvghnp gierlvallv
      121 egrsddfrgm ppaglavlhl dgplepgnar ldafwsp
//
LOCUS       WP_284395000             491 aa            linear   BCT 25-DEC-2024
DEFINITION  rhomboid family protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284395000
VERSION     WP_284395000.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Koonin,E.V., Makarova,K.S., Rogozin,I.B., Davidovic,L.,
            Letellier,M.C. and Pellegrini,L.
  TITLE     The rhomboids: a nearly ubiquitous family of intramembrane serine
            proteases that probably evolved by multiple ancient horizontal gene
            transfers
  JOURNAL   Genome Biol 4 (3), R19 (2003)
   PUBMED   12620104
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10483871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..491
                     /product="rhomboid family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=54989
     Region          126..302
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
     Region          <412..491
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
ORIGIN      
        1 mfyaipldnr ptwrnppwmt vliivvnllv fwgpqrweak avdraaqvyl dsplpgielp
       61 pfvqwlkdtg hrdaeraqrm lathrehall rwmeheegfq krlhaglvvr addpqyadwk
      121 aararyeaal pepftrrwaq syekdapprp vtwitaaflh astghllgnm vflflfgcsv
      181 elalgrwryl afyllgavgg slmagwayag qgsyglgasg avsalmgmya vlyrlrrvrf
      241 fyqlffyfny vtapallllp awianellqh wlsgrgvaym ahlgglltga almwgagllr
      301 rkaieapppe aaaapddgfd ahvaqarqsa qamqferalv qwraaaqlrp rdvpvlsawf
      361 ktaslwpage dfhraarrif rlpgqdaatl dfqhasyrty ldharpsarl vpddmaglar
      421 rfvragqwsd aeklltalhr tapqhaalge lvgmlvtall qsgrreqama wlpqlqqlap
      481 gsaplrlleg r
//
LOCUS       WP_284395134             449 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Dyella lipolytica].
ACCESSION   WP_284395134
VERSION     WP_284395134.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 449)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 449)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..449
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=49383
     Region          145..441
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrpinflqta tfrmavlqam lfavivaalf gfvwreihey vadqllnavk vetasllgaa
       61 hagtlepqir erlevpqegd dyyllsdadg shiagnliyr pqvegwqrvp isgaygrhkg
      121 hanqvdlyvs rldggkwltv grdnrdigel dedlsrffff svgiamlfal lsggiaghif
      181 vksvdrlsar aerivagees gplrlergsa efvrlagrln rilermhalm enmrqvsndi
      241 ahdlrtpltr lrqrletaat ieqepvrqri aieqsiaevd gvlatfaall risriqarer
      301 qagfapvdls elfasmadty gpvaedtghs vsarvqpgla fkgdralltq mlsnlienai
      361 hhtpvgtrit lslintiegv igcvedsgpg iptgerqrvf qrfvrldssr tspgsglgla
      421 lvaaiadlhr ipivlfdrrp glaiemrft
//
LOCUS       WP_284395283             343 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284395283
VERSION     WP_284395283.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..343
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=35905
     Region          40..341
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 miskascaal raffsrpvsg hrvrpllaag lavlalwgtg araapaaefp dkpvrivipf
       61 pagaaadtam rvvarkmseq wrqpviidnr pgaagfqava sappdgytll mgagsgmvta
      121 pllsskltyn psrdfvpvgr vvvnvpiltt hpslqvrtvq elialarkdp galnystsgn
      181 gspghlsmel fqaatgtrmv qipykgggpa vnelaggyvq lginavpsva aqikagklvp
      241 lavasakrsr afpevptmae aglknfeydi wyalfapagt padrvqnisk vlgaalndae
      301 vtallvaqga epapttpqel arfmqedtar waklvkdrnl kld
//
LOCUS       WP_284395299             218 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: SGNH/GDSL hydrolase family protein [unclassified
            Acidovorax].
ACCESSION   WP_284395299
VERSION     WP_284395299.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..218
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=23672
     Region          18..211
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 mgdavfgpqr pcsveldgds ilfgfdpast twrhaqtpaq rilarrprwv iddrtaaglq
       61 aydlvrgyda pfdsappelf prgpqgpfdt ephpsrivvl qvgvndharp gfdieafedd
      121 yrglircvhs lghaavvtgi tpvsdkifgp aalatmqain aairrvaadt rtvhahwdsm
      181 pfsvdrdttd gihptqaasn rladrltval ertfrlga
//
LOCUS       WP_284395305             631 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Dyella lipolytica].
ACCESSION   WP_284395305
VERSION     WP_284395305.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..631
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=70521
     Region          62..531
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mrlrcgllit vllaallqgc tltraqirqa daivatsvdr qttcdradhc aipsplldaa
       61 nkaladstss epqhvvtlld dseaalvari nliraarqsi dvqtyiwded dtgqlvlnel
      121 idaarrgidv riladqlfsf edpallerla rvspnlqirl ynptfqnsrt pplefaagvl
      181 ccfmkfnqrm hnklllvdds igitggrnyq nryfnwdndf nyvdrdvmvg gpaardmass
      241 fklfwnhrrs vplirlrdvn rlirrdpapp pwpaphytdp drvadaqaea edpdwlaqhl
      301 vdtslhtgkv effsdrpakt dqptkrdaqe ftthlmhlls gaqhevvmqt pylvmsrraq
      361 kifknlrrqv pppqiivstn slastdafav yavsykrrki yltrygfdiy emkphaefad
      421 daylqanvdd edgdettpav pgmagakhkr fpgtdrrpgl fgsngrrnrp aplvssgrrf
      481 glhakslvvd dslamvgshn fdprsdhynt eagviiydqr fasqlrasim qatepqnawi
      541 iaprkptipv lgqisqaigd lsaklplfdi wpfryatsyd ikpgcgpllp tdpdfsrcya
      601 pagdfpdvdi spkllytrli iafgasgqnv l
//
LOCUS       WP_284395380             162 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Dyella lipolytica].
ACCESSION   WP_284395380
VERSION     WP_284395380.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 162)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 162)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..162
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18762
     Region          8..158
                     /region_name="NUDIX_MutT_Nudt1"
                     /note="MutT homolog-1 and similar proteins; cd18886"
                     /db_xref="CDD:467596"
ORIGIN      
        1 mpytpivatl gyvlspdrrk vlmihrnarp ddqhlgkyng lggkmepged iaecmrreir
       61 eeagiecetm hlrgtlnwpg fgkqgedwlg fifiidtfng epytqnpegt lewvdvdrim
      121 elpmwegdrh flplvfdrdp rpfhgvmpyk dgrmhswsft rl
//
LOCUS       WP_284395426             185 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Acidovorax sp. SUPP2825].
ACCESSION   WP_284395426
VERSION     WP_284395426.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..185
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=19760
     Region          1..115
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mpapqglepp sewiqrwahl vppgasvldv acgsgrhlrw lqgrghpvtg vdrdpdalat
       61 lrglgeilca dieagpwpla drtfgavvvt rylwrpllpt lvasvapggv llyetfaagn
      121 etvsrparpd fllrpgellq acaglctvay edgfldaper fvqriaavrl qegaaparhr
      181 lappl
//
LOCUS       WP_284395454             309 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Dyella lipolytica].
ACCESSION   WP_284395454
VERSION     WP_284395454.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..309
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33321
     Region          3..296
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mqpvskarlq ihfcvllwgf tailgklitl palqlvwwrt llvagallli prvwrglram
       61 tmrlrlayag igvlvslhwl tfyasiklan asvgatcial gpvflafiep wvarrrfdpr
      121 elliavavvp gvamvvggvp agmrigiavg vlsalfvalf gsfnkrlveh gdpltvtcie
      181 lgtgamfltv mgplmphtgp afqvphvhda vlllalafgc tllpftlalv alrhisafat
      241 qmitnlepvy aivlailllg eqrqldawfy agvvvilmav fahpllhrgd rqpaqaellg
      301 taeshnivd
//
LOCUS       WP_284395620             144 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Dyella lipolytica].
ACCESSION   WP_284395620
VERSION     WP_284395620.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..144
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15999
     Region          16..140
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mtivstdsqr davslytasi svrwrdldaf nhvnnsnylt fleesrlqwl qqipgpwfte
       61 qampvmaase lnyrrpiawp sqlhvelfca rlgnssitia hrivdaadse llycdghvvl
      121 vwmdpatgks vplpqavrda geaa
//
LOCUS       WP_284395712             143 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Dyella lipolytica].
ACCESSION   WP_284395712
VERSION     WP_284395712.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..143
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=15483
     Region          1..139
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mrigndrrsd dfeinvvsli dvlltllmff vltttfvqhs rlkvelpqas aedrdmqppv
       61 itvmvdrdgh fyvgsdevtg agvdplkeai arvagddrnq tvtiradamt ahqnvvtamd
      121 algqlgfthl siattptqse agq
//
LOCUS       WP_284395743             313 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Dyella lipolytica].
ACCESSION   WP_284395743
VERSION     WP_284395743.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..313
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33816
     Region          17..302
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 msaitplrde nlqqrlhaai aqvnrvllgk arqvklaftc liagghllle dvpgvgkttl
       61 ahalaasfal dfqrvqftsd llpsdiigvs myeretgqfr fhpgpvfagl lladeinrat
      121 pktqsallea maerqvtvdg qthalpepff vvatqnpldl agtfplpdsq ldrfmlrvsl
      181 dypdasaere lltgsdrrdl ltrltpqlda asltalyrqi qtitaspall dylqalltas
      241 rrhpdirvgl spraglslla aarawamlsd rghvlpediq alfvplaahr lvaargasge
      301 tlartllsev avd
//
LOCUS       WP_284395790             129 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Pseudomonas putida].
ACCESSION   WP_284395790
VERSION     WP_284395790.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..129
                     /product="YybH family protein"
                     /calculated_mol_wt=14303
     Region          20..126
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mdqplqvrqa aanlvaafas ndtaryfacf sedatflfht lpqpllsrra yedlwaqwqa
       61 egfavlaces gnahvslqgd vaifmhdvat hiriageehq lseretivfr hqgdqwlach
      121 ehlsvvspa
//
LOCUS       WP_284394921             610 aa            linear   BCT 25-DEC-2024
DEFINITION  LTA synthase family protein [Dyella lipolytica].
ACCESSION   WP_284394921
VERSION     WP_284394921.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..610
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=65795
     Region          3..535
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mavafvlltg lldgndgvaa sqllaqptfp lanampgvml allilaltrr tflsfglayl
       61 vqammygvna lkvanlgtpl lpadfrmvgq lrkggmhvlg sylphspwpy lamlagaali
      121 aamwryeppl fasrtggkrl vsgsvlaatl atlligvpgw rnvynghklw lepwsaaatt
      181 shsglvsslv mfhlqdrrtq qkadpaavgk llqttgnavr armyapvdqg talpdivvvq
      241 sesffdpsiv rgyenahltp nlarlaaggm sgplhvptyg ggtirtefev ltglslryfn
      301 nmqfpylqln dkvvpsmvrt lrahgyetva ihgndptfwn rntaftalgf drfvsqsgfp
      361 anaamdgkym adsamtdeim sqlkdagapq flfaisleah gpydvppkds vardaipvps
      421 avdakdkvev qnyiyhmqha deelgrlaal lakrsrptll lfygdhlpgl tdayrttgfv
      481 ddqnmlgqpg twllidprnp gnpqridmas wmlpglller agihddayya ltqvlapsla
      541 kltrapgatp ppidaqqqqf dsdmasvavl rmkgkldrll pasllptnta vakrddaeav
      601 pagaamgmhr
//
LOCUS       WP_284395875             233 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Dyella
            lipolytica].
ACCESSION   WP_284395875
VERSION     WP_284395875.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 233)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..233
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=24913
     Region          2..233
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 miefghgthv glrrtrnedt ycadatlglf lvtdgmgghq hgevasalar daivervrgg
       61 lslveavhga aaqllehaqr yddalpmgtt vaairfseqg yevawvgdsr iyqwhnglrr
      121 ishdhslvqe lvasgvinea qaarhpqrnv ltqalgital aqlhismakg qlepgmsflv
      181 csdglteevs dnaianivdr qdlaaqecid hlllaaldgg gsdnitaila rir
//
LOCUS       WP_284395940             233 aa            linear   BCT 25-DEC-2024
DEFINITION  acid phosphatase [Dyella lipolytica].
ACCESSION   WP_284395940
VERSION     WP_284395940.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130290
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..233
                     /product="acid phosphatase"
                     /EC_number="3.1.3.2"
                     /GO_function="GO:0003993 - acid phosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=25129
     Region          34..222
                     /region_name="PAP2_acid_phosphatase"
                     /note="PAP2, bacterial acid phosphatase or class A
                     non-specific acid phosphatases. These enzymes catalyze
                     phosphomonoester hydrolysis, with optimal activity in low
                     pH conditions. They are secreted into the periplasmic
                     space, and their physiological role remains...; cd03397"
                     /db_xref="CDD:239491"
     Site            order(114,121,144..146,179,185,189)
                     /site_type="active"
                     /db_xref="CDD:239491"
ORIGIN      
        1 mkrsallllm lligqtalad ddgakpaive lsnllppppa agsiaaqhdl qivlstqrtr
       61 taadmlaaka dtersvfrfa dvlgsalqpt dlpktaaffa rtaefdkeav keaksywlrp
      121 rpavvstqvh plakekandw sypsghatfg yttavllanm vpekrsaifa radlyaqhri
      181 vmgahfpsdv eaghlagtvi aadimqdpsw kqdyeaarle lrhalgltan plh
//
LOCUS       WP_284395976              74 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Dyella lipolytica].
ACCESSION   WP_284395976
VERSION     WP_284395976.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 74)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..74
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=7892
     Region          3..>64
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 msqipetgyl rlpqivgkpa tdsapgipal ipvskstwwa girsgrypkp vklgeritaw
       61 kvediralia raaa
//
LOCUS       WP_284396037             271 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Dyella lipolytica].
ACCESSION   WP_284396037
VERSION     WP_284396037.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..271
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29256
     Region          1..260
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtqarplsli tgasagigaa fahalaargh dvvltarrtd rletlaadlq aahgvnatvl
       61 tsdladphav eklcqtldqr glkvdwlinn agygvpgrfd qsdwtvhadf lrvlvtapte
      121 lawrliggmr ergygrivnv aslaghvpgs aghtlyaask aymikfsqsl aleneatgvn
      181 vcalcpgftr sefhdvtgtr plvnkmpdfm wqsaeqvvqe giaavergda vyvtgrfnrt
      241 vksvfklmpd klalrmsakq srryraqdss h
//
LOCUS       WP_284396057             318 aa            linear   BCT 25-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Dyella lipolytica].
ACCESSION   WP_284396057
VERSION     WP_284396057.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..318
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35650
     Region          4..308
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msvmknfali gaagyiaprh mqaikatgnk llaaldpnds vgiidshfpd adffteferf
       61 drhvdmrrra rnggqidyvs icspnylhds hmrfalrsga saicekplvl npwnidglse
      121 ieretgrkin tilqlrlhpa iialrdrvrg eqgghkhevd ltyvtsrghw ylqswkgdtk
      181 ksggiatnig vhffdmlhyi fgtlqintvh lssdtkaagy leyenarvrw flsvdiedvp
      241 aaqresgqrt yrsitvdgee iefsggftdl hnrsyeeila grgfsleenr taietvaair
      301 tgkvvsfand ghpflnkk
//
LOCUS       WP_284396198             712 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Acidovorax sp. SUPP2825].
ACCESSION   WP_284396198
VERSION     WP_284396198.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 712)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 712)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..712
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=75787
     Region          68..712
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mhptiarpva lgmalawlal aataqtptpa dpaaerspal pavtvtapat paaqrssrla
       61 tgtagssldt pfsvttvpae lvrqqggttl qdalrnvpga qadsgfngsh tqffilrgav
      121 tdsgtgsnrv lrdgvrlsny pytpafvesv dvlrgpgaal gvrsepggtv nlvtrqpqla
      181 nfgsaslgag ahgaleasid lnrvlsaene laarvtatrs qasqwrhved rldgiklgla
      241 qsdgnryhlr anveatnqty qpdyglpalg grpvavprdr qlgepfgdst tnnriydlhg
      301 dvalsahtrw sadfthleah stsiknllng splagqpagt yarvsawepg terridsfst
      361 alsstqgtga vthqlyfgad yykevlnqpa lsvpastspa invfdpvygr vtappagavl
      421 aqslttqdle svsasaqdqi dfgawsvvag lrftrqrfly gtagvlpvee srwnpklavl
      481 rrlsetdtly anvstgtspn qvasssnqsl psrrsaqvea gwkslwrgga vvsdlavyrl
      541 dqknmiasdl stplnnfdft tagsarsqgi easlsgqvtd rvavaatyaf thakylqnpv
      601 yggmsvpnva rhaatlwaqy awnaqwktga glylqsrrfa deanttvlpg yarvdlsqtw
      661 tttlahgqsv evqatvrnlf dqhyfvsshl hvsrwitpgq grnafvsaty rf
//
LOCUS       WP_284396241             225 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Dyella lipolytica].
ACCESSION   WP_284396241
VERSION     WP_284396241.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..225
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24538
     Region          50..148
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mhndpsneng ilhswqqnae awtntvrdgl iesrrlvtdr aivdavldgq prsvldlgcg
       61 egwlvralat rgiqavgvda vpaliarase rggefqvasy ediaagrlpl rvdalvcnfa
      121 llgkesaerl vaslpsllse dgrfvvqtvh plvacgeqay vdgwrqegwt gfgtafpspa
      181 pwyfrtlasw vglfaetgwh lcemreplhp etgrpasvif ilqrh
//
LOCUS       WP_284396465            1017 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Dyella lipolytica].
ACCESSION   WP_284396465
VERSION     WP_284396465.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..1017
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=114172
     Region          34..1017
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mkefkpfrld pvnhrlwrvs degepapvtm takafdvlry lvehpgrlvs heellealws
       61 gvavqpevlk ghvlairnal nddaqhpryl ethrgrgyrf iadvmtaqkt dnrlshtsap
      121 lligrasplk alrdalaqar ngqpkivfvr gdagigktal vetfcrevss qhttqsfgrc
      181 iegfggaepf ypiievlsrl ikgangnkvq dalvtvapsw gnqlagllsr ehqarlqrva
      241 hisarsrmlg efcelievla edevfvllle dlhwadfstl dlisafarrk ssvkllllat
      301 yrsdecavrg talrqlvnel llhklcesvd liglsqqdia eyvqsddsee srsfvqlllh
      361 csggnplflg tildhlqnih masvdqgrwk ndvplsqisl eiperinhvv etkistldde
      421 tqraleaasa vgqifnpvvp ataaglsarr feeicealsr trtfihrcgt dtlaggqvvr
      481 lyrfshallr evllnrqgpl rlaqshalig keleksypse lrahaafelv eqfsnarews
      541 kgltylkial qtakrryahq dalaildkad aiavhlsnge reltqtvlle drasiyatnh
      601 dpralqafth lvqmseqlry seiqaraelg laftlswrda taciphlena arlsnaqtep
      661 qlkarirlss aiwriwiagw dpnqakicee nliplrngsd rqitawglie ysmvclissr
      721 yrecletvdt nlemlvghav drpefnifra iwmahlgrpw aytllgewgr alkefdasea
      781 lfvgnanrys ictlemlrgf lyliagdyqa vkdicsklgf ykdktghqpa alytlvlane
      841 irhctllaga aeiglgnldg gidtlkqler dmleqpaltd wywlfllews lanallqsgd
      901 ielarlhadr midrsdrtie vtwrtlarel rcriaieegd lehalrlind alhmadvmga
      961 pivdwrvhrt aaqlyrlqgd sagaslhqql fneksqrlld slpsdhrlra sfarlma
//
LOCUS       WP_284396547             362 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Acidovorax sp.
            SUPP2825].
ACCESSION   WP_284396547
VERSION     WP_284396547.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..362
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39219
     Region          10..360
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 meftdlktqy qklrpdidar iqkvlehgqy ilgpevhele erlaaytgak ycitvangtd
       61 alqiaqmalg igpgdevitp gftyiataet vallgarpvy vdvradtynl daskleaait
      121 pktkaiipvs lygqcadfda inavaarhgi pviedaaqsf gatyhgrksc nlttvacasf
      181 fpskplgcyg dggaiftnde alarvmrqia rhgqdrryhh irvgvnsrld tlqaavllak
      241 ldsfdeeikl rqqvadryhq llrsagisti pliaanqqsa waqytvraqe rdrvqavlsg
      301 agvptaihyp lplnkqpava dpdvqlpvgd rlaqevlslp mgpfltvsdq drvvsaltka
      361 me
//
LOCUS       WP_284396606             381 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Dyella lipolytica].
ACCESSION   WP_284396606
VERSION     WP_284396606.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..381
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42284
     Region          40..367
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mpqalpptls givgtnrast gvtrqieand dvaaiglwla eyhssphtfr syrkeaerll
       61 lwatqlrgka vsslmredvl ayeaflaapl ptwcddalar hgyhrrlftg plsdrsrrqa
      121 lgilaglfny lvragylagt pfalqprrrg argtrrtier yleralwqdv lakveqwpqt
      181 sprekqryer arwvlrvlye talrateaaq anegdlrhrr grwwlhvtgk ggvegdvpvs
      241 dalmadfary rtfygllptp nsngrcplil giagrttplt atavylvvkd alvrvadale
      301 padpvgaarl rqasthwlrh taathqaeag npvhhiqhnl rhssiattsi ylhaeedarh
      361 asttkahaga shdpydkdgt a
//
LOCUS       WP_284396640             215 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Acidovorax sp. SUPP2825].
ACCESSION   WP_284396640
VERSION     WP_284396640.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 215)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..215
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22673
     Region          45..123
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          143..215
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mkkllapmlm aavlavaafp alsqghapaa aaqkpakpdl vkgeatftav cvachaadgn
       61 saiainpkla qqhpeylvkq lqefksgkrn npvmkgfasa lsdddmrnia wwvaskqakp
      121 gfakdkelva lgeriyrggi adrniaacag chspngagip vqyprlsgqh adytaaqlva
      181 frdgvrsnsl qmtqvaakln dreikavady iaglr
//
LOCUS       WP_284396658             757 aa            linear   BCT 25-DEC-2024
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Dyella lipolytica].
ACCESSION   WP_284396658
VERSION     WP_284396658.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..757
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=80473
     Region          61..>197
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          209..737
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mkpvsgspqd khddvdlsrr halqagglti aflwlggtgv asammnarrq pgdaaaslad
       61 gnppfapnaf iridtsgavr lvmpsaemgq giytgcsmll aeelgvgldq itvehsppsd
      121 elygipalgg qmtggststr atwpvlreag avartmlvsa aatnwhvdps tctvdrgvih
      181 htpsgrslgf gevataaakl pmpdkvqltd pkdfkligkp mrrvdssdki kgatqfgldv
      241 ripgmkvatv macptfngkl aavddiaara ipgvvdvlrl dnavavvgdh fwaakqglqa
      301 lhiswdhgen anlttqqlrd alaesarhgk sivarndgaq pqgttiqsey qspmlahatm
      361 epmnatvlvt adkcevwtgt qvparaagea aritgltqdk itlhnqylgg gfgrrletdw
      421 veqavafakq vsyplkvvwt reedirhdrv rpmyhdvisa vldangrpvw ygyrtsggsv
      481 larfappamg kdgmdsdave cvadvpydip nakvewirhd mppglvvgww rgvgpthnlf
      541 vvesfmdela hhagkdpley rrallqkspr alavlnlaae kigwggqplp arigrgialg
      601 epfgshvcai veaevtpqge vrlrrvvval dcgiavniss ieaqvqggvl fglsaamfng
      661 itikdgaieq snfndyrnlr ineapmvevh rvinaeppgg lgevgtaiaa palanaifaa
      721 tgvrlyklpv drdllvqnad alksvasaaa htgrnvt
//
LOCUS       WP_284396685             317 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Acidovorax sp. SUPP2825].
ACCESSION   WP_284396685
VERSION     WP_284396685.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616068
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..317
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=34460
     Region          62..203
                     /region_name="Methyltransf_32"
                     /note="Methyltransferase domain; pfam13679"
                     /db_xref="CDD:379330"
ORIGIN      
        1 mkrakaaagq ggassssagr tapkpspedq vlqelrpgqs iellkalhil tregrlnqds
       61 rrklkqvyhl fqfiepllqe lsqdghaatl adhgagksyl gfilydlffk algrghiygi
      121 etraelvehs ralaqrlafe rmsflnlsva estdaaalpq ridvvtalha cdtatddaia
      181 fglakqaram vlvpccqaev aaclrqgkal qlsrtplael wrhplhtrem gsqitnvlrc
      241 lhleasgyqv tvtelvgweh smknelivar ytgqkkrsaa erlrailaef gleqtlaarf
      301 glppeadtap gavpatv
//
LOCUS       WP_284396709             251 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor [Dyella
            lipolytica].
ACCESSION   WP_284396709
VERSION     WP_284396709.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 251)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..251
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28442
     Region          11..243
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mapsedksps ihvlvvdded larrnlilll rndpdiasvt ecgsgleaiq eikrskpdlv
       61 fldvqmpecd gfdvlellga dmpetvifvt aydayalraf eagaldyllk pfddarfhra
      121 larakeklar yaptqrrsis riavksrsqt lfinvadidw ieaasyyaci hvgadthilr
      181 rtlqeleqdl dartfarihr siivnldrvr glelqdngey evvldstarl rlsrryrkri
      241 qdrlgelsss r
//
LOCUS       WP_284396790            1015 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Pseudomonas putida].
ACCESSION   WP_284396790
VERSION     WP_284396790.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1015
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..1015
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=99212
     Region          <2..1008
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mtsivtamst aqiaalstkq isalgtsdia alssaqagvl staqiaalst sdvvslstaa
       61 iaafnasqlk algkddvavl aasqvavlss tqvaafsttq iaamttsqvg alagtmttaq
      121 igvlstkqia gvstttmaal staqlaaist kdiaalttaq lgavatadla vlstaqitam
      181 ttaqvgalaa kmstaqigal tvtqtaglst svigalsttq lqsistkdiv alstsqvagl
      241 sttvlgnltt aqlkaietkd iaamsttqlg alttaqvgtl asaqiaamsg tqidslgskl
      301 ataqiatlst kqiagvsttt iatlstaqla aiptkdiaam tttqlgavat adlallstaq
      361 itamttaqvg alaakmstvq igaltaaqta glsttvvgtl staqlqaist kdiaalstsq
      421 vgglsttvlg nlttaqlkai etkdiaamst tqlgalttaq vgalataqva amsgaqvdsl
      481 ggklgtaqia slstkqiagv stttmaalst aqlaaistkd iaaltttqlg avatadlaal
      541 tttqitamtt aqvgalaakm staqigalta aqaaglsttv vgtlstaqlq aistkdiaal
      601 stsqvaglst svlsnlttaq lkaietkdia amsttqlgal tttqvgalat aqlaalsttq
      661 idslgakfst tqisalstkq iagvsttsma alttaqvaai tskdiaaltt tqlgslstaa
      721 vgalstaqis alsttqvgtl qanlstgqia alstsqvtgl naaslttaql qaietkdiss
      781 lvttqlsals igqignlttg qvaalkyaqv nalvtsfttn qigalttaqa ggltttalng
      841 lsstqlqais tkdiaaltts qvaglsttsl aalsttqvks meavdvaals ttqagamtta
      901 qvtsltttqi aalkyaqvsa lasnlstgqi gllsttqisg itttvlagls ttqvaaistk
      961 diaalttaqv sslttsqiat lstsqvnals rtqvgsmtsa qlgqlsttqi pylnv
//
LOCUS       WP_284396830             405 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pseudomonas putida].
ACCESSION   WP_284396830
VERSION     WP_284396830.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..405
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=44239
     Region          64..398
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mpqaahltra pnqqgqtpve qdshqgieha falfnqvssq lsqsysllea rvselkgela
       61 vvsaqrieel sekerlanrl qnlldllpgg vividgqglv reanpaacel lgepligelw
      121 rqviarsfap rkddgheisl rdgrrlsiat rsldaepgql vllndltetr rlqdqlarhe
      181 rlsslgrmva slahqirtpl svamlyashl adseqqlsae trqrfagtlk erlhelehqv
      241 rdmlvfarge lplgdrvtpk alfqalqqaa qthvqghtvr wqcdshlgel lcnrdtlvga
      301 llnlienalq asdgparlkv hlfrrertlh lcvsdagsgi aaellarlge pflttkatgt
      361 glglavvkav vrahqgtisl rskvgrgtcv rvelplidgq laegv
//
LOCUS       WP_284396877             438 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Dyella lipolytica].
ACCESSION   WP_284396877
VERSION     WP_284396877.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 438)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 438)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..438
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=47822
     Region          176..438
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mnriastapk rwlprsmasr lyliilagll laqglsmalq syeryesavs vmlntvenev
       61 gtsvaildrl paqerpdwlg rlqrdnyrfv ldagqpgmpl isersrqltr siakqvgady
      121 hvhadavsvk peryqvhftl hdgspltlei tphmapvasw lpvvltlqll lllactwlav
      181 rlatrpltql aqaaesmtpt adgprmseng ptevaqaaaa fntmqervar hlkerlhila
      241 sishdlqtpi trmrlraenl eegeertkil kdlremehlv regvayarsa hggaetpvri
      301 nveaffeslv fdyqdigrpv tlsgsingta ivrqqalrrv lgnlidnaik ygggaevgaw
      361 rteqgalcia vsdrgpgipe esleqvlqpf yrleasrnrd tggaglglai aaqltraigg
      421 nlalanregg glvatvtf
//
LOCUS       WP_284396910             204 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Dyella
            lipolytica].
ACCESSION   WP_284396910
VERSION     WP_284396910.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..204
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=21594
     Region          4..152
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 madewldane raraarfhfe rdylayvmah aiwrialsvc lgtetdrvpl thtsngqpql
       61 pgtslstsls hsgnyvamai cgaptvgidi eqspprivld dllttictpa eaaalqelpp
      121 aartqtlltl wtrkeallka fgvglaqapa tlsamsdepv appaqavgpw pcrvrtlevp
      181 fdcvgalaap vavvacnlhy lsva
//
LOCUS       WP_284396933             442 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Dyella lipolytica].
ACCESSION   WP_284396933
VERSION     WP_284396933.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..442
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=48071
     Region          169..395
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mspavlqvap hryaaarpgg amfvlslvyl mltiirpqdy mpaltgipll pvvlllafll
       61 wlgsntkvfa gpqflllllf llalmvsdaa ngwvggalvq lktfgpivia ffvlasaiaa
      121 sprrvvvaff vfvlcsivla lhgwnqtrvg vgwtgtplsl dgriqyvgif ndpndlgllf
      181 atafpmavyl sgrggflrrv iwlagaalll ygifltnsrg amlavvaiga vylwrrrglv
      241 talvlsgvgl vgmmmmpsrl qqldvsessa fgrvdawyeg lhmflakplf gvgagnftdy
      301 neltahnsli lvlaetgffg yiiwlafvgy gfwmmltilr qapppsddae qakawqverg
      361 laftlllslt glftaaffls rsytvllylv aalvvgeyag arqrfpdlph frladgwwrw
      421 lpiamisiaa lfvmvalllh sa
//
LOCUS       WP_284396945             312 aa            linear   BCT 25-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Acidovorax sp.
            SUPP2825].
ACCESSION   WP_284396945
VERSION     WP_284396945.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..312
                     /product="isopenicillin N synthase family dioxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35284
     Region          8..311
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 mggmgaetsa reirridlsd fehrkaeiae qlwsasveig ffqvtghgip vqdirnafar
       61 aqaffdlrre tkaqwplarn agwehkaqvr pstrtpdqke syqvtrprma glwpseaelp
      121 gfqeatlrfe aqcwhvgmql lscfadrlgf dpdfftrahd pssaayqstl rmlhyfavdp
      181 alkdelglwr agahtdfdcl tllfqrpgqg glqvlpgkem esrqwtsvep aegvitcnig
      241 dmltrwsddq lpsnfhrvrt plpheyqgar yslaffcqan edavvegpgr kyppitagdy
      301 lrqritanfa ky
//
LOCUS       WP_284397038             151 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [unclassified Acidovorax].
ACCESSION   WP_284397038
VERSION     WP_284397038.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..151
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16518
     Region          3..105
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 makrkslads pcpvarsldv vgdrwsmliv rdafdglrrf gefqaslgaa rnilsdrlrt
       61 lveegvleia pasdgsayqe yvltakgetl fpvvvalrqw geahlyarge khsvlvdrat
      121 gkplpkallr ledgrvvrpa dtlvkkvrar p
//
LOCUS       WP_284397178             222 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pseudomonas putida].
ACCESSION   WP_284397178
VERSION     WP_284397178.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17581992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..222
                     /product="helix-turn-helix domain-containing protein"
                     /calculated_mol_wt=24577
     Region          1..>60
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          <86..215
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mdigqrirea rkargltlea lanqvdtdtg nlsrlergkq gasqelltki fsvlqlgvad
       61 vehirpkgty pgltydldnl iyvspeenra rkgypliswv tagelarspd hhhpadaewi
      121 sstenagmng fwlrvrgdsm tctgnpsfpe gslilvrpea diisgkyyvv emldsgemtf
      181 kqyvedagik ylrplnagyr tieidgncrf igrvidtkmt gl
//
LOCUS       WP_284397310             247 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Pseudomonas putida].
ACCESSION   WP_284397310
VERSION     WP_284397310.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..247
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25713
     Region          3..245
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mgvivitggs rgigastaqh larrgmgvil tykrssdaar qvvadiehvg gkavaleldv
       61 advgsfvsfr eaviealqen wgisglaglv nnaghglfkp lesvsenqfd allgvhlkgp
      121 ffltqtllpl leanacivnl tsattrvata gvapyasfkg glevltryma kefgerrira
      181 nsvspgairt elggglndef eallasqtal grvgepedva rvigtllsae gvwinaqnie
      241 vaggyni
//
LOCUS       WP_284397325             166 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Dyella lipolytica].
ACCESSION   WP_284397325
VERSION     WP_284397325.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..166
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18490
     Region          73..156
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 miklvrieaq saqtykairl aalkqdplsf gstyerevsf sdkewltras sldgedrvgf
       61 faledeeafg lvvcfrdnkd ptvgdvismw vapiarrrgv gsdllkairh waqergiqtl
      121 rllvtslnas gisfyerngf vrtgktapyp htpdifeiem tlstcg
//
LOCUS       WP_284397363             104 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [unclassified
            Acidovorax].
ACCESSION   WP_284397363
VERSION     WP_284397363.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 104)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 104)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..104
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11437
     Region          12..100
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdptpidper lrqaasqavs alkalanedr llllcqlsqg eqcvsdlqar lgiqqptlsq
       61 qlgvlrtqgv vetrregkni hyrvadaall eilavlyrly cpke
//
LOCUS       WP_284397474             324 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284397474
VERSION     WP_284397474.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..324
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33822
     Region          23..320
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mrfirhtall aalalapfla gaqewptakp ityvvpftpg gstdiigrvl anklgealkq
       61 svvvdnkpgq aggigasfaa kappdgytlf ggtisthain aslyknlsyn pvkdfepval
      121 vatlpnvliv npalgvnsvk eliellkkdp skrmfassga gtsthlagem fgdligvklt
      181 hvpykgtppa ltdvaagqvs fmfdqmtaal plakagrvkl lavttgqria lapelptmie
      241 sgvagfemss wqavyapkgt pkavvqrlna eivkalkqpd vvdklhtqlg mdivgstpea
      301 laahmakeip rwaelvkksg asad
//
LOCUS       WP_284397619             203 aa            linear   BCT 25-DEC-2024
DEFINITION  KdsC family phosphatase [Acidovorax sp. SUPP2825].
ACCESSION   WP_284397619
VERSION     WP_284397619.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..203
                     /product="KdsC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=21400
     Region          33..202
                     /region_name="KdsC"
                     /note="3-deoxy-D-manno-octulosonate 8-phosphate
                     phosphatase KdsC and related HAD superfamily phosphatases
                     [Cell wall/membrane/envelope biogenesis, General function
                     prediction only]; COG1778"
                     /db_xref="CDD:441384"
ORIGIN      
        1 mdqpltrata gaatpaiqpl pplrpalqfd aqlllraqgv rvaffdvdgv ltdgglyfse
       61 agetlkrfht ldghgikllq kagitpavvt grdapalrlr lknlgvvhar fstedkrpaa
      121 esilaelgld waqaavigdd wpdlplmrrc alacapchah iearavahhv taaaggagaa
      181 refcdlllva sgryaqllea yta
//
LOCUS       WP_284397734            1639 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-glutamate dehydrogenase [Dyella lipolytica].
ACCESSION   WP_284397734
VERSION     WP_284397734.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 1639)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1639
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..1639
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=182072
     Region          1..1634
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 mnairaandi plasivleel kksgfptkrl deaqffigaf fariastdih lhtpaewatv
       61 iaglidfmqq rqpgraavrv igaghaarna veivtddmpf lvdtvsmvls thspihavih
      121 pvvkvsrdan gqlqrigdeh glaesvmhfe vdhladdaka rliaqieaal edvraavrdw
      181 aamrdkalai aadlpnrklp ldaasvkeag eflrwlaeen ftflgyreye vtqadgdevl
      241 rsvegsglgi lhksersvap rslrtlvate lpqsgstdai iltktnarsh vhragnmdyi
      301 gvlkfdangk pvseqrflgl ftsnaymtrp qdvpmvrqrv eavltrsglk rdsysgkslr
      361 hilqtlpqee lfqasedelf ttatgvlelq qrartrlfvr rdrygrfftc lvfvprdrfn
      421 ttvreniegm lrevfhgesl dsnvlmgesa larlhvtvrp hlgdhpkfda qeletrlqhi
      481 vrnwhdglrd nlaghtgeaq avalfnhfgk vlpagyiedv speaaahdvv alaglksdds
      541 ihlnlyndpr dqslrfkvih vgapiplsea lpmlenmgvr mlaehvytle sdgrlltihd
      601 felktkapla fdlphlrerf ergfealwrg qaesdgfnnl vlsaqadwrq vavlrgycky
      661 lqqvgiafsq symeetlnry paiaglliel fnakfdprre qlsaaeleks qadlrremqt
      721 lipaetqkak pelidgivaa lahtreqqvh vlwealkall ddvasldder illsfmntir
      781 atlrtsffql wdgvprhyis fkfdskqvpd apkpvpyrei fvysprvegi hlrfgpvarg
      841 glrwsdrred frtevlglvk aqmvkntviv pvgskggffv khppvggdrd aqlaegiacy
      901 rlfinglldi tdnlvegklv pphdvvrhdn ddpylvvaad kgtatfsdia naisiehgfw
      961 lgdafasggs ngydhkgmgi takgawesvk rhfralgrds qtedftcvgi gdmsgdvfgn
     1021 gmllsthirl laafdhrhvf ldpnpdtaks faerermfkl prsswedydk slisagggvw
     1081 prsvksipis aevrsalglk advqhmspnd llnailkapv dllwnggigt yvkaasetha
     1141 dvgdrannal ringaelrck mvgeggnlgf tqkgrieaaq hnvllntdfi dnsagvdtsd
     1201 hevnikilld davqrheitd egrnqqlasm tdevgqlvlw dnyrqnqait lmehqsakri
     1261 gsmahfirtl egeglldrqv enlpsetelt erktrgqglt rpelsvllsy dkirlyqqll
     1321 dsdvpedpyl skelvryfpa plhekyaahm qrhrlkreii atavtnstin rmgatfmmrm
     1381 qedtgqgpaa iakaytaare ilgardlwaq ieaedskvae ntqvdaimqi wsmlrhitrw
     1441 llsrpggtle iaanveryqa avaelsatvp daltpagkad fgtsqekweg lglpaglalr
     1501 laklpelram ldmvevaqqt gqpvakvanv fyelgealdl ewlrgqieal pvdghwhaqa
     1561 rgslldelnh qhralatqvl alsggnknvs pvqawlerdd atlkytrsml seiltqnady
     1621 piasvavrrl aqlaqvpva
//
LOCUS       WP_284397787             306 aa            linear   BCT 25-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Acidovorax sp. SUPP2825].
ACCESSION   WP_284397787
VERSION     WP_284397787.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Kutner,J., Shabalin,I.G., Matelska,D., Handing,K.B.,
            Gasiorowska,O., Sroka,P., Gorna,M.W., Ginalski,K., Wozniak,K. and
            Minor,W.
  TITLE     Structural, Biochemical, and Evolutionary Characterizations of
            Glyoxylate/Hydroxypyruvate Reductases Show Their Division into Two
            Distinct Subfamilies
  JOURNAL   Biochemistry 57 (6), 963-977 (2018)
   PUBMED   29309127
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10187381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..306
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=33122
     Region          1..304
                     /region_name="GDH_like_2"
                     /note="Putative glycerate dehydrogenase and related
                     proteins of the D-specific 2-hydroxy dehydrogenase family;
                     cd12164"
                     /db_xref="CDD:240641"
     Site            order(45,64..66,89,221,269)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:240641"
     Site            order(65..66,83,89,93,137..141,159..162,164,191..193,
                     197..198,219..221,245..246,269,271..272,304)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240641"
     Site            order(92,94..96,98..99,102..103,106,108,111..112,114..115,
                     119..120,122,125,128,152,243,247,250..252,254,258..259,
                     261,264,266..268,270..271,275)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240641"
ORIGIN      
        1 mnitfcctht kadpwlqglq aalpgahitv wqpgappadf avvwappqqf mdeqagiqal
       61 fnigagvdal lalrlppgaq vvrlddagma vqmaeyvcha vvrhfrefea yeadmraggw
      121 ayrrprlrse fsvgvmglgv lgervakala hfefpvngws rspkavegvr afhgaegfdg
      181 flaasrvlvn llpltpdtqd ilnrdtlsrl qpggyvvnva rgahlieddl ialidaghla
      241 gatldvfrte plpadhplrt hpritttpht sartlreesi aqiarkiaam qrgepvagiv
      301 dprrgy
//
LOCUS       WP_284397806             447 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Pseudomonas putida].
ACCESSION   WP_284397806
VERSION     WP_284397806.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..447
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48435
     Region          49..>440
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mtfivwfaml gmvllllals ssylrwmpvt ssvvclalgi glgssglgfl hldvskssew
       61 mehltevavl fslffsglkl rlplhdrrwl aafylagpvm mmciggvtlv lhyglhlewg
      121 vsvligaila ptdpvlatlv qvadaqdedp vrfslsgeag lndgvafpfv ilglflqqnp
      181 gqawladwlm kdmlwavtag lllgywmgrg lgkltlflrl rnddstvspn dylalalial
      241 ayvlaesiqa ygflavfaag lglrqaevht ssgpqqpaae hlvqpvvghq hvapelavtg
      301 dvkglddsqv aagimlgdml afgslieram evflvtllgv vliehwdwra llvagalfll
      361 irpfsialfp irglvdirqr gllgwfgirg igsfyylfha lnhgllpgya vlstnlvlsv
      421 valsillhgl svqpllarye awkkras
//
LOCUS       WP_284397837             312 aa            linear   BCT 25-DEC-2024
DEFINITION  GGDEF domain-containing protein [Dyella lipolytica].
ACCESSION   WP_284397837
VERSION     WP_284397837.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 312)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..312
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35665
     Region          27..310
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 maisdskles essvyktlle straipwrid watmqfayig pqieellgwd qsswvtvqdw
       61 adrmhpedrd wavnfcvaqs kagvdheady ralkkngdyv wirdvvhvvr nddgsvdsli
      121 gfmfdiserk rteeqlaalr releelsfkd gltgvanrrr fdvvmetewa nacrnkqpis
      181 llmldidcfk qyndhyghle gdqclkrvak llglaatrpr dfvarfggee filvlpdtne
      241 teaykiasrc relianehip hegsdiskyl tasiglstli pecadeatpi ieqtdrrmyq
      301 akqrgrntiv nd
//
LOCUS       WP_284397904             747 aa            linear   BCT 25-DEC-2024
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Pseudomonas putida].
ACCESSION   WP_284397904
VERSION     WP_284397904.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..747
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=80412
     Region          30..>215
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          205..742
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mntpvdspae llklqlgetv nlsrrrflag tavgalvlgf glpmgsarvq aaateergtq
       61 vpafleirpd gtvrllspfm eggqgpftam aqivgeeldv dpvnfvvdsa ppgeayvvme
      121 ngmritggsm svrmsyptmr rlgalaraml lqagaeqlgv pvdelsttpg nvvhttsgrs
      181 ipygdlagra mdlpvpdpas vklrdpsqfr wigkpvrrld aydkstgkaq ycidikvdgm
      241 lhaavqhapr lgmtvgslrn eeqvkamkgv hsvhqlpgav avvaerwwha kraveavqvd
      301 wqeptadskv rpmpadfssd awrehlatve gpardeeneg diagalsnak tkveasyhnq
      361 ylnhaqlepp salarfnpdg tldvwlpnqa pdmfrddiak rtglepahin lhspllggff
      421 grhflydsan pypqaialak avgrpvkliw sreeeflrdv lrpvavvkfr agldadgmpv
      481 aleavsateg ptealagkqg ekidptaleg lsgkayaian kriaqiyvkg pamlgywrsv
      541 gnslndffye sfldeladkg gkdpfelrlh llrdnprltn llnavadlsg gwkrgpftae
      601 dgskrargva maspfgseaa viaevsieng qvkvhdiwea idpgsivnpa iiehqvngav
      661 alglsqtlve eavyvdgkpr arnydlypil ppsrmarvhv rivesgakmg gigepplpav
      721 apavanavaq ltgqrvrslp lsrhtfs
//
LOCUS       WP_284397944             276 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Pseudomonas
            putida].
ACCESSION   WP_284397944
VERSION     WP_284397944.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..276
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28505
     Region          4..218
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtglgvahlt alqlaparlv rearhagfsa vglrlhpvma galaypvaag sqamrelrav
       61 lagegvrvtd iefvsltaqt rvadyqplla agaelgavsl tvsgddedva rltsnfaalc
      121 elarghglrv dlefmrwrpv atlqqacavv tgagqansgv lvdalhlfrs ggqvvdigav
      181 dphllravql cdapmlapae aliiaeareg rllpgegqlp latllaalpg dvkisvevpc
      241 aglpaeqrlq aaaqvthawl hgrrpvspav qvaghc
//
LOCUS       WP_284397986             271 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sugar phosphate isomerase/epimerase family protein
            [Pseudomonas].
ACCESSION   WP_284397986
VERSION     WP_284397986.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..271
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29495
     Region          6..244
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtdrifslaa ltvlelsppd mveaaaragy shvglrlvpa teqeqhfplv adadlrrqtq
       61 arlrdtgikv ldleilrlkp etsvadfepi lavgaelggt ellvagndpd earlterfaa
      121 lcdlaagygi yphlefmpwt dvrdlsqamr vvanadrsng cvlvdafhfn rsrsslddla
      181 qlapqrmrya qlcdvagpvp admdeilrqa rnerrfpgdg dadlvsllrg lpptvplsle
      241 iptrqlleqg vsgeqracma lekamavlat v
//
LOCUS       WP_284398028             616 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: DUF3857 domain-containing transglutaminase family
            protein [Pseudomonas].
ACCESSION   WP_284398028
VERSION     WP_284398028.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12125919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..616
                     /product="DUF3857 domain-containing transglutaminase
                     family protein"
                     /calculated_mol_wt=67162
     Region          47..176
                     /region_name="DUF3857"
                     /note="Domain of Unknown Function with PDB structure
                     (DUF3857); pfam12969"
                     /db_xref="CDD:432907"
     Region          194..>315
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mlkkpylaav llpvtmlwag lahaftdgid rsitlekvaq tfvvqkdgsf rldvdsvmli
       61 neeraiktna qhpvsynrsl etlevveayt qkpdgrkvqv daahikeqqe qasaqapmfq
      121 dsvnkvvifp evavgdrlvl ryqrnratpl fpgqfeditv pqfypvgqfs ltydlpqgmp
      181 lqadargfka sspasgegrt vyrwdyvpaa rarietgavs yldyghylav stfsgfkdfa
      241 qayqaratve vtpqiselak rltaglptar ekaltlsdwv reniryvavy vsaggvvpha
      301 aqtvldnryg dckdhvalle allgaagiks tpalvnqgta yvfpkvptlg vlnhvityvp
      361 gldlyldstd psvaagylpl tvlnkrvllt atgefgktpa mqlnqvssdl lfkvktdgga
      421 dftnvstvkg wasemsrfgl klmkpedrem lvervlaayg qrgsgsikie pptangdfvs
      481 nvdghtenlv nlpgpvgvat ltslaggisq nvysftleke rsqsfvcign dtvetsrfef
      541 paqvnvlaip kpvklhdgnv dysarysqeg navlverrfk fshpdvvcsp edftamkpal
      601 eamirdlqsq iivqag
//
LOCUS       WP_284398184             472 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Pseudomonas putida].
ACCESSION   WP_284398184
VERSION     WP_284398184.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..472
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=52136
     Region          5..332
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(7..8,11..12,44,47,101..102,154)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(99,102,176..182,211,237..242,271,297..301,303)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mlwacillpq laldtvlrer ddpdtplvll ggptqrrvlq svspaaaalg lragqtltaa
       61 ralaegftcv eadprrieqv qqllaawayr fsaqvslhyp ralllevgss lqlfgpwplf
      121 earlrqelad lglrqrivla snpvaarmla nahdglavgd adatraallg mpitriglpa
      181 daaeafarmg lrqlgqvlsl prdtlakrfa pqvqlhldql lglrnlglaf yqppdrfetr
      241 lelnfdvesh qallfplrrm lndlaaflag rdcgvqrfcl hlehaegpdt lltvgllaae
      301 rdaamlfelt rgrleplrip apvrnvrlva edlptfvpqh qalfdpraqq aqpweqlrer
      361 lrarlgdeav kglsaaadhr pecawqlteq gaqgsmpvap gtrpgwllpa pmaldtasyq
      421 vhgqaeries gwwdggdvrr dyyrietrdg lrgwayrdlg qagplwlqgw fa
//
LOCUS       WP_284398227             345 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284398227
VERSION     WP_284398227.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..345
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=38345
     Region          1..341
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mstqhrgnlf dlmricaasa vifshhfhit htasptwlhs dmvggvavmt fftisgylvt
       61 qswlrqpkal aflskrflri wpgvlfavlt nvflfgiffn slpatdflah pdtlgyfrnl
      121 llikdypylp gvfennpikh lmngplwtip ieslcylvla gagllgvfrs rwlaglaava
      181 yiaffltarn adltgemqhw feypayftyg aliavfrdaf harsgrlllv laplaavlff
      241 rlqmehtagl lllppllvhi gslnvpalaf lqrggdpsyg iylygcpvqq svyalwpdla
      301 fipslmlsva laavagyasw hlvespalrf krwfqrtpva pqaap
//
LOCUS       WP_284398239             443 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Pseudomonas putida].
ACCESSION   WP_284398239
VERSION     WP_284398239.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..443
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46924
     Region          24..428
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(33..34,37..38,41,73,123..124,126..128,131,151,
                     154..155,158,262,265..266,269..271,274,301,305,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mrtldvhpii dnarftpfhw mvmawcglll ifdgydlfiy gvvlpvimke wgltplqaga
       61 lgsyalfgmm fgalafgsla drigrkkgia icfalfsvat ilngfassps efgiyrfiag
      121 lgcgglmpna valmneyapk rlrstlvaim fsgysvggml sagvgifmlp rfgwesmffa
      181 aavpllllpv ilyylpesig flvrkgrtee arallkrldp qcdvqaddvl qaadrkaggg
      241 asvlelfrng lairtlalwl affccllmvy alsswlpklm anagyslgss lsfllalnfg
      301 gmagailggw lgdrynlvkv kvaffiaaal sisllgvnsp mpvlyllifi agattigtqi
      361 llyagaaqmy glsvrstglg wasgigrnga ivgpllggal mginlplqln fiafaipgai
      421 aalamavhla sgrrqaraia aqa
//
LOCUS       WP_284398256             774 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pseudomonas putida].
ACCESSION   WP_284398256
VERSION     WP_284398256.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 774)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 774)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 774)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..774
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=85995
     Region          101..762
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mirrslssas plrllilmlc aatlaflwgl hitqkaaarq dalsakaaeh lnlasivges
       61 lrqlvdraqa vgrvtqddmk vlrqgnfsla rilaedpvfk rmslydrqgr llsashtdga
      121 salpedwlrq lqrhvarygf kpflpsvqap dqqatlpnwr lpfllpltdl pgreienilv
      181 vqldigylav lfqhidlgss glvrllqddg lerlridtsg vvvagdglqp elpdtgsdag
      241 mltqyaagda yqslyrhvpe rgfsvvvsqr qdeilapstl aysrqfwlnl smtlmiiasl
      301 lwtlrllrkr qeafsaleha qqvnqqligr ledehrrssh aaatdhlsgl hnrrqfveva
      361 aqaltrqrgk rrlmailfid mdrfksinds lghkigdlll qavagriqrl lelgdeasrf
      421 ggdefvvlla gersedqina wvrelvqrls atyaldgqev ntspsvgvsi cprdgqdids
      481 lirsadaamy sakqagraqy rffdpslnla diqaftleqa fgsalaerqf vlhyqpqirl
      541 dtqqvlgyea lvrwdhpefg llypdrfidl aersgfivdl gwevlrlace alagwdvqgr
      601 etrlavnvsa lqlrqgdfam rllnelqrya iapqrlelei tettildpes tavehlhtlr
      661 gaglgisldd fgrgyagfah lhslplsklk idrsliapls nspddspivs stiilakrlg
      721 levvaegvet reqvvclkla gcdiaqgyhf srplspaqlr eyppfngvee kacv
//
LOCUS       WP_284398273             268 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Dyella lipolytica].
ACCESSION   WP_284398273
VERSION     WP_284398273.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 268)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 268)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14398448
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..268
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29680
     Region          20..114
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          181..258
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 msrkrqtaif drladdgsai atlthnypag hviplhfhdr dqlvyasrgv mtvqtdggaw
       61 ivpthrgvwi pkgvphsiam sgavamrtly lqprlakvlp rdccvinvpp llkelilhac
      121 tvgplwkser aqrhlvdmiv dqlqviqmvp lqlpnltdsr arrvaetllt epgnrqplah
      181 icktsgaslr tierlfldet nmtfgkwrqq lrmmhamrll gegakvthaa ldagystpsa
      241 fiaafrktfg ttptsyfetf artpsapt
//
LOCUS       WP_284398318             796 aa            linear   BCT 25-DEC-2024
DEFINITION  efflux RND transporter permease subunit [Pseudomonas putida].
ACCESSION   WP_284398318
VERSION     WP_284398318.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Sandhu,P. and Akhter,Y.
  TITLE     Evolution of structural fitness and multifunctional aspects of
            mycobacterial RND family transporters
  JOURNAL   Arch Microbiol 200 (1), 19-31 (2018)
   PUBMED   28951954
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Hand,N.J., Klein,R., Laskewitz,A. and Pohlschroder,M.
  TITLE     Archaeal and bacterial SecD and SecF homologs exhibit striking
            structural and functional conservation
  JOURNAL   J Bacteriol 188 (4), 1251-1259 (2006)
   PUBMED   16452406
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
REFERENCE   4  (residues 1 to 796)
  AUTHORS   Arkowitz,R.A. and Wickner,W.
  TITLE     SecD and SecF are required for the proton electrochemical gradient
            stimulation of preprotein translocation
  JOURNAL   EMBO J 13 (4), 954-963 (1994)
   PUBMED   8112309
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..796
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86442
     Region          39..774
                     /region_name="MMPL"
                     /note="Predicted exporter protein, RND superfamily
                     [General function prediction only]; COG1033"
                     /db_xref="CDD:440656"
ORIGIN      
        1 mkyakaragr lvercadlll arrkllltvf llltlglgys athtqldpgf nkqipvrhey
       61 mlnflefsqy ftganrflvs vrwkgegdiy npefldtlrk vtddvffing vsrasvtslf
      121 tanvryieit eegffgdvvv pprftasaed laqvrsnaar sgqvgrlvan dlksamvrad
      181 lqdvdpqtgk svsyvevakr ledirgkyss dqievnivgf aklvgdvveg lmtvigffvv
      241 aflitglllw lysrslrltv vallvallpv vwllgllplm glgidpmsil vpflifsigv
      301 shavqmtnaw kqevlagkds lqaahlafck ifipgslall mnalgfgvim lidipivhel
      361 gvtacigvml miitnklmlp iiisylrler svlskervqq qsrhplwwrl salaeprpal
      421 avlvlsvmll svavlkarql evgdigagap elraesrynq dnskivssys igldvlavfv
      481 qaqgleeacl spsvmravea fdfqmrsvtg vqsvqsvagf gktviagnne gnprwaaipg
      541 sarglsqgar aympedglvt dgcqqmqilv fltdhdgatv shvvqeakri iaqvqvpeir
      601 fflgggnvgv maasndavkr aevlmlvalf gsvllfcwlt fkslravlci lvplaivavl
      661 cnalmamlgi glkvatlpvm algvgvgvdy giylyeriqh emagganlrh afyqamcqrg
      721 taavftaltm aigvctwafa plkfqadmgv llsfmflvnv lgaifllpal aawfnlgkpl
      781 vavkanraar ahvfes
//
LOCUS       WP_284398374             297 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Acidovorax sp. SUPP2825].
ACCESSION   WP_284398374
VERSION     WP_284398374.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..297
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31793
     Region          32..292
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 msretalplg daaarpgdag tqheyllrgh gpnagtgvll ihgltgtpne mrllakglhr
       61 agftvlavql aghcgtqddl vatrwqdwha svqrgadrla mvtggrlvac glsmgavlal
      121 alaadrpaqv agvvalsptf rydgwsmpay trlsfllplf rmlgigrrrv fmeqppygik
      181 daalrervva qmqsgdsaaa glpgnpwwsv iemralaahv rrrldavrsp clvlharhdd
      241 iasaanaqai vqgvryapve lvllddsyhm itidrerrav vartvafaeh varggtp
//
LOCUS       WP_284398442             153 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Dyella lipolytica].
ACCESSION   WP_284398442
VERSION     WP_284398442.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..153
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17134
     Region          10..138
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mrtsgvlhtt vnmvvpffdv dsmdvvwhgh yvkylevarc allddighny tqmkasgyaw
       61 pvidlqlryv qaarfgqhlt vradlvewqn rllihyliqd aasgqrltra ssvqvavkls
      121 ngemqlvspe vftdaverrl hdvshnpsss vat
//
LOCUS       WP_284398462             394 aa            linear   BCT 25-DEC-2024
DEFINITION  thiolase family protein [Dyella lipolytica].
ACCESSION   WP_284398462
VERSION     WP_284398462.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 394)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..394
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40348
     Region          6..393
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 msdvsvviag akrtaigsfl gqftgvptpk lgatairaal eqagiaagdv nevimgcvlp
       61 anlgqaparq aslqaglpaa tgcttvnkvc gsgmkaimfg hdlikagsaa vvvaggmesm
      121 tnaphmvnar tgirygdgql vdhmawdglt npydgkamgv fgelcadkyh fsreeqdafa
      181 iesvkraqaa qasgafagei vpvtvsgrkg dvqvdtdeqp grsditkvps lkpafrkeng
      241 titaassssi sdgaaavvll saddakargi kplarivaha thsqepewft tapvsaiskv
      301 ldkagwkvsd vdlfevneaf avvamapmre lgipheklnv nggacalghp igasgsrlvv
      361 tllnalktrg lrrgiatlci gggeataiav erld
//
LOCUS       WP_284398482             197 aa            linear   BCT 25-DEC-2024
DEFINITION  YdeI/OmpD-associated family protein [Dyella lipolytica].
ACCESSION   WP_284398482
VERSION     WP_284398482.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Pilonieta,M.C., Erickson,K.D., Ernst,R.K. and Detweiler,C.S.
  TITLE     A protein important for antimicrobial peptide resistance,
            YdeI/OmdA, is in the periplasm and interacts with OmpD/NmpC
  JOURNAL   J Bacteriol 191 (23), 7243-7252 (2009)
   PUBMED   19767429
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..197
                     /product="YdeI/OmpD-associated family protein"
                     /calculated_mol_wt=22066
     Region          18..192
                     /region_name="YdeI"
                     /note="Uncharacterized conserved protein YdeI,
                     YjbR/CyaY-like superfamily, DUF1801 family [Function
                     unknown]; COG4430"
                     /db_xref="CDD:443542"
ORIGIN      
        1 manrdprvda yiaksanfaq pilehiravv haacpeveeg lkwgfphfgy kgammcsmaa
       61 fkqhcgfgfw qrkevvgaea eegmgqfgki ttikdlpnkk amtdyirkam alndagikkk
      121 rptaarkppp ktpadfaall tkhaaardty esfspsaqre yvdwiteakt datrqkritt
      181 alewlaegkq rnwkymk
//
LOCUS       WP_284398493             359 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Dyella lipolytica].
ACCESSION   WP_284398493
VERSION     WP_284398493.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..359
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40581
     Region          8..341
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 msssgatnnf dfiriaaatm vvfshqyali sqpeprpfgl ftlgtlgvli ffstsgylvm
       61 qswerdphaw rfiarrllri wpalavvtlf avlcigpift tltfhdyfra ketwgyfshl
      121 ylrttpnlpg lfegnpihvv ngslwtipie aqwyglllaa gmcgllrprf ryfllamval
      181 yaayiylifd vqhnplsafp frkfgceygt ffcygavlhc mrhawvnrvm ltfgslllla
      241 cllavsnhqy aavyvllpfi viwlgnkstp vlkragrfgd fsygiyvyaf lmqqlvvsvm
      301 giyrpyllvl lissagtmic avlswhlver pslalkrylp kqslvderlt rvttpsatg
//
LOCUS       WP_284398603             311 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Dyella lipolytica].
ACCESSION   WP_284398603
VERSION     WP_284398603.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..311
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33690
     Region          51..263
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mqdtheneid grrqflkcma wagagtlwlm ksgvlqaqpl gdgaaakdas fsfvqisdsh
       61 igfhkapnmd vaatlrqslt qinaqttrpa fvlhtgdlth lskpeefdtl aglmqeahvg
      121 rtfyvpgehd vigdngaeff rrfgerqqsg gwysfdqggv hfvglinvln lragglgslg
      181 adqlawlknd laglspdtpl vvfahmplwp lypswgwgtd dsaealtylr rfgsvsvlng
      241 hihqiqqkve gtitfytars taypqpapgv gpgpgplqsv tpealhrylg irdvrhvrga
      301 halavtdevl s
//
LOCUS       WP_284398744             105 aa            linear   BCT 25-DEC-2024
DEFINITION  Rieske (2Fe-2S) protein [Dyella lipolytica].
ACCESSION   WP_284398744
VERSION     WP_284398744.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..105
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=11410
     Region          4..105
                     /region_name="NirD"
                     /note="Ferredoxin subunit of nitrite reductase or a
                     ring-hydroxylating dioxygenase [Inorganic ion transport
                     and metabolism, Secondary metabolites biosynthesis,
                     transport and catabolism]; COG2146"
                     /db_xref="CDD:441749"
ORIGIN      
        1 mseawvevgt rsellpgeyk vvwdgdtaia vfnidgdlya vedicthdgg elaggdvvgf
       61 evecprhgar fdlrtgaptc ppayepiarf piresdgliw trddr
//
LOCUS       WP_284398816            1662 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Dyella lipolytica].
ACCESSION   WP_284398816
VERSION     WP_284398816.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 1662)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1662)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1662)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1662)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1662
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..1662
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=180931
     Region          53..144
                     /region_name="bMG1"
                     /note="Bacterial Alpha-2-macroglobulin MG1 domain;
                     pfam17970"
                     /db_xref="CDD:465597"
     Region          247..1651
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mkrlsigrrl hgglvgllfl vslgllsach hheagspalq gapagsssth aaatqpfsll
       61 sassqttdsr taialhfsav lasaqsfdql iavtgpngev vsgswglqdd gktlnfpfvn
      121 pdqhyavvlh agllaadgrt lghevkrdvy sgnlqaavgf asmgsvlpar gsrglplvsv
      181 nvhdadieff rvhddalsdl fcaypdnkhr dnyeldhqpn dwsrcehgdr akraitdmgd
      241 svyanhytlg gaqnertvty ipvqdvsqla qpgvymavvk qggtfangyd taiffvsdlg
      301 lhlrvyhdnv llhvaslhdg spisgvevei dgasgnaklk attdgdgnal iaykvdpadv
      361 liarhgkdvs vlpfnrpald vsnfditgrp eapfevfaws grdlyrpget lhasallrdy
      421 dgkpmkpqal fvrlkqpdgr slvdtrldpr dlnyfdlsqv ipedaptglw qlefrlnpgs
      481 keavqafpfh veeflperlk vdlaspqarl vpneplklav tssylygapa dgnrftakll
      541 vkpevhplpn lpdtffgnpl vdlpknandv vdtkldaqgh leqdvalpdd vkpvaplavt
      601 lsgsvyetgg ravtrllnkv ywpapelvgv rpqfdptqga esqgrasfei lradvdgklv
      661 agshlkvrlq reirdfywly ehgdewksna nvqlqqidek didiaagqra qvdfpvewgg
      721 yrlevydpdt klttvypffa gyswddentg kearpdkvkl aldkaryrag dtmkvtvtpp
      781 hdgpgvllie sdhllytrni datagatfdi pvtkdwerhd vyvvalvfrg gdaterttpa
      841 ramgiehvtm drndrriplk lsapammrpg npldvtvqaq glsgqhayvt lsavdqgvln
      901 itnypvpdaw awmfakralg idaydlysrv ieamdgeqak lryggdmssk alphaarlnp
      961 kvqivdlfag pvafdaqgka tlrvqvpdfn gslrlaalay tderfgnadg nitvraplvv
     1021 epstprvmaa gdkaqisldl knlsgkdgva kvsvkssdfv hvdnaarsvp lkdgssttll
     1081 mpvtanagag vatidihaql ndyqidrhfe favrpawpee vrsvpmvied gkavrldasq
     1141 taglfpatvh sqltlstlpp lpynsalrel llypygcieq ttskgyaaly mdektakalg
     1201 iaglsdaqrq aavesalari asfqasnghf sfwggtspie tfttpyvvdf mldardagfa
     1261 vpqdvlqkal qrlsddllag ghpyfsyehh dhmriadeay sgfvlarvnr aplgtlraif
     1321 dndrqklvgp lplvhlgial klmgdneraq kaideafawn kerpwyvgdy gsdlrdlavm
     1381 valthtygmn kpeydvklid warnatanvr atqekipyyh wswsylstqe qvaiarvaha
     1441 fdaasnapla aslniggkte qvpsdkfiwt rnltpaelas gvsvqpsgka tvfatfdvag
     1501 ipskapaada sqvdvrrayf ttdgkswsgd tlkegesliv elviearmnm pdaivtdllp
     1561 gglevenlnl ggaqqwegvv vdgiemdqht gaadivheey rddrydaalr llrgqaahvf
     1621 ylvravtpgt yavppplved myrpavrgvg amplsslkvi ep
//
LOCUS       WP_284398858             398 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudomonas putida].
ACCESSION   WP_284398858
VERSION     WP_284398858.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..398
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44021
     Region          8..385
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mastakqqny dvvivggavn gsatayflan npdfngsvlv ierdwtynks atalssssir
       61 qqfsnpinie isrfgaefvr sfpevmavdg drpdlafhen gylflgddkg yevlrrlhdt
      121 qvshgadvhl ldpeqlqrkf pwvnidslag asygrsgegw fdslgmlngf rrkarsmgie
      181 yienevvsvq regdrvtgvq lasgerigcg llvncagtrg tkvarmagld ipveprrrsl
      241 fvfdcrtple gtvpltidpt gvffrpegkf ylggtypknd pevdfedfdv lheefdeevw
      301 pilaervpaf egikvvnfwa ghydfcvldh naivgphnev nnflfcngfs ghglqqapai
      361 grglselity ggyrsldlga lsyqrvidnk pfledsvi
//
LOCUS       WP_284399010             380 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284399010
VERSION     WP_284399010.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..380
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40617
     Region          1..363
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mssasrssli dtvkglacat ivahhlvfyg pmsdvalplm pqvmawlsqh grmavqvflv
       61 lggylaaasl aptgaarfds aseqigrrfv rlavpyaval vlavlasaav rpfldhpsvp
      121 gepspaqlva nalmiqdivg eealsagvwy vgidfqlfal aallfsavrr wpgvsrpqae
      181 rlgkalvlag talsllwlnr epgldmwacy ffgsyglgml acwtvrapra ragllaiaal
      241 gvvalavefr eriavawvaa lvlvlwlrwg qpwlsarwpa gassavphpl erlgrmsysv
      301 flvhfpvcll vnaafqqawr nsaamnllgm atafglslaa grllywrveh hvpswtvalr
      361 wqaglvgtgv vvafaagrfg
//
LOCUS       WP_284399076             154 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Dyella lipolytica].
ACCESSION   WP_284399076
VERSION     WP_284399076.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 154)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..154
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16684
     Region          <11..129
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 msrrilhscg malwlicagt ahaqssdnal ytratlrdah geaifrhicq gchmpdakga
       61 tgagtypalt gnprlaspqy maavilfgrh dmpsfetkls tnrsffedak lsdaqiaevi
      121 nyvrthfgnh ysdsitaaev tamhpqdnpv kpkp
//
LOCUS       WP_284399160             721 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Acidovorax sp. SUPP2825].
ACCESSION   WP_284399160
VERSION     WP_284399160.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 721)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 721)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 721)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..721
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=76764
     Region          79..721
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mhrhasraep rfaptplarl vhhcvgagll iaaagagaqt aartaldevv vsdqaeaigg
       61 lqktysggqf arggnlgilg ntdlmnvpfs ttnytselid nqqartvadv vmndasvrtl
      121 tsrggfgddf qvrgftlsns dismnglfgl apstsiplet iervevlkgp galtngvgps
      181 gsvggsinvv tkraadvplt rltttymgka qfgthldvgr rfgednqwgv rvnglvrgge
      241 gnidggkqnl glgsvgldya gartrwslda fatrgetkef rpqinfagta tsvpavpdar
      301 lnfypgtklq dnvktvmsrl ehdlndrttv ygslgymdmd yeqtfpsgrp dalgnfrvsn
      361 ayydqytksk aadvglrtrf ktgsvghtla lganylnqet gyfyatsatt nasnlynpsp
      421 lpamtvarga pgkssvtdqs slaladtmaf lddrllvtlg lrhqtmeqen ftpttgvsts
      481 rydksavtpl agvvfkparn isvyanytag ltrgatagvt tanagetfap qkskqhevgv
      541 kvdwgqlttq aaiyqikkpg avtdpvtnvy sfggeqrnrg leltaygevq rglrlmasaa
      601 fndakltrta gglnqgnnaa gvpdrtfnlg ldwdtpwvqg lslngrviht spvyadaanr
      661 lrvgnwtrld igaryatkvs gkpvvlrasl enafdknywv vsnyvtvgap rtlmlsaaid
      721 f
//
LOCUS       WP_284399210             686 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Dyella lipolytica].
ACCESSION   WP_284399210
VERSION     WP_284399210.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..686
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=75773
     Region          <471..684
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
ORIGIN      
        1 mnllntikpa mqfnrpgwal llaalaltva vywpgltgaw ffddypnivd nhgvqpssas
       61 vpslinaals spssefkrpl aslsfaanyl ftgltpywmk ltnlvihlln gllvfllsrq
      121 llfaattlnw rsdskgtits dvprnardrt tqvelnaali atgwmllpin ltavlyivqr
      181 mesmanlfvl lglmgyvasr qrmlefncss datlseslfg ranemrmssi mrcavsiiip
      241 taigllaket avmlplyall iewvlfrfkt lsgkydlgit alfllvlflp mvvgltwlvp
      301 gllnpqtwaa rdftlstrll sevrivtnyi awsllptpqd lsfyhddfri stgllspwtt
      361 lasmlaligl iaiaitqrsr rplvalgigl flachlltgt iipleliyeh rnyfasfgll
      421 lavipmlsai apmssekstr fvlsrrvllv gllllwgset altsiawgnp lrlaeelaar
      481 apdspraeye lgrtyiiysd ydpaspftkl ayapleraaa lpgasilaeq alifmnarmd
      541 lplkdawwds liaklkahkt tvqdesslat ltqcarehsc nlpkdrmmaa fmaalshpdp
      601 darllanyad yawnvlddrp lgermaeeav kadprepayr itlirmlavq grkadaldal
      661 qkleslnigg rlnsdlaklh tlqglq
//
LOCUS       WP_284399247             285 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Dyella lipolytica].
ACCESSION   WP_284399247
VERSION     WP_284399247.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..285
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31058
     Region          9..281
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mpdlpltawi viagvlgllv gsflnvvilr lperldalwr qeahdvlgle haqqtlppgi
       61 vresshcphc khplaaydni plfswlwlkg rcrycqapis iqyplvellt ailsaivvwk
      121 lgptwvalag lfftwslval sgidlrtqll pdqitlpllw aglllslghl fvepksailg
      181 aaigylslws vywlfklltg kegmgfgdfk llaalgawmg pvallpvill ssfigaligg
      241 amialrkhar evpmpfgpfi amagwvwfia gdyllhaylg ltgmg
//
LOCUS       WP_284399223             270 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Dyella
            lipolytica].
ACCESSION   WP_284399223
VERSION     WP_284399223.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..270
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29552
     Region          5..266
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrftvigatg figgalvkkm ramgfevltt srdtielpsk pghiiyaagv tadfrerpfd
       61 tldanttvaa rvlkeadfds flylsstrly rhaghgqesa aislrsdepd qlydltkltg
      121 eaicyasgrq gvriarlanv lgsdfrsknf vfeiirdace kgiielrtsl dsskdyiyld
      181 dvvdilpkia lsgkyncynv asgrsishrd llkpiqsasg asltvrvgap vdtspsinid
      241 rlktefsfep tsvlpilaal vteyrkqirc
//
LOCUS       WP_284399307             509 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Pseudomonas putida].
ACCESSION   WP_284399307
VERSION     WP_284399307.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..509
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56895
     Region          11..381
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mprfktlgae rlalialavm lvgagigwrq pmnvdeerfl gvalemlqsg dwfiphraae
       61 iygdkpplfm wtvalfsqlt gspkvalylp glmsaatitw vlhdlgrrlw srrigviaal
      121 lflatyqsys ilrtgqidsf lclwvalgfy gmvrhllsgp awgwfylaca amglgiiskg
      181 vgfvpalmll pyawavrqgw hgvvampgqg wrwslgllcl lsgcavwlvp llvsiaqggg
      241 aaelaylnei llrqtasryt nawdhrepfw yffvkvipky wlplvlalpw lvpawrrqlq
      301 krdgrfllll gwvalvllff sfssgkrkly ifpalpglvl aiaplipwll krwllgrpaw
      361 rkayvavali wfalwfargf veplkegrnp healmseaar atggaelvlv nwreghwlfa
      421 rqpivhfgft gqsradaaay wlrhnptafa lipaselgrc fsadkarklg etsraewyvv
      481 gadadnghcq taapghvyrf awadapvar
//
LOCUS       WP_284399416             360 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Pseudomonas putida].
ACCESSION   WP_284399416
VERSION     WP_284399416.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..360
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39755
     Region          34..357
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mlkglllvlc lalataeaed wpdpawqndp arfdwqavda yafpprtapd rsgirtdall
       61 iirdgrilhe rytapttaat ahltwsvsks vlatlmgvaq gegrfqledp vtrfypamrg
      121 hpgirmadll hwasgldwqe dyeyaplkss vvamlytrgr edmaaytaar gasaspgqry
      181 lyssgdsnll aaalrgmlda gqypdypwha lftplgidsa vwerdragty vgssylylsa
      241 rdlarigllm qrdgrwqgrq llpkawvafn rtafdhaepv pgeatpgghw wlnqplagaa
      301 rpwpsapddt yaalghwgqa lyvlpaqklv vvryaddrdg syqhdellkr vlaamaregt
//
LOCUS       WP_284399373             540 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Pseudomonas putida].
ACCESSION   WP_284399373
VERSION     WP_284399373.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..540
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=58375
     Region          1..532
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mndqpllvvr dlsisyqasg qatqavkhla fslaqgetva ivgesgsgks tlanallgll
       61 pgtaridsgq lwvdgldvvr aserqkrqlr grtvglvpqd pmvslnptlr igqqigealv
      121 laqggrsrsv dadvlellaq vgldnpavra rqyphelsgg mrqrvliaia lagnprliia
      181 deptsaldvt vqrkildhlq rlvaergisl liithdlgma tdradrllvm kqgelveqgp
      241 paqivqapqh pytrallnaa pafsarrqpr qlapgskpil slqgvgktfe lpkvkgqdks
      301 fvalqgldlq vhpgqtlaiv gesgsgksta lrialgletp sqghvlfdqq dvtghgwrqf
      361 rplrrrmqlv qqnpfaaldp rftvfdsive plvsfgllkg aaleqrarql iervhlplhy
      421 ldrlprelsg gqrqrvaiar alalqpelll ldepvsaldv svqaqilall delqrelgma
      481 yvlvshdlav vasmadqvlv lrrgqvverg tvaqvfdrpt sdytreliaa vpgrlvtvaa
//
LOCUS       WP_284399418             420 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Dyella lipolytica].
ACCESSION   WP_284399418
VERSION     WP_284399418.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..420
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45623
     Region          2..408
                     /region_name="FucP"
                     /note="Fucose permease [Carbohydrate transport and
                     metabolism]; COG0738"
                     /db_xref="CDD:440501"
ORIGIN      
        1 mnrfrmlaal aliymvfail lnsvgtvilq sistfgvdkp qasllelfkd lpiaitsllv
       61 asflplfgyr rammialgiv afacvlmply psfhttellf tcvgisfalt kvavyssigl
      121 ltndrsehgr ltntveglfm vgvliagwlf safvdrsapa npswlnvywv lavicvlviv
      181 llatsqldes aartdettsm rgslaemlhl flrplvyvfl asaflyvlie qsfstwlptf
      241 nneilklpna msiqvasila aasaigrita gqvlrrmpwy allnlcvvgm gllvtltlpl
      301 ahgvtartdi gwfnapiaay lipligllma piypvinsva lsslpkpsha amtglivifs
      361 alggtlgsri taiifsrfng ihafyfslvp mslilitlfl fkretdragq ktaritftak
//
LOCUS       WP_284399526             747 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284399526
VERSION     WP_284399526.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20305241
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..747
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80036
     Region          85..642
                     /region_name="YCCS"
                     /note="TIGR01666 family membrane protein"
                     /db_xref="CDD:130727"
     Region          371..641
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mrispehrlr aalrvalshy vfnglsvafg lllisagvhg wlgaaaaasa svgvivtapp
       61 dlpgpargkf wqmlpapllg vplffgvqml hpselalgll ivpasfvafl amawgkrgvp
      121 iavavmfsmv fsmavpptpg vdpltaalat tghfalgaal yvvysvvanh alnaryrvqs
      181 vadallalaa lmrvqarqft pvdlqgppap alagallhrq aalaeqlqaa rnivlesprt
      241 prrqrlagml llvlemrdhl laceldldtl kahpghapvv vglrdvlhhv ademerlada
      301 mligrrptaf adhrphlaal rweeapqpqs vpeganpspr llargladri ghindealrm
      361 ialargeaep nlavvranwq mfvsptawsw hpfnglwrwd applrhaira alamgvgyav
      421 aqalpwgtha ywilltivvv lrgslaqtle rrnsrvagtl lgcvlalall smhptalgli
      481 valtlaqava hgfavrryli tavaatvlgl vqshmlhags stafalferl adtligtgva
      541 wafsyvlpsw ertqipalvs rtlaaqalha realalgqlq avdnapelaw rlarreayds
      601 lsalvqatqr slsepravrp pleplerlqv hcyqllaqlt avktmlllrr ghleperlqa
      661 plattaeaig nalsaprtaa daampprisp gpeplpdpfd aqlgpwllrr lglavglaee
      721 lrsdadqvlq smntkapdaq pvaersa
//
LOCUS       WP_284399589             407 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Dyella lipolytica].
ACCESSION   WP_284399589
VERSION     WP_284399589.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..407
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=44662
     Region          144..389
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mamtnfnhir llritgliay lcdgtplftt waterldllh rpnfalllft lfylvfgvly
       61 llvtnnlgsr thvgarlfgl llmtaaaliv gwyshsglsa ilmvvvsvvl pwlvpfwigv
      121 awmvlqtlcl avvfatfpel kysitlallq aiiytayall gfvastvasq qaderevqrr
      181 lnselratra llaestriae rmriarelhd lighhltals lnlevashls neaasvhvrk
      241 aqstarllla dvreavselr qddaidltqa lqslidgvps lrvhlaippr fsvedprraq
      301 vllrcvqeii tntakhagar nlwlsftynd enllslnard dgrgttailp gnglsgmrer
      361 laefggdvsm nsgvgqgfil dvclplgeps vlahtpsrfe ppalslt
//
LOCUS       WP_284399729             174 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA polymerase sigma factor [Dyella lipolytica].
ACCESSION   WP_284399729
VERSION     WP_284399729.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..174
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19353
     Region          1..173
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 maaaqagdqr ayarlltdsv sliravarrq gvpvdtlddv vqetlltvhr vrhtfdpsrs
       61 ydawlsaias rraidtlrsh grrdrrevhd efaldhhadr ddasagaere qeatrlreai
      121 ktlppgqrea veqlglkeqs laeaaertgr ntgalkvnlh ralktlrdrl hges
//
LOCUS       WP_284399768             194 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA polymerase sigma factor [Dyella lipolytica].
ACCESSION   WP_284399768
VERSION     WP_284399768.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..194
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21748
     Region          10..179
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mneatidada tdrmllqrms tgdrvalstl yhsyhgrlcr flsrltrrtd vieevvndcf
       61 wivwqksgef rgdsrvstwi mgiayrcglk alrqhgdepv eddalsddra pssdpdedre
      121 lrdwlskgld rlsadqrvvv elvygvghsl ddvaaimqcp vgtvkarlfh arvklrnvlp
      181 tlagespvmk esvs
//
LOCUS       WP_284399924             791 aa            linear   BCT 25-DEC-2024
DEFINITION  efflux RND transporter permease subunit [Pseudomonas putida].
ACCESSION   WP_284399924
VERSION     WP_284399924.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Sandhu,P. and Akhter,Y.
  TITLE     Evolution of structural fitness and multifunctional aspects of
            mycobacterial RND family transporters
  JOURNAL   Arch Microbiol 200 (1), 19-31 (2018)
   PUBMED   28951954
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Hand,N.J., Klein,R., Laskewitz,A. and Pohlschroder,M.
  TITLE     Archaeal and bacterial SecD and SecF homologs exhibit striking
            structural and functional conservation
  JOURNAL   J Bacteriol 188 (4), 1251-1259 (2006)
   PUBMED   16452406
REFERENCE   3  (residues 1 to 791)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
REFERENCE   4  (residues 1 to 791)
  AUTHORS   Arkowitz,R.A. and Wickner,W.
  TITLE     SecD and SecF are required for the proton electrochemical gradient
            stimulation of preprotein translocation
  JOURNAL   EMBO J 13 (4), 954-963 (1994)
   PUBMED   8112309
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..791
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86792
     Region          12..774
                     /region_name="MMPL"
                     /note="Predicted exporter protein, RND superfamily
                     [General function prediction only]; COG1033"
                     /db_xref="CDD:440656"
ORIGIN      
        1 mhphhqdkat llerlifnnr pvvialcvlv siflfwqatq irpstsfekm iplqhpfieq
       61 mmehrndlan lgntvrisve avngdifdkd ymetlrqvhd evfyipgvdr aglkslwsps
      121 vrwsevteeg fsggevipnt yngsqdsldt lrdnvlksgq vgrlvgnnfk ssivdvplle
      181 sypdpqdpgk qvkldyqqfs hlleekirdk fqaqnpnvki hivgfakkvg dlidglvmva
      241 mffgvalait wvllywftwc irstiavlit tlvavvwqlg lmhavgfgld pysmlvpfli
      301 faigishgvq kingialqss dadnaltaar rtfrqlflpg miailadavg fitlliidig
      361 virelaigas igvavivftn lillpvaisy vgiskkaier skkdatrehp fwrllsnfas
      421 akvapvsvtl alvafagglw ysqnlkigdl dqgapelrpd srynqdnsfi isnystssdv
      481 lvimvktppe qcsvhstmap idelmwtmqn tpgvqsaisl vtvskqvikg mnegslkwet
      541 lsrnpdilnn siaradglyn gdcslapvlv flndhkaetl ervtaaakaf adrhnkeglq
      601 fllaagnagi eaatneviks aeltiltlvy icvavmclit frsfaatlci vlplvltsvl
      661 gnalmaymgi gvkvatlpvv algvgigvdy giyiysrles flraglplqe ayyqtlrstg
      721 kavlftglcl aigvctwifs aikfqadmgl mltfmllwnm fgalwllpal arflikpekm
      781 vgkeggsifa h
//
LOCUS       WP_284399926             342 aa            linear   BCT 25-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Pseudomonas putida].
ACCESSION   WP_284399926
VERSION     WP_284399926.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Rengstl,B., Oster,U., Stengel,A. and Nickelsen,J.
  TITLE     An intermediate membrane subfraction in cyanobacteria is involved
            in an assembly network for Photosystem II biogenesis
  JOURNAL   J Biol Chem 286 (24), 21944-21951 (2011)
   PUBMED   21531723
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Komenda,J., Nickelsen,J., Tichy,M., Prasil,O., Eichacker,L.A. and
            Nixon,P.J.
  TITLE     The cyanobacterial homologue of HCF136/YCF48 is a component of an
            early photosystem II assembly complex and is important for both the
            efficient assembly and repair of photosystem II in Synechocystis
            sp. PCC 6803
  JOURNAL   J Biol Chem 283 (33), 22390-22399 (2008)
   PUBMED   18550538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..342
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=35744
     Region          60..211
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          143..297
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
ORIGIN      
        1 mreplrapak rgawpwaasa vlalalgvwa dsaqaaaade ystesakasq sllidathag
       61 krlvvvgdrg hilfsddqgg twtqarvptr qlltavffld dkrgwavghd aqilasndgg
      121 atwskqfedl areaplldva fldaqhgfav gaygallett dggqhwqdva erldnpdqlh
      181 lngiarvrda glfivgeqgg mfrsadngqt wakvqgpyeg slfgvigtaq pnallayglr
      241 gnlfrstdfg dswqpielkv argnlefgla satllddgtl vlvgnggsvl rsadggqtfs
      301 vynradrial agvsglangg lllvgqggvh ladaqgaega sq
//
LOCUS       WP_284399959             356 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Acidovorax sp. SUPP2825].
ACCESSION   WP_284399959
VERSION     WP_284399959.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..356
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35987
     Region          41..353
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtppgadart arrsavplri alrraapvgi alalvllvma sltagsapvs wreaavalag
       61 pwagafgapa gdmaqaivrd lrlprvvlal lvgatlalvg gllqsttrnd ladpflfgls
      121 sgastgavav itltgewlga wtlpaatfag aavaagavll lvrraggqgp aqtvlaglav
      181 sflfgalthg lvfagdqraa havvfwslgg lglarwdnlw laclglavpm vfvwrrhral
      241 dallagddta hslgiaperl rtqafvvaav ataccvalag vigfvglmvp hlarrlsgpl
      301 haaflplagv lgaglllasd lvartllgsq elpvgivtag igalfvmall rrrvad
//
LOCUS       WP_284400077             665 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidase U32 family protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284400077
VERSION     WP_284400077.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..665
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=73776
     Region          6..307
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
     Region          457..518
                     /region_name="DUF3656"
                     /note="Collagenase; pfam12392"
                     /db_xref="CDD:463557"
ORIGIN      
        1 msllphqiel lspardadig ieavnhgada vyiggpafga ragagndlrd lerlvrhahr
       61 fhsrifvtln tilrddeleg arqmawqvyn agadaliiqd mglleldlpp iqlhastqtd
      121 irtpekarfl qdaglsqivi areldlqeia avraatdpar ttieffvhga lcvaysgqcy
      181 ithahtgrsa nrgdcnqacr lpyevldgsg riiahekhvl smkdnnqsdn lralidagvr
      241 sfkiegrykd mgyvknitah yrklldeiie erefsaepla rsssgrttft ftpdpdqnfn
      301 reftdyfvng rqddigafdt pktpgraigw vtkvgenfae lelsspdtvl hngdglcyyd
      361 lqkelvglqi nraeavnark glwrvfpkdp iagfkdlrkg lqinrnrdmd wvrtldkkss
      421 drriglwaql setpdgfdlt ltdedgfvgs aaivhphqra tdgpqaeatl reqlgrfgat
      481 vfsvhdials lsqpwfvpas alnplrrdav aalesaraag lvrlpraepv qppapfpedt
      541 ltylanvfnq kahdfyvkhg vkvidaayes keeegevslm itkhcvrfsm slcpkqakgv
      601 igvkgtikae plqlingkek ltlrfdckpc emhvvgkmkk svlnqhardm qavpmqfyrt
      661 rpvag
//
LOCUS       WP_284400186             264 aa            linear   BCT 25-DEC-2024
DEFINITION  XRE family transcriptional regulator [Pseudomonas putida].
ACCESSION   WP_284400186
VERSION     WP_284400186.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..264
                     /product="XRE family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29185
     Region          <40..>86
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          129..259
                     /region_name="COG2932"
                     /note="Phage repressor protein C, contains Cro/C1-type HTH
                     and peptisase s24 domains [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442176"
ORIGIN      
        1 mkkpirtpls aeqladakrl heiykqrake sredpskptl tqtevgerce wkspqstvsq
       61 ymtgkvalnl ealvklseal dfepaqvspt laagirrash qvphtteaan splpdgaded
      121 eldgryayvp qydakaaagl gsenphveir stlafkrewl rvkgakpdql iviyaeggsm
      181 wptindgdvl lvdrsridpv dgqvfvlags egaivkrlvq gplgqwilrs dnddkdeypd
      241 ryhlrsngne hriigkviwr ggdl
//
LOCUS       WP_284400210             319 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284400210
VERSION     WP_284400210.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..319
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33288
     Region          24..317
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mrafvispli aacalaatva qaafpdrpit ivvpyapgga adavarvlat rmgarlgasv
       61 ivdnkagasg tigasyvaka tadgytmlyd atpysinphl fpkmpyasta lqplslvlla
      121 pnalivkads pfknvndlia kakaepgkln fasggsgtvq rlaaelfrqk lqldmvhvpy
      181 ksggpaiadv mggqvdfmfg tiaasyplvs ggklralavs aperskrlpd vptvaetvip
      241 gyeayewngv flpagtpepv aaklqqalve vlkedevkqr ladlgaqaig stpaefvtfl
      301 kkedakwgev vrkgdikld
//
LOCUS       WP_284400266             394 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Dyella lipolytica].
ACCESSION   WP_284400266
VERSION     WP_284400266.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..394
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42854
     Region          29..393
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mptysrtlrl lvslliacai asayaaqdak seaeqaqtrq qladlrakmq alakeqadta
       61 arrdsvnatl akqsdavaga akavrdtdaq iaakqqqldq lqtqrtalnq nlnsqraaia
      121 dllratyavg qgsdlrlllg dediariars layskyfqqd rlqkvqqlmt eltklqdlet
      181 qitaeqqalq atraqrlqqa daleqqrkeq qrlasqidtq ykneaqrlag mkqneqsldd
      241 lllklqkaid eaareaarra rpnpalpgve pgkvlanirg nlpwpaagav hnfgngvlia
      301 aprgsevhav argrvvyahf lrgygqliil nhgngwlsmy gnnesllhgv gddvaagegl
      361 gtaglttsds tgvyfelrhd gkpvdprgwl sqkr
//
LOCUS       WP_284400311             327 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284400311
VERSION     WP_284400311.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..327
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33713
     Region          30..325
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mirsllsfta lalalgataq aqtappaaty ptkpvrlivp fppgggtdil srlvatklte
       61 vtkwtvvpdn ragaggtigi teavkaaptg ydlvvgqkdn lvvapwlykn lpwdptkdli
      121 avahvaytpv iiatgansrf ktladvvaaa raepgkityg spgngttihl agdlfekaag
      181 iklshipykg snpalmdala gnvdllvssv psamgqiksg klrplavtsa krssslpdvp
      241 tvaesgykgf dvsswygifa pagtpanvvt tvntevnkll aspemqaaiq aqgaepesls
      301 aaqfstllkt dyakwkgive asgakie
//
LOCUS       WP_284400319             119 aa            linear   BCT 25-DEC-2024
DEFINITION  YchJ family protein [Dyella lipolytica].
ACCESSION   WP_284400319
VERSION     WP_284400319.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459551
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..119
                     /product="YchJ family protein"
                     /calculated_mol_wt=13461
     Region          4..117
                     /region_name="YchJ"
                     /note="Uncharacterized conserved protein YchJ, contains N-
                     and C-terminal SEC-C domains [Function unknown]; COG3012"
                     /db_xref="CDD:442249"
ORIGIN      
        1 magythccgp lhegavaqta eslmrsrysa yvlkredyll atwhssnrpa slklatqqpa
       61 ptwlgldvkh heedgehatv efvarlrygg gkaqrmheis rfvreqgrwy yldgrfpeg
//
LOCUS       WP_284400571             325 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284400571
VERSION     WP_284400571.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..325
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33915
     Region          20..323
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mhahpafrrt lllcgltlla agpaaaqdsy pskpitivvg yppggstdlt grtvaqelga
       61 rlgvpvvien vggaggaiga qkvasaapdg ytllvgasne iainklvtkk vkydvkdfta
      121 igviasqplv lvastgsgvk nateftqrvs rnpgkysygs sgvgtslhla gemvkeqgkl
      181 fmthipyrgv apltndllgn nlefgvfvls sglphiksgk vvalgtteak rsaitpdipa
      241 laelpqyknv digvwfalmg paklpkpvhd klkkalnetl qspdfrkkme asgstvasts
      301 lnadqfiaae vakyqkivef akiee
//
LOCUS       WP_284400726             447 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Dyella lipolytica].
ACCESSION   WP_284400726
VERSION     WP_284400726.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..447
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=48585
     Region          1..442
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mrtvliiddn pavgealsll lslhdvkpls altpdeglam lerqavdvvi qdmnftadtt
       61 sgeegvelfr airqrhadlp villtawthl etavelvkag aadylakpwd dskllatven
      121 llelsestre vnrnrqerrk rrealqrkyd ldglvfasea martldlacq varsdvpvli
      181 tgpngagker iaaivhansa vrggafiavn cgalpgelie aelfgaeaga ytgankareg
      241 rfeladggtl fldeignlpl pgqmkllrvl etgqferlgs grtrkvkvrv lsatnadlka
      301 miragtfred lyyrlnvidv nlpplserid dilplaehfl agraqlndaa realltyswp
      361 gnvrelknai eraallagag pitpeqlnlp qqagaaavrn ldepsrelve salhkaegvv
      421 sraaqslgls rqalyrrmer yglisqt
//
LOCUS       WP_284400786             403 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Dyella lipolytica].
ACCESSION   WP_284400786
VERSION     WP_284400786.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..403
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=45255
     Region          14..388
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mgkmlvaagd elgmrgagpr npgidllrgv sillvvlhhi glriplkrgv lagylpewll
       61 gavnyngyes vfvffvisgf liagntlrrw gsldrvdara fyarrfaria pcliallavl
      121 aalhllgvqd fviqragqtl prallaalgl hlnwyeghfg ylpgnwdvlw slsieetfyl
      181 gfpvvcllir rtwvlvlmli llalslpwth aalvhneiwq ekaylpgmaa iatgvlgali
      241 arrwqprerw airawievgc vglaaiflie qwlwpaihdg clllltvsvm clliglqwrq
      301 adgawhawrg mewlrsfgrl syeiylshmf vvvavvrlfr mygadmkwgv lwyvpavplc
      361 wllgnvvsrw ismpcerwlr arllasaskp sreivtasss etv
//
LOCUS       WP_284400944             651 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Dyella lipolytica].
ACCESSION   WP_284400944
VERSION     WP_284400944.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..651
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=71726
     Region          394..645
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mrngrarala aalcllmpav vaagdpvsve afahrggfsm prlspdgkyl avaleqgedh
       61 svqiyhlddm hhpknlrlpf hqlpydiewa gperlvvela kfvgtldhpe rqgeiiaana
      121 dgkrilpmfi reeaqagrgg lqytadngya tiaslpskan ghfymqtymw ndekntwlyd
      181 vnadngvrhl igqinvgdmd ftldpdgkvr yaqgldlsan yvvyrmqndr wvsladgehg
      241 drfepitfsq dkqhlyarts vkggplslvq tnadgtqsql lakddfgsvg yvqwtpqnep
      301 isaspvtgip tsivingdqp lsqiyqvlls kfpnqfvsfs sfsedgtili fkvssdrdpg
      361 tyylfdmkar tvaklfsena sidpdkmgsr vpmhfiasdg mpleailtvp hgatmnnlpm
      421 vllphggpfd isdtwffdtd aqflasrgyl vlqinyrgsg grgpgfvdag ygkwgtriqq
      481 dlidgvkwae aqhygdpkrv cvfggsfggy sammtvirap glfkcaigea giydlammyd
      541 kgdikertig rsyleqaigk dpselaansp dkladkidvp vllihgeade rapyaqakam
      601 raaleaahkp yewlikpneg hgfykeenrv dmynhvqsfl eknigpgvqa n
//
LOCUS       WP_284401088             106 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY domain-containing protein [Dyella lipolytica].
ACCESSION   WP_284401088
VERSION     WP_284401088.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..106
                     /product="PepSY domain-containing protein"
                     /calculated_mol_wt=11140
     Region          31..82
                     /region_name="YkoI"
                     /note="PepSY domain containing protein, regulator of
                     zincin peptidase activity [Posttranslational modification,
                     protein turnover, chaperones]; COG3212"
                     /db_xref="CDD:442445"
ORIGIN      
        1 mrskhdlawm aaglllaagt vvaqsspqgg lsldeavqqv qqrvggkvls aeprhigrkv
       61 eyrikvltpd ghvkvlavps damrppaaaq spkkspiggs ykkekh
//
LOCUS       WP_284401210             458 aa            linear   BCT 25-DEC-2024
DEFINITION  leucyl aminopeptidase family protein [Dyella lipolytica].
ACCESSION   WP_284401210
VERSION     WP_284401210.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Drinkwater,N., Malcolm,T.R. and McGowan,S.
  TITLE     M17 aminopeptidases diversify function by moderating their
            macromolecular assemblies and active site environment
  JOURNAL   Biochimie 166, 38-51 (2019)
   PUBMED   30654132
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Lowther,W.T. and Matthews,B.W.
  TITLE     Metalloaminopeptidases: common functional themes in disparate
            structural surroundings
  JOURNAL   Chem Rev 102 (12), 4581-4608 (2002)
   PUBMED   12475202
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415720
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..458
                     /product="leucyl aminopeptidase family protein"
                     /EC_number="3.4.11.-"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0030145 - manganese ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0019538 - protein metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49195
     Region          30..457
                     /region_name="PepB"
                     /note="Leucyl aminopeptidase [Amino acid transport and
                     metabolism]; COG0260"
                     /db_xref="CDD:440030"
ORIGIN      
        1 msalielrsh rhattpieat daihlgatrk rlsvaqrnwl dengfdaqlg svcllpdeng
       61 klarvlvgvd rqdplaalaa lpmtlpvgty tlaaesvald aqlaalgwal gayqftryrk
      121 srrapaklav daktaaalap lieatalvrd lvntptedmg pkqladavkq lgkthkakvr
      181 ewvgdelled nfptihavgr ashraprlie lhwgkashpk lvvvgkgvcf dtggldlkps
      241 dgmrwmkkdm ggaahaiala glvmqaklpv rltllipave navagnamrp gevivtragh
      301 sveidntdae grlvlcdala ygaeqkpdli vdfatltgaa rvalgpdlpa lfanddaiae
      361 valtcgrava dplwrlplwr pyrkmldsyl adfanagasr hagaitaalf merfvpegmp
      421 wvhldtyawn dadrpgrprg geamglralf aylqkryp
//
LOCUS       WP_284401168             270 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfotransferase family protein [Dyella lipolytica].
ACCESSION   WP_284401168
VERSION     WP_284401168.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..270
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=30135
     Region          6..200
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mrsihfisgl prsgstllaa llrqnprfha nmsspllgmv namlgemsdr nefstfitda
       61 qrrrtlrglf ehyygeefaa evvfdtnraw caklpvlcel fpdlkmiacv rhvswivdsv
      121 ervvrnnalh pssifsfqtg gtvytraegl angegmvgya ynalkeafyg ehaqhlmllq
      181 yetlvsdpak amaavydfvg espfqhdfdn vhfdaeafda ragtpglhai grkvaaqert
      241 tvlppdifrr fendafwlna qanirgvkvv
//
LOCUS       WP_284401186             225 aa            linear   BCT 25-DEC-2024
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Acidovorax sp. SUPP2825].
ACCESSION   WP_284401186
VERSION     WP_284401186.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..225
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23343
     Region          41..206
                     /region_name="YdeN"
                     /note="Predicted esterase of the alpha/beta hydrolase fold
                     [General function prediction only]; COG3545"
                     /db_xref="CDD:442766"
ORIGIN      
        1 msssaptpls asgrpvgrld gaapqaapsa rtaaggpvsv vivpgwrdsg pghwqslwae
       61 rlpgarrvvq ddwvtparap wvaalertvl eaphpvvlva hslgcitath mgepaaarvq
      121 gallvapadp erravlsdfa pvpyaplpyr silvassndp ycpirlagay arawgsefvr
      181 lpqaghvnvd sghgewplgw allhslvdga ewglghgate srsaa
//
LOCUS       WP_284401214             336 aa            linear   BCT 25-DEC-2024
DEFINITION  trypsin-like serine peptidase [Dyella lipolytica].
ACCESSION   WP_284401214
VERSION     WP_284401214.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..336
                     /product="trypsin-like serine peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=35984
     Region          122..314
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mkricskfwn klgvrtigwt cvalgmataf hsahaqqgpn gegvtnnrmd apieaspiqe
       61 npsdiiefwd egkmklaets egmpwrplek pfggdqsgyv vmpepyteha lskvngmlfy
      121 resagklahc sasvilsrsk slvltaahcv qayarwkemm vfvpayngaa egagrapygk
      181 wpvkqafipy lsagehevdn dvavlsiyps mpftkgsypi eqvvggglap lmtdsgdfka
      241 vevigypgaw ipgdgpynge qrrcvghatd sphgvglfvp mcatqsgnsg gplvlnhggp
      301 lspevigvvh nghnyarlrp ttfgviypea dnaalh
//
LOCUS       WP_284401241             323 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284401241
VERSION     WP_284401241.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..323
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34137
     Region          1..321
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mtlnrrhamv ygaaalastt amgqtanwpt ktlrlivpyp pggssdiiar aisqplsdll
       61 kqnvivenkp gangnlgadf vakaqpdgyt mllcdvgala ispsvytklp fnpskdlrga
      121 tmlaysphml vvhpsvpann lkelialskt adlnfavtat gsaphlagva lerasgarwq
      181 yvpykggvta iqdtmagqtq vlmngmlatl phvqsgklkv lalskatrmp lladvptiae
      241 qgipgfesgt wqgilvprgt pdpivqrlnt alisvirtpe irsrlagqga evvtmaaaeq
      301 dkffekerar wasvvsaaqi rld
//
LOCUS       WP_284401244             285 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Dyella lipolytica].
ACCESSION   WP_284401244
VERSION     WP_284401244.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..285
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32430
     Region          8..275
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mdqspvspel dnievelfvq alqrrhgydf sqyapaslkr rvrqlsdqle cktisglier
       61 vmhepqllpr llegltvpas dmfrdpvmfr alreqvlpvl asypqiniwq agcahgqevy
      121 slailleeag lyertqifat dlseralqqa qegiyparea qqwsrnyqas ggtrsladyy
      181 sarynllkld qrlrrnvtfa rhnlvsdgvf ceahlilcrn vliyfsnllq dhvlsqfrds
      241 lvrggflclg lresldyass sadfspfagp lriyrlasrs erkla
//
LOCUS       WP_284401262             442 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Dyella lipolytica].
ACCESSION   WP_284401262
VERSION     WP_284401262.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..442
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48760
     Region          51..410
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mqfrklplli agllgvttpl iaapvaqaas pasqpdpvvh parydatdln attsipperi
       61 kasldayahw ldvvaqrnev aglatavvvd gkvayereig yadtstqepi tpdtvfrlas
      121 lskafatalt gllvddghfs wdtklaevlp ffqlkdaqas sevtvkdilg qrlglphnty
      181 drmlednvpy eelvrkldev sltcnvgqcy gyqnvafsli gdliyaetgd ffyhqvdkri
      241 ffplgmttas ygrealessk swarphrpsg ehswtpfdpn dayyrvapaa gvnaslhdme
      301 hwliaqmggr pdvlsqplle ylhtpvvptp sethaspwrr arltsasyal gwrvftyage
      361 tmvfhageve gyrtmiaffp kyhigmvslw nspgaigtdl mpmvfdsilg lphvdwagve
      421 seppadkasp arphhkhryr rd
//
LOCUS       WP_284401265             366 aa            linear   BCT 25-DEC-2024
DEFINITION  lactonase family protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284401265
VERSION     WP_284401265.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..366
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=38517
     Region          32..363
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 maisssflra valapvaaat lmaasgaasa atwvyvsnad sqdvsvyeld raagklqpve
       61 tvpvggqamp mavspnkrql yvalrsqpfr vvtlaidpas grlkkqgeaa ladsmanidt
      121 datgrwlfaa sypghkitvn sidkdglvga vqqliptapn ahaihadaan ryvfatslgg
      181 dhlsswrfda atgkltanep altavapeka gprhfvwdka qrymyvvdel daalhvmayd
      241 aergtlrevq rtttlppgft gkpwaadlhl spdgrtlyas ertsstlstf rvdaatgqle
      301 plgqvpteks prgfavdssg rfliaagqds hsvslhpidp atgvpgtptr vaagknpnwv
      361 eivdlp
//
LOCUS       WP_284401280             388 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Dyella lipolytica].
ACCESSION   WP_284401280
VERSION     WP_284401280.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..388
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42898
     Region          11..386
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mdqtrspflv fgapqideae iaevvaclrs gwlgtgprva qlerdfaifr gvqheraaav
       61 nsctaalhvs mlaagiepgs evittpltfc atvnailhag lvpvladvdp vtqnidpdai
      121 eaaitprtra ilpvhfagrp camdrimava rkyglvvied cahaveseyr gqplgtfgdf
      181 gcfsfyvtkn ittgeggmil grseeqvara rvlalhgmsk dawhrfgdkg ykhyqvvecg
      241 fkynmmdvqa aiglhqlarv eeswrhrdei wrrydqafaq lpirlpapad setrhgrhly
      301 tvmldaqrcg iarddfleam nvarigtgvh ylsipehpyy qrrfgwrpeq wpnamklgre
      361 tvslplspal sdadvervvd avrsilhg
//
LOCUS       WP_284401282             417 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfotransferase family protein [Dyella lipolytica].
ACCESSION   WP_284401282
VERSION     WP_284401282.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..417
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=47124
     Region          13..234
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mseieanhhq gpifvvgspr sgtsiltwcl gqhanilpqe esgwmgefai gtgvryqtgn
       61 qhgdrsqlta lgvdreaffk tfgdaidami hrhrprqeqn ckrsarenpa qvdsafnisr
      121 sdvepksrwv dgtpeysfyi ygltllfpha rfvhivrdvr svvdsmlnfk qsackelvkt
      181 eqqayeywlr tvqacvqaer algprvvhrl ryddlvhrpe wairgvlefl gepfmapcie
      241 plarrinsse vpngfcavdp rtnpavveqa irlseqlqrp feegplspge ladlkarfdr
      301 rvafmseldt eyalgqekvc klskrldrcg lilvcyflla lvatapgvlr ygwwqmnfqn
      361 avwlvgavag lafyvtlrra glrsfvigmi hrcgwhrrag daglhklknt frnadvp
//
LOCUS       WP_284401307             392 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Dyella lipolytica].
ACCESSION   WP_284401307
VERSION     WP_284401307.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..392
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=42447
     Region          14..392
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mrkstrnaar qvklglgtra ihagqhpdps tgaimtpiya tstyvqespg vhkgyeysrt
       61 qnptrmayer cvteleggaa gfafasglaa aatvldllds gshviamddl yggsyrlfer
      121 vrrrsagldf sfidlnddha lkralkpntr miwaetptnp mlklvdlkkv aafarkhgli
      181 lvvdntfcsp iiqrplefga dlvlhsatky lnghsdmvgg ivvagtsdla ermgflqnsv
      241 gavagpfdaf lamrglktlh lrmkahcega melatwlqkh aaverviypg lkshpqhala
      301 rrqmdgfggi ismevkgglk karrvlercq lfalaeslgg vesliehpai mthasvplan
      361 rkrlgisdsl irlsvgvedi ddlkqelasa la
//
LOCUS       WP_284401338             333 aa            linear   BCT 25-DEC-2024
DEFINITION  FecR family protein [Dyella lipolytica].
ACCESSION   WP_284401338
VERSION     WP_284401338.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20752687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..333
                     /product="FecR family protein"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0016989 - sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36218
     Region          13..53
                     /region_name="DUF4880"
                     /note="Domain of unknown function (DUF4880); pfam16220"
                     /db_xref="CDD:435227"
     Region          102..325
                     /region_name="FecR"
                     /note="Periplasmic ferric-dicitrate binding protein FecR,
                     regulates iron transport [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG3712"
                     /db_xref="CDD:442926"
ORIGIN      
        1 mtkmkqdeiv qvaadwwvrl repdaegetv erwlawtsed vrhletferv nelasrlgsl
       61 dnvsrqglik afaraatpsp rwlplaaaaa favvvlagay vawtrfasgi ssqvyasava
      121 qnrditlpdg tqvalgaast ltthfshgqr rvdlsggeaf fqvihdnsrp fvvaagdvsi
      181 rdigtafdvr rtgqrvtiav tqgrvqiadt nqtpgkaqsg tlevsagqlv sydpnmssmt
      241 igsiapeqat awrndrlefi deplsvvian lnrysarplh iadadldkls ytgtirtdai
      301 dswlgalpqv fplrvntead qvilsdaehp prr
//
LOCUS       WP_284401506             329 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284401506
VERSION     WP_284401506.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..329
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34690
     Region          22..327
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mhrrtllkna laaagataga ampwaaqaqs dypsqpirwv vpypagggtd vlartvaeal
       61 rgplgqqivv dnrpgastni gaqmvatarp dgytlmsadn allaynehlf sklpfspekd
      121 ftyiaglsrf plalvvhpaf eaktvkdlla yaranpgkln yaspgngslh hlamemfknr
      181 tqtflthipy rgaapalqdv mggqvpcmfl dlaaglpviq agkvralaig sakrvpglpd
      241 vptlaeagvp ntevyafqgv lgpaglppal vtrlntevnk alasppvvkr mqdfgmeplg
      301 gtpeqframa raeakrwgei ikaagvkld
//
LOCUS       WP_284401379             466 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Dyella lipolytica].
ACCESSION   WP_284401379
VERSION     WP_284401379.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..466
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=51714
     Region          5..328
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(7..8,11..12,43,46,99..100,152)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(100,174..180,209,235..240,269,295..299,301)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mlwaclllpq laldgvlrrr addtplvlvd gavnartvva vnasaraagl rigqrltaaq
       61 allarfeavq ydaadvarwq qflagvayry ssqvallpha ivlevsksqs lfgswsvmer
      121 rlredfsalg fryriaaapt phgayvlagv sdgqtalshe gmqhlldhvp lsksrlptpa
      181 mdalprmgvr rlgqllrmpr dglqrrfgae llramdrlig dlpaglelyt ppdtvdwsie
      241 lsheveniaa lvfplrrmts dlaaylsgrd ggvqrfvlkl ehrdraatdv pigmlspers
      301 advlfdaarg rleqvqlpap vlvlrliaad lpgfvpagrd lfderpahal pfeqlrerlr
      361 arlgddavyq wgttidprpe hsqriaaqdd tpleprprpt wllqrpiplr galrviagpe
      421 rletgwwdgg dtrrdyyvve temgqrawaf capgersgwm lhgwfa
//
LOCUS       WP_284401413             429 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Acidovorax sp. SUPP2825].
ACCESSION   WP_284401413
VERSION     WP_284401413.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..429
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=47275
     Region          4..418
                     /region_name="cyclopro_CfaB"
                     /note="C17 cyclopropane fatty acid synthase CfaB;
                     NF040703"
                     /db_xref="CDD:468667"
ORIGIN      
        1 mkpllhalqa rleslpvdls lelpggqrlg raqapvalqf rdrrslaall sgevgdlgaa
       61 ivegrvrfeg rmrdlvaaaa allhgdpare qagwwtrmma rarsravhti trdaqhvrfh
      121 ydlsddfyal wldprrvysc ayyrdgamdl aqaqeakldh icrklrlapg qrfldigagw
      181 gglllwaaeh ygvdatgitl srnqhahvsr liaerglsgr vrmelrdyre lqhpepapfd
      241 riasvgmfeh vgrahmpdyf atvrrllrpg glllnhgits ggvdnaqlga glgdfiekyi
      301 fpggellhvs avlhdlaasg lemvdtenlr phyartlwaw sdalearlqe alrvlsagvg
      361 apqgeralra yrlylagsam gfergwmalh qmlaarpdgd latgalrgaq sdypftrdym
      421 hartgpagh
//
LOCUS       WP_284401577             155 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284401577
VERSION     WP_284401577.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..155
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=15827
     Region          1..132
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mafgrlertt gpqpmsdinm tplvdvmlvl vvifiltapl lassirldlp radgatpgap
       61 pqsvtvvldk egqaylddvp lapqalaarl aqlareqpdt evqlradtav pygrvvevmg
      121 aanaaglrri gfvadpaaps aapvspaaaa aaaar
//
LOCUS       WP_284401838             115 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Dyella
            lipolytica].
ACCESSION   WP_284401838
VERSION     WP_284401838.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..115
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12586
     Region          12..99
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 msselstnsp gfvvlyrwrl hpgmessfie awsrlsdllr sergslgsrl hhgsdglwys
       61 yaqwpsaqar kdafsagsvd lhasaqiera iaegypevtl epvadflvvp ahnvt
//
LOCUS       WP_284401869             399 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Dyella lipolytica].
ACCESSION   WP_284401869
VERSION     WP_284401869.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..399
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=43674
     Region          187..386
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mmaldgwter edtaatgwlr rllilgmawl ivgmavmpag asynpgkayq yvlaltmwlp
       61 mmvliamkpq rllafwrlpl mswatvllvw gwvslawtha arpadeaarn lsillflvac
      121 qwvfggneyr trrvligcsl vmalvavgvi vndmlhptsd grltgigvma npnlaaagma
      181 aallclwpwr fdgwrgalvk wlaisalasf vlltftrsaw aalfaalvvv vlsrggrraw
      241 lyaglicllg alsvaaglsv llargwslrp qifeqsmdlf mqhplrglgq gsafqleags
      301 evlvhahnmf sqlaielglp gvllwtgiwl tlgwrawrhr hetlgqvilg lwvfgtvavq
      361 fdlpylldsp rpgwlitwlp lalstafdrg lqakpagga
//
LOCUS       WP_284401882             494 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Acidovorax sp. SUPP2825].
ACCESSION   WP_284401882
VERSION     WP_284401882.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..494
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53245
     Region          12..494
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mnaplptaat apasglewrn gfaalgpdff telvptplpa phwvatsvda aqqlgvpaaw
       61 lasdaalqvc sgnallsgmq platvysghq fgvwagqlgd graillgeta gglevqlkga
      121 grtpysrmgd gravlrssir eflcseamha lgvpttrala ltgspapvqr evvetaavvt
      181 rtapsfirfg hfehfaardl lpqlrtlady vidryypecr gpdapggnpy aallqavser
      241 taellahwqa qgfchgvmnt dnmsilglti dygpfqflda fvpghvcnhs dtqgryafhr
      301 qpnvaywnlf rlgqallpli edvalaqaal asyqtvfpaa flqrmrgklg lqaahdgdaa
      361 lvdgllnlla qggvdypifw rrlshavasg dfepvrdlfi dragweswll sfsehpgqsn
      421 prhmadsmlk cnpkfvlrnh lgeqairaat qgdfaplhtl qallaepfde hpgheawadf
      481 ppdwassiei scss
//
LOCUS       WP_284401904             395 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Acidovorax sp.
            SUPP2825].
ACCESSION   WP_284401904
VERSION     WP_284401904.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..395
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=43147
     Region          3..370
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mtarslktwt wlhkwsslvc tvfmlllclt glplifhhei ghllgtevea ppmpagkphv
       61 sldrvldvar aqhpdrvvqf asqpedstdl wfatltptpa ptedfrsvav dartgallaq
      121 prfdegfmyv mfklhvdlfa glagklflgf mgllllvaiv tgvvlyapfm rklrfgevrr
      181 erstrvkwld lhnllgivtl vwafvvggtg mintwadllv kywqydelsa llapyngqpi
      241 tpvaerasvq ksldaalara pgtklsfiaf pgtsfssphh htfflrgnep ltsrllqpvl
      301 vdaktaevta apklpwylva llvsqplhfg dyggmpmkil walldiatii vlgsglylwl
      361 grraaspata spgktasgea apaspltaar aplkr
//
LOCUS       WP_284401949             132 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Dyella lipolytica].
ACCESSION   WP_284401949
VERSION     WP_284401949.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 132)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 132)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..132
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15050
     Region          17..102
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mqithvrftv nhmvhyqtrl dttfaalsdv trrgvleqlg gsdasitdla qrfhmtltgm
       61 kkhvsvleqa glvitekvgr vrtcklglrl leeeaawieq hrqlwsarfd aldkivedln
      121 rkekanarsk rr
//
LOCUS       WP_284402050             461 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Dyella lipolytica].
ACCESSION   WP_284402050
VERSION     WP_284402050.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..461
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49353
     Region          128..455
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msiskksiga wllcivvavl lalaglglwk rpdhairvat asvsdvlcsg vfvsglapdr
       61 vfaenyaadk glalllphlh ysvdrvhrri ttdwhgrfen vatyypnygc alawqtpdas
      121 tlqaasgaag paeteavvnp sdplirdala rafeepatgp lrhthaivil hdgnivaeqy
      181 aegfgpdtpq igfsvsksvv nalvgilvrk geldihapap iaawkdsgdp rhgitldqlm
      241 rmtsglslae edngfdpvsi mlfrmhdmas yaaqaplkat pgqtweyssg ntllvagvir
      301 dkvsggapgl irfahkelfd pigmrhvlme fdsaqtligs triyasardw arfgqlyldg
      361 gtvngqrilp aqwdtysssp tldspygsgf wtnvaakgdt qariegmppd aymasgaqgq
      421 rivivpakhl vivrlgttvd ppnydikglv rlvadvstai k
//
LOCUS       WP_284402171             213 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Dyella
            lipolytica].
ACCESSION   WP_284402171
VERSION     WP_284402171.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..213
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=24182
     Region          <25..159
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mrttlghdva giaaglsmdt ihvwllnyrr eqrraplral lgaylgllpd dvvlvddeyg
       61 rpeltepwnr flqfnwshsv dkaiivvahg vtpgidieri rprpramqla erffhreeaa
      121 alaavdesqr ertflelwtg keavlkalgr glafglnrlr ltmepvphlh wldgddasqw
      181 qlhrldpdtd hvasvawrgs srsidmwtla drd
//
LOCUS       WP_284402175             140 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Dyella lipolytica].
ACCESSION   WP_284402175
VERSION     WP_284402175.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..140
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=14804
     Region          1..134
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mafstgsgkg pmadinvtpl vdvmlvllii fmitapimth nvridlpqpn pnvipppnpp
       61 epvhlkidqs ggfywndtpl dengikaqma iigaqkdanl qpevqidaad avsyqvvarv
      121 ladaksygln kvgftdsngg
//
LOCUS       WP_284402188             458 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Dyella lipolytica].
ACCESSION   WP_284402188
VERSION     WP_284402188.1
KEYWORDS    RefSeq.
SOURCE      Dyella lipolytica
  ORGANISM  Dyella lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Dyella lipolytica"
                     /db_xref="taxon:1867835"
     Protein         1..458
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50237
     Region          58..458
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mamrlrsleg rltillalaa ligalvyagv tgwplpqilk wmheslglki stpdraeaiv
       61 icaivlapls wwlghmvmep vkrllraleg avasyrdgdf sisialdrrd elgdlirvhn
      121 elgqtlreqr qnlaqrelll dtvvqntpva lvltdsggrv ayaniaarhl fnegrslngl
      181 hfgtliedap ealrkateat edalfsvemd gseetfhlsq rafrlqgrph rlqlfrrmtr
      241 elsrqevaaw krvirvvshe lnnslapiss lahsgaelar rgdvqrlpsv fatigerarh
      301 lhgfidgyar faklpaprla avewkpflda lalhcrfqlq gnvptqpgwf dpvqieqvli
      361 nlvknahesg sapegvtlsl tlighelrie vgdrgpgmse avlaqallpf ystkrsgtgl
      421 glalareise ahggrialan redgglrvtl ilpqtaat
//
LOCUS       WP_284402474             339 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284402474
VERSION     WP_284402474.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..339
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=36003
     Region          35..337
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mpllfpithr atrriaaala caaaatfsfa ahgeaagwpr qpitlilgfp agsgidvvar
       61 alqeplgqkl gqpividyks gaagniasef vararpdgyt lafgtaathg snaalypklp
      121 fdvendfvpv gplidvsnvl tinpdvidak tlqefvalvk ahpgkynyas tgngagthma
      181 faefnarlgl dmvhvpykgg peaitsvvrg etccimnqvq tvlphyksgk vrllgvttsk
      241 pvaavkevpt iassglpgtq gfdssiwfgl fapkgtdaav vqklntalrq vleqpevrer
      301 fesqgnavri etpaqfrqtv htdrakwaqv vkdaririd
//
LOCUS       WP_284402485             758 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Acidovorax sp. SUPP2825].
ACCESSION   WP_284402485
VERSION     WP_284402485.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 758)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 758)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20158983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..758
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..758
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=81526
     Region          133..>407
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          299..750
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mtddhsvprt pqqarasrwa lgvgvaimca iglvllfllt vatnnralye rnyawlfgln
       61 vlvavlllav lvwvvvrlav rlrrgrfgsr llvklagifa vvgllpglli yvvsyqfvsr
      121 sieswfdvkv egalsagvsl arvtldtias dmamqtrtas sqlaqvpdaa agvvlerird
      181 qlgasdvvlf stagqpvasa gqsrfdlspe rpsaqllrna rqqratfqie glddiadpaa
      241 vqnarvktlv avgnasvgll veprylqatl rlpqvlvsna iavqeanrey qeralaregl
      301 rrmyigtltl slflavfgav llavllgrql arpllvlaeg vrevasgnls pkavlqgnde
      361 lggltrsfav mtqqlsdart avehsmgevd aarahlqtil dnltagvivl daegrirstn
      421 pgatrilrap maafegrpla dvpglaefas avqghfeafl gdreqhgldh wqhsfdlygs
      481 pasgvaangt slvargaelp nalrllvfdd iseivsaqra qawgevarrl aheiknpltp
      541 iqlsaerlem klsgklqdae qavltksvrt ivdqvdamkr lvnefrdyar lpaaelhald
      601 lnalvtdvlq lygaenatvp veaeldprcp eiagdaqqlr qvihnllqna qdaseptreq
      661 ggaagapvri ttrwsqssrr vrltvtdsgt gfpnhilqra fepyvttkpr gtglglavvk
      721 kiadehgarv dlvnrveegv vlgaqvslsf apghvvah
//
LOCUS       WP_284402521             321 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284402521
VERSION     WP_284402521.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..321
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33695
     Region          1..319
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mqrkpflrav lgalaltaaa sgfaqtypnk pvrvvipfpp ggtldavgrm laqklgeqtg
       61 qsfvidnkpg gsgviggdav akaaadgytl lfsastftta pmtlksvpfs vtqdftpval
      121 vakaplsvav nkdlpvtdik sllgyakshp gkmtfavgsi gsaghlstel lkragkidyl
      181 ivpykgtapa fqdliggqid gfidpilgsl qyhksgmlkv vavtsaqrvp nlpdvptvae
      241 tipgfefysw yglwapaktp papvqrlnae vnkalagdma qklkdqgllv tpgsvddfak
      301 fqradmersq kivtegnira e
//
LOCUS       WP_284402567             280 aa            linear   BCT 25-DEC-2024
DEFINITION  DODA-type extradiol aromatic ring-opening family dioxygenase
            [Acidovorax sp. SUPP2825].
ACCESSION   WP_284402567
VERSION     WP_284402567.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Vaillancourt,F.H., Bolin,J.T. and Eltis,L.D.
  TITLE     The ins and outs of ring-cleaving dioxygenases
  JOURNAL   Crit Rev Biochem Mol Biol 41 (4), 241-267 (2006)
   PUBMED   16849108
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Siegbahn,P.E. and Haeffner,F.
  TITLE     Mechanism for catechol ring-cleavage by non-heme iron extradiol
            dioxygenases
  JOURNAL   J Am Chem Soc 126 (29), 8919-8932 (2004)
   PUBMED   15264822
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..280
                     /product="DODA-type extradiol aromatic ring-opening family
                     dioxygenase"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016701 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30086
     Region          20..276
                     /region_name="45_DOPA_Dioxygenase"
                     /note="The Class III extradiol dioxygenase, 4,5-DOPA
                     Dioxygenase, catalyzes the incorporation of both atoms of
                     molecular oxygen into 4,5-dihydroxy-phenylalanine;
                     cd07363"
                     /db_xref="CDD:153375"
     Site            order(26..28,65,130,186,240,268..269)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:153375"
     Site            order(26,65,240)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:153375"
ORIGIN      
        1 msdlerarap tdsgrnaelp alylshgapl favdagetgp altrwgqevq arfphlrgvv
       61 vmsphwmprs pkvmtgpqpa twhdfggfpp alyalrypaa gapalaetvl arlrsagiaa
      121 egdaerpfdh gawvplmhlf pdahfpvvqv alpstagpae vyamgaalqg lrsegvlvvg
      181 sgsmthnlae ffgganeplp yvsefsrwie davqrrdwpa lldyrrqaph aerahpsedh
      241 flplffalga agpeaqahyl srevrygala mdafalqsaa
//
LOCUS       WP_284402574             409 aa            linear   BCT 25-DEC-2024
DEFINITION  GGDEF domain-containing protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284402574
VERSION     WP_284402574.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 409)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 409)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 409)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..409
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43768
     Region          125..407
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mpsaarphsp ppggsparra adgvlppppg lrgridralf gqskqvrirm sqcllafgll
       61 clialvqqae vmlglvdarq aypltafalg tsfvccvlvr sgqgrrlaph dpslsmlqsv
      121 laatalgway aitgpargal lgllaplfll ggmfqlragq trvlmaywlv lvtgvilwrt
      181 sgdpprydpr vevihwafsl ivvtavaala irigrlrsrl arqkatltea lelsrklaeh
      241 daltgllnrr amgdlltlhw tvgaavqpqd grpgepatap mamammdidh fkqvndthgh
      301 avgdavlqrf aeiaqagvrg rdvlsrwgge eflllmpgtg qsgamrvler lrgqmerggf
      361 ealapglavt fsagvakrvp gephaatver adkalyrakh ngrnrfeag
//
LOCUS       WP_284402700             230 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Acidovorax sp.
            SUPP2825].
ACCESSION   WP_284402700
VERSION     WP_284402700.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..230
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=24565
     Region          5..183
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mplqrllepl ptgiegycld fdlesdgalp ldvlspaera rtsrflraad rrrfaetraa
       61 trrlladrld cgpaevplaq dahgkpfvdr sgevplfnvs hsgghaliav aepgavsvvg
      121 idieqcrggl didslaqtvl tdrervavar atdpqralyq cwvgkeavlk aigvgiaehl
      181 rcvgihpgrd grwsvestvp qwsgleamal aappgyvaal awrsklpapv
//
LOCUS       WP_284402680             756 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: RelA/SpoT family protein [unclassified Acidovorax].
ACCESSION   WP_284402680
VERSION     WP_284402680.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 756)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 756)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 756)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 756)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..756
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=83491
     Region          45..752
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mnavlnkpsa qdprpgesga aggtsaaaan aaaasfaalt enlgyldaas ieqvrqayrf
       61 adeahlgqlr nsgepyithp iavaaqcatw kldgqalmaa llhdamedcg vtksdlidrf
      121 glpvaelvdg ltkldklqfn treenqaesf rkmllamard vrviliklad rthnmrtlsd
      181 mprskwgris setleiyapi ahrlglnqty relqdlsfrh lhpwryatls kavnksrnrr
      241 rdivqrvqte vdtafsklgm karlagrekt lyaiyqkmdt khlsfaqvtd iygfrvivpt
      301 vvdcytalgv lhqmykpvpg rfkdhiaiak lngyqslhtt lvgpsgvnie fqmrteemhv
      361 vaeagvaahw lykaqdadgs aaerlgtkwl qslldiqnet rdaaefwdhv kvdlfpdavy
      421 vftpksqima lprgatvvdf ayaihsnvgd rttaakinne qvplrtelkn gdvveiitap
      481 vstpnpawlg fvrtgrarsk irhylktlah tesaglgekl ltqalraegl erlptesenq
      541 alwdkllrft gnrtrnelmt diglgkriag ivakrlmvlm tehghrpdal lltreryssh
      601 etlsqggvtl dgsenasvqy anccrpvpgd pivgylgrge glvvhnaqcs vakklqhkds
      661 erfiavdwad eptrmfetgi vvtvangkgv lariaaelas seadivhvdm ddeaamdttd
      721 lrfviaardq shveaslrnl rrtpavlraf rvlpqg
//
LOCUS       WP_284402641             313 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family oxidoreductase [Acidovorax sp. SUPP2825].
ACCESSION   WP_284402641
VERSION     WP_284402641.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Blankenfeldt,W., Kerr,I.D., Giraud,M.F., McMiken,H.J., Leonard,G.,
            Whitfield,C., Messner,P., Graninger,M. and Naismith,J.H.
  TITLE     Variation on a theme of SDR. dTDP-6-deoxy-L- lyxo-4-hexulose
            reductase (RmlD) shows a new Mg2+-dependent dimerization mode
  JOURNAL   Structure 10 (6), 773-786 (2002)
   PUBMED   12057193
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437758
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..313
                     /product="SDR family oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009226 - nucleotide-sugar biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0019305 - dTDP-rhamnose biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=34886
     Region          19..304
                     /region_name="RfbD"
                     /note="dTDP-4-dehydrorhamnose reductase [Cell
                     wall/membrane/envelope biogenesis]; COG1091"
                     /db_xref="CDD:440708"
ORIGIN      
        1 mrgddlrefn elsaleglri litgaggmlg qafarhlaqq vptalvaald rhafdvrqre
       61 qaqalrawrp divihcavcs dvnwcedhad aaaqvqiegt rhvvelarec rarffypqtf
      121 liydgsqtvd eatpprplsv ygrlkleaeq ivleaspqal tvrmggffge hardknfvgk
      181 liphlagllr sgvdrmeigd riwqptltdd laynslllla rgeagrfcma shgqasffel
      241 areivlrlgl drrieiarvp aesmarkeka vrpdavvmrn aalqargldr qrtwqdslaa
      301 yldhpyftgm fap
//
LOCUS       WP_284402748             334 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284402748
VERSION     WP_284402748.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..334
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=35506
     Region          7..332
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mgiqynrrnl lqelaalggt sllgqaaaqt gkaawptkpi rlivpfnagg atdiiartvg
       61 ealakrvgqp vvvdnrggaa gilgtdavtk aapdghtllv slstsmlinq flytklpydp
      121 qkditpitqi aaapvtlvvh psvpasnmke llayvkahkg klsygswgvg syahlagaym
      181 sktmdadmth vaykgeapmi qeliggqlql cfssalntkp fidagrlkai gvtgkqrmdi
      241 lptlpsiyeq gvpddayaif gwvamgapag lpkeivdqly ghlreiakdp kvlertvgag
      301 fmplmnspea frenyqrdmp vwkalvdeag akld
//
LOCUS       WP_284402877             701 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Acidovorax sp. SUPP2825].
ACCESSION   WP_284402877
VERSION     WP_284402877.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 701)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 701)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..701
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=75177
     Region          24..701
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mraalqgrtl fgralvsrha fsgeearall vgepnvamvl ldvasepvgg avaaagtpla
       61 lvdfirhtar lpnarivlrt gqpgpvmdld tllqydindy rpkselthdr llalvvtsvr
      121 syqrlcaaea srrslelivr ssasllettd prafasgvit qlaallgvac halvcaqqge
      181 tadrfqvlaa agrfagladg pfdavaarpe wgvlrrvleg rgngyaadgg valhighqgr
      241 qgmavfidvp aargaldtqm ldvfcanlgt llhnhgllar lheyayydpl vrlpnrahfv
      301 ekvdecarlg trghilalld iddfsatndv mghrfgdcll ervaralsaa lppgvllarl
      361 gadtfgvlga vaqvslqrll dcvrqplavn gvaqkvsltc gyvflpevpq agadlvkdat
      421 ialkrakrdh rgqhleysdh mgaeartral llsdlraaid taklflvyqp qidlatrrlv
      481 glealvrwra ddgqlispdq fipvaehsgl ivalgkwvls tacacmrell aaghapgrma
      541 vnvssvqlqd paffdtvcaa ladsglkgpq leleitesva alptqllnst lsslraqgis
      601 iaiddfgtgy sslsylerla ldrikidrsf vrhlgephgv riaemvaqlg rklglqvlae
      661 giedaaalra lldmgchegq gyhiampmek galmawlqqr r
//
LOCUS       WP_284402984             327 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2825].
ACCESSION   WP_284402984
VERSION     WP_284402984.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2825
  ORGANISM  Acidovorax sp. SUPP2825
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Acidovorax sp. SUPP2825"
                     /db_xref="taxon:2920879"
     Protein         1..327
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34071
     Region          1..325
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mnrkklllsa vicalgvasw apamaqeapf ptkpitlvip fppggatdvl grligkkmgd
       61 llgqsvvidn ragagttiga ayaakatpdg ytllmssgtt ftvnpavrpk lpydpvksfe
      121 pigiagrtsl illankdvpa advkqfvalv kaapdkysyg sfgagttsqf agemffhaag
      181 lkiqhvpykg sapamtdlmg gqipftvdtv saalpqlkdg kikaiavtag krsallpkvp
      241 tlvesgypgl emdtwlamva prglppavks rleltlaqvv sdpetrdkmi avgfepayas
      301 sktvaelidr elplmraiaq ragitad
//
LOCUS       WP_284403070             747 aa            linear   BCT 25-DEC-2024
DEFINITION  T6SS phospholipase effector Tle1-like catalytic domain-containing
            protein [Pseudomonas syringae].
ACCESSION   WP_284403070
VERSION     WP_284403070.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 747)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 747)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10561933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..747
                     /product="T6SS phospholipase effector Tle1-like catalytic
                     domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=81667
     Region          41..371
                     /region_name="DUF2235"
                     /note="Uncharacterized alpha/beta hydrolase domain
                     (DUF2235); pfam09994"
                     /db_xref="CDD:462937"
ORIGIN      
        1 mqvqqnihrh gqaerdyqda lclaagrrvl ppccktlhis lffdgtgnnl nndlyapgtp
       61 hptniarlfr atigdghagg tahrgeasrl tdvagtgygq yfkyympgvg tpfaevgdld
      121 ystvglagaw fgeerinwgl lmlvdalrrt lglpqldnas llaavqamgt wpglgfvngq
      181 anraavfskq lkaieqplrf altqpghgtp rllglklyvy gfsrgataar afvswlnelm
      241 ryqpflaldd lqiplsveyl glldtvasvg fadimpgadg hmawadgnqe lpggglvkrc
      301 lhlaasfeqr lcfplesirr esgsypvnsl eviypgvhsd lgggyppgdq gkafsqdnve
      361 gdglllsqia lndlyadafv hgaplkvpre slpiglrhee wramefdvvk gfdvalpvvn
      421 rfnawrqmtl glppvshpls ieqiehyqpl tsattleqaa rtqlgwitaw ridryafasl
      481 kqatfylqas dteadetvrd qakaarnnnq aavkkrrlqq laierngrta kkplepgvkd
      541 fdadmaqtql reaavefaaa yrdpdhqasm lsqvtpanap pvavyriita darvecrqmk
      601 aagqarvsql fappagrynh pdektrgavd eignatqppg llralfddqv hdsrawflys
      661 lgrepmgsyf rermvffgea srrelalnpe tretmvagit plpdsglsva arpavmdaqr
      721 maeaqqaika lweaqypkas gvsdals
//
LOCUS       WP_284403202             340 aa            linear   BCT 25-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Pseudomonas
            syringae].
ACCESSION   WP_284403202
VERSION     WP_284403202.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Rengstl,B., Oster,U., Stengel,A. and Nickelsen,J.
  TITLE     An intermediate membrane subfraction in cyanobacteria is involved
            in an assembly network for Photosystem II biogenesis
  JOURNAL   J Biol Chem 286 (24), 21944-21951 (2011)
   PUBMED   21531723
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Komenda,J., Nickelsen,J., Tichy,M., Prasil,O., Eichacker,L.A. and
            Nixon,P.J.
  TITLE     The cyanobacterial homologue of HCF136/YCF48 is a component of an
            early photosystem II assembly complex and is important for both the
            efficient assembly and repair of photosystem II in Synechocystis
            sp. PCC 6803
  JOURNAL   J Biol Chem 283 (33), 22390-22399 (2008)
   PUBMED   18550538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..340
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=36236
     Region          58..251
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          190..327
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
ORIGIN      
        1 mrepfhwrtr lctgmslaif tccsfadsap vaaadtaaya iesakasrgl lldvahagar
       61 lvavgdhghi lysddqgktw gqarvptrql ltavffvdeq hgwavghdaq ilassdggks
      121 wdkqfedlkr eaplldvwfk dlnngfaiga ygallntsdg gqhwqdvsdr ldnedqyhln
      181 giaqikdagl fivgeagsmf rssdegqtwe klegpyqgsl fgvvgtaqpa sllayglrgn
      241 lfrssdfgdt wqpielngar gpvefglasa tllsdgtlvl vgnggsvmrs tddgqtfevf
      301 nrpdrislag vtanlqgnli lvgqggvrvt sptgaettqq
//
LOCUS       WP_284403205             572 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Pseudomonas syringae].
ACCESSION   WP_284403205
VERSION     WP_284403205.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..572
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=63438
     Region          106..200
                     /region_name="VWA_2"
                     /note="von Willebrand factor type A domain; pfam13519"
                     /db_xref="CDD:463909"
     Region          326..>454
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          403..433
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <417..>525
                     /region_name="MDN1"
                     /note="Midasin, AAA ATPase with vWA domain, involved in
                     ribosome maturation [Translation, ribosomal structure and
                     biogenesis]; COG5271"
                     /db_xref="CDD:444083"
ORIGIN      
        1 miaalwphwf rpqwllilpl lalliwrlwh rqkragrwqm llpthfhavl lnggrgsnsk
       61 lpwlalglaw llalfallgp swqrveqisq kpvdplvvil eltpqmlatd tpptrleqar
      121 rklldllqkr sdaqtaivvy agsahtlvpl sddlvtshnl ldairpsimp mtgqradlav
      181 hkaltllkqg algqgrilll tsslseqerq girealrgqs ppllilgigt aegapvtqen
      241 gsllkddqga ilvprrdsas lndfadqvgg syrqargdee dlrslgllas pqhvrsdghl
      301 vqlntwadqg hwlllpllli aalagrrgwl fclpllfmfp qnsqafefqd lwlrpdqqgq
      361 rlleqhrpae aaqrfddvrw kgvalyeaqd yasaaqqfaq gnsatdhynr gnalvrsgel
      421 eaaldayeqa ldrqpefpaa qanralvqgv ldqakvqkpa qdeqnkadqg eegqqasqdp
      481 nssaspaden psrtdqpgts eslppdtsgq aasgsamdde httrpptpga dspitgerrq
      541 eleqwlrqip ddpgellrrk fryeqqhqek tr
//
LOCUS       WP_284403216             784 aa            linear   BCT 25-DEC-2024
DEFINITION  T6SS phospholipase effector Tle1-like catalytic domain-containing
            protein [Pseudomonas syringae].
ACCESSION   WP_284403216
VERSION     WP_284403216.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 784)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 784)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 784)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10561933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..784
                     /product="T6SS phospholipase effector Tle1-like catalytic
                     domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=86894
     Region          69..361
                     /region_name="DUF2235"
                     /note="Uncharacterized alpha/beta hydrolase domain
                     (DUF2235); pfam09994"
                     /db_xref="CDD:462937"
ORIGIN      
        1 msemnnnskd kawgppvfpa ggrfptktsd vtknynkqda eqnafqqerd dqgrrtqrft
       61 ccyslhislf fdgtnnneks dtqdghptni aklfhaslrg teaneqgyfs yympgvgtpf
      121 peigemdysd gglqfatgge drinwalvsl adalhmaltq pktplsqarr agaveamstw
      181 ktpmmsalge gnrrrimkel laplqgrkaq pkvlsvklyv ygfsrgaaea rtfvtwlsql
      241 fdtpegaelp kqellglpvs veflgvldtv asvgiahaap ffaghmdwad dtqllpdarr
      301 fpnlvkccrh fvagfeqrsc fpldsirnen gqypantyev vypgvhsdvg ggypqndqgk
      361 aregthelvs qivlhdlyaa afaagaplqv peevlpdtfn nssekfwrtl sestntdfkv
      421 nprvverfna wrlktlpgva advsvedsay gplrlnttve dtladqlgwi tgwrigryvn
      481 dpqgdndsyk rqpfftgane vsaydegeqr knyeskqqev vknrlnnrea amnypgpriy
      541 epqidktqlk qaaeefksdy tgqkrkqtsw qgtvtdvvlr davfllnend eskdydalkt
      601 agdqrskqlf rdargtssad pdmallvalf ddqihdsraw fmhdtlksre lwagyffyrm
      661 tyfgndnsrd lspvvvagrl lgvamiagat vygikrrgvl ggvgglaagm gaatigyqvi
      721 dkasgmalpf lpgaeqllqp tshvgqvaae lkrqieqddf arrmerttam lrqagslfes
      781 gvta
//
LOCUS       WP_284403238             678 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pseudomonas syringae].
ACCESSION   WP_284403238
VERSION     WP_284403238.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 678)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..678
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75748
     Region          162..668
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mplrqrlenl pvgqkllaal lvlmttvllv anltfigaay yisqeamapq alqtigrlis
       61 sanlneraly sptearallk elksygplra aalydndger leqmqqgqsl elprhfkdld
      121 swrltefrst qvitvpkgde ppghlllvas selppafytg tltaslgilv fsvllwlvva
      181 rqirrlitep iyqleelsrq vtreenyalr aepgnvdeig slaeafntml srieareqql
      241 krarddsqea ydqaqglaee trhtnrklel evqvrskiek kltgfqnyln siidsmpsam
      301 ialdeqlyvt qwnqeatals gttldealnq piflafepmr sflpqikhtv erhsvtkier
      361 vnwikndear hyaltfyplt gdagrgvvir idditqrisl eemmvqsekm lsvgglaagm
      421 aheinnplga ilhnvqnirr rlspelpkni eqaeadgidl aqvnlylesr evpklldgiq
      481 qagaraakiv shmlnfsrls srqlspsdlp alvdqaveia sndfdltigf dfqgqhiirq
      541 fdpelgpvpc ianeleqvll nllknaaqai hqrpeseepg riilrtrlnp pwaeiqvedn
      601 gigmsesvrk rtfepffttk eigqgtglgl svsyfiitnn hkgqmevqss lgtgtcftlr
      661 lplvanqvnv qqqvisks
//
LOCUS       WP_284403266             181 aa            linear   BCT 25-DEC-2024
DEFINITION  1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase [Pseudomonas
            syringae].
ACCESSION   WP_284403266
VERSION     WP_284403266.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Ju,T., Goldsmith,R.B., Chai,S.C., Maroney,M.J., Pochapsky,S.S. and
            Pochapsky,T.C.
  TITLE     One protein, two enzymes revisited: a structural entropy switch
            interconverts the two isoforms of acireductone dioxygenase
  JOURNAL   J Mol Biol 363 (4), 823-834 (2006)
   PUBMED   16989860
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Dai,Y., Wensink,P.C. and Abeles,R.H.
  TITLE     One protein, two enzymes
  JOURNAL   J Biol Chem 274 (3), 1193-1195 (1999)
   PUBMED   9880484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..181
                     /product="1,2-dihydroxy-3-keto-5-methylthiopentene
                     dioxygenase"
                     /EC_number="1.13.11.53"
                     /EC_number="1.13.11.54"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0010308 - acireductone dioxygenase
                     (Ni2+-requiring) activity [Evidence IEA]"
                     /GO_function="GO:0010309 - acireductone dioxygenase
                     [iron(II)-requiring] activity [Evidence IEA]"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /GO_process="GO:0019509 - L-methionine salvage from
                     methylthioadenosine [Evidence IEA]"
                     /calculated_mol_wt=20347
     Region          1..181
                     /region_name="Adi1"
                     /note="Acireductone dioxygenase (methionine salvage),
                     cupin superfamily [Amino acid transport and metabolism];
                     COG1791"
                     /db_xref="CDD:441396"
ORIGIN      
        1 msslsvyhvs spdvpnkvlt hlediastla ehgvafdrwe aatpitpgas qqevinayrt
       61 qidtlmtrhg yvtvdvisln sdhpqktelr akfleehrhg edevrffvag rglftlhidd
      121 yvyavlcekn dlisvptgtr hwfdmgenph fvairlfnnp dgwvanftge diagrfprle
      181 d
//
LOCUS       WP_284403300             784 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pseudomonas syringae].
ACCESSION   WP_284403300
VERSION     WP_284403300.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 784)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 784)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 784)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 784)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..784
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=85341
     Region          131..772
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mklkvsfqar iagvlialll ivvgavflav kvatgdavrt qaqaqlevgs rvferlidlr
       61 gkrlrdavql lsadfgfrda vasadsstir svllnhgkri nasdmfllgm dgvviastet
      121 qvpegsrfiy dqalrgakra gqsvlivpgg gtphllvest vlaplpigrv vmgftidsdi
      181 aeelrslsgl evsfltveng lsgdlistqp pamhaglvel mrsssegqml lteqsnlnfl
      241 sqtlmlaksd nggdgqvial lqspldkayq afapldekif wismaallas ligtlalars
      301 vslpvralat aakrigdgdy etpvtmarsd elgmladain tmqhgiavre gqlahnalhd
      361 nmtglpnral vmerlgssia adrpvallym gienlktise sssaegvdql lrqvgqrlqg
      421 nsrpgdtvar lsanefllll dnttsdgavg iadallrlls epqridnhdy aleccigitv
      481 ypehgdsaqe lvnraaiark daafipgrlq iyqdgrdlah qrqiclirdl rkapqngelm
      541 lhyqpkldir qsyvrqaeal lrwthprfgn vspaefivla ertgsinllt nwvieeamrq
      601 laewrqrglv lqvsvnisad dllgddlagy vmkllkqygv paeqlvfeit esavmsepek
      661 alivlhrlrd cgislsvddf gtgysslahl krlpvqelki dqsfvrnlde tsedavivrs
      721 tiemshnlgl kvvaegveyq hsldllrrwh cdtaqgylis rpltaaafea wittfqtsps
      781 lmvn
//
LOCUS       WP_284403316             385 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Pseudomonas
            syringae].
ACCESSION   WP_284403316
VERSION     WP_284403316.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..385
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=44365
     Region          6..376
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mngaifpwre nsrfqllidg paffprmiaa idraeqqvdl elylveagac adavvralve
       61 agrrgvivrc lfddfgskaf daglrkqltd agvilrfynp ihwrrgvrnf yrdhrkilvv
      121 dkaqavvggt gvtdefwepd kevsqwhevm veitgplvld wqalfdrqfh anarrfawrp
      181 kqnfgldhlp kapvageglg rvayadsrqh rdilqslvrt lhsgqkriwl atpyflptwk
      241 vrralrsaaa rgvdvrlllt gprtdhpsvr yaghryyprl lragvkvfey qpcflhlkmv
      301 liddwvsigs cnfdhwnlhf nleanleahd pgltrdvvas fekdfalsae itledwkarp
      361 lwrrvkqrlw gwidrlvvnl ldqrn
//
LOCUS       WP_284403335             306 aa            linear   BCT 25-DEC-2024
DEFINITION  class II glutamine amidotransferase [Pseudomonas syringae].
ACCESSION   WP_284403335
VERSION     WP_284403335.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Zalkin,H. and Smith,J.L.
  TITLE     Enzymes utilizing glutamine as an amide donor
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 72, 87-144 (1998)
   PUBMED   9559052
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Zalkin,H.
  TITLE     The amidotransferases
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 66, 203-309 (1993)
   PUBMED   8430515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..306
                     /product="class II glutamine amidotransferase"
                     /EC_number="2.4.2.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006541 - glutamine metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33297
     Region          2..296
                     /region_name="GlxB"
                     /note="Glutamine amidotransferases class-II
                     (Gn-AT)_GlxB-type. GlxB is a glutamine
                     amidotransferase-like protein of unknown function found in
                     bacteria and archaea. GlxB has a structural fold similar
                     to that of other class II glutamine amidotransferases...;
                     cd01907"
                     /db_xref="CDD:238888"
     Site            order(2,150..151,176..177,201)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238888"
ORIGIN      
        1 mcgivglylk npalesqlgk lfepmleamt drgpdsagfa iygdevadgw vkltlqatte
       61 hydfraliaa legtlnvpld wfqnasavvl kiqaeeapvr aalaelapsv rimsagqsie
      121 ilkgmglpre istrfglasm kgshiightr matesavtme gshpfstgsd lclvhngsls
      181 nhfrlrqnlr regihfetdn dtevaagyla wrlqqgdslk qaldksledl dgfftfaigt
      241 rngfavirdp iackpailae tddyvamase yqalsslpgi enarvwepvp atmyiwerep
      301 vegarp
//
LOCUS       WP_284403337             509 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Pseudomonas
            syringae].
ACCESSION   WP_284403337
VERSION     WP_284403337.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..509
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=56130
     Region          <201..496
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mtspfnalpd plsyaqtlvs yysilsqade rrpllegfvr aaaelsgges sqlflldskh
       61 kclglaaqiv egvirscask asregyrdlp llqfsllqnr ivsipeisss pyatdclpvq
      121 eyawqsllci plpsrdsipv gllvcasrqc rpldgyadsl salgsfvisq lgllalpdkp
      181 dsaapyprrp aakpaqfglt gnsaalgrtt hllgkvldst ctilltgetg tgkevvsral
      241 heygprrlna fvvqncaafp ealleselfg yrkgaftgad rdrrglfdta hggtllldei
      301 gdmpmllqak llrvlqegei rplgsnevrk vdvriiaath rdlpkliaeg rfredlyyrl
      361 aqfpielppl rkrvedieil arhfsdmacr qsqkepvqws eaalsvlsgy afpgnirelk
      421 gfveravllc ednklrpehf piasdsvshp vcltlrehie qfergvlmec lrdsngnrsr
      481 aartlgvsrr tllyrlahlk mgathekrd
//
LOCUS       WP_284403462             663 aa            linear   BCT 25-DEC-2024
DEFINITION  GumC family protein [Pseudomonas syringae].
ACCESSION   WP_284403462
VERSION     WP_284403462.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 663)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..663
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=74320
     Region          6..656
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 minirsfrdl lrlffifkrd vkitvlatfv iillgafllp nryestalll vkpgrdsstv
       61 pielsdrqai vipsglrdpl ldeermltgr pimravseky laelsmappe tgvlasikng
      121 ikavvgavad gvrsvlqfig lvenrsqsdr laedleknfk vshepgssvm elrftwndpa
      181 taqtvlktwi eeyqlqrtkt lgrvslyafy esevkstgdn iieykkqiqn ylnqlsavsi
      241 sqrladtsqg lndlrternn ttrsiastka gldllkkqla eqpktvsagr elalnpnrqd
      301 lqtringkev erqemlrsfk eqappirain eeidnlkkll ngqdatvqrs esitpnpiyn
      361 rmqnvyadqq tsyarlqtqf aqqnvqiaql etdrqqalnl epelsrlqne ldaaeksyal
      421 ykdsleksri dreldnsqis niatieeatf npsrvfpksl lmlllalpls fvvgalalyf
      481 fylldqrihd gdkiessfgv pvwtslpdle raqersaaft snlhrvygil pldqveergl
      541 tlgftsvksg agvsfvierl stllaeqghr vrsqgpgpas pgeivlinas alsanqdafv
      601 llrkaelivl vvraedttvp mledtlhnln tafkkvdgii inrrrfevpe qvlrflkrig
      661 srg
//
LOCUS       WP_284403477             357 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Pseudomonas syringae].
ACCESSION   WP_284403477
VERSION     WP_284403477.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..357
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40523
     Region          1..350
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mkmislqylr gfaallvvvg hnsffldgdw ighipallgv diffivsgfi mtlityqsse
       61 rpisfmirrl friwpaffvv wlmsylfvyp eralgemvcs lyfclqdysl vapsfgfsvl
      121 gppwtltyev vfyliftism sisyryrsyv calvflvssv gfqlyynghf yfssqsspdi
      181 vvvhvwqvwi klisntitfe fiagmmlael mlanrlpdls lagrrlmqlt lllaiisaci
      241 mgwqdygisg gfwlaliivv svvmlsyrse vegnkplvfl gdisyslylv hyslmmllik
      301 vipgnapfve ragvfilsia asivlaffmf ewvekpfika gkkvagvlsg wqkfsmr
//
LOCUS       WP_284403486             446 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Pseudomonas
            syringae].
ACCESSION   WP_284403486
VERSION     WP_284403486.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..446
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=49935
     Region          3..444
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 msprqkiliv ddepdirell eitlgrmkld trsarnvaea hdwlarepfd mcltdmrlpd
       61 gnglelvqhi qhgyphvpva mitahgnldt aihalkagaf dfltkpvdln rlrelvnsal
      121 slpcatqpvr sidsrllgds ppmrnlrnqi gklarsqapi yisgesgsgk elvarliheq
      181 gprinkpfvp vncgaipsel meseffghrk gsfsgahedk pglfqaahng tlfldevadl
      241 plamqvkllr aiqeksirsv ggqqeqvvdv rilcathkdl nvevaagrfr qdlyyrlnvi
      301 elrvpslrer redidqiaas vlrrlagnst qpvvrlhaqa letlksyrfp gnvrelenml
      361 eraytlcend eihasdlrla esaspqaqqg anladidnle dylesierkl ilqaleetrw
      421 nrtaaaerls lsfrslryrl kklgld
//
LOCUS       WP_284403548             319 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284403548
VERSION     WP_284403548.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..319
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=32674
     Region          29..318
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mrrdtflksl aalaaagalp lsaraatavk mmlpanpggg wdttgralgr alqdagvass
       61 vtydnkggaa gaiglaqfvn sskgdpnalm vmgsvmvggi itgkppvnls qatpiarlts
      121 eynvfvlpas spfktmgdvi aqlkkdpgsv kwgggsrgst ehiaaamiar eagvdpakin
      181 yvafrgggea iaailggnvt iggggysema eyintkkmvp vavtsgqrlk gssvptlkeq
      241 ginveignwr gvyaapgisa eqrkglvdmv akalkskswa eslekndwtp awlagdefga
      301 fvdaefaslr atmvktgmv
//
LOCUS       WP_284403653             207 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Pseudomonas syringae].
ACCESSION   WP_284403653
VERSION     WP_284403653.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..207
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23340
     Region          32..151
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mkldpqtlaq itattvshyn rvaddfregt rdhdvsqnid allrhiegsa pwqildfgcg
       61 pgrdlktfta mghvavgldg serfaemara etgcevfqqn fleldlpqgr fdgifanavl
      121 fhiprqelsr vlcelhttlk pggvlfssnp rgenqegwng erygayhdle twrqlltdag
      181 ftelehyyrp aglprdqqpw lasvwrr
//
LOCUS       WP_284403654             494 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Acidovorax sp. SUPP3434].
ACCESSION   WP_284403654
VERSION     WP_284403654.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..494
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53260
     Region          12..494
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mnaplptaat apasglewrn gfaalgpdff telvptplpa phwvatsgda aqqlgvpaaw
       61 lasdaalqvc sgnallsgmr platvysghq fgvwagqlgd graillgets ggqevqlkga
      121 grtpysrmgd gravlrssir eflcseamha lgvpttrala ltgspapvqr evvetaavvt
      181 rtapafirfg hfehfaardl lpqlrtlady vidryypecr gpdapggnpy aallqavser
      241 taellahwqa qgfchgvmnt dnmsilglti dygpfqflda fvpghvcnhs dtqgryafnr
      301 qpnvaywnlf rlgqallpli edvalaqaal asyqtvfpat flqrmrgklg lqaahdgdaa
      361 lvdgllnlla qggvdypifw rrlshavasg dfepvrdlfi dragweawll sfsertgqsn
      421 prhmadsmlk cnpkfvlrnh lgeqairaat qgdfaplhtl qallaepfde hpgheawadf
      481 ppdwassiei scss
//
LOCUS       WP_284403766             471 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Acidovorax sp.
            SUPP3434].
ACCESSION   WP_284403766
VERSION     WP_284403766.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..471
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51576
     Region          1..468
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mahalvvedd adsarmlasl lhtggftaat asslrdarrq ialqrpdivl ldlqlpdgng
       61 lslceevell sysevvlitg hasldtsiqa lrlgaadyli kpvdtrrlna vlsrarspst
      121 llaeiqdmrl qwestgrfgh llgrssimre vyeqiacvag tsvsvfvtge sgsgkelvar
      181 slhdlsrrrd gpflavncga ispqliesev fghergsftg adrqhlgffe ranggtlfld
      241 eitemplelq vkllrvletg tfmrvgstea rhtdvrivaa snrelaqavv dgalredlly
      301 rlnvfplhlp plrdrledlp llaqhflddi aareggrktl ttaaldrlae yrwpgnvrel
      361 rnvlqrafvm tqegpvterw lprdlvpsqp qpqlpiqpla pqqpevaapa ngaatptelr
      421 lplgsslaev eralilatfa hcgqrreqta amlgismktl ynrlkeygas a
//
LOCUS       WP_284403768             346 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Acidovorax sp. SUPP3434].
ACCESSION   WP_284403768
VERSION     WP_284403768.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 346)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 346)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..346
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=36973
     Region          <7..207
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mpqwlsmagv ghelrtplga lsaalevial tphpmhiqse acavaarqtr hlsslledlq
       61 dvlaaregrm elrrvavdfs elarqaweal vnsnggydct qqiapglrvm adprlmrrai
      121 dqllcracka gapgmrmdlt vstqggevrv evhglprddm grpsgtacpl nlhvrigapa
      181 tladlladhv iqlhggriap ladeegryla lpclaeappp parlrrqkvl valhdgqdrq
      241 aagqtlerqg ylvlegtamq paldlllqnv pdlvlasaqp aaaarhlata areagyagcm
      301 vavapamhse qealdtagar ragfdawaaw sdwpqvvtdm lesrsd
//
LOCUS       WP_284403816            1123 aa            linear   BCT 25-DEC-2024
DEFINITION  UvrD-helicase domain-containing protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284403816
VERSION     WP_284403816.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 1123)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437585
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1123
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..1123
                     /product="UvrD-helicase domain-containing protein"
                     /EC_number="3.1.11.5"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=122534
     Region          20..1097
                     /region_name="RecB"
                     /note="3#-5# helicase subunit RecB of the DNA repair
                     enzyme RecBCD (exonuclease V) [Replication, recombination
                     and repair]; COG1074"
                     /db_xref="CDD:440692"
ORIGIN      
        1 mtlaayehng rpvtreafya iacdpdrsva veacagagkt wmlvsrmlra lldgcaphei
       61 laitftrkaa gemrqrlqew leefaqaepe rlarelvarg ippdralekr allqtlyrsm
      121 lesgrpvqir tfhswfaall gtaplavlha rglpgnyell eddaeavrqv wppflqqvad
      181 daalhadyla avashgrsqt hkalgaalsk riefeladaa gvidasvppf haqfpdlqgl
      241 dspahalegd aararwlaha salgtesnkt pqkaadavvd afacedpher lerlrraffv
      301 akedrlsknl ekfavaqeae aelqrlclar rqheawghhh rmarltralv aafaalkrdr
      361 gwvdmndver talvmlsdpv lsgwvqerld arvrhllvde fqdtnplqwq alhawlsgyv
      421 gagggrapsv fivgdpkqsi yrfrraephv flaaqafvrq glggdllscd htrrnatgvi
      481 davnhvmqaa qgqgeyagfr dhttestdpg mrlrlpaita pddgagpafd pmawrdsltq
      541 prheaeetlr mrectqaarw vagriadgvp prevmvlark rdrlaamqda lrdlhlpcvq
      601 pekaelaeap evqdvvalld alvspghdls laralrsplf gvgddtlvrl alwrrqpenl
      661 ecswldlllk sehdalefiv lgadlalykg wfdalpphda lqafythrdv laryaaaapa
      721 tqrasvlanl rallsaalqi dggryltpya fvramkragq rapgrvdaqa vrlltvhgak
      781 gleahsvlll dtdtrpqkae tmgvlvdwpg eeplprrfvf lasestppps avdmlaaeqa
      841 erqreelntl yvamtrakhc lavssvqpss sapgswwnrl apllqdeden vlaepageal
      901 pqndrraqdh allaelpaws pppkpepdgp avlavavstp asrqgeamhq lleqaamata
      961 ggpapsgggw patrlarlaa dfdlapesaa laaemaqril ggqgawawqa davdravnea
     1021 tivhagqtlr idrlvrrtds ggasvwwvld yksaadperr phlmaqlary reavqaqmps
     1081 hvvraafltg dgrmvevgse tapppppppp pppppapvqg alf
//
LOCUS       WP_284403822             324 aa            linear   BCT 25-DEC-2024
DEFINITION  N5-glutamine methyltransferase family protein [Pseudomonas
            syringae].
ACCESSION   WP_284403822
VERSION     WP_284403822.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Schubert,H.L., Phillips,J.D. and Hill,C.P.
  TITLE     Structures along the catalytic pathway of PrmC/HemK, an
            N5-glutamine AdoMet-dependent methyltransferase
  JOURNAL   Biochemistry 42 (19), 5592-5599 (2003)
   PUBMED   12741815
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..324
                     /product="N5-glutamine methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=35228
     Region          <147..260
                     /region_name="RsmC"
                     /note="16S rRNA G1207 methylase RsmC [Translation,
                     ribosomal structure and biogenesis]; COG2813"
                     /db_xref="CDD:442062"
     Region          <245..298
                     /region_name="COG4309"
                     /note="SirA-like two-layered alpha/beta sandwich domain,
                     DUF2249 family [General function prediction only]"
                     /db_xref="CDD:443450"
ORIGIN      
        1 msvslpdvsl pgaslpdhaa lialaqrlkt ngyrfttptp lthqqvnqrp enrtaaslrd
       61 vfgwsrlipe tmlplaeaqg lleagilers edglksrvrf sslddlllmh safptldeds
      121 vffgpdtyrf aqsinrhlqs tshpikraad igcgtgagal liavarpdaq vyavdinpka
      181 lhfaqanaiv aglqnmecch sdilsgltgn fdlivanppy mkdakrrayr hggdalgadl
      241 svrivresld rltpggslvl ytgvamvgeh dpffeavrdd idhaalawty reldpdvfse
      301 elleegyedv driaavelvv trqg
//
LOCUS       WP_284403875             143 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Pseudomonas syringae].
ACCESSION   WP_284403875
VERSION     WP_284403875.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..143
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=15480
     Region          1..141
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mkfrrrrpre nidinlvsli dvvfilllff ivtttftret qlrvdlpqav tgtpevdaaa
       61 khldiainad gvfslnnqll pkndlatlid alqresagdt slplsisadg ktphqsvita
      121 mdaagklgfs hlrmttveat pan
//
LOCUS       WP_284404059             638 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Pseudomonas syringae].
ACCESSION   WP_284404059
VERSION     WP_284404059.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..638
                     /product="PhoX family protein"
                     /calculated_mol_wt=68930
     Region          21..632
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mklleenqtt dlenmvganr agltrrgfis agalcgaamf lggnilsrtv lansvsaasg
       61 vllgfesipt atadsislpk gytssvlisw gqplqadgpa fdpsgkgtaq aqevqfgdnn
      121 dgmclfpmqg hkdralmain neytnyrylf dhgkepqsae evqkalaaeg vsvievqqkn
      181 gkwqfvqdsr ynrrvhgntp inlsgpaagh dwlktdadks gthalgtfqn cssgqtpwgt
      241 yltceenftd cfgssnpeqk fdagmkrygv vaaskeinwh phdprfdvak npnevnrhgw
      301 vveidpfdpk stpvkrtalg rfkhenaaft qtkggravvy mgddergefi ykfisrdkid
      361 hqnpkanrdl ldhgtlyvaq fdagdsnpdh pkgkgqwiel thgkngldaa agfnnqaevl
      421 iharmaasvv katrmdrpew ivvspkdgqv yctltnnvkr gdegqpvggp npraknqygq
      481 ilrwseegsn asamafdwdl fvvagnpavh agtpqagssn inaqnmfnsp dglsfdeagr
      541 lwiqtdgdss nkgdfagmgn nqmlcadpas geirrflvgp vgceitgisf apdyktmfig
      601 iqhpgenggs tfpehlpngk prssvmvitr edggiiga
//
LOCUS       WP_284404060             373 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Acidovorax sp. SUPP3434].
ACCESSION   WP_284404060
VERSION     WP_284404060.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..373
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40689
     Region          142..370
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mrlaqfirqa reeilaesfa yatqipalqg saasvlrnhl plvlntiald leqpqsreqs
       61 idkslghaap paeesaaqsh gtlrarigld ieqlvaeyrv irscvlrlwt eacepnefvi
      121 qdtvrfneai dqavaesvaf haaeiakwrh iflgvlghdl rgplnammlt aellervesk
      181 sngqamylvg allrngrrln alldslleyn katlgvgmql nreavdlgae cqeefemlqq
      241 afpkrqiqlq itgdtrgafd rsrvrqavsn lvsnaaqhsp egsavavivv gqetaveitt
      301 envadpipqd vlntlfdplr rnaseagass ghlglglfiv reiarahqge vtattadgvi
      361 rfrmvlpksp rta
//
LOCUS       WP_284404098             146 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Pseudomonas syringae].
ACCESSION   WP_284404098
VERSION     WP_284404098.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..146
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16503
     Site            order(20..21,23,50,53..54,61..62,64..65,90,93..94,97..98,
                     101)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          21..>106
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Region          48..84
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mldlddelye kisemsdlgn sfmddgeypr alktfeeale llpaprntwe aytwlkagia
       61 dalfsvkdye rateelydam ngpdgasnpf illrlgqsly eqskpegidf lckaymlege
      121 eifseedgky lalvkdrlat nqsqlh
//
LOCUS       WP_284404192             712 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Acidovorax sp. SUPP3434].
ACCESSION   WP_284404192
VERSION     WP_284404192.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 712)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 712)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..712
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77077
     Region          62..712
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mkpvlraraa alpfalaaay pglcahaqte gsaapatlsp vtvtedrgva tplvlpstag
       61 srleltpfet pasvaivpge liralgttsv idaktlapgm ssanspgngg nvlsargftg
      121 vnsvkqlyng lelsnaggvv sfpfdpwnve riealygpas vlygagaigg avnvvskrpd
      181 paqasheigl gvgsdnarhe afsstgpmgn glsyrvdlsh rsadnwvdrg asdtlaasas
      241 lrydlspqln filaadygrq kpmhylgtpv fngapvpgte tlnyniadsd lffqdqwttl
      301 dtewkpsadv tvhntlyrlt hnrryrdatv ftylpatasv rrssyrdisy srqtqegvnt
      361 yarfqgriag mknaflagfq lersfynrfd nvrggtstvd alhpvpglyr dawrgesipm
      421 yyldldrvgv ffenhltlsq rwsvvaglrs dsyrteredr qlrnttrgkv sgtsgslgvv
      481 fnpvpevaly gqiataqdpv tslasiganq qgfglsqgrq iefglkqslw ggrfdwtlaa
      541 yhlvkkdllt anlanptlqe qvgqqssrgi easasvrlga wrvevngtvl dpkfddfqaq
      601 vgsgtqqlag kvpmtvpkrs anlsafwdfa prwtartalq yvgqrfvnnt ntaslpsytv
      661 vqagvnwram pgmtldlrve nlfdkryatq gsevqwilgr prtvwltgth af
//
LOCUS       WP_284404295             772 aa            linear   BCT 25-DEC-2024
DEFINITION  T6SS phospholipase effector Tle1-like catalytic domain-containing
            protein [Pseudomonas syringae].
ACCESSION   WP_284404295
VERSION     WP_284404295.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 772)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 772)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 772)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10561933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..772
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..772
                     /product="T6SS phospholipase effector Tle1-like catalytic
                     domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=84611
     Region          67..396
                     /region_name="DUF2235"
                     /note="Uncharacterized alpha/beta hydrolase domain
                     (DUF2235); pfam09994"
                     /db_xref="CDD:462937"
ORIGIN      
        1 mpeikhanvw ypppfplqgr lpsravqvqq nihrhgqaer dyqdalclaa grrvlppcck
       61 tlhismffdg tgnnlnndly apgtphptni arlfratigd ghaggtahrg easrltdaag
      121 tgygqyfkyy mpgvgtpfae vgdldystvg lagawfgeer inwgllmlvd alrrtlglpr
      181 ldnasllaav qamgtwpglg fvngqanrae vfskqlkaie qplrfaltqp ghgtprllgl
      241 klyvygfsrg aaaarafvnw lnelmryqpf lalddlqipl sveylglldt vasvgfadim
      301 pgadghmawa dgnqelpggg lvkrclhlaa sfeqrlcfpl esirresgsy pvnsveviyp
      361 gvhsdlgggy ppgdqgkafs qdnvegdgll lsqialndly adafvhgapl kvpreslpig
      421 lrheewrame fdvvkgfdva lpvvnrfnaw rqmtlglppv shplsieqie hyqpltstit
      481 leqaartqlg witawridry afaslkqatf ylqasdtead etardqakta rnnnqaavkk
      541 rrlqqlaier ngrtakkple pgvkdfdadm aqtqlreaav efaaayrdpd hlasslsrvi
      601 panappvvvl riitadarve crqmkaagqa rvsqlfappa grynhpdekt rgavdeisna
      661 tqppgllral fddqvhdsra wflyslgrep mgsyfrermv ffgeasrrel alnpetretm
      721 vagitplpds glsvaarpav mdaqrmaeaq qaikalweaq ypkasgvsda ls
//
LOCUS       WP_284404397             493 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pseudomonas syringae].
ACCESSION   WP_284404397
VERSION     WP_284404397.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 493)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..493
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=54599
     Region          <63..478
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 myamdlpydp dfedaerwrf vltstafall smvvpfillk rlmqrlqtsy ndllvaqals
       61 dslarhdpls gllnrrvfne qlvarlqqes tqtavflidl dkfklindth ghavgdaaic
      121 avaeslrdat tgwqasvarl ggdefslavs gdfsqfelaa laenvlakia mssaglprvt
      181 lsatlgvais pldgsdaevl lqradsamyr gknggratfh fyevsfereq rlqevfvqel
      241 rhaieekhiq pfyqpivslp gqrlagfell arwlhsergi ilpmdfipva eqlglikqlt
      301 eslllqafdh ardwpsdftl sinvtslmie sldfpdwleq lasegrfpln rlevevtena
      361 lvanvdsarl nlerlramgv svalddfgtg ysglyhltkl aidkikidrs ffdtslnnqs
      421 emvkailalg kslrmkitae gvehedladw laahgcdfaq gylfgrplpf aqvtallams
      481 eragpvraqa nvv
//
LOCUS       WP_284404454             371 aa            linear   BCT 25-DEC-2024
DEFINITION  MDR/zinc-dependent alcohol dehydrogenase-like family protein
            [Pseudomonas syringae].
ACCESSION   WP_284404454
VERSION     WP_284404454.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Gonzalez-Duarte,R. and Albalat,R.
  TITLE     Merging protein, gene and genomic data: the evolution of the
            MDR-ADH family
  JOURNAL   Heredity (Edinb) 95 (3), 184-197 (2005)
   PUBMED   16121213
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..371
                     /product="MDR/zinc-dependent alcohol dehydrogenase-like
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40905
     Region          20..369
                     /region_name="Zn_ADH2"
                     /note="Alcohol dehydrogenases of the MDR family; cd08256"
                     /db_xref="CDD:176218"
     Site            order(56..58,61,177,181,201..206,225..226,230,253,
                     269..270,272,292..293,317..319)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176218"
     Site            order(56,87..88,177)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176218"
     Site            order(119,122,125,133)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176218"
ORIGIN      
        1 mstatertae qlspvipatm qavvcygped yrletvdvpt pgpdeiltkv elcgicmgdi
       61 ktyrgapsfw gdaeqpryvk ppmipghefv crvvalgpga ekrgvqigdr viseqivpcw
      121 gcrfcnhgqy wmcqkhdlyg fqnnvqgama qymiftkegi vhkvpdsiap deailiepla
      181 cslhaaeran vdfddivvva gagtlglgii gavrmrnpkk livldmkper aalalrmgad
      241 evwnpaevdv lakireitdg ygcdiyieat ghhkavnqgl amlrklgrfv efsvfndeat
      301 vdwsiigdrk eldvlgshlg pymypraidf ignrkidmrn vvthkfalad fkeafavmer
      361 gdkslkvvle p
//
LOCUS       WP_284404457             356 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Acidovorax sp. SUPP3434].
ACCESSION   WP_284404457
VERSION     WP_284404457.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..356
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36066
     Region          41..353
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtppgadart arrsavplri tlrraapwgi alalallvma sltagsapvs wreaaaalag
       61 pwagafgapa gdmaqaivrd lrlprvvlal lvgatlalvg gllqsttrnd ladpflfgls
      121 sgastgavav itltgewlga wtlpaatfag aavaagavll lvrraggqgp aqtvlaglav
      181 sflfgalthg lvfagdqraa havvfwslgg lglarwdnlw laclglavpm vfvwrrhral
      241 dallagddta hslgiaperl rtqafvvaav ataccvalag vigfvglmvp hlarrlsgpl
      301 haaflplagv mggalllasd lvartllgsq elpvgivtag igavfvmall rrrlad
//
LOCUS       WP_284404763             203 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Pseudomonas syringae].
ACCESSION   WP_284404763
VERSION     WP_284404763.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..203
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=22000
     Region          3..201
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 masgrqgavr agadgpvqwl ptllcgrpks rkdlvhqprs srpselllvv vdasastrrh
       61 ealsqakgll sqvfddayrr rarlalltas gstprwqhqg lkassalnpw ldalgagggt
      121 plsaalqqam twleqrqkrh paeqqrvlvm tdgrikqlpt lpafncasll idiekgpirl
      181 grarelaasl gadyrhidel klv
//
LOCUS       WP_284404863             248 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Acidovorax sp.
            SUPP3434].
ACCESSION   WP_284404863
VERSION     WP_284404863.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..248
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27796
     Region          26..244
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 malirsivhl lwmgitvvpy tllillvrlf gassrtryri arawlklstd aarvimgirt
       61 ritgmehlpt dptqgvvllv khqstyetfl mpaimprpla yvfkkellyv pffgwsigsl
      121 dmihidrgqr arafvkvlqq grallakgtw vimfpegtrv ergrkgqyks ggtrlaieag
      181 vpvvpiavts akvwprkavi krpgtvdvsi grpiptegrk pdelmrevea wiesemqrld
      241 peayapgr
//
LOCUS       WP_284404903             444 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF2345 domain-containing protein, partial [Pseudomonas syringae].
ACCESSION   WP_284404903
VERSION     WP_284404903.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         <1..444
                     /product="DUF2345 domain-containing protein"
     Region          <1..430
                     /region_name="COG4253"
                     /note="Uncharacterized conserved protein, DUF2345 family
                     [Function unknown]"
                     /db_xref="CDD:443395"
ORIGIN      
        1 ttraardrsf evgfeaipya ekvcfrpalq nkpqiagtvp arvtstrehd pyghidiegr
       61 ykvnflfdrd swkpgteslw lrlarpyagd thglhlplic gtevaiafeq gdpdrpyiah
      121 alhdsqhpdh vtlgkrdytr nvlrtpannk lrmedlrgqe hiklstehgg ksqlnlghlv
      181 daqkqmrgeg felrtdgwga irggkglfis adeqvraigd vltmepassq vqgakqqiad
      241 wqdiaqahrs rrpaidglqq fqdsakdlsa sailisapkg igavtpasll lksgdalyvq
      301 sndeinlaaa qrmslhanqa isllaqqegm rlvsgkgple ieshddvlnl iaqkditlqs
      361 vqghlqltak ngitlacggg yiritpagai dihtpgklnl kgqhvwettt sqsfpmpelp
      421 qsvcngclki aqaqaagaam rtad
//
LOCUS       WP_284404969             345 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284404969
VERSION     WP_284404969.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..345
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=38306
     Region          1..341
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mstqhrgnlf dlmricaasa vifshhfhit htasptwlhs nmvggvavmt fftisgylvt
       61 lswlrqpkal aflskrflri wpgvlfavlt nvflfgiffn smpaadflah pdtlgyfrnl
      121 llirdypylp gvfennpikh lmngplwtip ieslcylvla gagllgvfrh rwlaglaava
      181 yiaffltarn adlggemqhw feypayftyg aliavfrdaf harsgrmllm lapvaavlff
      241 gfqmehtagl lllppllihi gslnvpalaf lqrggdpsyg iylygcpvqq svyalwpdla
      301 fipslmlsva laavagyasw hlvespalrf krwfqrapva pqaap
//
LOCUS       WP_284404983             292 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Acidovorax sp. SUPP3434].
ACCESSION   WP_284404983
VERSION     WP_284404983.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 292)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..292
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=29973
     Region          <18..279
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mdgprsdlpd avgrvqadev vrlraeldaa rqeqeaflra vshdlrapvr hilaygrllr
       61 etvaesnadp eamqfldtia qagqqlggmi dgliqlgrig sapatpapva lgpvlqsava
      121 aartaaavap spksgaakap asseegsaga widavqwdlp aaeacpvlwa dagwlqevlv
      181 alldnalkfs rgaqppriav qvrpapgerv ditvqdngag fpaaqagqlf qvfqrlhpas
      241 qfeglglgla rcrrlvarmg gtigisaaph qgctvclqlp aagapgpdaa ag
//
LOCUS       WP_284404991             415 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284404991
VERSION     WP_284404991.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..415
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45318
     Region          13..406
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mtapdpsqdi dfplegvrvl dlsrvfagpl cgqvladfga evikvehpgr gddtrdwglr
       61 igktettyyn smnrnkrsit ldlqspeglq iirdllpqfd vvihnfktgg aeklglgyeq
      121 lkalrpgliy cavagydssg peakrpgydl viqgeaglma lngeatqppl kfgvavvdlm
      181 tgmyaaqavl aalfrrertg hgrliemaly dcgimvtgyy gldamqlgrd perygnahps
      241 ivpygmydaa dgpliiavgn naqfdkfcrq vierpdived prfstnvnra rnrvelgpll
      301 kalihafprd lllerltaag ipcgrvaglh ealtsertrr sgllrdmphp vvgttpvfap
      361 pyrmdgqrlp irsapptlge gtrevlhrll smsdaelqql qqrgvltlpd dsppa
//
LOCUS       WP_284405074             363 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Acidovorax sp.
            SUPP3434].
ACCESSION   WP_284405074
VERSION     WP_284405074.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..363
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39354
     Region          10..363
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mqfidlksqy qavkndidar ihkvldhgqy imgpevaeme qalaaytgal hciscasgte
       61 allmsllalg vgpgdevitt pftfaataet ivlagatpiy vdieadtcli dataieskit
      121 prtkaimpvs lygqvadmda inaiaaahgi aviedaaqsf gatykgrksc nlstigctsf
      181 fpskplgcyg dggalftndd alakilreir vhgqerryhh vrvgvggrmd tiqcavvlgk
      241 lqrfeweier rlklgemyre gltsagcnar llvvrpdrdc vwaqytlfve erekvqqqll
      301 aqgvptavhy plslnrqpaf rndvsaaeti kshwaaahvm slpmsadlqd sdidrvvaam
      361 ari
//
LOCUS       WP_284405010             479 aa            linear   BCT 25-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Acidovorax sp.
            SUPP3434].
ACCESSION   WP_284405010
VERSION     WP_284405010.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..479
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=50690
     Region          1..478
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mldllifggt vvdgsgaarr qadvgiaggr ilavgdlsaq parqrhdavg rivcpgfidv
       61 hthddrlllt spagphpklt qgvttvvtgn cgislaplls netppapldl lgaddwrydr
      121 fgdyldalea agpalnaacl vghstlrvrh vpdlrrpata peaermardl adaldsgafg
      181 lstglyyppa raataeevia vgaplsaaqg litmhirdea daiddalrea lhigqalgvs
      241 tvlshhklig qrnhgrsvnt lamvdtaals qpvcmdcypy nasstmllas rvgqsrevlv
      301 twsvgdpsaa gkslfalare rgcspeslve plspagavyf amheddvrri lghpltmvgs
      361 dglahdavph prlwgtfprv lghyardqrl fsletavhkm tglsarrfgl rdrglvaqdh
      421 aadivvfdet ciadratfeq ptapsagida vfingqlaca hghtvnahag qvlrrqrsf
//
LOCUS       WP_284405189             297 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Acidovorax sp. SUPP3434].
ACCESSION   WP_284405189
VERSION     WP_284405189.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..297
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31756
     Region          32..292
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 msretalplg daaarpgdag tqheyllrgh gpnagtgvll ihgltgtpne mrllakglhr
       61 agftvlavql aghcgtqddl vgtrwqdwha svqrgadrla mvtggrlvac glsmgavlal
      121 alaadrpaqv agvvalsptf rydgwsmpay trlsfllplf rllgigrhrv fmeqppygik
      181 daalrervva qmqsgdsaaa glpgnpwwsv iemralaahv rrrldavrsp clvlharhdd
      241 iasaanaqai vqgvryapve lvllddsyhm itidrerrav vartvafaeh iarggtp
//
LOCUS       WP_284405131             376 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Acidovorax sp.
            SUPP3434].
ACCESSION   WP_284405131
VERSION     WP_284405131.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..376
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=39993
     Region          34..374
                     /region_name="HisC"
                     /note="Histidinol-phosphate/aromatic aminotransferase or
                     cobyric acid decarboxylase [Amino acid transport and
                     metabolism]; COG0079"
                     /db_xref="CDD:439849"
ORIGIN      
        1 mtspatpaat ppsaldrirp dvramhaytv qpsagllkmd amenpfrlpa dlqaalgerl
       61 galalnrypg driadlkaal adyvgmpdgq tivlgngsde litllalaca qpgtgqratl
      121 lapmpgfvmy plsaqlqgld fvgvpltadf eldepamlaa iarhrpaity iaypnnptat
      181 lwdegavqri idaagaqggi vamdeayqpf asrtwidrmr aepgrnahvl lmrtlskfgl
      241 agvrlgylmg pralvaeidk vrppynvsvl nceaalfale hagvfaaqaa elrheraall
      301 aalrampgve kawdseanmv llrvadaart yegmkarkvl vknvstmhpl lanclrltvg
      361 naadnaqmla alqasl
//
LOCUS       WP_284405251             318 aa            linear   BCT 25-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284405251
VERSION     WP_284405251.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..318
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34976
     Region          16..286
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 msetspsrfd tsfgnlrirr vagslggevl glqlsgeldd atiadltaal vrhkvlffrg
       61 qthlddaahq afgarlgktv ahptvpsptg trifeldask gggradswht dvtfidafpk
      121 ygilrgvtip ayggdtvwan taaayarlpe dlqrladglw avhsndydyg aervvveeer
      181 lnhhrkvfvs svfeaehpvv hvhpvsgera lllghfvkki agfsstesar lfeilqnrvv
      241 rlentvrwqw qqddvaiwdn ratqhfaind ygtqarvvrr vtvhgepava vdgrrsrtrv
      301 rpeatndaqi dsvitata
//
LOCUS       WP_284405239             529 aa            linear   BCT 25-DEC-2024
DEFINITION  trypsin-like serine peptidase [Acidovorax sp. SUPP3434].
ACCESSION   WP_284405239
VERSION     WP_284405239.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..529
                     /product="trypsin-like serine peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=54981
     Region          268..453
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 makgkwmarg aalvvvaslv sgcggggggd sgavtvsaap sevlqvdsav qpagaedavs
       61 rtkqraagpr veparvalpa fvrpkaaqsr hdgarwvgda raieatatad glqrllqwtp
      121 langgmkaav sfasedaqgl rlgvrvrqip deavvrvyrq drpdavyett gqailqaigr
      181 niaagdasdn artwwtphsg aseatleiel pagvpaaald vavpalahlf enlslppega
      241 qaakavgdai acnldascfd eyapqrdava rmlfvdngka yvctgtllnd rdatrtpyfl
      301 sanhciasqt vastlqtdwf frsqacnsat lsprstartg gatllyasad tdtallrlne
      361 apppgavfaa wdagpqaest avvgihhprg dlqkistgsi mgtlactndt dgsmlcdsst
      421 dasagyydvg fdrgtvedgs sgsaifhggr vigtlygfas saqcsvddvr vygrfdlayq
      481 kglkqwlspp vsvpvawrhp argfgaphgp agrrgdgpap fwhewlaar
//
LOCUS       WP_284405304             568 aa            linear   BCT 25-DEC-2024
DEFINITION  two-component system sensor histidine kinase NtrB [Acidovorax sp.
            SUPP3434].
ACCESSION   WP_284405304
VERSION     WP_284405304.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 568)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 568)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 568)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 568)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..568
                     /product="two-component system sensor histidine kinase
                     NtrB"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009399 - nitrogen fixation [Evidence
                     IEA]"
                     /calculated_mol_wt=61598
     Region          200..526
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 mpalkrasal lsadapfarl wgsflsgrim vaaallllqg lgvalnqsye plllgicagy
       61 lvatvlllvl agnappgphs wlqwmcsigv dlalistlqi lhvgsmnftp lfglpilmag
      121 vlgtltlalg ttaavtllll awawwlgssg gsdatqryfq taltgtgyfi vaylvhqlas
      181 rlnreqqlaq asqmaakvqe qvsalvihnl sdgvlvldqr dtvrianpaa lrllgtnarh
      241 alpfsmahss pwkpllamar qtfqkgqpqs advdvlhpgq splalhvraw ltssqeiare
      301 tggehlcvmf lhdlremear lrteklasmg rmsaavahei rnplaaimqa nalleeelhe
      361 pgqkrlahmv qqnaerlari aeevldiarv qhqishapas tvvlcdavaq vwsdwqaqdp
      421 gkrraqlale anrapvefda ehlrrvlvnl ldnalrymgg epdslyvaty vgaagavalq
      481 vwsdgapldk tverhlfepf fssesrssgl glyicrelcq rhgasigyqr ltrnlprgav
      541 ggnaftvvfr knarpqdpnt tlfdtivv
//
LOCUS       WP_284405334             490 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284405334
VERSION     WP_284405334.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 490)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..490
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=54912
     Region          9..486
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mehtfssglv wfrrdlrsnd haalyhalrq caqvhcafvf dreildalpr adrrvefire
       61 slveldealr alsedphggl ivrhaiahqd ipalaqaldv qavfanhdde plalerdarv
      121 rgaldgmgkr lltfkdhsif eraevltqsg tpytvftpyk nawlrkaddf ylssypverh
      181 aarlaprpag lrrgvpslqs lgfeptgles lhlptgmqga qalfedflgr idhygeardf
      241 pavkgpsyls vhlrfgtlsp rvaaraaher srkgsaeaat wlseliwrdf yfqilahhph
      301 vagasfkpay daiewesgah akalfaawce grtgyplvda amaqinqtgy mhnrlrmvva
      361 sfltkdlgld wrwgecyfae klndfdlsan nggwqwasss gcdaqpyfri fnpvsqsekf
      421 drdgkfirry lpqlsglqgk alhapwtapp lelqaagvvl gkdyprpvvd hdearqrtla
      481 rygvvkaakd
//
LOCUS       WP_284405370             284 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: AAA family ATPase [unclassified Acidovorax].
ACCESSION   WP_284405370
VERSION     WP_284405370.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..284
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32342
     Region          2..266
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mkfqgsqsyv atqdlmlavn aaitlqrpll vkgepgtgkt mlaeevsrel gmpllqwhik
       61 sttkaqqgly eydavsrlrd sqlgdadsse rvkdirnyiv qgvlwqafta dqpvallide
      121 idkadiefpn dllreidrme fycyetreli rakhrplvfi tsnnekelpd aflrrcffhy
      181 ikfpeaetmr kivdvhfptl kaellavamk tfydvrglpg lkkkpstsel idwlkllvae
      241 diplealqsa dqkvavpplv gallkneqdv glfeklvfmn qrnr
//
LOCUS       WP_284405392             375 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: vWA domain-containing protein [unclassified
            Acidovorax].
ACCESSION   WP_284405392
VERSION     WP_284405392.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10530473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..375
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=41220
     Region          148..369
                     /region_name="VWA_CoxE"
                     /note="VWA domain containing CoxE-like protein; pfam05762"
                     /db_xref="CDD:399053"
     Site            order(219,221,223,278,304)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238739"
ORIGIN      
        1 mtpltipdpl qrwrlllgep aepacgalgd aaqaadaale wlygrdsdra ergersaglg
       61 psalstpdwi ntihtlfpke vierlerdav erygidevvt nlevleriep sesllravlh
      121 tkhlmnpqvl aaarrlvaev vrrimeklat evrqafsgsr drrrlsrmkv arnfdfrrtl
      181 qanlrrwdaa rgklyverpi fisrtrrhae pwdivllidq sgsmvdsvih savmaaclwq
      241 lpgmrtrlva fdtqvvdlta dvsdpvellm kvqlgggtdi aravayaqsl vanpvrtivv
      301 lvsdfyeggd pgelvrrvka ltgagakvlg laaldaqaep aydremaarl vkegaqvgam
      361 tpgqlagwla ekvqa
//
LOCUS       WP_284405461             294 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Acidovorax sp.
            SUPP3434].
ACCESSION   WP_284405461
VERSION     WP_284405461.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 294)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 294)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..294
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=31928
     Region          7..255
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 maerkpfagg valvtggagg lgraisarli qrgmhcllvd idpqaldrav qalgplamah
       61 vadltdptar qllvqqvqar wgrldllvnn agmvgttpfe qrgqdsirne lelnlmapll
      121 lthsllpllq ctgngrvvsi vslggmfplp estvysaskf glrgamlclg ldgarlgvrf
      181 sivnpsatet pmlmreaihg gnklqfmdpp qmpdevalqv mrcldqpcle rfvrpaeswt
      241 vrlamllpnc lvralplfqr raeqghqryl dslvarglvr qeegvwvcva darr
//
LOCUS       WP_284405471             471 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: cytochrome b [unclassified Acidovorax].
ACCESSION   WP_284405471
VERSION     WP_284405471.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Tolkatchev,D., Yu,L. and Yu,C.A.
  TITLE     Potential induced redox reactions in mitochondrial and bacterial
            cytochrome b-c1 complexes
  JOURNAL   J Biol Chem 271 (21), 12356-12363 (1996)
   PUBMED   8647838
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Howell,N.
  TITLE     Evolutionary conservation of protein regions in the protonmotive
            cytochrome b and their possible roles in redox catalysis
  JOURNAL   J Mol Evol 29 (2), 157-169 (1989)
   PUBMED   2509716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..471
                     /product="cytochrome b"
                     /GO_function="GO:0008121 - ubiquinol-cytochrome-c
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=52921
     Region          17..463
                     /region_name="QcrB/PetB"
                     /note="Cytochrome b subunit of the bc complex [Energy
                     production and conversion]; COG1290"
                     /db_xref="CDD:440901"
ORIGIN      
        1 mahefkdisp nastgakvtn wfenrfptaf dayrvhmsey yapknfnfwy ifgslallvl
       61 viqivtgifl vmhykpdaak afesveyimr dvpwgwliry mhstgasaff vvvylhmfrg
      121 llygsyrkpr elvwifgcai flalmaeafm gyllpwgqms ywgaqvivnl faaipfigpd
      181 lallirgdyv vgdatlnrff sfhviavplv llglvvahll alhdvgsnnp dgveikgpna
      241 prddkghpld gipfhpyytv hdifgvcvfl fifsavvffa pefggyfley nnfipadplk
      301 tpahiapvwy ftpfysmlra itsemmyali acvvlaagfg vvkgrlpvfi kvaivaiaaa
      361 aialmlsida kfwgvvvmgg aviilfflpw ldmspvksir yrpgwhkyly gifvinfval
      421 aylgvqppsp lgervsqvgt lfyfgffllm pwwsrlgepk pvpdrvifka h
//
LOCUS       WP_284405485             120 aa            linear   BCT 25-DEC-2024
DEFINITION  bleomycin resistance protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284405485
VERSION     WP_284405485.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..120
                     /product="bleomycin resistance protein"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=13143
     Region          15..118
                     /region_name="BLMA_like"
                     /note="Bleomycin binding protein (BLMA) and similar
                     proteins; cd08349"
                     /db_xref="CDD:319937"
     Site            order(15..17,45,52..54,56,70..74,79..80,83,116)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319937"
     Site            order(39..40,45,56,58..59,72,98,105,107,111..113,115)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:319937"
ORIGIN      
        1 msrppapagl vhatvpvlas ldldesaafc adrlgfaprl rtgdyliaer dgcelhfwlc
       61 terhiaents cyvrgdtral hadfaargla vdppreqpwg mrelyvidph gnllkfgesl
//
LOCUS       WP_284405541             401 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284405541
VERSION     WP_284405541.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..401
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=42278
     Region          35..374
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mqdaqplydl aplarmvllg avialgplaw vwlrnrgtsr vrrlqaltvl tlfltfdlvl
       61 fgaftrltds glgcpdwpgc ygnasplgah aeisaaqqam ptgpvthgka wvemihryla
      121 sgvgmliivl tvgawwqrsr aarrqgpppa lspwwptatl vwvclqgafg altvtmklfp
      181 aivtlhligg lvllallcvq avrethaarg vppvalgrgl rgllvattvl lavqivlggw
      241 vstnyavlac ttfptcqgsw wpdmafgqgf eiwrplgllq dgshitfagl taihyahrla
      301 ayavllalgl lawrlhraal lpaqarwiag lalmqfatgl snvvldwplv aavlhtggaa
      361 alvvvltwal aasravgaar plaaaagtpt taptgatris a
//
LOCUS       WP_284405579             322 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284405579
VERSION     WP_284405579.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..322
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33720
     Region          4..320
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mwcriplpgl alaaavlipl sasaqewptr pvrilvgsap gggtdamara vadrlgpllk
       61 qptvvenrpg asntlaadat akstdghtmv mgvvtahaia phllklaydn nrdlvpvafv
      121 gavpnvlvvt nalpaqsvke lvalakkapg tinfassgag stqhiaaemf kdaagidlmh
      181 vpykgsgtal vdlvggqvqm sfdtmpsvlg qiksakmral avttpqrnpq lpqvptmaea
      241 glpqvdisaw ygiympaatp kavqqkvhda vnevlampet qtrlgavgae lkpisqaefi
      301 afqnaefkry gdlirknhir id
//
LOCUS       WP_284405634             151 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Acidovorax sp.
            SUPP3434].
ACCESSION   WP_284405634
VERSION     WP_284405634.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..151
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16444
     Region          3..105
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 makrkslads pcpvarsldv vgdrwamliv rdafdglrrf gefqaslgaa rnilsdrlrt
       61 lveagvleia pasdgsayqe yvltakgetl fpvvvalrqw geahlyarge khsvlvdrat
      121 gkplpkallr ledgrvvrpa dtlvkkvrar p
//
LOCUS       WP_284405695             323 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284405695
VERSION     WP_284405695.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..323
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34148
     Region          24..321
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mkhlipalla acglaaavap araqqppypn apitlivpfa agsgtdsvar tvgqklaerl
       61 kqpvlvdnkp ganaqvaaqi vakakpdgyt lfmttntshs anpalyshlk ydpikdftpv
      121 arvgelpfal avhpgvpakt laelidyara npgklsyatp nstslvames ikhiaqvdvl
      181 sipyksspqa mtdlvggqvq vyvadlgsgk smltsdkvrt lgitttqpsp llpgvppigq
      241 tvkgfdltsw ngifgpagmp paivnrlnte lqavlaekdt qdklaqigfq vwpsktpqef
      301 atyvadqlah wrtliqqari qpe
//
LOCUS       WP_284405717             361 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Acidovorax sp. SUPP3434].
ACCESSION   WP_284405717
VERSION     WP_284405717.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10191051
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..361
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39172
     Region          33..359
                     /region_name="Esterase_713_like-3"
                     /note="Uncharacterized enzymes similar to novel bacterial
                     esterase that cleaves esters on halogenated cyclic
                     compounds; cd12810"
                     /db_xref="CDD:214009"
     Site            order(214,237,335)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:214009"
ORIGIN      
        1 mqrhlcktlt allggtvalh ahaapqetaa sapiavqaqg sfavggtvvq spgtyvlgqp
       61 gpagqtlhgd harvtyqipv narqlplvmw hgfgvfsktw ettpdgregf qtiflrrrfp
      121 vylvdqprrg gagrstvagq itaepdeqrw fnvfrlgvwp nfypqvqfpg dpeslnqffr
      181 qmapdtgpld npvavdamsa lfrrigpgvl vthsysgglg wkavmdnpai ravvsyepgs
      241 gfvfpegevp ptlpsltgpl ngvavpmaqf kaltripivl yygdnipaap stdpgqdnwr
      301 vrlamarlwv eavnrhggda klvhlpeigi rgnthfpfsd lnnvqvadqm qqflsskrld
      361 r
//
LOCUS       WP_284405850             248 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Acidovorax sp. SUPP3434].
ACCESSION   WP_284405850
VERSION     WP_284405850.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..248
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=27166
     Region          1..244
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mhilivddea larsrlrtll adcdarhtaa eaanaadala qlqpsggraf dtvlldihmp
       61 gqdglalaha mrtlpyppai vfvtahadha vsafeldavd yltkpvrrer lekalgkalr
      121 arhpgatpap tapipdgetl liqdrgrter vplaevlyfk aeqkyltvrt avrsyildgs
      181 lselearhgd rflrihrnal varravrale khydpeegeg wavrlhglte llavsrrqva
      241 avreelag
//
LOCUS       WP_284405854             491 aa            linear   BCT 25-DEC-2024
DEFINITION  rhomboid family protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284405854
VERSION     WP_284405854.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Koonin,E.V., Makarova,K.S., Rogozin,I.B., Davidovic,L.,
            Letellier,M.C. and Pellegrini,L.
  TITLE     The rhomboids: a nearly ubiquitous family of intramembrane serine
            proteases that probably evolved by multiple ancient horizontal gene
            transfers
  JOURNAL   Genome Biol 4 (3), R19 (2003)
   PUBMED   12620104
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10483871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..491
                     /product="rhomboid family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=55072
     Region          126..302
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
     Region          <412..491
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
ORIGIN      
        1 mfyaipldnr ptwrnppwmt vliilvnllv fwgpqrweak avdraaqvyl dsplpgielp
       61 pfvqwlkdag hrdaeqarrm laahrehall rwmeheegfq krlharlvvr addpqyadwk
      121 aararyeaal pepftrrwaq syekdapprp vtwitaaflh astghllgnm vflflfgfsv
      181 elalgrwryl afyllgavgg slmagwayag qgsyglgasg avsalmgmya vlyrlrrvrf
      241 fyqlffyfny vtapallllp awianellqh wlsgrgvaym ahlgglltga almwgaglvr
      301 rkaieapppe aaaapddgfd ahvaqarqsa qamqferalv qwraaaqlrp rdvpvlsawf
      361 ktaslwpage dfhraarrif rlpgqdaatl dfqhasyrty ldharpsarl vpddmaglar
      421 rfvragqwsd aeklltalhr tapqhaalge lvgmlvtall qsgrreqama wlpqlqqlap
      481 gsaplrlleg r
//
LOCUS       WP_284405856            1993 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284405856
VERSION     WP_284405856.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 1993)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1993)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1993)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1993)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1993
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..1993
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=215539
     Region          313..1990
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mtttthsfra lalalalgaa aqahalsiis fspqgevsrv rqavakfdgp avnfgdpkap
       61 aplsvscsda eagqgtgrwt serewvydfk gdlppgvrct aqvksgfksa agaelsgtks
      121 yafntggpyv qnirpgtyqp ideeqffmlq lngpatlasv qanvwcvadg vgervpvrli
      181 egaqreglla sqgldktaak eplkyvtlac nrrltsggrv qlvfgkgvat psgvgntiek
      241 ryeykvrepf aadfrceren aqsaclpirp mflsfnapvp rklaeavrlr sdketlkpri
      301 dgegdgdtvv ngvrfdppft aqtaftvqlp kdfkdasgrt lrnadsfplk vgtgamppla
      361 kfaaspfgvv eryaegpkep allpvtlrnv eaalkvqgle agkpadgaap akvstlqpgs
      421 dadiiawyrk vrrydgylvs rksarrdvkg alpaalesds seyvqsrmvs llsgqggvkt
      481 ldlpkpvnnd prpfevvgip lptgfhvvei aspllgksll derhgegrtm yvrtsalvtn
      541 lgvhfklgre nsaawvttld kgqvvagakv rvsdcngrel atgttdaqgv alfdglspep
      601 pscqgddgge qayfvsarap gadgvqdmaf twsdwqrgie pwrfnlptsm eprpderaht
      661 vfdrtllrag etvsmkhllr tenrkgfglp deqpdtlvit hvgsgqqytq dltwrktatg
      721 glsaentfav ppaaklgvyq vqlqggshsr nsfesgqfrv eefrlpvleg ritptdkkpl
      781 vrvrsvptdv qvnyvaggga anlpvrvsal vrgksaqwsd fdafsfmppn qrgaqsqshs
      841 ddeeaaagqd arviadklal tldkngagkl aidnvplarr pqelvleaty adpsgevqtl
      901 rstqtlwpaa vvagiktegw vsaaqkirfq alalgldgkv qegvplqvqa iaritttsrk
      961 rmvggfysyd nktetkdlgt vctgksdsrg lllcetklee agevelvata rdkdgntsea
     1021 assvwvtrqg eiwfggedhd ridllpekkt yqpgetaklq vrmpfrhata lvsveregii
     1081 dtrvvqlngq dptvqvkiee gwgpnvyvsv lalrgrlrev pwysfftwgf kaptewwsaf
     1141 wyegkeyvap tamvdlskpa yrlgvaeirv gtqahqiqvk vvadkesypv rgkaqvtita
     1201 tlpggkpaag aevalaavdq allelmpnts wnlldamlqr rswgvqtsta qmeiigrrhy
     1261 grkavpaggg gghsqarell dtlllwqpai qldangqakv tvplndaltt fkivavadag
     1321 tglfgtgatq iratqdlqii sglpplvred dqfraqitlr nttqaamkve vaaratllql
     1381 dkqsvdippg esrevawtvt apaqlaqtrt eailweiear dtagangard alkatqriip
     1441 avpltvqqat lvqvdgsfnl dvnppadalp grgglkmslq pklaeglpgv rdwfanypfa
     1501 cleqktskav glrdgtlwqt vvaqlptyld adglanyfpp qagsanrgsd tlttyllsaa
     1561 heaaslhpef alpdearaam ergltafveg riqrdfwspr kdldmrkiaa iealsrygka
     1621 sgrmlgsvti apnqwpthtv idwlnilkrv ndvpqrdqrl aeatqvlkar lsyqgtklif
     1681 sterddywww lmqngdvnta rlmlavmddp awkddmgrla ngfisrqqng awhtttanlw
     1741 gglalekfsa kfeatpvagv traalgsgna svdwakverv kasdatgaah qttwfgapas
     1801 pgnfknnsmf lpwsptggke nlavthqgtg kpwltlqsva aiqlkapfaa gyaikktitp
     1861 veqavpgkyt rgdvlrvtle vnasadmtwv altdpipgga tilgsglgrd seiatqgekr
     1921 sgsawaafee rsfeayrsyy eylpkgtika eytvrlnnvg dfalppsrve amyapemfge
     1981 tpnarvkvea aar
//
LOCUS       WP_284405870             468 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Acidovorax sp. SUPP3434].
ACCESSION   WP_284405870
VERSION     WP_284405870.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 468)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 468)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 468)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..468
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=51565
     Region          147..459
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mpsakshwpr sfrgrlllly vagmllsggl vmavvmvlle plerymlqhs vieraesiar
       61 iirfdgaglp vgldrsride wpfaslseev vlrivdphga vfyttdgkrf plapeglgfd
      121 pqrkgfalqr dgvamhaatv plqrpdrlwy vqfaisdriv lllqhsiglp alrkgivatc
      181 ltflvifvia mhltlrrvle plriaslqaq ritpqslgdr lalgdlpsel vplvdafnra
      241 ldrvqlgfqt qqeflanaah elktplslir aqvelggqgg gkaggsehsr yllqdidrma
      301 rqvqqllhla easeqrnyri ercdprsail easdfmdrva ersqvqialf fdegvglwda
      361 drgalftllk nllenaiqhs pphrvvrlqv hgrgfvvsde gpgvapehlg klcerfwrga
      421 srrdegaglg lsicqeiaaa hgwtiearng avglevrvth asapgpgq
//
LOCUS       WP_284405875             178 aa            linear   BCT 25-DEC-2024
DEFINITION  group I truncated hemoglobin [Acidovorax sp. SUPP3434].
ACCESSION   WP_284405875
VERSION     WP_284405875.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Keppner,A., Maric,D., Correia,M., Koay,T.W., Orlando,I.M.C.,
            Vinogradov,S.N. and Hoogewijs,D.
  TITLE     Lessons from the post-genomic era: Globin diversity beyond oxygen
            binding and transport
  JOURNAL   Redox Biol 37, 101687 (2020)
   PUBMED   32863222
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Bustamante,J.P., Radusky,L., Boechi,L., Estrin,D.A., Ten Have,A.
            and Marti,M.A.
  TITLE     Evolutionary and Functional Relationships in the Truncated
            Hemoglobin Family
  JOURNAL   PLoS Comput Biol 12 (1), e1004701 (2016)
   PUBMED   26788940
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Wajcman,H., Kiger,L. and Marden,M.C.
  TITLE     Structure and function evolution in the superfamily of globins
  JOURNAL   C R Biol 332 (2-3), 273-282 (2009)
   PUBMED   19281958
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Vinogradov,S.N., Hoogewijs,D., Bailly,X., Arredondo-Peter,R.,
            Guertin,M., Gough,J., Dewilde,S., Moens,L. and Vanfleteren,J.R.
  TITLE     Three globin lineages belonging to two structural classes in
            genomes from the three kingdoms of life
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11385-11389 (2005)
   PUBMED   16061809
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Wittenberg,J.B., Bolognesi,M., Wittenberg,B.A. and Guertin,M.
  TITLE     Truncated hemoglobins: a new family of hemoglobins widely
            distributed in bacteria, unicellular eukaryotes, and plants
  JOURNAL   J Biol Chem 277 (2), 871-874 (2002)
   PUBMED   11696555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..178
                     /product="group I truncated hemoglobin"
                     /GO_function="GO:0005344 - oxygen carrier activity
                     [Evidence IEA]"
                     /GO_function="GO:0019825 - oxygen binding [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18382
     Region          65..175
                     /region_name="TrHb1_N"
                     /note="truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 1 (N); cd00454"
                     /db_xref="CDD:381253"
     Site            order(67,72..73,76..77,80,110..111,114,143,146,150,153,
                     164,167)
                     /site_type="other"
                     /note="apolar tunnel"
                     /db_xref="CDD:381253"
     Site            order(81,90,93..94,97,101..102,105..106,108..110,112,120,
                     122..125,128..129,132,134,138..139,142,167,170,174)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381253"
     Site            order(83,86..87,145,148,152..154)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381253"
ORIGIN      
        1 mpipatprfa vppcrapraa alalaaalat avpaaaqqpa agatppgaaa saavpataap
       61 eglydalggk pgiarimsgl vdrafkderi gplfketkpq alkdsltdqi cvlsggpcry
      121 egadmksaha dlpirkrdfn vlvellqdam deqgiaftqq srllallapm hrdiitvr
//
LOCUS       WP_284406018             330 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284406018
VERSION     WP_284406018.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..330
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34174
     Region          4..328
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mtdlsrrqwm laascswlst lpfaahaqqa aawpsrpiri vvaypaggvs dvvaralgdk
       61 lsaqlgtsvv vdnkagaggs igmdavakaa pdgytlgfss isplvlnphl gkspfdpakd
      121 iapvasvmvs pvlllgtpas qakdfrqlla takaqpgavr watsglaslg himleqimqs
      181 tqakithvpy kgggqqlnda lsgqfevlst nagpavmqhi qagklralav gsparldtlp
      241 dvptlaelgi paanvsslfg vfapartpap ilerlnaein ralalpdlra rleatdnvpq
      301 ggkaadfvrq iaeesqnnar iiraagiqmn
//
LOCUS       WP_284406061             323 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284406061
VERSION     WP_284406061.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..323
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33698
     Region          1..321
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mqrrpliaaa flaasfplas taqaqdfppk kpvtlvvgfa aggsadiaar iiakklgeni
       61 gqsvvvdnkp gaggnlahaq vangpsdgsm llfgsigpls iaphfmkvay dplkdlapis
      121 mgvafpnvlv vpastgiktl gdfvakakre pgkldyastg pgsaahlage llndeakidt
      181 lhvpykggap alqdvlggrv tafyaappsa lphiesgkli plattgltrp aylpnvptva
      241 etypgfnatn wyafvasakt pkplldrwnt eivkvlntpe vrdnllkhgq tasptgreel
      301 gqfiaaehak wgriirerki tad
//
LOCUS       WP_284406035             185 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Acidovorax sp. SUPP3434].
ACCESSION   WP_284406035
VERSION     WP_284406035.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..185
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=19698
     Region          1..115
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mpapqglepp sewiqrwahl vppgasvldv acgsgrhlrw lqgrghpvtg vdrdpdalap
       61 lrglgeilca dieagpwpla grtfgavvvt rylwrpllpt lvasvapggv llyetfaagn
      121 etvgrparpd fllrpgellq tcaglctvay edgfldaper fvqriaavrl qegaaparhr
      181 lappl
//
LOCUS       WP_284406123             388 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284406123
VERSION     WP_284406123.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..388
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=41368
     Region          8..383
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mppqaqvspe apndqfrsls pavwrastvl fdtvadftsr kdrlfdgyty gvtgtpttra
       61 leervaaleg ahhcvavpsg qaalclials lleagdhvlv adsaygplrt fardylqrfg
      121 iehdtfdpla gadlasllrp qtklvflesp gsitmemqdi paivevtrta gvrtvldnsw
      181 asplgfrgip vgvdivveaa skllsghsdl llgtiatdsr slyeafrttq svlgqavsae
      241 dcflalrgmd tlevryshqc asalavasal tshdavtevl fpprpgdrsh trwaasftgg
      301 gcvlsfvphf hgdaaihqff salrvfqiga swggvhslaa yypeteqrkr khcafsagiv
      361 rlsiglepsg kliadleqal haagalps
//
LOCUS       WP_284406124             365 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284406124
VERSION     WP_284406124.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..365
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=38228
     Region          41..363
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mividldskv lsftglrntr tapwcwwvgp tnierttamd rrsllqkgga asavmllpga
       61 slwaqapypd rpiklivpws aggstdvlar avgqsmadgl gkpvvidnrp gaagrlgvda
      121 mvksaadgyt laiielahai apsiyqkmpy dimndaaais tlgvsplvlf vdaqkyqagq
      181 hqkfvadakk aaeplsiats gtgsishlaa glyakeakle lqmipykgsa paltdvaagv
      241 lsghfctlas asslfsagki vplmvtgnrr vpqlanvpsa selglntmdf gqwwalvapv
      301 kvpkpiital hkatvtalad kqvqsrissl aiqlgscspd eaqafiraea ikwakvvnsl
      361 gikpe
//
LOCUS       WP_284406161             710 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Acidovorax sp. SUPP3434].
ACCESSION   WP_284406161
VERSION     WP_284406161.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 710)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 710)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..710
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72486
     Region          137..703
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtkhshdlsh aghdghdhag hdhvpapapa sarpatapri dvsccgggcs stapqagtka
       61 aaaptgeahg dhghasegdh dghdhgalpg wgrlaaalva atgaellhll gpdttpwrva
      121 gmgvaaaail laglgiyrsg lrslmrgqlg isalmavavt gafligqwpe aamvmalyal
      181 aeriedravg rardaigall alspdqadvr gpdgqwrtvp aadvavdstv rirpggrvpl
      241 dgvvttgrsa vdessvtges lavdkapgdp vyagtlnaqs elefrvtaaa gqttldriir
      301 aveqaqsara ptqrfvdrfa avytpavfam avavaigapl lfgwtwldai yralvllvia
      361 cpcalvlatp vtvvsglaag arrgilikgg nwlelargvr avafdktgtv tagrpvlvgr
      421 esfgsdgaqd vaaalagrsd hpvskaiaag lgtpaglpev edftalpgrg vqariagatw
      481 llgnrrlaqe kglwtdavea aaaaheaqgr svtlladgqa vralfavadt lrpqsaqava
      541 dlralgivpv mltgdhaaaa qaaareagid evqagllpeq klsaiaalqq khgmtamagd
      601 gindapalak adigfamgga gtdvametad vvimnddlrr vaetvrlsrr thavlmqniv
      661 lalgikavff glalaghatm wmavfadmga sllvvanglr mlrseslskk
//
LOCUS       WP_284406324             334 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284406324
VERSION     WP_284406324.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..334
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34986
     Region          9..332
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 msimkieatm rrrtlvctgl saaavlaapa fadnfpskpi rlivpappgg gtdgvarlta
       61 haltesvgwt fvpdnlpgag gnigfdttfk avkdgytlam gessnmvinq flygripfni
      121 ekdmqpvali arvpmvlvvs ssgpyksmng lveagkkrsl sfassgngtl ahlvgelwkr
      181 ragvdmqhip yrgaapamtd liggqvdlaf tsipvampmi rggkvralav magerlplln
      241 dvptmaeagy kdmeasvvwg mvgpagmppa vvsrinaetn kalqrpavvq qlvamgaert
      301 pgsfggdpes fakvlreera kwapvvkasg atvd
//
LOCUS       WP_284406299             274 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284406299
VERSION     WP_284406299.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..274
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29123
     Region          <161..266
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mashddtpis edalhaltdg rlsaaqaeal rarlardaet qataaawqaq raqlqalhaa
       61 wdaapvpdsl rraagrleav rerearwwrl ggmaasllla fglgwtvhgq wptdhrgqaa
      121 grmadaapav arrfaqqaav ahavyqpeqr hpvevaaaqq ehlvqwlskr lgrplripvl
      181 aaqgyelvgg rllpgdtgar aqfmyqnaag ervtlylgal aagqpgaadt afrfdadgpv
      241 pcfywtdggf gyalsgalpr aallglatav hpql
//
LOCUS       WP_284406330              98 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Acidovorax sp.
            SUPP3434].
ACCESSION   WP_284406330
VERSION     WP_284406330.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 98)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..98
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=10451
     Region          30..81
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mavgssfphr ttpavapqpa avpaapanpe flttdeagaf lrlsprtlek qrvlgggprf
       61 rkfgarvvya aadlrawadr htygmtsdpg yvqrdsvr
//
LOCUS       WP_284406339             583 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Acidovorax sp. SUPP3434].
ACCESSION   WP_284406339
VERSION     WP_284406339.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 583)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 583)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..583
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=63591
     Region          1..443
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mylaqlniln frklqkaelh fqpglnvlvg annvgktavv dalrallagh depyprldsd
       61 dvhhpkggkp tgdivfqyif rglqpddead flaalkpgan gelvaritir yaeadkagrl
      121 rakrwcgdhe dvglttdmme nlrgvylppl rdasqglkps rtsqlsrlfq lladdagrdg
      181 invvlkalde elkkhlpivn thkaissrhg tmlgpqlaql lelglsasdf qrlasrlsll
      241 vdafeieqng lgfnnlifma vvlselaknp easyrslive epeahlhpql qavllrylet
      301 vqatdgekpv qlfvtshspn fasiadldsl tclvdtgaav etffprtvtf gkgkrekler
      361 yldvtraelf farrvifveg aaelmlvsvl aekagfklre havslisveg lnfdsfmplf
      421 gksalkipva vitdadpvde padgsepqal ypapgqaikv sdntakmkes eddfikvfhg
      481 lktfeydlal hadnrtamlk alkelhpkia vaveaevlaa gsdaekaral faglferkqn
      541 nvqkgrfgqa laqvfsepga acvvpeyira aithacqagp akp
//
LOCUS       WP_284406361             655 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Acidovorax sp. SUPP3434].
ACCESSION   WP_284406361
VERSION     WP_284406361.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..655
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=69134
     Region          16..508
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mhkeisgsan clapgvqvge yrlsdvigeg gfgivyrard lsldrivaik eympstlagr
       61 kesnqihvrs qhrgafdagl rsfinearll akfshpalvh vyrffeangt aymvmqyyeg
      121 qtfrtflnqq pkamdeqwls tiiapildvl emlhaadcyh rdiapdnifl qssgmpvlld
      181 fgaarriigd mtqaltmvlk pgfapieqyv ddgampqgaw tdiyqlgall ylsitgrppa
      241 tsvarmindp vstlvpencp gfsarflsgv hhalaikpqd rpqsigdlrh llglkavtls
      301 wpssglmgls aaeesdpsmd apvhvpsava apaaftapqp paeavapvap hpdarhgavp
      361 seahapvvsg ldtthqhrps tevrpskaas apvhappsps aessakahsr ktklatsqqg
      421 sghtpptkrp vwlipalgfa alvvvaggaw witsgddaak taavaqdaqe sdqwmlaari
      481 ntpdslrtyl slfpngahra eaeeriaalt savapasapv aqqapasapv vaasapmvva
      541 dvapakvppa svptpaasap aapsalptpe eaarvpaqat rtadaenkgk iilrvmpwgn
      601 vsvdrvpagt tppltqltls eglhridisn pvaptvtqmv lvkkgesvvl thkfe
//
LOCUS       WP_284406492             495 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Acidovorax sp. SUPP3434].
ACCESSION   WP_284406492
VERSION     WP_284406492.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..495
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=55219
     Region          72..>330
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mhavmcgaaq pasnlcrvaa cfgfsmqeli aalgscpylc aekeivqggl fntlelcsif
       61 npslkekimq firniaqggf gkvelvvdqg qqfarkvfsp tlnasesewe kmkkrfirec
      121 svqsqlnspa fmeilssdls gdkpwyimpl aektlytaih ekdateisag ladvlnalee
      181 lhglgyvhrd lkpqnvlkhq grwkladfgl ilppptdttk ltsmhsswat eaycapeqrs
      241 dfghvssaad iyafgcilhd vygttyripy srhtapgdig aiiekctesk perrfqsiqa
      301 lrsalatiae qttgasfasg dalgwalwla dpsnwntptl hafarylqtd lpkadlnrvf
      361 kamtdesiln faqidsdywk sviieycdwi qrggfsfeyc dvvgkrlesi fnigdieika
      421 laalsaakla ydhnrwfvme ivlnlcsdki sdliakriai eitamefqdy fyrcarnigk
      481 srsdyhpfis tilpi
//
LOCUS       WP_284406543             368 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Acidovorax sp.
            SUPP3434].
ACCESSION   WP_284406543
VERSION     WP_284406543.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..368
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39555
     Region          68..329
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mplrtlcgaa llllasacts vppastapap aafpgaswep qpvaeqgpac rrgleaagdy
       61 lrtldttalm avqdgrvlfg ygpveavsiv fsvrksvlsm lygppvadgt idldrtladl
      121 giddtggllp ierqatlrdl ltarsgvyha aanggddaaa apargsqvpg ryflynnwdf
      181 naagtaferl tgrgiyqafa ddlaaplqlq dfdparhvrs gdarrsehla ypfflstrdm
      241 arlghlmlqq grwrgrqiip adwvvqttrp ttpasqmhpa htarrgfgyg ylwwllqepp
      301 dsplagayma wgvhgqyilv vpkrqmviah krqvpvagdw nvswvgpkaf lhaarllaaa
      361 pcrageap
//
LOCUS       WP_284406562             333 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284406562
VERSION     WP_284406562.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..333
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=35040
     Region          10..330
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mapklfparq rrqvllhafa aalpvlasgs alaqaawptk tisltvpfpa ggttdvlara
       61 ladrltvslg qpvivesrpg agatigadyv arskpdgytl lmgavhhtia tsvykklpyd
      121 fqkdlapitt valvpnvlvv hadnpartva dlvaqaraqp gkltfgsngn gtaqhligtq
      181 fqgltgtslg hipykgsgpl atdllggqit msfdtitpvl phikagklra lavstlqrss
      241 alpevptlde aglkgfdlgt wfgvlapaat prdildrlna emvkviqspe frkrmadiga
      301 epvgntreqm aqqirseter farlvadakv vid
//
LOCUS       WP_284406630             116 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA recognition motif domain-containing protein [Acidovorax sp.
            SUPP3434].
ACCESSION   WP_284406630
VERSION     WP_284406630.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Muto,Y. and Yokoyama,S.
  TITLE     Structural insight into RNA recognition motifs: versatile molecular
            Lego building blocks for biological systems
  JOURNAL   Wiley Interdiscip Rev RNA 3 (2), 229-246 (2012)
   PUBMED   22278943
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Clery,A., Blatter,M. and Allain,F.H.
  TITLE     RNA recognition motifs: boring? Not quite
  JOURNAL   Curr Opin Struct Biol 18 (3), 290-298 (2008)
   PUBMED   18515081
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Maris,C., Dominguez,C. and Allain,F.H.
  TITLE     The RNA recognition motif, a plastic RNA-binding platform to
            regulate post-transcriptional gene expression
  JOURNAL   FEBS J 272 (9), 2118-2131 (2005)
   PUBMED   15853797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..116
                     /product="RNA recognition motif domain-containing protein"
                     /GO_function="GO:0003729 - mRNA binding [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=11770
     Region          2..84
                     /region_name="RRM"
                     /note="RNA recognition motif (RRM) domain [Translation,
                     ribosomal structure and biogenesis]; COG0724"
                     /db_xref="CDD:440488"
ORIGIN      
        1 msskiyvgnl pysvtdailq snfaefgnvs sakvmmdret grskgfgfve masaeaaqaa
       61 itglhgmsvd grsivvnlar preegggsgg ysaagygank rsdvgygtgg fgggry
//
LOCUS       WP_284406876             319 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284406876
VERSION     WP_284406876.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..319
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33341
     Region          24..317
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mrafvispli aacalaatva haafpdrpit ivvpyapgga adavarvlat rmgarlgasv
       61 ivdnkagasg tigasyvaka tadgytmlyd atpysinphl fpkmpyasta lqplslvlla
      121 pnalivkads pfknvndlia kakaepgkln fasggsgtvq rlaaelfrqk lqldmvhvpy
      181 ksggpaiadv mggqvdfmfg tiaasyplvs ggklralavs aperskrlpd vptvaetvip
      241 gyeayewngv flpagtpepv aaklqqalie vlkedevkqr ladlgaqaig stptefvtfl
      301 kkedakwgev vrkgdikld
//
LOCUS       WP_284406789             829 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Acidovorax sp. SUPP3434].
ACCESSION   WP_284406789
VERSION     WP_284406789.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 829)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 829)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 829)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 829)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..829
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..829
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=87737
     Region          63..803
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mlshrfeppp drpdltagtp apdapcaera lllddpqewa sfgrarlpag agadadataq
       61 tweshmvleg mhcaacalti edvlravpgv aqadvsaatr rarvvwnaah vrpsqwiaav
      121 rragyralpa mdafaraqrq gehrralwrw lvagfcmmqv mmyawpayva qpgdltaeme
      181 qllrwaswvi tlpvvifacg pffanalrdv rlrrvsmdlp valgmaitfg vstagtfdps
      241 gifgrevfyd sltmfvffll tgrwlelrlr drtagaleav mnrlpdsver lqadgafvrv
      301 avrrlavgdt vrvlpgeafp adgritrgdt ladealltge stpvarpegs avtagsynlq
      361 savqvkverv gadtrfaqiv almesaslqk prlaqladri arpfliavla aaalaaawww
      421 ptdpghalmv avavlivtcp calslatpva mltaagtlar qgvlvrhlqa lealagvdtv
      481 vfdktgtltr dgmavrgvhp apgqeradal alaaavarhs vhpvsralva aasreglpaa
      541 srwhvlevhe lagqglvarl reagegadga adargrlalg ertvrlgsvr hagaggpagd
      601 gaggsatgqq vllseqrsdg trvelarfdw sedlrpeapr avrrlrdagv avqllsgdrp
      661 gavrriaaqv gieraqgdct pqdklallqa eqlrghrvam vgdglndgpv lagahvsfaf
      721 graaplaqsr adfvvmggdl eqvvqtllla rrtlrvvrqn lwwaalynal cvplavvgwm
      781 pawlaglgma lssllvvana arlaagtgsp hapaaapaah sdvplpegv
//
LOCUS       WP_284406879             339 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284406879
VERSION     WP_284406879.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..339
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34859
     Region          32..337
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mttsipsspk trlarrslla aagaallgpl ltrpalaqgd wpagkiitwv vpyppggstd
       61 vlgrnvaqrv gaalgtnviv dnkagatgti gaafvakapp dgytllgtsi gpqaiaphlm
      121 grlpydpiag fepvitigti philvvganq pfktvadlva aakaqpgkla fasggngtil
      181 qmqgellqqq tgarfihvpy kgdtpalqdt laeqvqfmfa paaaalphvq agklralavt
      241 saqrlkslpt vptmgevgmk dfvveqwqav fapaktpaai vqrlnqeisk alkdpgvaal
      301 adklgvtlvg gtpqqlgdlq kadsakwakv iqdgnikae
//
LOCUS       WP_284406905             327 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284406905
VERSION     WP_284406905.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..327
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33745
     Region          30..325
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mirsllsfta lalalgataq aqtappaaty ptkpvrlivp fppgggtdil srlvatklte
       61 vtkwtvvpdn ragaggtigi teavkaaptg ydlvmgqkdn lvvapwlykn lpwdptkdli
      121 avahvaytpv iiatgansrf ktladvvaaa raepgkityg spgngttihl agdlfekaag
      181 iklshipykg snpalmdala gnvdllvssv psamgqiksg klrplavtsa krssslpdvp
      241 tvaesgykgf dvsswygifa pagtpanvvt tvntevnkll aspemqaaiq aqgaepesls
      301 aaqfstllkt dyakwkgive asgakie
//
LOCUS       WP_284406937             329 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284406937
VERSION     WP_284406937.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..329
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34650
     Region          22..327
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mhrrtllkna laaagataga ampwaaqaqs dypsqpirwv vpypagggtd vlartvaeal
       61 rgplgqqivv dnrpgastni gaqmvatakp dgytlmsadn allaynehlf sklpfspekd
      121 ftyigglsrf plalvvhpaf eaktvkdlla yaranpgkln yaspgngsph hlamemfknr
      181 tqtflthipy rgaapalqdv mggqvpcmfl dlaaglpviq agkvralaig sakrvpglpd
      241 vptlaeagvp ntevyafqgv lgpagmppal vtrlntevnk alasppvvkr mqdfgmeplg
      301 gtpeqframa raeakrwgei ikaagvkld
//
LOCUS       WP_284406944             458 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Acidovorax sp.
            SUPP3434].
ACCESSION   WP_284406944
VERSION     WP_284406944.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..458
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=49169
     Region          8..456
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mtaspslghi llvddepayq rlgssflrel ghrvtvagsg eeaawafgqd rahvvlldla
       61 mppsmdpeag leligqfags vvvvlsghgd relalraaek gawdfltkpi dpdmlrfvvs
      121 ramhksrlde elrelrareg sedlgivgqs paaqqlramv rrvagtsvsv mvlgptgtgk
      181 elvaralhqc sarrqgpfai ihcgalssel leselfghlk gsftgahrdq pglvetahgg
      241 tlfldevgem ppamqvkllr flqegtflpv ggremkkadv rvvsathrdl egmiqdggfr
      301 edlfyrlkgv vmripalaer gmdvpllaah flrrvapqal fapdaqawla tqpwpgnvrq
      361 lralvesaga liapghlrid ldllrfasgd lahlpdagpa daaaaapvga ldaaifelet
      421 rmvreameat qgnqseaarr lgisraglik kltrlglr
//
LOCUS       WP_284406952             656 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Acidovorax sp. SUPP3434].
ACCESSION   WP_284406952
VERSION     WP_284406952.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..656
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=70957
     Region          14..654
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mdeeegpalt qvpgwawaay vaagvawvag gdallawllg tdagggthag lwgsakdiaf
       61 vlasaalava glrrlqaada aalvrrgraw armargaeqr qrlattvvdn aiegmvvtda
      121 nnrilsvnaa ftrlmgytea ellgqtprlf ksgrhdrafy ealwtelsrt grwqgeiwnr
      181 rkngevfper mslstvrdga gvvthyvclf tdisqehtqr qrlaflahnd pltglpnrtw
      241 faqrleeata qarvsgesma vlllnldrfk dvndsyghav gdevlrhiar rlesalrpgd
      301 lagrlagdev gvlvrnapse eeaaaiartl iaavaepwrs pegfevvaga svgislfprh
      361 gdsaqallqg ahaavygake rgrgawcffs etmtraarer lalesrlraa lalghlqlhy
      421 qpqvdiatgr vigaealvrw mdpqegmisp arfipvaehs gvigplgewv mheacrqgqa
      481 wreaglpglt mavnvsprqf hltdlagcaa salsasgypp tyleleiteg alaerpeear
      541 qvllrlrglg lrmaiddfgt gysslahlkr fpidvlkidq gfirdlpqnt ddmaictaii
      601 amghslglav laegvetpeq laflrergcd ryqgylcqrp lpaeaftall haqaga
//
LOCUS       WP_284407053             183 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284407053
VERSION     WP_284407053.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..183
                     /product="YceD family protein"
                     /calculated_mol_wt=20216
     Region          1..180
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mtkefsphrl dvkafaqggg hlsghdsllk yerlaqeakg lhpdlmvdwq vdgevrsthg
       61 iggqiwlrlt vnaalpmtcq rclgsvdvpl qvqrefrfva deataealdd esdedllals
      121 refnlrelie dellmalplv prhdecpapv pmessdedfe easaqkpnpf aalaalrkdk
      181 aed
//
LOCUS       WP_284407302             247 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Acidovorax sp. SUPP3434].
ACCESSION   WP_284407302
VERSION     WP_284407302.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 247)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..247
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25790
     Region          4..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mntnqiahia alvgepartg mllalmdgra ltareladaa hvtpatasrh lallvearll
       61 svrsqgrhry lrlasaevar lleglmqlaa gqapparpva vgprdaalrr artcydhiag
      121 rlgvavaehl lqegaivfdt eaggqvtdra aavlgrlgld lagpsagppq rgprplcrpc
      181 ldwserrphl agrlgalvca hcldqgwlvr regsralait ppgaaalqgw lgtarwsgvv
      241 qaplpga
//
LOCUS       WP_284407321             153 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284407321
VERSION     WP_284407321.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..153
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=15711
     Region          1..132
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mafgrlertt gpqpmsdinm tplvdvmlvl vvifiltapl lassirldlp radgatpgap
       61 pqsvtvvldk egqaylddvp lapqalaarl aqlareqpdt evqlradtav pygrvvevmg
      121 aanaaglrri gfvadpaapa apsavpaspa aar
//
LOCUS       WP_284407329             223 aa            linear   BCT 25-DEC-2024
DEFINITION  OmpW/AlkL family protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284407329
VERSION     WP_284407329.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006882
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..223
                     /product="OmpW/AlkL family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23584
     Region          18..223
                     /region_name="OmpW"
                     /note="Outer membrane protein OmpW [Cell
                     wall/membrane/envelope biogenesis]; COG3047"
                     /db_xref="CDD:442281"
ORIGIN      
        1 mkpfswacva iaaaavcgta saqvagtlsl ragvtqispq vksgnlsaps fpgtrvdvhs
       61 ataltgglny mltdhwavdv piglpfkhsf ygdgaiggvg kvgetkvvpa tvfaqyrfqe
      121 anaafrpyvg lgvtyakffk erttatlngl tggtpanptt asiddkwgvt aqvgfvwqfn
      181 erwfldaayy kgflktttrl ssgqnidikl npnvfavgig yrf
//
LOCUS       WP_284407438             306 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Acidovorax sp. SUPP3434].
ACCESSION   WP_284407438
VERSION     WP_284407438.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 306)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..306
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32962
     Region          10..288
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mqaqhkiksl ldqlntvivg ksaqvqdcva cllagghlli edvpgvgktt lahalartfg
       61 lqfsrvqfta dlmpsdltgv svyergkesf vfhpgpvfaq vlladeinra spktqsalle
      121 ameekqvsve getralphpf fviatqnphd qlgtfalpes qldrflmris igypdraaer
      181 lllagadrre mvdsmlplls gdelaqlqqq vlavhtadpl lnyvqdlmaa trsgrwflqg
      241 lspragialv raakaqalis grdyvapddv qavlpqtvah rlvpvgdagr gaveqvramv
      301 davplp
//
LOCUS       WP_284407518             329 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3434].
ACCESSION   WP_284407518
VERSION     WP_284407518.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..329
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34797
     Region          8..326
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mnqrphaisr rvalalclan trlpfaatak eefpnkpvrl ispfpaggst dilarllskh
       61 mfpasgqalv venvpgaggn vgaalvarsp adgytleiga msthamngsi yknlsfdpmn
      121 dfdtvallay ainavavsas vpvrtfpell ayiranpgkv nystggigth nhltvallak
      181 tagldivhvp ykgggpavaa lvqdecqlya ggaslllpha qagkvrlvav tektrsellp
      241 dlpsvsetlk gfevtnwyga faprgleasr rallnqeihr vialpevaer lkglgmvhas
      301 lsplqvrdvl qadhdlwsrt iqslriase
//
LOCUS       WP_284407496             376 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Acidovorax sp.
            SUPP3434].
ACCESSION   WP_284407496
VERSION     WP_284407496.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         1..376
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42086
     Region          3..364
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
ORIGIN      
        1 mptsvvsphf yrdpdhhare meglfreswv fvcmrfeldg lvhrgvqvgg vslllqcdsq
       61 grpraflnvc shrhaqlces gahrgparcp yhgwvydreg vpvgipakhc fpevvaepar
      121 frlqefncea vgqfvfvris eggpalreyl geqyaflera sqgmqgllde frepvganwk
      181 ivienalegy hvpavhsrtf mqvdgmdrae taprffledr rhshlehaad aqwvarfarm
      241 eskigqwpwr fahythhhif pnltvtsfmg ysfhvqsfep taprqttvhs rtvgveftgt
      301 tpagakmmeh ihadghaftr kvfaedggic tkvqagvdqa erpalvgagi edrvahfqaa
      361 yaralqgset pmggka
//
LOCUS       WP_284407948             602 aa            linear   BCT 25-DEC-2024
DEFINITION  fructose-specific PTS transporter subunit EIIC [Acidovorax sp.
            SUPP2539].
ACCESSION   WP_284407948
VERSION     WP_284407948.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01427.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..602
                     /product="fructose-specific PTS transporter subunit EIIC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022877 -
                     protein-N(PI)-phosphohistidine-fructose phosphotransferase
                     system transporter activity [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=59983
     Region          4..87
                     /region_name="PTS_IIB_fructose"
                     /note="subunit IIB of enzyme II (EII) of the
                     fructose-specific phosphoenolpyruvate:carbohydrate
                     phosphotransferase system (PTS). In this system, EII (also
                     referred to as FruAB) is a fructose-specific permease made
                     up of two proteins (FruA and FruB) each...; cd05569"
                     /db_xref="CDD:99911"
     Site            order(10..13,15..17)
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:99911"
     Site            order(10,12..13,16..17)
                     /site_type="active"
                     /db_xref="CDD:99911"
     Site            10
                     /site_type="phosphorylation"
                     /note="phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:99911"
     Region          138..600
                     /region_name="FrwC"
                     /note="Phosphotransferase system, fructose-specific IIC
                     component [Carbohydrate transport and metabolism];
                     COG1299"
                     /db_xref="CDD:440910"
ORIGIN      
        1 mahliaiaas qagpahsfmt gealraaaer lghhialsvr sslgaqggwt ddellradav
       61 iiaadmavdr tglpaarlhe ttpgavlada advvraalar agaggssega vaahggaapa
      121 aaavpavaaa daahplriva itscptgvah tfmaaealeq gaqalghtik vetqgsvgaq
      181 naltadeiaq adlvviaadt qvdrarfagk rlyatgtkaa ihdaaavfaq aaaqaavwgg
      241 aptagaaaap gaapagaaar stertgpykh lmtgvsfmlp fvvaggllia lafalggiyv
      301 yddahqgtlg wtlfqigaka gftlmlpala gyiafsiadr pgiapgmigg llagtvgagf
      361 lgaiaagfia gyavhwmnra irlprtldgl kpvlllpllg tlvvgvlmmm vigkpmagvm
      421 aaltewlkgl qtgsavllgv ilgammafdm ggpvnkaayv fsttliasgv anpmaatmaa
      481 gmvpplgial acwvfrsrfs aeereaskav avlglafite gaipfvardp lrvipacmag
      541 aavagglsmm wniglqaphg gvfvlaipna vnhvvlyala iaagtgvtal algvlkrrva
      601 va
//
LOCUS       WP_284407733             362 aa            linear   BCT 25-DEC-2024
DEFINITION  cysteine dioxygenase, partial [Acidovorax sp. SUPP3434].
ACCESSION   WP_284407733
VERSION     WP_284407733.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3434
  ORGANISM  Acidovorax sp. SUPP3434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Chen,M., Zhu,J.Y., Mu,W.J. and Guo,L.
  TITLE     Cysteine dioxygenase type 1 (CDO1): Its functional role in
            physiological and pathophysiological processes
  JOURNAL   Genes Dis 10 (3), 877-890 (2022)
   PUBMED   37396540
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Joseph,C.A. and Maroney,M.J.
  TITLE     Cysteine dioxygenase: structure and mechanism
  JOURNAL   Chem Commun (Camb) (32), 3338-3349 (2007)
   PUBMED   18019494
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14410663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Acidovorax sp. SUPP3434"
                     /db_xref="taxon:2920880"
     Protein         <1..362
                     /product="cysteine dioxygenase"
                     /EC_number="1.13.11.20"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0017172 - cysteine dioxygenase activity
                     [Evidence IEA]"
     Region          224..329
                     /region_name="cupin_CDO"
                     /note="cysteine dioxygenase, cupin domain; cd10548"
                     /db_xref="CDD:380416"
     Site            order(224,226,244,255,257,313,327,329)
                     /site_type="active"
                     /db_xref="CDD:380416"
ORIGIN      
        1 ylihhrqlkg qcvvllrsln plihltflsd eqkgvnliqd gsvatrwiav vlplflssst
       61 lfqtmttssi sspsravspr seraevadta ssnkrpagss qpggdarldg lparspdasa
      121 egasakrprt slpgadagia areaqldkvy ttlslqarqt haanqkrlea gvqkllqnas
      181 vqaeiavgkd vrdcvadalk glleeaqlst diykpkdatq lagygryllh sqakegesfc
      241 lqlfafdarq ktpihdhpne casfilkgnl seriyrptge tkdktpladk tdknarpqgs
      301 wagfgpdelg vphslknksg dialsvhlyr dmdglsegqq iaaktkfert pkapkpavap
      361 ae
//
LOCUS       WP_284407993             327 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284407993
VERSION     WP_284407993.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..327
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34312
     Region          4..324
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mnvsttrrqa lvlgasgalp mlaraqagad fpthpvrliv pfapggstdi lgrllskhlf
       61 pasgqpmvve nmagaggnlg aalvarspad gytleigams thamngslyk qlafdpmndf
      121 dtvamlayai nviavspsvp vrtfpellay iranpgklny asggigthnh ltlallakta
      181 qldivhvpyk gggpavaall qgecqmfagg aslllphaqa gkvrliavte ktrsdllpdv
      241 psaaetlkgf evtnwygvfa pkgldvarra linheinrvt glpevaerlk glgmvrapvd
      301 pvqlreilqa dyrlwsstik slgisse
//
LOCUS       WP_284408013             568 aa            linear   BCT 25-DEC-2024
DEFINITION  two-component system sensor histidine kinase NtrB [Acidovorax sp.
            SUPP2539].
ACCESSION   WP_284408013
VERSION     WP_284408013.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 568)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 568)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 568)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 568)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..568
                     /product="two-component system sensor histidine kinase
                     NtrB"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009399 - nitrogen fixation [Evidence
                     IEA]"
                     /calculated_mol_wt=61571
     Region          200..526
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 mpalkrasal lsadapfarl wgsflsgrim vaaallllqg lgvalnqsye plllgicagy
       61 lvatvlllvl agnappgphs wlqwmcsigv dlalistlqi lhvgsmnftp lfglpilmag
      121 vlgtltlalg ttaavtllll awawwlgssg gsdatqryfq taltgtgyfi vaylvhqlas
      181 rlnreqqlaq asqmaakvqe qvsalvihnl sdgvlvldqr dtvrianpaa lrllgtnarh
      241 alpfsmahss pwkpllamar qtfqkgkpqs advdvlhpgq splalhvraw ltssqeiare
      301 tggehlcvmf lhdlremear lrteklasmg rmsaavahei rnplaaimqa nalleeelhe
      361 pgqkrlahmv qqnaerlari aeevldiarv qhqishapas tvvlceavaq vwsdwqaqdp
      421 gkrraqlale agrapvefda ehlrrvlvnl ldnalrymgg epdslyvaty vsaagavglq
      481 vwsdgapldk tverhlfepf fssesrssgl glyicrelcq rhgasigyqr ltrnlprgav
      541 ggnaftvvfr knarpqdpnt tlfdtivv
//
LOCUS       WP_284408076             613 aa            linear   BCT 25-DEC-2024
DEFINITION  autotransporter assembly complex protein TamA [Acidovorax sp.
            SUPP2539].
ACCESSION   WP_284408076
VERSION     WP_284408076.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..613
                     /product="autotransporter assembly complex protein TamA"
                     /GO_component="GO:0097347 - TAM protein secretion complex
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=66455
     Region          32..613
                     /region_name="TamA"
                     /note="Outer membrane translocation and assembly module
                     TamA [Cell wall/membrane/envelope biogenesis]; COG0729"
                     /db_xref="CDD:440493"
ORIGIN      
        1 mllsslvalq gcsllpgake gtvdnntiqs dagagtgpda fslevrapda vrdyltrhme
       61 lqrfrqlpdl qsseitrllg aaesnarell gtlgyfsptl titmqetpga agaprtitve
      121 vepgpqtrva radidftgte adspqfanrr arvqrswsla pgqpftqdaw dgaksqglrq
      181 lqatryptas iaksraeida drneaqlgvt ydpgppyrfg alrvqggkry sadgarriar
      241 lptgadysea qlldaqmrla ssgyydavfl sletdgtdpq aapvvaqvre aplqkvvfgv
      301 glstdsgprl svdhihnqlp gigwravskv svdrknklls tdwtdlpged gwrwftgaqv
      361 qrettgdyev nssrlrggrs kstdhidrsy flqhdtaksq gtdappssaa isanygwtgr
      421 yfnnttnptr gfglaaelgv gttlrperdp fvraylrwqs fypmgrvdmg egvtrtsrla
      481 lraeggavla rraaeipvtt lfltggdttv rgygyreiga rtsngqlygg rylavasaew
      541 qrpiefrgnr tdfetamfid agavadragd ldprvgvgag lrwrspvgpl qadvaygvqa
      601 kqlrlhlrlg fsf
//
LOCUS       WP_284408050             490 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284408050
VERSION     WP_284408050.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 490)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..490
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=54891
     Region          9..486
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mehtfssglv wfrrdlrsnd haalyhalrq caqvhcafvf dreildalpr adrrvefire
       61 slveldealr alskdphggl ivrhaiahqd ipalaqaldv qavfanhdde plalerdarv
      121 rgaldgmgkr lltfkdhsif eraevltqsg tpytvftpyk nawlrkaddf ylssypverh
      181 aarlaprpag lrrgvpslqs lgfeptglks lhlptgmqga qalfedflgr idhygeardf
      241 pavkgpsyls vhlrfgtlsp rvaaraaher srkgsagaat wlseliwrdf yfqilahhph
      301 vagasfkpay daiewesgih akalfaawce grtgyplvda amaqinqtgy mhnrlrmvva
      361 sfltkdlgld wrwgeryfae klndfdlsan nggwqwasss gcdaqpyfri fnpvsqsekf
      421 drdgkfirry lpqlaglqgk alhapwtaap lelqaagvvl gkdyprpvvd hdearqrtla
      481 rygvvkaakd
//
LOCUS       WP_284408077             395 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284408077
VERSION     WP_284408077.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..395
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=45846
     Region          1..395
                     /region_name="CoxE2"
                     /note="Uncharacterized CoxE-like protein, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3825"
                     /db_xref="CDD:443037"
ORIGIN      
        1 mlidffytlr agqlpvsvke yltllealqa gvvgpnsdda wslddfyhla rtvlvkdekh
       61 fdkfdrafga yfkgvemvad frkdipvdwl rkilereltp eqkaaiekmg wdelmetlkk
      121 rleeqkerhe ggnkwigtgg tspfghggyn pqgvriggag knksavkvwd qraykdyddt
      181 qelgtrnikv alrrlrkfar eghemeldlp dtirstaana gyldikmvpe rhnnvkvlll
      241 mdvggtmdeh vqrveelfsa vktefkhlef yyfhncvydf mwknnrrrfa ekfptwdiir
      301 kynkdyklif vgdatmspye ilqpggsvey dneeagaewl qrlihafprf awinpepqgv
      361 wqyrqsigii qqivgqrmyp lslkgleetm rllsk
//
LOCUS       WP_284408105             338 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284408105
VERSION     WP_284408105.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..338
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34496
     Region          7..336
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mtfpavrrrt lmvalslaga lgtataqsap dalatpgwps kplriivgfp pgsspdltar
       61 tfseplaqal ghpvivenkv gaggnigada vakatdghti glfingnlti akllnpavpy
      121 dpqkdlapls lvgtsplvlt apasqpdvpa hadaraflaa arqagsrwsy gtpgvgtvgh
      181 lgtellkara giapvhvpyp gypqvatgml ggqlqmallp palalsqert gklrligvts
      241 agrstlvpgv pslaeagvpd lnleiwnafa apatmpaavq arlsaliadi arspdvrakl
      301 fqqgwqvagt spqglanriq adtalmarvi rtqgirad
//
LOCUS       WP_284408111             251 aa            linear   BCT 25-DEC-2024
DEFINITION  HesA/MoeB/ThiF family protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284408111
VERSION     WP_284408111.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..251
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26620
     Region          2..248
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mtddqllrys rhimldeigi egqerilaah alvigagglg spaalflasa gvgritlvdd
       61 dvvdltnlqr qiahttervg epkvhsaaqa lqalnpgvrv davqaradke wldewvsqat
      121 vvldcsdnya trhavnaacv ahhkplvtga airfdgqitv idprdplspc yacifppdaa
      181 feetqcatlg vfapmvgiig amqagealkl ivgfgeslag rlsmldgrsm ewtvmkiprh
      241 ghcsvcghat p
//
LOCUS       WP_284408157             186 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Acidovorax sp. SUPP2539].
ACCESSION   WP_284408157
VERSION     WP_284408157.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..186
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=20897
     Region          1..145
                     /region_name="COG4627"
                     /note="Predicted SAM-depedendent methyltransferase
                     [General function prediction only]"
                     /db_xref="CDD:443666"
ORIGIN      
        1 mklnvgcgrn tlagwlnlds qalpgvdiva dldacaatpl pladgsveef llshvlehip
       61 rvlpmmqelh rvarhdarmv irvphgasdd afedpthvrq lfhgsfgyfs qpyywradyg
      121 ycgdwitdrv eltvaqrlrg laheqiweci qsqrnvvvem vahlravkpa rmplrdlqnv
      181 pqivlv
//
LOCUS       WP_284408202             575 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Acidovorax sp. SUPP2539].
ACCESSION   WP_284408202
VERSION     WP_284408202.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 575)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 575)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..575
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64010
     Region          4..574
                     /region_name="COG4986"
                     /note="ABC-type anion transport system, duplicated
                     permease component [Inorganic ion transport and
                     metabolism]"
                     /db_xref="CDD:444010"
ORIGIN      
        1 midkrffprq vvqatgnrwd wallplvlav lfalawggsq marpyqvgdv lplsldpwml
       61 pyyllrttlr mfialgaslv faclfaalaa kyrmaervmv plldilqsip ilgflsitvt
      121 gfialfpgnl fgvecaaifa iftsqawnma fslyqsmrtv paelreaaav fqlsgwqrfw
      181 rlelpfampg llwnmmmsms ggwffvvase aisvshqdik lpgvgsyial aieardlgai
      241 gwaivgmlvg ivlydqlffr pliawadkfr feeggseaqp tswllswmrr tsqlkrvval
      301 fvvplewslt rlrrrhdgts irarpsvphp altragdall aaavmlaviw lvrfihsevg
      361 whevghvfvl gtytlvrvvv lillaavvwv pvgvwigmnp rwagrlqava qflaafpanl
      421 mfplavvliv rwhldpnlwl aplmvlgtqw yllfnviaga ssvpselrya aqnlglsgwl
      481 rwkryllpav fpsfvtgait asggswnasi vaeyvtwgdt tlqadglgsy iahmtaigdf
      541 prialgigvm cvfvmgmnhf vwrrlyamae nrmhs
//
LOCUS       WP_284408190             294 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Acidovorax sp.
            SUPP2539].
ACCESSION   WP_284408190
VERSION     WP_284408190.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 294)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 294)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..294
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=32101
     Region          7..255
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 maerkpfagg lalvtggagg lgraitarli qrgmrcllvd idpqaldrav qalgplamph
       61 vadltdptar qllvqqvqar wgrldllvnn agmvgttpfe qrgqdsirne lelnlmapll
      121 lthsllpllq ctgdgrvvsi vslggmfplp estvysaskf glrgamlclg ldgarlrvrf
      181 sivnpsatet pmlmreaihg gnklqfmdpp qmpdevalqv mrcldqpcle rfvrpaeswt
      241 vrlamllpnc lvralplfqr raeqghqryl dslvarglvr qeegvwvcva darr
//
LOCUS       WP_284408302             229 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Acidovorax sp.
            SUPP2539].
ACCESSION   WP_284408302
VERSION     WP_284408302.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..229
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=24919
     Region          5..184
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mhlepmpdal pagieifrld ldlqadaqqa lqhltpeers rarryvrrad rvrfaqtrna
       61 vrcllgqrlg ccpsevplsm gphgkpfvde apqcapvfnv shsgdhalia ladpcgvmhl
      121 gvdieqqrsd ldadvmldvv ctaqerdsvr rapdvlsafy qrwvgkeavl kaigigvaeh
      181 lcsidispqa dgrlaiasev pewngfqama lpappgyaaa lawrtkesi
//
LOCUS       WP_284408361             273 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Acidovorax sp. SUPP2539].
ACCESSION   WP_284408361
VERSION     WP_284408361.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 273)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..273
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28838
     Region          123..270
                     /region_name="NUDIX_Tnr3_like"
                     /note="thiamine diphosphokinase Tnr3 from
                     Schizosaccharomyces pombe and similar proteins; cd03676"
                     /db_xref="CDD:467544"
ORIGIN      
        1 msgqpvpgwv paarrqaqqp paaprlpflv aghavgsvae gvldeialtp gdslpwllsk
       61 kehlgaaawh ldapagdvta alaalaqalr qagrcgawrd eqlavrnaag erigtverga
      121 vrplglatqa vhlvasapdg rawvqqrafd kpthpgrwdt lmggmvsaad tldtaleret
      181 weeaglriga lhavahgghv efarpssdge gvgymverid wfhatvpegl vpenqdgeve
      241 rfellpaaev harlargeft peaalvlagf ygw
//
LOCUS       WP_284408442             445 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284408442
VERSION     WP_284408442.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..445
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=48532
     Region          319..430
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
ORIGIN      
        1 mssasqapag pvpfwhrlnq ffafplqrkp lfystvlavc smlygvlffl pdvlavllie
       61 vgillaasry gfkvvamgsr glqraedfpd rlddewtalp wklfgillvq givvgwlqrv
      121 stglaelawl avsfllpatm illvqtgslf aslnpaaawg vvriigwpyg llcfflflls
      181 qgaaialall mplfkgwlll plgnwlfiyf gwvmcsllgy amyqnheafg idllpgggld
      241 ddappdrrtp rqiaqeatda lvaqqitdgd lagalgtaye dqrlhgdelp aqrryhrvla
      301 ltdktdtlll haqrfiplll nagqttealk afvtcrerda qfviadaght lalantawng
      361 gdarqaiall ggfdrrfkgh alvpkayelv arvllqgmnr pdmalkvlat lqarhadsps
      421 vaevqwllra hlpqpaagge apstp
//
LOCUS       WP_284408444            1992 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284408444
VERSION     WP_284408444.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 1992)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1992)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1992)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1992)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1992
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..1992
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=215388
     Region          312..1989
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mttthsfral alalalgaaa qahalsiisf spqgevsrvr qavakfdgpa vnfgdpkapa
       61 plsvscsdae agqgtgrwts erewvydfkg dlppgvrcta qvksgfksaa gaelsgtksy
      121 afntggpyvq nirpgtyqpi deeqffmlql ngpatlasvq anvwcvadgv gervpvrlie
      181 gaqregllas qgldktaake plkyvtlacn rrltsggrvq lvfgkgvatp sgvgntiekr
      241 yeykvrerfa adfrcerena qsaclpirpm flsfnapvpr klaeavrlrs dketlkprid
      301 gegdgdtvvn gvrfdppfta qtaftvqlpk dfkdasgrtl rnadsfplkv gtgampplak
      361 faaspfgvve ryaegpkepa llpvtlrnve aalkvqglea gkpadgaapa kvstlqpgsd
      421 adiiawyrkv rrydgylvsr ksarrdvkga lpaalesdss eyvqsrmvsl lsgqggvktl
      481 dlpkpvnndp rpfevvgipl ptgfhvveia spllgkslld erhgegrtmy vrtsalvtnl
      541 gvhfklgren saawvttldk gqvvagakvr vsdcngrela tgttnaqgva lfdglspepp
      601 scqgddggeq ayfvsarapg adgaqdmaft wsdwqrgiep wrfnlptsme prpderahtv
      661 fdrtllrage tvsmkhllrt enrkgfglpd eqpdtlvith vgsgqqytqd ltwrktatgg
      721 lsaentfavp paaklgvyqv qlqggsnsrn sfesgqfrve efrlpvlegr itptdkkplv
      781 rvrsvptdvq vnyvagggaa nlpvrvsalv rgksaqwsdf dafsfmppnq rgaqsqshsd
      841 deeaaagqda rviadklalt ldkngagkla idnvplarrp qelvleatya dpsgevqtlr
      901 stqtlwpaav vagiktegwv saaqkirfqa lalgldgkvq egvplqvqai aritttsrkr
      961 mvggfysydn ktetkdlgtv ctgksdsrgl llcetkleea gevelvatar dkdgntseaa
     1021 ssvwvtrqge iwfggedhdr idllpekkty qpgetaklqv rmpfrhatal vsveregiid
     1081 trvvqlngqd ptvqvkieeg wgpnvyvsvl alrgrlrevp wysfftwgfk aptewwsafw
     1141 yegkeyvapt amvdlskpay rlgvaeirvg tqahqiqvkv vadkesypvr gkaqvtitat
     1201 lpggkpaaga evalaavdqa llqlmpntsw nlldamlqrr swgvqtstaq meiigrrhyg
     1261 rkavpagggg ghsqarelld tlllwqpaiq ldangqakvt vplndalttf kivavadagt
     1321 glfgtgatqi ratqdlqiis glpplvredd qfraqitlrn ttqaamkvev aaratllqld
     1381 kqsvdippge srevawtvta paqlaqtrte ailweieard tagangarda lkatqriipa
     1441 vpltvqqatl vqvdgsfnld vnppadalpg rgglkmslqp klaeglpgvr dwfanypfac
     1501 leqktskavg lrdgtlwqtv vaqlptylda dglanyfppq agsanrgsdt ltayllsaah
     1561 easslhpefa lpdearaame rgltafvegr iqrdfwsprk dldmrkiaai ealsrygkas
     1621 grmlgsvtia pnqwpthtvi dwlnilkrvn dvpqrdqrla eatqvlkarl syqgtklifs
     1681 terddywwwl mqngdvntar lmlalmddpa wkddmgrlan gfisrqqnga whtttanlwg
     1741 glalekfsak featpvagvt raalgsgnag vdwakvervk asdatgaahq ttwfgapasp
     1801 gnfknnsmfl pwsatggken lavthqgtgk pwltlqsvaa iqlkapfaag yaikktitpv
     1861 eqavpgkytr gdvlrvtlev nasadmtwva ltdpipggat ilgsglgrds eiatqgekrs
     1921 gsawaafeer sfeayrsyye ylpkgtikae ytvrlnnvgd falppsrvea myapemfget
     1981 pnarvkveaa ar
//
LOCUS       WP_284408484             420 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284408484
VERSION     WP_284408484.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..420
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44379
     Region          7..420
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mtttpqapag alagirvldl srvlagpwct qvladlgadv vkverpgvgd dtrhwgppfl
       61 kddagndtaq aayftacnrn krsvtidmat pdgqalirqm aqqadvvven fkvgglrqyg
      121 ldhaslraan prliycsvtg fgqdgpyaer agydlmiqam tglmsitgra dgepgagplr
      181 vgvavidlft glyasnaila alhvrertge gqhidmalld vgmavlanqa sgflatgqap
      241 trqgnthpsl vpyqdfptad gamllaignd gqfarfcaaa grpewaqdar fatnplrvkh
      301 rtelvpalqe vtrtrttadw itllqdkavp cgpvntlaea fddpqvqarg lrveqarwpq
      361 gepgdgigri agvasplrls atppvlhrap palgqhtdev laglgldaer iaqlraanvv
//
LOCUS       WP_284408503             379 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Acidovorax sp.
            SUPP2539].
ACCESSION   WP_284408503
VERSION     WP_284408503.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..379
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43067
     Region          12..371
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
ORIGIN      
        1 msdlslqlqq aasqlpvssy fdealfqrel etifqrgpry vghqlsvpda gdyyalpqeg
       61 egralvrnaq ggvelisnvc rhrqavmlkg rgtlqghgkg haggnivcpl hrwtyspggq
      121 llgaphfaqd pclnlnnygl rewngllfed ngrdisadla gmgpraelsf dgfsldrvem
      181 hecnynwktf ievyledyhv gpfhpglgnf vtcedlswef qkhysvqtvg vastfgkpgs
      241 diyrkwhdvl lryregklpe rgaiwltyyp himvewyphv ltvstlhpvs ptktmnmvef
      301 yypeeitafe refveaqqaa ymetciedde igermdagrr alyergdnev gpyqspmedg
      361 mqhfhewyra amgdavpqr
//
LOCUS       WP_284408518             279 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Acidovorax sp. SUPP2539].
ACCESSION   WP_284408518
VERSION     WP_284408518.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 279)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 279)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..279
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=29889
     Region          10..279
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mnlppsrapr aliaedepll aaalrqelar awpdlqiaat vgdglaavqq aldlrpdvll
       61 fdirmpgqsg leaaaelada wpadtpfpal vfvtaydqya vqafeaqavd yllkpvqper
      121 lrkavqklqa alarqaapaa ldfeatlarl ralvalpgaa apgmagaaah papltviqas
      181 sgaqihlvpv advvvfeaad kyvrvltatq eylirtplke laaqldantf wqvhrgtlvr
      241 asaiasavrd esgrlhlrlr erpetlavsr lyahrfkam
//
LOCUS       WP_284408572            1207 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Acidovorax sp. SUPP2539].
ACCESSION   WP_284408572
VERSION     WP_284408572.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 1207)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 1207)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13208672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1207
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..1207
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=133433
     Region          352..>387
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Site            359..365
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:438708"
     Region          <529..1203
                     /region_name="DNA2"
                     /note="Superfamily I DNA and/or RNA helicase [Replication,
                     recombination and repair]; COG1112"
                     /db_xref="CDD:440729"
ORIGIN      
        1 mkkvnsetqr nissalqlwq afeylnpqkp pevkreknlc nweipvdsps dhdmpwvdpe
       61 krddldklfm vredstkrfl lyagvlpgev ytnaarvild tpaihddekp spanaaslvl
      121 aiddegyvag lpfvsstpwa lgnlaaasrk gtrfdfrgff gtdgaeaatv ealkallvkr
      181 tllppqadns relstvssll tseqdeakae eirktyrtit addvramtal lfknlgwaps
      241 seapwviktq svgkkskkem ddplnsfyae evetvqrafl agdtgaalnq flasiesper
      301 vdldakgdka plvdglhpsk lplaawpgsh plvtaqqfav ntihrdlasa glfsvngppg
      361 tgkttmlkdi vatvvqqrad almafnhpnd afseelkved hkykvwklda slcgygmvva
      421 sanngaveni slelpglsai deavkldyfs evsdsmglkr kesrpaspqt wglisaalgn
      481 stnrnafast fwfpnkeckk lpdgtpnpla qvslpewvdn qkasapswqd akaryqsarq
      541 raaaevkeaa dladtlerlp rsqdtlvqlq aqetelqgel vqlesaaska kqasdaavaa
      601 lvvstsrleh aqalaaskak heeavalasa hvtsrpvgdv nalmmemaea eseekasqrn
      661 lvnhdrcrpg lltrwfsrdk vaewearhrq lndlieraqk kfqdaqklmh siehwdtklr
      721 slheqeqkck savnaachrm enagfprits lsvvaaehak cqgnasacrh elqrvtglfq
      781 qrtstldelr stqaqlsgki atmvkkleaa slrdssrkaw hlfalsrdef hqvspyqddg
      841 alfnarrelf vaamelhkaf vvhawsklkp tlsvfidllq gklhgwrvqg gvmplwdaff
      901 vtvplgstaf asfprlfkgv kgndlawvli deagqatpqq aigaiwrskr vvivgdpiql
      961 epvvnipqel vaplqaycdt lpkyvppdas vqtladrsnr ygtlmgsked gtdiwlgspl
     1021 vvhrrcinpm fqianaiaye nrmvygtred asfaatpsaw ldasnddaqg hwiesqakra
     1081 legiekltdg kvrdekgklr iyvitpfrlv germrdllrv rfgretaqem cgtvhtfqgk
     1141 eadfvifllg gdparrgvis syagrkpnlv nvavtrakkr lyvignkefw csasdfndyy
     1201 ktmerlm
//
LOCUS       WP_284408638             542 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Acidovorax sp. SUPP3334].
ACCESSION   WP_284408638
VERSION     WP_284408638.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 542)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 542)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 542)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 542)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..542
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57482
     Region          38..541
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mprllsalrs lpllllaaal tlpvlavlas wlpgtvggae agailremaa tvlpgyfatt
       61 vwlglavaig aavvgtataa avtlfdfrgr rtlewllllp lampayvtay aytdflqfsg
      121 plqvwlrety glqgrllpev rslggavwvf ifslypyvyl lartalgera ahlmeaarll
      181 gaplarrvrt valplarpav aagvalvlme tladfgvvsy fgiqtfttgi ykawlsmdnr
      241 laaaqlatil lvlvmlllql eqraqrrmrf aaggvgrags aeaqpqrlqg lrgvaawavc
      301 llpvifgfva pmafmlrpla adwsvlpwsr flewagnsvr lggitavlav aialvlafav
      361 rrragpltrg vaqlaslgya vpgavivvgl llpvgwlqaa apqwglpsii tatavgivwa
      421 ylvrfcaval qsmqsgyari paslddsarm lgaggaglla rvhwpllkrs taaaallvfv
      481 dvmkelpatm vlrpfnsdtl avvayqlard erlgeaalps lalvavglvp vvllsrtlrs
      541 rq
//
LOCUS       WP_284408640             328 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Acidovorax sp.
            SUPP3334].
ACCESSION   WP_284408640
VERSION     WP_284408640.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..328
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35343
     Region          1..326
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrasrllsiq mlletqgrms aqaladalev svrtlyrdvd qltaagvpiy aergrhggfa
       61 llpgwkttlt gltpseaqav flsglsgpag dlglgedvag arlklltalp apwredaqri
      121 sarlhldpvd wyreseptph lstvaaavws grqlalryes wadtvertvg plglvlkagv
      181 wylvalpigh gakdggprty rissiraaea lgtsvrrpar fdlpaywtqs irrfesslyt
      241 geaallatpa glkglsalsa avaravataa psrrkdgrra vtipiesvdh acgqlmrqsp
      301 evevlrpaal rralmeriea tarlyrlr
//
LOCUS       WP_284408686             575 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Acidovorax sp. SUPP3334].
ACCESSION   WP_284408686
VERSION     WP_284408686.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 575)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 575)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..575
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63803
     Region          4..574
                     /region_name="COG4986"
                     /note="ABC-type anion transport system, duplicated
                     permease component [Inorganic ion transport and
                     metabolism]"
                     /db_xref="CDD:444010"
ORIGIN      
        1 midkrffprq vveaggnrwd wallplvlav lfalawggsq marpyqvgdv lalsldpwml
       61 pyyllrttlr mfialgaslv facifaalaa kyraaervmv plldilqsip ilgflsitvt
      121 gfialfpgnl fgvecaaifa iftsqawnma fslyqsmrtv paelreaaav fqlsgwqrfw
      181 rlelpfampg llwnmmmsms ggwffvvase aisvshqdik lpgvgsyial aieardlgai
      241 gwailgmlvg ivlydqlffr pliawadkfr feeggseaqp tswllswmrr taqlkrvaav
      301 fvvplewslt rlrrrhdgts irarpsmphp altragdaal aaavmlaviw lvrfihsevg
      361 wgevghvfvl gtytlvrvvv lillaalvwv pvgvwigmnp rwagrlqava qflaafpanl
      421 mfplavvliv rwhldpnlwl aplmvlgtqw yllfnviaga ssvpselrya aqnlgltgwl
      481 rwrryllpav fpsfvtgait asggswnasi vaeyvtwgdt tlqadglgsy iahmtaigdf
      541 prialgigvm cvfvmgmnhf vwrrlyamae nrmhs
//
LOCUS       WP_284408743             656 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Acidovorax sp. SUPP2539].
ACCESSION   WP_284408743
VERSION     WP_284408743.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..656
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70959
     Region          1..491
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mhiesvtitg frcygpvptv ihlspgltgf vganasgkta alqalmrlfg vtralrtvvl
       61 sdfhvpptea qrpksrtlti dvrlslpela dgsataatva pvfrhirver pggtplcrlr
      121 lrarwdddgt vegtvsqels wigtaeptvr ddqafpvapa drgliqlfyt pairdaatqi
      181 rattgalaar llraiewsag tqsavnaate qlttafgsek aiqaisrsls qrwdalhegd
      241 idcapelslt srrfeevvar igvmfkrgpa gqdrgleals dgqqslfyfa laaavfdver
      301 aavagrirgf rsedlsvpal tlfaveepen hvtpyylsri lkqirslvet gagqalvssh
      361 apsvlgripp edvrycqrdt asgtstvkpi pmpagsveai kfvrnaflaf pelyfarfvl
      421 lvegdseriv lprlaealdl lvdpsfvaiv plggrhvnhf wrllkglgip yatlldldlg
      481 rdgggfgrvk nvlqqllalg tpreqimtls ndtvltdehl atmdtwdgan legwldyler
      541 sssvffcwpl dldlamlhaf paayaatieg tgprmtneaa aevvlgtagp gltgytgnaq
      601 pfcahmaayr yhflthskpa thlralthid lpalragmpp alkrvlqria vevspl
//
LOCUS       WP_284408767             132 aa            linear   BCT 25-DEC-2024
DEFINITION  tautomerase family protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284408767
VERSION     WP_284408767.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..132
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=14313
     Region          <14..59
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mphtvihlcg padaalarra tdavaeitqr vlgkalpvia ttvqfipaeq wfiggaslae
       61 lgqstfhldi sitdetntka ekarylrevh aafsdllprl hevsyihlid araaaygygg
      121 rsqewrhqqa gv
//
LOCUS       WP_284408842             739 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Acidovorax sp. SUPP2539].
ACCESSION   WP_284408842
VERSION     WP_284408842.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 739)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 739)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 739)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..739
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=79637
     Region          30..711
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mpsplapplt gflpshhdpl vvaasfaval lasyvtlsla rrvrtsqsri glawwaagsl
       61 vmgtgiwsmh flgmlafelp ialgftpait alswlaavaa savalglasm ervrrrhlav
      121 galamgagis amhyigmram hlsigivwng fyvalsvava vlasatalyl fqalrgmhgh
      181 rrrvfqaaas lvmalaicgm hylgmaaaqf pqgtvclsad slggsglaam vaiftlllml
      241 stlfisilda rlqnvarrlt rslqdsnakl qqanaelqkr afadaltglp nrllfedrla
      301 hallrlertn hhrvldrlav lfvdldgfkp indsfghaag dailseaaqr lraearesdt
      361 vtrvggdefl llledvgnta dcivvanril aalalpfqva grqvqigcsi gvvlhpdhgd
      421 rdklvanada amyaakragg ngyamfephm gsdasdqlel qndlrhalar gelalhyqpk
      481 idgkrgring veallrwhhp krgmvsplvf iglaerfgli gqlgawviee acrqmadwar
      541 sglrmrvain lsvhqlresg laeriehalq fhgldssqll ceitesvame dtkatqrtfe
      601 glarigvfls iddfgtgyss lnylrqlpaq qlkidrsfvn dleheedara vvdavvrlah
      661 alglrvvaeg vetsgqrdil lamrcdelqg ffyarpmpad vllawaqgdk pegsadfaps
      721 viggleales lpfdaaprg
//
LOCUS       WP_284408866             284 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Acidovorax sp. SUPP3334].
ACCESSION   WP_284408866
VERSION     WP_284408866.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..284
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=30189
     Region          14..284
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mtstpascaa prgliaedkp llaaalrhel aqawpelqiv atvgdglvav qqalalqpdv
       61 llfdirmpgq sgleaaaela dawpagtpfp alvfvtaydq yavqafeaqa idyllkpvqp
      121 erlrktvlkl raalerqaap aaldfeatle rlralvslpg aggagaaglp gaapqapplt
      181 viqassgaqi hlvpvadvvy feaadkyvrv ltatqevlir tplkelaaql daevfwqvhr
      241 gtlvragaia savrdesgrl hlrlrdrpes lpvsrlyahr fkam
//
LOCUS       WP_284408884             330 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284408884
VERSION     WP_284408884.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..330
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34794
     Region          29..328
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mnhsplqrrg vlrgaaaagl alatgrvlaa dpwpakpvnl vvpfpagggt dafarpfaaq
       61 fakstgkmli idnrggaggt vgasfaakaq pdgytlfmgg thhviapsmy pkldydiekd
      121 fiplallanv pqvlvvnprt vqattmpqfl dflrrnpakl nyasagagts hhlagelfkl
      181 qtktfithip yrgagpalqd liggnvdmmf dglgssaahi kggrikalmv agarrnpafp
      241 dvpcaaevgl pdytvttwyg lwapkgtpad lqariveetq rlgtaedlka vwakngadyg
      301 glsqtqfaam vhsevrrwak vvkdsgakld
//
LOCUS       WP_284408906             829 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Acidovorax sp. SUPP2539].
ACCESSION   WP_284408906
VERSION     WP_284408906.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 829)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 829)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 829)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 829)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..829
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..829
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=87557
     Region          68..803
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mlshrfeppp drpdlaagtp apdapcaepa lllddpqewa sfgrahlpag sgadadataq
       61 tweshvvleg mhcaacalti edvlravpgv aqadvsaatr rarvvwnaaq vrpsqwiaav
      121 rragyralpa mdafaraqrq sehrralwrw lvagfcmmqv mmyawpayva qpgdltaeme
      181 qllrwaswvi tlpvvifacg pffanalrdv rlrrvsmdlp valgmaitfg vstagtfdpa
      241 gifgrevfyd sltmfvffll tgrwlelrlr drtagaleav mnrlpdsver lgadgafarv
      301 avrrlavgdt vrvlpgeafp adgcitrgdt ladealltge stpvarpegs avtagsynlq
      361 savqvkverv gadtrfaqiv almesaslqk prlaqladri arpfliavla aaalaaawww
      421 ptdpghalmv avavlivtcp calslatpva mltaagtlar qgvlvrhlqa lealagvdtv
      481 vfdktgtltr dgmavrgvhp apgleradal alaaavarhs vhpvsralva aasreglpaa
      541 srwhvlevhe lagqglvarl rgagegadga adarsrlalg ertvrlgsvr hagaggpagd
      601 gaggsvmeqq vvlseqrsdg trvelarfdw sedlrpeapr avrrlrdagv avqllsgdrp
      661 gavrriatqv gieraqgdct pqdklallqa eqarghrvam vgdglndgpv lagahvsfaf
      721 gravplaqsr adfvvmggdl eqvvqtllla rrtlrvvrqn lwwaalynal cvplavvgwm
      781 pawlaglgma lssllvvana arlaagtgsp hapasapaah sdvplpegv
//
LOCUS       WP_284408973             420 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284408973
VERSION     WP_284408973.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..420
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44392
     Region          7..420
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mtapsqapag alagirvldl srvlagpwct qvladlgadv vkverpgvgd dtrhwgppfl
       61 kddagndtaq aayftacnrn krsvtidmat pegqalirqm aeqadvvven fkvgglqqyg
      121 ldhaslraln prliycsvtg fgqdgpyaer agydlmiqam tglmsitgra dgepgagplr
      181 vgvavidlft glyasnaila alhvrqrtge gqhidmalld vgmavlanqa sgflatgqap
      241 trqgnthpsl vpyqdfptad gavllaignd gqfarfcaaa gcaewaqdar yatntlrvqh
      301 raelipamqa vtrtrttaew iallqdkavp cgpintlaea fddpqvqarg lrveqsrwpq
      361 gaagdgvari agvasplrls atppvlhrap palgqhtdev ltemglaper iaelrtrkvl
//
LOCUS       WP_284409140             606 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Acidovorax sp. SUPP3334].
ACCESSION   WP_284409140
VERSION     WP_284409140.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..606
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=67031
     Region          86..550
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mnpanpadap trqalaldaa alrqkyaher darlkpqrna qyigtdagfe aleddpyieq
       61 plvreavdet idvlvvgggf gglvcaanlk kagiddfril dkagdfggtw ywnrypgaqc
      121 dtesyiympl leetgyvpte kyahapeifa haqriarhfg lyersllqtq vaemnwdeat
      181 rrwiistdrg dvlraryvft asgplnrpkl pnipgierfk gklfhtsrwd yaytggnasg
      241 gltgladkrv avigtgatav qcvpyvaqya qhlyviqrtp vnvgergnap tdpawakslq
      301 agwqrermhn fngwiegvka ekdlvadgwt rlfygvragw iptdgtpltp eiamplaeqa
      361 dfrigsewre rvaqtvkrpd vadglkawyg vlckrpafnd nylpafnrdn vslvdtrgag
      421 ldeigehgft hagveypvdc ivfatgfevg tdysrrsgft vrgvggktla qhfengmrsl
      481 hgfyahgfpn ffflgvgqng vkpnftdmlt eqvehlvdli nttrkvgatr ieatasaeaa
      541 wlqtlvdksq maraylaact psyfndeggd lnkswianny gggtlefaql lkawrergdh
      601 eglnvq
//
LOCUS       WP_284409183             280 aa            linear   BCT 25-DEC-2024
DEFINITION  DODA-type extradiol aromatic ring-opening family dioxygenase
            [Acidovorax sp. SUPP2539].
ACCESSION   WP_284409183
VERSION     WP_284409183.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Vaillancourt,F.H., Bolin,J.T. and Eltis,L.D.
  TITLE     The ins and outs of ring-cleaving dioxygenases
  JOURNAL   Crit Rev Biochem Mol Biol 41 (4), 241-267 (2006)
   PUBMED   16849108
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Siegbahn,P.E. and Haeffner,F.
  TITLE     Mechanism for catechol ring-cleavage by non-heme iron extradiol
            dioxygenases
  JOURNAL   J Am Chem Soc 126 (29), 8919-8932 (2004)
   PUBMED   15264822
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..280
                     /product="DODA-type extradiol aromatic ring-opening family
                     dioxygenase"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016701 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30145
     Region          20..276
                     /region_name="45_DOPA_Dioxygenase"
                     /note="The Class III extradiol dioxygenase, 4,5-DOPA
                     Dioxygenase, catalyzes the incorporation of both atoms of
                     molecular oxygen into 4,5-dihydroxy-phenylalanine;
                     cd07363"
                     /db_xref="CDD:153375"
     Site            order(26..28,65,130,186,240,268..269)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:153375"
     Site            order(26,65,240)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:153375"
ORIGIN      
        1 msdlerarap tdsgrnaelp alylshgapl favdagetgp altrwgqevq vrfphlrgvv
       61 vmsphwmprs pkvmtgpqpa twhdfggfpp alyalrypaa gapalaetvl arlrsagiaa
      121 egdaerpfdh gawvplmhlf pdarlpvvqv alpstagpae vyamgaalqg lrsegvlvvg
      181 sgsmthnlae ffgganeplp yvtefsrwie damqrrdwpa lldyrrqaph aerahpsedh
      241 flplffalga agpeaqahyl srevrygala mdafalqsaa
//
LOCUS       WP_284409215             735 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Acidovorax sp. SUPP3334].
ACCESSION   WP_284409215
VERSION     WP_284409215.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 735)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 735)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 735)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 735)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..735
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=78715
     Region          58..733
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mrplcptasl wltpllalsa pgamaqeggg tagalptvvv keqampgald qpaegasrlg
       61 lsvretpasi dvvsrqvlge rglrtvteaa qaavgvtagd fpaepsafsm rgfansqint
      121 lyngikigpp nmtsrvmdta nlerieflkg aaslmsgega sggavnfvtr aphrgpvqte
      181 vetaagsfge rrlrlgsggt tvwkdldyri dmsgsesdgp vqatgqhnrh lsggldwhvq
      241 pglkffvage ikrdrgssyw gtplvsaaap giepeggvvs gtytsgfngs algpvaidrr
      301 tlrtnynvld nrnearetwl ragmdwridk aftlrtqvyr ytaartwfnn eiaafnagtg
      361 lvdrerfyva qdqtsvgqkt elqwdgqiag rdnrwvaale ysdldltrpg aanfpgdsvs
      421 lvnpdrgtyg pltrqwqtsg vrntvlaled rfsvapgwal igglrhesie lsrtstdaag
      481 asrtgfpfdk twhpttgrlg vtwapaagtt iygqyatgad vaannlfllr gtqpldltrt
      541 rnleagvkqs fwqdrgewtf avydsqrrnv yaaqggqsla lagslqsrga easlalrpda
      601 hwsvwsnlal nraryedyal agggslsgnt ppnaprvvan agvgyrfvag vpvqvsaslr
      661 hvgerfhsda ntvrlsayta ldaavavdva rgvqltlrgr nltnrvyaaw adpfypdqil
      721 lgaprsfela lrwvl
//
LOCUS       WP_284409357             701 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Acidovorax sp. SUPP2539].
ACCESSION   WP_284409357
VERSION     WP_284409357.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 701)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 701)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..701
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=75367
     Region          105..701
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mraalqgrtl fgralaprha fsgeearall mgepnvamvl ldvasepvgg tgaaagtala
       61 lvdfirhtar lpnarivlrt dqpgpvtdld tllqydindy rpkselthdr llalvvtsvr
      121 syqrlcaaea srrslelivr ssasllettd prafasgvit qlaallgvac halvcaqqge
      181 tagrfqvlaa agrfavladg pfdavaarpe wsvlrrvleg rcngyaadgg valyighqgr
      241 qgmavfidvp aargaldtqm ldvfcanlgt llhnhgllar lheyayydpl vrlpnrahfv
      301 ekvdecarlg trghilalld iddfsatndv mghrfgdcll ervaralsaa lppgvllarl
      361 gadtfgvlga vaqvslqrll dcvrqplavn gvaqkvsltc gyvflpevpq agadlvkdat
      421 ialkrakrdh rgqhleysdh mgaeartral llsdlraaid taklflvyqp qidlatrrlv
      481 glealvrwra ddgqlispdq fipvaehsgl ivalgkwvls tacacmrell eaghapgrma
      541 vnvssvqlqd paffdtvcaa ladsglqgpq leleitesva alptqllnst lsslraqgis
      601 iaiddfgtgy sslsylerla ldrikidrsf vrhlgephgv riaemvaqlg rklglqvlae
      661 giedaaalra lldmgchegq gyhiampmek valmawlqqr r
//
LOCUS       WP_284409375             401 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284409375
VERSION     WP_284409375.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..401
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=42264
     Region          35..374
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mqdaqplydl aplarmvllg avialgplaw vwlrnrgtsr vrrlqaltvl tlfltfdlvl
       61 fgaftrltds glgcpdwpgc ygnasplgah aeisaaqqam ptgpvthgka wvemihryla
      121 sgvgmliivl tvgawwqrsr aarrqglppa lspwwptatl vwvclqgafg altvtmklfp
      181 aivtlhligg lvllallcvq avrethaarg vppvalgrgl rgllvattvl lavqivlggw
      241 vstnyavlac ttfptcqgsw wpdmafgqgf eiwrplgllq dgshitfagl taihyahrla
      301 ayavllalgl lawrlhraal lpaqarwiag lalmqfatgl snvvldwplv aavlhtggaa
      361 alvvvltwal aasravgaar plaaaagapt taptgatris a
//
LOCUS       WP_284409377             444 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Acidovorax sp. SUPP2539].
ACCESSION   WP_284409377
VERSION     WP_284409377.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..444
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47329
     Region          21..444
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 maaraclafa galclahpaw allpiqhwte psgarvwlve spaipmvdvq vdfdagarrd
       61 paaqaglasa vaamsskgvr aqgdepamde nalgeawadl gasfeaaadr dglsfslrsl
      121 tepdlldraa rlaarqlaqp sfpqdiwqre rsrwaaalke setrpgtaaa kafgsavygs
      181 hpygqrttpd tlgrieiadm qayhgryvet crarvsivga vtrpqaqalv atllsqmpar
      241 dpatcqplpp vpevqalaap vqqdipfasa qahvligqpg farrdpdfla llvgnhilgg
      301 ggftslltse vrekrglsys vysqfspgln tgvflvglqt rpdqaaeavk vsrdvlarfv
      361 aqgpteaqlk aakdnliggf alridsnrkl lanvvniawn dlpldylehw tdrvqaltaa
      421 dvraamarkl qpdrmvtvvv ggqp
//
LOCUS       WP_284409391             307 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284409391
VERSION     WP_284409391.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..307
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=32219
     Region          2..305
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 msvaalaqgf psrpirivig fpaggpldqh arlltdklqa vlgqpvvvdy ksgaggtvga
       61 qdvmkappdg htlmlantgv mvinpalysr lpyqtlkdft pvartamqpl allvnpklpa
      121 ktlpefiqya rakpgqvnfg sagnggishl vpemfktatg lfmvhipyrg sapaftdlma
      181 gqvqfmaesi pqaaayhkqg kvralavtsr qrnpalpdvp taiesglkgf evvgfygfla
      241 pagtpkdvva klsdafgqvl qspevrermv sqgadpaflg adafaaflat emprwatava
      301 qsgakld
//
LOCUS       WP_284409395             820 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Acidovorax sp. SUPP2539].
ACCESSION   WP_284409395
VERSION     WP_284409395.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 820)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 820)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 820)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 820)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..820
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..820
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=90114
     Region          160..817
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mrwlsshrpd wevspsdfaa grdgvarspa favpgacqal vldlergata lpdwaaqgrt
       61 qplvlcldpa qealaaralr lgpgdyvlra edgahlpqla qrlavllqah aphgpmpaav
      121 palpwpdepp sqrallqttl asmsqglytv gpdgritvyn drvlellelp ralfdarptl
      181 melkqlqqar gdfgesaelv daqarayvqs aggipspavy wrrtrhgrtl evhttqlpdg
      241 gmvrtftdvt dhvrtqaelr vsearfrsls dlssdwyweq dasfrfihfv ggrnpvgmep
      301 gevvgrtrwe lgalnmteed waahrrllda repfrelelq rlasdgtayw vsisgvpvfd
      361 eagafqgyrg vgrsitdrkq veaeierlaf fdvltglpnr rllidrlyra tlsvgrtgrh
      421 gvllfidldn fkdlndtlgh dmgdrllvqv aqrlqgcvrq sdtvarfggd efvvlaeglp
      481 aeawaasada sllarkigna lslpylldgi shhstpsigl tlfgesagsv ddllkhadma
      541 myqakaagrn avrffdpgmq aavsaraale aelrralqvg elmlhyqpiv drrgqmlgae
      601 alvrwqhpqr gmvspgefip vaeqsglivp lgqwvlehgc rqlvawsrsa atahlvlsvn
      661 vsvrqfrqpd fvdqvlqalr esgaqprlfk ielteslllt dvedviarme klrshgvgfs
      721 lddfgtgyss lsylkrlpid qlkidqgfvr dvltdpndaa ivrtilalah sldldvvaeg
      781 vettgqlqfl qrhgchafqg ylfgrpapat vleravrpal
//
LOCUS       WP_284409530             153 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284409530
VERSION     WP_284409530.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..153
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=15683
     Region          1..135
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mafgrlertt gpqpmsdinm tplvdvmlvl vvifiltapl lassirldlp radgatpgap
       61 pqsvtvvldk egqaylddvp lapqalaarl aqlareqpdt evqlradtav pygrvvevmg
      121 aanaaglrri gfvadpaapa apsaapaspa aar
//
LOCUS       WP_284409746             219 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Acidovorax sp.
            SUPP3334].
ACCESSION   WP_284409746
VERSION     WP_284409746.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..219
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=24378
     Region          <22..211
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 maatkkiagd epqliapayw aearkhlvkk drvmkrlipe lgdvalrqrg dafttlarsi
       61 vgqqvsvasa qkvwnrfaal prtmtpasvl klkvddmrga glsarkvdyl vdlalhfdsg
      121 klhvkdwdam ddeaiteelv airgigrwta dmflifhlar pnvlplddat liqgisqhyf
      181 sgdpvsrsda revaeawkpw csvaswyiwr slaplpvdy
//
LOCUS       WP_284409749             390 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Acidovorax sp.
            SUPP2539].
ACCESSION   WP_284409749
VERSION     WP_284409749.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..390
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41776
     Region          <29..360
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 matlpawpaa partatatpa apeaglawif edprskalla eveqvapsda gvlitgesgt
       61 gkeliarylh srsprsaapf vavgcgafse alvdselfgh esgafpgafg aqpgwfeeah
      121 ggtifldevn dlplavqnkl lrvlqqrevv rvggrqpipi dvrivaaasv dlqalvlqqr
      181 frkdlyyrln vvslevhtlr erpgdivpla rhfidaysrr lgyprpqltp aaeralqqap
      241 wpgnvrelen tihrtlllge grtldaadlr lsgtarpgte peapapaapp qaaspstpgl
      301 pllrqavrql ceahvpalyq tvedavllev frwchysqse aarvlglsrn vvrarlirlg
      361 evgaprraga dagappaefp pdtdsespsp
//
LOCUS       WP_284409765             319 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284409765
VERSION     WP_284409765.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..319
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=32778
     Region          29..318
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mrrdtflksl aalaaagalp lsaqaanavk mmlpanpggg wdttgralgr alqdagvass
       61 vtydnkggaa gaiglaqfvn sskgdpnalm vmgavmlggi itgkppvnlt qatpiarlts
      121 eynvfvlpan spfktmgevv aqlkkdpgsv kwgggsrgst ehiaaamiar eagvdpakin
      181 yvafrgggea iaailggnvt iggggysema eyintkkmvp vavtsgqrlk gssvptlkeq
      241 ginveignwr gvyaapgisa eqrnaliamv dkalkskswa esmekndwtp awmagdefgt
      301 fvdtefaslr atmvkagmv
//
LOCUS       WP_284409805             325 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284409805
VERSION     WP_284409805.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..325
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33813
     Region          27..323
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mhahpafrrt lllcglalla agpaaaqdsy pskpitivvg yppggstdlt grtvaqelga
       61 rlgvpvvien vggaggaiga qkvasaapdg ytllvgasne iainklvtkk vkydvkdfta
      121 igviasqplv lvastgsgvk naaeftqrvs knpgkysygs sgvgtslhla gemvkeqgkl
      181 fmthipyrgv apltndllgn nlefgvfvls sglphiksgk vvalgtteak rsaitpdipa
      241 laelpqyknv digvwfalmg paklpkpvhd klkkalneal qspdfrkkme asgstvasts
      301 lnadqfiase vakyqkivef akiee
//
LOCUS       WP_284409893             323 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284409893
VERSION     WP_284409893.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..323
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34192
     Region          1..321
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mslnrrhamv ygaaalastt amgqtanwpt ktlrlivpyp pggssdiiar aisqplsdml
       61 kqnvivehkp gangnlgadf vakaqpdgyt mllcdvgala ispsvytklp fnpskdlrga
      121 tmlaysphml vvhpsvpann lkelialskt adlnfavtat gsaphlagva lerasgarwq
      181 yvpykggvta iqdtmagqtq vlmngmlatl phvqsgklkv lalskgtrmp lladvptiae
      241 qgipgfesgt wqgilvprga pdpivqrlnt alisvirtpe irsrlagqga evvtmavaeq
      301 dkffekerar wasvvsdaqi rld
//
LOCUS       WP_284409897             203 aa            linear   BCT 25-DEC-2024
DEFINITION  KdsC family phosphatase [Acidovorax sp. SUPP2539].
ACCESSION   WP_284409897
VERSION     WP_284409897.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..203
                     /product="KdsC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=21286
     Region          33..202
                     /region_name="KdsC"
                     /note="3-deoxy-D-manno-octulosonate 8-phosphate
                     phosphatase KdsC and related HAD superfamily phosphatases
                     [Cell wall/membrane/envelope biogenesis, General function
                     prediction only]; COG1778"
                     /db_xref="CDD:441384"
ORIGIN      
        1 mdqplarata gaatpasqpl pplqpalqfd aqlllraqgv rvaffdvdgv ltdgglyfse
       61 agetlkrfht ldghgikllq kagitpavvt grdapalrlr lknlgvvhar fgtedkrpaa
      121 esilaelgld waqaavigdd wpdlplmrrc alacapchah iearavahhv taaaggagaa
      181 refcdlllva sgryaqllea yta
//
LOCUS       WP_284409906             366 aa            linear   BCT 25-DEC-2024
DEFINITION  lactonase family protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284409906
VERSION     WP_284409906.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..366
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=38593
     Region          32..363
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 malpsaflra salaplaaav lmaasgaasa atwvyvsnad sqdvsvyeld raaarlqpve
       61 tlpvggqamp mavspdkrql yvalrsqpfr vvtlgidpas grlkklgeap ladsmanidt
      121 datgrwlfaa sypghkitvn sidkdglvga vqqliptapn ahaihadaan ryvfatslgg
      181 dhlsswrfda atgkltanep altaiapeka gprhfvwdka qrhmyvvdel daalhvldyd
      241 aergtlrevq rtttlppgft gkpwaadlhl spdgrtlyas ertsstlstf rvdaatgqle
      301 plgqvpteks prgfaidssg rfliaagqds hsvslhpidp atgvpgtptr vaagknpnwv
      361 eivdlp
//
LOCUS       WP_284409977             723 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Acidovorax sp. SUPP2539].
ACCESSION   WP_284409977
VERSION     WP_284409977.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 723)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 723)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 723)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 723)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..723
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..723
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=79689
     Region          76..723
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mthpdhapaa aalaffhpra taiaaallag maglpatals qpqaeaasqa alptvhvtse
       61 ydaddvrpeg vttatktyma pkdipqtidt levnkyksyg indlavmldg vpgvntkydm
      121 rgegvmirgf nadsgdiyrd gvresgqvrr stanveriei lkgpasvlyg rssgggiinm
      181 vskqarfdak ssinlrggsw dnvggtldin rvlnenvavr ltadreqans frsgirnrne
      241 mvspsilvdt rtglrwtgqy tydtvwrvpd rgpaydqlpa gvsirtgfah pddmvedrlr
      301 vlrsdlsydf npawsvrwva skreasqdfd hyfagtycna rgrtstgasc dyagrvrpny
      361 awqqtrnetl sntvdltgkf tlaglqhdll vgmeaseeer qprlssgaas ftydplrpip
      421 wapkpaqgap tqynlheaqs ralylqdlvs lgtqwkllag lrydrfdfhs tnlltsagrg
      481 ydgdsvsprl gvvwqpvreh siyaswnksy spyggrgmit vdtsasavyd depqhsrqfe
      541 igaksdwldg klstqvsvyq lehyniryrp davndpftwa vrgkersrgi efsaagrvap
      601 swyvrggvgl msakvtedrs apanvgkylq dtaqrngnvf lryapqspwy geigvthtsa
      661 rwlnaantsr lpaytrwdam vgwraapwtv tvavtnlldk eywrsvdmpg aprgvlvsat
      721 yqf
//
LOCUS       WP_284410170             384 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Acidovorax sp.
            SUPP3334].
ACCESSION   WP_284410170
VERSION     WP_284410170.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..384
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40499
     Region          42..382
                     /region_name="HisC"
                     /note="Histidinol-phosphate/aromatic aminotransferase or
                     cobyric acid decarboxylase [Amino acid transport and
                     metabolism]; COG0079"
                     /db_xref="CDD:439849"
ORIGIN      
        1 mtstatptaa avasaplpac galdrirpdv ramhsyavqp ssgmlkmdam enpfrlpaal
       61 qsalgerlga lalnrypgdr iadlkaalaa yagmpagham vlgngsdeli tllalacaqp
      121 gagqratmla pmpgfvmypl saqlqgldfv gvpltadfel depamlaaia rhrpaityia
      181 ypnnptatlw degavqriid aagavgglvv mdeayqpfas rtwidrmrae parnthvllm
      241 rtlskfglag vrlgyliapa alaaeidkvr ppynvsvlnc eaalfaleha evfaaqaael
      301 rqertallaa lralpgveka wdseanmvll rvadaartfe gmkarkvlvk nvstmhplla
      361 nclrltvgna adnaqmlaal qasl
//
LOCUS       WP_284410286             151 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Acidovorax sp.
            SUPP2539].
ACCESSION   WP_284410286
VERSION     WP_284410286.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..151
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16446
     Region          3..105
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 makrkslads pcpvarsldv vgdrwsmliv rdafdglrrf gefqaslgaa rnilsdrlrt
       61 lveggvleia pasdgsayqe yvltakgetl fpvvvalrqw geahlyarge khsvlvdrat
      121 gkplpkallr ledgrvvrpa dtlvkkvrar p
//
LOCUS       WP_284409954             397 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Acidovorax sp.
            SUPP3334].
ACCESSION   WP_284409954
VERSION     WP_284409954.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..397
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=43360
     Region          3..361
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mtarslktwt wlhkwsslvc tvfmlllclt glplifhhei ghllgtevqa pampagtphv
       61 sldrvldvar aqhpdrvvqf asqpedstdl wfttltptpa ptenfrsvav dartgailaq
      121 prfdegfmyv mfklhvdlfa glagklflgf mgllllvaiv tgvvlyapfm rklrfgevrr
      181 ersarvkwld lhnllgivtl vwafvvggtg mintwadlli kywqydelsa llapyngqpv
      241 tpvaerasvq ksldaalara pgtklsfiaf pgtsfssphh htfflrgnep ltsrllqpvl
      301 vdaktaevta apklpwylva llvsqplhfg dyggmpmkii walldiatii vlgsglylwl
      361 grrpssapaa aatgrgkpas gkaalasplt artpvrr
//
LOCUS       WP_284410312             111 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284410312
VERSION     WP_284410312.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..111
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=11876
     Region          <3..109
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mlggkvraig vasaqriatl pdvptlqeqg lagfeayawq gvsvpagtpp etiaklnkal
       61 vealdftevk arfqalgvdg mpgtpqdmar yvksererwg rlirdngirl d
//
LOCUS       WP_284410362             249 aa            linear   BCT 25-DEC-2024
DEFINITION  cupin domain-containing protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284410362
VERSION     WP_284410362.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..249
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27240
     Region          43..205
                     /region_name="AraC_binding_2"
                     /note="AraC-binding-like domain; pfam14525"
                     /db_xref="CDD:434015"
ORIGIN      
        1 mastsiamqs eptgdrqame cairtwstda vpaaqradyw vgavcdcfld mevepgqrqa
       61 fsatlasmpc gglrvnrvsg saqrvrrtlq girrsggdnf yyllckessp chvaqddaga
      121 arllpgdlal idsrrrylle fpeavdtvsi qipigwldtw lpaadcwlgr rvdgaagwgr
      181 vlsayvtqlr teqparlgtl qaehpgrfvv aglrycarga aparpaaahr alrvpalwra
      241 rphrrrrgr
//
LOCUS       WP_284410365             221 aa            linear   BCT 25-DEC-2024
DEFINITION  OmpW/AlkL family protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284410365
VERSION     WP_284410365.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006882
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..221
                     /product="OmpW/AlkL family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22618
     Region          1..221
                     /region_name="OmpW"
                     /note="Outer membrane protein OmpW [Cell
                     wall/membrane/envelope biogenesis]; COG3047"
                     /db_xref="CDD:442281"
ORIGIN      
        1 msvavgslia alpaqayaqt paspdassps pwriytgpah igfstsaevr aggqivpgas
       61 akadsndsig fgaiydfhpg wsaelalglp pttalkgtga lagagtlgkv kygpavlsvr
      121 rqlwdggpvr pyigaginyt lvlesrdgfv sslhvkngig pvlqaglevp ldarwsffvd
      181 akkiwlktta tgtlpalgga pahakvrldr lvvtagvsyr f
//
LOCUS       WP_284410471             118 aa            linear   BCT 25-DEC-2024
DEFINITION  FmdB family zinc ribbon protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284410471
VERSION     WP_284410471.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10021090
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..118
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12515
     Region          1..47
                     /region_name="CxxC_CxxC_SSSS"
                     /note="putative regulatory protein, FmdB family;
                     TIGR02605"
                     /db_xref="CDD:274226"
ORIGIN      
        1 mptydyqcat cggfdalrsl alrnepaacp rcsaesprvf asaprlacvs peqrrafdtn
       61 eraqhaprss hngdegsygr mrhpagcgcc gsgkrsatvt aangakafps krpwmish
//
LOCUS       WP_284410382             485 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Acidovorax sp. SUPP2539].
ACCESSION   WP_284410382
VERSION     WP_284410382.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 485)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 485)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 485)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..485
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=51274
     Region          174..481
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrslriqlll fwafllaaca lvaaiivvly qtgsgaqvas sraratqace diatryaksv
       61 ptvpadspqt dllrvllhvv llevpqvegg vwragsgmla yayptyegsg vkidvpaaeq
      121 plivesakqa gstgqpivnl vrgsrevlvv aacplaahpg tavwtmtrah agaiaaqdtl
      181 rtgiavlall vvgsgawlgw mllrglrqvr rlegalaqaq gdavphlert gireldrivd
      241 gfnafgtrle dararlkeal aqrhrdlrlt algrmtasva heirnpiaam rlkadnalaa
      301 pparhadala sivtqidrle glvqsllslv qplnlsprtv plgpwlqerl dtarpgsqar
      361 gvrlalrgea padavfdpvh aaraidnlld navrhapagg eavlsaqvda artlctltve
      421 ddgpgvpedl raqlfepfat gradgnglgl alarevalah ggdlhyapre gggarfilel
      481 pwras
//
LOCUS       WP_284410472             327 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284410472
VERSION     WP_284410472.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..327
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33631
     Region          30..325
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mirrllsfta lalalgataq aqtaapaaay ptkpvrlivp fppgggtdil srlvatklte
       61 vtkwtvvpdn ragaggtigi teavkaaptg ydlvmgqkdn lvvapwlykn lpwdptkdlv
      121 avahvaytpv iiatgansrf ktladvvaaa raepgkityg spgngttihl agdlfekaag
      181 iklshipykg snpalmdala gnvdllvssv psamgqiksg klrplavtsa krstslpdvp
      241 tvaesgykgf dvsswygifa pagtpasvvt tvnaevnkll aspemqaaiq aqgaeaesls
      301 aaqfsallks dyakwkgive asgakie
//
LOCUS       WP_284410520             283 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Acidovorax sp. SUPP3334].
ACCESSION   WP_284410520
VERSION     WP_284410520.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..283
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=31960
     Region          47..279
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 mntaadtapa pslaaegasp qvvdavalar lygeplfalp tdlyippdal evfleafegp
       61 ldlllylirk qnfnildipm vgvtrqylvy vdeirsrnle laaeyllmaa mlieiksrml
      121 lppkkqegsa epedpraelv rrlleyeqik laaaglsrlp qygrdflraq vhieqslqpr
      181 fpdvhvadlq eawrdilrra klvqhhritr eelsvreyms avlktlqgrr fvpfeelfep
      241 ekgstvlvvt fiallelake tlieitqaea fapiyvrlay tpv
//
LOCUS       WP_284410545             438 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284410545
VERSION     WP_284410545.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..438
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=47850
     Region          140..407
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mkpsdvfarl sgvaafmvpg lalwlrsgys wgavvlllcs latagvwlrr ppgreawwlf
       61 asivamgfvw aldfdpaqgg wsnldrpsky llalpclfyl layppravwl wwglavgacg
      121 agligiyqtg vlhllrangy tnaiqfggls lllglmcsaa llvqwgrwap wqrvgwvvci
      181 llgfegslls esrggwlvlp lalpvcawlq arcgqrrlam vgaalilagm aglmalkahd
      241 vrsrvdearq eitqyeskgd aassvgqrla hwklawsmgl drpltgwgry gyeaekqrrv
      301 aagqahpfvl rfshahnevl difakrglpg vavlllfyav plalfwptrr rvcrttehgt
      361 mdpqvlclrm vgvllpiayi gfgltqvflg hnsgtmfylf mcmlvlailq grerdalrrr
      421 aapaavppgp grpaaass
//
LOCUS       WP_284410579             338 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284410579
VERSION     WP_284410579.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..338
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34647
     Region          6..336
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mifaalhrrt fmvalslaga lgtasaqpaa kapatpgwps kplriivgfp pgsspdltar
       61 tfseplaqal ghpvivenkv gaggnigada vakatdghti glfingnlti arllnpavpy
      121 dpqkdlapls ligtsplvlt apsaqpdvpa dadaraflda arkagnrwsy gtpgvgtvgh
      181 lgtellkara giapvhvpyp gypqvatgml ggqlqmallp palalsqert gklrligvts
      241 agrstlvpgv pslaeagvtd lnleiwnafa apatmpaevq arlsaliaei arspeirakl
      301 fqqgwqvagt saqglanriq adtalmarvi rtqgirad
//
LOCUS       WP_284410645             307 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284410645
VERSION     WP_284410645.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..307
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=31747
     Region          2..303
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mpasafaqaf pnkpitiivp faaggttdil arvigqglsa elgqsvvvdn ragaggnigg
       61 qmaarapadg ytlfmgtagt hainaalykk mpfdpvkdfa pltrvanvpn llvanpnqpy
      121 ktvqeliaya kanpgkvnfg ssgsgssihl sgelckslak vdmrhvpykg sapavtdllg
      181 nqigimfdnm psaiqhvrsg klrpiavtta krspelpdvp tiaeagvpgy eatswfgmfa
      241 pagtpapiva qlnkalvkvl sqaetkkkla dqgaepvset peqfaafiqa esakwgkvvk
      301 esgasvd
//
LOCUS       WP_284410666             221 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Acidovorax sp. SUPP3334].
ACCESSION   WP_284410666
VERSION     WP_284410666.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 221)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..221
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23524
     Region          18..108
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          <135..210
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mnkklttifa lavacvtavs qaqetkgdak agqgkiamci gchsipgyqa sfpevhkvpm
       61 isgqgeryit salnaykkgd rkhptmrgia dsltdqdiad vsayyaaqvr eganlpakpt
      121 repsvqvaql lqkgacvsch gdnfskpidp sypkisgqha dylfvalkay kadpnnthlg
      181 rsnaimagia kqftnaelka lagyigsldg elqvvpqsrf r
//
LOCUS       WP_284410667             284 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Acidovorax sp. SUPP3334].
ACCESSION   WP_284410667
VERSION     WP_284410667.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..284
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32396
     Region          2..266
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mkfqgsqsyv atqdlmlavn aaitlqrpll vkgepgtgkt mlaeevsrel gmpllqwhik
       61 sttkaqqgly eydavsrlrd sqlgdadsse rvkdirnyiv qgvlwqafta dqpvallide
      121 idkadiefpn dllreidrme fycyetreli rakhrplvfi tsnnekelpd aflrrcffhy
      181 ikfpeaetmr kivhvhfptl ksellavamk tfydvrglpg lkkkpstsel idwlkllvae
      241 diplealqsa dqkvsvpplv gallkneqdv glfeklvfmn qrnr
//
LOCUS       WP_284410750             327 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284410750
VERSION     WP_284410750.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..327
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34412
     Region          6..320
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mnkrwtrrtl caglaatafa lpsaaqpaap ypskpieliv aygpgggtdl varllarhle
       61 kqlegsvvvl nrpgagggig fgelarakpd gytigfintp nvltipierk ssfhwsqydl
      121 lgnlvddpgg faihntnnit tlaglaaysk ahpgavtvgt tgtgsddhla mllferatgt
      181 klthvpykga gevraaatgq qivigainvg evlayqkggt pirllgqmsa ersslapqvp
      241 tfkeqgiaie laslrglaap kglpeairkk lvdaiatiaa dpafkqqaea myaplryltp
      301 aayaaeleat eanfrklwae mpwqdrp
//
LOCUS       WP_284410670             395 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284410670
VERSION     WP_284410670.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..395
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=45760
     Region          1..395
                     /region_name="CoxE2"
                     /note="Uncharacterized CoxE-like protein, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3825"
                     /db_xref="CDD:443037"
ORIGIN      
        1 mlidffytlr agqlpvsvke yltllealqa gvvgpnsdda wslddfyhla rtvlvkdekh
       61 fdkfdrafga yfkgvemvad frkdipadwl rkilereltp eqkaaiekmg wdelmetlkk
      121 rleeqkerhe ggnkwigtgg tspfghggyn pqgvriggag knksavkvwd qraykdyddt
      181 qelgtrnikv alrrlrkfar eghemeldla dtirstaana gyldikmipe rhnnvkvlll
      241 mdvggtmdeh vqrveelfsa vktefkhlec yyfhncvydf mwknnrrrfa ekfptwdiir
      301 kynkdyklif vgdatmspye ilqpggsvey nneeagaewl qrlihafprf awinpepqgv
      361 wqyrqsigii qqivgqrmyp lslkgleetm rllsk
//
LOCUS       WP_284410777             325 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284410777
VERSION     WP_284410777.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..325
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33933
     Region          27..323
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mkllraktcl agallcvaav aaqaqtpsap lkivvpspag gpadasahiv adgakaalgn
       61 vtvenkpgag gnvgadlvak apaggnllvm gavathavnp wlyksfpydp ikdfkpialv
      121 artpnvlvms aeqakalgin sttelvqylk khpdqlkygs ggngsighia gemfksltnt
      181 rmahmpfqgs apalkalqaq evslvfdnla sslplikagk lkalgvtslg rdddlpdvrs
      241 indevqgfnv vtwfglfapd alpdadarry amaftagmks paslerfkkm glepedvtle
      301 sfgqfvrseh skygflikaa kikmd
//
LOCUS       WP_284410797             606 aa            linear   BCT 25-DEC-2024
DEFINITION  RecQ family ATP-dependent DNA helicase [Acidovorax sp. SUPP2539].
ACCESSION   WP_284410797
VERSION     WP_284410797.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Larsen,N.B. and Hickson,I.D.
  TITLE     RecQ Helicases: Conserved Guardians of Genomic Integrity
  JOURNAL   Adv Exp Med Biol 767, 161-184 (2013)
   PUBMED   23161011
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Rezazadeh,S.
  TITLE     RecQ helicases; at the crossroad of genome replication, repair, and
            recombination
  JOURNAL   Mol Biol Rep 39 (4), 4527-4543 (2012)
   PUBMED   21947842
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Bernstein,K.A., Gangloff,S. and Rothstein,R.
  TITLE     The RecQ DNA helicases in DNA repair
  JOURNAL   Annu Rev Genet 44, 393-417 (2010)
   PUBMED   21047263
REFERENCE   5  (residues 1 to 606)
  AUTHORS   Chu,W.K. and Hickson,I.D.
  TITLE     RecQ helicases: multifunctional genome caretakers
  JOURNAL   Nat Rev Cancer 9 (9), 644-654 (2009)
   PUBMED   19657341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..606
                     /product="RecQ family ATP-dependent DNA helicase"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0043138 - 3'-5' DNA helicase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=65568
     Region          28..503
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
ORIGIN      
        1 mpvippqpip aspkrarqpr aprkpsaari qsvlkktfgl relragqrev idrvlqsent
       61 lavmptgagk slcyqlpalm iegrtvvvsp lialmrdqcd slrergvpav qlhsgltpqe
      121 treaeqaiad gsarivlttp erladaefla lvassgpigl lavdeahcis qwghdfrpaf
      181 leiagavarl grptvlalta taagpvaadi rkqlgipaag vvdtgtyrpn lryraealan
      241 eadkrarlid ivkaaegsgl vyaatvkaaq evhaalraad vaaglyhgrm paaerseaqd
      301 afmrgevrvm vatnafglgi dkqdvrfvvh yqmpgglday yqesgragrd gdpadctllf
      361 lrkdkavqqf flagrypsad didalyqalr dpapqdpgvw tldslqarld rprsklqvgl
      421 gllqrhkivs karsgalslr ktelepasvr allqayadkr eqdqqalerm vfyaqtgrcr
      481 wqvlleyfdp sdepqrcgtc dncirmahla qqalaeraad tvrnlgatdl gemgepvias
      541 aaqarrdaqa lelgatvrvk rygqgtvaai daisvtvdfa dgtqrcfqpd fvqrfvprga
      601 rakpls
//
LOCUS       WP_284410850             285 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Acidovorax sp. SUPP3334].
ACCESSION   WP_284410850
VERSION     WP_284410850.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..285
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32551
     Region          <41..161
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mttlfdriqq rfwgppqwda erisdewfra hfhyaadvvq hwlgsaldvk tarllnfgcg
       61 dgitdlalal rhgataihgi dirqeysklp riareqlglr rvpkalsfet iapatplagr
      121 rpvdgifsws tfehvskdql epiardlyaa lnpggvfflq ieplyfspfg shlrryddvp
      181 whhllvsdee lwaiiqaheg pidgaerdfg fddfgvegyk rfvfneyktl nrltadelva
      241 lmtqvgfhvi rqerrslema vppalqdkyp qelllnneif lllgk
//
LOCUS       WP_284410946             215 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Acidovorax sp. SUPP2539].
ACCESSION   WP_284410946
VERSION     WP_284410946.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 215)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..215
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22645
     Region          39..123
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          143..215
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mkkllapmlm aavlavaafp alsqghapaa aaqkpakpdl akgeatftav cvachaadgn
       61 saiainpkla qqhpeylvkq lqefksgkrn npvmkgfasa lsdddmrnia wwvaskqakp
      121 gfakdkelva lgeriyrggi adrniaacag chspngagip vqyprlsgqh adytaaqlva
      181 frdgvrsnsl qmtqvaakln dreikavady iaglr
//
LOCUS       WP_284411042             342 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Acidovorax sp. SUPP2539].
ACCESSION   WP_284411042
VERSION     WP_284411042.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..342
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37009
     Region          15..311
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mdtpsqpsgt atlmeqilye vkrvvvgqdr flervmvaml sqghllvegv pglaktltvk
       61 tlastvqgqf kriqftpdlv padlvgtrmy nqrtgefstt rgpvftnlll adeinrapak
      121 vqsallevmq erqvtiaget hrvpepflvm atqnpieteg tyalpeaqvd rfmmkvlvgy
      181 pseeeefvia qralapavqv aavattgqla alqaecrtvy vdpsllqyav rlvaatrapa
      241 qyglpglapr iacgasprat ihlaegaral amlrgrayvl pedmadlapd vlrhritlsy
      301 ealsdgldad aligqlmahl papprplhhd aqdgarhepq ra
//
LOCUS       WP_284411053             597 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Acidovorax sp. SUPP3334].
ACCESSION   WP_284411053
VERSION     WP_284411053.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 597)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 597)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..597
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62419
     Region          68..>590
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mqrhiplpla lgaalpwlgl saiaqvstpp dtagtrspsl pavtvtapat paaqrspgla
       61 tgtagstldt pfsvttvpge rvrqqggttl qdalrnvpga qadsgfngsh tqffilrgav
      121 tdsgtgsnrv lrdgvrqsny pytpafvesv evlrgpgaal gvrsepggtv nivtrkpqls
      181 nfgsvllgag glgagglgag ghgaletsvd lnrvlsadhe laarvtatrs dasewrhvkd
      241 rlggiqvgla qsdgnryhlr asleathqty qpdyglpaln grpvpvprdr qlgepfgdst
      301 tnnriyslhg dvalsadtrw aadfthlqaq stsiknllng splpgqpagt yarvsawepg
      361 terkidslst alsstrsagt lthqiylgae yyketlnqps lsvpastspp invfdpvygr
      421 vsapppgavl aqslttqnle sfaasaqdqi dvgawsvvag lrfarqrfvy gtagvlpvqe
      481 srwspklavl rrlsdadtvy anvstgtspn qvasssnqsl psrrsaqiea gwkslwqggl
      541 lvsdvavyrl dqknmiaadl stplnnfdft tagsarsqgi easltgqvtd scratct
//
LOCUS       WP_284411125             183 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284411125
VERSION     WP_284411125.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..183
                     /product="YceD family protein"
                     /calculated_mol_wt=20277
     Region          1..181
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mtkefspqrl dvkafaqagg hlsghdsllk yerlaqeakg lhpdlivdwq adgelrsthg
       61 iggqiwlrlv araafpmtcq rclgpvdvpl everefrfva deataealdd esdedllals
      121 refnlrelie dellmalplv prhdecpapv pmestdedfe easaqkpnpf aalaalrkdk
      181 sed
//
LOCUS       WP_284411205             142 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284411205
VERSION     WP_284411205.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..142
                     /product="YybH family protein"
                     /calculated_mol_wt=15936
     Region          1..131
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mnapggtneh iiraarafsn raianqdida isslwmedvl vltstsvqll gaeanrryyq
       61 aqftrrpdtl wvrtpssvga psswriahee gdwtgqwses dgrvqlrgry maqwvctegd
      121 wriqgeiyvp tsrvfdqgvv hv
//
LOCUS       WP_284411185             268 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Acidovorax sp.
            SUPP2539].
ACCESSION   WP_284411185
VERSION     WP_284411185.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..268
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28632
     Region          41..253
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mptpnqlhlw ddrffyitpa iqsgltarss atllacgdgr pftlvthgge vlrctaalva
       61 phvprrldad gcgllslnid pasavfrgls drlggagilp ldarcfgprl reafegavhg
      121 qlpaealral svdmvhtvcg qrpgpapmdp rvvrvlsrlq araaegavpl qelaacaqls
      181 pdrlthlfre qtglsikryl lwakirravh mlatarpltd aalaggfads ahmshafqrc
      241 fglppsflar agqvsvvvda haqrvwhg
//
LOCUS       WP_284411340             252 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfite exporter TauE/SafE family protein [Acidovorax sp.
            SUPP3334].
ACCESSION   WP_284411340
VERSION     WP_284411340.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..252
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26748
     Region          1..251
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mewiivslas llagfvdaiv gggglilvpa lfatfpnapp atllgtnksa siwgtgiatw
       61 qysrrvqmrw qamlpaaaag fvgafagawt vtvvsadslr kllplillav llytlarkdl
      121 grhhtprfeg kietqlacvi gltvgfydgf fgpgtgsffv flfvrllgyd flnasvsakl
      181 lnlatnvaai ilfaakghvw whfavplava nvvgsvigth malkhgtgfv rgifivvvss
      241 lilktgydaf lr
//
LOCUS       WP_284411562             648 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Acidovorax sp. SUPP3334].
ACCESSION   WP_284411562
VERSION     WP_284411562.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..648
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=70632
     Region          2..610
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mtttfpqlll qhaaerptaa alrdkeygiw qthtwaglaa mvealcaglh qaglqagehl
       61 vvvganrprl yatmlaaqsl gaipvplyqd avaaeciypl nnaevrfcvv edqeqvdkll
      121 eirtqcpals hlyfddprgl rnygepglas ldalaeagaa fvaqnagwfr aqvakvqpgd
      181 vaamfftsgt tgnpkgvvht hatlldraqa gaefdhlths eevlaylppa wigqnifsys
      241 qwlacgyvvn cpesastvsi dlkevgptyy fapprifegl ltsvmirmed agtlkrkmfh
      301 acmavarrvg parmdgqpvg lldrikyalg dllvygplrn nlgfsrvrva ytageaigpd
      361 lftfyrsigi nlkqlygste tavfvclqpd hqaradtvgv pirgvqiqva dngeilvksa
      421 gllkeyyknp aataevltad gwyrtsdagf ldahghlkii drvkdvgriq ggandgamfa
      481 pkyvenklkf fpyikeaval gdrrekvcam vnidfdavgn waerrnlpya gytdlaqkpe
      541 vyelirdcve kvnadlasda llagsqvsrf lvlhkeldad dgeltrtnkv rrgfiadkyg
      601 tlvealyagr teqfietqvk fedgrtgsvs atlkladakt faptkqaa
//
LOCUS       WP_284411468             185 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Acidovorax sp. SUPP2539].
ACCESSION   WP_284411468
VERSION     WP_284411468.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..185
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=19707
     Region          1..115
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mpapqglepp sewiqrwahl vppgasvldv acgsgrhlrw lhgrghpvtg vdrdpdaltp
       61 lrglgeilca dieagpwpla grtfgavvvt rylwrpllpt lvasvapggv llyetfaagn
      121 etvgrparpd fllrpgellq acaglctvay edgfldaper fvqriaavrl qegaaparhr
      181 lappl
//
LOCUS       WP_284411576             778 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Acidovorax sp. SUPP3334].
ACCESSION   WP_284411576
VERSION     WP_284411576.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 778)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 778)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 778)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..778
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=85042
     Region          102..776
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mnlralrrsl ilrlvgisll lllivqaagv vvvqtfivrn araqiersld vdervwrwll
       61 dqnavrlkea stllasdygf rsavnsgdad tiqsvlenhg arigaamtal ldarmhlqat
      121 spsrspadyq saidqavpal vaqplgsqia vvqgmpyqfv mvpmraplvv gwvlmgfpvn
      181 etlvsemqql lsvdvaiqir dpagavsvpv sslpdramsd lrdfrmgger dvggetllvr
      241 avrldsgats aralllrsld dvvspyrqlq vllgvitvvg lvlfaigsaf marrltmplh
      301 slvdathrls qgdyaapieh ttrhdeignl arsfdrmrld isgqqnqirr ladidrltgv
      361 pnrerfrral meamgpeggg rpvavialdl drfkhvngvl gyalgdrllq avaerigmqa
      421 rssqdivarl ggnqfammll gadaasarem aqriirafet pmafgdrtvd lsagmgiacw
      481 pgpaqdadtl lshaeiamya akqrlsgall yepsmdlssa vslslltelr ravdrnelrl
      541 flqpkvtltg qpgnaaealv rwqhpergmv ppmqfipfae qtgfvrqltl wmfeqavvfl
      601 aqpqvqalsl qisinlstrd lldpelsnrf gallerhgvg asafcleite saimdeplra
      661 eamlnrlseq gfklsiddfg tgysslaylk rlpvdelkid ksfvigmaad dgdeqivrst
      721 idlahnlgls vvaegvetva ilerlralhc ddaqgyyisr plpmddflaw hasaaerk
//
LOCUS       WP_284411663             322 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ferritin-like domain-containing protein [unclassified
            Acidovorax].
ACCESSION   WP_284411663
VERSION     WP_284411663.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10560096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..322
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34003
     Region          187..286
                     /region_name="DUF2383"
                     /note="Domain of unknown function (DUF2383); pfam09537"
                     /db_xref="CDD:430673"
ORIGIN      
        1 msdfndanrd pltnepgahp vgtgvgaagg amagaaagaf ggpigaavgg vagavvggla
       61 gkaaaesvnp tvedaywres ydrepyyvkg raydeyrpay elgwssvgry dgdfdavepn
      121 lardwgtars tsrleweear paaraawera grgttlgsds aygntydntt alvdnddvvd
      181 vlddllescr dgeygfkasa ehadspelkg iflrhaseca aaatelerei rnhggepssg
      241 gsmsgalhrg wvsvkaamst rddkavleec ergedaavar yrkalkaslp anvramverq
      301 aegaqrnhde vralrnrfqa aa
//
LOCUS       WP_284411664             338 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Acidovorax sp. SUPP3334].
ACCESSION   WP_284411664
VERSION     WP_284411664.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..338
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34093
     Region          37..331
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msagapggrr aawlgaglla vsavllmaga cvgstgfesl lrmgqdpvaw qivweirlpr
       61 tlgawlagal lglagavaqg lfrnpladpy llgsasgaal ggavamalfg vspmaaqwla
      121 rlgvtgmafl gaagavaltl llargvqhtl rlllagvivg vvlgalrdlv elaspdilqa
      181 mqaftlgsts fvgwvscalm agawglcsva awtlsraldg ltlgeataas lglplgpmrm
      241 glvaamalat gtavaqtgli afvglaaphl vrsivkathq rhivlsslmg aslllaadil
      301 arwllapqel pvgvltaalg gtyllwlmhr rsalghsl
//
LOCUS       WP_284411704             710 aa            linear   BCT 25-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Acidovorax sp.
            SUPP3334].
ACCESSION   WP_284411704
VERSION     WP_284411704.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Shan,L., Mathews,I.I. and Khosla,C.
  TITLE     Structural and mechanistic analysis of two prolyl endopeptidases:
            role of interdomain dynamics in catalysis and specificity
  JOURNAL   Proc Natl Acad Sci U S A 102 (10), 3599-3604 (2005)
   PUBMED   15738423
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Polgar,L.
  TITLE     The prolyl oligopeptidase family
  JOURNAL   Cell Mol Life Sci 59 (2), 349-362 (2002)
   PUBMED   11915948
REFERENCE   3  (residues 1 to 710)
  AUTHORS   Polgar,L.
  TITLE     A potential processing enzyme in prokaryotes: oligopeptidase B, a
            new type of serine peptidase
  JOURNAL   Proteins 28 (3), 375-379 (1997)
   PUBMED   9223183
REFERENCE   4  (residues 1 to 710)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 710)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..710
                     /product="prolyl oligopeptidase family serine peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=78585
     Region          11..701
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mpeptqpael pvddpvqded pylwleavds dralawvrer nahseavlta rpeyaptreq
       61 llgildaqdr ipsvvrraqw lynlwqdghh rrglwrrttl aeyrqrepaw etvldldala
      121 eaegenwvwg gaevlgpayr halvslsrgg adatvirefd lttrqfvegg fhlpeaksdl
      181 gwidadtvyv stdfgegsmt esgyprivkr wrrgtplada vtvfegevsd vgvgvgvdtt
      241 pgfertvftr midfyrhevw laegpvaapp apvrldvpdd aipdflrgtl llqlrsdlvl
      301 geqrfvagsl lhadaaawlr gervaaalft ptdarslagy dttrdhvllq vmdnvaerle
      361 lwhrtgadtg pftgrtvdtp fpgqlgvtsl ydplladdpl aehyllsytd fitpgslfla
      421 staqderewl kagaarfdaq gmrteqcfat sadgtrvpyf vlwprgaqad grnptlvygy
      481 ggfeqaltpw yaadygrawc ekggvfvvan lrgggefgpa whqaavrehk qrsyddliav
      541 aqdliargvt qprhlgiqgg snggllvgav mvqrpdlfna vvcqvplldm rryhmllaga
      601 swmaeygdpd dpadwaflaq yspyhrvrpd aryprvlftt strddrvhpg harkmaarml
      661 aqghdllyye ntegghggaa dnaqrahlla lefaylwqql gvspgtspsa
//
LOCUS       WP_284411775             328 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284411775
VERSION     WP_284411775.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..328
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33072
     Region          32..326
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mpipsisrrg alaalaaslc gaagtaaaqa gypgraitlv vpqqaggand aiarvvaqkl
       61 seqlgqpvvv dnrpgaggnv gtaaaakakp dgytllltad saqvinpwly qhtgfdpvkd
      121 fepvaplata gyvlvahpaf pasnvaelva lakarpghya iasagngtln hligemlqkt
      181 agislqhvpy kgsaaaatdv vggqvplsvq slpssiafik agklkvlgvv ntqrvaalpd
      241 aptlgetlsg fgqtpwyglf apagtppavv arlqaevaka leqkdvadrl aavgcepfkg
      301 gsaqlaalvr ddlarwgrvv kdtgakld
//
LOCUS       WP_284411827             404 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Acidovorax sp.
            SUPP3334].
ACCESSION   WP_284411827
VERSION     WP_284411827.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..404
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43113
     Region          <38..374
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 msnlpawpaa pvraapaapt ahpaptphas aeagmawife dprskallae veqvapsdag
       61 vlitgesgtg keliarylhg rsprsaapfv avgcgafsea lvdselfghe hgafpgafga
      121 qpgwfeeahg gtifldevnd lplavqnkll rvlqqrevvr vggrqpipid vrivaaasvd
      181 lqelvrqqrf rkdlyyrlnv vslevhtlre rrgdivplar hfidaysrrl gyprpqltpa
      241 aeralqqapw pgnvrelent ihrtlllgeg rtldvqdlrl sgtaragaep dapaaaagaa
      301 apppqaasps ppglpllrqa vrqlceahvp alyqtvedav llevfrwchy sqseaarvlg
      361 lsrnvvrarl irlgevgapr ragadagapa aefssatdse spap
//
LOCUS       WP_284411842             318 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)H-dependent flavin oxidoreductase [unclassified
            Acidovorax].
ACCESSION   WP_284411842
VERSION     WP_284411842.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..318
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=33363
     Region          10..312
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 msqlppalqk lslpvigspl fiisnpqlvi aqckagivgs mpalnarpae qlddwlaeit
       61 ealaahdkah pdrpsapfai nqivhksndr lehdmqvcak ykvpivitsl garedvnqav
      121 hgwggivlhd iinnkfahka iekgadglia vaagagghag vkspfaliqe irqwfdgpva
      181 lsgaiasgga vlaaqamgad fayigsafia thearaqeay kqaivdgnsd divysnlftg
      241 vhgnylapsv raagldpdhl pesdpskmnf ggdakkawkd iwgcgqgiga itevtgaadl
      301 varlrreyqa argrlavi
//
LOCUS       WP_284411844             380 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284411844
VERSION     WP_284411844.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..380
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40500
     Region          1..363
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mssasrssli dtvkglacat ivahhlvfyg pmsdvalplm pqvmawlsqh grmavqvflv
       61 lggylaaasl aptgaarfds aseqigrrfv rlavpyaval vlavlasaav rpfldhpsvp
      121 gepspaqlva nalmiqdivg eealsagvwy vgidfqlfal aallfsavrr wpgvsrpqae
      181 rlgkalvlag talsllwlnr epgldmwacy ffgsyglgml acwtvrapra ragllaital
      241 ggvalavefr eriavawvaa lvlvlwlrwg qpwlsacwpa gapsavphpl erlgrmsysv
      301 flvhfpvcll vnaafqqgwp dsaamnllgm atafglslaa grllywrver qvpswtvalr
      361 wqaglvgtgv vvafaagrfg
//
LOCUS       WP_284411879             185 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA recognition motif domain-containing protein [Acidovorax sp.
            SUPP3334].
ACCESSION   WP_284411879
VERSION     WP_284411879.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Muto,Y. and Yokoyama,S.
  TITLE     Structural insight into RNA recognition motifs: versatile molecular
            Lego building blocks for biological systems
  JOURNAL   Wiley Interdiscip Rev RNA 3 (2), 229-246 (2012)
   PUBMED   22278943
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Clery,A., Blatter,M. and Allain,F.H.
  TITLE     RNA recognition motifs: boring? Not quite
  JOURNAL   Curr Opin Struct Biol 18 (3), 290-298 (2008)
   PUBMED   18515081
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Maris,C., Dominguez,C. and Allain,F.H.
  TITLE     The RNA recognition motif, a plastic RNA-binding platform to
            regulate post-transcriptional gene expression
  JOURNAL   FEBS J 272 (9), 2118-2131 (2005)
   PUBMED   15853797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..185
                     /product="RNA recognition motif domain-containing protein"
                     /GO_function="GO:0003729 - mRNA binding [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=17035
     Region          2..86
                     /region_name="RRM"
                     /note="RNA recognition motif (RRM) domain [Translation,
                     ribosomal structure and biogenesis]; COG0724"
                     /db_xref="CDD:440488"
ORIGIN      
        1 mgnklyvgnl pysvrdsdle qafgqfgavt sakvmmerdt grskgfgfve mgsdpeaqaa
       61 iqgmngqplg grsivvnear pmeprpprsg gfgggggggg yggggggrsg gggygggggr
      121 gdgggggygg gggreggggy ggggggrgdg gfrspygsgs rngggggrsg gggggygggg
      181 gssgy
//
LOCUS       WP_284411881             130 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA recognition motif domain-containing protein [Acidovorax sp.
            SUPP3334].
ACCESSION   WP_284411881
VERSION     WP_284411881.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Muto,Y. and Yokoyama,S.
  TITLE     Structural insight into RNA recognition motifs: versatile molecular
            Lego building blocks for biological systems
  JOURNAL   Wiley Interdiscip Rev RNA 3 (2), 229-246 (2012)
   PUBMED   22278943
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Clery,A., Blatter,M. and Allain,F.H.
  TITLE     RNA recognition motifs: boring? Not quite
  JOURNAL   Curr Opin Struct Biol 18 (3), 290-298 (2008)
   PUBMED   18515081
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Maris,C., Dominguez,C. and Allain,F.H.
  TITLE     The RNA recognition motif, a plastic RNA-binding platform to
            regulate post-transcriptional gene expression
  JOURNAL   FEBS J 272 (9), 2118-2131 (2005)
   PUBMED   15853797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..130
                     /product="RNA recognition motif domain-containing protein"
                     /GO_function="GO:0003729 - mRNA binding [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=12823
     Region          2..86
                     /region_name="RRM"
                     /note="RNA recognition motif (RRM) domain [Translation,
                     ribosomal structure and biogenesis]; COG0724"
                     /db_xref="CDD:440488"
ORIGIN      
        1 mgnklyvgnl pysfrdddlq qtfsqygavq sakvmmerdt grskgfgfve mgsdaeaqaa
       61 iqgahgqnfg grdlvvnear pmeprpprsg gggfgggngg gggygggggg grsfgggggg
      121 ggygggrssy
//
LOCUS       WP_284411891             501 aa            linear   BCT 25-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284411891
VERSION     WP_284411891.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..501
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=52328
     Region          14..497
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mllfdprsia vpaghfiggr fvpdagriav lrpsdgqwha dlpladaatv daavqdawqa
       61 wcttdwarra prerarvlrr wadmieadgp qlapleavcs trpardaaaw dvpftaeglr
      121 ffaeyadklg gevaatrhdh lgmvvaepyg vvgaitpwnf plvmmswkvg aalaagnavv
      181 lkpsemtpfs avrlaqlave agvppglfnv vqgdgrttgd altrhpriak mtftgstrtg
      241 aaimatcalq gpkpvtlelg gkspqlvfdd apdidrlagl iagaitgnag qvcvagsrli
      301 vqrgiapelv erigarfaal rpgatwdgta tlppiisapq aarildiver ardagaqlrc
      361 ggglfddvag gvaagaagga yfqptllegv aadspavqee ifgpvltvqt fdteeeglal
      421 aahahyglaa gvhtadigra lramrgisag tvwinrygrs adfviptggy hqsgigkdlg
      481 rqaveanlrf ksvlidfaaa h
//
LOCUS       WP_284412044             386 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Acidovorax sp.
            SUPP3334].
ACCESSION   WP_284412044
VERSION     WP_284412044.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..386
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=41042
     Region          34..263
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mnfspttpaa mlaawfmrht spngvrrvaq lngavatdvg svrednqdrv alvrgrdrsg
       61 gcfivaalad giggmkqgae caaltlgtfi dsvvadaqls tepgdwlasg ahranravha
      121 klageggstl vaallmngrp phwlsigdsr ayqayngklh qlslddtidg qlgksgggrr
      181 rdllqfvgig dvlephiepi vsasgsmllt sdgvhfiead ylakvvyyap dlgfcvrrlt
      241 elakmlggpd natvaalsld alavnaethl hgvyevwdpf gelqimfdcg prqyvatspq
      301 qasaadtpkh vyaaplppvv spgnetkpan srqeeptdeg satknmahqk kprssrkkpk
      361 qspadpgehr dadepqlfie fpnkkp
//
LOCUS       WP_284412140             341 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284412140
VERSION     WP_284412140.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..341
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=35223
     Region          48..339
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mnpffhpqpr pephphasrr halaatvaav lglavagpaa aqapaypskp itfvvpfaag
       61 satdqlarai gqsvttdtkq avvvdnkaga sgmiaaqava kaapdgytvl ittntthaan
      121 ehlykklsyd pvkdfvpvtg lgkggqvlvv naaapyknvg eliaaakksp gklsfgsgss
      181 ssrvagemlk qlagvdilhv pyksnplait dllggqidlm itdtstgvpq ikagklralg
      241 ystkkrgaql pdvptieeag vkgydmgywf aayvpagtpa pvvvrlnell gqatksaaaq
      301 sfydmagsea wtttsdelak fqaaetqkwg qvikaagiqp e
//
LOCUS       WP_284412211             661 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Acidovorax sp. SUPP2539].
ACCESSION   WP_284412211
VERSION     WP_284412211.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 661)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..661
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..661
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=69708
     Region          16..507
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mhkeisgsan clapgvqvge yrlsdvigeg gfgivyrard lsldrivaik eympstlagr
       61 kesnqihvrs qhrgafdagl rsfinearll akfshpalvh vyrffeangt aymvmqyyeg
      121 qtfrtflnqq pkamdeqwls tiiapildvl emlhaadcyh rdiapdnifl qssgmpvlld
      181 fgaarriigd mtqaltmvlk pgfapieqyv ddgampqgaw tdiyqlgall ylsitgrppa
      241 tsvarmindp vstlvpencp gfsarflsgv hhalaikpqd rpqsigdlrh llglktvtls
      301 wpssglmgls vaeesdpsmd apvhvpsafa apaafaapaa ftapqlpaea vapvaphpda
      361 rhgavpseah apvvsgldta hqhrpstevr pskaasapvh appspsaess akahsrktkp
      421 aasqqgaght pltkrpvwli palgfaalvv vaggawwits gddaaktaav aqdaqesdqw
      481 mlaarintpd slrtylslfp ngahraeaeq riaaltsava pasapvaqqa pasapvvaas
      541 apmvvadvap akvppasvpt paasapaaps alptpeeaar vpaqatrtad aenkgkiilr
      601 vmpwgnvsvd rvpagttppl tqltlseglh ridisnpvap tvtqmvlvkk gesvvlthkf
      661 e
//
LOCUS       WP_284412362             113 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Acidovorax sp. SUPP2539].
ACCESSION   WP_284412362
VERSION     WP_284412362.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..113
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11483
     Region          6..110
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mtvhpsylil glaialevvg ttalkasdgf trlvpslitg vayaasfyal slalktipvg
       61 vayaiwsgvg ivlisvvgcv vfrqrldapa mvglgliiag vlvvnlfsks tgh
//
LOCUS       WP_284412423             302 aa            linear   BCT 25-DEC-2024
DEFINITION  amidohydrolase family protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284412423
VERSION     WP_284412423.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..302
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32144
     Region          26..297
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mhresfatpv rfsagsaapr tvlpkdacdc hvhvydgrfp aapgarllpp dasaqdyral
       61 qhrigtartv lvtpstygtd nrcmleglaa lgpqargvav idghesdaql qrlhdagvrg
      121 arlnlslgvs gtvqsltpla criaplgwhl qllmapdlla aqgevlrrlp vplvfdhfgr
      181 ispaqagqhp ahallqdllq rgqawiklsg gyivserqst edpaldalaa sylrcaperv
      241 vwgsdwphat assgahpmpd darqvdrlvd wagqsgdaat lhrvlvdnpa alygftppss
      301 fa
//
LOCUS       WP_284412446             198 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: OmpW/AlkL family protein [unclassified Acidovorax].
ACCESSION   WP_284412446
VERSION     WP_284412446.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006882
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..198
                     /product="OmpW/AlkL family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21124
     Region          16..198
                     /region_name="OmpW"
                     /note="Outer membrane protein OmpW [Cell
                     wall/membrane/envelope biogenesis]; COG3047"
                     /db_xref="CDD:442281"
ORIGIN      
        1 mkknllalav lcaltsgaaf aqtaegpwlv raravnldss nkdstglgls indktlpevd
       61 isyffnrnia aelvltvpqk qrlsssalna qigtlkhlpp slmlqyhfdt agfrpyvgag
      121 vnytrfssvr lpagvsidks swggalqvgv dipltknlvl nfdvkkvyiq tdvfaagakl
      181 gtfkidpvla gvglgwrf
//
LOCUS       WP_284412505             112 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Acidovorax sp.
            SUPP2539].
ACCESSION   WP_284412505
VERSION     WP_284412505.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..112
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12860
     Region          28..89
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mrlqpaslpl pgsnaysdlp qfpkhnvlpf rrtirrhelr qivplaetti yemerrgefp
       61 rrfnltprcv vwdlaeveaw iderkqapra gatkpdvylr ktrpvragsa qg
//
LOCUS       WP_284412571              90 aa            linear   BCT 25-DEC-2024
DEFINITION  transcriptional regulator [Acidovorax sp. SUPP2539].
ACCESSION   WP_284412571
VERSION     WP_284412571.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008341
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..90
                     /product="transcriptional regulator"
                     /calculated_mol_wt=9609
     Region          10..73
                     /region_name="YdaS"
                     /note="DNA-binding transcriptional regulator YdaS,
                     prophage-encoded, Cro superfamily [Transcription];
                     COG4197"
                     /db_xref="CDD:443351"
ORIGIN      
        1 mtyqqavfla cetlgsqaal akaievapal vhqwrsgsrp vpvqhclsie ratgaavsrr
       61 dlrpddwhli wpelapgaeq spskaeathg
//
LOCUS       WP_284412574             106 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Acidovorax sp. SUPP3334].
ACCESSION   WP_284412574
VERSION     WP_284412574.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..106
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11664
     Region          14..102
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdpqatpidp erlrqaatqa vaalkalane drllllcqls qgeqcvselq arlgiqqptl
       61 sqqlgvlrtq gvvetrregk nihyrvadas lleilavlyr lycpke
//
LOCUS       WP_284412768             653 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Acidovorax sp. SUPP3334].
ACCESSION   WP_284412768
VERSION     WP_284412768.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 653)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..653
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=69682
     Region          16..519
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mhkeisgsan clapgvqvge yrlsdvigeg gfgivyrard lsldrivaik eympstlagr
       61 kesnqihvrs qhrgafdagl rsfinearll akfshpalvh vyrffeangt aymvmqyyeg
      121 qtfraflnqq pkamdeqwls aiiapildvl emlhaadcyh rdiapdnifl qssgmpvlld
      181 fgaarriigd mtqaltmvlk pgfapieqyv ddgampqgaw tdiyqlgall ylsitgrppa
      241 tsvarmindp vstlvpencp gfsarflsgv hhalaikpqd rpqsigelrh llglktvtls
      301 wpssgmmglg aaessfspsl dfdapavvsi paaapapspa eavptplipq leagritaqp
      361 qalqpipipp ahqqeripse arasrdvqsv ipppltpsvp rpdirarkvk taqvkgeava
      421 qrspskravw llpalgfaaf vliagggaww ftignegakq evvlpnsqel dqwglasrin
      481 tpdslrtyls lfpsgthrae aeerlaglms palpasvpla pqapasaplv vasaapaavt
      541 dvaaaklpvp papaastpal pavmpppedp artlaqaara adaenkgkii lrvmpwgnvs
      601 vdrvpagttp pltqltlteg lhridisnpv aptvtkmvlv kkgesfvlth kfe
//
LOCUS       WP_284412859             132 aa            linear   BCT 25-DEC-2024
DEFINITION  MerR family transcriptional regulator [Acidovorax sp. SUPP3334].
ACCESSION   WP_284412859
VERSION     WP_284412859.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..132
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15118
     Region          6..126
                     /region_name="HTH_GnyR"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     regulatory protein GnyR; cd04776"
                     /db_xref="CDD:133403"
     Site            order(7..9,23,42..44)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133403"
     Site            order(55,58,62..63,72,93,97,103,107,110..111)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133403"
ORIGIN      
        1 malttytisd lakefdlttr amrfyedmgl lqpertgpgg rtrlysardr trlrltlrak
       61 rlglslteak aiidlydspr dtgvqlrkfl dvlgehrkql eeqmadlqan leevreheke
      121 arallakaek kk
//
LOCUS       WP_284412870             381 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284412870
VERSION     WP_284412870.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..381
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=42213
     Region          23..371
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 maalgasrga aviaptaqga nrfnllrlaa avavllshge flyrltmavp faghsvgsla
       61 vycfffisgy lvcqswerep hlglfwakrv arifpgliva tafsvfvlgw amtqlstqqy
      121 wsdartwinf fnnalglafm qvlpgvfenn pfarsvngsl wtiryellmy vllslagvag
      181 wtrrrwvypv aallmavswq warvagwndy vdagprwfka ffhwfqwsdv sgfgvvfllg
      241 ctfaayrvrs gawllpvagm ggvlalatpf awsvqlgvwm lvaagifwaa hagagrskgw
      301 predlsygvy iyafpiqqav teiglqrgws laaclavslv stlvmaafsw fciekpgvry
      361 grrvveqwsr rrslrvqsap v
//
LOCUS       WP_284412890             225 aa            linear   BCT 25-DEC-2024
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Acidovorax sp. SUPP2539].
ACCESSION   WP_284412890
VERSION     WP_284412890.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..225
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23332
     Region          41..206
                     /region_name="YdeN"
                     /note="Predicted esterase of the alpha/beta hydrolase fold
                     [General function prediction only]; COG3545"
                     /db_xref="CDD:442766"
ORIGIN      
        1 msssastsss asgrpvgrld gaapqaapsa rtaagspvsv vivpgwrdsg pghwqslwae
       61 rlpgarrvvq ddwvtparap wvaalertvl eaphpvvlva hslgcitath mgepaaarvq
      121 gallvapadp erravlsdfa pvpyaplpyr silvassndp ycpirlagay arawgsefvr
      181 lpqaghvnvd sghgewplgw allhslvdga ewglgqgate trsaa
//
LOCUS       WP_284412964             360 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284412964
VERSION     WP_284412964.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..360
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40563
     Region          1..359
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mslipatilt gflgsgkttl lkrllseahg qkiavienef geenidndil vteskeqivq
       61 msngciccti redlretlql laakkrqgll efdriviett gladpgpvaq tffmdeeiae
      121 tylidsiitl vdakhapqql ndrqearrqv gfadqiflsk tdlvgkeetd alihrlkhmn
      181 prapikavhf gevplaevld lrgfnlnakl didpeflked dhghghdhdh ghqdhdhehg
      241 ehcdhpshqh genhgrhhhh dddvksfvyr aerpfdpakl edflgaivni ygprmlrykg
      301 vlnmkgterk vifqgvhqlm gsdlgpqwae deprlskmvf igldlpkdif lqgleqclae
//
LOCUS       WP_284412975             581 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Acidovorax
            sp. SUPP3334].
ACCESSION   WP_284412975
VERSION     WP_284412975.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 581)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..581
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=63137
     Region          10..561
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 msrsvnytss pllasktpvw rskfivamva lgfvglgara ayvqvfgnaf fqkqgevrfa
       61 rtlelpanrg rivdrnglil assvpaasiw aipedveqdn pevreklqql akllemplpa
      121 lktkladedk tfvwikrqld wevgqqiaal dikgiyqrke ykrqypeges aahvvgftnv
      181 edhgqegmel afdqqlagka gsrrvikdrl grvvegigae vppvdgqdmq lsidskvqff
      241 ayqklrdqva lhkakagsvv vldahtgell alanypsyvp dkrqnltgeq lrnraltdvf
      301 epgstmkpft iglaletgrv rpdtiidtnp grvtitgsti sdtsnhgvlt vegviqkssn
      361 vgttkiamqm pakemwetfs aagfgqkpqi hfpgvvtgrl rpyktwrpve qatmsygygl
      421 saslfqmars ytvfsnggki ipatmlkshe pavgvpvfse rtadqvrkml qmaagpggtg
      481 qqaqtvgysv ggksgtarkq vgksyasgky rawftgmapi dkpriivavm idepsngvfy
      541 ggavaapvfs avvqqtlrmm gvqpdmavkp qivantvees l
//
LOCUS       WP_284413026             373 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Acidovorax sp. SUPP2539].
ACCESSION   WP_284413026
VERSION     WP_284413026.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..373
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40402
     Region          152..370
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mrlaqfirha reeilaesfa yatripalqg saasvlrnhl plvldaiald leqpqsreqs
       61 idkslghaap paeesaaqsh gtlrarigld ieqlvaeyrv irscvlrlwm esgqptafam
      121 ddtvrfneai dqavaesvaf haaevakwrh iflgvlghdl rgplnamllt aqllervgsq
      181 npeqatylvg allrngryln vlldslleyn katlgvgtpl hrqavdlgaa cqeelemlqq
      241 afpkrrirwq itgdargdfd psrvrqavsn lvsnaaqhsp edsevavivv gqaaaveitt
      301 enlsdpippe vldtlfdplr rnaspsgass gnlglglfiv reiakahqge vtastadgvi
      361 rfkmvlpkss kaa
//
LOCUS       WP_284413055             503 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Acidovorax sp.
            SUPP3334].
ACCESSION   WP_284413055
VERSION     WP_284413055.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 503)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..503
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=54370
     Region          4..489
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mnanaatilv vddepdlrtl yeltllregy rvetaanlle arqqlqaqrf davitdmrlp
       61 dgfgmellhe lrdqqrrerc vvmtaygsae navealrsga fdyltkpvdl kqfrsvvasa
      121 iqgtggvppp rsartgqaar apheatgttt tlsldrlige seamrnvkqr iakvarsmap
      181 vlirgesgtg kelvaralha ssqradgplv avncgaipen lleaeffgar kgsytgatqd
      241 rdgyfqaarg gtlfldeigd lplamqskll raiqersvra lgstaeetvd vrivsathrd
      301 laadvqsgrf rqdlyyrlnv ievvipplre rredlpalca tllariaqes gapvppltqn
      361 aldriamhpl tgnvrelenl lhravalsdg eelhveppha safdaaradm aaaapavsaa
      421 agtdasgnqr nanpaasval psdlqawldq qereilvral retgfnrtat aarlgislrq
      481 iryriarldi aapndsdand dse
//
LOCUS       WP_284413118             269 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284413118
VERSION     WP_284413118.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..269
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29601
     Region          4..217
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 msvlmhlsdl hfgahdprvc aavgrlvqtl dvsllvvsgd ltqratarqf aqahefltgl
       61 gvpqllvmpg nhdvplfaww erlgrayrry erwwgrdlep vcdvagflav gvnttrpwrh
      121 ergslshaqi davaerlaaa prdrwrivvt hhplvvhpts dtehrphrag ealarwreag
      181 aqlllsghah epglaevlpg lwaaragtav svrlrahapn slvtlerrda gppglgalpa
      241 rhrltrwdyd arvqaflplp ardlassgt
//
LOCUS       WP_284413123             328 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284413123
VERSION     WP_284413123.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..328
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34514
     Region          4..326
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(41..42,46,122,126,129,150,153..155,174..175,179,194,
                     218..219,240..244,265..268,315,317)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(134,233..234,247..252,260..267,270..271)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mslavqirqh ggpeelqivd vtvgepgpge irihhhavgl nfidvyhrtg lyplqmpaai
       61 gmegagivea vgegvthlka gdraayasnp pgsyaevrlm paktvcklpd aigfetgaam
      121 mlkgltaqyl lkktlpaegl qpgdhvlfha aaggvgliac qwakalglql igtagsdekc
      181 rlalangaah ainyrtedfa arvkditggk gvkvvydsvg kdtwekslec lrpfglmatf
      241 gnasgpvapf apgalgakgs lyvtrqtlft hiatreatqa maddlfavvq sgavkihieq
      301 ryalrdveqa hrdlearktt gctvltls
//
LOCUS       WP_284413125             277 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Acidovorax sp. SUPP3334].
ACCESSION   WP_284413125
VERSION     WP_284413125.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 277)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..277
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29446
     Region          125..272
                     /region_name="NUDIX_Tnr3_like"
                     /note="thiamine diphosphokinase Tnr3 from
                     Schizosaccharomyces pombe and similar proteins; cd03676"
                     /db_xref="CDD:467544"
ORIGIN      
        1 msalaptapg wlpaaralaq rpaaaarlpf avagrivgsv aegvldeiia mppenmpvml
       61 skrehygvag whldsaagda saalallada lrragrcgpw rdeqlavcsa agerigtver
      121 gavrvlgiat ravhlvaiap dgrmwvqqra fdkpthpgrw dtlmggmvsa adtldtaler
      181 etweeaglri aalqdvvhgg hvdfarpsdd gegagymver idwfhatvpe glapenqdge
      241 verfellaaa qvharlarcd ftpeaalvla gfywpqk
//
LOCUS       WP_284413396             116 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: RNA recognition motif domain-containing protein
            [unclassified Acidovorax].
ACCESSION   WP_284413396
VERSION     WP_284413396.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Muto,Y. and Yokoyama,S.
  TITLE     Structural insight into RNA recognition motifs: versatile molecular
            Lego building blocks for biological systems
  JOURNAL   Wiley Interdiscip Rev RNA 3 (2), 229-246 (2012)
   PUBMED   22278943
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Clery,A., Blatter,M. and Allain,F.H.
  TITLE     RNA recognition motifs: boring? Not quite
  JOURNAL   Curr Opin Struct Biol 18 (3), 290-298 (2008)
   PUBMED   18515081
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Maris,C., Dominguez,C. and Allain,F.H.
  TITLE     The RNA recognition motif, a plastic RNA-binding platform to
            regulate post-transcriptional gene expression
  JOURNAL   FEBS J 272 (9), 2118-2131 (2005)
   PUBMED   15853797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..116
                     /product="RNA recognition motif domain-containing protein"
                     /GO_function="GO:0003729 - mRNA binding [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=11798
     Region          2..84
                     /region_name="RRM"
                     /note="RNA recognition motif (RRM) domain [Translation,
                     ribosomal structure and biogenesis]; COG0724"
                     /db_xref="CDD:440488"
ORIGIN      
        1 msskiyvgnl pysvtdailq snfaefgnvs sakvmmdret grskgfgfve masaevaqaa
       61 itglhgmsvd grsivvnlar preegggsgg ysaagygank rsdvgygtgg fgggry
//
LOCUS       WP_284413435             274 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Acidovorax sp.
            SUPP2539].
ACCESSION   WP_284413435
VERSION     WP_284413435.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 274)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..274
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29407
     Region          13..262
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mndraptieg phmeykdkvv livgassgig rtlalrlagm gaqvvamarr edrlrhlsae
       61 iaarggrcsl qvadaqdpaa alravqgala ehgridllml naggapaidm rsmtagevlg
      121 ymrsnydvav nvlfpaldam rrqrsgvvva tnslagllgv plqgpycaak galkllidtc
      181 rvefaefgir fvsvypgfia teataddgmp aplqmsedra vdhllralqg rymdyafprp
      241 maalvwlana lpkrlvvril rrdvpplgpe lrpw
//
LOCUS       WP_284413622             659 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Acidovorax sp. SUPP2539].
ACCESSION   WP_284413622
VERSION     WP_284413622.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 659)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..659
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=71219
     Region          11..653
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mdeeegpalt rvpgwawaay vaagvawvag gdallawllg tdagggthag lwgsakdiaf
       61 vlvsaalava glrrlqaada aalvrrgraw armargaeqr qrlattvvdn aiegmvvtda
      121 nnrilsvnaa ftrlmgytea ellgqtprlf ksgrhdrafy ealwtelsrt grwqgeiwnr
      181 rkngevfper mslstvrdga gvvthyvclf tdisqehtqr qrlaflahnd pltglpnrtw
      241 faqrleeata qarvsgesma vlllnldrfk dvndsyghav gdevlrhiar rlesalrpgd
      301 lagrlagdev gvlvrnapse deaaaiartl iaavaepwrs pegfevvaga svgislfprh
      361 gdsaqallqg ahaavygake rgrgawcffs eamtraarer lalesrlraa lalghlqlhy
      421 qpqvdiatgr vigaealvrw mdpqegmisp arfipvaehs gmigplgewv mheacrqaqa
      481 wraaglpglt mavnvsprqf hltdlagcaa salsasgypp tlleleiteg alaerpeear
      541 qvllrlrglg lrmaiddfgt gysslahlkr fpidvlkidq gfirdlpqnt ddmaictaii
      601 amghslglav laegvetpeq laflrergcd ryqgylcqrp lpaeaftall raqvggaah
//
LOCUS       WP_284413649             329 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284413649
VERSION     WP_284413649.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..329
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34674
     Region          22..327
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mhrrtllkna laaagataga ampwaaraqs dypsqpirwv vpypagggtd vlartvaeal
       61 rgplgqqivv dnrpgastni gaqmvatakp dgytlmsadn allaynehlf sklpfspekd
      121 ftyiaglsrf plalvvhpaf eaktvkdlla yaranpgkln yaspgngsph hlamemfknr
      181 tqtflthipy rgaapalqdv mggqvpcmfl dlaaglpviq agkvralaig sakrvpglpd
      241 vptlaeagvp ntevyafqgv lgpaglppal vtrlntevnk alasppvvkr mqdfgmeplg
      301 gtpeqframa raeakrwgei ikaagvkld
//
LOCUS       WP_284413692             372 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Acidovorax sp. SUPP2539].
ACCESSION   WP_284413692
VERSION     WP_284413692.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..372
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39986
     Region          6..366
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mssrnefdtl ilgggvvgms igfgmaragd svcvldgsds sfrasrgnfg lvwvqnkglg
       61 rpgyarwtmr sakdwqalad dllsltgvdv elqqpgglam sfdqqtlvah arkldalgqe
      121 lgmdypyqvl dhdqlrkltp aigpdvvgav ycpldghvsp lrtlralvqg fyarggrlis
      181 gvhvekiehe agqfkvqagd qtyiagrvvl aaglankela pqvgldapvr pvrgqilvte
      241 rmqpflfhpt hyvrqtgegv vqigdskeev gmddgtthge lariaaratr tfpmladanv
      301 vrtwgalrvm spdgypiyqq stqcpgafvv tchsgitlap vhagplvdwm rggaepteiq
      361 gfkaerfdvq ah
//
LOCUS       WP_284413697             487 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Acidovorax sp. SUPP3334].
ACCESSION   WP_284413697
VERSION     WP_284413697.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 487)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..487
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=53224
     Region          21..485
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 msdeawfdqf iqlgaggatr ygaamqacta qlttlfervt gpysgldpae llrrlhavdf
       61 satsvrpldd vleevsrdia shaivvqhpn ciahlhtppl vsslaaerfi aaqnlsmdsw
      121 dqsgaatfve qkvvghlcgl fgypdgadgv ftsggtqsni mallmardwf lweryqyrvq
      181 fnglgafaer lrivasaksh ftvdkaasvm glgekavvkv pvlddgsmda nqldaivdql
      241 ladgliafal vgtagttdhg aiddlgrlaa varrhgmwfh vdgaygsali lgeerhrlag
      301 leqsdsltvd fhkmwfqavs cgtlllregt rfrhllykse ylnrdtddlp nlvdktlstt
      361 rrfdalkvyv mlravgtevl grmvdhllrq trkvadlvrl hsgfellapp rlstllfryv
      421 ghaaggdmda fnrrlrahll tsgqavlget tiagraalkl tllnpcllmd dfdrllsmia
      481 daaerld
//
LOCUS       WP_284413778             345 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284413778
VERSION     WP_284413778.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..345
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=38226
     Region          1..341
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mstqhrgnlf dlmricaasa vifshhfhit htasptwlhs dmvggvavmt fftisgylvt
       61 qswlhqpkvl aflskrflri wpgvlfavlt nvflfgiffn slpatdflah pdtlgyfrnl
      121 llikdypylp gvfennpikh lmngplwtip ieslcylvla gagllgvfrs rwlaglaava
      181 yiaffltarn adltgemqhw feypayftyg aliavfrdaf halsgrlllv laplaavlff
      241 glqmehtagl lllppllihi gslnvpalaf lqrggdpsyg iylygcpvqq svyalwpdla
      301 fipslmlsva laavagyasw hlvespalrf krwfqrtpva pqaap
//
LOCUS       WP_284413809             275 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Acidovorax sp. SUPP2539].
ACCESSION   WP_284413809
VERSION     WP_284413809.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..275
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29697
     Region          5..275
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mtldlhpldd alalepagah rytgrttpay wnmvgpfgga taavllqavl qhpdrlgepl
       61 sltvnyagav sqgpftvqat pvrtnrstqh wtlsivqpga dgewvttttg tavtaarret
      121 wsladtpmpt apgpdtlepl akglgvawld ryemrpvaga lpqrwdgsgd sslsqlwmrd
      181 aparpldfca laaladvffp rvwlrrahrv pagtvsltvy fhagreqlaa tgtgfllgqa
      241 raqefrngff dqtaqlwnda gtmlasshqi vyyke
//
LOCUS       WP_284413826             285 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Acidovorax sp. SUPP2539].
ACCESSION   WP_284413826
VERSION     WP_284413826.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..285
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32481
     Region          <41..161
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mttlferiqq rfwgppqwda erisdewfra hfhyaadvvq hwlgsaldvk tarllnfgcg
       61 dgitdlalal rhgatsihgi dirqeyaklp riakeqlglr rvpkalsfet iapatqlagr
      121 rpvdgifsws tfehvsqdql epiardlyaa lnpggvfflq ieplyfspyg shlrrydevp
      181 whhllvsdde lwaiiqaheg pidgaerdfg fddfgvegyk qfvfneykal nrltadelva
      241 lmtragfhvi rqerrsvqmd ipaalhgqyp delllnneif lllgk
//
LOCUS       WP_284413848             744 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284413848
VERSION     WP_284413848.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20305241
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..744
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79607
     Region          85..641
                     /region_name="YCCS"
                     /note="TIGR01666 family membrane protein"
                     /db_xref="CDD:130727"
     Region          370..640
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mrispehrlr aalrvalshy vfnglsvafg lllisagvhg wlgaaaaasa svgvivtapp
       61 dlpgpargkf wqmlpapllg vplffgvqml hpselalgll vvpasfiafl amawgkrgvp
      121 iavavmfsmv fsmavppahg meplaaalat tghfalgaal yvvysvianh alnaryrvqs
      181 vadallalaa lmrvqarqft pvdlqgppap alagallqrq aalaeqlqaa rnivlesprt
      241 prrqrlagml llvlemrdhl laceldldal kahpghapvv grlrevllnv ademerladv
      301 mligrlptaf adhrphlaal rwddeaalpq pdnatpsprl largladrvg hindealrmi
      361 alargeaepn lavvranwqm fvsptawswh pfnglwrwda pplrhairaa lamgvgyava
      421 qalpwgthay willtivvvl rgslaqtler rnsrvagtll gcvlalalls mhptamgliv
      481 altlaqavah gfavrrylvt avaatvlglv qshmlhagss tafalferla dtligtgvaw
      541 avsyvlpswe rtqipalvsr tlaaqarhar ealalgqlqa vdnapelawr larreaydsl
      601 salvqatqrs lsepravrpp leplerlqlh cyqllaqlta vktmllqrrg hleperlqap
      661 lattadaigg alaaprtadg appaarvspg peplpdpfda qlgpwllrrl glavglaqel
      721 rsdadqvldl mavpvaeprk ppea
//
LOCUS       WP_284413968             262 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Acidovorax sp.
            SUPP3334].
ACCESSION   WP_284413968
VERSION     WP_284413968.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..262
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27447
     Region          7..229
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtqasavlit gassgigaty aerfaqrghd lvlvardqar letlaarlra dfkvavdvlp
       61 adltnptdva tvearlrdda rigilinnag aaqsggilqq tpdsierlia lnttsltrla
      121 aavaprfaea gtgaivnigs avgfapefgm siygatkayv lflsqglgve lsakgiyvqa
      181 vlpagtrtei weragidsst mtdlmdvgel vdaalvgfdr reavtipplh vaerwdaldg
      241 arqgllsdlr qahaaeryhg ak
//
LOCUS       WP_284414121             333 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284414121
VERSION     WP_284414121.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..333
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34225
     Region          9..329
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mteisdntpi prrawlrwsa gagmawlaga vqaadypskp irlvvpappg ggtdmmarll
       61 snalnsalgw tvvvdnvpga ggnigldkaa kaapdgytla mgessnltvn qalykkmpfd
      121 vardltpval makvplvlvv sakgpyrsva dlagaakrka vtfassgngt lahlcgelwk
      181 gkagldlvhv pyrgaapamt dlasgqvdmf aasitaalpm iqagllrpla vasplraaal
      241 pniptmaesg fqgieaavif gvvapagtpd tvvsrlnqei nhalkqpqlr qslidqgaip
      301 eslggtvpaf asllkderak wgqvvrdsga svd
//
LOCUS       WP_284414503             665 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidase U32 family protein [Acidovorax sp. SUPP2539].
ACCESSION   WP_284414503
VERSION     WP_284414503.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..665
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=73849
     Region          6..307
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
     Region          457..518
                     /region_name="DUF3656"
                     /note="Collagenase; pfam12392"
                     /db_xref="CDD:463557"
ORIGIN      
        1 msllphqiel lspardadig ieavnhgada vyiggpafga ragagndlrd lerlvrhahr
       61 fhsrifvtln tilrddeleg arqmawqvyn agadaliiqd mglleldlpp iqlhastqtd
      121 irtpekarfl qdaglsqivi areldlqeia avraatdpar ttieffvhga lcvaysgqcy
      181 ithahtgrsa nrgdcnqacr lpyevldgsg riiahekhvl smkdnnqsdn lralidagvr
      241 sfkiegrykd mgyvknitah yrklldeiie erefssepla rsssgrttft ftpdpdqnfn
      301 reftdyfvng rqddigafdt pktpgraigw vtkvgenfae lelsspdtvl hngdglcyyd
      361 lqkelvglqi nraeavnark glwrvfpkdp iagfkdlrrg leinrnrdmd wvrtldkkss
      421 drriglwaql setpdgfdlt ltdedgfvgs aaivhphqra tdgpqaeatl reqlgrfgat
      481 vfsvhdials lsqpwfvpas alnplrrdav aalesaraag lvrlpraepv qppvpfpedt
      541 ltylanvfnq kahdfyvkhg vkvidaayes keeegevslm itkhcvrfsm slcpkqakgv
      601 igvkgtikae plqlingkek ltlrfdckpc emhvvgkmkk svlnqhardm qavpmqfyrt
      661 rpvag
//
LOCUS       WP_284414382             266 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Acidovorax sp.
            SUPP3334].
ACCESSION   WP_284414382
VERSION     WP_284414382.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 266)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..266
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27953
     Region          6..231
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mphpnsnkva litgassgig avyadrlaar gydlilvarr adrlkalser iakthgvqae
       61 avvadlrdta dlarveails anerlhllvn nagiarlgpv aqrsaedals qitlnitalt
      121 rltqavlpaf iarkqgviin iasvlgihal pvsavyggtk afvlqysrgl qqelagtgvk
      181 vqlvlpasta teiwdlsgvp laaldkdalm ttehlvdaal agldqgetit wpsvadmglw
      241 dkyeaarael fastqvgtpa prynvi
//
LOCUS       WP_284414619             297 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Acidovorax sp. SUPP3334].
ACCESSION   WP_284414619
VERSION     WP_284414619.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..297
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31727
     Region          33..292
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mpresatahg eavasassad trheyllrgh gtnattgvll ihgltgtpne mrllakglhr
       61 agftvlavql aghcgtqddl vatrwqdwha svqrgadrla qatggrlvvc glsmgavlal
      121 alaqdrpgqv agvvalsptf rydgwsmpay trlsfllplf ralgigrrsv fmeqppygik
      181 daalrervva qmqsgdsaaa glpgnpwwsv iemralaahv rsrlgkvrsp clvlharndd
      241 iasaanarai vqgvrhapve lvllddsyhm itidrerrtv vartvafaeq iargtap
//
LOCUS       WP_284414738             240 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Acidovorax sp.
            SUPP3334].
ACCESSION   WP_284414738
VERSION     WP_284414738.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..240
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26305
     Region          1..>233
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrradrlfqi vqlirgrrls tadflakrle vsartiyrdv adlqhqgvpi egeagvgyrl
       61 gagfdlpplm fsqgeanalv aaarlaqswl dtglsvqves algkilsvlp paaraaaqaq
      121 alyapamavd prtqallrpl reavqsrnvv rlnyadelgr pserrvrplg cfyggrvwtl
      181 sswcelredf rgfrvdrivs ldvrperfav epgrtladmm revrrragad sepgpgsgpg
//
LOCUS       WP_284414656             746 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein [Acidovorax sp.
            SUPP3334].
ACCESSION   WP_284414656
VERSION     WP_284414656.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 746)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 746)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 746)
  AUTHORS   Porat,A., Cho,S.H. and Beckwith,J.
  TITLE     The unusual transmembrane electron transporter DsbD and its
            homologues: a bacterial family of disulfide reductases
  JOURNAL   Res Microbiol 155 (8), 617-622 (2004)
   PUBMED   15380548
REFERENCE   4  (residues 1 to 746)
  AUTHORS   Kimball,R.A., Martin,L. and Saier,M.H. Jr.
  TITLE     Reversing transmembrane electron flow: the DsbD and DsbB protein
            families
  JOURNAL   J Mol Microbiol Biotechnol 5 (3), 133-149 (2003)
   PUBMED   12766342
REFERENCE   5  (residues 1 to 746)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   6  (residues 1 to 746)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   7  (residues 1 to 746)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   8  (residues 1 to 746)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   9  (residues 1 to 746)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12109673
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..746
                     /product="protein-disulfide reductase DsbD family protein"
                     /EC_number="1.8.-.-"
                     /EC_number="1.8.1.8"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=77025
     Region          67..180
                     /region_name="DsbC"
                     /note="Disulphide bond corrector protein DsbC; pfam11412"
                     /db_xref="CDD:463273"
     Region          363..744
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 mshrllqrll palfliassa fhisagaqfn pktssattaa gasgssstvt tphvqaelva
       61 hapdgvapgk plwlglsith qpewhtywmn sgdsglptem ewqvpagiea gaiawpvprk
      121 ipignlanyg yegtvllpvp mtvssaftpg plartatfhl raswlvcrke cipeegefil
      181 qlpirsttal nagafeaaqq ahpqpvpapa gggaassarv dgnaialtva glppalrgqa
      241 leffpetagv ietaadwtqa wqgdvwtarv plsaqrsagp vpmpvvlaha grgwraelpv
      301 eggwpqaapm agvspaleaa lranaaqggg appaapqvta aplatlmaal agallgglil
      361 nlmpcvfpvl aikvvgfaqh aqnrrahrig glaytagvvl sfmalgalml alraageavg
      421 wgfqlqspgv vallaalftv vglnlagvfe fgrflpssva tlqarhpald afltgvlava
      481 vaspctapfm gaslgltatl paaqalavfa alglglalpy laaswvpava ralprpgawm
      541 dtlrrfmafp mfatvvwlvw vlgqqsgidg aaallallvm lsmaiwaltl agrtrwaiap
      601 fsiaalaymt aawgpkviei apgpattasa aataggwrpw qaglpeqlva qgqpvfvdyt
      661 aawcvtcqyn kkttlahedv lkdfaaknva llradwtrrd paitaalaql grsgvpvyvl
      721 qapgrapvvl seilgvqevr aaiagl
//
LOCUS       WP_284414821             312 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Acidovorax sp.
            SUPP3334].
ACCESSION   WP_284414821
VERSION     WP_284414821.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..312
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=34833
     Region          5..239
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mknakiilpg gaglvgqnlv ahlklhgyhn lvvldkhasn lailrqvhpd ivaedadlae
       61 pgawerhfeg adavvmlqaq igapqadpfv rnnltstgri laliqrhria htvhisssvv
      121 esvaqdhyte tkraqekmvl dsgipcvvlr ptlmfgwfdr khlgwlsrfm rkvpvfpipg
      181 sgrymrqply aadfcriivr cieerrvggv fnitglekvd yidiirqika atgagawivk
      241 ipyglfslll kvwalfdkdp pftadqlkal vahdefevid wpgifgvrat pfaeaihetf
      301 nhpeysrvvl ef
//
LOCUS       WP_284414835             448 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Acidovorax sp. SUPP2539].
ACCESSION   WP_284414835
VERSION     WP_284414835.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..448
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=49244
     Region          <22..281
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(42,116..122,151,177..182,211,243..247,249)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mlghwaallp iplpaspspi dvtalgiwal qftprvalle dsvvaemsas arlfggmqpl
       61 hdlletgame lgariawapt gtaalalvhh aanredcdgf raplahwldp lplaaitava
      121 ahhatlarig crtlgdvral prgglsrrfd kallqamdqa yglrpevydw itlpetfhar
      181 lelmsrveta pallfgarrl llqmagwlaa rrlgataftl rwchdvmrak dagtggeltv
      241 rtahptqhve hfarllaehl akvqllapag diellvseva piveesrsli petlrkgsst
      301 dlaleriqar lgegcvrrpi lcedhrlewm qcwesnafkr rkaaepayel plptwvleep
      361 lrlierdnrp iyqgplqlll gpdrveggww hrseaceggg ggggkdakpl nvqrdywlal
      421 sphagvlwvf qqrlagdqta wflhghfg
//
LOCUS       WP_284414995             689 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Acidovorax sp. SUPP3334].
ACCESSION   WP_284414995
VERSION     WP_284414995.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 689)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 689)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 689)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 689)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..689
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..689
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=76250
     Region          21..689
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mpdtssqadg ppqdphcsss llrlladsvp allayfesst lrcvfanqgy aestghtvea
       61 ilgktvqeai gdaawasiqp qvqqvlqgqr vqytrkqrsr ggptrmievn liphlhhqlg
      121 lmgafvlind ithhweaera vreseermrk fsqateeaiv fhreglvtdf nealtrlmgy
      181 tlaevrgrrm ldfvseafrp iteayvregr edpyeatvlh rdgrhvpvei vgksmpwkga
      241 dyriavlrdi sarrqaqerv aflathdalt qlpnrgtlmq rltevieaar rlpqaaavlf
      301 inldhfktvn dslghqagdm llcevsrrlv qgvrpgdiva rvggdefvvv lgdapdrpsa
      361 lavadqllad vcavfhaegt plsvsvsigv smypedgdsa telvrradaa mqqakhsgra
      421 nrqayapgmd ipsagvlqhe rllrdaimhg afvlhyqpqv rledgmlvgf ealvrwrhpe
      481 rdlvgpidfi afaearglit pigrwvlfea crqtrawhde glpqvpvavn lsalefrqrd
      541 vageiasvlh qtglaprfle ieitesvlmh dadqvrstld alkalgvrva iddfgtgyss
      601 laylkrypid klkidrsfva dtpgneddva ivtaivqmgr slqiqtvaeg vettaqhdll
      661 ralgchlaqg ylisppmdpr qtrewllkr
//
LOCUS       WP_284415024             156 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Acidovorax sp. SUPP2539].
ACCESSION   WP_284415024
VERSION     WP_284415024.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..156
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16994
     Region          18..153
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mnaptvstps rrlpeprsay svfrtittrw adndayghvn nvvyyswfdt avnaylierg
       61 tldihageti glvvetqchy faplafpqtv eagirvahvg rssvryevgl faegapesaa
      121 gghfvhvyvg redrrpralp qalldalapl riavgt
//
LOCUS       WP_284415054             580 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Acidovorax sp. SUPP3334].
ACCESSION   WP_284415054
VERSION     WP_284415054.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..580
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=61003
     Region          1..460
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          511..576
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(534,543..545,552)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            544
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mkkvlianrg eiavriarac adygiasvav yanadidavh armaseaygl dgdrpadtyl
       61 hiekllaiak rsgadavhpg ygflsesaaf aqavidaglt wigpsptaia rlgdkveark
      121 ialkvgaplv agtsepvnda sevlafaeqh glpiiikaaf ggggrgmkva wrmdevaely
      181 dsavreavta fgrgecfveq fldrprhiea qvladthgnv lvlgtrdcsl qrrnqklvee
      241 apapfiseeq rarihqsard icaeagytsa gtvefllsgn gtisflevnt rlqvehpvte
      301 qttgidlvle qlriadghal tvtetpkplg hsiefrinae dvgrgflptp gpvhhfapps
      361 gpgvrvdsgv qsgsvvpgtf dslmaklivt gatreqaiar akralsefki egvasvlpfh
      421 ravighpdfv ggegfkvhtr wietdfapdl aaalraepva dttlvrtame idgrrvslgl
      481 ppellrglqs apggapagag aadkatedpn avaapiagtl qtwkvaegdt vakgdviavm
      541 eamkmemqvt ahragtialr aaagsyhaag ktiadiqdak
//
LOCUS       WP_284415079             230 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Acidovorax sp.
            SUPP3334].
ACCESSION   WP_284415079
VERSION     WP_284415079.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..230
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=24713
     Region          5..183
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mslqrlpdpl psgieayrld fdlscdetph wpllsaveqa ragrfmqsad rlrfsatrta
       61 trqllarrls cqpvdlplaq daygkpfvdm kgavplfnvs hsgshalial adssafssvg
      121 idieqrragl dvdalseavl tdleksavvq aadpqeallq rwvgkeavlk aigvgiaehl
      181 rcvgihpgpe grwvlettvp ewsdveampv aapsgyaaal awrsrvqnpg
//
LOCUS       WP_284415116             436 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Acidovorax sp. SUPP3334].
ACCESSION   WP_284415116
VERSION     WP_284415116.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..436
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=48089
     Region          147..414
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mtlptpstgl ptdgahagat aattlpartt wrsrpleril rrlltnvscg tltvelpgge
       61 raegrgaepg phgtivlhrw kplwrlavgg dlglaesyrq gewsspdlaa llelgvrnea
      121 gwgralqasl parlvarlfh lrrantrrgs rqniafhydm gndfytqwld pdmlyssaiy
      181 gtgqesleqa qhaklariat llspkagerv leigcgwgal aialardtga nvtgltlsse
      241 qlrharqrvq eesltervdl rlqdyrdveg qfdhivsiem leavgerywp ayfetlkerl
      301 rpggravvqv itiadehfeq yrsttdfiqr yifpggmlps psrlrdalar aglalqaaet
      361 fgpsyattla ewrhrflsaw psieplgfda pfrrlweyyl cyceagfstg rvdvglytiv
      421 hadagaapvr aapspg
//
LOCUS       WP_284415121             300 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Acidovorax sp.
            SUPP3334].
ACCESSION   WP_284415121
VERSION     WP_284415121.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..300
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=32831
     Region          3..245
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mkfsvfqvsr rggretnedr mgycytress lfvladgmgg hpegevaaql alqtvsaafq
       61 rhakpkledv hgfladalla ahhqilryaa drgmldtprt tlvvavvqeg caswihcgds
      121 rlymvrggdl ftrtrdhsyl elrnmplqgi ervnrnvlft clgsptkpiy ditgpvaleq
      181 gdrillcsdg lwgtldddti arqlsrlpvs qsvpdlveda lrkagdtsdn vtvvalewet
      241 pdafestqgi stdsisddgf sstiqagpld mvdddmddea iersiaeine airrsaarka
//
LOCUS       WP_284415171             648 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Acidovorax sp. SUPP2539].
ACCESSION   WP_284415171
VERSION     WP_284415171.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2539
  ORGANISM  Acidovorax sp. SUPP2539
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Acidovorax sp. SUPP2539"
                     /db_xref="taxon:2920878"
     Protein         1..648
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=70885
     Region          2..610
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mtttfpqlll rhaaerptda alrekeygiw qthtwsglaa mvetlcaglh qaglhagehl
       61 vvvganrprl yatmlaaqsl gaipvplyqd avaaeciypl nnaevrfcvv edqeqvdkll
      121 eiraqcpals hlyfddprgl rnysepglas ldalveagta fvaqnpgwfr aqvdrvqpgd
      181 vaamfftsgt tgnpkgvvht hatlldraqa gaefdrltsa eevlaylppa wigqnifsys
      241 qwlacgyvvn cpesagtvsi dlkevgptyy fapprifegl ltsvmirmed agalkrkmfh
      301 acmavarrvg parmdgqpvg lldrikyalg dllvygplrn nlgfsrvrva ytageaigpd
      361 lftfyrsigi nlkqlygste tavfvclqpd nqaradtvgv pirgvqiqva dngeilvksa
      421 gllkeyyknp tataevltad gwyrtsdagf ldahghlkii drvkdvgriq ggandgamfa
      481 pkyvenklkf fpyikeaval gdrrekvcam vnidfdavgn waerrnlpya gytdlaqkpe
      541 vyelirdcve kvnadlagda llagsqisrf lvlhkeldad dgeltrtnkv rrgfiadkyg
      601 tlvealyagr teqfietqvk fedgrtgsvs atlklddart faptkqaa
//
LOCUS       WP_284415185             778 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: putative bifunctional diguanylate
            cyclase/phosphodiesterase [unclassified Acidovorax].
ACCESSION   WP_284415185
VERSION     WP_284415185.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 778)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 778)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 778)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..778
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=84784
     Region          102..776
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mnlralhrsl ilrlvgisll lllivqaagf avvqtfivrn araqiersld vdervwrwll
       61 tqnavrlqea svllaadygf rsavnsgdse tiqsvlenhg arigaamtal ldtrmhlqat
      121 spsrtpadyq savdqavpal vaqpqgsqia vvhgipyqfv mvpmrapllv gwvlmgfpvn
      181 etlvsemqql lsvdvaiqvr datgavavpv stlpdralad lrdfrmggeq vlggetllvr
      241 pvrldsgats aralllrsln dvvapyrqlq allggitvag lvlfalgsaf marrvttplr
      301 slvsathrls qgdydapieh trrldeignl arsfdrmrvd iagqqgeilr ladtdrltgv
      361 pnrerfrrai meaigpgsgg rpvavialdl drfkhvngvl gyalgdrllq avaerisgqt
      421 rspqdviarl ggnefamllp gadeaaardm aqrilrafet pmafddrtvd lsagigiacw
      481 pgpaqdadtl lshaeiamya aklrlsgalv yepsmdsssa vslslltelr ravdrnelrl
      541 flqpkvsltg qpghaaealv rwqhpergmv ppmqfipfae qtgfvrqltl wmfeqavifl
      601 aqprvqdlal risinlstrd lldpelsnrl gtllarhgvs aasfcleite saimdeplra
      661 eamlnrlseq gfklsiddfg tgysslaylk rlpvdelkid ksfvigmasd dgdeqivrst
      721 idlahnlgls vvaegvetvs ilerlralhc ddaqgyyisr plptddfiaw haaaaerk
//
LOCUS       WP_284415322             347 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Acidovorax sp. SUPP3334].
ACCESSION   WP_284415322
VERSION     WP_284415322.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 347)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..347
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38434
     Region          1..314
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 mlkrmrlknf tvfseadltf spqlnvivge ngagkthllk aaysvlaasy eegrkphaea
       61 ptktalqsvf anklvnvfrp eslgrlarrk qgrercdial efsvpdlntd fsfatnskse
      121 vaigslpkkw lptapaylpt relltifpnf vavyesrfle feetwrdtcl llgtplkkgp
      181 lqqrikellr pleaamdgsi dlgtngrfyl qqrngrmemp lvaeglrklg mlarliasgv
      241 lldkghlfwd epeanlnprl vrevagvits lslagiqifl athslfllre ldillnehkg
      301 iraqffglhs sangmaiaqg stlsdmgdit sleeslaqsd rylames
//
LOCUS       WP_284415489             283 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Acidovorax sp. SUPP3334].
ACCESSION   WP_284415489
VERSION     WP_284415489.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..283
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32081
     Region          15..282
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 msddsvaqqr kktfdieqhl lveaiyrryh ydfrgyaqas lkrrlqtalt rfncrtvsql
       61 qhlvlhdaev fpamleyltv qvsemfrdpt yfralretvv pvlrtypslk iwvagcstge
      121 evyslaillr eegllertli yatdinanal qkaeagiyai ervpsftenh arsggktsls
      181 ehytaaygrv vldkslrrhi vfsdhslatd svfaevqlvs crnvliyfdr dlqnralglf
      241 sdalcrkgfl glgskeslrf sahagsfdel vpqdriyqkk aga
//
LOCUS       WP_284415531             739 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Acidovorax sp. SUPP3334].
ACCESSION   WP_284415531
VERSION     WP_284415531.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 739)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 739)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 739)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..739
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=79563
     Region          35..711
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 msselahplt gflpshhdpl vvaasfavav lasyvtlava rrvrtsqryi glawwaagsm
       61 vmgtgiwsmh fvgmlafelp ialgftgglt fvswlsavaa cgvalgmagl agfrwphlva
      121 galamgigis amhyigmqal hlsigivwna gyvvlsvvva vlasatalwl fqvlqpmrgt
      181 rrrlfqagas lvmgvaicgm hyigmaaaqf pqgtvclsan alggagltam vviatlvlli
      241 stlfiailda rlqntarrlt qslkesnakl hqanaelqkr afadaltalp nrllfedrli
      301 hallrlervn hhrvvdrlav lfvdldgfkp indsfghaag dailieaaqr lraearesdt
      361 varvggdefl llledvgnaa dctvvanril aaiakpfqva grqvqigcsi givvhpdhgd
      421 rdklvanada amyaakragg ngyamfephm gsdasdqlel qndlrhalar gelslhyqpk
      481 idgkrgring veallrwnhp qrgmvsplvf iglaerfgli gqlgnwviee acrqmadwar
      541 sglrmrvain lsvhqlresg laeriehalq fhgldasqll ceitesvame dtkatqrtfe
      601 glarigvfls iddfgtgyss lnylrqlpaq qlkidrsfvn dleheedara vvdavvrlah
      661 alglrvvaeg vetsgqrdil lamrcdelqg ffyarpmpad vllawaqgdk pegsadfaps
      721 vlgalevags lpfdmtqrg
//
LOCUS       WP_284415655             202 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Acidovorax sp.
            SUPP3334].
ACCESSION   WP_284415655
VERSION     WP_284415655.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..202
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=22670
     Region          5..190
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mksasantfd eayyqrfyfd kktsvvdpqh merlgtfvcs ylkylrvpvq rvldvgcgtg
       61 lwkdivaqhf paasyqgvef spylcerygw qqgsvvdyqa sgepfdlvic qgvlpylgpp
      121 dlkaalrnlg qlsrgalyve avsredyerd iidedltdar ifrhsatlyr rglqegalel
      181 ggglwlsrka evplfelehv gg
//
LOCUS       WP_284415738             269 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284415738
VERSION     WP_284415738.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..269
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=28331
     Region          6..266
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mfpasgqalv venvpgaggn vgaalvarsp adgytleiga msthamngsi yknlsfdpmn
       61 dfdtvallay ainavavsas vpvrtfpelr tyiranpgkv nystggigth nhltvallak
      121 tadldivhvp ykgggpavaa lvqdecqlya ggaslllphv qagkvrlvav tektrsallp
      181 dlpsvsetik gfevtnwyga faprgleasr ralinqeinr vialpevadr lkglgmvhas
      241 lsplqvrdvl qadrdlwsht iqslrisse
//
LOCUS       WP_284415785             149 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284415785
VERSION     WP_284415785.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..149
                     /product="YybH family protein"
                     /calculated_mol_wt=15861
     Region          1..132
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mtrstfraat lggsaddtea afyealqtgd ierlmacwae eddivcvnpg gprllgagai
       61 raaftamfeh gtlrarpsqv hrvqalasav hsvvehvevv ldggvreaiv qstnvyhktp
      121 qgwrlvahha spgtvheaqr pgqpppvlh
//
LOCUS       WP_284415802             319 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP3334].
ACCESSION   WP_284415802
VERSION     WP_284415802.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..319
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33797
     Region          6..316
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mkrflaalsl gvlalgaqaq awpekpvtlv vpfppggstd qvaravgpri tekfkqsflv
       61 dnrpgatgti gatyvqraap dgytflvtsl gplvivphll kglqydamng fdlitvavqs
      121 pnvlvvpans phktvadvia yekanpgkms fasagngssd hltaelfwqq tgtkgmhipy
      181 kggapahtdl iggqvdasfq ninavaqyik askmralait spkrspvlpd vptlaeagvp
      241 nvevaswqai vapkglppav rekahaafve alkdpkvreq ftsigfemvt ntpeqfaafq
      301 qqesarwnkv ievgkisid
//
LOCUS       WP_284416007             313 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: amidohydrolase family protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284416007
VERSION     WP_284416007.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..313
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33677
     Region          50..313
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mersahlsrr slllgtaala alprlgksqt aapvrwsagt apparkappr atdchfhtyd
       61 agyptapgaa ltppdaspdd ykalqrrlgt trgvlvtpst ygtdnslqla smtalgadnf
      121 rmvavfaedv sdselkrlds lgargvrfnl pfpgpltmas letlsprlaa lgwhceinmr
      181 pqqleaaqdl lkrlpsrivi dhlgalpadg lnstsyaiir rlldkgntwv klsgaylnsr
      241 ppyaesagit aayvraaper mlwgsdwphp trkaddkpdd aelfdlmana mpdqatlqrv
      301 lvdspaelyg fap
//
LOCUS       WP_284415832              75 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Acidovorax sp.
            SUPP3334].
ACCESSION   WP_284415832
VERSION     WP_284415832.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP3334
  ORGANISM  Acidovorax sp. SUPP3334
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 75)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 75)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 75)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Acidovorax sp. SUPP3334"
                     /db_xref="taxon:2920881"
     Protein         1..75
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=7861
     Region          1..56
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mlriddvcff tglgrstvya kvkagdfpgp vqlhgacvaw retevdawia trpaaqpgca
       61 arkpvraaag artcm
//
LOCUS       WP_284416233             601 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: PHA/PHB synthase family protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284416233
VERSION     WP_284416233.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 601)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   4  (residues 1 to 601)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..601
                     /product="PHA/PHB synthase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=67021
     Region          50..599
                     /region_name="PhaC"
                     /note="Poly-beta-hydroxybutyrate synthase [Lipid transport
                     and metabolism]; COG3243"
                     /db_xref="CDD:442475"
ORIGIN      
        1 mtdvpnntnp qktfdaeafa tniaramets gkalaaylkp retgevqdrp paeiaevvks
       61 ftavadywls dkdrasdiqm kiakgyldlw gsasrrlage dappaispsp rdkrfadpew
      121 ksnqfydfvm qayllttqwa qdlvhnaegl dphtrkkaef yvnqitnala psnfvltnpe
      181 vlrqtvassg dnlvrgmqml aedieagkgs lkirqsdpan levgvnmatt pgkvifqnem
      241 mqliqyapst envlrtplli vppwinkfyi ldlrpeksfv kwcvdqgltv fviswvnpdk
      301 klgtktwddy mkegpltamd viekvtgemk vhtlgycvgg tmlattlawl adkrrqrvts
      361 atflaaqvdf thagdllvfv detqisaler dmqaagvleg skmamafnml rsndliwsyv
      421 vnnylkgqpp qafdllhwns datrmsaanh syylrncyle nrlstgtmvl dntlldlskv
      481 kvpvynlatr edhiapadsv lygsqffggp vkyvlsgsgh iagvvnppss gkyqywtndq
      541 ihdislkdwl kgaqehkgsw wpdwrawlse ldpeevpars vgteayppie dapgsyvrvr
      601 a
//
LOCUS       WP_284416294             506 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified
            Bradyrhizobium].
ACCESSION   WP_284416294
VERSION     WP_284416294.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 506)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 506)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 506)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..506
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55679
     Region          4..496
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mapeirhrrt lgqilllsag ffvlvvista svllvnkars dsawvvhtve aenqinalll
       61 evrraesgar aylltqspdf lrdheaavaa irplldrlat lvadnqvqvq nlarlrgiie
      121 trlsqfdrek alvaagdlpg avalvrdvgs tdssaimrat aeemrgeeer lfaqrtttad
      181 ksqqlativt vvgstlvvll aiisvllvrr stsardeaea klresnlnle atvdertadl
      241 reaneeiqrf ayivshdlrs plvnimgfts eleelrndif rriatlarav saapppaega
      301 epelegadkq lsedftealg fikssiakmd rlitailnlt regrrefvpi ridtrdlieq
      361 ivstlahqad eanttirlep lptivsdrla leqifsnlid naikymkpgv pgdiairart
      421 klgfaifeit dngrgidprd hqrifdlfrr agtqdrpgqg iglahvralv rrlggtmsva
      481 seldqgstft itlpinwnas nrnsdr
//
LOCUS       WP_284416308             416 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [unclassified
            Bradyrhizobium].
ACCESSION   WP_284416308
VERSION     WP_284416308.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..416
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44821
     Region          6..414
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mqslpqtadv ivlgagivgv ssayairerg lsvvlvdrkv pgeetsygna gilssgsilp
       61 lnkpslfsal psylgnrnaa lrwnpswtlr niewvlrfla navesrvrpr atalhgliga
      121 slqlhrdwiv ragepqrire tgwlkawrsd alaaakaeqa flaeygikse lldrqaisal
      181 epnmlpvykv gllhsqtasv dspgnvtkay armfegaggm lrqseirall adgdgwrvvl
      241 gegeirarhv vvalgpwspd ilrplgykvp mafergyhqe ftpnpvrqll rpihdaegsf
      301 lmtpmengvr vtsgveltdr dapsnfaqle qvvplargvv efgdaiaqpw rgarptlpds
      361 lpmigpaprh sglwlafgnq higlttgpat gaaiaamiag eapsfdasaf apsryl
//
LOCUS       WP_284416329             103 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [unclassified
            Bradyrhizobium].
ACCESSION   WP_284416329
VERSION     WP_284416329.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 103)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 103)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 103)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..103
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11345
     Region          8..96
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 maqlfhpsre ditlagvlsa ladpmrlriv kslmeqkdcm sctaaapcpd makstlsnhf
       61 rilresglih ttkqgvehrn vvreadlnar fpkllktilg yae
//
LOCUS       WP_284416366             308 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: 2-hydroxyacid dehydrogenase [unclassified
            Bradyrhizobium].
ACCESSION   WP_284416366
VERSION     WP_284416366.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Kutner,J., Shabalin,I.G., Matelska,D., Handing,K.B.,
            Gasiorowska,O., Sroka,P., Gorna,M.W., Ginalski,K., Wozniak,K. and
            Minor,W.
  TITLE     Structural, Biochemical, and Evolutionary Characterizations of
            Glyoxylate/Hydroxypyruvate Reductases Show Their Division into Two
            Distinct Subfamilies
  JOURNAL   Biochemistry 57 (6), 963-977 (2018)
   PUBMED   29309127
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10187381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..308
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=33270
     Region          2..306
                     /region_name="GDH_like_2"
                     /note="Putative glycerate dehydrogenase and related
                     proteins of the D-specific 2-hydroxy dehydrogenase family;
                     cd12164"
                     /db_xref="CDD:240641"
     Site            order(47,66..68,91,223,271)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:240641"
     Site            order(67..68,85,91,95,139..143,161..164,166,193..195,
                     199..200,221..223,247..248,271,273..274,306)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240641"
     Site            order(94,96..98,100..101,104..105,108,110,113..114,
                     116..117,121..122,124,127,130,154,245,249,252..254,256,
                     260..261,263,266,268..270,272..273,277)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240641"
ORIGIN      
        1 misiallsrp glmdpmkall arelpgvtvs swpepatrea elavcwkpep galaampklk
       61 lihsiaagvd nilsdptlpd vplcrivdpd itsamtefvl watlyfhrdf drvisnardg
      121 lwrrydqyaa kdrrvgilgl galgtdaalr lvdlgfavsa wsrspkqlag vttfsgadal
      181 daflsetdil vsllpltpst vglldaarls rlpkgaalil csrgehvvtd dlvgllrsgh
      241 lrgavldvfe qeplpsdhpl wrepgvlvtp hmaaiaswet itlqvadnar rllrgeplln
      301 tvdrargy
//
LOCUS       WP_284416471             221 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [unclassified Bradyrhizobium].
ACCESSION   WP_284416471
VERSION     WP_284416471.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..221
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24203
     Region          1..206
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mkaylfdldg tlvqseahka ralaaacaaf gaphadptly sevmgqdwet vtshffttyr
       61 idvgladfnq rfraiysdli eagvpltdga refiracrnt gallglvssa dhwmvdrild
      121 rvgmadgfdv iitkddvmhh kpdpqaylla msrlniaper tlvfedsaag lkaatdagcr
      181 cvvvrhpfnq rhdlsaafre ivsftepdvm ghdacigqrt t
//
LOCUS       WP_284416534             412 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [unclassified
            Bradyrhizobium].
ACCESSION   WP_284416534
VERSION     WP_284416534.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..412
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44096
     Region          16..409
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mrsaivlggg mvgvgtalhl qsrgwsvalv drrepgrets ygnagiiqse avrpyamphd
       61 iagvldiala htndvhytla glphhvrpll qywwnsfpar hevltrtyaq lisraapehe
      121 plieaagagn lvrrdgfrvl hrnqqqfdke ageaeaigka fgvkfkllsa sdlakaepgl
      181 nesglgglhw qepwtvsdpg slvtsyadlf vkrggkllqg dattlapqgs gwavttsegr
      241 ieaeavvval gpwspeflkr fgydipmvrk rgyhrhysgg apldlplrda afgylmnpma
      301 kgvrittgae lsapdakptp vqlgkaeaaa rqlidlgkpv epepwlgtrp cmpdmlpvvg
      361 qaarhkglwl hfghghqgft lgpatgrila elmsgeapsv datacaparf ga
//
LOCUS       WP_284416574             286 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FAD binding domain-containing protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284416574
VERSION     WP_284416574.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..286
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=30705
     Region          4..271
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mkarafsyrr aytvdealda hasngddarf iaggqslvpa lalrlqapri lidinhieel
       61 rgvtregewl rigaltrhce mltepliaef apllraaapf vahpairnrg tlggsvalad
      121 pasefpamml aldaeieiag asgrrrvrad effidlfeta aapgelvtai fvprfrcnqr
      181 icfdelarrr gdyalvgcgm qatckdglie giriaffsvg nvptrarsae aavsggrida
      241 eriaaaqaal dsdlappesd evppamrlhl arvllgrllg rlgeva
//
LOCUS       WP_284416666             129 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [unclassified Bradyrhizobium].
ACCESSION   WP_284416666
VERSION     WP_284416666.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..129
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14605
     Region          9..109
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mkrknftrrp gcaveatldl idgkwkgvil yhlqggsqrf gelrrlmpgi tqrmltkqlr
       61 aleedglvir kvyaevpprv dytlsevges lrpvievlrn wgerhqdrls capvadtine
      121 tiktphqta
//
LOCUS       WP_284416667             453 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces albus].
ACCESSION   WP_284416667
VERSION     WP_284416667.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albus
  ORGANISM  Streptomyces albus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Streptomyces albus"
                     /db_xref="taxon:1888"
     Protein         1..453
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=48189
     Region          5..69
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mepncqldal ldqsgmsrag laarvnrlgn ragitlrydh tsvarwlkgq rprgrvpeli
       61 cevlgcqlgr pltlsdigmd vpsagrtlta pvtaepaglg rfveraallw rsdrlhcdrp
      121 gpalltgaaa vapiwqwenp pddvdvsrtg gpgpevtead vavlhtargh yehlyrnagg
      181 vatrsrvvgf lngevapllr gtyddatgrr lhraagslaa isgicaydad eqglaqryfh
      241 qalrlgkasg dllfggyvva llvnqalflg dtrhalacag svlrtlgprt saalatdlya
      301 mqatayarlg drrnahacmh raetssgrir peeepeetgy vqpglvevrl aesllllgel
      361 saaagyaqaa arapahvrgr vnrlatltdv alhagepera avtaaqmvds aqgiesqrlr
      421 grmrrvkqrl sqhsgasaae aakliedsls vpf
//
LOCUS       WP_284416810             136 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acetyl-CoA carboxylase biotin carboxyl carrier
            protein [unclassified Bradyrhizobium].
ACCESSION   WP_284416810
VERSION     WP_284416810.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Li,S.J. and Cronan,J.E. Jr.
  TITLE     The gene encoding the biotin carboxylase subunit of Escherichia
            coli acetyl-CoA carboxylase
  JOURNAL   J Biol Chem 267 (2), 855-863 (1992)
   PUBMED   1370469
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423502
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..136
                     /product="acetyl-CoA carboxylase biotin carboxyl carrier
                     protein"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=14055
     Region          9..129
                     /region_name="AccB"
                     /note="Biotin carboxyl carrier protein [Lipid transport
                     and metabolism]; COG0511"
                     /db_xref="CDD:440277"
ORIGIN      
        1 mtfdqlhdit awmadagide lelsgpsfwl rlgrgqtqar dgqasaqppg askppcqvvt
       61 aptvgvflhr hplhaamlap egarvkagqa lgllrigsll vpvtapsdgi agamliahet
      121 vvgygtalva lhpler
//
LOCUS       WP_284416912             241 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase [unclassified
            Bradyrhizobium].
ACCESSION   WP_284416912
VERSION     WP_284416912.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..241
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26099
     Region          40..159
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mnargptdea rrrpaidfhd diatrwetlh rsrafkarta tmlgllprqd lagqrwldag
       61 cgtgtlsrll aqrgcvvtgv dasaemigla rrfqadteqp aglrfdqiat ieslpfsdgs
      121 fdgvlcasvl eyvpdvagal reihrvlrpd glvllsipnr asllrqgfkl afaassriga
      181 rpvfrymavs kfeasadaat qmmkdigfsv lglnfsgtpl pafldhsplf gtlinilarr
      241 t
//
LOCUS       WP_284416942             756 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: GumC family protein [unclassified Bradyrhizobium].
ACCESSION   WP_284416942
VERSION     WP_284416942.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 756)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 756)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..756
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=80776
     Region          14..732
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mrqaalneal sgfdavariw rrrgvfalva gavlalavva lvvlpvryla tasviiaeqe
       61 pgantsaawa qkvgdpadme sqllvirspr llrqimsspg vvdavvgecq rgrllgsaea
      121 cqrlktdvga fidhvdgrfs vasagrsrvi nisyqssspe vaqtlanalt qtfledqrte
      181 gansrevass wlwqelkqld qqlreaddki qkfrrtkglm rganapisse rltsigqqls
      241 qaeaaradaa arlqeikseq ergptdapsv lqsrtiadlk qqlttvsaql asaagvlgpk
      301 hpsilaltre qaiiqqrlvd emqsiaasaq ktfdantalv nalkkqmdta kaeagsatld
      361 easiesmvrd teikrqqyae lykkaselet drrvlrgstr lvslaelpsk pffpkkipfl
      421 aagltlavif gvaaalladq farlrttpks apdmpkpvss evvasvdaap psvpdlpeqa
      481 epsivpiemp spperkshlp svadvsilac lprlktlrqm salgailqgy qplaipqvlr
      541 lasedgefqq tlhdlvhelg vdqatrpqri avtspesgdg ktttvcalae hlaaagsrvl
      601 lvecdlahpi faqvmalpph rgwlralehg tplrddvlnt ehahldvlpa gaatgpvgdi
      661 leainldall aglddydvil idtplparnd flagidwavv cvrsdrslie pavttvnrsr
      721 algagdvgiv vtmteserhv mpqpqvasaa ayaeag
//
LOCUS       WP_284417083             292 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: HpcH/HpaI aldolase/citrate lyase family protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284417083
VERSION     WP_284417083.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..292
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31271
     Region          1..280
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mirprrsllf mpgsnarale kgrnlpadgl ildledsvap dakaaareqi akavaadgyg
       61 krellirins ldtpwwsddv amagqaatdg ilvpkvstve dlrtvtnrla evgadpalkv
      121 wamietarav ldadllaatv hetgsrlagf vfgpndisre trirmlpgra tmlpmishci
      181 latrahglei ldgpysdfan adgfsqeciq ardlgfdgkt lihpgqidtc naiftppsae
      241 iaearkilaa felpenasrg aiqidgrmve rlhaemarrt iaiadaiaam gk
//
LOCUS       WP_284417106             468 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284417106
VERSION     WP_284417106.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..468
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50681
     Region          134..459
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mslrrfsvgl lvfagllvag wltyrpdral raattavaem icaktfvsgl dpqttfaetm
       61 erpglrrlra vmryrvetdm rmveasllgl hgsralfhdg lgcvslqgqk apyvphsdvs
      121 tlratetppa lpdfaetnpv eptdpalqaa ldhafeepag pplrrtkavv ivkdgrliae
      181 ryaspigidt pligfsmtkt vtnallgilt rqgrlslsmp apvaewrdpt dgrheitieq
      241 lmrmtsglal detnsgfdpt sqmeihrdma afavhaplia ppgqrwayss astqilarii
      301 rdaaggpeqt ielawrelfn plgmrhvtlq fdgtgtmqgh anmlasardw arlgqlylgd
      361 gvvgnrrilp egwvamsata tldtdygagl wtnrsqhvha qgrarqgipa daffafgllg
      421 qrlvimpsqr mvvvrlgdai dpdgdikgva rlvreviaat espataak
//
LOCUS       WP_284417185             523 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alkaline phosphatase D family protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284417185
VERSION     WP_284417185.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..523
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58224
     Region          13..512
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mtlriarpqp pvlsrrrfls taaagvatls mprlsraadr pqithgvqsg dvgmdggvvw
       61 aradrpsqmm vevattesfk darrlppiaa lpesdftakm llddlpsgqd ifyrvkfrdl
      121 aftaaesepv vgrfrtapgn krdvsfvwgg dvagqgwgin pddggmftfa tmkkhrpdff
      181 lhsgdtiyad gpiksevklp dnkvwknltv eekakvaetl defraahkyn fldenvrafn
      241 aevpifvqwd dhevtnnwsa skelpaayke rniqllaara arafhemypm resivepgrv
      301 yrtinygphl dvfvldersy rganganled kygpssyfig peqmrwlkqa llnsratwkv
      361 iasdmplsli vyddaanrkg seaiaqgdgp argreleiae ilrfiktapi qntvwltadv
      421 hyaaahyydp nkaqfqdfep fwefvsgplh agtfgpneld ntfgpevrfi kapgldkqnl
      481 ppsagmqffg hvkidgasgq mtvtlrdrad valwsttldp kla
//
LOCUS       WP_284417246             253 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [unclassified Bradyrhizobium].
ACCESSION   WP_284417246
VERSION     WP_284417246.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..253
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=27561
     Region          19..226
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mlslgvtpia rerpcnnllr rlsgtdyali spyltedqav sndllyspgd dvqvvhfpcg
       61 paltsylvpn edgrdveail vgregavggi vsegflpayt rivvkfggpf arlplsrlaa
      121 aklqsktlrn vfaryadcml aqmfqstacn aihsieqrta kwivaamdrt dgepvvplth
      181 eqlatllgvg rsyvsrvvqt fraegildtr rgafmvrdfd alkqrsclcn eavkthfeev
      241 lrgvypteqa aag
//
LOCUS       WP_284417423             473 aa            linear   BCT 25-DEC-2024
DEFINITION  class II fumarate hydratase [Streptomyces albus].
ACCESSION   WP_284417423
VERSION     WP_284417423.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albus
  ORGANISM  Streptomyces albus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Woods,S.A., Schwartzbach,S.D. and Guest,J.R.
  TITLE     Two biochemically distinct classes of fumarase in Escherichia coli
  JOURNAL   Biochim Biophys Acta 954 (1), 14-26 (1988)
   PUBMED   3282546
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Streptomyces albus"
                     /db_xref="taxon:1888"
     Protein         1..473
                     /product="class II fumarate hydratase"
                     /EC_number="4.2.1.2"
                     /GO_component="GO:0045239 - tricarboxylic acid cycle
                     heteromeric enzyme complex [Evidence IEA]"
                     /GO_function="GO:0004333 - fumarate hydratase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006099 - tricarboxylic acid cycle
                     [Evidence IEA]"
                     /GO_process="GO:0006106 - fumarate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50245
     Region          7..472
                     /region_name="FumC"
                     /note="Fumarate hydratase class II [Energy production and
                     conversion]; COG0114"
                     /db_xref="CDD:439884"
ORIGIN      
        1 mtdstssaey rtehdsmgev rvpahakwra qtqravenfp vsgqrlerah iqalarikaa
       61 aavvnarlgv ldqeradavr aaaeevadgr wdehfpvdvf qtgsgtssnm nmnevlatla
      121 terlsgsdgd glqvhpndhv nasqssndvf pssihiaata avtadlipal ehlaqalerr
      181 aeefadvvks grthlmdatp vtlgqefggy aaqmrygver lraalprlae lplggtavgt
      241 gintppgfaa avieevartt glplteardh feaqgardal vetsgqlrti avgltkisnd
      301 lrwmssgprt glaeialpdl qpgssimpgk vnpvipeavl mvaaqvtgnd vtvatagaag
      361 nfelnvmlpv iaknllesir llsnaarlla drtvdgitan aerareyaes spsvvtplnk
      421 yigyenaaav akkalaerlt ireavlrsgy vergeltveq ldealdvlrm thp
//
LOCUS       WP_284417436             713 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Streptomyces albus].
ACCESSION   WP_284417436
VERSION     WP_284417436.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albus
  ORGANISM  Streptomyces albus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 713)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 713)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Streptomyces albus"
                     /db_xref="taxon:1888"
     Protein         1..713
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=77462
     Region          <10..>106
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          146..710
                     /region_name="COG4425"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:443540"
ORIGIN      
        1 meraaedrla plprtpgahn anslsdppag tddptdtghp pahtdrspst tngtpadtte
       61 patteltsta eptsttnptp gadipaapps aqdedtppmg daapeagpas gaqaarwrav
      121 argarrrlaa lvrrpyweap nssyvlrrwp gltalwcatl ffwlsltpsl vprpwplqgv
      181 iggitaamgy aigglaewli rlalapllrr ygrllpgrrh lrpsrhprps qrwrarawla
      241 yyalstllti aalslsadaq relrrlqgmp aaltwhslmi allalgictf lvalgravrl
      301 gtralirvlg rfvprplaig agllvsatvv vfgtrdvvfd rgvidvaahl aektdkstkd
      361 gitrprsslv sgstaslvhw ddlgyegrnf tgsslsadqi asvtgkgarq pvrvyvgqes
      421 aptfrararl avrelertga fdrdvlavag ttgrgwvnst daepleyihh gntaivavqy
      481 sylpswasfl vdkeqagrat ralveavrar wleipaaerp klvvfgeslg aygieaafdg
      541 pddllakvdg avlagtpnfs pirreltahr dpgspvwrpe ydegrhfrfa qwprkdlarp
      601 gpestwgtpr vvylqnasda ivwwspelal hrpcwlrepl gpditgavnw fplvtfwqtt
      661 vdmavsygvd aphghrygng sveawaavap segwtdadte rlrrfmdrre apy
//
LOCUS       WP_284417521             361 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: PHA/PHB synthase family protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284417521
VERSION     WP_284417521.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..361
                     /product="PHA/PHB synthase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41008
     Region          <1..360
                     /region_name="PhaC"
                     /note="Poly-beta-hydroxybutyrate synthase [Lipid transport
                     and metabolism]; COG3243"
                     /db_xref="CDD:442475"
ORIGIN      
        1 mnasapfdql asiperiqte vqraiqrsik gveyfttsgp tlgstpkdvl svrgtmslyh
       61 yrpqadeiyr vpilivmatt nrgyildmvp gqsfiefllk rgydvymldw aapkpeekgl
      121 rmedyvldfi pycvrrvqed sgehdvtvig ycfggvlsll yasifhdgpm knlicfttpi
      181 dfremtlfqn lsdrryfdvd hlvdsignvp peiifssfem lrpasravsq vqlweniwnd
      241 dyvksyrmfd rwatdtlpla geyfraitkd lmwdnklyng tmsvgghrcd laeirvpilh
      301 avaehdhivp yeaarhlipk vgstdkeevi lkgghvslva ganavrrlwp kldswlggrs
      361 t
//
LOCUS       WP_284417526             256 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: esterase/lipase family protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284417526
VERSION     WP_284417526.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..256
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27408
     Region          40..141
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 msasahalrp psealmlleg ralpelgafl aalpllsmap rgdghpvlvl pglvasdmst
       61 rplrsflngk gyaasgwqqg rnlglrpgvq qamvdlveqm sdhhgrkisl vgwslgglya
      121 rqlakvmpdr vrsvitlgsp fagspkstna wrvyemasgr radeedlrfg galsdpppvp
      181 ttaifsrsdg icawqgcken nstisesiev esshcgmghh paavfavadr laqpegqwqp
      241 fdrggwrslv fpdphr
//
LOCUS       WP_284417613             524 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: purine-cytosine permease family protein
            [Streptomyces].
ACCESSION   WP_284417613
VERSION     WP_284417613.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..524
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53661
     Region          22..469
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 maeegthgag rgqggadvva gapgdqafkv ethgidpipd aerhggardv fwvwfgsnlt
       61 ftyvingala vlyglsfwqa savvvigglt ffvisaagls gvrtgtatlv israpfgvrg
      121 nlpagvlnwi vsigytiint vvgaqaleaf ladlgwhgtg prtlallvtl altfgvatwg
      181 hatvqlaerw layllaagfa vllvlllpga dfhghgggaa aglsgwslal vvtfagpfsy
      241 mpmpadytry lprttrlrsl twcgalggfv ssvglgiagv aaatrtdmtd avagtekllp
      301 gwfqtaflll vlggsvtnsi ltlyssslnl qvlgvpwsra ralmisivvt algsygalfl
      361 adftasltsf lsllilvfap wsgvfladml lrrcrydtta lhagrhggyw yragyhpagm
      421 talvaglvfa tltcdselwt gplvaplgga dltvlsavvs gllyaalarh vrpaapdgap
      481 aapagttatg dgapaasega paaydgvpaa spapraapag rshd
//
LOCUS       WP_284417632             401 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284417632
VERSION     WP_284417632.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..401
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43785
     Region          1..393
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mgplagikvi dmttvlmgpy aaqtlgdyga dvikvespdg dvtrkigpwr hpgmgpvtln
       61 tnrgkrvicl dlkkpagrda vlrmvkdadv llynirpqam arlnlgyelv salnprlvya
      121 gvfgfgqdgp yaakpayddl iqggaalsyl mavagdgtpr yvpnalvdri vgltavgaic
      181 aslvhrdrtg rgqrldvpmf etmaafimgd hmggltyepp ldrggyarhl spdrrpykta
      241 dghicvivyn dkqwdaffta sgrtdlrade rfnsfarraa nidivyaela rifetrstae
      301 wtalldeadi pvmpmhdles llhdphlvat nffpvvqhpt egpirttrvs atwsetkaep
      361 qrlaarlneh gaeilrelgy sadeiatmir dgattpspar e
//
LOCUS       WP_284417660             326 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: Bug family tripartite tricarboxylate transporter
            substrate binding protein [unclassified Bradyrhizobium].
ACCESSION   WP_284417660
VERSION     WP_284417660.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..326
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33410
     Region          22..323
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mksfcarlig asvavtfvvt flagapasaq qlelkvmapa apgggwdqta ramqqafvas
       61 gvarsvqvtn vagaggtvgi aqfvngakgd gnqlmvngfv mvgalamnks pvtleqvtpi
      121 arlteeiqvi vvpaaspikt aqdlaaalka diakvtfagg saggvdhvma alfagtvgad
      181 akkvnyipfs gggeslaail ggkvtagisg lseydgqiks gklraigvss enripgvdip
      241 tfkeqgidlv lanwrsvvaa pgitpeqkkt lseavekmvk sdswkdilkq kgwddaylpg
      301 dafaeflkke nvrvtdvlrs vglvks
//
LOCUS       WP_284417677              98 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Bradyrhizobium].
ACCESSION   WP_284417677
VERSION     WP_284417677.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 98)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..98
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11372
     Region          10..65
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 marhedtglr rtirrhqlre mvpladttiy emeqrgefpr rfalsprcvv wdlseveawl
       61 slrrstpltr aphpdvnlrq srpvkgpdra rrsaskae
//
LOCUS       WP_284417719             263 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: c-type cytochrome [unclassified Bradyrhizobium].
ACCESSION   WP_284417719
VERSION     WP_284417719.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..263
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28311
     Region          <72..194
                     /region_name="TsdA"
                     /note="Thiosulfate dehydrogenase TsdA, contains C-terminal
                     cytochrome c domain [Inorganic ion transport and
                     metabolism]; COG3258"
                     /db_xref="CDD:442489"
ORIGIN      
        1 masrlgmcrq tvrsrmsrsp kliiavalat fagsvalagg pgekiaakte sksepkteak
       61 teanapqrfn igraptveei rgwdidvrpd gqglptgkgt vaqgeklfmd ncaschgefg
      121 egagrwpvla ggkgsltsdn pvktvgsywp yastlfdyvr hampfgspqs lkvdeyyalv
      181 ayvlylndvi tdqnfeltdk nlatikmpne ggfimddrat sekafwqkep cmknciapvk
      241 itgratavdv tpedkdgkpr gve
//
LOCUS       WP_284417726             700 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: protein-disulfide reductase DsbD family protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284417726
VERSION     WP_284417726.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 700)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 700)
  AUTHORS   Porat,A., Cho,S.H. and Beckwith,J.
  TITLE     The unusual transmembrane electron transporter DsbD and its
            homologues: a bacterial family of disulfide reductases
  JOURNAL   Res Microbiol 155 (8), 617-622 (2004)
   PUBMED   15380548
REFERENCE   4  (residues 1 to 700)
  AUTHORS   Kimball,R.A., Martin,L. and Saier,M.H. Jr.
  TITLE     Reversing transmembrane electron flow: the DsbD and DsbB protein
            families
  JOURNAL   J Mol Microbiol Biotechnol 5 (3), 133-149 (2003)
   PUBMED   12766342
REFERENCE   5  (residues 1 to 700)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   6  (residues 1 to 700)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   7  (residues 1 to 700)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   8  (residues 1 to 700)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   9  (residues 1 to 700)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12109673
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..700
                     /product="protein-disulfide reductase DsbD family protein"
                     /EC_number="1.8.-.-"
                     /EC_number="1.8.1.8"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=73645
     Region          38..155
                     /region_name="DsbC"
                     /note="Disulphide bond corrector protein DsbC; pfam11412"
                     /db_xref="CDD:463273"
     Region          297..690
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 msirhpgwlg lllgallfat tgaragasrp qpnletrlvv gdvaradsgv ttawagldvr
       61 ldagwhtywr sagdagappe fdwtgstnva dvtvewpapr rfseqdidtf gyeehvlfpl
      121 rvrfrdqaap ahlklkavlf vcsiictqqe trleadipat shqpndqali eewrqsvpre
      181 tapglsvtal rierqpkpql rlearatppl rapdvfvdgn eavssgraqv snssdgavti
      241 hvplrgldqa aagqilrvtl idgdraieat lpvdadavaa ksatarphaa aasiwsvlgv
      301 allggfilnf mpcvfpvlsl klvslvdhdp arapsrrpaf lataagiias fvtlalvlsg
      361 lkaagaevgw glqfqqpafl iamiavlaaf ganllglfei hlpwwiagrl ggatgrntma
      421 ghaingfvmt llatpcsapf vgtavafals qaapqillvf talglgmaap ylglaaaprl
      481 aalfprpgrw mltlravaal amiataswll rvladisgva taavlaavll vpaliltmlr
      541 fplrrtfaga gvivaiglml taatvisppd spgqsgeiaw rplvpadiaa qvraghtvfv
      601 digaswcvtc kvneklvids tavrsrltsd vvavradwts hddaiaaylq sfgryglpfn
      661 vvfgpgapag ivlpelltpq ivldaidtas tisqkethkt
//
LOCUS       WP_284417735             109 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [unclassified
            Bradyrhizobium].
ACCESSION   WP_284417735
VERSION     WP_284417735.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 109)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 109)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 109)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 109)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..109
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11921
     Region          9..97
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mkfdadimev aadqasdllk alsnrhrlli icqlvdgers vgelatllgl rdstvsqhla
       61 llrkdglvta rrdgqtiyys itseparevl ktlyqvycat pppkpvptl
//
LOCUS       WP_284417796             347 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Streptomyces albus].
ACCESSION   WP_284417796
VERSION     WP_284417796.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albus
  ORGANISM  Streptomyces albus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces albus"
                     /db_xref="taxon:1888"
     Protein         1..347
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37264
     Region          16..307
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mttyderanl selsatagev lrcvesvieg kpevvrlslt vllaeghlli edvpgvgktm
       61 lakalaasvd csvrriqftp dllpsditgv svydqqrkdf efkpgavfaq vvigdeinra
      121 spktqsalle smeerqvtid gqtyelpdpf mvvatqnpve megtyplpea qrdrfmarvs
      181 igypspaael emldvhgsas plqdlrpvah ahdvvkliet vrgvhvsdav rryavelvaa
      241 trahpelrlg aspratlhlv raakaaaala grefalpddi qalaapvlah rllptaqaql
      301 nrrtaeqvvt eivqrvpvpa vgrtpaapgm ppapygqppq hggtrgy
//
LOCUS       WP_284417877             404 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FAD-dependent oxidoreductase [unclassified
            Bradyrhizobium].
ACCESSION   WP_284417877
VERSION     WP_284417877.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..404
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=43754
     Region          13..401
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mkviiigagi gglclaqslk rsgldvalye rdaapfdrrq gyrlhldadc vsaikealap
       61 elyalfeats mnplpyttim dtqfniqrrf qtddysktqh hvadgiathl nvnratlrei
      121 llhdladich wgaqfirfet deggvtahfd gcapvhgdil vaadgagssv rtlrapqarf
      181 mdsgvraiyg kltldtarkv lpahaladif taafdsskkl ilgvgpvifp mrpdlaaesl
      241 lptaplsrqd dyvgciisgr kelfgddahl qamdshdlqa vaadllrpws aeaarvpeaa
      301 npdsfffirm tssipfelap mprvtllgda ihamtpslgr ganvalrdam llarhirdir
      361 nqevsidagl qayetemtgy gfgvvrhsae mgarllgqdp lpgt
//
LOCUS       WP_284417935             177 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: VOC family protein [Streptomyces].
ACCESSION   WP_284417935
VERSION     WP_284417935.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..177
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18734
     Region          51..174
                     /region_name="PhnB"
                     /note="Zn-dependent glyoxalase, PhnB family [Energy
                     production and conversion]; COG2764"
                     /db_xref="CDD:442048"
ORIGIN      
        1 mraravrmwa agtagaaalt vglvagapsg agavsptsar ptvqeapryg qptlytenid
       61 emldfyheaf gfrvdyrfpe qgpavfgtvs lgdsyyltfc tydvikestp lkrigpskrk
      121 qseiavlapd vdaaytkaka agarglmtpk dqpwgersay vsdpagnlvq isthngs
//
LOCUS       WP_284418022             142 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: GlcG/HbpS family heme-binding protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284418022
VERSION     WP_284418022.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..142
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=14286
     Region          1..136
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 madltldtar kildatlakg vekklkplav mvldargclk aaaaqdgtsl mraevahgka
       61 ygalalglgs ralfqraqeq affidavntl aqgrmvpvpg gvlildgttl lgavgvsgdt
      121 sdndeicaia gieaaglkan pg
//
LOCUS       WP_284418061             230 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: SGNH/GDSL hydrolase family protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284418061
VERSION     WP_284418061.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..230
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=24173
     Region          50..223
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 maaktqarlg fvvfaviaaa aatfvlsrrs aapsgsdhrt vrqlvvhynm qarpddpivv
       61 lgdsiveaat lpasacghpi vnaglagagt rsdlagwlkp algpkqpfai ivslgvndal
      121 tdkpdqaavf agryeallre laklttrlfi vefppvevrg pftaamekta masitgyraa
      181 lpdlakraga tflplppmes pftlegihln sagyrswdqa iqqgtelacr
//
LOCUS       WP_284418082             486 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: flavin-containing monooxygenase [unclassified
            Bradyrhizobium].
ACCESSION   WP_284418082
VERSION     WP_284418082.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..486
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=54384
     Region          1..451
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mstehvdvli vgaglsgiaa ayhlqhkcps krfailegrg aiggtwdlfr ypgirsdsdm
       61 ytlgysfkpw tdpkaiadgp qilkyvrdta tengidrhir fnhrvisasw ssaearwtve
      121 iersteqgtr epvsmtcgfl fmcsgyyrye sgylpdfkgm adfkgrivhp qawpddldys
      181 gkrvvvigsg atavtlvpam aksaahvtml qrsptyvvsr pardalankl rehlpaslay
      241 hlirwrnvlf gmyffqlsrr kpdrvkqlil ggvraalgpd ydvathftpr ynpwdqrlcl
      301 vpdgdlfqti reqrasvvta gietftergv rltdgrelea divvtatglv lqvlggieia
      361 vdgrtvdfsr tlnykgmmys dvpnlaatlg ytnaswtlkc dltceyvcrl lnymdrhgyr
      421 qcvphnddat vtplpslsfs sgyvqravad lpkqgskrpw rlyqnyaldi vslrfgkidd
      481 gvmrys
//
LOCUS       WP_284418100             175 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: D-glycero-alpha-D-manno-heptose-1,7-bisphosphate
            7-phosphatase [unclassified Bradyrhizobium].
ACCESSION   WP_284418100
VERSION     WP_284418100.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..175
                     /product="D-glycero-alpha-D-manno-heptose-1,7-bisphosphate
                     7-phosphatase"
                     /EC_number="3.1.3.83"
                     /GO_function="GO:0034200 - D-glycero-beta-D-manno-heptose
                     1,7-bisphosphate 7-phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19619
     Region          7..171
                     /region_name="HisB1/GmhB"
                     /note="Histidinol phosphatase/D-glycero-mannoheptose
                     bisphosphatephosphatase, HAD superfamily [Amino acid
                     transport and metabolism]; COG0241"
                     /db_xref="CDD:440011"
ORIGIN      
        1 mttaqlkpaa fldrdgvinh ddnyigsper irwmpnvaha irrlneagyh vflftnqsgv
       61 arglfteddv lslhdwmrae laaqgavidd irycpyhteg sverylrehp wrkpqpgmil
      121 dlmqhwpirr egsfvigdrv sdmaaaeaag lpgflfaggd ldafvtevia qtsrr
//
LOCUS       WP_284418107             336 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: MraY family glycosyltransferase [unclassified
            Bradyrhizobium].
ACCESSION   WP_284418107
VERSION     WP_284418107.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Anderson,M.S., Eveland,S.S. and Price,N.P.
  TITLE     Conserved cytoplasmic motifs that distinguish sub-groups of the
            polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase
            family
  JOURNAL   FEMS Microbiol Lett 191 (2), 169-175 (2000)
   PUBMED   11024259
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Lehrman,M.A.
  TITLE     A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P
            transferases
  JOURNAL   Glycobiology 4 (6), 768-771 (1994)
   PUBMED   7734839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10160628
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..336
                     /product="MraY family glycosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=35217
     Region          36..278
                     /region_name="GT_WbpL_WbcO_like"
                     /note="The members of this subfamily catalyze the
                     formation of a phosphodiester bond between a
                     membrane-associated undecaprenyl-phosphate (Und-P)
                     molecule and N-acetylhexosamine 1-phosphate, which is
                     usually donated by a soluble UDP-N-acetylhexosamine
                     precursor; cd06854"
                     /db_xref="CDD:133464"
     Site            94..95
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133464"
     Site            207..210
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133464"
     Site            order(254,265..268)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:133464"
ORIGIN      
        1 mianpaaivv aialiaagmc avlivllrpl lqryalarpn arsshkiptp qgagiavvgt
       61 tlvvggafas vfgfapltml fiavpllalv glvddirpip vlprfilqgl avglvvltap
      121 ddlrlfpipl aieralllia glwfvnlvnf mdgldlmtvv eavpitatlv lfglsgslpw
      181 pataiaaalc gallgfapfn rpvakvflgd vgslpiglll gwgllhlawq gaiagalllp
      241 lyylvdatft llrrmarrep fwaahrthfy qratdngftv tgvvrevvvl navlavlaga
      301 svalnsvmad avllviglaa vgfvlrrfsr prsrga
//
LOCUS       WP_284418221             396 aa            linear   BCT 25-DEC-2024
DEFINITION  cytochrome P450 family protein [Streptomyces albus].
ACCESSION   WP_284418221
VERSION     WP_284418221.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albus
  ORGANISM  Streptomyces albus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 396)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces albus"
                     /db_xref="taxon:1888"
     Protein         1..396
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=43535
     Region          16..395
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(53,60,82..83,90,94,101,230..231,234,238..239,242,
                     275,280..281,284..285,287,310,337..339,342..343,345..347,
                     351)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(60,76,78,81,83..84,170..171,179,229..230,233..234,
                     238,281,284..286,386)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mtalpqpfde sframphavy nklrdekavh rvalpdgtav wlvtrdadvr agladrrlsv
       61 nkahstggyq gyalppalda nllnidhddh irlrrlvsqg ftprraeamr agiqavadrl
      121 adrleerles egtadlvhdf atplpltvvc dlfgvpepdr rpfgswvstm lalespqqva
      181 eavtsvhdfl ralvderrka pgddllsali aardeddrlt edelcslafl vlgagienvq
      241 hllsagflal lrhpgqlaal rgdssllpda veelmryahs qltairrfpt epveiagttv
      301 pagdtvllcp asanrdpery papdrldirr rdnahlslgq gmhyclgapl armqtglale
      361 tllgrfpglr paveedrlqw rtsfrshalr alpltr
//
LOCUS       WP_284418172             150 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Bradyrhizobium].
ACCESSION   WP_284418172
VERSION     WP_284418172.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..150
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16085
     Region          3..134
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mpghlarrfq qiavavflse veaagfdltp vqyaalaaia anpaidqitl agliaydrtt
       61 itgvidrlaq kglvvrqasa rdrrsrelli tdegrralda itpaveaaqr lmvrgltkae
      121 tnelirlmqk aiaagndlsr aplregtaer
//
LOCUS       WP_284418284             490 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: N-acyl-D-amino-acid deacylase family protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284418284
VERSION     WP_284418284.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..490
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=51386
     Region          10..490
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mtdtqpssds fdliirggtv idgtraprfe advgirdgri vavgeldgrt aarvidaagr
       61 ivapgfidsh thddsavlvd pgmtckvsqg vtsvvtgncg vsiaplkpgs prpmplglls
      121 pgdgriaeya sfagyvaalr aapaavnvap mvghtslras vvsdlgraas eaeiaamrgh
      181 vqealdagai gvstgtfypp aeaapteeii evcrpltgsg gvyathmrne andvirslee
      241 sfaigkaldv qvvishhkvv gpanfgrtke tlplitkams cqcvaldcyp ynasstmlht
      301 dpaklqvkvv vaaskphpem agrdladiaa awgvdrleaa krlqpasaiy famdeadvkt
      361 ilafeptmig sdglpfgerp hprlwgtfpr vlgyycrele lfsletavwk msgltaqnfg
      421 ikgrgtiavg nhaditifda akvrdtatyd dpcvpaagie avvvngaltw wqgahqnara
      481 gqvisraarp
//
LOCUS       WP_284418524             261 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase [unclassified Bradyrhizobium].
ACCESSION   WP_284418524
VERSION     WP_284418524.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..261
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28030
     Region          31..259
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mnqavesads pafiavgtgd qsrqiavrar pgnppglfwl ggfnsdmkgt kalaldawaa
       61 ergracvrfd ysghgesggr fvdgtigrwl eesvavfrqv crgpqvvigs smggwmalll
      121 arallqepae atlaglvlia papdfteelm wkgfapeirq eieangvwmr pseygepypi
      181 traliedgrn hlllggainv gcpvrilqga qdpdvpwqha falahrlpad dvvltmiqdg
      241 dhrlsrpqdi armlaavgei g
//
LOCUS       WP_284418580             246 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: metallophosphoesterase family protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284418580
VERSION     WP_284418580.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..246
                     /product="metallophosphoesterase family protein"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26712
     Region          2..226
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mrfaaiadvh gnhlaleavl adihaqavte ivnlgdmasg pldarrtmdr lmaldavhvr
       61 gnhdrwlidr prekmgawer paiaqlesgh ldwlrtipat avyrdqvflc hatpdddnvy
      121 wlesvapdga vtcapldeie riaagisqsl ilcghthtar avrlrdarli vnpgsvgspg
      181 fsynvphphv ieagtpdary aileltsagw svsfrhvpyd hqamaalart ngdaefasal
      241 atgwvr
//
LOCUS       WP_284418588             835 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified
            Bradyrhizobium].
ACCESSION   WP_284418588
VERSION     WP_284418588.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 835)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 835)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 835)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 835)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..835
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=90791
     Region          326..827
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          589..824
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 msgvivvmrq tllsctslar rglmglaata lapatsgfag dgapadaist lfelsrqdva
       61 evtamlallg fsvvaavalv rtrlaaarke arlradvael qlqadryral lfaepqilia
      121 wpagghrpqi sgdtsllvpq eqpqrilafg twlppepalq ldhavealre agegfllhlt
      181 tshghaleam graiggqaiv rirelsglrr elaetqhrlk slgeetdslr alaaalpwpi
      241 warqangalt yvnaayaraa dardvpdais rnlelldsad rtdlqralga ggrfegrlpi
      301 vtggerrihd vraftlgngs agvavdasea valsdalvrm heahrrtldq lssgvavfdg
      361 qrrltfynds yrrlwdldta fldsqpddss vldrlraark lpeqsdfraw kvklheayra
      421 veaakdtwfl pdgralsvvt tpnpeggvty lfddvtesfa larrydglir vqretldsla
      481 egvavfgsng rvelfnpafa rmwrltpesl rehphidtve swcrplydda vawrtvreai
      541 tsienrldia lklerkdgsv ldcmsrplpd gatmltfqdi tdtenveral resnealeaa
      601 gqmkidfvhh vsyelraplt tiigfahfls dpstgpltpk qaeyldyvtk stnallaltn
      661 nildlatida gamklelgpv daakaieaaa egvqdrlatd rirlevavda nvgsfvgder
      721 rvvqvlynll anavgfsppd ssvmvsarrt dhsvafavtd sgpgippevk dkvfewfesh
      781 sqgsrhrgag lglslvrsfv elhggkvrmd svvgkgttvt cdfptdhiaq rnaae
//
LOCUS       WP_284418622             239 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [unclassified Bradyrhizobium].
ACCESSION   WP_284418622
VERSION     WP_284418622.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..239
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25258
     Region          9..219
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 madatpaskl dlvifdcdgv lvdseviscq ahadvlslcg ypitadqvfd rflgrsskqa
       61 tqeieaelgr slpedfnarl qerlfrtfeq elqpiagiae vldtldlpvc vassgshqrm
      121 rvslgatrly drlaphifss sqvengkpap dlflfaaaqm narpaacvvv edslagiqgg
      181 vaagmtvlgf hggshgrpgh adrlkaagat lvfddmrqlp lilsrlgdka aplagfsav
//
LOCUS       WP_284418632             397 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284418632
VERSION     WP_284418632.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..397
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42098
     Region          2..390
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mqskaeidsv lrqkadagei pgvvavaads ngviyegafg krdlgradpm tsdsvfwias
       61 mtkaitcaag mqlveqgrls ldapigavlp dlaapqvldg fdakgepilr paktaitlrh
      121 lmthtagfcy dmwngdmaay vqkagtpgii tckndalklp lasdpgtrwe yginidfvgk
      181 aveaasgqtl dtylrdnlfa plgmddtgfk lgaaqrarlv gmhargedgs lapipfeieq
      241 epefhmgggg lygtagdyir ftrmilnngr gngnqvlkpe tvaamrdnhi gelemtkmaa
      301 avpgvtndvd lypdivkkwg lsfmittaqt aegrsagsla waglantyyw idpardvtgv
      361 ilmqllpfad rlcletfagf ergvyaglga aggqkaa
//
LOCUS       WP_284418709             339 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces albus].
ACCESSION   WP_284418709
VERSION     WP_284418709.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albus
  ORGANISM  Streptomyces albus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Streptomyces albus"
                     /db_xref="taxon:1888"
     Protein         1..339
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36791
     Region          16..304
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mpktssrlls llsllqthrd wsgdelarrl evtsrtvrrd idrlrelgyp ihaakgpsgg
       61 yrlgagsrlp pllfddgqav alalalraaa tgdaigedaa ralatvrqvm pprlrhridl
      121 lqvtavrppg aggdalhvdt rlltevsrav hareelrfdy ertpgsgrqa rraqphhlvt
      181 rcghwyviaw dpdrddwrtf rldrlhlrtp ngprftprpl pggdvaaflt grfrgtdgtt
      241 tdwpcrgevv lglpvqevap fvedgiveql dsghcrlvlg swswtglaaa larfdtdirv
      301 vgppqladaf aalaarcaha aatappapea aaaqgdtef
//
LOCUS       WP_284418764             430 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: S1C family serine protease [unclassified
            Bradyrhizobium].
ACCESSION   WP_284418764
VERSION     WP_284418764.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 430)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..430
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=45838
     Region          50..>242
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mvalcsagaa glsswaaaqg lpgaeavyas apprllqirt lvadagrqts tgsgflvsad
       61 glaitnyhvv sdaalepkty rleytgadgt qggvtllavd lpndlalvrv dkqdapffaf
      121 dkaaldgtlp kgerlyslgn pldlgftiie gtynglvehs yndhihftga lnpgmsggpa
      181 vnaqgqvvgv nvatrrggql isflvparfa stllargkda kpapgdlrkd viaqlaswrg
      241 alyksladeg frdrvfgsyq apetraawfe cwastnasas pkprasinst sckaeasvyv
      301 asdlntgtve vnhsytksid lnqfqfatvl tqlaqprlam ggsfrkwytp qhcredfvgv
      361 taaadhpplr vmwcaqgyre fdglydvalv avtqdradea lvsrlslqai ayddalrlgr
      421 sflerlqvar
//
LOCUS       WP_284418828             329 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Streptomyces albus].
ACCESSION   WP_284418828
VERSION     WP_284418828.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albus
  ORGANISM  Streptomyces albus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Streptomyces albus"
                     /db_xref="taxon:1888"
     Protein         1..329
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=35758
     Region          <126..231
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mnpdtafngy icanvlhgle rlgvfellrd eksldmdrfc atngldsavf ralvgaaesf
       61 gyldvrgaqv ratsvgedva rylgfftwgv ggyhdifasa apvargerrf gvdlhrdegm
      121 valgsaqadt almrhildee iagidfrtlv dlgagvserv srlvkarpgt rgigidisrp
      181 atelardtva gyglagtvep vcadvldilf ngqeidggda advvmsfmfl hdllaaperr
      241 eevvprlrka fprahtflla dttirprned gdgrlpvfss gfelahalmg vplhtreeye
      301 elferggmkl rrsvpfgaph tylfvleas
//
LOCUS       WP_284418866             529 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: Y-family DNA polymerase [unclassified
            Bradyrhizobium].
ACCESSION   WP_284418866
VERSION     WP_284418866.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..529
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=57246
     Region          12..350
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(15..16,19..20,57,60,114..115,167)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(112,115,191..194,223,247..252,283,309..313,315)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mravsanrrr ilslwlprlp ierikrqqaf tgappeskpq vvvikdanal lihaldeaaa
       61 rhgvslgqpl anaravcpdl vvheadlaad aqmlegiadw cdrftplval dpphglaldi
      121 tgcvhlfgge tklmrsvcda ltvhgltvsa aiaanavcar tlnrqvhgri vpdgeeaaav
      181 aplpvaalgg seavtlglrr aglktigdva argrneitar fgaaftrvla qalgeadapi
      241 sprkvppdyi vekrfaepva tdtviaasls slaamlvaam aqqgkgarrl eacffrtdgl
      301 vrviavdtgq pvteagvidr lfrerldaln dpldpgfgfd mirlsasrse ivvqqqrdld
      361 ahvhdndela alidriaari ggkrvivhlp idthiperaa lplpaqqnla atstaawper
      421 aegepplrpl rlfarpeaiq viagvpdgpp arfvwrraah avvraegper vamewwrpdg
      481 qgltrdyfrv edehglrfwl yrdglydrel eqpeglpvqp awymhglfa
//
LOCUS       WP_284419027             257 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: HpcH/HpaI aldolase family protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284419027
VERSION     WP_284419027.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..257
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27710
     Region          7..240
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 msatpkpfnr lkhawrdrkp tfgaiatips iqtvrimaqq ldwiivdleh gpidlstaha
       61 mitatagtpc vplvriaane phlakapmdl galginfpmi ssraeaekav rsvrypprgd
      121 rlwgpfhapf hwnvsmadym atadddmvcm vtiehveave rideimatpg idiavigpgd
      181 latsinkrgq lddpqvksli araeagilks gvpiggaars aeqanamier gylalalgfd
      241 wslfqrgiaa sfegikr
//
LOCUS       WP_284419029             109 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [unclassified
            Bradyrhizobium].
ACCESSION   WP_284419029
VERSION     WP_284419029.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 109)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 109)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 109)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 109)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..109
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12332
     Region          3..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 miqaetvtiv mraladptrr avferivnsd eitvveltrg ssvtqgaisq hlkalkqagl
       61 vcerpegrkv yyraeprgle pladwmshyg vfwrdrfanl rhllkdidp
//
LOCUS       WP_284419051             289 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284419051
VERSION     WP_284419051.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..289
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30285
     Region          <19..244
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 maravcfaat rpsptsfsal aglplahqpg evwdyglsvd vlarvvevvs aqpfdqflee
       61 rlfrplgmvd tgfsvppskl srlvdppsgg wggppdsisa dvakptvlfs gggglastaa
      121 dylrfcqmll nggaldgvri lepvtvrrmt analppqvrf aginsgivgp lsgstwglgf
      181 airsdpkmsv vpgslgsfmw mgaggtyfwi dpeqqliaiq lvqvasgtga sfnagfrnla
      241 ygalripdqg vpvpvtidrt aleafvgtyr fasvssrdlq tefgasafr
//
LOCUS       WP_284419072             148 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: SRPBCC family protein [unclassified Bradyrhizobium].
ACCESSION   WP_284419072
VERSION     WP_284419072.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10141965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..148
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=15365
     Region          3..146
                     /region_name="CoxG"
                     /note="Carbon monoxide dehydrogenase subunit G (CoxG);
                     cd05018"
                     /db_xref="CDD:176853"
     Site            order(5,7,9,18..20,22..23,28,32,38,44,46,48,50,52,57,61,
                     65..67,70,76,78,80,92..94,96,98,107,109,111,113,127..131,
                     133..135,137..139,142)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176853"
ORIGIN      
        1 mamtmtgevq laapreqvwd klndpevlkt cipgceeler tedgglrava kmkvgpvsar
       61 fkgkvtlsdl dppngykisg egeggvagfa kggavvalae kdggtlltyn veaqiggkla
      121 qlgqrlingt akkladeffa nfakavqg
//
LOCUS       WP_284419175             953 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces albus].
ACCESSION   WP_284419175
VERSION     WP_284419175.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albus
  ORGANISM  Streptomyces albus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 953)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 953)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 953)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 953)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467590
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..953
                     /organism="Streptomyces albus"
                     /db_xref="taxon:1888"
     Protein         1..953
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=101410
     Region          <35..910
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          885..938
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mvtgsarswk ipprleklvd eqaattaaer dghtvireee lhrllaavgp prpgarrkda
       61 lltvvgmpga gkttlaeava erfaadggrv lwadsspset dlafsclhql lrpvrkdmda
      121 lparqrealh aafgltersg vpdlmligia vltllsdhaa eqplllivdd aqwadiasld
      181 alffaarrla depvtllvtt rdsalgglaa repavvlepl grgaaerlld lqprvptglt
      241 rervldqaeg nplalvelar aaassddavr gpdgplpvtd rlerlyagrl aalpgetrra
      301 vvrlaavdae dpsravlswl pdiadpvwap aeeaglvrrg agrlrhghpl srlavyhaag
      361 aqerraahle laelfrgqdp drhawhlaaa tvgasarvsa aledsadrar hrsgyaaaah
      421 mleraadlhp drgestrllg aatrtavltg rldsverlaa rtragtddpt aaacaalqvg
      481 rlmalttshs aafgqlmrpa aaladrapga alealaaaav vrfysgdvtq lheierllar
      541 ttkhpahvfg ererllagwv esvahpeaad prlalrlpal agaareepet ltllavaawl
      601 ldetepaara fddafaswts qgplpdglgg vaalayleqg rwaraqsact elaavasrag
      661 ldhaaacaaa teallralrg dvagarsrar yalslvdpqe srsvsalahr algtaataeg
      721 dhetayrhyr vlfdgqgnpa hyhlsypalp elaaaaarge rredaarivd gvegtltnag
      781 alaprrtalv rlsrallapa deaerhftaa lenpvlgrrp feraqallay gewlrrrrri
      841 adarpplvea eavfrrlaaq pwaaraqael raagarsrma apdafaaltp qqqqivrlaa
      901 lglsnrevae klylsprtvs shlyrafpkl gitsraqlrd vvedaapgag trt
//
LOCUS       WP_284419297             396 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase family protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284419297
VERSION     WP_284419297.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..396
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=43321
     Region          6..387
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mnddqrfigs ltglrfvaaa tvavghgaps lgrgwpaeli aqvssigmtm ffvlsgfvlw
       61 lnyarrfqae hvaaalrefa iarfarlypm yavvviaivg ylaiargfsa pslgfiltmt
      121 qawfpvqnst mlvavvpslq hlwsisvelf fyllfpfvcf alagvvrlst miwlalanil
      181 afaltiaaff tfgdavlqal vpslqhdgmq wltyyapylh vaqflagcfa amiyqnrsvs
      241 qpdaaerrtv tavfwlsvas lacapvllfl qprlpgwsfs ielavrliei vgfsivfvaa
      301 sgygharwls srtiiiggec sysiyllhpf lirlamigks dapgvlelll rlglfvaivt
      361 avawitymli espsrawirr afgtsapcev ihakas
//
LOCUS       WP_284419318             322 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase
            [unclassified Bradyrhizobium].
ACCESSION   WP_284419318
VERSION     WP_284419318.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 322)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..322
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=34919
     Region          1..302
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mkdfagriav itgggtgmgr elarqlvaeg cnvamcdvsa eamaetrrlc eaeglpqglr
       61 vtthvadvsi eaqlqrfrde lieqqatdri hllfnnagig gggslftnsr eqwertfnic
      121 wggvylgvrt flplllkade ahivntssvn gfwasvgmgv shtaysaakf avkgfteali
      181 ndlrlnaphi kcsvvmpghi gtsivsnsrk mqsgtdtdel seteialarq rmtgmgidvs
      241 aksdadiqna arerarsfle dapttaaqaa kiildgvkae qwrilvgeda klldmrvrqs
      301 peqayepeff qrfaqeagwk lg
//
LOCUS       WP_284419450             344 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase family protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284419450
VERSION     WP_284419450.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..344
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37300
     Region          110..336
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mrlldtspeg egefadclai vqriddhdee swyqewmrsa damraeafaa anagspdtar
       61 rkwlraidly dvaaspfssc lmrqaevaag irvcavdcln agvpqgevvt ipwradysle
      121 ayflpapdrn gpaptvvcvc epgqrkeksl vkfagqaaer glsllvvdll gpgpasrfde
      181 ivgrrdleta igsimdyvce redvddaria iladdwsssf vargiardpr yaaavcdagl
      241 wdihervcls rrltpderag lpsasdcrva rqimcpvlva fpesgwlrad iaarlvaqmk
      301 rehldvtlei lasqrggasd dapasaavld wiaarlasap klrs
//
LOCUS       WP_284419865             338 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FAD binding domain-containing protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284419865
VERSION     WP_284419865.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..338
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35869
     Region          1..325
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mnsfdyarag diaeavklka ampdakfiag gtnlidlmky hveqprrlid isrlplttve
       61 etstggvrig alvpnstlay hpvierrypl lasailagas aqlrnmastg gnllqrtrca
      121 yfydvatpcn krtpgagcaa vgglnrnhai lgasadciat hpsdmcvala aldatvhvtg
      181 aqgeraiafa dfhrlpgdrp dldntlrade iitaialpvq gfaanhsylk irdrlsyafa
      241 lvsvaaalel dggrirharl alggvahkpw rsdaaeavlr aqapdaeafg raadvlleda
      301 hahahnafki plarraiirt ltqaanatpq iqsiktir
//
LOCUS       WP_284419922             272 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: methyltransferase family protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284419922
VERSION     WP_284419922.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..272
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29756
     Region          <191..262
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mvsnsisssh larltallra alaaphgagr falavatglv chalfalavl smigamfygm
       61 sesfgrvprp wayaanagll lqfplvhsll lgrgrrwlar lgphgttlat thyaiiaslq
      121 llclfalwtp sgiiwwraeg vafivlclay asawlllira swdagaevqs galgwlslma
      181 draprfpdmp vtglfaiirq piylsfalal wpvpvwtpdq lavalvlsay cllaprwker
      241 rfmqiygarf aayrarvpyv vpcwpsrreq tp
//
LOCUS       WP_284420116             390 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [unclassified
            Bradyrhizobium].
ACCESSION   WP_284420116
VERSION     WP_284420116.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..390
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40410
     Region          5..366
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtrridcdva iiggglvgss salalrgmgf tvtlldkgfc gaqasgvnyg gvrrqgrppe
       61 qlslsqrsha iwprlqqlig idgeflrsgh lklarsaadl asleqyaadv apfgldlelv
      121 ghnqlserfg iggdvvggsf cpgdghanpr lvatafaaaa rragaevlen tkvlgatrls
      181 ggfaleaegl gvtarivins agawadsfas vfgepvpler typsmivtep ldpflgvnig
      241 iegggiyarq vtrgnvvvgg eraaplddpd ysrprsdgvl timqraself gplrhaqair
      301 fwsgteatmp drnpvigpsa ttpglfhafg fsgagfqiap gvgevlaelv rdgetstpia
      361 pfaitrfspa sqpgdasqaa mttgsketsp
//
LOCUS       WP_284420161             336 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: zinc-dependent alcohol dehydrogenase family protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284420161
VERSION     WP_284420161.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 336)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..336
                     /product="zinc-dependent alcohol dehydrogenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=35029
     Region          1..336
                     /region_name="MDR7"
                     /note="Medium chain dehydrogenases/reductase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cd08276"
                     /db_xref="CDD:176237"
     Site            order(40..42,45,143,147,168..173,191..192,196,211,
                     236..237,239,258..259,283..285)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176237"
ORIGIN      
        1 mkayhvngha gagrlvqvdv rkpepghgev rirveaasln yrdliildra gqggldgrip
       61 lsdgagvvda vgpdvvqwqv gdrvaasffr dwvsgpykaa yvasalggst mdgmlaehvv
      121 lpatavvavp ehltsieaat lpcaavtawh glvtrggmgr gdtllvqgtg gvalfglqfa
      181 talgaraivi sssdeklart kalgaailin yhttpdwdla lmtatsgqga shvlelggpd
      241 tydrsirsla sggkivqvgv ltgfgpkpdl arlqwenadi igvtvgsvah ftamnrflsd
      301 htihpivdrv fgfdeapqaf ahlrsgahfg kivvkl
//
LOCUS       WP_284420261             306 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: 4-hydroxy-tetrahydrodipicolinate synthase family
            protein [unclassified Bradyrhizobium].
ACCESSION   WP_284420261
VERSION     WP_284420261.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097240
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..306
                     /product="4-hydroxy-tetrahydrodipicolinate synthase family
                     protein"
                     /EC_number="4.3.3.7"
                     /GO_function="GO:0008840 -
                     4-hydroxy-tetrahydrodipicolinate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009089 - lysine biosynthetic process via
                     diaminopimelate [Evidence IEA]"
                     /calculated_mol_wt=32955
     Region          8..294
                     /region_name="DHDPS"
                     /note="Dihydrodipicolinate synthase (DHDPS); cd00950"
                     /db_xref="CDD:188637"
     Site            order(48..52,88,90,113..115,144,146,256..257,276,278)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:188637"
     Site            order(49..50,141,146,169,194,196)
                     /site_type="active"
                     /db_xref="CDD:188637"
     Site            169
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188637"
ORIGIN      
        1 midtrtrlqg lwlplitpfr dgaldepslr elirhyaakp idglvlgats geglalswde
       61 rarlvhtvrd elaaigralp iclgvggvat sdliealdrt aswpidfyli ssppyvrpsq
      121 rgllahftal adraahpivl ynipyrsavg ldndtllqla ahpviaglkd ccanraqtqd
      181 liarrpagfg iltgedaqsf dalragadga illsahlete tfaailqhvr agrhdaaaac
      241 waqvegltrl lftepspapa kywlarigli asaqlrlpmv evgpelaarl dqeierrrpa
      301 tqgrva
//
LOCUS       WP_284420289             351 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sugar phosphate isomerase/epimerase family protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284420289
VERSION     WP_284420289.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..351
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39040
     Region          8..323
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mrmikgpgif laqfvadaap fnsfdsicgw aaslgyegvq iptwdgrlfd lhkasesqdy
       61 adeikgiaar hglaitelst hlqgqlvavh paydaafdgf aapevrgnps artswavdqv
      121 kraivasrrl gltahatfsg alawpyiypw pqrppglvea aldelarrwl pildhadeng
      181 vdlayeihpg edlhdgvsye mflqrvnnhr ranllydpsh fvlqqldyla yidiyherik
      241 afhvkdaefn ptgrqgvygg fqswvdragr frslgdgqvd fgaifskltq ydyaswavle
      301 wecaikhpeq gaqegaefik nhiirvteka fddfagsgtd dmanrkmlgl s
//
LOCUS       WP_284420381             133 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [unclassified Bradyrhizobium].
ACCESSION   WP_284420381
VERSION     WP_284420381.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..133
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14894
     Region          15..121
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mtaqstseta plrckpqhfs secpsrvlid qiadkwsmmv lavldsgplr fnaikkqleg
       61 vtqkaltqcl rrlernglva reviadspva vqyeitplgr tlqppfraly awtiakmpev
      121 eqarqafder rgr
//
LOCUS       WP_284420397             457 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: vWA domain-containing protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284420397
VERSION     WP_284420397.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466432
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..457
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=50679
     Region          3..452
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 mqenlhrffr aargagvhvs paesidamra vasvgfadrt vlrdsllltl aksedekkal
       61 gacfdlffah vdptqseahd eaqqdaaqna tegapqtaqn ageqtnaelg plaqmllaqn
      121 tadisaaian assavglsei ryftqrglfs srmleamgiq rlrddldala dsnpaqaerl
      181 qagldglrdt vrdavaqala lygreetenl rheilrnaql srieprqvae mralirqiar
      241 rlreryskpr krqrrghldv rrtlrrnaaw gsvpfltawk rrhrdrpriv alcdvsgsva
      301 rvsdffllli hslhdvvsdv rsfafsghli evseileqks aeeamaeimd kvgfgssdyg
      361 sslvdfekqf maavtpqttv ivlgdarsnk ldpradilka iserakrvvw lnpegrmtwg
      421 wgdsempryq tfcnvarpca taqqleravs divsayq
//
LOCUS       WP_284420426             452 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sigma-54-dependent transcriptional regulator
            [unclassified Bradyrhizobium].
ACCESSION   WP_284420426
VERSION     WP_284420426.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..452
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=49767
     Region          9..441
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mtheqpigvi yveddedvri gavqalqlag lavtpfgsve aaggivragm pfvvvsdvrl
       61 rgksgtewls elhrldpdlp vilvtghgdi smaveamrng aydfiekpcs seqlvsvvrr
      121 aldkrrltle vltlrsalad rqgieasllg rspqiqevrr lvanlastnv dvtiygetgt
      181 gkdvvarclh ahsvrrggny vavncgglpe slveselfgh eagaftgatk qrigkieyah
      241 ggtlfldeie smplsvqvkl lralqdrlie rvgsnkpvav dcrvvaaska nlyelserkq
      301 fradlyyrlg vafielpplr erredipilf ehftleaakr ferdapivde qtmslllsya
      361 wpgnvrelrn vadrfvlgvl drkvldrsga aaselslprq leniersiie dalrrklgdv
      421 qataallsip kqtlydkikr lavkvdsvke kh
//
LOCUS       WP_284420473             506 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: malonate--CoA ligase [unclassified Bradyrhizobium].
ACCESSION   WP_284420473
VERSION     WP_284420473.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Pohl,N.L., Hans,M., Lee,H.Y., Kim,Y.S., Cane,D.E. and Khosla,C.
  TITLE     Remarkably broad substrate tolerance of malonyl-CoA synthetase, an
            enzyme capable of intracellular synthesis of polyketide precursors
  JOURNAL   J Am Chem Soc 123 (24), 5822-5823 (2001)
   PUBMED   11403625
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11482749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..506
                     /product="malonate--CoA ligase"
                     /EC_number="6.2.1.76"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0090409 - malonyl-CoA synthetase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0090410 - malonate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54006
     Region          1..503
                     /region_name="PRK07514"
                     /note="malonyl-CoA synthase; Validated"
                     /db_xref="CDD:181011"
     Site            order(160,163..168,170..171)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341264"
     Site            order(163,203..204,207..209,249,251,255,277..279,298..303,
                     307,322,382,394,402,405,408,437,473)
                     /site_type="active"
                     /db_xref="CDD:341264"
     Site            order(163,277..279,298..303,322,382,394,402,408)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341264"
     Site            order(203..204,207..209,249,251,255,277,299,301..303,307,
                     405..407,437,473)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341264"
ORIGIN      
        1 mtwnlfdrll asastdpsic iekddgtkls yaelaalsgr fanflaglgi gpdhrvackv
       61 eksvealaly latlragavy lplntaytpa eseyfirdaq ptlivcdpke qaalraitdk
      121 aggrietldp ngkgsladaa aacasafatv prgkddlaai lytsgttgrs kgamlthgnl
      181 vsnaltlveq wrytsddvli halpiyhihg lfvagnvtfa ararmifmqk fdaeailaam
      241 aratvlmgvp tfyvrllqsp klspaatanm rlfvagsapl laethrawne rtgheilery
      301 gmtetgmits npfegpripg svgrplpgve lriadpetga llgtdevgmi evkgpnvftg
      361 ywqmpektas efrpdgffit gdlgkispeg tvqivgrgkd liisggfnvy pkeieteida
      421 ipgvaesavv gvphadfgeg vtaavvrtpg aavderaila alsgrlakfk qpkrvifvdd
      481 lprntmgkvq knllrerfad lyaakg
//
LOCUS       WP_284420511             377 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: PepSY-associated TM helix domain-containing protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284420511
VERSION     WP_284420511.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..377
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=41204
     Region          1..374
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mrlwvqvhtw tslismvfll mlcltglpli fhqeidhyle deisapemps gtpllpldrl
       61 iasaqqrlpe qhvlfvapke aesiavvtms ptaipvpgqf hrltvdartg avlgeegphq
      121 dvmdvilrih rdmftglpge lflglmglvf aasiisgvvi ywpfmkrlqf gtvrnrsarl
      181 rwldlhnllg ivtvswalav gltgtintla vplfdlwraq tmpallaayq gkplaeaksv
      241 ggavdavraa fpdrlvafvt mpttarfgsp qhlivwtkgg tpftarmfqp vlvdandsak
      301 mvapgvswyl ralqvsrplh fgdygglplk iiwalldvit iivlssglyl wvakrwgskr
      361 rlatsaaatv apvtvsp
//
LOCUS       WP_284420682             183 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces albus].
ACCESSION   WP_284420682
VERSION     WP_284420682.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albus
  ORGANISM  Streptomyces albus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Streptomyces albus"
                     /db_xref="taxon:1888"
     Protein         1..183
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19260
     Region          12..>83
                     /region_name="AF2118"
                     /note="Predicted transcriptional regulator, contains an
                     XRE-type HTH domain (archaeal members contain CBS pair)
                     [Transcription]; COG3620"
                     /db_xref="CDD:442838"
ORIGIN      
        1 mdaaaqdpta karqlqsqwy geplgtlfrr liddlglnqa rlatvlglsa pmlsqlmsgq
       61 rakignpavv qrvqalqala aevargdvsa adatsrmeei rrtaggsvlg ntsqtassgt
      121 sqtpvkrvvr eiqallrsvs daadiidasn alapthpela eflrvygagr tsdavkhyea
      181 hqs
//
LOCUS       WP_284420898             502 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: pyridoxal phosphate-dependent decarboxylase family
            protein [unclassified Bradyrhizobium].
ACCESSION   WP_284420898
VERSION     WP_284420898.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 502)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..502
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=53710
     Region          24..484
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mtadlrsdss lqpaetldpq dwgevraqgh rmlddmfdyv agirdrpvwq pmsqdtrqrf
       61 rselphaptd laevyrdfse lvvphatgnv hpgfmgwvhg ggtvvgmlae mlaaglnanl
      121 ggrdhapiev erqvvdwtrq lfgfphgasg ifvtgtsman lmavlvarra algasvrsag
      181 lgdagrqlra ytskaahgci akamdicglg sdalrsvavd aahridiaal raavtadraa
      241 glhpflvvas agtvdigaid dlaavaalcr teglwfhvdg afgalamlsp elapklagia
      301 qadsialdfh kwgqvpydag fllvrdgerh rdafaspaay lrretrglaa gtewpcdlgp
      361 dlsrgfralk twftlrtfgt drlgrmiars celarhleaa vraepelell apvnlnivcf
      421 ryrcedadai ngaivadihe agiaapsttm ldgrlairaa ivnhrtetdd vdrmmaavlm
      481 fgrrraagla plidveappl ap
//
LOCUS       WP_284420914             155 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [unclassified Bradyrhizobium].
ACCESSION   WP_284420914
VERSION     WP_284420914.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..155
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17303
     Region          15..146
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mtetarrdqt prledfpyrl tdnvrfgdld pnqhvnnavy atyfetgrvt lmkdpryglt
       61 qpglawimvr ldmhfraelr wpgtielglg vvklgrtsvt ceqvvfsdgr cvasatavmv
      121 lidevtrkpa plppqlieal qpwvrrgvti vppaa
//
LOCUS       WP_284420920             377 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified
            Bradyrhizobium].
ACCESSION   WP_284420920
VERSION     WP_284420920.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 377)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20324114
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..377
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39955
     Region          4..95
                     /region_name="MlaB"
                     /note="Binding protein subunit MlaB of the ABC-type
                     intermembrane phospholipid transporter Mla, contains STAS
                     domain [Cell wall/membrane/envelope biogenesis]; COG3113"
                     /db_xref="CDD:442347"
     Region          131..372
                     /region_name="MlaE"
                     /note="Permease subunit MlaE of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG0767"
                     /db_xref="CDD:440530"
ORIGIN      
        1 mtgspdlqrs gegnalslra tgawtarfap slerlvadae klagktkdvs idvsqvskld
       61 tfgawlierl rrsfttatve aridglsany aslvdevrrv smapdgdatt vtitgmlgqi
      121 glsvagilgt vaalidmlga vivasgrvli hprsfrltst ihhleqvcwr avpivvlitf
      181 ligciiaqqg ifhfrrfgad ifvvdmlgvl vlreigvllv aimiagrsgs aytaelgsmk
      241 mreeidalrt mgfdpievli lprmlalvia lpilaflgdi aalyggglva wfyggvdpea
      301 fllrlrdais idhftvgllk apvmaavigi vacveglavq gsaeslgrht tssvvkgiff
      361 vivmdgvfai ffaavgm
//
LOCUS       WP_284420971              81 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: Lrp/AsnC ligand binding domain-containing protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284420971
VERSION     WP_284420971.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10470669
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..81
                     /product="Lrp/AsnC ligand binding domain-containing
                     protein"
                     /calculated_mol_wt=8813
     Region          6..77
                     /region_name="AsnC_trans_reg"
                     /note="Lrp/AsnC ligand binding domain; pfam01037"
                     /db_xref="CDD:426007"
ORIGIN      
        1 mvpffvqikc klgqsyvvan alaeaeiase iystagnfdl lvkfyvdkdt dighfvnekv
       61 qvlpgiqdth tiitfkafsa s
//
LOCUS       WP_284421050              93 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284421050
VERSION     WP_284421050.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10475648
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..93
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9981
     Region          26..69
                     /region_name="HTH_3"
                     /note="Helix-turn-helix; pfam01381"
                     /db_xref="CDD:460181"
ORIGIN      
        1 msdrklssrs arvvaageal agerwqsala rasgvkqqll amiasgerep tddvyrkvaa
       61 glkkeavrla rtsgrvhdma drmlselgel eed
//
LOCUS       WP_284421167             785 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit [unclassified
            Bradyrhizobium].
ACCESSION   WP_284421167
VERSION     WP_284421167.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 785)
  AUTHORS   Sandhu,P. and Akhter,Y.
  TITLE     Evolution of structural fitness and multifunctional aspects of
            mycobacterial RND family transporters
  JOURNAL   Arch Microbiol 200 (1), 19-31 (2018)
   PUBMED   28951954
REFERENCE   2  (residues 1 to 785)
  AUTHORS   Hand,N.J., Klein,R., Laskewitz,A. and Pohlschroder,M.
  TITLE     Archaeal and bacterial SecD and SecF homologs exhibit striking
            structural and functional conservation
  JOURNAL   J Bacteriol 188 (4), 1251-1259 (2006)
   PUBMED   16452406
REFERENCE   3  (residues 1 to 785)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
REFERENCE   4  (residues 1 to 785)
  AUTHORS   Arkowitz,R.A. and Wickner,W.
  TITLE     SecD and SecF are required for the proton electrochemical gradient
            stimulation of preprotein translocation
  JOURNAL   EMBO J 13 (4), 954-963 (1994)
   PUBMED   8112309
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..785
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..785
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84674
     Region          27..773
                     /region_name="MMPL"
                     /note="Predicted exporter protein, RND superfamily
                     [General function prediction only]; COG1033"
                     /db_xref="CDD:440656"
ORIGIN      
        1 mlevrhdnev hvekaeqrpa dsiafgierl glfavkvpil scvvllvliv aavfgikriq
       61 iddslsqlfr sdskefqqye avtkkfpaee fdvlvvvegk tllarpnlek lrdfvtdlql
      121 vegtrglvsl fsarqapapg klpaalfpsd lpegeaydkf ietvksneii rgkllsedgt
      181 lalivlslep kvvasndlgk vvgeirklmt ddlagtdlav qlsgvpvmql eirnavardg
      241 ltynvlgila gciiaiiffr kvsfmiaaaf ppliaillal galgwanfnl nmflnvmtpl
      301 imvisfsdsm qltfaardrl iagqdkftaf knavlvvgpa cvlthatagi sfialqfsds
      361 dlirkfgeag laatiialia vlslvpvfgv llvrnektfa vkfqggdagv qalrnfcywi
      421 avrmvgrpgl fsliavlfvg glavvystle pryrladqvp dkqqavaasn rldakltgan
      481 pvnvliqfpk gaslyapetl qtiadvhatv ektagvgnvw svetlrrwla ekagssdtat
      541 lqeyvslipe hlvrrfidke qdavvvagrv pdldssqllp vvdkldreld tvrkkhpgye
      601 vavtglaaia arnsasmiqk lnhgltiefa lvamfiglaf rswvvmlaci lpgifpvvms
      661 gtllwamgeg lqfasvvalt vsfglglsat ihflnrlrme sapgvsaava veratvlvgp
      721 alilttvvla cglvvtvfsd lpslrlfgwl safsmvaalf adlfilrpta mflinlsqkl
      781 krkpv
//
LOCUS       WP_284421287             343 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD-dependent epimerase/dehydratase family protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284421287
VERSION     WP_284421287.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..343
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=37259
     Region          2..322
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkalvtgang flgrhvvnal largievram vrpatrvdal gwpasvdivr adlrssrdlv
       61 gafagvdvli hlaavvsgge daqfagtvag terlleamsg sacrrlvlcs sfsvydytaa
      121 rgvldetspl qqtpdvytrg gytvakwwqe rvtrryveqh gwdltvlrpg fiwgrgnsyl
      181 aalgqqigrh hvvigpltrv pmthvencad vfalaaadsr aigqtlnivd gpgecvwtyl
      241 sdymrgtgar gwrlpiphwl astvvrlafv tvfrratkvp ailtpkkfda mlkplrfdnr
      301 klrdtlgwtp pldyqqclar tygpvtapte apaswssgta asi
//
LOCUS       WP_284421357             312 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: TauD/TfdA dioxygenase family protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284421357
VERSION     WP_284421357.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..312
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35273
     Region          26..301
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 msfyrdfndk laiqawngar repyhtievr qigptagaei ggvdlskevs deqfaeirra
       61 ldenlaivfr dqdiskddhk rfarrfgksl hrhelaasrf rhdgpfdpef lswktdansr
      121 ftagdgwhpd vscdpspiav sllrvtrtpp lggdtafanm ylayeflsdp ikqlldglta
      181 ihdgslawta gygakpdpgk typqsehpvv vthprtgrkf lyvnasftsh ivqltrresd
      241 allqllfrhv egqlalqtrv qwrpnsllvw dnwasqhhav wdyypeerwg ervsvvtgei
      301 pqarlglsea ae
//
LOCUS       WP_284421374             315 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: TauD/TfdA dioxygenase family protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284421374
VERSION     WP_284421374.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..315
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34628
     Region          21..293
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 masvhsvsss tppsrsipss dvvrlsarig aeirnvrlsg dlpndlvkei ndlllqhrvv
       61 ffrgqdhldd agqerfakrl gdlvphptvg aikgtasile ldsargggra dswhtdvtfv
      121 daypraavlr gvvipefggd tiwsntaaay qdlpaplqrl adelwavhsn aydyaatrsr
      181 atdadrkhfd evftgtvyet ehpvvrvhpe tgertlllgh fvqrfagirk adgqklfdlf
      241 qsyitapent vrwrwktgdi aiwdnratqh iavndygdqh rivrratidg dvpvgvdgrt
      301 svtrvkapka vgraa
//
LOCUS       WP_284421438            1271 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: AfsR/SARP family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_284421438
VERSION     WP_284421438.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 1271)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 1271)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   3  (residues 1 to 1271)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 1271)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1271
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..1271
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=132342
     Region          7..247
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          <238..379
                     /region_name="PHA03378"
                     /note="EBNA-3B; Provisional"
                     /db_xref="CDD:223065"
     Region          365..1218
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          1021..1049
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(1022,1025..1026,1029..1030,1032,1062,1065..1066,
                     1069..1070,1072..1073,1104,1107..1108,1111..1112,1115)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          1060..1093
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1098..1127
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mgvrylyrvl gttqalradg tavplggarl ravltalala gggavrtgql aaavwaedee
       61 aptdetaavq alvgrlrral grdavesvtg gyrlaasrdd idlfrferla aegaaaladg
      121 dpakaadlld dalalwrgpa ladlpdgggp agiraadrav aarrdraraa lalgraeeil
      181 pavrelaaah pldeplqall iralretgrt aealavyeqv rsriadrlga dpgtelrtlh
      241 aelltgdpap apsggpapap sgssfpaspg gpatapsgss fpapsggpat apsggpfpep
      301 pagptsgpsg dpaaappggp asappggrsq glpggpapas pggpapapsv gpspassdgp
      361 vpaspggpap vrsvddapas vpagaaggrg appyaagagr vpagarrpgn lrsmltsfvg
      421 rddelraige elsasrlvtl tgpggagktr lsleaaalat ergatwsdgv wvaelagvrg
      481 qnaqretaea vltalggret vltgsaaegl vaatdptagd plaqlaehca grrillvldn
      541 cehvidaaar vaetllmecp gvtvlatsre plgvpgesvr pveplpdpva lrlladrgaa
      601 arpgfrteed peacaeicrr ldglplaiel aaarlrsltp rqlasrldrr frlltsgsrt
      661 vlprqqtlra vvdwswelld gperavlrrl avfaggcele qveevcadlf peaadagghd
      721 gtggsaaavl gslvdkslvv avpnragagt gmryrlletv aeyaagkldg epgereraer
      781 rhlvayrela rtadpllrgp qqaawldrle sehdnirtal rrafaardeq emlclvlsmg
      841 wfwqlrghrs dasawaeatv tlgpdpfasp lrparpvhep ctaapppmtg evlwearrgv
      901 rlmvladaed gidlvrrpar qaelrnvtra ytpgmpqvcr lpgcmwlfaw mltgdfaalk
      961 elcdaqvrac relgyewela falqlrskll sdrpggwdqs gedaaeslei frragdawge
     1021 aealsgraea laargefaea atdyrmaier aaqlgahsqv pqlksrlgav lvelddpaqa
     1081 aegdrlmrea teeseglpgd gpnfaavqla vhlvrrgepa raqelleple arfedkspql
     1141 fagmvqgima wghlvagrpa dalaklrvsi vrtrevlada vtphltlsql ltaagalagl
     1201 grgreagrll gaydglaavp egrfphpler earqsaekav rellsereya dahaegdgls
     1261 ieeavalvrn a
//
LOCUS       WP_284421601             441 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase family protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284421601
VERSION     WP_284421601.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..441
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=47712
     Region          <185..346
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 msrlaapfsp gaslpriayl esirglaaiq vlllhllsaf lpelvassps smiaatihas
       61 plsflydgys avyvffclsg yvltrsferk gcspalqila ravrlglpal aatvfaaalm
      121 lmfgranaea grilgsawls gqwdvdlsvl silrdgtlna lllgyrdlpa gtllapwqte
      181 lshsfvvpfw tlsiefqgsi lilflcwcar rswwlwlavm iagtlftirs ahvcffvghl
      241 lasahyaerp pshrrltata lvvaglhccv ladvwqpgwl irlcssetqw llagqfapmq
      301 qkaygamlil agvmdlrswr tvlarpmlva lskfsfplyl vhwpimcgpa saafvaltaf
      361 vdtrlaqlca iavgiaasaa asvvfltidr yavrlssrfr rspvvrpasi lrahiagpfp
      421 vpaealatas dqaeryshsp g
//
LOCUS       WP_284421736             324 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)H-dependent flavin oxidoreductase [unclassified
            Bradyrhizobium].
ACCESSION   WP_284421736
VERSION     WP_284421736.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..324
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=34789
     Region          9..316
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mktaitemfg iehpiiqggm hyvgfaelaa avsnagglgv itgltqrtpe llakeiarcr
       61 dmtdkpfgvn ltflptfsap pypeyiaair eggikvveta grspeqympa lkaagikvih
      121 kctsvrhslk aeqigcdavs vdgfecgghp geddipnmil lpraaeelki pfvasggmad
      181 arslvaalam gaagmnmgtr fiatkeapvh envknalvna seldtrlvmr glrntervlr
      241 nkgveqllei erekgkqlki edihdqvagv ypkvmidgdm dagawscgmv aglihdvptv
      301 kelidrimld aeriirerli gvla
//
LOCUS       WP_284421747             142 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: tautomerase family protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284421747
VERSION     WP_284421747.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..142
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=15082
     Region          2..60
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mplitvtyas qrrspslkkd iaetitalta rilgkdpkvt avivseadaa dwfaggasla
       61 eqglasywid vhvtegtntk dekaaylaav faamaellgl lhhetylhvd evradaygfg
      121 glsqerryva arlgvppqpd aa
//
LOCUS       WP_284421799             309 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: CobW family GTP-binding protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284421799
VERSION     WP_284421799.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..309
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33049
     Region          1..309
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mivpvllvag algagkttll nhllanpdgr riaavvndfg avdidaqllg kvteevislk
       61 ngciccslqg dllrtlssvi krdpapdaia ietsgisdpa eiirnlmdpv ifkvapletv
      121 vtlvdpqrlq ddpdiaqdal wrsqlraadf vlltksdlld raaldrarai igqtkpqsai
      181 feiargivap dllfsrdlra prelprqmpt msepfatvtw tshaplslvr fqqvigqlap
      241 rtlrikgvlq fsehpgmpil fqsvatrgtl apspvppadg ltaqlvligr egeldaadid
      301 allrgvivs
//
LOCUS       WP_284421834             225 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284421834
VERSION     WP_284421834.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18527488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..225
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=24326
     Region          36..109
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          122..222
                     /region_name="COG3837"
                     /note="Uncharacterized conserved protein, cupin
                     superfamily [Function unknown]"
                     /db_xref="CDD:443048"
ORIGIN      
        1 makgaakhpk kdgkaeapra epelltgsla preasptles eigaevrrlr kdldltvael
       61 gvaagisagm lskiengsis pslatlsala kalnvpiarl frengeerdc sfvkggqgvr
      121 ierrgtkagh lydllgyslg gdvvvepyli tlkgnavpyt dfrhagvefi ymlsgkvryr
      181 hadrlyllep gdalffdaaa rhgpeelika pmtylsviiy prrnr
//
LOCUS       WP_284421862             959 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ATP-binding protein [unclassified Bradyrhizobium].
ACCESSION   WP_284421862
VERSION     WP_284421862.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 959)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..959
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=103800
     Region          13..918
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mpdndtqdsa isfgpfrllp ksrllekdga plhiggrald ilivlaqrpg evvdkrelvq
       61 riwadvhvde gslrfhiaal rkvlgdagks aryvvnvpgr gycfaaplaq avpsvapapv
      121 eaaapraplp pslakmigre dvvekissgl sqhrfitvvg pggigktava vtvahrrsad
      181 fagqvvfidl gplrdprlaa taiasavgla vnaddplpal lahlqdkrtl lifdscehvl
      241 etlaplaerl vrdlpmlhvl atsresfrse gerifrlfpl dcppqrddlg vaeilaypaa
      301 qlfveriaqg sgpfelsaed apfvadicrr ldgialaiel aagrvnaygi agtaslldsr
      361 fslqwrgrrt aiprhqtlsa aldwsydllp apestvlrrl svfvgpfspe aaaavasgdg
      421 lsaaetseai dnlvtksliv psgartlryr lldttrtyal gklglsgeqr rlaqrhaeyf
      481 rdvldraete tsaplhawls tyggkldnvr aaldwafsad gdaalgialt aaavtlwvrl
      541 slfaecrert rtalavlgdn adgvdrlrmq llgalgwslm ygegrarear pileatlela
      601 drlddkdfrl ralwglcidq fnngefgkar aladrfttia asspdntdlm ladrlmaval
      661 hylgdqaear iridrvnasl hmltekpkif pldlgvstqy frarilwlqg qadqalelaa
      721 rnieegrang haltfcsvlg qsacllaffa gdydaaqrhg aellghadrh airlwglwar
      781 afnamivarr gdsaaglpll reeldragda rvlprflpll gelaacfgea gqvdrglaai
      841 edvlkrcder qerwylpeli rikgelmlkd aeqstgaeac freamaiaae qgarfwelrc
      901 aislarlgmi qgrnaeaaev letvcgrlte gadtadirma rglitqlrar aaaasspgg
//
LOCUS       WP_284421904             955 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ATP-binding protein [unclassified Bradyrhizobium].
ACCESSION   WP_284421904
VERSION     WP_284421904.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 955)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..955
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..955
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=104140
     Region          5..915
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Site            order(578..579,582,606,612..613,616..617,622..623,652,
                     655..656,659..660,663)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          604..644
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          651..679
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mipqdplsqg devsfgsfvv rvserslrkg atpvhlppra ldillvllqq agsvvdkhdl
       61 marvwpdvtv dagslrfhig vlrkvlgdge agarfvatvp gkgysfvcpv syrmsaeadd
      121 rsravetnyg lpprlsrmig rddvvekvcg mllkdrfvti vgpggigktt vaiaaahqtn
      181 pqvasavaff dlgplndpml vptavastlg lmvqsddptp aiisfihdks mllildsceh
      241 vitsaaalae hifqhapkvr ilatsrealr vegeyvfqlp slenppldvq tvsdvlafpa
      301 arlfmdrvla sgssfelnda dapivgeicr rldgialaie iaasrviafg vkgtaalldd
      361 rfrllgqgrr talqrhqtlt aaldwsygll sdneslvlrr savfvgffsm raviavvgpd
      421 dlseelafea vaslvdksli avasgtsear yrlldttray alsklidrdd dngvfqrham
      481 fylrwaeqhe svrlteagrd gasaydphlg niraalewsf lqteksigis ltaataplll
      541 esslvtecrr wtelamvnld essrgtsrev tlqaalglsl mfsqgnseea raslerglev
      601 aedledlpsq lqligrlhlf hyrtgnfrea lkyaerseav alkmndqgal aaassllgvs
      661 hhlmedleka rgylesavrh ipaskhvdsl rlgldyrnra giclartlwl lgyadratel
      721 arqvsieagk lnhpltlcia liwavsvylw ngdwenaeqs ierlidharn raivayeaag
      781 igvrgylavm rgdhqaglpm lryalietra hryelmttaf ksalaegllm agqarealda
      841 addalatvar ngdmfnaael lrikghvfla etmkdmprae glfiqsleaa ktcgarawel
      901 rtatslaslw rsqgrfvssv ellenvlesr tegfgcpdfi narkllsdca rrvap
//
LOCUS       WP_284422000             294 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: metallophosphoesterase family protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284422000
VERSION     WP_284422000.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..294
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32186
     Region          4..267
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 maaftlahls dphlapqsrp rlselagkra lgylnwtrnr ykyhrsdild llvsdlhtqm
       61 pdqiavtgdl vnfalesefp laqawlrtvg ppdkvtaipg nhdayvrstr lrfaesfady
      121 fggdaagpat fpslrrrgpl alislssavp sapflatgrl gsaqlaalaq llesiahepl
      181 frvllvhhpl rsanrmkrlt dgkalialla rhgvelvlhg hdhvhstiwi dgperkipiv
      241 gvpsasslah ghtpaaayni favardgnhw rcdmtvrgvn ealrvreirq irli
//
LOCUS       WP_284422065             104 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [unclassified
            Bradyrhizobium].
ACCESSION   WP_284422065
VERSION     WP_284422065.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 104)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 104)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..104
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11710
     Region          4..85
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 miesdifkal adptryvife klaagrmnas alrdgmaisq pamsqhlavl rnaglvreer
       61 qgrfvnyevd pkglaliarw ltkyraywps rvdalktllk dmdq
//
LOCUS       WP_284422117             791 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284422117
VERSION     WP_284422117.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..791
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=89149
     Region          680..772
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
ORIGIN      
        1 mvyariftlq iflqtlfvvt gevkssyayv idgmtlgekl passyakrfs ecsdsrdfdg
       61 yqwckriqpr ptslgrgqat tqilrskdgt ltylmttvap vslsksivqa eidelsrenk
      121 eqpikldwyq trdgitavig vwgklelari hkddigrtda lidpledpdk stdqglpifr
      181 vageagyvyc asfdasgrgh rhyvaanmaq aaittfvptl eeavrddqtr saddfslwik
      241 vaqdsrriav aaspavanre ldkifqryrq kklqsrvwal lplgvsetlg qkihwtevny
      301 gpntlypeir erileflaan pkgrfsefly ytigefekgl avnpssvikt elryamgyaa
      361 lrpllegvvk rlndpeihla dgdsiesvis llnhearyrs trlsavdpef vsraavakpl
      421 felvlndess rladdaaymi gwlafhqnkm qealgyaara mnvgngdyss aatrlvlrif
      481 erytpqqqva aleeipalsq qpaiwykvar dayrrfdyty vidvaeralr ylqapsdqlp
      541 attdpiliaq alkkikhkya ddpnfveipy vlqasreive lstsiksiad srpdaankiv
      601 rmavikysrl tdatddvasr krmaplahrd lrqalhlidi slaqlpkktq ldslrewlly
      661 rkvrilvsfd prkvptsvvd lsnefpgssl lddamaeqly segvrlknve aaertfqalv
      721 dkfpranaid naytwmaiiy hcanrapeeh rmnfeiirrf pttrhalyaa kreavggsvs
      781 csvwsddden l
//
LOCUS       WP_284422142             375 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Bradyrhizobium].
ACCESSION   WP_284422142
VERSION     WP_284422142.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..375
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40954
     Region          184..370
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mesehyaqal daiyqglaep sgitdalesi rtligaegat fevidtaarr plifhssgva
       61 saegddylah faprnprlpv alrqqrggls wdyqvmdegt mkrdpfyaef lpraglryfl
      121 slvldqspqr lvavtlqrsp rrghvgtsei almkrltphl qraygmrnsl iaaggrdiat
      181 avldllkdgi alldpkgail hanpalhtia tesglfrlds rgiqfgssel rsryarvfst
      241 vmrddalads daaldflapr psglpactis lralrhprpa sdcpdaavmm lvhdplrdsa
      301 aahllqdlhg ltraeaqlac alsagmtave yaahrgvkvt tvythlkrtr ektgwrsvae
      361 ltrrvhqisi rlres
//
LOCUS       WP_284422216             443 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [unclassified
            Bradyrhizobium].
ACCESSION   WP_284422216
VERSION     WP_284422216.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..443
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=49631
     Region          9..409
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 makaasqltl tdalirtasl ppgkaqhylh ddklpglalr mratgartwv ylftkpgvrg
       61 tqrktlgpwp kfnekaarka atiaagevir gvdpnddkre arrlqaaekq rttlatlive
      121 dgayetsltg rqvvnwrpam salrrglkdh vedsaadltr rnimaavdki aktgkrgaak
      181 dfrkhvhtfl ewcvgegyve hnvlagyrap ketraqrvgr rmkgraltda eivkvwqacg
      241 klgtfglltr mcllggarrs eptmiewkrh vmqdritfdg awtkmglhhd vprthlidev
      301 laaakhfqra tsdyvfpspk tggqmsgftk mvkrlvkeae vdkftmhdlr rslrtimsrc
      361 gydneiqrlc vgqkpggidq vynhdeqwii rkmafeaahd yiaelvgaer tgkvvrlqrt
      421 npldpiktel lgrlrehfaa ggv
//
LOCUS       WP_284422219             450 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein [Streptomyces albus].
ACCESSION   WP_284422219
VERSION     WP_284422219.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albus
  ORGANISM  Streptomyces albus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Streptomyces albus"
                     /db_xref="taxon:1888"
     Protein         1..450
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47891
     Region          14..346
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mgsttggerr gavdgripvv vlagflgsgk ttllnhllrr argtrigavv ndfgsieida
       61 mavsgqvdsm vslgngclcc avdtsdmdev ldvlarpaag mdvivieasg vaepetlirm
      121 vlasnsphiv ygglvevvda aefdavrerh pelerhvgaa dllvlnkadr vtaerrdalh
      181 telerlapgr pvvpasfgri dpellfdrvh rprppveqls fdvllygdde ecdgsgaedg
      241 sghqqhlhaa yeavefaadr pmdprrfldf ldgrpeglyr mkgyvdfgaa dpdnvyemha
      301 vggflrfapq rrapseqrrt elvmigagid gealrtglta caadpddapd eralwgvlry
      361 vdhrsdeeet agtpdtsadg dgwngdgrcp gevseyddwd gipygegppt vaadgeeppt
      421 vaasgegnlt ttvshgqaps paaehvpase
//
LOCUS       WP_284422360             358 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Streptomyces albus].
ACCESSION   WP_284422360
VERSION     WP_284422360.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albus
  ORGANISM  Streptomyces albus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Streptomyces albus"
                     /db_xref="taxon:1888"
     Protein         1..358
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39958
     Region          52..355
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mpgedqsgvk trkepvtgpv tqktvpwrsl plgdklafta avllpprftp ervrydrryr
       61 tldkyrfivg flilplvfya vfvispffqa iyysftdwag gatanfvggd nyvkmwndek
      121 fwdslrssll llvvvplitl algiflaymi taggrhrrge aisgvfgssf ykvvyffpqv
      181 lsialiavvw qqvyssrsgl lngalgavgl dgleqrwlgg dyklalfstm aviawsfvgf
      241 yvvlfsaamg aipkdiyeaa lldgagrttt ffrvtlpliw dtvrtgwiym giqaldafav
      301 vlimvpkhal kvtpvylyer frdgqfgyat aigvvllals mvftlvvmri grrdriey
//
LOCUS       WP_284422460             352 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FAD binding domain-containing protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284422460
VERSION     WP_284422460.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..352
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=36615
     Region          1..329
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mnrfdyvkps tvaeaiaaas apgatylaag tnlldlmkgn vvrparlvdi tqlteltrie
       61 tsgngdvrig alvrnadlah esgfardfpa vaeallsgas aqlrnaatag gnllqrtrca
      121 yfydaasacn krtpgagcda rggdshqhav lgwseaciat npsdfcvpla afdavveieg
      181 vsgrrevale alhllpgttp eretvlapge mivairlpaa arafarhary lkvrernsya
      241 favvsaaagl viengtikqa rvalggvaar pwrardaeal lagrpaepdv lqqaaeaalr
      301 eakpsgdnah kiplarsliv ralqaaaqgt psrmpalpas pfssipgvlh da
//
LOCUS       WP_284422475             328 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase family protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284422475
VERSION     WP_284422475.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..328
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34718
     Region          10..328
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mssvmngcrv latlvvclsa tlaqaaglrs idipadaegp aihgmvwypc aekpaeipig
       61 afiltgamdc plagthlplv vashgrggsl fssrdtaevl adhgfvvaai nhpgdtardl
      121 srsgdlsvfv erptdirrli dvmigsspfa ahidrdrigf fgfsrggytg lvllgadpdw
      181 agaasdycqp irrlfcqeil dkrtpsqplt hdprikaavl adplaiffsp aslapikvpv
      241 qlwassrggd gvlpshvafv danlpaghdy rvvpnsghfa fflcppalvq aqselcadap
      301 gfdraafhte fnaevlaffr arlarpae
//
LOCUS       WP_284422519             347 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            albus].
ACCESSION   WP_284422519
VERSION     WP_284422519.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albus
  ORGANISM  Streptomyces albus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces albus"
                     /db_xref="taxon:1888"
     Protein         1..347
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38322
     Region          60..344
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mrsahsehpe ldrklrrrgf lgvaagataa allspgtata apgpatgqah ghrpivphgk
       61 lgiqlytvrd qiqklgfapv fralerygyd svefagytqg tgeitlrglk rlmrdhglrg
      121 igshvgywst dpaaytfatq lekvvddaaa lglphvgtaa spdrygrtvd awkraaedfn
      181 tygaaararg lkfyqhnhqm efgfaedkph irlydvllae tdpelvhlem diywayagqh
      241 rfsvrpdgtp apfdpldyvl ahphryplfh vkdgehdeas pdgyhmvdvg dgdidyehfv
      301 htvlrrhrgr aghhwlmerd davdpaanpa gsltsarrsa aylrgkr
//
LOCUS       WP_284422698             378 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [unclassified
            Bradyrhizobium].
ACCESSION   WP_284422698
VERSION     WP_284422698.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..378
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40524
     Region          2..365
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mkdydvaivg ggllgsaiaw glgrlgqrva vldegdiakr asranfalvw vqskglgmpa
       61 ytgwtvrgsk awpklaeelk aqtgldvvlq qnggfhltlg eaeyeqrsql varmhnqtga
      121 adyrmemmpa advkkmlpli gpevsggsfc pydghvnslr tfralhagmk afgvdylper
      181 avsaivrdgn efrlataqge iraakvvlaa gnanatlapm vglsapmgpt rgqivvtert
      241 mpflphpltt irqtdegtvm igdskedeld drvqnhpina vmsdraqrtf phlarlnvvr
      301 swtgirvmpk dgfpiyeqse thsgafvacc hsgvtlaanh afeiarmvkd galdtelvga
      361 ftakrfetaa gaggsgyy
//
LOCUS       WP_284422713             408 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified
            Bradyrhizobium].
ACCESSION   WP_284422713
VERSION     WP_284422713.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 408)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..408
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43509
     Region          23..254
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          163..408
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnrwipfewi aavrflregr lqtlfiivgi aigvavivfm samlaglean fikrvltsqp
       61 qiqlltpdqv arplrngngv iedaivqrps qrvisidqwp kirdqmlamp evaavsptis
      121 gsalairgda sravtlsgie pesyftivkv pdyivagepr ltsetiiigt elardlgavv
      181 gdklnvqaas ganrvltvag lvdlgnkgvn qraayvalrt aqsllgmvgg vttiditvhd
      241 iyaaediaqr iqaanlvkad swiktnsqff tavraqetsn tlirvfvgls vafgiaavli
      301 vsviqrskei gilramgtsr grilrvfllq ggmlgfigsl fgaalgagal mywhavqrqa
      361 dgselfplil errlfvital latvtgllaa tapalraakl dpvvairg
//
LOCUS       WP_284422936              89 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: BolA family protein [unclassified Bradyrhizobium].
ACCESSION   WP_284422936
VERSION     WP_284422936.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..89
                     /product="BolA family protein"
                     /calculated_mol_wt=9645
     Region          1..89
                     /region_name="BolA"
                     /note="DNA-binding global transcriptional regulator BolA,
                     affects cell shape, cell division and biofilm formation
                     [Transcription, Signal transduction mechanisms]; COG0271"
                     /db_xref="CDD:440041"
ORIGIN      
        1 mrtrdaiiek lreaftpesl dvqdeshlhe ghmghqpsge thfrvyivsq afsgksrvdr
       61 hrlinaalaa elagsvhala lhakapgea
//
LOCUS       WP_284422989             297 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: polysaccharide deacetylase family protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284422989
VERSION     WP_284422989.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..297
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33057
     Region          33..287
                     /region_name="CE4_HpPgdA_like"
                     /note="Catalytic domain of Helicobacter pylori
                     peptidoglycan deacetylase (HpPgdA) and similar proteins;
                     cd10938"
                     /db_xref="CDD:200563"
     Site            order(39,41,114,118,248)
                     /site_type="active"
                     /db_xref="CDD:200563"
     Site            order(47..48,57..58,60..62,64..65,69,73,92,95..97,
                     116..117,119..120,123..124,127,130..131,134,154..155,157,
                     175..181,200..202,207..209,211..213,227..228,231..232,235,
                     254..256,258..259,262)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:200563"
ORIGIN      
        1 mpdskalagi plipsntapp apdypwpapy kaamflsfdi daesawtskd pahaarlvtm
       61 sfggfearvg tpkllellad ldlkatffit gwavdahpam aeavlkaghe ighhgyhhll
      121 pdpgdpfiie eiergfetlq rrlgvrpigy rapfgefcee lrvalvrqgi vytssfrddv
      181 rpyrhrladg kpgtieipvt asyddwmhgl sarfsprsif prehvlsmwk deldevrdwg
      241 amvttvlhpq vsgrpmrfrl lrefltyaks cqdvwittga eiaanyqhhe aaeakga
//
LOCUS       WP_284423049             266 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FAD binding domain-containing protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284423049
VERSION     WP_284423049.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..266
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=27603
     Region          1..265
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 myettyhras svdeaaalfa kgseakflag ghtllpvmkq rlagpsdvid igkikdligv
       61 qlsgdtlvik aattyydimt ntdvkkaipa isyltsvlgd pavrhrgtig gsianndpaa
      121 dfpaalislg atvktnkrsi aaedffkglf ttaledgeii tevafpvpek agyakmrhpa
      181 srfaltgvfv tktksgdvrv aatgasqsgv mrvsaieaal ksnwsasaid gvtvsaagll
      241 sdihgssdyr anlvkvmaqr avqaag
//
LOCUS       WP_284423107             411 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284423107
VERSION     WP_284423107.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..411
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44223
     Region          37..411
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtpptaapsm pfgalrslsp plpddrpeal glsavrlqra sdafkrevdk gtlpgatllv
       61 grrgrigwfd aigrqapdad tpmrpdsifr ifsmtkpivs lgimmlaedg dlllsdpvak
      121 fipefadqkv gidnggtlel vplaqpmtvq dllrhtsgla yehtgtgpvh llyqqsrvrs
      181 rkitnaehas ivaglplicq pgaefnysrs tdilgriiev vsgqslgafl sarilnplgm
      241 netgfftsea nahrlaepfa kdpwtgeavn lfkmteqplm esgggglvat tmdyarfcam
      301 llnhgsldgt rlvgrktlel masdhlgppv ktmgtllspg hgfglgfavr reagiapfpg
      361 spgtffwsgi agtffwidpk eelfcvfmaq apgqrdylrt lvrdvvyaav e
//
LOCUS       WP_284423215             321 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: 2-hydroxyacid dehydrogenase [unclassified
            Bradyrhizobium].
ACCESSION   WP_284423215
VERSION     WP_284423215.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Kutner,J., Shabalin,I.G., Matelska,D., Handing,K.B.,
            Gasiorowska,O., Sroka,P., Gorna,M.W., Ginalski,K., Wozniak,K. and
            Minor,W.
  TITLE     Structural, Biochemical, and Evolutionary Characterizations of
            Glyoxylate/Hydroxypyruvate Reductases Show Their Division into Two
            Distinct Subfamilies
  JOURNAL   Biochemistry 57 (6), 963-977 (2018)
   PUBMED   29309127
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10187381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..321
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=34701
     Region          7..319
                     /region_name="GDH_like_2"
                     /note="Putative glycerate dehydrogenase and related
                     proteins of the D-specific 2-hydroxy dehydrogenase family;
                     cd12164"
                     /db_xref="CDD:240641"
     Site            order(55,74..76,99,236,284)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:240641"
     Site            order(75..76,93,99,103,147..151,169..172,174,201..203,
                     207..208,234..236,260..261,284,286..287,319)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240641"
     Site            order(102,104..106,108..109,112..113,116,118,121..122,
                     124..125,129..130,132,135,138,162,258,262,265..267,269,
                     273..274,276,279,281..283,285..286,290)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240641"
ORIGIN      
        1 mtkgalalli hggtdnwspq rwkarfndvc sdrpvvllpd agldpadvhy aavwkpvpge
       61 lagfpnlrvi fnlgagvdal madktlpsvp lvrvavddlt qrmteyvvlh vlmhhrqely
      121 lresqrakrw apkyqwpaaa igvgilglgt lgidaaevlk rigfqvagws rsekqvqgie
      181 tfhgaaqlnt flartdilvs llpltpdtrg ildrkmfaql rrssplgapa minagrgglq
      241 neadilacld dgtlgavsld vfgqeplpad spfwthpkvv ltphnaadtd adaisryvae
      301 qigafeagga lrnlvdrvrg y
//
LOCUS       WP_284423237             422 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284423237
VERSION     WP_284423237.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..422
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45168
     Region          37..420
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mnklslaaaa vafttivapl aaaplpeakp devgfsqagl armddffare iaakrvpgav
       61 vaiardgklv hykaygqldp vkgtpmplda ifalasmtkp maavgaltlm eqgrlplqsk
      121 lsdyypgfag mkvgvaqedg tlqfepqirp ilihdlyrht sglmyggrpd saspvarlyp
      181 dgtapaiegd tqafieritk lplahqpgtq feysfsidvl gavvekvseq rlgeylsanl
      241 wkplgmvdat fapteaqrpr larpfpkdpl tgkpqaikll dtptksdcgg acsfatigdy
      301 vrfgqmllng geldgqrils pktvhhmtsn hlgpeikntv atiephragf gfglgvavrt
      361 seglsavpgn pgefswngaf gtqffcdpke rlvvvvgtaa pgdlrkyyre qvqdivygam
      421 vr
//
LOCUS       WP_284423357             279 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: segregation and condensation protein A [unclassified
            Bradyrhizobium].
ACCESSION   WP_284423357
VERSION     WP_284423357.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..279
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=30927
     Region          21..263
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 mtaeilsfet grpttelaea epalvvdveg yegpldllla larqqkvdla kismlaladq
       61 ylqfieaark irlelaadyl vmaawlaflk srlllpeppa aegpsaeema talanrlrrl
      121 eaireaanrl mnrpqfqrdv fprgnpeaia evrrpkftat lfdllsayai qrqsrvvtsv
      181 hmakrtvwsl aearaslerl vgmtevsddw gclddylldy vaepaqkatv fassfaavle
      241 lvregkleln qkqafaplyf rkrppiqpga maapdltve
//
LOCUS       WP_284423425             372 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284423425
VERSION     WP_284423425.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..372
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39766
     Region          1..372
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mrvldfstti agphcarmla dmgadvikie saegetmrtr ppvrggcsta fgqlnvgkks
       61 vvldlksrea veavrrlvga advlvenfrp gvmqrlgldf avlsalnprl iycsisgygq
      121 tgpsaelpay apvihaasgy dmahlsyqpg rsrpdycgiy hadvvtgtya fgaiasalyq
      181 rertgrgqhi dcsmlesmls ltlneiqwsq fpvaqpsrpt fgpaecrdgy vmiaiasekt
      241 fqnlmtvigh pewvgdvrfe kysdrranwg almdgveaws rqlsvagcld alnaggvpss
      301 ayrsvadala dpqiahrgal advedaagsf kvvnlpfrms eavvtagpra aslgehtadi
      361 lreaaaidaa kr
//
LOCUS       WP_284423561             367 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ATP-binding protein [unclassified Bradyrhizobium].
ACCESSION   WP_284423561
VERSION     WP_284423561.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 367)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 367)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 367)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 367)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10543770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..367
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39521
     Region          86..224
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
     Site            90..97
                     /site_type="other"
                     /note="Walker A motif"
                     /db_xref="CDD:99707"
     Site            order(91..98,163,207)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:99707"
     Site            159..164
                     /site_type="other"
                     /note="Walker B motif"
                     /db_xref="CDD:99707"
     Site            223
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:99707"
ORIGIN      
        1 mttqdaskag aqlrssaeal hadelaalaq edtrarpaqw rlspqavvty lmggrtksgv
       61 eispkyignr rlietavatl atdrallilg vpgtakswvs ehlaaaisgs semivqctag
      121 tdenqirygw nyalllakgp sreamvatpl mrameagriv rfeeltrmps dvqdtlitvl
      181 seklmpipei ndsihatrgf nmiatanard kgvnelssal krrfnvvvlp lpadldeevk
      241 ivtkrvgeig gglelpkiap adqeimrivt vfrelrdgqt ldgrlklksp sgslstaeai
      301 avtigawaea ghfgsgvida qsmaanlvga ivkdpvqdkv vlqeyletvv rerkpwadly
      361 gairdvm
//
LOCUS       WP_284423565             184 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: glycine-rich domain-containing protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284423565
VERSION     WP_284423565.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..184
                     /product="glycine-rich domain-containing protein"
                     /calculated_mol_wt=21621
     Region          24..157
                     /region_name="COG4278"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443419"
ORIGIN      
        1 mlraqvkvdv qadepdwtpa rqelwrriaa hdfepatpln ftqrlardhg wsldearati
       61 eayrrfcfla mvsptpvtps eavdevwhqh liysrdywtt wcgerlqapl hhdptpggpe
      121 aqmtyrrqya etlalherff gppspdlwpa thlrfagpry hvtdrtywli lprpsawlrr
      181 llrr
//
LOCUS       WP_284423666             459 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: M16 family metallopeptidase [unclassified
            Bradyrhizobium].
ACCESSION   WP_284423666
VERSION     WP_284423666.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..459
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49577
     Region          20..445
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mntmtfarrv acaltvataa ftlapaaqaa tkiqrlvspg gieawfvqda tvpliameya
       61 feggatqdpa gkpgvgnlva dlldegsgdl dsktfherld rraielsfqv ardnfrgslr
      121 mlrdnkdeaf dllrtaltsp hfdsadverv rsqvisglrr ettnpsslag rkflelafpn
      181 hpygrpangt ldsvpaitvd dlkdytrrvl akdtlkvavv gdvdpatlgk lldqtfgslp
      241 akaeltpvpd vaaakppqrv lvaldvpqtv itfggpgirr hdpnfmaayv vnhilggggl
      301 ssrlykevre krglaysvyd allwmdhsal figntatrfd ragetiaave qeirriadeg
      361 ptqqeldeak syingsqmla ldtssklaqa llqyqldkmp idyiekrsei vnavtlddak
      421 kaakqlwsqg lltavvgrtp qasaepaqvp ptapvtktn
//
LOCUS       WP_284423681             299 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: TPM domain-containing protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284423681
VERSION     WP_284423681.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Sirpio,S., Allahverdiyeva,Y., Suorsa,M., Paakkarinen,V.,
            Vainonen,J., Battchikova,N. and Aro,E.M.
  TITLE     TLP18.3, a novel thylakoid lumen protein regulating photosystem II
            repair cycle
  JOURNAL   Biochem J 406 (3), 415-425 (2007)
   PUBMED   17576201
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..299
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30418
     Region          1..248
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrvrsavkal latllvclat mvladvavpq ltgrvvdqtg tlsssdiasl tqklrdletr
       61 kgsqvavliv pttqpeaieq ftirvaeawk igrkkvddga llvvakndrk lrievgygle
      121 gsltdvtarr iidevitprf rsgdfaggid agvdriigvi ngealpapqp qashgvdldi
      181 dsivsyapva ffgaiflggv lrtlfgrllg slatggamgi lawvlvgsmt lallssvagi
      241 viafiagglp atmpsssgrr ggwssgssss gwssgsssds gsfsggggsf ggggasgsw
//
LOCUS       WP_284423720             419 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: Glu/Leu/Phe/Val family dehydrogenase [unclassified
            Bradyrhizobium].
ACCESSION   WP_284423720
VERSION     WP_284423720.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..419
                     /product="Glu/Leu/Phe/Val family dehydrogenase"
                     /EC_number="1.4.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016639 - oxidoreductase activity, acting
                     on the CH-NH2 group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45607
     Region          9..417
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 msvyagpvfe maanqfnvia dhlgipader drlllpkrai tvscpihrdd gtiavyegyr
       61 vqhlltmgpt kggtrfaptv digevaalai wmswkcalvg lpyggakggv tvdlstlsrr
      121 eleslsrrym qemipfvgph tdvmapdmgt neqvmawfmd tysmyqgqtv teivtgkpvf
      181 sggtlgrrea tgrgvahtsr rvmdvlgidp akstavvqgf gnvgsyaalg fhqmgmkvia
      241 vsdhtgalhd prglnipalm eyasargsia gfstelafdp keiltlacdi lvpaavervi
      301 dakvaanlkc riiaeaangp ttpdadlvld qrrdeiflip dilcnsggvv vsyfewvqdl
      361 qqlfweeeev mrreyqildr afermvtrak adgishrtaa maigvekvrn akntrglfp
//
LOCUS       WP_284423834             468 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284423834
VERSION     WP_284423834.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..468
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49591
     Region          127..467
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtrrrlllvl astvtlsala igaarardvp qvatgfiasv lcseifvsgl dpdrilsetq
       61 aampgagllt wamdirldra akdvtvtllg lgrshavfrd glgchmdhge tadspairpa
      121 aptpallpdi apprvvtpvt palaaaldra faepdappfr rthavvvlkd gkviaeryaq
      181 gftldtpllg fsatksmtat ligilirqgk lalhapapva awqsegnprr aitvdhllrh
      241 taglalgssq qasllsalep vnrmkyvead raafaesipl ettpgavsny hdgntvilsh
      301 lirdatggsa advlrfahre lfdplgmrsv tiefdaagtp egssqmlata rdwarlgqly
      361 lddgviagrr ilpegwveyv saptpgafvg lgagfwtnrg dsfganyris hgwprdaffa
      421 kgsigqyvvv ipserlviar fgrtvnwppe adgvaqlvsd vmaatrge
//
LOCUS       WP_284423729             272 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD-dependent epimerase/dehydratase family protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284423729
VERSION     WP_284423729.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..272
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30116
     Region          3..230
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mprilmtgas ggigsslrkl lppiypdlll sdlrppadls sqetfkaadl adlsqvealc
       61 egvdgiihfg gysvegpwnd ilqaniiggy nlfeaarrkg vkrvvfassn havgfyprhr
      121 kidndvqprp dgrygvskvf gealgslyad khglqvtclr ignfgdkpld krrlsiwlkp
      181 edlvqlcrig lehpdihfev lygvslnera wwdnqraydl gyrptgrsed frehalaeqa
      241 klpadpigdy fqggafctte fdgdtsriid wg
//
LOCUS       WP_284423860             612 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: AMP-dependent synthetase/ligase [unclassified
            Bradyrhizobium].
ACCESSION   WP_284423860
VERSION     WP_284423860.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..612
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66518
     Region          22..610
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mlqpsptddh alaagglaai atlpelwrwr vrqspdheay rqadpqsgsw tsfswretda
       61 ivdrwrrala adafdrgdri ailmpnglah lamdqaalsr glvpvpmhav dnadsiayil
      121 adcgarlllv dsderwneia avgqalpdlk rivcaalrsr dsaasdprlv avdtwleaaa
      181 aaaprsndit iaphdlaaiv ytsgttgrpk gvmlshdnvi snvkaihqrl aadtgdvfls
      241 flplshtfer tagyyypiai gacvayarsv kqlsddliav rptilvsvpr iyeriyslvm
      301 hhravanvie ralldltvai ggrrfdarhg httrssvvdq iawpllqrlv adkvlarfgg
      361 klrvavsgga piaepvvrlf lalglevlqg ygmtetspvv svntpddndp rsvgralpgi
      421 evrigdndel mvrgpgvmlg ywhrpeetar ikesdgwlht gdqaridqgr ititgrikdi
      481 lvtstgekia padletailt dplfeqaivi genrpfvaai vvlnptgwae qqarlaahgq
      541 rgteaeaasl lrhiartvka ypayatpkav hwtlepwtiq aglitptlkn krpaierafa
      601 keieaiyakr pa
//
LOCUS       WP_284423901             101 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: c-type cytochrome [unclassified Bradyrhizobium].
ACCESSION   WP_284423901
VERSION     WP_284423901.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 101)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 101)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 101)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..101
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10809
     Region          <1..99
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mpriialsvl llilatvpaa addldhgrql aerwcaecha vgtepakfrr arpfvaiaak
       61 dgltrdllvk flllphatma nnplspadaa dlatyvlslr k
//
LOCUS       WP_284423912             516 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acyl-CoA synthetase [unclassified Bradyrhizobium].
ACCESSION   WP_284423912
VERSION     WP_284423912.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..516
                     /product="acyl-CoA synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016405 - CoA-ligase activity [Evidence
                     IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0032787 - monocarboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=55225
     Region          11..496
                     /region_name="FACL_FadD13-like"
                     /note="fatty acyl-CoA synthetase, including FadD13;
                     cd17631"
                     /db_xref="CDD:341286"
     Site            order(162,165..170,172..173)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341286"
     Site            order(165,282..283,303..308,387,399,402,413,493)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341286"
     Site            order(165,205..206,255,257..258,261,282..283,303..308,387,
                     399,402,410..413,474)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341286"
     Site            order(205,257..258,261,282,410..412,468,474)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341286"
ORIGIN      
        1 mpvryydwia hharrtpgkt amvdlgsnrr ftyaefdarv arlaahlrga cgigkgdrva
       61 vlalnatetl evqfacfrvg aifvplntrl tipelqfivg daapkvmihd ddladtalav
      121 srlcavatal rygpaasyel aiatakplmd vepvtlddvs timytsgttg qpkgamithg
      181 mtfyncvnlg gpayitpssv lltvlplfht gglncytnpv lhvggtvlim rafdpglalq
      241 lisdpalgin vffgvpaiyq fmaqhpafat adfsrltigg vggapmpvpl lntwensgva
      301 lqqgygmtet spavlaldre dagrkagsag kpvlhtevri vrpdgsdaai gelgelwvrg
      361 pnvtpgywnr pdanrssftd gwlhtgdatr vdeegfyyiv drwkdmyisg genvypaeve
      421 nvlhqlsava eaavigiadp qwgetgmaii avkpghslse adihahcqan larfkcprtv
      481 rfvdalprna tgkihkptlr ksfatasatd lvqqas
//
LOCUS       WP_284423942             652 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: putative bifunctional diguanylate
            cyclase/phosphodiesterase [unclassified Bradyrhizobium].
ACCESSION   WP_284423942
VERSION     WP_284423942.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 652)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 652)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 652)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 652)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..652
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..652
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=69994
     Region          25..640
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mqsaptdpka aalakaqaas slqnifltlf anvaialsla lliylregsa pilwwlaaav
       61 afavlraawv shlkssgkie rdphrvlrtl tmmafasgll wsvvplglpv fthahnvndv
      121 vfimagtttg aiiqslaysr maiafgaplm gatilrmlls ggdvgyivaa diafltvmlf
      181 rsarlgelnf iashsttiaa teladslaaa nqtlerlvri dsltglanrs hfrtvagaac
      241 aggqgvafll fdvdnfkiin dtrgheagdr vlqmvaallg aacgaddlpv rlggdefivv
      301 lqgedvaara valgerlmsa lerpvliagq pltvscsigi aaqaegaidl eelsaradaa
      361 lyrakddgra cmrvfdaqmq saltlqrrld aelhaalarr elhvefqpqv amasrevigf
      421 eallrwnhpc aglipppdiv saairlrlsg qltefvgerv caflraldrk kahgirvsin
      481 vsprefpihs paqtlklvse rygvdpkrie ievteeamfd pkrcadelkl idqygfglai
      541 ddfgvghssi anlmaveidt ikidrsfidg iaddrrdqql vaaitavalp lghriiaegv
      601 ereadaeclr mlgcsygqgw lygkpmkedd aiawlvrhrq aaaaveplpr sa
//
LOCUS       WP_284423969             337 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: zinc-dependent alcohol dehydrogenase family protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_284423969
VERSION     WP_284423969.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..337
                     /product="zinc-dependent alcohol dehydrogenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=34524
     Region          1..336
                     /region_name="MDR7"
                     /note="Medium chain dehydrogenases/reductase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cd08276"
                     /db_xref="CDD:176237"
     Site            order(40..42,45,143,147,168..173,191..192,196,211,
                     235..236,238,257..258,283..285)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176237"
ORIGIN      
        1 mkcyelqgpg gidalalvdk pvpapgrgev lvrltaasln yrdlltvkgg ygsrqkfplv
       61 plsdgagvve aagdgvaafa pgdrvigsff eswtggepse akmraalgga vdgtlseyri
      121 fpahalvrtp ahltdveaat lpcagvtaws avvklggirp gqtvltqgtg gvsifalqia
      181 klagarvvat ssseakiarl kalgadvtln ykttpdwgka arditgqgvd lvvevggvgt
      241 lnesiratri ggtiafigvl agapaselrl plmvmqqqrl qgvtvgavdd lqalanalal
      301 hqvkpvvdrv fpfaeareaf hymssgahlg kvaiaig
//
LOCUS       WP_284424038             246 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: metallophosphoesterase family protein [unclassified
            Bradyrhizobium].
ACCESSION   WP_284424038
VERSION     WP_284424038.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..246
                     /product="metallophosphoesterase family protein"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26851
     Region          3..234
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mllaiftdih anrqafaacl eaarargaer liclgdivgy gadpewsvdt vmemvanggl
       61 avrgnhdnav stvsesmnse aqaamewtrg rlsaeqrrfl aelpmsvgdd drlfvhseas
      121 spprwryvqt sadaarsmia teaqvtfcgh ihrpalysms atakmtsftp tanmpvqllr
      181 grqwlavvgs vgqprdgdpa acfvtfdtkt reitycrvpy dveaaaqrir dnglppwlaq
      241 rlsmgr
//
LOCUS       WP_284424352             435 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Acidovorax sp. SUPP1855].
ACCESSION   WP_284424352
VERSION     WP_284424352.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..435
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46200
     Region          56..376
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mrlpaddatn gwsailpara prpalqgpvr adwlvlgagc aglaaarrla elrphahvvl
       61 vdagtvgdna sgrnsgfaid vphnvgssle elrqaahyqr llaagladlq rriaahaidc
      121 qwrragkyhc avspaagrtl dhhaqelral gepherldrd alaarlgtry faaglytpgt
      181 vllnpaalcr gladalpaqv alyentpvha ldiaphavva httqgrieap qlivasnafa
      241 qqlglfqvet fplatfgsls apltpaqrer lgapqgwgvt pvnavagatl rytddhrllv
      301 rqgfeyaprf rvaaavrerv rrahravfda rfpqladvpl ahfwegaiai trngaprwgr
      361 fapnvhgvag cngvgivkht vlgalaadla lgqdhpliad alalgaparm ppapflglgv
      421 rayiarekwa graer
//
LOCUS       WP_284424325             712 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Acidovorax sp. SUPP1855].
ACCESSION   WP_284424325
VERSION     WP_284424325.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 712)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 712)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..712
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=75895
     Region          68..712
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mhptiarpva lgmalawlal aataqtptpa dpaaerspal pavtvtapat paaqrssrla
       61 tgtaglsldt pfsvttvpae lvrqqggttl qdalrnvpga qadsgfngsh tqffilrgav
      121 tdsgtgsnrv lrdgvrlsny pytpafvesv dvlrgpgaal gvrsepggtv nlvtrqpqla
      181 nfgsaslgag ahgaleasid lnrvlsaene laarvtatrs qaskwrhved rldgiklgla
      241 qsdgnryhlr anveatnqty qpdyglpalg grpvavprdr qlgepfgdst tnnriydlhg
      301 dvalsahtrw sadfthleah stsiknllng splagqpagt yarvsawepg terridsfst
      361 alsstqgtga vthqlyfgad yykevlnqpa lsvpastspa invfdpvygr vtappagtvl
      421 aqslttqdle svsasaqdqi dfgawsvvag lrftrqrfly gtagvlpvee srwnpklavl
      481 rrlsetdtvy anvstgtspn qvasssnqsl psrrsaqvea gwkslwrgga lvsdlavyrl
      541 dqknmiasdl stplnnfdft tagsarsqgi easlsgqvtd rvtvaatyaf thakylqnpv
      601 yggmsvpnva rhaatlwaqy awnaqwktga glylqsrrfa deanttvlpg yarfdlsqtw
      661 taklangqsv evqatvrnlf dqhyfvsshl hvsrwitpgq grnafvsaty rf
//
LOCUS       WP_284424355             156 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284424355
VERSION     WP_284424355.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..156
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=15924
     Region          1..135
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mafgrlertt gpqpmsdinm tplvdvmlvl vvifiltapl lassirldlp radgatpgap
       61 pqsvtvvldk egqaylddvp lapqalaarl aqlarerpdt evqlradtav pygrvvevmg
      121 aanaaglrri gfvadpaapa apsaapaspa aaaaar
//
LOCUS       WP_284424438             320 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284424438
VERSION     WP_284424438.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..320
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33580
     Region          1..318
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mqrrqwiaav aaatvlprms faqdkplrii vpfppggatd iagralqepl qrllgqpvvi
       61 enragaggsi gmaevgraag dgltlgvatl sthgvnpavf sklpydpvkd fagvteivka
      121 pgvivvnpkv lpvkdfaelv kylkanpgkv syatpgngti ghmwgelfks stgtsmvhip
      181 yrgagpaind vvggqvpvyf dqvasslphv ksgklkalav swperldvlp evptyaqlgf
      241 pqanepswfg lvapvstpaa avlrvqqava aalrepavre rlagqglyas gtspadfsqq
      301 ivreidkmke vaayakiqld
//
LOCUS       WP_284424528             368 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Acidovorax sp.
            SUPP1855].
ACCESSION   WP_284424528
VERSION     WP_284424528.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..368
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39540
     Region          68..329
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mplrtlcgaa llllasacts vppastapap aafpgaswep qpvaeqgpac rrgleaagdy
       61 lrtldttalm avqdgrvlfa ygpveavsiv fsvrksvlsm lygppvadgt idldrtladl
      121 giddtggllp ierqatlrdl ltarsgvyha aanggddaaa apargsqvpg ryflynnwdf
      181 naagtaferl agrgiyqafa ddlaaplqlq dfdparhvrs gdarrsehla ypfflstrdm
      241 arlghlmlqq grwrgrqlvp adwvaritqq ttpasqmhpa htarrgfgyg ylwwllqepp
      301 dsplagayma wgvhgqyilv vpkrqmviah krqvpvagdw nvswvgpkaf lhaarllaaa
      361 pcrageap
//
LOCUS       WP_284424588             580 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Acidovorax sp. SUPP1855].
ACCESSION   WP_284424588
VERSION     WP_284424588.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..580
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60746
     Region          1..460
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          513..578
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(536,545..547,554)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            546
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mkkvlianrg eiavriarac adygvasvav yanadidavh armageaygl dgdrpadtyl
       61 niekllavar rsgadavhpg ygflsesaaf aqavidaglt wigpspeaia rlgdkveark
      121 ialkvgaplv agtsepvkda seviafaeqh glpiiikaaf ggggrgmkva wrmdevaely
      181 dsavreavta fgrgecfveq fldrprhiea qvladthgnv lvlgtrdcsl qrrnqklvee
      241 apapflsddq rarihqaahd icaeagyasa gtvefllsgs gaisflevnt rlqvehpvte
      301 qttgidlvve qlriadghpl avtetprplg hsiefrinae dvgrgflptp gpvvafsaps
      361 gpgvrvdsgv qsgstvpgtf dslmaklivs gatreqaiar aqralrefki egvasvlpfh
      421 ravighpdfv ggdgfkvhtr wietdfapdl aaalraepva dttlirtame idgrrvslgl
      481 ppellrglqs vpggapvapg agggdkaeqd pnavgapiag tlqtwkvaeg dtvakgdvia
      541 vmeamkmemq vtahragkia lsaaagsyha agtaiariqd
//
LOCUS       WP_284424624             347 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Acidovorax sp. SUPP1855].
ACCESSION   WP_284424624
VERSION     WP_284424624.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..347
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=40018
     Region          71..225
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mpkstanair waeqgivpdq mvrygisrll kerlqemrsg daeataeqtq afvdamrrae
       61 laplpdkane qhyevpaeff gavlgphrky ssgywgdgaa tlaqaeeaal lrtckhagla
      121 dgqrilelgc gwgsltlwma qrypasrita vsnshsqray inaeaakrgl snvqvitcdf
      181 nrfdiaarfd rivsvemfeh lrnwpqafan vsrwlapggr ffmhvfahre apypfeerda
      241 sdwmskhffs ggmmpsddla lhcqddlqlr rrwrwdgthy ertarawldn mdlqhdalmp
      301 lfrrtygeda qawwsrwrlf flsveelfgf dggqqwwvsh ylfdrrd
//
LOCUS       WP_284424634             300 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: PP2C family protein-serine/threonine phosphatase
            [unclassified Acidovorax].
ACCESSION   WP_284424634
VERSION     WP_284424634.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..300
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=32798
     Region          3..245
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mkfsvfqvsr rggretnedr mgycytress lfvladgmgg hpegevaaql alqtvsaafq
       61 rhakptledv hgfladalla ahhqilryaa drgmldtprt tlvvavvqeg saswihcgds
      121 rlymvrggel ftrtrdhsyl elrnmplqgi ervnrnvlft clgsptkpiy ditgpvaleq
      181 gdrillcsdg lwgtlddeti arqlsrlpvs qsvpdlveda lrkagdtsdn vtvvalewet
      241 pdafestqgi stdsisddgf sstiqagpld mvdddlddea iersiaeine airrsaarka
//
LOCUS       WP_284424740             294 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Acidovorax sp. SUPP1855].
ACCESSION   WP_284424740
VERSION     WP_284424740.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..294
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31522
     Region          5..284
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 melgpwgdas vlgilgllig sflnvvihrl pkmmerqwaa ecadfaaman kdaasteapv
       61 apvesfnlwt pasrcpacgh avqwyenipv lsylwlrgrc sackvrispr yplvelatgg
      121 lfffcgwhwg ttltavawcg fsaalialaf idwdttllpd ditlpllwag liasamqwtt
      181 vplfsavmga vggylslwtv ywafklatgk egmghgdfkl faalgawfgw palvpiilia
      241 svigafigig mkfasqlreg gyvpfgpflv gsglaamvfg petilqgllr slgl
//
LOCUS       WP_284424890             652 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284424890
VERSION     WP_284424890.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 652)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 652)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 652)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 652)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..652
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..652
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=71506
     Region          358..506
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mspttpspfh rtwspaprrt pwsvlrglaa lcaaavlcgc agvtvssmsp reylsqrrgd
       61 vltsgrvsea teevlrvigs dadtcaddla dcrnqlaasn giseeqrlsa laevwlqvgl
      121 egerdrsapl pqdealdawm esaryawayl fftqrspger afedrqtqvr dyynfatqrv
      181 vsllfqryra egrrsdeart lgawrissna sdirlpsdap lpeelipatt lrfsgvrnty
      241 rrdgfgtelv aasvpepgeq tpapfkempy paatallrfp gktlgevlrt qevqvaiydp
      301 yhtarvelgg qqvplagnft agyglwlars gfatqamrtl lgwsdrldap rihlmqpydp
      361 nrrtivmlhg lasspeawin vanevlgdaq lrdayqvwqv yyptnaplal nqhdirealv
      421 qtlahfdpag tarasrdivl vghsmggvla rllvsesgdt lwdevigrpv lppedqarlr
      481 edlgpflvfh pmpqvsravf iaaphrgtpf anktlsrwla nmvtlplavl erfgdatrtl
      541 araqatqpss ggvpprlpns idnladtdpf vraaadlpig prvryhsimg redpgtplaq
      601 ssdgivpygs ahlagaesel vltshhsvqe npraileirr ilrealaaep vr
//
LOCUS       WP_284424863             325 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284424863
VERSION     WP_284424863.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..325
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33414
     Region          5..322
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mrvarpipaf fcalglvata apalaqgtyp dhpvkvival paggsadmia rmvgqkmaae
       61 lgqpfvvdnk agasgqigtp mvaraapdgy timvspasfl ttnksifktl pydpqadfvp
      121 itklvnqpmv lvakdaqkfp svaavlqaar aapgrvtyas sgdgspqhla almfgtrtqs
      181 smlhvpykgg apaindtlag nvdlmfavlp ealphiqsgk lqalavmsaq rsavlpqvpt
      241 maesgvpqve lsawvgllap artpqpvidr lrsaahaala gdtqtrlaas gmevapgttq
      301 qlqdtiaaei klhaelvkaa glapq
//
LOCUS       WP_284424891             747 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284424891
VERSION     WP_284424891.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20305241
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..747
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80048
     Region          85..642
                     /region_name="YCCS"
                     /note="TIGR01666 family membrane protein"
                     /db_xref="CDD:130727"
     Region          371..641
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mrispehrlr aalrvalshy vfnglsvafg lllisagvhg wlgaaaaasa svgvivtapp
       61 dlpgpargkf wqmlpapllg vplffgvqml hpselalgll ivpasfvafl amawgkrgvp
      121 iavavmfsmv fsmavpptpg vdpltaalat tghfalgaal yvlysvvanh alnaryrvqs
      181 vadallalaa lmrvqarqft pvdlqgppap alagallhrq aalaeqlqaa rnivlesprt
      241 prrqrlagml llvlemrdhl laceldldtl kahpghapvv vglrdvlhhv ademerlada
      301 mligrrptaf adhrphlaal rweeapqpqp gpeganpspr llargladri ghindealrm
      361 ialargeaep nlavvranwq mfvsptawsw hpfnglwrwd applrhaira alamgvgyav
      421 aqalpwgtha ywilltivvv lrgslaqtle rrnsrvagtl lgcvlalall smhptalgli
      481 valtlaqava hgfavrryli tavaatvlgl vqshmlhags stafalferl adtligtgva
      541 wafsyvlpsw ertqipalvs rtlaaqalha realalgqlq avdnapelaw rlarreayds
      601 lsalvqatqr slsepravrp pleplerlqv hcyqllaqlt avktmlllrr ghleperlqa
      661 plattaeaig nalsapraaa daampprvsp gpeplpdpfd aqlgpwllrr lglavglaee
      721 lrsdadqvrq smntkapdaq pmakrsa
//
LOCUS       WP_284424932             427 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Acidovorax sp.
            SUPP1855].
ACCESSION   WP_284424932
VERSION     WP_284424932.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..427
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=47592
     Region          59..427
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mkktgrtllt valtfvatta ivlfalnfta gekkvqhqip rlyttahpqy eramgsllgp
       61 gitsgnevve llngdqifpp mlaairaaqk svtfetyiyw sgdigkqfad alseraragv
      121 kvhvlldwvg sskmdesyft emkaagveve kfhkphwynl arlnnrthrk llvtdglvgf
      181 tggvgiapaw tgnaqdpdhw rdshyqvkgp avaqmqatfl dnwlkvtgkv mhgeayfpai
      241 aqsgtqkaqm fssspssgse smqlmyhlai tssersldls vayfvpddlt rqlmldalar
      301 gvrirlitpg ehtdtetvka asratwgell qagaeiyeye ptmyhckvmi vdqlmvsvgs
      361 tnfdnrsfrl ndeanlnvyd apfaqrqtvv feddlkrsrr vtyqdwldrp mreklaekaa
      421 sllqtql
//
LOCUS       WP_284425046             294 aa            linear   BCT 25-DEC-2024
DEFINITION  cysteine dioxygenase [Acidovorax sp. SUPP1855].
ACCESSION   WP_284425046
VERSION     WP_284425046.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Chen,M., Zhu,J.Y., Mu,W.J. and Guo,L.
  TITLE     Cysteine dioxygenase type 1 (CDO1): Its functional role in
            physiological and pathophysiological processes
  JOURNAL   Genes Dis 10 (3), 877-890 (2022)
   PUBMED   37396540
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Joseph,C.A. and Maroney,M.J.
  TITLE     Cysteine dioxygenase: structure and mechanism
  JOURNAL   Chem Commun (Camb) (32), 3338-3349 (2007)
   PUBMED   18019494
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14410663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..294
                     /product="cysteine dioxygenase"
                     /EC_number="1.13.11.20"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0017172 - cysteine dioxygenase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31125
     Region          156..262
                     /region_name="cupin_CDO"
                     /note="cysteine dioxygenase, cupin domain; cd10548"
                     /db_xref="CDD:380416"
     Site            order(156,158,176,187,189,246,260,262)
                     /site_type="active"
                     /db_xref="CDD:380416"
ORIGIN      
        1 mttssissps ravsprsera evadtassnk rpagssqpgg darldglpar spdataegas
       61 akrprtslpg adagiaarea qldkvyttls lqarqthaan qkrleagvqk llqnasvqaa
      121 gkdvrdcvag alegllkeaq lstdiyqpks nelagygryl lhshakeges fclqlfsfad
      181 kqktpihdhp necasfilkg nlweriysps dspagaqvpl atkdkknerl qgsmdgfgpt
      241 qldvphslkn tsgdialsvh lyrdmdglsd sqqiaaktrf erapkaakpa vapa
//
LOCUS       WP_284425106              97 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Acidovorax sp.
            SUPP1855].
ACCESSION   WP_284425106
VERSION     WP_284425106.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 97)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 97)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..97
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=10109
     Region          25..80
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mpntlpapnp taaepaplqa rpyrerllrv ddvcfitglg rstvyakvka gdfpgpvqlh
       61 gacvawrete vdawiaarpa vptlpaaraa rpagvaa
//
LOCUS       WP_284425121             781 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Acidovorax sp. SUPP1855].
ACCESSION   WP_284425121
VERSION     WP_284425121.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 781)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 781)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 781)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 781)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..781
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..781
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=79648
     Region          17..780
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mnptptapps psdsapgtld lgiggmtcas csgrveralr kvpgvqeatv nlaterahvv
       61 yaasaagvag agaameaqlr ravrnagyep rapqaqdaea rgqspwagfg pvalglalsa
      121 plvlpmllgl lperfgallg phgmlpawlq wllatpvqfw lgarfykagw halkaragnm
      181 dllvaigtsa gyglslwlwl tapaghaphl yfeasavvit lvllgkwlea rakrqttaai
      241 ralhalrpdv ahlvgadgev dvpvaevmag drivvrpger ipvdgtvleg htqvdesmlt
      301 geplpvprta gealtggsin gdgrvvvqvs avgaetvlar iirlvedaqa gkapiqrlvd
      361 rvsavfvpvv lgialatllg wlwvgaggea avihavavlv iacpcalgla tpaaimagtg
      421 vaarhgilir daealerahr vgtvafdktg tltvgqprlt afevapgqdg dallaavagv
      481 qggsehplar avvqearrrg lqlpapqavs avpgrgtegt aagrhfrvgs lrwmeelgvp
      541 lgalagpaaa lqsagatvsa vaeappgevp tgegtagpaw vlrallafgd epkpgareal
      601 aalrarglrv vmvsgdhrga aeamarrlgl dpdagevmae vlpgdkaacv arlrsealag
      661 pgahrpagha vamvgdgvnd apalaaadvg mamgngtdva mqaagitlmr gdprlvaaal
      721 dishrtvaki rqnlfwafay nvagiplaal gylspvvaga amalssvsvm analllkrwr
      781 v
//
LOCUS       WP_284425146             312 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Acidovorax sp.
            SUPP1855].
ACCESSION   WP_284425146
VERSION     WP_284425146.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..312
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=35002
     Region          5..239
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mknakiilpg gaglvgqnlv ahlklhgyhn lvvldkhasn lailrqvhpd ivaedadlae
       61 pgtwerhfeg advvvmlqaq igapqadpfv rnnltstgri ldliqrhria qtvhisssvv
      121 esvaqdhyte tkraqekmvl dsgipcvvlr ptlmfgwfdr khlgwlsrfm rkvpvfpipg
      181 sgrymrqply aadfcriivr cieerrvggv fnitglekvd yidiirqika atgagawivk
      241 ipyglfylll kvwalfdkdp pftadqlkal vahdefevid wpgifgvrat pfaeaihetf
      301 nhpeysrvvl ef
//
LOCUS       WP_284425177             281 aa            linear   BCT 25-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284425177
VERSION     WP_284425177.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Bagautdinov,B. and Kunishima,N.
  TITLE     Crystal structures of shikimate dehydrogenase AroE from Thermus
            thermophilus HB8 and its cofactor and substrate complexes: insights
            into the enzymatic mechanism
  JOURNAL   J Mol Biol 373 (2), 424-438 (2007)
   PUBMED   17825835
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..281
                     /product="shikimate dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29722
     Region          7..278
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 mqqqtingst rliahlgypt eafkapmiyn pwfaqqgina lvvpmgvqae dypatlqvlr
       61 rmtnwhgalv tmphkvstla lvdaltptar iagacnaivr rpdgtllgdq fdgagfvrgv
      121 qrkglalagr ralvsgsggv gsaiaaslaa agvaelalfd vdghraqala drlrqhypal
      181 rtavgrndpa gfdlvvnatp lgmreddplp fdvdriapgt fvgevvmaqa htpllqaama
      241 rgcpvqqgtd mlfemipayl effgwggatp ealravariv y
//
LOCUS       WP_284425271             462 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Acidovorax sp.
            SUPP1855].
ACCESSION   WP_284425271
VERSION     WP_284425271.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..462
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=49274
     Region          1..460
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 marllvvddd aafreslvet lqslghevhg agggaealrr veshrysaif ldqrmpgmdg
       61 lqtlqalaar marlppvlvl tayasgsgti eamrlgafdh ltkpvsraav vevleralrs
      121 eadagataaa paplpdaqed geligiseam revhkrigma aasdapvlie getgtgkelv
      181 aralhrhstr vagpfvavnc aaipkelles elfghvkgaf tgaaterpgc fraadggvll
      241 ldeigdmape vqakllralq egevtplgsh rpvkvnvrvl aathrdlaaa vregrfredl
      301 ryrldvlhiv lpplrerlad ivplaehflr gaaapqpakr lsagaarall dhawpgnvre
      361 lrnamercha lqrgpvvgat dlglqpsptt pddlghshra gasdalpaaw legslpqaie
      421 qlerrmlaha laqaqgnrsl aarrlgihrq llyskltqyg ie
//
LOCUS       WP_284425276             417 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [unclassified Acidovorax].
ACCESSION   WP_284425276
VERSION     WP_284425276.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..417
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44641
     Region          8..408
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mtdnthstsr tgplagvril dltsvimgpf atqilaqlga evikvetpdg dnmrhvgpmr
       61 hpgmghiflh anagkrsial dlkhpegrea alrlaercdv lisnvrpqal arlgldpasv
      121 aarnprlihv sccgfdqegp daarpayddl iqgatgipwl mqrygapepa yapttlsdrv
      181 tglhavyavt aalyarektg qgqaivvpmf eamaqfilgd hmagltfepp qgeagyarll
      241 tthrkpyata dgmlcvliyn dkhwrsffaa igeigeaqgl aqdprfathg araanidavy
      301 aevarilrtr ttaqwqalld aadvphmpmn spadlltnpq lratgflhds vhptegpmha
      361 mahptrwsat ppprtlapap qlgehtrall aeagytptqi dallaqnach aatgepa
//
LOCUS       WP_284425306             345 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284425306
VERSION     WP_284425306.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..345
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=38373
     Region          1..341
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mstqhrgnlf drmricaasa vifshhfhit htasptwlhs dmvggvavmt fftisgylvt
       61 qswlrqpkal aflskrflri wpgvlfavlt nvflfgiffn slpaadflah pdtlgyfrnl
      121 llirdypylp gvfennpikh lmngplwtip ieslcylvla gagllgvfrs rwlaslaava
      181 yiaffitarn adltgemrhw feypayftyg aliavfrdaf harsgrllll laplaavlff
      241 glqmehtagl lllppllihi gslnvpalaf lqrggdpsyg iylygcpvqq svyalwpdla
      301 fipslmlsva laavagyasw hlvespalrf krwfqrtpva pqaap
//
LOCUS       WP_284425366             307 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284425366
VERSION     WP_284425366.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..307
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33480
     Region          120..217
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mtnarwqrgm vvcnlllaag wlvwqwpasp lravaglaav mlllrlfmgl qfvcmarvnr
       61 rasradgvpv pslaqmaraw saearwasvv fgwwqpfrst avpdwlpppv aggpppargv
      121 vlvhgficnr gfwtpwmkvl rsrghpfvav tmepafgaid dyvdtldeav rrvtaatgrp
      181 pvvvghsmgg lavrawlrar qadarvhrvi tlgsphqgaw aarfsrsang rqmvpggewl
      241 rqlaqdeppg raalftcfys ncdnavypaa tatldgadnr lreglahvqm afhppvvrec
      301 ldliaap
//
LOCUS       WP_284425483             144 aa            linear   BCT 25-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284425483
VERSION     WP_284425483.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..144
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=14347
     Region          9..131
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mqmpetglsr lsasqaqqlv qsalitglde glavsaaavd ssghllafar addaflgsid
       61 asiakartav yfrrdtaamq qaleqgktay laladvlple ggvpllvggt lvgglgisga
      121 asahdgvlar aiasllnsls grtt
//
LOCUS       WP_284425594             574 aa            linear   BCT 25-DEC-2024
DEFINITION  PHA/PHB synthase family protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284425594
VERSION     WP_284425594.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 574)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   4  (residues 1 to 574)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..574
                     /product="PHA/PHB synthase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=62833
     Region          54..572
                     /region_name="PhaC"
                     /note="Poly-beta-hydroxybutyrate synthase [Lipid transport
                     and metabolism]; COG3243"
                     /db_xref="CDD:442475"
ORIGIN      
        1 madseapwga dtqafqqfqq mlgkgwtqam qafqqaapag aagafakapa apvqfapekl
       61 aalqqqyvke attlwtqgaq anasadrrfs seawaqnpva afsaaaylln artlmglvda
      121 veadaktrar irfgveqwma amapsnflaf naeaqkkaie tqgesiakgv anllhdlrqg
      181 hvsmtdeslf evgrnvatte gavvfenalf qlieykpltd kvherpflml ppcinkfyil
      241 dlqpenslir havseghrtf vvswrnpdds lahktwddyv qegalaaigt vqditgaaqi
      301 nalgfcvggt ilsnalavla argeepvasa tflttlidfs ntgildvfid eafvqfrelq
      361 mgkggmmkgq dlastfsflr pndlvwnyvv gnylkgetpp pfdllywnsd stnlpgpfya
      421 wylrnfylen nlvrpgrltv cgeaidlnlv dlpvyiygsr edhivpidaa yastqvlpgk
      481 krfamgasgh iagvinppsk kkrshwlred gqlpgtldew lkgatehpgs wwtdwsrwlk
      541 ghagklvaap kaygrgtrfk atepapgryv kqka
//
LOCUS       WP_284425647             356 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Acidovorax sp. SUPP1855].
ACCESSION   WP_284425647
VERSION     WP_284425647.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..356
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36001
     Region          41..353
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtppgadart arrsavplri alrraapvgi alalvllvma sltagsapvs wreaavalag
       61 pwagafgapa gdmaqaivrd lrlprvvlal lvgatlalvg gllqsttrnd ladpflfgls
      121 sgastgavav itltgewlga wtlpaatfag aavaagavll lvrraggqgp aqtvlaglav
      181 sflfgalthg lvfagdqraa havvfwslgg lglarwdnlw laclglavpm vfvwrrhral
      241 dallagddta hslgiaperl rtqafvvaav ataccvalag vigfvglmvp hlarrlsgpl
      301 haaflplagv lgaglllasd lvartllgsq elpvgivtag igavfvmall rrrvvd
//
LOCUS       WP_284425734             225 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284425734
VERSION     WP_284425734.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..225
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24089
     Region          26..>149
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mpsrfpdsps qdrshlltqe alpwivngra sdeqraevek hlaqcadcrd elqtqqqvqa
       61 amalpptrvp deqagldkll arieldalcd qplpktaava rrqggrltya latfavlqav
      121 alafmghrls eqepsafqtl ssppapgaag vdqpnairvv pdgritladw kalldslnlq
      181 vvsgpnamga yavsakdmrq sntqalerlr stpgmqmvep iggpp
//
LOCUS       WP_284425740             323 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284425740
VERSION     WP_284425740.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..323
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34155
     Region          1..321
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mtlnrrhamv ygaaalastt amgqtanwpt ktlrlivpyp pggssdiiar aisqplsdml
       61 kqnvivenkp gangnlgadf vakaqpdgyt mllcdvgala ispsvytklp fnpskdlrga
      121 tmlaysphml vvhpsvpann lkelialskt adlnfavtat gsaphlagva lerasgarwq
      181 yvpykggvta iqdtmagqtq vlmngmlatl phvqsgklkv lalskatrmp lladvptiae
      241 qgipgfesgt wqgilvprgt pdpivqrlnt alisvirtpe irsrlagqga evvtmaaaeq
      301 dkffekerar wasvvsaaqi rld
//
LOCUS       WP_284425743             366 aa            linear   BCT 25-DEC-2024
DEFINITION  lactonase family protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284425743
VERSION     WP_284425743.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..366
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=38505
     Region          32..363
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 maisssflra valapvaaat lmaasgaasa atwvyvsnad sqdvsvyeld raagklqpve
       61 tvpvggqamp mavspnkrql yvalrsqpfr vvtlaidpas grlkkqgeaa ladsmanidt
      121 datgrwlfaa sypghkitvn sidkdglvga vqqliptapn ahaihadaan ryvfatslgg
      181 dhlsswrfda ttgkltanep altavapeka gprhfvwdka qrymyvvdel daalhvmayd
      241 aergtlrevq rtttlppgft gkpwaadlhl spdgrtlyas ertsstlstf rvdaatgkle
      301 plgqvateks prgfavdasg rfliaagqds hsvslhpidp atgvpgtptr vaagknpnwv
      361 eivdlp
//
LOCUS       WP_284425744             331 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284425744
VERSION     WP_284425744.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..331
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33970
     Region          20..329
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mqrrtfiaaa aaaaaagsli glpafaqgtw ptgktitylv pfaaggttdt lgrlisqqlg
       61 talgttvvvd nkggaggsvg seiaaraapd gytllggtis shainvslyp klgydpvksf
      121 tpvtligtnp vvlvvaassp yktlkdvlda argksgglss asagtgtsqh lalellayks
      181 gvkfthvpyk gsgpaiqdvi ggqvdmmfdt tvvaaphiqs gklraiavts akrlgsmpdv
      241 ptvaesglkg ladfevqswq aifvpagtpe pvvtrlhtei rkilaqpdmq trlksfgmep
      301 admttaqiat fqkaevakwa qvikaanikv d
//
LOCUS       WP_284425785             549 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Acidovorax sp.
            SUPP1855].
ACCESSION   WP_284425785
VERSION     WP_284425785.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..549
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=59257
     Region          6..401
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mkgngnfrqs mswlhtwcgl vcgwllcaif ltgtlsvfre pitrwmearp vladagagtq
       61 gavphalaqa vrhlaaqapg arfwrielpq apgdalllaw rdgranqmaa lhpvtgavlp
      121 lpwgrategg rhfmsfhyml qwnalgfwvv gwvsmamlva lvsgvvvhrr ifqdfftlrp
      181 gkgqrswmda hnatavltlp flfmivytgl aifytsympw plqaaygsge tayarfqael
      241 hhgegealrr prtgrpaalh dlapllqrar dltgqpprmv vieapgdana tvrvlgprea
      301 epgagqrral lnlvatavfd gvigtvlqvr rpdpdvafas eqvhavmesl hfarfggwpm
      361 kwlyfasgll gtvmvatgtv lfsvkrhrac gnefgratag vyraiealnv aavagigvac
      421 igylhanrll paelpgralw eiraflavwl atllhaalrp prrawveqlg aaaalcvalp
      481 alnawttgqh lgryalagdg qragvelaal afgaalawaa yrtgqgwhga rkavpgvprr
      541 paprggvqg
//
LOCUS       WP_284425896             690 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Acidovorax sp. SUPP1855].
ACCESSION   WP_284425896
VERSION     WP_284425896.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 690)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 690)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..690
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=76616
     Region          21..690
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mpdtssradg psqdphcsss llrlladsvp allayfesst lrcvfanqgy aestghtvea
       61 ilgktvqeai gdsawasiqp qiqqvlrger vqytrkqrvr sgpprmievn liphlhpklg
      121 lmgafvlind ithhweaera vreseermrk fsqateeaiv fhreglvtdf nealtrlmgy
      181 slaegrgrrm ldfvseefrp vteayvregr eepyevtvlh qdghavpvei vgktmpwkgs
      241 dyriavlrdi tarrqaqere aflarhdalt qlpnrttlme rlttvieaaq rtpqaaavlf
      301 idmdhfktvn dslgheagdm llcevarrlv qgvrsvdiva rvggdefvvv lrdaqdrpsa
      361 lavadqllad vcavfhadgt plsvsvsigv smypddgdta aelvrradaa mqqakdsgra
      421 nrqayapgme tpstgvlqhe rllrdailhg afvlhyqpqv rlddgalvgf ealvrwrhpe
      481 rdlvgpidfi afaearglit pigrwvlvea crqmrawhde glpqvpvavn lsalefrqrd
      541 vageiagvlr qtglaprfle ieltesvlmh dadqvrhtld alkalgvrvs iddfgtgyss
      601 laylkrypid klkidrsfvs dtpaneddva ivtaivqmgr slqiqtvaeg vetdaqrdll
      661 ralgchlaqg ylisppmdpr qtrewllkkr
//
LOCUS       WP_284425950             316 aa            linear   BCT 25-DEC-2024
DEFINITION  Gfo/Idh/MocA family oxidoreductase [Acidovorax sp. SUPP1855].
ACCESSION   WP_284425950
VERSION     WP_284425950.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..316
                     /product="Gfo/Idh/MocA family oxidoreductase"
                     /calculated_mol_wt=35912
     Region          1..>199
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
     Region          158..297
                     /region_name="GFO_IDH_MocA_C"
                     /note="Oxidoreductase family, C-terminal alpha/beta
                     domain; cl21649"
                     /db_xref="CDD:451345"
ORIGIN      
        1 mknfaligaa gyiaprhmra ikdtgnhlav aydindsvgi idsispqsdf fteferfaeh
       61 ahqlkrdpvt aldyvsicsp nylhhahiaa glrlgcdvic ekplvptpql mdelarieqe
      121 tgrrvfnilq lrhheailkl rdkvaaapkd tkfdveltyi tsrgkwyles wkgdprksfg
      181 vatnigvhff dmlhfifgkl qnnrihlsee tkaagyleye rarvrwflsi dandlpeevk
      241 gkkptyrnid vsgeqlefse gftdlhttsy reilegrgyg ladarhciet vdvirsasia
      301 adrdervhpf vrrkgy
//
LOCUS       WP_284425974             226 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Acidovorax sp. SUPP1855].
ACCESSION   WP_284425974
VERSION     WP_284425974.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 226)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..226
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=24070
     Region          28..>49
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cl00447"
                     /db_xref="CDD:469772"
     Region          42..214
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mssaaspavi ctvdtvlltl qggalqallv rrdkapyaga walpggyiha qddadaqasa
       61 arvlrekagl qspyleqlat fsglardprg wslavaycal vpgealqgip prqgvklvpv
      121 dalpplpfdh ramvdtalar vrskslyssl pvhlcgdaft lpqlqavyea vlgeplnkvs
      181 frrkmdeldm lepvpglvqg gahrpaqmyr lrpafrkala lssral
//
LOCUS       WP_284426014             393 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Acidovorax sp. SUPP1855].
ACCESSION   WP_284426014
VERSION     WP_284426014.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..393
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=44336
     Region          2..391
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mkltdtklrt lsepgkhsdg lglylevtka ggrywrmkyr fagkekrlaf gvypdvslka
       61 areaagkark llqdhqdpge arkeqkarav henrntfeav aldwlthqsa rwepitmgri
      121 raslendifp tlgsrpmavl kardvmeavk avetrgaadq agrvlqrvka iyrwavther
      181 iesnpmldlv pseilkprtv qhraalaeke lpefmrrlas ydgspsivlg lrmlmltacr
      241 pgevrgarwa eidhaaalwt ipaermkmre ehrvplsrqa ldvldkmeai sggrelvfps
      301 lyypskplse ntfnsalarm gyksiatahg fralfstvan ehgwnpdvie rqlahreqne
      361 iraayhrtty iadrtklmqw wadsldaaap gha
//
LOCUS       WP_284426040             184 aa            linear   BCT 25-DEC-2024
DEFINITION  group I truncated hemoglobin [Acidovorax sp. SUPP1855].
ACCESSION   WP_284426040
VERSION     WP_284426040.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Keppner,A., Maric,D., Correia,M., Koay,T.W., Orlando,I.M.C.,
            Vinogradov,S.N. and Hoogewijs,D.
  TITLE     Lessons from the post-genomic era: Globin diversity beyond oxygen
            binding and transport
  JOURNAL   Redox Biol 37, 101687 (2020)
   PUBMED   32863222
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Bustamante,J.P., Radusky,L., Boechi,L., Estrin,D.A., Ten Have,A.
            and Marti,M.A.
  TITLE     Evolutionary and Functional Relationships in the Truncated
            Hemoglobin Family
  JOURNAL   PLoS Comput Biol 12 (1), e1004701 (2016)
   PUBMED   26788940
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Wajcman,H., Kiger,L. and Marden,M.C.
  TITLE     Structure and function evolution in the superfamily of globins
  JOURNAL   C R Biol 332 (2-3), 273-282 (2009)
   PUBMED   19281958
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Vinogradov,S.N., Hoogewijs,D., Bailly,X., Arredondo-Peter,R.,
            Guertin,M., Gough,J., Dewilde,S., Moens,L. and Vanfleteren,J.R.
  TITLE     Three globin lineages belonging to two structural classes in
            genomes from the three kingdoms of life
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11385-11389 (2005)
   PUBMED   16061809
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Wittenberg,J.B., Bolognesi,M., Wittenberg,B.A. and Guertin,M.
  TITLE     Truncated hemoglobins: a new family of hemoglobins widely
            distributed in bacteria, unicellular eukaryotes, and plants
  JOURNAL   J Biol Chem 277 (2), 871-874 (2002)
   PUBMED   11696555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..184
                     /product="group I truncated hemoglobin"
                     /GO_function="GO:0005344 - oxygen carrier activity
                     [Evidence IEA]"
                     /GO_function="GO:0019825 - oxygen binding [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19054
     Region          71..181
                     /region_name="TrHb1_N"
                     /note="truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 1 (N); cd00454"
                     /db_xref="CDD:381253"
     Site            order(73,78..79,82..83,86,116..117,120,149,152,156,159,
                     170,173)
                     /site_type="other"
                     /note="apolar tunnel"
                     /db_xref="CDD:381253"
     Site            order(87,96,99..100,103,107..108,111..112,114..116,118,
                     126,128..131,134..135,138,140,144..145,148,173,176,180)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381253"
     Site            order(89,92..93,151,154,158..160)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381253"
ORIGIN      
        1 mpipatprfa lppcraprta alalalaaal atalatalpa aaqqpaavat ppgaaafgaa
       61 pataapegly dalggkpgia rimnglvdra fkderigplf ketkpqalkd sltdqicvls
      121 ggpcryegad mksahadlpi rkrdfnvlve llqdamdeqg vaftqqsrll allapmhrdi
      181 itvr
//
LOCUS       WP_284426038             410 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Acidovorax sp. SUPP1855].
ACCESSION   WP_284426038
VERSION     WP_284426038.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132427
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..410
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=44915
     Region          20..387
                     /region_name="PolY_Pol_IV_kappa"
                     /note="DNA Polymerase IV/Kappa; cd03586"
                     /db_xref="CDD:176459"
     Site            order(22..23,25..27,85..86,89,92,146,201)
                     /site_type="active"
                     /db_xref="CDD:176459"
     Site            order(47,101,144,146..147,194,226..232,261,263,286..293,
                     321,344..347,349,378..379,383,386)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176459"
ORIGIN      
        1 madvtapeep aaplprriah ldmdafyasv ellrypqlkg lpavigggrr aqdealvaey
       61 agreskipva afprlkdyvg rgvittatyp arqfgvgsam glmkaarlcp qaillpvdfp
      121 syrrfsrmfk evivsiapvm edrgvdevyi dfthvpggqr dggrslarli qksildatgl
      181 tcsigvapnk llakmasefn kpngisivqe gdletrvwpl acrkingigp kadaklqshg
      241 ihtvgelaar prdwlvrhfg kasgawlhea awgrddrpvv tesepvsmsr ettfdrdlha
      301 vrdraelgri ftdlcervag dlqrkgyvgk tigiklrydd fkiatrdlti dhptqdaati
      361 rraagqclkr vpldkrlrll gvrvgnllte qaareapvar qgpmtpglfd
//
LOCUS       WP_284426061             491 aa            linear   BCT 25-DEC-2024
DEFINITION  rhomboid family protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284426061
VERSION     WP_284426061.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Koonin,E.V., Makarova,K.S., Rogozin,I.B., Davidovic,L.,
            Letellier,M.C. and Pellegrini,L.
  TITLE     The rhomboids: a nearly ubiquitous family of intramembrane serine
            proteases that probably evolved by multiple ancient horizontal gene
            transfers
  JOURNAL   Genome Biol 4 (3), R19 (2003)
   PUBMED   12620104
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10483871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..491
                     /product="rhomboid family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=55109
     Region          126..302
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
     Region          <412..491
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
ORIGIN      
        1 mfyaipldnr ptwrnppwmt vliilvnllv fwgpqrweak avdraaqvyl dsplpgielp
       61 pfvqwlkdsg hrdaeqarrm laahrehall rwmeheegfq krlhaglvvr addpqyadwk
      121 aararyeaal pepftrrwaq syekdapprp vtwitaaflh astghllgnm vflflfgfsv
      181 elalgrwryl afyllgavgg slmagwayag qgsyglgasg avsalmgmya vlyrlrrvrf
      241 fyqlffyfny vtapallllp awianellqh wlsgrgvaym ahlgglltga almwgagllr
      301 rkaieapppe apaepdhgfd ahvaqarqsa qamqferalv qwraaaqlrp rdvpvlsawf
      361 ktaslwpage dfhraarrif rlpgqdaatl dfqhasyrty ldharpsarl vpddmaglar
      421 rfvragqwsd aeklltalhr tapqhaalge lvgmlvtall qsgrreqama wlpqlqqlap
      481 gsaplrlleg r
//
LOCUS       WP_284426046             468 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Acidovorax sp. SUPP1855].
ACCESSION   WP_284426046
VERSION     WP_284426046.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 468)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 468)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 468)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..468
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=51609
     Region          142..459
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mpsakshwpr sfrgrlllvy vagmllscgl vmavvmvlle plerymlqhs vieraesiar
       61 iirfdgaglp lgpdrshide wpfaslseev vlrivdphgv vfyttdgkrf plapqglgfd
      121 pqrkgfvlqr dgvamhaatv plqrtdrlwy vqfaisdriv lllqhsiglp alrkgivatc
      181 ltflvifvia mhltlrrvlk plriaslqaq ritpqslgdr lalgdlpsel vplidafnra
      241 ldrvqlgfqt qqeflanaah elktplslir aqvelgghsg gkdggsghsr yllqdidrma
      301 rqvqqllhla easeqrnyri ercdprsail easdfmdrva ersqvqiall fdegvgpwda
      361 drgalftllk nllenaiqhs pphrvvrlqv hgrgfvvsde gpgvapehlg klferfwrga
      421 srrdegaglg lsicqeivaa hgwtigarng avglevrvth asapgpgq
//
LOCUS       WP_284426124             376 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Acidovorax sp.
            SUPP1855].
ACCESSION   WP_284426124
VERSION     WP_284426124.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..376
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=39951
     Region          34..374
                     /region_name="HisC"
                     /note="Histidinol-phosphate/aromatic aminotransferase or
                     cobyric acid decarboxylase [Amino acid transport and
                     metabolism]; COG0079"
                     /db_xref="CDD:439849"
ORIGIN      
        1 mtspatpaap ppsaldrirp dvramhaytv qpsagllkmd amenpfrlpa nlqaalgerl
       61 galalnrypg driadlkaal adyvgmpdgh aivlgngsde litllalaca qpgtgqratl
      121 lapmpgfvmy plsaqlqgld fvgvpltadf eldepamlaa iarhrpaity iaypnnptat
      181 lwdegavqri idaagaqggi vamdeayqpf asrtwiarmr aepgrnahvl lmrtlskfgl
      241 agvrlgylmg pralvaeidk vrppynvsvl nceaalfale hagvfaaqaa elrheraall
      301 aalrampgve kvwdseanmv llrvadaart yegmkarkvl vknvstmhpl lanclrltvg
      361 naadnaqmla alqasl
//
LOCUS       WP_284426200             414 aa            linear   BCT 25-DEC-2024
DEFINITION  M20 family metallopeptidase [Acidovorax sp. SUPP1855].
ACCESSION   WP_284426200
VERSION     WP_284426200.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Turner,A.J.
  TITLE     Exploring the structure and function of zinc metallopeptidases: old
            enzymes and new discoveries
  JOURNAL   Biochem Soc Trans 31 (Pt 3), 723-727 (2003)
   PUBMED   12773192
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10119591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..414
                     /product="M20 family metallopeptidase"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44324
     Region          15..413
                     /region_name="M20_like"
                     /note="M20 Zn-peptidases include exopeptidases; cd02697"
                     /db_xref="CDD:349869"
ORIGIN      
        1 msstyqslda widqhfdeev rflqalvrvp tdtppgnnap haertaellq afgyeaerhp
       61 vpeaevkayg mesitnlivr rpygegataa ggrtvalnah gdvvppgegw thdpyggeiv
      121 dgkiygrata vsksdfasft falraleava kptkgavelh ftydeefgge lgpgwllrqg
      181 ltrpdlllaa gfsyevvtah ngclqmevtv hgkmahaaip htgvdalqga vailnalyaq
      241 naryqqitsk vdgiehpyln vgrieggtnt nvvpgkvvfk ldrrmipeen paeveaairq
      301 viaeaaagca gitvdikrll lanamqplpg naplvaalqk hgealfgqpi pamgtplytd
      361 vrlygeagip gviygagprt vleshakrad erldledlrr atkvvartlh dllg
//
LOCUS       WP_284426299             309 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284426299
VERSION     WP_284426299.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..309
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=31945
     Region          2..306
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 maggvsaqaw hshpvrvivp fpasgatdlv arvvtqrvsq dlgqqmvvdn rpgaggtiga
       61 aeaakapadg ytlllttsst haisphlmpr laydprkdft pvahvadaas vllvtpslpv
      121 ksvadliaya kahpgqlnya ssgngtivhl naaafsaqag iemthvpykg taqsiadlat
      181 gqvhvlfdsi ptgmphvksg rlralavtsq qrsalapelp tlaesglpgy ssvtwfgvya
      241 pagappalve rihqafakam qapdviasla klgveparps taaqfaamvq adsarwaavi
      301 rerkitleq
//
LOCUS       WP_284426374             346 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284426374
VERSION     WP_284426374.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..346
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=35950
     Region          53..344
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mnpffqpqpr pephrhvshr hasrchalaa ivaavlglav agpaaaqapa ypskpitfvv
       61 pfaagsatdq laraigqsvt tdtkqavvvd nkagasgmia aqavakaapd gytvlittnt
      121 thaanehlyk klsydpvkdf vpvtglgkgg qvlvvnaaap yknvgeliaa akkspgklsf
      181 gsgssssrva gemlkqlagv dilhvpyksn plaitdllgg qidlmitdts tgvpqikagk
      241 lralgystkk rgaqlpdvpt ieeagvkgyd mgywfaayvp agtpapvvar lnellwqatk
      301 saaaqsfydm agseawttts delakfqaae tqkwgqvika agiqpe
//
LOCUS       WP_284426461             383 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Acidovorax sp. SUPP1855].
ACCESSION   WP_284426461
VERSION     WP_284426461.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..383
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40324
     Region          44..244
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mnntstpipt taprlsaevp gghgaggqpp paaapaavpq wlsmagvghe lrtplgalsa
       61 alevialaph pmpiqseaca vaarqtrhls slledlqdvl aaregrmelr rvaldfsela
      121 rqawealvns nggydctqqi apglrvmadp rlmrrvidql lcrackagap gmrmdltvst
      181 qggevrveah glprddmgrp sgtacplnlh vrigvpatla dlladhviql hggriaplad
      241 eegrylalpc laeappppar lrrpkvlial hdgqdrqaag qtlerqgylv legtamqpal
      301 dlllqnvpdl vlasaqpaaa arhlataare agyagcmvav apamhseqea ldtagarrag
      361 fdawaawadw pqvvtdmles rsd
//
LOCUS       WP_284426462             469 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Acidovorax sp.
            SUPP1855].
ACCESSION   WP_284426462
VERSION     WP_284426462.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..469
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51395
     Region          1..466
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mahalvvedd adsarmlasl lhtggftaat asslrdarrq ialqrpdivl ldlqlpdgng
       61 lslceeaell sysevvlitg hasldtsiqa lrlgaadyli kpvdtrrlna vlsrarspst
      121 llaeiqdmrl qwestgrfgh llgrssimre vyeqiacvag tsvsvfvtge sgsgkelvar
      181 slhdlsrrrd gpflavncga ispqliesev fghergsftg adrqhlgffe ranggtlfld
      241 eitemplelq vkllrvletg tfmrvgstea rhtdvrivaa snrelaqavv dgalredlly
      301 rlnvfplhlp plrdrledlp llaqhflddi aareggrktl ttaaldrlae yrwpgnvrel
      361 rnvlqrafvm tqegpvterw lprdlvpsqp qlpiqplapq qpevalptng aatptelrlp
      421 lgsslaever alilatfahc gqrreqtaam lgismktlyn rlkeygasa
//
LOCUS       WP_284426490             343 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284426490
VERSION     WP_284426490.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..343
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=35754
     Region          49..341
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 miskascaal raflsrpvsg hrarpllaag laglalwgag ahaapaaefp dkpvrivipf
       61 pagaaadtam rvvarkmseq wrqpviidnr pgaagfqava sappdghtll mgagsgmvta
      121 pllsskltyn psrdfvpvgr vvvnvpiltt hpslkvrtvq elialarkdp galnystsgn
      181 gspghlsmel fqaatgtrmv qipykgggpa vnelaggyvq lginavpsva aqikagklvp
      241 lavasakrsr afpevptmae aglknfeydi wyalfapagt padrvqnisk vlgaalndae
      301 vtallvaqga epapttpqel arfmqedtar warlvkdrnl kld
//
LOCUS       WP_284426585              89 aa            linear   BCT 25-DEC-2024
DEFINITION  BolA family protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284426585
VERSION     WP_284426585.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..89
                     /product="BolA family protein"
                     /calculated_mol_wt=9429
     Region          7..87
                     /region_name="BolA"
                     /note="DNA-binding global transcriptional regulator BolA,
                     affects cell shape, cell division and biofilm formation
                     [Transcription, Signal transduction mechanisms]; COG0271"
                     /db_xref="CDD:440041"
ORIGIN      
        1 mtvlaitaea maarlqerln psalqvldes aahaghvgan gtgfgthfrv rissplftgr
       61 prvaqhrlvy dalqefidqg ahaiaievl
//
LOCUS       WP_284426637             490 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284426637
VERSION     WP_284426637.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 490)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..490
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=54870
     Region          9..486
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mehtfssglv wfrrdlrsnd haalyhalrq caqvhcafvf dreildalpr adrrvefire
       61 slveldealr alskdphggl ivrqaiahqd ipalaqaldv qavfanhdde plalerdarv
      121 rgaldgmgkr lltfkdhsif eraevltqsg tpytvftpyk nawlrkaddf ylssypverh
      181 aarlaprpag lrrgvpslqs lgfeptglks lhlptgmqga qalfedflgr idhygeardf
      241 pavkgpsyls vhlrfgtlsp rvaaraaher srkgsagaat wlseliwrdf yfqilahhph
      301 vagasfkpay daiewesgth akalfaawce grtgyplvda amaqinqtgy mhnrlrmvva
      361 sfltkdlgld wrwgeryfae klndfdlsan nggwqwasss gcdaqpyfri fnpvsqsekf
      421 drdgkfirry lpqlaglqgk alhapwtaap lelqaagvvl gkdyprpvvd hdearqrtla
      481 rygvvkaakd
//
LOCUS       WP_284426803             339 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284426803
VERSION     WP_284426803.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..339
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=36029
     Region          30..337
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mpllfpithr atrriaaala cvaattfsfa ahaeaagwpr qpitlilgfp agsgidvvar
       61 avqeplgqkl gqpividyks gaagniasef vararpdgyt lafgtaathg snaalypklp
      121 fdvendfvpv gplidvsnvl tinpdvidak tlqefvalvk ahpgkynyas tgngagthma
      181 faefnarlgl dmvhvpykgg peaitsvvrg etccimnqvq tvlphykagk vrllgvttak
      241 pvaavkevpt iassglpgtq gfdssiwfgl fapkgtdaav vqklntalrq vleqpevrer
      301 fesqgnavri etpaqfrqtv htdrakwaqv vkdaririd
//
LOCUS       WP_284426825             738 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein [Acidovorax sp.
            SUPP1855].
ACCESSION   WP_284426825
VERSION     WP_284426825.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 738)
  AUTHORS   Porat,A., Cho,S.H. and Beckwith,J.
  TITLE     The unusual transmembrane electron transporter DsbD and its
            homologues: a bacterial family of disulfide reductases
  JOURNAL   Res Microbiol 155 (8), 617-622 (2004)
   PUBMED   15380548
REFERENCE   4  (residues 1 to 738)
  AUTHORS   Kimball,R.A., Martin,L. and Saier,M.H. Jr.
  TITLE     Reversing transmembrane electron flow: the DsbD and DsbB protein
            families
  JOURNAL   J Mol Microbiol Biotechnol 5 (3), 133-149 (2003)
   PUBMED   12766342
REFERENCE   5  (residues 1 to 738)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   6  (residues 1 to 738)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   7  (residues 1 to 738)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   8  (residues 1 to 738)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   9  (residues 1 to 738)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12109673
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..738
                     /product="protein-disulfide reductase DsbD family protein"
                     /EC_number="1.8.-.-"
                     /EC_number="1.8.1.8"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=76146
     Region          61..174
                     /region_name="DsbC"
                     /note="Disulphide bond corrector protein DsbC; pfam11412"
                     /db_xref="CDD:463273"
     Region          356..736
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 mshrllqrll palfliaasa fhigagaqsg tkttgsgsgs stvttphvqa elvahapegv
       61 apgkplwlgl sithqpewht ywmnsgdsgl ptqlewqvpa gieagdiawp vprkipignl
      121 anygyegtvl lpvpmavsda fapgplarta tfhlraswlv crkecipeeg dftlqlpirs
      181 ttalsagafd aaqqahpqpl papaagapas sarvdggaia ltvaglpaal rgkaleffpe
      241 ttgvietaad wtqawqgdvw tarvplspqr sasptpmpvv lahagqgwra elpltggwpp
      301 laamasispa leaalranaa qgggapaapt vtaaplgtll aalagallgg lilnlmpcvf
      361 pvlaikvvgf aqhanhrrah rigglaytag vvlsfmalga lmlalraage avgwgfqlqs
      421 pgvvallaal ftviglnlag vfefgrflps svaslqarhp avdafltgvl avavaspcta
      481 pfmgaslglt atlpaaqala vfgalglgla lpylaaswvp avaralprpg awmdtlrrfm
      541 afpmfatvvw lvwvlgqqsg idgaaallal lvtlsmavwa ltlagrtrwa iapisialla
      601 ylttawapkv leitpspava aaaataggwr pwqaglpeel vakgqpvfvd ytaawcvtcq
      661 ynkkttlahe dvlkdfaakn vallradwtr rdpaitaala qlgrsgvpvy vlqapgrppv
      721 vlseilgvqe vraaiagl
//
LOCUS       WP_284426857             300 aa            linear   BCT 25-DEC-2024
DEFINITION  amidohydrolase family protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284426857
VERSION     WP_284426857.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..300
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32111
     Region          27..299
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mhlpaipapv phsagvsrps rllpamacds hmhifdprfa psvhwkrlpp dapvaayrrl
       61 qrrlgtarsv vvtpstygtd nactldaleq lgdtargvav vgagvsdael ghlaarrvrg
      121 lrvnfvspqs wgattpemlt tlasrvarhp hcggwhiqvf adadqivalr pvlqalpvpl
      181 vidhlgridp aegpsaqayg vlhrlldggn twvklsgaym rskargptyd dtlplgralv
      241 qaaperlvwg sdwphttepp gtvndadlvd llhawtgsqa aamdrilvdn paqlygfeav
//
LOCUS       WP_284426858             319 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284426858
VERSION     WP_284426858.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..319
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33322
     Region          24..317
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mrafvispli aacafaatva qaafpdrpit ivvpyapgga adavarvlat rmgarlgasv
       61 ivdnkagasg tigasyvaka tadgytmlyd atpysinphl fpkmpyasta lqplslvlla
      121 pnalivkads pfknvndlia kakaepgkln fasggsgtvq rlaaelfrqk lqldmvhvpy
      181 ksggpaiadv mggqvdfmfg tiaasyplvs ggklralavs aperskrlpd vptvaetvip
      241 gyeayewngv flpagtpepv aaklqqalve vlkedevkqr ladlgaqaig stpaefvtfl
      301 kkedakwgev vrkgdikld
//
LOCUS       WP_284426950             318 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284426950
VERSION     WP_284426950.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..318
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=33063
     Region          1..317
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mkpftyeraa svqaaaaaaa gnpqarfiag gtnlldlmkl qieapthlid inglgldrie
       61 plpegglrig alvrntdlaa hagvrrdygl lsrallagas gqlrnkatta gnllqrtrcp
      121 yfydtnmpcn krqpgagcaa iggvtrqhav vgaseaclat hpsdmavamr aldavvetvr
      181 adgqprripi adfhrlpgnt phietaldag efitavtlpa paggthiyrk vrdrssyafa
      241 lisvaavlqk dgtgrvalgg vahkpwrmas adaalpqgaq aataqllgaa rpthenafkv
      301 alvertlagv laeakgqs
//
LOCUS       WP_284427011             234 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Acidovorax sp.
            SUPP1855].
ACCESSION   WP_284427011
VERSION     WP_284427011.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 234)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..234
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25761
     Region          1..>224
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrradrlfqi vqlirgrrls tadflaqrle vsartiyrdv adlqhqgvpi egeagvgyrl
       61 gagfdlpplm fsqgeanalv aaarlaqswl dtglageves vlgkilsvlp paaraaaeaq
      121 alyapavavd prtqallrpl reavqsrhvv rlhyadeqgr pserrvrplg cfywgkvwtl
      181 stwcelrddf rgfrvdrivs ldvlderftv epgrsladml rhvwgrpgvg pggg
//
LOCUS       WP_284427040             613 aa            linear   BCT 25-DEC-2024
DEFINITION  autotransporter assembly complex protein TamA [Acidovorax sp.
            SUPP1855].
ACCESSION   WP_284427040
VERSION     WP_284427040.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..613
                     /product="autotransporter assembly complex protein TamA"
                     /GO_component="GO:0097347 - TAM protein secretion complex
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=66500
     Region          32..613
                     /region_name="TamA"
                     /note="Outer membrane translocation and assembly module
                     TamA [Cell wall/membrane/envelope biogenesis]; COG0729"
                     /db_xref="CDD:440493"
ORIGIN      
        1 mllsslvalq gcsllpgake gtvdnntiqs dagagtgpda fslevrapda vreyltrhme
       61 lqrfrqlpdl qsseitrllg aaesnarell gtlgyfsptl titmqetpga tgaprtitve
      121 vepgpqtrva radidftgae adspqfanrr arvqrswsla pgqpftqdaw dgaksqglrq
      181 lqatryptas iaksraeida drneaqlgvt ydpgppyrfg alrvqggery sadgarriar
      241 lptgadysea qlldaqmrla ssgyydavfl sletdgtdpq aapvvaqvre aplqkvvfgv
      301 glstdsgprl svdhihnqlp gigwravskv svdrknklls tdwtdlpged gwrwftgaqv
      361 qrettgdyev nssrlrggrs kstdhidrsy flqhdtaksq gtdappssaa isanygwtgr
      421 yfnnttnptr gfglaaelgv gttlrperdp fvraylrwqs fypmgrvdmg egvtrtsrla
      481 lraeggavla rraaeipvtt lfltggdttv rgygyreiga rtsngqlygg ryltvasaew
      541 qrpiefrgnr tdfetamfid agavadragd ldprvgvgag lrwrspvgpl qadvaygvqa
      601 kqlrlhlrlg fsf
//
LOCUS       WP_284427129             378 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Acidovorax sp. SUPP1855].
ACCESSION   WP_284427129
VERSION     WP_284427129.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..378
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41396
     Region          1..371
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 msalavvtvi aialamwfrf aisdavalgq lppearqeml qlradphhna srlwqlfaqy
       61 ydvvdflpgi anrdwwllaa mvigaipviv lcglyvsrpl srqftmvaha arrvsegdfs
      121 aratvvtdap qeliglavdf ndmtarlqry erevsessam vahelrtpln aamgrlqgml
      181 dqvfpcdesq llmvhrqleq lnrlvgdlhl lslaragqls lehedflled liqerlawas
      241 qrlnavglap qvsiprgtrl tgdrdrigqv llilvdnair yaasgqqlsi dvqasngdih
      301 lsvcdrgpgv eaeslarmte rfwraehsrd rhlggsglgl siacaiceah ggslemvgrs
      361 ggglcarvrl phppqras
//
LOCUS       WP_284427139             156 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Acidovorax sp. SUPP1855].
ACCESSION   WP_284427139
VERSION     WP_284427139.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..156
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17005
     Region          18..153
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mtvptvstpl rrlpeprsay svfrtittrw adndayghvn nvvyyswfdt avnaylierg
       61 aldihageti glvvetqchy faplafpqtv eagirvahvg rssvryevgl faegapesaa
      121 gghfvhvyvg redrrpralp qalldalapl riavgt
//
LOCUS       WP_284427204             375 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284427204
VERSION     WP_284427204.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10530473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..375
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=41223
     Region          148..369
                     /region_name="VWA_CoxE"
                     /note="VWA domain containing CoxE-like protein; pfam05762"
                     /db_xref="CDD:399053"
     Site            order(219,221,223,278,304)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238739"
ORIGIN      
        1 mtpltipdpl qrwrlllgep aepacgalgd aaqaadaale wlygrdsdra ergersaglg
       61 psalstpdwi ntihtlfpke vierlerdav erygidevvt nlevleriep sesllravlh
      121 tkhlmnpqvl aaarrlvaev vrrimeklat evrqafsgsr drrrlsrmkv arnfdfrrtl
      181 qanlrrwdaa rgklyverpi fisrtrrhae pwdivllidq sgsmvdsvih savmaaclwq
      241 lpgmrtrlva fdtqvvdlta dvsdpvellm kvqlgggtdi aravayaqsl vanpartivv
      301 lvsdfyeggd pgelvrrvka ltgagtkvlg laaldaqaep aydremaarl vkegaqvgam
      361 tpgelagwla ekvqa
//
LOCUS       WP_284427220             484 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Acidovorax sp. SUPP1855].
ACCESSION   WP_284427220
VERSION     WP_284427220.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..484
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52584
     Region          28..465
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mkraitllgl lacvhagaqt plsaptplpp saqdtqaqrp pstgvrqftl kngmqllvqp
       61 drraptavhm vwlrvgamde vdgtsgvaha lehmmfkgsk tvppgefsrr vaalggqena
      121 ftsrdytgyy qqipanrled vmkleadrfa nnqwpdaefk reievvkeer rmrtedqpra
      181 alieqlyaat fiaspyrrpv vgwmsdldam taddvrafhr qwyvpanavv vvagdvdpdk
      241 vrvlaekyyg ripvravpar kprvepvqqg irriaykapa eqayvalafr apsitrlenm
      301 adsdrdalsl lvlsavlsgy dgarlerals qgpdrvadss dssasvvgrg psvflltgvp
      361 apgktpqqve dalraevari aregvseael arvktqwaas tiyqrdslqs qasdlgsnwv
      421 qglppdadtr liallravtp aqvqsvaary fgddqltvgt llpqpmapga krappaagad
      481 grmh
//
LOCUS       WP_284427243             444 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Acidovorax sp. SUPP1855].
ACCESSION   WP_284427243
VERSION     WP_284427243.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..444
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47327
     Region          21..441
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 maaraclafa galclahpaw allpiqhwte psgarvwlve spaipmvdvq vdfdagarrd
       61 paaqaglasa vaamsskgvr aqgdepamde nalgeawadl gasfeaaadr dglsfslrsl
      121 tepdlldraa rlaarqlaqp sfpqdiwqre rsrwaaalke aetrpgtaaa kafgsavygs
      181 hpygqrttpe tlgrieiadm qayhgryvet crarvsivga vtrpqaqalv atllsqmpar
      241 dpatcqplpp vpevqalaap vqqdipfasa qahvligqpg farrdpdfla llvgnhilgg
      301 ggftslltse vrekrglsys vysqfspgln tgvflvglqt rpdqaaeavk vsrdvlarfv
      361 aqgpteaqlk aakdnliggf alridsnrkl lanvvniawn dlpldylehw tdrvqaltaa
      421 dvraamarkl qpdrmvtvvv ggqp
//
LOCUS       WP_284427342             479 aa            linear   BCT 25-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Acidovorax sp.
            SUPP1855].
ACCESSION   WP_284427342
VERSION     WP_284427342.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..479
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=50738
     Region          1..478
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mfdllifggt vvdgsgaarr qadvgiaggr ilavgdlsaq parqrhdavg rivcpgfidv
       61 hthddrlllt spagphpklt qgvttvvtgn cgislaplls netppapldl lgaddwrydr
      121 fgdyldalea agpalnaacl vghstlrvrh vpdlnrpata peaermardl adaldagafg
      181 lstglyyppa raataeevie vgaplsaaqg litmhirdea daiddalrea lhigqalgvs
      241 tvlshhklig qrnhgrsvnt lamvdtaals qpvcmdcypy nasstmllas rvgqsrevlv
      301 twsvgdpsaa gkslfalare rgcspeslve plspagavyf amheddvrri lghpltmvgs
      361 dglahdavph prlwgtfprv lghyardqrl fsletavhkm tglsarrfgl rdrgliaqdh
      421 aadivvfdet ciadratfeq ptapsagida vfingqlaca hghtvnahag qvlrrqrsf
//
LOCUS       WP_284427387             501 aa            linear   BCT 25-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284427387
VERSION     WP_284427387.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..501
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=52447
     Region          14..497
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mllfdprsia vpaghfiggr lvpdagriav lrpsdgqwha dlpladaatv daavqdawqa
       61 wrttdwarra prerarvlrr wadmieadgp qlapleavcs trpvrdaaaw dvpftaeglr
      121 ffaeyadklg gevaatrhdh lgmvvaepyg vvgaitpwnf plvmmswkvg aalaagnavv
      181 lkpsemtpys avrlaqlave agvppglfnv vqgdgrttgd altrhpriak mtftgstrtg
      241 aaimascalq gpkpvtlelg gkspqlvfdd apdvdrlagl iagaitgnag qvcvagsrli
      301 vqrgiapelv erigarfaal rpgatwddta tlppiisapq aarildiver ardagaqlrc
      361 ggglfddvag gvaagapgga yfqptllegv aadspavqee ifgpvltvqt fdteeeglal
      421 aahahyglaa gvhtadigra lramrgisag tvwinrygrs adfviptggy hqsgigkdlg
      481 rqaveanlrf ksvlidfaaa h
//
LOCUS       WP_284427470             334 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284427470
VERSION     WP_284427470.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..334
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=35460
     Region          7..332
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mgiqynrrnl lqelaalggt sllgqaaaqt gkaawptkpi rlivpfnagg atdiiartvg
       61 ealakrvgqp vvvdnrggaa gilgtdavtk aapdghtllv slstsmlinq flytklpydp
      121 qkditpitqi aaapvtlvvh psvpasnmke llayvkahkg klsygswgvg syahlagaym
      181 sktmdadmth vaykgeapmi qeliggqlql cfssalntkp fidagrlnai gvtgkqrmdi
      241 lptlpsiyeq gvpddayaif gwvavgapag lpkeivdqly ghlreiakdp kvlertvgag
      301 fmplmnspea frenyqrdmp vwkalvdeag akld
//
LOCUS       WP_284427524             438 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284427524
VERSION     WP_284427524.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..438
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=47971
     Region          140..407
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mkpsdvfarl sgvaafmvpg lalwlrsgys wgavvlllcs latagvwlrr ppgreawwlf
       61 asivamgfvw aldfdpaqgg wsnldrpsky llalpclfyl layppravwl wwglavgacg
      121 agligiyqtg vlhllrangy tnaiqfggls lllglmcsaa llvqwsrwap wqrvgwvvci
      181 llgfegslls esrggwlvlp lalpvcawlq arcgqrrlam igaalilagm aglmalkahd
      241 vrsrvdearq eitqyeskgd aassvgqrla hwklawsmgl drpltgwgry gyeaekqrrv
      301 aagqahpfvl rfshahnevl difakrglpg vavlllfyav plalfwptrr rvcrttehgt
      361 mdpqvlclrm vgvllpiayi gfgltqvflg hnsgtmfylf mcmlvlailq grerdalrrr
      421 aaqatvppgp grlaaass
//
LOCUS       WP_284427597             376 aa            linear   BCT 25-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Acidovorax sp. SUPP1855].
ACCESSION   WP_284427597
VERSION     WP_284427597.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..376
                     /product="MlaE family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40824
     Region          130..371
                     /region_name="MlaE"
                     /note="Permease subunit MlaE of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG0767"
                     /db_xref="CDD:440530"
ORIGIN      
        1 mteddsqpri trddtpegpc avlhgrwgaa elgtrrhwra lsaqlsetrg gpaigwdlrs
       61 lqwldhvgaq llwnhwgrdw perlalddgq rdmlervaef sttrppdtpw rlaeqvdrlg
      121 vqvlhalshm rhllelvgql fidifraars prrapwrdms ghlyrmgata mpitaivgfl
      181 igvvlaylms lqlrqfgaes fivnilgisl irelgpmlaa ilvagrsgsa itaqigvmrv
      241 teeldamrvm giphgfrlvm pravalavam pliavwttlc alaggmlaad lalgvspayf
      301 vqalpnavsf pnlvmavaks vvfgvsiali gchwglrvkp ntqslgegtt asvvssitmv
      361 iivdalfaia fknlgi
//
LOCUS       WP_284427723             464 aa            linear   BCT 25-DEC-2024
DEFINITION  class II fumarate hydratase [Acidovorax sp. SUPP1855].
ACCESSION   WP_284427723
VERSION     WP_284427723.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Woods,S.A., Schwartzbach,S.D. and Guest,J.R.
  TITLE     Two biochemically distinct classes of fumarase in Escherichia coli
  JOURNAL   Biochim Biophys Acta 954 (1), 14-26 (1988)
   PUBMED   3282546
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..464
                     /product="class II fumarate hydratase"
                     /EC_number="4.2.1.2"
                     /GO_component="GO:0045239 - tricarboxylic acid cycle
                     heteromeric enzyme complex [Evidence IEA]"
                     /GO_function="GO:0004333 - fumarate hydratase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006099 - tricarboxylic acid cycle
                     [Evidence IEA]"
                     /GO_process="GO:0006106 - fumarate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48972
     Region          4..462
                     /region_name="FumC"
                     /note="Fumarate hydratase class II [Energy production and
                     conversion]; COG0114"
                     /db_xref="CDD:439884"
ORIGIN      
        1 mgaatrtehd afgpveipad rlwgaqtqra lavfdigeer fpacllhtfg lqkqaaaran
       61 rrlgtldalr adaieaaaee lrtglldahf pltiwqtgsg tqtnmnanev lanranqrlg
      121 qppgtrspvh pndhvnasqs sndsfptvmh latalelrdr lvpalallqs rlqeratafa
      181 gvlkiarthl mdavpmtlgq gfdafarqvg hgidrlhatl prlcllaqgg taagtglnap
      241 pgfdvafcee asalagmaft pnpskfegmg ahdalvevsg alnvvaasla kiandlrllg
      301 sgprcglgel ripddgltss impgkrnpti aevvaqaawq vmgnhttitl agasghfeln
      361 vakpvliynl lqsirvlads arvfseqlvq gieadterla anvdnallla talnpvlgyd
      421 rvaritream ergitpkaaa valgfltgde ydrrvdaram agpg
//
LOCUS       WP_284427752             346 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284427752
VERSION     WP_284427752.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..346
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=35664
     Region          47..344
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mvpiasraha hpgprtrttt grralvvsaa lalcglaapl aavhaadayp tkpvtllvpy
       61 paggandava rlvgqklgda lkqpmvidnr pgagttigtt vaakaapdgy tlvlgslash
      121 avsphlyakp gydavadfap igligvvpmv lvvaqdspyt svralveaar kqpgalnygs
      181 sgngsplhla aelfkqaaqv qinhvpykgg nahtmdlmgg rldmildtlt sasplikggk
      241 vralavaapa rlpelpdvpt faeagypgfe vnawyalyap aktskdvvat lntalnavlr
      301 qpevlermaa lgvrpqpgtp qalarftqde lgrygkviqa ngirid
//
LOCUS       WP_284427867             104 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Acidovorax sp. SUPP1855].
ACCESSION   WP_284427867
VERSION     WP_284427867.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 104)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 104)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..104
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11467
     Region          12..100
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdptpidper lrqaasqavs alktlanedr llllcqlsqg eqcvsdlqar lgiqqptlsq
       61 qlgvlrtqgv vetrregkni hyrvadaall eilavlyrly cpke
//
LOCUS       WP_284427956             278 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP1855].
ACCESSION   WP_284427956
VERSION     WP_284427956.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP1855
  ORGANISM  Acidovorax sp. SUPP1855
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Acidovorax sp. SUPP1855"
                     /db_xref="taxon:431774"
     Protein         1..278
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=29490
     Region          9..273
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mrishpavls rrrlvlsgsa aavsllpwri gsaqstwptk plrlvvpfap ggsseivara
       61 vaaemsktig qnvfvdnkpg aagniamqev anstdehtli lghigtlavn pyifpklayd
      121 anrdfapitl vskvpsrgtg pmltdlmagr lqaaavgapa llpfikagkl rciatgtaqr
      181 lpqlpdvptv aeqgfkgfem tqwyglmaps kwpkahlakl eteavkaars plvkeklsqe
      241 talavgntsa efdafikseq arwkpviara qikpegmg
//
LOCUS       WP_284428074             267 aa            linear   BCT 25-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Acidovorax sp.
            SUPP2522].
ACCESSION   WP_284428074
VERSION     WP_284428074.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2522
  ORGANISM  Acidovorax sp. SUPP2522
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Acidovorax sp. SUPP2522"
                     /db_xref="taxon:511900"
     Protein         1..267
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27742
     Region          13..251
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mpaseaawsg sgdlntaivw vhaaqrivvl tgagvsaesg vptfrdaqtg lwaqvrpedm
       61 asepgfradp agvwawyehr rallqgvqpn aghgaladfa rrhpgrltlv tqnvdglhqm
      121 agsegvlclh gelrgnrwld dprgccdlah aeagapprca tcgnlvrpav vwfgeslpid
      181 ilgqaeeavs acdlmlvvgt agavypaagl ahmarrigar vvivnpapse ldgtahavlr
      241 gpsaevlpll lgrdrpagdt ppaaapr
//
LOCUS       WP_284428154             290 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP2522].
ACCESSION   WP_284428154
VERSION     WP_284428154.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2522
  ORGANISM  Acidovorax sp. SUPP2522
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Acidovorax sp. SUPP2522"
                     /db_xref="taxon:511900"
     Protein         1..290
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=29953
     Region          3..288
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mspwaaggtn dllcrllare agrllgqpmv venkpgasgv igttavarak adgytltlgs
       61 tpgyataqal ypqlpydplr dfapvigvat vpnvlvvpps lpvhsvreli ayvkarpgql
      121 syssvgqgst qhlcaklfer mtgtemihvp ykgtapalqd llagritlaf enmppllpqi
      181 rsgaltalav tsatrvsqlp qvptvaesgl peftasvwya vfapagvpas imarlqeaft
      241 salalsevas qlaglglttl asdaaatraf vqadaakwgg iiraagikpe
//
LOCUS       WP_284428198             376 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Acidovorax sp. SUPP2522].
ACCESSION   WP_284428198
VERSION     WP_284428198.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP2522
  ORGANISM  Acidovorax sp. SUPP2522
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Acidovorax sp. SUPP2522"
                     /db_xref="taxon:511900"
     Protein         1..376
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39441
     Region          6..369
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mergsdvliv gggiqgmsaa lqlarrgigv cvlekdyvgr hasgvnaggv rtlgrhlsel
       61 plsikakslw ltaqdwlddd cgfrpvgqir vaetqaafaq lqtrsslvss lgleyrehvi
      121 daselydrlp altphcvggl fvaddgyanp yrtvlamkha avragavvee rsavahlgyk
      181 dggwsaklqd grtfradvll ncagawgqri aamlgdeval kpngsmlmit arlppmvgpv
      241 vgaagrslsf kqfpngtvli ggghrapvdl dtnqanvllp giakaaetai tlfpfmasah
      301 avrfwsgieg fmddglpvig pslgspkafh afgfsahgfq lapavgevma dlvsqvepat
      361 pieafsvgrq prspsa
//
LOCUS       WP_284428401             379 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Acidovorax sp. SUPP950].
ACCESSION   WP_284428401
VERSION     WP_284428401.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..379
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39912
     Region          1..373
                     /region_name="FucP"
                     /note="Fucose permease [Carbohydrate transport and
                     metabolism]; COG0738"
                     /db_xref="CDD:440501"
ORIGIN      
        1 mmclaialnf lpvylttfsd tfgkqgglta eqlgripaim flsfiiailv tgpladrgda
       61 rriilfglit ttaglvlvgf apsyafllfa vavmgfgagv ldmilspivv alqperrsaa
      121 mnwlhaffcv gavgavlias iglkwdvswr mvalgitiap ivtfllflgl rlppliqeda
      181 qreampqlik qpyfiaclia iflggatetg lsqwlptyae qglgyskevg gfalagfsvg
      241 malgrmaaal lheriapisl mlgccavtig lffiisfpps pavaiaasia agfsgsclwp
      301 tmlaitaday prggatmfgv ltafgnagcs lipwlvgiii eyseihigll avalcpagmi
      361 glllwmsrrs rrqapalah
//
LOCUS       WP_284428427             373 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Acidovorax sp. SUPP950].
ACCESSION   WP_284428427
VERSION     WP_284428427.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..373
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40315
     Region          152..370
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mrlaqfirha reeilaesfa yatripalqg saasvlrnhl plvldaiald leqpqsreqs
       61 idkslghaap paeesaaqsh gtlrarigld ieqlvaeyrv irscvlrlwm esgqptafam
      121 ddtvrfneai dqavaesvaf haaevakwrh iflgvlghdl rgplnamllt aqllervgsq
      181 npeqatylvg allrngrhln vlldslleyn katlgvgtpl hrqavdlgaa cqeelemlqq
      241 afpkrrirwq itgdargdfd psrvrqavsn lvsnaaqhsp egsevavivv gqaaaveitt
      301 enlsdpiape vldtlfdplr rnaspsgass ghlglglfiv reiakahqge vtastadgvi
      361 rfkmvlpkss kaa
//
LOCUS       WP_284428458             331 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284428458
VERSION     WP_284428458.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..331
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34060
     Region          20..329
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mqrrtfiaaa aaaaaagsfi glpvfaqgtw ptgktitylv pfaaggttdt lgrlisqqlg
       61 talgttvvvd nkggaggsvg seiaaraapd gytllggtis shainvslyp klgydpvksf
      121 apvtligtnp vvlvvaassp yktlkdvlda argksgglss asagtgtsqh lalellayks
      181 gvkfthvpyk gsgpaiqdvi ggqvdmmfdt tvvaaphiqs gklraiavts akrlgsmpdv
      241 ptvaesglkd ladfevqswq aifvpagtpe pvvtrlhtei rkilaqpdmq trlksfgmep
      301 admttaqiat fqkaevakwa qvikaanikv d
//
LOCUS       WP_284428459             366 aa            linear   BCT 25-DEC-2024
DEFINITION  lactonase family protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284428459
VERSION     WP_284428459.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..366
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=38505
     Region          32..363
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 maisssflra valapvaaaa lmaasgaasa atwvyvsnad sqdisvyeld raagqlqpve
       61 tvtvggqamp mavspnkrql yvalrsqpfr vvtlaidpas grlkkqgeaa ladsmanidt
      121 datgrwlfaa sypghkitvn sidkdglvga vqqliptapn ahaihadaan ryvfatslgg
      181 dhlsswrfda ttgkltanep altavapeka gprhfvwdka qrymyvvdel daalhvmayd
      241 aergtlrevq rtttlppgft gkpwaadlhl spdgrtlyas ertsstlssf rvdaatgqle
      301 plgqvpteks prgfavdasg rfliaagqds hsvslhpidp atgvpgtptr vaagknpnwv
      361 eivdlp
//
LOCUS       WP_284428477             453 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Acidovorax sp. SUPP950].
ACCESSION   WP_284428477
VERSION     WP_284428477.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..453
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=48304
     Region          26..450
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mpatasatpa laehatqara agpadrrrhv vvigagivgt vcaiemlrsg rqvtllnpha
       61 pageeatsyg nagwlsshsi lppagpgmwk qvpgylldpq gpltvrwgyl pralpwlwrf
      121 lrsgrtpahv artahalrql lrdapalhar lsgeagvphl vaqrgllhay rsradfeada
      181 lgwrlrgeeg iafetvegas lrvqepdlap aygfgvrvae aghcanpgay laalvahaqs
      241 lgarwvtgqa tglhieagrl havrtdqgdl pcqgaviaag aysrplalaa gdrvwldter
      301 gyhamldvqa ragerapagp rtstmvmdrk livhqmehgl rvagqveiag lhaapdwrra
      361 rillghvfdl ypslpraale dgarfwmgrr pstsdglpci gpasacadvi hayghghvgl
      421 gasartgrvv aqcmdgqppe idlapfrpqr wrr
//
LOCUS       WP_284428546             154 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: SixA phosphatase family protein [unclassified
            Acidovorax].
ACCESSION   WP_284428546
VERSION     WP_284428546.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..154
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=17088
     Region          4..151
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mmdlilwrha eaeelreged dldrpltarg ekqaarmaaw ldrqlpdglr vlssparrte
       61 atakalgrky klraellpgg tpqellelaq wpksrgavlv vghqpvlgqa vasllalqap
      121 ecairkgsvw wlrqrqrpet tetillavqs pdfl
//
LOCUS       WP_284428746             736 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Acidovorax sp. SUPP950].
ACCESSION   WP_284428746
VERSION     WP_284428746.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 736)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..736
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=78189
     Region          70..736
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mnqhtpiala valalatfgl qanaqatats adaptlptvt vgasadasaq glspaypggq
       61 varggragil gtrdametpf sitsytneli qdrqarsvge vlqndagvrl argfgnfqet
      121 yfirgfllds ddvaynglys llprqyiate lfervellrg asaflngaap ngggiggain
      181 llpkrapnep lsrvtvgtgs ggygqvstdi arrfgpdnst girlnaayrd gdtavdheks
      241 qlglvsvgld wrsrdvrlsg digwqdnklk gtrtnvtlng ananfipaap dasanfsqpw
      301 tysnerdlfg tfrgevdisp dvtawgawgl rrseesnsla nlsvsnsttg egstyrfdnt
      361 rkdrvntgel gvrgkartgs vghewvasas yfdaekdnay afdflntrpg slyaytpyaq
      421 pafsanagyg gtlaspnltg rtrmtsfavg dtmsfvqdtv lvtlglrhqk ldvadyaygt
      481 saltnryeqs rtsplasavf kaskqlslya nyveslskge tapatangtp vvnrgeqlsp
      541 yvakqkeigl kydagriggs lalfsttkpr aivnaanvfa ssgkdrhqgv elnvygeatr
      601 glrvlggmtw ldakqretgn aalngnrvig vprlqanlga ewdvpgaqgl aldarvvrtg
      661 atyandantl rvpawtrldl gvryatewsg rlvtlrarvd natdrnywas aggypgsgyl
      721 vvaaprtftl sasvdf
//
LOCUS       WP_284428818             405 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Acidovorax sp. SUPP950].
ACCESSION   WP_284428818
VERSION     WP_284428818.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..405
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42376
     Region          16..390
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 msrtgsagtg aeshwdaivl gggmagasca walaqhrrvl llereahcgy hatgrsaalf
       61 seyfgnrtvr altaasrpff eappvgfasv plvaprgvva latqddvdcg ridtalaagh
      121 hahqparvig ldaalsrcpv idprpyrcav wrpsvmdidv dalhqsylrg iraaggrvqt
      181 aagvewaegd asghwtvhtv agrfhtpclv naagawadea arqagvatid lvpkrrtavi
      241 vdlpdgmpgq palaswpmvt dladtfyfkp eagrllvsps detpmppcdv qpeewdvava
      301 vdrlqqattl avrrvahrwa glrsfvadgs pvlgaagnap gffwaaalgg ygiqiapavg
      361 qalaslvltg glpdhfverg lsaaalspdr ptlaeapcer lealp
//
LOCUS       WP_284428821             337 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Acidovorax sp.
            SUPP950].
ACCESSION   WP_284428821
VERSION     WP_284428821.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..337
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35530
     Region          49..319
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 msatgahpaa vlmgaqasam rlpvcdhysg vearmrksle lqaamaaelg rcvfdvtldc
       61 edgapvgrer ehaalvahla rtaspgarva arvhavdhpa faedmatiag eaatrlchim
      121 vpkvesvddv lhaekallaa sagqvplhvl lespaavqra feiaahprvq sisfglmdfv
      181 sahagaipas amgsqgqfeh plvvraklei aaachahgkv pshcvvtefn dadalrtaag
      241 raarqlgytr mwsihpaqir pileafapeq deiaqaaqll staahadwap vsvdgvlhdr
      301 asyryfwqvl erahqtgral paaaqawfaq paagpqa
//
LOCUS       WP_284428840             712 aa            linear   BCT 25-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Acidovorax sp.
            SUPP950].
ACCESSION   WP_284428840
VERSION     WP_284428840.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Shan,L., Mathews,I.I. and Khosla,C.
  TITLE     Structural and mechanistic analysis of two prolyl endopeptidases:
            role of interdomain dynamics in catalysis and specificity
  JOURNAL   Proc Natl Acad Sci U S A 102 (10), 3599-3604 (2005)
   PUBMED   15738423
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Polgar,L.
  TITLE     The prolyl oligopeptidase family
  JOURNAL   Cell Mol Life Sci 59 (2), 349-362 (2002)
   PUBMED   11915948
REFERENCE   3  (residues 1 to 712)
  AUTHORS   Polgar,L.
  TITLE     A potential processing enzyme in prokaryotes: oligopeptidase B, a
            new type of serine peptidase
  JOURNAL   Proteins 28 (3), 375-379 (1997)
   PUBMED   9223183
REFERENCE   4  (residues 1 to 712)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 712)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..712
                     /product="prolyl oligopeptidase family serine peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=78366
     Region          9..702
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mpestppiat pahdpaqded phqwleavds eralawvrer nahseavlta rpeyaptreq
       61 lldimdakdr ipsvvrrgdw lynlwqdghh rrglwrrttl agyrapepaw etvldldala
      121 laedenwvwg gaevlgpeyr halvslsrgg adatvirefd lvsrqfveag falpeaksdv
      181 twidaetvyv stdfgegslt esgyprivkr wrrgtplasa vtvfegeasd vgvgvgvdrt
      241 pgfertvftr midfyrhevw ltegpaeapd aapvrldvpd daipdfvrgt lllelrsdlv
      301 lgeahfaags llhadaaawl rgerraaalf tptatrslag ydttrdhvll qvmdnvaerl
      361 elwhrpggeg vpfvgravdt pfpgqlgvta lydplladdp laehyllsyt dfttpaslfl
      421 astadderel lkagparfda egmrteqcfa tsadgtrvpy fvlwprgaqa dggnptliyg
      481 yggfehaltp wyaadygraw ceqggvlvva nlrgggeygp awhqaavreh kqrsyddlia
      541 iaqdliargv trpahlgiqg gsnggllvga vmvqrpdlfn avvcqvplld mrryhtllag
      601 aswmaeygdp ddpadwafia ryspyhqvra daryprvlft tstrddrvhp gharkmaarm
      661 laqghdllyy entegghgga adnaqrahll alefaylwqq lgprpaaana ar
//
LOCUS       WP_284429031             491 aa            linear   BCT 25-DEC-2024
DEFINITION  rhomboid family protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284429031
VERSION     WP_284429031.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Koonin,E.V., Makarova,K.S., Rogozin,I.B., Davidovic,L.,
            Letellier,M.C. and Pellegrini,L.
  TITLE     The rhomboids: a nearly ubiquitous family of intramembrane serine
            proteases that probably evolved by multiple ancient horizontal gene
            transfers
  JOURNAL   Genome Biol 4 (3), R19 (2003)
   PUBMED   12620104
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10483871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..491
                     /product="rhomboid family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=55047
     Region          126..302
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
     Region          <412..491
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
ORIGIN      
        1 mfyaipldnr ptwrnppwmt vliivvnllv fwgpqrweak avdraaqvyl dsplpgielp
       61 pfvqwlkdsg hrdaeraqrm laahrehall rwmeheegfq krlhaglvvr addpqyadwk
      121 aararyeaal pepftrrwaq syekdapprp vtwitaaflh astghllgnm vflflfgfsv
      181 elalgrwryl afyllgavgg slmagwayag qgsyglgasg avsalmgmya vlyrlrrvrf
      241 fyqlffyfny vtapallllp awianellqh wlsgrgvaym ahlgglltga almwgaglvr
      301 rkaieapppe aaaapddgfd ahvaqarqsa qamqferalv qwraaaqlrp rdvpvlsawf
      361 ktaslwpage dfhraarrif rlpeqdaatl dfqhasyrty ldharpsarl vpddmaglar
      421 rfvragqwsd aeklltalhr tapqhaalge lvgmlvtall qsgrreqama wlpqlqqlap
      481 gsaplrlleg r
//
LOCUS       WP_284429036             158 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF2269 family protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284429036
VERSION     WP_284429036.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..158
                     /product="DUF2269 family protein"
                     /calculated_mol_wt=17158
     Region          2..156
                     /region_name="COG5528"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:444279"
ORIGIN      
        1 mntylalkwi hilssvllvg tgfgsafylf fanrsgsvaa qavvsrlvvr adtwfttpag
       61 ivqpvtgaam atmagwplst pwlatsialy aiaglcwlpv lwlqwrmaam ardaaaqgtp
      121 mpalytryar wwealgypaf vamlavfflm vhkpalwg
//
LOCUS       WP_284429111             273 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Acidovorax sp. SUPP950].
ACCESSION   WP_284429111
VERSION     WP_284429111.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 273)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..273
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28634
     Region          123..270
                     /region_name="NUDIX_Tnr3_like"
                     /note="thiamine diphosphokinase Tnr3 from
                     Schizosaccharomyces pombe and similar proteins; cd03676"
                     /db_xref="CDD:467544"
ORIGIN      
        1 msgqpvpgwv paarrqaqqp paaprlpfvv aghavgsvae gvldeialtp gdslpcllsk
       61 kehhgaaawh ldapagdvta alaalaqalr qagrcgawrd eqlavcnaag erigtverga
      121 vrplglatqa vhlvgsapgg clwvqqrafd kpthpgkwdt lmggmvsaad tldtaleret
      181 weeaglrtsa lhavahgghv dfarpssdge gvgymverid wfhatvpegl vpenqdgeve
      241 rfellptaev harlargeft peaalvlagf ygw
//
LOCUS       WP_284429112             328 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284429112
VERSION     WP_284429112.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..328
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34628
     Region          4..326
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(41..42,46,122,126,129,150,153..155,174..175,179,194,
                     218..219,240..244,265..268,315,317)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(134,233..234,247..252,260..267,270..271)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mslavqirqh ggpeelhvvd vdvgdpgpge irirhhavgl nfidvyhrtg lyplsmpatl
       61 gmegagivea vgegvthlka gdraayasnp pgsysevrvm paktvcklpd aigfetgaam
      121 mlkgltaqyl lkktlpaegl qpgdhvlfha aaggvgliac qwakalglql igtagsdekc
      181 rlalangaah ainyrtedfa arvkditggk gvkvvydsvg kdtweksldc lrpfglmatf
      241 gnasgpvpaf ppgllgakgs lyvtrqtlft hiatreatqa maddlfavvq sgavkihieq
      301 rhplrdvqqa hrdlearktt gctiltle
//
LOCUS       WP_284428977              67 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Acidovorax sp.
            SUPP950].
ACCESSION   WP_284428977
VERSION     WP_284428977.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 67)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..67
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=6995
     Region          27..>67
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mqtsiaihpv lqpsgpvsaa apqqrverll rlqdvrlmtg lgkssiyaai qagkfpspvn
       61 lthhava
//
LOCUS       WP_284429115             269 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: metallophosphoesterase family protein [unclassified
            Acidovorax].
ACCESSION   WP_284429115
VERSION     WP_284429115.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..269
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29698
     Region          4..217
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 msvlmhlsdl hfgahdprvc aavarlvktl dvsllvvsgd ltqrataeqf eqahafiagl
       61 gvphrlvmpg nhdvplfaww erlgrayrry erwwgrdlep vcdvdgflav gvnttrpwrh
      121 ergslshaqi davaqrlasa prdrwrivvt hhplvvhpts dtehrphrag ealarwreag
      181 aqlllsghah epglaevlpg lwaaragtav svrlrahapn slvtlecpap vrsgaevlpa
      241 rhrltrwdyd arlqaflplp prdlgsagt
//
LOCUS       WP_284429145             580 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Acidovorax sp. SUPP950].
ACCESSION   WP_284429145
VERSION     WP_284429145.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..580
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60650
     Region          1..460
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          513..578
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(536,545..547,554)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            546
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mkkvlianrg eiavriarac adygvasvav yanadidavh armageaygl dgdrpadtyl
       61 niekllavaq rsgadavhpg ygflsesaaf aqavidaglt wigpspeaia rlgdkveark
      121 ialkvgaplv agtsepvkda seviafaeqh glpiiikaaf ggggrgmkva wrmdevaely
      181 dsavreavta fgrgecfveq fldrprhiea qvladthgnv lvlgtrdcsl qrrnqklvee
      241 apapflsddq rarihqaahd icaeagyasa gtvefllsgs gaisflevnt rlqvehpvte
      301 qttgidlvve qlriadghpl avtetprplg hsiefrinae dvgrgflptp gpvvafsaps
      361 gpgvrvdsgv qsgstvpgtf dslmaklivs gatreqaiar aqralrefki egvasvlpfh
      421 ravighpdfv ggdgfkvhtr wietdfapdl aaalraepva dttlirtame idgrrvslgl
      481 ppellrglqs vpggapaapg agggdkaeqd ptavgapiag tlqtwkvaeg dtvakgdvia
      541 vmeamkmemq vtahragtia lsaaagsyha agtaiariqd
//
LOCUS       WP_284429247             120 aa            linear   BCT 25-DEC-2024
DEFINITION  bleomycin resistance protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284429247
VERSION     WP_284429247.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..120
                     /product="bleomycin resistance protein"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=13317
     Region          15..118
                     /region_name="BLMA_like"
                     /note="Bleomycin binding protein (BLMA) and similar
                     proteins; cd08349"
                     /db_xref="CDD:319937"
     Site            order(15..17,45,52..54,56,70..74,79..80,83,116)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319937"
     Site            order(39..40,45,56,58..59,72,98,105,107,111..113,115)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:319937"
ORIGIN      
        1 msrppaparl vhatvpvlas ldldesaafc adrlgfmpll rtddyliaer dgcelhfwlc
       61 terhiaents cyvrgdtral hadfaargla vdppreqpwg mrelyvidph gnllkfgesl
//
LOCUS       WP_284429202             433 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Acidovorax sp. SUPP950].
ACCESSION   WP_284429202
VERSION     WP_284429202.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..433
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=48062
     Region          143..410
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mtlptpstgl ptdgthavas mprratwrsr plqrvlrrll tnvrcgtltv elpggeraeg
       61 rgtepgphgt lvlhrwrplw rlavggdlgl aesyrqgews spdlaallel gvrneagwgr
      121 alqaslparl larlfhlrra ntrrgsrqni sfhydmgndf yaqwldpdml yssaiyatgq
      181 esldqaqqak lariatllap ragervleig cgwgalaial ardtgasvtg ltlsseqlrh
      241 arqrvhdeal tkhidlrlqd yrdvegqfdh ivsiemleav gerywpayfe tlkerlrpgg
      301 ravvqvitia daqfeqyrst tdfiqryifp ggmlpspsrl rqalanagla lqaaetfgps
      361 yattlaewrh rflsawptie plgfdapfrr lweyylcyce agfstgrvdv glytivhapp
      421 sapdtpgash rpg
//
LOCUS       WP_284429249             321 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284429249
VERSION     WP_284429249.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..321
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33690
     Region          8..319
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mrlrnclaaa tlaclsvaal aqgfpsrpir ivigfpaggp ldqharlltd klqavlgqpv
       61 vvdyksgagg tvgaqdvmka ppdghtlmla ntgvmvinpa lysrlpyqtl kdftpvarta
      121 mqplallvnp klpaktlpef iqyarakpgq vnfgsagngg ishlvpemfk tatglfmvhi
      181 pyrgsapaft dlmagqvqfm aesipqaaay hkqgkvrala vtsrqrnpal pdvptaiesg
      241 lkgfevvgfy gflapagtpk dvvaklsdaf gqvlqspevr ermvsqgadp aflgadafaa
      301 flatemprwa tavaqsgakl d
//
LOCUS       WP_284429254             294 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Acidovorax sp. SUPP950].
ACCESSION   WP_284429254
VERSION     WP_284429254.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..294
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31504
     Region          5..284
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 melgpwgdas vlgilgllig sflnvvihrl pkmmerqwaa ecadfaaman kdaasteapa
       61 apvepfnlwt pasrcpacgh avqwyenipv lsylwlrgrc sackvrispr yplvelatgg
      121 lfffcgwhwg ttltavawcg fsaalialaf idwdttllpd ditlpllwag liasamqwtt
      181 vplfsavmga vggylslwtv ywafklatgk egmghgdfkl faalgawfgw palvpiilia
      241 svigafigig mkfasqlreg gyvpfgpflv gsglaamvfg petilqgllr slgl
//
LOCUS       WP_284429260             575 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Acidovorax sp. SUPP950].
ACCESSION   WP_284429260
VERSION     WP_284429260.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 575)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 575)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..575
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63938
     Region          4..574
                     /region_name="COG4986"
                     /note="ABC-type anion transport system, duplicated
                     permease component [Inorganic ion transport and
                     metabolism]"
                     /db_xref="CDD:444010"
ORIGIN      
        1 midkrffprq vvqatgnrwd wallplvlav lfalawggsq marpyqvgdv lplsldpwml
       61 pyyllrttlr mfialgaslv facvfaalaa kyrtaervmv plldilqsip ilgflsitvt
      121 gfialfpgnl fgvecaaifa iftsqawnma fslyqsmrtv paelreaaav fqlsgwqrfw
      181 rlelpfampg llwnmmmsms ggwffvvase aisvshqdik lpgvgsyial aieardlgai
      241 gwaivgmlvg ivlydqlffr pliawadkfr feeggseaqp tswllswmrr tsqlkrvval
      301 fvvplewslt rlrrrhdgts irarpsvphp altragdall aaavmlaviw lvrfihsevg
      361 whevghvfvl gtytlvrvvv lillaaavwv pvgvwigmnp rwagrlqava qflaafpanl
      421 mfplavvliv rwhldpnlwl aplmvlgtqw yllfnviaga ssvpselrya aqnlglsgwl
      481 rwkryllpav fpsfvtgait asggswnasi vaeyvtwgdt tlqadglgsy iahmtaigdf
      541 prialgigvm cvfvmgmnhf vwrrlyamae nrmhs
//
LOCUS       WP_284429347             251 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: HesA/MoeB/ThiF family protein [unclassified
            Acidovorax].
ACCESSION   WP_284429347
VERSION     WP_284429347.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..251
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26655
     Region          2..248
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mtddqllrys rhimldeigi egqerilaah alvigagglg spaalflasa gvgrislvdd
       61 dvvdltnlqr qiahttervg epkvhsaaqa lqalnpgvrl daiqaradke wlddwvgqat
      121 vvldcsdnya trhavnaacv thrkplvtga airfdgqitv idprdplspc yacifppdta
      181 feetqcatlg vfapmvgiig amqaaealkl iagfgeslag rlsmldgrsm ewtvmkiprh
      241 ghcsvcghat p
//
LOCUS       WP_284429359             249 aa            linear   BCT 25-DEC-2024
DEFINITION  SCO family protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284429359
VERSION     WP_284429359.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..249
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26376
     Region          101..236
                     /region_name="Sco1"
                     /note="Cytochrome oxidase Cu insertion factor,
                     SCO1/SenC/PrrC family [Posttranslational modification,
                     protein turnover, chaperones]; COG1999"
                     /db_xref="CDD:441602"
ORIGIN      
        1 msgskssdas fahaaslppd apqgahplgl tvhslppagg amaavqqsrq grwkmlgill
       61 vcaapvvasy ftyyvlrpeg rrnfgeliap qrampagmat taldgapgrl dqlqgqwllv
      121 svapgacgta cqnhlylqrq lreslgkdkd ridwvwlvtd gaapppeiqp glqkaqvlrv
      181 daqalsawla patghaiedh lyvvdpmghw mlrfpaglda agaakakrdl erlmrasasw
      241 dqpgrtgap
//
LOCUS       WP_284429384             613 aa            linear   BCT 25-DEC-2024
DEFINITION  autotransporter assembly complex protein TamA [Acidovorax sp.
            SUPP950].
ACCESSION   WP_284429384
VERSION     WP_284429384.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..613
                     /product="autotransporter assembly complex protein TamA"
                     /GO_component="GO:0097347 - TAM protein secretion complex
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=66486
     Region          32..613
                     /region_name="TamA"
                     /note="Outer membrane translocation and assembly module
                     TamA [Cell wall/membrane/envelope biogenesis]; COG0729"
                     /db_xref="CDD:440493"
ORIGIN      
        1 mllsslvalq gcsllpgake gtvdnntiqs dagagtgpda fslevrapda vreyltrhme
       61 lqrfrqlpdl qsseitrllg aaesnarell gtlgyfsptl titmqetpgs agaprtitve
      121 vepgpqtrva radidftgae adspqfanrr arvqrswsla pgqpftqdaw dgaksqglrq
      181 lqatryptas iaksraeida drneaqlgvt ydpgppyrfg alrvqggery sadgarriar
      241 lptgadysea qlldaqmrla ssgyydavfl sletdgtdpq aapvvaqvre aplqkvvfgv
      301 glstdsgprl svdhihnqlp gigwravskv svdrknklls tdwtdlpged gwrwftgaqv
      361 qrettgdyev nssrlrggrs kstdhidrsy flqhdtaksq gtdappssaa isanygwtgr
      421 yfnnttnptr gfglaaelgv gttlrperdp fvraylrwqs fypmgrvdmg egvtrtsrla
      481 lraeggavla rraaeipvtt lfltggdttv rgygyreiga rtsngqlygg ryltvasaew
      541 qrpiefrgnr tdfetamfid agavadragd ldprvgvgag lrwrspvgpl qadvaygvqa
      601 kqlrlhlrlg fsf
//
LOCUS       WP_284429393             755 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Acidovorax sp. SUPP950].
ACCESSION   WP_284429393
VERSION     WP_284429393.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 755)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 755)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 755)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 755)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..755
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..755
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=80597
     Region          89..755
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mtttsffssa lpapplqpqp isartprkar splahavlaa lagfgpaaap aqdaplssvp
       61 tlapvtvsgt paeplgrlnl dtpaetgsrl gltpretpas vtvvdrasie argaqdtqei
      121 lraipgvtah napgsmaasy rgfsnnsvtq lyngitvqyg satravdswi ydrveavgga
      181 ssflygagav ggslnyitkt pdrsgdfaeg rlragsyglk easvglnrri agpqdggagp
      241 shfaridvnh rdagswtagt qtrstqlaas llsdlgggft hllayeyqkd avdrpywgtp
      301 vlnpavgalr idpgtrftny nssdgtyahr vqwlrsvaqw rvsdalqwrn tlyaydalrd
      361 yrnvetyqfn aantqvsrgs aylqrhdqql vgnrteatwh gtlagrpsdw afgldvsvnr
      421 qtrfpnslag tvstvdpyrf tterffdipg mapgfradrd nrvqttavfv enrtalvpgv
      481 nlvtalrqer ialdltnrra vtatspatfe rsytpttgrl gvvwdvapga nvyaqyatas
      541 dppsgslsta sfadvannsa lttgrqleag akfdfwggrg tatvaafqit rrniasqdpn
      601 npaftvlvge qssrgaevav glrltdrwhl qanamrtrar yeqfvqggvs lagrtptntp
      661 esvanlwlgy avtpalqata garrvgsisa daantqywps ytlldlglsw klsptatlsg
      721 hlrnatdrly aaearsaqvy lgaprtvdvs lqvaf
//
LOCUS       WP_284429437             517 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Acidovorax sp. SUPP950].
ACCESSION   WP_284429437
VERSION     WP_284429437.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..517
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=54996
     Region          47..>367
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
     Region          <137..>247
                     /region_name="IucD"
                     /note="Lysine/ornithine N-monooxygenase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3486"
                     /db_xref="CDD:442709"
ORIGIN      
        1 mtiatptdst lapapaglaa learlrqdlq wlglparrwv pprlteagep vldvaivggg
       61 maglalgasl ahmgvqaplf drapegfegp wattarmetl rspkeltgpa lglpaltfra
      121 wfeaqfglpa waaldkiprl qwmdylrwyr rvlgldvrnr qrvlavrpra dglvridlad
      181 danggaphhv larhavlatg rdglggpwvp dwaralpagr wahsanvwdg aalrglrvav
      241 vgggasamds aataleagaa rvdllvrrae lprvnkgkga gnpgmahgfw slpdewkwrf
      301 rhylnvqqvp pphgstlrvs rhanahfhlg agvhgasvrp dgavrletak gplaadfvif
      361 ctgfrtdwal rpefaafapa vrlwqdrfvp pageddaela aspdlgplfe fqekapgacp
      421 gldrvhcfny ggalsqgaga gdipqisdga qrlarglaar lladdaalhy aamqryeepe
      481 ldgdewtpaa fpaygpeaaa paasapalpe sapevtr
//
LOCUS       WP_284429447             500 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Acidovorax sp.
            SUPP950].
ACCESSION   WP_284429447
VERSION     WP_284429447.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..500
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=53874
     Region          4..486
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mnanaatilv vddepdlrtl yeltllregy rvetagnlqe arqqlqarkf davitdmrlp
       61 dgfgmellhe lrdqqrrerc vvmtaygsae navealrsga fdyltkpvdl kqfrsvvasa
      121 vqgtggvppp rsarpgtapr apqeavaggt tlsldrlvge seamrnvkqr iakvarsmap
      181 vlirgesgtg kelvaralha ssqradgplv avncgaipen lleaeffgar kgsytgatqd
      241 rdgyfqaarg gtlfldeigd lplamqskll raiqersvra lgstgeetvd vrivsathrd
      301 lsadvqsgrf rqdlyyrlnv ievvipplre rredlpalca tllariaqes gapvppltqn
      361 aldriamhpl tgnvrelenl lhravalsdg eelhveppha saadaarada gaspapggdp
      421 pgngtprsah paasvplpsd lqawldqqer eilvralrdt gfnrtataar lgislrqiry
      481 riarldiaap ndsdanddse
//
LOCUS       WP_284429466             264 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284429466
VERSION     WP_284429466.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..264
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26665
     Region          14..243
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mtaarpgaad eapslrerlv agdflfatfv kttshqtvev laatgldtlv ldaehapfgp
       61 esldrsllaa racalpvlvr vpyprgaaiq qaldmgaagv mvphvdsaai alevvraary
      121 ggtrgysasp raggygqrsm adhlrlsdah tavivqiesg eavaqareia avpgvdclfv
      181 gpadlavslg adgpgdprva eaiarvcaag ratqcavgcf vsdaaqvagl ralgiaffvv
      241 gsdqallraa arqamagale siaa
//
LOCUS       WP_284429491             318 aa            linear   BCT 25-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284429491
VERSION     WP_284429491.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..318
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34946
     Region          16..286
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 msetspsrfd tsfgnlrirr vagslggevl glqlsgeldd atiadltaal vrhkvlffrg
       61 qahlddaahq afgarlgktv ahptvpsptg trifeldask gggradswht dvtfidafpk
      121 ygilrgvtip ayggdtvwan taaayarlpe dlqrladglw avhsndydyg aervvveeer
      181 lnhhrkvfvs svfeaehpvv hvhpvsgera lllghfvkki agfsstesar lfeilqnrvv
      241 rlentvrwqw qqddvaiwdn ratqhfaind ygtqarvvrr vtvhgepava vdgrrsrtrv
      301 rpeatndaqi dsvitata
//
LOCUS       WP_284429557             395 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Acidovorax sp.
            SUPP950].
ACCESSION   WP_284429557
VERSION     WP_284429557.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..395
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=43196
     Region          3..368
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mtarslktwt wlhkwsslvc tvfmlllclt glplifhhei ghllgtevea ppmpagtphv
       61 sldrvldvar aqhpdrvvqf asqpedstdl wfatltptpa ptedfrsvav dartgallaq
      121 prfdegfmyv mfklhvdlfa glagklflgf mgllllvaiv tgvvlyapfm rklrfgevrr
      181 erstrvkwld lhnllgivtl vwafvvggtg mintwadllv kywqydelsa llapyngqpi
      241 tpvaerasvq ksldaalara pgtklsfiaf pgtsfssphh htfflrgnep ltsrllqpvl
      301 vdaktaevta apklpwylva llvsqplhfg dyggmpmkil walldiatii vlgsglylwl
      361 grraaspatt spgktasgea alasplttar apikr
//
LOCUS       WP_284429564             741 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284429564
VERSION     WP_284429564.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 741)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 741)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 741)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 741)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..741
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=81215
     Region          18..740
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mgqggagsas prsdavpqli aatalslpeq agalararaf aepllssetl etgentfaha
       61 eavasilkni ggseamqaas ylvhacshln kpeeviakaf gqnfaalave ttklmrvqqq
      121 areaqlagqp vddpatqten vrkmllafsr dlrvvmlrla srlqtlrfya atkravspgi
      181 arealqvfap lanrlgiwqm kweledlsfr flepetykqv arlldekrae revymeqlrg
      241 rleselrars isasvqgrpk hiysivkkmr gksldfehvf diralrvvvp svkdcyaals
      301 wvhehfkpid aefddyiakp kpngyqslht vvrdetgkai eiqirtqamn dhaehgvaah
      361 waykeagtkg yagvsasgey dakiavlrql lawerdmagt vqhgglfedr iyvltpdaav
      421 velpqgatpv dfayavhtsv ghrcrgarvd gamvplntpl qngqtveitt vkegrpsrdw
      481 lnaelgylts hrarakvraw fnaqathett argreavekl lqregktaik lddlavqlgf
      541 ktadalfevv gkdefslrti etllrppepv lqpddylllk ktrtsetapk ggvlvvgids
      601 lmtqlakcck pappdsirgf vtrgkgvsvh radcsnfrem aarsaeriie vewgqskasa
      661 gagpsvypvd vsveaadrqg llrdisevfa rektnvigvq tqsvkgtawm tftvevadsg
      721 rlnkvlgiva tvqgvrsarr r
//
LOCUS       WP_284429568             349 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Acidovorax sp. SUPP950].
ACCESSION   WP_284429568
VERSION     WP_284429568.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 349)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..349
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35325
     Region          48..342
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mpsqpvpaas haaqpgpgpr raawlgacll vvsalllvvg acvgstgfds llrmgqdpva
       61 wqivweirlp rtlgawlaga llglagavaq glfrnpladp yllgsasgaa lggalamvvf
      121 gvspmaaqwl arlgvtgmaf lgaagavalt lvlargvqht lrlllagviv gvvlgalrdl
      181 velaspdilq amqaftlgst sfvgwvacal magawalcgi aawtlarald gltlgeataa
      241 slglplapmr aglvaamala tgtavaqtgl iafvglaaph lvrsivkvth qrqivlsslm
      301 gaalllaadi larwilapqe lpvgvltaal ggtyllwlmh rrsmqghsl
//
LOCUS       WP_284429569             783 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Acidovorax sp. SUPP950].
ACCESSION   WP_284429569
VERSION     WP_284429569.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 783)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 783)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 783)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..783
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=82952
     Region          22..757
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mpagagadad ataqtweshv vlegmhcaac altiedvlra vpgvaqadvs aatrrarvvw
       61 naaqvrpsqw iaavrragyr alpamdafar aqrqgehrra lwrwlvagfc mmqvmmyawp
      121 ayvaqpgdlt aemeqllrwa swvitlpvvi facgpffana lrdvrlrrvs mdlpvalgma
      181 itfgvstagt fdpsgifgre vfydsltmfv fflltgrwle lrlrdrtaga leavmnrlpd
      241 sverlqadga fvrvavrrla vgdtvrvlpg eafpadgrit rgdtladeal ltgestpvar
      301 pegsavtags ynlqsavqvk vervgadtrf aqivalmesa slqkprlaql adriarpfli
      361 avlaaaalaa awwwptdpgh almvavavli vtcpcalsla tpvamltaag tlarqgvlvr
      421 hlqalealag vdtvvfdktg tltrdgmavr gvhpapgldr adalalaaav arhsvhpvsr
      481 alvaaasreg lptasrwhvl evhelagqgl varlreadeg adgaadargr lalgertvrl
      541 gsvrhagasv pagdggegga tgqqvvlseq rgdgtrvela rfdwsedlrp eapremrrlr
      601 dagvavqlls gdrpgavrrv arqvgieraq gdctpqdkla llqaeqargh rvamvgdgln
      661 dgpvlagahv sfafgravpl aqsradfvvm ggdleqvvqt lllarrtlrv vrqnlwwaal
      721 ynalcvplav lgwmpawlag lgmalssllv vanaarlaag tgsphapaaa paahsdvpll
      781 egv
//
LOCUS       WP_284429632             306 aa            linear   BCT 25-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Acidovorax sp. SUPP950].
ACCESSION   WP_284429632
VERSION     WP_284429632.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Kutner,J., Shabalin,I.G., Matelska,D., Handing,K.B.,
            Gasiorowska,O., Sroka,P., Gorna,M.W., Ginalski,K., Wozniak,K. and
            Minor,W.
  TITLE     Structural, Biochemical, and Evolutionary Characterizations of
            Glyoxylate/Hydroxypyruvate Reductases Show Their Division into Two
            Distinct Subfamilies
  JOURNAL   Biochemistry 57 (6), 963-977 (2018)
   PUBMED   29309127
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10187381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..306
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=33096
     Region          1..304
                     /region_name="GDH_like_2"
                     /note="Putative glycerate dehydrogenase and related
                     proteins of the D-specific 2-hydroxy dehydrogenase family;
                     cd12164"
                     /db_xref="CDD:240641"
     Site            order(45,64..66,89,221,269)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:240641"
     Site            order(65..66,83,89,93,137..141,159..162,164,191..193,
                     197..198,219..221,245..246,269,271..272,304)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240641"
     Site            order(92,94..96,98..99,102..103,106,108,111..112,114..115,
                     119..120,122,125,128,152,243,247,250..252,254,258..259,
                     261,264,266..268,270..271,275)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240641"
ORIGIN      
        1 mnitfcctht kaepwlqglq aalpgahitv wqpgappadf avvwappqqf mdeqagiqal
       61 fnigagvdal lalrlppgaq vvrlddagma vqmaeyvcha vvrhfrefea yeadmraggw
      121 ayrrprlrsd fsvgvmglgv lgervakala hfefpvngws rspkavegvr vfhgaagfdg
      181 flaasrvlvn llpltpdtqd imnrdtlsrl qpggyvvnva rgahlveddl ialidaghla
      241 gatldvfrte plpadhplrt hpritttpht sartlreesi aqiarkiaam qrgepvagiv
      301 dprrgy
//
LOCUS       WP_284429690             773 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Acidovorax sp. SUPP950].
ACCESSION   WP_284429690
VERSION     WP_284429690.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 773)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 773)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 773)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..773
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=82589
     Region          77..773
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mkhsnpvkkp rslrlaegva aslstamllp waamaqtapp qdatvlptvt vqdqaidpnp
       61 naevgapyka ktsadvrhtr plaetpqtis vvtkaaidds gftdlkqila aqpgitlgtg
      121 engnafgdry iirgqearsd vfvdglrdpg mttresfaie qleitkgpns tfagrgsagg
      181 ainaitkqat ldydfsrisv gagsdgyrra tldankgfsd qfalranaly stegvpdrdp
      241 skrrreglal sglweananl svtldyyglr ardkypdlgs yllgtvpnrv patgvpvyaq
      301 sqdflnsdvd altarvkwri apdktltslt rygtsdngyv vtgasggtry sngtpftsas
      361 lsthngwqev kyfahqtnlr wdteiagkkn elifgleytd hqvtrgnyav tntgafncrt
      421 qagtgantay clsgpsgavt pglnsimgrq iaqtpwandw qvksfalsam dtvdltdqwt
      481 vfggvradyt dfslvtrnat taaqtgnysy tdtllnghlg vsykinpmgi vyasygsaqd
      541 inggesdtgt ssgygglvvy ngsaagakpe tsrnleigtk wnlldnkllf taaafqttks
      601 dvmeganyds lgtfntgknr vrgvefglvg nvtsqftvqa gvafmkskvl ksataanvgl
      661 plsnfadrsf svqgkyqltp alsvgatarh esdrcggqpd tgasytngtc aqpvpsftvy
      721 dlfasyrlnk hadirvnvln agdkdyytav yrsgsflykg dgravrvtld yef
//
LOCUS       WP_284429695             307 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284429695
VERSION     WP_284429695.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..307
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33510
     Region          120..217
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mtnarwqrgm vvcnlllaag wlvwqwpasp lravaglaav mlllrlfmgl qfvcmarvnr
       61 rasradgvpa pslaqmvraw saearwasvv fgwwqpfrst avpdwlpppv aggpppargv
      121 vlvhgficnr gfwtpwmkvl rsrghpfvav tmepafgtid dyvdtldeav rrvtaatgrp
      181 pvvvghsmgg lavrawlrar qadarvhrvi tlgsphqgaw aarfsrsang rqmvpggewl
      241 rqlaqdeppg raalftcfys ncdnavypaa tatldgadnr lreglahvqm afhppvvrec
      301 ldliaap
//
LOCUS       WP_284429723             296 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase [unclassified
            Acidovorax].
ACCESSION   WP_284429723
VERSION     WP_284429723.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..296
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=33030
     Region          107..219
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mndltappqk asdwlalgiq hlerdervla aealrhalqd retrltahql ieqhtlpgaf
       61 sqmmglncei araddifrff eghpsstnpl rdyladgwrt lselmtllet vdrpllktpr
      121 fmefasghgr ftrhlvkalg adrvtvsdvv pdamafaqrt fgvrsvlsst vpeslvwdqq
      181 ydvvfvlslf shlprrtwar wlqclydgva pggvlvfsth glkaaahdsv aldddgfffa
      241 pssesqaidv qeygtaftse dfvlariaet vgadklvhrs lvhfwnhqda yvlakp
//
LOCUS       WP_284429757             639 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Acidovorax sp. SUPP950].
ACCESSION   WP_284429757
VERSION     WP_284429757.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..639
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=68424
     Region          23..492
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 msaitstepp tdvhhvdalp agtrlgefev lsllgvggfg mvykafdhsl lrfvaikeym
       61 psalaaraqg qslwvrsstq eqsfqaglas fvsearllaq fdhpslvkvf rfweanhtay
      121 mvmplytgmt lkqarahmrt pppeawlrkm lwsvlsalrv lhdgqtlhrd ispdniflqd
      181 sgppvlldlg aarhaisdhg hqhtavlkvn yapieqyndg esdlrqgpws dlyalgavvh
      241 gslcndtplp atlrsirdrm vpfsrvaktv rrqfgveyst pfvaaisqal alrpderpqs
      301 ideflrtmdm vappegidqf dfraelgdiw vepadrrgtg vavpmidits vplpavgvpl
      361 paplaaavea ptvdtgaqlh idrqeagdtv vsdgqdtvfm dggqevadtv tggdtvfeer
      421 rpqhperlgr pktrrsqaag eeapasavag vrhrpllwas agvvavavva aglwwsasrd
      481 tphptkytpe dqiitelaep papvasapae lipvvdeaat apalpaasaa svaaapafvv
      541 asaprpkpvp rkvaeptpaa vaaeapaspe papvpaatpk pavarvagpd eacanagfia
      601 rpmcihqqcq naavanhplc venrrrleae errrtmlsq
//
LOCUS       WP_284429774             440 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284429774
VERSION     WP_284429774.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..440
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=46822
     Region          197..412
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mkrwglalli lwvhvgdplv awlygggtwl qatwlrpird ltvlalaalc lltvrmpral
       61 lvsvlafggl alayapvglv hglpagvvlg slgvilvpmv fllagygcfs tprnlrfgas
      121 alvwlglast lfgmweivnt qfwvdtvrlp dylanikgvm pkdtdphtgl pwnffggety
      181 arraggllaa plaqgqflvt aalaalglwq trwpwrallv caglfvgvwm sgtrgsmlag
      241 ivallgyllt srglvrsata rvllvgaalv amvwasygiv vaswnfrdgs tighwwalqr
      301 nladlgqval wggglgrqga faarqaltdl gggegalfsi ayqmgvpcal lflglvfwcl
      361 rtlwqahvrh gdrlalatfw llcgmvttfv ssenaltvsg aggfwlllgg mlrqcaaatr
      421 fgaavepgti rapcihaara
//
LOCUS       WP_284429788             254 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Acidovorax sp. SUPP950].
ACCESSION   WP_284429788
VERSION     WP_284429788.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..254
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28648
     Region          70..190
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mswsvfdwrs llesaggrll yralrhregr syvwlrltss aplfqdygtt smnryprlfa
       61 fvrealtdca sprllsfgcs tgeevlslrq yfphaditgl dihpghiarc lqqqqgqpdp
      121 gmrfrvagdt aaeatatyda ifclavmrrg dlarhrgecc dhlirfqdfd aqledfarcl
      181 rpggllvlrh anfrlrdara arwfdpvlrv ptparadtpl fgpdnrrltq qgddeavfrr
      241 rplpsgvpsg kgiq
//
LOCUS       WP_284429797             415 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284429797
VERSION     WP_284429797.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..415
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45396
     Region          13..406
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mtapdpsqdi dfplegvrvl dlsrvfagpl cgqvladfga evikvehpgr gddtrdwglr
       61 igktettyyn smnrnkrsit mdlqspeglq iirdllpqfd vvihnfktgg aeklglgyeq
      121 lkalrpgliy cavagydssg peakrpgydl viqgetglma lngeatqppl kfgvavvdlm
      181 tgmyaaqavl aalfrrertg hgrliemaly dcgimvtgyy gldamqlgrd perygnahps
      241 ivpygmydaa dgpliiavgn naqfdkfcrq vierpdived prfstnvnra rnrvelgpll
      301 kalihafprd lllerltaag ipcgrvtglh ealtsertrr sgllrdmphp vvgttpvfap
      361 pyrmdgqrlp irsapptlge gtrevlhrll smsdaelqql qqrgvltlpd dsppa
//
LOCUS       WP_284429810             327 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: Bug family tripartite tricarboxylate transporter
            substrate binding protein [unclassified Acidovorax].
ACCESSION   WP_284429810
VERSION     WP_284429810.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..327
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34087
     Region          1..325
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mnrkklllsa vicalgaasw apamaqeapf ptkpitlvip fppggatdvl grligkkmgd
       61 llgqsvvidn ragagttiga ayaakatpdg ytllmssgtt ftvnpavrpk lpydpvksfe
      121 pigiagrtsl illankdvpa adlkqfvalv kaapdkysyg sfgagttsqf agemffhaag
      181 lkiqhvpykg sapamtdlmg gqipftvdtv saalpqlkdg kikaiavtag krsallpkvp
      241 tlvesgypgl emdtwlamva prglppavks rleltlaqvv sdpetrdkmi avgfepayas
      301 sktvaelidr elplmraiaq rasitad
//
LOCUS       WP_284429802             326 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284429802
VERSION     WP_284429802.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..326
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33749
     Region          3..324
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mttltrrrfs alalavallp qihamaqgal sagpitmivg wpaggpsdnv arltavrmse
       61 algqsividn kggaggnigs daaarakpdg stimlatvas hglnsalypk lnhdpikdfa
      121 pigmittsps vllvptdspf lsvadllkaa qarpgqlnyg sggvgssqhl aganfkkitg
      181 advthipykg tapamtdlma grvdfvlttg amsfirsgkl rplavaarqr lpalpdvptf
      241 eeagvkgfht dswyglvapa gtpraaldkl naalatalrn pevqkqfldq gslpvkpmgv
      301 defwsfvqqq mplaaeqvrv sgakae
//
LOCUS       WP_284429818             479 aa            linear   BCT 25-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Acidovorax sp.
            SUPP950].
ACCESSION   WP_284429818
VERSION     WP_284429818.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..479
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=50784
     Region          1..478
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mfdllifggt vvdgsgaarr qadvgiaggr ilavgdlsaq parqrhdavg rivcpgfidv
       61 hthddrlllt spagphpklt qgvttvvtgn cgislaplls netppapldl lgaddwrydr
      121 fgdyldalea sgpalnaacl vghstlrvrh vpdlrrpatp peaermamdl aegldagafg
      181 lstglyyppa raataeevia vgaplsaaqg litmhirdea daiddalrea lhigqalgvs
      241 tvlshhklig qrnhgrsvnt lamvdtaals qpvcmdcypy nasstmllas rvgqsrevlv
      301 twsvgdpsaa gkslfamare rgcspeslve plspagavyf amheddvrri lrhpltmvgs
      361 dglahdavph prlwgtfprv lghyardqrl fsletavhkm tglsarrfgl rdrgviaqgh
      421 aadivvfdet ciadratfeq ptapsagida vfingqlaca hghtvnahag qvlrrqrsf
//
LOCUS       WP_284429827             606 aa            linear   BCT 25-DEC-2024
DEFINITION  RecQ family ATP-dependent DNA helicase [Acidovorax sp. SUPP950].
ACCESSION   WP_284429827
VERSION     WP_284429827.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Larsen,N.B. and Hickson,I.D.
  TITLE     RecQ Helicases: Conserved Guardians of Genomic Integrity
  JOURNAL   Adv Exp Med Biol 767, 161-184 (2013)
   PUBMED   23161011
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Rezazadeh,S.
  TITLE     RecQ helicases; at the crossroad of genome replication, repair, and
            recombination
  JOURNAL   Mol Biol Rep 39 (4), 4527-4543 (2012)
   PUBMED   21947842
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Bernstein,K.A., Gangloff,S. and Rothstein,R.
  TITLE     The RecQ DNA helicases in DNA repair
  JOURNAL   Annu Rev Genet 44, 393-417 (2010)
   PUBMED   21047263
REFERENCE   5  (residues 1 to 606)
  AUTHORS   Chu,W.K. and Hickson,I.D.
  TITLE     RecQ helicases: multifunctional genome caretakers
  JOURNAL   Nat Rev Cancer 9 (9), 644-654 (2009)
   PUBMED   19657341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..606
                     /product="RecQ family ATP-dependent DNA helicase"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0043138 - 3'-5' DNA helicase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=65552
     Region          28..514
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
ORIGIN      
        1 mpvtppqptp aspkrarqpr aprtpsaari qsvlkktfgl ralragqrev idrvlqsent
       61 lavmptgagk slcyqlpalm iegrtvvvsp lialmrdqcd slrergvpav qlhsgltpqe
      121 treaeqaiad gsarivlttp erladaefla lvassgpigl lavdeahcis qwghdfrpaf
      181 leiagavarl grptvlalta taagpvaadi rkqlgipaag vvdtgtyrpn lryraealan
      241 eadkrarlid ivkaaegsgl vyaatvkaaq evhaalraad vaaglyhgrm paaerseaqd
      301 afmngkarvm vatnafglgi dkqdvrfvvh yqmpgglday yqesgragrd gdpadctllf
      361 lrkdkavqqf flagrypsad didalyqalr dpapqdpgfw tldslqarld rprsklqvgl
      421 gllqrhkmvs karsgaltlr ktelepasvr allqayadkr eqdqqalerm vfyaqtgrcr
      481 wqvlleyfdp snepqrcgtc dncirmaela rqalveraad tvrklgasdl gemgepvias
      541 aaqarhdaqa lelgatvrvk rygqgtvaai dpisvtvdfa dgtqrcfqpd fvqrfvprgt
      601 rakpls
//
LOCUS       WP_284429873             316 aa            linear   BCT 25-DEC-2024
DEFINITION  Gfo/Idh/MocA family oxidoreductase [Acidovorax sp. SUPP950].
ACCESSION   WP_284429873
VERSION     WP_284429873.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..316
                     /product="Gfo/Idh/MocA family oxidoreductase"
                     /calculated_mol_wt=35713
     Region          1..>199
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
     Region          158..297
                     /region_name="GFO_IDH_MocA_C"
                     /note="Oxidoreductase family, C-terminal alpha/beta
                     domain; cl21649"
                     /db_xref="CDD:451345"
ORIGIN      
        1 mknfaligaa gyiaprhmra ikdtgnhlav aydindsvgi idsispqsdf ftgferfaeh
       61 ahqlkrdpat aldyvsicsp nylhhahiaa glrlgcdvic ekplvptpql mdelarieqe
      121 tgrrvfnilq lrhheailkl rdkvaaapkd tkfdveltyi tsrgkwyles wkgdprksfg
      181 vatnigvhff dmlhfifgkl qdnrihlsee tkaagyleye rarvrwflsi dandlpeevk
      241 gkkptyrnid vsgeqlefse gftdlhttsy reilagrgyg ladarhciet vdvirsasia
      301 adrdervhpf vrnkgy
//
LOCUS       WP_284429876             367 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Acidovorax sp.
            SUPP950].
ACCESSION   WP_284429876
VERSION     WP_284429876.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..367
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40316
     Region          10..361
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 meftdlraqy rrlksdidvr iqkvldhgqy ilgpevhele eqlatytgak ycitvangtd
       61 alqiaqmalg igpgdevitp gftyiataet vallgakpvy vdvspdtynl dpslleaait
      121 prtkaiipvs lygqcaefdh ineiaakyri pviedaaqsf gatykgrksc nlttlacasf
      181 fpskplgcyg dggaiftsde elarvlrqis rhgqdrryhh vrvgvnsrld tlqaavllgk
      241 lvvfdeeiak rqmiadqyas kllpipqiac psikngnlsv waqytirsnh rddlqqalkk
      301 ldipttvhyp lplnkqpave dgskqlpigd qlpnevlslp mgpylsdsdq slvaraiqqf
      361 yfenpsa
//
LOCUS       WP_284429881             287 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD-dependent epimerase/dehydratase family protein
            [unclassified Acidovorax].
ACCESSION   WP_284429881
VERSION     WP_284429881.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..287
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30812
     Region          2..285
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrycvvgsgg yigrflcehl ikqghsvdkv ssslaggidp ttgllpeldl aqvdvvvyla
       61 qspfyrqlpq raphllavnc vsavhvaiaa qasnvskfiy astgnvyqas fdafkehstl
      121 ergnwyslsk imgeeglrla aggmdltclr ifgvygpgqa dklipnliar vtrgetvtvd
      181 rqpsaaeaqp eglrtnpiyi ddtvraiemv agirgvpvmn fagdevlsir qmveiigeva
      241 gtspqvavnd heragdligd tslfrshytp pltpfkegiq kvleasq
//
LOCUS       WP_284430090             321 aa            linear   BCT 25-DEC-2024
DEFINITION  tRNA dihydrouridine synthase [Acidovorax sp. SUPP950].
ACCESSION   WP_284430090
VERSION     WP_284430090.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Finet,O., Yague-Sanz,C., Kruger,L.K., Tran,P., Migeot,V.,
            Louski,M., Nevers,A., Rougemaille,M., Sun,J., Ernst,F.G.M.,
            Wacheul,L., Wery,M., Morillon,A., Dedon,P., Lafontaine,D.L.J. and
            Hermand,D.
  TITLE     Transcription-wide mapping of dihydrouridine reveals that mRNA
            dihydrouridylation is required for meiotic chromosome segregation
  JOURNAL   Mol Cell 82 (2), 404-419 (2022)
   PUBMED   34798057
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Bou-Nader,C., Bregeon,D., Pecqueur,L., Fontecave,M. and Hamdane,D.
  TITLE     Electrostatic Potential in the tRNA Binding Evolution of
            Dihydrouridine Synthases
  JOURNAL   Biochemistry 57 (37), 5407-5414 (2018)
   PUBMED   30149704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414563
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..321
                     /product="tRNA dihydrouridine synthase"
                     /EC_number="1.3.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0017150 - tRNA dihydrouridine synthase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /calculated_mol_wt=34842
     Region          3..312
                     /region_name="DusA"
                     /note="tRNA-dihydrouridine synthase [Translation,
                     ribosomal structure and biogenesis]; COG0042"
                     /db_xref="CDD:439812"
ORIGIN      
        1 mtlllapmeg lldfvlrdvl trvggvdrcv sefiritgtl lpdkvflryl pelrhggrtl
       61 agvpvraqll gsdpvsmaen aarlaalgpe gidlnfgcpa nvvnrhggga allkeperia
      121 avveavrrav pphlpvsakm rlgyhdasla recaqamqag gacelvvhar tkadgyrppa
      181 yweqipavrd avsipvvang eiwtvadaqr crevsgcsal mlgrgmvadp glalairsad
      241 agdadvpalp wsalqphlsd fwrlvcedle prqragrlkq wlnllrrrfp egeaayqqvr
      301 tmtdqqditq wlhrqpmpdp a
//
LOCUS       WP_284430187             545 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Acidovorax sp. SUPP950].
ACCESSION   WP_284430187
VERSION     WP_284430187.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..545
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=59769
     Region          149..535
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 myrarlslaf aalvalvciq aafvywgthr vndyaqhsrl asdilselld lsankqrlrv
       61 watqrlmnan avpevrerll ermhqsaaal aelarrdlal whelahregm smpqevpqlv
      121 rvtelledni qavearlaql qplepgadfp avweelnatf dmargldlre lingaierqr
      181 savpvaraat ergldvlrqq aitlvivtla vaallalhln rrlqrpldrl lagtralqag
      241 aldhrvatgs kdefdrvaqh fnamaaelqq hrahadaarr eledavqart helsvahetl
      301 qrvdqrrrql fadlghelrt patairgeae iamrggdrpa qeyrqtlqri vggvdqltkv
      361 ihdllliart eadqlvirpr ridlqalvtd aaeqaaalgg lhgvaveplp papggplmvn
      421 adadrlrqal mivldnavry sqrggtvrvg cqpgpdgeaq vlvrdegigi eaeelpavfq
      481 rfvrgqrara hradgtgigl siaqsivhah hgrididsqp gvgtvvqitv psashpetls
      541 peeta
//
LOCUS       WP_284430227             297 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Acidovorax sp. SUPP950].
ACCESSION   WP_284430227
VERSION     WP_284430227.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..297
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31809
     Region          32..292
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 msretalplg daaarpgdag tqheyllrgh gpnagtgvll ihgltgtpne mrllakglhr
       61 agftvlavql aghcgtqddl vatrwqdwha svqrgadrla mvtggrlvac glsmgavlal
      121 alaadrpaqv agvvalsptf rydgwsmpay trlsfllplf rmlgigrrrv fmeqppygik
      181 daalrervva qmqsgdssaa glpgnpwwsv iemralaahv rrrldavrsp clvlharhdd
      241 iasaanaqai vqgvryapve lvllddsyhm itidrerrav vartvafaeh varggtp
//
LOCUS       WP_284430347             433 aa            linear   BCT 25-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Acidovorax sp. SUPP950].
ACCESSION   WP_284430347
VERSION     WP_284430347.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..433
                     /product="Glu/Leu/Phe/Val family dehydrogenase"
                     /EC_number="1.4.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016639 - oxidoreductase activity, acting
                     on the CH-NH2 group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46393
     Region          21..431
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 msntngtrtq helpsylqad dlgpwgnylq qvdrvtpylg nlarwvetlk rpkrilivdv
       61 pieldngtia hfegyrvqhn lsrgpgkggv rfhqdvtlse vmalsawmsv knaavnvpyg
      121 gakggirvdp kklsrgeler ltrrytseig lligpskdip apdvntngqv mawmmdtysm
      181 ntgatatgvv tgkpvdlggs lgrveatgrg vftvgveaak ltglplegar iavqgfgnvg
      241 giagklfaea gakvvavqdh tgtifhqggl dvpallehvk ktggvggfgg adviakedfw
      301 gvdceilipa alegqitkhn agqikaklvi egangpttte addilhdkgv lvlpdviana
      361 ggvtvsyfew vqdfssffws edeinarlvr imqeafagiw hvaqehkvsl rtatfivacq
      421 rilharemrg lyp
//
LOCUS       WP_284430378             441 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Acidovorax sp. SUPP950].
ACCESSION   WP_284430378
VERSION     WP_284430378.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45531
     Region          26..398
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(35..36,39..40,43,75,125..126,128..130,133,153,
                     156..157,160,267,270..271,274..276,279,306,310,360..361,
                     365,369,385,388..389,392..393,396)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mtpsmaagip aadraafgpl qlrvtllcai vamldgfdtq siayvapria edwglkpsaf
       61 gpifaaglfg lmagafllsp aadrwgrkki illstfifgl falltawats mnellayrfi
      121 tgvglgaamp niialtseya pqrlratlvt vmfcgfplgs tlgglisswl iahfdwhsvf
      181 vlggvlplll lpvlaallpe slrylaasga apahyepivk saypgedpat vmtglrgeaa
      241 gvqagfsvfe lfrhgrlptt mllwlaffmn llvmyflvnw lptllksagl plekailsta
      301 mlnlggvvga lalgrlidrf saytvlgaay aasagfiali afsgqnltgl lagaalsgfg
      361 vvgaqigcna laaaiypthi ratgvgwalg vgrigaivgp laggallaaa wtpasiilva
      421 avpavlaaaa vlllgrvrrd a
//
LOCUS       WP_284430433             637 aa            linear   BCT 25-DEC-2024
DEFINITION  B12-binding domain-containing radical SAM protein [Acidovorax sp.
            SUPP950].
ACCESSION   WP_284430433
VERSION     WP_284430433.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   2  (residues 1 to 637)
  AUTHORS   Banerjee,R. and Ragsdale,S.W.
  TITLE     The many faces of vitamin B12: catalysis by cobalamin-dependent
            enzymes
  JOURNAL   Annu Rev Biochem 72, 209-247 (2003)
   PUBMED   14527323
REFERENCE   3  (residues 1 to 637)
  AUTHORS   Ludwig,M.L. and Matthews,R.G.
  TITLE     Structure-based perspectives on B12-dependent enzymes
  JOURNAL   Annu Rev Biochem 66, 269-313 (1997)
   PUBMED   9242908
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..637
                     /product="B12-binding domain-containing radical SAM
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0031419 - cobalamin binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=69755
     Region          201..560
                     /region_name="YgiQ"
                     /note="Radical SAM superfamily enzyme YgiQ, UPF0313 family
                     [General function prediction only]; COG1032"
                     /db_xref="CDD:440655"
ORIGIN      
        1 msastprvla vippmtqlnt pypssayltg flrsrgvtaf qedlalalvl rllspeglqa
       61 vaarvqalpe arrspavqsf aaqqdrylat vapaiaflqg rdstlahria grhylpegpr
      121 fasldvyvdd eggdplgwaf galglhdkak hiatlylndl advlrdavde rfefvryaes
      181 lagsqptfdp ladalaappt lvdemlealt heaiarhtpd vvllsvpfpg svyaafriaq
      241 aikaryphia tvlgggfvnt elrelaeprv fdhfdyvtld agerpllall ehlqgqrgrq
      301 rlvrtfvrgd dgavqyvnmm eadiafaevg tptwdglpld rylslldmln pmhrlwsdgr
      361 wnkltvahgc ywkkcsfcdv sldyisryeg asaavladri eqivretgqt gfhfvdeaap
      421 pkalkalate liernagisw wgnvrfektf tpelaelmad sgciaisggl evasdrllql
      481 mkkgvsvdqv arvtraftda gilvhaylmy gfptqtvqdt vdaleyvrql fangciqsgf
      541 fhrfactvhs pvgknpgeyg vtlaplppgg fakndvafid ptgvdhdalg galkkaiyny
      601 mhgigldedv rawfpfkvpk ttvarhrier alasrah
//
LOCUS       WP_284430465             251 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Acidovorax sp. SUPP950].
ACCESSION   WP_284430465
VERSION     WP_284430465.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..251
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26486
     Region          118..210
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mhrlpwplpa llawaaawla ylglqgrvap vaaliaacav gtaasvlgtg wwrrgliaag
       61 fplslalsga asvpawawlv plallllvyp lnawrdaplf ptphdallgl aravalpaga
      121 rvldagcglg dgllalrray pqarvagvew swplrllcal rcpwaevrrg dlwradwsgc
      181 tmvylfqrpe smaralakaq aemapgtwlv slafevpgat pharlppdgg havwiyrmga
      241 apvagrpaaa l
//
LOCUS       WP_284430450             309 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Acidovorax sp. SUPP950].
ACCESSION   WP_284430450
VERSION     WP_284430450.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 309)
  AUTHORS   Khuri,S., Bakker,F.T. and Dunwell,J.M.
  TITLE     Phylogeny, function, and evolution of the cupins, a structurally
            conserved, functionally diverse superfamily of proteins
  JOURNAL   Mol Biol Evol 18 (4), 593-605 (2001)
   PUBMED   11264412
REFERENCE   7  (residues 1 to 309)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   8  (residues 1 to 309)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14398393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..309
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33341
     Region          42..150
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          82..297
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mpstahstpa papsaaprpr ravsyvsslt pdlfvpagtr pvrakarwlp adtqvlphrh
       61 pwaqvaistt gvirltaaqg tyivppsral wippgvehav tmvqdadlrt lyfhqprgrc
      121 gpgvpigaar addaawrqcr vlevspllra lvcempfepd dsatpptpel lrrerhlsal
      181 iceelrraaa lrlgvdlprd krllhlceav ladptrheal edwardtgas prtvarlfra
      241 elgstftqwr qqvilakava laaerlpvgq iaaelgysas afsamvrrav gmpparflgl
      301 qspaglgpg
//
LOCUS       WP_284430496             781 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Acidovorax sp. SUPP950].
ACCESSION   WP_284430496
VERSION     WP_284430496.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 781)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 781)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 781)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 781)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..781
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..781
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=79673
     Region          17..780
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mnptptapps psdsapgtld lgiggmtcas csgrveralr kvpgvqeatv nlaterahvv
       61 yaasaagvag agaameaqlr ravrnagyep rapqaqdaea rgqspwagfg pvalglalsa
      121 plvlpmllgl lperfgallg phgmlpawlq wllatpvqfl lgarfykagw halkarsgnm
      181 dllvaigtsa gyglslwlwl tapaghaphl yfeasavvit lvllgkwlea rakrqttaai
      241 ralhalrpdv ahlvgadgev dvpvaevmag drivvrpger ipvdgtvleg htqvdesmlt
      301 geplpvprta gealtggsin gdgrvvvqvs avgaetvlar iirlvedaqa gkapiqrlvd
      361 rvsavfvpvv lgialatllg wlwvgaggea avihavavlv iacpcalgla tpaaimagtg
      421 vaarhgilir daealerahr vgtvafdktg tltvgqprlt afevvpgqdg dallaavagv
      481 qggsehplar avvqearrrg lgvpapqavs avpgrgtqgt aagrhfrvgs lrwmeelgvp
      541 lgalaapava lqsagatvsa vaeappgevp tgqeaagpaw vlrallafgd epkpgareal
      601 aalrarglrv vmvsgdhrga aeamarrlgl dpdagevmae vlpgdkaacv arlrseaaag
      661 pgahrparha vamvgdgvnd apalaaadvg mamgngtdva mqaagitlmr gdprlvaaal
      721 dishrtvaki rqnlfwafay nvagiplaal gylspvvaga amalssvsvm analllkrwr
      781 v
//
LOCUS       WP_284430510             104 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Acidovorax sp. SUPP950].
ACCESSION   WP_284430510
VERSION     WP_284430510.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 104)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 104)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..104
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11449
     Region          12..100
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdpipidper lrqaasqavs alkalanedr llllcqlsqg eqcvsdlqar lgiqqptlsq
       61 qlgvlrtqgv vetrregkni hyrvadaall eilavlyrly cpke
//
LOCUS       WP_284430515             318 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284430515
VERSION     WP_284430515.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..318
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=33079
     Region          1..317
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mkpftyeraa svqaaaaaaa gnpqarfiag gtnlldlmkl qieapthlid inglgldrie
       61 pvpegglrig alvrntdlaa hagvrrdygl lsrallagas gqlrnkatta gnllqrtrcp
      121 yfydtnmpcn krqpgagcaa iggvtrqhav vgaseaciat hpsdmavamr aldavvetvr
      181 adgqprripi adfhrlpgnt phietaldag efitavtlpt paggthiyrk vrdrssyafa
      241 lisvaavlqk dgtgrvalgg vahkpwrmas adaalpqgaq aataqllgaa rpthenafkv
      301 alvertlagv laeakgqs
//
LOCUS       WP_284430521             145 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Acidovorax sp.
            SUPP950].
ACCESSION   WP_284430521
VERSION     WP_284430521.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..145
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16033
     Region          2..106
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mnikkssest cpiarsldvl gdawtmlilr dansgltrfd qfkkslgiap tmltkrlatl
       61 tdekllekrq yserppreey vltqagrdyl pvlfmigawg rkhrgagqlv rfldaengtd
      121 iqpvaidavt gaeigtraik mvnpe
//
LOCUS       WP_284430568             130 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA recognition motif domain-containing protein [Acidovorax sp.
            SUPP950].
ACCESSION   WP_284430568
VERSION     WP_284430568.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Muto,Y. and Yokoyama,S.
  TITLE     Structural insight into RNA recognition motifs: versatile molecular
            Lego building blocks for biological systems
  JOURNAL   Wiley Interdiscip Rev RNA 3 (2), 229-246 (2012)
   PUBMED   22278943
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Clery,A., Blatter,M. and Allain,F.H.
  TITLE     RNA recognition motifs: boring? Not quite
  JOURNAL   Curr Opin Struct Biol 18 (3), 290-298 (2008)
   PUBMED   18515081
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Maris,C., Dominguez,C. and Allain,F.H.
  TITLE     The RNA recognition motif, a plastic RNA-binding platform to
            regulate post-transcriptional gene expression
  JOURNAL   FEBS J 272 (9), 2118-2131 (2005)
   PUBMED   15853797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..130
                     /product="RNA recognition motif domain-containing protein"
                     /GO_function="GO:0003729 - mRNA binding [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=12894
     Region          2..86
                     /region_name="RRM"
                     /note="RNA recognition motif (RRM) domain [Translation,
                     ribosomal structure and biogenesis]; COG0724"
                     /db_xref="CDD:440488"
ORIGIN      
        1 mgnklyvgnl pysfrdddlq qtfsqygnvv sakvmmerdt grskgfgfve msndaeaqaa
       61 iqgahgqnfg grdlvvnear pmeprpprsg gggfgggngg gggygggggr sggfgggggg
      121 ggygggrssy
//
LOCUS       WP_284430635             390 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Acidovorax sp.
            SUPP950].
ACCESSION   WP_284430635
VERSION     WP_284430635.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..390
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41758
     Region          <29..360
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 matlpawpaa paraatatpa apeaglawif edprskalla eveqvapsda gvlitgesgt
       61 gkeliarylh srsprsaapf vavgcgafse alvdselfgh esgafpgafg aqpgwfeeah
      121 ggtifldevn dlplavqnkl lrvlqqrevv rvggrqpipi dvrivaaasv dlqalvlqqr
      181 frkdlyyrln vvslevhtlr erpgdivpla rhfidaysrr lgyprpqltp aaeralqqap
      241 wpgnvrelen tihrtlllge grtldaadlr lsgtarpgte peapapaapp qapspsppgl
      301 pllrqavrql ceahvpalyq tvedavllev frwchysqse aarvlglsrn vvrarlirlg
      361 evgaprraga dagappaefp sdtdsespsp
//
LOCUS       WP_284430663             680 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: two-component system sensor histidine kinase NtrB
            [unclassified Acidovorax].
ACCESSION   WP_284430663
VERSION     WP_284430663.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 680)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 680)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 680)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 680)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 680)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 680)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..680
                     /product="two-component system sensor histidine kinase
                     NtrB"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009399 - nitrogen fixation [Evidence
                     IEA]"
                     /calculated_mol_wt=75680
     Region          310..679
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 mtdgepflwp whrwrsawkr wslwallvll vagmlvtqvw lagryeasev qnrldrdaad
       61 avadirqgfa hnlqnlqalh vgtpdlaswe sraaallsvr relvrlewrs ptlevrahve
      121 tpyrpvqwda emrsgmhsni alacanarrv sgpsysgsyf qpqgdgrgse mmelclplmq
      181 dgrnegfvva tyslhnvlid lvvpslkrgq evsfteadgt rlamvgasrr gtrlfsaqql
      241 fdlpgatlvl rmdswhsaps vfpnvltalv tamsialvtv lvvlvrdnrr rlraerdlgd
      301 alafrkamed slvtglrard lqgrityvnp afcemvgfta qellgqsapv pywppefade
      361 yrqrqairls slhpppregy estfmrkdgv rfpvlifeap linaqglhtg wmsafldvse
      421 qrrveemsra sqerlqatar latvgemasl lshelnqpla aissyasgsl nllppgggpp
      481 qeplhdvhva lqriaqqaer agrvirsvhd fvrrrdqsre vvsvhdllea vmplirlqar
      541 klevfvkisv dadlppvlcd rtmveqvlln larnsmqamd dpatpqrile lrvrraasna
      601 hnawlefmvi drgcgiaqdv geklftpfft trpegmglgl slcrtvveqh ggflghapne
      661 prgtvftftl paasadsshp
//
LOCUS       WP_284430818             144 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: GlcG/HbpS family heme-binding protein [unclassified
            Acidovorax].
ACCESSION   WP_284430818
VERSION     WP_284430818.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..144
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=14364
     Region          9..131
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mqmpetglsr lsasqaqqlv qsalitglde glavsaaavd ssghllafar addaflgsid
       61 asiakartav yfrrdtaamq qaleqgktay laladvlple ggvpllvggt lvgglgisga
      121 asaqdgvlar aiasllnsls gwtp
//
LOCUS       WP_284430835             262 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Acidovorax sp.
            SUPP950].
ACCESSION   WP_284430835
VERSION     WP_284430835.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..262
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=28600
     Region          7..254
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mtkpfrltas tgihkgdrey qqdqvaliah pryngcvlgv vadgmggrsg grkasdqvml
       61 tarqwferys pdtddtatml khmveeahiv irltaisaeq ephstvaafi inprgdchwa
      121 hagdsriyhf qgarlahrts dhsyvqalvd rgeiteaean thphsnilvg clgtesdppv
      181 aqhmipqllp gdvllacsdg vwhyfspael asvvdslspr eateflieka rsrargggdn
      241 lslaivkiea lveekkparl vr
//
LOCUS       WP_284430877             327 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284430877
VERSION     WP_284430877.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..327
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33757
     Region          23..325
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mirsllsfta lalalgataq aqtpppaaty ptkpvrlivp fppgggtdil srlvatklte
       61 vtkwtvvpdn ragaggtigi teavkaaptg ydlvmgqkdn lvvapwlykn lpwdptkdlv
      121 avahvaytpv iiatgansrf ktladvvaaa raepgkityg spgngttihl agdlfekaag
      181 iklshipykg snpalmdala gnvdllvssv psamgqiksg klrplavtsa krssslpdvp
      241 tvaesgykgf dvsswygifa pagtpanvvt tvnaevnkll aspemqaaiq aqgaepesls
      301 aaqfsmllkt dyakwkgive asgakie
//
LOCUS       WP_284430934             198 aa            linear   BCT 25-DEC-2024
DEFINITION  OmpW/AlkL family protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284430934
VERSION     WP_284430934.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006882
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..198
                     /product="OmpW/AlkL family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21152
     Region          16..198
                     /region_name="OmpW"
                     /note="Outer membrane protein OmpW [Cell
                     wall/membrane/envelope biogenesis]; COG3047"
                     /db_xref="CDD:442281"
ORIGIN      
        1 mkknllalav lcaltsgaaf aqtaegpwlv rarvvnldss nkdstglgls indktlpevd
       61 isyffnrnia aelvltvpqk qrlsssalna qigtlkhlpp slmlqyhfdt agfrpyvgag
      121 vnytrfssvr lpagvsidks swggalqvgv dipltknlvl nfdvkkvyiq tdvfaagakl
      181 gtfkidpvla gvglgwrf
//
LOCUS       WP_284430946             315 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284430946
VERSION     WP_284430946.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..315
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=32729
     Region          16..312
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 maialaaafa gpawaqggyp nkpvtlvvpt aaggttdlsa rmlaqalgpv lgqsvvvdnk
       61 gggngniaag avkraepdgy tllmqysgyh visplltrqk qwepgdfqpi anvlsapqii
      121 vvrdglpvkt ladliayaka hpgklnyass gngslqhvtg amleqqggvk mvhvpykgtg
      181 palqdllggq vdltfgtapp fmphiqagkl rvlavtgkqr laslpdvptt aeagypkvda
      241 tswfalfapa hvpkavvdkl vadvrtvvqn pafqqkaleq gatadyqgpq plaervkadl
      301 anwaqvvkas riead
//
LOCUS       WP_284430987             295 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Acidovorax sp. SUPP950].
ACCESSION   WP_284430987
VERSION     WP_284430987.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 295)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 295)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007114
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..295
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28972
     Region          58..153
                     /region_name="CytC5"
                     /note="Cytochrome c5 [Energy production and conversion];
                     COG3245"
                     /db_xref="CDD:442476"
     Region          <220..292
                     /region_name="CytC5"
                     /note="Cytochrome c5 [Energy production and conversion];
                     COG3245"
                     /db_xref="CDD:442476"
ORIGIN      
        1 msdtpheeah tgpiknpkql lltvffsfvv pifaiiglvm yvtsgtkpad gaanperala
       61 eriqkvgmve vrdanrplrp geevfkgqca achatgaaga pklgdaaawg priktgfeal
      121 vhsalagkga mapqgggdfn dteiargvay manaagakfe epaapaaaga sgaatgasda
      181 aaaptaaaap asaaqataaa apapaaapat ptttaaagag ealykqacqv chaagiagap
      241 kfgdkaawae rlkdgidgmt riaiagkgam pprggtqasd adihaavefm anaak
//
LOCUS       WP_284431208             356 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Acidovorax sp. SUPP950].
ACCESSION   WP_284431208
VERSION     WP_284431208.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..356
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36049
     Region          41..353
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtppganart arrsavplri alrraapwgi alalallvma sltagsapvs wreavaalag
       61 pwagafgapa gdmaqaivrd lrlprvvlal lvgatlalvg gllqsttrnd ladpflfgls
      121 sgastgavav itltgewlga wtlpaatfag avvaagavll lvrraggqgp aqtvlaglav
      181 sflfgalthg lvfagdqraa havvfwslgg lglarwdnlw laclglavpm vfvwrrhral
      241 dallagddta hslgiaperl rtqafvvaav ataccvalag vigfvglmvp hlarrlsgpl
      301 haaflplagv mggalllasd laartllgsq elpvgivtag igavfvmall rrrvad
//
LOCUS       WP_284431238             665 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidase U32 family protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284431238
VERSION     WP_284431238.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..665
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=73786
     Region          6..307
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
     Region          457..518
                     /region_name="DUF3656"
                     /note="Collagenase; pfam12392"
                     /db_xref="CDD:463557"
ORIGIN      
        1 msllphhiel lspardadig ieavnhgada vyiggpafga ragagndlrd lerlvrhahr
       61 fhsrifvtln tilrddeleg arqmawqvyn agadaliiqd mglleldlpp iqlhastqtd
      121 irtpekarfl qdaglsqivi areldlqeia avraatdpar ttieffvhga lcvaysgqcy
      181 ithahtgrsa nrgdcnqacr lpyevldgsg riiahekhvl smkdnnqsdn lralidagvr
      241 sfkiegrykd mgyvknitah yrklldeiie erefsaepla rsssgrttft ftpdpdqnfn
      301 reftdyfvng rqddigafdt pktpgraigw vtkvgenfae lelsspdtvl hngdglcyyd
      361 lqkelvglqi nraeavnark glwrvfpkdp iagfkdlrkg leinrnrdmd wvrtldkkss
      421 drriglwaql setpdgfdlt ltdedgfvgs aaivhphqra tdgpqaeatl reqlgrfgat
      481 vfsvhdials lsqpwfvpas alnplrrdav aalesaraag lvrlpraepv qppapfpedt
      541 ltylanvfnq kahdfyvkhg vkvidaayes keeegevslm itkhcvrfsm slcpkqakgv
      601 igvkgtikae plqlingkek ltlrfdckpc emhvvgkmkk svlnqhardm qavpmqfyrt
      661 rpvag
//
LOCUS       WP_284431440             501 aa            linear   BCT 25-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284431440
VERSION     WP_284431440.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..501
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=52349
     Region          14..497
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mllfdprsia vpaghfiggr lvpdagriav lrpsdgqwha dlpladaatv daavqdawqa
       61 wrttdwarra prerarvlrr wadmieadgp qlapleavcs trpvrdaaaw dvpftaeglr
      121 ffaeyadklg gevaatrhdh lgmvvaepyg vvgaitpwnf plvmmswkvg aalaagnavv
      181 lkpsemtpfs avrlaqlave agvppglfnv vqgdgrttgd altrhpriak mtftgstrtg
      241 aaimatcalq gpkpvtlelg gkspqlvfdd apdidrlagl iagaitgnag qvcvagsrli
      301 vqrgiaaelv erigarfaal rpgatwdgta tlppiisapq aarildiver ardagaqlrc
      361 ggglfddvag gvaagaagga yfqptllegv aadspavqee ifgpvltvqt fdteeeglal
      421 aahahyglaa gvhtadigra lramrgisag tvwinrygrs adfviptggy hqsgigkdlg
      481 rqaveanlrf ksvlidfaaa h
//
LOCUS       WP_284431451             388 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284431451
VERSION     WP_284431451.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..388
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=41436
     Region          8..383
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mppqahvspe apndqfrsls pavwrastvl fdtvadftsr kdrlfdgyty gvtgtpttra
       61 leervaaleg ahhcvavpsg qaalclials lleagdhvli adsaygplrt fardylqrfg
      121 iehdtfdpla gaglaswlrp qtklvflesp gsitmemqdi paivevtrta gvrtvldnsw
      181 asplgfrgip vgvdivveaa skllsghsdl llgtiatdsr slyeafrttq svlgqavsae
      241 dcflalrgmd tlevryshqc asalavasal tshdavtevl fpprpgdrsh trwaasftgg
      301 gcvlsfvphf hsdaaihqff salrvfqiga swggvhslaa yypeteqrkr khcafsagiv
      361 rlsiglepsg kliadleqal haagalps
//
LOCUS       WP_284431452             365 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284431452
VERSION     WP_284431452.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..365
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=38139
     Region          41..363
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mividldskv lsftglrntr tapwcwwvgp tnierttamd rrsllqkgga asaamllpga
       61 slwaqapypd rpiklivpws aggstdvlar avgqsmadgl gkpvvidnrp gaagrlgvda
      121 mvksaadgyt laiielahai apsiyqkmpy dimndsaais tlgvsplvlv vdaqkyqagq
      181 hqkfvadakk aaeplsiats gtgsishlaa glyakeakle lqmipykgsa paltdvaagv
      241 lsghfctlas asslfsagki vplmvtgnrr vpqlanvpsa selglntmdf gqwwalvapv
      301 kvpkpiital hkatatalad kqvqsrissl aiqlgscspd eaqafiraea ikwakvvnsl
      361 gikpe
//
LOCUS       WP_284431585             157 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Acidovorax sp. SUPP950].
ACCESSION   WP_284431585
VERSION     WP_284431585.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..157
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=16014
     Region          1..139
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mafgrlertt gpqpmsdinm tplvdvmlvl vvifiltapl lassirldlp radgatpgap
       61 pqsvtvvldk egqaylddvp lapqalaarl aqlareqpdt evqlradtav pygrvvevmg
      121 aanaaglrri gfvadpaapg ipsaasaspa aaaaavr
//
LOCUS       WP_284431695             296 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Acidovorax sp.
            SUPP950].
ACCESSION   WP_284431695
VERSION     WP_284431695.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. SUPP950
  ORGANISM  Acidovorax sp. SUPP950
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 296)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Acidovorax sp. SUPP950"
                     /db_xref="taxon:511901"
     Protein         1..296
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=32272
     Region          6..277
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mtterhvflt ggtgfigrhv laslleaghr vtvlrhpada palvhprlvw lsramdqlap
       61 adlagadvlm hlaspgvppq qadwqtlfyw nvtvllqlld taraagvkrs vlagtfaeyg
      121 rsadafdfip asaplapayg yaaskaagfq aahahaieha melcylrifs vfgegqyagn
      181 fwpalrlaas qgldfsmtpg aqvrdyvpve tvarafrhaa errdvetgrp wvrnvgsgrp
      241 vsmqdfaqhw wsvwkasgrl lvgalpyrpn evmrcvpeme adlflsgseh egqrfa
//
LOCUS       WP_284431935             779 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284431935
VERSION     WP_284431935.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 779)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 779)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 779)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 779)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 779)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..779
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..779
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=83572
     Region          40..773
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 msaeatnpat pgpvagpaar wraridlrrl graallgpaa rdrlpdaigh vadahrahhp
       61 dadleplrra wvlaesshrg qmrksgepyi thplavtlil aelgaetttl tasllhdtve
      121 dtdvtldqvg eefgaevrfl vdgvtklekv dygaaaepet frkmlvatgn dvrvmsikla
      181 drlhnmrtlg vmrpekqari akvtrdvlip laerlgvqal kteledlvfa ilhpeeyeht
      241 relivdnasr addplaeiad evrgvlreag iqaevvirpr hfvsvhrtar krgrlrgadf
      301 grllvlvged adcyavlgel htcmtpvvse fkdfiavpkf nlyqslhtav argdgqvvev
      361 lirthqmhkv aeagvvalgn pyvgppeeps aldgervdpt rpgwlsrlld wqaaapdadt
      421 fwstlredla qdreitvfrp dggtlglpeg atcvdaayaq ygedahaclg arvngrlatl
      481 stvlkdgdtv qllmgqdpaa epskewleha htpaariaiq rwiathpshe taegeeaeer
      541 ggtvdatpat kaedvretqv gqvargdadp vrtsatesra adtpdsggri iaearasdgp
      601 dlddpaadga gadragvdrp aadrpaadrp gaavtlidpp gatvrlagcc tpvppdeitg
      661 favrggvvtv hrvecaavdr mkgvgrrevg vrwgdtaecr vtlyaesfgr phlladltea
      721 magegaeivs atveppsqqr vrhtytvqlp daallpalmr amrnvagvyd vsraqtlgg
//
LOCUS       WP_284432128             110 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Streptomyces
            sp. TUS-ST3].
ACCESSION   WP_284432128
VERSION     WP_284432128.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..110
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12117
     Region          9..>81
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 msgprtgepv rvvlrmeivs grerefeelw leiartigrs panrgqvlar agavdgasvy
       61 yvytdwtdea sfrafetsrd hednrrrlgp lraggdmtvt avvhtlegpa
//
LOCUS       WP_284432200             400 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284432200
VERSION     WP_284432200.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..400
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41053
     Region          29..376
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mskrltcdvv vvgagmvgaa calfaaragl dvivvdrgpv aggttgageg nllvsdkepg
       61 pelelallsg rlwadlakev gdaveyelkg gvvvaatpea lealdrfatg qrsagvgaqr
      121 vdadelrsle phlapglagg vlypqdaqvm ptlaaahllr ssgarlfgga vtevlrgadg
      181 avrgvrtdrg eihapqvvna agtwggelaa lagvhlpvlp rrgfvlvtep lprlvrhkvy
      241 aadyvadvas dsaalqtspv vegtaagpvl igatrervgf drslslpalr alaagatrlf
      301 pflervramr tylgfrpylp dhlpaigpdp rvpglfhacg hegagiglst gtgrliaqal
      361 tgqapdldla pfrpdrfpas ppasvshpsp rpssdteeas
//
LOCUS       WP_284432355             346 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            sp. TUS-ST3].
ACCESSION   WP_284432355
VERSION     WP_284432355.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..346
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=36726
     Region          4..310
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mtrravviga tgqigraava altgdgwavt avsrgggrde gwpaevrtar adrgdddala
       61 aavgegcdvl vdmvaygpad arqllsladr vgsavvissv svyeddkgrn fdtqgepegf
      121 pefpvrvted qrtiapgeas ystrkagler ellaagdrlp ttllragaih gphcrtprel
      181 yfvkrnldgr prrllayggr srfhpanvhn iaelvrlaaa tpgsralnav dpdaptvaei
      241 aaaidavmgv etesvlidgp ppsptvgdtp wsvpvpvvfd msaaerelgy rpvvarypdr
      301 laetvafieg qlagrdwkea ypkmfqtygd lfdyaaeday ldspga
//
LOCUS       WP_284432437             245 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family oxidoreductase [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284432437
VERSION     WP_284432437.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..245
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=25644
     Region          7..244
                     /region_name="fabG"
                     /note="3-oxoacyl-ACP reductase FabG; PRK05653"
                     /db_xref="CDD:235546"
     Site            order(17,19..20,22,41..43,89..91,139..141,154,158,
                     184..185,186)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187535"
     Site            order(113,141,154,158)
                     /site_type="active"
                     /db_xref="CDD:187535"
ORIGIN      
        1 mgnlsfdftg htviitgaar giglvlgrhl rtsgadvvlv drdedelrva aeeldtlwva
       61 advtsssdae rvvatalaet grvdvlvnna gilrdgvlwk ltdddwdavl avhaggtfrf
      121 tracvphfra qrygrvvnvt sysglhgnig qanyatakag iigftrtaak elarfgvtvn
      181 aispnaetrm vssvpaekra eltagipmgr fgdpsemcaa vaflaseeag yitgavlpvd
      241 gglsi
//
LOCUS       WP_284432655             444 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284432655
VERSION     WP_284432655.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 444)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..444
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47307
     Region          40..415
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(146,148,285,287,318..320,365)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mgvrrrrhrl aaagtvaglm fataacgsgs gsagssdpnt levwtrsnpd daatydrvfa
       61 aftrktgiri dyqpvinfdq qlqsrastrd lpdvmindta lmgsyqsqgl lkpvdpasia
      121 ggdritaksw sstvgvdgkh ygipysrqaq tlmirkdwlk klglkapttw qemlsvakaf
      181 atedpdgdgk adtygivapa saqngyaamw gssflwqgga eiirpdgkgk ytpamdsaaa
      241 vhavtwmkdn lfcgekgvvq pgaitavtgt atnfqdgnag mymtgpynit tydttpgkkt
      301 yevvpapagp aggdvladge nvylgartgk drqelalasf lvspegqria mtsvdghqpv
      361 vripvnttld aakvrndprw svvqkayeta seqfpnapdf apikqdtada lnsiftycgg
      421 dvrsqlkeln dtlagdlkdq dllk
//
LOCUS       WP_284433003             215 aa            linear   BCT 25-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284433003
VERSION     WP_284433003.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..215
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=22713
     Region          5..198
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mtealhhrmy llaydeaarg pydrsrtgll vraavltela lrgrltdagd ggvtvtgtgs
       61 tgdpvldevv ddvlrgargq gwkqlvrrrr rrtltavedr laalglvtvq sswtgrgrrv
      121 tvsdraalra vhdrvsavlh gdapvheipa adtaltalaa agkvrsvlsr rdarvlrerv
      181 dactnrlgal apgleravqg lnttmiaaqg gmggg
//
LOCUS       WP_284433007             379 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284433007
VERSION     WP_284433007.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..379
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=40433
     Region          125..374
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mshaiqrase laldettvta lraelkttad evvqaiidev ppyanalsgh mgatirravr
       61 talghyldla sgkatggdag daayelgrge vrdgrsmdal lsayrvgarv awrclaagav
      121 paglpaaeva kfaeltfayi delsaasaag hadelaargr dherhlehla rdllagaspd
      181 vllasaqrag wqppgsltav llpaaqarpa yrtldpstlv lddlpdatgv llvpeadrsh
      241 llrqlterta vvgparpwvr asasyaravr arslsadird tedhlpelvl sadvdafadl
      301 raralaplrt lpaatarrle etlrewllhq grrdevaaal fvhpqtvryr msqlrelfpd
      361 laspqrvlel tlavglgad
//
LOCUS       WP_284433053             423 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284433053
VERSION     WP_284433053.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..423
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44675
     Region          144..411
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mrssrlvaas lvgvvvsgla vpnavaasag ftshrapals apsspskgat ltlpaprgry
       61 atgesafrlv dderadpwvp gqqyrelmis vfypavhtgg rpfthqfpta vaaavgtsve
      121 annelpaglv nwaatrthsv rdaapapgrf pvvlyspgag dprdwnvtla edlasrgfvv
      181 vtvdhtgeap avqfpdghmv gngpmmtawa dafrngttla fltkvmaart adtelvlerl
      241 tslparltrv mdlhrvgmfg hsgggftaan amygdprika ginmdgtley nvepdgtnls
      301 evalhgldqp fllmgsssad ggsdvhreps wasfwrhqrg wkadvtlnds vhasftdaea
      361 llpqlagrvp detlaaavgt vdsrravaan ralvasffdr flkgrddhll dggpsphpit
      421 fvr
//
LOCUS       WP_284433097             300 aa            linear   BCT 25-DEC-2024
DEFINITION  amidohydrolase family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284433097
VERSION     WP_284433097.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..300
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32560
     Region          3..291
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mtridahhhv wrlkdspkdt pgpsprphdw ldtpamkpvr rdftlddlaa etastgidrt
       61 ilvqvlpdae etaefltlaa ssdlvagvvg wadltaadma dsldalrrgp ggellvgirh
      121 lvqaeadpaw lnrpdvrrgl gavadanlvy dlltvphqlp aalatvralp eltfvldhvs
      181 kppiasgeqe pwaarvrela aepnvfckls gmvteadrrt wttddlrpya dvvldafgps
      241 rvmfgsdwpv cllaasyqqv vrtteeltsa lsaaeraevf ggtaarayrl plerlreeap
//
LOCUS       WP_284433086             347 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284433086
VERSION     WP_284433086.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..347
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36472
     Region          23..339
                     /region_name="Tdh"
                     /note="Threonine dehydrogenase or related Zn-dependent
                     dehydrogenase [Amino acid transport and metabolism,
                     General function prediction only]; COG1063"
                     /db_xref="CDD:440683"
ORIGIN      
        1 mtlatrylsa rtldtapvts tppgpgevel apayvgicgt dlhifhgdmd trvavpavlg
       61 hemagrvvrv gpdvedwapg davtvmplrw ddtcpacrng hqhicqhldf igidspgamq
      121 qrwtvpastl vrlpdslpld raalveptav avhdvgraev rdgervvvvg ggpvgvlial
      181 vaqaaggdvr vvelsahrrl laeelgltvw dpaaddlael vgqwtggaga dvafevsgaa
      241 ggvdtavevl gvrgrlclva ihsrprevnl hrffwreltl vgarlydrsd fekavalvad
      301 gtvpadrlis kvvpltqapa afealegggd vmkilvdctd eaqeaav
//
LOCUS       WP_284433112             343 aa            linear   BCT 25-DEC-2024
DEFINITION  saccharopine dehydrogenase family protein [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284433112
VERSION     WP_284433112.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..343
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35996
     Region          5..341
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 matghtvtvy gayghtgrfv vahlqergfv pvlsgrdapk lkaladeypg levrpasvdd
       61 pasldhalag aaavinaagp fattaapvie aalragipyv dvaaeieana dtftqfadra
      121 rdtgtaivpa mafygglgdl lataamgdwt eadeahiayg ldhwaptdgt raagkvsaer
      181 rngrrvrftk gqleyhsddl ptlrwsfpdp vgqrsvigef tmadvvtips hlsipevrty
      241 mtteaatgva spdsptptav deqgrsaqtf lvdvvvrrgg terravaggq diyavtapla
      301 veavhrlltg rtrtvgvasa gemfdapdfl ralsphisle vap
//
LOCUS       WP_284433137             108 aa            linear   BCT 25-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284433137
VERSION     WP_284433137.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 108)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..108
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12187
     Region          3..107
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 msldtpqaet rrerltkhea lerleherts rltqlraide arsdaeeqvm stqkdtikrv
       61 laeveaafar vgdgsygncr ncakpipver leilpytpfc mpcqrdaa
//
LOCUS       WP_284433163             463 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284433163
VERSION     WP_284433163.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 463)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..463
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=49069
     Region          24..463
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mqnaqrsnms vsrpphvdnr vwgdedevva aavnyawrrl trapdpvsga rsaadlalaa
       61 gtaitpwgig geaalklfdr vlapatraqn avtnlayipa aptraalafe avtgaanifa
      121 gtweagagai haenealawl tkllgwpdts agcfvsggts gnlsalvaar aaaaglrsrp
      181 tdgwkivcad sahssirtaa qamdvevvta avdregrltg aavsaalesv dgvfavvata
      241 gttnaglvdd legiadacer hrvwlhidga yggaglaaps vrhlysgier adsfivdphk
      301 wlfapydcca llyrdpavar aahsqsahyl daidrdvhnp adlalhlsrr arglpfwfsl
      361 avhgtdryar aveqtlttsr lvadairasd hlrltidphl svllferpgw sprdyaswsa
      421 rvaetgamlc vptrwndttv lrmafvnpdt raadvihvld tlr
//
LOCUS       WP_284433181             115 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Streptomyces
            sp. TUS-ST3].
ACCESSION   WP_284433181
VERSION     WP_284433181.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..115
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12698
     Region          14..90
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mtepapaslp dppyyavvft avrtagdngy gemderlfrl aadqpgflgv daarradglg
       61 itvsywrdee siaawrnhae halarahgre hwytsfslhv akveraycft radda
//
LOCUS       WP_284433205             539 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284433205
VERSION     WP_284433205.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..539
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57434
     Region          1..503
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mpdavvigag pnglvaanvl adagwsvevl eeqpepggav rhdrgvdpaf vsdlfssfyp
       61 laaaspvlaa lrledhglrw snapsvlahp ltdgscalld rdldttaqsl dtfapgdgda
      121 wrrldevwqs lrhdildalf tpfppvrata rlawrlraag glrmartlvl pvrrlgeeef
      181 rgqggrllla gnalhadlap esagsggfgw lmsmlgqtyg fpvpvggsga ltqalarrle
      241 argghvrcgq rveevvvrgg ravgvrtagg davparravl anvsvpalyg rlldpehlpa
      301 qllddlrrfq wdfatfkvdw aldgpvpwra eqasragtvh ladgvdeltr faaqlamrqv
      361 pdrpfllfgq mttadatrsp rgtesawayt hvpheigada adegitgqwd tkdqelmadr
      421 veaqverfap gfrglirarr ilapptlqam danlsggain ggttalhqql vfrpvpgtgr
      481 petpvpglfl assgahpggg vhgapganaa raalhrhrpp gltraqrllt rrdrtgsrr
//
LOCUS       WP_284433248             264 aa            linear   BCT 25-DEC-2024
DEFINITION  S1 family peptidase [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284433248
VERSION     WP_284433248.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Perona,J.J. and Craik,C.S.
  TITLE     Evolutionary divergence of substrate specificity within the
            chymotrypsin-like serine protease fold
  JOURNAL   J Biol Chem 272 (48), 29987-29990 (1997)
   PUBMED   9374470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475742
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..264
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=26757
     Region          35..257
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mpiraarttr pttrttavvt tavlaaaalw staapasaik gggpattkar pyamliefeg
       61 rqfcggtlva ptklltaahc vesagdvatl tvvggrtrvd gtdgkeravt sarldsrygg
      121 pgsahdaavl tldrpmpyrt ipvagpkdgk lvadgrtatv vgwggtgpge qatrlkqakl
      181 vlspvaacqp ytdpetdpaa mlcgkprpgt tdsicpgdsg gplisggkvv givssgnkyc
      241 deqypvsvfv radsvaadlg iptr
//
LOCUS       WP_284433343             478 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284433343
VERSION     WP_284433343.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..478
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51613
     Region          1..317
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msslptstpa aqgvdaagiq afldaleaep nlhphslmll rhgqvvasgw wapyapdrpq
       61 llyslsksft ataagfavae glirlddpvi syfpefeadi tdprsrtmlv rhvasmasgh
      121 aeetldrara rdrdelvrgf llvppdrdpg tvfaynqpat ytlaavvqrv tgqklteylr
      181 prlfeplgig evawiadrrg relgfsglha ttdaiarlgq lhlrggvweg erllpeswva
      241 eatrvqiahe apavggwsdw qqgygfqfwm srhgyrgdga ygqfcvvlpe qdavlaitse
      301 tvdmqkvldl awehllpafg agplpggeaa daaladrltr laappaegkp apadraqdwn
      361 taftphggtc vdqptltaie vdpggrvtlv ddgdrlelaq aaaqsgwtvv depvpvavsg
      421 gwtdaetlvv dvafletphh llvtcslgdr tftarwrtqp lhagplrrmr apvqsegt
//
LOCUS       WP_284433399             312 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            sp. TUS-ST3].
ACCESSION   WP_284433399
VERSION     WP_284433399.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..312
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=33745
     Region          15..312
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mttnqsqsqs qsqsillaga sgvlgrhiak altdaghkvt glgrsegngv radlmdrdal
       61 lravdgqhfd tvvhaatalr kppmrhrdmh atdalriegt ahlieaaqlt garrfvaesm
      121 vfgygygnfg drliteddey gprgadaele rhlagmrtke qltfgtpgle gialrfgafy
      181 gaggtetive llrkrqlpvp adrdrvlpwv elsdagrava aavehgrpgq aynvvdrtpm
      241 gfrghllcva eefalpkpmt vplwatrpls yahtmfrarm rvsaakaere lgwtpaypss
      301 rdglaalraa tr
//
LOCUS       WP_284433259             319 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284433259
VERSION     WP_284433259.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..319
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34798
     Region          72..314
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          229..316
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 metlvfdsdd ldrteeffsq ayarmrigng tpdssrarih rsaidsvsvd eleldfdmsy
       61 avtplgricl cmvhegtied hvyqgvsdsf gpgdvvsfap pelsyagrvh aarynitmld
      121 pslldqvaat agtrrpepvr ltghrpisaa agdrlrttir ylqdhvlada avadhplvas
      181 taaqhlaaav latfpntast dptgpdrqda hptalrrala fiddhadrpl tvaqiaeaah
      241 isvralqyaf rrhldstpla yvrrvrlaha hdelaaadpe dgstvtdiaa rwglyhpgrf
      301 atlyrdsyer apsrtlheg
//
LOCUS       WP_284433462             514 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284433462
VERSION     WP_284433462.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 514)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 514)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 514)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..514
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=56219
     Region          3..495
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mtllvvigsa vgahllgrta easdrllrgi qpaqteayrl qaalvnqetg irgyaitadr
       61 qflapytqgk rdqansgarl religdrpel aadlkaiesq aadwrrsyae plaasvtpgr
      121 pkpldqqkad qgkkefdrlr tlwnrqttdl tkaveqgrsh laheravrns vlggmlavfl
      181 lagiacavlv rilvtrplea lrtasmrvsg gdfdyvitgg gpadltavan avegmrwhiv
      241 aeleasrdhq relsrqaadl deqavelrrs naeleqfayv ashdlqeplr kiasfcqlle
      301 krygdklddr grqyidfavd garrmqvlin dlltfsrvgr vndarvpvgl dqaldkalan
      361 lgtaveesda rvdrpehlpe vvgdptllam lwqnlvgnal kfrhpdrtph vsitcgtdpa
      421 epgsllicvt dngigipeqf kekvfiifqr lhgrdayggt giglalckki veqhggriwi
      481 dtahtdgtrf cftlpsiaes peasgigtee kvlt
//
LOCUS       WP_284433485             266 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284433485
VERSION     WP_284433485.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 266)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..266
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28694
     Region          1..266
                     /region_name="COG4587"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443644"
ORIGIN      
        1 mgswrlyaav aaggfrryat yraatfagvf tntvfgvilv ytylalwdek phlggydqaq
       61 avtyvwlgqc lystlalqgg gaekdvieri rtgeiavdly rpadlqlwwl asdlgrslfq
      121 ligrgvipfa fgalffpmal ptdvtswaal fvalllamiv sfgirylaal svfwlmdgmg
      181 imqavmitgv fcsgivfpln afpgvlgdiv ralpwaaqlq mpadvlmget dplgayafqa
      241 twavvllaag rllqsaatrr vvvqgg
//
LOCUS       WP_284433562             520 aa            linear   BCT 25-DEC-2024
DEFINITION  purple acid phosphatase family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284433562
VERSION     WP_284433562.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Klabunde,T., Strater,N., Frohlich,R., Witzel,H. and Krebs,B.
  TITLE     Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on
            crystal structures
  JOURNAL   J Mol Biol 259 (4), 737-748 (1996)
   PUBMED   8683579
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11244734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..520
                     /product="purple acid phosphatase family protein"
                     /EC_number="3.1.3.2"
                     /GO_function="GO:0003993 - acid phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=56724
     Region          11..>75
                     /region_name="DUF839"
                     /note="Bacterial protein of unknown function (DUF839);
                     cl23843"
                     /db_xref="CDD:474079"
     Region          73..161
                     /region_name="Pur_ac_phosph_N"
                     /note="Purple acid Phosphatase, N-terminal domain;
                     pfam16656"
                     /db_xref="CDD:465220"
     Region          185..470
                     /region_name="MPP_superfamily"
                     /note="metallophosphatase superfamily, metallophosphatase
                     domain; cl13995"
                     /db_xref="CDD:472684"
     Site            order(193,195,220,264..265,356,392)
                     /site_type="active"
                     /db_xref="CDD:277317"
     Site            order(193,195,220,264,356,392)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277317"
ORIGIN      
        1 mgvpeqlaer msmaeqheyl rtrfsrrtmi rggavtlgav aggafvpgav aqaatptrtf
       61 asattvdgal vapfgrhlay gndprtemtv swqvpvavkk pfirigahpw dlsrkieaev
      121 rtlytpagvg asadhtqyyv haklsrlrpg rtyyygvghq gfdpaephlt gtlgtfttap
      181 ahkkpftfta fgdqgvsyhg landslllgq npafhlhagd iayadpagag ktadtgfdsr
      241 vwdqflaqte svaksvpwmv sygnhdmeaw yspngyggee arftlpdngp dkahlpgvys
      301 fvygntaiis ldpndvsfei panlglsggt qtkwfegqlk kyraakdidf iivffhhcay
      361 ctstahaseg gvrqewvplf ekytvdlvin ghnhqyertd vikgdkvakk lpigetaype
      421 tegvvyvtag aagrslyaft apdsyeghln eqesvasfin tkdgkvnetv awsrvrylny
      481 sflrvdvepa skghyarlkv sgiaetgdri dhftvarrak
//
LOCUS       WP_284433614             510 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284433614
VERSION     WP_284433614.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18609803
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..510
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=55281
     Region          69..340
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
     Region          348..>463
                     /region_name="DUF3520"
                     /note="Domain of unknown function (DUF3520); pfam12034"
                     /db_xref="CDD:432277"
ORIGIN      
        1 merqrtrqvv lalavaggll ltgcgggedg ggkssadgsr ggsygsafpa pdqprgeqds
       61 desrdhdspe reapdllstf aldvdtasyg yarrtlaegr rpdpstirpe efvnsfrqdy
      121 drpdgngftv tvdgartdrd dwslvrvgla trsaeedsdr rppaaltfvi disgsmsepg
      181 rldlaqqsla tmtdrlrddd svalvtfsde aetvlpmtrl gghreriqea vdsleptyst
      241 nlgagvetgy rtavdglreg atnrvvlisd alandgdtdp dsildridta rrehgitlfg
      301 vgvgsdygda lmerladkgd ghtvyvsgad daekvfceel pqnidltard akaqvafdpr
      361 tvrqfrligy dnrrvadddf rddrvdggev gpghtvtaly avrtepgadg hlatatvrwq
      421 dpdtrapher saaletfdds lreanprfqv davaayfada lrdtstedrl pgrptmrela
      481 dwadeladrt edgtvrglad tirqarhlad
//
LOCUS       WP_284433638            1021 aa            linear   BCT 25-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284433638
VERSION     WP_284433638.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1021)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 1021)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   3  (residues 1 to 1021)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 1021)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1021
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..1021
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=111401
     Region          2..247
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          127..1021
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          726..754
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          765..795
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          806..834
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(807,810..811,814..815,817,847,850..851,854..855,
                     857..858,887,890..891,894..895,898)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          845..875
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          886..913
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          925..961
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          966..994
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mefeirlsgs veirtagrrs dlgstktrlt laalawdagr tvsvdtlihr vwdehppaka
       61 realhahisr irgalrmagg dappivsrtn syalevdper vdlrcytscv erarslrdng
      121 deesglrlld raealwhgep lagitgswae hlraavretg lvaamtraei lldagkfsda
      181 vpvllplaea hpvdealaer lavalygsnr taeatrllqr trqrvvrdig ldaghglhrv
      241 hqgilagtpa rdllpragae dgrpprptrr vpdnlprdvp wagrrdelrr ltaalcegrg
      301 asdvvtveai hgmggvgksa lavhlahrlr drfpdgrihl hlggcstdrt pptparalte
      361 llrllglatk elpqeldelv alwrsmardr rmlvilddat sseqirpllp gasptavvvt
      421 srrrlpglpg vrpvsldvlp pedaaelfaq rlgrardtdp aevaeivric ghlplaieia
      481 asrllarasw ttsdllrqlg egrghltqlr dldrtltqvf aisyealnae qqlvfrrigl
      541 hvgvdfgpga iaaltglppt taehileell ahhlvaepvp hrftmhdllr dyartliesg
      601 gteseddarq avqslvkhyl htadradrla ypfrsrtdld esdptpapcp eivdaqsaeq
      661 wlitesanlm dtlnwlvhhg teqqlalsvh vlagfldmeg hlaaaepllm raaahwdaag
      721 dsparvrall dlcavhthgs rydraistaq ealgiarslr drdlececvh qlsiplwqtg
      781 qyrsalsflq esldflsqtg dplriarcrn llginllhla enekalayft salsdfteig
      841 dergkysaln niaelhkrag npkaaelayr qavivaermg nprdratlqm nmasvldalg
      901 radealtlyg lalpvlrdvg drraeaialt rigrahrtag rteealrqhi aalemtraih
      961 aageeaevly dlalaerdag lttralthle qslavsrsig agaeevraag llaelrgevp
     1021 a
//
LOCUS       WP_284433659             448 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284433659
VERSION     WP_284433659.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18609919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..448
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=46905
     Region          14..240
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
     Region          394..440
                     /region_name="VWA_3_C"
                     /note="von Willebrand factor type A C-terminal domain;
                     pfam18571"
                     /db_xref="CDD:408355"
ORIGIN      
        1 manfsksnvp qfamdvyqne ylpeggrevn aivtvtatgg gtigsavaap hlwsaeqgps
       61 aavaimvdcs gsmdypptkm rnardataaa idtlrdgvhf aviggthvak evypgggrla
      121 vadattrdqa kqalrklnag ggtaigtwlr ladrllssae vairhgillt dgrnehespe
      181 dlkasldaca grftcdargv gtdwevkevt giasallgta divadpaala sdftqmmeta
      241 mgkevadval rvwtpvgtti kfvkqvaptv eeltdrrtea gpragdyptg swgdesrdyh
      301 vcvevpvani gqemlaarvs lvvpqpdggt qnlgaqglvr avwtddmvas tsinpqvahy
      361 tgqaelaqai qqgldlrkag didgataklg ravqlandsg nadtakllsk vvdvvdattg
      421 tvrlkakvee ademtletrs tktvrvkk
//
LOCUS       WP_284433699             347 aa            linear   BCT 25-DEC-2024
DEFINITION  fatty acid desaturase family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284433699
VERSION     WP_284433699.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..347
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38110
     Region          6..341
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mttnttvrpp psetsgsdfa rlsrkiadag lmgrrpgyya vritvvaaly vggwaavalv
       61 sdswwtlaaa gflavvfgqv allahdaahr qvfrrrrase asgriagtgv gmsygwwqdk
      121 htrhhanpnh eeldpdldpd llvwsqdqar aakglprlig rwqaflffpl ltlegfnlhv
      181 ssvkalgnrs lkhraldgal lfghfalylt fllwllppgm aiafvavhqg lfgvylgslf
      241 apnhkgmpil tgedrpdflr rqvltsrnvr ggrftdialg glnhqiehhl fpsmpspnlr
      301 kartivrryc eelgvdyvet gliasyrlal islhqagapl rhpgvpa
//
LOCUS       WP_284433804             551 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284433804
VERSION     WP_284433804.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12021846
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..551
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=58674
     Region          14..371
                     /region_name="FAD_binding_3"
                     /note="FAD binding domain; pfam01494"
                     /db_xref="CDD:396193"
ORIGIN      
        1 mnqragqadh ptnrvpvliv ggslvglsts vflgrlgvrh tlverhagts ihprgrgnnv
       61 rtmelfrtag vepmirqaaa tlagnhgilq tptlvgdage wlfreidpgg glarfspasw
      121 clcsqndlep vlldhaerlg adlqygtell sfdsgpsgvt aivksretge httyladylv
      181 aadgprspvr eqlgigqsgp gdlfsnvsit frsrrlaevv gerrfivcyl tdpeadgall
      241 pvdnrenwvf hapwhperge mleeftderc iahirravgv adldveitgr apwhaaqrva
      301 rryrsgrvfl agdsahemsp tgafgsntgi qdahnlawkl aavlggwage plldsydaer
      361 rpvaeatsar aavrsaehsh pgyapppgtg ggpqrgilnv algyrypqga vvgadpetpv
      421 vpdrldlsga pgsraphltv rhqgdqistl dlyersfvll sgvgaesgwh eaavrlteqt
      481 svplvsyrlg ggsgaeltte gdtdwaaahg ttpegavlvr pdgfvawrsa gpvpdaeqal
      541 rqvlstllgt v
//
LOCUS       WP_284434055             365 aa            linear   BCT 25-DEC-2024
DEFINITION  TolB family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284434055
VERSION     WP_284434055.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..365
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=39078
     Region          93..230
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 msgravatsc pvtsvsgipl rtalllaftg tttaaaqhap rtepvstaad gtqgdgasst
       61 aitapngryt alrspatnla pqgpahpgic ssirdlttge vtkieqplrt prfsadgrwa
      121 tytdwpsrtm naflsdlstg triqvgapds rdasaepdis adgryvahrw ighpqfptri
      181 dlyerltgth etvstgpqds tldmnkpsis gngrrvayqd sgtgdvwivd pcrhqrragr
      241 rprhrradrg rrrhpchcgp aerqrprpgd gfdrrllctg pdqhspdirv aavspdgrrl
      301 ltrdadvnlp lhgryggrev pvghgsatag slsahgrsvv ystvdahvvp gdtngmydvi
      361 qrrss
//
LOCUS       WP_284434069             922 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284434069
VERSION     WP_284434069.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..922
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=99372
     Region          <9..898
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mvwsgvhqaa rppligryae reaigrllas vrdgfsavlv ltgdagvgks rlleyaaqsa
       61 pdltvirlvg veaetrlgyg alhrllrpyl grlsalpqrq realnaafgl tdaspsdrhl
      121 vglaalslls daatgapmlc lvddvqwldr esaetlafvg rrlyadclgl lfagrdgtgd
      181 hdvfgalpal rleglaqaea ralltdgvag hldqtvaerl vtgtggnpla llelavnlgs
      241 eqlagvaplp eplplnrqle ehfrqsaarl padtqtllll mamtptddqa tlwraagalg
      301 lsvrsgtpav aagilnrgii aefrhplirs avhsaaspee rrrvqaalaa tssperrawh
      361 laeatrgpdd svaaeleaas eraqtrggys eqalvltraa emtthpgkra eryldaaaah
      421 lasgnlpavq pllelatpdl tgpvararat slrasvemfy arprevpaml ldavadlrst
      481 dpvagwdllr eatyaaivgg rmitgtttre vakatadawr epalpawspd plmaalarsv
      541 aygyadaapa laaalarlrs adelqdqhaf svmisaagde lwdieakrei leklvttgrr
      601 rgalhglsma llalstveiw dgrfaaaesc yieaydymta tgfsasgdfn kallyawtgr
      661 eaelraavat mraysenlgi gltyrwigqv lsifeigrgr yrealdalla vftdhplilg
      721 dinlagmvea glragdrkaa vmamermeer aplagtpwal gllarcralm tdddtaeqly
      781 qesisqlekv pvavelawsr llfgewlrrr rrradarvql rsayesfesw gaapfaerar
      841 vellatgeta rkrtadtqfd ltpqelhvat raasgltnae iatqlfvtts tiefhlsrvf
      901 rklgitsrkq iqrklresda gd
//
LOCUS       WP_284434120             298 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Streptomyces].
ACCESSION   WP_284434120
VERSION     WP_284434120.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..298
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32899
     Region          14..69
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(19,23,48)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(22,47)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(29..30,41,44,48..49)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          97..278
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 meansnptvr rrflgaelrr lrlasglkst evaerlmvsq pkishlengr rtisprdvrd
       61 lcalyevtdq qaidtlmqma resgqpgwwh aygdipqsvy ialetdaasl hayapsvipa
      121 llqtpayaha vieetipqlt veeagtrlkv clrrqhriyn parplrlwvv ldesalrrvv
      181 gspdvmreql ehlnalgaep hitvqvlpct agahpglsgq fsilhfadns anpvvhlery
      241 tsdlyldkps dvqhyrvlhd hlqaqalspd nshdfitdai ksyiaaasgp ravigsgp
//
LOCUS       WP_284434188             131 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284434188
VERSION     WP_284434188.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..131
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14038
     Region          7..64
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(10,14,39)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(13,38)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(20..21,32,35,39..40)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 manalqqlir erldlkgwsy gevarrggvp rstvhhlatt drvvrmpqst tleglskgle
       61 lpldtvrraa aeacgihvyg tpaaqssegt alhpadpevd lliasvqkls addrrhvaal
      121 veslldrtpk n
//
LOCUS       WP_284434331             541 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284434331
VERSION     WP_284434331.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..541
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59921
     Region          16..540
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 masrhhpelr aaarhfgrrh fltvtaaaaa lafgtqlpar gaagsteldg aripsdpftl
       61 gvasgdplpd svllwtrlap apfepdgglp qqyvvvewel alderfaapv rsgvaiaype
      121 yhhtlhievt glepdrihyy rfrtgtwlse tgrtrtapaa gtataslsya avscqaysdg
      181 yftahrhlse ddvdvvlhlg dylyeyavns agghraytdr klpdlfnrea rtledyrlry
      241 alyksdpdlr avhathpfvv twddhetenn yagtvsendd ppeefllrra aayraywenq
      301 plraaqlpng pdaqlyrrlq wgtlarfdvl dtrqyrsdqv yadtkhtggp lqddptrtit
      361 geaqeswlid gwrdspalwn vlsqqvcfsq rkldltaepk msmdawdgyr asrrrvldga
      421 ksagvenlvv mtgdvhaaya fdikddfddp asatlgteft atsvasgrdg aekpstwdty
      481 lranphlrfy dgrrgyvrvt ldrqqaradf rtvsavttpg apittsasfv teaghpglap
      541 a
//
LOCUS       WP_284434369             279 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284434369
VERSION     WP_284434369.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..279
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31219
     Region          23..82
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(28,32,57)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(31,56)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(38..39,50,53,57..58)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          96..274
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mgsdvgteap gppepdsgil rvfgrqlkrf rlraglerae fgartgysas tiaafeqgrr
       61 vppprfidva dgildadgvl qemkeevara qfpaffrdaa rleaeavelh vyatkavpgl
      121 lqtkeyarav famwrpllse gvitqrvaar larheffare plptisfvie eavlrrplgg
      181 wpvmrgqlen illygqrrnv eiqviptele ehaglegpft lietrdgrri ayveghkdsr
      241 lhterkpvre ieeqygilra qaltpraslt fiekllgdq
//
LOCUS       WP_284434447             273 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284434447
VERSION     WP_284434447.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..273
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29892
     Region          36..153
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mtetptrlhe eilayyargk edarlregga pagrleywrt qdvlrrllpa aparildvgg
       61 gsgvhadwla rdghavelvd pvplhveqas rlpgvtarlg darelaapda sydvvlllgp
      121 lyhlperadr lraltearrv lrpgglvvaa tinryaqlhd llreeryftp ehrertdavl
      181 vdgrhpyhde gfftvahfaa phevtaefaa arlttvgqyg iegvawlmgg vedwlddpdr
      241 ratvlaacrh ieseptllga sghlltvggr psa
//
LOCUS       WP_284434574             330 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284434574
VERSION     WP_284434574.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..330
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34554
     Region          1..328
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mrefaydral dvsgaltlld adpdarflgg gtnlvdlmkt gverptrlvd vrelpldgie
       61 vtadgglrig atvtnsnlaa hpevrrrcpa laqavlagas gqlrnmatvg gnllqrtrcg
      121 yfadvtkpcn krvpgsgcpa iegehhnhai lgasehcvat hpsdmgvalt afdavvsyet
      181 adgpgalpla dfylpvgdtp hretalpqga litgvtlppa pvaarsryrk vrerasyafa
      241 igsvaaaldl rdgvvrdvrl afgavasrpw rateaervlt gapadaetfa aaadaelaaa
      301 kplphnaykv tlmrnlvvav ltelteeaar
//
LOCUS       WP_284434578             796 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284434578
VERSION     WP_284434578.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..796
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=86550
     Region          31..796
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          668..696
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(669,672..673,676..677,679,709,712..713,716..717,
                     719..720,743,746,753,756..757,760)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          707..737
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          742..776
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdaelvtlav sagsvlvgam ltdtwaaakn rlialwlryq pdeapavaha ldqtqghlar
       61 tgdssrppdr aaaesqwqer lsvflaehpq aagalaglig qmgtqqaayt vhgdnvinit
      121 tlgradplqp rqlpgasrhf vgriaeidsl salmahtsgt ggmvvisaid gtagvgkttl
      181 alhwahrvas rypdgqlyvn lrgfdpsgep iqpheairgf ldafgvdasr lpasaeaqas
      241 lyrtllagrq vllvldnard tdhvrpllpg satcmvivts rnqltgliaa egaypltvdl
      301 ltadeshell aqrlgadrla repeatdeii ercarlplal sivaarishr qalplrtvad
      361 qllhargild aldtgdtmtd iravfswsys llppeparlf rllgthagpd ittpaaaslg
      421 amppdsarra vshlirshlv dehtpgrhtf hdllrtyaie qsqitdtase qaqarlrtas
      481 hylhtahtaa llldphrtpl plappepgtq petlsaydqa lawyeaehsv llntlaqasa
      541 haldthvwql awtltdyldr cghwhdqatv qalalaaaer lddplglahs hrnlahsctr
      601 lgryadainh fqaavdafsr lgadslqagv rlnyawalel tgsydqalqq aqaaldlyrs
      661 lqdevghars lnavgwyqtl sgdhdsalin ceealvrlrr lgvqhdeayt lesiahayrg
      721 lgqlpqasar yhealdlfhr lgdlyyeaai hnrlgeldqa sgritqarnh weqaldildt
      781 lrhrdaedlr arlqql
//
LOCUS       WP_284434580             290 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284434580
VERSION     WP_284434580.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..290
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31205
     Region          17..77
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(23,27,52)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(26,51)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(33..34,45,48,52..53)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 marpeqplkr dgsplrefav qlrslraasg ltyaqlaaqt aysvstlqea aagrrlptls
       61 vtlafakasg gdpeewrqhw ervhalsrsn ghsarpdave psaaghftpm aypegpagss
      121 tapreqhkhs rllrrtrrlw ligavvtvva aaaacaavfa vsdpparasa tvivvqnkva
      181 igpdqlveds tpvylssrtv srcarrgckl sdtdmwsgak lvatcwtrge rltnqdaase
      241 giqrnknrvt sdvwyrtewp dgrtgylsev yvvssdrggl glgrcspras
//
LOCUS       WP_284434579             343 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            sp. TUS-ST3].
ACCESSION   WP_284434579
VERSION     WP_284434579.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..343
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=37052
     Region          2..294
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkifitgdlg ylgrvlhall raeghevggl daglfergpg rpsrdvrdik gsdmagfdav
       61 vhlaavcnda cgelstsath ainhgatvrl aalarnlgvg rfvlasscsv ygdsparead
      121 etcpvtplta yaasklraer alsglaadgf wpvalrfatl fgpstsfrsd illnrmvgta
      181 vrsgvirvnn aeirrpvlhv edaayailhv lnapppllrm gvfnvgdtkl nhqlgefadm
      241 vqqavpsasi rqepatdhrs ysvrfdrfqd afprwspqhs vergiaelar yyrsdttsmh
      301 tlaaswgstd rrahllslia aglvgqdlrw rpptartrqa pri
//
LOCUS       WP_284434663             586 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284434663
VERSION     WP_284434663.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..586
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=59085
     Region          54..550
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mlaatlgaal afgtpgalag tlpvapstap aakahapaaa pasqsatwva gtraylvita
       61 pgdssavrsa itanggtvfs nfdaigviva hsasstfaat mrgvagvqqv gatrtsdvpa
      121 daynpalpan paqastpage pvradmsqik adqawavnpg sasvtvgild tgvddqhqdl
      181 apnfdaadsv scaygkpdtr agawrdvdth gthvagtvaa akngkgvvgv apgvkiaavr
      241 vaepgnafff aenticgfvw agdhgfkvtn nsyytdpwqf ncpdnidqaa iiegvkraqe
      301 yaegkgslqi aaagnenydl ahkttdsasp ndstpvtrti tnacldipte lpgvvtvaan
      361 gtgvtkasfs nygqgvidva apgsnvystv pgggygsksg tsmatphvvg vaaliasanp
      421 gitpaqlrak laeqandiac psdsrctgtt annsffgegq vdalkavgat pppgkyfenl
      481 adfavndnat vespitvtgv tgnapatlkv gvdikhtyig dlkvdlvapd gtvytlhnht
      541 ggsadniaqt ytvnasseva ngtwklrvnd naasdtgkid awnltf
//
LOCUS       WP_284434873             474 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284434873
VERSION     WP_284434873.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 474)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 474)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 474)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 474)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..474
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50806
     Region          1..466
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          237..467
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mgrlarlwar prprllslrt tfavsfaavt aavtvlvgvl sysaaarlvr vdqesvfdqv
       61 vqdlrsevrq qrmttedfss sapghdlvrp artdvqvlgp tgavadpgrp glpvtsgdrr
      121 iaaaypagrm vlhkevsvgs dvyriatvsl gggrgavqva qefsdtedll ralqqrtfll
      181 maavvvgagl fgwwlarrit rrliiltsaa edvartrrlg idvpvtgyde vgrlgrafdr
      241 mlgrlaqsee dqrrlvqdag helrtpltsl rtnisllrri delppatrde lvadltqear
      301 eltdlvnelv dlaagqadne ppqrvdlaev aeevaglarr rtgreilvha ngstvtdgrp
      361 amlqravsnl venaakfdrd gaapieisvs aftaagpvrv evldrgpgia dadlvrvfdr
      421 fyraadarsl pgsglglsiv revalshgga pfafprdggg tvigftvggd psrg
//
LOCUS       WP_284434935             413 aa            linear   BCT 25-DEC-2024
DEFINITION  LolA family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284434935
VERSION     WP_284434935.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Tajima,T., Yokota,N., Matsuyama,S. and Tokuda,H.
  TITLE     Genetic analyses of the in vivo function of LolA, a periplasmic
            chaperone involved in the outer membrane localization of
            Escherichia coli lipoproteins
  JOURNAL   FEBS Lett 439 (1-2), 51-54 (1998)
   PUBMED   9849875
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..413
                     /product="LolA family protein"
                     /calculated_mol_wt=41519
     Region          <145..294
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mapyesdnsa taadaeelra arrrkaaryv vpatvvgvaa atiglvpala dsgdpdlpki
       61 saqeliekia asdvqqlsgt vkittdlglp dlgglesslg saagpsgsgd gssadpstkl
      121 telasgthtl rvaadgedkq kvsllenaae yslihngkdv wgydsksnsv fhttasesdg
      181 kqkeelpatp kdlaeealka adkttsvtvq gtaqvagrda yrlvikpkdd gstvgqitva
      241 vdsatglplk ftltpasgga avvdagftqv sfakpaastf dftppkgakv eegdagkape
      301 hseglgrgsa gefgkgpage fgkgapegln vigdgwdsia tfdtggqgvp sgsevggdvg
      361 gflnslgdkv sgkfgegtvf ktrlinalit ddgkvyvgav tkdalvkaad agk
//
LOCUS       WP_284434957              69 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284434957
VERSION     WP_284434957.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 69)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..69
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=7942
     Region          9..69
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 maapsrrrre pkdelvpltd vldeigitra twyrwrdrgy tpearrtpsg ricvrrsvld
       61 afkeeldaa
//
LOCUS       WP_284435032             376 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284435032
VERSION     WP_284435032.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 376)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10543770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..376
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40306
     Region          94..232
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
ORIGIN      
        1 msvsveptsv epkqeepaea lrphaeeafa gelaalaaqd drprparwkl spwavatyll
       61 ggtlpdgtvi tpkyvgprrl vevavitlat drallllgvp gtaktwvseh laaavsgdst
      121 llvqgtagtp eeairygwny aqllangpsr dalvpspvmr amaegmtarv eeltripadv
      181 qdtlitilse ktlpipelgq evqavrgfnl iatandrdrg vnelssalrr rfntvvlplp
      241 esveaevdiv srrvdqigrs ldlpaapdgi teirrvvtvf relrdgmtsd grtklkspsg
      301 tlstaeaisv vtnglalaah fgdgvlragd vaagilgavv rdpsadrviw qeyleavvre
      361 rdgwkdfyra crevsa
//
LOCUS       WP_284435118             590 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284435118
VERSION     WP_284435118.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..590
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62222
     Region          1..465
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          522..588
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(545,554..556,563)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            555
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mrkvlianrg eiavrvarac rdagiasvav yadpdrdalh vraadeafal ggdtpatsyl
       61 diekvlgaar esgadaihpg ygflsenaef aqavldagli wigpppqair dlgdkvaarh
      121 iaqragaplv agtpdpvsga devvafareh glpiaikaaf ggggrglkva rtleevpely
      181 dsavreavaa fgrgecfver yldkprhvet qcladthgnv vvvstrdcsl qrrhqklvee
      241 apapflsdaq vaelyssska ilkeagyvga gtveflvgmd gtisflevnt rlqvehpvte
      301 evagidlvre mfriadgeel gygdpelrgh sfefringed pgrgflpapg tvtrfdapsg
      361 pgvrldagve sgsvigpawd sllaklivtg atreqalqra araleefqve gmataipfhr
      421 vvvkdpafap eltgsadpft vhtrwietef vneikpfaap adteaeddad retivvevgg
      481 krlevslpss lgmslartgl aagakpkrra akksgpvasg dtlaspmqgt ivkiaveegq
      541 evkegdlivv leamkmeqpl nahktgtikg lsaevgasit sgaaiceikd
//
LOCUS       WP_284435120             206 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284435120
VERSION     WP_284435120.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..206
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=21228
     Region          7..180
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mtdqprrrlv lasqsparla llrqaglape vlvsgvdeda vsaptpaela lalaeakasv
       61 vsakpevkga lvigcdsvld ldgqalgkpa daeeatarwk amrgragtlq tghcvydtts
      121 gryvsavast vvrfgeptda eiaayvasge plyvagaftl dgrsapfieg idgdhgnvig
      181 lslpllrrll aqlgvgitel waptee
//
LOCUS       WP_284435356             247 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284435356
VERSION     WP_284435356.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..247
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26410
     Region          51..226
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 maltaalpgv alagcgqrag hgegaysgle avpeklgadg ttitvgnpha pvrvhlyedp
       61 rcpvceefes tgggpelrea tvrgetrtey tlasflddrl ggsgskkavn alraalaegr
      121 faeyhqvlyr hqpeesedgf tddrllelae rvdglrspaf dsavkgmkyr afvkasekay
      181 edaggsarpg gpgtptaein tiripadyng vlfdapvfsn llreirrepe dwqnyvfpdv
      241 attpgpf
//
LOCUS       WP_284435417             599 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284435417
VERSION     WP_284435417.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 599)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..599
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=64287
     Region          43..575
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 malnrrkfle ksavtgagva lagavgapaa qaaesgrkpv krysltvmgt tdlhghvfnw
       61 dyfkdaeykd sagnaqglsr istlvnqvra ekgrcntlll dagdtiqgtp ltyyyakvdp
      121 itakggpvhp maaamnaigy davalgnhef nygietlrkf eeqcafpllg analdaktlk
      181 pafppyfikk fhvkgappvk vavlgltnpg iaiwdkayvq gkltfpglee qaakwvpklr
      241 smgadvvvvs ahsgssgtss ygdqlpyven saalvaqqvp gidailvgha hveipelkvt
      301 ntktgktvvl seplayaerl slfdielvle kgrwsvesvs skvlnsnsva ddpkitkllk
      361 adhdvvvqyv nqvvgtatqk lttvearykd apiidlitkv qedvvraala gteyaslpvi
      421 aqaspfsrts eipagdvtir dlsslyvydn tlvaklltga qikayleysa eyfvrtaaga
      481 avdvekltna gnrpdynydy vsglsydidi aqaagsrikn ltyngaaldd aqkfvfavnn
      541 yrangggafp hvasatelws esteirtria ewvtakgvld pkdfasvdwk ltregtpvf
//
LOCUS       WP_284435420             464 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284435420
VERSION     WP_284435420.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 464)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..464
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=48149
     Region          16..459
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mhtpplasgp egrdvlrpll dtvlealeeg ararggplpa ggpsevaarv raavgdvlpd
       61 egdpealrhl vralaegsad pahplcaahl hcpplavaaa adlaasvlnp sldswdqapa
      121 aseleslvtg tlanevypdp prgagnrats phgpdalvtt ggtesnqlal llaretqgpg
      181 vrlvcgenah hslpraawll glpepvivpt phgtldpatl dtalrgpsvv aatagttdag
      241 lidplpeiaa lcaqrgarlh idaaygagll fsarhrarlt glsvadtvtl dlhkigwqpv
      301 aagllavrdk ndlaalhqra dylnadddte aglpdllgrs lrttrrpdvl kiavtlrtlg
      361 rrglaalvdq vceqarefak avdehpgfel happtistvl frpagatdda vaavrrqlle
      421 dgravlgrar adgrlwlkat llnpttrpad lagllnlveg ttpr
//
LOCUS       WP_284435466             552 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284435466
VERSION     WP_284435466.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..552
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59503
     Region          45..521
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mtsrprttes nslsprrrtv vkaaaatavl agplaaalpa raaaetpafl hgvasgdplp
       61 dgillwtrvt ptveavpgsg lgpdtevgwi vardkaftnv vakgsvtata asdhtvkadv
      121 rglapatdyw frfsaggads paartrtapa adaavanlrf gvvscanwea gyfssyrhla
      181 argdldawlh lgdyiyeygt geygtrdtvv rqhaptheil tladyrirhg kyktdpdlqa
      241 lhavapvvai wddhefanda wsggaenhte gaegawsarq aaakqayfew mpvrpalagt
      301 tyrrlrfgkl adlslldlrs frsqqvavgn gsvddpnrti tgraqldwlk aglkssdttw
      361 rlvgnsvmis pfaigslsad llrplaellg lpkeglalnt dqwdgytddr rellahlrsn
      421 airntvfltg dihmawandv pvdagtypls asaatefvvt svtsdnlddi lkvpegtvta
      481 laapviqvan rhvhwvdtdr hgygvldita draqmdyyvl sdktkqnats awarsyrtrt
      541 gtqkvertyt pv
//
LOCUS       WP_284435480             500 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284435480
VERSION     WP_284435480.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..500
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53161
     Region          25..492
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mariavigag mgamaaaarl avaghrvavy ertetyggav rrferdgfgf dtgpglltlp
       61 avyrdlfikt gkeplesvve lvqvdpssrh lftdgtevsl pnasragvva aldealggga
      121 garwgdflir areawdrtrr plleeplwpn wqvltrepyp avphkrllrt rractlheig
      181 awelrdprla alldgcalty gvdpgtapas aavlpymeha fgtwyvrggl relaravyer
      241 cvqrrvefhf gaevtgvlek dgraaglels dgtvveadtv vgagpwrlrg lvpgrelyga
      301 kdvppdaedl hpgrvvvgla lrgarepdav hrtvvygpap gdeldlfvrg etpeptvrid
      361 rpddaalrpd aghesvvlta tvpcgrghdw vtpgvvdafv ekmtaaaera ipglrervlw
      421 revrtpvdte retgaeggav pppslaggeg tlhpsnstav pglftaggws hpggglahag
      481 msgalvaglv vegpefrgsq
//
LOCUS       WP_284435496             258 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284435496
VERSION     WP_284435496.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..258
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27412
     Region          17..216
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mygtmkvaig gplkvafrpw veglenipae gaailasnhl sfsdsfflpa vldrkvtfia
       61 kaeyfttpgi kgrltaaffk gvgqlpvdrs gargageaai rsgldvlerg elfgiypegt
      121 rspdgrlyrg kpgglarval asgapvipva midtekiqpp gkvmpklmrp girigepldf
      181 sryqgmehdr fvlravtdev myeimklsgq eyvdiyataa krriseaaka ekaakaaaak
      241 aeaavakaeq depgssas
//
LOCUS       WP_284435500             598 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284435500
VERSION     WP_284435500.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..598
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63992
     Region          1..598
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mrefslpaly evpadgnltd ivrrnaaqhp dvaviarkvg gqwqdvtata flaevhaaak
       61 gliasgvqpg drvglmsrtr yewtlldfai wsagaitvpv yetsspeqiq wilsdsgata
      121 cvveldghsa avesvrqqlp alkhvwqieg ggieelgrag kdisdaavee rsslakaddp
      181 ativytsgtt grpkgcvlth rsffaecgni verlrplfrt gecsvllflp lahvfgrlvq
      241 iapmmapikl gmvpdikqlt delasfrptl ilgvprvfek vynsarakaq adgkgkifdk
      301 aadtaiaysk aldtpsgpsl glkikyktfd klvysklrav lggkgeyais ggaplgerlg
      361 hffrgigftv legygltesc aatafnpwdr tkigtvgqpl pgsviriadd gevllhgehl
      421 fkgywnneaa taealtdgwf htgdigtlde dgylritgrk keiivtaggk nvapaviedr
      481 irahalvaec mvvgdgrpfv galvtideef lgrwaeehgk pagstaasla adadlnaaiq
      541 aaiddgnaav skaesvrkfr ilssqfteet ghltpslklk rnvvakdyad eieaiyak
//
LOCUS       WP_284435606             585 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284435606
VERSION     WP_284435606.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..585
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=63927
     Region          292..580
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 macspsqrls shvpdqetrh pgatagperr dsrplaaldp hgllalshtl ftcaeqseiv
       61 rlamrhvsal gpyhaeagyl atgdglsrvp ahvagaptvd daqmselgea dgsvslperp
      121 wnrafglrga ggllgyivvs shsgpdeqgd fllstlvrlt stalslaatc asqhesagel
      181 srlrterdta lrgldamrst lhwqrtvdea larvaarggg ehaitqalye ltglsalved
      241 rfgnlrswag pdrpdpypvr ssthqeemlr qvaheagpvr vkdrlialar prgdvlgvla
      301 iedpgatade htmfaldhaq rslaqelmhm reltevevrl rrqliddlle gtdetsayar
      361 aeavghdlqr thyvvvvhwp gngatssftr averatatta trplitrrgd rmvllteatp
      421 dddavhaala helgtpdgai gvstpcespd gvprcyqeal ralevrqnsr qrsgttffed
      481 lglyrilgpg ndlreledfv qewlgrlidy daehdtelve tlsryfdcgg nyddaaaalt
      541 vhrstlryrl qrireisdrd ladvdtrlnl qvatrvwkii lggrh
//
LOCUS       WP_284435779             550 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284435779
VERSION     WP_284435779.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..550
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=60239
     Region          29..150
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          242..547
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mnhdhptarp ldagdrdsgt pgqaltiadv lalpvlaagq pqvvtgvthl drpvrwvhit
       61 eltdpasflk ggelvlttgm plpddttgvr ryvdelagig aaalvielvr ryhrppdalv
      121 hacrarglpl itlakdvnfl evtqvvhali lgnqaeamrr tqriheafta ltlrgagted
      181 vvraaadmsg rtvvlenmvh qalicepsgt tleealtdwe qrsratppgd rtdlrgpegw
      241 ltapveyqge rwgrvamlpa ptdktfgpeh vtvlertama ltvarlihst pweriahrna
      301 lrdlveqrhr spqdalarlt alglptensr flavvvdlpa agttaqpeir lsqelrttgi
      361 palvgelapa rlgallalgp shpwrptveq lsratldlvp qavvsvgtev ddltdaprsf
      421 hqatrvaeat ppdqplpqgr sfheltdvgl rrllyalrqd triqdyterq lgrlidhdtr
      481 hgtdllttlr hyldaagnkt saarrgglsr etfyqrlrti erlldcdfes geqrtalhva
      541 ltaldvlrvr
//
LOCUS       WP_284435800             387 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            sp. TUS-ST3].
ACCESSION   WP_284435800
VERSION     WP_284435800.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..387
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42673
     Region          95..383
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtafndeavt gdalrrtlgv srrrflstct avtgaaiaap vfgaapalaq drspagghdh
       61 grsalvpphk rgiilytvrd avgrdplasd lpsgfrevfk qlsrygyrqv efagygqhan
      121 apggadlgtv qgarllrswl ddyglraqgs hgyiprswpl taadrdtfkr wleianilgm
      181 ehmgtgadpt ntpyradwdv aaqkwntlga iacregikly thnhdsaydf lldggpldaq
      241 grptrssgir kleyflkvtd rksvyleldv fwahvaqykf htytahdgsq rervfdpaal
      301 vernstrfpl fhakdgvlnp qsglgydmvp fgtgdidyrr fftrvgakny rnpmveqdna
      361 psttvpgqsl dfarigyqnl aalrarh
//
LOCUS       WP_284435784             228 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Streptomyces].
ACCESSION   WP_284435784
VERSION     WP_284435784.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..228
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24401
     Region          <44..223
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msslnvppal lrwvtgidva tadasaavdv pdhattlllr tdkhelivmg prtraayhva
       61 vpghscvqvr mrpgraqall grplndladr alplrelpgl dvdhlaadpv talekaladr
      121 pepserleea arllvgatva etaarlhise rrlhtlftdg tglspkhftr idrvrtvlaa
      181 dggrwadiaa tagyydqshm taefrhfmgv ppaaytagrh paaiscta
//
LOCUS       WP_284435846             491 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284435846
VERSION     WP_284435846.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..491
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52738
     Region          141..482
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mnateprrhw wprsvragaa latastaavi lfgigwwvhh dvyrqstqia eeqalaqlws
       61 lvdqvnegvv pvrtsavpye vvatgrrsav aygggivdfg pgtrhvlpap tghgspnfvr
      121 lpvnrdynsg vrgdmaggty evfsadisaq elggdkaaal gvaadarlrv yvlvlpqtae
      181 eitgttdrll lraglvslvl iaaaayfavr ialrpveair vltasvtasd prervtvpas
      241 gheitalatt instlqrldn aaaqqrrfva daahelrspl ttllasleva laypertdwp
      301 aaattaarqt rrlhalaedl lllarldtrt paahpesvdl aalasrlteq yppterpltl
      361 tcdstapaca hgnpgeyerl lrnlvdnaar haahriqitv rnegdwvvlt vhddgpgvpa
      421 eeaeriferf vrlddarsrd hggtglglai ardlahrhrg tltltpqpfg acfrlrlpra
      481 pepagtraar a
//
LOCUS       WP_284435821             392 aa            linear   BCT 25-DEC-2024
DEFINITION  cytochrome P450 family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284435821
VERSION     WP_284435821.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 392)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..392
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=42139
     Region          14..391
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(52,59,82..83,90,94,101,226..227,230,234..235,238,
                     271,276..277,280..281,283,306,333..335,338..339,341..343,
                     347)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(59,76,78,81,83..84,166..167,175,225..226,229..230,
                     234,277,280..282,382)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mtdptqdpsf lqdpyptyaa mrsscpvqpl ptgsgghpgy vvtgyaeare algdarlskd
       61 taaffagkks rrrlhpavah tmlatdpprh trlrklvtka ftagavaqlr pfiarvtdel
      121 ldqwpvgerf dfvaglavpl pvivicellg vpagdrpavr rwsgelfaag rpdvidaash
      181 rmadymtglv aakrldpgdc lldrliaard gaerlseeel vslavlllva ghetttnflg
      241 naalallqrp aewdrlrqnp ddvpavldel lrfdspvsta tfrytteavt lggvdipagv
      301 pvlvalgaan rdpvrfpspd lldldrdaaa hlgfghgihr cvgaplakae aeialravlt
      361 rfpgirlavp serlqwrrtr lvrglaalpv vv
//
LOCUS       WP_284435864             324 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284435864
VERSION     WP_284435864.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..324
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35918
     Region          16..322
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mqktssrlls llsllqthrd wsgrdlaerl ditsrtvrrd idrlrelgyl ittvkgpggg
       61 yrlaagnhlp pmlfdddqai alavalqtvt vgtaladdav ralatlrqvm phrlrhridl
      121 lrvtavqppa ghevprtdgq vlvevsrtih areelrfdhm pgsgtsadap rrvqphhlvt
      181 wrhrwylvaw dldredwrtf rvdrmrprtp tgprfaprel pggdvaafvt srfrgndgtr
      241 arwpcegevi lhlpaadvap faedgvveel gphhcrltlg swswtglaga varfdtdiev
      301 vgpprlasaf aelsarcara akva
//
LOCUS       WP_284435895             469 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Streptomyces
            sp. TUS-ST3].
ACCESSION   WP_284435895
VERSION     WP_284435895.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 469)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468627
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..469
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=53308
     Region          46..>241
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
     Region          207..468
                     /region_name="RHO_alpha_C_MupW-like"
                     /note="C-terminal catalytic domain of Pseudomonas
                     fluorescens MupW and related aromatic ring hydroxylating
                     dioxygenases; cd08882"
                     /db_xref="CDD:176891"
     Site            order(214..215,219,222..223,226,228..229,231,233,376..377,
                     429..431,433..437,448..451,455,458,462)
                     /site_type="other"
                     /note="putative alpha subunit interface [polypeptide
                     binding]"
                     /db_xref="CDD:176891"
     Site            order(223..224,226..227,229..230,234,346..347,349,357,359,
                     366,368,413,416..417,423..424,427)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176891"
     Site            order(223..224,226..227,229..230,234,346..347,349,357,359,
                     366,368,413,416..417,423..424)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:176891"
     Site            order(229,234,427)
                     /site_type="other"
                     /note="Fe binding site [ion binding]"
                     /db_xref="CDD:176891"
ORIGIN      
        1 mmdetsepdt arcpgpsvqd yldqdsrpvp aalryehndh lgsedidtar ftsrawaere
       61 mrqvwrrvwq facleseipe vgdheiyeig ddslivvrta pdeirafvnv clhrgrklrt
      121 gggnvsefrc sfhgfawnld gtmqsppcaw dfphvtpekf alpeaqvatw rgfvfinmdp
      181 yaesfdsyrg tfddyyiwpl enrykslhia kvlpcnwkva qdafiesfhv iathpqmlpw
      241 ladansqydv madqpnwnrm iniqgapsph vaesvteedv letfydsraf yaaaqgrdlv
      301 mqegdelpai ppggtarkvl aermraqlaa tsqqdfsqta dtelldainy llfpnfnpwg
      361 gaksniiyrf rpngldpdsc taeiifmssp kqpgevpapa kirwvpedml fadipelgvl
      421 gpvfdqdcen lpyvqqglka mrkpgitlan yqesrirhfn rtldqwmdk
//
LOCUS       WP_284435938              89 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284435938
VERSION     WP_284435938.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..89
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9032
     Region          2..69
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mpiavdidvm larrkmsvge ladrvgitpa nlavlkngra kavrfatlaa lcevlecqpg
       61 dllrweaedg tgekapstgg ttagaaasp
//
LOCUS       WP_284435980             301 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284435980
VERSION     WP_284435980.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..301
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30052
     Region          228..296
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mseppvlvcp ecgapraadg tpsctcahra aeahlesrta eaaaaedfdp vrirpfvevg
       61 eepadpavep erphgagdls dtvvlgadag papleqplae pqaagapagr rrrttvvagt
      121 gaavavlitg gvvgglftyd gpardgsvag gvragvpevp pssngpsvta sspaatstrs
      181 sappssspsa qadesasptg tvtpsgppss aaatatvapr ptvsngqppv lglgdhgpev
      241 velqlrlqqv glydgeadgd fdqqvqsavr tyqvtrfvlq desgvygkat rtslesetse
      301 p
//
LOCUS       WP_284436045             649 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284436045
VERSION     WP_284436045.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 649)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 649)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..649
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=70334
     Region          4..183
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mpvkvsvvip vynpgnyied ciaslrrqsl ppdefeaifv ddgstddtpa rldavaaete
       61 nfkvihqeas gwsgkprnvg iaasegefvm fvdnddylgd ealermydya vangadvvvg
      121 kmagkgrgvp velfrrnhpr atvdnaplid sltphkmfrr afldriglrf pegrrrledh
      181 vfvteaylra dnvsvlgdyv cyyhlkrdda snagfqrfdp vgyfknlrea ldvvekytep
      241 gptrdrlfrr wlrnemverm rgkrllaape dyrkelftei rgvvverfgp gvaaglqptq
      301 qvvaaliadg rlddlvefae weasvaskve pdgvewdggv lkfglsaela sggtpmsfpa
      361 egssaplsep pasvaeavdw vgahsvagfk ratvdlllre rassaqyfqs veftresvpv
      421 edgrvrlvlr gtaavdpaia adggplgsgl wdvfvrvklg gwtkqsrlgp vslkgrtaad
      481 agvaggrvvl pywtakqgtl aldvdtager lqlgqvtpge vtvagdrvev pvpfhvpgdt
      541 pvlleltrgs gaasakvpgt lrpqgsaall eavlpvaelt gaawrvalsp apdaerprfh
      601 plpfalrvkg gqvqvvavrp prpatgqrmv rrarrlagrl vsglrarrk
//
LOCUS       WP_284436056             133 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284436056
VERSION     WP_284436056.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 133)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 133)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 133)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..133
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14565
     Region          9..85
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mpdaplwtal adphrraiva lllerprpvg eiveacglsq pstskhlkvl reaglvrvrq
       61 daqrrvyald papiaeldaw lapyrklwna sldalgarld atapttseee peepeepeep
      121 eapeepqepa pkd
//
LOCUS       WP_284436091             396 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284436091
VERSION     WP_284436091.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..396
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41659
     Region          45..226
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mtyrttpttr mtqavrrpsr palalveevr avgraaraaf rgpgrerdll vqslkasaaa
       61 ilawlvagvw mgdpmalmap wvavvlvqat vysslmqaar qlgaiccgtv lasvalavtg
      121 stlgavalsv pplvllanwp rfgdqgiyga ttalftlatg aagassvghr vgqaalgavi
      181 glavnafvlp pvhlrdvren laalareagd vlhtvagdlr dgewdahgws hasarlerrl
      241 ealrsargws reslrltaap lravrrppap vpseqdderw srvtghiral trtlavaadd
      301 drapapptgp vldayadllq ligdschaes drllaaggea rpddhaesam relrgqlqdg
      361 lrehagqgae gttvlgtlll qaenlwsetv ptgrhg
//
LOCUS       WP_284436228             280 aa            linear   BCT 25-DEC-2024
DEFINITION  amidohydrolase family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284436228
VERSION     WP_284436228.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..280
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29962
     Region          3..277
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mtvvdahhhl wdlsvrdqdw iaadsplrrn ftpadlvpra aaagvdrtvl vqtvtvpeet
       61 peflalaaah elvagvvgwt dltrpdvage larlralpgg shlkgirhqv qgepdpkwll
      121 rpdvhrglta vaeaglvydl vvlphqlpac veaaealprl tfvldhlgkp piasgalepw
      181 atdvralaal pntvcklsgm vteadlsswt lddlrpyadt vldafgpdrv mfgsdwpvct
      241 lgatygevld iarrltpest harifgatat rvygldapgs
//
LOCUS       WP_284436234             415 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase 5 family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284436234
VERSION     WP_284436234.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Sharma,K., Dhillon,A. and Goyal,A.
  TITLE     Insights into Structure and Reaction Mechanism of &#946;-Mannanases
  JOURNAL   Curr Protein Pept Sci 19 (1), 34-47 (2018)
   PUBMED   27739373
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Ketudat Cairns,J.R. and Esen,A.
  TITLE     beta-Glucosidases
  JOURNAL   Cell Mol Life Sci 67 (20), 3389-3405 (2010)
   PUBMED   20490603
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467628
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..415
                     /product="glycoside hydrolase 5 family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45531
     Region          6..331
                     /region_name="COG3934"
                     /note="Endo-1,4-beta-mannosidase [Carbohydrate transport
                     and metabolism]"
                     /db_xref="CDD:443135"
ORIGIN      
        1 mpsavrfgvn ytpsvgwfhh wldfdldsvr adldsiaalg ldhirvfplw pyfqpnrtli
       61 reravsdlvr lvdaaaergl dvnvdglqgh lssfdflpaw trtwhrrnlf tdpqvvegqa
      121 aylrtlaaal ddrpnflgmt lgneinqfsa gphpdpdpat ieqidawltr mlaaceegap
      181 grlhlhaeyd atwyqddqpf tpaqaarhga vtavhswvfn gtaqrhgras vpaehhaayl
      241 velakafadd phrpvwlqev gapaplvppe haaafteatv vhaldcedlw gitwwcshdv
      301 sreladfpel eyglglltnd rkpkdtarvl eraaragaga pgrratalvv padpasrsrc
      361 apggpvfeaw frlaadgarp ttvldthaad qdhlaargit evvtsdqvlp phkdh
//
LOCUS       WP_284436293             453 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284436293
VERSION     WP_284436293.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..453
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=46639
     Region          130..408
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mgrhqgsdth tgsafrarla llallcsilv pllvaglrsv lwalvgiagl aiaavgvwwt
       61 lahtgalrvl glvlsvtapl tvlalysasg mlgpaclslv lwmlavasar talapprsaa
      121 grveaphdpw ivmnprsggg kvgrfglvek araagarvvl ldghqdvagl atqavaegad
      181 llavaggdgt qalvaevaar hdvpfvvipa gtrnhfaldl gldrddpaaa lqaltdgvel
      241 rvdlgfaadr vfvnnasfgt yasvvadpay rdaklhttlr tlpglltged apglrmragg
      301 tsvgglqall vsnnpylrav dagrpgrrer ldsgllgvlg vrvantaqaa rlvrggrsgs
      361 llrlradevv vdadtadiav gidgehvvlp tpvvcrtepg alrvhvprhr pgkplagapa
      421 dwprvarlar gglfthgrga tatepghgrk rhv
//
LOCUS       WP_284435931             548 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 27 protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284435931
VERSION     WP_284435931.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Bhatia,S., Singh,A., Batra,N. and Singh,J.
  TITLE     Microbial production and biotechnological applications of
            alpha-galactosidase
  JOURNAL   Int J Biol Macromol 150, 1294-1313 (2020)
   PUBMED   31747573
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Kitaoka,M.
  TITLE     Diversity of phosphorylases in glycoside hydrolase families
  JOURNAL   Appl Microbiol Biotechnol 99 (20), 8377-8390 (2015)
   PUBMED   26293338
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19064013
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..548
                     /product="glycoside hydrolase family 27 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57340
     Region          43..326
                     /region_name="GH27"
                     /note="glycosyl hydrolase family 27 (GH27); cd14792"
                     /db_xref="CDD:269893"
     Site            order(50,85..86,127,168,170,204,226,230)
                     /site_type="active"
                     /db_xref="CDD:269893"
     Region          338..412
                     /region_name="Melibiase_C"
                     /note="Alpha galactosidase C-terminal beta sandwich
                     domain; pfam17801"
                     /db_xref="CDD:465512"
     Region          419..547
                     /region_name="beta-trefoil_Ricin_XLN-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold,
                     found in Streptomyces olivaceoviridis
                     endo-1,4-beta-xylanase and similar proteins; cd23418"
                     /db_xref="CDD:467297"
     Site            order(435..438,448,450,453,457..458)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(444,477..480,490,492,495,497,499..500)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(463,467,469,473,477..479,490,492,495,499)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467297"
     Site            order(520..524,533,535,542..543)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
ORIGIN      
        1 mprptgrrlf rvfaaaalav aasltasaht tasaapgspa ltpplgwnsw nsfgcgitea
       61 qvrqaadamv ssgmrdagyr yvvvddcwfd pqrdaagalr asptkfpsgm kalgdyihgk
      121 glkfgiyqvp gertcaqtsg aypgstgsrg heaqdaatfa swgvdylkyd wcsssgtrde
      181 qvarftlmrd alratgrpiv ysinpnsfha itgatynwge vadlwrtted lldiwqngnt
      241 nsypmgvgnv lditaplaaq sgpghwndpd mlvvgrpgls ltesrshfal wallsaplma
      301 gndirtmsad vsailrnprl lavnqdalga ggrrvrddgd tevfakplsd gsvavglfnr
      361 gggtatistt aaqvglsggp ftltdqwtga tsstsgqisa svpahgvavf rvsggsplaa
      421 ttsrlrgnas grcvdvdnas taagatallw dchtaanqlw ttwaggeirv fgdkcldayn
      481 qgtangtrvi twpcngqdnq kwtlgsdgti rnvhaglcld vngsgtanat plvlwscngq
      541 agqkwsra
//
LOCUS       WP_284436297             893 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284436297
VERSION     WP_284436297.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 893)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 893)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 893)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 893)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19885573
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..893
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=96349
     Region          31..>379
                     /region_name="PRK04841"
                     /note="HTH-type transcriptional regulator MalT"
                     /db_xref="CDD:235315"
     Region          <602..798
                     /region_name="TPR_MalT"
                     /note="MalT-like TPR region; pfam17874"
                     /db_xref="CDD:436107"
     Region          706..893
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <833..892
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mvvstvatgd rnsavppgsr adplgdpyls trfavpsrpa tflarprltr hldqalrtpl
       61 tmvngsagag ktllvadwta gldrqvtwlt vetgeqkpgm fwayflqalr asgtplsdrv
      121 hcpadpnrvg hkvlseiaed lvgrdpallv vldefdrvsg sevaeqlefv lqhagsglrl
      181 vlvtrnepvf slhryraaga lteirdaela ltpeeaaall elhglslpag avralvertr
      241 gwaaglrlca laaqespdpe tylkefeadh stvadfllae vlrrqpretq dlllrvsvld
      301 rfcpdlvngl thrtdteril adlhrdnafv eqlgqgwyrl hplfgeilqt hlrvrnpgle
      361 pdlhrsaaqw lqrrgtlpea lahgaaaadw dftagalvdd laigqfftgl rsddlnelfs
      421 rmgpeatgpa telvraardl aqsdldrgma hlhhaeagla geegdpaaaq lscalleava
      481 arltgspara eqaaetaeev rtevpahlld khpelpalll thlgstrlwa gryedaraal
      541 teaadcpgga ltvlpreesm ghlalidyln gwpgraehka laavseterf slpqpsgsgi
      601 erlvlaavav drneldraqa lldeadelaf etqdpvkaag raiatarlql argnaraame
      661 satpalstav aspwadsler vvasavhlae gryetaadll ghlpddrpaw lveaariqla
      721 agrtgtalel ldsvpaesrp gpavtvraal vraraahaag daetarrfve qallgarrer
      781 lrrpfleagr wikpflvapp lralaagwll pdpgagrpaa agpppapivv qelsererdv
      841 lqrlarmmst qeiaadlyls vntvkthlks lyrklavnrr seavrrardl glm
//
LOCUS       WP_284436324             440 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284436324
VERSION     WP_284436324.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..440
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45646
     Region          20..411
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(30..31,34..35,38,72,122..123,125..127,130,150,
                     153..154,157,255,258..259,262..264,267,294,298,347..348,
                     352,356,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mssspsplsa rggrlallvv glcwlavlfd gldmfiygsv lphlletrtf gltpdqagdl
       61 gsyatfgmlv galaagtvad rigrkklmvs cvtlfslasg lcaladgvav fglgrtlagv
      121 glggllptai smvsdyaprg rgaivigllm tahhaggils ayvakwlvdp vgwraafwvc
      181 vlpllfapvl akflpeslsl lvakgraeea ralagrydve vpaartggag drwgnlanlf
      241 rgnewiqtll ywaasfggll lvygvatwlp tlmraegyel gsalsfvvvf nlggivgmlv
      301 agraadrfga priaaiwfal taagvfllsv hlstavtmiv vfltgvflns aqtmiyatvs
      361 irsradnrat avgwtsgmgr fgavfgpwlg gqllasgngd rgftafavag lssmvfigva
      421 alrgsrqapt gserelvaah
//
LOCUS       WP_284436389             453 aa            linear   BCT 25-DEC-2024
DEFINITION  HesA/MoeB/ThiF family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284436389
VERSION     WP_284436389.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..453
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47539
     Region          106..>363
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mteaaavtve afgrprikpe hrayrtvdgn vrvgsvihgi gaeiadpqgw vwtlveamdg
       61 trgpsqvvee vlrthpdltg edareamadl laagfvddaa ataplppree drysrgvpll
      121 rwmdlaprts pwdaqlrlre arvlligvgg tgghaaqalv asgvghlhcv dpdvvelsnl
      181 nrqplyrepd lghpkadtav ttlrslnsdv tvtgerrevr gpedltelva gtgepvtgtg
      241 epvrtpcaag pvedpagrtk gpggrtgsap vgsapsdrrr pvgslggpgr aasssqhdpa
      301 pppspsspyd llvlaadrpe airrwvnrvc laaglpwvda gyrgplvtag vyvpgrgacw
      361 eclrdgemar rdlrlgpgqd pevasprmpw npasavtagl sgallahaal alltgapame
      421 pgfrfgvnlm lpgdpvhqrt prrpdcpacg erg
//
LOCUS       WP_284436428             389 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284436428
VERSION     WP_284436428.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..389
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42742
     Region          71..359
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 magkrrqfgr vrklpsgryq aryvgpdgll rpapetfatk rdaddwladk qtemrrgdwh
       61 dpdagkvpfg eyaaawvrer elttttrqly gsllrhhlep tfgtvnvaei spplvrrwra
      121 dklssgtgpt tvakayalmr avlgtavgdl lirrnpctik gastvhtper ptatvqevyd
      181 ladaiqpryr alvlmggflg lrwgelvglh rrdvdldlra vrvrravael nngqreikap
      241 ksaagkrtva ipaaivpeir ahldvyaehg adgrvfvgak gatprrnhfn rlwhkacsda
      301 gikglhfhdl rhtgntlaas tgastrelms rmghstaraa liyqhasadr drliadavsg
      361 lvdkgrkkak kakkkqdrkp kghagdteg
//
LOCUS       WP_284436568             210 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284436568
VERSION     WP_284436568.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..210
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23257
     Region          7..200
                     /region_name="HAD_sEH-N_like"
                     /note="N-terminal lipase phosphatase domain of human
                     soluble epoxide hydrolase, Escherichia coli YihX/HAD4
                     alpha-D-glucose 1-phosphate phosphatase, and related
                     domains, may be inactive; cd02603"
                     /db_xref="CDD:319790"
     Site            order(12..16,117..118,150,174..175,178..179)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            145
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mptdrhrivl fdlfgviarh qrpgalekma archssldaf ttaywthrpp ydagrhtast
       61 ywtdvlhals hpadtdadad tieelrltdi dswsrvdedm iayvrslrnr arvallsnip
      121 adhadaflaa qpwlndldhv afsgrigaak pdpaafrhcv talhaapsdf lfvddreenv
      181 raaqavgmng hvfdsraela pvvdawlpsr
//
LOCUS       WP_284436597             328 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284436597
VERSION     WP_284436597.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..328
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34356
     Region          4..327
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mrgrshalrg allalslflv tgcqvlpdge gadtglrimv pnipgggydt tartvarvlq
       61 etgvdsgvqv fnlpgaggtv glqrivnerg ngrlvlqmgl gvigashvah akasviettp
      121 larlveeaga vvvrrdspyr siddviaawk rnpaslkvgg gsspggpdhl lamelakavg
      181 ikphrvgyva ygggggdllp alldgkvdfa ttgfgefldq idasqlrvla vtsprpidal
      241 pgvptlkasg idlvfsnwrg vvappgikga drkrwiealt amhrsrqwka elrrhgwtda
      301 fttgdafaay lseqdtsvar lvrdlgld
//
LOCUS       WP_284436653             995 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 35 protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284436653
VERSION     WP_284436653.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 995)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 995)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 995)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 995)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 995)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15708332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..995
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..995
                     /product="glycoside hydrolase family 35 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=107526
     Region          61..399
                     /region_name="AmyAc_family"
                     /note="Alpha amylase catalytic domain family; cl38930"
                     /db_xref="CDD:476817"
     Region          415..577
                     /region_name="BetaGal_dom2"
                     /note="Beta-galactosidase, domain 2; cl19747"
                     /db_xref="CDD:473202"
     Region          586..645
                     /region_name="BetaGal_dom3"
                     /note="Beta-galactosidase, domain 3; pfam13363"
                     /db_xref="CDD:463856"
     Region          685..806
                     /region_name="BetaGal_dom4_5"
                     /note="Beta-galactosidase jelly roll domain; pfam13364"
                     /db_xref="CDD:463857"
     Region          856..964
                     /region_name="BetaGal_dom4_5"
                     /note="Beta-galactosidase jelly roll domain; pfam13364"
                     /db_xref="CDD:463857"
ORIGIN      
        1 melsrrtfsa lagttalgfa lsgsggettr ayashsvptg papgapaadr vrhtvgydkh
       61 sllvdgrrlv lwsgemhpfr lpspslwrdi lqkmrahgfn avsvyvawny hspgpgqydf
      121 tgvrdldlfl rtatetglyv ilrpgpyina evdgggfpgw ltatagrart sdpaylsyvd
      181 ewltavdaia arhlftkgrg tvllyqiene ydafvdeplg rdymshlykk vradgidvpl
      241 fhndkgrngy wtpgsfntgg eergwlygfd gypqpsevpp dwgdfgaggl kggatasprt
      301 pgfipefggg wfdpwggaaf dgkgyaearr trdaayerrf qltnlangit vhnvymtfgg
      361 tswgwlpapq vytsydygaa fdearrptpk lapthqlghl lrtvpdfakl dradavraad
      421 erlkvyhltn pdtasqvyvv rndtdapitt tipdagidva ftvaahdarl ltanlqlggr
      481 ilkfataqpm mclkvgrmdv avftaphgem aqvllecpee plvtrgdaep awnydlgvlr
      541 itapmgvggl arvrveaggs dtplllifad dpgslrlfpi dtptgtvlvy gpslvrgvtl
      601 dgasahltgd tvegtgmevw gprgmgritw ngrplrtsat pmgslradmp atpgllpvpa
      661 vgevrlpalg nwrrrtenfe slpdyddsgw ttadrtssys vtpvpkgqpv lfaddygfhy
      721 gdvwyrgrlt dadelesvsl sygtgtqgll mawldgeplg thrmpvpdkg tarkgswtat
      781 atfevpaatg rsprvlsvlv rrmahdmdgg sadshkaarg ltsvtfkgas pkvswriqge
      841 tasdavrgpl nngglygerk gwhlpdfgee hwesaklpra drrqgvtwyr ttfrlavdtg
      901 idasigltld ddperayraq iflngwnmgq yvndvgpqht fvlpngilrt rgtntlalav
      961 lsdgttesgp gdvrltllga aaggvpvaqv dspgr
//
LOCUS       WP_284436686             300 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            sp. TUS-ST3].
ACCESSION   WP_284436686
VERSION     WP_284436686.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..300
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32060
     Region          17..291
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtdpraqprp tpgvtplrfg ygtngladlr lddaltllae lgyegvgltl dhmhldpiap
       61 dlaartrrla hrldalglta tvetgaryvl dprrkhgpsl ldpdpddrar rvdllvravq
      121 vaadlgahav hcfsgitpqg tdrdtawkrl aetltpvlda ataagiplai epepghllaa
      181 ladfhhlrtt lgdppalglt ldighcqcle pqppadcira agpwlrhvqi edmrrgvheh
      241 lpfgdgdidf ppvlaalaat gyqgltvvel prhshagphf aelslpflrq aealsqgstp
//
LOCUS       WP_284436703             608 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284436703
VERSION     WP_284436703.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..608
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66703
     Region          1..608
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mreftnppla laapvgglad vvfehaqndp vhialgrkdg dgrwrdvtsa efrdevmala
       61 kgllaqgirf gdrvaimsrt ryewtlfdfa lwtigaqvvp vyptssaeqc fwalydaect
      121 aaivehedha mtiatvidrl pqlhrlwqld sgavqelyda gtaiedevvh rhrqavtpds
      181 vatiiytsgt tgrpkgcvit hgnfmyeadt vierwepvfh skkgdeaatl lflplahvfg
      241 rmvqvaairg rvrfghqpqm naaallpdla afkptfflgv pyifekvfna srrkaekegk
      301 agpfekavdv avkyaeamea kawgigpgps aglrmqhqlf dklvyskmra amggrikqam
      361 tggsamdrkl glffagagvh iyegygltes taaatanppe rtrygtvgqp ipgmtvhiad
      421 dgeiwlygan ifqgylnnek atdetlhdgw latgdlgsld edgyltitgr kkeilvtsgg
      481 ksvspgvlee rvrdhplvsq civvgndrpy vaalvtldqe avehwlgmrd kprmspaqlv
      541 rdadletevr ravvaantlv sqaesirtfr ilaqpfteeh glltpslklk rkaietayan
      601 evealyra
//
LOCUS       WP_284436729             259 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284436729
VERSION     WP_284436729.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..259
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27700
     Region          <23..149
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 msdtahdttn ggpprltrlt fhgplseara dalvrrlala kpasvldlgc gwgelilril
       61 aavpaatgtg idlaaedlnr grrnaealgl adrvrfvqes avgtsrgpad lvlcvgsshv
      121 ltateppghl pdalrelrrl vrdggrvllg egfwqrtptp aelsgmwpga aasdqvdlas
      181 lvdlavaagf rpewtetasl deweefesgy qadaevwlad hgdhplaaat rerldrhraq
      241 wlsyrgvlgl ayltlvpvr
//
LOCUS       WP_284436867             164 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-class carbonic anhydrase, partial [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284436867
VERSION     WP_284436867.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130171
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..>164
                     /product="beta-class carbonic anhydrase"
                     /GO_function="GO:0004089 - carbonate dehydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
     Region          35..164
                     /region_name="beta_CA_cladeD"
                     /note="Carbonic anhydrases (CA) are zinc-containing
                     enzymes that catalyze the reversible hydration of carbon
                     dioxide in a two-step mechanism in which the nucleophilic
                     attack of a zinc-bound hydroxide ion on carbon dioxide is
                     followed by the regeneration of an...; cd03379"
                     /db_xref="CDD:239474"
     Site            order(35,37,44,46..48,60,63,82,87,97,100,159)
                     /site_type="active"
                     /note="active site clefts [active]"
                     /db_xref="CDD:239474"
     Site            order(44,46,97,100)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:239474"
     Site            order(45..48,54..55,60..62,64,66,77..78,81..82,159,
                     161..162,164)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239474"
ORIGIN      
        1 mstspprtat vtdrlveanr ayaagftdpg mgarpvlrva vvacmdarld lhaalglelg
       61 dchtirnagg vvtddtirsl tisqralgtr svvlihhtgc glqtltedfr helelevgqr
      121 pawaveafrd vdqdvrqsmq rvrtspflph tddvrgfvfd vatg
//
LOCUS       WP_284436871             533 aa            linear   BCT 25-DEC-2024
DEFINITION  formate dehydrogenase beta subunit [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284436871
VERSION     WP_284436871.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11555116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..533
                     /product="formate dehydrogenase beta subunit"
                     /GO_component="GO:0009326 - formate dehydrogenase complex
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=56100
     Region          10..100
                     /region_name="TRX_Fd_FDH_beta"
                     /note="TRX-like [2Fe-2S] Ferredoxin (Fd) family,
                     NAD-dependent formate dehydrogenase (FDH) beta subunit;
                     composed of proteins similar to the beta subunit of
                     NAD-linked FDH of Ralstonia eutropha, a soluble enzyme
                     that catalyzes the irreversible oxidation of...; cd03063"
                     /db_xref="CDD:239361"
     Site            order(10,12,46..48)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239361"
     Region          106..515
                     /region_name="NuoF"
                     /note="NADH:ubiquinone oxidoreductase, NADH-binding 51 kD
                     subunit (chain F) [Energy production and conversion];
                     COG1894"
                     /db_xref="CDD:441498"
ORIGIN      
        1 mntpshstat vyvprdsaar svgadevaha lqqaagrgdf aldvvrngsr gmlwleplve
       61 vvtpqgrvgy gpvapedidg llaagmldga dhplrlgivd elpwlarqnr vtfarvgvtd
      121 plsaedyeah gglaglraal elgpadvvae vtasglrgrg gagfpagikw ktvldcedel
      181 kfvccnadeg dsgtfadrmv megdpfmlie gmtiaahavg anegyiyirs eypdavatmr
      241 raigiarehg wlgrnilgsa ldfdlhvrvg agayicgeet smleslegkr gmvrakppip
      301 aieglfgkpt vvnnvltlat vpvvmaegaq ayqdlgvers rgtqvfqlgg niahggivet
      361 afgitlreli eeygggtrsg rpvrtaqvgg plgaylpesm fdlpmdyeaf aaagamvghg
      421 gvvvfddsvd maaqarfame fcaeescgkc tpcrvgavrg vevidkivag thrdenlall
      481 edlcdlmteg slcamggltp lpvrsalthf pddflggrrl leihpvrate gta
//
LOCUS       WP_284436882             326 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284436882
VERSION     WP_284436882.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..326
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=34202
     Region          52..320
                     /region_name="2-desacetyl-2-
                     hydroxyethyl_bacteriochlorophyllide_"
                     /note="2-desacetyl-2-hydroxyethyl bacteriochlorophyllide
                     and other MDR family members; cd08255"
                     /db_xref="CDD:176217"
     Site            order(62,64..65,70,129,133,153..158,177..178,182,209..210,
                     212,232..233,259..261)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176217"
ORIGIN      
        1 mkpdarafwl rspgegeire aalsapgede vlvrslysgv srgtetlvfr gqvpesqyaa
       61 mrapfqegdf pgpvkygyls vgvveegpaa lkgrtvfclh phqtryvvpa savtvvpddv
      121 paaravlagt vetavnalwd aapligdria vvgggmvgss vaallarfpg vrvqlvdtdp
      181 araktaealg vgfaspadal gdcdlvvhas ateqglarsl elltaegtvv elswygdrrv
      241 alplgevfhs rrlvirssqv gtvspargnr sygdrlalal elladprlda litgesafee
      301 lpevmpllas geipalchlv rygksa
//
LOCUS       WP_284436883             132 aa            linear   BCT 25-DEC-2024
DEFINITION  6-pyruvoyl trahydropterin synthase family protein [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284436883
VERSION     WP_284436883.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Phillips,G., Grochowski,L.L., Bonnett,S., Xu,H., Bailly,M.,
            Blaby-Haas,C., El Yacoubi,B., Iwata-Reuyl,D., White,R.H. and de
            Crecy-Lagard,V.
  TITLE     Functional promiscuity of the COG0720 family
  JOURNAL   ACS Chem Biol 7 (1), 197-209 (2012)
   PUBMED   21999246
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Colloc'h,N., Poupon,A. and Mornon,J.P.
  TITLE     Sequence and structural features of the T-fold, an original
            tunnelling building unit
  JOURNAL   Proteins 39 (2), 142-154 (2000)
   PUBMED   10737935
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..132
                     /product="6-pyruvoyl trahydropterin synthase family
                     protein"
                     /EC_number="4.1.2.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14336
     Region          1..132
                     /region_name="QueD"
                     /note="6-pyruvoyl-tetrahydropterin synthase [Coenzyme
                     transport and metabolism]; COG0720"
                     /db_xref="CDD:440484"
ORIGIN      
        1 mfsitvrdhi miahsfrgev fgpaqrlhga tflvdatfrr eqldddnivv diglatqelg
       61 avvselnyrn ldnepdfagi ntsteflakv iadrlgerie kgalgegakg lagltvtlhe
      121 shvawasyer al
//
LOCUS       WP_284436915            1016 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-mannosidase [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284436915
VERSION     WP_284436915.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1016
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..1016
                     /product="alpha-mannosidase"
                     /calculated_mol_wt=112018
     Region          248..1012
                     /region_name="MngB"
                     /note="Alpha-mannosidase [Carbohydrate transport and
                     metabolism]; COG0383"
                     /db_xref="CDD:440152"
ORIGIN      
        1 mhderrriee rvqrahdqri kpaiyaatvp feveawqapg epvsfeeaaa arytpfamdt
       61 pwgppwgttw frmrgqvpae wagkrveavi dlgfvgdwpg nqaealvhlp dgrplkavnp
      121 lnqyvpvanp atggeqidyl veaasnpdil kdnfskvtpm gdkltagsap lytfqradla
      181 ildenvwhld ldlqvlrelm vhlpdheprr heilhaldra mdaldlddva gsaaavrevl
      241 apvlakpaha sahtisgvgh ahidsawlwp iretkrktsr tfsnvtslad eyddfifacs
      301 qaqqyewvrd nyphvwariq dsvkkgqwap vggmwveadg nlpggeamar qlihgkrffi
      361 ehfgietkgv wlpdsfgyta aypqlaklag ndwfltqkis wnqtnkfphh tfwwegidgt
      421 rifthfppvd tynarfsgee mdravrnyse kgggrrslap fgwgdggggp treimerarr
      481 ladlegspkv vvehpddffa qaraeypdap vwvgelylel hratytsqar tkqgnrrseh
      541 klreaelwat taalhapgya ypyekldrlw ktvllhqfhd ilpgssiawv hreaeaeyar
      601 vaeelealta eavaalgagg trafntspfd raevvragdq alayvevpan gsaeltgaep
      661 arpvgvsgrt ldnglvrvev aedgtlssvf dlragrevlg dkgnllrlht dlpnywdawd
      721 idshyknryt dlleptsvev vsedpllgai rvtrafgkgs titqtitlra gspridfetd
      781 idwheaekil kaafpvdvra ahssaeiqfg hiqrpthtnt sweaarfevs ghrwvhvgep
      841 gygvavlnds tyghdvsrtv redggttttv rlslvrapri pdpeadqgth rftysllpga
      901 sieetvaegy slnlplrvad aagapepvvs vdgqgvtvea vkladdgsgd vvvrlyesgg
      961 grasgvlrtg fplagaqitd llerpletap veddgvavql rpfqvltlrl sragvs
//
LOCUS       WP_284437046             426 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284437046
VERSION     WP_284437046.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..426
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=45411
     Region          187..407
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mttaraparq epgtgpgarp rilltlvlia aampvrlass vpginsvsvl dillgavait
       61 lvvdlafrpl dvgypelfal lcvpvvvcgm smlwtqdrga tfratvvyae givaylfvvr
      121 elngaspdrv mtyirryscl lvvpavllll rtpgfgpeet glphdsdryl syytrlshpa
      181 lgpsnnlatv laffvpllly wghvrhdrrf tlagcvtlaa vvctlsrgvv lglltaavla
      241 glgsllrrrr vgtrafgkia aavavvvmav allyrlvpdt dtvlagrlsp analirsqfa
      301 veavgkiaer pllgygggap pdgmwelarv hntylqqmvs fgvllgafvs lalagtavff
      361 fsrwrtsapa rvvgftlvaq lvvfavessf egtvlrvlfy lsvglaamvv raseerpvap
      421 psrgrn
//
LOCUS       WP_284437058             437 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284437058
VERSION     WP_284437058.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..437
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=46011
     Region          1..434
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrltvigtgy vgavhaacma highqvlgvd vdpdriaalt agrppfyepg lagmlkrtvd
       61 agrlrfstsv aeavrfatmh fvcvgtpqlp gadaadlrhv eaaverlaah lpggaesvlv
      121 vgkstvpvgt aerlagrlgt aadvawnpef lregravqdt mcpqrivvgv ptaraearlr
      181 evyapltavg vpfiatdpat aelvklasns flatkisfin amaeicdgtg advltlaeam
      241 gadprigprf lvpglgfggs clpkdirafa araeelglge svaflrqide intrqrrrtv
      301 elaerlvags fpgrrvavlg aafkpgsddv rdspalavae avrgrgaqvc vhdpeaadna
      361 rvahpalrfa pdvtktcdra dvvlhltewp qyreldpval asvvrtpaiv darhtldpka
      421 wqaagwtlca pgrprlg
//
LOCUS       WP_284437277             279 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284437277
VERSION     WP_284437277.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..279
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30773
     Region          28..88
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(32,36,61)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(35,60)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(42..43,54,57,61..62)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          100..274
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msvdaavepg wevdpddewg vaviatvgrq lklrreavgm raaefgeavg ygedlvykie
       61 ggkriprqey ldradevlga ggllsaawed vkkvrypkkv relaklegqa veigvyepns
      121 vhgllqtpdh aravisaaqp pytpddverm vtarlarqsv fervpapsih fvleeaalrr
      181 piggtmvwrr qlehllevgr lhnvmlqvmp lntevhsgld gkievlkfpd gtavgrsegr
      241 ptsdpkqlri lelrygtira qalspreslv lieqllget
//
LOCUS       WP_284437358             505 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: flavin monoamine oxidase family protein [unclassified
            Streptomyces].
ACCESSION   WP_284437358
VERSION     WP_284437358.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..505
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52248
     Region          48..505
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 marerqipsl splprlsrrs liggaaaaag aaaltgtaas pasaattrdv dvaivgagla
       61 gltaardlva ggktvavlea rdrvggrvln lplanggvte gggefigptq drikaladsl
      121 gvgtfatynt gknllykdgk ktayatdgil gsvppidaag lanaaivqas lddmaktipl
      181 dapwtaakae ewdrqtfetw lranavipsa kflldvacts ifsaeprels llfvlfyiaa
      241 agnettpgtl erltetagga qelrfvggsq lvpiklaatl gdrvvlnapv rtiaksgaky
      301 vvtadgvtvt akrvvvavpp plaaritydp llpaardqlt qrlpmasvgk aiaiydtpfw
      361 radglngqvv sdtgvisstf dnsppdasyg almgfieade arkfdaasea evkaavlkdy
      421 vtyfgskaas ptsfvlqrwn neaytrggpv sigapgvltq ygpalrapvg gihwagtets
      481 ihwmgfmdga vrsgervake vlsvl
//
LOCUS       WP_284437449             234 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284437449
VERSION     WP_284437449.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..234
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24124
     Region          <104..216
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          153..205
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mgvrlmvvdd hrllaealas alklrghrvl aaaapaagaa elvisrapev cllgtatpae
       61 pgmfdpvvki krerpqvavl vlgpvpsprg iaaafaagas gyvrhderie gveraimkar
      121 ageaavapql lqgafselln paaqpddegq rllqmltpre vevlvrvadg edtrliaagm
      181 giapstarth vqrvlmklgv gsrleaaala artglldrag pvaqaqpqpp aagl
//
LOCUS       WP_284437533             377 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Streptomyces sp.
            TUS-ST3].
ACCESSION   WP_284437533
VERSION     WP_284437533.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..377
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40000
     Region          23..377
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrdlrrrsll agalavplta slpvlpaqar tasgpdagal raaiaglpda nataalvrvg
       61 gsdgswrgss gvhdlesgrp adpgarfrag sttkvvtaat vlglvaegri dlgrpvqhyl
      121 pglldsrfrp vtvrqllnht sgipagdglg ttfekvyahr fdtlaperva asagakepef
      181 cpgkqqhyln inytflglli ervtgrsyaa eagrlvlapa gmrdtyfpgt dprilgphnr
      241 gyqavrradg ttefvdvtew nqadrfaagd mistiadler lltglfrgri vprplmrevf
      301 svpsgitgas ysagglqrfe idgkvywvks ggrygynsai aatcdlsrtl vysvnstdak
      361 sedanpvvvr iitaalr
//
LOCUS       WP_284437877             585 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD/NAD(P)-binding protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284437877
VERSION     WP_284437877.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11816065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..585
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64456
     Region          2..542
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
     Region          6..151
                     /region_name="NAD_binding_9"
                     /note="FAD-NAD(P)-binding; pfam13454"
                     /db_xref="CDD:433222"
ORIGIN      
        1 mrrslvivga gprgtglier iaanapelyd gsgldlhlvd phppgagriw reaqspllwm
       61 nshaedvtmf tdetvamegp vrpgptlhew agiegrtfad rqlqgaylrw vheravaalp
      121 psvsvhhhpr ralrvsgpre grqqvwlegr srplladlvv lalghldael ddeqqdlaay
      181 arthdlvhlp pdftadsdls alapgepvlv rgfglafvdl malltegrgg rydgdtylps
      241 grepvlhvgs rrgvpyhski gydwtgerpp lprflgpdri dellarpggf afgrdvwplv
      301 ekelgfahyh rlftvhpert amswadfeek yaavedlver etlvasavpd prdrldlarl
      361 drplegvrya theefqeglr eyveadlsrr hdpryspdla vflgllsvyg qlvrlgdigg
      421 rwhgffsyla sgppgprlrq llalsragvl rfvgadmevr aedgvfrass ptvpghsvea
      481 ralvearlpe ptvrraldpl lrelyaegaa espdgllrvd radgrvldrs grphprrfal
      541 gphtdgrtpg aftrprtggp afrqndatar aalrflgela graaa
//
LOCUS       WP_284438027             275 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284438027
VERSION     WP_284438027.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..275
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30317
     Region          197..>267
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mmtttlrpte plqrgadgal srhysvcvns rpvgaihlat hpsfgtavaq irdlridepd
       61 rrrgrgtvaa laaeevargw gcgqlevrvp adagpalrla tmlgyvhrnr gmekqlgata
      121 pelpagsrar pmtqaefepw arrgileytr dwtergvpet eararserdn rqlverglvt
      181 eearysvleh egvrvgvlwv efvddkafvy dveseeafrg rghgrslmll aeaqaiasgr
      241 rvlglnvfag ntpaerlyes lgyttvgysm yksll
//
LOCUS       WP_284438185             460 aa            linear   BCT 25-DEC-2024
DEFINITION  nitrate/nitrite transporter [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284438185
VERSION     WP_284438185.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 460)
  AUTHORS   Yan,H., Huang,W., Yan,C., Gong,X., Jiang,S., Zhao,Y., Wang,J. and
            Shi,Y.
  TITLE     Structure and mechanism of a nitrate transporter
  JOURNAL   Cell Rep 3 (3), 716-723 (2013)
   PUBMED   23523348
REFERENCE   6  (residues 1 to 460)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   7  (residues 1 to 460)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..460
                     /product="nitrate/nitrite transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48381
     Region          41..432
                     /region_name="MFS_NRT2_like"
                     /note="Plant Nitrate transporter NRT2 family and Bacterial
                     Nitrate/Nitrite transporters of the Major Facilitator
                     Superfamily; cd17341"
                     /db_xref="CDD:340899"
     Site            order(51..52,55..56,59,91,145..146,148..150,153,172,
                     175..176,179,247,250..251,254..256,259,287,291,343..344,
                     348,352,385,388..389,392..393,396)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340899"
ORIGIN      
        1 mtapstapap qnrggrwieq wdpedetfwk etgekvarrn lffsvlsehi gfsiwtlwsv
       61 lvlfmgpeyg ltpadkfllt smvtlvgavv rvpytfavai fggrnwtiis agllliptva
      121 afavmkpgts fstflvvgll agigggnfas smtninaffp lkkkgwalgl nagggnigvp
      181 viqlialaii gasggprvll giyiplilva avlaalymdn lssvkndtga akdaakdaht
      241 wimsflyigt fgsfigyafa fgqvlqvqfg rtplqaaylt figpllgsli rpfggwladk
      301 yggakitlyn yvamaaatgi livasmqksl alfvcvfvvl fvlsglgngs tfkmipgifq
      361 tkalakgleg eaaaaygrrl sgasmgliga vgalggvgin lafrqsfltn gsgtgafvtf
      421 llyyalcfgv twavylrrta vqgeataaae tkpqlsyaev
//
LOCUS       WP_284438189             807 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Streptomyces sp. TUS-ST3].
ACCESSION   WP_284438189
VERSION     WP_284438189.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TUS-ST3
  ORGANISM  Streptomyces sp. TUS-ST3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 807)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 807)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 807)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Streptomyces sp. TUS-ST3"
                     /db_xref="taxon:3025591"
     Protein         1..807
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=87705
     Region          16..790
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 maaqaqptav gsvqdsvrdr eisveqehld rvyrrleeki heaeflmnda akrgqvgtpg
       61 alaerdaqvf ragvhlnrln nefedflfgr idlllgkdgk kgpdgaytav epaegavrdd
      121 ntadiaetlh igrigvldse yaplvidwra paaapfyrst pvdpgrvvrr rvirskgrkv
      181 lgveddlmrp elrafldghq lpvigdgalm aalgqarsht mrdivasiqa eqdlvirapa
      241 asvtyveggp gtgktavalh raayllyqdr rrysggiliv sptpllvayt egvlpslgee
      301 gqvairaigs lvdgveatly dspavarakg syrmlkvlrk aargalelga dgsgrapgrs
      361 sdsgqlafgd sgepddgagr gngagtavsp ksgpptrlrv vafgrrlele adelerirrn
      421 alsgtapvnl lrprarklll dalwarsgag srhtdpelaa elrssfdedi vsedsfiefl
      481 dawwpeltpk dvlaamader rlgrwarril npgevrrvar slrrdglsvh diavldelqa
      541 vlgvparpkr rreldpldql tgleelmpvr eetqreraer laqerveyah vivdeaqdlt
      601 pmqwrmvgrr grhatwtvvg dpaqsswsdp deaaeardea lgtrprrrfq ltvnyrnpse
      661 iadlaakvla lampgsespr avrstgvepr fvavgrslae tvraeaarll elvdgtvgvv
      721 vamqrreeaa rwlaglgdrv valgsleakg leydatvvvs paeiadespa glrvlyvalt
      781 ratqqltvvs gdrdqpdaqa vpdllrd
//
LOCUS       WP_284438234             150 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium guaraldiae].
ACCESSION   WP_284438234
VERSION     WP_284438234.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium guaraldiae
  ORGANISM  Corynebacterium guaraldiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Corynebacterium guaraldiae"
                     /db_xref="taxon:3051103"
     Protein         1..150
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=16486
     Region          1..>146
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mrflpelegv ralaalavvv thvsfqtatg wawaerldyg vavffvlsgf llwrrrhaht
       61 agqyvlsrva rlaplylvcv vvvlallpda spltlpqvit nltgtqlyia dglipgltql
      121 wslcvefafy avlpllawll dklsarrglr
//
LOCUS       WP_284438437             354 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Komarekiella delphini-convector].
ACCESSION   WP_284438437
VERSION     WP_284438437.1
KEYWORDS    RefSeq.
SOURCE      Komarekiella delphini-convector
  ORGANISM  Komarekiella delphini-convector
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Komarekiella.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 354)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 354)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Komarekiella delphini-convector"
                     /db_xref="taxon:3050158"
     Protein         1..354
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38854
     Region          22..325
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mystleqkyq riqkelmaga ialggvllig tlwywlvegw swqdaaymtv itlatvgyge
       61 tqplgsrgrl ftialillgv vnigyivnrf teaiiqgyfq egirlrqqkr lmesltqhyi
      121 icgfsrtgrq iakefrsegv sfvvidseie svqraqnegy tayqgdatld dtllkvgier
      181 aicivaalps daenlytvls aktlnpeira iarasteeal qklqrggade vispyitggk
      241 rmaaaalrpq vldfvdgilt gadrqlymee flldpafcpf vgqtlqkarl rsqsgalvla
      301 irrvdgnlig gptgetvlmp gdrlicmgta eqlrslnqil gpigsqklre pknt
//
LOCUS       WP_284438459             783 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Prevotella
            communis].
ACCESSION   WP_284438459
VERSION     WP_284438459.1
KEYWORDS    RefSeq.
SOURCE      Prevotella communis
  ORGANISM  Prevotella communis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 783)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 783)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 783)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Prevotella communis"
                     /db_xref="taxon:2913614"
     Protein         1..783
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88833
     Region          106..747
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mmfltisvsa qdiyssaena ykigridsal vilkshensf qgtdrqkayr lislcclald
       61 mteesekyag qllkenknyy gslqdpvrfv dminrlregr gttiktasgq eelieeapvp
      121 vtiitremid mlsnnrnigq ilaayvpgms eictyafsnv amhgvytngq ekilvmengh
      181 rlnarstnng kldyaistek idhievlrgp asslygnval tavvniitkr gneingvkgk
      241 ygygtfgthr adlvagatfl gadvmawasl ytsegerldi pkgsgysqtq hdgyvyvgry
      301 egrpsfdvgf nlqlndftlm lnrksgklvp qyswyaetyd ydrfrqfcgv tpgysideth
      361 lnlsynkdfn hsnlnmtiyg dwykfqdyqa vsdsmityef ksdgsgtpvi gadgkpvtrl
      421 yhgvfqddnw eeytigatak fstnyhigkt kgnllagaqf efyripinef ffgedynrfi
      481 iittpespnq lnvgheksis gfiqnkhyft dqlilnaglr ydkkyrrndm sveafsprva
      541 lvyvpsktfs vkasysrsfv dapyfyrqnt qntykgsedl mpeymnaiql dflgsigghf
      601 dydvnlfynh ltdlicnnqs tdlnapkyvn sgslkvagie telsykttaf rsrlnttfqr
      661 amsaeqyyyy dhhiysipsv tanlaceqrl fdkknhslwl sgnlrytsrt lnkansrvtg
      721 sedfylnera lvdlrlkydy nktmqlsldc dnvfntcyei ggtsyipyry pgrtlmgtva
      781 fkl
//
LOCUS       WP_284438676             796 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Prevotella
            communis].
ACCESSION   WP_284438676
VERSION     WP_284438676.1
KEYWORDS    RefSeq.
SOURCE      Prevotella communis
  ORGANISM  Prevotella communis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 796)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Prevotella communis"
                     /db_xref="taxon:2913614"
     Protein         1..796
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90029
     Region          119..760
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 minhlriylt vvaltllamp asaqdvyvqa enaykigrid salvllkrne kaflgtdrqk
       61 ayrlmslccl aldqpeqsey yaglllnenk yffgsledpv rfvdminrlr egrgttikta
      121 sgqeenieea pvpvtiitre midmlsnnrn igqilaayvp gmseictyaf anvamhgvyt
      181 ngqekilvme nghrlnarst nngkldyais tekidhievl rgpasslygn valtavvnii
      241 tksgneingi kgkysygsfg thradltagt tflgadvmaw aslytskger itipagsgys
      301 qtphdgyayv gryegkpsyd igvtiklndf nlmvsrkygk lvpqyswyaq tydydryrqf
      361 fgvtpgysvn enhlnleydk sfgssnlnia lygdwyqfqd yqvvsdsmyn vefnpdgsgt
      421 pkigpdgkpv mrlyhgvyqd dnweeytiga takyssnyki gnqhgnllag aqfefyripv
      481 nefflgeeys nitivttpes pnqlnvghek sisgfiqnkh yftdqlilna glrydkkyrr
      541 ndmsveafsp rvalvyvpsk tfsvkasysr sfvdapyfyr qntqntykgs edlmpeymna
      601 iqldflgsig ghfdydvnlf ynhltdlicn nqstdlnapk yvnsgslkva gietelsykt
      661 tafrsrlntt fqramsaeqy yyddhhiysi psvtanlace qrlfdkknhs lwlsgnlryt
      721 srtlnkansr vtgsedfyln eralvdlrlk ydynktmqls ldcdnvfntc yeiggtsyip
      781 yrypgrtlmg tvafkl
//
LOCUS       WP_284439713             484 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Cellulomonas xiejunii].
ACCESSION   WP_284439713
VERSION     WP_284439713.1
KEYWORDS    RefSeq.
SOURCE      Cellulomonas xiejunii
  ORGANISM  Cellulomonas xiejunii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Cellulomonadaceae; Cellulomonas.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 484)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Cellulomonas xiejunii"
                     /db_xref="taxon:2968083"
     Protein         1..484
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=51514
     Region          12..468
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mhellsaasa dayvdamrgt vdrvatrfrt ttrpfsgasr ehlqslvdav dldgpgrgta
       61 aalrevdelf aqhavwfhdp aytahlncpv alpavaaeav laainpsvdt ydqstvgtlm
      121 errvvawtaa rigflagggv ftsggtqsnl qalllareha latapgvtlr dlvvlatass
      181 hfsvqrsayl lgmapdavrl vpvdergrmr pdalaialrh vaddgrhaaa vvatagttdr
      241 gcvdplagia dvcdtadawl hvdaaygcgl lvsrtrrpll dgierarsvt vdfhkaffqp
      301 vsssalvvrh asdlrlvahh hdylnpaged epnqvdvslq ttrrfdalkl wttlralgad
      361 rigemvdatl dlaaavhalv dgdpdlrlla ptdlstvlfr yqpdglddar adalvgqvrr
      421 vlfgsgralv arttldgrpc lkltllnpdt tvadvrhvle lvrqvaaall egddllrpdv
      481 aval
//
LOCUS       WP_284439719             321 aa            linear   BCT 25-DEC-2024
DEFINITION  cold-shock protein [Cellulomonas xiejunii].
ACCESSION   WP_284439719
VERSION     WP_284439719.1
KEYWORDS    RefSeq.
SOURCE      Cellulomonas xiejunii
  ORGANISM  Cellulomonas xiejunii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Cellulomonadaceae; Cellulomonas.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Cellulomonas xiejunii"
                     /db_xref="taxon:2968083"
     Protein         1..321
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33571
     Region          1..67
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
     Region          81..142
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
     Region          162..222
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
     Region          259..321
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mpqatvrwfd aergfgflnl gddaddlfvh aseivgddnr kvlregqeve yelgegdrgp
       61 qarrvritge yaadtplgvl gtvswyepgk gygfitpdsg dgeifvhssa ivgggvvreg
      121 qrvafmvvpg ekgpqaehll plgaqtapag aaaavadgad gtitfydadk gfgfatrdtg
      181 gedvfvhake lvgatalaeg dritfsvaes drgpqargvr lvggaarrgp saapgrgrte
      241 rprssagprs sgaparggqg vvarydadrg fgfitpdagg ddlfvhvsvv rggealyegd
      301 rvrfevrqsd rgpqadrvel l
//
LOCUS       WP_284439732             796 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Cellulomonas xiejunii].
ACCESSION   WP_284439732
VERSION     WP_284439732.1
KEYWORDS    RefSeq.
SOURCE      Cellulomonas xiejunii
  ORGANISM  Cellulomonas xiejunii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Cellulomonadaceae; Cellulomonas.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 796)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 796)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Cellulomonas xiejunii"
                     /db_xref="taxon:2968083"
     Protein         1..796
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=87267
     Region          58..785
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 madklgagtd avtspvpvvp apaeaqtagt gangsheset spgstsrvra rlarlsgrsv
       61 paypalepvl qavrtnhpka dlsvieqayv vaehahrgql rksgdpyith pvavatilae
      121 lgmtpstiva allhdtvedt eysleqlrsd fgpevamlvd gvtkldkvay gdaaqsetvr
      181 kmvvamsrdi rvlvikladr lhnartwkfv saasaekkar etleiyapla hrlgmntikw
      241 eledlsfatl ypkvydeivh lvaerapare eylatvrdqv gadlrtakik atvtgrpkhy
      301 ysiyqkmivr grdftdiydl vgvrvlvdtv rdcyaalgal harwnpvpgr fkdyiampkf
      361 nlyqslhttv igpggkpvei qirthdmhrr aeygvaahwk ykettksngp qdaagndmtw
      421 lrqlvdwqre tadpaefldl lrdeiagaev yvftpkgdvq alpagstpvd fayavhtevg
      481 hrtmgarvng rlvpldstle ngdvvevfts ksetagpsrd wlafvkspra rnkirqwftk
      541 erreeaiehg kdaiakamrk qnlpiqrlms healvalane mrfadvsaly aavgegqasa
      601 asvvqrlvhs lggepaqeed laeaarpgat grrvrsgdpg vvvkgvedvw vklakcctpv
      661 pgddiigfvt rgagvsvhrt dclnvdalrr qperivdvew thtssqlflv qiqvealdrs
      721 rllsdvtrvl sdhhvnilsa svstsrdrva lsrfvfemae pshltsvlsa vrkvegvfdv
      781 yrvtgsrgae epaira
//
LOCUS       WP_284439831            1549 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus
            oleatilyticus].
ACCESSION   WP_284439831
VERSION     WP_284439831.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus oleatilyticus
  ORGANISM  Paenibacillus oleatilyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 1549)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 1549)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 1549)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1549)
  AUTHORS   Ho,Y.S., Burden,L.M. and Hurley,J.H.
  TITLE     Structure of the GAF domain, a ubiquitous signaling motif and a new
            class of cyclic GMP receptor
  JOURNAL   EMBO J 19 (20), 5288-5299 (2000)
   PUBMED   11032796
  REMARK    Erratum:[EMBO J 2001 Mar 15;20(6):1483]
REFERENCE   5  (residues 1 to 1549)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 1549)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   7  (residues 1 to 1549)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   8  (residues 1 to 1549)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12385630
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1549
                     /organism="Paenibacillus oleatilyticus"
                     /db_xref="taxon:2594886"
     Protein         1..1549
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=175221
     Region          5..>865
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          1174..>1453
                     /region_name="GAF"
                     /note="GAF domain [Signal transduction mechanisms];
                     COG2203"
                     /db_xref="CDD:441805"
     Region          <1488..1549
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mnpnlefqvi divsedsrmr lyrgilvdyd plnpvlirta kceeggaaeq gllrrefeit
       61 eslqldgivk pialrtfgss lvlvladdgr islreylsrs ggfdqgtfvq lacaiasivk
      121 elhrrhivhl dlrpdhilvh pdtlnvsltg lghalhlvmd nplrpddlhf ftdrlpyisp
      181 ehtgrmarqi dersdlyalg vlfyemltgq lpykaaeple wihahlaqap lplihlsqtv
      241 dltvnaivmk lleknaenry phadalladl skigemdepf rmkdvlygre deisllsqaf
      301 hstccgstei vyvsgpagig ktslleevfl rqkthlretf yitgkfeqis kespyypiiq
      361 afrgllrhll gessdrveaw rsklrdalss neaiiaailp elklligdfa aaeelppdea
      421 kkrfiyafrk fvqalaskeh plvlfiddlq wadtsslqli hsllcdpesq ylmfvgayrd
      481 sdpepkklpg yeedgsvtee vavrhiplra ltleqmnpiv mdalhcdade alpltevlyh
      541 ksggnpfhlk qmfqrfqddr llrynhedrr whwslgqiie rqpfftvhel mehklhriss
      601 eaqellriaa ctgsefhatf iakvsgqpve tvgsvlssal degliasssp dgyrflhdnf
      661 qkmlysrmdd etrqrthlsi grwlrdlnge qsedfftavh hlnigsgvie drqetvqlme
      721 mnlvagkrak astafdialv ffrkggallg agdwdrhytl cfelcaerae ceylcgnhed
      781 terlvgqlll qtrnpierar vwmiritqci nlgqyqeatv lglqglkefr idiapapska
      841 avvsellrve lwlrrhdkrl aflpemtdkd rvaaihmifa imastfftnk dvffqllcqa
      901 irlslkygnt avsaaiysmy gmflgialrk yekgyemakv glelserynv tsikgithmi
      961 fggvlcqfvg sadegdvyle kalrfgmesg dyvyssysmg ahinslytra pldalskkin
     1021 eylavlaetk defvlqnfhl yrqfilalqg etaepcsfnd qdfeeerflk hiyseetfst
     1081 tlfqyntykt qlcyfngkfd eaalwaqqae kfaayathlp hlpeclfyea lallsdpgml
     1141 rsgnnrvkrv krivrrfktw vrwspdnfls klclmeaewa kvakryaaae amydkairea
     1201 reqgniqmes vacelaanyy akqgrakiac fywqaavegy kqwgirgkar lleerlhalr
     1261 gagkaesvls deqpffsspt aaetaphdrg irqeaqaaer mdlvailkat qaiahkmdld
     1321 avlveimstl mnyagaqkga llteshgely vrvyaddevn ifgthtpled nellpggiar
     1381 yvsrtkesvh ytgtedswll hnpyllkhrp ksvlcmpvtv hgasvgvlyl entlvagvfs
     1441 perisicham aaqslyicel lrslgqfdne pengkgsprt phpmeeplte remevlalla
     1501 tglsnkeiae qlvvavgtvk vhvkniftkl kvnrrtkaia qakelqlld
//
LOCUS       WP_284439883             159 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Paenibacillus oleatilyticus].
ACCESSION   WP_284439883
VERSION     WP_284439883.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus oleatilyticus
  ORGANISM  Paenibacillus oleatilyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 159)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Paenibacillus oleatilyticus"
                     /db_xref="taxon:2594886"
     Protein         1..159
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18153
     Region          8..148
                     /region_name="NUDIX_MutT_Nudt1"
                     /note="MutT homolog-1 and similar proteins; cd18886"
                     /db_xref="CDD:467596"
ORIGIN      
        1 mkinyvhcfi aqdqqflmlr rnnppfknmw ncvggkmmpd etpreavire vkeetgldlq
       61 svqfkgiatw nqaggmyifv adqftgdlte ctegtlawks kewimqspev vssirtildd
      121 vlatdvpvey alfytgaeye gelwkyvvfg ncehhdspr
//
LOCUS       WP_284440267              79 aa            linear   BCT 25-DEC-2024
DEFINITION  ferric iron reductase, partial [Yersinia pestis].
ACCESSION   WP_284440267
VERSION     WP_284440267.1
KEYWORDS    RefSeq.
SOURCE      Yersinia pestis
  ORGANISM  Yersinia pestis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10533483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Yersinia pestis"
                     /db_xref="taxon:632"
     Protein         <1..>79
                     /product="ferric iron reductase"
     Region          1..>78
                     /region_name="FhuF"
                     /note="Ferric iron reductase FhuF-like transporter;
                     pfam06276"
                     /db_xref="CDD:428860"
ORIGIN      
        1 afftydlvfm ppgenlmlvl esndpvhllm kdigeeiail ngdirlpdai kfiqvtfkdd
       61 lkikyilldi fycifrylt
//
LOCUS       WP_284440288             234 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Streptomyces vilmorinianum].
ACCESSION   WP_284440288
VERSION     WP_284440288.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces vilmorinianum
  ORGANISM  Streptomyces vilmorinianum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Streptomyces vilmorinianum"
                     /db_xref="taxon:3051092"
     Protein         1..234
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24421
     Region          4..169
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 msalaavlfd mdgtlvdtev lwwdateeia arlghrltht dapevvgrav edtaahlvri
       61 tgapdrdgvv talttafqer vdegaplrpg agrlladleq egvpfalvsa sprsvvdsvv
      121 ggalarvpfa ftlsaddtdr tkphpdpyra aarrlgaspe acvaiedspd gaasadaagc
      181 rvlvvpsllp vpsgqrrtfa dsledvslde lrslvtdgta alptdsrlep rvrg
//
LOCUS       WP_284441087             174 aa            linear   BCT 25-DEC-2024
DEFINITION  ESPR domain-containing protein, partial [Escherichia coli].
ACCESSION   WP_284441087
VERSION     WP_284441087.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10585893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>174
                     /product="ESPR domain-containing protein"
     Region          1..47
                     /region_name="ESPR"
                     /note="Extended Signal Peptide of Type V secretion system;
                     pfam13018"
                     /db_xref="CDD:463773"
     Region          62..>168
                     /region_name="Peptidase_S6"
                     /note="Immunoglobulin A1 protease; pfam02395"
                     /db_xref="CDD:396804"
ORIGIN      
        1 mnkiyslkys aatggliavs elakrvsgkt nrklvatmls lavagtvnaa nidisnvwar
       61 dyldlaqnkg ifqpgatdvt itlkngdkfs fhnlsipdfs gaaasgaata iggsysvtva
      121 hnkknpqaae tqvyaqssyk vvdrrnsndf eiqrlnkfvv etvgatpaet nptt
//
LOCUS       WP_284441515             216 aa            linear   BCT 25-DEC-2024
DEFINITION  adenylate kinase family protein [Chlamydia gallinacea].
ACCESSION   WP_284441515
VERSION     WP_284441515.1
KEYWORDS    RefSeq.
SOURCE      Chlamydia gallinacea
  ORGANISM  Chlamydia gallinacea
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
            Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolution and classification of P-loop kinases and related proteins
  JOURNAL   J Mol Biol 333 (4), 781-815 (2003)
   PUBMED   14568537
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Schulz,G.E.
  TITLE     Structural and functional relationships in the adenylate kinase
            family
  JOURNAL   Cold Spring Harb Symp Quant Biol 52, 429-439 (1987)
   PUBMED   2841070
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Schulz,G.E., Schiltz,E., Tomasselli,A.G., Frank,R., Brune,M.,
            Wittinghofer,A. and Schirmer,R.H.
  TITLE     Structural relationships in the adenylate kinase family
  JOURNAL   Eur J Biochem 161 (1), 127-132 (1986)
   PUBMED   3023080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Chlamydia gallinacea"
                     /db_xref="taxon:1457153"
     Protein         1..216
                     /product="adenylate kinase family protein"
                     /EC_number="2.7.4.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019205 - nucleobase-containing compound
                     kinase activity [Evidence IEA]"
                     /GO_process="GO:0006139 - nucleobase-containing compound
                     metabolic process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=24367
     Region          20..204
                     /region_name="Adk"
                     /note="Adenylate kinase or related kinase [Nucleotide
                     transport and metabolism]; COG0563"
                     /db_xref="CDD:440329"
ORIGIN      
        1 mvdksiansi klyakpfssi llfgppgagk dflgnfiahg gsqvyvslgd ifrcypiwsp
       61 irqlfhkyav sgtlipdddv iavwnyyiqg liavgkflpe rqdllisglp rtleqaklle
      121 syitvrhvii levheeatll ertqhslysk grinevgidv lqkrlesykk didaliryyp
      181 lhkvsrisad qrpmevlrdi lsrlahvfsh pgkpvd
//
LOCUS       WP_284441596             386 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Chlamydia
            gallinacea].
ACCESSION   WP_284441596
VERSION     WP_284441596.1
KEYWORDS    RefSeq.
SOURCE      Chlamydia gallinacea
  ORGANISM  Chlamydia gallinacea
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
            Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Chlamydia gallinacea"
                     /db_xref="taxon:1457153"
     Protein         1..386
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43319
     Region          4..383
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mgikniliid depllrdfls elllsrgyvp scadnvkhgc hkikteqfdl iisdmnmpdg
       61 tgldiikttk kyaphlpvlv itaygtiena vqamrygafn yltkpfssea llafiqkaeq
      121 lqdlvhenll lksqvptesh pliaespsmk eilskakkaa rssanifihg esgcgkella
      181 ffihshsprs lhpyikvnca aipetllese ffghekgaft gasakkagrf elahrgtlll
      241 deiteipvhl qakllrviqe kefehlggtk tlsvdvrils tsnrnlkeav eektfrqdlf
      301 yrlnviplyl pplrerkedi lplaqyflek fcalnnrplk tlsekaklal mdypwpgnir
      361 elsnviervv ilenpthlte smlalc
//
LOCUS       WP_284441880             389 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Chlamydia gallinacea].
ACCESSION   WP_284441880
VERSION     WP_284441880.1
KEYWORDS    RefSeq.
SOURCE      Chlamydia gallinacea
  ORGANISM  Chlamydia gallinacea
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
            Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Chlamydia gallinacea"
                     /db_xref="taxon:1457153"
     Protein         1..389
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43203
     Region          7..374
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 msinsllker lekqkhrhll rslqttshlk dftsndylgf arsselhrmc lsafsslssl
       61 gstgsrlltg hstlaheaeq hisayhnmes alifnsgyta nlglisalas hqdrvihdly
      121 ihasihdgir lskakkipfr hndmqhlekr lsepfsgntf vcvesiyslh gsiaplitlc
      181 klcknygahl ivdeahalgv vgskgegyvt slglqkdvta tvytfgkalg ihgaavagss
      241 llkeylinfc rafiyttapp lhvfkticla yqynktagpl reklyhwiay lqmqakslsk
      301 apfqnnsqtp iqplyisgsq harniakkfq tagfdvrpiv sptvkqkeel lrvclhafnt
      361 kkeiddflnl lddiqtssct llsqeftqk
//
LOCUS       WP_284442085             361 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Elizabethkingia
            anophelis].
ACCESSION   WP_284442085
VERSION     WP_284442085.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..361
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=42023
     Region          <257..359
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mdinllilll tagallllsf lmlsnalrvn rkpnfyfgic lfiwssffwd dlllgdllqn
       61 eiiyittrfi qflaplvfyq svhfysnpyy kyrikdtghl ilailflill mikpdinhkd
      121 fqtiylsmvl gnalfytgls ylkilkhrkn ieffassken idlrwilwii yatiaasitt
      181 afynifsges alniyisiff mlvvyivafy tirqkeiypk gldvedidte fseinsgikn
      241 klmddsglee fkikltilme aeklyldnel nlvklaekmn isghqlsyvi nqgfgenfff
      301 fvnkyrvkra eelltdsayk qytilaigye agfnsktsfn nafkkltsft pteyrknrsd
      361 l
//
LOCUS       WP_284442242             247 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Elizabethkingia anophelis].
ACCESSION   WP_284442242
VERSION     WP_284442242.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 247)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..247
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29538
     Region          54..247
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mkkntipean nnlqtlvetn dfikqlsidc vifgfhnksl kvlmlkyfnm diwalpggfi
       61 fkdenvddaa yrllyerthl deifleqfyt fgnknrtesd ihnrltknke idlpkdhwlf
      121 qrhisigyya lidytlsstf pdafsekcew fdvhnlpkei afdhreiiek gmeflrknld
      181 ykiygsnllp ekftmkelqn lyeyilgepl rrnnfqrkml sldflerlek kfdgsankap
      241 yyykfkk
//
LOCUS       WP_284442271             421 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Elizabethkingia anophelis].
ACCESSION   WP_284442271
VERSION     WP_284442271.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..421
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46391
     Region          7..419
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtqnkgkali igagiaglss ayyllkkgwq veileqndls nncsygnagm ivpshftpla
       61 apgvvtqgfr wmfnskspfy vkpslsskli swglqflrhs nqkhvdasas airdlnlass
      121 klynelakte dfnfelnqng ilmlyktekv aeeetelahi akelgldvdv ldwkgiqdle
      181 pninldvigg inykcdghld prklmtqmis ylknngvtfy tqhrvsgfet seskinavia
      241 ngkkftadqy imtggsflpe laqkadikiq lmpgkgysfm ytpensaykl ehaalllear
      301 vavtpmsgqi rfggtmelak hqhkinmnrv egivasipky mpdfqvtlpk eseiwygyrp
      361 capdglpylg assklknlii gggggmmgls lgpvfgrtvs eiangeklsv didifrperf
      421 n
//
LOCUS       WP_284442278              85 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Elizabethkingia anophelis].
ACCESSION   WP_284442278
VERSION     WP_284442278.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 85)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 85)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 85)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 85)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 85)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..85
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=9483
     Region          4..>64
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 msdltvvnid deypalqiik qyceqiegid llksfqnphe altyleenkv dliildinmp
       61 gingallqaa lyfsdirnpi ccksi
//
LOCUS       WP_284442421             705 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein [Chlamydia
            gallinacea].
ACCESSION   WP_284442421
VERSION     WP_284442421.1
KEYWORDS    RefSeq.
SOURCE      Chlamydia gallinacea
  ORGANISM  Chlamydia gallinacea
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
            Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
REFERENCE   1  (residues 1 to 705)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 705)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 705)
  AUTHORS   Porat,A., Cho,S.H. and Beckwith,J.
  TITLE     The unusual transmembrane electron transporter DsbD and its
            homologues: a bacterial family of disulfide reductases
  JOURNAL   Res Microbiol 155 (8), 617-622 (2004)
   PUBMED   15380548
REFERENCE   4  (residues 1 to 705)
  AUTHORS   Kimball,R.A., Martin,L. and Saier,M.H. Jr.
  TITLE     Reversing transmembrane electron flow: the DsbD and DsbB protein
            families
  JOURNAL   J Mol Microbiol Biotechnol 5 (3), 133-149 (2003)
   PUBMED   12766342
REFERENCE   5  (residues 1 to 705)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   6  (residues 1 to 705)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   7  (residues 1 to 705)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   8  (residues 1 to 705)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   9  (residues 1 to 705)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12109673
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Chlamydia gallinacea"
                     /db_xref="taxon:1457153"
     Protein         1..705
                     /product="protein-disulfide reductase DsbD family protein"
                     /EC_number="1.8.-.-"
                     /EC_number="1.8.1.8"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=77181
     Region          48..157
                     /region_name="DsbC"
                     /note="Disulphide bond corrector protein DsbC; pfam11412"
                     /db_xref="CDD:463273"
     Region          297..684
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 mnkikryfqt ilatacfllp msmrtlyaqe kgkeelgasl isadshiprg gqfrvgiria
       61 gpegshiywk npgevgsplk icwnlpegfv vneehwpapq vfeeegttyf gydstaliva
      121 disspanveg egadiqahve wlacsdscip gkadlklslp ygesnevihp ddardfartl
      181 qlrprvlaeg qqvvlekssd gkiivnipvs seaekawfis ekadrifacs eeeaikvgtq
      241 tqwklsvktr dhiqsnqele gvllltdrlg rqlesfiirg hiagdpvtps sgilgyatil
      301 vmaffgglll nimpcvlpli tlkvygliks ageqrssvir nglcftlgvv gcfwalagva
      361 vflkmlghni gwgfqlqepm fvatlmiiff lfalsslglf evgamftnlg sklqsaemgt
      421 prstaisslc ngilatlvtt pctgpflgsv lglvmsltfa sqlliftaig lgmalpylif
      481 aifpkmlsll pkpggwmsaf kqltgfmllg tvtwlawifg setsttalii llsglwlsgl
      541 gawiqgkwga pvsprrmrav astvffgcil galslsfvas ryfvemhnpa esetwqpfss
      601 aklaalrkeg hpvfvnftak wcltcqmnkh vlyahtvqei fkqhgvvtle adwtrqdpgi
      661 teelarlgra svpsyvyypp nqkepivlpe kltqtvienm ffsqr
//
LOCUS       WP_284442367             500 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Chlamydia gallinacea].
ACCESSION   WP_284442367
VERSION     WP_284442367.1
KEYWORDS    RefSeq.
SOURCE      Chlamydia gallinacea
  ORGANISM  Chlamydia gallinacea
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
            Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Chlamydia gallinacea"
                     /db_xref="taxon:1457153"
     Protein         1..500
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=56500
     Region          12..>251
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mdcqskapih yvgayaihgi lreksgsavy qgfcsethky laikvltqpi rsdnervcrf
       61 lkegqvlaql shphivklhq tgkyrdglyi aleyipgisl reyilsqgis lfqaidhils
      121 lgyaleylhs rgilhgdlkp envlitpqgk itlidlglag rpslsaanyp rcwgtpsyms
      181 peqkqgegis eqseiyslgl iayelllgnl aygrvllsli peeigkilak alqpspkdry
      241 dsvtsflndl riyrygeniy kdtrqkdfsi tayeeltqqr lwlspleiav peyisvslhe
      301 qgypvlpyvy hesfvsegvf klwfcyslsg kdtlaltlik glinqwayed narmvirkih
      361 recirlhtpv dslgiaiicv svprekqels wtscgktsfw lkkqkkvpqn ftttsmgvgk
      421 icslqiqetk vaweigdeai lrtlqadgye qslycplste lkdrkqtaif cpiesvqhgm
      481 tkkndrtlcp stlislkrir
//
LOCUS       WP_284442684             547 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Elizabethkingia
            anophelis].
ACCESSION   WP_284442684
VERSION     WP_284442684.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 547)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..547
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=64359
     Region          71..321
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          <426..537
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrkkyenlke ndekalstvs lliakakkek ineelmhaye davyysskne nkiiyadsti
       61 vtakktlnnd lisrsylgkg iiyyynlkry kyaldeylka yeyskkgndn yqknkviyhl
      121 givksylgyy ndalelfnec isyfepktig nyhpneiynn skgylnslhl aivcyihlgd
      181 fekanfltnk glgfierlgk nefsleksyl lkckgvlefq nndfnkaiqt fnqaipiles
      241 nndfawasvv dfyigksyis lhqedaavaq fkkvdsifqk hnfilpelre nyellinyyr
      301 knndpkqely ytkvllkadg iltrdftyls skihreydtq nlvdiqnkle nqnkwglgmi
      361 illciivsvl vynvwkyyqn ekkiktkykk lednlqhhie pepssvpyen issqskstms
      421 eevykdlqdk lekfekekqf lekgmtlnkl anifetnsty lsqfinetks mnfsrylgil
      481 rinyitqlmy enekylnyti qslsdecgia srqnfsdlfq einglrptef ikkrkkdied
      541 mksstne
//
LOCUS       WP_284442720             313 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Elizabethkingia
            anophelis].
ACCESSION   WP_284442720
VERSION     WP_284442720.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..313
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35214
     Region          1..290
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mitkdgkpvy kkafgksnle lntdlnpesv fqlgsitkqf taiaililee qgklkvtdpv
       61 skyvpdypfg dkitihhllt htsgikdftk mkslqdiaqk emtpkmmvdf fknepidfap
      121 gekfeynnag yvllgyiiel tsgvtyenfi qknifdktgm tnsyyasdrk viknraygyh
      181 kkgnvyvnks iisfsvpfss gslmsttadm lkwqkalnqn lllkpeniqk sfrkyklnsg
      241 qeftygygwh ikeiigqptr ehggsifgfk tmgiyfpkqd iyvlglsncd cnsptkvtsd
      301 iaalaiktlg sqk
//
LOCUS       WP_284442734             482 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Elizabethkingia
            anophelis].
ACCESSION   WP_284442734
VERSION     WP_284442734.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..482
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=55791
     Region          6..>215
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          <360..475
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtkdtdkdea yaagenilrl aitdeeraka yakmgkamyd knsyaeaiql lekgdhyaqi
       61 sgstyerffi nfylsdayaq vgfsgkaqrs wqiaskeagk lkkympagfm idqrcitnle
      121 ededyckaiq qrlkliehis kadidistqr innaanysgl aydyikcgdm mkakqallea
      181 kyiyenyyda ehllslpryy lskaiiavke gskaegkhwf dmafetavkk kltndeeliv
      241 rerllsnidt nkelqhqnid yytkfykdkv kqarraakne idkketkvvn qnkkinillv
      301 ivtvlvlsfl yvykrkvrlr skllntlsrl rqtkepvtva htekrkkvte gptvikdpnt
      361 eavllrrldk fekteqyitk gitlpkmavl lktnttylsy iikthrdsdf sqyinrnrin
      421 yivgklknhp eylnykigyl aeecgfpths qfgsvfknet gmspsqfins lkqekskers
      481 rn
//
LOCUS       WP_284442753             421 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Elizabethkingia anophelis].
ACCESSION   WP_284442753
VERSION     WP_284442753.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..421
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46361
     Region          7..419
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtqnkgkali igagiaglss ayyllkkgwq veileqndls nncsygnagm ivpshftpla
       61 apgvvtqgfr wmfnskspfy vkpslsskli swglqflrhs nqkhvdasas airdlnlass
      121 klynelakte dfnfelnqng ilmlyktekv aeeetelahi akelgldvdv ldwkgiqdle
      181 pninldvigg inykcdghld prklmtqmis ylknngvtfy tqhrvsgfet seskinavia
      241 ngkkftadqy imtggsflpe laqkagikiq lmpgkgysfm ytpensaykl ehaalllear
      301 vavtpmsgqi rfggtmelaq hhhkikmnrv egivasipky mpdfqiahpk eseiwygyrp
      361 capdglpylg assklknlii aggggmmgls lgpvfgrtvs eiangekpsv didifrperf
      421 n
//
LOCUS       WP_284442794            1946 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Elizabethkingia anophelis].
ACCESSION   WP_284442794
VERSION     WP_284442794.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 1946)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1946)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1946)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1946)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1946
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..1946
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=222250
     Region          325..1945
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mqriakifsl llvilsgisl haqnyydqqw kkindnyakg mvksnlpivl diqkqamkdn
       61 ntielinalk aefvivnqtr ddekndsasq ffdkikkhek nlkgdellvy ralqikfvdd
      121 ylkqnqwkiq drtnidnqdf gqietwskld fkkyftqgfn dlgkvkneir kismnkyqkl
      181 fantqdisyf psvqdwvalq hidflkdnvl ftpnelkann akileiyndq iatnsvnpkl
      241 fyeylkaqye vsfgqlpeae arkkyeaivn sstdgdykvy ilndiaggla sanpkeamai
      301 lkkakemypk sefqnniknt ensittpvit vsyesftlpq qpihlsvnyk nadafamniy
      361 qvtdinsfis hikdsyrnpl lkvakqlvkk enyqlkntgd yknhissvel salknglyia
      421 eyivegksqg sywfsvtdsr iiynkilsng snnvlrlisr nngeskkntn lnfydyseyn
      481 kpvvkssakt dpqgifvfpe nktrnykryl iedseknisf ieayggnyyd qprvdatekt
      541 aqifldraiy rpgqtvyfkv intqysnkke tvvvgmkqki klvdvngedi seqsfttnef
      601 gsysgnfilp kgklngqfml etdegsvsfr veeykrpnfe itfedikgey kfgqtihmkg
      661 kavsfsgvpl snatlnyeik kqdiryryfy wftptsnens ilgtvktnek gefdipvdlr
      721 kdeklkgiqv neyvvnasvt dtngetqens stfrvasvsh fieteevkpa faneeikvkv
      781 atknynnqkl gksyqaklsl lespdrifrn nfedfvqdvp vfskenfiqk fphdyfdkse
      841 lannrkekqt vlqktaadee fslgklaagt yklvfynieg qdtiktenvf evwdrkslgn
      901 gqkpffrlmn nqkdyargek akvylysaip eakvyvyvqn gngetkteek yikngvleye
      961 ieipadpavk qlnlqftlaa yndiqtlstn lpvrneaepm kielttfrdk iqpgskekwt
     1021 vkitgknkek avaellanmy dmsldqfaan nytfrnfnfe rfiqqnygvg teslnsvrfn
     1081 krekylnakt vfapyfnwfd qygalgglat nvrirggstl rkanvayeat mdmalpapva
     1141 aakvadsssk kaieevvvvg ygkvkkkedl dkvpvrsnln etaffypnlk tdkdgnvsfe
     1201 ftspealtkw klmflahdkn anaatleqti vtqkdfsvtp nyprflregd einmqvklnn
     1261 lvekalngsv qlqilnadtn edisskfgln nliqnfdina tssksvswtf kvpnnvsgii
     1321 iktvakagqy sdgeqkavpv lpnrmlvtda lpifvkegqt ktfvldqlks nnsttianvs
     1381 ntlelttnpi wevlfalpsl kndinnsadv vfnkwfadvl asevfkanpr mkkifeeyqe
     1441 kgllesnlek nqelkqllle etpwvfeakd ekqqmqmlar lfdannmrns ilddwstlkq
     1501 lqngdggfsw yagspssfst slyilknlgk inewlkdkgg vndyqntpqn emvsaltayl
     1561 dreinrywkq kgmnpwnnlv ldyldtrhyw eaqyplkntg ailksqviak aktakitdft
     1621 fyglsraall fnnyglkdvs dklmtylket stdtktqgvy wkqnldawgw yaskainhal
     1681 amqafnklkp ndaiiedmki wlitqkevnh wetsrataev iytimnsgks wttpeadkat
     1741 viwggkeltk tdvqatgyik savkspeldk klaevtvtkp gpgivqgglf wqyyedldkv
     1801 kssetyisvt kelykkvkte ngeelkkita dtplrvgdkv tvrmilntdr pmeyihikdm
     1861 raagfeptev lsgyqwknnl gyyqstkdas tnfyieqmpk gkyvfeydvv aniagkfsng
     1921 ittmqnyyap qmnahtqgtn vtvvph
//
LOCUS       WP_284442855             270 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Elizabethkingia anophelis].
ACCESSION   WP_284442855
VERSION     WP_284442855.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..270
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30814
     Region          19..268
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mktlfnlill lvfshplfaq kvirekifsa kmkkeistii vapdikphqq yktvyilhgy
       61 sgnpertlkq dipdlqakak ayntiyilpd gnynswyvds pvdqksqykt figselvryi
      121 dehyptkaek tsrgilgwsm ggfgslyigt sfpeafgivg sscgaldfrt fnegynnyqv
      181 dkvlgplssl gseyilsdnt dkmlntgqyy ildcgindff isknqsfhqd lltkkvehly
      241 ieslgehnte ywsralsnql slfenyfnhr
//
LOCUS       WP_284443431             500 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Chlamydia gallinacea].
ACCESSION   WP_284443431
VERSION     WP_284443431.1
KEYWORDS    RefSeq.
SOURCE      Chlamydia gallinacea
  ORGANISM  Chlamydia gallinacea
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
            Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Chlamydia gallinacea"
                     /db_xref="taxon:1457153"
     Protein         1..500
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=56534
     Region          12..>251
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mdcqskapih yvgayaihgi lreksgsavy qgfcsethky laikvltqpi rsdnervcrf
       61 lkegqvlaql shphivklhq tgkyrdglyi aleyipgisl reyilsqgis lfqaidhils
      121 lgyaleylhs rgilhgdlkp envlitpqgk itlidlglag rpslsaanyp rywgtpsyms
      181 peqkqgegis eqseiyslgl iayelllgnl ahgrvllsli peeigkilak alqpspkdry
      241 dsvtsflndl riyrygeniy kdtrqkdfsi tayeeltqqr lwlspleiav peyisvslhe
      301 qgypvlpyvy hesfvsegvf klwfcyslsg kdtlaltlik glinqwayed narmvirkih
      361 recirlhtpv dslgiaiicv svprekqels wtscgktsfw lkkqkkvpqn ftttsmgvgk
      421 icslqiqetk vaweigdeai lrtlqadgye qslycplste lkdrkqtaif cpiesvqhgm
      481 tkkndrtlcp stlislkrir
//
LOCUS       WP_284444038            1113 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein, partial [Campylobacter lari].
ACCESSION   WP_284444038
VERSION     WP_284444038.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter lari
  ORGANISM  Campylobacter lari
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 1113)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1113)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1113)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1113)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1113
                     /organism="Campylobacter lari"
                     /db_xref="taxon:201"
     Protein         <1..1113
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
     Region          <1..1113
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 vpnrikvsmq apksikenek ldfnisskyl fgtpasnlqy qadlfvskke yknskypeyi
       61 fsnpsvlvqk yqdnlkgmld engftkqeft lndflkntpy nleasirarv fekgsrsvea
      121 lvnsqvilhe yfvgikrlkn hylssgsivn feaivsdlde nlianreiky tiyandysww
      181 wdydnyddfl kslkkdkntq ivtqgtilsk dkpvkiefdp keyhgemfie ledvqsktst
      241 geffyissfg apsnadivss lkiksdkkey kpnetafief esvkgakaii tlndnvkvlk
      301 rfvidthedi tkveipilke ympnvyvsvi llqdydqytn dralrlfgvv plnvvdeqsk
      361 ieldlkvpdk impkqdfeve iqsknkqsyt ytiaivdegl ldvnafktpd iwgyfyqktr
      421 fnmsiydtyd kiiaknisnv skvlttggdv flesranksk ndekarrfkp vvlfqepvqs
      481 dengyaklkf nmpsylgsvr vmvvannlag fgsaskdiqv sapavmletl pralrlddef
      541 kflvqvfkvd ddvknaklkl ktknslinfe ndeilidfsn ekskdiyvna kvnsnklgve
      601 eielslnakd ytytqntqid ikalntitye gksfkipant smefkitqdy inpvaflsvs
      661 skpilninhr lkylqnypyg cieqstsavl pqlflqkldq gankqkninn inallskyan
      721 fqtanggfay wqglkdsdaw gsnyagmfmi lakergyyvg egmfkawldy qkryvlkaqt
      781 nkeirinsly llalakepnl simnaiyeds aylqslnnvs lwqlsaaykl agfdevalni
      841 aknlsikpdg kanythtygs flrdeaiian aykivygkdn dellddikkt leshawlstq
      901 stgyalyala nsfsdesskt inaslkinge skklnasfsk fefnqgsali eakedtyvhf
      961 gvegikkgia epfaqrmyie rsfydengne idesaikssq ifymklkisn knypgasnia
     1021 ltqilpsgwe ivydllddea pdfvknsyyd fvdirddkim yffplysdes reffvklsav
     1081 tpgvytlsga yaeamydnay kalseskrvk vvq
//
LOCUS       WP_284444133             246 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Streptococcus
            parasanguinis].
ACCESSION   WP_284444133
VERSION     WP_284444133.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus parasanguinis
  ORGANISM  Streptococcus parasanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Streptococcus parasanguinis"
                     /db_xref="taxon:1318"
     Protein         1..246
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28246
     Region          2..143
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 matyetfaav ydavmddsly dlwtdfslrh lpktkdkkkl lelacgtgiq svrfsqagfd
       61 vtgldlsadm lkiaekraas skqkidfieg nmldlsqagt ydfvtcysds icymqdevev
      121 gdvfrevyna lnedgvfifd vhstyqtdev fpgysyhena edfamlwdty edaaphsivh
      181 eltffvqeed gsfsrhdevh eertyevlty dilleqagfk sfklyadfed keptktskrw
      241 ffvaqk
//
LOCUS       WP_284444403              55 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family transcriptional regulator, partial [Escherichia coli].
ACCESSION   WP_284444403
VERSION     WP_284444403.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 55)
  AUTHORS   Nazaret,F., Alloing,G., Mandon,K. and Frendo,P.
  TITLE     MarR Family Transcriptional Regulators and Their Roles in
            Plant-Interacting Bacteria
  JOURNAL   Microorganisms 11 (8), 1936 (2023)
   PUBMED   37630496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 55)
  AUTHORS   Will,W.R. and Fang,F.C.
  TITLE     The evolution of MarR family transcription factors as
            counter-silencers in regulatory networks
  JOURNAL   Curr Opin Microbiol 55, 1-8 (2020)
   PUBMED   32044654
REFERENCE   3  (residues 1 to 55)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   4  (residues 1 to 55)
  AUTHORS   Grove,A.
  TITLE     Regulation of Metabolic Pathways by MarR Family Transcription
            Factors
  JOURNAL   Comput Struct Biotechnol J 15, 366-371 (2017)
   PUBMED   28694934
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 55)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (residues 1 to 55)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   7  (residues 1 to 55)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   8  (residues 1 to 55)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10581578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..55
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>55
                     /product="MarR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          12..>47
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
ORIGIN      
        1 mimsllndvq kfieahpgct sgdiadafag ysrqrvlqsv sklrqsgrva hrceg
//
LOCUS       WP_284446256             168 aa            linear   BCT 25-DEC-2024
DEFINITION  deoxycytidylate deaminase [Paenibacillus hunanensis].
ACCESSION   WP_284446256
VERSION     WP_284446256.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus hunanensis
  ORGANISM  Paenibacillus hunanensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Maley,F. and Maley,G.F.
  TITLE     A tale of two enzymes, deoxycytidylate deaminase and thymidylate
            synthase
  JOURNAL   Prog Nucleic Acid Res Mol Biol 39, 49-80 (1990)
   PUBMED   2247612
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788416
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Paenibacillus hunanensis"
                     /db_xref="taxon:539262"
     Protein         1..168
                     /product="deoxycytidylate deaminase"
                     /EC_number="3.5.4.12"
                     /GO_function="GO:0004132 - dCMP deaminase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006220 - pyrimidine nucleotide metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0009972 - cytidine deamination [Evidence
                     IEA]"
                     /calculated_mol_wt=18913
     Region          1..159
                     /region_name="ComEB"
                     /note="Deoxycytidylate deaminase [Nucleotide transport and
                     metabolism]; COG2131"
                     /db_xref="CDD:441734"
ORIGIN      
        1 mrkdwdtyfm diahmvstrs rcprrhvgav lvqgkkllgt ayngapmgvp dcseagcmis
       61 eaveivrvdg vetmvkkqrc irtihaeqnl llftdradre gstvyvtdep cwtcanmlan
      121 sgvveivyhr sylkdtdkvh emmgqkgiif rqlqayeppr ktvayeip
//
LOCUS       WP_284446392             128 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Paenibacillus
            hunanensis].
ACCESSION   WP_284446392
VERSION     WP_284446392.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus hunanensis
  ORGANISM  Paenibacillus hunanensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Paenibacillus hunanensis"
                     /db_xref="taxon:539262"
     Protein         1..128
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14850
     Region          21..117
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msdyneqqpn neppekryrv gveaalevmg gkwkpliiyh lmdgakrtse lrrlipditq
       61 kmlttqlral ekddiivrnv yteipprvdy eltpygrslk paldllcywg eehlnkvygd
      121 kskvleef
//
LOCUS       WP_284445241             570 aa            linear   BCT 25-DEC-2024
DEFINITION  type IV pilus twitching motility protein PilT [Curtobacterium
            citreum].
ACCESSION   WP_284445241
VERSION     WP_284445241.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Mattick,J.S.
  TITLE     Type IV pili and twitching motility
  JOURNAL   Annu Rev Microbiol 56, 289-314 (2002)
   PUBMED   12142488
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006640
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..570
                     /product="type IV pilus twitching motility protein PilT"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0043107 - type IV pilus-dependent motility
                     [Evidence IEA]"
                     /calculated_mol_wt=59149
     Region          <58..236
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          190..530
                     /region_name="PilT"
                     /note="Type IV pilus assembly protein PilT, pilus
                     retraction ATPase [Cell motility, Extracellular
                     structures]; COG2805"
                     /db_xref="CDD:442056"
ORIGIN      
        1 mnesvydiea gddpvagwhp gtpgnevggr raarlaaaaa aaaasassap sgtsaddrps
       61 vptssnavyd lsaepdwgap tawspappat agsvpastgv aagagswppp agdpvavpva
      121 qpqaapatpp aavppstaay gyagsvtehl pvvpavatts lqavpatsgh aadpashpei
      181 gftrhareva dadlitalsq vvyqgasdlh vtadapptvr vdgslrpavp ggpwarnkvi
      241 aalktlltpe qagqfdheqe ldfayslspe frfrvnyyqq rgnwgaafri iptkiktlkq
      301 lgipqhvgef aklprglvlv tgptgsgkst tlaalidlvn etradhivtv edpiefmhdh
      361 kkaiinqrev gadthsfaaa lkhvlrqdpd viligelrdl etisvaltaa etghlvfatl
      421 htqsapgtid rvidvfpphq qgqirtqlaa tlegvvcqtl vpkangsgrv vateimkttp
      481 aianlvregk tyqitsamqa grdagmhtmd qdlaelvnvg tvtraaamek vhdedgfdrl
      541 vqrvespsds saaaiaasei dfgdkysggh
//
LOCUS       WP_284446599             120 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Fluviibacter
            phosphoraccumulans].
ACCESSION   WP_284446599
VERSION     WP_284446599.1
KEYWORDS    RefSeq.
SOURCE      Fluviibacter phosphoraccumulans
  ORGANISM  Fluviibacter phosphoraccumulans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Fluviibacteraceae; Fluviibacter.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 120)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 120)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Fluviibacter phosphoraccumulans"
                     /db_xref="taxon:1751046"
     Protein         1..120
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12971
     Region          14..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 metlsaadll aalghesrls iyrllvkagp eginassiae qlalpaatts fhlshlsrvg
       61 lirgrqesrf ifyatdysvm dellafltdk ccqgqsclpk teqvnttekr rkkavsaiss
//
LOCUS       WP_284446669             140 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Fluviibacter phosphoraccumulans].
ACCESSION   WP_284446669
VERSION     WP_284446669.1
KEYWORDS    RefSeq.
SOURCE      Fluviibacter phosphoraccumulans
  ORGANISM  Fluviibacter phosphoraccumulans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Fluviibacteraceae; Fluviibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Fluviibacter phosphoraccumulans"
                     /db_xref="taxon:1751046"
     Protein         1..140
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=14609
     Region          1..140
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mnfrrgsgrd epeinlipfi dvllviiifl mmtttynkvs gieidlptas ssnatppeei
       61 avsvtasgtv vidgqsmtrp tvdavatalk aalakrgtak ppvvsinada kathqsvidv
      121 mqaahqadls qisfttrsgs
//
LOCUS       WP_284446767             153 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Fluviibacter phosphoraccumulans].
ACCESSION   WP_284446767
VERSION     WP_284446767.1
KEYWORDS    RefSeq.
SOURCE      Fluviibacter phosphoraccumulans
  ORGANISM  Fluviibacter phosphoraccumulans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Fluviibacteraceae; Fluviibacter.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Fluviibacter phosphoraccumulans"
                     /db_xref="taxon:1751046"
     Protein         1..153
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16350
     Region          <1..138
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mtaryfeiid rlygdvspth garqllstaq sqncrvavvt snssertsaw lsrvgltgfv
       61 dfivsgeqvk ygkpdpepyl lasqivdcpv driiaiedsv qgatsaigag lytylltpac
      121 kapfahegav pvlslehiad dlwggkrspq psq
//
LOCUS       WP_284446783             580 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Fluviibacter phosphoraccumulans].
ACCESSION   WP_284446783
VERSION     WP_284446783.1
KEYWORDS    RefSeq.
SOURCE      Fluviibacter phosphoraccumulans
  ORGANISM  Fluviibacter phosphoraccumulans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Fluviibacteraceae; Fluviibacter.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Fluviibacter phosphoraccumulans"
                     /db_xref="taxon:1751046"
     Protein         1..580
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65814
     Region          24..382
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mkrkhtagag rqpglnlepr aqpaslfmal wgvavlclav vtyffgldsl qipkngdefp
       61 yahiarltae sghwlplqst ldhmrntkpp llfwqgilst hwgqdwtlwq lrypnvlytl
      121 atallvgllg wkisgrhilt gliaavvwla ffstyrfgrp fltnagevfw lflpffllly
      181 ggkhsfespw kiplgigvav gigllyksfa lllpvglgla fwylryrryh paeflkrdiy
      241 kliliallsl gifalwfafd pdpqavwnef vigenagkfd phgpsylskm fwgngsiwtl
      301 mpgyglnagl lalivfgtmg laiwrlfrqk dlsndekylw wwvlilfvvf cfpsqrssry
      361 lleampalai lialvwfrln rwllfattli ctititaigy lgwllqqdvg htlysgteav
      421 llaivlcglv lslliprllp wltlpavfaa ylaltgflsv fdgpmgryke svqwrvagqt
      481 vwvpynfnaa yeqyrfllpg adirgyrsdt nspqtllrqn ypllivqqpl dapictdcki
      541 lgerlelkgr qsdeeikaml rgdvakhlfl rellldnrkn
//
LOCUS       WP_284446787             199 aa            linear   BCT 25-DEC-2024
DEFINITION  YcbK family protein [Fluviibacter phosphoraccumulans].
ACCESSION   WP_284446787
VERSION     WP_284446787.1
KEYWORDS    RefSeq.
SOURCE      Fluviibacter phosphoraccumulans
  ORGANISM  Fluviibacter phosphoraccumulans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Fluviibacteraceae; Fluviibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Fluviibacter phosphoraccumulans"
                     /db_xref="taxon:1751046"
     Protein         1..199
                     /product="YcbK family protein"
                     /calculated_mol_wt=21811
     Region          78..199
                     /region_name="YcbK"
                     /note="Uncharacterized conserved protein YcbK, DUF882
                     family [Function unknown]; COG3108"
                     /db_xref="CDD:442342"
ORIGIN      
        1 mkiprhdrrq flhrafklta ggvalpfaga akaafpraqs avpelisgpq rvlafnhtht
       61 reridltyai ndqyvpdalr tlnrflrdhy sgtvgqmdpq lfdllhqvrl alggsalpaf
      121 evisgyrcpe tnshlrnsrg ggvakrslhm egkaidvrlp gvplaelrda aialgvggvg
      181 yypseqfvhi dtgrvrrwg
//
LOCUS       WP_284446858             373 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Fluviibacter
            phosphoraccumulans].
ACCESSION   WP_284446858
VERSION     WP_284446858.1
KEYWORDS    RefSeq.
SOURCE      Fluviibacter phosphoraccumulans
  ORGANISM  Fluviibacter phosphoraccumulans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Fluviibacteraceae; Fluviibacter.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Fluviibacter phosphoraccumulans"
                     /db_xref="taxon:1751046"
     Protein         1..373
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=39594
     Region          35..371
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mttliglrrt nlpfargevk fheyrrnqmr ldqflgielp iiqapmagvq nsaltiavsn
       61 agglgslpca mlsadelrye lqtiksksdr pfnvnffche spvpdertat awralfndyy
      121 aelgiqptak psgaarmpin meiaelvcey apavvsfhfg lpsqeimdti hscgakilss
      181 attveeaiwl eahgadavia qgleagghrg mflseeistq vgtfalvpqi vqavklpvia
      241 sggiadargv raamdlgasg vqvgtaymlc peantsavhr talksdsarv taltnifsgr
      301 pargivnrlm relgpinsdt prfplaaaas aplrakaesm gsgdfsplwa gqnvsgckei
      361 sagvltkala erl
//
LOCUS       WP_284447012             283 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein [Fluviibacter
            phosphoraccumulans].
ACCESSION   WP_284447012
VERSION     WP_284447012.1
KEYWORDS    RefSeq.
SOURCE      Fluviibacter phosphoraccumulans
  ORGANISM  Fluviibacter phosphoraccumulans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Fluviibacteraceae; Fluviibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Fluviibacter phosphoraccumulans"
                     /db_xref="taxon:1751046"
     Protein         1..283
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29937
     Region          225..281
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mskkikttat pasivapaas ldwgsglpwg nslpfgfaae ramqppilmn agqeitgndl
       61 lalaeqhvde syvlgarapm sdadwkgpwd caefvswcvy qragilfgte prhdplhada
      121 ytgywaqqak tagatvpvad alvtagaill ryplpgaigh iafsdgeggt ieahssktgv
      181 irgkaggrrw dvgvmipgir yyrgdeditp tppagvirlt qpltrssrvt qiqerlrels
      241 yavgpadgiy gpqtahaaar fqadhglvad gevgpatwka lkl
//
LOCUS       WP_284446863             412 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Fluviibacter
            phosphoraccumulans].
ACCESSION   WP_284446863
VERSION     WP_284446863.1
KEYWORDS    RefSeq.
SOURCE      Fluviibacter phosphoraccumulans
  ORGANISM  Fluviibacter phosphoraccumulans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Fluviibacteraceae; Fluviibacter.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Fluviibacter phosphoraccumulans"
                     /db_xref="taxon:1751046"
     Protein         1..412
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=43744
     Region          36..401
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mvdakatlhd qhshilpslq plleqgaltp lkiggrtllp ivqggmgvgv sahslagtva
       61 scggigtias vdlrhlhtdl aeqtrrvrge egkalieaan qealrreirv akelaqgrgm
      121 iavnvmkals ayqdyvttal qegvdalvvg aglpldlpdl aadypnvali pilsdargvk
      181 iimkkwarak rlpgaivieh pgyagghlga asvgdlhdar fdfetvipet ravlrefgve
      241 atvpiiaagg irsyddirrm qslgaaaaql gtafavtaeg daspafkeil agareedmve
      301 fvsvaglpar avktpwlthy mekveklqar akekaqciky fdclahcglr dgngkvgqfc
      361 idhqltlayk gegnkglffr gvgdlpfgnq irsvkdlmst llmanvtlsp qt
//
LOCUS       WP_284447124             563 aa            linear   BCT 25-DEC-2024
DEFINITION  M17 family metallopeptidase [Fluviibacter phosphoraccumulans].
ACCESSION   WP_284447124
VERSION     WP_284447124.1
KEYWORDS    RefSeq.
SOURCE      Fluviibacter phosphoraccumulans
  ORGANISM  Fluviibacter phosphoraccumulans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Fluviibacteraceae; Fluviibacter.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Lowther,W.T. and Matthews,B.W.
  TITLE     Metalloaminopeptidases: common functional themes in disparate
            structural surroundings
  JOURNAL   Chem Rev 102 (12), 4581-4608 (2002)
   PUBMED   12475202
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
REFERENCE   3  (residues 1 to 563)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087321
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Fluviibacter phosphoraccumulans"
                     /db_xref="taxon:1751046"
     Protein         1..563
                     /product="M17 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=58906
     Region          <217..548
                     /region_name="Peptidase_M17"
                     /note="Cytosol aminopeptidase family, N-terminal and
                     catalytic domains. Family M17 contains zinc- and
                     manganese-dependent exopeptidases (EC 3.4.11.1), including
                     leucine aminopeptidase. They catalyze removal of amino
                     acids from the N-terminus of a protein and...; cd00433"
                     /db_xref="CDD:238247"
     Site            order(232,234..236,280,283,325,331,336,339,342..343,375,
                     377..380,382,384..388,394,396,400,436..440,443,469..470,
                     472,477,479..480,485,487,497..498,500,534)
                     /site_type="other"
                     /note="interface (dimer of trimers) [polypeptide binding]"
                     /db_xref="CDD:238247"
     Site            order(321,326,333,344,403,405,407,431)
                     /site_type="active"
                     /note="Substrate-binding/catalytic site [active]"
                     /db_xref="CDD:238247"
     Site            order(321,326,344,403,405)
                     /site_type="other"
                     /note="Zn-binding sites [ion binding]"
                     /db_xref="CDD:238247"
ORIGIN      
        1 mpvtsprara prssadvlpp dwqpvlprvf lesgklkdsv lnelthvlvl fpasllaggq
       61 lpqglpgavl lkqilgrqrk kptallrvga gsgkmpqeal vpeattlggg lirwlavdpd
      121 astflrhqql rqalsgllae qparldivfh gsagfvasam pdaayvaavn rvsmpktvaa
      181 dkttkaagta ksgktgeirl wvgardqafl stslagvmat aeantltral cvlppnqltp
      241 gsfralipgq ikglgircdt ydvaqlkkmk agaflavaqg speqdaaivr ltyvpkvkpv
      301 krdpkdksat qalpyvalvg kgicfdtggh nlkparymag mhedmagaai alsviqaaar
      361 lqlpvrvdaw lalsrndigp gayrqgdvvt alngstieiv htdaegrmvl adtltlaaaa
      421 kpdmvldfat ltgsmttalg nrmsgffasq rhlgarleev gaaagerlmp fvmpddydsa
      481 lesqvadikq ctldgeadhi laarflncfv gdaawlhldl saatckgglg aigtdttgfg
      541 aaltvqllqs iavkglprss paf
//
LOCUS       WP_284447212             275 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Fluviibacter
            phosphoraccumulans].
ACCESSION   WP_284447212
VERSION     WP_284447212.1
KEYWORDS    RefSeq.
SOURCE      Fluviibacter phosphoraccumulans
  ORGANISM  Fluviibacter phosphoraccumulans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Fluviibacteraceae; Fluviibacter.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Fluviibacter phosphoraccumulans"
                     /db_xref="taxon:1751046"
     Protein         1..275
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=31379
     Region          18..250
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 mlygqpivdm pqdlyippda lsvmldafeg pldlllylir kanvdildip matltkqyle
       61 yveamrsenl elaaeylvma amlieiksrm llprpkadfe eetedprael vrrlieyeqm
      121 klaareidal pkaeidfqwl nvwvdkeavv rhpdvsaedl haawlsvvrq aklhthhkia
      181 reelsvrehm glilrtlrhk egytefaelf dptggvpvvv vnfiallelc kehllemtqt
      241 aafapiyvrl ptdvpeqsmf evpeafdgte egedv
//
LOCUS       WP_284447469             599 aa            linear   BCT 25-DEC-2024
DEFINITION  ABCB family ABC transporter ATP-binding protein/permease
            [Fluviibacter phosphoraccumulans].
ACCESSION   WP_284447469
VERSION     WP_284447469.1
KEYWORDS    RefSeq.
SOURCE      Fluviibacter phosphoraccumulans
  ORGANISM  Fluviibacter phosphoraccumulans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Fluviibacteraceae; Fluviibacter.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 599)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Fluviibacter phosphoraccumulans"
                     /db_xref="taxon:1751046"
     Protein         1..599
                     /product="ABCB family ABC transporter ATP-binding
                     protein/permease"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66398
     Region          1..599
                     /region_name="ATM1"
                     /note="ABC-type transport system involved in Fe-S cluster
                     assembly, permease and ATPase components
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5265"
                     /db_xref="CDD:444078"
ORIGIN      
        1 msrhrnkpvg pagneplhvw ttlksllpwl wayrgrmiaa fgclllakla svyvpivfkn
       61 middlgggqd allvlpvgll llygfarlas tgftelreil fvrvtqqavr rialsvfthl
      121 hnlslrfhle rqtggvsrdi drgtraisnl isytlysilp tiielvlvmg vlaykydqvf
      181 vwitlasivc yvgftvvisn wrihirravn eadsaantra idslinyetv kyfnneafel
      241 drydeamrrw edasvrsqmt ltmlnmgqql iiviglvtmm whaaqgvvag tmtvgdlvlv
      301 nafliqlymp lnffgvvyre irqaltdier mfgllntqre ivdapdaqal ptapisvvfd
      361 rvdfaydpar pilnhvsfei pagktvaavg hsgagkstla rliyrfydvt ggqilmngld
      421 ikkidqsslr ggiaivpqdt vlfndtlyyn ilygnplatr eqviaaakaa hlhefvetlp
      481 dgydakvger glklsggekq rvaiarallk nppilvfdea tsaldsktek aiqismevaa
      541 rgrttliiah rlstvmnade ilvldagrii ergrhaalla angvyaqmwa lqqqdrdad
//
LOCUS       WP_284447677              86 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Fluviibacter
            phosphoraccumulans].
ACCESSION   WP_284447677
VERSION     WP_284447677.1
KEYWORDS    RefSeq.
SOURCE      Fluviibacter phosphoraccumulans
  ORGANISM  Fluviibacter phosphoraccumulans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Fluviibacteraceae; Fluviibacter.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 86)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Fluviibacter phosphoraccumulans"
                     /db_xref="taxon:1751046"
     Protein         1..86
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9822
     Region          1..50
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
ORIGIN      
        1 mqpehirtlr lnrnesqtef wqrfgvnqrt asriergqpl ppsvaillrl yldgvvgead
       61 leraqrryri alhhqpaiae vrasap
//
LOCUS       WP_284447869             593 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF885 domain-containing protein [Pseudoxanthomonas mexicana].
ACCESSION   WP_284447869
VERSION     WP_284447869.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..593
                     /product="DUF885 domain-containing protein"
                     /calculated_mol_wt=64555
     Region          1..590
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
ORIGIN      
        1 mrrrellvga malgltwpla armagsnpas dtagdapaed irlagllqrh aealkaeegg
       61 pdrladysla arvrrrqatl qrlaelggie raalsatatl dydtarfvye amadqygryg
      121 fsdlnlrpsp yvvsqmngay fwlpdgiggr spmkdaadad ryvdklgqfa valdqeteqi
      181 rhdaglgvip pdfilaktlr qiatlrdaap tgnaltasal arardagiad ldrrasaifv
      241 grivpalqrq saalaallpr sddragiwar pdgeayyasa lhsnttasya pgelhqlgla
      301 wveelsaeid qllraqglar gsvgermaal drdprflqsd teagrqaiid yasahldrik
      361 gllprgfrvi pdrpvevqri spaiqdgapg afysassdpa qtstiflnlr svaenalwri
      421 ptllhhegip ghhfqdsvls eagglslfrr tvrfsawteg walyaeqlad emgafesdpf
      481 grigylqgql fracrvvvdt glhharwtrq qaidwmvana gehrdaaere idrycvypgq
      541 acsfmvgkqq ivasrekarq rlgarfdtra yndfilasgp lpmqvldgav ala
//
LOCUS       WP_284447870             597 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF885 domain-containing protein [Pseudoxanthomonas mexicana].
ACCESSION   WP_284447870
VERSION     WP_284447870.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..597
                     /product="DUF885 domain-containing protein"
                     /calculated_mol_wt=66957
     Region          1..590
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
ORIGIN      
        1 mrellkaava mlvlvaaspa amawtppdar erfgllvaes qkaddalhpl rlaerglpps
       61 gavfvdpqse afarqlatnk raelsglagi draslgekdq iaydafryqa eqalgdidsg
      121 ihairnlvpl nasfglhvef pdylsgvrfk tvedyergla qlegfagymd stvdrleqgm
      181 argyhqprvv vnnvlgqvea fltlpveenp fyspvtrfpd tigaadrarl aaayrriier
      241 rttpayerwr tflrdrylpv ategaglwam kdggrvyasl lvqhttttms aqqihqigls
      301 evariraame qarqatgfdg dlpaffehvr tgpefyyskp edlighferi ekkvwermpe
      361 lfsrrpraaf elrplpalgd qrgtgyyrag ppdasepgvl ffnmamlntr piptletlql
      421 hegvpghhyq islvqedesl pdllrfgqvp ataytegwgl yaeslgqelg mfsdpyqwfg
      481 hldmemlrsm rlvvdtglha lqwdrqraid ymlantsmap rdvaveidry itnpgqacay
      541 kvgelkfqel rrraterlgp dfdirrfhdq vldtgalpld vleakidrwl msgeaaq
//
LOCUS       WP_284447909             363 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Pseudoxanthomonas mexicana].
ACCESSION   WP_284447909
VERSION     WP_284447909.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..363
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38524
     Region          9..347
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 meiatdnari slrndysega hprllqalav asaevnrgyg ldvhsaraaa lirdrlggda
       61 dvhflaggtq tnlvalaafl rpheaviapa sghiathetg aieasghkvl tvatpdgkls
      121 palirpcidg hhgehmvkpr lvyisnstew gtvysaeelq alggfcrdhg lllyvdgarl
      181 asalttegnd vdlallagqa dafyiggtkn gallgealvi vnpvlrtdfr hiikqrgaml
      241 akgmvvgaqf ealfedglyf vlathanama arlrdilqra gvplavdsps nqvfpvlpda
      301 mverlrsfve fetwerrgdg ttvirlmtsw atpesdieaf aatfsalyte gravgaaqqa
      361 qga
//
LOCUS       WP_284447936             395 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Pseudoxanthomonas
            mexicana].
ACCESSION   WP_284447936
VERSION     WP_284447936.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..395
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42711
     Region          13..385
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mdnpspfrsr lrtgpagplt gvkvldlsay iagpygctll adqgadvikv eppdgdnlrq
       61 ypstleresr aflgvnrskq gialdlkqaa dhaallrlvr eadvlvhnfr psvpkrlgid
      121 fdrlslinpr liycavtgyg etgpmkdkag ydqvlqamtg mctlqgkrgg apeiiygsvv
      181 dyyaaallaa gvssalyere rsgrgqfvgi sllrsaltmq sarmiwaege aldigrdmrs
      241 ggvtgihpar egylylsant prfwkalcrl tgldaladdp rydsvrkrae raaeivpqlh
      301 aalqartame wethfgdevp caaarrvedm fehpqvlaed mvaeiahpvv gsyrgvtrpi
      361 afgrtpgpvp faaptfdqda ehvlgtpspq vlnag
//
LOCUS       WP_284447940             404 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Pseudoxanthomonas
            mexicana].
ACCESSION   WP_284447940
VERSION     WP_284447940.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..404
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42782
     Region          20..402
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mlslaacata aptpkalpha pmdavlvdav gpegylgava vvaergtvvy rgvfghadlq
       61 grqplredai frlysmskpv tsvaalmlae egrlqldapv atylpafagl qrvaggsvea
      121 pelvpvprvl tvrhllthta gfatggddir vasallqaea pedatdlagy aqrvarapla
      181 tepgtrfryd gvntevlarv vevasgqpfd vflrtrifrp lgmhdtgfev plaqrgrvma
      241 lttrdaegrr vladtpsace pgirlrayts gagglystaa dylrfarmla eggkregvrl
      301 lredtvammm sdqlgrfdpp vpapepgegf glggyvvtdp avatrpgsrg qfgwsgaast
      361 yftidrergl villmsqhlp tesapappkl aapfyravys avtr
//
LOCUS       WP_284448143             259 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Pseudoxanthomonas mexicana].
ACCESSION   WP_284448143
VERSION     WP_284448143.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 259)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..259
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28942
     Region          2..252
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mklsalvvdd epiarhavvr llredpdiav agecgdgvsa vaairdlspd lvfldiqmpa
       61 itgldvvati gaprmpatif vtayeqfavr afdanavdyl vkpfsrerfa etlrrakqrl
      121 aaargadadt ttrimqalas lqrredyler ipvredervv lvevddivci kasgnsvrlh
      181 ladrvhelre tmtalaarld prhfarvhrs aiinvrrvre ihpwfngyhv vtmdtgqqlr
      241 msryqheafl rlatlgrgd
//
LOCUS       WP_284448164             394 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Pseudoxanthomonas
            mexicana].
ACCESSION   WP_284448164
VERSION     WP_284448164.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..394
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43479
     Region          9..384
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mawphsasaa rddgagwipp dtfladlprl mqalrvpaig mavvergevv warnlgvtna
       61 etrapvaddt lfedaslskp vfaylvlqla dqgvidldap lvryrrmdyl adhpwvdmvt
      121 ardvlrhstg mpnwrkdpah eklvpaakpg tridysgeai fwlqlvvekl tgesldesmq
      181 rllfgpagmr dssytwskdl aersvyghra vedeeagmpp qmlretwnaa qtvadrwgkp
      241 lsawryedaq ralpevqait pkglvnwpgd ilanaaaslr ttpsdyarfm almvrtphap
      301 wqiteatrta mltrqievpg rwtdkglgwn leatprgpvf yhsgsnggif knfalgdarg
      361 qralvaltng gsgnvlyrrv vraatghdll afdl
//
LOCUS       WP_284448301             196 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Pseudoxanthomonas
            mexicana].
ACCESSION   WP_284448301
VERSION     WP_284448301.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..196
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22037
     Region          39..150
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mlrkaqrrlw mkyalrgvgg ndnharldla yrmpdpwnme spmerarfea tngvieqafg
       61 rvgsvleigc geghqtqyla rlsdeqygld vspaaierar vrlpqahfaa vdlfqqpwge
      121 erhrfdlvta cevlyylsdp aatvarmrhl grcglvtffa pacgrvgphv eaipglqktw
      181 ihhggtawli gwwrda
//
LOCUS       WP_284448365             155 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pseudoxanthomonas
            mexicana].
ACCESSION   WP_284448365
VERSION     WP_284448365.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10475648
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..155
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16258
     Region          <22..64
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mdvqdlldta kaaqnittdk glaealgvtk qavsnwrkgv slpdtvtcat lagytglpla
       61 qvlgivgear aisreekavw rklaasaalv allvaptlvq sahaatlhal pqaaamtdtg
      121 avmqvvlgim rnsrgtemgw wtrllrwfqp gsvkl
//
LOCUS       WP_284448446             181 aa            linear   BCT 25-DEC-2024
DEFINITION  KdsC family phosphatase [Pseudoxanthomonas mexicana].
ACCESSION   WP_284448446
VERSION     WP_284448446.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..181
                     /product="KdsC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=19192
     Region          13..172
                     /region_name="KdsC"
                     /note="3-deoxy-D-manno-octulosonate 8-phosphate
                     phosphatase KdsC and related HAD superfamily phosphatases
                     [Cell wall/membrane/envelope biogenesis, General function
                     prediction only]; COG1778"
                     /db_xref="CDD:441384"
ORIGIN      
        1 mplshlhdlt ddvlaraari rlacfdvdgt ltdgrlylds egreqktfhv qdgqglvllk
       61 ragievafit arggtvavar grelgvqvft gvkdklarvr elgaglglgm eqvafmgddl
      121 pdvpafrevg laiapadahp wtaqyahwrt rrcggqgaar eacdlllgtq ghaplleggt
      181 a
//
LOCUS       WP_284448563             761 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein [Pseudoxanthomonas
            mexicana].
ACCESSION   WP_284448563
VERSION     WP_284448563.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Porat,A., Cho,S.H. and Beckwith,J.
  TITLE     The unusual transmembrane electron transporter DsbD and its
            homologues: a bacterial family of disulfide reductases
  JOURNAL   Res Microbiol 155 (8), 617-622 (2004)
   PUBMED   15380548
REFERENCE   4  (residues 1 to 761)
  AUTHORS   Kimball,R.A., Martin,L. and Saier,M.H. Jr.
  TITLE     Reversing transmembrane electron flow: the DsbD and DsbB protein
            families
  JOURNAL   J Mol Microbiol Biotechnol 5 (3), 133-149 (2003)
   PUBMED   12766342
REFERENCE   5  (residues 1 to 761)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   6  (residues 1 to 761)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   7  (residues 1 to 761)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   8  (residues 1 to 761)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   9  (residues 1 to 761)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12109673
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..761
                     /product="protein-disulfide reductase DsbD family protein"
                     /EC_number="1.8.-.-"
                     /EC_number="1.8.1.8"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=80418
     Region          30..144
                     /region_name="DsbC"
                     /note="Disulphide bond corrector protein DsbC; pfam11412"
                     /db_xref="CDD:463273"
     Region          179..294
                     /region_name="DsbC"
                     /note="Disulphide bond corrector protein DsbC; pfam11412"
                     /db_xref="CDD:463273"
     Region          372..761
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 mtpirtlpal lllflaslla paasaaitqd dllpvdeafv ltataparer ieirwkitdg
       61 yylyrhrtgv eadagfaaqp lqlpkgkayr deffgdvety rgelvatlpg rpapgtdsvs
      121 lkikyqgcad agicyppqtr tlkvalppta gdafvplggg alagnllgqt pqagmdalpl
      181 peeqafafea iafngnelll rftpargyyv yrdrtsmale gaqgvslqap rwpkgkahrd
      241 ehfgdvvvyf dqaevpvplk rdradavtat lrvtfqgcqt dgicyppmtr rvklaipsgt
      301 vtpastpdtp apatvapppt attpvdatpd tttsaasiat dvertrppee vlarnprgts
      361 sllvalalal tgglilnlmp cvlpilslka lslaesgreg gdarrralwy tagvlvsfva
      421 vgalaialra agqalgwgfq lqqpwvvgll ayvmfavgls lsgvfaighr lagtghglas
      481 rrgpvgdfft gvlavvvasp ctapfmgval ayaftaptpl allvfavlgl glalpfllig
      541 fvpalasrlp rpgawmdtlk qvlafpmylt avwllwvlgk qrgidavgla lvglvllalg
      601 lwwfqrarfa vaplqralal alavsalvpl amlhrlpaei aaapttegha aysaerlaal
      661 raegrivfvd mtadwcvtck anekavlntp afrellathd avmltgdwtn vdpaitafle
      721 ahgavgvply vlyprgggag evlptvltqd gmrraferaa r
//
LOCUS       WP_284448690             256 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: LytR/AlgR family response regulator transcription
            factor [Pseudoxanthomonas].
ACCESSION   WP_284448690
VERSION     WP_284448690.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas
  ORGANISM  Pseudoxanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 256)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 256)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Pseudoxanthomonas"
                     /db_xref="taxon:83618"
     Protein         1..256
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28084
     Region          6..256
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mnfrgviaed eellrtalss llkeawpqlq ivaecedgas alesiaelqp dvafldirmp
       61 gltgievarg ladasprtqv vfvtaydqya idafeqgaid yllkpitrer llatvqriqa
      121 raaaghpdga tleallrhls arempaskpp lvwitasagk dtklimvddv ayfqadnkyt
      181 tvmtaegesl lrtplrelld sldaatfkqi hrstivnmka vasvsrddtg rgrlklknrp
      241 etltvsqpfm slfrnm
//
LOCUS       WP_284448712             416 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudoxanthomonas mexicana].
ACCESSION   WP_284448712
VERSION     WP_284448712.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..416
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45635
     Region          7..414
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mnpphddvli igggaiglat alalldagrg vrileagavg ggashgncgt itpshappla
       61 apgvvaqalr wmftpdaply lkprvdpalw hwllrfavrc nprdwrqstq araallndar
      121 arladwvsry dlqcefeeeg ldyvfrdprr fqqyvdesvv lktfgiatqv fggtdyeree
      181 pamlpgvaga irfpgdarlr pdryvaelar vvrerggvie eqcrvdrlep msdgvrlats
      241 qgerkggdav ialgawtpaf arrlgirapi qpgkgysity srparvprhp mvlkdrsvcv
      301 tvwdsgfrlg stmefsghdd tlnatrlaal ergareflre pvgaevherw cgwrpmtwdd
      361 lpllgrapgq rkvwiaaghg mlgismstat gqlmadlmtg rppafdpspy rperfa
//
LOCUS       WP_284448720             202 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Pseudoxanthomonas
            mexicana].
ACCESSION   WP_284448720
VERSION     WP_284448720.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..202
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=22979
     Region          1..174
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mtkhydadyf qrwyrdgdig gaprlarkva lavavaeyhl erpirtvldi gcgegawrap
       61 llklrpklqy lgfdsseyai rrfgrtrnlh yarfedfqyl rpcepvdllv csdvlhyvpt
      121 relmrgltgl aelcggiafl etfakeddfe gdhdgfqsrr aawyrqafnn egfqsvgnhc
      181 wlaprlagdv aaleaadyrp it
//
LOCUS       WP_284448832             443 aa            linear   BCT 25-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Pseudoxanthomonas
            mexicana].
ACCESSION   WP_284448832
VERSION     WP_284448832.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..443
                     /product="metal-dependent hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46802
     Region          33..>93
                     /region_name="NagA"
                     /note="N-acetylglucosamine-6-phosphate deacetylase
                     [Carbohydrate transport and metabolism]; COG1820"
                     /db_xref="CDD:441425"
     Region          73..420
                     /region_name="Met_dep_hydrolase_A"
                     /note="Metallo-dependent hydrolases, subgroup A is part of
                     the superfamily of metallo-dependent hydrolases, a large
                     group of proteins that show conservation in their
                     3-dimensional fold (TIM barrel) and in details of their
                     active site. The vast majority of the...; cd01299"
                     /db_xref="CDD:238624"
     Site            order(91,93,259,279,352)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mnrtalalal aacglpaapd alaagpaapr tlalhcervf darsgkvlge htvlvrdgri
       61 aevipgrakl adaesivlad htctpgwtdl hvhldgessp qsysegfrld pvdfayrsvg
      121 yaektlmagf tsvrdlggev tlhlrdavnq gavkgprifa agtsiattgg hadptngfnt
      181 hlshlmgppg ptegvinsid darqavrqry kdgsdvikit atggvlsyak sgdapqftvd
      241 evkaivdtar dygfrvaaha hgkegmkrai lggvtsiehg tymdeevmrl mkqhgtwyvp
      301 tisagrfvae kakidgyfpa vvrpkaerig aliqdtagka yrngvkiafg tdmgvgphgd
      361 narefvymve agmpaayalq aatiraaevl gvddqgviea gkradivavp gnpvddinav
      421 lkvdfvmkdg qvyrrptlda par
//
LOCUS       WP_284448944             572 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Pseudoxanthomonas mexicana].
ACCESSION   WP_284448944
VERSION     WP_284448944.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..572
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63427
     Region          30..304
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mtpmhlrnap rwqtplllll mawallaglg mrepmpadep rfvlaartmv etgqwlfphr
       61 gielyaekpp vfmwlqaasy lvvrdwqvaf llpsllaall tlwlsgdlar rlwgrhavpy
      121 avfglfvclq falqakraqi dmvlvgmttl slwallryll ekpspwllal gtfaaglgtv
      181 tkgvgflpll vfipwlwvrl ksrqalpphr glhalaglag fiagagvwlv pmlsvaltsa
      241 dpalhayare mlfkqtgtry anawhhvkpa wyylqtmltl wlpgvllapw llpawwrrvk
      301 rvdarhalll gwallvlvff saspgkrevy ifpmlpalav aaapllpgll rrravratlw
      361 aymavlvvva galgawllaa pparlqslve grgmdmdtva qlgrwlvgfa mvaavatfai
      421 arasrhrvgv alvtvtaalw taygmgfmpa lspdssaqal mqrvgqrigp daelamlgwr
      481 eqhllqadhp vtdfgfkqpw vdqwqhahaw lleaperrwl flrkeaigpc ldpakvvdig
      541 asnrrawila pgdawregcd vpadwsadvs ed
//
LOCUS       WP_284448962             410 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pseudoxanthomonas mexicana].
ACCESSION   WP_284448962
VERSION     WP_284448962.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 410)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..410
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=45082
     Region          104..408
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mwlggyalll taavmlhgfl vneiaerlvw dsllkteleh hlqrraddpr yrwsdtddlq
       61 lyastdarpl ppevvglpeg ihdelmlgdr evlvlvrtvq gvkytlvldi telesqedtl
      121 tlivlglait lvvvmgalva wglrrslrpl tglaadigtl spdrtgqrit vpekattelv
      181 viagalndyl rrheafvere rifidttshe lrtpvaiiag aselaleqpd lpaparqqvq
      241 rihrtardve rliallltla kdparlsrss dvvmlhellp diiddhrhll agkdlhvivd
      301 dlqpcsvsap lhivqaaign llrnaiensd rgqihvrlda datvtlqdpg hgmtpedisr
      361 lyaqmarggg regggigldl larlcehlgw tlsiqsapgr gtisrlrlsr
//
LOCUS       WP_284449049             473 aa            linear   BCT 25-DEC-2024
DEFINITION  class II fumarate hydratase [Pseudoxanthomonas mexicana].
ACCESSION   WP_284449049
VERSION     WP_284449049.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Woods,S.A., Schwartzbach,S.D. and Guest,J.R.
  TITLE     Two biochemically distinct classes of fumarase in Escherichia coli
  JOURNAL   Biochim Biophys Acta 954 (1), 14-26 (1988)
   PUBMED   3282546
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..473
                     /product="class II fumarate hydratase"
                     /EC_number="4.2.1.2"
                     /GO_component="GO:0045239 - tricarboxylic acid cycle
                     heteromeric enzyme complex [Evidence IEA]"
                     /GO_function="GO:0004333 - fumarate hydratase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006099 - tricarboxylic acid cycle
                     [Evidence IEA]"
                     /GO_process="GO:0006106 - fumarate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49280
     Region          10..457
                     /region_name="FumC"
                     /note="Fumarate hydratase class II [Energy production and
                     conversion]; COG0114"
                     /db_xref="CDD:439884"
ORIGIN      
        1 mtskktagrt rvehdsmgel qvpaealwga qtqravqnfp isgrpmprgf iralglvkaa
       61 aaevnaglgl lpkgvakavq taanevarge hdahfpidvy qtgsgtssnm naneviatla
      121 sragkaqvhp ndhvnlgqss ndviptairv aaqlaavedl lpaighlrkt vdakgralgk
      181 vvktgrthlm dampltfgqe fsawsaqlas aqariedtlk rvrrlplggt aigtginadp
      241 rfgarvakal saatgtrfes aankfeglaa qddavelsgq lsalavaltk iandlrwmns
      301 gplaglgeve lpalqpgssi mpgkvnpvip eatvmvcaqv mgyhtavtva gqtgnfqlnv
      361 tlpliahnll damqllsnvs rlladdciag lrvrearvke aldrnpilvt alnpvigyek
      421 gaaiakqayr qnrpvlevar eitglpektl kplldpavla kggihgkagg ggg
//
LOCUS       WP_284449054             450 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Pseudoxanthomonas
            mexicana].
ACCESSION   WP_284449054
VERSION     WP_284449054.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..450
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=48860
     Region          1..444
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrvaifgtgy vglvtgtcla evghdvicvd idpakvdgln qgivpiyepg lspmvkanha
       61 agrlrfttda asaiahgdvv fiavgtppde dgsadlqyvl avartigrhi grpctvvnks
      121 tvpvgtadkv raaievelaa rgadvafdvv snpeflkegd avndcmrpdr ivigaahpqa
      181 verlrrlyap fnrnherivv mdvrsaeltk yaanamlatk isfmneiani aervgadveh
      241 vrqgigsdpr igwhfiypga gyggscfpkd vqalartaqq hgyvpellqa vegvndrqkg
      301 hlfellqrhy drgedegvrg ktfavwglaf kpntddmrea ssrrllselw eagarvrayd
      361 peaheeasri fgerddlvlc rdayaalega dalfvvtewk qfrspdfvrl rdalgdavif
      421 dgrnlydpve veaagiayyg igrgrsvhag
//
LOCUS       WP_284449065            1689 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-glutamate dehydrogenase [Pseudoxanthomonas mexicana].
ACCESSION   WP_284449065
VERSION     WP_284449065.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 1689)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1689
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..1689
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=187127
     Region          62..1686
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 mnaarspkka skqtskpeas katqavtpka tptkkvaarp vqaakaakgk agvattaeaf
       61 tlapildair krisgasaqa eartfaeafy krmeedeyph hgaegwaaia tdmlafarlr
      121 kpgaanvrvf natqkshgwd sphtvlqivn ddmpflvdsv smalaemgvg vhvlghplvr
      181 ftrdragkvt avgegkhesl mlleidrlpp eemaqvekri rsvldevrai vrdwsamrek
      241 mlaladdmat rrmpaddegr reaqeflrwa aadhftffgy reyrvekgtg ilaavedsgl
      301 gllregdttp prniktlaah ylpqggsvda liltktnrrs tvhrpgnmdy igvlefdakg
      361 npiaeqrfig lytssaynrr pweiplvrer heyvmqksgl spsghsgkal rhiletlpre
      421 elfqssdeel yrtamgilgl qervrsklfl rrdrygrfys alvyiprerf ntdvrlries
      481 llkdamrgey vdssvllges plaqlhitir pkageqvevd tsalegdiah llrnwqddlr
      541 etliarhges kglllaggyg ralpagyiev vspegaardv ehlaaltgkd dlrlslhesr
      601 rkrpgqgrlr lnlyrqetdi plsdalplme nmglrviseh pfrletaqga ryiqefevep
      661 vngafdverl apafeeafar iwrgdaendg fnklvlaagl awrqvallrg yckyllqtgv
      721 pfsqsyveet lnrypllarl lvelfearfd patgseskaq ikegqdrfae qlkalagdde
      781 aaaktlaalv earggkreqq ieaahrallk lmdrvssldd drilrgfmga ieatlrtsfy
      841 qrgkdgqpah tisfkfdsak vpdlpkprpy reifvygprv egvhlrfgpv argglrwsdr
      901 redfrtevlg lvkaqmvknt vivpvgakgg ffvkrppvgg drdavlaegi acyklfiqgl
      961 lditdnivgn rivppvdvvr hdqddpylvv aadkgtatfs dianglalah gfwmgdafas
     1021 ggsvgydhkg mgitargawe svkrhfralg rdsqtqdftc vgigdmsgdv fgngmllseh
     1081 irlvaafdhr hifldpnpda arsfkerarm fkvprsswad ydakliskgg gihprsaksi
     1141 ditpevraal siadgvksmt pnelmsailk apvdllwngg igtyvkasne thadvgdran
     1201 ndlrvdgrdl rckvvgeggn lgltqlgrie aaqhgvllnt dfidnsagvd tsdhevniki
     1261 llngvvqakk lsmdarnkll admtsevadl vlwdnyrqnq aislmermsv srlgskqhfi
     1321 qtlesqglld rqieflpsda elaerkargq gltrpelsvl lsysklvafq qllesdiped
     1381 pylskelqry fpqplqkkya temekhrlkr eiiatavtnt tinrmgatfl lrmqedtgrs
     1441 paevakafti tretldaral wnqidaldgk vpesvqidal qviwqvqrnf trwlltrqgp
     1501 ipaiataver yhdgfneira adgvlpdslr paynaslqaw kdkglpaala gqiaalpyle
     1561 pscdiielar arklkpvevs kvhyrlgeal hlpwlqdqie alkvdgrwha vargvlrdel
     1621 aahqrtltnq vlslpggnad akvrawlgrd daglrftlnm lnelaaqktl dyptasvavq
     1681 rlgqlasqg
//
LOCUS       WP_284449078             472 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Pseudoxanthomonas
            mexicana].
ACCESSION   WP_284449078
VERSION     WP_284449078.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 472)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..472
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=53126
     Region          1..469
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mpnalvwfrh dlrlddnpal raaldqgftp ipvyvhapqe egewspgaas lawlhrslaa
       61 ldadlrargs rlllregpsa palqalveqt gavavfwnrk yepatqprda slkkrlreqg
      121 lqvesfngcl lfepwdlatq qggpykvftp fwrsalarwr apatwdapga lpafedalpg
      181 esldawrlap algwdagfwk vwtpgeagar ealevfidga lngyrtdrdr pdrtgtsrls
      241 phlhfgeiap wrvtaelera rtaansadmd gyirelgwre fayhllhhfp qtttqnlnpr
      301 fahfdwakvd pkalkawqhg rtgvpivdag lrelwatgym hnrvrmivas yltkhlryhw
      361 lqgarwfwdt lvdadlannt lgwqwtagtg adaapyfrvf npvtqaekfd pkgtyiahwv
      421 pelaavpvpl rfapwekpdv msriapdypr rplvdlaegr egalaayrkt gd
//
LOCUS       WP_284449143             434 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Pseudoxanthomonas mexicana].
ACCESSION   WP_284449143
VERSION     WP_284449143.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..434
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47210
     Region          110..403
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mlvavllpse arsadapach agayrlldgs vvgidrlsep aqlrwqrvdg ttgllspadg
       61 awrsttgwtg rpdgkvvrfg ecgegriafd rqagskiafd itetrfagkg eqlrgrlvlp
      121 hgddpvpiav ivhgsedysg vdfyaaqhlf paqgvgvfvy dkrgtgqstg tytqdfhlls
      181 ddavaalhea rrlagpraar igflggsqag wvaplaaskt dhaafvvvgy gmadsplaed
      241 rdqvmldlrr agygdevmak areiteatga vvasrreadw erlevlrrry adepwypaik
      301 gefsglllqh treqieataa qhdkgttwny dtmpvlralr ipqlwilaga dreappeetl
      361 rrlvalgeag hpittvvfpg tdhgirefet gdddtrtytr iadgyqrmqi dwiltgtfph
      421 apygrarava qpgr
//
LOCUS       WP_284449395             419 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Pseudoxanthomonas
            mexicana].
ACCESSION   WP_284449395
VERSION     WP_284449395.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..419
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=45290
     Region          5..419
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mphrlratcv avllagvsfv aaapaqtsre aeqklqrvrs elksiaqerr klegergaas
       61 rqlreadekv grtsrslaet eaamrreaaa laelqqrrdt lqaqqqrqra qlgalvraay
      121 qqggdaplkv llsqdrvada nrllayhryv qrdqarrida lstdlaaleq veqeivarra
      181 qleaaraqqr davmqlekdr ktraslvadl deryqdraak ekalgqdars lerllanlra
      241 aaaraeaerr aaarraaaea aaaekrenaa gtgrstrdsa parpvvasap plkvgglgwp
      301 vsgsllaryg grmpdgrtst gvligaaagt pvtavadgtv vfsewmtgyg lilildhgng
      361 ymslyahnds llkdsgdrvk rgdavarvgt sggqgqaaly felrrngqpv dpsswlqrr
//
LOCUS       WP_284449447             410 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Pseudoxanthomonas mexicana].
ACCESSION   WP_284449447
VERSION     WP_284449447.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..410
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=45747
     Region          19..400
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mprlvnrlnd ralrgnllpg lyrdgngllf nvgptggrsw ifrytsptsr krrdmglgpy
       61 ptvtlaaarg raeearrliv qnvdpldqar gdlqaaraal aakvtfgecl qsyvaaraeg
      121 wkndkhkaqw issvrthaar lipmyvdsit tddvfaalep iwsektetat rvrqrvesvi
      181 dwattkrlre gdnparwrgh lenllpapes lkqvahhaal hfrdvpkfmg rlhakeslaa
      241 halritvlsc lragevvgar weefdmrakv wiipahrmkg pksqrrdhai plvgalldav
      301 rslprlsety lfpgggakgl tlttdavlnc lqglhpdyae mtthgfrssf rdwvgdatdf
      361 dealaelala hkvknkveaa yrrqtaldkr relmmawgey askgttpkrs
//
LOCUS       WP_284449283             978 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Pseudoxanthomonas mexicana].
ACCESSION   WP_284449283
VERSION     WP_284449283.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 978)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 978)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 978)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 978)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..978
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..978
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=106005
     Region          15..919
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mtlqhsplre airvalaata mytcaaaaqd stqdpttldr ievtgsrirq vdmesaapvl
       61 tisrddierq gfqsiadilq nisatgapai sramplssge nvggqfidmr nlgtartlvl
      121 vngqrigast sglqdislip taaverievl kdgassiygs daiagvvnii trsgvegaqa
      181 qlyhgqydeg dgkitradfv lgfngdrgsl ttaveyrkee evmardrpys aypqgqwhpt
      241 rgwttvsqwg vinlpaslgg nrvldagadw rdignfhaln tntgtsaadp agstadksnp
      301 nqqthlrtpl esrslfvdgs fdltedirlr gsmlysqrea arqiagypfq sasfglmmsa
      361 dsyynpvgth hgyaaptavn farrtweipr vdkptsttwr ftvglegsfq agerfydwdv
      421 nylynnnkvh qenygnlnla rvaravgpsf lnangqvqcg tptnpipltd cvawnpfipf
      481 gragdggltd nralidylfq tlnstgetet eaftanlsgs lfalpggelg favgvesrke
      541 sgrfipdama vtgnsttlsa gptrgsyrvd elnaelsipl ladlpgaeel sfsvatrysd
      601 ydtfgdttns kvgfkwkpvd svlvrgtyae gfraptindl ygggsqtfsf ftdpcdtlfg
      661 asagnaavra rcaqdianad tyrqlaqgfv pagspnsqtp vaffngsnpd llpesseskt
      721 lgvvwspgfa sglnvsldww niriedtiva dtptqmlndc yiqndaarca aftrdpvlgf
      781 vnnltfngin agyretegyd ldlsyrlate aagdfrlvwq ttytardeik tdtnpatlpq
      841 qlvgyatspg figtfrvrsn anltwtfgsf gatwgaryys sqketclsaa lfpdecsdpg
      901 fvaanpaqsr avhkrgsvtf ndielrwtap wdatisvgan nvfdregpqf ysqpsanvsy
      961 hgqydigrfl ymkylqrf
//
LOCUS       WP_284449577             406 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Pseudoxanthomonas
            mexicana].
ACCESSION   WP_284449577
VERSION     WP_284449577.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..406
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42550
     Region          9..406
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 msagvpqsla gvrvldltrv lagpwctqvl adlgadvikv erpgsgddtr gwgppflkda
       61 dgnetpesay ylcanrnkrs ltvdlstaeg qavirrlamr sdvlvenfkv gdmarhglda
      121 atlraahpql vycsitgfgq dgpyaqragy dfavqglggl msvtgaadge pqkvgvavad
      181 lftgmyatva ilaalrhrda tgegqvidma lldaqvamla nlgshylvgg evparqgnah
      241 anivpyqvfa vadghiivav gndrqfarlc ellglaalgq darfatnagr vrhrdalipv
      301 lqqafrardr haclasleaa gipcgpvndl aevfadpqvr argmvvetah pradtvplvg
      361 splklsatpv esprappmlg qhtdsvlrev gysdgeiaal rssgai
//
LOCUS       WP_284449687             349 aa            linear   BCT 25-DEC-2024
DEFINITION  FecR family protein [Pseudoxanthomonas mexicana].
ACCESSION   WP_284449687
VERSION     WP_284449687.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20752687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..349
                     /product="FecR family protein"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0016989 - sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37925
     Region          9..50
                     /region_name="DUF4880"
                     /note="Domain of unknown function (DUF4880); pfam16220"
                     /db_xref="CDD:435227"
     Region          125..347
                     /region_name="FecR"
                     /note="Periplasmic ferric-dicitrate binding protein FecR,
                     regulates iron transport [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG3712"
                     /db_xref="CDD:442926"
ORIGIN      
        1 mtdskrieqh aadwlvrrda gdwaprdqra leawlsasar hkvaflrlea awaeagrlqa
       61 laaglpaggp pprteaagpg apasglpdlr gitfaprhth arpgrwrhgv aaalamlalg
      121 saawggwqlt grqqahyasa vgqvqtltlp dgslatlssd sqldvritrq erhvaltrge
      181 affdvahdrr rpfvveaqgr rvaavgtrfs vrrnpedvrv vvtegkvrle trigddgraq
      241 pvsllpagsv atagrngvlv rsvpvadaer ylewregflt fddtslaeaa aefnrfnark
      301 leladatvad lrvggnfrws naegfarlle qgfpvrverh perivlhar
//
LOCUS       WP_284449605             360 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Pseudoxanthomonas
            mexicana].
ACCESSION   WP_284449605
VERSION     WP_284449605.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..360
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40356
     Region          2..358
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mtinvtkpfl ppieeygeyl kgiwsrewlt nngplvnele lqlkrllgld hllyltngtv
       61 alqlaikalg lrgevittpf syvattsslv wegctpvmad icprtlnidp dkieeklteh
      121 ttailathvy gnpcdvdrie giarkhnvrv iydaahafgt kvngrslfsy gdvsttsfha
      181 tklfhtiegg avvtpdpell rlmaqmrnfg hvsptefgav gingknsemh aamglcnlky
      241 vpdilakrri lssrydegln gcairrpeia knceynyayy avvleseeal vsvldvlhlh
      301 nivprryffp slselkyvhd qsapisedis rrvlclplyn dlsfeevdmi crlikralry
//
LOCUS       WP_284449560            1632 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Pseudoxanthomonas mexicana].
ACCESSION   WP_284449560
VERSION     WP_284449560.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas mexicana
  ORGANISM  Pseudoxanthomonas mexicana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 1632)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1632)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1632)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1632)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1632
                     /organism="Pseudoxanthomonas mexicana"
                     /db_xref="taxon:128785"
     Protein         1..1632
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=177216
     Region          57..1631
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mraffiglia aaalagckrn esgqlpeasg epikaqaakv egfalvgayp dqhdgdlaia
       61 lefsrplvss qdfdallvvk dangavvkgs wvlddkglvl rfpsveaakd yevtlkagls
      121 aadgtrlgkd dtrkvhtgel dpavgfasqg svlparesrg lpvvsinvpe vdveflrvse
      181 kqlpkffaey qrggrrgswd ldseygdstp lgklaepvyl nrfvlggkpn ervltylpiq
      241 direlqdpgl yfavmkrtgk fagefetaff tvsdiglhtr aykdklfvht aslqdgsatg
      301 svelkvldar geavlagktd gngnallnya lhaghvlvat rgkdvsmlpf nqpaldlsef
      361 avagreqawf dvfawsgrdl yrpgetvris allrdndgrp vpapkqgggq pvflrlkqpd
      421 gkvfretrlq pgaqgyfsfe qaipteaptg rwqvefrtdp askeavqgmt lrieeflper
      481 mkldldaaqp vlkpgealkl kataaylyga pasgnrftak lavaieqhpl dqlpgyffgd
      541 ptmelpkdak diidttlpen gvlqedialp aeakprspia aivsgsvyet ggrtvnrtlk
      601 rvlwpanalv girplfddkd gadananagf evvrvdaggk pqpgkglkat lvrelrdyhw
      661 nydedggwdy dftrrfenkd trtldvgaga skidfpvewg eyrldvfdpa tglttrypfr
      721 agwswddqnr gldarpdkvk laldrtgyra gdtlkvtvtp phagkgllmv esdrmlyvqa
      781 idakpgstfs ipvtkdwerh dvyvtalvfr ggsapskitp aravgvvhvp mdrrdrrvav
      841 glsvpkqmrp eqnlpvtvsv pelagqlahv tvsavdmgil nitrfpvpda naqffaqrrf
      901 gvdaydiygr viesfeggsa kirfggdmal salpqakrpt srvqtvdlfs gpvkldgkgn
      961 arvalkvpdf ngtlrvsalv ysdtrygnrd retvvrapiv aeaslprvla pgdrstvtld
     1021 vqnftgktgv fkvtvngegp ldigegsrtt dlavdakrtl tfpvtadegy ttakvrvrve
     1081 gngfkvdrry dvpvragwpa vlrsrtqvld slapvemgag fadglmpgsv tarmtvsalp
     1141 pipfasalkg aleypygcae qttskgyaal elddatakml gidgldakkr rermegafgr
     1201 lasmqvsngh fsmwgdddyv npgltpyiae flldareggf avpdavlqka ltrlnedlla
     1261 ggaqfygydr rdhlkfanqa yagyvlarvn raplgtlral ydnergkslt glplvhlgia
     1321 lslqgdktrg akaitegfak tgdrpeylgd ygtklrddal mialvherkl akpefdrrai
     1381 slgreldarr nsgwlwlstq eqvalarlgk almvdqkklv sgqwsiggda eavapvrlfg
     1441 rsvdyaalar glrfvpegsp plyasldvag iprsapapdn rqigierryy ttdgkewkgg
     1501 tlkegealiv rvgitanvam pdalftdllp agleienfnl gdakqwaevv vdgiaisdrg
     1561 saadvkheef rddryvaalk ldrgdtakvf ylvravtpgt ytvppslved myrpdirgvg
     1621 kaspstitvv qp
//
LOCUS       WP_284449811             301 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Spongiibacter
            tropicus].
ACCESSION   WP_284449811
VERSION     WP_284449811.1
KEYWORDS    RefSeq.
SOURCE      Spongiibacter tropicus
  ORGANISM  Spongiibacter tropicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae; Spongiibacter.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Spongiibacter tropicus"
                     /db_xref="taxon:454602"
     Protein         1..301
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=32169
     Region          2..261
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkvlvvggsg liggdaalyl kshghdvtim arsvptapvl aalpfvqgdy vnddmsdgrl
       61 ngfdavvfaa aadirqvpmd gsvtpedfyr kvndeavprf faaareagvr ravyigtfyp
      121 qvashrigec pyvtsrsntd eavramssds ftvcslnlpf vmghipgldi phigalvaya
      181 sgalselpvf apkggtnhit shavaqatla aldhgesgra yllgdenysw keylelwfea
      241 agnpqtlevr eddhpllpnv imfagpgatv syepeaveel aydrhqinat intlvkayse
      301 a
//
LOCUS       WP_284449847             260 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Spongiibacter tropicus].
ACCESSION   WP_284449847
VERSION     WP_284449847.1
KEYWORDS    RefSeq.
SOURCE      Spongiibacter tropicus
  ORGANISM  Spongiibacter tropicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae; Spongiibacter.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Spongiibacter tropicus"
                     /db_xref="taxon:454602"
     Protein         1..260
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28937
     Region          51..157
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mleseyfemn rvgwdkraaa hfeskfydlp gflagetslr eielaelgdv kgqsllhlqc
       61 hfgmdtlswa rkgavctgvd ispvaiqkar elaeelklns efvctdvysf qrsgsalydi
      121 vftsygaicw lpditrwaev vagnlavggr fyiadfhsiy dllagysyft qvqpdvdeeg
      181 tytenggdet aklatwshpm ssvinalvnv giqiervsef pfspyncfeg mverepgrfy
      241 lshkgndvpi vysitgrkva
//
LOCUS       WP_284449880             108 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: DMT family transporter [Spongiibacter].
ACCESSION   WP_284449880
VERSION     WP_284449880.1
KEYWORDS    RefSeq.
SOURCE      Spongiibacter
  ORGANISM  Spongiibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Spongiibacter"
                     /db_xref="taxon:630749"
     Protein         1..108
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11328
     Region          3..106
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mspwaylgla iaaevvatsa lkasegfsrf wpsalvvlgy glsfyllslt lksiplgvvy
       61 avwsglgivl ialvaylmyg qrldlpallg ialilsgvvi ihrfssvs
//
LOCUS       WP_284450061             242 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein, partial
            [Spongiibacter tropicus].
ACCESSION   WP_284450061
VERSION     WP_284450061.1
KEYWORDS    RefSeq.
SOURCE      Spongiibacter tropicus
  ORGANISM  Spongiibacter tropicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae; Spongiibacter.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Spongiibacter tropicus"
                     /db_xref="taxon:454602"
     Protein         <1..242
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
     Region          <2..242
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 srlisyydyv nkarsqqlre yqstltalse lipeiaeete alsdtekrla qqqeqlkvqq
       61 qkrerslakl erelsgqqld lgaldkerkn legvleaigr eitniaipdn yrpfkqmrga
      121 mpwpvagkrl nrfgaprqgs airwqgiqia gkegdpvrai hngrvvyadw lrgaglliiv
      181 dhgndylsly ahnqsllrse gdwvrggeai atlgnsgglr qnglyfeiry kgrptnpasw
      241 cr
//
LOCUS       WP_284449985             136 aa            linear   BCT 25-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Spongiibacter
            tropicus].
ACCESSION   WP_284449985
VERSION     WP_284449985.1
KEYWORDS    RefSeq.
SOURCE      Spongiibacter tropicus
  ORGANISM  Spongiibacter tropicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae; Spongiibacter.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 136)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 136)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 136)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Spongiibacter tropicus"
                     /db_xref="taxon:454602"
     Protein         1..136
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15681
     Region          17..132
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mpetfarqhr drdggymnpd hlaafsrqln alrentlati rqaqntlger aepgdeadra
       61 qheedtrlal rtveretrll rkidaalrri rdgeygycle sgeeiglerl rarptaeyca
      121 evkvqmeeke khygkr
//
LOCUS       WP_284450164             379 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Spongiibacter tropicus].
ACCESSION   WP_284450164
VERSION     WP_284450164.1
KEYWORDS    RefSeq.
SOURCE      Spongiibacter tropicus
  ORGANISM  Spongiibacter tropicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae; Spongiibacter.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Spongiibacter tropicus"
                     /db_xref="taxon:454602"
     Protein         1..379
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40357
     Region          1..378
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mgplqglrii eieglgpapf agmmfadmga evisvtrksa aegsapinsi sergkksial
       61 nlkdpravea llklcetada liegfrpgva erlgigpddc marnpklvyg rmtgwgqtgp
      121 msqaaghdin yislsgalhg igragdkpvp plnlvgdfgg ggmflafgvv samleagrsg
      181 kgqvvdvsmv egsaalmhmm ysyynlgafg wrdergvnvl dtgahfyevy etqdgkylsv
      241 gpiepqfyql lkelmeldet vfgnqydver wpelkeqlqa lfktrtrdaw cdllegtdac
      301 vapvlsmsea pqhphnvarn sfvdvgghvq pcpapkfsrs epatpkpapl qgvdtdavla
      361 glgydadsla alradgvlt
//
LOCUS       WP_284450182             493 aa            linear   BCT 25-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Spongiibacter
            tropicus].
ACCESSION   WP_284450182
VERSION     WP_284450182.1
KEYWORDS    RefSeq.
SOURCE      Spongiibacter tropicus
  ORGANISM  Spongiibacter tropicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae; Spongiibacter.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     BTLCP proteins: a novel family of bacterial transglutaminase-like
            cysteine proteinases
  JOURNAL   Trends Biochem Sci 29 (8), 392-395 (2004)
   PUBMED   15288868
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Spongiibacter tropicus"
                     /db_xref="taxon:454602"
     Protein         1..493
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=54974
     Region          <331..444
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 msllsvflca caaspapnvp psppvgvesr wqvlqrdgqp lgrrqqwhyc agercfssev
       61 tdiavqqpga pvsisrvrld yvesrdaqgl saskqlrska anhrlqlirq gdgwqlqqae
      121 rrnairlesa plfpvalqrs mlenrgqapl vtrewsfssl tletiryrft pisqspldpe
      181 qrelllpwlq qiawridrer qtergwqwqa ewfsdvnftp iaernlsags dlwllpcder
      241 crdqalqppq hvyqrlirsp yrisdealrg kiryqlggva daelpatgeq qvrrqddkll
      301 vsicddcgde sapdsgslqa amaanywlph hdsamqrvve evlgdaelsp raamqrltrf
      361 vtghmdevat ysgygtalda lqsghgdcte halllaalgr aagipsrlvm glaynnerfl
      421 grrfvfvphm wvqawtgdrw esfdsglgaf tagyialals aegdqasfla mnalldtlsi
      481 dsavqlrsrp aep
//
LOCUS       WP_284450210             695 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Spongiibacter tropicus].
ACCESSION   WP_284450210
VERSION     WP_284450210.1
KEYWORDS    RefSeq.
SOURCE      Spongiibacter tropicus
  ORGANISM  Spongiibacter tropicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae; Spongiibacter.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 695)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 695)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Spongiibacter tropicus"
                     /db_xref="taxon:454602"
     Protein         1..695
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=75680
     Region          24..690
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mnfwrfdads avlghplags ydpllvglsv viscfagita laladrmtas psrsakawwq
       61 lggaaalgfg iwsmhftgml afklpehadm qynagltlis llpamagsva alyfisqanf
      121 sglhlqlcsi alaggigvmh ytgmeamqmp glrydlplfi asfgiaylla ltalsirryl
      181 raqkqlpena vsyisgtiig isvsgmhyta measrfyaig dghaiqsvvs sanlasgigl
      241 faalilglsi vaawidrqvg fqrllnlekm ahtdaltglp nrvlyesqle daleknqrqg
      301 dnlalmyfdl nkfkpindty ghaagdlllr efasrlkhsl rehdlaarlg gdefaallrg
      361 fskvedvami aerildslat pvrldrlely lstsigisic pddaqskdel iqladeamyr
      421 akagklgycf agyqlgrlse eyqlatdait raldrseisl lyqpiidlqt rqiiaveafa
      481 rfpnqnsqsp leffelaerr gktrelsdlv lravcrqasq wlkdgiefgr iavnisdmqt
      541 rhpdfskcll gimqqfsvpg erlelelsas cfkspndgik sqiiaakarg vtitlddada
      601 nalqaisecp vqkvkisrnl vadsvhstka raliktiatl slelgyelsc ggieteeqlk
      661 rvtdagcrsg qgylfyhpmt adlfaskias ltgvq
//
LOCUS       WP_284450335            1107 aa            linear   BCT 25-DEC-2024
DEFINITION  UvrD-helicase domain-containing protein [Spongiibacter tropicus].
ACCESSION   WP_284450335
VERSION     WP_284450335.1
KEYWORDS    RefSeq.
SOURCE      Spongiibacter tropicus
  ORGANISM  Spongiibacter tropicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae; Spongiibacter.
REFERENCE   1  (residues 1 to 1107)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437585
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1107
                     /organism="Spongiibacter tropicus"
                     /db_xref="taxon:454602"
     Protein         1..1107
                     /product="UvrD-helicase domain-containing protein"
                     /EC_number="3.1.11.5"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=123387
     Region          1..1099
                     /region_name="RecB"
                     /note="3#-5# helicase subunit RecB of the DNA repair
                     enzyme RecBCD (exonuclease V) [Replication, recombination
                     and repair]; COG1074"
                     /db_xref="CDD:440692"
ORIGIN      
        1 msallsppdq lqreqavept rsvllsapag sgktgvlllr ylrcllcver pehvvaitft
       61 nkaageiker vmgalqsaes mpinsvfdrd irdavlavre hqarlnwnll ensarlriat
      121 fdsfcgslvr rlpllsglga aapvsdseal yreailelfr qldepscppp lrealesllr
      181 ygsnrietlq pllsallakr dqwqedilga dldvmdaalt alvseafhvh wsrlqafgve
      241 elfaayrdss gvcddhgwaa elpvpeqvtv edlpllsaig rsicnnngql ykpgsvqhak
      301 fkkgqpgteq akdwlkraqd ddpdaiaadw qalavlpppv lpegsrelvg hfcialryll
      361 ahlrlvfeqr ggvdfgeial raihalraes ggevseamll edriehilvd emqdtsvsqi
      421 ellkalcqdw mpddhrsvff cgdlqqsiya frgslvslfd elrqsagfag kalsllqlra
      481 nfrssptlvn wvndcfrglf aerdsayvea lpqrqnigrv qvhpiamakg vdaagsaaqr
      541 eaeavvaiiq raqqenpaas iailvrsrrh lrqitpalka aniafsgqdi dsltelpavm
      601 dvlsmlralw headdvawsg llrapfvgls wddllslret glplrealfk velhrslsee
      661 grqacdhlve alnwldarpe srdlrwalrs lwhrlggpac ieahqqadid rvlsvldeha
      721 psgvlediaa leaalsrlya appsstvelm tihkskglef dvvilpglgn rgrnddrpll
      781 awqrlqqhml fgpkpqrsgg deqrlydylc gvqkqalsee ldrllyvalt rakgelhlfa
      841 vakmnskddl kpdagsfler lwpvvapdfe aaelldesda eapmrvplap rlrgfsatln
      901 plwqplltee salqrvqrqs enavlednie eravgivfhe lmerlgrqqg gkrliedrar
      961 legalrqrlr hhchpepgle aslarvlkll dntldceqgq wilrsydwqa seqtirrrmg
     1021 gqwqtlildr afvdpaegqp ccwivdykta eakgaledff aqqveryank mqiyrealra
     1081 tgleypisaa lyfpahqrll cldding
//
LOCUS       WP_284452464             407 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Parachlamydia acanthamoebae].
ACCESSION   WP_284452464
VERSION     WP_284452464.1
KEYWORDS    RefSeq.
SOURCE      Parachlamydia acanthamoebae
  ORGANISM  Parachlamydia acanthamoebae
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia;
            Parachlamydiales; Parachlamydiaceae; Parachlamydia.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 407)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Parachlamydia acanthamoebae"
                     /db_xref="taxon:83552"
     Protein         1..407
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47330
     Region          1..406
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 mllqfsvknf rsfeseevln lsagkgselr dsntfefsqn qrlvcsaviy gpnaggksnl
       61 iraifflqqf vlasstayqe kqkiplqpfr lnaksqneps efsidfvcnd trftyhvalt
      121 edqiiseely aypkkyrqtw ftrkwnassk ayewyhgpsf kgehkvweqm tranalylst
      181 avqfnseqlk piflwfrdql villkngpaq eiyfnpdltf qflkdpktep wihkfmecad
      241 igienfhlie eevppikkva vrtqhkmlds dqkvlfdlfl desdgtqrlf sqaggwlkal
      301 reglvlfvde ldlhlhpniv kylielfhnp ktnpknaqli ftthdtslld sdlfrrdqvw
      361 fvqkdeqhgs rlyslldfkp rkgeaigkgy lqgrygalpy igkfrfs
//
LOCUS       WP_284452524             109 aa            linear   BCT 25-DEC-2024
DEFINITION  Rieske (2Fe-2S) protein [Parachlamydia acanthamoebae].
ACCESSION   WP_284452524
VERSION     WP_284452524.1
KEYWORDS    RefSeq.
SOURCE      Parachlamydia acanthamoebae
  ORGANISM  Parachlamydia acanthamoebae
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia;
            Parachlamydiales; Parachlamydiaceae; Parachlamydia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Parachlamydia acanthamoebae"
                     /db_xref="taxon:83552"
     Protein         1..109
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=11746
     Region          10..109
                     /region_name="NirD"
                     /note="Ferredoxin subunit of nitrite reductase or a
                     ring-hydroxylating dioxygenase [Inorganic ion transport
                     and metabolism, Secondary metabolites biosynthesis,
                     transport and catabolism]; COG2146"
                     /db_xref="CDD:441749"
ORIGIN      
        1 mtikkninqd ctklglvsdi pegksiiveg peglqialfk lngevfaldn acphmggplg
       61 egciehgavt cpwhgwqfdi qtgycenmpg enarkipihv edgviyled
//
LOCUS       WP_284452565             182 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Pseudomonas protegens].
ACCESSION   WP_284452565
VERSION     WP_284452565.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas protegens
  ORGANISM  Pseudomonas protegens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Pseudomonas protegens"
                     /db_xref="taxon:380021"
     Protein         1..182
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=20397
     Region          5..>165
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mfvtlngiqa lralavvfvi fshlfsiegk yateailpna tlvgmsgvdi ffvisgfimv
       61 yvtdgkrdgl lrvieflyrr vvriypiywv ytslvlvlym vvpslvnsga padilasyal
      121 wptenpflva vgwtlshemy fyiffcllff msdrylslll vvwgggvsli gglyeggvry
      181 lr
//
LOCUS       WP_284452688             582 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Parachlamydia acanthamoebae].
ACCESSION   WP_284452688
VERSION     WP_284452688.1
KEYWORDS    RefSeq.
SOURCE      Parachlamydia acanthamoebae
  ORGANISM  Parachlamydia acanthamoebae
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia;
            Parachlamydiales; Parachlamydiaceae; Parachlamydia.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Parachlamydia acanthamoebae"
                     /db_xref="taxon:83552"
     Protein         1..582
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66072
     Region          3..577
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mkpfktlvdv ihyiaeqknp kalnhleneq wkafsssdfv tsvkyltlyl ntlqfnrger
       61 igimapcsaf wtiadfaill aggisvplfa nishenfeye vdqaeikvlf isgeeqwkml
      121 hahqghfkqi iafdekpnal tlseayrigk eidakdpdly psllskmtek dvatiiftsg
      181 stglpkgvel tqtslvsllh idpfhwnpkt drylsvlpla hifaralnli mvawgisvyy
      241 ladvkklgea aqqvkpslmi lvprilekiq anmwakvnag nfmtrligrw alrlaaqkes
      301 sfwrqifhpi adtlvysrlr eafgnrlrli isggahlnpd vyhfflaigf pvyegyglte
      361 aatvscnrfn rikvgtiglp fegmtvslsp egellvkggl vmkgyykspe atqnaftedg
      421 wlrtgdraqi deegfitilg rlkelfkttk geyispvpie qalakdrlvd maiiiadsrk
      481 yatclifpdf eaikkiqkkl nkeqipmeef lqgpeikqhm ykllvsinkh lnhweelhdf
      541 rvvaehpsie ggeltptmkl rreviekkye dlinsmyfee lv
//
LOCUS       WP_284452912             423 aa            linear   BCT 25-DEC-2024
DEFINITION  trypsin-like serine peptidase [Parachlamydia acanthamoebae].
ACCESSION   WP_284452912
VERSION     WP_284452912.1
KEYWORDS    RefSeq.
SOURCE      Parachlamydia acanthamoebae
  ORGANISM  Parachlamydia acanthamoebae
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia;
            Parachlamydiales; Parachlamydiaceae; Parachlamydia.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Parachlamydia acanthamoebae"
                     /db_xref="taxon:83552"
     Protein         1..423
                     /product="trypsin-like serine peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47542
     Region          75..230
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mysytdysss vkafeslipa tggsqyasll gqfrvqrlpq aniceviqkd pveeghlndp
       61 ydvslaetlk kiqaavgkvn detgqlgtcs llsfnlaivp yhciagqelk nltvvfqnvi
      121 ynrcecrgep fpvqgvvecd veldyaimql ggdpgrkygw lplcpdsgic seplllhhpl
      181 gkplkvsvhh mendtkttpi fgrlltyhdt dygssggayv nprghffamh lgteremtgf
      241 nllriaisie tviqhhprgl lsafarkelp qdatiqtrqc verltpydyp yitlekfiha
      301 nlsngnyilr kptrdlpgvm iehyqakhtp qwpkpypgkk gssfngfyld eiielaeaim
      361 asrplfrefh aknvagnlir insadilvsk elskklknvr tvnlyaafdf qtkywsihfy
      421 pek
//
LOCUS       WP_284452993             666 aa            linear   BCT 25-DEC-2024
DEFINITION  glycogen debranching protein [Parachlamydia acanthamoebae].
ACCESSION   WP_284452993
VERSION     WP_284452993.1
KEYWORDS    RefSeq.
SOURCE      Parachlamydia acanthamoebae
  ORGANISM  Parachlamydia acanthamoebae
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia;
            Parachlamydiales; Parachlamydiaceae; Parachlamydia.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 666)
  AUTHORS   Dauvillee,D., Kinderf,I.S., Li,Z., Kosar-Hashemi,B., Samuel,M.S.,
            Rampling,L., Ball,S. and Morell,M.K.
  TITLE     Role of the Escherichia coli glgX gene in glycogen metabolism
  JOURNAL   J Bacteriol 187 (4), 1465-1473 (2005)
   PUBMED   15687211
REFERENCE   4  (residues 1 to 666)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
REFERENCE   5  (residues 1 to 666)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445913
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Parachlamydia acanthamoebae"
                     /db_xref="taxon:83552"
     Protein         1..666
                     /product="glycogen debranching protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004133 - glycogen debranching enzyme
                     activity [Evidence IEA]"
                     /GO_function="GO:0019156 - isoamylase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0005980 - glycogen catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=76712
     Region          7..665
                     /region_name="PulA"
                     /note="Pullulanase/glycogen debranching enzyme
                     [Carbohydrate transport and metabolism]; COG1523"
                     /db_xref="CDD:441132"
ORIGIN      
        1 mselqsfqve kgsplnlgif gdcgginfsl fvhqaqnvtl hlflkptdpp iaqiplfqtg
       61 eiwhayvknl padliyafei kkedgshytk vldpyakslt sthiwgksgn yapscahpsa
      121 ntfdwqnvks phlplqnlvi yemhvrgftq hpssqvshpg qflgviekip hlidlginav
      181 ellpiqefne neyqklfpnq ekqlynywgy stvnffspmk ryaseensgv viqefktmvr
      241 elhrhgievi idvvfnhtae ggkkkpgfcf raladeiyyi qdeekqykdy tgcgntvnsn
      301 hpvvrefild clrywvvemh vdgfrfdlas altrdeqgip vplppvieai sedpilskvk
      361 liaepwdagm lyqvgdfypq knrwcewngr yrdsirrfik gtdhqkgefa trisgssdmy
      421 gngraptssi nfitvhdgft lrdlvsynmk dnlsngednr dgtndndswn cgeegvtena
      481 qilqlrerqm rnfhlilmls qgipmllmgd eyghtkkgnn ntwcqdneln wflwdqlknh
      541 nafyryykel ihfrhahpil qrstflepdd idwhgeepfq pqwevdnrfi aftlknpnkk
      601 gtlyaafnad gfpikvyipa splstqwywi vntskdspdd flenpipmnl ehyemppysa
      661 llleak
//
LOCUS       WP_284452997             230 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Parachlamydia acanthamoebae].
ACCESSION   WP_284452997
VERSION     WP_284452997.1
KEYWORDS    RefSeq.
SOURCE      Parachlamydia acanthamoebae
  ORGANISM  Parachlamydia acanthamoebae
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia;
            Parachlamydiales; Parachlamydiaceae; Parachlamydia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Parachlamydia acanthamoebae"
                     /db_xref="taxon:83552"
     Protein         1..230
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26757
     Region          73..>158
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mdedsdtywq llklnfkvky rnfkefcaiv rrfyknrqfc qcdllllrey lwqnpfaisk
       61 kflirhgekn vhaygetplt slakiaeacq itpkdvvyel gcgrgrgcfw lhcfyqcrvv
      121 gidfvpsfiq kaekvrkrcd leaidfrced msksdfsggt vfylygtcle dslikklikk
      181 fkqlpsgtki mtvsyplsdy ssgfnlhrtl svpftwgegi vyiqevkksk
//
LOCUS       WP_284453021             198 aa            linear   BCT 25-DEC-2024
DEFINITION  STN domain-containing protein, partial [Escherichia coli].
ACCESSION   WP_284453021
VERSION     WP_284453021.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10659146
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>198
                     /product="STN domain-containing protein"
     Region          21..72
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          72..>198
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 vniapgsldk alnqyaahsg ftlsvdaslt rgkqsnglhg dydvesglqq lldgsglqvk
       61 plgnnswtle papapkedal tvvgdwlgda rendvfehag ardvirredf aktgattmre
      121 vlnripgvsa penngtgshd lamnfgirgl nprltsrstv lmdgipvpfa pygqpqlsla
      181 pvslgnmdai dvvrggga
//
LOCUS       WP_284453089             413 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Vreelandella aquamarina].
ACCESSION   WP_284453089
VERSION     WP_284453089.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella aquamarina (Halomonas aquamarina)
  ORGANISM  Vreelandella aquamarina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Vreelandella aquamarina"
                     /db_xref="taxon:77097"
     Protein         1..413
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=48026
     Region          3..408
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mgklhdktvk klikenpsvr hadgnglylm tpkrgdaywm lryttpatkl rreytigkvd
       61 dwsladarde aaklrlaikr egadpvqerq kvnqnpfktl ndlyadyyel rkreiashhk
      121 ekslyereva wrigkvelek irpvdiseil rdvatgyddn kprptlsndl mrllrnlfdh
      181 gikldvtrfn paspfrprda ggeekaanyp mtepevieff nklrvipaqf srenylacal
      241 liatctrkme llaapwlefd lenriwylpe ertkkrraid iplaepavew lnelkvrscg
      301 sdwvfparri skkartphvc entlnhalkk lfekklfsfd krrvhdlrgt artklgklgf
      361 ddnlaqrcln qlpgnrtdrv ynkhayfeer reahealcew lapivrgevs sge
//
LOCUS       WP_284453267             483 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Vreelandella
            aquamarina].
ACCESSION   WP_284453267
VERSION     WP_284453267.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella aquamarina (Halomonas aquamarina)
  ORGANISM  Vreelandella aquamarina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Vreelandella aquamarina"
                     /db_xref="taxon:77097"
     Protein         1..483
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51085
     Region          9..457
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mdftlppllt amvdrgngll wgsvliylli gaglyftvmt raiqiryfgh mfkllrssre
       61 ssggissfqa lstslaarvg tgnlagvava iyfggpgaif wmwmtamvgm atsfvestla
      121 qayktdhgdn tfrggparyi erglglrwla vlfsicliia fglafnsvqa nsiaqameqa
      181 faiptwamgl vlmaivapii fgglksiakv aelvvplmal lylilalvvv alnisdlpaa
      241 imtivqsafg ieqaaggamg yaisqaimng iqrglfsnea gmgsapnaaa tastrpdhpa
      301 aqgfiqmlgv fldtlvicta taaiiimagp ellaseesng iqltqmalss hvgewggmfi
      361 availlfaft svianysyge snieylagrr aplavmlyrl avlgmimvgs vaslgaiwnf
      421 adlsmgmmai inlvaillls piafalfkdy dtqlkagkep vfdpsqfpkl ankvdpnawp
      481 tkk
//
LOCUS       WP_284453288             335 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase family protein [Vreelandella
            aquamarina].
ACCESSION   WP_284453288
VERSION     WP_284453288.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella aquamarina (Halomonas aquamarina)
  ORGANISM  Vreelandella aquamarina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Vreelandella aquamarina"
                     /db_xref="taxon:77097"
     Protein         1..335
                     /product="zinc-dependent alcohol dehydrogenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=35539
     Region          1..335
                     /region_name="MDR7"
                     /note="Medium chain dehydrogenases/reductase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cd08276"
                     /db_xref="CDD:176237"
     Site            order(41..43,46,142,146,167..172,190..191,195,210,
                     235..236,238,257..258,282..284)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176237"
ORIGIN      
        1 mqaielqqpg gldklnvvdv aapgepgpge ikvrlhassl nfhdyavvag miptddkrip
       61 msdgagvvea vgegveefav gdavvstffp ywlegparvg dftttpgdgv dgyareqvir
      121 patwftrqpi gyshvesatl ttagltawra lvvdgglkag dtvlvlgtgg vsifalqfak
      181 lmgarviats ssneklerlr slgaehtiny retpewgkav kaltdgkgvd hvievggpst
      241 lpqsidavki gghisligil tgregdipta klmakqaklq glivgsrrhq iemidaieat
      301 nlkpiidref plseiaeafr hqesgkhfgk icltf
//
LOCUS       WP_284453656             440 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Vreelandella aquamarina].
ACCESSION   WP_284453656
VERSION     WP_284453656.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella aquamarina (Halomonas aquamarina)
  ORGANISM  Vreelandella aquamarina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Vreelandella aquamarina"
                     /db_xref="taxon:77097"
     Protein         1..440
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=47938
     Region          1..439
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mqisvfgtgy vglvagacla dvghqvicmd idanriaqls rgeipifepg lsqlvahnva
       61 agrlrfttda ahavtesdtl fiavgtppde ggsadlqyvl svaesigqhm qgyklvvdks
      121 tvpvgtaerv sdtisrvlqq rkvehpfdvc snpefmkega aiddftrgar iivgteserv
      181 kermkacyap ynrnhdklmf msvraaeltk yaanamlatk isfmnemanl aerlevdied
      241 vrrgigsdpr igyhfiypgc gyggscfpkd vhaleqaalq lgytpellka veavnqrqkq
      301 tlytklqesl gnlegkviai wglafkpgtd dmreapsral mealwaagak vqafdpeamg
      361 ecrrlygerd dlmlagdriq avkgadalvi ctewkefrtv dftwlasqln nklvvdgrnl
      421 yapsalseag vcyvgvgrks
//
LOCUS       WP_284453842             650 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Streptomyces kordofanensis].
ACCESSION   WP_284453842
VERSION     WP_284453842.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces kordofanensis
  ORGANISM  Streptomyces kordofanensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 650)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..650
                     /organism="Streptomyces kordofanensis"
                     /db_xref="taxon:2898276"
     Protein         1..650
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=68165
     Region          1..459
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          575..640
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(597,606..608,615)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            607
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mfdtvlvanr geiavrvirt lralgvrsva vfsdadagar hvreadtavr igppaagesy
       61 lrvdrlleaa artgaqavhp gygflaenaa faracaeagl vfigppadai almgdkirak
      121 etvraagvpv vpgssgsgls dgelaaaare igmpvllkps aggggkgmrl vrdeaalade
      181 iaaarreara sfgddtllve rwidrprhie iqvladghgn vvhlgerecs lqrrhqkiie
      241 eapsvlldaa traamgeaav qaarscgyrg agtvefivpg gdpsqyyfme mntrlqvehp
      301 vtelvtgldl vewqlrvaag eelafrqddv tltghavear lcaedpargf lpsggtvlal
      361 repqgegvrt dsglsegtev sslydpmlsk vivhgpdrat alrrlraala dtvtlgvptn
      421 agflrrllah pavvsgdmdt glvereadal vpdgvpeevy eaaaavreea laarpdgrgw
      481 tdpfsvpsgw riggerlpvt hhlriagldp vahrvratgr tvtadrvtvt ldgvthtfhr
      541 agtwlgrdgd gwnvldhdpv aasltgsaha gadsltapmp gtvtvvkvav gdevaagqgl
      601 lvveamkmeh visaphdgtv veldvtpgtt vamdqvlavv ephaaqedak
//
LOCUS       WP_284454433             219 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase, partial
            [Cupriavidus campinensis].
ACCESSION   WP_284454433
VERSION     WP_284454433.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus campinensis
  ORGANISM  Cupriavidus campinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 219)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Cupriavidus campinensis"
                     /db_xref="taxon:151783"
     Protein         <1..219
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
     Region          1..205
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 dgmgghavgd fasraivqal sglgppgsld galddartal lavnqalide aarmkvrvig
       61 stvvamlace rrcgclwagd srlylfragh lkqltrdhsq verlrargli taeeakhhpa
      121 hntitravga atrldldvlt levgdgdmfl lcsdglsnev edagiaavla asagdcaaaa
      181 nelvqqalvn gghdnvsvvv lraedigggs dmtllnpev
//
LOCUS       WP_284454454             215 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Cupriavidus campinensis].
ACCESSION   WP_284454454
VERSION     WP_284454454.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus campinensis
  ORGANISM  Cupriavidus campinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Cupriavidus campinensis"
                     /db_xref="taxon:151783"
     Protein         1..215
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24269
     Region          101..209
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mehagpsygl wtlvvlnvai fvmfafsffk pasardwrsf gaftafival fvemygfplt
       61 iyflsgwlgq tfpgvdllnh naghllellf gwggdphlgp fhilsylvlg ggfwllaaaw
      121 pvlyeaqrqg qlactgvyar vrhaqyiafv limfgfllqw ptlltllmfp vlvvmyarla
      181 hneeqesarr fgqaweeyaq rvpcfiprwg araqp
//
LOCUS       WP_284454553             633 aa            linear   BCT 25-DEC-2024
DEFINITION  ABCB family ABC transporter ATP-binding protein/permease
            [Cupriavidus campinensis].
ACCESSION   WP_284454553
VERSION     WP_284454553.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus campinensis
  ORGANISM  Cupriavidus campinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 633)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Cupriavidus campinensis"
                     /db_xref="taxon:151783"
     Protein         1..633
                     /product="ABCB family ABC transporter ATP-binding
                     protein/permease"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=70206
     Region          12..616
                     /region_name="ATM1"
                     /note="ABC-type transport system involved in Fe-S cluster
                     assembly, permease and ATPase components
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5265"
                     /db_xref="CDD:444078"
ORIGIN      
        1 mrrystsads ppesakslfp aggkprsdwq tvrnllpyvw hykwrvmlal tclvaakvan
       61 lgvpvlmkkl idsmniapgd taallvvpvg livaygvlrl sgtlftelre ilfskvtqsa
      121 vreialqvfr hlhalslrfh lerqtggmsr diergtrgiq slisyslysi lptlvemslv
      181 igffvvrydi wfaaittcal vgyivftivv tewrthfrrk mneldsranq kaidsllnfe
      241 tvkyfgneey earrydenlr tyrtaairsq nslsflnfgq qtiialglil irwratggga
      301 agtltlgdlv lvntlmiqly iplnflgviy reikqsttdm drmfvllgtn qevadtpgal
      361 plqvrgaevr frhvgfgyes nrvilddvdf tiaagtttav vghsgsgkst larllfrfyd
      421 vtrggievdg qdirnvrqss lrasigivpq dtvlfndsiy yniaygrpea trdevieaar
      481 aaqidtfire lpqgydtpvg erglklsgge kqrvaiartl lknppilvfd eatsaldsrt
      541 eqaiqaelmr laqnrttlli ahrlstvvha dqilvmdhgr ivergthael mrangryaem
      601 wliqarsaae gaveaaspsd vlaidvgdat qda
//
LOCUS       WP_284454557             132 aa            linear   BCT 25-DEC-2024
DEFINITION  tautomerase family protein [Cupriavidus campinensis].
ACCESSION   WP_284454557
VERSION     WP_284454557.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus campinensis
  ORGANISM  Cupriavidus campinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Cupriavidus campinensis"
                     /db_xref="taxon:151783"
     Protein         1..132
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=14647
     Region          2..59
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mphinlqisg qpdaeltrra aatvaeltqr ilrkeenvia vtvgylpreq wiiggkalse
       61 rsdgrnafql disvtdetnt kaekaeylrq sfaalselig dvnevsyiyv idaraaaygy
      121 ggktqefrhq hr
//
LOCUS       WP_284454677             313 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Actinomadura madurae].
ACCESSION   WP_284454677
VERSION     WP_284454677.1
KEYWORDS    RefSeq.
SOURCE      Actinomadura madurae
  ORGANISM  Actinomadura madurae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Thermomonosporaceae; Actinomadura.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Actinomadura madurae"
                     /db_xref="taxon:1993"
     Protein         1..313
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=33024
     Region          9..311
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 maalpllngl rvpvfcapmf lvsdpdlvva actagvvgtf nhlnartagd ferwmdeita
       61 rldearradp grtvapfavn vavrrapree rydhdmevir eyevplvism ngsprriaet
      121 vhgyggvlih dvpsvelark avdagadgli alcggagght gtaspfalvp qirrffdgpl
      181 alagavsdgr giraaqslga dyaymgtrfi atqecgvpta ykellvsqgt edvvatdait
      241 glqanflrgs ivgagldpaa lpapkglfqp aipedikgwr dvwsgghgvg liddvpsvae
      301 lvdrlrreyl ats
//
LOCUS       WP_284454683             226 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Actinomadura madurae].
ACCESSION   WP_284454683
VERSION     WP_284454683.1
KEYWORDS    RefSeq.
SOURCE      Actinomadura madurae
  ORGANISM  Actinomadura madurae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Thermomonosporaceae; Actinomadura.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 226)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 226)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 226)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10543770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Actinomadura madurae"
                     /db_xref="taxon:1993"
     Protein         1..226
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23832
     Region          77..>182
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
ORIGIN      
        1 msgtdrhqrp paevrfaeel drlreddsgp vppgwalslt aarrfivgde algvtrkfvg
       61 dtalidralv tlatsrglml vgepgtaksl lseliaaavs gastltiqgg aattedqiky
      121 swnyallvse gpstrslvpa plltgmaegk ivrfeeitrc plevqdslls plsdrvlavp
      181 elsravaggr ggrpptqnra rtrwcsrgtg stssrprtpa tgastr
//
LOCUS       WP_284454696             898 aa            linear   BCT 25-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Actinomadura madurae].
ACCESSION   WP_284454696
VERSION     WP_284454696.1
KEYWORDS    RefSeq.
SOURCE      Actinomadura madurae
  ORGANISM  Actinomadura madurae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Thermomonosporaceae; Actinomadura.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 898)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Actinomadura madurae"
                     /db_xref="taxon:1993"
     Protein         1..898
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=95348
     Region          30..880
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mparrhhagt atgtaeisad preplpllrk elgtgdggls greavrrlav ygpnqvrrre
       61 krsllrllst qllhplalll wgagalafva gmpvlgwail avilvnavfa llqehqaera
      121 vealaaylpe qarvvrdgrr qavdvaglvp gdlilleegd kvpadarlad galeldlsml
      181 tgesapverv aapaeegigl lhepnlvfsg ttctggeara ivfatgghte lgriaalsqr
      241 aprgdsplet qvkkvawlia avavgmgavf lligalvglp ltdalmfaig llvanvpegl
      301 lptitlalav gvrvlarqga vvkrlsavet lgstnvictd ktgtltqnrm rlqaywtpqg
      361 gvmpseetpp aelaqaitec ttvsydqagd lqgdpteial vlgsgpdlpa rlaarddrrr
      421 avfrfdarlr lmstvaqadd hlavhvkgap eavlarcsgv drpavmavvd elarkglrvl
      481 avavrnlppd aerprrreda etglrllgla glydpprpev adavrrchda glrvhivtgd
      541 ngataaavar evgigvprlh vvpesekvhd heldelltgd geivfarssp etklkvadal
      601 rahgrivamt gdgandapal hqahigvamg rsgtdvarea stmvltddnf ativtaiesg
      661 rrvydnvrkf ilyifahavp eivpflvfal sggliplplt vlqilaidlg tetlpalalg
      721 repaepgimd rpprsssqgv isrdmliraw gylglvsaal vmfvfvyvlw ragwhpgdst
      781 gdgaalhhay ltattatfag lvtcqigtam aartdhaslr qtglttnpll lagiafevgf
      841 aavviylppf qhlfgtaalp wdvlaiiatf piivwatdel rrrhrrqhtr ptndvtkp
//
LOCUS       WP_284454756             669 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA-transferase family protein [Actinomadura madurae].
ACCESSION   WP_284454756
VERSION     WP_284454756.1
KEYWORDS    RefSeq.
SOURCE      Actinomadura madurae
  ORGANISM  Actinomadura madurae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Thermomonosporaceae; Actinomadura.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17584058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Actinomadura madurae"
                     /db_xref="taxon:1993"
     Protein         1..669
                     /product="CaiB/BaiF CoA-transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=73936
     Region          13..410
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
     Region          445..>627
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 msttnqvaar pfldgirvle lanelgeycg kllaglgadv vkveppegee trrygpfhhd
       61 vpdpdrslcf whfnlgkrsi vldldsaqgr aefaglaeta dviidsrprg yldergigye
      121 rlresnpali hvrispfgdt gpwaghvgsd lvhlalggvm mncgydpdps gcydtppvap
      181 qmwqsyqiag emavmavlga ltyrlrtgrg qtldtsvhqa vsanteldtp dwvllrmehh
      241 rltgrhsmpd stvpslaitk dgryvmpyrt ylksfgtdwd anlrvlrkyg mqadlddpey
      301 rdedfrlqpm tamhindvtd tlvgrlrydr eiwrdaqaeg lpwapirrpe envdddhwqa
      361 rdtffavhhp elgetftyvg akwfcpevpw hrgprppllg ehtatvpaew raarperrra
      421 vrppresrsr daapssvsrh gkpfalsgvr vidlswmlas agagrflaam gadvikveha
      481 srwdsmrfgy gmcppggrae rdaatgpita pevtdpdrcg hfmdvnagkr gislnlkhpr
      541 gkevleelir eadmivegfs pgtmermglg yerlkelnps ivyvqqsgfg qhgtygaara
      601 fgptaqgysg ltemsglpsp fprpgsatpt stgsapttwp trcsppctaa rppvrgatst
      661 hrrrrrgst
//
LOCUS       WP_284454962             647 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Alloalcanivorax xenomutans].
ACCESSION   WP_284454962
VERSION     WP_284454962.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..647
                     /product="PhoX family protein"
                     /calculated_mol_wt=71773
     Region          30..641
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 msgewrtdpd dweaqddhpv lrsseghwls ltrrgvlkgg lglaavfvgg cavtggarpr
       61 igftplpaqt dpgfdavrvp agyravpfys wgdpidaeap rwradagndw rdqlrqagdn
      121 hdgmhyfpfa dnpnghgllv inhekvatdf lhprgatvlh deqgrprrpd eevnkelaah
      181 gvsvieiakd rdgqwrrimt ssynrrisgl tpmilsgpaa gaeamrtasd ptgrrvigtf
      241 ancalgytpw gtylaceenw pnyfvnrdae dyrrrpqqar yrlsqgersn yylwetaqsr
      301 fdatpdrslp hqgevnepnr fgwvveidpf dpdstpvkrt amgrlvreca tpsladdgrm
      361 afyfgddtrg eyiykfvprd ryraddpaan relldhgtly vavfhddgrg ewrplrhgqg
      421 plnaangfpd qaavlinarg aadllgatrm drpewvavrp gsrevyvtlt nndecgvddg
      481 qpvnaanprp rnlhgqilrw rerdndpaat vfdwelflla gypaggeapa hqwgtiqgdv
      541 fsspdglwfd pagrlwietd yddespdhqa mgtnqllcad pdsgevrrfl vgprgceitg
      601 itgtpdgrtl wvnvqhpgis ypasdghtrp rsttvlitrd dggeigt
//
LOCUS       WP_284455106             127 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Alloalcanivorax xenomutans].
ACCESSION   WP_284455106
VERSION     WP_284455106.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..127
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13833
     Region          6..123
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 myleperhrs paisltplid vvfillvffm latrfgawkd lpvsvvpsea verqddktwl
       61 elhvnaegkv dwngevlsle qlgerlaghd eavlitgdpd aplqaalaav dvaraaglke
      121 vqlellp
//
LOCUS       WP_284455115             232 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Alloalcanivorax
            xenomutans].
ACCESSION   WP_284455115
VERSION     WP_284455115.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 232)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..232
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26314
     Region          1..>222
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mqraerlivl vdtlrrhrwp vtasalgeql gvstrtiyrd iqsliglgap idgeagvgyl
       61 lrkgffmppl mfspveleal llgarwvgqq gdkeladaan saldkiatav ppalrevled
      121 tglwagpssa prrgeplfvl rralreelkl rivyrdvegr eternvwplt laffegaril
      181 aawcelredf rhfrtdriad lqvmeesypg srrllaqrwl qaerqrrsrk es
//
LOCUS       WP_284455168             403 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Alloalcanivorax
            xenomutans].
ACCESSION   WP_284455168
VERSION     WP_284455168.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..403
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43434
     Region          1..395
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mfellkgirv ldlstvvlgp fashlladlg advikveape gdifraaapa rhtgmgagfl
       61 nlnrnkrslv idlkttegqa tlhklikgad vllhnvrpaa aqklgiddat vrslnprlvy
      121 caavgfggdg pyaddpaydd imqaisglas lnhtpdsppa faptvladkv aglyatigia
      181 aallhrertg qggsveapmf eslvsfllae hlsghvfqpp lgslrydrlm tpyrrpyrta
      241 dgylavlpyt srhwqrflgl vgrhdlanad wvldpsrrse rigelyqvaa ecmpaqttay
      301 wlaalkeqdi pcgpvntled llddphlqav dffqeidhps egkllgtrhp lrfigavthp
      361 drpaprlged sqsvladagf sdaeiralra ravvsmpaan dpg
//
LOCUS       WP_284455185             545 aa            linear   BCT 25-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Alloalcanivorax xenomutans].
ACCESSION   WP_284455185
VERSION     WP_284455185.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..545
                     /product="long-chain-fatty-acid--CoA ligase"
                     /EC_number="6.2.1.3"
                     /GO_function="GO:0004467 - long-chain fatty acid-CoA
                     ligase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=59082
     Region          21..536
                     /region_name="FC-FACS_FadD_like"
                     /note="Prokaryotic long-chain fatty acid CoA synthetases
                     similar to Escherichia coli FadD; cd05936"
                     /db_xref="CDD:341259"
     Site            order(194,197..202,204..205)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(197,315..316,337..342,423,435,438,449,530)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(197,240..241,288,290..291,294,315..316,337..342,423,
                     435,438,446..449,511)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(240,290..291,294,315,446..448,505,511)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mtasqapsqv rgaaafaaep vyqaleetaa rfpqrpalyf egvrlsyadf hrlvnraarg
       61 fqdlgvkpgv hvglflgntp hyaiaflgvl raggtvvnys pldaertlah kiedshsdim
      121 vtldvpellp rirgfletsr lrtlvvgtpt dfagagatsd ameavilsfa dllnnegdfq
      181 pypvadpent lavlqytggt tgvpkgaelt hgnltcgcqq lmaalagdlq tgqervlavl
      241 ppfhiysmtv nllfgirlaa elylhsrfdp davlkavheh rlsvlpavpt mfialihhpq
      301 vgeydltslr lcnsggaplp vevqqrfqel tgcrlgegwg mtettavgty tpltgerppq
      361 gscgclvpgv smkiapmdae gslaagerge icvagpnvmp rywnnpdatt asftedgyfr
      421 tgdvgymdqr gyvyivdrtk dmilcsgynv yprvieeaiy ehpdveevsv igvkdsyrgq
      481 spmafvrlrq saasltlesl qdfladrlgk hemvralalr delpktpvgk lskkelydet
      541 asfsl
//
LOCUS       WP_284455193             276 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family oxidoreductase [Alloalcanivorax xenomutans].
ACCESSION   WP_284455193
VERSION     WP_284455193.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Persson,B. and Kallberg,Y.
  TITLE     Classification and nomenclature of the superfamily of short-chain
            dehydrogenases/reductases (SDRs)
  JOURNAL   Chem Biol Interact 202 (1-3), 111-115 (2013)
   PUBMED   23200746
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   6  (residues 1 to 276)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10793067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..276
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29649
     Region          1..274
                     /region_name="PRK08278"
                     /note="SDR family oxidoreductase"
                     /db_xref="CDD:181349"
     Site            order(13,15..18,37..39,46,69..71,97..99,120,147,164,168,
                     192,196..197,199,201..202)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187663"
     Site            order(74,109,111,114..115,118,123,126,130,133,151,153,155,
                     162,166,173..174,176..178,180..181)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187663"
     Site            order(121,149,164,168)
                     /site_type="active"
                     /db_xref="CDD:187663"
ORIGIN      
        1 mstlsgktlf itgasrgigk aiglraardg anivlfskta ephpklpgtl ytaaeemqea
       61 ggktlvcvgd irheedvada vqqaeetfgg ldilvnnasa isltstests mksydlmhqv
      121 nargtflasr lclpllrrae nphilmlspp lnlnpawfgr hlaytmakyg msmcvlglad
      181 eyrnrvgvna lwprtaints avrnllggeq svqasrqpsi madaahaili qpanqcsgnf
      241 fiddevlaae gvdldrykvd pslsddqllp dfflds
//
LOCUS       WP_284455195             441 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC1 kinase family protein [Alloalcanivorax xenomutans].
ACCESSION   WP_284455195
VERSION     WP_284455195.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..441
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0004672 - protein kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=49058
     Region          13..421
                     /region_name="AarF"
                     /note="Predicted protein kinase regulating ubiquinone
                     biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport
                     and metabolism, Signal transduction mechanisms]; COG0661"
                     /db_xref="CDD:440425"
ORIGIN      
        1 makrirnpla gggrllkltg mttsiatrva thqvkswfqd dalretnrea lmrhigreva
       61 atlgemkgav mkvgqiasqm qdilpkeise qlavlqnasa pmpfhvirrq lethlggklg
      121 dhfrefsetp faaasigqvh davtrdgesv vvkvqypavr ssidsdmrhl krilrlgsll
      181 kvneaaldsv fqeirsrlne eldyhqearn lnhlrefhrd qpwlviprvh aslsgeavlt
      241 lsredgvplh qvndengfdq plrnllgerl fdalaaeifq lgtvhcdphp gnfafrrdgs
      301 ivmydfgavk qlseedielf gkvinaatkg dwehldagli elgarrpdsh pppgfydrwv
      361 plilsgfspe pvnfadarvh ldivetarkt plsalltfqp ssrtllverv vsghywtmka
      421 lgvhsaflpr lqssmamskv g
//
LOCUS       WP_284455235             530 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Alloalcanivorax xenomutans].
ACCESSION   WP_284455235
VERSION     WP_284455235.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 530)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 530)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 530)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..530
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58109
     Region          27..528
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mpvtadrrpd ryliiagala lavllpvsvl lsawrgdese twrhlvdtvl wrllghtawl
       61 vigvgigvll lgvslawlva tqdfpgrrvl dwalllplam psyvlafvvv qgldyagpvq
      121 tvlrqwwpgf sgfsarhpfw viatlslvfy pyvymlarla fltqgravme qarllgrgpw
      181 aaffqvalpm arpaiaagla lalmetladf gavsvfnfdt fttaiykswy glfnlaaaaq
      241 lasllllfvl lalwlerrgr grarygdrgg rpmvavrsrw awlmtcyagl vvvlafvlpa
      301 grllywtldd vargldarfm slalrtltlg isagvlvvgl asvlawlqrl rphrlmralv
      361 rtatmgyalp gsvlavgivi gfaaidrqlg qwfgwrqllv gslgalflay virfmavafg
      421 pvesalervr palleaartl gappleaarr vllpmvapgl italllvgid imkempatll
      481 lrpfgwdtla vriyeltaeg ewqraalpsl alvavgllpv yllvrrlrhs
//
LOCUS       WP_284455299             409 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Alloalcanivorax
            xenomutans].
ACCESSION   WP_284455299
VERSION     WP_284455299.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..409
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44820
     Region          32..400
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtrlslpagf nasavtvprh ltpvtdrgde caaaeaglrp qqvatiwrhv rglyrtgmnp
       61 aialclrrrg qvfldrtlgy adagqqrllt tdtpiclfsa skavtamlvh hlaergeldl
      121 drpvchyipe ygamgkhrtt lmhvlthrag vprihepvaa edlfdyerim tllcrakpen
      181 pgrqqayhai tagfvlgevi rrvtgesida lldrvirrpm gmryftyglr epavapaena
      241 vtglqlppvn aflthavgap leevvglsnd prfldatipa gnlyataeea crffqmlldd
      301 gryqdqqlfr petvrfatgr aatkggrldr tlmvplafsp gfmlgarals lygpgtsnaf
      361 ghlgfisiyc wadrdrdlsg allttgkaal grhfpallkl qmainrhta
//
LOCUS       WP_284455359             268 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Alloalcanivorax
            xenomutans].
ACCESSION   WP_284455359
VERSION     WP_284455359.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 268)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..268
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29138
     Region          8..262
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtdntatttl itgaasglgw alaqvafqrg hrlilvdrda malankseql aamdpsrvth
       61 faldltdgpe rdclieriaa rgrldvlinn agithrslaa rtelrvfrqv mavdweapva
      121 ltlgclpllr dsggcvinig smagwmpvlg ragycsakaa laqffevlrg evadqgvgvl
      181 mvypsflatp iesnalgfdg kpaaharssv grvrsagwma ervmdaferg ekrlfpdrft
      241 lmasllwrla pdlyhrlmrr rfavelns
//
LOCUS       WP_284455404             556 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Alloalcanivorax xenomutans].
ACCESSION   WP_284455404
VERSION     WP_284455404.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..556
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=62280
     Region          3..414
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mfqnfrlama wvhtwfglfl gfvlmvvfff gslsvfdrei drwaipesrf epqpmpsfde
       61 ilkpvfedmq psresvdqmr srvdgpmpeh fdtpvrwgvy tthrdpvlgl fagyqvpnah
      121 npdelvwgtr tidprtgesl pddqlkigsr ffyplhysln lhwkdlgywi vglaalimlv
      181 alvtgvimhr klfrelftfr pnksnqrsil dlhnltgvva lpfhfmfaft glvifagiyf
      241 pvthtqlepl hdlhevmesq etglpherag vaapiasvda mvaeaqrrwa ardmagdvgf
      301 lalqhvgdan gyvsiyragt drialtgegi hfnastgevl redpppsave ridefltglh
      361 lqhfrhwllr wlyvlggltg caciatgflf fvekrkrqha krgqigsrvv dalavttvtg
      421 mliatlgili anrllpvslp argtweqycf wgiwglamvh afwrtapvar arlapawgeq
      481 cwaiavlavs avvlnwittg dhllktlgqg ywpvagvdlf mlvsalvavl tarrlqrrar
      541 pqpadsgels geaaha
//
LOCUS       WP_284455413             313 aa            linear   BCT 25-DEC-2024
DEFINITION  FecR family protein [Alloalcanivorax xenomutans].
ACCESSION   WP_284455413
VERSION     WP_284455413.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20752687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..313
                     /product="FecR family protein"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0016989 - sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35127
     Region          14..56
                     /region_name="DUF4880"
                     /note="Domain of unknown function (DUF4880); pfam16220"
                     /db_xref="CDD:435227"
     Region          103..313
                     /region_name="FecR"
                     /note="Periplasmic ferric-dicitrate binding protein FecR,
                     regulates iron transport [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG3712"
                     /db_xref="CDD:442926"
ORIGIN      
        1 mspmqehrpp pldqeanrwl ahlhsgrare qdhqdldrwr rrspaheaay qraqtlwrhl
       61 galsldgvsl dngaemaapr rqrrllplal aaavvlalvf lgqspwrlwr adlrtaageq
      121 lsrdladgsh lvlngnsaan whlddvsrri ellrgealfq vaadrqrpft vqagdarirv
      181 tgtrfnvare gddvlltvie gqvlasdrrh retlnpgqav rwkdgglqdp vsvdaawaea
      241 wtrgrlivrd lpleevvrrl eryqdtpiwv lgdarhrrvs gvfdtgdpaa mltalaasls
      301 ihqyrlpgli ilr
//
LOCUS       WP_284455409             486 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Alloalcanivorax xenomutans].
ACCESSION   WP_284455409
VERSION     WP_284455409.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..486
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53889
     Region          1..486
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 msspygfhfd ngytrlperl farceptpva apvgvlfnta lagqlgldas tldspdgaal
       61 lagntlaess epiaqayagh qfgypnmlgd graillgeql tpdnqrrdiq lkgagrtpfs
      121 rggdgraalg pmlreylise amhalgiatt rslavvatge pvyretvlpg ailarvaash
      181 lrvgtfqfaa gqrdpellat lvdytlqrhy pelresdnka lalldsvmer qldlivhwmr
      241 vgfihgvmnt dnvtlsgeti dygpcafmdq yhpdtvfssi dhqgryaygn qpaitqwnlt
      301 rfaetllpli dtdtdtavqk atnvirsfsg rydakwlamm raklglfgdd pvdatliqdl
      361 ldwmqrrqad ytntfrdlig etapvegiyq deafenwhqr wqarlsrnak plkssfclmr
      421 nnnpaviprn hkveealnaa vrdddlgpth rlldalshpy qdrddiddyr qppkptervl
      481 qtfcgt
//
LOCUS       WP_284455536             181 aa            linear   BCT 25-DEC-2024
DEFINITION  1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase
            [Alloalcanivorax xenomutans].
ACCESSION   WP_284455536
VERSION     WP_284455536.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Ju,T., Goldsmith,R.B., Chai,S.C., Maroney,M.J., Pochapsky,S.S. and
            Pochapsky,T.C.
  TITLE     One protein, two enzymes revisited: a structural entropy switch
            interconverts the two isoforms of acireductone dioxygenase
  JOURNAL   J Mol Biol 363 (4), 823-834 (2006)
   PUBMED   16989860
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Dai,Y., Wensink,P.C. and Abeles,R.H.
  TITLE     One protein, two enzymes
  JOURNAL   J Biol Chem 274 (3), 1193-1195 (1999)
   PUBMED   9880484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..181
                     /product="1,2-dihydroxy-3-keto-5-methylthiopentene
                     dioxygenase"
                     /EC_number="1.13.11.53"
                     /EC_number="1.13.11.54"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0010308 - acireductone dioxygenase
                     (Ni2+-requiring) activity [Evidence IEA]"
                     /GO_function="GO:0010309 - acireductone dioxygenase
                     [iron(II)-requiring] activity [Evidence IEA]"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /GO_process="GO:0019509 - L-methionine salvage from
                     methylthioadenosine [Evidence IEA]"
                     /calculated_mol_wt=20489
     Region          1..181
                     /region_name="Adi1"
                     /note="Acireductone dioxygenase (methionine salvage),
                     cupin superfamily [Amino acid transport and metabolism];
                     COG1791"
                     /db_xref="CDD:441396"
ORIGIN      
        1 msnlkifrdg epdnpqlvvd skaamavela kvgiryeqwe atkpltaspp qeevleayae
       61 didrlkreeg yqtvdvvsmq pdhpdkaafr ekfldehrhs edevrffveg qglftlhied
      121 qvyevlctkg dlisvpanta hwfdmgpnph fvairlfnnp egwvanftgs diagrfsrle
      181 n
//
LOCUS       WP_284455637             400 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Alloalcanivorax xenomutans].
ACCESSION   WP_284455637
VERSION     WP_284455637.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..400
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=45461
     Region          1..400
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mtvrrrfvvl hryiglvmsg fliiagltga llvwyyelda linpqwlrve ppathsepls
       61 pfvlrekvde afptaavnwm mltspdahsp vrffiapepg taalpidevf vdpysgnilg
      121 grlwgditqg vtnlmpfvhr lhhslalgtl gtwafgivsl lwildcfiga wltfpprqsr
      181 ngpprprrfw krwipawkvr whapphkrhf dlhragglwp walllvfaws svamnlhaei
      241 yrpttetfla fqedplihvp vrelpsrhpq igweqgfria rqrletlaae rdfsieaver
      301 faylpdknal klmartgrdv nqrfgetwvy vdattgsplg hylptgeasg dtlttwlttl
      361 hiatvgglpy rlvvtllglv vamlsvtgvm iwwrkrkarr
//
LOCUS       WP_284455639             304 aa            linear   BCT 25-DEC-2024
DEFINITION  FecR family protein [Alloalcanivorax xenomutans].
ACCESSION   WP_284455639
VERSION     WP_284455639.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20752687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..304
                     /product="FecR family protein"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0016989 - sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33452
     Region          9..53
                     /region_name="DUF4880"
                     /note="Domain of unknown function (DUF4880); pfam16220"
                     /db_xref="CDD:435227"
     Region          86..272
                     /region_name="FecR"
                     /note="Periplasmic ferric-dicitrate binding protein FecR,
                     regulates iron transport [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG3712"
                     /db_xref="CDD:442926"
ORIGIN      
        1 msdlnrirqq aaewvvalqe agsdertrlq aeceiwqaed prqrqvleqi qriwqapepa
       61 lerrrkrrrq ltglgsllll awsgtqlpwa ywgadyrtaa geirtvplpd gsqivlnsns
      121 amdldytega rtvklvrgel latvakgrdt pfqvetrdis atalgtqytv kladtysrva
      181 vqestvavts hnsgatlrla sgqqadlnrd gliaqstapt hrpdwangql vfnstplprv
      241 ierlghhrag ilaldealga sqppphftgv lpaddsdaal allsdaldle vkhftpwyvi
      301 lsrk
//
LOCUS       WP_284455656             355 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Alloalcanivorax
            xenomutans].
ACCESSION   WP_284455656
VERSION     WP_284455656.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..355
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=39826
     Region          1..65
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          185..279
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 migerlkrar aaaglsmral aekagvsanm ikkyehdqsm pgsraliala kalnvrseyf
       61 frsveiqleg veyrkrastp agllkriead ildqaerwqe lanlwpsfpv psfempsdlp
      121 eavssleqvd alacqirsvw rlginpipdl vaeleskgil viltdvddls kfdglqasva
      181 naplivvsah wpgdrqrftl ahelghlllh grlgpeldee kacnrfacaf llpdsglfeh
      241 lgkrrhhlep qelymlkhec glsmaaclrr aydlavisda yykktqiffg kngwrkkepg
      301 dpypqerttl fpqlvyralg eeiigeskaa ellnmplsrf hrerqmelig esadq
//
LOCUS       WP_284455693             283 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Alloalcanivorax xenomutans].
ACCESSION   WP_284455693
VERSION     WP_284455693.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..283
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31118
     Region          83..188
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mswifclllv lmlipgaltl vfyllwyydr rafpsptpad retalrplpa llavareais
       61 ltvlvlsypl rlvqdaspqr srqqgqkpii lvhgyggnst nflwlqwwlr rrgwanvysv
      121 sytpphinar klaqqvadhv nrilaltgae kadlvchsmg gplaryalkn lglagkvdrv
      181 itlgsphrgs risalfaprg aaaqmrydsp fikeleegga cpggaryqvi ystmdnfilp
      241 assalldgae rtvhvpylgh callysrrva ravaeglqde slg
//
LOCUS       WP_284455736             305 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Alloalcanivorax
            xenomutans].
ACCESSION   WP_284455736
VERSION     WP_284455736.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..305
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32904
     Region          1..305
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mnitvifnpt agggrdrrlr hfirtleqgg arvrlyhtrs pgdairylkg ledqgdcvva
       61 aggdgtvnev lnglrpgval alfpigtanv lakelglprh peaaakvvls grslpvtpat
      121 lngrrfmvmc gvgydawvvd qvdlilkrri gklayalsmi rqlarygkvs yrvavdgrpl
      181 dcfsavitng ryyggsfvls rqaniarakl qvllfqrsgv wfllgclval mlgrlerrdg
      241 vasvsaekvt vevsrylags evrpvgevaw prpgpepiqa dgdpagwlpa eialenqavl
      301 vrvpq
//
LOCUS       WP_284455846             295 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Alloalcanivorax
            xenomutans].
ACCESSION   WP_284455846
VERSION     WP_284455846.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 295)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..295
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34034
     Region          23..264
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msrsprksag dwplrwdlll ryrlieiial wegrlttnhl mrafgigrqq askdinlylk
       61 qyapgnlvyd rslkgyrpgp gftprftlga adeylqmvrt redlagafeq lavrelniem
      121 lpvpnrglrp evlrpliqac rerrrleiey vslahpepep rvihphtvvf sgyrwhvrgw
      181 ceknreyrdf vlsrigdgar lltpasrdar qdrawqtvit lrlapdprld arqqaliaad
      241 ygmedgelal ptraalvgyl lqwlrleqtp nrppeaqqiv lmnrdecrpw liggn
//
LOCUS       WP_284455939             146 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Alloalcanivorax xenomutans].
ACCESSION   WP_284455939
VERSION     WP_284455939.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 146)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 146)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008128
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..146
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15491
     Region          1..146
                     /region_name="CytC556"
                     /note="Cytochrome c556 [Energy production and conversion];
                     COG3909"
                     /db_xref="CDD:443115"
ORIGIN      
        1 mkkvsllipv laagllsacg kgpneaaeyr esvfkatawh fgtlgamakg eqpfdqavfe
       61 ekagivadls rlpwegftda gsadgshakp aiwenradfe gkaqdfqdaa aelaemagsa
      121 dqqalfaqvg kvgetcrach teyrer
//
LOCUS       WP_284455988             503 aa            linear   BCT 25-DEC-2024
DEFINITION  purple acid phosphatase family protein [Alloalcanivorax
            xenomutans].
ACCESSION   WP_284455988
VERSION     WP_284455988.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Klabunde,T., Strater,N., Frohlich,R., Witzel,H. and Krebs,B.
  TITLE     Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on
            crystal structures
  JOURNAL   J Mol Biol 259 (4), 737-748 (1996)
   PUBMED   8683579
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11244734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..503
                     /product="purple acid phosphatase family protein"
                     /EC_number="3.1.3.2"
                     /GO_function="GO:0003993 - acid phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=55099
     Region          69..166
                     /region_name="Pur_ac_phosph_N"
                     /note="Purple acid Phosphatase, N-terminal domain;
                     pfam16656"
                     /db_xref="CDD:465220"
     Region          174..452
                     /region_name="MPP_superfamily"
                     /note="metallophosphatase superfamily, metallophosphatase
                     domain; cl13995"
                     /db_xref="CDD:472684"
     Site            order(183,185,210,243..244,325,362)
                     /site_type="active"
                     /db_xref="CDD:277318"
     Site            order(183,185,210,243,325,362)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277318"
ORIGIN      
        1 mdsrftrrai vraillgmas stltacgggg sgssppstps tpspnqpddp etpeepecpp
       61 eetagaqppr glhaswtdhp httrtltwft dgttdpgtrv qygpvtgdad scsltneafp
      121 fevtgtahet ygvealthva tltglqagqa vryrvgsdng gwsptrvlap tringfrfch
      181 fgdhglrdas qrvlsnvedl apdffivagd lsyangdqpv wdryfdmlep laarvpvmtc
      241 pgnhenkdgg gqgyrtrvsq pgkgiyygfd ynrvhfffst ggslltdlss ttellvelaa
      301 mekdlaeawr rrrdgeidfi vfvqhytlwt ncegrdpanf alvaveeqil lrydvdlvlv
      361 ghdhvfersh pmgygklsdn gyvqvtqggg gqslyelied panwaavsrv chgftvvdve
      421 drriharsya vsdedgnlyp egeeilldef tlaprvaapt gitplstreq rparslaeld
      481 vdlnamlkht lqrnlthdmn emh
//
LOCUS       WP_284456015             322 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Alloalcanivorax
            xenomutans].
ACCESSION   WP_284456015
VERSION     WP_284456015.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..322
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=33892
     Region          10..310
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mglplslarr lrlpliaapm frvsgpelvi aacrqgvigs fptancrtve eydrwlseis
       61 aaltaedapf cpnlimrrrs lkeelacllk hkvemvitsv gapepviapl hdigclvfad
      121 vanvrhaeka iaagvdglil ltagaggqtg wangfafara vralfdgpmv laggisdgqa
      181 lwaaqalgcd lgymgtkfia treslaadgy kqmlvdsrld dimlsraftg letntlrpsv
      241 iaagldpddl ptnmteqraa alygggsghs gpkrwvdvws aghsvsgvgt ipsvaelvae
      301 tmqeyrrara etlallhtng gg
//
LOCUS       WP_284456199             364 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Alloalcanivorax
            xenomutans].
ACCESSION   WP_284456199
VERSION     WP_284456199.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..364
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39577
     Region          10..362
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mqfidlaaqq arikdkidta iqkvlahgqy ilgpevsele erladytgak ycitcangtd
       61 alqiaqmalg vgpgdevitp gftyiataet vallgakpvy vdidprtynl dpgkleeait
      121 sktkaiipvs lygqcadfda insiadkygi pviedaaqsf gatykgrksc nlttvattsf
      181 fpskplgcyg dggavftcde elatiirqia rhgqnrryhh irlgvnsrld tvqaaillck
      241 ldifndelml rqqaaenynl fleekegagi vtpyldsgnt sawaqytvqi anrdnvqeml
      301 evngfptaih ypiplnnqva vkdekanlpv gnkasenvls lpmhpylsqg eqkklvetlk
      361 dias
//
LOCUS       WP_284456242             295 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Alloalcanivorax
            xenomutans].
ACCESSION   WP_284456242
VERSION     WP_284456242.1
KEYWORDS    RefSeq.
SOURCE      Alloalcanivorax xenomutans
  ORGANISM  Alloalcanivorax xenomutans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alloalcanivorax.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Alloalcanivorax xenomutans"
                     /db_xref="taxon:1094342"
     Protein         1..295
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=32322
     Region          37..290
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mnslpqamll lpynapwdwq qfhdhfalra lagverlsre rywrsfrlan vsgwfsvspq
       61 pghdalalsy sasaipclpe lqqrvrrmfd ldaepqrigr hfaqdpylat lvarnpglrl
      121 ptafdpfeqa vraivgqqvt vkaavtisgr lvtrlgeplp vsdgtgldrl fpsaaaiaga
      181 nldgigmpgk rvqtlqhfag lvasgalhld lrhgseglie rlcalpdigp wtaeyialra
      241 fgaadafpas dlgllkaplw gadgidarql karaeawrpw rayaaahlwh dysqr
//
LOCUS       WP_284456298             382 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfotransferase family protein [Blastomonas fulva].
ACCESSION   WP_284456298
VERSION     WP_284456298.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..382
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=43644
     Region          84..329
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 malgfseivn aarekvavpd pdsdswkegl eillhdhtrq drltergemi vrnryvetla
       61 armqvdeyir rnpavldqpi drpvfilgmp rtgttmlsym ldadpanrsm lrweaynaap
      121 paapgalkad prclaevard enmlkmapkv aaahfepgdg ptecvhliaq dfrslmlavt
      181 ttvptyhdwl mftdmttafe hrkrvlqilq stnpgrwvlk mpsdslfirq lfktfpdarv
      241 iwthrdpyav vgsslgmrgn srpmfevdeg aeymrqyfpl qlalhasrpl evsaerpddi
      301 yhcyyddlva dpltqlkqiy rwlgddwtet aeagmqgwld snpqnkrgkh sysleewglt
      361 rkdlepyfsd ylrahpvark dg
//
LOCUS       WP_284456351             601 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF885 domain-containing protein [Blastomonas fulva].
ACCESSION   WP_284456351
VERSION     WP_284456351.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..601
                     /product="DUF885 domain-containing protein"
                     /calculated_mol_wt=65949
     Region          10..596
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
ORIGIN      
        1 mhspsfqlsr rtligamaas tltplpamaq gssasqalra llerseaada alnplraart
       61 gksagalfvd plgddyakal rankvvalad lkaidrtglp aadriaydvf dyqtrqtltl
      121 fdsglfevqr maplnpsfgl hiefpdflss gaapfataad ydaalvridg fvgymdstia
      181 rlkqgraqgy lqpkvivanv laqvdamlkl pveqspfwtg itrmpdsiaa derkritatf
      241 raavegkvyp ayrgwatylr dtylpdapea pglwamkggd alyawdlarh ttttrsaddi
      301 hqlglsevar iraemeavra kvgfdgdlka ffehvrtdpr yycktpeell grfkaieeri
      361 wpaiprlfha rpkapfevrp lpalgdqrgt gyyrvgppdg vspgilffnm smlgtrpipt
      421 letltlhegi pghhfqltla aenadlppll rhgqatayte gwglyaeslg selgmftdpm
      481 qlfghldmem lravrlvvdt gihakrwgrq qaidymlant smaprdvvve idryiaypgq
      541 acsykigelk frelrtaaak algprfdird yhhqvlstga lpmdvldaki rswitagggk
      601 a
//
LOCUS       WP_284456353             391 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Blastomonas fulva].
ACCESSION   WP_284456353
VERSION     WP_284456353.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..391
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40810
     Region          2..382
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 meradvaiig gglvgcataw qlarkgasvv lveagdinag asgqnagslh fqierrflen
       61 gdalaeqgaq ivalsrhavi dwrtieqelg adlhvamhgg lmvaetaeqv alletkaare
      121 sreglavrtl dgdearaiap ylspgilaan fsadeghadp raitpalaea ikregatvrt
      181 gtrvqtiahv ggrfvirgdg lalsadqllv aagawsadic alinihmpiy pvallmnate
      241 rvppmvphlv qhvgrrlslk qthagnllig ggwpsrlaqt snggfdlsae aqmipesltg
      301 nllaardvvp gvtrlnlirs wtgvtaitsd qlpivgpvpr mpglwvaagg saftlgltfa
      361 rlmadammgg dadelsllsp arfehlngfm g
//
LOCUS       WP_284456483             137 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Blastomonas fulva].
ACCESSION   WP_284456483
VERSION     WP_284456483.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..137
                     /product="YybH family protein"
                     /calculated_mol_wt=15281
     Region          5..129
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 msgfrgased qlairalids ytdavfrrdp qdwgatwted alwnlagtev rgrevivalw
       61 tqamagfpfv affaqvgsil idgdratgrv ytheylelad gsvsrpigqy ldvytrtadg
      121 wrfaerhfsi lketqak
//
LOCUS       WP_284456482             461 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Blastomonas
            fulva].
ACCESSION   WP_284456482
VERSION     WP_284456482.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468627
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..461
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=52404
     Region          43..455
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
     Region          208..457
                     /region_name="RHO_alpha_C_MupW-like"
                     /note="C-terminal catalytic domain of Pseudomonas
                     fluorescens MupW and related aromatic ring hydroxylating
                     dioxygenases; cd08882"
                     /db_xref="CDD:176891"
     Site            order(216..217,221,224..225,228,230..231,233,235,365..366,
                     418..420,422..426,437..440,444,447,451)
                     /site_type="other"
                     /note="putative alpha subunit interface [polypeptide
                     binding]"
                     /db_xref="CDD:176891"
     Site            order(225..226,228..229,231..232,236,336..337,339,347,349,
                     356,358,402,405..406,412..413,416)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176891"
     Site            order(225..226,228..229,231..232,236,336..337,339,347,349,
                     356,358,402,405..406,412..413)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:176891"
     Site            order(231,236,416)
                     /site_type="other"
                     /note="Fe binding site [ion binding]"
                     /db_xref="CDD:176891"
ORIGIN      
        1 medasrtypa drcpaitvde ildldsrtvp qevrgdswrd lgtepvtaer ytsaaffeae
       61 kkhmwpnvwq maaredellq pgdyvvynnv grsylimrqd dgsvkafhnv clhrgrklrt
      121 esgsaddltc pfhgfawktd gaikhipcew dfqhlkerdm slpelrverw qgfiyvtest
      181 tqvslrdymg aevydrfgrw rldecytalw vgkvinanwk avseafmeaw hsivthpqil
      241 pytgdantry smwgdhanla ltpfglpsph laadnlsedd iiaafsrtsg rsaslegrkl
      301 aegetartam aetnranyld algydssdis dsemldafty nifpnlspwg gfvpnvvyrw
      361 rpwpdqnatl mevrllgrkp kdgampeaae mrflgpdqpw atvtewgalg evfdqdmenl
      421 pyvqeglias annrvelgry qegrirqfhq tmdkylagql p
//
LOCUS       WP_284456493             351 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Blastomonas fulva].
ACCESSION   WP_284456493
VERSION     WP_284456493.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..351
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38263
     Region          <11..343
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 metldalama dmivgnstai reirglvrfa aetrasvlit gpsgtgkelv ahalhrassr
       61 aaspfiavns gaiprelies elfghekgsf tgamarrigh feaantgtlf ldeigempld
      121 mqvrllrvle dhkvrrigsn ddvnvdvrli aathqclesa iaegrfradl fyrlnvlpie
      181 lpaladrved vpmlvqhfls rgfasdnppv ftdealailm ahdwpgnvre lknlveraav
      241 ffqgmevgtd qmamllrpar saraavaapv avelpenvva laapmaatpr farpmdlreh
      301 lqneekrvli ealestggvv saaarlvmlq rttfvekmkr yqigremals a
//
LOCUS       WP_284456498             442 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Blastomonas fulva].
ACCESSION   WP_284456498
VERSION     WP_284456498.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..442
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47467
     Region          68..>438
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mtgvrwhsvi pdspkldvta fadplftsli gafllehyki wllviglvvl lvawlplllk
       61 klplslpiif vglgmavfsf tplsvfsphp vespvmieka tefiviislm gaglkigrpf
      121 tlanwgitir llaivmplti gaialsghwi lglplasall lgaclaptdp vlasdvqier
      181 pnsddgdear faltseagln dalafpfvyl alaasagtlg fatmgtwlwq dvvwrlsvga
      241 lmgaaggwll gqiiyrlpqn trlsrtgdgf ialgatlviy attefafgyg flavfvaglm
      301 lnrsaagdnf nselhdfade terlvmmvll vlfggiltgg elladigwdn vlvaalvllv
      361 irpmigwlal idlrrpaler fviaffgirg lgsvyylafa lnhgafedqh alwetvglii
      421 lgsillhgis vtpimqrlnr ga
//
LOCUS       WP_284456565             610 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF885 domain-containing protein [Blastomonas fulva].
ACCESSION   WP_284456565
VERSION     WP_284456565.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..610
                     /product="DUF885 domain-containing protein"
                     /calculated_mol_wt=66251
     Region          6..607
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
ORIGIN      
        1 mhhtirfavs alaialavps tialapaiaa qpaeanqdaa lttfldaefe eaikqqpqla
       61 trlgrkdggd qwndigdeaa eaqlawrkas varmkaqfdr aklspeaqvn ydiwaleaer
      121 aemqqanrvy rppfysrlys ahsqlpdfli nthtvadatd lknyiarlrg ipavldvaia
      181 rtkaseaagi rapkfqieti itgsekltsg apfgdgpdaa lwadvkakte alvaagklpr
      241 aeadamlaea raaivalkpa ydrvvawara slpnapsgkv gaitlpegaa yyanelklnt
      301 tsdytaeqih sigqsevari eaeqdalakq agfkdrsayy aerarlnppr pyddaartky
      361 lttanafvah trsllepyfn slpkygievv repafsevag gaahasapsp dgsrpaktyv
      421 hlvgtvpdpa amytlmchea vpghnmqgdi qvrqtsgpkf ravtgyvafg egwalyaeal
      481 ckemnafpdi aadflrldae lfraarlvvd tgihamgwte deavaymntt grqpiersrs
      541 eirryitlpg qatgykmgml kivelrqrae sklgkkfdik gfhdlliasg sqplsilerr
      601 vddwiarsat
//
LOCUS       WP_284456513             406 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Blastomonas fulva].
ACCESSION   WP_284456513
VERSION     WP_284456513.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..406
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44328
     Region          1..406
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msifvsdpad lgfnqhller ipahinskyl esqclphaal ligrgheiah lslqgearpg
       61 qplqedaifr iasmtkpits vafmqlveeg rialsdpvhr ilpewrnlgv fvsgggnqpf
      121 vtrptsqpmr midllrhtsg ltygfqertp idaayrkhkl eafagpdlee lvrilagipl
      181 qfdpgtswny sistdilgai lqrvdnkpld qiiadrvtgp lgmvdthfqv peskldrvpd
      241 cfvfhptekm kmydsgatta wgrapsqlsg gggmastlad yhrfcrmlln ggnldgvril
      301 grktldlmis nhlpgggdlt qhskalfsea enagagfglg fattidsaat gvpgsvgdfy
      361 wggmfstaff vdpiedivmi fmtqlmpsst ypirreiktm lyaave
//
LOCUS       WP_284456634             349 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Blastomonas fulva].
ACCESSION   WP_284456634
VERSION     WP_284456634.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..349
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37640
     Region          36..333
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 madsdikpra llkraarlpv ladvalrlgf afflialvil ihwldraglk dnfdneisfl
       61 dvvyftmisv tttgfgdiap vsdrsrlies vvvtpvrvav ififvgtays fvlkrtwekw
      121 qmsriqqrlt ghivvlgfgt sgseavreli argtepgciv vidqhepsla raeamgcnvl
      181 nadaardetl rdvhidracs aivsagrddt silivltirh lapevpisvv vraadnella
      241 rqagantvin pvsfagllla gscqgphiss yladlasssg rvvliermvr peevglplkd
      301 ikdgvgvriy rdgkpygfwd desaslsagd lvvvitqgdg rppvtmand
//
LOCUS       WP_284456696            1064 aa            linear   BCT 25-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Blastomonas fulva].
ACCESSION   WP_284456696
VERSION     WP_284456696.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Rengstl,B., Oster,U., Stengel,A. and Nickelsen,J.
  TITLE     An intermediate membrane subfraction in cyanobacteria is involved
            in an assembly network for Photosystem II biogenesis
  JOURNAL   J Biol Chem 286 (24), 21944-21951 (2011)
   PUBMED   21531723
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Komenda,J., Nickelsen,J., Tichy,M., Prasil,O., Eichacker,L.A. and
            Nixon,P.J.
  TITLE     The cyanobacterial homologue of HCF136/YCF48 is a component of an
            early photosystem II assembly complex and is important for both the
            efficient assembly and repair of photosystem II in Synechocystis
            sp. PCC 6803
  JOURNAL   J Biol Chem 283 (33), 22390-22399 (2008)
   PUBMED   18550538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..1064
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=115832
     Region          71..259
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          172..355
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          523..710
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
ORIGIN      
        1 mkrvpgfigl acwlftgsav laqdanelkv aeeaeetplp ddeqayftsl twrnigpdrg
       61 grsisatgsa arpneyyfta vggglwkttd sgvswkpmtd gkldtaavgg vavceanpdi
      121 vylttgetql rgnilpgsgv wksidaaktw tkigladvqn farvridpkd cdtayvagfg
      181 hygepnaerg vfkttdggka wrkvlfrdak tgavdisidp knprtiyaal weawrkpwgm
      241 ssggegsglf rssdggeswt eltrmpgmpq tgligkigvs vspvdasrvy amiehasegg
      301 lyvsddagas wrrandsgdl rqrsfyysrl vadpvvkdrv yalnveffrs ddagktltki
      361 ktphsdnhdl widpannqrm ieandgganv svnggeswtk qayptaqmyr vsiskhfpyf
      421 vcggqqdnst icvpsrdwkh vnalgggqyg faagggesgy vtndpanpei fyagsyggtl
      481 drydrrtgqs rainvlpdnp mgysasdvae rfqwtfpivf dphdpqslyv tsqhvwrtrn
      541 egqswerisp dltradpktl gasggpitld qtgvetyatv falapsrrer gliwagsddg
      601 lvhltrdggs dwvnvtprrl panlkittie dsphadgtay ltghrhllgd fapyvmkttd
      661 ygrswtsita gipanemars iredpkrpgl lylgtergvw vsfdsgkrws klqrnlpavq
      721 vsdlavtdnd lviathgrsf wvldnigvlr qlengaprse rlfapapavr dvdegvaidy
      781 flparpkqla ldilgadgal iqsfagnpvd pkkkddkded edddpfkprp aqtttmkpgl
      841 nrfvwkmrhp gftdfpgmil wtsrnrgita vpgqyqarlt vdgevftqpf eirsdprlvg
      901 vtqadlqarf dfssrvsqrv seanaavlli rgikeqtaaa atdpaadaal rgqlsdfdtq
      961 lgaieaqlyq vrnrsrqdpl nypimlndkl agligvaesa earptdqsle vfatlsgqld
     1021 tqlaaldrli ggtlptlnaa lgaaglaqiv rrqqevpppa aqae
//
LOCUS       WP_284456725             405 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Blastomonas fulva].
ACCESSION   WP_284456725
VERSION     WP_284456725.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..405
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44135
     Region          10..401
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mesvserpia rplegvrvld lshalsgptc tsllallgad vikverpeig ddfrhyteha
       61 glpgmsipfa aanagkrsit ldlkqpaaik vvrtlaqrsd mlvenfrpgv atklgldwps
      121 lrtinpglvy asisgfgqtg tlrdwtaydh ivqamsgimw mngnpdeepm kvgfpiidtf
      181 sgymavigll salhrrdqtg egdyvdvaml dsafnlmgaa ipvyfysgev rgrtgnrgyr
      241 lvatsetykt adgyisigan hhhqiealcq vlhcewlled erfathrarv dnhdalraal
      301 sdifrehnge eveprlaarh vpvafvrnlg qvlshphfke rdifleaqlp gspepvkmvg
      361 pgfqlssgkf ssgavpslge htdailaeld ldaetlaqlk ehata
//
LOCUS       WP_284456751             389 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Blastomonas fulva].
ACCESSION   WP_284456751
VERSION     WP_284456751.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..389
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42647
     Region          134..381
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 malfeyfpny iwnlsvaiai esggqigeii dmcqpirdaa angadagtpq fmrawvetgd
       61 kliglagede ergrafsaaa kleraalyll vaermqgqgs pdraatyaka ldtfkramtl
      121 gdhavervei pyegstfpal ycrapgdgpk pvvvycngld sskellywsk lphalaargi
      181 sslcvdqpgt gealrlnnlp atphsekwas pavdwlekqp dvdparigmt gislgghfap
      241 ravafeprfa sgavwganhn waevqqkrlr regenpvphy wahvmwvfga sdmddfhaks
      301 kdmtlngvmd rikvpflvth gekdrqigle yahqsfeqlt ncpqrelkif tareggvehv
      361 gadnmsfgrd yiadwfaetl ggrtsaarp
//
LOCUS       WP_284456801             177 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Blastomonas fulva].
ACCESSION   WP_284456801
VERSION     WP_284456801.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..177
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=19676
     Region          68..177
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mpepvrggtv aamydeppql pridasiaps vgfppplvfl gfillglltd rllglpvmpi
       61 srdltwagfa lmmagimvli vslglfrayg enpepwtpsq aiiargpyrh srnpmylamv
      121 iihigyaiwd asmgvllfvp fafiaidrav iakeekylat rfgkpyedyc rrvrrwl
//
LOCUS       WP_284456769             476 aa            linear   BCT 25-DEC-2024
DEFINITION  spinster family MFS transporter [Blastomonas fulva].
ACCESSION   WP_284456769
VERSION     WP_284456769.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..476
                     /product="spinster family MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006869 - lipid transport [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49689
     Region          25..393
                     /region_name="MFS_spinster_like"
                     /note="Protein spinster and spinster homologs of the Major
                     Facilitator Superfamily of transporters; cd17328"
                     /db_xref="CDD:340886"
     Site            order(34..35,38..39,42,75,125..126,128..130,133,153,
                     156..157,160,239,242..243,246..248,251,280,284,335..336,
                     340,344,364,367..368,371..372,375)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340886"
ORIGIN      
        1 msesatrevl dqpmhapgyr awmmtllvav yasssldrli iavlgpaika dlrisdlqfg
       61 llggiafafl ytafgipvar ladrrnrivi vsiatavwsa mtalcglaan ftqllllrig
      121 vglgeagcsp pcyslisdqy pprmragaia ilglgvplgs mvgaflggwa sefiswrsaf
      181 vmaglpglll aalvyltlke pargmfdpaa srigtpppfv avlraiaakp aflhltaaaa
      241 lcifcnlgln lfiptflvrs hglsysqagl yfglvtgisa aigttglgll iarlarrdvr
      301 wygwgpalvl vagapfyilg lvqtdfaagy glilasscig faflgpsiga tqnmmeprmr
      361 asaaavllfa mhmvggglgp tfmgwasdlf aarafgvgya ascpsglapv dasssiasac
      421 naaseeglry alvacalfff waafhafmat rtmardlmpa vpqpvqtpal sqevsp
//
LOCUS       WP_284456808             516 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Blastomonas fulva].
ACCESSION   WP_284456808
VERSION     WP_284456808.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..516
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54137
     Region          53..515
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mrgtgilwel lakasetsts tskaghgpgl nrrdvlagla amglasawdg salaaagrts
       61 riaiigagla glvaldrlva agldatiyea rgriggrvlt stglpetnly vedgahlvnt
      121 nhadilalar rfniglidrg amvarerfvv dgaelseael iaevrplaar iaadatlvde
      181 dfernaprfd amsvrqyldg agaaatprar alveatirte ygsepgdvsa lelffnlpai
      241 addrvalisg sderyslagg sstipralae plmdrirtgh allsvrrkgk alvlafangq
      301 svtadrviit vpaqilrtid fgdtlppawq sltqefscgr nekinagytt rpweplvgag
      361 gaawaartge pglfsefwga sagqdsvpeg vltwffggsq vsglqdlgpe gilracerei
      421 apavpglaar tlrrtawaad pyaqgaysrf lpgqltryaa hfwsedddgk vtaplpsgai
      481 lfagehlsds htgymngaaq tgrlaanqii agvnra
//
LOCUS       WP_284456933             243 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Blastomonas fulva].
ACCESSION   WP_284456933
VERSION     WP_284456933.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..243
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25686
     Region          5..>108
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mtfdhdiima yvdgeldlvt srrieraadq dqalaamiaq qralktrlka hfdpaldepl
       61 perltrplev aaipvsdarr rfgwptfaam aaslalglvi gprllapdta letapgagpv
      121 gvrgemlvaq gglanaldrq lasaqpastd irigltfrdr qgavcrsfds aaiagiacrq
      181 ddrwalrqav agsaqstyrq agasdllaav damragdvad aaterawqag gwvaprpgrp
      241 grr
//
LOCUS       WP_284456943             547 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Blastomonas fulva].
ACCESSION   WP_284456943
VERSION     WP_284456943.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..547
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=57435
     Region          18..328
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mnaaaldhlf vgqdfaaapg cvaallegee vvwqrcfgla rldtatplta atrmriasit
       61 kpmvaltlaa ledegrlals dplsrhvpeh rfgadptlgq mlamksgvpe typlvwlglg
      121 daarlaehsq almalllaqr mlnfrpgert lyanantvll hlvaeratge plarlmqrrv
      181 fdpagmasav lddglahrlp ataiayakag egftpadpaa veaapggvia slidliawhr
      241 wlrgnphdwr arlagavrhd dgspsgyaqg fvrqslsgvp vighagghsg wasdylyape
      301 kdvaviilan radanayera reilvtalgl ppdpgatpal lgpappplwe atyasaeaia
      361 slsvsgsrge iavdgrrmpr gadglfrrtl gvepfvidaa dtaappaelk rwegnhavtf
      421 grvdapsals slavtgtyac aslphpvtik ddgkgglrvl tgpvwpggkg wplvpvsgvl
      481 frchmpdgap sevhlrfeld esgavagvtf gflrllrisl drvapdagea wraigqaapq
      541 lligdap
//
LOCUS       WP_284457001             402 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Blastomonas fulva].
ACCESSION   WP_284457001
VERSION     WP_284457001.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..402
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=43628
     Region          15..400
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mkrnagqdpa itsrwrpatr airggtvrse fgetsealfl tsgyaydcae daaarfngeq
       61 agmtysrlqn ptvemlekri slmegaeatr cmasgmaamt aallcqlqmg dhvvasralf
      121 gscrwltdtl lpkfgietti idgreldqwe aairpntrvf ffetpanptm diidmqavcd
      181 iarargitsv vdnafatnvl qrpmeygadv vaysatkmmd gqgrvlagav cgtddfitnt
      241 llpftrntgp tlsafnawvv lkgletldlr irrqsenamk vasflegrve rvnypglpsh
      301 pqhnlamaqm eaagpifsvy vgggrarahg llnalelvdi snnigdsrsl mthpsstthh
      361 glgeearmav gitedmlrln vgledvddvi edldqalrti gl
//
LOCUS       WP_284457026             675 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Blastomonas fulva].
ACCESSION   WP_284457026
VERSION     WP_284457026.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 675)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 675)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 675)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 675)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..675
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=73973
     Region          3..660
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mgmpvmsgvv qlsaavrark vvhdlfaqet ddaelaraqf lsfskqmpll ylilvcnasa
       61 vmvaffqpdl ifktfvlpas icvialvraa wwwrqdgaql fsdaeiaksn rrtcmlavvm
      121 tlafefwcmw iyssgdayar ghltfflalt qvstvfclmt mraaamrvaa sstlcfviff
      181 svvddsrmlv eavvlgcvgl gmmivthryn ldfsklirsq rdlrnrqaet eklsdenrri
      241 altdalsglp nrrqllvnld riddqtvdal dnlavlfidl dgfkdindth ghqagdslir
      301 slsvrireic pphsmlarvg gdefvvliet pqaasvaasm aerisneial pvlvdrhvlq
      361 vgasigiatn angactshel lrradtamyh vktgkkgkia vydaaldrgr lrrmeieaei
      421 gtgldkgefd vfyqpvidah sgqivateal irwprraagv lvpqqfieia eatgqihplg
      481 mfvleracrd vgplgdlsls vnvspaqfrd pgflrqvahv leqtrfpagr lqleitegyl
      541 lsqpetairt irsfkamgls ialddfgtgf tsihylrtyg fshvkidksl lvdlgpgska
      601 sflvagainl argldmevta egvetheqaa llraagcdrl qgflfgrpmp iadlramcaq
      661 gtgdlrqgpp alral
//
LOCUS       WP_284457138              65 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Blastomonas fulva].
ACCESSION   WP_284457138
VERSION     WP_284457138.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 65)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..65
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=6564
     Region          2..45
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(3,28)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(10..11,22,25,29..30)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 maraglgisg rafadmagvg yatlarfeag atvtddvrvr ieaalleaga qftrragrvg
       61 vtvpe
//
LOCUS       WP_284457160             749 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Blastomonas fulva].
ACCESSION   WP_284457160
VERSION     WP_284457160.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..749
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=73521
     Region          <17..749
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mktsiytsvs alalmiaapa vaqdntstvd qlgtaakatv vqsgsgnnsd vdqngngaat
       61 fasgpnagrt lvadvdqtgt ngvstvnqqg nrssatldqg gngmrssiiq gnsatdkgnt
      121 atviqngtgg gvgtgsfvtq tgndgqayvn qgaatngavs tvtqmgtnqr asvfqlsgaa
      181 dsnvsqagga anvfvsqdgs sesdiiqsgg nseasvrqig dgnsslvtqt gnnadagdpd
      241 nnltnfdtni gvsqtgddnt stvtqtgndq vadviqtgnl ntasitqdgn fadasvtqtg
      301 nnnigtvirq dgdgtgdnnp ltspvtpadn ataditqtgd fndasisqaa vpvdativqt
      361 gddnvstitq tstsagalat stqtsddnls tivqasdata lvtqggnqpn pgpfagrann
      421 vsdvqqqala ggssatvdqd gvlnkstitq naanstasve qdnifntsti tqtgtggafa
      481 dvsqgggygd nlstvtqtvg atatviqtgq psvgpaftnv sditqsgegg easvtqngsn
      541 nestvdqaai dgqatvnqdg tfltssitqg tpaadaranv tqtgtdndsi vsqlagasga
      601 eadvtqggsg ndstvtqsas tsafveqigd gndstvtqtg asaaglraaa dvqqlgdlgi
      661 slveqdgagn satliqtaas sgeeseilqs gdantalvtq agtgnfslvd qtgdnnaatv
      721 sqsssdnisn vfqsgngnsa vvtqgggvn
//
LOCUS       WP_284457188             548 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Blastomonas fulva].
ACCESSION   WP_284457188
VERSION     WP_284457188.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..548
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59295
     Region          5..528
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mtmtidrrll ikagtfglaa lsipgaaqal fagrgfthgv ssgepsgnsv llwtryvads
       61 darltaelsp tpdfarpvgg gsvtasaard hiakltvtgl kpdswyfyrf vaadgstspv
      121 grtrtlpvde tagfnigvfs csnlpfgwfn gyahaaarnd ldlavhtgdy vyeygldvyp
      181 trgqalpgrs vqpdhemvtl adyrlryasy rldadlqrlh qvvpmiamwd dheiandsyr
      241 dgaqnhqsds egdyatrrri aeqvyrewmp vadlapadpl wtsyqignla tlirtesrls
      301 grdkpielse afagggdiaa alarfrdekw vdparrmlgd dqarwlgaqf kaskasgtrw
      361 qvwaqqcvmg smklpletad wvprdapaiv rsrsaaglaa skaglpfnmd awdgypvqre
      421 allqsaqaad adlvvlsgds hngwgfdlda ggkpagvefa ghsisspgfe ayaptiapad
      481 vagalvrgnp qlkwadtssr gymtlqltqq satahwhklr tirerstdla essslsvlpg
      541 rrtiampg
//
LOCUS       WP_284457264             938 aa            linear   BCT 25-DEC-2024
DEFINITION  CHAT domain-containing tetratricopeptide repeat protein
            [Blastomonas fulva].
ACCESSION   WP_284457264
VERSION     WP_284457264.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   3  (residues 1 to 938)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Classification of the caspase-hemoglobinase fold: detection of new
            families and implications for the origin of the eukaryotic separins
  JOURNAL   Proteins 46 (4), 355-367 (2002)
   PUBMED   11835511
REFERENCE   4  (residues 1 to 938)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20368473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..938
                     /product="CHAT domain-containing tetratricopeptide repeat
                     protein"
                     /GO_function="GO:0004197 - cysteine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=98585
     Region          <44..235
                     /region_name="FxSxx_TPR"
                     /note="FxSxx-COOH system tetratricopeptide repeat protein;
                     NF040586"
                     /db_xref="CDD:468560"
     Region          155..183
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(156,159..160,163..164,166,196,199,201,204..205,
                     207..208,239,242..243,246..247,250)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          194..225
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          209..932
                     /region_name="COG4995"
                     /note="Uncharacterized conserved protein, contains CHAT
                     domain [Function unknown]"
                     /db_xref="CDD:444019"
     Region          238..266
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          640..932
                     /region_name="CHAT"
                     /note="CHAT domain; pfam12770"
                     /db_xref="CDD:432771"
ORIGIN      
        1 mikaavalas giglflgapa haapdrtrld alitqfeaad ansdvegyrk iadqtlaear
       61 rlypaghpei aaralyvaqa laasgemdpa kaevdriipv lagaqgykad wrnalslray
      121 ilnfkgdhag alaineqlaa eyasdpssqg irdhavtlsn laasylehgr lddalarnae
      181 airiglaldp vpqdvaiwsa nrvvyfysag rtedaivtaq egiaqaggal gtdhpamanl
      241 yanlgailmr inrphdamap irqayeliek anggpnqnsa tmrtqfaqal vragqhkdal
      301 afldyatpii daqlgaqsdr slvardtrlv alialgqgaq aealarella vrdarlpdgh
      361 rdrantrdnl akaafsienw atardaaaqa vdlrskalsp dhpdlllsra fllrvedrgd
      421 lrpatelvae arqvfealtl naqlargsaq aerqrpaygw laevfarrga addafraqqw
      481 aartalddtl aiaaselsak adpqlasllv rrrelvaarq glearidang arpdpkfdla
      541 gvsndlagnr seiaaldagl tpeqrnslmf apasvkdiqa tgargdvsim itdigdswlv
      601 taldagrvlq tlvgadapvd alvaqlrava dptgdgvldr aassqlfaal fpgetaalvr
      661 sarqlyvtan gslgslpfgl lsadragrgl lmekstivrr vgvprgrtaa faptgntlia
      721 fggvkgapar tlmamrsast artiadlpdl pdsrrelaal gqaigtgsaq llvgddatee
      781 alrratvppg avlafathgl lsgeldglse palllspagn ddgllkpsei gamnlpaglv
      841 ilsacntaat sstdrpqlag lvqgfflaga ervlashwpv rddvarrlsv stvrgmnnrl
      901 apaealrrai aqvrkgsdge paidkpalwa vfelfean
//
LOCUS       WP_284457266             646 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Blastomonas fulva].
ACCESSION   WP_284457266
VERSION     WP_284457266.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..646
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=67553
     Region          422..626
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mhfddrlttv lagdvpggaa avaqyrqlvd ilgqigasaa derhalglar ihslrsavse
       61 sdrlltvqcl sgrlvspvlv qylaaetpqi asaairaarl tdsqwaalvp alptrargfl
      121 rhrrdlgart ralldqlgly dtalpdaaaq valaepeaqs gvaepiasdp vptadlpsad
      181 visteptaea aapiadalqp deplpieala svanvatape sggpqsigei vkriealqev
      241 rfkqamedrp atavpdwnrl ghavqgdaiq adaitgdams rdatqdddrs aadeplavap
      301 esvtpeefrf stgvdgaias asgvalgavy glslalpama gfrgvdaava tafsrrmpvr
      361 ggranlggaa glsgewrida dpvfdrasgr figyngmvrr pmawesagpq ddgamlagrd
      421 glrqivhelr tplnaimgfs eiieqqlfgp vaaeyrdmal rirqdarqll sgfddldtal
      481 rldrnalddp agqvapgdlv drligrvqpl ldhagarlei galpagavia vspqaidriv
      541 prlaaaligs capdevltls faqhadaldl rfsrprslaa lnrdqlfdvd rasaghddgg
      601 pllglgfclr lvrnllaaqg gelaveadal cltlpctris aeaars
//
LOCUS       WP_284457309             103 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Blastomonas fulva].
ACCESSION   WP_284457309
VERSION     WP_284457309.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 103)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 103)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 103)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..103
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11400
     Region          20..96
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mrdmrtyqhp dlstvtieha lhalsdpvrl divrqldrei eascaaldgg rpkssmshhf
       61 rvlraaglvh triagvqhmn tlrrdevdkr fpglldavlg vkg
//
LOCUS       WP_284457384             783 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Blastomonas fulva].
ACCESSION   WP_284457384
VERSION     WP_284457384.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 783)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 783)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 783)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..783
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=85545
     Region          73..764
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mdsstlplrg rfrslatrit vwygvvialt fgafiivatd gveryaesva tkematnaat
       61 fdkilelqar qmrtsadvla adfgfreafa lddqptitsa leslrvraga plaimiplqg
      121 dfistgapmn ateqdalwea vdsgidrgvf qvggryhnav aapvlipdla gwlvlarpld
      181 aaamrelarl apagmsarir asgplpggid lsqasgrapv etrldgervl ywskplpald
      241 nslkprvvlr yelssalaey npikylllal savgltlsvl igafvsrgit rpiatlenaa
      301 reisrgsrdt vsittddevg rlaesfnsmv esikereqri thialhdelt glpnrklfae
      361 qlefalgrra sthriaimyf dldnfkavnd tlghpvgdel lravaerlrt smpgalisrq
      421 ggdefailid qiephakial ladrvsavfh safqlsdhrl etsssigiav apgdgdcpde
      481 liknadlaly rakkegrncs cffeqamdle arkrhqmeid mreavregqf llnyqplfsl
      541 eknrvmgfea lvrwqhplrg lvspaefipl aedtgmivpi sewvlneacq ragqwpddir
      601 iavnlspvlf knaglpllvm qaldkaglkp nrlelevtes lfidniertt amlnalrdcg
      661 vrialddfgt gysslnylrs fpfdkikidk sfvddlatdi ssqaiigait alasalgmet
      721 iaegvedkdq lealraqgcs niqgylfsrp vgielvdami admrytqaep geaaeparar
      781 rva
//
LOCUS       WP_284457399             389 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfotransferase family protein [Blastomonas fulva].
ACCESSION   WP_284457399
VERSION     WP_284457399.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..389
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=43184
     Region          92..332
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mtmtmtvtal dtgtllaaas aqaglsdfgd psfregfdvl vkalndearl teaasgrvaa
       61 sivatlvnrl qvedhlarhp qlldapivkp tfvfglprtg ttlainllaa dparrsfmrw
      121 eafasappaa kgelrsdpry haeqakldms lkyvphisam hhedadssce cqfamsptfc
      181 sqvydsqydv psyhawfmkt dyrpafryhk rlmqllqqdn kghwtfknpw hplyldalte
      241 iypdaqlvmt hrdpadvvas acslvyavrk lysedvdpia vaevsletfg amidrtlaye
      301 akhgagsihh iqykeltadp igemhklyth fgdaltddaa aamqnmldsn pqgkhgkhay
      361 aledygltrd kvyshfadyi erfaipvkg
//
LOCUS       WP_284457413             151 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Blastomonas fulva].
ACCESSION   WP_284457413
VERSION     WP_284457413.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 151)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 151)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 151)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008128
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..151
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15770
     Region          10..149
                     /region_name="CytC556"
                     /note="Cytochrome c556 [Energy production and conversion];
                     COG3909"
                     /db_xref="CDD:443115"
ORIGIN      
        1 msirkgvmia lasglvfapa favsadivks ridsyrelga afkavndglr ggdvqavlia
       61 qsarqirnaa kaqyqlfpag sgpragvktn akaeiwtkpk pfraaqdafs vaadrfyaaa
      121 tkgspatira eaaklgatck achdqfrskv d
//
LOCUS       WP_284457437             151 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Blastomonas
            fulva].
ACCESSION   WP_284457437
VERSION     WP_284457437.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 151)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10648172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..>151
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          17..75
                     /region_name="GerE"
                     /note="Spore transcriptional regulator GerE (stand-alone
                     HTH domain) [Cell cycle control, cell division, chromosome
                     partitioning, Transcription]; COG5905"
                     /db_xref="CDD:444607"
ORIGIN      
        1 mgdsvsqpsl devrwtrlte kqracldlll erqtskqiar rlgiskptvd qrltaargil
       61 gatnrdeaav lyarlkqtyd rvtydpvqlp ypanevppvv pdtkpgdvmi ledsaatpgg
      121 stsrnfwrhd hdlkarilim aamlvvavil i
//
LOCUS       WP_284457505             258 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein, partial [Blastomonas
            fulva].
ACCESSION   WP_284457505
VERSION     WP_284457505.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..>258
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          60..>251
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkhwlrspvv waasglaaag llvglsvsrg ggvvpgtpai aaqasqllpd tperwqgkvd
       61 yaafdarinr lmrdpemvgl svatvengrl afvrgygfad reaglavtpq tvfrwasvsk
      121 gvagtlaykl aeegrlslsa plasfgtslk lsggaenrla ipdllahrlg lsrnaydgkl
      181 esgdpapmlr nmlstvpqqc lpgdchsyqn vaydafseiv gnatrmpyem aaqqqlfapl
      241 gmvsaglgma nltgaksw
//
LOCUS       WP_284457539             432 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Blastomonas fulva].
ACCESSION   WP_284457539
VERSION     WP_284457539.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..432
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45576
     Region          33..428
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mskvlnqmpn lsrrhvlgsa gllglfaamp gyaramatgd fgliraqved yvaskkvagm
       61 lvslgfgaqe aaligagnla ldiptpvdan slwrvysmtk piagmaamil vdqgklkldq
      121 piadfipefa nmkvltdpak nldavpaktm itprhlmtht aglgynivtk gplleeynkl
      181 ginpaavskt pipgfpmpap tppidefarr vaslpliaep gtiwsysigl dllgyviqva
      241 sgmelgaflq kamfdplgmt ssywtvpqse vprlstnyap fagalipidp aqdsifttpp
      301 afpfggaglv ssardydrfl gmlvgkgqlg gtrimseata llgmsnllpq tavtkgtwve
      361 dqgfgaggrv glgnakgpag tygwggaagt vafvdhvrgi rasgftqymp aesypfqref
      421 pkmiydqlqa mg
//
LOCUS       WP_284457555             361 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Blastomonas fulva].
ACCESSION   WP_284457555
VERSION     WP_284457555.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..361
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38877
     Region          1..346
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mlgalaapat aqtddnvrie ltftadqlgr skvsglahrp smreatlddp vriasiskla
       61 vgvavmrlvd kqaldldrdv slylgwrlvh pqhpgtkitl rlllshqsgl tddagyfipl
      121 dakladllaq peawdashap gsffryanvn ypvvaavmea atgrrfdrim teevfdplai
      181 pacynwsgck tearkdaitl yrpdgsiard dwitqpeqca smttrdgrcd ldaylpgqng
      241 safgpqgglr isagglarlg qmllnggdgl ltpqsfaeli raqwrfdgsn gdddkgyfta
      301 fglgvqrieq adgrvwighp geayglragl wvdraggqgv vristghaed ypvghclvac
      361 p
//
LOCUS       WP_284457612             466 aa            linear   BCT 25-DEC-2024
DEFINITION  leucyl aminopeptidase family protein [Blastomonas fulva].
ACCESSION   WP_284457612
VERSION     WP_284457612.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Drinkwater,N., Malcolm,T.R. and McGowan,S.
  TITLE     M17 aminopeptidases diversify function by moderating their
            macromolecular assemblies and active site environment
  JOURNAL   Biochimie 166, 38-51 (2019)
   PUBMED   30654132
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Lowther,W.T. and Matthews,B.W.
  TITLE     Metalloaminopeptidases: common functional themes in disparate
            structural surroundings
  JOURNAL   Chem Rev 102 (12), 4581-4608 (2002)
   PUBMED   12475202
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
REFERENCE   4  (residues 1 to 466)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415720
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..466
                     /product="leucyl aminopeptidase family protein"
                     /EC_number="3.4.11.-"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0030145 - manganese ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0019538 - protein metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49307
     Region          29..463
                     /region_name="PepB"
                     /note="Leucyl aminopeptidase [Amino acid transport and
                     metabolism]; COG0260"
                     /db_xref="CDD:440030"
ORIGIN      
        1 mmdlshlvqp digqparllh lvdkaglmaw lasapprvrn hlaamrftar phelvvvpgd
       61 tadewsvvlg vadvanlrpw clakapevla agtfrlagdv rpgdavigwa laqhrlttyk
      121 kpeenpqgsr vlltgdparl pdriaeaeat awvrdmvntp aedmgpgdle saaealarry
      181 gatlevtrgd alatgypmih avgraaarsh aprlielhwg redhprvaii gkgvcfdsgg
      241 ldiksaagml lmkkdmggaa halalaqlim raglpvrlhm lvgavenais gnafrpgdvl
      301 rsrkgitvei gntdaegrlv lgdclakase tppdvminfa tltgaarvav gpdlpalfan
      361 sdpladglva sgravgdpcw rlplwpgyed myvsdiadig nsggafagai taalflqrfv
      421 gegvpwahfd tyawrptprp gqpkggealg lraswhylrg rygaag
//
LOCUS       WP_284457614             506 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Blastomonas fulva].
ACCESSION   WP_284457614
VERSION     WP_284457614.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..506
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=56793
     Region          11..456
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mkhekpsdlk aathldvlii gagisglgma vhlkekcpgr sfaildqrsd iggtwnlfqy
       61 pgirsdsdmh tlgfefepwr eqkaiadgps ilsylrrikd erglndhlrl ghkvlsasws
      121 ssdarwtiaa evegqgvchl tanylfmgtg yydydegydp afegresfgg qivhpqfwpk
      181 dfdyagkriv vigsgatavt ivpsmtdkaa hvtmlqrtpt wywsrpakdw lanslraimp
      241 dewayrfirf knvrmqqlsf krarenpkkv gdyllkrirk imgskmnepd fqppygpweq
      301 rlclvpdgdm fkairdgkad ivtdhierft ptgidlksgk hldadviita tglklamagk
      361 vafsvdgqpv dftqhyyykg cmfsdvpnma ivfgylnasw tlkvdivadf vcrtlnhmaa
      421 tgtdvavpvl gsdgpvneee ifdfssgyvq ralhilpkqg drmpwrlnqd ylfdrkvlre
      481 eavddgvlaf rkadahapqq taiaae
//
LOCUS       WP_284457695             389 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfotransferase family protein [Blastomonas fulva].
ACCESSION   WP_284457695
VERSION     WP_284457695.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..389
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=43656
     Region          86..334
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 msapltvagl eaaarqatgl tdfgpdtgwr egferlvvav eamepnnqlr hlathnivgq
       61 lstrlrfved drlhpeiaaq pidpplivvg lprtgttisy dllcldpaar aprewewyip
      121 wpptetasfd tdpriaevta myenwlqhap qlldiqrfdc tqpgecnhgm qfhfgstnfp
      181 aelgvpdyar wlregrvegq yvshrrllqn fqwkgpkgrw tlkspqhlfd lpalleaypg
      241 amlvwthrdp altfsslssf iagflaafgg dkdkaaigrd vvdtwiagmn ralaaradpa
      301 iesriidlah kdvvadpmga irrihtrfgl dfseahqlri erfladnpaa krigrhqhsp
      361 eqygidvaev rvrmkdyydr fgsllgrpq
//
LOCUS       WP_284457745             501 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Blastomonas fulva].
ACCESSION   WP_284457745
VERSION     WP_284457745.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..501
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=55415
     Region          12..440
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mvsdrqniaa gtqqpekfdv iivgagisgi gsatllrkhc pdlsfailea leghggtwli
       61 hkypgtrsds dlftfgygfk pwtgqpiasr dqildylgda iadaglgpfi ryghsvtsan
      121 wsnetaswkl tverkgaddv vqmeasflwm cqgyyrhekg ytpqwpgmdr fkgqiihpqh
      181 wpegldlagk nvtvigsgat aatlipalad rcahvtmlqr tptyfaaghn adalaeelrr
      241 ldvdptwvhk imrrkvvrdr adlldrahss pdklkamlig gvqallpqgf dverhftppy
      301 rplqqrvafv pdgdlfkais agkasvvtdt istfddtgiv ldsgeridad vvitatgfdm
      361 avmgdipfsi dgapvnfaqt ityrgimftg ipnmawvygy ghyswtlrad lvagfvcrll
      421 dhmhksgars vmpvlrpedq gmelkpwvdt dylnpgyllr sldrlprrgd tpewqhsqdy
      481 fyeseaipai dltdpvfays h
//
LOCUS       WP_284457914             456 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Blastomonas fulva].
ACCESSION   WP_284457914
VERSION     WP_284457914.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..456
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=50471
     Region          192..427
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mskilkgprk qsarkielwl ylalltvvfv fggssrddys glvllrpici vaffyylsrl
       61 qwhqikmhvf vlafsaamff lllvhliplp pamwsalggr viiydvlsya qspeammpls
      121 mtpnrtlnaf yalfvplavl lgylsldeqg qlaalrviai llilgavvti iqasgldlyl
      181 yqirsdtpag lfanrnhhav aivslalils cyilpkyiqp rllpsqylll llavnallfp
      241 vvlisgsrtg talflltflv villssgrdr kaisrwlslp fvtammgsfi flslsltrgr
      301 ttawsrfisl dddlrygvwg tvwqvmpsyw pwgsgigsav evyqlhepds aliptysnhv
      361 hndwmevvlt agapgailll vaiaayfwvv wdlsrsrqkd vglrwvglai isvlgiasiv
      421 dyplrtpala slfalaavwa agrmrdenin egkaid
//
LOCUS       WP_284457948              69 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Blastomonas fulva].
ACCESSION   WP_284457948
VERSION     WP_284457948.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 69)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..69
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=7555
     Region          10..66
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mqpqpgpcgr lmsikdvvre tslnkatiyr riasgtfpsp rslggrrvaw retdveswka
       61 dpvgwrgdg
//
LOCUS       WP_284458027             134 aa            linear   BCT 25-DEC-2024
DEFINITION  MerR family transcriptional regulator [Blastomonas fulva].
ACCESSION   WP_284458027
VERSION     WP_284458027.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 134)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140991
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..134
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14656
     Region          1..126
                     /region_name="HTH_CadR-PbrR-like"
                     /note="Helix-Turn-Helix DNA binding domain of the CadR-
                     and PbrR-like transcription regulators; cd04785"
                     /db_xref="CDD:133412"
     Site            order(2..4,18,35..37)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133412"
     Site            order(49,52,56..57,66,77..78,81,84,88,94,98,101..102,109,
                     114..115,120,122)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133412"
     Site            order(77,112,120)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:133412"
ORIGIN      
        1 mkigelanat askvetvryy ekigllpppa rtsanyrtyg tdhlsrlsfi rrardlgftl
       61 eavrelltls ddkaqscdav dgiarihlte idrkiadlsa lrgeldrvig scrhgtvadc
      121 kiietlgprk mvsa
//
LOCUS       WP_284458028             147 aa            linear   BCT 25-DEC-2024
DEFINITION  MerR family transcriptional regulator [Blastomonas fulva].
ACCESSION   WP_284458028
VERSION     WP_284458028.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140991
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..147
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16049
     Region          6..134
                     /region_name="HTH_CadR-PbrR-like"
                     /note="Helix-Turn-Helix DNA binding domain of the CadR-
                     and PbrR-like transcription regulators; cd04785"
                     /db_xref="CDD:133412"
     Site            order(7..9,23,39..41)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133412"
     Site            order(53,56,60..61,70,85..86,89,92,96,102,106,109..110,
                     117,122..123,128,130)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133412"
     Site            order(85,120,128)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:133412"
ORIGIN      
        1 mtqqgfpiga lsqqcgcnie tiryyerigl ipradrrgry ryyttgdadr lrfikraral
       61 gfaieeirnl lrlaksasns gidacadaka iaqsnlqivk arledlkrme avltdaigac
      121 dqdsfrgcpi laalsgtywt gesgtpa
//
LOCUS       WP_284458062             667 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Blastomonas fulva].
ACCESSION   WP_284458062
VERSION     WP_284458062.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..667
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=72301
     Region          419..664
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mstanrgtlt gvamgaalaw lgvptiaqaq aaapdlarim gsrpevedas lspdgtklay
       61 lapvngqgsv lmvvdlsred rpqravfkad gepnrmtscn wtgntrllcs iiasvmvdnr
      121 atyatrmvav daiggdakvi dvrrgggerl glalyggdvi dwnpsdeghv lmvrdyvpet
      181 sigtrlaqek eglgvdlvnt rtlaartveq pdlgaiefis dgygkvrikg srsvrdgyvm
      241 egrryfyrtp dskawvamsv vdasregfdp havdatanla yglkrldgrm aaysmaldgs
      301 gketlvfahp qvdvsgfirv grrnrvigvr yvtdvaqvhy idpdiaamtk alsgavpdlp
      361 lirvvdtsed erkmliwags dtnpgayflf drdartlgnl laarsaldti plakmepvry
      421 rardgveipg yltlppgkas aaglpaivmp hggpsardew rfdwlvqffa lrgyavlqpn
      481 frgsagygsd wfqrngfqsw qtavgdinda ghwlvsngad arrlaifgws yggyaalqsn
      541 vmepdlfkav vavapvtdle klkadrqgws dfvqvsryvg sgphikdgsp arnaeafkap
      601 vlmfhgdidr nvdvgharlm dsrlrsagks selhifedrd hyledsvirs kmlstsagfl
      661 ektlalp
//
LOCUS       WP_284458114             266 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Blastomonas fulva].
ACCESSION   WP_284458114
VERSION     WP_284458114.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..266
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29654
     Region          1..207
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mprvsvivpv rngsatiesa ihsliwqtyq dmkiyivndr stdntyelce rmagtsdkil
       61 lvdnpgqgis salnyavels dstyiarmda ddisfperlk rqtelldnsp dlavvgsafi
      121 rfgalnkfaf vptdeascyy csrlfspfch pttvfrrsal eeigggydgn yngaedfelf
      181 srmldsfkga niadplfayr ihpsqvsatq seqqrrlsrt iikrnvdkvv asmgrakayr
      241 tilqniprsm mpnalrsfra llmvsg
//
LOCUS       WP_284458200             974 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Blastomonas fulva].
ACCESSION   WP_284458200
VERSION     WP_284458200.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 974)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..974
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..974
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=105166
     Region          31..444
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          521..952
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mfkpfrslia vsalaltvai apayaqqaap vaelvktvni pyqqfkldng ltvivhedrk
       61 apivavsiwy dvgskhepkg ktgyahlfeh imfngsenak gdyfeylkkl gatdfngttw
      121 fdrtnyfqtv pkaglegalf lesdrmghll ngitqekltn qigvvqnekr qgdnqpyglv
      181 eykqiemlmp tehpyghsti gsmadlqaas lddmkkwftd hygpnnailv lagdinvaea
      241 rplvekwfgd iargpqvakl npplptldav kvaemkdkvp tarlyrfwsv pglndpdfaa
      301 ldvaatvlgg lassrldnil vreeqtavav tastlpfvhg svfeayvdvk pgadieavsk
      361 rfdeiladfi akgptadevq rvatreaagr iagleqvggf tgkavtlaeg alysndpafy
      421 ktqldrlaam tpekvtaatt kwltrpvakl hvlpgerday addaggsagq aegdgpamra
      481 plprtgvlaa pafysslasd aiaagaaskq plaavdrttf peagavpdld fpdveeatls
      541 ngikvrfarr savpvvrvav sfdagyasdp kdalgtnslm iallkegtrt lnsiqlaeaq
      601 erlgtninat sdldrtivsm samkpnlgas ldlladvirn pafdakeler vrvqqltriq
      661 aefsepqgia lrnlppllyg ashpygvplt gtgdpavvtk ltrdqlaayh sqwmrperas
      721 ifvvgdttlk dmlpmleqrf gkwpsnrmal mqkdfsaaip agqgriilid rpnspqslil
      781 agqvlnakgt dnllaletan dimggdflsr inmdlretkg wsygsrsliq rpkndvpfli
      841 fapvqtnqtg psvsaiidqm ngfigdkgvt peeldrtvkg sslelagtye rsssvlsqmq
      901 sdalygrptn yaeslaaqyr smdaaklnga mrealdpktl twlivgdaak iedqlkalnm
      961 pievrraapa agdk
//
LOCUS       WP_284458258             389 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Blastomonas fulva].
ACCESSION   WP_284458258
VERSION     WP_284458258.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..389
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=44787
     Region          7..387
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mimitsmktt sntdpktkaq ntrrvsfgdg lfryerpggs sswvcrvqkq ghrrdfglgs
       61 cskvslaear erarevrsqm emgldpqfer rkleavptfk daaqkvfdih sktwrngkhh
      121 aqwmrtlemy vfpsigkhkv dkitgpmird vlaeiwlakp etarrvrqri gavldwayas
      181 gyreteapmr aiskglprqp rkdghfpamp yekvskfilk lraresfsrl alefaiytaa
      241 rsgevrgmtw devdmeealw tlpkermkaf rehvvpltpr plrilrrcaq lrlrdcqyvf
      301 pgirsnkpls dmtlsmlmke mgqpftphgf rssfrdwvse etshpsdvae aalahtvank
      361 teaayrrgnl lekrrvmmae waaycdkds
//
LOCUS       WP_284458271             278 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Blastomonas fulva].
ACCESSION   WP_284458271
VERSION     WP_284458271.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..278
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=28999
     Region          1..251
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mtgtwlivne asgsydadvi adivtrfadg gqpvdcvvrc pddtlptper leaegvsila
       61 iyagdgttns alkaaqgwdg dvlilpggtm nllaralhge hscqdiiaya crdrhtrrln
      121 tvqigeniay vgviagptts wakvrenarh advadlvftt ipaaisesls gpqvgieghd
      181 gtypaifaap rentlalcgf tassigevia hagawldgdf rdgprvdlge asratlvsds
      241 dsigllidge padcapgdtl vlgraphnfi dtrgpadr
//
LOCUS       WP_284458274             342 aa            linear   BCT 25-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Blastomonas fulva].
ACCESSION   WP_284458274
VERSION     WP_284458274.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..342
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=36778
     Region          20..330
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(26..27,29,69..71,92,120..121,124..125,127..128,131,
                     135,137,145,147,149,151..157,159..163,181..182,185..186,
                     286..287,294,300..306,308..311,313)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(70,93..95,118,257,304,307)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240626"
     Site            order(94..95,122,171..175,193..195,198,227..229,233..234,
                     255..257,281..282,304,306..307)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 mpanassqps apqhapgarp rvvvtrklap svearmaelf dvvlneddha fsrdelaaam
       61 adcdalvptv tdaldaelia gagdrlklla nfgagvdhid lkaarakgii itntpgvftd
      121 dtadmtmali lsvprrlaeg eklvrsgewd gwspsgmlgh riggkqlgiv gmgrigqava
      181 hrargfgmdv ryhnrrrlpe sleqmlgasf epdldalvaq sdiitlhcpr spetrglida
      241 rriglmkpra ylintargei vdeaalidal eagriagagl dvythepqvd prllalknvv
      301 llphvgsatf egrrvagekv ianirfwfdg hrppdqvleg wm
//
LOCUS       WP_284458297             380 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Blastomonas
            fulva].
ACCESSION   WP_284458297
VERSION     WP_284458297.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..380
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42828
     Region          6..370
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
     Region          179..>287
                     /region_name="SRPBCC"
                     /note="START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC)
                     ligand-binding domain superfamily; cl14643"
                     /db_xref="CDD:472699"
ORIGIN      
        1 maflgtrpip akpyydpawf elerdavfrr swlqighvce lpdlgsfvrr elevlgasll
       61 vvrgkdgtlr afhnvcthrg tqlveevqgk ratfscpyhm wtfggdgall sapdfdsfgl
      121 dkrdcalkqv aldvcagmif vnfaaqpqdl rewlgeladq metlpvarat tfseysyyia
      181 anwkltydnf qenyhlrfih prsgqsafsa enpfgypkey afhdphrtqt iwtnpnprpa
      241 pmladafarl vprameqgll ttphhrtyfa lfpsffmlgt plqnfvhvvy pvtatqsrgv
      301 irlywvgdda naserfgrea imgtardvhc edvavieagq rglssgaleh ihfqtqealc
      361 rhlfnmveaa vvayqaeqia
//
LOCUS       WP_284458328             459 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Blastomonas fulva].
ACCESSION   WP_284458328
VERSION     WP_284458328.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..459
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48763
     Region          249..457
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mnaqipslde aglttvwvaa etgridrngm llhaddrlmr lhqqlggsts ggelavppll
       61 elarhsmrlg mrlsrpvkaa gssalidmwc ectpdaegva lllthwreha lpdrsdated
      121 gadfiaepgv aylqldrler vvrysppaga gtddassgll lkpvtavlep sdgsafarae
      181 qidgqrvtla gderewiasl rpagtatgcv itlrhapplp dpaappempp lfdgerigql
      241 fgrqigpalr lpigriiana etiggrlegp lradyanyas diaaagrhll alvddladle
      301 aidgagfsaa repvdladia rraagllalk asdrkiridk psedemlpat gefrrvlqvl
      361 lnllgnainy apdgsmiwlr lddgpgwasv tvadqgpgls aedqqrlfnk werlgrsgdg
      421 gsglglyisr rlalamqgdl tvesapghga rftlllptd
//
LOCUS       WP_284458401             574 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Blastomonas
            fulva].
ACCESSION   WP_284458401
VERSION     WP_284458401.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 574)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 574)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..574
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=61908
     Region          16..531
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mtalasgshr vrlaskrqhm tltaqvrlva vlalfgigvg aillrltfig vfgeqaqaat
       61 rsalvdpgrg divdrngvpl artidgyavr vvperligdr kvlagklaqi fpdtseqrfl
      121 dllsrskpty lrhravpeev nrvhalgevg iefprekerf ypqlqlaahv lgyvhpdghg
      181 vsgmeralda elidpkkrlt psalsvdirv qaaledelgr amksydakaa agvvldvetg
      241 evmamtslps fnpnqfdass aafeanqvty rffelgstfk pltvaaaida gtvtnlsrry
      301 dasrplkvag fqirdshssg rwlnvpetlv hssnivtaqi adelgperlq avmrklhfdr
      361 paqinlretv kplwpaswgr ltnmtvsygh giavsplhla sayaamvngg vyrpatlmkl
      421 kpsdvprger vfkastsarm nqllrmivrd gtgrkaeapg frvggktgsa ekpgaggykr
      481 ssvvatfaav fpmdaprfvv limidepagn sassfqrtag wtaapvvarl vprigpmlgi
      541 ipddrrdvdv selmpllwka pvragakgga ddpa
//
LOCUS       WP_284458456             531 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Blastomonas
            fulva].
ACCESSION   WP_284458456
VERSION     WP_284458456.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..531
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=56252
     Region          6..385
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mslvnqatsk rllavhgwsg vllglflyvv vitgtvavls qeigawsisg artqapfsqp
       61 ldarvrqlaq tvepkyredi tiypnasgtm lvffhthgvn sagkpddvgv rfllepgtlk
      121 vaardegygs elpddrdsal dyfisilhis lhapdpvgly ltglagfvml favisgiilh
      181 rhlikdlfva prlssrllnr rdrhilagsw slpfgfllaf tgtffsfaga iglpivamva
      241 fggdqekmte tlvgapetvs erpadmanld smiarsvart gtqpsfisia hwgtadsray
      301 lyhlpsgrav easthvydma sgryhgvkpd lgtrpsfgst vyawmgplhf ghfagllskl
      361 iwvslglaas yvtltglrlw verrpdmpsg rvlgvaipmv gygvpigltg aalgflrnyp
      421 agdpvsgtal gfvwgcafav llagvlirrg dasavfmavl glamvalpla rlatggqgwp
      481 dlvgaghavv vmidlmllag gvfalhrsrr gdaigrsarg egqasaavpa e
//
LOCUS       WP_284458536             417 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydroorotase [Blastomonas fulva].
ACCESSION   WP_284458536
VERSION     WP_284458536.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Gojkovic,Z., Rislund,L., Andersen,B., Sandrini,M.P., Cook,P.F.,
            Schnackerz,K.D. and Piskur,J.
  TITLE     Dihydropyrimidine amidohydrolases and dihydroorotases share the
            same origin and several enzymatic properties
  JOURNAL   Nucleic Acids Res 31 (6), 1683-1692 (2003)
   PUBMED   12626710
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10784973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..417
                     /product="dihydroorotase"
                     /EC_number="3.5.2.3"
                     /GO_function="GO:0004151 - dihydroorotase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006221 - pyrimidine nucleotide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=43744
     Region          11..412
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
ORIGIN      
        1 msklptrplt itngrlvlpg raepvpgalr iigdriaeig dvtpgsddav hdargaliap
       61 glvdlgvfai dppafhfggi sraalmpdqs ppldhparvr faaysgkpdf wvhplaaatr
      121 dlagsemaei glmkeagara vatgrrwivd tgvmhrlmqy camldlpliv hsqdhglsgn
      181 avatagemat rlglpqapse aesiaiardl slvrmtgarv hfrqvttrag laliraakae
      241 glpvtagitp ahlflsdval ggfrtfarls pplrceddrq aaiaavgdgt ldviasghdp
      301 rgpedkrlpf tdsqpgmaga etllplslgl vrdgvister lfdliaanpa rilgvqagal
      361 rtgyeadvvv vdadrpwqvd sakmaasagn tpfdrlpvqg rcvalfkggr lvdqmka
//
LOCUS       WP_284458587             362 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Blastomonas
            fulva].
ACCESSION   WP_284458587
VERSION     WP_284458587.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..362
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=40095
     Region          1..358
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mqtldwlhrw tggliglvla vlglsgtvll hrdawmmlph ahdtqvadna avvgaleaim
       61 adpysrpgsv lfatqslgln rltyadgsga ytdqsgavvs rwdsvwgrpe lflfdlhhhl
      121 lggdtgewli glaglcglff vlsglvlwwr trrtfrfrll psrltrpail whhrdmgvvl
      181 apllllaift gtsmifrpva alvlgpsapa tigaalkape paptpladqp dwrqivrtar
      241 qlfpdaeirl islpkqdggp itmrmklpee wlpngrtmlw fasdtgrlie arnalllpsq
      301 vqwfntfypl haakvgglpy rlvmtlvgla ltllgsltvw tfwfrrrpst rqaesrrpvt
      361 ve
//
LOCUS       WP_284458597             661 aa            linear   BCT 25-DEC-2024
DEFINITION  S9 family peptidase [Blastomonas fulva].
ACCESSION   WP_284458597
VERSION     WP_284458597.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18486225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..661
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..661
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=72526
     Region          69..107
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          84..240
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          113..153
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          158..198
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          168..335
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          205..244
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          251..288
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          296..325
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          399..652
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mrrarwwtav sglcaalcma atgpiearet daaepsvppp aamladgvpp ipmslvadtr
       61 pyleyrtasf agwnpqdrsm littrfgnva qlhrvaapgs arrqisfeee pifggtwspd
      121 gsmllvekda ggnevsqiya ldsgrmtllt dgksrhalgp wsddgrlvaf gsnmrtgvfn
      181 diyvmdprdp ksaqlvlssd sggwaaidfa pngrdllvfn yvsvtdsqlh linvetgtfr
      241 qvsrdatpva ygnlkfapdg rlwvssdkds dvqriglldm dtglftpmid ggrwdisnfd
      301 iaydgktiay vvneagfsrl hlydiasgek rlvtglppge igtgmkfapw gtlgftvfsn
      361 qspgdaysld pvtlqitrwt esetggldpa knvmpelvei ksfdgepvsg llyrpdpqrh
      421 pgkrplimsi hggpegqata gflgrtnylv nelgialfyp nvrgstgfgk rfvsldngpy
      481 lredsvkdig alldrlarhp mldqrrfgvt ggsyggymcy asairygrrf naancivais
      541 nfvtflente eyrrdlrrle ygdervpalr akleeisplt hvdelkipll vvtgandprv
      601 paseadqiie airsrggtaw hllarneghg frrkenadym fwttlafwqr hllgakgrat
      661 d
//
LOCUS       WP_284458669             355 aa            linear   BCT 25-DEC-2024
DEFINITION  Leu/Phe/Val dehydrogenase [Blastomonas fulva].
ACCESSION   WP_284458669
VERSION     WP_284458669.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Brunhuber,N.M. and Blanchard,J.S.
  TITLE     The biochemistry and enzymology of amino acid dehydrogenases
  JOURNAL   Crit Rev Biochem Mol Biol 29 (6), 415-467 (1994)
   PUBMED   7705101
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10500541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..355
                     /product="Leu/Phe/Val dehydrogenase"
                     /EC_number="1.4.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37025
     Region          13..124
                     /region_name="ELFV_dehydrog_N"
                     /note="Glu/Leu/Phe/Val dehydrogenase, dimerization domain;
                     pfam02812"
                     /db_xref="CDD:460706"
     Region          149..352
                     /region_name="NAD_bind_Leu_Phe_Val_DH"
                     /note="NAD(P) binding domain of leucine dehydrogenase,
                     phenylalanine dehydrogenase, and valine dehydrogenase;
                     cd01075"
                     /db_xref="CDD:133444"
     Site            order(183,185..187,206..207,211,240..241,262,264)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133444"
     Site            294
                     /site_type="active"
                     /note="Phe binding site [active]"
                     /db_xref="CDD:133444"
ORIGIN      
        1 mqsywdlpdf deheavqyvh drasglsaii aihstklgpa gggtrfwhya dkgraitdal
       61 rlsrgmsykn amaglpmggg kaviladads rktpemlaaf gdaiealggr yvtaedigms
      121 dadmvaiskr trfvsglpvq qegsaggdpg pftangifqg vkaavhfklg tdrlkgvria
      181 vqgtgsvggg larllaaega dltladvnad raqaladelg attvsadrim qveadvfspn
      241 algaildses ieklnvkiva ggannqlarp hhadmlvdrd ilyapdyvin aggiisvale
      301 yfaqaegrta qvedvlarlt gipqrltgiw qesrstgqsp aavadamaqk ligrg
//
LOCUS       WP_284458717             120 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Blastomonas fulva].
ACCESSION   WP_284458717
VERSION     WP_284458717.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 120)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 120)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..120
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12758
     Region          1..95
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mddpgsqtwa vdalgalahe trlavfrmlv ragpdgmvag aiaeqqsvpp stmshhlatl
       61 eraglvqser esrlihyrad ypamrrlltf lledccqgtp emcgdlvagl gcapalpeka
//
LOCUS       WP_284458758             143 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein, partial
            [Blastomonas fulva].
ACCESSION   WP_284458758
VERSION     WP_284458758.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..>143
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          9..>143
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mthrfkasll avsaltsvpa maqqeadpar gasddviivt arkteetlqe apttvsvvta
       61 aaidrlgldn ltdiaktvpg lvfddtfgrd anrpvirgqa nilgqsgvaf fidgiyysgs
      121 ladydvdtve rfevvkgpqs aly
//
LOCUS       WP_284458810             151 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Blastomonas fulva].
ACCESSION   WP_284458810
VERSION     WP_284458810.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..151
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=16491
     Region          2..>150
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 msltdarerr ddvrkmirag ddplhsrkme kirarlsadn sfqsvaenli avrfvasqka
       61 evtiekarwh lshltptigp rpidavepae llavlkkiek agkretavrt kafasrvfrh
      121 gvamalckhd paampggala tpsvthraal l
//
LOCUS       WP_284458813            1572 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-glutamate dehydrogenase [Blastomonas fulva].
ACCESSION   WP_284458813
VERSION     WP_284458813.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 1572)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1572
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..1572
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=169635
     Region          27..1570
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 maetpiaasg adagssvssn atplidpqqh arlravlada flkgalpgen egfddaacse
       61 aadfalrama rrpssdtvlt iestpgqtgh rhmrlaiind dmpflvdsia aaisrfglai
      121 drvihpvval rrdadgllse iytdeapger resvvyleve radarqrkal etalmgamad
      181 vraavtdwpm lqaamaadaa amadgegaal lrwfldrnmt qlahlryrrd gsaeaplgia
      241 rindqpllaa hsfdqafawf esgkaaplii ksnfistvhr rapldlvilp iwedgrvaal
      301 svhggiwtsa alaaapervp vlrahlkllm dkfgfspngh agkalshalt alphdlliaf
      361 slenlerval tamsladrpr sklvtvqssl rrhlfvfawl prdevstgrr eaiermvlea
      421 sggktlswsi sledgeiali ryvidmrdga aavddaalds alramvrgwe psveealial
      481 gedsraaala sryapqfpma yrsdcgpkea aldivrlrdl dsperhgarl yrraddaaqh
      541 lrlklysltg aiplsqtvpa lenfgfdvle evptalgadd sghihdfllh lrgtgdaesl
      601 mlragaieaa isgtlegkae ndpfnrliaa tgleqraviw lrawyrylrq aglpygigtv
      661 vdalhdapdi ahalialfia rhdpaftgdr eaatqanlaa itsgltqvsa idddrllrmv
      721 ralvmailrt nafapaasla mvmkidsakv pglpaplpwr emfvyspqve gihlragpva
      781 rgglrwsdrr ddfrtevlgl mkaqrvknav ivptgakggf fpkqlpdpat dregwlnggk
      841 dayktfirtl lsitdnivdg kvvhpaqvvv hdgedpyfvv aadkgtatfs dtanaiaaef
      901 dfwlgdafas ggsqgydhka mgitakggwv svqrhfaemg vdvqsdpvrv agcgdmsgdv
      961 fgngmllsks iklvaafdhr hifldpdpda aaswaerqrm falprsswdd yekaliskgg
     1021 gvfpramksi pltaevkaml glegdeiepa alisailrae vdllwfggig tyikaasenn
     1081 idvgdpsndq lrinaeqlrc kvvgeganlg vtqaariafs mlggrintdf idnsagvdcs
     1141 dnevnikigl aavmraglld epsrnallas mtddvsmlvl ednrlqalgl siaeragvka
     1201 lpsyirlieh feeqgrldrk vegladnatl krraqeghgl trpelavvls takltlqdai
     1261 eripladdpt mrpellaafp pqmreaygdv lmqhqlrgei iatklanrmi nrlglihpfe
     1321 laeeegctlg dvacafiaae rlfalpaiwa efdhaemdeq vrlmlfdata nivrvhiadv
     1381 lrasadglmp gaivaalkpg vdaliaqmdn llnaearlqa arqaqdlvgq gassvhaahi
     1441 vrltgldgaa glanlastsa tdpmlltqaf adlgatlgld wtqmtaarms psdpwerllv
     1501 sglardfqqm rldflqrakg sdpqdyvagw teanlprikq frtlvdrarm daapsvamla
     1561 qiasqarill ar
//
LOCUS       WP_284458930             400 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [Blastomonas].
ACCESSION   WP_284458930
VERSION     WP_284458930.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas
  ORGANISM  Blastomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Blastomonas"
                     /db_xref="taxon:150203"
     Protein         1..400
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43428
     Region          1..400
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mrlpltgyri lsaeqygagp ygtmflaqmg aevikieppn kpgqpggdta ravgphflre
       61 neslyfqtfn lnkksltldl qsergrailr dlaatshamv nnlrgdlpar lgldyaalgp
      121 inpsivcahl saygrdnpra kwpgydylmq aeagflsltg epdgppvrfg lsivdfmtgt
      181 qmtvgllaam ldaqrsgtgc didvdllsta ahqmsypavw ymneadvtpr aprsahpsvt
      241 psqmfrsadg wmfvmaqlpk fwtilvdtig rsdlkddprf rkpadrlanr dvltevldav
      301 fgtqptqhwv dllsgkvpva pvhdlasamd npflqetgmm qqvehpdrpe lrvlaspirv
      361 dgqrlparag pllgadnddv lasiglsadd iaalkrdgiv
//
LOCUS       WP_284458982             402 aa            linear   BCT 25-DEC-2024
DEFINITION  nitrate/nitrite transporter [Blastomonas fulva].
ACCESSION   WP_284458982
VERSION     WP_284458982.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 402)
  AUTHORS   Yan,H., Huang,W., Yan,C., Gong,X., Jiang,S., Zhao,Y., Wang,J. and
            Shi,Y.
  TITLE     Structure and mechanism of a nitrate transporter
  JOURNAL   Cell Rep 3 (3), 716-723 (2013)
   PUBMED   23523348
REFERENCE   6  (residues 1 to 402)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..402
                     /product="nitrate/nitrite transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41411
     Region          14..384
                     /region_name="MFS_NRT2_like"
                     /note="Plant Nitrate transporter NRT2 family and Bacterial
                     Nitrate/Nitrite transporters of the Major Facilitator
                     Superfamily; cd17341"
                     /db_xref="CDD:340899"
     Site            order(24..25,28..29,32,64,116..117,119..121,124,142,
                     145..146,149,218,221..222,225..227,230,258,262,312..313,
                     317,321,336,339..340,343..344,347)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340899"
ORIGIN      
        1 mnkgfwsagh rptlfaafly fdlafmvwvl lgplapmiat dlglndaqkg lmvaiptlag
       61 avlrlvngvl vdkigpkstg aigqlivigg latawmlgvn sfggtvalgv ilgfagasfa
      121 valplasrwy paehqgtalg iagmgnsgtv laalfaplla kafgwnavlg laciplaitf
      181 viymvlakda pnppapksif ayleplkkad awwfmlfygv tfggfvglaa slsiyfvdef
      241 altpvvagyc taacvfagsl vrpmggalad riggtktlma vyliaaavlt tisfgpptvg
      301 lalalfvcam lalgagngav fqlvpqrfkd eigvmtglvg faggvggfyl asslglakql
      361 tgspqwgfli faglalvafa slvsvktrwr atwttdlega ri
//
LOCUS       WP_284458984             319 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent aminotransferase, partial
            [Blastomonas fulva].
ACCESSION   WP_284458984
VERSION     WP_284458984.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         <1..319
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
     Region          31..313
                     /region_name="HisC"
                     /note="Histidinol-phosphate/aromatic aminotransferase or
                     cobyric acid decarboxylase [Amino acid transport and
                     metabolism]; COG0079"
                     /db_xref="CDD:439849"
ORIGIN      
        1 lsllgasplv ptdtpppfss rlsrcshldc raarqeglar dhltlssgsl daltlltvai
       61 aaggrvvapq ptyathliya arqgietdwv plradhhidl dgmlaaigpr tklvyicnpn
      121 nptglrpdpd alrafciaaa akvpvlvdea yfelapdphr qsmaalvreg hdvivtrtfs
      181 kvyglagfrv aytlarperi allnsritts rnqaglaaat aclgdsayla gaiaylkgcr
      241 eqiyricqan glrylpsdgt fvyvdcgmpa aemqkrlaal svevrlfege ayrnwmrvgt
      301 atpeelayfg kvlpaalkg
//
LOCUS       WP_284459000             520 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Blastomonas fulva].
ACCESSION   WP_284459000
VERSION     WP_284459000.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..520
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=57812
     Region          2..489
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mlsrrlfiaa apltligapg llraqsvfrt fpfalgiasg dpspdgfviw trlapdpleq
       61 hggmamtpmp vkwevasddr fttivaggev iarpemahsv hvevaglqpn rpywyrftag
      121 gersfmgrar tlpmagaamd klkfgvvgcq nyedgyfgay nylareeldf vfhygdyiye
      181 yrgsptrany fggglqvpvr qhagqalydi adyrqryaqy ktdtdlqrah aahsffptfd
      241 dheiennwva gisggddpap geafelrraa alqawyehmp vrkinmprfg ggqfhrtarf
      301 gnlaeiqlld trsyrsdqac ddgfkplceg vndktaqvlg aeqeawlakn lsrnqarwnc
      361 lgqqimmmsl drrraanedt rianmdswaa yevprqrmls rmaglgnviv ltgdehqnfv
      421 gdlvhrdkvv gteivatsis sggdgadlry gseqmmknnp elkflndqrg yvvcevtpda
      481 wlshfqvvdk vsvrantmkr rataeithgv pgarmtglsa
//
LOCUS       WP_284459054             390 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Blastomonas fulva].
ACCESSION   WP_284459054
VERSION     WP_284459054.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..390
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42288
     Region          82..339
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mlkplaalal lattaatpad datyrarfea fmanpaqfdy spmeavpgap kvrrlpasra
       61 priaaaalde aaryaqanrs sallawrdgk leasryfgat trdtplvaks lakpltaiai
      121 graiqlgkik gldqriadfi pelagtpkaa ilvrhlldmr sglldqgysp npehpwnray
      181 ldpdhgayiv rdypltdppg tryayanaps elialviera tgrryaefis nevlaplgaa
      241 ggevwvnrpq glahsgccik lpaetwmkla illlddgkvg grrllpkgyv ramrtgtpqn
      301 pnfglglwlg epyrerrgfg apgtagpqvl hsaayldpem flfdgnsnqt vhispkhrli
      361 vlrmgetppk tpewdnaklp nllirglglr
//
LOCUS       WP_284459056             500 aa            linear   BCT 25-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Blastomonas fulva].
ACCESSION   WP_284459056
VERSION     WP_284459056.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..500
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=51725
     Region          30..497
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mafarpplsd svtaflarrg qgqglligge wtggqgetfa tvdpaigdqi gvlprggape
       61 idaavaaara alagwkattp lnrakilwaa adlieahide laeietldqg kplfvgrwae
      121 ipgavnqfrf fagqamaieg qviessidyq pagkkmaswt krepvgvvga ivpwnsplvl
      181 tamklapala agctivlkpa entslsalrl gellmeagvp agvlnivtgl ggeagaalaa
      241 hhgvdkiaft gstqtgraii daakgnlkrv slelggkspm ivmpdadler aipgvanaif
      301 fnggqvcvag srlyvhsaik dellkgvaay aqglvaghgl dpatqmgplv srlqaervvg
      361 fisaardgga tvltggerfg dagtfvqptv itdvtpdmpi vreevfgpvl vaqefddada
      421 viaaandsdy glaasiwtqs lshahrmada ietgtvwinc hlmydaalpi ggikqsgygr
      481 dsgraaldsy lewktvcavi
//
LOCUS       WP_284459086             258 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF1223 domain-containing protein [Blastomonas fulva].
ACCESSION   WP_284459086
VERSION     WP_284459086.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..258
                     /product="DUF1223 domain-containing protein"
                     /calculated_mol_wt=26868
     Region          19..258
                     /region_name="COG5429"
                     /note="Uncharacterized conserved protein, DUF1223 domain
                     [Function unknown]"
                     /db_xref="CDD:444181"
ORIGIN      
        1 mkllwitaaa vlttlaisal hapsqgsalg nsapsparla isqsgpvvae lftsqgcssc
       61 ppadavaarl ardpailvis rpvtywdrlg wkdslgreen trlqrqygdr afaganiytp
      121 qlvidgsaqg vgsqeanark qivragaira rsgvtvrvtr tadggrsivl qgrpgtgaev
      181 mlislssret vnigrgengg rsvsytnvvl detplgrwsd ggraivlrpd qldtrgadrh
      241 alvirrgagg aiigsali
//
LOCUS       WP_284459192             303 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Blastomonas
            fulva].
ACCESSION   WP_284459192
VERSION     WP_284459192.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..303
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=31883
     Region          4..298
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 msviamtggt gfvggasida alasghqvra ltrrpqpere gvtwvpgald dphslselci
       61 gadcvlhiag vvnapdragf iagnitgten mlaaakaagv arfihvssla arepalsnyc
      121 wskaeaearv iasgldwqmv rppavygpgd temldlfrma argvvmlppg grmsvvhvad
      181 laallvrlag gagdanaihe vddgaprgws hkdfadalgd avgrkvrafs tpklalhlaa
      241 qgdrllrgka akltpdrary iahsdwtadp drkppsqlws akiptrqgla dtarwyraqg
      301 wlk
//
LOCUS       WP_284459224             151 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein, partial [Blastomonas fulva].
ACCESSION   WP_284459224
VERSION     WP_284459224.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..>151
                     /product="YybH family protein"
     Region          37..149
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mnigmktima lsialpaaaw aqsdaraada ravkavlssy kkaiekldaa gterlfttna
       61 qifetgaseg syttylahhl gpelkqfksf rfsdykvdvr fegpvalate tyryriqpkt
      121 geaaerlgva tsvlkkvggs wkivsmhnsa r
//
LOCUS       WP_284459309             128 aa            linear   BCT 25-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Blastomonas fulva].
ACCESSION   WP_284459309
VERSION     WP_284459309.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..128
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=12801
     Region          1..99
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mansiaeaal vscrtlnrdv vvaivdrggn lialqrgdev gphntnaaer kaftalstkt
       61 stsrlaqraa tepasanlas vaellllggg lpiihdgevi ggigvagsgg sesdeqcama
      121 althgtrq
//
LOCUS       WP_284459477             323 aa            linear   BCT 25-DEC-2024
DEFINITION  FecR family protein [Blastomonas fulva].
ACCESSION   WP_284459477
VERSION     WP_284459477.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20752687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         1..323
                     /product="FecR family protein"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0016989 - sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35098
     Region          11..51
                     /region_name="DUF4880"
                     /note="Domain of unknown function (DUF4880); pfam16220"
                     /db_xref="CDD:435227"
     Region          72..316
                     /region_name="FecR"
                     /note="Periplasmic ferric-dicitrate binding protein FecR,
                     regulates iron transport [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG3712"
                     /db_xref="CDD:442926"
ORIGIN      
        1 misdrpdtla qqaiawhmrl aeggaddwaq fvewleadpa hgdvydqveq tdedaraaml
       61 emghafvgep iandntaqvs srprrwwigg avaasiaava vlgsgvlpmr atyeistaag
      121 esrtisltsg drivlngttq imldrnnprf arldhgeavf dirhdpddpf vlylgedrie
      181 dvgtvfnvth ergetrigva egavlynpds davtltagql lhdpggdrpi irrsvataav
      241 gawqqgrlsy drapysevvs dlaratgrni sldpalanre ftgtirisqd egqlrndvad
      301 lldvtttqek avwrltartr gar
//
LOCUS       WP_284459502             539 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein, partial
            [Blastomonas fulva].
ACCESSION   WP_284459502
VERSION     WP_284459502.1
KEYWORDS    RefSeq.
SOURCE      Blastomonas fulva
  ORGANISM  Blastomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Blastomonadaceae; Blastomonas.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Blastomonas fulva"
                     /db_xref="taxon:1550728"
     Protein         <1..539
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          3..507
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 aalidgvkln dpstpgggfn fghlltgnie rievlrgpss vlwgsqaigg vinmitrqpt
       61 eelavnlrge ygyrdtgqlv gnisgkagpl sasagagyfr tdgissfsea rggterdgye
      121 nygangnfnl alsdaisida rgwysegrvn idgfpapafa fadvneesrt reivgytgin
      181 aalfdgrfrn rlgyaytdtr rrsialdgpa tetfvghgrn erieyqgifd iaegwqltgg
      241 leretsrfss ssfgaapslg raridslygq ivatpakglt ltggvrhddh nrfggattfg
      301 asgvfapgeg ntafrasyae gfkapslfql qsdfgnqqlq perskgwdag itqslvegrl
      361 qasatyfrrn ssdliifvsc vapltgican rpsgtydnva raraegveig ltmqpvdalr
      421 lqanytytda tnrspgnanf grqlvrrpqh smtalidyrw gfgletgvtl thvganfdna
      481 nnsrkvegyv ladlrasfpl teridiygrv enlfderyet vfrygspgra gyagvrlry
//
LOCUS       WP_284459570             350 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Cupriavidus campinensis].
ACCESSION   WP_284459570
VERSION     WP_284459570.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus campinensis
  ORGANISM  Cupriavidus campinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Cupriavidus campinensis"
                     /db_xref="taxon:151783"
     Protein         1..350
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36283
     Region          1..343
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mlqkplhgvr vvefegigpg plaammladm gaevialtra eqaagaqplg gaaanplhrg
       61 ktveitdlks pggkaraldl igqsdvlieg frpgvmerlg fgpaecaaln prlvygrmtg
      121 wgqdgplsra aghdlnyval tgllslsark gqmpivppsv lgdaagalgm afgvacalvd
      181 argngrgsgr grvvdaaiid ivammgtlvh wirangqidg tkpspfhdsp fydvyacadg
      241 gfislavvep afhalllskl gltdvnpadq ydtttwpalk eriaalirsq prahwcalle
      301 gsdacfapvl slaeaarhph naargiyqtt psgaieaapa prfqalnait
//
LOCUS       WP_284459643             212 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Chryseobacterium
            sp.].
ACCESSION   WP_284459643
VERSION     WP_284459643.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..212
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=24661
     Region          18..164
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 miilysfide srhkflmdry lnafsedfke dvlkyrrwqd aqlsllgrvl lqhglsahyg
       61 ineadigrlp nnkpflkghp ihfnishskn lvacviadfp igidiefsde tinyldfefq
      121 mtagefeeih hsedkissff sywtkkeavl kaegsgmmis ldsfeilnne cviegkkfft
      181 keffidkryh cciasedlni knksicyelf qn
//
LOCUS       WP_284459747             400 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Cupriavidus campinensis].
ACCESSION   WP_284459747
VERSION     WP_284459747.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus campinensis
  ORGANISM  Cupriavidus campinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Cupriavidus campinensis"
                     /db_xref="taxon:151783"
     Protein         1..400
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=45685
     Region          1..393
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mltdtklrnl kprdklyken drdglyvavt pagaisfryn ysihgrqeti tfgrygvggi
       61 tlaearerlg eakkmiaagk spakekardk arvkdaetfg awaekwlrgy qmadstrdmr
      121 rsvyerelkp kfgnqklvei thedlraltd aivergapat avharevmlq vfrwaiergq
      181 kvenpaelvr pttiakfepr draltpdeig lmyqymerig ttpsiraaak lllltmvrks
      241 eltnatwsei nfsealwtip kermkrrnph lvflsrqald ifialktfag gsdyvlpsry
      301 dsdlpmssat lnqvltltyr laqkegksla kfgphdlrrt astllheagy ntdwiekcla
      361 heqrgvravy nkaeyreqrt amlqdwadmi dewtlkrpka
//
LOCUS       WP_284459766             343 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Cupriavidus campinensis].
ACCESSION   WP_284459766
VERSION     WP_284459766.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus campinensis
  ORGANISM  Cupriavidus campinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Cupriavidus campinensis"
                     /db_xref="taxon:151783"
     Protein         1..343
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37583
     Region          1..342
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mqhfasdnya gfcpeslkyf leanasghek aygddswtqq vcdrirnlfq tdcevffvfn
       61 gtaanslals slcqsyhsvi chelahietd ecggpeffsn gsklltapgv ngkltadave
      121 alvtrrtdih ypkprvvslt qstevgtvyt veevraiaai akrrqlrvhm dgarfanava
      181 algvhpseit wragvdvlcf ggtknglpvg eavvffdrrl aedfayrvkq agqlaskmrf
      241 isapwlgmle ndvwlsnarh anamaqllhq rivdipgvri mfptesnavf aelplpaiea
      301 lrargwlfyt figaggcrlm cswdlqpetv eafaadirga cal
//
LOCUS       WP_284459873             621 aa            linear   BCT 25-DEC-2024
DEFINITION  NACHT domain-containing protein, partial [Cupriavidus campinensis].
ACCESSION   WP_284459873
VERSION     WP_284459873.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus campinensis
  ORGANISM  Cupriavidus campinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 621)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Cupriavidus campinensis"
                     /db_xref="taxon:151783"
     Protein         1..>621
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          35..>523
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mtilsylprr gtktlangar dtrlladwae vdayvllgep gsgkstaflr eaesaddchf
       61 vtarnliavg ppdgwaggtl fidaldegqv ssgsflatfd airkklaelg rprfrlscre
      121 aewfsggaad lkfvspnkev velqleplsd aevrelvesw vpsrlpeank flakseqlgv
      181 aplfgnplll dlvvravgsd rwpeskeety elacrqlaqe hnpvhqrgqr gknfaleetl
      241 hqagllsall vissapsiai ddalpgessv svstvvaalr lstdeihatl stplfgaagf
      301 nrvprhrtva eylgakaisr lvqrdglpis rvlslvcgnd grvvdamrgl yawlcvhcrt
      361 erlllverdp lglilygdvr pfsvtekmal ldalheeatq yrwfrnenws aqpfgalgtp
      421 dmvqvfadrl rgasrdpahq avldcildai rygspmsvlt pglvdivrdp tywprirkaa
      481 ldallvndds egnaarqlln evdsghvedd edeligallt hlyptllpph qmmaylrkpk
      541 sdslfgdfky fwkvkfvnat prfalpalae rfassiktle aaadgqrddd ledvreiaar
      601 llarallecg ddstpeqiys w
//
LOCUS       WP_284459892             386 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Chryseobacterium sp.].
ACCESSION   WP_284459892
VERSION     WP_284459892.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..386
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=42722
     Region          18..385
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mtqkfvsifn sttimllkdk kvaiigagpv gltmakllqq kgievtvyer dkdpqariwg
       61 gtldlhkdsg qkamkkagll eayykaalpm gitiadeqgk tlftkpitpq nqfdnpeinr
      121 nnlrtilles lphdsvswdr kcidlkvcgg kwlllfengl qatadlvisa nggmsamrkf
      181 vtdtaieetg tiiiqgdiph petdcpefyq lcngnrlmaa fqgkllvvnp dnngaltygv
      241 ifkkpdnted nlqdtddirk fllknfahwd kryqnlvqlt psflslptrk lplsapwktd
      301 rplpitligd aahlmppfag qgvntglmda lilsgnltgg sydslqtain dyeqqmfiya
      361 seaqisssin eiemrhpdfs ftqlin
//
LOCUS       WP_284459919             621 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein, partial
            [Chryseobacterium sp.].
ACCESSION   WP_284459919
VERSION     WP_284459919.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 621)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 621)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 621)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         <1..621
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          <1..571
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 sgfqsqisna nsisdlqgll ggdftsqela yrglerkdfs lragqsklrs aqlffnseip
       61 vnddwkvysf ggysyrlgna ggfyrlpnne rninavtpng ylpqieatvn dyslaagikg
      121 kwngwnvdfs ntfgknafsf gvvntfnasl tdhsprsfea ggsefsqntv nldfskkynv
      181 lhglnlafgg eyryenykvn agkensyasy difgnvvtan tpenekvtdf fgnirpagaq
      241 vfpgfspena vsgsrnsvaa yadvelevtd rwllegalry enysdfgstf nyklatnvkl
      301 apnfnwrgav stgfrapsla qiyysststl iqqgkttqvg tfrnnseaaq algipklkqe
      361 tsqsystgit wripalslaf tadvyyikik drvvltdlff rpngsftpgs dqavlqdafd
      421 varasaanff anavdsqtkg lditvsqtsk issgvslenn lginlnqtkr igdihaspkl
      481 vsqidnyfse pnrvyfeeav prikatlsnt lklsdfslvl rnsffgkvtd advvdanfdg
      541 itesgehfvl nsrfvtdlsv gydfnknisa tigsnnlfni lpskspniss ltadnqfvys
      601 rqvsqygigg rfvfarvefk f
//
LOCUS       WP_284459922             225 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Chryseobacterium sp.].
ACCESSION   WP_284459922
VERSION     WP_284459922.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 225)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 225)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 225)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..225
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=26184
     Region          3..223
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mntikcvvvd deplaislle nyirkipffe lvfstenpil aleyikdnds dlifldiqmp
       61 eltginfmki vgarqkyilt tayseyaleg yehniidyll kpvsfdrfqk stlkarerfs
      121 vneetdshff vkssgqqhrl lfndilfies ikdyvnirte deeyivldtl ksmenqlpdq
      181 firihksfii nldkiksiga kkvmlskqei pigdiyranl ldklk
//
LOCUS       WP_284459938             421 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Chryseobacterium sp.].
ACCESSION   WP_284459938
VERSION     WP_284459938.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..421
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46126
     Region          7..419
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtqnkgkali igagiaglss ayylvqkgwq veileqnnls nncsygnagm ivpshftpla
       61 apgvvaqgir wmfdskspfy vrpslnsnli swglkflkhs nqqhvdrsas airdlnlass
      121 alyneiaqke efdfelnqng ilmlyktekv aeeetelahk ainlglavdi ldqkgiqele
      181 pntkldvigg inykcdghmn pmklmkqmis yltsngvifh tqhrvtgiet sgsyikavia
      241 nnsrftadrf vmtggsflpe laqkagikih lmpgkgysfm hrpvnpvntm ehaalllear
      301 vavtpmggqi rfggtmelas hqdkinikrv egivgsipqy lpdfqvelpk qsdiwfgyrp
      361 capdglpylg qssqlknlii aggggmmgls lgpifgktvs elandqkptv eikifnperf
      421 s
//
LOCUS       WP_284459977             103 aa            linear   BCT 25-DEC-2024
DEFINITION  lactonase family protein, partial [Chryseobacterium sp.].
ACCESSION   WP_284459977
VERSION     WP_284459977.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..>103
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
     Region          <2..>103
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 mflpdlgadk irsyhfenek heplspaepp ftqavlgsgp rhltfhpngk yaycieemgg
       61 vvsvygydkg rlapiqridt hsekfkedfe ssdvhispdg lfl
//
LOCUS       WP_284460063             340 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase family protein [Chryseobacterium].
ACCESSION   WP_284460063
VERSION     WP_284460063.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium
  ORGANISM  Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Chryseobacterium"
                     /db_xref="taxon:59732"
     Protein         1..340
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=39967
     Region          1..337
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mkitqitftr flaamaivis hfnkdmflyq idyisniflk anvgvsyffi lsgfimivay
       61 hkkdrinyfd yyknrfariy plyvlgllly litrysgfsf ykaflyllgl qswipgeami
      121 lnfpgwsisv eflfylifpl lynhfyskgn ksvwvitaii wmvtqvfcsl yagslyyegp
      181 hteshellyy fplmhinefl vgnlaglffv knhkqknydv pvivifllil lalifvplfy
      241 hnglmallfi pliilisknn gtltrifslk pleylgeasy avyithipvl yilreileqy
      301 nfgidtifwm ymgvlmitsa lfyqfiekpl rdyikkikis
//
LOCUS       WP_284459982             241 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial
            [Chryseobacterium sp.].
ACCESSION   WP_284459982
VERSION     WP_284459982.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         <1..241
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
     Region          10..241
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 dfpsvisyif mfpialtfyy sirksiyist lffltipfsl lynyyfvdnv dksdslyytf
       61 sntytvvcaf ilfcvcfyyl iqiqklkavl vfleensvti dpfpglerke kirfvqesfl
      121 edtdlpipfy edlfskieeh mksqkpwrnp dynlkqlakd vnsntqyvss ainscsrnnf
      181 ksylndfrln afitlinnkn eefsledayl tigfynrstf nrvfkskfqm tpqeylssqs
      241 n
//
LOCUS       WP_284460066             313 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Chryseobacterium sp.].
ACCESSION   WP_284460066
VERSION     WP_284460066.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..313
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35940
     Region          1..>117
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkisviipvy naekfvsqav esalqfnevh eviliedrsp dnalqvckql iekndrikly
       61 qhpdkgnhga gptrnlgiqk atgdfiafld addyflpnrf daekelfkdp kvegvygalg
      121 vhyytekake qyypvfgdkl ttvhkkhgpk dvfpgqiyll gsfglfsidt ltirrdalvk
      181 kmnalfkasl rlhqdseflf rlsyyldlyp gildkaiamr gvhennritq vdskkinpat
      241 trvllwqevd nwakneetip dhiklhinrm yrsfriattp apqkwgvilk hlisdypsir
      301 sgiyninfrk nlf
//
LOCUS       WP_284460078             164 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor, partial
            [Chryseobacterium sp.].
ACCESSION   WP_284460078
VERSION     WP_284460078.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 164)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 164)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 164)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         <1..164
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
     Region          <4..159
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 hkipacifvs shpelaatvf eintldfitk pltaerfhys mqrlfdffkv kekcdcydal
       61 fgenfikike ggnisqirkt dvlylealkd ytriitlekn hcildslgnl llknffdsfv
      121 rihrsyavpr hlirgksche ielthhiklp igrayknnls ffep
//
LOCUS       WP_284460085             274 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284460085
VERSION     WP_284460085.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..274
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31959
     Region          35..274
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mdetnptpak laddavaykq irgtdnynkt tkctyflvvl fikgsgihyi ddrefpiann
       61 qlhflfpgqh hhwvtgpetv ahkivvgqki fetfsssdef sfmrhnlnpv fklsetmfth
      121 vdaemegikr dvtflnhdds wkrilqlrmd iiasmmrrea esyikdnllp rtnaitkkfw
      181 dlinenyieh ksiswyadkl avtpnylnil ckkhmnmtat dmihykimqe akkqlrfsed
      241 siktitfnlg fdnmaafssf fkkksnfspk eyra
//
LOCUS       WP_284460168             144 aa            linear   BCT 25-DEC-2024
DEFINITION  bleomycin resistance protein [Chryseobacterium sp.].
ACCESSION   WP_284460168
VERSION     WP_284460168.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..144
                     /product="bleomycin resistance protein"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=16952
     Region          12..135
                     /region_name="BLMA_like"
                     /note="Bleomycin binding protein (BLMA) and similar
                     proteins; cd08349"
                     /db_xref="CDD:319937"
     Site            order(12..14,44,51..53,55,78..83,88..89,92,133)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319937"
     Site            order(36..37,44,55,57..58,80,115,122,124,128..130,132)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:319937"
ORIGIN      
        1 mnadtikfnr lipellvtdi dnskkfymeq lgftleyere edcfalisye gaqlmleqns
       61 sdswltdqlv fprgrginfq ievnclddii dkietnklay frepkeiwyr intmeegvke
      121 lliqdsdgyl lrfqqylger evsq
//
LOCUS       WP_284460223             336 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Chryseobacterium sp.].
ACCESSION   WP_284460223
VERSION     WP_284460223.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..336
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36345
     Region          22..329
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtqhiktwsl lillpmllii vslmigssqn igfgelfhhi alefglsedk agfqeslhti
       61 lwqvrlprii ltflvgasla ssggvlqavf rnpivdpftl gissgsafga alamlfpima
      121 vnisafifgv iavvityavs yagaktsivs mvlagmivsg vftafltvlq ylsdpyrlqa
      181 ivqwtmgnlh taswqkvhta vfpiligllv ivilrwklnl lalgdheama vgvnplwlkl
      241 ilmavatmvt assvaavgvi slfglivphi srmifgpnnh itvwanisig gtfllliddf
      301 srtvmpfeip igvftmiiga pvfiylmrrn ainwns
//
LOCUS       WP_284460308             186 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [Chryseobacterium].
ACCESSION   WP_284460308
VERSION     WP_284460308.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium
  ORGANISM  Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Chryseobacterium"
                     /db_xref="taxon:59732"
     Protein         1..186
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=20328
     Region          <51..>180
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          64..94
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          99..124
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          142..169
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mktakvnikn lflglilvgg asfvnaqttq tdsanntant aatsqtgnpt idglkkqiea
       61 npkdteslsk latayqdasd wtnaidtwkk isallpdwap syysqayayq sakddanakl
      121 ayekyiatvk peeveqnkkn layayfyiaf aeqqsdpnka kehiaksiqy dptnqdaikl
      181 sktlns
//
LOCUS       WP_284460419             705 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Chryseobacterium sp.].
ACCESSION   WP_284460419
VERSION     WP_284460419.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 705)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 705)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 705)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 705)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..705
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80028
     Region          6..655
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mkkkvlsils lsaiflvsaq qqdslkqkki eevvvtgqyt qqsinksiyk vevinaeqik
       61 nmaatnvadv lnqslnvlii sdrqsgnsta nlmglggeyt kvlidnipvv gdiglgnnid
      121 ltklnvnnve rievvrgsmg vdygsnavag viniitkkng qkpltlnasv qeetvgkeyd
      181 fkkkgegrhi qtlnvgynin dhwyvganin hndfqgfrgt qegykyfeqd gkrgylwqpk
      241 dvlnvdgivr ysknktsify kfgfvnekln yynptvgehf ysvtdrtyfs ndrdylttry
      301 lhqlnvqtkl gavnytgdfs yqtqdrkyrd fkydipnrkv igdkvayqsy nkadvfysrg
      361 vfsnfldskk idfqlgyeld htsgyagnia gtfqgtdnik rkifnyanfm siewnatdwl
      421 slrpgyrlal sdkfdaqhny sltarvkate ndnfrlvvgs anrfpnfdel ytymvdsnhd
      481 irgnenltpe qgmtvsvnge kkiatdsgwn lgvgasatyl hvkdriesvt vsrqplkyqy
      541 lnlnkyesyl feanfraqkn qlalaanvay ygiakqlkdg davspndffy tleanavvny
      601 tvpninttls lfykytgktq efvlssdlkn peyrigerdd fhmmnfivtq pffknqlels
      661 lgvknifdvs airdttlpgn theaadpnin lfygrsylar lsynf
//
LOCUS       WP_284460482             316 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284460482
VERSION     WP_284460482.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..316
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=37225
     Region          <215..316
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrhsdikelr neqdfkdfyl ndapvsfcee cnsvsythgn gfleiakleg lkkgqkaieg
       61 kqtrrkfysi illtegkiee tighqtyhfk agtlyfvsen qlhiinrwse dvkgvfcmfd
      121 adyfllcikh qiklnqfpff qmsrkpfiel seretemmeh lfwklnsekc qkttfnddll
      181 trmflniill eaeriynknt aeepfslsrk dqltarfqll vnqhfiekkq vadyadllyi
      241 hpnhlndtik evtgfpashf iqkqliqeak srllqtnatv smiamdlnft ddsyfgrffk
      301 kqtgvtplqy rknhkh
//
LOCUS       WP_284460505             417 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284460505
VERSION     WP_284460505.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..417
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47189
     Region          18..405
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mknlnysflf vlmiifcqaq kkqsaelikv qkeltdkltk iskntsfngf gvalvndhdi
       61 lyqngfgvat lkplqkyden tvqniasvsk tligiavlka qelgklkldd pvnqylpfkv
      121 tnpyhpqipv tirqltthts sindntayln ntivlkdtvn lanhlhidis ptrfnppsak
      181 isieeflthv lsekgkwyak dvftenkpge lfnysnigat laalvlekat gmsydtftak
      241 yileplqmnh sgwkfnainf skytqtfink qtpypyysln typdgglltt ssdmskylle
      301 lmkgyfgngs ilskesykey ftpqlkaenf kdrsnseysd eynmgitmgf gstgnfghtg
      361 gdpgmnsviw ffkdqrmgry livntdwdqk vsgkdqkaiy dlldeyfikl dalsrlh
//
LOCUS       WP_284460507             308 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284460507
VERSION     WP_284460507.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..308
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34932
     Region          14..303
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkrssqmgnf ngnilvsenn riiyhasfgf tdatktkklt tdyrfnigsi tkefsgvall
       61 qlqeqgklki edhvsqyipe lpkwanevti kdllqytsgl pnvnwkkikn dkdifddlkl
      121 idkldfvpgt qydynmnnvf lrqfilerit gipfnlyaek fifkpckmts svmtpfenen
      181 niakgfnnds vadkadlplt ggtylttldl lkwsgclhsn kvinadslfe lgqqfnllet
      241 qsslgqakfk nrkliehvhd grygnyealf vsdpnkklti illgnnhngk lfeisdaiag
      301 ilknkkek
//
LOCUS       WP_284460269             437 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Chryseobacterium sp.].
ACCESSION   WP_284460269
VERSION     WP_284460269.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..437
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50689
     Region          32..435
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 msknnilwll ynllaitsgi tayhffleek wfsmmlfill mivfvalmyf slaaqdskve
       61 kvissirnkd fslfpqeegs plldssmrly yqskeeqfsl ssykllyesi ldqmetglii
      121 lsenktrevf yvnnaflsil qvprynrwel yaskvpefyk iiedthyqss qeffdisihs
      181 nsrqsfslrt qqvkntqhnf yiitlesvqk iieqkeklaw nnlmkvishe llntltpvns
      241 liqnleyisn qetidhedqq dmkeslmvin skskqllnfv dhyrqvaelp kpvlspvslk
      301 kviesaarfl ksefekhhiq mvpdiedytv sadekmiers linlylnaih avsekeykli
      361 tttvksqnnr iivsitdngs giipeikdki flpffttran gsgigltlak simeahggyl
      421 nyktleegss felwflk
//
LOCUS       WP_284460526             368 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Chryseobacterium sp.].
ACCESSION   WP_284460526
VERSION     WP_284460526.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..368
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41662
     Region          13..368
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 misiweletf yskrdiiiig agfsglwtav sikekypeks vliiernavp lgastrnagf
       61 acfgsltevi adaqkmgwek tldlvamrfn glqkireyfk sdeidfelsg gyeilnneep
      121 lqhldivnek lrsvtglekt yhlkqdkied fglgkskfli enicegslhs gkllqkllek
      181 chelkvsflf gtaveniden pdevlvhlse glsvktdqli yctnafsskf lekeeiipar
      241 gqilltepie nlklkgtfhy degfyyfrnl enrvllgggr nqdfkteett tfetteflqn
      301 hlenflkevi lpdheykial rwsgimamgs ektpiikqls ekqfcavrls gmgvalapki
      361 geivvemi
//
LOCUS       WP_284460529             241 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Chryseobacterium sp.].
ACCESSION   WP_284460529
VERSION     WP_284460529.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 241)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..241
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26981
     Region          1..235
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mltahtikil qsldkkkfrq kynlflvegn kiicelpnsn ikvkeifstd pqkldrsdip
       61 vshisenelk kisflktpkd svavcylaae ermedkniql vldgiqdpgn lgtiirladw
      121 fgieqiicse dtvdfynpkv iqasmgsftr vnivytdlve ylsetdnvni gtdmdgesiy
      181 sfqrpekinl ilgnegngmr peteallqqr itiprfgssq steslnvsma agiilgqlfs
      241 k
//
LOCUS       WP_284460539             474 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Chryseobacterium sp.].
ACCESSION   WP_284460539
VERSION     WP_284460539.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18640651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..474
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=55649
     Region          9..326
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          <394..454
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mfpnfrikil yliffsfsvf fdaqdfsfqp epikttleyr krldaegalk yninaltqye
       61 knddtkgvim vytnigsils gldrnkesle yldkakkell hsndpflkan lyneygrnyt
      121 rlglyeqsna afdqaasyik kitnlkqref alaynyswkq qnfpkdknld slqaikkkil
      181 gskpnitsyt rtadkfiaek khldsaeyym nkafaysnta sdiekatawf sygdlynikg
      241 nkekaleyyl ksldvfqktk ntpgslltvy dtlssvyksl neieksnefl rkytilhddi
      301 sknekeavnl avntlidlkh eekgkerrmf yvivmlivvs fglllyfirk iyikkvlkkd
      361 kilekkiiet dvlklkvnns fdeiiqlmes rsplflvrfk evypefyekl ithtpelteh
      421 dikfsayirl nltnkeicqy enisvrgiet kryrlkkklk lssntdlqkw ildl
//
LOCUS       WP_284460598             494 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284460598
VERSION     WP_284460598.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..494
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=56645
     Region          176..469
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtkythfilp ffifffsntq aqiektdaly ktimsrdsll fsvgfntcni sqmenmlsdr
       61 lefyhdkdgi sdkkkfmidf knglckapem rqvkrvlidk sseiypmyqn gklyaviqng
      121 shefsekekg kpeklggkak ftnfwmieng swklakslsf dhqakstiqe nipgddqtie
      181 swlkdnkipt lglgiieegk lkqirvfgei kkgvpapynt yfnvasltkp vtamvalrlv
      241 slgkwkldep ldqywvdpdv lndprhrklt trlilshqtg fpnwrwmnpd kklnfqfepg
      301 tqyqysgegf eylrkalekk lgkplnqlar elifqplsmn dtdyiwnqht eesrfaigyn
      361 kegqpyptek nkvanaaddl httiqdygnf mvsvmkgehl kpevfqemtk nqvktkenky
      421 fglgfeiydl gngnyalshg gadlgtccia fvlpksgkgi liftnvddgy kvyeklvvhy
      481 lgeegkkiva ietk
//
LOCUS       WP_284460677             573 aa            linear   BCT 25-DEC-2024
DEFINITION  polysaccharide biosynthesis protein [Chryseobacterium sp.].
ACCESSION   WP_284460677
VERSION     WP_284460677.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 573)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 573)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 573)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18500220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..573
                     /product="polysaccharide biosynthesis protein"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=64741
     Region          66..186
                     /region_name="FlaA1"
                     /note="NDP-sugar epimerase, includes UDP-GlcNAc-inverting
                     4,6-dehydratase FlaA1 and capsular polysaccharide
                     biosynthesis protein EpsC [Cell wall/membrane/envelope
                     biogenesis, Posttranslational modification, protein
                     turnover, chaperones]; COG1086"
                     /db_xref="CDD:440703"
     Region          229..514
                     /region_name="Polysacc_synt_2"
                     /note="Polysaccharide biosynthesis protein; pfam02719"
                     /db_xref="CDD:426938"
     Site            order(233,235..238,258..259,285..287,308..310,312,327,350,
                     366,391..394,397..398)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(259,261,265,269,283..286,289,292,310..313,316,320,
                     323,326,398..399,404)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187548"
     Site            order(312,352..354,362,392..393,399..401,404..405,
                     416..418,422,424,459,486,489)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(328,352,362,366)
                     /site_type="active"
                     /db_xref="CDD:187548"
ORIGIN      
        1 mflfktyagi irystffdff kivwasgstl ivllglnfis elilgkpvyl ypvlflfffi
       61 stflmfffrm vtkqlfrmfr nskkdpckir iavigveges vslanaiihn pghayqlagf
      121 lsarpdskka mllghkiynk qsllrndhwv sqfdailine tmprpkmedw talalnkglk
      181 ilkapnvnht keegiiggir plqiedlldr apikieseev ksrhynksil vtggagsigs
      241 eivrqvaqld sslivvvdqa esplhelkle llerfpnqkf kfvladisnl yrleklfedy
      301 sfsivyhaaa ykhvpliedn pheaifvnig gtknlallsr qynvdrfvmv stdkavnptn
      361 vmgaskraae lfvqslqdss dnttkfittr fgnvlgsngs viphfrkqia kggpvtithp
      421 diiryfmtip eacelvlqag tmgnggeiyv fdmgkpikil dlakrmikls gytpdvdiki
      481 dfiglrpgek lyeelltdns ttipthheki miskdpvmef edieilckqi mrsaikkdgl
      541 qvvkilkiiv pefisnnsef eildktpeye vyq
//
LOCUS       WP_284460703             267 aa            linear   BCT 25-DEC-2024
DEFINITION  arylamine N-acetyltransferase family protein [Chryseobacterium
            sp.].
ACCESSION   WP_284460703
VERSION     WP_284460703.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Zhou,X., Ma,Z., Dong,D. and Wu,B.
  TITLE     Arylamine N-acetyltransferases: a structural perspective
  JOURNAL   Br J Pharmacol 169 (4), 748-760 (2013)
   PUBMED   23517104
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Sim,E., Walters,K. and Boukouvala,S.
  TITLE     Arylamine N-acetyltransferases: from structure to function
  JOURNAL   Drug Metab Rev 40 (3), 479-510 (2008)
   PUBMED   18642144
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Sim,E., Westwood,I. and Fullam,E.
  TITLE     Arylamine N-acetyltransferases
  JOURNAL   Expert Opin Drug Metab Toxicol 3 (2), 169-184 (2007)
   PUBMED   17428149
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Sinclair,J.C., Sandy,J., Delgoda,R., Sim,E. and Noble,M.E.
  TITLE     Structure of arylamine N-acetyltransferase reveals a catalytic
            triad
  JOURNAL   Nat Struct Biol 7 (7), 560-564 (2000)
   PUBMED   10876241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..267
                     /product="arylamine N-acetyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31313
     Region          3..252
                     /region_name="NhoA"
                     /note="Arylamine N-acetyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2162"
                     /db_xref="CDD:441765"
ORIGIN      
        1 mdqlklekyl ervhfsgape mnmetlkrih qlhpqyipfe nidpytgnvp slnlddvfnk
       61 lvtesrggyc feqnlllrev lkyigfdtrl qqarvvwkre edaiaakthl llivnmhgqe
      121 ylvdcgfgiv tltaplllhn eepqqtpnge fkiskkegly ilwfwkekwl pvyrfalehv
      181 epldldianw ylstypesmf kknlvlskvd eearytfsdh tlnirketne kesvaiehde
      241 qlfqilkdif glkenavkll kekitke
//
LOCUS       WP_284460708             150 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial
            [Chryseobacterium sp.].
ACCESSION   WP_284460708
VERSION     WP_284460708.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         <1..150
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
     Region          <57..148
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 ylfvaldkpe ffrgvnsllk pisdvapkqk sspiiddekn kqieslkdfm vkkepyldss
       61 ltiqdlaeql kmpvkdlstl inlymdkhff dfvneyriek akeilkdplq keltileily
      121 qvgfnskssf stsfkkytgt tptdfrknpn
//
LOCUS       WP_284460720             318 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein, partial [Chryseobacterium sp.].
ACCESSION   WP_284460720
VERSION     WP_284460720.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..>318
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          76..295
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
ORIGIN      
        1 mirsllfmvl iilfscnqra rqqdeknfdt tlwkkneqfr lsgdydslls lntryyrkad
       61 qmgyedgkal cyiniaelni tlvnyqktrv lfdkareile nsqnnlhkak fyimyghfns
      121 tltkpdkafe dynealnnls ksddsplkdk llfdlyielg syfalkkdyg kglklfqkaq
      181 klddtgfaec iigdyiymyr nqdsaykyia tayhktnisg kkdkialyan tmmgewykae
      241 eqydeaeeml lqaleidkkt rrihanysky iyndlrmvye rkgdrekayf ylnayndams
      301 ktntaiytti nqdmesfi
//
LOCUS       WP_284460726             291 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284460726
VERSION     WP_284460726.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..291
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33646
     Region          <185..290
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mallitldnv yklynldpsk ktegivilsq qndpnkkyts hsrlfdglll gfmvqgsmks
       61 qihfldyein tgdiailqpq lmidtkslse daqivtigls ldfitefpil refvmnnqir
      121 wqpiirlqpe ditlqnellt liqnfyhkkp spnktqmlrh lvmvlismis evysnsannk
      181 slvknrthei iddfyllisk haneqrnvaf yakklhltpq ylssflkqkt gksalqwidh
      241 itilhaktll kssnlsikei snelyfeets vfcryfkriv gmspktyrne s
//
LOCUS       WP_284460757             245 aa            linear   BCT 25-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Chryseobacterium sp.].
ACCESSION   WP_284460757
VERSION     WP_284460757.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Bagautdinov,B. and Kunishima,N.
  TITLE     Crystal structures of shikimate dehydrogenase AroE from Thermus
            thermophilus HB8 and its cofactor and substrate complexes: insights
            into the enzymatic mechanism
  JOURNAL   J Mol Biol 373 (2), 424-438 (2007)
   PUBMED   17825835
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..245
                     /product="shikimate dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27869
     Region          5..244
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 mdsnkkigli grnisysfsk kffenkfqkl mlkgftydii dlneideveh lfsspellgf
       61 nvtipykeki idyldelsde aekigavncv lirdgkktgy ntdafgfekt lflhkqptqd
      121 kalilgngga akavkyildk nnipskiisr nteinfenld qetvkehkii iqctpvgtfp
      181 nvedclsfpf daissdhlvi dliynpnytk fiinaaekga ktvngyymle qqaekaweiw
      241 nfqkk
//
LOCUS       WP_284460781             898 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: TonB-dependent receptor plug domain-containing
            protein [Chryseobacterium].
ACCESSION   WP_284460781
VERSION     WP_284460781.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium
  ORGANISM  Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 898)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Chryseobacterium"
                     /db_xref="taxon:59732"
     Protein         1..898
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=99266
     Region          112..743
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mkrivlsaal figsvtilyg qerkidlnag tfevkkcgmi yankndityt ggceiivkqp
       61 gqapktiflk kneklvvkdk kaaivytdvv sdiridgiel takkknfsei eikqealqni
      121 qsfsigdvlq qlpgqyiqpf dnakfknivf rtasgasits sstslsgdea gnkafgvqvm
      181 vndialsnne nmqsynsayg spfgigfttt agksgtltpa qpnfgvdlre ipteniesie
      241 viqgipdaky gdltsglikv ttfakrsplr ldasiregty qlgltrgfsl kndqalnvsa
      301 dymnsivdpr tslvgydrfs snilwgints niknklsfaf sqntsngkkd pddlqgivls
      361 sknksfslsn nfkyvfkgnk kifrsigadm glsyatqlte rkyflnqgar pygnamensv
      421 yyapytppsy enmtyvdgkp invylnasad gvyatskkwv hsysagfnfr ygdnlgkgky
      481 gtagqfstia saggtangvr dynyqdnvla ttqyafyvqd nifkrlnnkh giranlglry
      541 diqngkstls prvntsyqmg dltlragvgl tskapslnql ytgpryfdml lgdyripghy
      601 tvgimqtvvt pgdnvdlkps kswktefgid yrlpfatinl tgyynklfdg fstisvakmm
      661 dkakveitav gtdvptfeiv gkdtfyylqn ritngyestd kglelmvsfk kiealnlitg
      721 fnasyvktks kknegiptia alpipdpafq yglyndaysn anmarasfsf dyhlpssgli
      781 iglrtdhfli deritsgrsi ypigyidpql ntvmipeger sdqkyqtlfr kaseeslsgl
      841 gkktlhnvhl rvtkdflsgf risiyvnnvf nlkayneygt lytnfspasf ganisykf
//
LOCUS       WP_284460822             971 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp.].
ACCESSION   WP_284460822
VERSION     WP_284460822.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 971)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 971)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 971)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 971)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..971
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..971
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=108378
     Region          22..969
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvrisrslg lvavlyftan fsaqtkvkdt lskenkidei vmigygsqkk snvtgaissv
       61 rakdiedips gkpeqvlqgr tagvsvvtns gqpgsaatvr vrgvtsfgag sndplwvvdg
      121 ivvdniawln qsdienieil kdgassaiyg vsaakgvilv ttkkgrkgkm nlsyngfygv
      181 gsaakkldll nasqygtiin ealtnagkdp rftnpqsfga gtdwqdvafn taermshefs
      241 isggndkstf yssfgyyeqd givlrdisny krmnvrlnst hkvfdfltig qtlsythqkt
      301 kginandeyg gplssvinld pitpvvvtdp allntspynn sglspylird afgnpygvst
      361 ivenemtnpl afrqtqlgky nwsddfvanv faelkfldhf tfkttlngkl sywgkeqftp
      421 kyylntnsrn tvfnsflres nrklewnten tltyqnkwga hnlsvligqg ayyynigsgn
      481 nttyinlpvn swedasfnfd vpqenrstva ndgvqthkas yfarviydye dkylftgtir
      541 rdgsskfakg qhwgnfpafs lgwnvsnenf wpenkivntl kfrggygvlg ndaienfrfa
      601 nflksgsnyt ygdnnivigy apttlenpnl rweetsqlni aadlkllqdf tltvdwfkkk
      661 ttdilrqvdi pgyvgaperp wrnvgdmdnt gveialgykk nwndfgisvn gnfsylknev
      721 trleddkiye nfatfqsmgp vtrfqvgspy gaffgyknag ifqtqaeida yrnangdliq
      781 pgakpgdfrr tdvngdgkis dedyeylgss vpkftygltv nlnyknvdlm ifaqgqggnk
      841 ifqglrrldl fysnyqttil drwtgpgtsn tvarldandd nknytkmsdy ylqdggfmri
      901 klvqlgytlp gdvskrfgan kirfyvtgen lftftkytgy dpeiavndsy gidrayypqa
      961 rtflfganiq f
//
LOCUS       WP_284460828             261 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase
            [Chryseobacterium].
ACCESSION   WP_284460828
VERSION     WP_284460828.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium
  ORGANISM  Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Chryseobacterium"
                     /db_xref="taxon:59732"
     Protein         1..261
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29160
     Region          1..259
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 metkesyavi tgasqglgka faenlakkni nvilvslphq nlkelteele knysikahyy
       61 evdlsihdnv mkltawlnqs feihilinna glggtkkfte assdyintil qvnvtatsli
      121 thqllpnllr qskayilnvs smaafspigf ktvypasktf ihsfsrglhe elkdtnvfvs
      181 vvnpgamktn tdvckriekq gflgrltlln pdkvasycih qlfkkdsvim vnpiswlimk
      241 ilpiwiklpl mtqaikreie a
//
LOCUS       WP_284460858             946 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Chryseobacterium sp.].
ACCESSION   WP_284460858
VERSION     WP_284460858.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 946)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 946)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 946)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 946)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..946
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..946
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=103006
     Region          11..879
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mrknnqkivs lgalffisvn fyaqtgdsik vktvdevkit vgsrnksrva tdtpvpvdvi
       61 nigsqsvlsp qtdlnqilny aapsftsnst tvadgtdhvd paqlrglgpd qvlvllngkr
      121 rhtsslvnin gspgrgsvgt dlnaipafai erlevlrdga saqygsdaia gvinvimkks
      181 tnnltaaita ggynskgsnd hsggwdgeky qldlnygakl gatgflnfta sflnraatgr
      241 agtatgdifn aynaieqral engvninslf gnitntsntq qivnyihqya pyvnyfspgm
      301 lmsiqnanti pelqtilrad vtaneliyrg lerndfnmrv gqsklgsgqv fmnsefdiss
      361 svrgyafggi syrsgnaagf yrrpnqsrts tslypngflp eiasdvidls laagfkgkvg
      421 nvnydisntf gqntfdytik ntanasmlss mqrefraggl gflqntinad fdtkfdwlqg
      481 fnmafggevr lerykiesge easwalydin gniqnpetva slkptdfmga trpggaqvfp
      541 gfrpenalkk grssvaayld teldvtnrwl vsaafrfeny sdfgstfnyk iasrykltdh
      601 iniraahstg frapslqqiy fnatatqfvg gtayevgtfs ndsqvakilg ipqlkqeesn
      661 sfsagftaki psanltftvd gyyikiknrv vltdqfsrps gvfpvdspey nlqkgfdqan
      721 ataatffana idtqtkgieg vishrlkise kvtlnsdlaa tvsktnrvge ihgsdiliqa
      781 gqvnryyset srvyleeavp rfkvslnnal elnnfsilvr nvyfgkvtdp nttdvngdgi
      841 vdsnmingkq vpvehpvwgg kvitdlsigy kftkglrlti gannlfdiyp dknygprslk
      901 tpsvdasgnp insidlsnqd qfvysrnvsq fgmngrflfv rmnlsl
//
LOCUS       WP_284460915             252 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Chryseobacterium sp.].
ACCESSION   WP_284460915
VERSION     WP_284460915.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 252)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..252
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29330
     Region          54..239
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mndidskeqi lkrsveakei ylphlsadpv ifgfdqnelk vllakmnyrk qwllpggyvh
       61 kdedldeavl rilesrtgvt nvfleefgvf gkrnrselyf edfddslfqk qrfisvgyya
      121 lynsseinpv ademsetcew vylkqlpeie lamdhreiid kalltlreki sykpigynll
      181 pekftlpelq klyeailgkt lnrgnfygki knlgilrkle eqrrggahks pdlysfdqen
      241 ytkalengln nw
//
LOCUS       WP_284460940             200 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II [Chryseobacterium sp.].
ACCESSION   WP_284460940
VERSION     WP_284460940.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..200
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22110
     Region          14..198
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 mnsninnqhs kskvlvfdny dsftynlvqi iekildqkvd vvrndkitle evgtydkiil
       61 spgpgipeea gilldlikky aptksilgvc lgqqaiaeaf ggslvnlsei fhgvatttei
      121 vkentlifkn itsglevgry hswavnpenf peeleitavd kdgmimalqh ktydvhgvqf
      181 hpesiltpeg etiiknfllq
//
LOCUS       WP_284461112             471 aa            linear   BCT 25-DEC-2024
DEFINITION  leucyl aminopeptidase family protein [Chryseobacterium sp.].
ACCESSION   WP_284461112
VERSION     WP_284461112.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Drinkwater,N., Malcolm,T.R. and McGowan,S.
  TITLE     M17 aminopeptidases diversify function by moderating their
            macromolecular assemblies and active site environment
  JOURNAL   Biochimie 166, 38-51 (2019)
   PUBMED   30654132
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Lowther,W.T. and Matthews,B.W.
  TITLE     Metalloaminopeptidases: common functional themes in disparate
            structural surroundings
  JOURNAL   Chem Rev 102 (12), 4581-4608 (2002)
   PUBMED   12475202
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415720
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..471
                     /product="leucyl aminopeptidase family protein"
                     /EC_number="3.4.11.-"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0030145 - manganese ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0019538 - protein metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52288
     Region          38..470
                     /region_name="PepB"
                     /note="Leucyl aminopeptidase [Amino acid transport and
                     metabolism]; COG0260"
                     /db_xref="CDD:440030"
ORIGIN      
        1 mklihkknkn ytqvfqlfte eewaksntnf nknistffng kkyetfihtd ektityfigl
       61 gkaslqdfev qqvgntfsqa qkerllavpt lvvadfinkk qceefvkgll igtynypfek
      121 thtfwapafe lhfenisqkt ldhigqkaea lsngqtacqe wlnkpanlkk pdifssylkn
      181 lakkqglkyt vfnrkkceel glgaylavnq gsaydaafti leykstvkna ktvglvgkcv
      241 lfdtggisik gsanlhymks dmggatavlg tliyaaemkl pvniiavlpi tdnavsekal
      301 lpsdvvtayn gktievidtd aegrmiladg lsylarnykt dcmidlatlt gssvrmfgdt
      361 cgalfsnned lknlliktgd htnqrlwnlp lwdiwkddiq sdvadlknis lkpigdciia
      421 akfleqfteg hpnwahldia gvafgnvkya kekaatgfgv qlladlieny h
//
LOCUS       WP_284461118             794 aa            linear   BCT 25-DEC-2024
DEFINITION  GumC family protein [Chryseobacterium sp.].
ACCESSION   WP_284461118
VERSION     WP_284461118.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 794)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 794)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 794)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..794
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=88709
     Region          1..767
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mntqdslqps evkknsdiei qeiikpyiqk wpwfvicvil aiaigwfmlr fvtpvykvqs
       61 tvlikdsknt sgggaemgml qdlsgfggmk tnsvdnelei fkskqimrnv vdsknlqvnv
      121 yvknglknie lykesspisi kvvneksdve fpkkpivvti kgntitlasd elqkeivgqf
      181 nslislpyan iiitknpdfn vnkvknintn vlqinissfe gkvtllqsll nvnlankest
      241 vitlalnypq vdkakdilns lvdaynrdai fdknsesqkt ldfidervkk isvelgdven
      301 kkedfksknk itdigteaki dlessaaart kqldldaqle ltnallnfvs kqgqysvlpt
      361 nvglsnaeat agistynqli lqrnrllesa tsenptvidv tkqinqmrsg viqslqrnkv
      421 slelasgeyq seqskvsgki srmptleklf rgierqqqik enlyllllqk reetaislai
      481 tapkarvidk aypsdapvsp kkaiiyfgal vigmlipfvv iylrellnnk ikskhdlqkl
      541 shspilgelp svlkgdpdiv qvndnspmae afrilitnmn fllpkkdtgk vvfvtstvkg
      601 egktftsvnl altlatpskk viiigsdirn pqlqryntsr kglkglteyl ysdqtaledi
      661 ihvtsfnphc dviysgmipp nptellsngr yeklleilka kydyiivdta plllvtdtfl
      721 fadltdatiy vtrsryteks liefansnid snkiknvgfv lndvdknhyg ygnkygygys
      781 akekswleki kekl
//
LOCUS       WP_284461163             469 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Chryseobacterium sp.].
ACCESSION   WP_284461163
VERSION     WP_284461163.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 469)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..469
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=52558
     Region          47..467
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mkghlksdse qidylldiik rqgteylnni tdrptsidht fipglqslpe tgygtekalq
       61 ifnekfepim vgsggprywg fvtggatpas ivgdwlatiy dqntqtvsgq gdisanieie
      121 tiqllltllq lpenflggfv sgatmsnftc lavgrqwlgk eqgrdiakeg vsgtvkilta
      181 tphsssiksl sllglgsdni vkikteegnr eainikdlee hilrltgepf ilissggtvn
      241 tvdfddfkai selkekynfw whidaafggf aacsdsykyl vegweyadsi tvdchkwlnv
      301 pyesavflik eqhkilqvet fqnsnapylg dplenfsyln flpensrrlk alpawfsima
      361 ygrkgyqeiv dkniswakqf geliensndf kllapvrlnt vcftlkdevk edevgrflek
      421 lndtgkvfmt ptfynqhngi raafvnwmts ekdvqlvfdl mneiiteik
//
LOCUS       WP_284461186             108 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Chryseobacterium sp.].
ACCESSION   WP_284461186
VERSION     WP_284461186.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 108)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..108
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=12481
     Region          <8..99
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 menrtfafvk tdkkliklff kditiikglg nyvevhtlnh kryiyykslk elidnlpdgf
       61 mrvhnsyivn iiniesfedn qlicgtlkia vaksykeclt talntmml
//
LOCUS       WP_284461221             424 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Chryseobacterium sp.].
ACCESSION   WP_284461221
VERSION     WP_284461221.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..424
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=48108
     Region          17..406
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mdnkktnpkk kqgksltkri tgwlhlwlgl vsgiivltvt lsgtvfvfcd eiidlcggsa
       61 kyvqvpanak krspeellaq fhqqvpdrka fyfdtykead rsfrvasatk ppkdknteka
      121 ekpkgkgrgp rgvfayhyld pytgkvmgst ksyeffyvva hihaqllagk fgktvvgvas
      181 iiffiqligg lilwwpkkwn kttrttafki ksgtkwrrkn ydfhnvfgfy sllpavfiti
      241 tglimaykvl tdltqtafgg vadahkiaek fdpkfnpekk alpftafidr nfkeipeakq
      301 irmsvprnds atvynvvaaq figlksitng ksreinkytg neiiypkevl mheviehmnf
      361 dlhvgywggm fgkiftfvig iictslpvtg fliwwgrknk stkktkeikt ihqhrkdehh
      421 eqlv
//
LOCUS       WP_284461361             538 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284461361
VERSION     WP_284461361.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..538
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=62522
     Region          <413..531
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkkiylffil fpfyaifaqn tkpskaeisq ieiidaeike ykasaasdpv tatkkllqlk
       61 ekceeihyin gamtssmglv llyynegnyk ktieesrfve kyakelqafd yvsdiyrmrs
      121 naygemglld eclkeleksl ididkikspn rriyrksliy esyagayekk gdikkqiiyr
      181 qksiaasiqi pgnepetina kyqnlayqya glgliysnlk vkdsasyyfe kaleiqesgk
      241 yniyvngrai llsdmakfyn dnggyhkail fakkaegfek qasmpyirkd iyhtlfnsyv
      301 etnrqdssky ysklymslsd sllksekenl itpvkqiisd kehenqdnir niliiaalvl
      361 slailigwly wrrknklvhg kyedliakin akqseedlel qsnvennvpk ssivitdeti
      421 kalllkldkf eksekylrkd lsltwmannl ntntkylsei ikvyrnhnft syinelriny
      481 ivkklydnpi yreykityla eecgyatprv fvnafkketg ftpsyfveql kissilyn
//
LOCUS       WP_284461392             248 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Chryseobacterium sp.].
ACCESSION   WP_284461392
VERSION     WP_284461392.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..248
                     /product="metallophosphoesterase family protein"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28551
     Region          4..227
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 miqiavfsdv hgnlpaldsv ledmekrgir qkfclgdlvd fapwgnevte kikdlnipcl
       61 mgnhderiaf dipvvplskh teeetlarfv aidhskkyit esnkkflsel pfhlqlnyki
      121 gekhwniqlv hsslssndty lyesesdevf ikmleesrsd vivmghthls fkkqfennsw
      181 alncgsvgrs keenrlasyl iltldeekii peiiqlnypl detvrriees eipdyyasfl
      241 rneqvsms
//
LOCUS       WP_284461411             806 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Chryseobacterium sp.].
ACCESSION   WP_284461411
VERSION     WP_284461411.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 806)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 806)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 806)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 806)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..806
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87772
     Region          29..754
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mkkkifkkki yalvlsgagt mayaqetvke nnidevvvtt grtkprtiit saipidnisa
       61 vqlkstgqvt fdkaltyavp sfnssqqtvs datahfdpad lrglgpsrtl vlvngkrknq
      121 saliyvndtp gkgevgtdlk sipsaalqnv evlrdgasaq ygsdaiagvi niilknsvgk
      181 stvnlfsgit segdgfniga dfntgirvak ngslnltlgy ssqnktnrag sttkdelfgv
      241 enawtqanpg lgmtigqpet kvanmfvnfe lptgetgkfy afggttyrng tsyglyrtpy
      301 wvtsdfgllt pkgqpyngfq pefktdvydy nltsgwkgmf gkwsfdgsat fgsnavdyvv
      361 gntintslga nsptrfkagg hqfsniigni dinrnfgtfv lgagvevrne nyqakageea
      421 syigtgaesf pglqpqnevn knrqnigayv ntewditknl llggtvryen fsdfgnnvsw
      481 kgnaryklld dklvfrgsvs tgfrapslhq iyysnvqtki tgntvanqgt fnndsqivrs
      541 dlgvpklnae kafnitggfa vkafknltvt adyyrikikd rvlfsgdigy ktgapgnpdt
      601 tnpvevildn nkitslkfft navntvtqgv dfvanyytsa igkgrlgiia afnynetkiv
      661 dniavppila engysenffd rkeqsriisa rpktktilsl sydiskfnfn lnntyfgsvt
      721 wqhatdpakd qtfsgkvvtd ivltykitqd lkisgvvnnl fniypdvids kgdivtdlgg
      781 rfkypwevnq fgfngttfql nvnytf
//
LOCUS       WP_284461430             111 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Chryseobacterium sp.].
ACCESSION   WP_284461430
VERSION     WP_284461430.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..111
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12086
     Region          1..111
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mllmliffmi tssaanqsai evnlpkagat ednipnpltv sikpdgsffv ddnpvnkgel
       61 eqiivnklan qtnksftira dentlhkdvv fvmeiaeknk lniaiatvkd k
//
LOCUS       WP_284461472             363 aa            linear   BCT 25-DEC-2024
DEFINITION  fatty acid desaturase family protein [Chryseobacterium sp.].
ACCESSION   WP_284461472
VERSION     WP_284461472.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..363
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42952
     Region          1..357
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mekpsyfkds ddaklfnelr kkvnqrveei pgnrdiyiqv kavilpliyi slyfvavlna
       61 evpwlyvlsf vvmgvflvli ylnliheaah nniykskrln flvlhifdfv gansyiwkkr
      121 hiashhaypn vdgwdtdieq sglllivpwi kakgvqkyqd kffflvyply lfnwmfirdf
      181 rdffdkervi lktqgripvi ekvkmigykl fyffyqivvp vmffkvsvgl algawflqvi
      241 sasifalfvl lplhplpdna fprldrnngl pfswlrhqfe vtndlkennw lvrnvlgnfn
      301 fhvahhlfpn ysymyyneit eeiekfakeh glaykrfpli talakhrdll rqnannayyi
      361 lee
//
LOCUS       WP_284461553             369 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284461553
VERSION     WP_284461553.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..369
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39645
     Region          26..365
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkkflllavi ifmtscshdd spdrkaqvqq klnaalsnfp glslsvktas gnytlvagda
       61 vinekpmaas alhymqsisk tftavavlkl keegkinlda kvntylpdic nhlpngniit
      121 vrqlltmtsg lpdyldsgqf lddvvagplp mtseqvlsyv ynqpakfapg tsfgycniny
      181 hllaliidrv tpnghrkyit dkiinalgls ntyyiagsan ttapvgttan ylqidgtftd
      241 mselqlgtvl tligddgiva svqdiagfyy kllhdktvvs pasleemkva vnhqgtptyg
      301 lglhfyktng glqaighegs gvgagayafy fpskntsvvl ctnagtlidt ikeeqlraly
      361 eeiigillq
//
LOCUS       WP_284461543             689 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Chryseobacterium sp.].
ACCESSION   WP_284461543
VERSION     WP_284461543.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 689)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 689)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 689)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 689)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..689
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..689
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78252
     Region          22..628
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mkrilfsitf lssycfsqet dslslhqnkn idstriskke iktssiedvv vtgtikpmsr
       61 skspvaveiy sqkffqknpt psifeaiamv ngvkpqlncs vcntgdihin glegpytmil
      121 idgmpivssl stvyglsgip nslvdrievv kgpassiygs eamggvinii tknaltapkl
      181 svdlmtttws ennldlstkf nvgknaasll slnyfsfqek idqnkdnftd ttlqsrisvf
      241 nkwnfkrken rqasfamryl yedrfggemq wnksyrgsde vygesiytnr aevfglyewp
      301 mkehivtqfs ynyhdqnsfy ganpfnalqk vafvqtywdr sfgkhditag ltfkrtfydd
      361 ntpgtlgadg itnapmkspi wgafiqdqwe indkntlllg yrydydkvhh svhsprlawk
      421 fspnpyhtlr fnfgtgfrvv nlftedhaal tgsrevvvks dlkpersvng nlnyiwkipv
      481 gtrmvnldas afytyfsnki vgdfdsdpdk iiydnlhgyg isrgaslnvd fsfsfplsan
      541 lgvtyldvyq kfdnenqktq qlhapkwsgt ynltykfpsn ltvdftgqfy gpmrlpvlpn
      601 dfrpeyspfy slaniqvsks fksgfevycg vknlfnftpk dplmrpfdpf dkhaddpisn
      661 pnhytfdtay gyapmqrirg flgvkytlk
//
LOCUS       WP_284461586             226 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Chryseobacterium sp.].
ACCESSION   WP_284461586
VERSION     WP_284461586.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 226)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..226
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25702
     Region          12..88
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mekeigyits ligdpirtti lwslldnkay tatelaihad tspqnismhl nklvqadllt
       61 verqgrhkyy rfskpevaya ieaignlipn drhkkivsnt gnssikycrt cydhlagkmg
      121 vliteallth kiidfdvnty ivtksgtrff aelevniedl kkqrrafarp cldwserkhh
      181 lagslgaall dkmlsldyir rtknsraill tskgkqylye rfkisv
//
LOCUS       WP_284461758             115 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Chryseobacterium
            sp.].
ACCESSION   WP_284461758
VERSION     WP_284461758.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..115
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13109
     Region          5..113
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msikkndink ekilalkdai ellggkwkfc ilhnlynyet mrfkdlqeta lgispkvlsk
       61 elqelednll itrtvnntkp vtvsyaltth aketedvvna linfglkhrk kikek
//
LOCUS       WP_284461771             513 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Chryseobacterium sp.].
ACCESSION   WP_284461771
VERSION     WP_284461771.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..513
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=58502
     Region          28..513
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mnierirqpf ikkfpgdfsg nliqrntpkv lfatispagf dqpkliafnk tlseeiglga
       61 feekdldflv gnrlpeniqt yatayaghqf gnwagqlgdg railageien nlgkktelqw
      121 kgagatpysr hadgravlrs svreylmsea myhlgvpttr alslaftged vvrdmmyngn
      181 pqlekgavvi rtaesflrfg hfelmsaqge yktlqelvdf tienyfpevt ssgiqrykdf
      241 fenictrtan lavewfrvgf vhgvmntdnm silgltidyg pysmmdeydl nftpnttdlp
      301 grryafgkqg qiaqwnlwql analhplikd ekfledtlnh fgthfweshd tmlcakfgfd
      361 ellkddedff tnwqglmqel qmdytlffny lekststadv kdffnhvsys lvndeklkkl
      421 edflstynsr lslntvsreq slaimkktnp kftlrnylly ecieeisigk tsmlekltda
      481 lenpyeerhp efsakrpnsy dditgcstls css
//
LOCUS       WP_284461809             439 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Chryseobacterium sp.].
ACCESSION   WP_284461809
VERSION     WP_284461809.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..439
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50931
     Region          225..436
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mmskskylip lfatlflill giqvffiykt yqvkerdiyr siqeglsnyt dkledvstke
       61 mkddslqsii ikyydkeisn keflthflan rqptreklnr yissrfkkeg ydisakiqyy
      121 siihlpdstk iidqpiiiye tknkvknski sttsswetss tqrndsnnke ierkntflvk
      181 sktefeiani kiivfkeltl liicciilla svlllyiftv knlirqqkqv evlhtvvdni
      241 shefktpiat lkiaaktlkk dwnpetlpli drqiyrletl msqlhkdeip dkvtavkped
      301 wsffiqdlaf tysttdftle nnisqelpfd knlmetvikn lcensvkyga sniivnisss
      361 qqhleievsd ngfgmetkel knifekfyri qannihnnkg lglglyivkr ivteyhgkvq
      421 vssqpkvgtt fkisipyen
//
LOCUS       WP_284461852             192 aa            linear   BCT 25-DEC-2024
DEFINITION  YdeI/OmpD-associated family protein [Chryseobacterium sp.].
ACCESSION   WP_284461852
VERSION     WP_284461852.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Pilonieta,M.C., Erickson,K.D., Ernst,R.K. and Detweiler,C.S.
  TITLE     A protein important for antimicrobial peptide resistance,
            YdeI/OmdA, is in the periplasm and interacts with OmpD/NmpC
  JOURNAL   J Bacteriol 191 (23), 7243-7252 (2009)
   PUBMED   19767429
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..192
                     /product="YdeI/OmpD-associated family protein"
                     /calculated_mol_wt=22295
     Region          1..192
                     /region_name="YdeI"
                     /note="Uncharacterized conserved protein YdeI,
                     YjbR/CyaY-like superfamily, DUF1801 family [Function
                     unknown]; COG4430"
                     /db_xref="CDD:443542"
ORIGIN      
        1 mnpkvdfffd katqwkeefe klrtialste lvedlkwgcp cytyegknif lihgfkeyca
       61 llffkgalmk dpdqiliqqs envqaarqir ftdiqqindl ekelqaymfe aveieesgak
      121 vemkktkdfe mveefqqkld enlalkeafe gltqgrqray llhfssakqs ktrdariekc
      181 ipqildgkgl nd
//
LOCUS       WP_284461856             284 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein, partial [Chryseobacterium sp.].
ACCESSION   WP_284461856
VERSION     WP_284461856.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         <1..284
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
     Region          2..284
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 sggtqanliv issilkpcqc aisassghvl nnetgaieat ghkilsiete dgklrpsdii
       61 pvleshknvp hqvmpklvyi snstelgtiy qateleelsd fcrqnrlylf mdgarlghgl
      121 tseisdltle rvaeltdify lggtkngali geaivintis lqedfafnik qkgallakgr
      181 llgiqflelm kddlyfdlak hanqqamkik nafrskgvqf ladtytnqif pivsneliev
      241 lsesfdffvw kkvnedfsai rlitswntgd davnsfieii nrel
//
LOCUS       WP_284461883             130 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein, partial
            [Chryseobacterium sp.].
ACCESSION   WP_284461883
VERSION     WP_284461883.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..>130
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          18..>126
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkkilsgilm mmihmaypqi qkveqvidsc vkkdnfngsv lvakggriel ltykglsnrh
       61 ynipfsdetr fhifsltktf taalimqlye rgkinldapi styypeykge aakkatiknl
      121 ltyssgrenk
//
LOCUS       WP_284461944             140 aa            linear   BCT 25-DEC-2024
DEFINITION  succinate--CoA ligase subunit alpha, partial [Chryseobacterium
            sp.].
ACCESSION   WP_284461944
VERSION     WP_284461944.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..>140
                     /product="succinate--CoA ligase subunit alpha"
                     /EC_number="6.2.1.5"
                     /GO_component="GO:0009361 - succinate-CoA ligase complex
                     (ADP-forming) [Evidence IEA]"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0004775 - succinate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0004776 - succinate-CoA ligase
                     (GDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0006099 - tricarboxylic acid cycle
                     [Evidence IEA]"
     Region          2..>140
                     /region_name="SucD"
                     /note="Succinyl-CoA synthetase, alpha subunit [Energy
                     production and conversion]; COG0074"
                     /db_xref="CDD:439844"
ORIGIN      
        1 msilvnkdsk vivqgftgne gtfhasqmie ygtnvvggvt pgkggsehlg kpvfntvada
       61 vekaganvsi ifvppafaad aimeaaeagi kvivcitegi pvadmvkvks yiadrdcrli
      121 gpncpgiits eeakigimpg
//
LOCUS       WP_284462015             203 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Chryseobacterium sp.].
ACCESSION   WP_284462015
VERSION     WP_284462015.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..203
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23953
     Region          3..197
                     /region_name="HAD_sEH-N_like"
                     /note="N-terminal lipase phosphatase domain of human
                     soluble epoxide hydrolase, Escherichia coli YihX/HAD4
                     alpha-D-glucose 1-phosphate phosphatase, and related
                     domains, may be inactive; cd02603"
                     /db_xref="CDD:319790"
     Site            order(9..13,109..110,143,167..168,171..172)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            138
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mkikniifdf ggvlmdwnpr yffkdyfkdd ekmeyfleni aqdewnieqd rgrtlaegte
       61 iqvkkfpewe keirayydnw tvmlksdipq nvevlrklkn tdyhlfgltn wsaetfpyal
      121 enydffqifd gkivvsgtek likpdpkiwy vlleryniqa gesvfiddnp kniemaqslg
      181 fetiqitpet nleqelaglg iel
//
LOCUS       WP_284462047             776 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Chryseobacterium sp.].
ACCESSION   WP_284462047
VERSION     WP_284462047.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20710189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..776
                     /product="TonB-dependent receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86928
     Region          29..117
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          106..721
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mqtsffkiaa asaalcfssw amaqqkyqvs gtvkdqknge lligvsvkva edpsinvian
       61 eygfyslslp egnykviisy pgykdfeqqi tvnqnikldl plsqqeqaak tidevvitgi
      121 kkdknltsaq mgtetlsikn ieklpvlfge kdvmktiqll pgiksngegs sgfsvrggat
      181 dqnlilldea pvynashllg ffstfnsdal kdasiikgns paqyggrlss vmdvkmkdgn
      241 nkdyninggi glissrlsve gpiqkekssf ivsgrrtyad lflktskdyk dnklyfydln
      301 lkanyqinen nrlylsgyfg rdvlglgntf stdwgnttat lrwnsiinst lfsntsfiys
      361 nydykislts ndntfglnsk iqdwnlkqdf twfagnkhsv rfglqsiyht itpssasgts
      421 vssfprnprk swenalyind dfkateklti nygarlsmfs vlggdtfnty dngiltdsry
      481 lekgdfgkty vnieprvtan yrinevssik ggysrntqnl hllsnsssgn ptdqwigssy
      541 tvkpeiadqv slgysrnfnn nnyelnaevy yksmqnqidf kngaqitfdt aadvesellf
      601 gkgrayglel iakkksgklt gwisytlskt erkidgindn kwynarmdkt hdlsvvatyq
      661 lnpkwsfsgl fvystgnavt fptgkyqlng qtvfqyssrn adrmpayhrm disatyepes
      721 nkrfrgswtf giynlyaren aytitfednp nnpgttramq tslfrlipni tynfkf
//
LOCUS       WP_284462137             271 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Chryseobacterium sp.].
ACCESSION   WP_284462137
VERSION     WP_284462137.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..271
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=30578
     Region          56..84
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(57,60..61,64..65,67,91,94..95,98..99,101..102,125,
                     128..129,132..133,136)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          61..268
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          89..119
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          124..152
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          158..186
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          191..220
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          225..252
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkksllllas isffslniyg qdkktaeecf kkadykcaee qysqlaekeq iqkfkseyyn
       61 ylgtaqrrlg ktdfafksye kalktdprsa svyvnlaslh sqkgdktkal eyienglkld
      121 aenpdfylir skiydsqgkk elamkdlnqi lsfapdnifa ktglanlkkn nddlegalkd
      181 ynkliaekpe sllyngradv ylkmkktkea ladvskaisi dpkfaqsfvt kamilfemak
      241 pkeacdnlnk avglgyekai ladyfakctk k
//
LOCUS       WP_284462178             280 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional helix-turn-helix domain-containing
            protein/methylated-DNA--[protein]-cysteine S-methyltransferase
            [Chryseobacterium sp.].
ACCESSION   WP_284462178
VERSION     WP_284462178.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..280
                     /product="bifunctional helix-turn-helix domain-containing
                     protein/methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /calculated_mol_wt=31325
     Region          <28..116
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          116..280
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mstqsqidyn riakaieyiq snfrlqpnle evaenihlsp ahfqkiftdw agtspkkflq
       61 fislehaknl lkeekasifd tayetglsst srlhdlfvki egmspaeykn ggknlainys
      121 fsespfgnil vastekgich mafendkesv lgnlkhkfpn asffekqdtl qknalsifdk
      181 dwtklntikl hlkgtdfqlk vweslltipm gklstygnla ekignpkssr avgtaigsnp
      241 vaflipchrv iqstghlggy rwgsdrkqmi vgwessqiys
//
LOCUS       WP_284462219             262 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284462219
VERSION     WP_284462219.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..262
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=30391
     Region          13..262
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mieikkysnq tghseprrii kytlfwcneg haeilidenv fvlkhhqivt itsgqfhqli
       61 svegdliale ftldffcksd sdielifhng lfchfgmnei itvqhadfft etltliekei
      121 kekpyqylis thslvelllv einrskiang deiwkpdalf lkflesvrnh fsenypvshf
      181 admlgsteak lnevsklhtn ktaqnviysl tiseakrlll yekltvkeia yqlgfndpfy
      241 fsnffkkhms lspkdyqksv kn
//
LOCUS       WP_284462242             609 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Chryseobacterium sp.].
ACCESSION   WP_284462242
VERSION     WP_284462242.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 609)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 609)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..609
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=69574
     Region          43..576
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mdikrslvlf lssygcflfg qekvvdtiyi fdsqmnkvkl fhpvktiste dakknssnls
       61 ellrfqsavy ikengrgavs spsfrgttaq qtafvwngin insnflgqgd innislfgyd
      121 qigikagggs viygsgaigg sihlnnnldf nkgfhgtlfs evasfntynn llkgaysnek
      181 fsfkasgnys vsendyevke aknyinrngq yyntnfniaa aykiaphhqv swiseffngq
      241 qhypvlfdne tetkyrtqnv rsllswdwnk tqfnnsfkaa yteenfqyfa kadgpqtsgg
      301 tgknyilknd fnyffnskwn fnvigeyqln kgegygsgid hvsrnmgsvs gllryfpvad
      361 lrleagirkd fvgkisspvl fsfsgkwnai hwytlglsvs rnfrapsfnd lywqpggnmd
      421 lkpetsyqfe lrnqfkvgdl qmsaapfyld irdmirwlpt fsgyyspvnt dhvrsygvea
      481 qmeymkrfgk hllkgslgyt ytnsqdlekk kqlmyvpfhk ftgnidyqye fikvyvqglf
      541 ngltytdsne krsealekyf vmnaglgltf hkeytigfkv nnvfnevyyt mfayplpkrn
      601 ysvslninf
//
LOCUS       WP_284462314             930 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Chryseobacterium sp.].
ACCESSION   WP_284462314
VERSION     WP_284462314.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 930)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 930)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 930)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 930)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..930
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..930
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=102115
     Region          12..882
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mknkktilsa svlfflgvft ygqekdsikt nkdkinsvee vvvlgsraga rskidspvpv
       61 dvfnlkeasv ilpqsnigqi lnaiapsfts tvqtnsdgtd hldpaqlrgl gpdqvlvlvn
      121 gkrrhtsalv nvngtpgrgt vgtdlnaips falnrievlr dgaaaqygsd aiagvmnlel
      181 krdtgkltgq igyggnltpt andhtgnfdg qniqldlnyg nkigtkggff nitwssqfrn
      241 ptyragtekg aiynaynaie qralndgvnl sslfsdikdt pnsqqiidyv hqyaqgvnyf
      301 ssaqlagiqg attiqdikdg agnviqkglq sllnfdvtdq elayrgqtrk dfnmqvgqsk
      361 lnnhqlfina evpinddwkv ytfggyslrh gtsggfyrrp resrtftgly pngylpqigt
      421 diqdislaag ikgkwdgwhi dfsntfgqns ftynigntgn tslrfaspse fdagglrftq
      481 ntinldfskk ydafeglnva fggehrfenf kmtageeasy ttydqygniw dgdpakrptd
      541 ffgaalpggs qvfngfrpen avnknrqsva ayadvefnft nwllvdaaar yenysdfgst
      601 fnyklasrik vapnfnvrla gstgfrapsi hqiyynvtss lfvtspqlps gvlldvgtfs
      661 ndsevagalg mpklkqetsk sasvgftyki psvnltftad gyftrinnri lltdqflkag
      721 vpdaakqiyd klninaaqff tnaidtetkg vdvvishnlr ftdikldnnf ainlnqtkqv
      781 gnihssgllq spdlekiyfs eksrvyleea vprvkaslsh tltwksasfy lrntyfgkvt
      841 gadvldangd giiefnehqk igdkiitdls vayqftknig ltlgvnnlfd iyptknlpas
      901 snndqfvysr stsqfgqngr yvfsrlnfnf
//
LOCUS       WP_284462326             153 aa            linear   BCT 25-DEC-2024
DEFINITION  thioredoxin family protein [Chryseobacterium sp.].
ACCESSION   WP_284462326
VERSION     WP_284462326.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 153)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..153
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=17893
     Region          1..147
                     /region_name="SoxW"
                     /note="Thioredoxin-related protein SoxW [Posttranslational
                     modification, protein turnover, chaperones]; COG2143"
                     /db_xref="CDD:441746"
ORIGIN      
        1 mkkialflml vpcfylsqmk tgtfselesl qkesprpvvi hlytdwcivc kiesfrlnkd
       61 kdlvkmmndn fylinfeaek trnkihfqgq efeylsngss gihelalals knknqpvypl
      121 wvfldknqnl vyyqegqmtp ekmkqkllei svl
//
LOCUS       WP_284462526             127 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Chryseobacterium
            sp.].
ACCESSION   WP_284462526
VERSION     WP_284462526.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..127
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14537
     Region          2..>87
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mkknelmqys cplgkamaal gskwkpiivl vikdrklrfg elavrinvis rkvltdqlre
       61 mesdgliire efkelpprve ysltekglal lpilylleew eakyqvkgly dkdcslvdnk
      121 tkkainv
//
LOCUS       WP_284462576             313 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284462576
VERSION     WP_284462576.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..313
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=37020
     Region          59..313
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mfrttfaflq ipvfylyiis vcysdfklkp kyllhllpfl ivnlvllprf yavdaaskms
       61 fiqnrqnmie fqfihilihl qviiyiitvf rvlrkskkly lenyagksin synwlfqfti
      121 vltilytval lknifkfsdy pyisewikig lwvsslfifc wylfkalnnp glfrnvdskl
      181 klvselvsee knneqspehe reyneellnl kkymverkpy lnssltiqdv sneteipvrd
      241 lsllinhqlg qhfydfvnty riesamnilk dntkskvtil eilyevgfns kssfntafkk
      301 htgntptfyr ksl
//
LOCUS       WP_284462587             265 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284462587
VERSION     WP_284462587.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..265
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=30698
     Region          1..106
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          178..251
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqisppkhla pfirhyisld nskndiknvr lftdgstgli lsgnmnlysh fseermplsf
       61 fygglnsykd fyskgtfsli avvfqpyfln illkvsakef knqiisvedv lknklqpyqe
      121 dlfnkvnpls vihslnifft nflseemdsd vhfitavqqy ilqnkgsass kdleifsgys
      181 erhlerkfen ymgmtpkkys niirlhyfls lmnkgikden mtilsyhagy sdqshmiref
      241 knnigltprq yvktenkmav nfiel
//
LOCUS       WP_284462670             273 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Chryseobacterium sp.].
ACCESSION   WP_284462670
VERSION     WP_284462670.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..273
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31773
     Region          70..174
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mkikdhflsq eifeiketet kgvyktspip sniskyyese dyishhqdsg slkeklykfl
       61 qsfnlqykkn ilvdrikkgs kvldygcgag efvryiendf etfgfepdsd arnaaqgkia
      121 kakilddink ieensldait lwhvfehien qdemlnafhg klkekgllii avpnptsyda
      181 khykeywaay dvprhvyhfs kngmenlisk ksdwkmrkik plvldsyyis mlsekykksp
      241 lfwlkatiyg tisnikalfs nefssliyii ekr
//
LOCUS       WP_284462710             351 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284462710
VERSION     WP_284462710.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..351
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39569
     Region          29..343
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mfrsflilsf sclslfcfsq kvknlkkdiq qevnqldqii ksahekgafn gnvlvsknnk
       61 iiykasfgft daaktntltd eyrfhlgsit kefsavallq leeqgklkls dhvskfipel
      121 pdwanevtik dllqytsgip nvnwktvknd kdifnglmla nqlsftpgte ydyninnlfl
      181 rqfiiehvtg mpyktyikkf vfqplkmnas imtpianekn iakgfnnqlv pdkeelpitg
      241 gtytttmdll kwadglhfqk vvnqnsiyel gqsfsipdsq salgnakfed kklkehfhdg
      301 ragsfeatlf sdvenkitii llsnsysgkl peiseaiyav lknkspnssq k
//
LOCUS       WP_284462766             363 aa            linear   BCT 25-DEC-2024
DEFINITION  fatty acid desaturase family protein [Chryseobacterium sp.].
ACCESSION   WP_284462766
VERSION     WP_284462766.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..363
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42966
     Region          9..357
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mekpiylkds ddtklfnelr kkvnqrveai penrdiyiqi kavilpliyv glyfvailna
       61 ekqwvyilsf vlmgislvli ylnliheaah nniykskrln glvlhifdfi gansyiwkkr
      121 hiashhaypn vdgwdtdieq sglllivpwi kakgvqkyqh rffflvyply lfnwmfirdf
      181 rdffdkervi lktqgripvm ekvkmvsykl fyffyqivvp vlffkvsigl algawflqvi
      241 aasifalfvl lplhplpdna fpkldkdngl pfswlrhqle vtndlkennw lvrnvlgnfn
      301 fhvahhlfpn ysymyyneit eeieefakeh hlaykrfpll talgkhrdll rqnannayyi
      361 lee
//
LOCUS       WP_284462801             513 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Chryseobacterium sp.].
ACCESSION   WP_284462801
VERSION     WP_284462801.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..513
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=59146
     Region          28..513
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mnierirqpf ikkfpgdfsn ntmqrntpkv lfstikpagf drpqliafnn ilseeiglgk
       61 yeekdlnflv gndlpenvqt yatayaghqf gnwagqlgdg railageiln dsskkteiqw
      121 kgagatpysr hadgravlrs svreylmsea myhlgvpttr alslaftgee vvrdimyngn
      181 pqlekgavvi rtaesflrfg hfelmsaqqe yknlqdlldf tienyfpeit ssdnqkykdf
      241 fenictrtan lmvewfrvgf vhgvmntdnm silgltidyg pysmmdeydl nftpnttdlp
      301 grryafgkqg qisqwnlwql analhplikd ekfledtlnk ygtyfweahd tmlckkfgfd
      361 elkkedeeff tnwqglmqel eldytlffnq lekitadldl kehfskvsyt flneeklekl
      421 knfiknyesr lklnsisred sqklmeksnp kftlrnylly ecieeissgn temlqkltka
      481 lenpyeeift efstkrpsgy ddttgcstls css
//
LOCUS       WP_284463033             252 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Chryseobacterium sp.].
ACCESSION   WP_284463033
VERSION     WP_284463033.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 252)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 252)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..252
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=29378
     Region          1..225
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mkiaiiedel lavnylknll dkqnivsise tvvlrskkqa ieffendsad lifmdihlgd
       61 gmsleifeqv elftpiifit afddyamrvf rhftidyllk pfeeedlhka lqkfisisnf
      121 dpepvlrsis tlrqddsevm krfmvregnk lksvdeqnia yffasgkylf latkdhqtyi
      181 yddtikdiiq klnsdlffkv nrkfiinkea vteiikhssq kvelrlspep evntgvfisk
      241 iqiteclnwl rn
//
LOCUS       WP_284463107             279 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Chryseobacterium sp.].
ACCESSION   WP_284463107
VERSION     WP_284463107.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..279
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32442
     Region          1..212
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkfsvliahy nnavlfrdcy ssllqqtyqn weavivddas seterdqvka iiagderfrf
       61 feneknsgvg vtksrliela tgevcgfvdp ddailptaie kamrvfehkk nvvltysrfm
      121 gcdkdlkpia pyksamqvrn kdpyffnypi qighfttfrk dvyeqtekmn pelriaedqd
      181 lylkmyekgd vyfiddtnyl yrahsggisq ndnkgrsydy faqvvfatmk rrnltsingk
      241 kipekytnhq eifslleyqh gigyrikkki iialqklfr
//
LOCUS       WP_284463159             767 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Chryseobacterium sp.].
ACCESSION   WP_284463159
VERSION     WP_284463159.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 767)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 767)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..767
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..767
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=90481
     Region          <2..152
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          436..666
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
ORIGIN      
        1 mynkleqlfy qgdleqciae geqyllsnpe deevlflmav ayhdrvyyeg heeaynaihd
       61 kvipylrril nvnpnniral ynilnyplsn eytlmqigrv kkhiteenka efigyaerll
      121 ddsenevygy dflvkiyesl genkpllnsl eagmyyfqre fadnrelrdk nrslfwikki
      181 ylldrekmis geeltalidr ehstfvsred sdfinladia yennapdlsl kmmlkaikgs
      241 nsamfiqekl vewhhrfael iqngfnnpdv fyyqliiern yadmlkiadd fykqhalevi
      301 nahpqifsgy hfagtyfyda mqyseaipll ekaverssna tawrrkvese yhlykiipse
      361 ipaftdlptd iynegvylne fieeiedeed qikwtevhtm vyqqayeafq ryyeaeqfes
      421 nyyndmhtra mccnnlaikh sllgdhlsai kvaseglkys efrelhlvli dallfeenye
      481 kaeealnnyf glyddededy lyknlyyrar qievlglqgs pevysdaeea lnyfyqhtmd
      541 npeisdydyr dleagknvle gilyprlese dhdtrlsyyk dlaerfpqep npqyalmqiy
      601 neeenyknva kaaknylenk kdfllndfdk aktiymivks nflqgdytea asvfsqydae
      661 nddamdpedy vlwlsygiri yeklnnkdqt lmlaerfnki yndeewgydd ltesvelaka
      721 vvlyqggnlk eahalldhvr sfpeydsiad eykaswkkpg lfskfgf
//
LOCUS       WP_284463194             203 aa            linear   BCT 25-DEC-2024
DEFINITION  N5-glutamine methyltransferase family protein, partial
            [Chryseobacterium sp.].
ACCESSION   WP_284463194
VERSION     WP_284463194.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Schubert,H.L., Phillips,J.D. and Hill,C.P.
  TITLE     Structures along the catalytic pathway of PrmC/HemK, an
            N5-glutamine AdoMet-dependent methyltransferase
  JOURNAL   Biochemistry 42 (19), 5592-5599 (2003)
   PUBMED   12741815
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..>203
                     /product="N5-glutamine methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
     Region          1..>193
                     /region_name="HemK"
                     /note="Methylase of polypeptide chain release factors
                     [Translation, ribosomal structure and biogenesis];
                     COG2890"
                     /db_xref="CDD:442135"
ORIGIN      
        1 mtisaykkyf kaelsdlyte sesaflsslf ihkivgfdnf qqrrfseqel liddekqlyn
       61 lvselktgkp yqqilgetef ygmkffvden vliprpetee lleiaireiq glevkekglk
      121 ildigtgsgv iplvlkkhfp naevssidfs ekalktahrn adyhqlkvqf ihgdylnfkl
      181 aenydiiisn ppyigieeei eir
//
LOCUS       WP_284463263             243 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Chryseobacterium sp.].
ACCESSION   WP_284463263
VERSION     WP_284463263.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..243
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28081
     Region          43..143
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mkenkydnps ffdqyekmlr sqlglegage whalknmlpd ftgkkildlg cgfgwhcrya
       61 mengaksvig idlsekmltk areinslegi qyerkaledv sypteqfdlv lssltlhyve
      121 sfdtiaqniy qwltsgghfv fsvehpvfta egsqdwvydk ngdktcwpvd ryfiegkrnt
      181 tflgenviky hrtltsylnt llkhgfkile iiepepsqem lkeipemkde lrrpmmllis
      241 vek
//
LOCUS       WP_284463305             562 aa            linear   BCT 25-DEC-2024
DEFINITION  C45 family autoproteolytic acyltransferase/hydolase
            [Chryseobacterium sp.].
ACCESSION   WP_284463305
VERSION     WP_284463305.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   True,J.R., Yeh,S.D., Hovemann,B.T., Kemme,T., Meinertzhagen,I.A.,
            Edwards,T.N., Liou,S.R., Han,Q. and Li,J.
  TITLE     Drosophila tan encodes a novel hydrolase required in pigmentation
            and vision
  JOURNAL   PLoS Genet 1 (5), e63 (2005)
   PUBMED   16299587
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Tobin,M.B., Cole,S.C., Miller,J.R., Baldwin,J.E. and
            Sutherland,J.D.
  TITLE     Amino-acid substitutions in the cleavage site of acyl-coenzyme
            A:isopenicillin N acyltransferase from Penicillium chrysogenum:
            effect on proenzyme cleavage and activity
  JOURNAL   Gene 162 (1), 29-35 (1995)
   PUBMED   7557412
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Tobin,M.B., Fleming,M.D., Skatrud,P.L. and Miller,J.R.
  TITLE     Molecular characterization of the acyl-coenzyme A:isopenicillin N
            acyltransferase gene (penDE) from Penicillium chrysogenum and
            Aspergillus nidulans and activity of recombinant enzyme in
            Escherichia coli
  JOURNAL   J Bacteriol 172 (10), 5908-5914 (1990)
   PUBMED   2120195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF040521.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..562
                     /product="C45 family autoproteolytic
                     acyltransferase/hydolase"
                     /calculated_mol_wt=64690
     Region          77..421
                     /region_name="C45_proenzyme"
                     /note="C45 family autoproteolytic
                     acyltransferase/hydolase; NF040521"
                     /db_xref="CDD:468523"
ORIGIN      
        1 mkktntnylp ykrlliylfp lfiliscgvs ksvnhlpevk qysleipkvn kindttfsyn
       61 qnfitknkqq lwelyikgnp lqlgynngal tqdlmqkqee iffskvegfv pskfkqklln
      121 gflkwynrkm ylnvredyqa elyglsqyss nqydfiasky lrnlylhgah dighamqdla
      181 mvgctslavw nentedgdll igrnfdfyvg ddfsknklve fvepedgipy msvswpgmig
      241 vvsgmnkegi tvtinagksk ipltaktpis lvtreilqya knideaiaia kkrkvfvses
      301 ilvgsahdkn aviievspkn fgiykvents kvfctnhfqs dtykndarnq kqikeshsay
      361 ryeklqellq eekklnpekm asilrnrsgl kdesigygne kalnqllahh avifspqkkl
      421 vwvssnpyql gefvcydlne ifsdqglqpn dfsksqlnia rdpfadsqef knyeeyrqis
      481 skindaihnk vilsdnfiah yqslnpdfwk gyfvagkyyf hkkeyskaki efekaltkei
      541 ttvpdqktve kylnkaikki nn
//
LOCUS       WP_284463330             420 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284463330
VERSION     WP_284463330.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..420
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47407
     Region          51..390
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mktrnlvliv tvflslfsck nkseskevsa enttnlpnyg nvdlanvftk adgqlsdkes
       61 ltgyidqyyk kiwdggdlsg gilvakgdei lyenyrgfgr egnqmpidkn tplhvasvsk
      121 tltamammkl ieagkiklsd hltqffpgfp ypnvtvqtll dqrsglpkye yfitkiqpap
      181 aelskpfitn qdvlnmiiky kpdlardtdt gfmycntnfa llallvekvt ktpfpqamke
      241 mvftplkmnn tyifqekdip taaqsfyyga nklypldrld liygdknvyt tprdlynfsk
      301 amfskdflkp elmqmvftpy snekagmnny glgfrmkifd ngekltyhng wwhgtnsvfa
      361 hllkskvtiv aignkysnkv ytalalsglf enfpvqkekl qtvmngskdt lnsghevfge
//
LOCUS       WP_284463419             334 aa            linear   BCT 25-DEC-2024
DEFINITION  DHH family phosphoesterase [Chryseobacterium sp.].
ACCESSION   WP_284463419
VERSION     WP_284463419.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..334
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=37257
     Region          9..332
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mftpaellei ntlltpenki vilthynpdg daigsslglk hylaakgiha evivpndfpk
       61 flkwmpeskk viiaeykrkl asdmifgadv ifcldfnsps rigllgdwlv kaqgkkilid
      121 hhqqpepfdf vysdtvipat sqmiyhfiea medeklvnqd maeclytgim tdtggfrfrs
      181 tsatthriia nliekgadpa mitsntwdtn tvsrlhllal vlgrievvne grvailsltr
      241 nelkefgfqk gdtegfvnyg lsiagvkmsa ffmedlyddf ikisfrskdd vdvnqfsrky
      301 fnggghinaa ggksddslsg tieifknrli eenl
//
LOCUS       WP_284463405             695 aa            linear   BCT 25-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Chryseobacterium
            sp.].
ACCESSION   WP_284463405
VERSION     WP_284463405.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Shan,L., Mathews,I.I. and Khosla,C.
  TITLE     Structural and mechanistic analysis of two prolyl endopeptidases:
            role of interdomain dynamics in catalysis and specificity
  JOURNAL   Proc Natl Acad Sci U S A 102 (10), 3599-3604 (2005)
   PUBMED   15738423
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Polgar,L.
  TITLE     The prolyl oligopeptidase family
  JOURNAL   Cell Mol Life Sci 59 (2), 349-362 (2002)
   PUBMED   11915948
REFERENCE   3  (residues 1 to 695)
  AUTHORS   Polgar,L.
  TITLE     A potential processing enzyme in prokaryotes: oligopeptidase B, a
            new type of serine peptidase
  JOURNAL   Proteins 28 (3), 375-379 (1997)
   PUBMED   9223183
REFERENCE   4  (residues 1 to 695)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 695)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..695
                     /product="prolyl oligopeptidase family serine peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=77310
     Region          15..692
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mlltagvlfs asfysqtmny pkalkgsqsd tyfgtavsdp frdlehdsda tkkwvdeeva
       61 ysqnylskip frdkiknqlk diwnyekisa pfkegdytyy ykndglqaqs vlyrtnsktk
      121 atevfldpnk fsekgttsls nlsfnkkgnl aaysiseggs dwnkiiiida itkkqidetl
      181 ldvkfsgisw qgdegfyyss ydkpkegtvl sgmtdkhkvy fhklgtkqse dklifggekt
      241 prrylganvs edqrylivsa anatngnely ikdlkkggdf vqivkgfdin agivdtegde
      301 lfistdkdap nmrlvkttis npapetwkdv ipqtenvlgi ssgggyffat ymvdaidkvk
      361 qfdktgklir eislpgkgnv sgfggkekek diyysfsnyi tpgttykfnv dsgksevyqk
      421 pkvkfnpddy vseqvfytsk dgtkipmmin ykkgtkldgk nptilysygg fnislqpsfs
      481 vvnaiwmeng giyavpnirg ggeygkkwhd agtkmqkrnv fedfiaagey lqskgytske
      541 ymalsgrsng gllvgatmtl rpdlarvafp gvgvldmlry nkftagagws ydygtaedsk
      601 emfeylksys pvhnvkagtc ypstmiitsd hddrvvpahs fkfgaelqek qacknpillr
      661 ieknaghgag ratdqvigen adllsfalye mgvkl
//
LOCUS       WP_284463427             251 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Chryseobacterium sp.].
ACCESSION   WP_284463427
VERSION     WP_284463427.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..251
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29519
     Region          4..209
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkdlvsiitp cynsaefiee tiqsvlsqty enwewlitdd lskdntveii rkyndprikl
       61 qvleknggag narnnslera kgryiaflds ddywypeyie tmtdymqehh aelvycnysr
      121 cdeqlqpilk dfladkvvtf snllktcrla pvstmydtkr vgkflfpiks kredhvmwln
      181 llkvipegmp inktmakyrm rensvsrnkk niikdqylvy kdfmgfstlk slyytanwam
      241 ngflkyskif n
//
LOCUS       WP_284463511             368 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284463511
VERSION     WP_284463511.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..368
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40957
     Region          44..344
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 miknlvfllp fcfllsckte tppppidkka vidstitafq ktlleqqids vfkkyqfngs
       61 vavfkdslpl yrkengysdf krkikidsst ifaigsvskq ftavlvllqi eqgklnvtdk
      121 vskylkefqi keyenitihq llnhtsglnm lggklmfksg sdfyysndgf nalgkivetv
      181 sgksydenav elfkkagmnh sstdeifkgt nfasaylgni nkaeevpnmp krlggkeigt
      241 paggilstiq dlhtwnnaly ggkilkpetl kqfmaksaer rhaifgkmgy aygimlnigk
      301 pnsyfhsgyv kgspslniyy petktsviil sniadeekgk glvfkphiev kkitdnlent
      361 lvqlkakh
//
LOCUS       WP_284463660             240 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Chryseobacterium sp.].
ACCESSION   WP_284463660
VERSION     WP_284463660.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 240)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 240)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..240
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=26816
     Region          5..237
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mmseklrciv iddepigkel ivdfvktipf lelqasyddp idaltylqsn evdiifsdiq
       61 mpkisgidli rsltkppsii fitahrdfal egfengvvdy lvkpvaydrf lkavnraker
      121 mqtasktevs spetpnpvdr ifikvngklv kvilddilyv ealgdylkiv tdtesfttla
      181 tlksmedili ppkffrvqrs fivklisvks vsgnvielnn gkaitiattk kdelfsllgi
//
LOCUS       WP_284463715             344 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Chryseobacterium sp.].
ACCESSION   WP_284463715
VERSION     WP_284463715.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..344
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38497
     Region          1..343
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mkfsfkndys egchpnilqa llqsnldqqa gygedeyslq akerikeriq kkdsevyfvs
       61 ggtqanlivi ssilrpyqca vsastghiln netgaieatg hkilsieted gklrpsdiip
      121 ileghsnvph qvmpklvyis nstelgtiyq akeleelsef ckqnrlylfm dgarlghglt
      181 seisdltler vaeltdvfyl ggtkngalig eaivinnpvl qedfafnikq kgallakgrl
      241 lgiqflelmk ddlyfdlakh anqqamkikh alqekgvkfl sdtytnqifp ivsndlikvl
      301 senfefyvwk kvdeefsair litswstgda avnqfievik relp
//
LOCUS       WP_284463785             369 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Chryseobacterium sp.].
ACCESSION   WP_284463785
VERSION     WP_284463785.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..369
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41658
     Region          6..368
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mlksvhhfqe sldkrkeegt lrrlqsrfeg idfysndylg farskelqni llkkindnpd
       61 llsgstgsrl isgnsnvvtt tesfiakkhk vssallfpsg ynanlalfst lpnrhdtiiv
      121 deqihrsvhd ackmsnarki kfkhndlndl envlkkqdrh cyiaieslys megdfapiqk
      181 isemarhyna allvdeahaf gvfghgliek ynlrdqitas vitygkalga hgaailcndt
      241 vksylinfas pfiyttsaqd fqwmsiktgy eflesnyktt eklqknikmf reqglnspss
      301 ekspiqaivi pdnqklgllq ktlsnegfat yaiysptvke gterlriclh sfnteeeiir
      361 ltgiikefn
//
LOCUS       WP_284463851             328 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Chryseobacterium sp.].
ACCESSION   WP_284463851
VERSION     WP_284463851.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..328
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35895
     Region          7..321
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mkkknilkgv lfvgigasiy gmlatfvkma yhdgfttsev ttsqfvlgla gllilnfiqt
       61 ltskqklslp nskelrmlml agtslggtsl fyyiavqyin vsiaivllmq svwfsvvves
      121 iltrklpnar kvvsvvivla gtilatnlin mdieldwhgv fwglmaaasy tltmftsntl
      181 athlpvfrks limltggsiv vfaflffaqi gpmyfdglks fylnftdnte hihpfnysif
      241 ltygfvlalf gtiippilfn igfpnaglgl gsivsslelp vsvtmafvll gekvlliqwv
      301 giililfaiv lmnlpskkek evsmaels
//
LOCUS       WP_284463897             226 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Chryseobacterium sp.].
ACCESSION   WP_284463897
VERSION     WP_284463897.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..226
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26383
     Region          1..>222
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mnridrllsv lttlqskkfv tadyiaekye isirtvyrdi kalgeigvpi dyepqkgytv
       61 lqgfflppvl ltsdeanali misklseryt dktiqknvsn aidkiksvlr ysekekadml
      121 qekigiyvsp etdhsrdylt iiqnaivnkr ilkisylnnl keaserevep igmsfytnqw
      181 hliawcwmrn eyrdfkvlqi qelkntdlpf rkenhftlee yinsls
//
LOCUS       WP_284463882             290 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284463882
VERSION     WP_284463882.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..290
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33729
     Region          <185..290
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 malfitldnv yklynldpsk ktegivilsq qndpkkkytt hsrlfdglll gfmvkgsmks
       61 qihfleyein tgdiailqpq lmietkslse daeiitigls ldfitefpil refvmnnqir
      121 wqpiirlqpe diklqnellt liqnfyhkkp ssnktqmlrh lvmvlismis evysnlpdnk
      181 slvknrthei iddfyllisk yasqqrsvaf yakklhltpq ylstflkqkt gksvlqwidy
      241 itilhaktll kssnlsikei snelhfeets ifcryfkriv gvspktyrne
//
LOCUS       WP_284463983             430 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Chryseobacterium sp.].
ACCESSION   WP_284463983
VERSION     WP_284463983.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..430
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=49672
     Region          106..398
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 matvkyylrs ksketniqmq lsvsrdlkmr tstgliisyt dwsdrtslpk qnnshtknii
       61 aqlsdlrnfv lneynkdfvn gvlfntnwlk gkiniffert dtnvddnfis nylkkfnelr
      121 kldsrtkdst dyqfivlaqk itnfqksqkk dytfpevdkr vmlefknwlt ktdnlmesta
      181 lrtlknfktv lldardngkt ihnqintfsi askpalkvfl dfqeieqikn tvivgkdiqf
      241 akdwliigcy tgqrvsdllr mnrkmiftkt dadgdsfkfi eltqektgkd vtiplhdeve
      301 kiltkydgdf pptfsdttfa snvsifnynl kkicklagik tmvkgkvfne klgkneikdt
      361 ekfnlvsshi crrsfatnfy gdkrfttpqi maitghstev mflsyigkts sdhaiitakt
      421 freikqqkts
//
LOCUS       WP_284464055             800 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Chryseobacterium sp.].
ACCESSION   WP_284464055
VERSION     WP_284464055.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 800)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..800
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..800
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=90812
     Region          <100..>289
                     /region_name="COG4946"
                     /note="Uncharacterized N-terminal domain of tricorn
                     protease, contains WD40 repeats [Function unknown]"
                     /db_xref="CDD:443973"
     Region          543..799
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mkiklticll aflnfydaqe nityqkpsae ilkladydrp pavlmnskkd wvvftyrpay
       61 ktlndlnqqe mklgglrinp vtniastvty fnnlkirkig dknetqvknl pseakiahll
      121 fspdekklaf tnttdkgvel wiidmqtata kkitqdalna nlgypyiwyn dsqsllirtl
      181 pqnrpalids skdlptgpiv stadgkvsqn rtyqdllknq qdeknfevlv ssevynvdln
      241 gnlkklmdkd mysglsfspd gnylltttik kpfsyivpln rfpststvyd tkgnvvkvvn
      301 evplneimpk gfssvrtgkr dmnwrsdapa alvytealdg gnqhkaaeyr deiftweapf
      361 aaapksffkm kqryedinwt ndhyavvsee wydtrntksf lidlnngesk viddrnvqdv
      421 ysdpgkfnkv knqygksvid mkggktylig dgftkdgqhp fidemdvksl kkkrlytsni
      481 knakenivdi lnpskgeilt tqeasnqypn yfkkniksnk teavtyfanp fesikdiyke
      541 vitykrndgv tlsgilylpa nydrkakkek lplliwaypr eykdkntagq stqndndftf
      601 ptygsfvywt tkgyavldha afpiigegkt epndtfitql vanadaaina vdqlgyidkk
      661 kvavgghsyg afmtanllth shlfacgiar sgaynrtltp fgfqseqrny wdvpevyntm
      721 spfmnadkmk tplllihgda dnnpgtftlq teryfqalkn lgapvrmvll pkeshgyqak
      781 enilhvlweq dqflekclkk
//
LOCUS       WP_284464080             979 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Chryseobacterium sp.].
ACCESSION   WP_284464080
VERSION     WP_284464080.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 979)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..979
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..979
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=110621
     Region          50..500
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          <119..146
                     /region_name="DdpA"
                     /note="ABC-type transport system, periplasmic component
                     [Amino acid transport and metabolism]; COG0747"
                     /db_xref="CDD:440510"
     Region          563..958
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mnllkkltiv ssiaaasfag hafgqdfqwk eatsngykyr yvtndptsar yytlkngltv
       61 ilsptnkepr iqtyiatkag sktdpadhtg lahylehmlf kgtnqfgskd wakekplldq
      121 idalyekynq tkdeakrkei ykeidkvsge aakyaianey dkmmagmgad gtnaftsfeq
      181 tvytedvpsn vidkflavqg erfrepvlrl fhteleavye eknrsldddg dkvfdmmfan
      241 lfpnnnygkq ttigtiehlk npslhairey ynnyyvpnnm giimsgdfnp devitkidka
      301 fsymkskpvp eykigqekai aspvikevvg pdsesvmlgf rfpgastkda rllnfvgsml
      361 tngqaglidl dlvkkqkllg afafpyalkd ysvlllqgkp tegqsldevk nlliqeidkl
      421 rkgefsddli qsivnnekkn iiqkdekyss rasllmdeft sevdhkanle yveeiskltk
      481 kdimdfaaky lqnnnyvavy kkkgedksiv kvdkptitpv svnredqspf lkkidempek
      541 aiapvwlnyd kditknklgd vdvlsvkntd nalfrmyyhf dsgkwnnkml plaaeylqyl
      601 gtndksseti srefyklass fnvsagneet yvsieglnen fdksialfed lirnckadqa
      661 aldaykarlk karanakqnk atimaglrsy aqygaqnpfn nvlsdaelda lkaedlinil
      721 hdlfnfkhkv lyygpksgde tvaslkpihk lpaslkelpk tktfvqiptd knkvlfahyd
      781 mvqaevfwvr nsdqynptlt ptvslfnnyf gggmgsivfq tireskalay stysyfalps
      841 kksdkdmvma yvgtqadkfn esttamnell ttlpkseqlf etaksglkks iaserisqdg
      901 iifsylkaqr lgnnfdmrkn vyeqapklsf adinafhdke mknknytycl vaaqdkvnea
      961 dmqklgevkk lnltevfgy
//
LOCUS       WP_284464109             546 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284464109
VERSION     WP_284464109.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..546
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=61647
     Region          28..359
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkpliktill lfsllstefc fgqshqkdel rkvdslvnhy sqagapgmav giirdgkvid
       61 kktyglanle dripvtdsta fdiasvskqf tafvallaeq egrlslnddi riylpelkql
      121 pykvtirqla nhthglpdft nikrlqgfgv esqvtnteav ntilaiksin fpsgeqykyn
      181 ntgfillaei lhriykkdfa dlvkeyifnp lhmnhtkavn dpekiipnka esykengdhf
      241 tkqplgqmen gssnifttld dlckwavnfq nptigsreiy qkmqqntfln sgekieyglg
      301 lqtgkykgld ivfhgggtag yrsyilhvpa hhlsivlmsn kgnfdglfia yklvdlvlkd
      361 heilpsppkk itytstelkq iggvyeidpg nymeittdgk nlyawgsktp lesvgdnkfv
      421 ipfiptahit fhtgklafsi gdfvfhckkv ilnpmdeskm dlnqfvgyyk neefntiyel
      481 iikdnklvar hainpdailh plgqesfysq epffghiqfk ydknnkmkgf ilsgsnmfni
      541 qfnkik
//
LOCUS       WP_284464272             840 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284464272
VERSION     WP_284464272.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..840
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..840
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=83785
     Region          34..>683
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mkkilllfgi lsglfmglsq apekmsyqav vrngsgqils nqaiairlsi lqgsaagpsv
       61 yserltgntn anglvtleig tgtvlsgtfs tidwpsgnyy lktetdpsgg ttytitgtsq
      121 llsvpyamya ksagssggtf tipyantvnn astlfsltnd gdgtslegnn nsatssiaav
      181 rgvvtstapg gfssgvrgin ngtgglgigv wgsqngsgwg vygvtpnglg vygnssasgt
      241 gvyansntgt gltatsnngi pasisilnna nannvlnast vgngvvvnvt tsgsgngvas
      301 stgagialrg tttaqssagv lgsntgngea vvglttsdia gavvgrndgg gygvrgfist
      361 ntsgtgigvf gqvglnsstg ragrfensnq tntvanilev etngngnipd ntqgnaasfl
      421 vdntnsvgaa vrgevntifg nfgaaaifgv ssgtggragl fyasnpsgng aslialtdgn
      481 gnaitanagk dgngvetnid gngnalyawv ptfstgragr fnifnennts dvitvttvgn
      541 giagnfkvdk tqgtsaavkg evnsmfanfg tagiygvssg tggygglfha snpagngpal
      601 iaiadgngng itanasnggd giettadgtg saifawvpnf gngraarfin fntantnpal
      661 tvethstgsl alfksgnpst anvaridntg rgffnggtqn sgadvaeafd vegsiseyes
      721 gdilvistss drtveksskp ysnlvagvya tkpgvlltee hidtdlsgkv pmgvigvipt
      781 kvclengkik rgdllvtssk agiamkadlk kvkigqvigk alqdydqkes gkiqvlvnik
//
LOCUS       WP_284464422             273 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284464422
VERSION     WP_284464422.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..273
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31722
     Region          <188..266
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtsvipqtdd sfvysctskd qwgyeqfvse hilafqlsge thifhqqgtf vlkksrvlla
       61 hrnqfaktlk vtasdteyka isiilktedl kkfatinniv cdkkysgknn ivlkpdnflk
      121 syfqslvpyl eqpedgnkrm vfskiteive lllninpefk sflfdfneph kinlekfmld
      181 nyhynapien fakltgrsla sfkrdfaetf ntpparwlke krleeayqli hqenkkpadi
      241 ylelgfenls hfytsfktky gvtpteslii kkl
//
LOCUS       WP_284464576             135 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Chryseobacterium sp.].
ACCESSION   WP_284464576
VERSION     WP_284464576.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 135)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..135
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15347
     Region          7..128
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 mqnktiidkl awielkdksi lstksygkdk yyipggkret getdeqalvr eiweelnvti
       61 dsktlhyigt feaqahghad giivkmtcys geysgelkas seieemkwln ysdkdkiskv
      121 dkiifdslhq nnlld
//
LOCUS       WP_284464581             306 aa            linear   BCT 25-DEC-2024
DEFINITION  Kelch repeat-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284464581
VERSION     WP_284464581.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Shi,X., Xiang,S., Cao,J., Zhu,H., Yang,B., He,Q. and Ying,M.
  TITLE     Kelch-like proteins: Physiological functions and relationships with
            diseases
  JOURNAL   Pharmacol Res 148, 104404 (2019)
   PUBMED   31442578
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Gupta,V.A. and Beggs,A.H.
  TITLE     Kelch proteins: emerging roles in skeletal muscle development and
            diseases
  JOURNAL   Skelet Muscle 4, 11 (2014)
   PUBMED   24959344
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Adams,J., Kelso,R. and Cooley,L.
  TITLE     The kelch repeat superfamily of proteins: propellers of cell
            function
  JOURNAL   Trends Cell Biol 10 (1), 17-24 (2000)
   PUBMED   10603472
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..306
                     /product="Kelch repeat-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=33429
     Region          22..285
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          33..77
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          125..172
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          176..218
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
ORIGIN      
        1 mktkllflsf lysllthaqt lqfkslanms vgrgaitssi vddniyvsng yqenggnanf
       61 iekynitdnk wsilnatlsp kkfansetyd nkiyifngwg nshleivdla thkvtkgavn
      121 rsytgnagsa ihngkiyvfg gsglngaatt vfsnrfqyyd iasntwhplp dmptareakg
      181 kivndklyvi ggfngtpsrl invydlktnl wtnqytmpag iyghslavsg nkifiaggvn
      241 nqsflayfdt ttntlhqlss nmiprrhaaa eiynnklyii ggsttsitks aiksiqvadi
      301 sdstlq
//
LOCUS       WP_284464595             232 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Chryseobacterium sp.].
ACCESSION   WP_284464595
VERSION     WP_284464595.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 232)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 232)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 232)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..232
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=27362
     Region          4..230
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 manltivgvd deypalelir hycdqiedvd llevfqnpee alqylqknrv dlvildinmp
       61 yingidlllk lpykplcifl tletqyavka feldvvhylv kpvdfetfkr avykakdflq
      121 fkksaedkkh gdfimfksny imnkvllkdi kwiqgfgeyi ilithlkkym ilermsnfee
      181 nfqnlgfiri hksyivlfsh issydsntiy lkdgeqlplg rtykkqlkey fg
//
LOCUS       WP_284464625             378 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284464625
VERSION     WP_284464625.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..378
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=44734
     Region          136..378
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mdkysfleit afigiflvff lalflltvkt khrlanwlla fflftnavda fkflirdfpv
       61 nfinleafrw sinylvpasf yfyvlsvcfs kfrlkpkhlw htipfvafnl ymaygiyfed
      121 raskvsfina lsespimhff yflfeflfqv yfiasflvir ksktvyleny tnpnisilna
      181 lykitilyyv lhflvlirwl vsfifgwgel rqwivtldgf afffctcwyl fvalnnpeff
      241 rgvnsqlkpi idlipkqkss piiddeknkq iialkefmik nepylnsslt iqdlaeqlnm
      301 pvkdlsslin lymnkhffdf ineyriekak eilknplqke ltileilyqv gfnskssfst
      361 sfkkhtgttp tdfrkslh
//
LOCUS       WP_284464647             141 aa            linear   BCT 25-DEC-2024
DEFINITION  SRPBCC family protein [Chryseobacterium sp.].
ACCESSION   WP_284464647
VERSION     WP_284464647.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..141
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=16456
     Region          4..141
                     /region_name="SRPBCC_CalC_Aha1-like"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of Micromonospora echinospora CalC, human Aha1, and
                     related proteins; cd07814"
                     /db_xref="CDD:176856"
     Site            order(5,7,9,18..20,22..23,28,38,43,45,47,49,58,60..61,63,
                     66,72,74..75,87..88,90,92,102,104,106,108,119..127,
                     129..131,135)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mstpiivqyt inapsekvwk altdqnemks wyfdildfel kignifnfye pggenkyhhq
       61 ceileiipnk klkhtwsypd fsdlkttvtw elesendetl vklthedien fkdlgdgfsr
      121 enftggwnsi lgqslkqyle k
//
LOCUS       WP_284464915             157 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Chryseobacterium sp.].
ACCESSION   WP_284464915
VERSION     WP_284464915.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..157
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=17844
     Region          <12..153
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mkmignldlf tlestepvvl tpleerlhag gygafpsaal dfpdesidfl kllvkdpvtt
       61 fpgrvsgdsl kdigilnedw cliqkgiear pndlvaaiie nqffikrfrp rygdknqike
      121 lklesanvef sdfditdete fflwgvvtwt fknwrkl
//
LOCUS       WP_284465041             589 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Chryseobacterium sp.].
ACCESSION   WP_284465041
VERSION     WP_284465041.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..589
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66673
     Region          1..589
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mnlaeaiilk nvekhpikaa igfkkkdeaw kelswkrfge iifkmgnalk eagvqendkv
       61 aiysdnssew mivdlaamai gaitvpiyst nnaeqaeyii ndsgakailv gnqmqydacl
      121 dilhkeenhl etiivskkav wikkefnsfy ledfiakasa eleickkend dtatliytsg
      181 ttgipkgvml thgnfikafd shfeffkfkn fedelslafl plshvfersw sllclyggar
      241 vyfledpkni akaleevkpt tmcavprffq kvyagvleka eegsslkkki fdwalktgwe
      301 taelrrneqs ipfglklkes vadmlvfski kdkmggrlwf lpcggaslsp evtrffesvg
      361 ihvtvgyglt ettatltlfp lthfehatsg kplpgveiri gesdeiqarg ngimkgyynr
      421 peetqkvfte dgwfktgdag kfddkgnlii tdrikdlmkt sngkyiapqq ienlltnnnf
      481 iqqimlvaeg rqfvsalivp nfeflqdyik knnipftnwe davkndkiis lykeklkelq
      541 dhladyekvk kftlmpaefd intgeitptl kvkrnvvlkk yadiiekmy
//
LOCUS       WP_284464919             385 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Chryseobacterium sp.].
ACCESSION   WP_284464919
VERSION     WP_284464919.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..385
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=45608
     Region          97..377
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mknkwtkpkl ktyplesgkd wyvwfrfngg hpirvredln nietfkerev yglalasvvd
       61 drlkrgwvpt kkkslpqped ksyniidamd ysftimknkl akrtyedyyf iykqvkpiii
      121 eldwhnhdik efesyhikll leacatkyew lnsrynkvsn vlrsiftvlk nefivkinpa
      181 rglkylenee fgkidlitde eqkliiehyn kvcpnfnivl rmiyesgirp aeirriqcsm
      241 idvdkkiitl preasktkgr rvpisndlkn ellnfdltdp dnylfgveap hsknidkkfi
      301 tapypiskss mqrmwtqnah dilkinkkmy wfkhkgandk eengmnlkti kevfghssek
      361 iteiyatkhq ekefekarsl mpkfe
//
LOCUS       WP_284465073             272 aa            linear   BCT 25-DEC-2024
DEFINITION  TPM domain-containing protein [Chryseobacterium sp.].
ACCESSION   WP_284465073
VERSION     WP_284465073.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Sirpio,S., Allahverdiyeva,Y., Suorsa,M., Paakkarinen,V.,
            Vainonen,J., Battchikova,N. and Aro,E.M.
  TITLE     TLP18.3, a novel thylakoid lumen protein regulating photosystem II
            repair cycle
  JOURNAL   Biochem J 406 (3), 415-425 (2007)
   PUBMED   17576201
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..272
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28429
     Region          1..>179
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mklrslkivf sfllicfytf vsaqytipek pavlypvfde agllsqqekd alnnklikfa
       61 dststeievi iikstkgddv nflatmfgeq wkigkkgvdn gvvflvated rtmsiqqgrs
      121 veqyltasva gqildyivtp nfkkglwydg inrgtsaime avqgkfkpea ttapsgdgsa
      181 lkiviiafvi fiiiailfgn rgggggggny dddddviitr kgrrnypggf fpfpgsfggg
      241 gfgggssggg gggfggfggg gsfggggasg gw
//
LOCUS       WP_284465063             493 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Chryseobacterium sp.].
ACCESSION   WP_284465063
VERSION     WP_284465063.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp.
  ORGANISM  Chryseobacterium sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Chryseobacterium sp."
                     /db_xref="taxon:1871047"
     Protein         1..493
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=53003
     Region          184..>486
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mkksvfflal flalnsctrd eiqnenpnte vtqkgpltek qinerinqai ktdgtfnwkh
       61 esdhflwsav fhgnrmvsvg fgsskddfdr skspdnqame neilsvikky egvdtarfll
      121 tsdkylnqmd viidkeetla alrqmktiry vepadyhyfe neakfnttgr ssgsgssgcg
      181 fssatlsavd ytsttpsaki pwaftkhnip eawgystgag vtiglidtgv speqtllggs
      241 fnngassgrt iskvgaynsd gsadqcghgt kmasvmtapr nnaglpvgva ynanliayra
      301 aenvvletss eqngvktaft dlgnnsnvki ismsmghifs vgkiedgvky ayargklifc
      361 aggtstsftn fvgvifpasm setqaitgvk egtsnqkcdv chsgsqidft fqmerasgst
      421 vpvlsyyngq adyvggssva taatagiaal vwaknpswtr dqvlnkmrqa atyypnvnss
      481 ygygninvlk avq
//
LOCUS       WP_284465107             256 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Diaphorobacter nitroreducens].
ACCESSION   WP_284465107
VERSION     WP_284465107.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 256)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 256)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..256
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=26896
     Region          <12..256
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mtgegippad tlaqlrsela qarqqisdmv aaqedflrgv shdlraplrh vtsygalvre
       61 vlqeqppqvd ealgflatme qsarrmaqmi dglqaiarar saalrprava ltvavqdaqq
      121 algaaaegaa wniapdlpvv qadaellaql lvqllgnavk fsrgvaqprv qvqaepaaqg
      181 gvritvrdng vgfdgtraqq lfgvfqrmhr eaefegvgag lalcqaiaqr hgahiqataa
      241 pgagctvale wpaaar
//
LOCUS       WP_284465119             603 aa            linear   BCT 25-DEC-2024
DEFINITION  ABCB family ABC transporter ATP-binding protein/permease
            [Diaphorobacter nitroreducens].
ACCESSION   WP_284465119
VERSION     WP_284465119.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 603)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..603
                     /product="ABCB family ABC transporter ATP-binding
                     protein/permease"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66345
     Region          12..600
                     /region_name="ATM1"
                     /note="ABC-type transport system involved in Fe-S cluster
                     assembly, permease and ATPase components
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5265"
                     /db_xref="CDD:444078"
ORIGIN      
        1 mrrygeaias dsprvrsdra tlqrllpylw qykwrvvaam afmvgaklan vgvplllkrl
       61 vdamtlpags ttallvvpvg lllaygalrl ansvfnelre lvfakathga araialktfe
      121 hlhalslrfh lerqtggmtr diergvrgie slvsfalfnl aatlvevllv lfilarqfdv
      181 wfavitltal vlyvaftvgv tqwriqfrrq anqfdsaahs kaidsllnye tvkyfnneqf
      241 earrydesle qlrqaqlksr stlgllnsgq qliiavglva mlwrategva agrmtlgdlv
      301 mvnafmiqiy iplnflgviy reirqnltdl dkmftlmdre qevadapgat dlaglepptl
      361 rfedvhfayd parpilrgvs feipagktva vvgpsgagks tlsrllyrfy diqqgritia
      421 gqdisavtqq slrrsigivp qdtvlfndtv ayniaygrtg asqaqveqaa raahihgfia
      481 aqprgyettv gerglklsgg ekqrvaiart llknppilif deatsaldsa neraiqaela
      541 saaqnkttlv iahrlstvvd aheilvmeag rivergthaq llahgghyar mwalqkndgq
      601 ngl
//
LOCUS       WP_284465269             267 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Diaphorobacter
            nitroreducens].
ACCESSION   WP_284465269
VERSION     WP_284465269.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..267
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=29029
     Region          14..254
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mtkafrlias tgihkgdrey qqdqvallsh prfngcvlgv vadgmggrsg grkasdqvml
       61 tarqlferys petddaaall khiveeahiv irltaisaeq ephstiaafv inprgdchwa
      121 hagdsriyhf qggrlvfrts dhsyvqalvd rgeiteaean thphsnilvg clgtesdppi
      181 tthliqqmqp gdvllacsdg vwhyfspael asvldsltpr eateflidka rsrargggdn
      241 lslaivkiet lveekkpprl aqltpan
//
LOCUS       WP_284465375             152 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Diaphorobacter nitroreducens].
ACCESSION   WP_284465375
VERSION     WP_284465375.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..152
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=16218
     Region          41..152
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mhwlehkipp plvaalvgva mwftaqasgg vtdsaprtaa avllalvgla fdvaglhafr
       61 rarttvnplr pggasalvvg gvyratrnpm yvglalllla wtvylgapla llgvaafvay
      121 itrfqivpee rvlaqkfgpe faayrsrvrr wl
//
LOCUS       WP_284465429             424 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Diaphorobacter nitroreducens].
ACCESSION   WP_284465429
VERSION     WP_284465429.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..424
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45460
     Region          74..300
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
     Region          226..405
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 msawrkrlat aglsvalvag giwvlnrvde aplphaervt ttasldiarg rylaragncl
       61 achtrqggva faggrgietp fgviyapnlt pdretgigaw sasefwralh ngrsrdgrll
      121 spafpypsyt rvtredsdai faflqslppv vqpgvpsrmr fpfntqaala vwralyfrpg
      181 vfepvpsrsa ewnrgaylvq glghcaachs prnamgavst dgrlsggmaa gwyapalnts
      241 neggvaewpr qdvvmllgag rspraavsgp maevvyhslq ylsdadlqam adylqalppt
      301 dkvaasrrpp spasmqrgwa tyerqcaqch ggegqgdpea fpplagnrav mlenpvnlvh
      361 mvlrggylpa tggnpqphgm ppflqrlsda evadvlsyir nawgnaasrv dtidvhrare
      421 grds
//
LOCUS       WP_284465528             330 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Diaphorobacter nitroreducens].
ACCESSION   WP_284465528
VERSION     WP_284465528.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..330
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34305
     Region          35..328
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mhtsrtpapl rrallasaal laaaspaafa qapaypskpi tivvgyppgg stdltgravg
       61 aelsnrlgvp vvienlggag gaigaqkvas sapdgytllv gasneiaink lvtkkvkydi
      121 ndftaiglva sqplvlvast gtgvknlaef tervrknpgk lsygssgvgt slhlagemik
      181 eqgqlfmthi pyrgvapltn dlvgnnlefg vfvlssglph iksgkvialg tteakrstva
      241 pdipalaesa qyknvdigtw falmapahlp kpvaerlkka lnetlespdf rkrmeaagst
      301 vaspsldvdk flaaevakyk kiiefakiee
//
LOCUS       WP_284465657             135 aa            linear   BCT 25-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Diaphorobacter
            nitroreducens].
ACCESSION   WP_284465657
VERSION     WP_284465657.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..135
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=13727
     Region          3..134
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mktkpelels dvkliaaaae aealknqwav tiaivddggh llwlqrldga aavsahiapa
       61 kahtaalgrr eskgyedvin ggrtaflsap alqgmleggv pimkngqclg avgvsgvksh
      121 edaqiaragi avigl
//
LOCUS       WP_284465743             556 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Diaphorobacter
            nitroreducens].
ACCESSION   WP_284465743
VERSION     WP_284465743.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 556)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..556
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=59815
     Region          40..504
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mallvlsfgg cgglpkdvdr pvsmaldtag eptelativq qlrqkagarh asgfsllsgp
       61 qeaygsrlal vqsaqktldl qyyaihadas sahllrsvvn aarrgvrvri llddfhstgr
      121 nalvmrmafe pniemrmfnp vagprasflg rmwgtvsdfs rvqqrmhnkl fladnmmgvt
      181 ggrnlgdayf gkaeaenfvd ldvlavgpiv admsrsfdsy wnnpraypvq slvsreeldr
      241 lraqvrssge kagpqagspg sttpadspra sspqwdtqpm dlrtvdfiwa paamlvdept
      301 kiplegdepa psaamrvgtt pgahpeasdt pqalpapaap vssgdtvvdg lltlmdrtrr
      361 elliispyfv pgddmkrafa rarqrgvrvr lltnslasnd apiahvgyar hredllamgv
      421 elyelrseqa glrsafgssg asaagasrsm lhskvivvdg rmvvvgsmnl dlrsqlhnte
      481 iallirsral aaeaaqqidt amregawhlq rsadgdlvwr apqgsgleda htdpdsslal
      541 rlllkllgpl apdhll
//
LOCUS       WP_284465793             116 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter, partial [Diaphorobacter nitroreducens].
ACCESSION   WP_284465793
VERSION     WP_284465793.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 116)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 116)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 116)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 116)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..>116
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          23..>116
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 maqlpqraap sastvgedpr htrkawsvli vstlaftvcf mvwmmfgvig ipikkmlnls
       61 stqfglltam pvltgslvrv plgiwtdryg grivmallma atvpaiwmmg yateyw
//
LOCUS       WP_284465803             236 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-L-isoaspartate O-methyltransferase family protein
            [Diaphorobacter nitroreducens].
ACCESSION   WP_284465803
VERSION     WP_284465803.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Edwin,R.K., Challa,N., Sharma,R., Satyamoorthy,K., Parsa,K. and
            Misra,P.
  TITLE     PIMT/TGS1: An evolving metabolic molecular switch with conserved
            methyl transferase activity
  JOURNAL   Drug Discov Today 27 (8), 2386-2393 (2022)
   PUBMED   35462043
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Furuchi,T., Sakurako,K., Katane,M., Sekine,M. and Homma,H.
  TITLE     The role of protein L-isoaspartyl/D-aspartyl O-methyltransferase
            (PIMT) in intracellular signal transduction
  JOURNAL   Chem Biodivers 7 (6), 1337-1348 (2010)
   PUBMED   20564550
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Kagan,R.M., McFadden,H.J., McFadden,P.N., O'Connor,C. and Clarke,S.
  TITLE     Molecular phylogenetics of a protein repair methyltransferase
  JOURNAL   Comp Biochem Physiol B Biochem Mol Biol 117 (3), 379-385 (1997)
   PUBMED   9253175
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..236
                     /product="protein-L-isoaspartate O-methyltransferase
                     family protein"
                     /EC_number="2.1.1.77"
                     /GO_function="GO:0004719 - protein-L-isoaspartate
                     (D-aspartate) O-methyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0030091 - protein repair [Evidence IEA]"
                     /GO_process="GO:0036211 - protein modification process
                     [Evidence IEA]"
                     /calculated_mol_wt=26162
     Region          24..228
                     /region_name="Pcm"
                     /note="Protein-L-isoaspartate O-methyltransferase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2518"
                     /db_xref="CDD:442008"
ORIGIN      
        1 mnmplntsad icdpteqary nmveqqirpw nvldeavlel latvrreefv ppayqgaafi
       61 dtqiplnpsv eeaerlgqvm laprvdarmf qdlqvqstdr vleigagsgy maallaarae
      121 rvvsleivpe laefarenlr sagvdnaevr qsdgaldpip dgpfdvivls gsvaeipqrl
      181 lgllrdggrl gafvghtpmm ratfvhrqgd ryettqpwdv vvprlrhfpe ptrfkf
//
LOCUS       WP_284465873             637 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Diaphorobacter
            nitroreducens].
ACCESSION   WP_284465873
VERSION     WP_284465873.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 637)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..637
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=66059
     Region          41..609
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mgswmqwank pygrrvrmga valaacgvla acggndddea qpleltvlhi ndhhstldak
       61 sktlklstgg aapvdvavea ggfarvtaaf dslakaagan vlklhagdal tgtlyfnrag
      121 adgeadaalm ntvcfdaftl gnhefdkgda glkgfldllk kgscktavls anvkfgagsa
      181 lnatkapgyv qpstvversg qkigivglti agktkasssp dadttfedev taaqreidkl
      241 raqsinkiiv mshvgygydk eiaaklsgvd vivggdshtl lgpdalkttg vgtpggaypt
      301 rvtdkdgknv cvvqaweyaq vvgelkvrfd gkgevtqcsg tphvligsdf tinklpptda
      361 ekkaidadva akgflrvtqp aaaattalqp fkdrvavfnk tnvavvpkel cfrrvpgnpg
      421 sggssptcna egsvhlrggd iqqlvaqayv degnakygga dislqsgggv rialdgtvta
      481 aqviqvlpfg nmlfrldvtg aevksmledg leavfkaggs tgpypytggl rfdvnasaaf
      541 gqrasglevr naatgtwgpi dpaktyrlfv lsfnatggdg yktlaavpaa rrldigvlda
      601 dvffsyidkq prdaatglpv lnrlphelys tksfagq
//
LOCUS       WP_284466108             208 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Diaphorobacter nitroreducens].
ACCESSION   WP_284466108
VERSION     WP_284466108.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..208
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=22341
     Region          8..205
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mtqehrfiyl asqsprrrql leqlgvrhel llpnaagdea edaeaieavl pgeapttyve
       61 rvtglkldaa varharrgls papilcsdtt valartiygk pedahdavrm lrelaghehr
      121 vltavalqvg prrltalsvs rvrfapmsra qiedyvatge plgkagayai qgraaayveh
      181 lsgsysgimg lpmyetarll raagvlav
//
LOCUS       WP_284466143             582 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Diaphorobacter nitroreducens].
ACCESSION   WP_284466143
VERSION     WP_284466143.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 582)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..582
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=62952
     Region          11..562
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mssrsvnyts spllasktpv wrskfivalv algfvglagr aayvqvignd ffqrqgevrf
       61 artlelpanr grildrngli lassvpaasi waipedvema kpevraklkd larlmdmpls
      121 tlqgkladed ktfvwikrql dwdvgqqita lglkgiylrk eykrqypege aaahvvgftn
      181 vedhgqegme lafdkdlagk pgsrrvikdr lgrvvegvga evppvdgkdm qlsidskvqf
      241 fayqklrdtv qahkakagsv vvldartgev lalanypsyv pdkrqnltge qlrnraltdv
      301 fepgstikpi tvglalesgr fkpetsvdtt pgrltitgst isdthnygll tvegviqkss
      361 nvgttkiamq lpaqemwetf savgfgqkpq iafpgvasgr lrpykswrpi eqatmsygyg
      421 lsaslfqmar sytvfsnggk vipatmlkth eapvgvpvfs ertanqvrkm lqmaagpggt
      481 gqkaqtvgys vggksgtark qvgksyasgk yrawftglap idhpriivav mvdepsngvi
      541 yggavaapvf sevvqqtlrm mgvapdmavk plivsndvee sl
//
LOCUS       WP_284466166             566 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Diaphorobacter nitroreducens].
ACCESSION   WP_284466166
VERSION     WP_284466166.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..566
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=61328
     Region          186..548
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mpsklaaaas plpfhrlwna fltarvmval allllqllgi alnqagepll fsiclgylva
       61 tvalrvwghg avpdprpgiq wlpsigldll lvsvlqalqq sgglnftplf glpvlmagvl
      121 gsltlalatt agatllllaw awwlgtygga gdgtqrylqa altgtgyfiv aylvhllaak
      181 ltseqqmarr sqmdarthra vsalvmqhva dgvlvldlhg qvrlanpaal lmlghkisgd
      241 ssltlthtaa fkplmdlaca tfqmerpqha dvnvlhdgqi pmalrvrawl thtqdtpdds
      301 pgeplcvmfl hdlremearl rteklaamgr msaavaheir nplaaivqan elldedlddp
      361 tqkrlthmvr qnadrlvrit edvldiarvq hqinqassst vvldamvqqv wndwtaqdpa
      421 rrqgqlvlda gaaqvefdae hlrrvlvnll dnalrykgpe pdslclatra tpggkagvqv
      481 wsdgapldks verhlfepff ssesrssglg lyicrelcqr hgaaighqrt trslargeva
      541 gnaftvtfrs lsrpadsasl fdtivv
//
LOCUS       WP_284466182             134 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein, partial [Diaphorobacter
            nitroreducens].
ACCESSION   WP_284466182
VERSION     WP_284466182.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..>134
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
     Region          5..>110
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 msqhtpshas rsalidctkg lacaaivwhh lafygpmsdv arqavpglid wlyeyarmav
       61 qvflvlggfl aaaslapqgl arftdpaqri arrfvrlvvp yavalviaiv vqaavqpwfd
      121 hasvsdvpdl gqll
//
LOCUS       WP_284466193             572 aa            linear   BCT 25-DEC-2024
DEFINITION  PHA/PHB synthase family protein [Diaphorobacter nitroreducens].
ACCESSION   WP_284466193
VERSION     WP_284466193.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..572
                     /product="PHA/PHB synthase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=63082
     Region          36..570
                     /region_name="PhaC"
                     /note="Poly-beta-hydroxybutyrate synthase [Lipid transport
                     and metabolism]; COG3243"
                     /db_xref="CDD:442475"
ORIGIN      
        1 mstnfdaswa dsarqfqqmv gegwsqmlqv lqpkemgaal smppagpvsf apdklaavqq
       61 rylqevqalw shalhhddap lsndrrfage nwahnplsaf svaayqlqah almglvdavq
      121 addktrarir fsveqwlaam apsnflvfna daqqkaleth gesiakgvan llhdlgqghi
      181 smtdesrfev grnvattega vvfenelfql leykpltpkv yerpllmvpp cinkyyildl
      241 qpdnslirha vaqghrtfvv swrnpdasla hktwddyide avltaiatvq qiagakqina
      301 lgfcvggtml atalavlaar geepvasctf lttlidfadt gildvfideg fvrmrelqmg
      361 qgglmkgqdl astfsflrpn dlvwnyvvgn ylkgetpppf dllywnsdst nlpgpyyawy
      421 lrnfylennl irpgrltvcg esldltqvql pvyiygsred hivpigaaya stqvlpgdkr
      481 fvmgasghia gvinppakkk rshwlredgq lpatldawla gatelpgsww ddwcawlqgh
      541 agrqiaapka ygkapkfkai epapgryvqq ka
//
LOCUS       WP_284466242             257 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator, partial [Diaphorobacter
            nitroreducens].
ACCESSION   WP_284466242
VERSION     WP_284466242.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 257)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 257)
  AUTHORS   Khuri,S., Bakker,F.T. and Dunwell,J.M.
  TITLE     Phylogeny, function, and evolution of the cupins, a structurally
            conserved, functionally diverse superfamily of proteins
  JOURNAL   Mol Biol Evol 18 (4), 593-605 (2001)
   PUBMED   11264412
REFERENCE   7  (residues 1 to 257)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   8  (residues 1 to 257)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14398393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..>257
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          51..155
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          55..>257
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mpspslrrpa pppaepaaas tagraarpar vlsyvesltp hlfvpsrerp vrakhrelra
       61 dtqvrphshp waqvaisttg vlrltvprgt yivppsralw ippgvehavt mvedadlrtl
      121 yfyqppgrcg pavaraqeep wrqcrvldvs ellravvrem ptdpddgapp ppellhrerh
      181 lsalildelr rassvrlgvd lprdkrlrhl ceavladptr hdtladward tgasprtvar
      241 lfrqelgstf tqwrqqv
//
LOCUS       WP_284466249             300 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Diaphorobacter
            nitroreducens].
ACCESSION   WP_284466249
VERSION     WP_284466249.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..300
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=32905
     Region          3..245
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mkfsvfqisr rggreknedr mgycytresv lfvladgmgg hpegevaaqi aiqtvsamfq
       61 rqakptlkdv qeflstallg ahhqilrygt tkdmldtprt tlviavvqdg raswihcgds
      121 rlylvragel lmrtrdhsyl elrnaaiagl ervnrnvlft clgsptkply dvagpvlleq
      181 gdrillcsdg lwgalddeti arqlgrqtvs navpdlveda lrkagdgsdn vtvvamewet
      241 pdtfestqgi stdsisddvf astiqagple sfaddlddet iersiaeine airrsaarkl
//
LOCUS       WP_284466306             586 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Diaphorobacter
            nitroreducens].
ACCESSION   WP_284466306
VERSION     WP_284466306.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..586
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62765
     Region          29..563
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mqrhddskpl tnllqaahas tppaadggrr rfvrqitlga aalgtlplaa cgggdddapa
       61 vqfahgvasg dpladrvmlw trvtppadfs aeipvqweva sdaafasiva rgevrtsaar
      121 dytvkvdatg lkpatayhyr fkafeatspt grtrtlptgs vaqvklavfs canypagyfn
      181 vyadaarrgd ldatvhlgdy lyeygqggya sgnaaalsrl sqpaneilsl adyrtrhaqy
      241 rtdadlqalh aaapmiavwd dheiandtwm ngaenhqvae gsfaarkava lqayhewmpt
      301 rnaqpdviyr sfafgnllal hmldtrvvgr daqvdyaaff kpggfdaagf taavgnparq
      361 llgtaqtqwl qqqmtassat wqmlgqqvlm grmnipapil metlqpgsgv tvsryaaiva
      421 kartapatlt peeqailaqp sipynldawd gyqaaretvl gmaramnknl vvlagdthna
      481 waselndmng npvgvefats svsspgfeey lpnenpatls aallqlvepl kycdtarrgy
      541 mvvtatatec raqwvyvnti tsrqfttsae ttlavqagtp grllkv
//
LOCUS       WP_284466318             729 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Diaphorobacter nitroreducens].
ACCESSION   WP_284466318
VERSION     WP_284466318.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 729)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 729)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..729
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77210
     Region          64..729
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mnrptplala ifvalqsmah aqgtpsapel ptvevnasad asaqglspay aggqvarggr
       61 vgilgtrdpq etpfsitayt neliqdkqar svgevlqnds gvrmargfgn fqeayfirgf
      121 vvgsddvayn glysllprqy iatelfarva alggaatflr gaapfgggag gtinllpkra
      181 pneplsrvtl gtgsggygha aldlarrfgp egstgirvna alrdgdtaid heesrlglls
      241 vgldwrsrnv rlsgdigwqd nklkgtrsnv tlgplatsip aapdakanfs qpwsysnerd
      301 lfgtlrgevd ltpditawga wgmrrskean slanlrvtns dtgagsvyrf dntrkdrvdt
      361 gelgvrgklr tgsvghewva sasyfdfekd nayvmdygnt lpanlydytp yaapafsaga
      421 lyggdlanpn ltgrtrlasf algdtlafmd dtllltvgar hqsikvqdya ygtsaplgsy
      481 dksrispaag vvfkassrls lyanyiesls qgetapatan gvpvvnhgqq lapyvskqke
      541 igvkydagri ggsvalfstt rpralvnadn vftaagedrh qgvefnvyge aarglrllgg
      601 atwlqakqra tgtaaldgnr vigvprlqan agvewdvpgv rglaldtrvv htgasyadda
      661 ntlrlpawtr ldlgvrylte vggrlltlra rvdnatnrny wasaggypgs gylvvgaprt
      721 ftlsasmdf
//
LOCUS       WP_284466325             107 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase, partial [Diaphorobacter nitroreducens].
ACCESSION   WP_284466325
VERSION     WP_284466325.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 107)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 107)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 107)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..>107
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          2..>104
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mkfqgsqnyv atqdlmlavn aaitlqrpll vkgepgtgkt mlaeevaqal dmpllqwhik
       61 sttkaqqgly eydavsrlrd sqlgdervkd ihnyivkgvl wqaftad
//
LOCUS       WP_284466339             607 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Diaphorobacter nitroreducens].
ACCESSION   WP_284466339
VERSION     WP_284466339.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 607)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..607
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=65779
     Region          36..598
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mdsfapaarp rsedgvthpp phrtddaadd saaaflqrig slsagtlera amdaapdgiv
       61 ladrqgrilm vnapmetisg ytnaqlcgqs idllvpvhar pehgqhmqry hqspsrrpmg
      121 mgrdlwlqrr dgsqvpvdia lghssshggt vvafvrdvsd lrrlearmhy qathdtltgl
      181 lnrwtfgqrl eqaiaeqaga qsppfallll dlddfkaind gyghaagdqv lqevarrlrg
      241 algtgdilar lggdeftvll pgvacaaqae cvaarlmqal cvpcrvqgfe lnfgasmgia
      301 lcpqdagdaa tllryadmam yhakhrgran fafyapsmgr kmaekiqlhe rlklalaygg
      361 ltlhyqpqve vatnrmvgve allrwhdpql gevsperfvp vaeatglile lgawvmaaac
      421 rqiaawerqg mrlrvavnls aqqlrqtdlv eqvarnlrth hvppellele vtesealadp
      481 eqacqvlnel ralgvavald dfgtghssla ylkrlpvshi kvdrefmrnv pasggdttlv
      541 ravvalahtm glrvvvegve treqlqflre mqcacyqgwl fakalapddv allyaagadv
      601 aaegalg
//
LOCUS       WP_284466343             460 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Diaphorobacter nitroreducens].
ACCESSION   WP_284466343
VERSION     WP_284466343.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..460
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48911
     Region          28..454
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 myktlktiaa raflisagai fytqsawall piqhwtepsg arvwlvespa ipmvdvqvdf
       61 dagarrdpap qaglaaaaal msskgvtagg pneppmdene lgeawadlga sfeagaerdg
      121 lafslrslte pdlldraarl aarqlgqpsy apdvwqrera rwsaaikead trpgtvaska
      181 fnaavfgghp ygqrataetl nniqpadlqa fhaqylqach arvsivgalt rsqaqtlvqt
      241 llsrlpapqa gacaplppva evqplaravq vdvpfasaqa hvligqpgfv rrdpdflall
      301 vgnhilgggg ftsrltnevr ekrglsysvg ssfspglngg afvvglqtrp dqaaqavqvt
      361 rdvlarfvae gpteaelraa kdnlvggfal ridsnrklla nvvniawndl pldylehwtd
      421 rvealtvadi raalqrklqp ermvtvivga qpaatakarp
//
LOCUS       WP_284466386             303 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Diaphorobacter nitroreducens].
ACCESSION   WP_284466386
VERSION     WP_284466386.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..303
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33688
     Region          110..213
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mtnarwqrwa vavhllliag wmawfwarsp alalagvaav plmfrlgmap qfflmawvcr
       61 gdatprprag qllrawwaes rwaslvfgww qpfrhqavad wlpprasdvp gprgvvlvhg
      121 flcnrgfwtp wlallrargh afvavtlepa fgsiddycrt iddavrrvae atgrvplivg
      181 hsmgglaara wlravpgseq rvhrivtlgs phhgtwparg arstngrqmr lhgpwvrqlg
      241 qdepparaav fvcwysncdn vvyppaaaml qgadnrfieg vahvemafhp rvlqdclall
      301 eqp
//
LOCUS       WP_284466429             519 aa            linear   BCT 25-DEC-2024
DEFINITION  malonate--CoA ligase [Diaphorobacter nitroreducens].
ACCESSION   WP_284466429
VERSION     WP_284466429.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Pohl,N.L., Hans,M., Lee,H.Y., Kim,Y.S., Cane,D.E. and Khosla,C.
  TITLE     Remarkably broad substrate tolerance of malonyl-CoA synthetase, an
            enzyme capable of intracellular synthesis of polyketide precursors
  JOURNAL   J Am Chem Soc 123 (24), 5822-5823 (2001)
   PUBMED   11403625
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11482749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..519
                     /product="malonate--CoA ligase"
                     /EC_number="6.2.1.76"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0090409 - malonyl-CoA synthetase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0090410 - malonate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55901
     Region          4..519
                     /region_name="PRK07514"
                     /note="malonyl-CoA synthase; Validated"
                     /db_xref="CDD:181011"
     Site            order(169,172..177,179..180)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341264"
     Site            order(172,212..213,216..218,258,260,264,286..288,307..312,
                     316,339,398,410,418,421,424,453,489)
                     /site_type="active"
                     /db_xref="CDD:341264"
     Site            order(172,286..288,307..312,339,398,410,418,424)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341264"
     Site            order(212..213,216..218,258,260,264,286,308,310..312,316,
                     421..423,453,489)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341264"
ORIGIN      
        1 mssssqnlfs alraafpadl dqtaveaasa agapllytwr dldrasaria nllaslklpe
       61 gsriavqvek sveamllyla tlragyvflp lntayqsaei eyfignaepa vvvctpgnfg
      121 wvskiaftag tqhvftlgdd rtgslleraa hfgdehravp rkaddlaail ytsgttgrsk
      181 gamlthgnll snaqvlkdyw gwkpgdvlih alpifhvhgl fvaihgalin gskmiwmakf
      241 dpkaviaamp ratvfmgvpt lyvrmlaepa ltqaaashmr lfiagsapll ietfkewqdr
      301 tghtileryg msetimltsn pyaadarhgg qaerrgstvg fplpgvglrv vddagkpvpv
      361 geigniqvkg pnvfkgywrm pektkeefsa dgwfktgdvg kvdergyvsi vgrskdliis
      421 ggynvypaei egyvnempgv aesavvgvph pdfgevgvvv vipkpgakvd gdaviaslks
      481 qlanfkipkr cfvttelprn tmgkvqknll rdqykglfa
//
LOCUS       WP_284466548             459 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Diaphorobacter
            nitroreducens].
ACCESSION   WP_284466548
VERSION     WP_284466548.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..459
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=48809
     Region          9..457
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mprlpappae lvsfleglpd phillddryr ilaangayrr qfgasggteg gaegsvvgrt
       61 chavshhaiv pcdqagescp laqarasgqr ervlhvhhta qgeeyvqiel apvagadgtt
      121 gffvekmvpl pvaaqpvpsa qgligrspaf qkmlglvarv apsraavlll gesgtgkelv
      181 ahavhqgslr arralvpvdc sslpealfes elfghekgaf tgaaqarpgl veaadggtlf
      241 ldevgdiplp lqvkllrlle tgtyrrvgst elrnadlrvv sathrnlqhm vaagrfredl
      301 yyrlstfpih lpplrerqgd iallacslle rvapppralq lsgaalalle trpypgnvre
      361 lrnllertal lcdgdtigae hvqqalscgl pplvsevgeg ameprasaal agssrlrrll
      421 ddqalqkala ahqgsraala rqlgisersl yrrlktlca
//
LOCUS       WP_284466566             635 aa            linear   BCT 25-DEC-2024
DEFINITION  B12-binding domain-containing radical SAM protein [Diaphorobacter
            nitroreducens].
ACCESSION   WP_284466566
VERSION     WP_284466566.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Banerjee,R. and Ragsdale,S.W.
  TITLE     The many faces of vitamin B12: catalysis by cobalamin-dependent
            enzymes
  JOURNAL   Annu Rev Biochem 72, 209-247 (2003)
   PUBMED   14527323
REFERENCE   3  (residues 1 to 635)
  AUTHORS   Ludwig,M.L. and Matthews,R.G.
  TITLE     Structure-based perspectives on B12-dependent enzymes
  JOURNAL   Annu Rev Biochem 66, 269-313 (1997)
   PUBMED   9242908
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..635
                     /product="B12-binding domain-containing radical SAM
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0031419 - cobalamin binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=69246
     Region          191..560
                     /region_name="YgiQ"
                     /note="Radical SAM superfamily enzyme YgiQ, UPF0313 family
                     [General function prediction only]; COG1032"
                     /db_xref="CDD:440655"
ORIGIN      
        1 mpaalprvls vippmtqlnt pypstayltg flrsrgvpaw qedlaialvl rllsrdglaq
       61 vaeraralpa naqspavqff laqqerylat vgpamaflqg rdstlahriv grhylpegpr
      121 faaldvyedd gsgdplgwaf galgltdkak hlatlylndl advlqgavda rfefvryaeq
      181 lagsqptfdp ladalaqapt fvdevlqqlt heaiarhqpg vvllsvpfpg svygafriaq
      241 alkaqhphiv tvlgggfvnt elreladprv fdffdyvtld agerpllall ehlqgqrgrq
      301 rlvrtfvrnd dgavqyvhla epdvafaeig tptwdglpld sylslldmln pmhrlwsdgr
      361 wnkltvahgc ywkkcsfcdv nldyigryeg asaqvladri aaivaetgqt gfhfvdeaap
      421 pkalkalaqe liargtgisw wgnvrfektf tpelaellad agciaisggl evasdrllgl
      481 mkkgvsvdqv arvtrafsda gilvhaylmy gfptqtvqdt vdaleyvrql fengciqsgf
      541 fhrlactvhs pvgqspeeyg vtlaplppgg fakndvafid ptgvdhdalg aglkkaiyny
      601 mhgigleqdv rmwfpfhvpk ttvrpgriar alaar
//
LOCUS       WP_284466573             265 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Diaphorobacter
            nitroreducens].
ACCESSION   WP_284466573
VERSION     WP_284466573.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..265
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27998
     Region          135..227
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mprrprrlhh lhappprriv lpwplpavlv waaawllfag lrgsvaplaa lglacavgva
       61 gsllaqgwwr rglialgfpl saalggaval pawgwllpla llllvyplna wrdaplfptp
      121 pgalhglqda aplpagapvl dagcglgdgl kalraaypqa rlhglewsgp lallcrlrcp
      181 warvrrgdlw aadwggydlv yvfqrpesma rvaakaraem apgswlvsla favpgvcpsa
      241 rldsfaghav wiyqlplpgd gaaph
//
LOCUS       WP_284466574             180 aa            linear   BCT 25-DEC-2024
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Diaphorobacter
            nitroreducens].
ACCESSION   WP_284466574
VERSION     WP_284466574.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..180
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19776
     Region          7..176
                     /region_name="YdeN"
                     /note="Predicted esterase of the alpha/beta hydrolase fold
                     [General function prediction only]; COG3545"
                     /db_xref="CDD:442766"
ORIGIN      
        1 mnpsqilllp gwqnsgpghw qtewerlhgy qrvqqhdwmr plrgdwsarl eevvadapge
       61 vvlaahslgc iltawwaaht rhahkvrgal lvapgdverp dlaaqipgwa piarqvlpfp
      121 avlvgsqddp ycsferaqtl agawgarfvd cgprghinad sdlgdwpegh allralmnkd
//
LOCUS       WP_284466646              43 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Diaphorobacter
            nitroreducens].
ACCESSION   WP_284466646
VERSION     WP_284466646.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 43)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 43)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 43)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..43
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..43
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=4669
     Region          <1..43
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 msratwwagv ktgrfpqpvk lgprttcwrs adidkliadl aak
//
LOCUS       WP_284466661             396 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Diaphorobacter
            nitroreducens].
ACCESSION   WP_284466661
VERSION     WP_284466661.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..396
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42509
     Region          2..392
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mtktirpldg itvislehav aapfctrqla dlgarvikve rpgsgdfarg ydqrvkgqss
       61 hftwinrske slaldvkqpq akaallqllk tadvlvqnla pgaaarmgls yealkahnpk
      121 livcdisgyg adgpyrdkka ydlliqseag flsvtgtpet psksgisvad iaagmyaytn
      181 ilsalllrgk tgegshidvs mleamgewmg ypmyyafdga pppprtgash asiypygpfv
      241 agdgktvmlg lqnerewkaf cdavlqrpev atdarfcsna qrnahrdalq alilqefstl
      301 saaqvverld qagianarvn dmadlwahpq laarqrwsdv dspvgripal lppgvnsafd
      361 yrmdavpavg qhnaailael gwsaeqidal qapqpl
//
LOCUS       WP_284466688             667 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: peptidase U32 family protein [Diaphorobacter].
ACCESSION   WP_284466688
VERSION     WP_284466688.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter
  ORGANISM  Diaphorobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Diaphorobacter"
                     /db_xref="taxon:238749"
     Protein         1..667
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=74501
     Region          6..307
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
     Region          457..518
                     /region_name="DUF3656"
                     /note="Collagenase; pfam12392"
                     /db_xref="CDD:463557"
ORIGIN      
        1 msllphqlel lspardadig ieavnhgada vyiggpafga ratagndird lerliqhahr
       61 fnsrifitln tilrddeleg arqmawqvye agadaliiqd mglleldlpp iqlhastqtd
      121 irtpekarfl qdaglsqivi areldlqqiq aireatdpsr ttieffvhga lcvaysgqcf
      181 ishahtgrsa nrgdcnqacr lpyevldgag riiahekhvl smkdnnqsdn lralidagvr
      241 sfkiegrykd mgyvknitah yrklldeiie ereftgepla rsssgrttft fepdpdqnfn
      301 reftdyfvng rkedigafdt pktpgraigw vtqigdnwfe levsdkatal hngdglcyyd
      361 lqkelvgvhi nraecvapkk giwrvfpkne itefkdlrkg leinrnrdmd wvrtlekkss
      421 drriglwahl aetadgfalt ltdedgfvgs asviqphqpa tdavkaeatl rdqlgrfgat
      481 rfavhamalq lsqpwfvpas alnqlrrdav valedartag fvrlpravpv qppvpfpedt
      541 ltylanvfnh kahdfyvkhg vkvidaayes keeegevslm itkhcvrfsm slcpkqakgv
      601 igvkgtikae plqlingkek ltlrfdckpc emhvvgkmkk svmnqhlkdm qaqplqfyrt
      661 rpaptsa
//
LOCUS       WP_284466699             324 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Diaphorobacter nitroreducens].
ACCESSION   WP_284466699
VERSION     WP_284466699.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..324
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33952
     Region          29..317
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mpasrrlata alalapfafa lpaaaqdgqp vrlivgyaag gpvdqgarlf apalskelgm
       61 pvmvenktga natiagsevv rskpdgmtlw faasptitis pnvmtkmpfd pakdltpvap
      121 ilsyynvlvv nnnepyksvr elvataksnp gklaygsagv ggsnhlgall fakrsgidmn
      181 hipykgnapa mtdviggqln mmldiistas ayihsgkvra iavtspqrna slpdvptfae
      241 sgidglkgfd vggwygvygp kgmspelvak lnkavnaalq qpelkkryke lgydewtgap
      301 qklaergaqe ramwatvtqg itvd
//
LOCUS       WP_284466704             323 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Diaphorobacter nitroreducens].
ACCESSION   WP_284466704
VERSION     WP_284466704.1
KEYWORDS    RefSeq.
SOURCE      Diaphorobacter nitroreducens
  ORGANISM  Diaphorobacter nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Diaphorobacter.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Diaphorobacter nitroreducens"
                     /db_xref="taxon:164759"
     Protein         1..323
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33493
     Region          28..321
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mnrrhlllsa aaigaalsap lshaqdapir lvvpyapggp ldvtaralae rvrdtlgvvv
       61 vdnkagaggn igadliaksa pdghtigiaa tathavnpwl ynrmpydaak dfagitqmvr
      121 vpnvlvvnaa raeqlkintl qdliayakan paklnygsgg ngsaghlage mfkqkagifa
      181 lhipyrgasp aqlallagev dfnidnlaaa apniksgklk alavtsleas pmlpgvppls
      241 qtfkgfaidt wwglvapagt pkpviaklnk aftealkape tktrfsalma epvattpeqf
      301 dafmaaerak yqqvvkasga kvd
//
LOCUS       WP_284466837             158 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Actinomadura madurae].
ACCESSION   WP_284466837
VERSION     WP_284466837.1
KEYWORDS    RefSeq.
SOURCE      Actinomadura madurae
  ORGANISM  Actinomadura madurae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Thermomonosporaceae; Actinomadura.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 158)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 158)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Actinomadura madurae"
                     /db_xref="taxon:1993"
     Protein         1..158
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15962
     Region          29..104
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(33..34,36,39,42..43,46..47,50,80,99..100,102..104)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(34..35,39..41,54..56,65..68,70..71,74..75,77..78,
                     84..86,91..93)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(54,57,99)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mghgapqrsg taaggasrar ldaasaarva ttlqalatps rllilarlre gplpatelaa
       61 evgmeqsacs hqlrllrnlg lvvgtrqgrs vvyalhddhv aelldqavyh vehlnsglsd
      121 avpasaasgt tagtvrpepa paaeagadpe kqpaatrg
//
LOCUS       WP_284466859             171 aa            linear   BCT 25-DEC-2024
DEFINITION  lipase family alpha/beta hydrolase [Actinomadura madurae].
ACCESSION   WP_284466859
VERSION     WP_284466859.1
KEYWORDS    RefSeq.
SOURCE      Actinomadura madurae
  ORGANISM  Actinomadura madurae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Thermomonosporaceae; Actinomadura.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18498059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Actinomadura madurae"
                     /db_xref="taxon:1993"
     Protein         1..171
                     /product="lipase family alpha/beta hydrolase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18003
     Region          <1..46
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
     Region          <2..151
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mlastgapkv divghsqggm mpryymkflg gaakvnklvg ivpsnhgtnm sglvelgsll
       61 gitqavvraa paagqqivgs dflkklnegg dtepgptyiv latkydevvt pytseflngs
      121 naqnvllqdk cpndtnahvg iafdpvmikf vlnsldiwgp ywpidcarpl g
//
LOCUS       WP_284466865             898 aa            linear   BCT 25-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Actinomadura madurae].
ACCESSION   WP_284466865
VERSION     WP_284466865.1
KEYWORDS    RefSeq.
SOURCE      Actinomadura madurae
  ORGANISM  Actinomadura madurae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Thermomonosporaceae; Actinomadura.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 898)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Actinomadura madurae"
                     /db_xref="taxon:1993"
     Protein         1..898
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=95284
     Region          30..880
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mparrhhagt atgtaeisad preplpllrk elgtgdggls greavrrlav ygpnqvrrre
       61 krsllrllsa qllhplalll wgagalafva gmpvlgwail avilvnavfa llqehqaera
      121 vealaaylpe qarvvrdgrr qavdvaglvp gdlilleegd kvpadarlad galeldlsml
      181 tgesapverv aapaeegigl lhepnlvfsg ttctggeara ivfatgghte lgriaalsqr
      241 aprgdsplet qvkkvawlia avavgmgavf lligalvglp ltdalmfaig llvanvpegl
      301 lptitlalav gvrvlarqga vvkrlsavet lgstnvictd ktgtltqnrm rlqaywtpqg
      361 gvmpseetpp aelaqaitec ttvsydqagd lqgdpteial vlgsgpdlpa rlaarddrrr
      421 avfrfdarlr lmstvaqadd hlavhvkgap eavlarcsgv drpavmavvd elarkglrvl
      481 avavrnlppd aerprrreda etglrllgla glydpprpev adavrrchda glrvhivtgd
      541 ngataaavar evgiglprlh vvpesekvhd heldelltgd geivfarssp etklkvadal
      601 rahgrivamt gdgandapal hqahigvamg rsgtdvarea stmvltddnf ativtaiesg
      661 rrvydnvrkf ilyifahavp eivpflvfal sggliplplt vlqilaidlg tetlpalalg
      721 repaepgimd rpprsssqgv isrdmliraw gylglvsaal vmfvfvyvlw ragwhpgdpt
      781 gggaalhhay ltattatfag lvtcqigtam aartdhaslr qtglttnpll lagiafevgf
      841 aavviylppf qhlfgtaalp wdvlaiiatf piivwatdel rrrhrrqhtr ptndvtkp
//
LOCUS       WP_284466889             949 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Actinomadura madurae].
ACCESSION   WP_284466889
VERSION     WP_284466889.1
KEYWORDS    RefSeq.
SOURCE      Actinomadura madurae
  ORGANISM  Actinomadura madurae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Thermomonosporaceae; Actinomadura.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..949
                     /organism="Actinomadura madurae"
                     /db_xref="taxon:1993"
     Protein         1..949
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=100373
     Region          <3..898
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mdgrpptrgt tfgrqreras idelltrvdg prvmlveget gigrtrllee aarraadegf
       61 avlgadttpe lrrpavleml lsvlgepgsn plpagqdrpa erlraalerr arstsllvvl
      121 ddlewadpat vlalrtlpir lasspvcwil arrtgsggte ldrlflrlqa ggavllqlrp
      181 lsgeavsdlv taalgarpdp dlrvladgag gnplllleli nglvdeggvv isqgharlit
      241 srlperariv vqgrlddldp aarrllevaa mlgpafhplv aadllgitps qllpsleail
      301 atgllaahee alvfrhdvvr esvimgipgp vrqalhvqig rtllehggrv eaaathlmag
      361 avpgvpevlq sldrasveml dtypavaael trraldltep adprrfartm tamrtlvaag
      421 dlvgaadlae aaldqcasgr siaelltals fvlvpmgqaa rasdtakavl dmpdlpdevr
      481 draelallqa eaglqesgsv ldraraivka ddvpgrglmt galivlamnd wdegdligal
      541 eftragvrqa fndgvhecrl hpglilasll vdvrlmdear ramvlgtggp dglgrdgwaa
      601 gpaivrsrid laegrpeeai rgaraaleaa eavgahllga carsalslaa lrsgdletat
      661 ehshgdgdag gpapppfdlt rselvraqvt eacdgpraav pglsrlldgl adhnraltcd
      721 ptaaawlvrt avaagepgpa eevvaaagrl aemnpglpsl taaaehargl lhgdpdllrn
      781 aaaehadqwa sasayedlgm llggvdgarg qtiqcldkal scyaaagaer daarirgrlr
      841 rmgerrrhwn hrerpaagwg sltgteqris glvsqgltnq riadqlsvsv htvafhlrqv
      901 frkldirsrv elarkvlehs ddppdahskk ssddteaesp psrkrprqe
//
LOCUS       WP_284466905             278 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Actinomadura madurae].
ACCESSION   WP_284466905
VERSION     WP_284466905.1
KEYWORDS    RefSeq.
SOURCE      Actinomadura madurae
  ORGANISM  Actinomadura madurae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Thermomonosporaceae; Actinomadura.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Actinomadura madurae"
                     /db_xref="taxon:1993"
     Protein         1..278
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30550
     Region          16..78
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(22,26,51)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(25,50)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(32..33,44,47,51..52)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          98..259
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mpprrqrpre spalvafgrq mrrmreakdv kqetiahltk vsgpqvsrie ngkkratrsf
       61 viavddylea ggslislwed lnkdghpvpi wfdwpkiead aidltcyqls vvaglaqsps
      121 yaatilkged eavaarlerq qillkegaps vtflvdeqvl yrpvgtpett reqlhhllsl
      181 gellnvtvqv vlsggehdgn gssfivatma dmsqvayvet airglttddp adlaaisrvl
      241 vdlrnrtlpg dmsrdlikkv aqdrwtstts pgesrrea
//
LOCUS       WP_284466993             269 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Actinomadura madurae].
ACCESSION   WP_284466993
VERSION     WP_284466993.1
KEYWORDS    RefSeq.
SOURCE      Actinomadura madurae
  ORGANISM  Actinomadura madurae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Thermomonosporaceae; Actinomadura.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Actinomadura madurae"
                     /db_xref="taxon:1993"
     Protein         1..269
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29925
     Region          16..78
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(22,26,51)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(25,50)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(32..33,44,47,51..52)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          93..262
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mpprrqrpre spalvafgrq mrrmreakdv kqetiahltk vsgpqvsrie ngkkratrsf
       61 viavddylea ggslislwed lnkdghpvpi wfdwpqvesd avmlvdwens vvpglaqtpa
      121 yalamlrgnq eavdarigrq avltrddglt sptvlfllde hvlynlvgtp qtmeeqlehl
      181 levgllpnit iqvvlgsgeh egvlgsfvva tmedrsevay ietavrgitt dnptdlsila
      241 rtlvelrsra ltqamsreli rkviqekwt
//
LOCUS       WP_284467009             151 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Actinomadura madurae].
ACCESSION   WP_284467009
VERSION     WP_284467009.1
KEYWORDS    RefSeq.
SOURCE      Actinomadura madurae
  ORGANISM  Actinomadura madurae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Thermomonosporaceae; Actinomadura.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Munoz-Lopez,M. and Garcia-Perez,J.L.
  TITLE     DNA transposons: nature and applications in genomics
  JOURNAL   Curr Genomics 11 (2), 115-128 (2010)
   PUBMED   20885819
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612959
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Actinomadura madurae"
                     /db_xref="taxon:1993"
     Protein         1..151
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16156
     Region          <43..80
                     /region_name="HTH_Tnp_4"
                     /note="Helix-turn-helix of DDE superfamily endonuclease;
                     pfam13613"
                     /db_xref="CDD:463934"
ORIGIN      
        1 mlgsvgrdel rddhrfiess cpprpnhlsg sglhatrgkh tslrkgetft elgagfgvst
       61 stawryvnet vdmlatraqp rqgagraded gllylldsts aqpdekadpi gneapatlae
      121 cpqecgmvdt ssrarqqgdw rapacclrps t
//
LOCUS       WP_284467357             478 aa            linear   ENV 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [uncultured Xanthomonas sp.].
ACCESSION   WP_284467357
VERSION     WP_284467357.1
KEYWORDS    ENV; RefSeq.
SOURCE      uncultured Xanthomonas sp.
  ORGANISM  uncultured Xanthomonas sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas; environmental
            samples.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="uncultured Xanthomonas sp."
                     /db_xref="taxon:152831"
                     /environmental_sample
     Protein         1..478
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=51699
     Region          <194..449
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mksaassekh vsngeswvsl kfrdsnrsrk mrstltlagv scttlgalwt vcylyygrpe
       61 lalafvglta vgllalcrrr hcdeaslslv ahgvfvvvlv isiidapigt vprsvhtffl
      121 plaagalfvf drsrryralv fplaclgafv afgsgeldwl apasspplgm rrlgaisnma
      181 caagllaail hiyrndvnar islerelara vgngeievly qpqvsangsm lgaealvrwr
      241 hpsgklltpd kfiplaeesq lirdvglevl rqacstlrrw sheqdlralv vavnvspvql
      301 ldpnfvasvk qvitsegvap aslefeltes alyvdtagvr akmhelkafg igwalddfgt
      361 gfsslamlrt lpvtklkidr qfvndakade ssrrllakiv eisevmgmva laegiedaqq
      421 cemlsamgcr hfqgflfgrp qpahdlerla flqagternl msgaatrapd apppssar
//
LOCUS       WP_284468073             515 aa            linear   ENV 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [uncultured
            Xanthomonas sp.].
ACCESSION   WP_284468073
VERSION     WP_284468073.1
KEYWORDS    ENV; RefSeq.
SOURCE      uncultured Xanthomonas sp.
  ORGANISM  uncultured Xanthomonas sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas; environmental
            samples.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="uncultured Xanthomonas sp."
                     /db_xref="taxon:152831"
                     /environmental_sample
     Protein         1..515
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=55597
     Region          3..388
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mkaatlrqfl sahswmglla gmalfiafya gainvfthdl eqwprpaavq apalppeqaa
       61 qaladavlar hpalaesytl mlpgegrtqp qlfafgpaae qafggmvqfq pgadgqpvql
      121 pqrsgfvafl ydlhftaglp rtfgtylfgv vcllygvalv sgvvlyapvl lkdlfalrrg
      181 rnvkrlwqda hnaigmlslp fhvifawsga vltlgvllla pfqylvfdgk lmqvlqpdfe
      241 laphvqpahv papmlpvael vararaanpg fvpeslsfhd agdanaqvel yghqeqrrln
      301 tlggvalraa dgkvlrvlsp qtmspgvaal rglqtlhfgd ygrwplqwly fllglggafl
      361 fysgnllwve arrkrrqvaq plrthvmarl ttgvclgcva gvsalfvaar llppgmerwa
      421 yyavfalgva wallrptarg ayelllacav ltalvplagl rgaagwvapw ssgtllaida
      481 calalawayw qmaraayrrg qggdphsvwa fpppr
//
LOCUS       WP_284469006             261 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Peribacillus simplex].
ACCESSION   WP_284469006
VERSION     WP_284469006.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..261
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28237
     Region          1..256
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mrktvlitgv sggigkelad rfakdghdmv lvartegkll elakeyqkky gvqatviakd
       61 vaspgvpeei vaelkekgiv vdylvnnagf glygtfletk leqetnmidv nvkaltvmtk
      121 lflpdmvkrg qggvmnvasl vgffpgpmms vyyatksyvl sftealenev sgtgvtvtal
      181 cpgltstgfv drsgmgaskl fqsgtimeag qvaeegyrgf lrgktlimpg arnrfvafip
      241 rlmprkmvtr mvrtmqdrtg h
//
LOCUS       WP_284469057             295 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: diacylglycerol/lipid kinase family protein
            [Peribacillus].
ACCESSION   WP_284469057
VERSION     WP_284469057.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus
  ORGANISM  Peribacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Peribacillus"
                     /db_xref="taxon:2675229"
     Protein         1..295
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32233
     Region          1..293
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mskvmiiinp ssgrekagki lpkaekalgd iydevsvrqt egegdatdfa keaceerfda
       61 vismggdgtv neivnglgeq qhrpifgiip lgtvndfars lgiplnpnta ieilkdmhik
      121 esdigkindr yfmnvlavga iaeatynvsv dqktrlgsfa yfiegakami kknpfpltve
      181 hdqgrwmgea hlliatmtns vggfeqlape aevndgklht fiikdlslpf ivkiipslmk
      241 geikghdeie yiqtsklnls ttdelavnid gdegfllpfq snvlhkhlrl fvpgn
//
LOCUS       WP_284469077             207 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: anti-sigma factor family protein [Peribacillus].
ACCESSION   WP_284469077
VERSION     WP_284469077.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus
  ORGANISM  Peribacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Peribacillus"
                     /db_xref="taxon:2675229"
     Protein         1..207
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23287
     Region          1..>96
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
     Region          118..>179
                     /region_name="CcmA"
                     /note="Cytoskeletal protein CcmA, bactofilin family
                     [Cytoskeleton]; COG1664"
                     /db_xref="CDD:441270"
ORIGIN      
        1 mncheeiiey mhdyldedik pehkevlreh lhncaecrdy fhemkkaval vqstshikap
       61 ddftakvmaq lpketkttga krwfkshpfm taaamfillm tgsifstynq dehfsvskqp
      121 nlvvegetvi vpagetikgn vvvqngniqi dgevegdvtv inghkymska gnvtgsinvi
      181 dqafewmwyk vkdtatslvp akeekke
//
LOCUS       WP_284469122             600 aa            linear   BCT 25-DEC-2024
DEFINITION  IucA/IucC family protein [Peribacillus simplex].
ACCESSION   WP_284469122
VERSION     WP_284469122.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..600
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=68639
     Region          4..592
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mngkqiaera tmqsflncyf retgncslee tknwpdlegs ipdsllvsnl lsqdiallvp
       61 vkywsetgrh iftfpiyyqn askqvreldy vtmvsivske llneqgrtds edelmlrvil
      121 ssqniqryve artedidalq spdftfieae qsllfghlfh ptpkskqgis ekdewiyspe
      181 lkgefqlhyf laepsiviqd ssevrsasei ikqelagdle issefrdtyc qkesrysiip
      241 ahplqakvli ekeevkrlie qgtliyvgpl gkkftatssf rtvysatsry mykfsvpvki
      301 tnslranlqk eldrgveiak lidskvgdvl keqhpsfrii kdpayltikt teqesgfdvd
      361 irenpfyenn eqasliaglc qdnaygapsr lgaiirklsa denrsteevs kdwfktylsm
      421 tlkpmlwlfe vygivleahq qnsiiqlqdg ypstfyyrdn qgyyyceskv drllkilpel
      481 seksfticsd evaeerlqyy fffnhllgli nnfgteglvs ektllqlvqe qletssresg
      541 deglnrviar llharelsck anlltrfhdm delvgsletq svyttienpf aqgvlavhek
//
LOCUS       WP_284469153             351 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Peribacillus simplex].
ACCESSION   WP_284469153
VERSION     WP_284469153.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..351
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37664
     Region          32..348
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mpkqsirtyl ttkwtfayli allfllfamt igisfgsvpv pisvliqiig keifhlpisa
       61 dpdvmltniv mnirlprvll aglvgaslai agaafqgllr npladpytlg issgasvgav
      121 ltiflnislp figlytlpal silcsvltml cvltfakkmd rsmkvetiil tgiifssfls
      181 afislmialt gdelrqiigw lmgsvsmrgw nyiviilpff iigsltlimn aselnamtfg
      241 edrakhlgvn vkrrkmwili agstltgaav avsgaigfvg lviphlvrki wgpdhkhllp
      301 lsllvgsgfl iladfvarti iapaelpigv itsligapaf alillkrrre g
//
LOCUS       WP_284469239             473 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Peribacillus simplex].
ACCESSION   WP_284469239
VERSION     WP_284469239.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..473
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=53792
     Region          203..468
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mkfiekqslf ilimcllvpl avphpitgym atvlmlvfig inkknlllil fvyfparpll
       61 melnsgltyt gdliiltlfi sllmenfkky ewhiskyhft vpfwlfclvg avagllngvg
      121 ifpilfelra llvtflllyi igelnlerkd ifrflkvili ftiflclhgi lekifsrtil
      181 lphewemwnl sptnrmriyg apanpnvfal flsiqlflsf flfqslkkyk pfvflasill
      241 sgtllltysr gtmiafgfaa lvfiiwtrnk sflkyavgaf glgllliyyp vlfasskvev
      301 sasvpmenma igstptsehe halsnrfsem fsnttlhqst ewgrlyvlik gleifkdhpi
      361 igtglatfgd satlsfsspi yqdykigerm ytdnqyiqil vqtgvlgfla vlafilftyr
      421 kiiksrngtl tvfticlmla allaglfyni ledktftlff ysclgfclqk dii
//
LOCUS       WP_284469265             368 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF4097 family beta strand repeat-containing protein [Peribacillus
            simplex].
ACCESSION   WP_284469265
VERSION     WP_284469265.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..368
                     /product="DUF4097 family beta strand repeat-containing
                     protein"
                     /calculated_mol_wt=41278
     Region          <193..368
                     /region_name="YvlB"
                     /note="Uncharacterized conserved protein YvlB, contains
                     DUF4097 and DUF4098 domains [Function unknown]; COG3595"
                     /db_xref="CDD:442814"
ORIGIN      
        1 mfmqeerkki lemiqdgkls aeeamgllee lekasqesea keqklqnels tvvvdkqseg
       61 stqdtfkkni qsskekiidf vetafkkike tdldfnfgks vevshifqhd ydflnevdvd
      121 iangkiriat wnqndvrvec qakvyrvedm eearknflee vdfsiedgkm kfkvreksik
      181 vdtimyiprk eyddihvrmf ngaitteslk senlkaktan gaihimqgtg dsceletgng
      241 mitisdtnfn yleaetlnga inadgyfkkv dvqtfngeiv ctnsgmdcds ihaksvtgkv
      301 qlilpqgkai egelksnlgs fnvslegmti ieeksdvvqk vlkfktvkee apvlhvfaet
      361 ktaaitvs
//
LOCUS       WP_284469293             451 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Peribacillus simplex].
ACCESSION   WP_284469293
VERSION     WP_284469293.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..451
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50736
     Region          144..445
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mkirtkiqsy sslflsvmli llsiivliaf llislererd lledkaslie eniltkdlis
       61 gdpdlmepyt pddgmvrifd tdgrliksft deedleglav ksinekgfdf skadgdyvlt
      121 yryaypeegk klgmievtqp qdtllenlst lalvlggasl fvillsifag kwlanlilkp
      181 isimsgtmmd ieksgefkri plsdqskdel qvmgvsfnrm ierlernynr qqqflsdash
      241 elktpitvie syssllkrwg mkdeaileea veaihheair mkqltehllq sasqsepskd
      301 iegkvelisf ceqiaqtfrr tanreikiqs efkeiyamai sskleqvlvi lldnamkyse
      361 sdiqilikqr aneifigvkd egagispehl phvferfyrv dssrarktgg nglglsiart
      421 lvesfggkle iqsevgegtl vtitlshqil i
//
LOCUS       WP_284469268             172 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase [Peribacillus].
ACCESSION   WP_284469268
VERSION     WP_284469268.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus
  ORGANISM  Peribacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Peribacillus"
                     /db_xref="taxon:2675229"
     Protein         1..172
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=19317
     Region          55..162
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mrrtfrypve ganslwhvyk tvpfwkvvkn fvviqlaryt pflsmknwly rtflhmkvgk
       61 htsfalmvmp dvmfpekisv gintvigynt tilaheylih eyrlgdvvig devliganst
      121 ilpglsigng aivsagtlvh kdvpegafvg gnpmkiiytk eemlerdqqt sl
//
LOCUS       WP_284469383             256 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Peribacillus].
ACCESSION   WP_284469383
VERSION     WP_284469383.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus
  ORGANISM  Peribacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Peribacillus"
                     /db_xref="taxon:2675229"
     Protein         1..256
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27520
     Region          19..254
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mediqistll llmffgflaa fidsvvgggg lisipallfs glsptaaiat nklassmgal
       61 tstiafirsg kvdfrfvakl fpfifigsll gawvvnfvsp ellkplilvl llaiaiytfl
      121 kkdwgqesty krltwqkaal fafaifaigf ydgflgagtg sfilfaflmi gfdflhsagn
      181 akflnfgsnl aalimfifld tvnfsygipm gismiagala gskfaikkgv ayvrvlfiiv
      241 tvilimknii dylmgs
//
LOCUS       WP_284469445            1054 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Peribacillus simplex].
ACCESSION   WP_284469445
VERSION     WP_284469445.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17689052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..1054
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=112648
     Region          402..668
                     /region_name="Peptidases_S8_Thermitase_like"
                     /note="Peptidase S8 family domain in Thermitase-like
                     proteins; cd07484"
                     /db_xref="CDD:173810"
     Site            order(448,483,546..547,633,636)
                     /site_type="active"
                     /db_xref="CDD:173810"
     Site            order(448,483,636)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173810"
     Region          727..789
                     /region_name="Big_6"
                     /note="Bacterial Ig domain; pfam17936"
                     /db_xref="CDD:465576"
     Region          <804..>1052
                     /region_name="Ig_like_BLP2"
                     /note="Ig-like repeat protein Blp2; NF040520"
                     /db_xref="CDD:468522"
ORIGIN      
        1 mkfknvsrft afvlifalii slmvplnsqa atatpienvk tikngdtldg kfdkpdvkwy
       61 qitptkeeiq kfshiefevn sdkilnisvy qdkekaekde snylvsskpd ekavidfpya
      121 wegtyyvkve yfgetddegn pipdaineae ysinahsvtl ppssgdeeel eacpvelsvn
      181 dkktgesmlk tlrvfrdevl tkssegrsls slyykaspfl alhlagnkka reavynhlvv
      241 ikpliedlne ngasstavis nkqqeaikal fnkaasvapa glkkdmnsia kkinldklag
      301 erivdiaska giklpaskni knkyivklkp gkslsavqsk vsgkgygtls apkrqevlyd
      361 dmyvvelknq anmstaalss ieklpeveyi epvktykals adiqspyqws lnnaggeegi
      421 kgadidnekl qslikkrnlk dtlvavidtg vdnsladlkd tvrmdlgknf idknekaidd
      481 hghgthvsgi iaakadngys mqginpvaki mpvkvldssg agdnekvalg ikyavdhgak
      541 vinlslggey srtieyalkh aaaknvmvvv asgndgtegl sypasskyai svgatnaldl
      601 vsdysnygak ldmvapgtgi pslvlngnvt ymdgtsmatp hvaaatalll sgnpglkvne
      661 vreilhetse yvafeeednv dpyedyeped geiiipeeel pvgkdlvsgy grlnaysals
      721 tvdlqakvnl vmdtqtkltg sakkgsviev kngkkslgkg taaangtftv tipvqkaeqq
      781 ltvnisdssk lavssikvfv nkgvtpnkpt vkalsdkdty vtgqsqadmk itiknnakkv
      841 igsgntdskg nfkvkiskqk agtklsvtat dlakreskaa tvtvidktap gapkvnevsd
      901 katlvtgkae igsivtvkyn nknigtatad kkgnfsikis kkkagsllya sakdkagntg
      961 kaakvtvkdk tapgapkvne vndkatkvtg kaeigstvtv kyndknigta ksdkngkfsv
     1021 kiskkkagsa lyvsakdkag ntgkvakvtv kksk
//
LOCUS       WP_284469639             279 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Peribacillus simplex].
ACCESSION   WP_284469639
VERSION     WP_284469639.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 279)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..279
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30217
     Region          1..243
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mnikgkwalv tgassgigeq farqlakegg hlvlvarskn klenlaselr kkhgvkvevi
       61 ptdlgkegap gelyrqcqll nleiemlvnn agfathglfe qmsgvrqhee vmlnvaavvd
      121 mthlflpdml crnsgavinv astagfqplp ymavygatka fvlsftqalw wenrnsgvqf
      181 ftlcpgatdt gffnvvgaee aavgkkdtpe rvvevalral kdgklyvvpg tqnyigtqig
      241 rfmtrkqglr lvggmlrprd gsannkkpag psdlaewmi
//
LOCUS       WP_284469696             347 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Peribacillus simplex].
ACCESSION   WP_284469696
VERSION     WP_284469696.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..347
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38735
     Region          3..347
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mkydviiiga gqaglsmgyf lhktnlsfli lekgkgigev wknrydslkl ftprsysslp
       61 glaldgnqsi yptkneiaey lssyakkfnl pvqlktevqg lfkasggfri ltdkgqfvak
      121 svvvstgpfq npvvpkfsnt lsenvlqihs sqyknsehls egpvlvvggg nsgaqiavel
      181 skeretylsi shkikflpqd vmnksifwwf dklgiykass ntkigqyikk qndpifgfel
      241 ksliksgkvi lkprtisvnn dnitfednsk vqvnnviwst gfisdyswid iaeifddkgk
      301 llhqrgitpv eglyflglpw qysrgsaliq gvgkdaeyly kyilelk
//
LOCUS       WP_284469752             196 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-class carbonic anhydrase [Peribacillus simplex].
ACCESSION   WP_284469752
VERSION     WP_284469752.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130171
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..196
                     /product="beta-class carbonic anhydrase"
                     /GO_function="GO:0004089 - carbonate dehydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21529
     Region          29..179
                     /region_name="beta_CA_cladeD"
                     /note="Carbonic anhydrases (CA) are zinc-containing
                     enzymes that catalyze the reversible hydration of carbon
                     dioxide in a two-step mechanism in which the nucleophilic
                     attack of a zinc-bound hydroxide ion on carbon dioxide is
                     followed by the regeneration of an...; cd03379"
                     /db_xref="CDD:239474"
     Site            order(29,31,38,40..42,56,59,81,86,96,99,171)
                     /site_type="active"
                     /note="active site clefts [active]"
                     /db_xref="CDD:239474"
     Site            order(38,40,96,99)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:239474"
     Site            order(39..42,50..51,56..58,60,62,76..77,80..81,171,
                     173..174,176,178)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239474"
ORIGIN      
        1 msiisrildy nkkfvdqnky eefqttkypn kkiviitcmd trllellpka mglkngdaki
       61 iknagaivsh pfgsimrsil vaiyelkvee vcvighhgcg mvglqsssll daakqkkvsq
      121 eqidvltnsg idlskwlsgf qcveesvtns vrliknhpll pdsiavhgmv ihpetgkleg
      181 iidgyskvas kdeihi
//
LOCUS       WP_284469820             120 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: group I truncated hemoglobin [Peribacillus].
ACCESSION   WP_284469820
VERSION     WP_284469820.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus
  ORGANISM  Peribacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Keppner,A., Maric,D., Correia,M., Koay,T.W., Orlando,I.M.C.,
            Vinogradov,S.N. and Hoogewijs,D.
  TITLE     Lessons from the post-genomic era: Globin diversity beyond oxygen
            binding and transport
  JOURNAL   Redox Biol 37, 101687 (2020)
   PUBMED   32863222
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Bustamante,J.P., Radusky,L., Boechi,L., Estrin,D.A., Ten Have,A.
            and Marti,M.A.
  TITLE     Evolutionary and Functional Relationships in the Truncated
            Hemoglobin Family
  JOURNAL   PLoS Comput Biol 12 (1), e1004701 (2016)
   PUBMED   26788940
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Wajcman,H., Kiger,L. and Marden,M.C.
  TITLE     Structure and function evolution in the superfamily of globins
  JOURNAL   C R Biol 332 (2-3), 273-282 (2009)
   PUBMED   19281958
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Vinogradov,S.N., Hoogewijs,D., Bailly,X., Arredondo-Peter,R.,
            Guertin,M., Gough,J., Dewilde,S., Moens,L. and Vanfleteren,J.R.
  TITLE     Three globin lineages belonging to two structural classes in
            genomes from the three kingdoms of life
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11385-11389 (2005)
   PUBMED   16061809
REFERENCE   5  (residues 1 to 120)
  AUTHORS   Wittenberg,J.B., Bolognesi,M., Wittenberg,B.A. and Guertin,M.
  TITLE     Truncated hemoglobins: a new family of hemoglobins widely
            distributed in bacteria, unicellular eukaryotes, and plants
  JOURNAL   J Biol Chem 277 (2), 871-874 (2002)
   PUBMED   11696555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Peribacillus"
                     /db_xref="taxon:2675229"
     Protein         1..120
                     /product="group I truncated hemoglobin"
                     /GO_function="GO:0005344 - oxygen carrier activity
                     [Evidence IEA]"
                     /GO_function="GO:0019825 - oxygen binding [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13382
     Region          7..118
                     /region_name="TrHb1_N"
                     /note="truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 1 (N); cd00454"
                     /db_xref="CDD:381253"
     Site            order(9,14..15,18..19,22,53..54,57,86,89,93,96,107,110)
                     /site_type="other"
                     /note="apolar tunnel"
                     /db_xref="CDD:381253"
     Site            order(23,33,36..37,40,44..45,48..49,51..53,55,63,65..68,
                     71..72,75,77,81..82,85,110,113,117)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381253"
     Site            order(26,29..30,88,91,95..97)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381253"
ORIGIN      
        1 mdqtlyekig geeaiakvvd yfynelvlkd dtvnhffekt dmekqrshqt kfisfalggp
       61 kqysgqsmak ahqgmnlqpa hfnaivkhln dalahfgvne adidtaltkv aslrndilnk
//
LOCUS       WP_284469876             476 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Peribacillus
            simplex].
ACCESSION   WP_284469876
VERSION     WP_284469876.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..476
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=54128
     Region          56..437
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 miaqtmikgf llvlllyfly vvvtavvlfy flkekeedrp ikhisaylge kdstvdrvll
       61 ledgyesgla rmrmiqeaqh sidiayyafg kgkscelilg alfeaadrgv kvrilldgis
      121 hglrgqlsgv ryalashdni elryyetfkp fkpwtwhnrl hdkiittdgk lgiiggrnia
      181 dkylaknapk nyvydrdvli fnaeqekdsv ivemkayihe lwthpytskv fadlskrqka
      241 qgkrvrdtll nqyskamqnn adfvnpaidw sksttptkkv sfiynpierf nkypfvwrsl
      301 vdiaananks vfiqspyivp tgpmkeyvpk nmnskadwti ltnsvtstpn viafsgylal
      361 rdsivetgak lyeysklysl hgksavydqr lsavgsfnld srsaflntes mviidsenfa
      421 tqligaiesk isgstlvadn kryieppedq kkeksffkat flnalskitv ywkrfi
//
LOCUS       WP_284470055             252 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Peribacillus simplex].
ACCESSION   WP_284470055
VERSION     WP_284470055.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..252
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27610
     Region          4..250
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mkyiesiknp qvkqwkkllt kkerdktgky lvegfhlvee alkeeivlev ivneetempg
       61 hfklegtevi yvksdimkai cdteapqgia avceqklthk tsinpdklll idavqdpgni
      121 gtmirtadaa gidavilgeg cadlynpkvv rstqgslfhm pvikgnlsei idelkqigtp
      181 vygtalegas pfeevekssr fallvgnegq gvskellkkt tknlyipiyg kseslnvgia
      241 agilmyhlrk si
//
LOCUS       WP_284470099             250 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Peribacillus simplex].
ACCESSION   WP_284470099
VERSION     WP_284470099.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..250
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=27392
     Region          2..249
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mmaihiylfv lglilgsffn vvglsvsagn sfanrrsacp scgrtltffe lipvisymmq
       61 ygkclgckar isplypsvem ltgvlfasap iflgwsdelw vgwtlislfm iifvsdvaym
      121 lipdkillff maiftvlrvs fplspwwdsi vgaaigfsll lliavvskgg mgggdiklfa
      181 vigfvlgmkm vllsflfacf ygaflgiigl ltgvlkkktl ipfgpyivlg tltayfwgds
      241 llhwyvtflr
//
LOCUS       WP_284470221             722 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Peribacillus
            simplex].
ACCESSION   WP_284470221
VERSION     WP_284470221.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 722)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 722)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..722
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=81421
     Region          1..687
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mnkkkkkkth vpfrlnilff lvfvlfsvli lrlgvvqivy gddyrreiek teevtvnnsv
       61 prgkmydrnl klmvdnqpld aitytrkqgt kqtemvetae klaklidkdt nkvterdkkd
      121 fwilknpkla akkitdkerk kveegelees dlyklqlkri teeeaklskk dmetlaiyre
      181 fasgyaltpq ivknkkvtke efarvsenld slpgvdistd wdrfytynkt lksvlgkvss
      241 seeglpsesl dyylardysr ndrvgksyie qqyedilqgq kakvrnvtdk sgnivdsevi
      301 tegqrgkdli ltidmdlqla tekiiekqli akkklgntkf ldrafvvmmd pntgevltma
      361 gkkyekdpkt gkssiedfal gnittsytmg ssvkgatvlt gyqqgaiqpg tyfydtklki
      421 kgtkakgsys nfgnindlta lkvssnvymf rtainiagak yvpneplnin ssafstmrns
      481 faqfglgtrt gidlpnemsg fkgsetspgk lldlaigqyd tytpmqlvqy vsaianggnr
      541 mkphmvkeir epvdnneelg pvdeeisptv mnrldmkedw ikrvqsgfek vtmeqggtay
      601 tyfghkpytv aaktgtaqaf ydgpnrtdys epqdtmnitl vgyapaknpe vafavvvpwa
      661 yqghtghsms keigeeimdt yfklkkerak kentetstdl kvengkdvqk dqaevrksqe
      721 ne
//
LOCUS       WP_284470252             685 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sigma-54 interaction domain-containing protein
            [Peribacillus].
ACCESSION   WP_284470252
VERSION     WP_284470252.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus
  ORGANISM  Peribacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 685)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Peribacillus"
                     /db_xref="taxon:2675229"
     Protein         1..685
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=76325
     Region          <106..>228
                     /region_name="PRK11360"
                     /note="two-component system sensor histidine kinase AtoS"
                     /db_xref="CDD:236901"
     Region          226..685
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mqkvmivggg vggttvlkll sesevfsivc madtnesaeg mlaakerrip tvtnwskgld
       61 wdldiifdtt gdpsvykkik rdmddqtili pgsvalimtk lfeeknrlin klenasakmd
      121 lilnttsegm vvidhegfii mfndsaeras dtkredvigr hikdlfpstg llrvmemnkk
      181 evnqeitltn gmelittrip lvnadkeiig afsvfrnkte avqlaeqitd lkeiqtmlqa
      241 iiqssdeais vvddqgrgll inpaytritg ltknqvigkp asidiyegds mhmkvlqtkk
      301 pvrgvnmrvg pkhkevivnv apiivdgclk gsvgvihdvs eiqaltheln rarqiirtlq
      361 akysfddiig aseemklpie qaklsartpa tvllrgesgt gkelfahaih nasdrkfnkf
      421 vrvncaaise slleselfgy degaftgasr ggkvgffeea nqgsifldei gelpaniqak
      481 llrvlqerei irvggtkpip invrviaatn inleqaissg sfredlyfrl nrmpifiapl
      541 rkrkedlkel aehlihkinq eygrsiegit adaihkmqiy nwpgnvrele nilgraiifm
      601 klnetiidiq hipdfieevp lkqeklmrps sgyvsgkpls eiidqyeaei iqqaiythng
      661 nktltakalg isvrnlyykm ekfel
//
LOCUS       WP_284470456             308 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: CobW family GTP-binding protein [Peribacillus].
ACCESSION   WP_284470456
VERSION     WP_284470456.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus
  ORGANISM  Peribacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Peribacillus"
                     /db_xref="taxon:2675229"
     Protein         1..308
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34657
     Region          1..307
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mkttevyilg gflgsgkttl lrnilkqese anrkvavlln elgsvsvdsg ligdevplke
       61 lfdgciccti qdklevqlhe lltennldav yiettgaahp vevldgimsp lfakrldykg
      121 iitvvdllrw rdreelspql rqllaeqihh adfillnkvd lvsemeaaql iysiqalntd
      181 avcllteyaa islislqqmq rkrqnghqkl dvhdhlhlta vvhtfegava qtdfedwlrg
      241 lpetvyrmkg yisfthsqlp hlfqysygmp mymnemmkmp lniviigekl dreiiigqlk
      301 aleakaaq
//
LOCUS       WP_284470505             483 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Peribacillus simplex].
ACCESSION   WP_284470505
VERSION     WP_284470505.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 483)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 483)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..483
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55059
     Region          165..395
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 mfyltpfntr ryrpgfhlvs dnwndygfyt lfnlfylden lneteighvk igykgqeegy
       61 iqlqnsfnsl pndyfslgqs vkfysklrrl gddvriecli glndlaffen iydevieeev
      121 vkssllrqvn kkiintqfrr iahggailte ydfkfdtqsg dkistfnfev ipeslpptni
      181 htiigtngsg ktttlkgiid gylgnslnee fsnaifisfs ifdknghyes nnsgkeyyyv
      241 gvkthdsktk sqedlklefh ntiksilskk ryhyllqmlv ilksdynlek fglinilkpf
      301 fntsqdneav ekcssllseg fdilssghqi illsitkivd livektlili depethlhpp
      361 llsafvrais eitiaenava ilathspvvl qevpkscvsi irkhgaqmni trprfetfge
      421 nigvlteevf gleipktgfh mllrkevekn pnydevlnlf nnelsieaks virthlnein
      481 gek
//
LOCUS       WP_284470516             281 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Peribacillus simplex].
ACCESSION   WP_284470516
VERSION     WP_284470516.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..281
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30632
     Region          1..243
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtiqgkwali tgassgigeq farqlakqgs hlvlvarses kleslaselr kmhgikaevi
       61 pmdlskegap selyqkcrll kvdiemlsnn agfatyglfe qvsgerqhee vmlnvaalvd
      121 mphlflpdml rrssgavinv astagfqplp ymavygatka fvlsftqalw fenrnrgvkf
      181 falcpgstdt sffnvvgaee asvgkkdtpe rvvevalsal kdgkvyvvpg mqnylgaqls
      241 rfitrkqglr lvgsmlrpre gynsnnknpg nqsdlagrti r
//
LOCUS       WP_284470566             274 aa            linear   BCT 25-DEC-2024
DEFINITION  dTDP-4-dehydrorhamnose reductase family protein [Peribacillus
            simplex].
ACCESSION   WP_284470566
VERSION     WP_284470566.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 274)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..274
                     /product="dTDP-4-dehydrorhamnose reductase family protein"
                     /calculated_mol_wt=31160
     Region          2..266
                     /region_name="dTDP_HR_like_SDR_e"
                     /note="dTDP-6-deoxy-L-lyxo-4-hexulose reductase and
                     related proteins, extended (e) SDRs; cd05254"
                     /db_xref="CDD:187564"
     Site            order(7,9..12,32..33,43..46,66..68,70,84,106..108,131,135,
                     150..153)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187564"
     Site            order(85,108,131,135)
                     /site_type="active"
                     /db_xref="CDD:187564"
     Site            order(108,131,152,168,177,183)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187564"
ORIGIN      
        1 mkvlilggkg maghvitayf qqnpqykvfy tsrdpedkds iylditiptk leeiiesikp
       61 diivncigil ndhasnnpkl afqvnsllph elvklternn gklihistdc vfsgtkgnyt
      121 egdipdgtsf yaqskqlgei isdkhltirt siigpelked giglfqwfmk qrnqiigyek
      181 vlwngvttle lakaiealie nnvtglyhlg senkvskynl lklikrtfnk tdieilpdsh
      241 ivldrtiknt rndfyyqipt yehmlkelks wmek
//
LOCUS       WP_284470581             238 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Peribacillus simplex].
ACCESSION   WP_284470581
VERSION     WP_284470581.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..238
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27565
     Region          1..200
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mekvsivvpf yncpyidkal eslvnqtykn ieiivvndgs tlysekidpf ldkiiyikke
       61 nggtasalnt gienatgdyl cwlssddify pektevqldl mkrenahfsy tsyycmdddg
      121 eiispiigiy psnqlelfka mirgniingc svmihrkvfe ligvfdetlq ythdydlwlr
      181 ivqnfkfhfv pqplllyrih temgskkheg niklenrlvv nrhhakmkql lvnelrkq
//
LOCUS       WP_284470649             439 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Peribacillus simplex].
ACCESSION   WP_284470649
VERSION     WP_284470649.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..439
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=47606
     Region          1..432
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mkiavlgtgy vglstgvcls eighsvicid tdeqkikslr qgvspiyepg lenllaqnaa
       61 agrllfttsh realngaeii iiavgtpqme dggadlsyiv qaakdiaanl vqssvvviks
      121 tvpvgtndfi kkimeelcne kvtfnmvsnp eflrqgsavm dtmkadriii gsdndeaakk
      181 vqemyrplnv pfiltsirsa emikyasnaf latkisfine vanlcgavga dvkdvakgmg
      241 kdkrigeafl qpgigyggsc fpkdvkallh taklngvhfs llketvaind fqqeilvtka
      301 inrlgdlkgk kvamlglafk petddmreap sikiarsltk lgaevvaydp vaidnakkil
      361 gdtirfassv reatldadav fivtewnefr qldletlmnt mrqpivfdgr ncleedrira
      421 ckkieyypig rpaivigmt
//
LOCUS       WP_284470667             389 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Peribacillus simplex].
ACCESSION   WP_284470667
VERSION     WP_284470667.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..389
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42133
     Region          53..387
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkvrsqitfa slallltgss llytsptsiv kaeltqness slqtstqqdh ysvkqamrdt
       61 lqlgfpgila ktseggkkwg yatgvanlst kkpmetdyrf rigsvtktft atvvlqlage
      121 nrlnlddsie kwlpgviqgn gyngnqitir qilnhtsgia eysrskdadf mdtkksytae
      181 eivklgislp pdfvpgkgws ysntgyvllg iliekvtgns yaeeienrii eplelldtfl
      241 pgnssvipgt khargysqpd etskikdvty ynpsagssag dmisdaddln kffsyllggk
      301 llkeeqlkqm lttvpvgrkg iegyglgife fklpngvsiw ghtggilgfs tiaggtlggn
      361 htlvvslnsl grdnspnpfk nilfaefnk
//
LOCUS       WP_284470749             458 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Peribacillus
            simplex].
ACCESSION   WP_284470749
VERSION     WP_284470749.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..458
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=52056
     Region          1..452
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mkmhvlvidd epaictalsf aledsyqvvt ttdpdeglrk idnqpfdivl ldlrignksg
       61 ldvlqkikqi apnvtvimmt ayssietsid aikkgayyyi ekpinieels lllmraaefk
      121 qmsnqletlh eelemqkgfg nflgnskamq rifsmiervk didssvlitg esgtgkelva
      181 rnihtlgrrk nkpmqivnca aipemllese lfgyekgafs gatqrkegkf vaanegilfl
      241 deisemplpl qvkllrvlqe revtplgsnt kisldvriis aanknleqmv iegkfredly
      301 frlnvipism pplrdrkedl pilmdyfikk hstdmnredk afsatarril ldyhypgnvr
      361 elgniieyav alsnskrmdd tdlpqyvqeq kfilqpngid ddfnsfripi gismkeieek
      421 vitatlqyck nhrqktaqil kiserslrdk ikliskee
//
LOCUS       WP_284470823             345 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Peribacillus simplex].
ACCESSION   WP_284470823
VERSION     WP_284470823.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..345
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=38563
     Region          1..341
                     /region_name="Tdh"
                     /note="Threonine dehydrogenase or related Zn-dependent
                     dehydrogenase [Amino acid transport and metabolism,
                     General function prediction only]; COG1063"
                     /db_xref="CDD:440683"
ORIGIN      
        1 mkalvwtenk qleykeveep qiqksndvkv kiygtgicgt dlnvlkgkmy aspnmvmghe
       61 svgivaevge svknvrvgdr vvidptqfcg kcyycrkglt cyceefdewq lgigshgtfg
      121 eyyvgedrfi yklpdsmdwe ratlieplsc vlsvvekani kpdesvlvlg sgpiglmvql
      181 iarklsritv ateighfrtk aaqkitkyvy hpqklnleei yrinqgrkfd vvidaignql
      241 ewaypliekg grlipmgfdd tyeftvkpfe llskgitivg tgeahhmmek alscaidlpe
      301 lsnlitdkvl ledfntafgd ligidsvtne rkdiksikti lvses
//
LOCUS       WP_284470920             261 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase
            [Peribacillus].
ACCESSION   WP_284470920
VERSION     WP_284470920.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus
  ORGANISM  Peribacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Peribacillus"
                     /db_xref="taxon:2675229"
     Protein         1..261
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28215
     Region          1..256
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mrktvlitgv sggigqelad rfakdghdiv lvarsegkll elakeyrnky giqttviakd
       61 vaspgvpeei vaelkekgvv vdylvnnagf glygtfletk ldqetnmidv nikaltvmtk
      121 lflpdmvkrg qggimnvasl vgffpgpmms vyyatkayvl sftealenev sgtgvtvtal
      181 cpgltstgfv drsgmgaskl fqsgaimeag qvaeegyrgf frgktlimpg arnrfvafip
      241 rlmprkmvtr mvrsmqdrtg d
//
LOCUS       WP_284470960             284 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Peribacillus simplex].
ACCESSION   WP_284470960
VERSION     WP_284470960.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..284
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31556
     Region          2..284
                     /region_name="COG4132"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443307"
ORIGIN      
        1 mrkikkqkiy llalllpfim fvigfeigpl vamikdsfya ddgiqvtidq yitifkskfy
       61 lqgiqnsivi slfsavtsvf iaviaaysft kfsqkiqnrl lmianmtsnf egiplsfsfi
      121 illgnnglft llfskiggdv fadfnlyswt glilvyiyfq iplaimliyp syqgikkqwk
      181 eassllggst lsfwlhigip vllpsivgtf silfansmga yatayslvgs nynllslqia
      241 slvasdvalk pqlgsamgvl laatmigamw fnermmrrir rdlr
//
LOCUS       WP_284470975             260 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase
            [Peribacillus].
ACCESSION   WP_284470975
VERSION     WP_284470975.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus
  ORGANISM  Peribacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Peribacillus"
                     /db_xref="taxon:2675229"
     Protein         1..260
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28567
     Region          1..253
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtaetvlitg atkgigyeft kvfaehyynl vlvardsall eqqaeslkke yglqvntfag
       61 dlsshttves lhrylkcegi didilinnag agglglmtel diqkemeylq lnmisltylt
      121 kliaddmvkr kqgkilnvas taafqptprm smygasksyv lffteaiaee lkgtgvqasv
      181 lcppstktpl tqglastrtk ifiknliepq avakcgfegl mknktviipg fknklmaksv
      241 gllprkwvti ytrklieqkv
//
LOCUS       WP_284471109             332 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Peribacillus simplex].
ACCESSION   WP_284471109
VERSION     WP_284471109.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 332)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..332
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=38727
     Region          <116..327
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mklknkyrll lfiavisvpf llllisilms viyenafktk nydipfhesf ayttmlivfi
       61 lsllflaflf snsinsllkk inilnktirn lasdekipnk levngndeig kliksvnlli
      121 erttyrelel kqqqelkkel lnklrhdint pltavrlqlf ylegqftdqa plieslyqqi
      181 dyiseltney niqstdtldn syilneevnm hdlletmvkk wgylynmhgi eliyhplnre
      241 lkwisndlwl qrlfdnifqn alkhskadkl eitieknvvi ikdngigfvi dsksrglglk
      301 iiediarilq ikynlqsner gtlfcftvek ti
//
LOCUS       WP_284471120             597 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Peribacillus simplex].
ACCESSION   WP_284471120
VERSION     WP_284471120.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..597
                     /product="PhoX family protein"
                     /calculated_mol_wt=65054
     Region          <175..578
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mkkgkivapl lsltvllpst tnvfaqpdkq vsvhkvefig mnapvtqdqr skmyseasvk
       61 vtytngsqqm lpleykslfq pgdefkngia gaaydakgnm ikspegtpyi stapdsntvi
      121 svkgklymvn hyeampsnet gnmpksmmln tlkqnkktge ltvtdtkpid fsadggiwtp
      181 cagslspwnt hlgseeyepd arsheanpen svvtqfarny yndktvignp ylyghtpevt
      241 vhpggkstav khfsmgrlss envkvapdnr tvyfgddgay tmafmyiadk ekdlsagtly
      301 aakwiqtgqe nggsadlkwl klghgtdsei kklahklkfs dmfeatndve fakangfkrv
      361 kaggrdewlk lkpgmekaaa flesrrygal lgatsefnkm etvelnkadn kiymtmstia
      421 ggmeanppdq vddiqvpkis sggiyelsla egqkdqngnt iksryvanem aglitgkdls
      481 skdaagntad sekisnpdni vfsermrtlf iaedggkhhn nygwaynvdt kklsriisap
      541 dggevtgiqa ldnlngftyl mvgsqnpgna gylsglpsld dkdserdddd knddhnd
//
LOCUS       WP_284471440             240 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Peribacillus].
ACCESSION   WP_284471440
VERSION     WP_284471440.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus
  ORGANISM  Peribacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Peribacillus"
                     /db_xref="taxon:2675229"
     Protein         1..240
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27565
     Region          <1..240
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mslrkgtike ymfksealae elellvylpa nfsplykysl viaqdgrdyf qmgrigrvad
       61 ellgneeien iivvgipykd rfdrrskyhp dgeqyiayir flahelvpfl ddefptyqmg
      121 hgraligdsl ggtvsllaal kyphtfgkci mqsplaneav mdavrnfedp hllelyhvig
      181 tgetdvpttd gnranfiepn relhkllkqk gfpcfyeefe gnhtwkywqa dlkrallemf
//
LOCUS       WP_284471497             171 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: antibiotic biosynthesis monooxygenase family protein
            [Peribacillus].
ACCESSION   WP_284471497
VERSION     WP_284471497.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus
  ORGANISM  Peribacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Peribacillus"
                     /db_xref="taxon:2675229"
     Protein         1..171
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=19478
     Region          66..166
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mnvfittgty dflkikkdkh pnekillmqn sgttvllhet sgktifsspr kyevvdgkgh
       61 lqdhgyvvmn nipvseegrp vfehrfkkra gfienepgfv alrilrpins etyviltiwe
      121 kqadfmswqk sssyqeahns dtkatitnss qkmfsgeayv tqytlvkdpq e
//
LOCUS       WP_284471538             294 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: PucR family transcriptional regulator [Peribacillus].
ACCESSION   WP_284471538
VERSION     WP_284471538.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus
  ORGANISM  Peribacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Peribacillus"
                     /db_xref="taxon:2675229"
     Protein         1..294
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33924
     Region          <95..292
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mlenlkqkfp naltnkkdtn dftdyvwfed srsilgiprs eitaeeirll ellfvpsinq
       61 nnlntfpgts wktflsepna plpltswenv rfihfkltha dyshsdfeda flafvpsdaa
      121 ivwenetagi lietvkdesl snkeliaiss tlesdfyvkt rmftgrfhpv nqdlhhhrnq
      181 ekkcfdlaqv hlpdlkvadl adiiphslin dlsvtnskwy ineilgktkq dteliktikt
      241 yiecnsnaty aakqlyihrn slqyridkft ertgldirnf rhaltaylii lmnd
//
LOCUS       WP_284471589             321 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Peribacillus simplex].
ACCESSION   WP_284471589
VERSION     WP_284471589.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..321
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=33809
     Region          8..309
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mkyicglfsi kypiiqggmg nisnaslaaa vsnagglgti gcgnmnpeqv eaiiletkgk
       61 tnnnfslnip invspytdel inlvfkhdip vvslsagnpa pfipllqkkn ikviaivasv
      121 khaqkaqaag advlvaegfe aaginsnlel ttftlipqis khvtlpvlaa ggigngqgva
      181 aalmlgasgv qlgtrliatq eapfhpsykq klidamgddt filgrsvgqv rrvlkdpyte
      241 kvldlekqgl spmnyremts evhhingamn gdvnngfmns gqvaglidni ptvkelldgm
      301 mkdakkqmed glsslstpfm i
//
LOCUS       WP_284471655             412 aa            linear   BCT 25-DEC-2024
DEFINITION  CynX/NimT family MFS transporter [Peribacillus simplex].
ACCESSION   WP_284471655
VERSION     WP_284471655.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..412
                     /product="CynX/NimT family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44346
     Region          33..401
                     /region_name="MFS_NIMT_CynX_like"
                     /note="2-nitroimidazole and cyanate transporters and
                     similar proteins of the Major Facilitator Superfamily of
                     transporters; cd17339"
                     /db_xref="CDD:340897"
     Site            order(35..36,39..40,43,75,124..125,127..129,132,151,
                     154..155,158,232,235..236,239..241,244,271,275,324..325,
                     329,333,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340897"
ORIGIN      
        1 msihqaanql eqtkmdikpr lglliigiil lganlraplt svgplvtsir dnlgisntls
       61 gslttlplls fallspfapr iarrfgmelt lflslillti gigirsvggv ltlfigtili
      121 glaiamgnvl lpslikhnfa rniglmtgty avsmnlcgai gsgisipiat ssglgwagal
      181 gcwgilslit vffwmpqlrr pfksgkdiqt aqkvkninlw rsglawqitf fmglqsfify
      241 tvitwmpeil eqkglnadea gwmlsimqla vipitfivpi lagrlqsqrl lvvppvtfli
      301 agifgilygs tifipvcmil igigvgtifs lsmmffslrt qstneatels gmaqsfgyll
      361 aaigpvlfgl lhdvthswti plfmlvvisa lifivgmrag kneyvttnes ls
//
LOCUS       WP_284471658             335 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Peribacillus simplex].
ACCESSION   WP_284471658
VERSION     WP_284471658.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..335
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35722
     Region          30..335
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 miqsalikkq rwilgalfal iiitiiigtc sgysnlslgr liptlfgqgt fkeefilysv
       61 rlpriiitll agmalalsga ilqgitrndl adpgiigins gagvaiaaff lffpidtgsf
      121 vymiplvafi galltacliy ilsfkkragl epvrlvligv gfsmalsglm ivlissaera
      181 kvdfiakwla gniwgtdwpf iwailpwlii lipftlykan rlnllglsep iaigvgvsie
      241 kerivllita valaaaavsv tggiafiglm aphiakslvg prnqlfipva iliggwllll
      301 adtigrnive pegipagimv aligapyfmy lllkk
//
LOCUS       WP_284471773             968 aa            linear   BCT 25-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Peribacillus simplex].
ACCESSION   WP_284471773
VERSION     WP_284471773.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 968)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 968)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 968)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 968)
  AUTHORS   Marahiel,M.A.
  TITLE     A structural model for multimodular NRPS assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 136-140 (2016)
   PUBMED   26429504
REFERENCE   5  (residues 1 to 968)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11684023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..968
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..968
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0044550 - secondary metabolite
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=111037
     Region          16..497
                     /region_name="Adenylate forming domain, Class I
                     superfamily"
                     /note="This family includes acyl- and aryl-CoA ligases, as
                     well as the adenylation domain of nonribosomal peptide
                     synthetases and firefly luciferases. The adenylate-forming
                     enzymes catalyze an ATP-dependent two-step reaction to
                     first activate a carboxylate...; cl17068"
                     /db_xref="CDD:473059"
     Site            order(157,160..165,167..168)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341228"
     Site            order(160,272..273,295..300,385,397,400,411,491)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341228"
     Site            order(160,199..200,248,250..251,254,272..273,295..300,385,
                     397,400,408..411,472)
                     /site_type="active"
                     /db_xref="CDD:341228"
     Site            order(199,250..251,254,272,408..410,466,472)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341228"
     Region          518..576
                     /region_name="PP-binding"
                     /note="Phosphopantetheine attachment site; pfam00550"
                     /db_xref="CDD:425746"
     Region          620..878
                     /region_name="Lys2b"
                     /note="Thioester reductase domain of alpha aminoadipate
                     reductase Lys2 and NRPSs [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG3320"
                     /db_xref="CDD:442549"
ORIGIN      
        1 misksmttnk lmsiteafkk magdnqskaa lydyerqity keldilsdnl akriidmgiq
       61 eetmigipsk rsielivgml aiiksgccyv pidekyplkr leymledtdm efflsfndhe
      121 gklseldiep ipfeikelsr eghtpvnrss englayviyt sgttgkpkgv mieqrsvvnl
      181 vlnseilein ennrvaqfsn pcfdaatfei wgallngatl flmtneftsf ddwkeaisig
      241 kvdvaffttg lfnamvdedp lifeglkkiv vggdkisish vkrlkqtigh fslingygpt
      301 ecttfaiche vedkdvdvip igkpltnvei rilseeqvev gdgeigeihi ggqgvmrgyl
      361 nqpqlteqal imddlnqtkw yktgdhgirl nngeilykgr kdsqvkirgf rielneiqdk
      421 ldkymkvess vvavkninde nyviayykqk denaknaekd ikdylgnelp nymiphffvr
      481 vddfplnang kvdkakllem dimqnktfla nqeygkkkev leiwrnilgn qslglddnff
      541 engghsilat klvyimketv lpeatlqill enntvnkfvg aleidssgsm eavmekdstl
      601 drslmekirk ictkpvqfek nmmitggtgf lgahllnkll relehvkiyc lvrfpsrnrl
      661 kdtlmkyglw qdefesrivv iegdfskhqf glddmtyekl sndvshvyhv gaetnffepy
      721 skskvsnvdg vveiikfass ytrkniyyas tlsvltgerk wdeedelvys pdlmigysqs
      781 kwvaeklllq areygltidi frlgrissns lngvwnekdm lykvfesfie qrilpfkeei
      841 hfelmpvdfv sefmykisrl nenqklgiyh mfndqrvsse fvtsffeknn ipysnmdlqe
      901 wlqslkektq sneihslsal sqlieestkl keseilqskt kkdmewlsmk mpeidsryve
      961 sfmkfmlk
//
LOCUS       WP_284471790             562 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Peribacillus simplex].
ACCESSION   WP_284471790
VERSION     WP_284471790.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 562)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 562)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 562)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..562
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=62731
     Region          28..555
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 miknrdtrlt iwllipvvlv lvayvlypsl rtfieslqkd gsislgnyqd ffvqesktnl
       61 ealwnsvyis ilsvlvsali giplafifnr ydfpgrsffs saailpivlp slvgvmafmf
      121 lygesglipn aikdmfgldk vpfkiggvsg ilivhaytmy vyfymtvsaa inkidpslee
      181 aaynlgankf kvfwkvtfpl ltpaivaasl lvfmismasf sapfllaggy rvlslqiyfs
      241 kingdmeiaa tqsvilsivs isfllfmrwy qnrkdyrmas kgigahrsev knpfmkwvmv
      301 gtgiigvlil llphftilll slvpdgtwtf qtyptvfnae nyrllfedpn ifkplrnsll
      361 maviatlanl vfgviasyvl vkrkfvgksf idilvmipwa lpatvigmnl ifafnepsvf
      421 sfgqilvgtf wilplayfir hiplvvrstn avleqlddsi eeaarnlgak wfytfrkvil
      481 piilpgvlsg tllafiesvg efptsvllyt isnrpisiei mnqlrmfnmg qaaaygmiqi
      541 tlivivlfis nkffgikaek al
//
LOCUS       WP_284472069             214 aa            linear   BCT 25-DEC-2024
DEFINITION  formylglycine-generating enzyme family protein [Peribacillus
            simplex].
ACCESSION   WP_284472069
VERSION     WP_284472069.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..214
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=24312
     Region          1..214
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 mvkipggeie lrddrikskw kadirpflla rypvtidlyy aisnkppnsi dgdlkpvvgi
       61 swndaisfcn qlshkaglre cysiskngen incdwevdgy rlpseaewqy ackagttgyr
      121 ygeidkiawy ngnsggkihe vgrkepnswg lhdmlgnvwe wcwdlydeqv ygayrifrgg
      181 swaeeargcg ascrrrshpt fciddlgfrl arsi
//
LOCUS       WP_284472930             792 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Hungatella effluvii].
ACCESSION   WP_284472930
VERSION     WP_284472930.1
KEYWORDS    RefSeq.
SOURCE      Hungatella effluvii
  ORGANISM  Hungatella effluvii
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Hungatella.
REFERENCE   1  (residues 1 to 792)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 792)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 792)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 792)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 792)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 792)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..792
                     /organism="Hungatella effluvii"
                     /db_xref="taxon:1096246"
     Protein         1..792
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=90046
     Region          <145..>196
                     /region_name="YnzC"
                     /note="Uncharacterized conserved protein YnzC,
                     UPF0291/DUF896 family [Function unknown]; COG4224"
                     /db_xref="CDD:443368"
     Region          550..782
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mknrhrisal lsflivvaaa vimtglypff ekeagrheqp ayedqaflrh lvfgnyvldl
       61 eqyqyangvv ispfehffpe gayelkngsl dgyaeqtaaa segagnpgde tapapeaasq
      121 ipkdealaag edtasflede dygyltdeeq symaeerqey lrnlrqncmm eyeswnryfg
      181 sirnaidfqv ldengsilmn yakdrniltd dsyvfrvvmh ydghgrmdvm qlggqdtsyl
      241 lnilqkfgev dpmeeyyweq ysskpqfkls npknitfaya mteqqlaeys larssswssy
      301 ynsgrvaqvf aglgifvala afllscfdvt raddskvlrv plgivlgvga ggigfgyslt
      361 slvavtnhgs lysgliranf lpkaadimvk lwnvfwwcip faiiywavlc mrdvfhigfk
      421 ryirertlcg lfygwcaglc rrfynflgsi nlqdnsdrti fkivgvnfii lavlcslwff
      481 gigaliiysi vlflvlrkyy rdltrkyril lratnqiaeg nldvtisedl gvfepfktei
      541 qkiqsgfkva vdeevksqkm ktdlitnmsh dlktpltaii tyvnllkddn avpeqrkayi
      601 dvleqksmrl ksliedlfei skansnnvtl nlvdvdivsl lkevslelsd kieestidfr
      661 wnlpdekivl pldsqktyri fdnlltnimk ygmpntrayi dmkrddggvv itmknvsane
      721 ltfnpkeite rfvrgdqsrn tegsglgmai aksfvelqng kmdveveadl friiirwpve
      781 qnpveeddee em
//
LOCUS       WP_284474202             143 aa            linear   BCT 25-DEC-2024
DEFINITION  response regulator transcription factor [Geitlerinema calcuttense].
ACCESSION   WP_284474202
VERSION     WP_284474202.1
KEYWORDS    RefSeq.
SOURCE      Geitlerinema calcuttense
  ORGANISM  Geitlerinema calcuttense
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Geitlerinematales; Geitlerinemataceae; Geitlerinema.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Geitlerinema calcuttense"
                     /db_xref="taxon:1471433"
     Protein         1..143
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15937
     Region          1..>129
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mskiliiede lpiranilel leaedfevle aangqegvnl akqhqpdlil cdimmpilng
       61 yevlkllqed setaiipvil ltakadnldi rrgmqlgadd yltkpctpde llqavemrla
      121 kqqalkaryv qaiaqveeql nhh
//
LOCUS       WP_284475415             489 aa            linear   BCT 25-DEC-2024
DEFINITION  polysaccharide biosynthesis/export family protein [Geitlerinema
            calcuttense].
ACCESSION   WP_284475415
VERSION     WP_284475415.1
KEYWORDS    RefSeq.
SOURCE      Geitlerinema calcuttense
  ORGANISM  Geitlerinema calcuttense
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Geitlerinematales; Geitlerinemataceae; Geitlerinema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12809731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Geitlerinema calcuttense"
                     /db_xref="taxon:1471433"
     Protein         1..489
                     /product="polysaccharide biosynthesis/export family
                     protein"
                     /GO_function="GO:0015159 - polysaccharide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0015774 - polysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52680
     Region          39..232
                     /region_name="Wza"
                     /note="Periplasmic protein Wza involved in polysaccharide
                     export, contains SLBB domain of the beta-grasp fold [Cell
                     wall/membrane/envelope biogenesis]; COG1596"
                     /db_xref="CDD:441204"
     Region          <365..451
                     /region_name="Wza"
                     /note="Periplasmic protein Wza involved in polysaccharide
                     export, contains SLBB domain of the beta-grasp fold [Cell
                     wall/membrane/envelope biogenesis]; COG1596"
                     /db_xref="CDD:441204"
ORIGIN      
        1 mnkriknigi asgvvftvlv geiafkpmar aqlpalpeaa plpatplqld ttyrlgpgdr
       61 vrvdifnvpe ysgeflilsd gslnlplggs ipvqgltlqq aqeqisarma rflrrplitl
      121 sltqirpiri aiageinrpg tytftlattg evglptvtri ieqaggitqa adlrqiqirr
      181 prldiprdas gnptqadqil tvdlwqllra gditqdlalr dgdslfipts tqvnldeaaq
      241 lsnasfadrt prsinvavvg evrrqgpytl etstannvas ltraiqvagg itptadirni
      301 qvrrptksgq aqtieidfwk llqegdirqd iplqngdtiv vatatdlapd eatelastsf
      361 spekitinvv geamrpgave vapntpllqg llaaggfnaq arrnrvelir lnpngtvsrq
      421 tiavdfnqpl ndqtnpplrn ndtivvnrsa paqiadtlnp flrvvgtvgg lvsfpgqvfq
      481 lfrllnfgf
//
LOCUS       WP_284475503             297 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase [Geitlerinema calcuttense].
ACCESSION   WP_284475503
VERSION     WP_284475503.1
KEYWORDS    RefSeq.
SOURCE      Geitlerinema calcuttense
  ORGANISM  Geitlerinema calcuttense
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Geitlerinematales; Geitlerinemataceae; Geitlerinema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Geitlerinema calcuttense"
                     /db_xref="taxon:1471433"
     Protein         1..297
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=33628
     Region          23..294
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mkiqytngan pwpircsere pvqiisgdvr eklreipent fhtcitsppy wgmrdyghen
       61 qigaedslpe yvnnlvscfr dvrrvlrndg tfwlnignty tsggrawrdk dtknkgrams
      121 yrpdtpeglk pkdligvawm vamalqldgw ylrsdivwhk pncqpesvkd rvtvsheylf
      181 mfsksenyyf dqeaiketta dgkakknkrt vwsintepck eshfavfpra lvrpcilags
      241 phnglvldpf fgsgtvgvvs ietgrkcvgv eakpeyvkia knrinaatps lfmdclq
//
LOCUS       WP_284475828             594 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Geitlerinema
            calcuttense].
ACCESSION   WP_284475828
VERSION     WP_284475828.1
KEYWORDS    RefSeq.
SOURCE      Geitlerinema calcuttense
  ORGANISM  Geitlerinema calcuttense
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Geitlerinematales; Geitlerinemataceae; Geitlerinema.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 594)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Geitlerinema calcuttense"
                     /db_xref="taxon:1471433"
     Protein         1..594
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=65748
     Region          25..589
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mapislgdri rqfslksllv tepsntrliw vwgillvgil gimgnlyklq vqqgpvlqqk
       61 areqqqfkar tyaprrpivd rngqilaidr paytlyahpi lfkerpeaia qalsqplnkp
      121 paellkqfrr resgiqlayd lseevarrig glhldglelt pyqqrlypqn nllaevvgyi
      181 nldrqgqggv easyqtfler stqeawvnra gnglilpdrl penfletdeq qlqltldsrl
      241 qrvarsalkq qletyrakrg tvmvmnanng eilslvtept fdsnvyykse lellknwavs
      301 dlyepgstfk plniaialel gairpnsvfn degqivvdgw piqnhdfstn ggrgalsitd
      361 ilkyssnvgm vhimrqipse tyytwleklg lgtksgidlp geaasqlker sqfiyspves
      421 atssfgqgfs ltplqllqmq amlanggfrv tphvvkglvd pqgqqhfspp ipppepvfsp
      481 qttqtvlgmm ekvvtdgtgq vaqiphyrig gktgtaqkah pqggyyerar itsfvgivps
      541 dpflsqntpr yvvlavidep qgedafgstv aapivksvme alitlehipp stsq
//
LOCUS       WP_284475962             745 aa            linear   BCT 25-DEC-2024
DEFINITION  GumC family protein [Geitlerinema calcuttense].
ACCESSION   WP_284475962
VERSION     WP_284475962.1
KEYWORDS    RefSeq.
SOURCE      Geitlerinema calcuttense
  ORGANISM  Geitlerinema calcuttense
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Geitlerinematales; Geitlerinemataceae; Geitlerinema.
REFERENCE   1  (residues 1 to 745)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 745)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 745)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..745
                     /organism="Geitlerinema calcuttense"
                     /db_xref="taxon:1471433"
     Protein         1..745
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=81960
     Region          8..707
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mdstdytegi dfqkywlvlk rhwlpassvf alivtlatyk aatadpvyea qgkllfkkqn
       61 ttsalvtdag akigqldtlt qfnnpldtea evissmpivk etvealnfrd dqgkfippgd
      121 flsqlnvkki egtdvlmiaf ksqypkeaad avnklmdiyi nnnilvnrre ataarefimq
      181 qlpdteetvr qaeaalrafk eensvvslqd eatsavisis nldsevikaq aqyedatars
      241 qalqsqmgln pqqalaintl sqsaaiqqvl teyqkvqdql avqrtryqsq hpiitnlerr
      301 eaalndllqe rvaqvlgnnq avdrrdlqig elqqqltadl vnaevqrlgl gsnvsalvra
      361 qgsyrdrana lprleqqqrd lqrqldaaqs ayqillrnlq evriaenqnv gnarvisyat
      421 lpvnpvapnk kllvaagvvg gsmlyvltaf llelmdpsik takelrmlfr ytllgmipat
      481 kkrfgfpgfs srreipllpt rdqpttytse ayrtlqanlk fispdreiri ivvtsavsqe
      541 gkstvaanla vataqlgrrv llidgdmrhs tqhqiwnltn vaglsdvian qakfniavre
      601 vmenldvlps gatppnplal idskrmasll eefrdnyefi iidtppfllv adalalgkmt
      661 dglllvtrpg iidtasagga reilaqsgqn vlglvvngvs agsepdgafq rvkayhkgky
      721 kdaaikkvtv psesssdpsf pdwdr
//
LOCUS       WP_284476009             251 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Geitlerinema
            calcuttense].
ACCESSION   WP_284476009
VERSION     WP_284476009.1
KEYWORDS    RefSeq.
SOURCE      Geitlerinema calcuttense
  ORGANISM  Geitlerinema calcuttense
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Geitlerinematales; Geitlerinemataceae; Geitlerinema.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Geitlerinema calcuttense"
                     /db_xref="taxon:1471433"
     Protein         1..251
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=28370
     Region          28..200
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mvaslegwlr cpvilteypd qrftlaenev qvwrvfegqq tfplerlqai lsleereraa
       61 kfrfetdrdr filargllrv llsyytgqaa adlcfrygef gkpeleppav cfnvshspgl
      121 ilyavtrdra vgidvesirt dfpdleiaqk ffapqefaml rqlppemrcl affwgwtcke
      181 ayikatgkgl slplnqftvs llptepaqll stvgdspdrw llqalnlgen yagalavegr
      241 dsqvkllelc i
//
LOCUS       WP_284476429             100 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl carrier protein [Geitlerinema calcuttense].
ACCESSION   WP_284476429
VERSION     WP_284476429.1
KEYWORDS    RefSeq.
SOURCE      Geitlerinema calcuttense
  ORGANISM  Geitlerinema calcuttense
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Geitlerinematales; Geitlerinemataceae; Geitlerinema.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Geitlerinema calcuttense"
                     /db_xref="taxon:1471433"
     Protein         1..100
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=11281
     Region          11..>66
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 medrvltssr tresiaeslv aiiedmtsdw dltstaeind ntqlisdlaf esidivqlvv
       61 aieenfhkrg lpfekvlmne gryvddlkvg elsdflyqnl
//
LOCUS       WP_284477116             407 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Geitlerinema calcuttense].
ACCESSION   WP_284477116
VERSION     WP_284477116.1
KEYWORDS    RefSeq.
SOURCE      Geitlerinema calcuttense
  ORGANISM  Geitlerinema calcuttense
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Geitlerinematales; Geitlerinemataceae; Geitlerinema.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 407)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 407)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Geitlerinema calcuttense"
                     /db_xref="taxon:1471433"
     Protein         1..407
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45477
     Region          8..406
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 mpdtnqprll sftldgwtal ggrvsvslrd rvgvlvgrng agksailegf daisssaigr
       61 lnpfrffdse sipkileiev ltpterrlgy ryeliffphs tdntdidest sdsseesqfs
      121 wnescqylde nkevlwttea gvttlrqgde pvitilgnts slrqahlpen arlklpdemr
      181 wirailrgvr llgkipirqt srrrpslirv sgrgmmasgs lglvdnlark ilrlldteel
      241 selekvcqrv glgskiteqk fvlsesskek vrgegdeyls svlidginlg llsdgtlrvl
      301 silleiissy psattiieep etqihpgmld kllneieayt fdgnlilsth spqvvawtsp
      361 dklnlvyrnq grtnirklqe eeirkvveyl deqgdlgdwl ysgilde
//
LOCUS       WP_284477120             735 aa            linear   BCT 25-DEC-2024
DEFINITION  GumC family protein [Geitlerinema calcuttense].
ACCESSION   WP_284477120
VERSION     WP_284477120.1
KEYWORDS    RefSeq.
SOURCE      Geitlerinema calcuttense
  ORGANISM  Geitlerinema calcuttense
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Geitlerinematales; Geitlerinemataceae; Geitlerinema.
REFERENCE   1  (residues 1 to 735)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 735)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 735)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Geitlerinema calcuttense"
                     /db_xref="taxon:1471433"
     Protein         1..735
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=80782
     Region          5..714
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mthledsdai dlkqyglvfk rrffpavivf caaigataai tflqkptyqa qgellfkknn
       61 vttnvtvvgk evpeihsppt npldtevaiv rsvatsegvm qaldlrdeeg qplkrkdflr
      121 rlsistlkdt dvlqisfksn dpqeavdvvn rlmqfyqend iqtnraqaaa vrrfieeqlp
      181 kseftvqeae anlrvfkenn rivaldqeas atvtllggle geitqakval nsantrvaal
      241 rsqtgidsqq aialsalsqs egvqkaiael qaienrlele rsrfldeapi iidletkqar
      301 lrgvlerrii evlgnspgai apgnlqmgql qldlmqqlvn sevdrlvvns qlnellneya
      361 ihkqranalp rlqesqrdle rqvevaqsty qtlltrlqev riaeeqnign vrviqaavfp
      421 erpiapqkki nfglggvvgi flavvaalvl dakdtriktv reareylgyt llgiipnfek
      481 idkglsygkd gervkpklpv kdaprslise syrmlyanlk flgsdrqvrv iavtsaipke
      541 gkstvsanla laiaqlgfrv llvdadmrhp sqqafwdtpk tvglsniive qvdpheaiae
      601 vmphlfvlta gslppnplal lnsrrmaali edcaqtydfv ildtpplsaa adarilsamt
      661 dgmlivvqpq lvdaasaiaa kellaqsgqn vlgmvinsvs pdnepdsyfy akeypmgvdy
      721 psptssnsrl kgmkl
//
LOCUS       WP_284475466             137 aa            linear   BCT 25-DEC-2024
DEFINITION  Crp/Fnr family transcriptional regulator [Geitlerinema
            calcuttense].
ACCESSION   WP_284475466
VERSION     WP_284475466.1
KEYWORDS    RefSeq.
SOURCE      Geitlerinema calcuttense
  ORGANISM  Geitlerinema calcuttense
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Geitlerinematales; Geitlerinemataceae; Geitlerinema.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Geitlerinema calcuttense"
                     /db_xref="taxon:1471433"
     Protein         1..137
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=15421
     Region          6..>120
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mkpfveivas lpvrqfapee flirqqspag hvfilaegtv riirddieic qihevgsffg
       61 evssltnqpt tasvqavtpv kahvienpmq fafdypvavy mmavqlaqrl ahvdtqltqi
      121 krdyqemyrr lseismv
//
LOCUS       WP_284475465             169 aa            linear   BCT 25-DEC-2024
DEFINITION  Crp/Fnr family transcriptional regulator [Geitlerinema
            calcuttense].
ACCESSION   WP_284475465
VERSION     WP_284475465.1
KEYWORDS    RefSeq.
SOURCE      Geitlerinema calcuttense
  ORGANISM  Geitlerinema calcuttense
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Geitlerinematales; Geitlerinemataceae; Geitlerinema.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Geitlerinema calcuttense"
                     /db_xref="taxon:1471433"
     Protein         1..169
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=18928
     Region          6..>119
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mtsfiemltp lpvkvfepgd aiideeyaha plyflkqgrv lisrggvsic evsepgaifg
       61 elsfllstpa tatvkaldrs elyyaenaeq flreypdtll evsrqlaqrl iaidrhfves
      121 knafdellad qesspthqpp ppttenhplv slwqktqksl vrywhgakd
//
LOCUS       WP_284478540             561 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC1 kinase family protein [Geitlerinema calcuttense].
ACCESSION   WP_284478540
VERSION     WP_284478540.1
KEYWORDS    RefSeq.
SOURCE      Geitlerinema calcuttense
  ORGANISM  Geitlerinema calcuttense
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Geitlerinematales; Geitlerinemataceae; Geitlerinema.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Geitlerinema calcuttense"
                     /db_xref="taxon:1471433"
     Protein         1..561
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0004672 - protein kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=62248
     Region          1..472
                     /region_name="AarF"
                     /note="Predicted protein kinase regulating ubiquinone
                     biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport
                     and metabolism, Signal transduction mechanisms]; COG0661"
                     /db_xref="CDD:440425"
ORIGIN      
        1 mlsltktssr qreilevvfr ngwdymrgll tggkaskpql pspevlrnil ielgpvyvkl
       61 gqllstrpdl lpgryidals tlqaqvpava wpeievlirq qlngpleeif aelnpqpvaa
      121 gsiaqthkat ltdgrkvaik vqrpgidlvi aqdialikgl aelvsisdfg sdfdlvalad
      181 efskallael dftqeasfad qlrrnlstsr wfdpkqvvvp qiywnltnkk llvmewldgv
      241 pilssslsas qylagsrtng tadaavvaeq rravttllfr affqqiyidg ffhadphpgn
      301 lfylddgrva lldcgmigrl dprtqqilte mllaivdids qrcaqltlql aessprvnla
      361 rlesdydrml rkyynlslse ikfseviyev ldvsrnnkvi lpgsmglyak alanlegvar
      421 tfdpeinlld qikplitdlf rrqllgddpl qtllrtaldv kslslqsprq lellldrmts
      481 etmhwnltlr dldplrrsld dsanrlsfsi vvgslimgaa iisakaqtaq llvpsnalfa
      541 aasflglwli vsilrsgrlr s
//
LOCUS       WP_284478697             308 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein, partial [Klebsiella pneumoniae].
ACCESSION   WP_284478697
VERSION     WP_284478697.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         <1..>308
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          1..305
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 vsvivndmse ldvdgvlian teivdaasnn fvsisadsis srsgiqklds alknllekrs
       61 adfilletsg sshplplvry lrehtqvslk aflslvdtvm lnddydggkk lipvfqehln
      121 kgtrgvesll aeqimfcnkl lltkndrlpf yvvtevarai hplnpqvaim avpwgnlqld
      181 ellsmpdydf hrvallidel qdaidavlpd etdkkydisw rvieddrpfh pqrlwdtchr
      241 fmgagvyrsk gffwlpgrdd lallwnqaag sinlefisyw kagvlthtdn sltkeeraai
      301 rqqlakmp
//
LOCUS       WP_284478842             402 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Morganella morganii].
ACCESSION   WP_284478842
VERSION     WP_284478842.1
KEYWORDS    RefSeq.
SOURCE      Morganella morganii (Proteus morganii)
  ORGANISM  Morganella morganii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Morganella.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Morganella morganii"
                     /db_xref="taxon:582"
     Protein         1..402
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=46363
     Region          2..392
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mtltarqvet akpkeksykl fdggglylev takgsrywrm kyrfggkekr lafgvfptvt
       61 laearemrnq akkvlaaggd pgevkkeeka iqklstgntf eaiarewhks kadrwslryr
      121 deiidtfekd ifpyigkrpi aeikplelle tlrrmekrga lekmrkvrqr cgevyryaii
      181 tgraeynpap dlataltppk kqhfpfltae elpyflkdla sytgsvitkt atkiilltav
      241 rtqelrfarw qdidlekgiw eipaevmkmk rphvvplskq vielfnslkp lsghyelvfi
      301 grndhrkpis kesvnqviel lgykgrltgh gfrhtmstil hekgynsawi etqlahidkn
      361 airgtynhaq yldgrrdmmq wyadymdele ssldnvvnvn fk
//
LOCUS       WP_284478950             249 aa            linear   BCT 25-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284478950
VERSION     WP_284478950.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Pereira,J. and Lupas,A.N.
  TITLE     The VCBS superfamily forms a third supercluster of beta-propellers
            that includes tachylectin and integrins
  JOURNAL   Bioinformatics 36 (24), 5618-5622 (2021)
   PUBMED   33416871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..249
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=26599
     Region          89..154
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mrraarlgaa allglaglia gpasacdasi vaarylaptd ryphgalgdp wewgalevtl
       61 alcdgmerrl rhdlpralvf edvqprrvdl dadgrpellt veshrrlgar laiwgqrdgr
      121 ltrlaatphi gqanrwlapl gaadldgdgr felayidrph lartlriwry adatltqiat
      181 apgltnhrfg dkdiagglrd cgagpeivta dadwqhlias rlrggtidsr vigpdtsaag
      241 faaalscae
//
LOCUS       WP_284478966             141 aa            linear   BCT 25-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284478966
VERSION     WP_284478966.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..141
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=13933
     Region          1..124
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mglsleqarg iiqaalaagr ardmrplsva vldagghpia feredgappg rfaiaqgkaf
       61 gaamtgmggr kqmsraeaqp yfmaalngvy ggqmvpvpgg vlvrdetgai igavgvtgdt
      121 sdndaavala giaavglvge d
//
LOCUS       WP_284478974             149 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Pseudodonghicola flavimaris].
ACCESSION   WP_284478974
VERSION     WP_284478974.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..149
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=17099
     Region          56..149
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mrridlpplw llgsallawa qgrylslgls fggdwaqflg gllvgaglll mllavyelrr
       61 qrttvmphrv pdrlvqsgiy srsrnpiylg dvlvlgglil rfdavlalpl lpiltwvler
      121 rfivpeedrm rrkyradfar yeqkvrrwv
//
LOCUS       WP_284479004             201 aa            linear   BCT 25-DEC-2024
DEFINITION  OmpW/AlkL family protein [Pseudodonghicola flavimaris].
ACCESSION   WP_284479004
VERSION     WP_284479004.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006882
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..201
                     /product="OmpW/AlkL family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21454
     Region          6..201
                     /region_name="OmpW"
                     /note="Outer membrane protein OmpW [Cell
                     wall/membrane/envelope biogenesis]; COG3047"
                     /db_xref="CDD:442281"
ORIGIN      
        1 mtrqaaalvf stalaavlag plaaqsqgdw tlgfglgyvd pksdngtlag asadvgdnaq
       61 piftaeyffr dnwgveilaa tpfkhnvfvg ggyaatvkql ppvvsvnyhv ptqtafkpff
      121 glgvnyttff eessplgnie lddswgvavq agldyeisdk navrfnvrwi dinsdvtlng
      181 anigeaeidp wvvavsyvhr f
//
LOCUS       WP_284479060             261 aa            linear   BCT 25-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Pseudodonghicola flavimaris].
ACCESSION   WP_284479060
VERSION     WP_284479060.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..261
                     /product="MlaE family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27012
     Region          11..259
                     /region_name="MlaE"
                     /note="Permease subunit MlaE of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG0767"
                     /db_xref="CDD:440530"
ORIGIN      
        1 mtvlldpiah lgravlsalg amgrvalfll lalrhlftpp fylreiltam lnigwlslpv
       61 vgmtavftgg alalqiysgg arfsaeavvp qivaigmvre lgpvmaglmi aarvtssiaa
      121 eiatmkvteq idalvtlstn pmkyltaprl laglitvpml vgigdilgia ggyfvstqsl
      181 gfntaayikn tvnflepldv isslvkgcvf ggiatlmgcy ygmnsgrgaq gvgratkssv
      241 eaaavlilaa nflitgvffs v
//
LOCUS       WP_284479076             302 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Pseudodonghicola flavimaris].
ACCESSION   WP_284479076
VERSION     WP_284479076.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..302
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33499
     Region          14..276
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mhkptsiaal qsllaaqryv cdralgtvay laltlgrplf legepgtgkt eiakalargl
       61 nrrlirlqcy egldaasavy ewnfpaqmia irtaeaegna drdslqrelf gpdflierpl
      121 lqamrpdehg apvllideid rtdepfeafl lealsdyqvt ipelgpivap eppivvltsn
      181 rtrevhdalk rrclyhwvdy pgfdreidil harvpeaaea lsrevvgfvq rlrtedlfkk
      241 pgvaetidwa kcllaldvia lspqviadtl gailkyqddi qrlqgaetsr ilddlranlt
      301 pg
//
LOCUS       WP_284479147             282 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Pseudodonghicola flavimaris].
ACCESSION   WP_284479147
VERSION     WP_284479147.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..282
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32138
     Region          1..237
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtarfestkd yvatddltva vnaavtlerp llvkgepgtg ktelakqvaa slglkmiewn
       61 vksttraqqg lyeydavsrl rdsqlgderv ydvknyikkg klwqafeade kvvllideid
      121 kadiefpndl lqeldkmeff vyetgetika kqrpiviits nnekelpdaf lrrcffhyir
      181 fpdepilrki vevhhpgikg slltaaltqf yelretaglk kkpstsevld wlklllaedm
      241 daedlkrdgv nalpklhgal lkneqdvhlf erlafmarkq qr
//
LOCUS       WP_284479156             639 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Pseudodonghicola flavimaris].
ACCESSION   WP_284479156
VERSION     WP_284479156.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 639)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 639)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 639)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..639
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=67201
     Region          10..512
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mvtpvdgalt pvtafalvga lgvgsqwlaw klrlpaivlm llagivigpv lgvfdpardi
       61 gdlmgpmisi avaiilfegg ltlnfhslag aaegvrrlvv lgaplgwlsa tlalhfvagl
      121 gwesaavfgg ilivtgptvi apllrtarlq krpsallqwe aivndpvgal aavlafevvv
      181 vvhadtsaah avwellrgig faalvgvfgg wgisrafdrg qvaeymkvpv lfaallagfa
      241 ladallhesg lltvtimgiw ianaglpsye emrrfkehat illvsgvfil laagmnldtl
      301 smldwraaaf vaaliliarp lpvllalagt kvpfrerllv altgprgvvl vavaglfger
      361 lvalgledaa riaplafviv aatvvlhgft lapvarllgl takgragvil vggsgfstal
      421 gevleklgvp vlvcdtniir lrgarnaglq tfygdilses aefgldligy drivalsend
      481 ayntlvttdl apeygranvf qlrretldtr rhtlpstlgg rriaggltyg elsrrmhqgw
      541 qlratrlsae fgyrafretf pdsvlvgelp ekgdlrlfep raddsdpklt tgaqvihlap
      601 pepapekape rrpekaaetp setaaktaps sgtgpadsa
//
LOCUS       WP_284479245             193 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II [Pseudodonghicola flavimaris].
ACCESSION   WP_284479245
VERSION     WP_284479245.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..193
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=20713
     Region          2..187
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 mlllidnyds ftynlvqylg dlgaemeiwr ndaldveaal amnpagills pgpcdpdrag
       61 iclpltlaaa ergipllgvc lghqtigqaf ggkvvrasei vhgkmgrieh sgkgvfaglp
      121 spfqatryhs lvvdrdslpd cleitawled gtimglqhrt lpihgvqfhp esiasehgha
      181 llknflndmk vpa
//
LOCUS       WP_284479160             264 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284479160
VERSION     WP_284479160.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..264
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=30090
     Region          20..263
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 madrdlfeed tlsvterlaa ealivdvdgf egpldvllml srtqkvdlrk isvlhlaqqy
       61 ltfvekakal rielaadylv maawlaflks rlllppdpte egpsgeelaa hlafqlerlq
      121 amrdvaarlm ardqkgrdff argqaedvmr irtvtysatl ldlmqgyarv rtrdefrpfv
      181 mdrhnvftme qaldrmrpli gfagdwtdit sylpdgwetd pvrrrsataa tfaaslelvk
      241 eghmeirqse tfapiqlrrk dqre
//
LOCUS       WP_284479251             113 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Pseudodonghicola flavimaris].
ACCESSION   WP_284479251
VERSION     WP_284479251.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..113
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11859
     Region          7..111
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mqlhivsyla lagaficevt gtaylqksvq ftkfaptaim avfyvlsfyl lsvalrtlpl
       61 gvayavwggl givvtaiisv vifrqsldam aifgiamivg gvvivnafsn ash
//
LOCUS       WP_284479714             500 aa            linear   BCT 25-DEC-2024
DEFINITION  malonate--CoA ligase [Pseudodonghicola flavimaris].
ACCESSION   WP_284479714
VERSION     WP_284479714.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Pohl,N.L., Hans,M., Lee,H.Y., Kim,Y.S., Cane,D.E. and Khosla,C.
  TITLE     Remarkably broad substrate tolerance of malonyl-CoA synthetase, an
            enzyme capable of intracellular synthesis of polyketide precursors
  JOURNAL   J Am Chem Soc 123 (24), 5822-5823 (2001)
   PUBMED   11403625
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11482749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..500
                     /product="malonate--CoA ligase"
                     /EC_number="6.2.1.76"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0090409 - malonyl-CoA synthetase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0090410 - malonate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53817
     Region          5..498
                     /region_name="PRK07514"
                     /note="malonyl-CoA synthase; Validated"
                     /db_xref="CDD:181011"
     Site            order(160,163..168,170..171)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341264"
     Site            order(163,203..204,207..209,249,251,255,277..279,298..303,
                     307,322,380,392,400,403,406,435,470)
                     /site_type="active"
                     /db_xref="CDD:341264"
     Site            order(163,277..279,298..303,322,380,392,400,406)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341264"
     Site            order(203..204,207..209,249,251,255,277,299,301..303,307,
                     403..405,435,470)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341264"
ORIGIN      
        1 myddnyliar lhaaavgqet rnfatfpara smtfgelfag aernaaalva mgvqpgdrva
       61 vqvdksieai qlylgtvmag aiflplntay ttpevayflg datprvvvcd pakyeaiegi
      121 agdarvvtld akglgtltda vvgrggftpv prgpddlaai lytsgttgrs kgamlshanl
      181 asnsemlrdy wqftkqdvli halpifhthg lfvatnvall agaqviflkg fdadeilkam
      241 pratalmgvp tfytrlladp rltreraanm rlfisgsapl lvdtheqwea rtghrilery
      301 gmtetnmscs npydgerrag tvgfplpgve arvmhdgkev qageigvlev rganvfkgyw
      361 qmpektaeel rpdgwfitgd mamidadgyv tivgrekdli itggfnvypk evesliddlp
      421 gvlesavigv phadfgeavv alvvpegegt tpeaitaaln gqlarfkqpk rivmidalpr
      481 ntmgkvqkka lrdtyaellg
//
LOCUS       WP_284479740             345 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudodonghicola flavimaris].
ACCESSION   WP_284479740
VERSION     WP_284479740.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..345
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35585
     Region          1..342
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 madvtiygag ifglatawac cargakvrvi dphgpgagas gglvgalaph vpenwndkka
       61 fqldsllmae afwagveaag gtsagygrtg rlqpiaddra lelarareit aadlwrdhat
      121 wavrplgdfg pwappsptgf lihdslsarm hprracaalv aalrakgaei vaegpveglv
      181 lhatgaagla elsahfgkvv gnavkgqaal laydagpgap qlfadavhiv phadgtlaig
      241 stserefedp tatdaqldav laravaampa ladvpvlerw aglrprsrsr apmlgahplh
      301 pgrfianggf kigfgmapkv aqvmadlmle grdtipegfr peasl
//
LOCUS       WP_284479780             188 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284479780
VERSION     WP_284479780.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..188
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20388
     Region          45..184
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mrlfrfltly malmlganva aaadlatlqa lregdmkkla lhetpkpvsd lafqkpdgag
       61 tatlaeyrgk yllvnfwatw capcrkempm lnalqeefgg egfqvvtiat grnspagikk
      121 ffdeigvtdl pryqdpkqal ardmgvlglp vtlivdpegr eigrlmgdad wtsesakaii
      181 aallleea
//
LOCUS       WP_284479772             299 aa            linear   BCT 25-DEC-2024
DEFINITION  cell division protein FtsX [Pseudodonghicola flavimaris].
ACCESSION   WP_284479772
VERSION     WP_284479772.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..299
                     /product="cell division protein FtsX"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=31251
     Region          25..282
                     /region_name="FtsX"
                     /note="Cell division protein FtsX [Cell cycle control,
                     cell division, chromosome partitioning]; COG2177"
                     /db_xref="CDD:441780"
ORIGIN      
        1 mnrgtirsyf igdaqadrvv ppsgftarlt lfaagamafl avfalalsla agrladrwas
       61 elarsatlri tapadqmaaq tevaltilrq tpgvararal spqeqaglla pwfgpgldla
      121 tlpvpqliev tedetgydaa glrlrlaaev pgavlddhtr wrrplveaat slrrigwisi
      181 aliggtmaam islaahaala anaqvievlr lvgardvyia safvrrftir aligavlgtg
      241 lgmggvlllp aasdeggflt glgfqglgwl wpllipilga lvafaatwaa arsrlkelt
//
LOCUS       WP_284479823             167 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Pseudodonghicola flavimaris].
ACCESSION   WP_284479823
VERSION     WP_284479823.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 167)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 167)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 167)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007442
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..167
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17395
     Region          67..165
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
ORIGIN      
        1 mfdtmtvtka asgvlgaflv lllakwaaeg iyqtgthgaa syvvetetda patdepemsf
       61 eemlasadig kgakvfkkcq achkiepgan atgpslfgvv grqvasigdf gysssmsehg
      121 gawtpeeldh fltkpsdavp gtamsfaglk kqadrvnvia yldsldn
//
LOCUS       WP_284479833             264 aa            linear   BCT 25-DEC-2024
DEFINITION  DODA-type extradiol aromatic ring-opening family dioxygenase
            [Pseudodonghicola flavimaris].
ACCESSION   WP_284479833
VERSION     WP_284479833.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Vaillancourt,F.H., Bolin,J.T. and Eltis,L.D.
  TITLE     The ins and outs of ring-cleaving dioxygenases
  JOURNAL   Crit Rev Biochem Mol Biol 41 (4), 241-267 (2006)
   PUBMED   16849108
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Siegbahn,P.E. and Haeffner,F.
  TITLE     Mechanism for catechol ring-cleavage by non-heme iron extradiol
            dioxygenases
  JOURNAL   J Am Chem Soc 126 (29), 8919-8932 (2004)
   PUBMED   15264822
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..264
                     /product="DODA-type extradiol aromatic ring-opening family
                     dioxygenase"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016701 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29131
     Region          5..263
                     /region_name="45_DOPA_Dioxygenase"
                     /note="The Class III extradiol dioxygenase, 4,5-DOPA
                     Dioxygenase, catalyzes the incorporation of both atoms of
                     molecular oxygen into 4,5-dihydroxy-phenylalanine;
                     cd07363"
                     /db_xref="CDD:153375"
     Site            order(11..13,53,118,174,227,255..256)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:153375"
     Site            order(11,53,227)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:153375"
ORIGIN      
        1 mslmptyfis hgggpwpwip dmaahlapla qslahmpael prrpkavlmv sghweaddfa
       61 vmhaahppmv ydyynfppht yeikysapga palaekvadl iaaaglpthl deemgydhgt
      121 fvpmalmype aemplfqvai rhsfdpaqhm algralaplr qedvlivgsg lsyhnlrefg
      181 prarvpsvef dtwlnqalal ppaerteail nwesapyarr charedhlvp lftalgaaed
      241 akvtrtyhqa eifggvtass frfd
//
LOCUS       WP_284479911             551 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Pseudodonghicola flavimaris].
ACCESSION   WP_284479911
VERSION     WP_284479911.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..551
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58943
     Region          36..384
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mllreraela ladlaagpsw rsmlflavfa lllflpgffs lppidrdetr faqasrqmve
       61 sgdfidirlg egtrykkpvg iywlqaaavk lvgvaqdqki wvyrlpsltm avaavlltyl
      121 ialslvgaqa alvaamllas cfvlggearl aktdatllat ilaaqlvlar lhmggaaalr
      181 ggwawlfwaa mgvsmlikgp igpmvvglti lalivlrrgi gwlaplrwgw glllfaaivl
      241 pwyvaitvts gdafwaealg rdllgkigeg qeshgapfga ymlavwltfw pasillpfgl
      301 wygwsarrmp avmfclawil pswlvfeita tklihyvlpt ypalamltaa gwlerreapl
      361 griyglflgl flllalglaa apvifslrfg vapgaiwalg vaisvagmiw vwaalrrgdr
      421 lapllgmgal slglsvslfg hlarlapiwp snamseiave adrlceapai lsvgyeepsl
      481 lllsprlplf rpaaaaaeia aaapcalvfv taeqkpafda ampktgevlg qvtgfalgga
      541 dqvdvtaylf r
//
LOCUS       WP_284479949             282 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Pseudodonghicola flavimaris].
ACCESSION   WP_284479949
VERSION     WP_284479949.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..282
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=30939
     Region          52..267
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          141..166
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(142..143,146..147,149,173,176..177,180..181,
                     183..184,207,210..211,214..215,218)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          171..201
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrhplvipac liaglalagc aekgdetver afrdvnvide tnlnevmltv adpneavdyf
       61 arstkstpdr idlqrglaqs lvrakrntea aavwgkvvgm pgateddsvd yadalirsgd
      121 wdrakktlds vppthesfkr yrleamvada nhewkradsf yeiavglttt pagvlnnwgf
      181 skltrgdypg aerlfgdair rdptlftakn nlvlargaqh nyslpvipmd qteraqllht
      241 malsavkqgd vntgkallre aidthpqhfe eavrslrale ts
//
LOCUS       WP_284479956             226 aa            linear   BCT 25-DEC-2024
DEFINITION  ZinT family metal-binding protein [Pseudodonghicola flavimaris].
ACCESSION   WP_284479956
VERSION     WP_284479956.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..226
                     /product="ZinT family metal-binding protein"
                     /calculated_mol_wt=24770
     Region          49..226
                     /region_name="ZinT"
                     /note="Periplasmic Zn/Cd-binding protein ZinT [Inorganic
                     ion transport and metabolism]; COG3443"
                     /db_xref="CDD:442667"
ORIGIN      
        1 mkqtlakrig altltallgt alqaaasgtt sgdhshdhah dhshadaqqk qiykgyfeds
       61 qiaprplsdw egdwqsvfpy lmdgtldpvm adkaahgskt aegykayyqi gyqtdvdriv
      121 idgdqvsfht gdnvvtgtya ddgyevltyk kgnrgvrfvf aktagdddap gfiqfsdhai
      181 apnkaghyhl ywgddraall qevtnwptyy pstlsgdqiv hemmah
//
LOCUS       WP_284480172             328 aa            linear   BCT 25-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Pseudodonghicola flavimaris].
ACCESSION   WP_284480172
VERSION     WP_284480172.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..328
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=35631
     Region          8..310
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(12..13,15,55..57,78,106..107,110..111,113..114,117,
                     121,123,131,133,135,137..143,145..149,167..168,171..172,
                     272..273,280,286..292,294..297,299)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(56,79..81,104,243,290,293)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240626"
     Site            order(80..81,108,157..161,179..181,185,213..215,219..220,
                     241..243,267..268,290,292..293)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 mprerlsvvv trrlpevvet rlselfdvrl reddtpmsra elveavktad vlvptltdsi
       61 dagliaqage rlklianyga gidhidvata rqrgvlvsnt pgvvtddtad mtialmlavt
      121 rripeglaam qkgdwtgwap taflggrisg rrlgilgmgr igqavarraa afgmqvhyhn
      181 rrrvrpeiee aleatywesl dqmvarmdvi svncpstpst fhlmnarrlt lmkptavivn
      241 tsrgevides alarlirdgg iagagldvye rgsdvasklr dlpnvvllph mgsatvegri
      301 emgekviini kthedghrpp dlvvpgml
//
LOCUS       WP_284480201             381 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284480201
VERSION     WP_284480201.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..381
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41700
     Region          5..381
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mweaervlrh avmngrlpfa vamvgtsggi rfsssigdad sgrpagedtv frifsmskai
       61 galaalilid rgvlspetpv adllpewadl pvlegwdgdt pilrpqrgta tlrhlathts
      121 gieyefwnad vakyletrgv ppalsgrkag lmypltsdpg trwgyglsid wlgrmveaad
      181 grpidrfcre eifaplgmrd trfepdgled rlaavrmraa dggfrpsrlt pprrpevygm
      241 ghalystapd ymrflrmvln ggtldsqril spetlrlmte dqmqglqfrk misvspkssa
      301 dvdlfpgqpv thsmaflrne taipgrrsag slgwagicnt hywidpardl aavlmtqslp
      361 fldppvaety aafesavyag l
//
LOCUS       WP_284480355             112 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284480355
VERSION     WP_284480355.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 112)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 112)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 112)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..112
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12625
     Region          22..107
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 malpqfsvdm sedeldrmvd nateasnflk aishegrmmi lchlvtgeks vteleellsa
       61 rqaavsqqls rlrleglvvp rregkaiyyr ladnrprril evvydlfcnd gd
//
LOCUS       WP_284480553             210 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284480553
VERSION     WP_284480553.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..210
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=21582
     Region          14..189
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mtekthdlsg ayslqtpeds valyagwakd ydqtfataed yrlpaataea fkaaggsgpv
       61 ldvgagtglc aaaltalgig pidaadispe mlkvagekgl yralieadlt kglplpetpy
      121 agvvssgtft tghvgpeeie allpiarpga lfaiaingah yeaagfsakl dalaqgpirn
      181 lwlpevriyg engrgahkdd talialfeka
//
LOCUS       WP_284480665             199 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Pseudodonghicola flavimaris].
ACCESSION   WP_284480665
VERSION     WP_284480665.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..199
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=21858
     Region          4..179
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 msvplilass sqirarllqn agvaveirpa rvdeetvkaa llaetapprd iadtlaelka
       61 rkvsekhpga lvlgcdqvle fdgrllskpe spdqaldqlk amrgkqhkll saavicrdgq
      121 pewrhigqvr lsmrqasdgy ladyvarnwd sirqavggyk leeegvclft ridgdyfnvl
      181 glpllellnf lmlrgeids
//
LOCUS       WP_284480983             455 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pseudodonghicola flavimaris].
ACCESSION   WP_284480983
VERSION     WP_284480983.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 455)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 455)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 455)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..455
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48585
     Region          122..442
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mtaprslqar laigiglllt llwlsattit alvlrhqmne fsdaalqeta qrllplalse
       61 iagrdddsvt qrlgvirvhh elftyilrda egrvllqsht adpsvfpryd gpgfqwtgth
      121 rlfndetldg qiritvaepl iyrramarrv qimmglplll vipvalaava lavraslapl
      181 rrfrsalaar gardlsplpt gglpaeitpl aetlndlltr lkaafeaers faanaahelr
      241 tplagaiaqa qridietadp garkrageie atlkrltrvs erlmqmarae ggrlrgdhaa
      301 dlrpvvrmiv qdlsrqaggk tlelelpetp vcsdldpdal givlrnltdn alrhglpdtp
      361 vriglspagr lsvanetatv padvldglaq rfergtarae gsglglaiva tiadrtggal
      421 rlfspspgrg sgftaevelp lggespppdt sppaa
//
LOCUS       WP_284480998             411 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudodonghicola flavimaris].
ACCESSION   WP_284480998
VERSION     WP_284480998.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..411
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43203
     Region          1..407
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 maeilvlgag mvgtatalal qarghdvvla drrapgqets ygnagviqge aaepyglptn
       61 pltllrlalg aenavrltaa gvlgqagall rylnnsrtar hraisavyar ltaraiaahe
      121 plvaasgaaa lmrphgfrva fetarafdaa rpeaerlaks ydrglrlldg aalaraepgl
      181 rlrypgaiew tdcwacsdpg alvagyadlf arrggqvtra eaesltraga gwrvtgpdgp
      241 ieaarvvlal gpwtpallkr fgyraptvak rgyhlhlrga ptlnlplmdt tvssvmspmr
      301 aglriatgae lvpmsapvnr sqiaraeara rrmfdlgdav eatpwvgtrp clpgmlpvlg
      361 elrrtpglwv hfghghqgft lgpvtaella etmagvpsdl asalhpdqai h
//
LOCUS       WP_284481042             505 aa            linear   BCT 25-DEC-2024
DEFINITION  formate dehydrogenase beta subunit [Pseudodonghicola flavimaris].
ACCESSION   WP_284481042
VERSION     WP_284481042.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11555116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..505
                     /product="formate dehydrogenase beta subunit"
                     /GO_component="GO:0009326 - formate dehydrogenase complex
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=52944
     Region          1..95
                     /region_name="TRX_Fd_FDH_beta"
                     /note="TRX-like [2Fe-2S] Ferredoxin (Fd) family,
                     NAD-dependent formate dehydrogenase (FDH) beta subunit;
                     composed of proteins similar to the beta subunit of
                     NAD-linked FDH of Ralstonia eutropha, a soluble enzyme
                     that catalyzes the irreversible oxidation of...; cd03063"
                     /db_xref="CDD:239361"
     Site            order(2,4,38..40)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239361"
     Region          91..497
                     /region_name="NuoF"
                     /note="NADH:ubiquinone oxidoreductase, NADH-binding 51 kD
                     subunit (chain F) [Energy production and conversion];
                     COG1894"
                     /db_xref="CDD:441498"
ORIGIN      
        1 mkiyvpldsa akalgadeva aaiaaeaear gleielirng trgmvwlepl vevedggerl
       61 aygpltpaev palldrtldt lgrvedmpff arqtrltfar cgltdplsla dyqahgglsg
      121 lrralgmtae avvdevktsg lrgrggagfp tgikwdtvrm ahasqkyivc nadegdsgtf
      181 adrmiiegdp fcliegmiia glgtgatkgy vylrseypva iellrqaidi aradgvlgss
      241 vlgsgrsfdm evrvgagayv cgeetsllns legkrgvvra kpplpalegf lgrptvvnnv
      301 islatvpvif ekgaqhyadf glgrskgtip vqiagnvkyg glfetafgmp lgelvndvag
      361 gtasgrpvka vqiggplgay fatadfdtpf gyeefdgqgg lighaglvvf ddsadmlhma
      421 rfamefcave scgkctpcrl gavrgvetld riaagdtgav plltdlcevm kdgslcalgg
      481 ftpypvlsal qrfpeefgtv keaae
//
LOCUS       WP_284481085             413 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284481085
VERSION     WP_284481085.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..413
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44010
     Region          1..413
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mqvakpqdrg ldparlarls dwmdryvaer kypgssilia rggeevyfna tgqrniedgl
       61 pftrdtlvri ysmtkpvtsv almmlvekgl fhldapvsef ipefndmqal vpgavridqt
      121 eacapptlhq lllhtsglsy pfnpgllgrk mdeekilfkp ndgpladmaa rvaalplsfv
      181 pgtsweysvg idiigrvvev asgkslaaff aeeilgplgm setgfsvpag agdrfaslyt
      241 plagdamaln saetggdslr ltdragrspf eaatmhsggg glvstiddym kfaemlrkgg
      301 sceggrllsp stinfmmrnh lpgdiasmgq qsfaeqpmvg tgfgiggsvv lepgrvgvpg
      361 nvgdfswggm astffwidrv ldltavfftq lspsssypsr aelkallhga via
//
LOCUS       WP_284481252             197 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Pseudodonghicola flavimaris].
ACCESSION   WP_284481252
VERSION     WP_284481252.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..197
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21271
     Region          <18..132
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mwdqryaqpg ylfgvapaaf ladragslap gstvlcvadg egrnssflaa eghrvtafda
       61 spvglekarg laaergvavd yhlsgiedwd wsqsfdvvvg ifiqfaapaq rdqlfrwmaq
      121 avapggllll hgytpkqvey gtggprdpsh myteemltqa fpgwellrca ayereidegp
      181 ghsgrsalid fiarkpl
//
LOCUS       WP_284481328             444 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284481328
VERSION     WP_284481328.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..444
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=48914
     Region          3..437
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 maqamkiaiv ddeqdmrqsi sqwlalsgyd tetfaraeda lkvlgpdypg ivisdikmpg
       61 mdgmqflkkl mgsdsalpvi mitghgdvpm aveamrvgaf dflekpfnpd rmsdlakraa
      121 narrltldnr alrkelsdgt qlmkkligss pvmerlkedi ldlsqadghv liegetgtgk
      181 tlvahalhaa gsragkkfvl iscaaleeda lskrlfgpmm pedsqlpaie earggtlvle
      241 diealsdalq arllsaineq gmpaetriia isnlqeagkt cedvlrpdlf yrlaalrvmv
      301 pplrqrgedi ltlftrlteq fseeygceap kvsaqeaaql lqapwpgnvr qlinvaerav
      361 lqsrrgsgti asllmsdhee mqpvmttegk plkeyveafe rmlidntmrr hkgsiasvme
      421 elclprrtln ekmakyglqr sdyl
//
LOCUS       WP_284481368             948 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284481368
VERSION     WP_284481368.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..948
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=93702
     Region          <2..>931
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 msnslliptt tdvtaanada vtggdydvil vregvrltas gssgnglvfg swsiatikgd
       61 iaarngdgiv fgdynavtvs qsatvsgflg amavsganna ivnngalasv sysitlsgan
      121 nsvvnagtis agdggisgll ggsiansgei atrgsalyfa dgrvivdnsg qitsssanai
      181 siadsgaiag qslvsntgml sgaqyglnid raavaltntg tiqggvggvh yvgasassaf
      241 aisianagli ssggvgidla savpehgltn sgtvtgyssg vhalgnrldl ensgtiegrs
      301 ehalllegld nsivnsgtlr arsdvisamg pldqfgaptm astdingtki lntgriqsel
      361 gsgivllgre nlivnrgevi addsglyllg tgtikntgtv taetagnwav ilsntdagag
      421 fpskvvndgl idspygrgvl aasgegarli nrgtiladrq aaqvggadal lvnhgviesq
      481 tsavvlaada llvnsgdilg tvqslwpgsv pgaldirnag tilapdlald llydsgavri
      541 vnkgsigvtg gttvlrvqda vaatpvstti lnagvltgav alsggadlfq grtgshvqgd
      601 idmaagadvl rnagviagdl rmgagddlyr grfegvvegt vfgddgndll rggagddtld
      661 ggadddtlhg grgediligg tgddtyiind tddviveaag egsdtvmtrl asfaltdrnv
      721 enltgtsnag qslsgnsrdn aitgadgddt lsgkagndrl dggagadmms ggagddtyvv
      781 ddagdgvien agggtdtvet dlasyslgtl anienltgts vagqvlggnt ldnvitgstg
      841 ndalygglgd dtlrgnggnd tmnggggsdt fiftagfghd ringfhagat gdadviaiss
      901 gliadyadll shtadvgant vitvdasnti tllgvqkadl dssdfwfs
//
LOCUS       WP_284481399             368 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudodonghicola flavimaris].
ACCESSION   WP_284481399
VERSION     WP_284481399.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..368
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38415
     Region          26..363
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtsadvivig ggiagisaaa alseemsvvv leaearlgyh atgrsaaifi rnygnatlra
       61 lnaasapffe apgeiadgpl lsprgemlva teeemptlsa yaagaegleh lspaqavelv
      121 pilrperica aviewdaqdi dvdlmmagyg rclkanggri etaaavrglr rhgglwqvdt
      181 prgiyrapli vnaagawage varlaaacpi rliplrrsaa llpapagydv tqwplfasaa
      241 eswyakpqsg klmispaded pvapqdawad dmvlaeglhr yeqavttpvt rvetswaglr
      301 tftadrspvv gfdpgtegff wlagqggygv qtapalarlt aalctatapq lagdvvrala
      361 pqrllpaa
//
LOCUS       WP_284481435             143 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Pseudodonghicola flavimaris].
ACCESSION   WP_284481435
VERSION     WP_284481435.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 143)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 143)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008128
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..143
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15042
     Region          5..143
                     /region_name="CytC556"
                     /note="Cytochrome c556 [Energy production and conversion];
                     COG3909"
                     /db_xref="CDD:443115"
ORIGIN      
        1 mtkriamali lagtaafahg gvqnpdvktr mmgmgdlarq mkliggmakg eaafdaeavn
       61 talarmseaa seipslfetp aedpqsealp viweefagft traselealt aelagsvtse
      121 aelrpvmqql gkacrachat fre
//
LOCUS       WP_284481515             165 aa            linear   BCT 25-DEC-2024
DEFINITION  SixA phosphatase family protein [Pseudodonghicola flavimaris].
ACCESSION   WP_284481515
VERSION     WP_284481515.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..165
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18462
     Region          5..149
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mtrrliltrh aksawdkpgl pdhdrplnkr gkraaealgd wlrrngylpd qvltssarrt
       61 qdtlrrmqld vvpdvtehly lvtanqilrv lsqahgdtvl llghnpgiaq faheilaepp
      121 thpkfhvypt gatlvvdfdi ddwaqaawrg geavdfvvpr elves
//
LOCUS       WP_284481521             515 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pseudodonghicola flavimaris].
ACCESSION   WP_284481521
VERSION     WP_284481521.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 515)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..515
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=56302
     Region          <74..502
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mqlpnssplt rlrnrilpvl mgppilaflp altlgafwlw geaalvitsl glpllfafig
       61 afddrarqps iprdavtglm lregfetale rtyadtqrsg mrsacfvldl ddykdlterh
      121 giaaadlvaq qtgericaal rnddvvarig dsrfavclsp vrvldlelci qlagrmqaav
      181 edpisldast vymtasvglc mrrrapgqda aawlqaatea laeaqrsgps girvysadth
      241 rrsqarndlr eeaafaleng qiqpwyqpqi stdtgkitgf ealarwvhpv hgvltpdnfl
      301 paleqaglle rlgqvilyha ltaikawdsa gvdvpsvgvn fateelrnpg lvdrirweld
      361 rfdltadrls veilesvvst dpddtiahni aglaklgcgi dlddfgtgha sfssirrfav
      421 srikidrsfv mksdrdpeqq rmiaailtma erleletlae gvetvgehal laqlgcdhvq
      481 gfgigrpmpf eqtldwiath haklrdapri gretg
//
LOCUS       WP_284481686             343 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284481686
VERSION     WP_284481686.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 343)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746489
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..343
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38156
     Region          34..203
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <150..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          251..332
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mleealvlda agrpirhdgr trsqdwdevq efcrkvympy rvrpldrrar pdatmisata
       61 grvtmtrfay gtgihlnefd peagnilvln tlrgglshqs dgtpattgpg esyvvdcsrt
      121 dywlegddah mqfnltiphr ameeiaerwf gfvpddalwt rrvkfagpgs rwlslldyaa
      181 raaragapgt pegalnrhle emiclellqh wadatglrld rgaraaaprh vrqaeeimta
      241 eareapaigd iarrvgvsar tlsegfrrfr glspraflaa rrleglradl ltaapersvt
      301 eialswgysn lgalaglyrn rfgerpsetr arsrhrhcap ksd
//
LOCUS       WP_284481745             346 aa            linear   BCT 25-DEC-2024
DEFINITION  heme-dependent oxidative N-demethylase family protein
            [Pseudodonghicola flavimaris].
ACCESSION   WP_284481745
VERSION     WP_284481745.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Ortmayer,M., Lafite,P., Menon,B.R., Tralau,T., Fisher,K.,
            Denkhaus,L., Scrutton,N.S., Rigby,S.E., Munro,A.W., Hay,S. and
            Leys,D.
  TITLE     An oxidative N-demethylase reveals PAS transition from ubiquitous
            sensor to enzyme
  JOURNAL   Nature 539 (7630), 593-597 (2016)
   PUBMED   27851736
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10571292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..346
                     /product="heme-dependent oxidative N-demethylase family
                     protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=40284
     Region          53..286
                     /region_name="DUF3445"
                     /note="Protein of unknown function (DUF3445); pfam11927"
                     /db_xref="CDD:463399"
ORIGIN      
        1 mtkhfndetf rgdytyynsp eairrfpfpf drdsymysvn ieqhpggpag spfeyafdvd
       61 ehyvaemkdr aitlaedplr cqslphmela gwdllelime akardypdlf glhkdgdrwh
      121 winrplridq rftfldattl pygpmeyitr qaqgdfallh eregnlwmda gmvtsqadws
      181 ldfdvgmnff ewhapvpkak kmgvfdkalk fllavqqgqa yrrlnwtmtv nprldtspen
      241 yhkwgpekrt itpqnvgrkq flrvelqsfw rlprsnaivf pircylacld dlasqpkwgr
      301 rlhrvlrdld pvlveykgfa vnrdiivahl aryddgapts pgifpd
//
LOCUS       WP_284481757             340 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Pseudodonghicola flavimaris].
ACCESSION   WP_284481757
VERSION     WP_284481757.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..340
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=37143
     Region          9..325
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 myltsiarfr aiaillivag hgfplaaiap qdlisgtlan litggttlfv cisgymfhhv
       61 fahrfafrrf itaklrtill pylalcvpit cyfvirnpef asetlgqsaa plqigkvivt
      121 galfqaywfa pfilcmflms plhlrflgla pqpqaliiia gliaavlvhr pvanlnplqs
      181 liyftpaylc glcasryraa llrrlreqet allaaallla lvqtglgqqg nlhsaalsws
      241 gidlmlpqkl llslaifall ergtgprldr lrpvsetsfs ifflhpvali liekagtqhp
      301 tglawinllw itaqavgfsm alalsarrll grrsrfllgy
//
LOCUS       WP_284481802             198 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Pseudodonghicola flavimaris].
ACCESSION   WP_284481802
VERSION     WP_284481802.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..198
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21502
     Region          1..192
                     /region_name="HAD_sEH-N_like"
                     /note="N-terminal lipase phosphatase domain of human
                     soluble epoxide hydrolase, Escherichia coli YihX/HAD4
                     alpha-D-glucose 1-phosphate phosphatase, and related
                     domains, may be inactive; cd02603"
                     /db_xref="CDD:319790"
     Site            order(7..11,105..106,139,163..164,167..168)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            134
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mtavvfdign vlvewdpcra wedklpdrda iaafmarvdf palnlrgdrg esfaslaaev
       61 vdpgdralll ayldgyhrti eakidgswdl lkrlraagva ihaitnwshe twpigvsvhp
      121 elgevfgvtv vsgqekllkp epaifrtlld rtglaaddcl fiddsprnvd garavgmdav
      181 hftspqalet altergll
//
LOCUS       WP_284481968             605 aa            linear   BCT 25-DEC-2024
DEFINITION  autotransporter assembly complex protein TamA [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284481968
VERSION     WP_284481968.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..605
                     /product="autotransporter assembly complex protein TamA"
                     /GO_component="GO:0097347 - TAM protein secretion complex
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=64032
     Region          23..605
                     /region_name="TamA"
                     /note="Outer membrane translocation and assembly module
                     TamA [Cell wall/membrane/envelope biogenesis]; COG0729"
                     /db_xref="CDD:440493"
ORIGIN      
        1 msslgrkfal rrgmtalcag awlacaagna qaldssltat gasedlqdsl ktasavmsag
       61 drgldnvqel iaaaqadyqt lvqvlydrgy fspvihirvd greaayidpl alpsridria
      121 ievapgpqfr fgtaeiapla entampeafa pgapastgai rdataagvqg wrdagyakat
      181 idsqritanh aaarldaqvr lrpgqklrfg klivagnsdv reeavqriag lptgetyspe
      241 tlqtvntrlr rtgtfstvtl heaetanpdg tldvtttled mpkrrisfgv emssnagldl
      301 smawmhrnlf hgaerlries signiggsed iegrlgirld rpdrlgpdds ifytfdieql
      361 erehysvsrt slgigarrvf spdlvgevav vgmyanadda fgdgrdfeyl glpitlewdk
      421 rdnpvnargg hllrletmpf fglsgsksgg rlmadarayr sfgatgrltl agrlqlgsvv
      481 gpaqsevspd llffsggagt vrgqpydslg idvggktagg rsflgasvel rgqitdkisa
      541 vgfldygavd assfigsdta shsgaglgvr ydlggfgpvr fdlaypvggd tgeglqyyig
      601 igqaf
//
LOCUS       WP_284481979             281 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Pseudodonghicola flavimaris].
ACCESSION   WP_284481979
VERSION     WP_284481979.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..281
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30708
     Region          4..>160
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 msgllsiilp ahnealwigd cleailasdp lpegwgleti vvpngcqddt agrsrahgad
       61 faargwtlqv velaaggklg alnrgddlar gavrvyldad vrvsppllrq iagaldtdlp
      121 ryasgtphva qarslatrly srfwerlpfv ttdapgfgif amntagrgrw kawpdiisdd
      181 tfarlnfapa ererlsafyt wplvegfanl vrvrrrqnig vreiaerfpq leanalatrp
      241 gkrrlarlal tdpagflvya avslavktpl yddhsrwarg r
//
LOCUS       WP_284482046             483 aa            linear   BCT 25-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284482046
VERSION     WP_284482046.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..483
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=52049
     Region          2..474
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mhadfiirga eiidgtgapr rrgdvavsdd rivatgdlsh wtagreieaa grvvspgfid
       61 phvhhdaalf mrpdmefmtn qgvttvingn cgfsiapvtr penlpgqlaa iagrpdlifa
      121 tyaayrdria aeppavnaac ligqstlran amddltkaat kselaemcrl ldgalaegai
      181 gvstgpfypp srastteeli elgkiahrhg klyvthmrde gdrviealee tfavgrescc
      241 gvhvshhkca glanhglstt tlkmiddemq qrdvgldttp wiasstilns grhkqatrvi
      301 vaesepypdm agrdladiar ewntdlddam erllpatgif fimaeedvqr ilsyehtiic
      361 sdgmptgkhp hprvwgtfpr vlghyvrdvg lfsleegvrr mtsmpadrfg lggrgriavg
      421 afadlvifdp atiaegatfe npiqpahgid rvfvngrevf aggkptgarp grpltqtapv
      481 qvv
//
LOCUS       WP_284482107            1110 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl-CoA carboxylase family protein [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284482107
VERSION     WP_284482107.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 1110)
  AUTHORS   Wang,Y., Yu,W., Li,S., Guo,D., He,J. and Wang,Y.
  TITLE     Acetyl-CoA Carboxylases and Diseases
  JOURNAL   Front Oncol 12, 836058 (2022)
   PUBMED   35359351
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1110)
  AUTHORS   Brownsey,R.W., Boone,A.N., Elliott,J.E., Kulpa,J.E. and Lee,W.M.
  TITLE     Regulation of acetyl-CoA carboxylase
  JOURNAL   Biochem Soc Trans 34 (Pt 2), 223-227 (2006)
   PUBMED   16545081
REFERENCE   3  (residues 1 to 1110)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
REFERENCE   4  (residues 1 to 1110)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20212453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1110
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..1110
                     /product="acetyl-CoA carboxylase family protein"
                     /EC_number="6.3.4.14"
                     /EC_number="6.4.1.2"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=117504
     Region          6..464
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          509..572
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(529,538..540,547)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            539
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
     Region          592..1105
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mrqdvtkili anrgeialrl aeavvelgmv pvavyseddk galhvrraqe aialngqgar
       61 ayldiagmia aaeqagaqai hpgygflses aefaravaaa gmvfigpspe aleelgdktr
      121 arqlaqrvga pvnpgldqaa dpeafrafmq elggdpivlk avaggggrgm rivreaaela
      181 dafeaasaea aaafgnpaiy aerflenarh ievqvladgt havhlwerdc tlqrrhqkli
      241 eiapapalap dmrqrlldsa vemaravgyc glgtfeylvg adgtlafiea nprlqvehti
      301 teeitgvdlv qaqirvvlga slfelgltqd qvpaprghav qlrvnmekma adgsalptgg
      361 rlsvyeapgg pgvrvdgagf aglrpspafd sllaklivha pgsltdtlar arralgafri
      421 egvetnipyl malldlpela sgkahtrlve aragalfeaa qrvpkpathc atsgksddpl
      481 avlaygrgtg gdaapgrapa dlgsgvtgap mqgtilavka apgdtlssgg ailvmeamkm
      541 qhtiaaetag rlrdvfvapg dmvalgdplf alepddsveg etveaealdp dhirpdleel
      601 iarraltrda arpeavakrh akgkrsaren iadlcdddsf teygdlviaa qrsrrslddl
      661 mrntpadgli tgmgtvngdl fdaevarcgv lhydytvlag tqgkmnhekt drmlhviern
      721 rrpliffceg gggrpgdvdv qsisglhvmt fnmqarlsgl vpmvgigsgr cfagnaallg
      781 ccdvviatrd atigmggpam ieggglgvfr peevgpsavq sengvidilv edeteavava
      841 kqylsyfqgp vadwqapdar mlrhvvpenr meaydvhaai egmadvgsvl elragfaagm
      901 vtalirvegr plgvvannpr hmagaidtpg adkaarflql cdahdlpvvf lcdtpgmmvg
      961 peiektalvr hcsrlfvigs nlevptctfv lrkayglgaq amaggsfrap nfvvswptge
     1021 fggmglegav klgyrkelea vadpeerkal ydkmvahmye rgkalstatm feidtvidpa
     1081 etrvwigmml esapprvpra gkkrpwvdtw
//
LOCUS       WP_284482193             137 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: RrF2 family transcriptional regulator
            [Paracoccaceae].
ACCESSION   WP_284482193
VERSION     WP_284482193.1
KEYWORDS    RefSeq.
SOURCE      Paracoccaceae
  ORGANISM  Paracoccaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Schwartz,C.J., Giel,J.L., Patschkowski,T., Luther,C., Ruzicka,F.J.,
            Beinert,H. and Kiley,P.J.
  TITLE     IscR, an Fe-S cluster-containing transcription factor, represses
            expression of Escherichia coli genes encoding Fe-S cluster assembly
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 98 (26), 14895-14900 (2001)
   PUBMED   11742080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Paracoccaceae"
                     /db_xref="taxon:31989"
     Protein         1..137
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=14451
     Region          2..137
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mrltsftdyg lrvlmrmaga pdrafttsel adefrvsrnh lakvisalaa aglletrrgg
       61 gggamlarap edirlgdvva aleadqalve cfavgtnsct ltpqcrlkar lahaeaafva
      121 dlnrgtladc vyrpena
//
LOCUS       WP_284482377             443 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudodonghicola flavimaris].
ACCESSION   WP_284482377
VERSION     WP_284482377.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..443
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47177
     Region          31..430
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mpgpqltpfv sdpdlpprvd vvvigggivg tstalelaer glsvllcekg eiggeqssrn
       61 wgwvrlsmrd preiplmiea lrlwegldar vggatgyrra gilftaadtk tfrqqerwae
      121 nlrpyqiear mvsgadldgl lpgrqiglkg alhtpldgra epqwaapava egaraagaav
      181 ltgcavravd laagrisgvf tergrvacea vvlaggawsr lfagnagial pqlkllntvm
      241 rtsaveggpe vsvwadrfal rkradggytv asgventcdl vpdsfrlmra flpalfhews
      301 slsfrlsgrw reearmprrw apgdvtpfet crvldpapse kvlkscwaea qrafpllqga
      361 qmlqswggmi dvtpdavpvi savegmagmh iatgfsghgf gigpgagrlm adlvtgaapv
      421 vdptpfrlsr fsdgsrvtld kgf
//
LOCUS       WP_284482613             147 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Pseudodonghicola flavimaris].
ACCESSION   WP_284482613
VERSION     WP_284482613.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..147
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16045
     Region          1..138
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mtqeiecyrg vvhpwlcdam ghmttrhyta mfddgsyhll aelgfgpeml arrqgfadvn
       61 lnmtmqaela agdltvvsgr viriggksmv lgysmrnrtt gdlaaeliat tvqfdlearr
      121 aievlpvird tarrlfpeae iapgsaa
//
LOCUS       WP_284482600             131 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Pseudodonghicola flavimaris].
ACCESSION   WP_284482600
VERSION     WP_284482600.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 131)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 131)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 131)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10601782
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..131
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13671
     Region          44..107
                     /region_name="Cytochrome_CBB3"
                     /note="Cytochrome C oxidase, cbb3-type, subunit III;
                     pfam13442"
                     /db_xref="CDD:463879"
     Region          <93..130
                     /region_name="Aconitase"
                     /note="Aconitase catalytic domain; Aconitase catalyzes the
                     reversible isomerization of citrate and isocitrate as part
                     of the TCA cycle; cl00285"
                     /db_xref="CDD:469706"
ORIGIN      
        1 mrfslpttrr alalglslcl tagtaaadel tvdpaaaaqt rgdrsgarla qntclqchgm
       61 gvgpdlrlqk ldyetlhhvt rhglnampaf reseisddel ravaayiasl rvapgatpgv
      121 vpgsiaereg h
//
LOCUS       WP_284482705             202 aa            linear   BCT 25-DEC-2024
DEFINITION  LolA family protein [Pseudodonghicola flavimaris].
ACCESSION   WP_284482705
VERSION     WP_284482705.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Tajima,T., Yokota,N., Matsuyama,S. and Tokuda,H.
  TITLE     Genetic analyses of the in vivo function of LolA, a periplasmic
            chaperone involved in the outer membrane localization of
            Escherichia coli lipoproteins
  JOURNAL   FEBS Lett 439 (1-2), 51-54 (1998)
   PUBMED   9849875
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..202
                     /product="LolA family protein"
                     /calculated_mol_wt=21308
     Region          16..190
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mrnlllslsl palilaapla qaaeklplsa isaylnglkt aespftqind dgtlttgtly
       61 lsrpgkarfq ydppgnaavi vgagtvvird pksnqppesy plsrtplsii lasrvdldra
      121 nmvvghtfdg tstvitaqdp dnpdygriel mftdtpvelr kwvihdasgg qttvilgkle
      181 tgmslpgslf lpvggsaptd kr
//
LOCUS       WP_284482789             426 aa            linear   BCT 25-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284482789
VERSION     WP_284482789.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..426
                     /product="metal-dependent hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45599
     Region          11..>71
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
     Region          52..404
                     /region_name="Met_dep_hydrolase_A"
                     /note="Metallo-dependent hydrolases, subgroup A is part of
                     the superfamily of metallo-dependent hydrolases, a large
                     group of proteins that show conservation in their
                     3-dimensional fold (TIM barrel) and in details of their
                     active site. The vast majority of the...; cd01299"
                     /db_xref="CDD:238624"
     Site            order(69,71,238,258,326)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mataqdatpi litnvnvfdg vhealienan vvvtgnlise istadlavag gtvidgggrt
       61 mipglidvhw htsyccapqs tvatgdilei airgamgser tlmrgfttvr dvggnpfatk
      121 kmidageivg prilpsgppm sqtgghfdyg ayqdvpsnpg dslwywnrvg lmliadgvdd
      181 itmrarevmr mgasqlkisg gggvssvydp ldvsqytlae lkafvevaes yntyvashif
      241 tdaaaqmaie agvktiehgn llsretlemm kehdvwlsvq pllndedaft frdpvsvqkw
      301 vdvtdgttas iqmakeigvk vafgtdmlfd aalaekqgkf lakmstwytp yevlkmatst
      361 naellelagp rhpyqagplg vlepgayadl ilvdgnpled idlvadaaan fdlimkdgki
      421 fkntld
//
LOCUS       WP_284482739             141 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Pseudodonghicola flavimaris].
ACCESSION   WP_284482739
VERSION     WP_284482739.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 141)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 141)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..141
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14755
     Region          <11..138
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mttrfltpnr llislpllav laacvadqmg mptaaegeal fadnctachd yhgeggalis
       61 gvkapdltri alrnggtfpr trvlsqidgy grgkvsadim pefgsllegd lvpvevegtm
      121 tptprplaal laylesiqve s
//
LOCUS       WP_284482833             329 aa            linear   BCT 25-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284482833
VERSION     WP_284482833.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..329
                     /product="isopenicillin N synthase family dioxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37007
     Region          7..329
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 miiyepphaa teiplidltd sfsddlekrk avaweihkac vdtgffyikn hgipqevmda
       61 qlklaaeffd lpmeekmkld svqqhstrgy epmaaqtlde gsppglkegf mssveagpdh
      121 rytklevpgt gpnqwpdeaf pefrpqyeay vekvldlgrh larlvalsle lpedyfdeal
      181 veplhycril kyppmpkdaa enqlgagaht dwglltlllq ddigglevrn adgqwisapp
      241 ipgtyiinlg emlpvitndr ykanfhrvln nktdktrysc ptfcdpeyfy kvecaptile
      301 hdgyakypam tagehlraqf ektfgiaak
//
LOCUS       WP_284482840             304 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Pseudodonghicola flavimaris].
ACCESSION   WP_284482840
VERSION     WP_284482840.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..304
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33034
     Region          1..208
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mlrftiiipc ynaettlart leslrfqtqp dwealivddg stdstravae rfaaedcrfr
       61 llpnpgkgpa sarnvalnaa rgdliafcda ddlweadklq rmlevfadpt vdaafarvaf
      121 fdeagsrtls tvpaeaisvq mllgenpvct msnlvvrrdv fratggfdca lvhnedlewl
      181 irlcacgfrl igvqhtlvhy rtsptglssd ldkmragrea alatalrfgf rpdaraeaih
      241 lrylarralr tgapvreall lacsgigtsp agffsdlrrg gltlagalaa pllpralrqa
      301 lfsh
//
LOCUS       WP_284482929             197 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284482929
VERSION     WP_284482929.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..197
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=20733
     Region          40..138
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 msdpetiaiy daratdyaaq nedyvrrdpq latfiaacpa gghvldlgcg pgtssallae
       61 aglkvlatda sagmvelagq hpgvtarqat fdeiegedly dgiwasfcll hapradfprh
      121 laalrralkp ggsfaigmkl gegeardkig rlytyytrea lmthlkdagf tpvsetsvkg
      181 egldgsmaql itvicdg
//
LOCUS       WP_284482952             113 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284482952
VERSION     WP_284482952.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 113)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 113)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 113)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..113
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12392
     Region          5..79
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(10..11,15..17,30..32,41..44,46..47,50..51,53..54,
                     60..62,67)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 madpldtvfa aladptrrai lamlleddma vtdvaepfem slaaiskhlt ilsraglisq
       61 errgrvkwck lepdalraas vwmqgfgqfe pvnldaferf levelkedae sga
//
LOCUS       WP_284482984             256 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Pseudodonghicola flavimaris].
ACCESSION   WP_284482984
VERSION     WP_284482984.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..256
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26771
     Region          3..239
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mpapknsfkq aladgqklig cwmsfaegpv aeimgtagfd wlvldgehap ndlrsirdql
       61 ialsasdsqp vvrvpigeaw mikqvldaga qtvlvpmvet gdqarelvra cryppegmrg
      121 vgaaggratm fgsipdyiat andqicllvq vesraglaal ddilsvegvd gvfigpadls
      181 tdmgykgdnt apevraaiad afsrikaagk apgilgttee siqafsdmga qflavgidvl
      241 vlaqaarkls arwkqg
//
LOCUS       WP_284483042             122 aa            linear   BCT 25-DEC-2024
DEFINITION  group I truncated hemoglobin [Pseudodonghicola flavimaris].
ACCESSION   WP_284483042
VERSION     WP_284483042.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Keppner,A., Maric,D., Correia,M., Koay,T.W., Orlando,I.M.C.,
            Vinogradov,S.N. and Hoogewijs,D.
  TITLE     Lessons from the post-genomic era: Globin diversity beyond oxygen
            binding and transport
  JOURNAL   Redox Biol 37, 101687 (2020)
   PUBMED   32863222
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Bustamante,J.P., Radusky,L., Boechi,L., Estrin,D.A., Ten Have,A.
            and Marti,M.A.
  TITLE     Evolutionary and Functional Relationships in the Truncated
            Hemoglobin Family
  JOURNAL   PLoS Comput Biol 12 (1), e1004701 (2016)
   PUBMED   26788940
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Wajcman,H., Kiger,L. and Marden,M.C.
  TITLE     Structure and function evolution in the superfamily of globins
  JOURNAL   C R Biol 332 (2-3), 273-282 (2009)
   PUBMED   19281958
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Vinogradov,S.N., Hoogewijs,D., Bailly,X., Arredondo-Peter,R.,
            Guertin,M., Gough,J., Dewilde,S., Moens,L. and Vanfleteren,J.R.
  TITLE     Three globin lineages belonging to two structural classes in
            genomes from the three kingdoms of life
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11385-11389 (2005)
   PUBMED   16061809
REFERENCE   5  (residues 1 to 122)
  AUTHORS   Wittenberg,J.B., Bolognesi,M., Wittenberg,B.A. and Guertin,M.
  TITLE     Truncated hemoglobins: a new family of hemoglobins widely
            distributed in bacteria, unicellular eukaryotes, and plants
  JOURNAL   J Biol Chem 277 (2), 871-874 (2002)
   PUBMED   11696555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..122
                     /product="group I truncated hemoglobin"
                     /GO_function="GO:0005344 - oxygen carrier activity
                     [Evidence IEA]"
                     /GO_function="GO:0019825 - oxygen binding [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13109
     Region          7..117
                     /region_name="TrHb1_N"
                     /note="truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 1 (N); cd00454"
                     /db_xref="CDD:381253"
     Site            order(9,14..15,18..19,22,52..53,56,85,88,92,95,106,109)
                     /site_type="other"
                     /note="apolar tunnel"
                     /db_xref="CDD:381253"
     Site            order(23,32,35..36,39,43..44,47..48,50..52,54,62,64..67,
                     70..71,74,76,80..81,84,109,112,116)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381253"
     Site            order(25,28..29,87,90,94..96)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381253"
ORIGIN      
        1 mpqtlyekyg gfktisrivm tfyemaldsd qigdyfadvd mprlidhqtk fisslmggpa
       61 sfsddrleav hralgishad fdemaallse aladhgvgat dvglvleaie gkrgiivars
      121 aa
//
LOCUS       WP_284483098             584 aa            linear   BCT 25-DEC-2024
DEFINITION  relaxase/mobilization nuclease domain-containing protein
            [Pseudodonghicola flavimaris].
ACCESSION   WP_284483098
VERSION     WP_284483098.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..584
                     /product="relaxase/mobilization nuclease domain-containing
                     protein"
                     /calculated_mol_wt=64092
     Region          1..584
                     /region_name="VirD2"
                     /note="Type IV secretory pathway, VirD2 component
                     (relaxase) [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3843"
                     /db_xref="CDD:443053"
ORIGIN      
        1 mpddrefrir pgrirstrvq qgrpfvaqal aaakkagggv sragrvtpsn rsrfgrgqra
       61 siqanrlita rtrgavikar vvrhsgtsap lgahldylrr dgvtrdgeka rlfgpgteda
      121 dgrafaercr ddrhhfrfiv spddapdmsd lqtftrdlvg rmeqdlgtsl dwvgvdhwnt
      181 ahphvhlivr gvrndgqdlv isrdyikegm rdraralvtq elgprsdldi rrtlerqfga
      241 erwtqldrql lrdagrsril dmapdsdrqp dafhalkvgr lrkleilgva dqigqsqwhi
      301 rddaevvlre mgergdiikr mhraltdrgi ergsssyvla aesldapvig rlvqrgldde
      361 lkgtayavvd gvdgrshhir lphldaagds apgsivelrt yddargqrrv alavrsdldl
      421 aaqvtapgat wldrqaiare plalsdqgfg aevrqaldar adhltsegla eqrggrvvfa
      481 rrllgtlrdr elqavgaqls getglpfgka gagdyvsgly rqrlalasgr famiegygad
      541 gafgfqlvpw spslekhlgr nvagvargdg gvdwdfgrkr glgl
//
LOCUS       WP_284483073             269 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284483073
VERSION     WP_284483073.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..269
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29343
     Region          27..267
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          181..261
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpfdpsettd lrlvtlaqlt qgggwqlela hdraehlliw itrgqgvall dgsrrgvgth
       61 nalfiparhl malemmrngf gqalvippas gltlprsvqh lrirdvasqs eltglidalg
      121 reqsggrplr hsamraygel iaiwlrrhid dlsearpsaa hrlvqaycar lvdsygsgag
      181 madiaqemgv tpthltrvcr setgrtaaal lterilyaar rlltatdtpv qdiarhlgfg
      241 saayftrfiq qhtghtptal rraarpdtk
//
LOCUS       WP_284483079             238 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284483079
VERSION     WP_284483079.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..238
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26917
     Region          2..107
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mrdrksygqf cpvamsadll ckrwtvliir elldgalgfn eirngvplms rtllsarlae
       61 leqagllrrn lpgpgrragy qlttagqall pviqalgdwg qewiepdlai gdvdygfllw
      121 nlrksvsrlp nmpanflvrl hfvdapeghk lhwlsyagpd idichtdpgg dvdvwiecel
      181 vafaeiwmgw rpfsdalrer kiqldgpraf tedpfrwlgr srhaetrkrp paervkpv
//
LOCUS       WP_284483121            1145 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Pseudodonghicola flavimaris].
ACCESSION   WP_284483121
VERSION     WP_284483121.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 1145)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1145)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 1145)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 1145)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 1145)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 1145)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 1145)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20693118
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1145
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..1145
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=126369
     Region          1..207
                     /region_name="AAA_27"
                     /note="AAA domain; pfam13514"
                     /db_xref="CDD:433272"
     Region          <184..800
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          549..1144
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
ORIGIN      
        1 mrlqrlsldr fghftdrhfd fgsasdghdf hiiygpneag ktttmeavlr lfygfplreg
       61 yafkhprnnl qvsarldidg vlrdftrlpt rsgslvdatg tplpeaalsa hlaglseedy
      121 rrllclddet ierggeeian aegdigrllf saaagvadls tvldqvrera dalwkkrgrt
      181 thmaelkral advekeikdr dvtasawkal kkdlrkaqea erearktrda lnltkarmea
      241 qrralplmge irdleqaias fasypdhldf dperlielnr drglatqnia rlteeianlr
      301 enrdavaldp krlelstala aledlaardr taqldldrre derraaeasm kqaawdlgvt
      361 spdvdlqglv lsgadiasle sarealreai sqekiearet aelkerviaa teamqdgapa
      421 deerpqvadi llrfdaetla payaaaqqai admkikarrs laalsfagvt fdhlpacpts
      481 rhqatnwaer hqdllhdlrt ttakrdehle daeargaqak slardaklis dadaedlrar
      541 rdarwaehla aldrqtaadf heamqghdia aearlaqsre laqlreigqa eaqararaaq
      601 tdkrletlre ertnieasvs aaaaqvglpd sitaaewldw rrsheaased aqalrdteet
      661 nqstlqrada llaelartlp fpptdltgal aaarrqaedd rkqtdahtta eatlrqaqrd
      721 larreeryak afkaredtkk twralvhdll gvalpperle asleplralr ehentraaag
      781 rrittmqadq kqftqeidsl arahgqepha taaktfaalk tlaekarsat etgrkldtai
      841 etaeadlveh kdrqnaidqe vatiamlfpd tttpgdigal reaairtqka idnraalaki
      901 trqvlaelgt tdietaraql aetsvaaleg eldsnrsdla haeeeltlai qnrtaaeyal
      961 aevkgddtva elveqkatle lqleeaaleh lelslghhla sdairryrds hrsgmltate
     1021 dcfasltqga yptlstqidk eseillavdg ngvskraaem skgtrfqlyl alraaaheql
     1081 vaqgtrlpff cddifetfde artsaacrvm eaigargqai ylthhrhvve iaksvcvtpp
     1141 vihel
//
LOCUS       WP_284483143             247 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF1223 domain-containing protein [Pseudodonghicola flavimaris].
ACCESSION   WP_284483143
VERSION     WP_284483143.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..247
                     /product="DUF1223 domain-containing protein"
                     /calculated_mol_wt=26487
     Region          1..245
                     /region_name="COG5429"
                     /note="Uncharacterized conserved protein, DUF1223 domain
                     [Function unknown]"
                     /db_xref="CDD:444181"
ORIGIN      
        1 mkpiaaslta lwmlaaaplc aqqaasaaap aadpvpgpvv velftsqgcs scppadrllr
       61 eltdredvlp lalhvdywdy igwkdvfaap gfthrqkaya raagrkmiyt pqmivmgqed
      121 vvgahamela elimshmrrp vsvmigaetr ggvlhvslqp lgpvqgpldv qlvrytpleh
      181 vqiargenag rdldyanvvt dwdvlgewdg tseaqfqadl kgdspaavlv qrsgfgpivg
      241 aarvrrd
//
LOCUS       WP_284483146             236 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284483146
VERSION     WP_284483146.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..236
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25984
     Region          1..>236
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 maktdrlfrl lhlirgltpp vtaarlaaam evsdrtiyrd ietlraagar iegaaglgyt
       61 mtedpalppq tftqleieal vlglsdvqar gdaplaaaaa daltkitatl perqqrqavq
      121 ainlvhrfaq paapaiditl lreaswaeea leiryrdnag avtnrrvhpl alayldnavm
      181 llgwcclrrd frqfkvtsil avqrtgdsfr phrvpllrdy varlrrgrnp apppre
//
LOCUS       WP_284483226             136 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284483226
VERSION     WP_284483226.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..136
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14910
     Region          14..115
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mkphpnpdal pardhphcma mrdllqkiss kwttlivthl epgpkrftel krgigitqks
       61 ltaslrdler dglvervvtp tipprvdyal tplgrtllep lrvltawave kapevatara
      121 hyaartapka asrgdt
//
LOCUS       WP_284483296             370 aa            linear   BCT 25-DEC-2024
DEFINITION  C45 family autoproteolytic acyltransferase/hydolase
            [Pseudodonghicola flavimaris].
ACCESSION   WP_284483296
VERSION     WP_284483296.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   True,J.R., Yeh,S.D., Hovemann,B.T., Kemme,T., Meinertzhagen,I.A.,
            Edwards,T.N., Liou,S.R., Han,Q. and Li,J.
  TITLE     Drosophila tan encodes a novel hydrolase required in pigmentation
            and vision
  JOURNAL   PLoS Genet 1 (5), e63 (2005)
   PUBMED   16299587
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tobin,M.B., Cole,S.C., Miller,J.R., Baldwin,J.E. and
            Sutherland,J.D.
  TITLE     Amino-acid substitutions in the cleavage site of acyl-coenzyme
            A:isopenicillin N acyltransferase from Penicillium chrysogenum:
            effect on proenzyme cleavage and activity
  JOURNAL   Gene 162 (1), 29-35 (1995)
   PUBMED   7557412
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Tobin,M.B., Fleming,M.D., Skatrud,P.L. and Miller,J.R.
  TITLE     Molecular characterization of the acyl-coenzyme A:isopenicillin N
            acyltransferase gene (penDE) from Penicillium chrysogenum and
            Aspergillus nidulans and activity of recombinant enzyme in
            Escherichia coli
  JOURNAL   J Bacteriol 172 (10), 5908-5914 (1990)
   PUBMED   2120195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF040521.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..370
                     /product="C45 family autoproteolytic
                     acyltransferase/hydolase"
                     /calculated_mol_wt=39892
     Region          11..352
                     /region_name="C45_proenzyme"
                     /note="C45 family autoproteolytic
                     acyltransferase/hydolase; NF040521"
                     /db_xref="CDD:468523"
ORIGIN      
        1 mgivpkliel egparargqs ygrqadtqlr hglgvyralf qdqgmswdsv layaaelrds
       61 lvrlvpeave elagiaegan vlleevlvvn grseiinlha qrprdlstad dgctaavvlp
      121 ewteagqllh aqnwdwlpdc aestvvlqir seqgpdilty veagglarag fnsegvaitg
      181 nnlvcgqdgk apfgvplsvi rrrvleaggy sqaltelyrl prtvsnnmti scatsgdcln
      241 fettpaqiyw qapeggclth anhftspaar tremdagiar gadtlfrdrr lrrlietggq
      301 ahtldslala lddrfgsprg iirtprgneg etnaylsatv amvlmdagag emrirqlpya
      361 sdtttrfsls
//
LOCUS       WP_284483277             624 aa            linear   BCT 25-DEC-2024
DEFINITION  polysaccharide biosynthesis protein [Pseudodonghicola flavimaris].
ACCESSION   WP_284483277
VERSION     WP_284483277.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 624)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 624)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 624)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 624)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18500220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..624
                     /product="polysaccharide biosynthesis protein"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=67120
     Region          124..241
                     /region_name="FlaA1"
                     /note="NDP-sugar epimerase, includes UDP-GlcNAc-inverting
                     4,6-dehydratase FlaA1 and capsular polysaccharide
                     biosynthesis protein EpsC [Cell wall/membrane/envelope
                     biogenesis, Posttranslational modification, protein
                     turnover, chaperones]; COG1086"
                     /db_xref="CDD:440703"
     Region          284..576
                     /region_name="Polysacc_synt_2"
                     /note="Polysaccharide biosynthesis protein; pfam02719"
                     /db_xref="CDD:426938"
     Site            order(288,290..293,313..314,342..344,365..367,369,384,407,
                     423,447..450,453..454)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(314,316,320,324,340..343,346,349,367..370,373,377,
                     380,383,454..455,460)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187548"
     Site            order(369,409..411,419,448..449,455..457,460..461,
                     472..474,478,480,515,548,551)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(385,409,419,423)
                     /site_type="active"
                     /db_xref="CDD:187548"
ORIGIN      
        1 mlkllnalsr nqrgyvflai dlallplall ftymvqalpt saidtlrrtl ailpylllaa
       61 aglskllglp niqlkayerh aigltalyal gltlalallt wiagpslppg thvifgivyf
      121 lavvatrmvl lqvvtaiyrr aqprrrvliy gagttgtqla qalsahdsid pvafvddnts
      181 lqgmllaglp vhppariarl vrdrridrvv lampslsqpk qaqiarrlqk mglevqvlps
      241 faqligeeal idkltplapq sflgrkaadt dlgqasenye nrvvlvsgag gsigselcrq
      301 llncrptrlv lyelselaly tvhqeleqlt egtgvelvpv lgsvtdprqv rkvladhgvq
      361 vvlhaaaykh vplveanplp glannvfgtr tlareaaavg verfilissd kavrptnvmg
      421 askrlaelvi qdlstrasgt iftmvrfgnv lgssgsvvpl fqeqvsrggp vtvtdprvkr
      481 yfmtireavq lvlkagaiae ggevfvldmg klvpilqlar qviesagytv rdaanpegdi
      541 eieivglrpg ekleeeltlc pdligtryqk ifcareqrls eievagilrg lrqalaagde
      601 aaaraviqhg vegyapgeag lksl
//
LOCUS       WP_284483300             602 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284483300
VERSION     WP_284483300.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..602
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=65907
     Region          19..546
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 meraemhdtp ktdtraggdp ilrieeleis fgptsvvrgv dlalrrgeil alvgesgsgk
       61 smigrailgl lpepgrvsrg rirfdgheit apsspeelrl lrgrsiglif qeplsslnpt
      121 mkigpqmfea mrlhtdltea qiraraldml rqvrldrpea lldryphefs ggmrqrimia
      181 svmmlkpall iadepttald avvqrevldi meevarangt svilishdla vvaryaerva
      241 vmekgdlvet gttravladp qhaytrrlla aaelgapdpv agragapllr venlsvdfre
      301 kkvlglfget vhhavrdvsl tiapgefvgl vgesgsgkst igraickltp kaagrvvfdg
      361 qpldqigage erhlrqrirv vfqdpvssln prmrigrivr eglrhdrsls dterqqaaer
      421 mleavglsrd maarfphals ggqrqrvaia raliarpdli iadepvsald vtiqaqilal
      481 lkrlqadygf aclfishdlh iveqlcarly vlhkgrlmee aatpalfasp rhpytrrlls
      541 asprlergek gvhlaehilp giagddlayy damrpeepyr lidlgaghrv airgeqagpp
      601 vr
//
LOCUS       WP_284483373             356 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease, partial [Pseudodonghicola flavimaris].
ACCESSION   WP_284483373
VERSION     WP_284483373.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         <1..356
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          <42..215
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 eadsdpmgyh rrnllpdrhg dhlgrpyase vtcglnravt nhrdhtllai eepeahlhph
       61 lqrsvyrhlf qsvdnpdqqk qmsvlltshs phiasvaplr silllkektd egttgcstas
      121 irltddevdd ltryldvtra emlfargiil vegdaekflv plfaealgcs ldmlgitvcs
      181 vagtnftpya kfltsldipf siitdwdpmp kskplavsrg iklavaiera rtkkiprala
      241 kelediaenk deddlagrfe dlgiytnirt letdlyedgf aadildtlne gkwskarqaq
      301 idawiadhds idhnqmlkli dvvgkgrfaq rlaskiegrk ppryiedair yvvnrv
//
LOCUS       WP_284483419             265 aa            linear   BCT 25-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Pseudodonghicola
            flavimaris].
ACCESSION   WP_284483419
VERSION     WP_284483419.1
KEYWORDS    RefSeq.
SOURCE      Pseudodonghicola flavimaris
  ORGANISM  Pseudodonghicola flavimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudodonghicola.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Bagautdinov,B. and Kunishima,N.
  TITLE     Crystal structures of shikimate dehydrogenase AroE from Thermus
            thermophilus HB8 and its cofactor and substrate complexes: insights
            into the enzymatic mechanism
  JOURNAL   J Mol Biol 373 (2), 424-438 (2007)
   PUBMED   17825835
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Pseudodonghicola flavimaris"
                     /db_xref="taxon:3050036"
     Protein         1..265
                     /product="shikimate dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27332
     Region          3..262
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 mitgqtrtlv iladpiahvr tpqvlnprle aegvdavlvp levppealea alrglagarn
       61 fagavitlph ktavpalcda lsdraaaaqs vnvvrrrrdg slygdlldge gfvrgfeqtg
      121 vtlcgkrvfl agaggaasai afalagrgva altianrsaa kagaliarls arfpdvafta
      181 aadpaghdia ingtslglrp gdalpfdpdr ldpgtlvaev imqpattall raatargltt
      241 hpgrhmlegq ltellrflth eedek
//
LOCUS       WP_284483453             424 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Sedimentitalea xiamensis].
ACCESSION   WP_284483453
VERSION     WP_284483453.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..424
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44952
     Region          9..424
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mtaagsdvil ermmalhpki idltldrvwr llaalgnpqd amppvihvag tngkgstlam
       61 iragiegagl sahaytsphl arfherirva gtligeaelt avldecytan ggdpityfei
      121 ttcaallaft rtpadftlle vglggrldat nvcpvpaltv itpvsmdheq ylgdtlaria
      181 fekagilkrg vpcivgpqep eaqdaiedva arvgapllch gqhwhvarer grlvyqdetg
      241 lrdlplpnll gehqvfnaga alaalrhlgl gddayeaavt raewparmqr ivrgplarsa
      301 pevelwldgg hnaaagialq kvlselpkrp tylicgmlnt kdvtgylrpl aaevegltav
      361 sipgesntlp seataraars vgmradeaes vaealrriae qapqarvlic gslylaggvl
      421 rdng
//
LOCUS       WP_284483519             390 aa            linear   BCT 25-DEC-2024
DEFINITION  thiolase family protein [Sedimentitalea xiamensis].
ACCESSION   WP_284483519
VERSION     WP_284483519.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 390)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..390
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40306
     Region          1..390
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mkevviagaa rtpmggfqgv fdgvvaadlg ghavraalrd agaktvdell mgcvlpagqg
       61 qaparqagfa aglgedvpat tlnkmcgsgm kaamigfdqi algqsdvmav ggmesmsgap
      121 yllpkmrgga righaqvidh mfldgleday dkgrlmgtfa edcaeafqft rdaqdqyala
      181 slsnaldaer sgafadeitp itlhtrsgea iittdeqpgk arpekipmlk pafrkdgtvt
      241 aansssisdg aaalvlasae taearglsvr arilghasha qapalfptap vpaarklldr
      301 igwhkddvdl weineafavv pmafmreigl prdivnvngg acalghpiga sgarimvtll
      361 nalekrnlkr gvaaiciggg egtaiaieri
//
LOCUS       WP_284483674             200 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Sedimentitalea xiamensis].
ACCESSION   WP_284483674
VERSION     WP_284483674.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..200
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=21818
     Region          3..200
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 marlelrgag ifkgflpppe qariveevrq ilraaplfap qtslgrpmsv rmssagrfgw
       61 ysdragyryv thhpggaawp dipagilriw devtglsrqp ecclvnwyge garmglhqdr
      121 deadfswpvv svslgddglf rigsrtrggk tesvwltsgd vvvmggaarl ayhgvdrirf
      181 gssrllpagg rinltlrvvt
//
LOCUS       WP_284483807             327 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Sedimentitalea xiamensis].
ACCESSION   WP_284483807
VERSION     WP_284483807.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..327
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35443
     Region          59..320
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mflsnlrfgv alagallsta afadplpswn dvdaksrita fvesvtdpqg dsyvtpgdrv
       61 avfdndgtlw aeqpayfqlf famdrvsqla eadpsiltsd vlkaaaagdl kgvfadgekg
      121 llevinlshs gmsvdafisd vqgwldtarh petgmafdqm iyqpmlells ylrdegfety
      181 ivsgggvhfi rafaetayni ppeqvigsat ktsyqivdgv plvvkepgia fvddkagkpv
      241 gidskigkrp ifvsgnsdgd fqmlewatag egprfglivh htdsareyay drdshigqla
      301 rgldegperg wlivdmardw ariwpae
//
LOCUS       WP_284483786             609 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Sedimentitalea xiamensis].
ACCESSION   WP_284483786
VERSION     WP_284483786.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..609
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67716
     Region          15..609
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 memsrvdive ylnfdgheti tslwadrcar ygdrvahrqk elgiwqaysw rdyyesarki
       61 gralmrlgvq kgepvlilse drrewlyidl gaasigaipa gvyttdspsq laylagdsga
      121 rtlfvendeq ldkylearad mpgietvvvl drdglahfsd pqvmfledly amgeaeerhe
      181 pgrfeeamka irpedprmli ytsgttgppk gamithrnmi fqlragrevl efhetdnllc
      241 flplchvler lvsveapian gcivnfaesp etvfdnlqev spnsfsgvpr iwekiysrvm
      301 ilrseagrvg twafdwalai gdryaraeap gpglrlahfi advtvlsnlr rmlglanarr
      361 vtsgaapisp dlihwfaalg vpmiegygmt etagiatint vehnligtvg palpgvemri
      421 detgelmigg pcvfggywnk pektaeaitc dgwlhtgdvg rigndgalti tgrlkdiiit
      481 aggknitpae iesklkfspy isdavvigdr rryltclimi dqenvekfaq drqipfsdfa
      541 sltragevre ligsvvsdtn khfanveqlk dfrlidillt aedeeltptm klkrnfvnqr
      601 haalidemy
//
LOCUS       WP_284483852             262 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Sedimentitalea xiamensis].
ACCESSION   WP_284483852
VERSION     WP_284483852.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..262
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=26974
     Region          1..261
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mysfevdkpg sveaavaalq ieeamalggg qtliptlkqr laspsrlvsl agiaemkgvs
       61 avdgvvtigg gtphatvare aagaypalaa lagnigdpav rnrgtiggsl anndpaacyp
      121 saalasgati vtssreiaad dyfqgmftta lhegeivtav rfpvpqaasy qkfeqpasrf
      181 alvgvflarf aegvrvavtg asedgvfrws eaeealnkef radaltglai apenmiadlh
      241 gtkeyrahlv svmtkraira vg
//
LOCUS       WP_284483877             211 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Sedimentitalea
            xiamensis].
ACCESSION   WP_284483877
VERSION     WP_284483877.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 211)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..211
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=22146
     Region          26..206
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtqlalitga srglgaalae alapshhiva varttgalee lddrikaagg satlapmdit
       61 dpkamqtlcr gihdrwgkld iwlhsaihaa mlcpanfvds kdwdksiain atatsvlipy
      121 vapllgpegq avffddprag dkffgiygat kaaqialaks waaetvktgp kvrvltpapm
      181 ptatrarffp gedrtalarp aeeaarllal l
//
LOCUS       WP_284483886             223 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Sedimentitalea
            xiamensis].
ACCESSION   WP_284483886
VERSION     WP_284483886.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 223)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..223
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24199
     Region          1..>218
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mprtdrlidi iailrdgrlh ragdlagrlg vsirtiyrdm drlaasgvpv qgtrgtgyra
       61 adritlpplt ltpqeldaln igvaivaeaa dpylkaaala ltdkldavlp aetvaeadaw
      121 ktaltpladt arglshmasl rsaikgkqkl rltcrdpggt rttrtvrplk ldnwghvwil
      181 tawcelcadf rdfridlida asplpelfvd epgkrlpdrp lrg
//
LOCUS       WP_284483977             121 aa            linear   BCT 25-DEC-2024
DEFINITION  HesB/IscA family protein [Sedimentitalea xiamensis].
ACCESSION   WP_284483977
VERSION     WP_284483977.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Lu,H.M., Li,J.D., Zhang,Y.D., Lu,X.L., Xu,C., Huang,Y. and
            Gribskov,M.
  TITLE     The Evolution History of Fe-S Cluster A-Type Assembly Protein
            Reveals Multiple Gene Duplication Events and Essential Protein
            Motifs
  JOURNAL   Genome Biol Evol 12 (3), 160-173 (2020)
   PUBMED   32108236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..121
                     /product="HesB/IscA family protein"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=12841
     Region          9..110
                     /region_name="IscA"
                     /note="Fe-S cluster assembly iron-binding protein IscA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0316"
                     /db_xref="CDD:440085"
ORIGIN      
        1 mfgipgkqav tltpkaaaqi tklmaskghs glrigvkkgg cagmeytmey vqatdpndei
       61 veqdgarvli apmaqmflfg teidyetsll esgfkfnnpn vseacgcges ikfnempans
      121 k
//
LOCUS       WP_284483978             304 aa            linear   BCT 25-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Sedimentitalea
            xiamensis].
ACCESSION   WP_284483978
VERSION     WP_284483978.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..304
                     /product="isopenicillin N synthase family dioxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33460
     Region          2..301
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 mipeldlrnl lrrdpgemsv laravqevgf ltvsgtdlts drvervlday raffrlpddd
       61 kravdmartg anrgwgapks eqvdpdanpd fkevfdcgye lpdrhpfekr nlgvyapnqw
      121 pekplgfrae ieayyseais vgreilsais dalgqssasf adafdppmal lrgnfysarp
      181 ewagdkdfgi aahtdygclt llamdgapgl evrmpdgrwe piiaapgtfv infgemlemw
      241 sggrikatlh rviggaweri svplflnpay dtnvappgsg qiilagehls rrfnetylhl
      301 ktag
//
LOCUS       WP_284483999             300 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Sedimentitalea xiamensis].
ACCESSION   WP_284483999
VERSION     WP_284483999.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..300
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=32775
     Region          57..293
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mktsirgvll slalgwsgat aglarcadhv pqpkpqnadr divgadldti rdrgfmtfav
       61 yedfppwsyl drgkpsgidi diarliaedi gveprfdlva agenldadlr nwvwkgpvvg
      121 gqvanvmmhv pydsefacrv eqvvftgqyh veeiaiayrr daypddppvp ayfrfdtvgv
      181 endsiadfyl safpggqlae nvtrypsvql amqglaeaat kaamgpkaql efgltpdldl
      241 happlpgfsv gswtvgvavh fayrplayav ddaifaamqd grmqrifddh gvtfrppelr
//
LOCUS       WP_284484126             354 aa            linear   BCT 25-DEC-2024
DEFINITION  HesA/MoeB/ThiF family protein [Sedimentitalea xiamensis].
ACCESSION   WP_284484126
VERSION     WP_284484126.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..354
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37136
     Region          101..347
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mglvlllaal iwglgvlmgt prrprfilia vlfgvvllaq lalpdghpir qatgkspalw
       61 lmlaaaaala vvygrmvgal rrragvrqas seqappkaaf sdseldryar hivlreiggp
      121 gqkrlkqarv lvigagglga palqylaaag vgtigviddd vvenanlqrq vihrdrdigm
      181 pkvfsaqaam qaqnpavtvr pyhrrltaei aadlfadydv ildgtdnfat rylsnatava
      241 agkplisgal sqwegqlsvf dparsgpcyq cifpeapapg lapscaeagv igplpgviga
      301 mmaveaikvv tdagtplrgq mliydalyge trtirlkara dcpvcgatar gpdr
//
LOCUS       WP_284484127             402 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Sedimentitalea xiamensis].
ACCESSION   WP_284484127
VERSION     WP_284484127.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..402
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=42595
     Region          8..402
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mnrrnttygp mttaihaged pdpttgasap aihmsstfvs qdvsgfsahd ltpdspyaya
       61 rwanptttml eakiaamqgt edclatasgm aaasaifftf lsagdhavis dvsyagvgel
      121 ardtlprlgi evsmvnmsdl navaaairpn trlvhsespv npiirltdla avsklahdgg
      181 aihstdatfa splgmdtgvl gidlvmhstt kyvgghgdav ggavagrsdl irrmrleasi
      241 hhggilspfn awliargast lplrmkahaa gaqavaewle thpavtrviy pglkshpqhd
      301 laqrqmtncs gmlsfqvgda atgqriaqqm idrfevihya vslghhrslm fwmeteglmq
      361 tsfrltgaaa edyrayagdg ifrlsvgled addlitdldr al
//
LOCUS       WP_284484517             284 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Sedimentitalea
            xiamensis].
ACCESSION   WP_284484517
VERSION     WP_284484517.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..284
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30800
     Region          117..267
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 msaanpspns yraapksvsg lfeivaimcq lsqgniapae alrrmtgllg teataicrvd
       61 lrsardattv ishearryhs edvgrldmsf argickdnig taitgsvwsg taedfgdrdp
      121 lalvfrhrrl aetvviplar qgssgdflel hfgdpvsagl lshleflgpv ladcwkartl
      181 glfsdmllsr rrvrshptar aailamenpc rlsraeyrvc lllsrglnnq svlsalsitm
      241 atlrthlrni yaktgtasqp elihlllnpa prrgtrdedd adva
//
LOCUS       WP_284484319             367 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Sedimentitalea xiamensis].
ACCESSION   WP_284484319
VERSION     WP_284484319.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..367
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=37895
     Region          28..342
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mirdrignmk elpmqsdldr aldfagflgi eapillapma gacppslsaa vaagggfgac
       61 galllspeqi agwasemrrs snggfqmnlw ipdpepardp areaelrefl gqwgpdvpdd
      121 aadapmldfa aqcqamldas pravssimgl yppefvarlk ergilwfatv ttvaearaae
      181 aagadvivaq gmeagghrga fnasdarsam vglfallpav vdavrlpvva tggiadarai
      241 aaalllgasg vqigtgflra peagtnpvwa dalgrtaped tiateafsgr lgrairnayt
      301 vaadgapapa pypvqralta pmradaartg ridsmqawag qsaaqalaep aarivtrlwr
      361 etctrlg
//
LOCUS       WP_284484786             360 aa            linear   BCT 25-DEC-2024
DEFINITION  two-component system sensor histidine kinase NtrB [Sedimentitalea
            xiamensis].
ACCESSION   WP_284484786
VERSION     WP_284484786.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 360)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 360)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..360
                     /product="two-component system sensor histidine kinase
                     NtrB"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009399 - nitrogen fixation [Evidence
                     IEA]"
                     /calculated_mol_wt=38419
     Region          5..356
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 mtsdssiwas lpipaflidg ndniadvnsa gegflnasak svigtpiwdq vaidapieea
       61 fgrarkngtp lfvndidvgs gsraplqcal qiapllghpg tmilmispre lagrmtqshs
      121 vksaaqsaig maemlaheik nplagitgaa qllsmnlspe dleltdlivt esrrivklle
      181 qveqfgnlse psfkpvnihd vldrarrsal lgfgahmkiv edydpslpla ygdpdqllqv
      241 ilnllknase aadpkggtir ihsyfehsfs lrradgsgqs lplqveiidd gpglpdkira
      301 dvfdpfvsgr dngtglglal vskiisdhhg wisvtsvpgh tvfrlslprv prglnpeets
//
LOCUS       WP_284484829             158 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Sedimentitalea xiamensis].
ACCESSION   WP_284484829
VERSION     WP_284484829.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..158
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17845
     Region          30..150
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mtlryhspls peeqidfglt apqpaaladr vryaeldvln hvnnksymgw fetlrvayfd
       61 mfcaryyagq plprtvlrna dmrfikemlm gedyvatarv tafrnssytv hqelwagdlr
      121 atltgvmvml hpdgsgrwpl pdglrrhfae sdgavaes
//
LOCUS       WP_284484984             159 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Sedimentitalea xiamensis].
ACCESSION   WP_284484984
VERSION     WP_284484984.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..159
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16753
     Region          5..143
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
     Region          70..>138
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mrdasirtat rgdlprlhda lcrlsadlgd vhradlaale qagfgarasf raalalrgdt
       61 tvgalvaspl fsttlggsgl fvsdlwvape ergqrlgqrl lafaagmqva ggaqfiklav
      121 yrdnpeaerf yrrlgfvpgp setslrlsga alenlkgqt
//
LOCUS       WP_284485047             263 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Sedimentitalea xiamensis].
ACCESSION   WP_284485047
VERSION     WP_284485047.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..263
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=29726
     Region          19..262
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 madatfqddt lsvadriaae alivdvdgfe gpldvlltls rtqkvdlrri svlqlaqqyl
       61 gfverakslr ielaadylvm aawlaflksr lllppdpted gpsgeelaah lafqlerlqa
      121 mrdvaarlmg rdrlgrdffa rgqgedvtri rtlrytatll dlmqgyarir trddfrpfvm
      181 drdsvftmeq alermrplig fagswtdlts yfpegwdgdp vrrrsataat faaslelvke
      241 ghleirqsdt fapiqlrrkd erq
//
LOCUS       WP_284485052             107 aa            linear   BCT 25-DEC-2024
DEFINITION  HesB/IscA family protein [Sedimentitalea xiamensis].
ACCESSION   WP_284485052
VERSION     WP_284485052.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Lu,H.M., Li,J.D., Zhang,Y.D., Lu,X.L., Xu,C., Huang,Y. and
            Gribskov,M.
  TITLE     The Evolution History of Fe-S Cluster A-Type Assembly Protein
            Reveals Multiple Gene Duplication Events and Essential Protein
            Motifs
  JOURNAL   Genome Biol Evol 12 (3), 160-173 (2020)
   PUBMED   32108236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..107
                     /product="HesB/IscA family protein"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=11183
     Region          6..107
                     /region_name="IscA"
                     /note="Fe-S cluster assembly iron-binding protein IscA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0316"
                     /db_xref="CDD:440085"
ORIGIN      
        1 mklppkvter afarlaeiga sdrgqalrva vegggcsgfq yeialdtpae ddlvlegmgq
       61 kvvvdtislp flenavidfs eeligarfvi dnpnatsscg cgtsfsm
//
LOCUS       WP_284485057             279 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Sedimentitalea xiamensis].
ACCESSION   WP_284485057
VERSION     WP_284485057.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 279)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..279
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31966
     Region          2..235
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mkfqgtkeyv atddltiavn aavtlerpll vkgepgtgkt elahqvadal glrmiewnik
       61 sttraqqgly eydavsrlrd sqlgeekvhd vrnyikkgkl wqafeaedrv vllideidka
      121 diefpndllq eldkmeffvy etsetikarq rpiviitsnn ekelpdaflr rcffhyirfp
      181 deitmrkive vhhpgikeql lttaltqfye lrdtaglkkk pstsevldwl klllaedlsa
      241 edlkrdgana lpklhgallk neqdvhlfer lafmargqr
//
LOCUS       WP_284485074             405 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Sedimentitalea
            xiamensis].
ACCESSION   WP_284485074
VERSION     WP_284485074.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..405
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44456
     Region          13..393
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 milppnvhda epippaarda iddlmlsgdl frytapkdap valleaefar migskyalav
       61 sscsaalfls lkalglprda rvlipgftfa avpsaivhad cvpvlcevgd nfridladfe
      121 trldqdisav iishmrghts dmdaimdlcd argipmieda ahslgttwrd rnigtigrig
      181 cfsfqsykml nageggilit ddadlvarav imsgayehnw kkhkgphgen tpdlelafar
      241 wqnelplynm rmsnltaavi rpqipelarr vrdgrknhdh vaarlngspy lsvppalpqe
      301 srapdsiqfn lvglsdsetr afaeaadarg lkvqifgmse dnarafwnwr flpdrpdlpk
      361 tramlmracd arlpvrltra eldviadivl qaidqvmhpa rtygt
//
LOCUS       WP_284485077             604 aa            linear   BCT 25-DEC-2024
DEFINITION  PHA/PHB synthase family protein [Sedimentitalea xiamensis].
ACCESSION   WP_284485077
VERSION     WP_284485077.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..604
                     /product="PHA/PHB synthase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=67651
     Region          47..597
                     /region_name="PhaC"
                     /note="Poly-beta-hydroxybutyrate synthase [Lipid transport
                     and metabolism]; COG3243"
                     /db_xref="CDD:442475"
ORIGIN      
        1 mtttqdsape lsgehierlt enlgkieals krlidvmtrk tghnaalngp kqdlfakaaq
       61 aywtqafqnp skiieqqvey wgkslkhfae aqetlakgkf qapedpgpkd rrfanplwds
      121 hpyfnfikqq ylinadaikq avdsvedmda kekqrltyfa tqivdmmapt nflatnpdal
      181 ekaletegqs lvdglenlis dleanngelv vrladekafe lgnniattpg dvvyrnkmme
      241 liqykpatdt vhevplvvfp pwinkfyild lkaqnslikw iteqgytlfv vswinpdsky
      301 adigmedyiq dgyltairev ksicnvkqvn aigyciagtt lamtlsllkq rgdksvksat
      361 fftaltdfgd qgeftpfltd dfidgiqaev edkgilpsfi martfsylrs ndlvytpair
      421 symmgeappa fdllywngdg anlpakmtlq ylrglcqenr ftqdgfdllg htlkvsdvdv
      481 plcsvacetd hiaawkdcyr gvqmmgsqsk tfimtqsghi agivnppsrn kyghytnedl
      541 sgdpkawldg adfhegswwp rwerwlmdrs gkkipardig dsdhpslapa pgtyvrmkas
      601 agkr
//
LOCUS       WP_284485115             320 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Sedimentitalea xiamensis].
ACCESSION   WP_284485115
VERSION     WP_284485115.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..320
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34640
     Region          1..319
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mtitkrmfvk lagatalagl iagpaaawep tkpvdfvima gagggadqia rfiqsvaekk
       61 dltnrplvpn nkgggsgaea lialngagdp dhtilvtlns ffttplrqen lgidvqtftp
      121 vammgvdpfv lwvhkdsgit tfeqwleevk kgdyvmggtg kgqedslvit yleqafdldi
      181 kyipykggga vakdlagkqi matvnnpaet kgfyaagdvv pllsfsderm pafpdvptlk
      241 ekghdfsyyn qravvgapgq seeaaayyqd lfktiyesqe wqdymasesl splwlspdeq
      301 kaywqtqvdr hkellaamge
//
LOCUS       WP_284485173             232 aa            linear   BCT 25-DEC-2024
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Sedimentitalea
            xiamensis].
ACCESSION   WP_284485173
VERSION     WP_284485173.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439579
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..232
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26025
     Region          4..218
                     /region_name="PssA"
                     /note="Phosphatidylserine synthase [Lipid transport and
                     metabolism]; COG1183"
                     /db_xref="CDD:440796"
ORIGIN      
        1 mtlsmrallv hlftatgavf amlamlaaae tkwslmflwl vvaffvdgid gplarryhvk
       61 hyapqfdgvl ldliidylty vfipafalfq sglmdgwtgw vaiivitfas amyfcdtrmk
      121 tkdnsfsgfp gcwnmvvlvv falepnfwvi lalvtalsia mflplkfvhp vrterwravt
      181 lpmalgwtff agwaawvdfh peswahwgli vtsvylvfag iaqqiiplpd ad
//
LOCUS       WP_284485343             239 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Sedimentitalea
            xiamensis].
ACCESSION   WP_284485343
VERSION     WP_284485343.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12044921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..239
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26992
     Region          20..162
                     /region_name="Autoind_bind"
                     /note="Autoinducer binding domain; pfam03472"
                     /db_xref="CDD:427319"
     Region          <174..237
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mattvnldqi lenldatsal eglqeiteal rdafqvdhiv yhwvdsagdq ygcgtysdew
       61 rnryleqsyh ridpviagcf qrfhpvdwkr ldwsskaarh flsealkygv gnqgfsipir
      121 gpngqfalft vshncsdetw skfteehsrd liliahyfnr kalefepgrq peksralspr
      181 evdamtllam gysraqvaea lsisehtlrv yiesarfklg alntthavar amsrglivv
//
LOCUS       WP_284485380             515 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Sedimentitalea xiamensis].
ACCESSION   WP_284485380
VERSION     WP_284485380.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 515)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..515
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=56370
     Region          <74..500
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mmnplsgqlt rfrnrivpvl tgppvlaflp avtlaafwlg gekalvmlal glpllfalag
       61 afgrwpngtg vprdsvtgll lrdgfdtvvr qvyedtetsg lrsacfilel ddyretvdry
      121 gltaadsivq rsgerilsal rdgdtvarig dsrfaiclma vrqldlelci qlsgrlqsev
      181 eepisldgms vytscsigfc lrsrapgktg qdwmnaataa ladanntgps airaysaeiq
      241 rktkarndlr dnaaaaleng qiqpwyqpqi stdtgkvtgf etlarwlhpv hgmiapdvfl
      301 pamqeaglme rlgqvmlyha ltalkawdsa gmdvprvgvn fatdelrnpr lvdkirweld
      361 rfelspnrls veiletvvtd npddtvtrni agladlgcri dlddfgtgha siasirrfsi
      421 srikidrsfv mkadrdpeqq rligailtma erleletlae gvetvgehal laqlgcdhvq
      481 gfgiarpmpf dqtldwitsh vaklqdapki grdvi
//
LOCUS       WP_284485547              85 aa            linear   BCT 25-DEC-2024
DEFINITION  BolA family protein [Sedimentitalea xiamensis].
ACCESSION   WP_284485547
VERSION     WP_284485547.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..85
                     /product="BolA family protein"
                     /calculated_mol_wt=9315
     Region          1..83
                     /region_name="BolA"
                     /note="DNA-binding global transcriptional regulator BolA,
                     affects cell shape, cell division and biofilm formation
                     [Transcription, Signal transduction mechanisms]; COG0271"
                     /db_xref="CDD:440041"
ORIGIN      
        1 msvteeirtr lqsafapsvl tvvddserhr ghagyrdgge shfnvtirad afrdqsriqr
       61 hravhsalgp elvgrihals ldidg
//
LOCUS       WP_284485562             317 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Sedimentitalea xiamensis].
ACCESSION   WP_284485562
VERSION     WP_284485562.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..317
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33574
     Region          7..316
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mriikglalg ailgtlgasa tlaeefpekp irfvtpyppg gshslhagii ttvaeayfgq
       61 pmisviragg ggvvaaaela qgdadgysvl fgdptinslr pqvedlpydi dafvpvarin
      121 yspavfvaaa dapfddldgm iayakenpdk liyssdnkng ftyvafemlk lktgtqmkgi
      181 efggggpaia qvlggntmay agapsvvgdh ieagtlkaic atdlerwekl pdvptcqeag
      241 vdivwhfwrg vlaragtped rvqmmsdafg klvedegflr lintinsrvg yldaeafgel
      301 lareqkdlke lydaigg
//
LOCUS       WP_284485703             329 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Sedimentitalea xiamensis].
ACCESSION   WP_284485703
VERSION     WP_284485703.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..329
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36082
     Region          9..317
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 msandaisdl kkrmaqsiig qtdvidrlvi gllangnllv eglpglaktr aikamarnld
       61 akfsriqftp dllpsdvtgt eiyhqaggea efrfepgpif anivladein rapakvqaal
      121 leameerqvt vagtthkmdp lfivmatqnp ieqegtyplp eaqmdrflmh vnityppved
      181 evevirlvrg eeiaaqadaa npseaekpap irqqavfdar teigqvhtsd amdrymadlv
      241 qatrtpaald edlarwisvg aspraslald rcsrahawma grdyvdpqdv raivhdvfrh
      301 rislsfeaqg edrrtddvtd aivrlvalp
//
LOCUS       WP_284485708             453 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Sedimentitalea xiamensis].
ACCESSION   WP_284485708
VERSION     WP_284485708.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 453)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 453)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 453)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..453
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48138
     Region          123..448
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mserlapllr smplrlalgl vvlfsvisli slaasflvtq rsfeqamrad ltqrmagfra
       61 apnatavaal vkaearvtdp ermvlsylap nrshfgnaai arddegyhiv sldqdspdlk
      121 grylaltavl hggqltiars rseiealrgv flnilglslv ptilialsgg lylahrgarn
      181 vnaiagtldr ltngdlqarv gmvegwsgdl adiadridqm araqeasvaa irqvssdiah
      241 dlktpiqrvs vhlqdlsdss dlptdarrhl esaqkeleai gsvfgsllqi aqiesgspks
      301 gfapvdlael lrtcadlygp aaaetghdvt teispdvplv sgdrnllmql lanlvenamr
      361 htpdgtqirl slafrdgsav lgvsdtgpgi psaetdnvlq rlyrldqsrg tpgsglglnf
      421 vsvvarlhda alhlddnapg lrvsltfppa qts
//
LOCUS       WP_284485717             379 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Sedimentitalea
            xiamensis].
ACCESSION   WP_284485717
VERSION     WP_284485717.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..379
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41142
     Region          4..379
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mngiqkaldk svaaqdvpfa vgmvgnadgi tfsgaageaa agrpaaedta frifsmtkai
       61 gslaamilid rgkmrmdtpv gdilpewndl rvlegfdgdt pvlrapktva tarhlathts
      121 gmeyefwnad vpkymeltgh psvlsglkas lnyplttdpg trwgygpsid wlgrmveavd
      181 grridafcsa eifeplgmad tafepdalqd rlctvrmrge dggfgpfela ppphpevygm
      241 ghalystapd ymrflrmvln rgqldgnrll sedsfdemla nqmrgltfqt mktsappvsa
      301 dvelppgsth sfiavrtetd ipgkrsagtq swagvcnthy wvdpkknlaa vimtqslpfg
      361 eprfmqtyda yeravyaal
//
LOCUS       WP_284485747             467 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Sedimentitalea xiamensis].
ACCESSION   WP_284485747
VERSION     WP_284485747.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..467
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=51759
     Region          56..435
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mpdgsiplsw pkasydpkyd piqdagpghn repaptywig tggtapeddg pvtadmeadv
       61 vvigsgytgl staihlakdh gmqpvvlean svawgcstrn ggqaqissgr lkrsqwikrw
      121 gvdvargmhr evseafdlfn hliadddinc dpqpgghyyi ahrdkvmagl ksecavlnet
      181 fgygakilsr eelhenhvrd qeaagalwep dgtcihaakl aygylrmarr lgarvhtasp
      241 vmgwqqqgdw hylrtpggiv ktksvtiata gytpvglhkr tkhrlmpils nsmvtrpltq
      301 seldecgikv tspltdtrtl rhyyrllpdn rvqigsrsal tgrdaenekh lnllrkglar
      361 kfpaldgisl dyswwgwvdv shdmmprivq pdprtrifya mgyggngvmy saqagrrmaq
      421 lvagkkteaf dlpiftsplp shgvltpfrr lgqrfaylwy ylndevi
//
LOCUS       WP_284485988             290 aa            linear   BCT 25-DEC-2024
DEFINITION  dimethyl sulfoxide reductase anchor subunit family protein
            [Sedimentitalea xiamensis].
ACCESSION   WP_284485988
VERSION     WP_284485988.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..290
                     /product="dimethyl sulfoxide reductase anchor subunit
                     family protein"
                     /calculated_mol_wt=30720
     Region          1..286
                     /region_name="DmsC"
                     /note="DMSO reductase anchor subunit DmsC [Energy
                     production and conversion]; COG3302"
                     /db_xref="CDD:442531"
ORIGIN      
        1 mhpapsvilf ttcsglgfgl lvwlgigfpa vtgrvafvff aiayllaagg liastfhlgr
       61 peralkaftq whtswlsrea wcavaaltlm alygaglvfl gtawpvvgla galaslatvf
      121 ttsmiytqlk tvprwhtvlt pllflaisvs ggalmagqtg lapwllllag ivqvavwlrg
      181 dgafdasgtt lasatglgei gtvrafesph tgtnyllref vhvigrkhar klrmisltlm
      241 tvlpvillll pfghvlaala vlshlagvav srwlffaeae hvvglyygkr
//
LOCUS       WP_284486055             602 aa            linear   BCT 25-DEC-2024
DEFINITION  ABCB family ABC transporter ATP-binding protein/permease
            [Sedimentitalea xiamensis].
ACCESSION   WP_284486055
VERSION     WP_284486055.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 602)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..602
                     /product="ABCB family ABC transporter ATP-binding
                     protein/permease"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66200
     Region          2..602
                     /region_name="ATM1"
                     /note="ABC-type transport system involved in Fe-S cluster
                     assembly, permease and ATPase components
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5265"
                     /db_xref="CDD:444078"
ORIGIN      
        1 msvtdtpiad dqrrsgwrti rrvspylwpd dqpwvkrrvv lalamlvlak liavgtpily
       61 keavdslake gvptlalgav gltvaygmar lmtvgfqqlr davfapvgqr alrrlaletf
      121 ahihrlslry hitrktggls riiergvkgv dfllrfllfs vgplilelal vgiiltvlfd
      181 iwylvivsvt iafyvwftfa vtewrvqlrr emndqdtdan qkaidsllny etvkyfgaea
      241 reaarydram qgyeraalkt ayslaflnfg qslfitagli gvmvlaalgv qsgtltvgdf
      301 vmvnaymiqi tvplnflgtv yreirqalvd mgemfdlleq paevtdrpda pdlrvsggei
      361 rldnvhfgyd pnrdilkgvd ltvpagrsva ivgatgsgks tigrllfrfy dvtggallid
      421 gqdlravsqd slhaaigvvp qdtvlfndti ryniaygrdg atqeeieqaa rdaqihdfia
      481 glpdgydttv gerglklsgg ekqrvgiart llkdppilll deatsaldsd tereiqgala
      541 ragegrtvit iahrlstiad adqivvlheg eivergthdq llarggryan lwnrqqsdrd
      601 aa
//
LOCUS       WP_284486110             444 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Sedimentitalea
            xiamensis].
ACCESSION   WP_284486110
VERSION     WP_284486110.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..444
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=48673
     Region          3..437
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 maqamkiaiv ddeqdmrqsi sqwlalsgyd tetfasaeda lkalgpeypg ivisdikmpg
       61 mdgmqflkkl mgtdsalpvi mitghgdvpm aveamrvgaf dflekpfnpd rmsalakrat
      121 garrlvldnr alrrelsdgt qlmnkligas pamerlkedi ldlgqadghv lidgetgtgk
      181 tlvahalhav gsragkkfvl iscaaleeda lakrlfgpml pedeqlpaie earggtlvle
      241 diealsetmq akllsvineq gtpaetriva isnlqeagrt sedvlrpdlf yrlaalritv
      301 pplrqrgedi ltlftrlseq fadeygceap kvsaqeaaql lqapwpgnvr qliniaerav
      361 lqsrrgsgti asllmsdhde mqpvmttegk plkeyveafe rmlidntmrr hkgsiaavmd
      421 elclprrtln ekmakyglqr sdyl
//
LOCUS       WP_284486170             437 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Sedimentitalea xiamensis].
ACCESSION   WP_284486170
VERSION     WP_284486170.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..437
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46797
     Region          22..432
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 msrifgfila lilalpaaaa vqveevtsps gidfwlvedh sipfvamdlr frggtsldap
       61 gkrgsvylmt alleegagdl daraharale slaasfsyda sddavsisar fltenkdaal
      121 allrdtihap rfdqdaierv raqilsslrs dakdpdsiar ttfsrlafgd hpygsdgegt
      181 vdtvsaltre divqahadvf akdrlyvslv gditpedagi lvdrlleglp aegralpgpa
      241 evtltggttv vdfdtpqsva ifgqtgidrd dpdffaayvl nqvlgggsfe srlmdevrek
      301 rgltygiysy lasrdlaavy lgsvasandr iaqaievirt ewaraasegv taeeveaakt
      361 yltgayplrf dgngpiaril tdmqmeglpr dyiatrndkm ravtvedvnr vaaelldpeg
      421 lrfvvvgape glgdstn
//
LOCUS       WP_284486328             674 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Sedimentitalea xiamensis].
ACCESSION   WP_284486328
VERSION     WP_284486328.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..674
                     /product="PhoX family protein"
                     /calculated_mol_wt=73452
     Region          32..668
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mnrtsilsdp eignkaeafe afddiptnpn lnrtigdvin arygrrdvlr gflgvsatta
       61 lfgtsalvap rqaaaapdsr ykfkelawgn dethhiadgy dadmllrwgd pittdapefd
      121 vmnqtaaaql kqfgynndyv gfwplndegt rgvlcvnhey tneevmfpgl grqdnqdfag
      181 mtpelidiem aahggtvvei argedgkwal vrdsrlnrri tpldtemtfs gpaaghdrmk
      241 tnadpdgmtv igtvnncagg mtpwgtylma eenfhgyfwt dvldaegkpd lsahldaasl
      301 krygvpglwy awgrfhdrwn idkepnepnr wgwivevdpm dptatpvkht algrfrhega
      361 ettvspdgrl vvysgddnrf dylykyvstg tlsddraans allsdgtlyv arfdedgsit
      421 wmplvhgtgp ltaangfvsq advlidtrla adalgatpmd rpedvqprgd gtayvmltnn
      481 trrkadqvna anpraessfg hiieikeagg dhaatsgtws ilvkcgdpsv aevgaqwnpe
      541 tsengwfgsp dncafdadgr lwistdqggs wgktgksdgl yaletegalr ghsqlffrcp
      601 vggelcgpyf tnngetlfla vqhpgtdgtk dlkgferesv fedpatrwpd fdpampprps
      661 vvvvtrkggg kiav
//
LOCUS       WP_284486364             384 aa            linear   BCT 25-DEC-2024
DEFINITION  FliM/FliN family flagellar motor switch protein [Sedimentitalea
            xiamensis].
ACCESSION   WP_284486364
VERSION     WP_284486364.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13389420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..384
                     /product="FliM/FliN family flagellar motor switch protein"
                     /calculated_mol_wt=40356
     Region          120..287
                     /region_name="FliN"
                     /note="Flagellar motor switch/type III secretory pathway
                     protein FliN [Cell motility, Intracellular trafficking,
                     secretion, and vesicular transport]; COG1886"
                     /db_xref="CDD:441490"
     Region          225..287
                     /region_name="FliMN_C"
                     /note="Type III flagellar switch regulator (C-ring) FliN
                     C-term; pfam01052"
                     /db_xref="CDD:460043"
ORIGIN      
        1 makpgsssal qrkmdasrds aasngrsaaa alrvaiaraa ddlfslplsv iglsqarlpq
       61 deldpylpdd rllilldgpq gqlgvaaldr aflvsliqqq tmgcltgaap derpftatda
      121 alaaplidat iaraaemadr pldirclsgy rfgaraesar aaklvldtqp frlfeltlef
      181 gggpqqgsva lmlpepkeia aaedgvppdm srprlgqave maraeltavi ctvkmslsdl
      241 srmkpgdilp lvqehldrte lvtiaghgva agrlgqingl ralrlnetgl rqastpepka
      301 faadigaqps fkndpdildg elapvaepak aqapagsldd fpvehdtdda lagmtpdeaa
      361 qeistlagls rdemeyddlp ltid
//
LOCUS       WP_284486400             442 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Sedimentitalea xiamensis].
ACCESSION   WP_284486400
VERSION     WP_284486400.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..442
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46625
     Region          27..395
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtsdrpenlw rhshrpdmel aaldgdtrsd llvigggftg csaaleaarg nadvvllear
       61 tighggsgrn vglvnaglwl ppddivaklg rdagtrlida lsvapdlvfr liaehgidce
      121 atrngtlhla hapsglrele srlrqgnrtg aplqlldage tarrsgsraf fgglfdprag
      181 tvqplaycrg laaaaraaga rifegspvre ivhdgthwia rvgghrvrar hlllatnaya
      241 dgiggapare fvpvhfsqfa taplpeplrr hilpggegcw dtdmimnsvr idrdgrviig
      301 gvgnvdgpga tihrrwaark lahfypelag lpfehawsga iamtsdhlpk vlsfgpnals
      361 vfgysgrgig pgtvfgkqaa rallrgdtda lpvpltesys eggkrartvf fevgalaaha
      421 lrpgpfvprk asspsalapg qd
//
LOCUS       WP_284486569             266 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Sedimentitalea xiamensis].
ACCESSION   WP_284486569
VERSION     WP_284486569.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..266
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=27430
     Region          9..266
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mtvvetyptl dqaaramggd aaflgggtlv mravnegvap arlirvtgpg lselrvsgds
       61 vrigagvtma dvlasrdlef lhpvarvigg pqvrnmatva gnlfaahpfg dfaaallald
      121 arvigagqgg arpvadvlrd raraglvaai evprprdpka fgflkvsrvk prgvsilsia
      181 aylpreggri rgarvafgam gpvplrssga eralegqslg aaaidsaasa ategldpptd
      241 eiasawyrke vagvhlkrll tdmerr
//
LOCUS       WP_284486596             495 aa            linear   BCT 25-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Sedimentitalea xiamensis].
ACCESSION   WP_284486596
VERSION     WP_284486596.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..495
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=51722
     Region          17..494
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mtdwkaraaa lydggfrpmf iggqwcears gaviearnpa dgsllatvpr ggaedidaav
       61 aaarkalegp warftpferq nlllriadrf eaeweslcls dtldmgmpiq rtlansrrvl
      121 gmlryyagqa vathgdtipn sfpgeiysat vrepvgvvga iipwnapiag siwkigpala
      181 tgctvvlkps eeasltvlmi arimqeaglp dgvlnivpgl gaeagaalaa hpgvdkivft
      241 gstatgqaia raatgnlkrv slelggkspv ivcrdadidk avpvaamavf ansgqiciag
      301 srlfvareih deflgrvady aaglrighgi eetteigpii sarqagriag ylaagpkega
      361 hlltgggsae gghlagghyf qptvfggvtd emsiareeif gpvisalpfd sidevvaran
      421 atpyglaagv fsthlgtahk lahrlragsv wvnmyhaidp avpfggvkms gygreggrgh
      481 vedyldtkai wintd
//
LOCUS       WP_284486629             125 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Sedimentitalea xiamensis].
ACCESSION   WP_284486629
VERSION     WP_284486629.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..125
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13357
     Region          1..124
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mfsfseprrs rkpsltpmid vvflllvffm lasrfghdaa lslaaaggga pyegpprlvv
       61 vtetglqlng qpltaedlpg rlaplmrdrd dlvvlradad tslqrligva qslrrsgitn
      121 lavve
//
LOCUS       WP_284486635             622 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Sedimentitalea xiamensis].
ACCESSION   WP_284486635
VERSION     WP_284486635.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 622)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 622)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 622)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 622)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..622
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=67810
     Region          7..590
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mtrsihlatv aaatlcaqpa isqtpfelde ivvsggftpi eeqrygrsat vltaedieng
       61 gfitvkealr tvpgvsvsgt gdnltqvrir gaeanhtlil idgvqasagd neyvlsglet
      121 anierievlr gpqsvfygsn asagviniit kkgnlgtefg gtveagdgya atarysfrtd
      181 rgglalglsr ldddgydysg sngeddgirr stinltgdyn vteqitlgft lrasdedsdf
      241 detnflamdp adyviddpdq tserqerqgs lyaefdaldg rliqrltfeg sdfetstngg
      301 dptkadrkaa kyllsygldg qmvsdtdhll nvlleweeds sstnseyrre tnsvameyrg
      361 alenglnlqg glryddnktf eddvvwtlaa sytfaqsgvr lhtsagtgsv npsyfelfad
      421 sfgfvgnpnl kpeknesfdi gvdvpfwgdr gsigltyfyd nltdeitavf dpvsgnstfi
      481 nedgksnrrg velsgslqat dslnlqldyt ylrarnpdgs ieirrpkhel slsatqefla
      541 grgqvtadlr yvagnydtqf fgnfdtkelp dyvtvdlsaq yeltdavqlt grivnlfdet
      601 ysdtwgyatr grtayvglra af
//
LOCUS       WP_284486733             240 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Sedimentitalea
            xiamensis].
ACCESSION   WP_284486733
VERSION     WP_284486733.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..240
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=25675
     Region          7..239
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mterpdiryn akthvglkrk vnedavlalp dqsiwmvsdg mggheagdfa srliadsiam
       61 ippgldpadr mhalrdairs ahriilgeak srgrgvigat vaalilangh fvalwagdsr
      121 iyrlrdgaie mlttdhsava elvlagqmtw deaeqhpqsn aitravgvgd sveldkvrgd
      181 vragdrflic sdgltkyatf kilrdaltaf pietvsdqli qmalsgggad nitvivldvl
//
LOCUS       WP_284486770             509 aa            linear   BCT 25-DEC-2024
DEFINITION  GumC family protein [Sedimentitalea xiamensis].
ACCESSION   WP_284486770
VERSION     WP_284486770.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..509
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=56585
     Region          3..>507
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mpnvgyylsl firrlpafll vaasvatvsi vvaftlppay esrmvlivea pqipdalaps
       61 tvrmpgpqrl qiieqrlltr anlldiarrl dvledqskmn pdeivlgmqa rtrvestrrt
      121 teasimtvtf eartprlaag vlneyltliq addatfrkgr agqtldffeq evarlnaele
      181 eraglilefk nanagalpdt lafrqqqqae rqlrleevgr eifslksqrq qlmamfeatg
      241 gvggslspaq qdladaekel enalivyspn nprvkvlqgr vdqlrqiaea evpqendepq
      301 tgtgnlaldf qlagidnrii alerqeeklt qeverleegi lktannanil edlqrdydnt
      361 lsqympavqr ladadtgeri ellsrgeris vieqpavpse ptkpnrimia gggtalgigl
      421 gaalvflmvf ssgaprrped likkldvwpi atlpyirtrr emiiqrgiki amivvilvgv
      481 pvvvwlvhty yqpldliadr vmnklgvrw
//
LOCUS       WP_284486781             519 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA synthetase [Sedimentitalea xiamensis].
ACCESSION   WP_284486781
VERSION     WP_284486781.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..519
                     /product="acyl-CoA synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016405 - CoA-ligase activity [Evidence
                     IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0032787 - monocarboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=56118
     Region          7..503
                     /region_name="FACL_FadD13-like"
                     /note="fatty acyl-CoA synthetase, including FadD13;
                     cd17631"
                     /db_xref="CDD:341286"
     Site            order(163,166..171,173..174)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341286"
     Site            order(166,280..281,303..308,393,405,408,419,500)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341286"
     Site            order(166,206..207,253,255..256,259,280..281,303..308,393,
                     405,408,416..419,480)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341286"
     Site            order(206,255..256,259,280,416..418,474,480)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341286"
ORIGIN      
        1 mhvtsilrra aqinpngtat ifkdrrqsws qmvtrvskla salqglgmqp ddrvallsln
       61 sdryveyffa tlwgggammp mnirwapaec ayalndagae illvddafap vaaamqadvp
      121 llktliycgd getpdgmlny edllaaaapv pdanrggndl agifytggtt gfpkgvmlsh
      181 tnfyvggmsn vselrledrc iylhaapmfh iadllwftav tivagthvvi pmftpddtle
      241 aiqthrpshv llvpvmlqmi mqspkladtd issvrliayg aspiteaalk qafrlfpnaa
      301 ftqafgqtel spvatilaad yhvldgpkag klrsagratr vceirivdps gtdlptgevg
      361 hiivkgpitm lgywnkpeat aeairdgwvy tgdagymdde gfvflmdrik dmvvsggenv
      421 ysaevenvig qhpavatsav igipseqwge svhaivilhp gasvtedeik ahchsliagf
      481 kcprsiefrt dpfplsgank vlktelrkpf wegwdrnia
//
LOCUS       WP_284486801             122 aa            linear   BCT 25-DEC-2024
DEFINITION  MerR family transcriptional regulator [Sedimentitalea xiamensis].
ACCESSION   WP_284486801
VERSION     WP_284486801.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..122
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14660
     Region          6..116
                     /region_name="HTH_GnyR"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     regulatory protein GnyR; cd04776"
                     /db_xref="CDD:133403"
     Site            order(7..9,23,39..41)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133403"
     Site            order(52,55,59..60,69,89,93,99,103,106..107)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133403"
ORIGIN      
        1 msdsrlsfke mcakfdvtpr tlryyeyiel lrpdregrsr fygpresarm klilrgrkyg
       61 fqleeirqwl liyekegtsa qmqafvemad rqmkeleiqr qqlevamrel qelrddtarn
      121 vp
//
LOCUS       WP_284486912             139 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Sedimentitalea xiamensis].
ACCESSION   WP_284486912
VERSION     WP_284486912.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..139
                     /product="YybH family protein"
                     /calculated_mol_wt=15190
     Region          1..133
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mterygdaae lrlidlvrdn hvgalntgda eawtaqfagd gvqmppnape nvgkerirqw
       61 fvgllsafkv qfeldveevr ivgdwaferg gyaislnpva ggpamvdngk yitiyrqgdg
      121 ngwkiardiw nsnspipaq
//
LOCUS       WP_284486983             210 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Sedimentitalea
            xiamensis].
ACCESSION   WP_284486983
VERSION     WP_284486983.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..210
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=22529
     Region          14..173
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mtrtrpdlds ayalrtpeds erlyeewaed ydssfatred yrlhiqtara fvaargqgpv
       61 ldvgagtglc gavladlgvg pldatdissr mldqamrkdi yrdaiaadvn kgipvpaesy
      121 sgvvssgtft tghvgpsals ellrvarrga qfalsvnakh ydsagfagaf dslsenrirn
      181 ltlqdtpiyg pratgahrdd rafialfeka
//
LOCUS       WP_284487131             279 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Sedimentitalea xiamensis].
ACCESSION   WP_284487131
VERSION     WP_284487131.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..279
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=30633
     Region          49..276
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mtvadalaiy geehaptvad parigyaida llpfwgnrsc advkgsttrl yakhrgvsvg
       61 tvrrelgtlr aamvycgkeg ylttvpmfpm paapetkqra mtrsevakll rvsprhlrhf
      121 ilvalytgtr rdatlnlrls gptttggwfd ldagilyrig sgeratrkrr apariprqll
      181 aharrwaarg dtwavewkgg rvgsvktsws havtdadlgw rptphtlkht aitwaiqgga
      241 tkedaagffs tstetiervy whlspdfqqg aldaierng
//
LOCUS       WP_284487154             526 aa            linear   BCT 25-DEC-2024
DEFINITION  formylglycine-generating enzyme family protein [Sedimentitalea
            xiamensis].
ACCESSION   WP_284487154
VERSION     WP_284487154.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..526
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=57345
     Region          111..314
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 mtgfrpglll llafltvqaa pdparaeeep wpldltdpah dsapadlmlp mpcgaamafq
       61 kvtvpvdasd pladrrvrlg qsldrtgysd yflpaflrgp fsdsdpgtth yfiaryeltr
      121 gqfralngdc appdrtdrla qgglgwfdav glaqtytewl yrthpealpr agdaagflrl
      181 pteaeweyat rggaridete flgltffgtg dprnyalfqa pgssrgrlgp vavrkpnplg
      241 lydvygnaee lmlepfrlna igrmggqvgg ivtrggsvls saeqmysaqr teyppydpat
      301 gaplrsetfg vrlviashia tsdarlrair drwialaggd gdaqkaedpv aqitrlieae
      361 vdprrkaald glkldlrrsr eqaqtalqqs aratllagav fvdslrenae ridskasnir
      421 mlidlqragn nsafygrqva ghvaeiaalr evqstfllsf raaletlsgd leaadreiay
      481 tvlreelsls argttlemld rfwldlaayq arpdinsadl lkiale
//
LOCUS       WP_284487328             313 aa            linear   BCT 25-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Sedimentitalea xiamensis].
ACCESSION   WP_284487328
VERSION     WP_284487328.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..313
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=32426
     Region          5..302
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(9..10,12,44..46,67,94..95,98..99,101..102,105,109,
                     111,119,121,123,125..131,133..137,155..156,159..160,
                     259..260,267,273..279,281..284,286)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(45,68..70,92,230,277,280)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240626"
     Site            order(69..70,96,145..149,167..169,172,200..202,206..207,
                     228..230,254..255,277,279..280)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 mtkivtlsrp mplpqieagg eavefvpvss aadipavala histaidpvd gdfiagmpeg
       61 qrlianfgvg vdnidlaaaa vrgivvsntp vvtedtadla ftlilgaarr vgkgerylra
      121 gkwsageapp algirvhgqa lglvgfgpia qavgrrakgf gmevlywnrt rredaetalg
      181 atfvpdlael lgqsdiisvh talvpatrnl inaerigqmr kgavlvntar ggivdeealc
      241 daleaghlga agldvfdgep qvlpalmerq dvlltphigs atsacrmdmt qcvlgnvvsf
      301 lesgsvqtpv ktg
//
LOCUS       WP_284487470              56 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Sedimentitalea
            xiamensis].
ACCESSION   WP_284487470
VERSION     WP_284487470.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 56)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 56)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 56)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..56
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..56
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=6218
     Region          1..56
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mtpeyltadq vaqmtgfstk sleayrakrq gppflkvghs vryraddvra wmeage
//
LOCUS       WP_284487476             186 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Sedimentitalea xiamensis].
ACCESSION   WP_284487476
VERSION     WP_284487476.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 186)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..186
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19036
     Region          13..>185
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtvalvlsma vdvslgpary algdvlqtlf apgsvevqmr vvvwdirmpm allavtvgas
       61 lslagaqmqt ilanplaspf tlglsaaasf gaalamvlgv alfpaaialm vpinafamam
      121 aasllifgls slrgvtveti vllgialvfs fnaalallqy faseqalsav vfwtmgsltk
      181 atwgtr
//
LOCUS       WP_284487488             442 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Sedimentitalea
            xiamensis].
ACCESSION   WP_284487488
VERSION     WP_284487488.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..442
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48731
     Region          109..438
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkpdlgvywm yrtaltcail atcvlaqpqt vlaqeqtpts etplarvkdi qeyfaqpena
       61 vsfqfaspet hyawqhvsqf yptarfarsg mptvlesaid eslgdisfsg mdgvtrtvse
      121 hfeampldam lvmkdgqivy eryktmtpdt ahitfssskv fsstilalle eegkvdlskp
      181 vtdyveelkg svwdtvtlre vadmqtglng tehdepnpds rtnpkqiwyr waatlgifpn
      241 qgendtfavl ramernkpgg evfeynsint wllariaeav edrpfaeift drvwskigad
      301 hdgtfimspn gyalafgmts vtlrdfarfg smftpsseav tgskvvsdev lkriqtsgnp
      361 daypdgyvgk vmspkfadaa geisnaymwd ailpdgdmfk ggvggqglyv spskdlvavw
      421 fttgdgsewn eamaraialh fd
//
LOCUS       WP_284487492             454 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Sedimentitalea
            xiamensis].
ACCESSION   WP_284487492
VERSION     WP_284487492.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..454
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50051
     Region          135..448
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mhviklpvas alilgafalp alaqdnplqk ylsvpgamtt lpveaakepw slqfsrdara
       61 afenfhyqmg gdhalyyqqn lsemlptaya aphsdyiple raiddsigen vrwttsegem
      121 plseyivhpn hrvqgmmmih kgkvvyeqyp gmnqmdrhaw mspgkatvgl ilalleeegk
      181 ldmskdvvny vpqlagtnwd gisvldaanm etglaleetl daiidpssii vrffaaefgs
      241 pnpltgemen wldilktaek legeepgevf ryssavtqvs vllaenldnm twadlfqerv
      301 wgkvgaredi mfhlmpdgta vthglisttl edfgrfgllf tpswaatahe divsdavler
      361 mqtagnpeaf rrgakfaglt defgeepkan slqwdavfed galykhgnvg qglyvdpard
      421 fvgvyfstng yippygedra qgflrqaaky lgge
//
LOCUS       WP_284487556             157 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Sedimentitalea xiamensis].
ACCESSION   WP_284487556
VERSION     WP_284487556.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 157)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 157)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008128
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..157
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17154
     Region          40..153
                     /region_name="CytC556"
                     /note="Cytochrome c556 [Energy production and conversion];
                     COG3909"
                     /db_xref="CDD:443115"
ORIGIN      
        1 mtqgfrpqhl aiavtlaalv lataalsqsg qisqvtnpgv qarmstmnra naalstlndm
       61 mggralfdrd ragaarkdlm aatksipsvf rkphadplsn arpliwsnwr dfklkakraq
      121 raawnidtds lsdlrqslpr mvlaclhchd tyrdgtr
//
LOCUS       WP_284487630             248 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Sedimentitalea xiamensis].
ACCESSION   WP_284487630
VERSION     WP_284487630.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..248
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=25947
     Region          <37..230
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mttrlkfana aaalaafcsf alagggmsqp rqnctddaml vfdasgsmae mgyngldapr
       61 ivearaalrd alpsitpyrr lglivygpgs gdscanidlr flprpdaagv iiadvdrvqp
      121 dgdtpltqsv rnaadalryk trpgtivlvt dgketcggsp cllaaelaqt gpgltvhvig
      181 frvrsaffsw kdspdagngd gqtvarclad rtgghyvste ntadlvralq ltlgcplygh
      241 gsrwrqtg
//
LOCUS       WP_284487614             505 aa            linear   BCT 25-DEC-2024
DEFINITION  malonate--CoA ligase [Sedimentitalea xiamensis].
ACCESSION   WP_284487614
VERSION     WP_284487614.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Pohl,N.L., Hans,M., Lee,H.Y., Kim,Y.S., Cane,D.E. and Khosla,C.
  TITLE     Remarkably broad substrate tolerance of malonyl-CoA synthetase, an
            enzyme capable of intracellular synthesis of polyketide precursors
  JOURNAL   J Am Chem Soc 123 (24), 5822-5823 (2001)
   PUBMED   11403625
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11482749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..505
                     /product="malonate--CoA ligase"
                     /EC_number="6.2.1.76"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0090409 - malonyl-CoA synthetase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0090410 - malonate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54722
     Region          1..503
                     /region_name="PRK07514"
                     /note="malonyl-CoA synthase; Validated"
                     /db_xref="CDD:181011"
     Site            order(160,163..168,170..171)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341264"
     Site            order(163,203..204,207..209,249,251,255,277..279,298..303,
                     307,322,382,394,402,405,408,437,473)
                     /site_type="active"
                     /db_xref="CDD:341264"
     Site            order(163,277..279,298..303,322,382,394,402,408)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341264"
     Site            order(203..204,207..209,249,251,255,277,299,301..303,307,
                     405..407,437,473)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341264"
ORIGIN      
        1 manplfdslf gkyagretpf lhldgggtvt haaflaraar fahvfrelga qagdrlaaqi
       61 ekspealaiy aaciqsgivf lplntaytad evayfvensg arilvcdgsr qaalapvaaa
      121 agavletlna dgsgslrdra esapdsfetv ardaddlaaf lytsgttgrs kgamltqtnl
      181 lsnaevladq wrftdtdvll halpifhthg lfvatnitlv aggsmiflpk fdqdriiaal
      241 pmattmmgvp tfytrllddp rftrdlvrhm rlfvsgsapl laethvqfee rtghrilery
      301 gmtetnmnts npydgerrag tvgfplpgve lkitnpetga rlpdgeigqi evrgpnvfkg
      361 ywqmpektre elredgffit gdlgliddrg yvqivgrnkd liisggyniy pkeielvldd
      421 qpgvlesavv gvphpdfget vvgvlvaepg adpdldaiaa avgkslarfk hprrllllse
      481 lprntmgkvq knllrdrfkd ifsgs
//
LOCUS       WP_284487658             449 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Sedimentitalea
            xiamensis].
ACCESSION   WP_284487658
VERSION     WP_284487658.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..449
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49049
     Region          109..418
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mksiakmsia tlpaiavaal cavssaplsa qdapdystaq elglmegfpp ppdkqvtkan
       61 amltgpfnrw syqnmrmfyp sanvpaadkv vplsktidwn fekgveikep gtdaskslad
      121 flketwadai vvirgdqivy ekflngmtsd tphqmmsatk sfggllglma vaegkvsede
      181 lvtqyvpeld vedgafagat fgqvlnmtns mdftevyddp tsgirtygav lgwtekvdgi
      241 dyparlydyl atlkvdpehp hgeifhyqtp ktdvvnwvtn rannasfqqa lydgiwskig
      301 aegetyvlld nnatlvaggg lnatpynlar fammmlnngk fngkqvvpas vvdkiaeggs
      361 ieafdsgpds ddfvhkkgew syraqwwvkh tpgmeafmai gihgqwiyid rahnvaivkq
      421 ssmppskdty ldgynlegfy giirylagm
//
LOCUS       WP_284487794             353 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Sedimentitalea xiamensis].
ACCESSION   WP_284487794
VERSION     WP_284487794.1
KEYWORDS    RefSeq.
SOURCE      Sedimentitalea xiamensis
  ORGANISM  Sedimentitalea xiamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Sedimentitalea.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Sedimentitalea xiamensis"
                     /db_xref="taxon:3050037"
     Protein         1..353
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35505
     Region          36..348
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mvtqiaaspl agdrsraarr lgyvlvgllg ltciaglavg aagtslwsal adlavgrela
       61 lrdkvvlwdi rvprvlmgml vgaalavsga vlqglfrnpl adpgivgvsa gaslgaviai
      121 vlggalplaa amgawivpvf aflgawgatm tlyriatrag rtsvatmlla gialtaltma
      181 ltglivyvad daqlrdftfw nmgslagatw gklavavpli llplaasgll arglnglalg
      241 eaaaghmgip vqrlkgaail ivaaatgaav sigggigfvg ivvphllrla tgpdhrfllp
      301 naallgaaml lladlvsrti iapaelpigi itaiiggpff lfillrqrgi vdl
//
LOCUS       WP_284488248             252 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Aeromonas caviae].
ACCESSION   WP_284488248
VERSION     WP_284488248.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..252
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28150
     Region          41..251
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mtlriilllc llvlaartig atevfhtaaq qasspkyvtl pdghvggicv dlfrlmeare
       61 palriegdqr flplrrlekk vqhgqldfif gvgesparrd hfivltpaif tvcyhlavrh
      121 ddpveirswq dvralgqgsi ilinhgsgai arlqdiggli idsggisnqa nyekllmkrg
      181 rfvyyrspgf esdlreqgla dkirilptvm eetpfyilfh rhsaperltl fantlqrlad
      241 sgelaalarr yp
//
LOCUS       WP_284488089             674 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein [Klebsiella
            michiganensis].
ACCESSION   WP_284488089
VERSION     WP_284488089.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella michiganensis
  ORGANISM  Klebsiella michiganensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 674)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 674)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 674)
  AUTHORS   Porat,A., Cho,S.H. and Beckwith,J.
  TITLE     The unusual transmembrane electron transporter DsbD and its
            homologues: a bacterial family of disulfide reductases
  JOURNAL   Res Microbiol 155 (8), 617-622 (2004)
   PUBMED   15380548
REFERENCE   4  (residues 1 to 674)
  AUTHORS   Kimball,R.A., Martin,L. and Saier,M.H. Jr.
  TITLE     Reversing transmembrane electron flow: the DsbD and DsbB protein
            families
  JOURNAL   J Mol Microbiol Biotechnol 5 (3), 133-149 (2003)
   PUBMED   12766342
REFERENCE   5  (residues 1 to 674)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   6  (residues 1 to 674)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   7  (residues 1 to 674)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   8  (residues 1 to 674)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   9  (residues 1 to 674)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12109673
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Klebsiella michiganensis"
                     /db_xref="taxon:1134687"
     Protein         1..674
                     /product="protein-disulfide reductase DsbD family protein"
                     /EC_number="1.8.-.-"
                     /EC_number="1.8.1.8"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=71562
     Region          38..144
                     /region_name="DsbC"
                     /note="Disulphide bond corrector protein DsbC; pfam11412"
                     /db_xref="CDD:463273"
     Region          267..674
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 mlnifrgfvf lllacagvah gadtgwltsp qndharirfq aekgndridg llsielasgw
       61 ktywrspgeg gvapqiiwnn geqarwywpa psrfkisglt tqgyhdrvai pmtiaaapgd
      121 vlegtltlst csnvclltdy rlrldfnqpa dgdfrdafar amrtipadtg itndlaahrv
      181 gsqlvitana tgewknagiy fdpmdggiva gdpdiraegs hlkvtvpvtd ewgeipatla
      241 gkalslvltn gekaqqinlt tgadlapaat vslgkivlfa llgglilnlm pcvlpvmgmk
      301 lsavlqagsd rgmvrlrfla tsagiltsfa llalmvtilk ltgaslgwgi qfqnpwfigl
      361 mvavtflfsl nlfgvvemll psaavsrlat aggagmagsf cegvfatlla tpcsapflgt
      421 avafalaapl qelwliflvl glgmaapwlf valfpqtaal lprpgrwmnt lkmalgvmml
      481 asslwlttll glhlgetagg mltlaltvaa piallvarpr atpafwlvii alaafagfqv
      541 rgllaegaiv sspeanaqqi rwqplseaai qsaladgkrv fidisadwcv tckvnehrvl
      601 nqpaiisala epdvvalrgd wskpsepiar flqsrnryai pfnqvygpgv pqgetlppll
      661 dqqsvlnalt harg
//
LOCUS       WP_284488274             715 aa            linear   BCT 25-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Aeromonas caviae].
ACCESSION   WP_284488274
VERSION     WP_284488274.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Shan,L., Mathews,I.I. and Khosla,C.
  TITLE     Structural and mechanistic analysis of two prolyl endopeptidases:
            role of interdomain dynamics in catalysis and specificity
  JOURNAL   Proc Natl Acad Sci U S A 102 (10), 3599-3604 (2005)
   PUBMED   15738423
REFERENCE   2  (residues 1 to 715)
  AUTHORS   Polgar,L.
  TITLE     The prolyl oligopeptidase family
  JOURNAL   Cell Mol Life Sci 59 (2), 349-362 (2002)
   PUBMED   11915948
REFERENCE   3  (residues 1 to 715)
  AUTHORS   Polgar,L.
  TITLE     A potential processing enzyme in prokaryotes: oligopeptidase B, a
            new type of serine peptidase
  JOURNAL   Proteins 28 (3), 375-379 (1997)
   PUBMED   9223183
REFERENCE   4  (residues 1 to 715)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 715)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..715
                     /product="prolyl oligopeptidase family serine peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=79039
     Region          29..707
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mraivsllal sllcacsgqp tredamsgnt rlhypvtrqg eqvdhyfgqa vadpyrwled
       61 drspeteawv eaqnrvtqgy laeipyraai keklaaswny akegapfreg ryhyffkndg
      121 lqnqnvlwrq qegkpaevfl dpntlspdgt taldqlsfsr dgrilaysls lagsdwreih
      181 lmdveskqpl eaplkdvkfs ginwlgnegf fyssydkpdg selsartdqh kvyfhrlgta
      241 qeddrlvfga ipaqhhryvg atvteddrfl lisaanstsg nrlyvkdlsq enaplltvqg
      301 dldadvslvd nkgstlyllt nrdapngrlv tvdaanpgpa rwrdliperq qvltvhsgsg
      361 ylfaeymvda tarveqfdye gkrvrevalp glgsvsgfng khddpalyfg fehyaqpptl
      421 yrfepksgai slyrasaapf kpedyvseqr fyqskdgtrv pliisyrkgl kldgsnptil
      481 ygyggfdvsl tpsfsvsvan wldlggvyav anlrgggeyg qawhlagtqq nkqnvfddfi
      541 aaaeylkaeg ytrtdrlair ggsnggllvg avmtqrpdlm rvalpavgvl dmlryhtfta
      601 gagwaydygt sadseamfdy lkgysplhnv rpgvsypstl vttadhddrv vpahsfkfaa
      661 tlqadnagph pqlirietna ghgagtpvak lieqsadiya ftlyemgyqq lprqp
//
LOCUS       WP_284488301             562 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Aeromonas caviae].
ACCESSION   WP_284488301
VERSION     WP_284488301.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..562
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=61780
     Region          31..>231
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mvsdrtllnq tslgwlllia llvlgaglgl rdpwpadepr faliaremve sgqwlfpmrg
       61 gelypdkppl fmwgiaigyv ltgsikvafl lpsllsgllt illvwelgrr lwdpatgfla
      121 gllllftvqf tlqaktaqid glvtffitlg lygflrfllc gggwrwywlg wfaaglgvit
      181 kgvgvlallv llpalwthrv qiraaplsaw lkallgplam alamglwlvp mleavtrsgd
      241 plllayrdni llrqtvtryt sawhhvkpfw yyitsvippf wlplslllpw lvvawrrair
      301 aqdrrillll gylvllvlff scspgkrgvy itpgtpalal ltapfigtll vrvwpgrlla
      361 glgwllggag lvgalvlafs drvasrlgel gpdpwlpllv lggslllina wlrrapltai
      421 lsslavgwli yscwisvrln evrtpeavma laaqkvpvgd elllagfkeq hllfslqpvk
      481 hypylmgdge qareaaawig aapgrwvlgs adlmmrcfdp akmenlgnrh rtdwllagpq
      541 alkpacrgls ptmvpfsytp ss
//
LOCUS       WP_284488320            1448 aa            linear   BCT 25-DEC-2024
DEFINITION  NACHT domain-containing protein [Aeromonas caviae].
ACCESSION   WP_284488320
VERSION     WP_284488320.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 1448)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 1448)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1448
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..1448
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=166499
     Region          38..759
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 miertfkdid eqqifdadkq nfltqlgwsd gltwevllrs krilliseag sgkthecreq
       61 acllaakgea affvelasla sthlrdllgy eeetrfdlwl asqseiatff ldsidelqlt
      121 rgsfrqaldr fvrgiennlg rvrvvvttrp ipfdmqlvrs klpvplqikp rsteekeref
      181 asmalgehmp issgqsnekp ipdwrtvalm plsnpqiael aelkgvknta ellsdierqn
      241 afefarrpqd lielcsdwqa gfqlrthrqq veasiriklk prdreerhel aelsidkaie
      301 gasrlalamw ltrrltirhs aksdngqqge aaldpsiils dwtqeerqtl lerplfgfas
      361 ygrvrfhhrs vseflaakkl qemrdkgmsl ralkrlllie tkgntivlps kraiagwlaa
      421 lnddifqair dheptlllde gdpasltlaq rkqalgayvq rygrggrrgl htpsiqikrf
      481 atpeltdein lqwqqdidnq evrcvlleli ergvicgcsd lvysvatdsm lveveriyai
      541 halqalndpr lgeiaalmvs qhpdwpdeiv reailalfps dlsvsqlcqs lgwlqwkkls
      601 vsnlswrlps liknaplvms qleelrdklv tlisdglqwr qeqwphmvsp rqylsstlaa
      661 vcirgldhqc seqwihacvl alrlrqheyd ddkihnelsq rineldsknr kqvfwaidal
      721 vqslcpiddi wkrvveiipy dslikltvql dqawvvndlq dknkpsfehq ilmhiaiyrl
      781 riplsdlrel vahqpdllsl ldeaikpseh dkaseelqrq daelrkqqem daaeiraswm
      841 mlhreiseyt dnvfsdehyk nmvwdlfrvm iitaddnnls gwnrpflesh fggivtdrlr
      901 tlfmaswreh rptlicerpe dqrstyleiw rlglaglyae aedtdwaspl tqeeamlaar
      961 ysllelnklp dwindlvryh psavsdifgk elewvlstst helhhsmllq rlhhapnsvt
     1021 mlfvprlvtw lseigllndd epqssgfisr ysrvielili hgdvdhqakl cfmakeyvnk
     1081 elaepvmliw lstlirlnpe sgvdvlegkl rdiepeplsk pvewftklfn erhdginirn
     1141 ngftpmlllr larlayqhir rqddaehegc ytpdmrdnae yarnailtal lepqgeegwq
     1201 vkhdmaidpl fshfkdrila laqeawakei dsvlldeqqc relehkgelp lttnaamftl
     1261 lhdrladlde llnsdespre lwaeihqekl mrraiaqelq hasnglykvv qeavtadeke
     1321 tdirlcslas nyeavielki edgnrwsanv lretireqla ikylsletrc sgalvitlsk
     1381 nrywqhpdsg erigleelke llddearrve remggavslt ihvldlrprl ltekqsrsgv
     1441 mkkrvnpa
//
LOCUS       WP_284488428             680 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Aeromonas caviae].
ACCESSION   WP_284488428
VERSION     WP_284488428.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 680)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 680)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 680)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 680)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..680
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=75082
     Region          54..680
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mnhsnptral lgvallavct spraedetlt vvgkrsqhee vatatrtatp aklvpqsies
       61 vkaseltafg qptlsealtg ipgvnasgdt rfdgvtirgf sasndfyldg lrddmqytrd
      121 lgniervevl kgpaavlygr gstggivnrv skvpqkgqas svsaqvgsfd srrfaadlng
      181 eagervqvrl nlaqedkdsf rddvtskrtl lapsvnweit dtlnwlvqye rnehdrtpdr
      241 gipgvdgrpa dvpiesvysd trrdfiddva qstrsrftwd indqwqlrqq lgyttldsqf
      301 dntyvtsvkg dkvtrarwqq dlkassltsn teaegqlqtg piahrllvgl eqgwqdrtpk
      361 lyqnanpipa gnlydpgslp tydgamklss dahhrvrgvg lyvqdqlslg dwhllaglrr
      421 ddftvtsrrn dldkeetlsv tslsprlglv wnpieehafy tsysktftpv ggeligitpg
      481 dknnnldpqh trlyeggvks dwlngrlatt lslyrlemyn krskdpldpt rviltglqrt
      541 dgielsaraq ltdeiylrgg vaiqdaeqvk adadlqgkrp mnvsrqngql fagyqsgkqg
      601 wfgetgmtav gdrfadnant ttlpgyarfd aragyrwpqw eaqlsvenlt dhdyfvsats
      661 aaqimpgtpr qlhltaayrf
//
LOCUS       WP_284488526             121 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Aeromonas caviae].
ACCESSION   WP_284488526
VERSION     WP_284488526.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10601889
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..121
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13414
     Region          6..>52
                     /region_name="AF0184"
                     /note="Predicted transcriptional regulator, contains
                     XRE-type HTH domain [Transcription]; COG2522"
                     /db_xref="CDD:442012"
ORIGIN      
        1 mskkptpesv ardyviaaks avaelmernq lnqssvarit gasqaavsrw lnpdteqffd
       61 lhhyallciy lkvppavilp padwtpgsyq avlkqliklp erdlvfllev hqlaratygk
      121 k
//
LOCUS       WP_284488605             868 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Aeromonas
            caviae].
ACCESSION   WP_284488605
VERSION     WP_284488605.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 868)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 868)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 868)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 868)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..868
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..868
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=93444
     Region          33..818
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mlrksrlsaa vafalasaav vatpvlaeeg qnveklqkik vtgsrisrvd vegatpvvsv
       61 tkakieqsgq qtvadylkqa synsfggvsp asgssfqsqs tvglrglgse rtlvllngkr
      121 vagsptmggt sinlntipma avervevnld ggsaiygsda iggvinvvlk egyegldfqg
      181 rigspseegg deksgsivag vagekgslma vyehdkkdvi ysrdrdylak qgndspsayg
      241 rnvegitgld angdpiwkyg plagatnadg sckepfvgfe ggcnfnygqv aaktasrsrd
      301 tlyvngryhi ndnvdfvpqi igsrvesfgr fapaagafti dpanpknaqf ftdngldaaa
      361 tqglgeaaya yyrfnnvgtr dnlvtdmtgs mnlgfegtia tesvgdmqwn agymysktdn
      421 kengtgyvlk saaqkaiedg kfvggefdas ttasmaadts rrstmdfyqw yagvqwdmge
      481 lpagpvswya gaeyndwvya dkydaqseag niigssgnss ggvrdvtaay ieslvpitdq
      541 ielnvagrfd kysdfgsafs pkaslryqpl dnlmlrtsws rsfrapslsd lysadsfsad
      601 wakdyvycea ngisaadcpn rqydttrtsn edlkeetadt wnfgvayspv ddlnlsldyy
      661 tikiedviql nslqsliyde lnsgssssit rnsqgkikga iapmvnlgtl etsgldlkvd
      721 ytydlnyatv rydlggtyil kykeglyagg pvidkigqkg lpqmrfssgv gvnvpqwwnm
      781 dtylsanyid sqsqdyiadt geevghiasq ttwnlnvgve apwngkiqvg vknmfnvgps
      841 lesdgftydd elysidgriy yldysqkf
//
LOCUS       WP_284488613             319 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Aeromonas caviae].
ACCESSION   WP_284488613
VERSION     WP_284488613.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Higgins,C.F., Hyde,S.C., Mimmack,M.M., Gileadi,U., Gill,D.R. and
            Gallagher,M.P.
  TITLE     Binding protein-dependent transport systems
  JOURNAL   J Bioenerg Biomembr 22 (4), 571-592 (1990)
   PUBMED   2229036
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467926
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..319
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35137
     Region          1..318
                     /region_name="SapB"
                     /note="ABC-type antimicrobial peptide export system,
                     permease component SapB [Defense mechanisms]; COG4168"
                     /db_xref="CDD:443329"
ORIGIN      
        1 mffyilrrit llvitllvlt lgayllefrl itqvldfwhg ypdflqriaa gdfglssvsg
       61 qpvldeirhy fpatltlcla afatsllvgi plgtlaalyq grspdlsima aglvgyaipv
      121 fwlgllmvmf fsldlgwlps sgqisllydv psitgiaivd vlmsqepwre aalhdalrhl
      181 vlpslvlavv pttevirhvr sslidvmkqn yikaaasrgl srrqivwrhg lknalppvlp
      241 llglqlgsvl tsamitevvf dwpgigrwlv ssialqdyaa irgaflvvas fvifisvstd
      301 llttimypar rkelyarqd
//
LOCUS       WP_284488859             215 aa            linear   BCT 25-DEC-2024
DEFINITION  XRE family transcriptional regulator [Aeromonas caviae].
ACCESSION   WP_284488859
VERSION     WP_284488859.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..215
                     /product="XRE family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23622
     Region          1..73
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          110..208
                     /region_name="COG2932"
                     /note="Phage repressor protein C, contains Cro/C1-type HTH
                     and peptisase s24 domains [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442176"
ORIGIN      
        1 msdiknvqan rlrhcrgvkg wtleetgkrl gvtgsrysnw eqalrspkye qmialaelfg
       61 ttpawlagft dhegnnasam dyvtldqsai svggetlnid nvanrsalhi dhvkarglne
      121 nrltaivaqg dsmdpliqdg aevlidrsrt tvstadlfai lvngqiwirw irpeldgsft
      181 vaaedsahyp dqklnaeqla slkivgriar ithdr
//
LOCUS       WP_284488747             264 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Aeromonas caviae].
ACCESSION   WP_284488747
VERSION     WP_284488747.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14398449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..264
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29945
     Region          33..113
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          174..256
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mgtltlaeqd rlladpnply frysqiqggn acaehahpwg qlslislgvm vvevggerlv
       61 appdyliwvp adlphtafne qtldytsiyv shalaprlpr epqllaltpl lralledftq
      121 rrvghmedew darqgelfie klartrcqps ylpqsrdrll apllaalqaa pednrtlvew
      181 aralhttert larrcqkelg mslgqwrtrl rlvkaldwlr gempvqeiaw rlgyastsaf
      241 iamfqreqgc tpqryrqqlg qpva
//
LOCUS       WP_284488854             424 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Aeromonas caviae].
ACCESSION   WP_284488854
VERSION     WP_284488854.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..424
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=48073
     Region          33..395
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mtatiitals davirrhsqd psvrqikdpr fsllfrfhkd rdrgsfhlrh yqggrerwkk
       61 vgafpdmttk vlfarlpeik gqlavdpasd nlavstwatv gdllcwyrdr sgdnanvsss
      121 rrssvksain rqllpvlsdv plgafsseke grtlldekli wpmqstysls fvksvfgvlk
      181 aafkqayrlk riesnplapw vfsdfiqari kpkdpslrve rltdfmgrlp acqgperlip
      241 llmllhgtrv getrhhrwdw idwrgstlti pgrftknkre hqiplssvav qalkeyqasq
      301 srrgvssvwl fpgakpgrpi gktkanelfq visekawtsh dlrklartvw adlgvdyivg
      361 elllnhtlkd ldatyihtam avqkrealtr yhdwlilqgl tietetetrs rkntpadqts
      421 eaaa
//
LOCUS       WP_284489047             352 aa            linear   BCT 25-DEC-2024
DEFINITION  GGDEF domain-containing protein [Aeromonas caviae].
ACCESSION   WP_284489047
VERSION     WP_284489047.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 352)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 352)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..352
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37706
     Region          79..334
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mdklllalse qvikardles ltrpllemla svtglestyl teidlgqssq hvlfarnvag
       61 lqipegmtve wsdtlcrrai ddeigytgdv aalwgdsqaa selgirsyls spvrtstgsl
      121 ygtlcgaste qkpavagaqq liaffahlia eqvereqllr qlqqandels rlalsdsltg
      181 lpnrralmle ltrlfslser aghpvliafv dldgfkaind ehgheagdrl ltamarqlse
      241 tlrggdllar fggdefvavg mgpfpdadtl dgavaafrqr lfehsvlslp vgdkvihypg
      301 asvgavavmp aevsveealn radasmyvvk rqrraagegg npppssqvsa pr
//
LOCUS       WP_284489171             266 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Bacillus sp. RB3].
ACCESSION   WP_284489171
VERSION     WP_284489171.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. RB3
  ORGANISM  Bacillus sp. RB3
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Bacillus sp. RB3"
                     /db_xref="taxon:3050012"
     Protein         1..266
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30907
     Region          3..254
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(18..19,21..22,25..26,63,67..68,71..72,110,114,121,
                     124..125,130,145,149..150,152..154,156..157,160..161,
                     164..165,192..193,195..197,199..201,203..204,206..207,211,
                     214..215,221,223)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(148,152,155..156,158..159,206,209..210,212..217,
                     220..222,226,228)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(169..176,194,197..198,201)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mhstyfhrmd gvvklflfif cmtltflffd frvllilfii gciglsiaki pfrkilivfs
       61 viftfsllns vmillitpth gseltesyta flhvgyatit yetlfyaatl slkyftllpf
      121 tllfiyttdp sefvsnlskl gihykityai nialryipdi qseykiikha qeargvafek
      181 geaslwvrik nrvlifwpli ihsleridtv snamdlrgfg kkdkrtwfyt skakredfia
      241 lfagififiv avylklnvfq nfwypf
//
LOCUS       WP_284489433            2178 aa            linear   BCT 25-DEC-2024
DEFINITION  amino acid adenylation domain-containing protein [Bacillus sp.
            RB3].
ACCESSION   WP_284489433
VERSION     WP_284489433.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. RB3
  ORGANISM  Bacillus sp. RB3
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 2178)
  AUTHORS   Konz,D. and Marahiel,M.A.
  TITLE     How do peptide synthetases generate structural diversity?
  JOURNAL   Chem Biol 6 (2), R39-R48 (1999)
   PUBMED   10021423
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01733.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2178
                     /organism="Bacillus sp. RB3"
                     /db_xref="taxon:3050012"
     Protein         1..2178
                     /product="amino acid adenylation domain-containing
                     protein"
                     /calculated_mol_wt=249885
     Region          21..>1911
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
     Region          1921..2157
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mldkftqqvl lssekfkkek eywldklsgd velsrfpcdc lslnnfqask esyycqfpsd
       61 iakravaisn nsdmllytil lsgvkyllsr ytnrddvvig mpvfkqgqee tvfqnnflll
      121 rtqinqednf keiiykiket ilesnehchf pfnkltqlls ldgesnnlpv lntivmlddi
      181 hcyestdkin sdmvirfmkn eeqlkvqvdy nstlyseglv srivnhlyni ldilmkdpnk
      241 samdldvmpk teknqilfdf nhttkvhktl lcetvtapql feeqvkqnpn qiaivcngke
      301 itykqlnika nqlarrlldq gvkresivgv mmersiemiv gilgilkagg aylpidtdlp
      361 kqrveymltd sgcshvltyq nsiikgvafq gsvinlmdip feeeqledlq itmepqnlay
      421 viytsgstgq pkgvmiehrs ltnflcamye dfsqdigitd nvlfsssisf dvtifeifvp
      481 lvygarmtiy qgekfdvpkl vqvileeqvt layipptlln eiydyfvrsn qkislnklfv
      541 gvepiktell akydhlfrgn lqilnlygpt eatvcctsyq yerdkeittq nvpigsplln
      601 tkiyildsfh rlqpigipge icisgiglar gyinrkelta dkfidhpfeh geklyktgdi
      661 arwlpdgnie ylgrvdhqvk irgyrielge ieasllkyet iktavviqre desgekylca
      721 yvvtekdipi pevraylatk lpyymipqqi isiqnipltq ngkidrkklp qpinnlkssh
      781 leptnsterk lveiwkdvlg iqrvgirdnf feigghslka trlisivnke fnvqlsiksl
      841 fkfpilvdfs kcilemeksn yisiepvkqq eyylastsqk rmfivdqfed gtnttynmpt
      901 ilkvagdick dkfenifqsl ierheilrts fqildgelvq kiepnvdfni eyvhvnekda
      961 dylihefisp fdlskppllr vlllriaeer hilvvdmhhi isdglsmgil ikefvelykg
     1021 nelpklrvqy kdyvmwqngp yyknliseqk nywlttlkge lpvlnfptdf qrptiqsfkg
     1081 nvcsftlgrd ltfkvnklat etgttpymil laiynillsr ytgqediivg spiagrshsd
     1141 tnhmigmfin tlvmrnylen ddefieflsr lklntleaye nqdypfeell egldlhrdts
     1201 rnplfdtmfv fqnmdmnpis igeleftpyp fkqsvskfdl slvateidnn ihlkveystk
     1261 lfkaetierl mvhftnivee vtnnprvrlr ninmlsieee hcimnefnkk ensnsnhllv
     1321 hkmfeeqvkr npnqiavvcn ekgityneln ikanqlarrl ldqgvkresi vgvmmersie
     1381 mvigilgvlk aggaylpidt dlpkqrveym ltdsgcshvl vhqnsiikgi efqgnvidlm
     1441 dmsfeeepge dmqmmiephn layviytsgs tgqpkgvmie hrsltnflca myedfsqdig
     1501 itdnvlfsss isfdvtifei fvpliygarm tiyqgekfdv sklvqvilee qvtlsyippt
     1561 llnevydyfv rdnqkivlnk llvgvepikt ellakydhlf rgnlqilngy gpteatvcct
     1621 syryesnkei ttqnvpigsp llntkiyild sfyriqpigv pgeicisgig largyinrke
     1681 ltadkfidhp fergeklykt gdiarwlpdg nieylgrvdh qvkirgyrie lgeieasllk
     1741 yetiktavvi dqedeageky lcayvvtekd ipipevrayl atklphymip qqlipihnip
     1801 ltqngkidrs klpklntldn snyvpprndi dsslidiwss ilgvnnigin dnffelgghs
     1861 lkglklfeni krmfnvqlpl sllfqnatie qlsdvisrnk gidseclipi qngtnkdsqw
     1921 fivhgqgggi lnyydlarel gedktvyglq sigyddnrfs nlsveemavr yieeikqvkk
     1981 egpytllgws fggivafema rkleelgdkv sflglldvhp ieqgkeilsl niknafeele
     2041 kfndqlgiek isfeqmseeq liesllkkft lnenscqqnf edpmmnklkv mianryaylk
     2101 ynckqkikad iflfnasind ihplvdynrw neytsgevya lqvpgshlsm lekphihelv
     2161 ksikmsfkqm lllahvnr
//
LOCUS       WP_284489023             494 aa            linear   BCT 25-DEC-2024
DEFINITION  M17 family metallopeptidase [Aeromonas caviae].
ACCESSION   WP_284489023
VERSION     WP_284489023.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Lowther,W.T. and Matthews,B.W.
  TITLE     Metalloaminopeptidases: common functional themes in disparate
            structural surroundings
  JOURNAL   Chem Rev 102 (12), 4581-4608 (2002)
   PUBMED   12475202
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087321
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     Protein         1..494
                     /product="M17 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=52586
     Region          26..483
                     /region_name="Peptidase_M17"
                     /note="Cytosol aminopeptidase family, N-terminal and
                     catalytic domains. Family M17 contains zinc- and
                     manganese-dependent exopeptidases (EC 3.4.11.1), including
                     leucine aminopeptidase. They catalyze removal of amino
                     acids from the N-terminus of a protein and...; cd00433"
                     /db_xref="CDD:238247"
     Site            order(45..46,59,73,85,180,182..184,228,230,259,265,270,
                     273,276..277,309,311..314,316,318..322,328,330,334,
                     370..374,377,403..404,406,411,413..414,419,421,431..432,
                     434,469)
                     /site_type="other"
                     /note="interface (dimer of trimers) [polypeptide binding]"
                     /db_xref="CDD:238247"
     Site            order(255,260,267,278,337,339,341,365)
                     /site_type="active"
                     /note="Substrate-binding/catalytic site [active]"
                     /db_xref="CDD:238247"
     Site            order(255,260,278,337,339)
                     /site_type="other"
                     /note="Zn-binding sites [ion binding]"
                     /db_xref="CDD:238247"
ORIGIN      
        1 mmtpfsyssp qitmqntsla evmagsaavk llliadsard tllatppfaa vatqialgqk
       61 apyslddsqg lqrvifmdar pvldhrlykq vrswvgslag lkathlalhl egfddehraq
      121 larvvlacll aadvtlptqk rseatrpgyq qlqlsppcel dmarlsaeae gnglarhlav
      181 lpaseldaqg yrafvqqlaq qegwqwqefd eaalatlgag aflavargsa ngqaaivrls
      241 ycpanpvrrl alvgkgichd sggynlkvgg smygmhldmg gsavalgtll aisraklpve
      301 vycwlaiaen higpqafrpg evvtalngtt ievvdtdaeg rmvladaltl aagdnpdlli
      361 dyatltgack ralgsrysga ftnrpewltt lialgqqsge rvwpfplded yddnldsewa
      421 dllqcapgas pdhidaarfl trfvpaelpw lhldlsgfrn kggngvvgse vtgfgvrltl
      481 tlldsplgmg apda
//
LOCUS       WP_284489440             476 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Bacillus sp. RB3].
ACCESSION   WP_284489440
VERSION     WP_284489440.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. RB3
  ORGANISM  Bacillus sp. RB3
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Bacillus sp. RB3"
                     /db_xref="taxon:3050012"
     Protein         1..476
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=55850
     Region          2..473
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mqnkiivmfq kdfrlydnpa lfeavqsgev lpvyvqdetf sigsaakwwl hhaiidvqkq
       61 lkalgstlii rkgniqeeil slikqldita vywnscydpd rlksnqkmkm iledkgiick
      121 efnshlllep wiikkkdnte ykvftpfyna fqkqvipkpi srvqsikwgs slpaslsvse
      181 lhllptipwt shmeaiwept eegayktfkk ffssklasys egrdfpnqna hsmlapylsf
      241 gqisvklmyh ylinksterq csffekqvis firqliwref syymlyhypf taykplnknf
      301 ehfpwnkeee llrvwqkget gypfidagmr elwqtgfmhn rarmavasfl vkhllipwqe
      361 gakwfmdtll dadianntmg wqwvagsgad aspyfrifnp itqgekfdkn geyirrwvpe
      421 lrdipnkyih kpweapehil qksniklgnt ypypivehka ardralcayk nmkefv
//
LOCUS       WP_284489441             405 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Bacillus sp. RB3].
ACCESSION   WP_284489441
VERSION     WP_284489441.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. RB3
  ORGANISM  Bacillus sp. RB3
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Bacillus sp. RB3"
                     /db_xref="taxon:3050012"
     Protein         1..405
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46383
     Region          27..391
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mdlqkgklyw nttfsntssy prleedikcd vliigagssg aqsayylses dlnivvvdkr
       61 kvghgsnltn taliqylgdk mffelvntfg eeyavkhmkl ceqaindiey adqnlpycsd
      121 fkrrdslyya syeedikkle kelyylhkhd fkatwlseeq igqrypfkkr aaiytyndge
      181 inpykfthsl leqaankgvq iyedteivgk klekecaify tkggnsitan kvivaagyeg
      241 lefkkeknat lissyavvtn pvedlsswyk rtliwetarp yiymrttadn riiigglded
      301 tniaqerdsk lihkkekivn efnklfpnit vepefylsaf yggthdglpi igmyeefpnc
      361 hfiyaygdng lvysmvlski vrdiiisgss pdlnlylqtr pklne
//
LOCUS       WP_284489663             271 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein,
            partial [Bacillus sp. RB3].
ACCESSION   WP_284489663
VERSION     WP_284489663.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. RB3
  ORGANISM  Bacillus sp. RB3
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Bacillus sp. RB3"
                     /db_xref="taxon:3050012"
     Protein         1..>271
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
     Region          3..>271
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 mervvitgmg vvspigndik tfwnnlikge sgivnidtfd vtnhktkiag fvqdfdadev
       61 lgkkearrld rfsqfalaaa eqawsdskld ldridverlg vyvgsgiggi etlienvdal
      121 rqkgprrvsp tlvpaimsna aaaqisikwn amgpsmspvs acaigntsig eafrlirsge
      181 advifaggte saitdlsias fgnatalstr ndnptkasrp fdenrdgfvm segagilile
      241 slshalhrea kiyaevigyg assdayhiva t
//
LOCUS       WP_284489897             325 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Blastococcus
            capsensis].
ACCESSION   WP_284489897
VERSION     WP_284489897.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..325
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35220
     Region          4..321
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 maakraerlv nlviallstr qfvtaarira tvpgyeaddg taradeafkr mferdkaelr
       61 emgvpletgr tsvfdtedgy riaradyelp eihltgeeaa avglalrlwe saqlagaaqs
      121 alvklraagv dvdtsrtlpi qprldrgeaa fepcyaaard rrrlqfdyrr pdedtavrrd
      181 vqpwgvvawh grwylvghdr drqaprvfrl grvvgtpkav gpagafeppa dldltavvag
      241 qaggeeqlvv vrvrpgtavg lrrhatslgp agdgddrlql rttepwalad qlaaygadvv
      301 veaptgmrda viarltrlaa mgvpa
//
LOCUS       WP_284489918             300 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Blastococcus
            capsensis].
ACCESSION   WP_284489918
VERSION     WP_284489918.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..300
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=32423
     Region          49..271
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mgaavsigar lqswhprtpp lpqdladlvr pgdpewfare laiavappww vwrlllrrfs
       61 wlvglfgrve vtgsipeelr rgplllaanh igdfdpvvia valsklgvap rimttggivs
      121 apvagplier tgairvergt elarhavrvt evalvhgghv vaypegrvgl apdfwpergr
      181 tgmarlalgl qvpvipvsqw gahevlqygn dwgklrtllr avvrrpalrv hvgppvvfdd
      241 lqmgrvgdan rarlriaaal trglrrlrad eldapafddp trpttavaaf pggivpddip
//
LOCUS       WP_284490015             291 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Blastococcus capsensis].
ACCESSION   WP_284490015
VERSION     WP_284490015.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..291
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=29684
     Region          3..273
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mkpapfryad pgsldealev laeegakvla ggqsllplls mrlaapatlv dinrvpglds
       61 ievtgdgvtv galvrhnsll hddaaarsqp lltratanva hpavrnrgtt vgsiahadps
      121 gemtavlalt dgsvtvagaa gsevvgwrdl fvgpletsia gpavvtsaff palpprsgta
      181 fqevarrkgd yavcgagvvv tldagrrvas vrasyvsvgl tpevhdltea vagspvekad
      241 waaagalart lvdpdtdiha sahyrrllvg vltertlaea aaeaaaratr e
//
LOCUS       WP_284490036             326 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Blastococcus capsensis].
ACCESSION   WP_284490036
VERSION     WP_284490036.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..326
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34247
     Region          1..324
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mkrtrsavla wtpvlalsla acsggdsggs tgadggfepr gdvtmvvpfg agggsdlagr
       61 atgtmieaan edltvsvenr eggsgavgys yflgesgnen lllatetall alpisgevef
      121 dytdftpimk laddftlmiv nadspyqtca dvveaakser itagisgitg ldnivftlte
      181 qetgaefdrv pfesggelta allggqidia slnpgeiigq lesgdvralc afseerydye
      241 aladiptaae qgidvsfaqf rgvlapggis eearqywidt meaaveteey qtyiednylq
      301 pntasgdefv eylegnnell qqvige
//
LOCUS       WP_284490038             421 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Blastococcus capsensis].
ACCESSION   WP_284490038
VERSION     WP_284490038.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..421
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44226
     Region          4..397
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mavetngpla gitvlevgaf maapfatmql adlgarvlki enptggdpvr dtgpfldges
       61 spfvrlnrnk esvaldlksp egkqaflrla aradvlvenl rpgamrglgf gyeairevnr
      121 rivyasasgw gqdgplaslp gldimaqarg glmsitgtpd gdpvkigvpi cdlvcamyva
      181 lgvtaalker drsgegqyld vsllesgvsf aiweagkyfa tgevgrplgs ahqstapyqa
      241 vrtsdgyvtv gavtpktwkg lcaalgleel ldderysdas trhghrdtli paieaatttr
      301 ttdevvaald eagvpcapia dygqvftddh lnqrhyfwda phptlgpvrq lgspmrlsrt
      361 parqdsagpq lgagtraale waeipadevd eliesgvaad pahavaaspa applpaddrp
      421 l
//
LOCUS       WP_284490184             201 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Blastococcus capsensis].
ACCESSION   WP_284490184
VERSION     WP_284490184.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..201
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21218
     Region          39..153
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mtepsmwtrl teenpehsaa yiqrfrdlaq aghdlvgear lvdamlprga rvldagsgtg
       61 riggflaaag hrvvgvdgdp vlvaeargqh paarwlvgdl aelelpaage adpfdvivca
      121 gnvvtflaps trgavlrrlr ahvapdgraa igfgagrgye fdeflddara agwtpdllla
      181 twdlrpftgt sdflvallrp a
//
LOCUS       WP_284490267             529 aa            linear   BCT 25-DEC-2024
DEFINITION  ParB/RepB/Spo0J family partition protein [Blastococcus capsensis].
ACCESSION   WP_284490267
VERSION     WP_284490267.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..529
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=55090
     Region          41..283
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mtstlpyggd adagslpfgg asapsaddka ghpapaedpv qqlvwldpst ltihprnird
       61 dlsdlsglat siaaqgvlea ltvvphakgd gtighllvag hrraaaalla gvpsvpcvvr
      121 pdlaaepddl agqarhvgam laenlhraal taveeargvq tmldlgdslt evarstglgr
      181 nrvtkaagva rlpadtaaav saagltldqa aavavyadda ettaaliaaa gegagqfaha
      241 ltrakrarqe vekiavlsad ltaagrtlld aaegrgqtri sqlahdgefl taevhascpg
      301 savyiatawn gpqavevctn paafghagry sgdpipntql aeeerdatde rritivnnre
      361 maaanetrre wvraflmrks vpraalrfav etmasdprvl arwlsgqsnl aqdaasadlg
      421 ieapglwrtt kgeltltsgk lvpdgrlpiv llahvagaie tamhrgtwrd pratdarwlr
      481 flagygysla eieqrivdgi dertssddfa phdndaasdp ddngapeac
//
LOCUS       WP_284490306             369 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Blastococcus capsensis].
ACCESSION   WP_284490306
VERSION     WP_284490306.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466432
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..369
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=39577
     Region          7..368
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 mpgrdvvdtv lgfartlrha gvgaspdrvs amlsalghld vldpaavywa grltlcagpd
       61 dldrydvafl awfsgqrari prtaaqpevr laasapldag tgegdddgda pdlaaqasad
      121 evlrhrdvag ltdaerahlr qlfallvpas pmrparrrrp avhgaihpgr tvrralrdgg
      181 evsrllhrra rprprrvvll idvsgsmtpy adallrfaha avrarpvste vftigtrltr
      241 vtrelrlrdp dralaaggqa ipdwsggtrl gevlkafldr wgqrgtarga vvvvcsdgwe
      301 rggtdllaaq marlrrlaha vvwvnphkgr sgyepltggm qaalpsvdhf vaghsmaafe
      361 elsgvisra
//
LOCUS       WP_284490330             285 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Blastococcus capsensis].
ACCESSION   WP_284490330
VERSION     WP_284490330.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..285
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=29834
     Region          3..284
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mipapfeyar pttvdevlqa laeggedvkv laggqslipv mrlrlaapet vvdlgrvael
       61 rgvreeddai vvgamtthsd vladplirqy aplvaeatat vadrqvrhrg tfggalvhad
      121 pagdlpaval aldadfviag pegrrtigas effvdyltta vqegellvev rlpklagswg
      181 mhyakfnrva qawsivavaa avrredgria earigltnmg ptplrarqve ealagaeatp
      241 eavaaaaaha aegtepssdl naqadyrqhl atvltrravs taagl
//
LOCUS       WP_284490355             476 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Blastococcus
            capsensis].
ACCESSION   WP_284490355
VERSION     WP_284490355.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..476
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48776
     Region          7..445
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mpkpptsdtv dllvigggta glvgahtaat lgartmlveq drtggdclwt gcvpskavla
       61 aataaadarg tgrlgvgtge vtvdfarvra hvesaiatiq pkdspaslta agvrvvlgta
      121 vltgsdtalv dgrpvrfraa llatgaaplv ppieglgtvd altsetlwdl eelprrlvvl
      181 gggpigcelg qafarlgaev tvvdgsdrvl gpedadaaal vaaalrrdgv elrlgaegtr
      241 vepgllhldd gssvpfdrll vavgrrprts dlgldaagve ldehgavavd dslrtsnprv
      301 waagdvtgkp yfthvsgmhg siaagnavlg lrrtvdpvvp rvtytspeva svgvspaear
      361 ergltvrrva hssvdravae gvtegftslv tdgrrrlvgg vvvgpraget lgeltlavrk
      421 glttadlagt thayptynda lvdaavkdvr arfarpvvrg vlrafvavrg rlldrr
//
LOCUS       WP_284490376             351 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Blastococcus capsensis].
ACCESSION   WP_284490376
VERSION     WP_284490376.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..351
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35466
     Region          42..347
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mattvdvpar daarpsaprl rarrlgtlll llvlvvaavl vsiavgtrsi gigevwgall
       61 dsspdtdeav ivrelrvprt vlgfmvgaal avagalmqgh trnplgdpgv lgvtagasla
      121 vvlaisllgi ttpggyvwfa fagalvsmvl vyaigsagrg gatpvtlala gaalsallfa
      181 lvraivvade qtldsfrfwv vgslagrdaa vswqvapfla vglvlalvna palnllglge
      241 dvarglgqri wlaravglaa itllagaata aagpiaflgl vvphavralt gpdhrwllpc
      301 sallgaalll vadvvgriva rpgelqvgiv laligapffi alvrrrrtag l
//
LOCUS       WP_284490457             371 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Blastococcus capsensis].
ACCESSION   WP_284490457
VERSION     WP_284490457.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..371
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=39797
     Region          7..367
                     /region_name="Tdh"
                     /note="Threonine dehydrogenase or related Zn-dependent
                     dehydrogenase [Amino acid transport and metabolism,
                     General function prediction only]; COG1063"
                     /db_xref="CDD:440683"
ORIGIN      
        1 maeqvlaavr tgpgttelre fpmpeiadda allkievagi cgtdvklyrk ptidapvimg
       61 henvgivaka gakwqeihgl regdrifveh yvgcmhcewc rlgeyrhcel tdwrtnpdar
      121 rygytssdnp grlwggfsqy mylpwnavth kvpdgvtael aglvtplsng iewalnaggv
      181 gyaktvliqg pgqqglsqvv asrqagasli vvtgttrdat rlqlakdlga davvdvlqed
      241 alatvleltg gkgvdvvldc tsgagtapvl lgidalkrre gvmvtqgeea afpdfplkkm
      301 tekcitlasa rghsyrsvel alaqlashrf plerlathsf gledvdhair alagetgeda
      361 lhislkpwgh e
//
LOCUS       WP_284490509             442 aa            linear   BCT 25-DEC-2024
DEFINITION  CynX/NimT family MFS transporter [Blastococcus capsensis].
ACCESSION   WP_284490509
VERSION     WP_284490509.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..442
                     /product="CynX/NimT family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45373
     Region          26..399
                     /region_name="MFS_NIMT_CynX_like"
                     /note="2-nitroimidazole and cyanate transporters and
                     similar proteins of the Major Facilitator Superfamily of
                     transporters; cd17339"
                     /db_xref="CDD:340897"
     Site            order(35..36,39..40,43,75,125..126,128..130,133,152,
                     155..156,159,231,234..235,238..240,243,270,274,323..324,
                     327,331,348,351..352,355..356,359)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340897"
ORIGIN      
        1 msrtarsapa ppadepsrrg vgliavaivl tglnlrtavt svgpvleeiq kglgissgll
       61 glvttmpvlc faligftgps lsarfrdshv lagallamsa glvlrstaga fvlflvgtal
      121 amvggalgnv llpslvkrhf pgrtgllvga ystamsvgaa vaavstapia aatgpngwrw
      181 algiwavlal vaatpwlavr atggtsrqth vsvrmrelvh srlaiamavf fglqsmqayv
      241 iigwsaqylr dtglsaaaag lllglnsvvg iplsavvpal tvrpriqrpl lcgfvacyvv
      301 gwlglwltpl aapwlwmtll algmgtfamv ltlmglrart pettaalstv tqswgylfsa
      361 agpllvgvlr gatgdytgmf vlalasvagl avtgwvvtrq ryvddevpgw spvqpredvl
      421 evagaeppvs spagrdggsp pg
//
LOCUS       WP_284490564             435 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Blastococcus capsensis].
ACCESSION   WP_284490564
VERSION     WP_284490564.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..435
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46761
     Region          147..412
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtspsplltg spvppaphlv eglyrrlges arrmvaefvr eiplyrrlpd eqlhgeiaqv
       61 crdnvlafvr ccrehrlpah geltaasaga arraeegvpl davlmayvig nqvtwqmlre
      121 qmppgqesev vsftpflqry lqamlhavtd ayveerrsie rydgsawrdl vrsvlegtpq
      181 velaerlgaq ladcytvval hlgptgdeqd advdpdvagr rkvrrvqaai drlpgrattl
      241 aslipagglv llpgcqgrlp asaettrave llaraadaep tavmvsapsp ealpnaaaqa
      301 rglldlvrll grpsgvhtpd dlvlehqlaa pgparerlaa lvqplrahpd lletarswla
      361 hdrgrretae tlhvhpntld krldriaqlt giqlsttrgv gllqaglvam hvhdstlgps
      421 teggrsagtp tspga
//
LOCUS       WP_284490699             192 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Blastococcus capsensis].
ACCESSION   WP_284490699
VERSION     WP_284490699.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..192
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20451
     Region          53..190
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mrrtvlalla gaalvsgcst gsdqvqanng gefrfvaatp vgevipeger avapefsgtl
       61 lgggefssee lagdvavlnf wgswcapcrv etpefqevya evrdegvefv glnvketseq
      121 falafverfg vefpsvydpr gevalafrdy panaipstiv ldrqgrvaav ytgavtqedl
      181 ravldrllae ev
//
LOCUS       WP_284490712             529 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Blastococcus capsensis].
ACCESSION   WP_284490712
VERSION     WP_284490712.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..529
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56031
     Region          24..415
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mtlryrlsal asnggdqvtv psvgvtcivg gnnagksqal rdivqiisdr sarpvavtai
       61 aaaltgdlsq seewlettav rqpappgypp sytpthggnq ltleqfntwi rgasdgllsh
      121 aatffywhat agalvgyatg gmgtpgmgpa asplgalfrd gdleerlsvl srevfgqplt
      181 ldrvngdvrl rvgdpglpap plnrptlqya davrrlasle hqgdgmrafm glalyvvagg
      241 aqvllvdepe aflhpaqara lgrwlateaq aqdrqiilat hdrdlvlgll daeapvkmir
      301 isrnsdrtsl helseaelsd iwadpvlrys nvlqglfheq vvvceadadc rfygavldal
      361 atesgsrsla datlfvpsgg kqrapvlaga lsrlgvsayv iadfdllndr dqlkaalvsv
      421 ngvwdqdldr lylavagwan qtsawpslkt qglsglkagt vysagkdlld rlasmrlllv
      481 pvgemesfdk svdghgspwv samlekgghk ssaearqlvg plaarsaat
//
LOCUS       WP_284490779             469 aa            linear   BCT 25-DEC-2024
DEFINITION  purple acid phosphatase family protein [Blastococcus capsensis].
ACCESSION   WP_284490779
VERSION     WP_284490779.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Klabunde,T., Strater,N., Frohlich,R., Witzel,H. and Krebs,B.
  TITLE     Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on
            crystal structures
  JOURNAL   J Mol Biol 259 (4), 737-748 (1996)
   PUBMED   8683579
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11244734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..469
                     /product="purple acid phosphatase family protein"
                     /EC_number="3.1.3.2"
                     /GO_function="GO:0003993 - acid phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=51267
     Region          <88..114
                     /region_name="Pur_ac_phosph_N"
                     /note="Purple acid Phosphatase, N-terminal domain;
                     pfam16656"
                     /db_xref="CDD:465220"
     Region          153..405
                     /region_name="MPP_superfamily"
                     /note="metallophosphatase superfamily, metallophosphatase
                     domain; cl13995"
                     /db_xref="CDD:472684"
     Site            order(160,162,199,243..244,341,377)
                     /site_type="active"
                     /db_xref="CDD:277317"
     Site            order(160,162,199,243,341,377)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277317"
ORIGIN      
        1 mpdthfepfv hlvdlapdra liawggfwfr rddsdgrwqv vgddelgdld lgrtgsigar
       61 sepygsavve vfdrsgdiva eartdtgnhv rvdglspdtg yryrirvdgl pwaegprmdw
      121 gpvprggldl rpgdraydlr frthpspdva vpldfavlgd ygigvltdtg sgrrqrqvad
      181 vldrlteepg vrvvitvgdn vypsagtrgs qgsgaqdsdw ygsfyqpyry alarvpmypt
      241 vgnhdtsdae ssddreqird nfhtdarftp evagsrasad pgmfyrfgfg advefvcidt
      301 slsrelpteh ffedpghqdf ldeafpddgg agrwwrfpfs hhpaycagph hpntaamver
      361 lvplfaragv raafaghehn fqlsrvdgid yfvsgaggkl redppegfgp agtvawaaqa
      421 hlllarvdgd tltvtpltav grdgaaerlt prapdgavve vpfvvrrdr
//
LOCUS       WP_284490888             771 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Blastococcus capsensis].
ACCESSION   WP_284490888
VERSION     WP_284490888.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 771)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 771)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 771)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 771)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..771
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..771
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=81320
     Region          90..759
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 maqwatrgas tsasgrllal tvalvaafaa glvhrpagsl wtdlhalvay nlpylpaaaa
       61 cwlaaaripp ertawrslav glllsipsna lrtaaaqapd sdvllygayg fssaaylcly
      121 gtlfgfirar vprfhpstwl dgligalgtv svgvafllgp yldgssgvll pmaqlawpaa
      181 dvvlmatlva vgailgvnvd rtlllstaam gfvllgdllf fwatvhgtaa dgdplelawl
      241 tgialtalaa hsarpdslpg sapaenratd grarvgwrll alplaaqtag llvlavgwgd
      301 alppaaawta igcalaalar tavtfrevra fheveqqart deltglanrr allekaeqvl
      361 vsasaprpaa lllldldgfk evndslghta gdqllrqvgp rllpalrtge mlarlggdef
      421 avllpeasld eaharaerlr almlqpfpve dirlhvgvsi gvatapvpaa tfqellrcad
      481 vamyaakaar egvhvyvpdp hggsgdrlrt meelraalhg dellvhlqpq vgfadgrvvg
      541 vealvrwqhp irgllspadl lpaaeqaglm rpltdkvlel altaaelwws tgavpvsvnl
      601 saanvndldl pgkvaaalhr hglpaealtl elvedtlmad pergrqvlae lrglgvrtsi
      661 ddygtgyssl aylrhlpade lkldrsltad vvsdrrasai vrhtvalahd lglrlvaegv
      721 edaascaalg rlgcdvaqgy aiarpmpvgd flhwlerpqh plldpersar y
//
LOCUS       WP_284490935             253 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Blastococcus
            capsensis].
ACCESSION   WP_284490935
VERSION     WP_284490935.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..253
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27179
     Region          2..214
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mlfywflkfv aigpparvvf rpkaegvenv patgaailas nhlsaadwif vplqlkrrvt
       61 flakaeyftg tgvkgflqra fftgagqvpi drssasaaed aiqtglrilr dgkllgiype
      121 gtrspdgrly rgkmgvarma letgvpvvpv amvyssralp fgkkitrvri rvgkpldfsr
      181 yeglagdrfv ersvtdeimy eimtlsgqey vdvygatvkk smdatgasan eviaglqppa
      241 geaadraptt lag
//
LOCUS       WP_284490944             337 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Blastococcus capsensis].
ACCESSION   WP_284490944
VERSION     WP_284490944.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..337
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35727
     Region          6..335
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 madrlvdlrs dtvtrptpgm rramaeaevg ddvyaedptv taleervaal fgheaalfvp
       61 sgtmgnqigm rlvcepgqei lcdadahvvt yemgaaaaif gistrtvvss ggrldaaqli
      121 eqvrpqdnwh ltataavave nthnrggglv qpldqlralw dwsrgagvav hldgarvwna
      181 hvasgvdlat ygrladtasv cfskglgtpv gsvlvasaer iatarlwrkr lgggmrqvgv
      241 laaaclyald hhlprlgedh ehaqllaerl gvdpatvqtn mvvlddleap lvaeaakaqg
      301 vlvsqvsarr irlvthldvd ragieraadv laelldr
//
LOCUS       WP_284490971             545 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Blastococcus capsensis].
ACCESSION   WP_284490971
VERSION     WP_284490971.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..545
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56398
     Region          9..526
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mtpptapset vdvvvvgsgh nglvaacyla reglsvevve sdevlggavs tverwpgvrv
       61 drgssahviv rhsgiveeld lathglhyid cdpwgfapap vpgdagpdgr plvfsvdlda
      121 tcasieaacg padaaayrrf vevwqprsra vvasfgraps aggllrsfwp lgapaegrar
      181 tpggelavdf lgsgdalldr wftserlkaa lawfgaqsgp pmsepgtaam vgwvallhdv
      241 ppghpvggsg gltqalrrrl esdggrvvlg dgaarllled grvagvetrs grvvrapavv
      301 aachigvtre lagdaappvl adaappigng fglvvraltd appsypgvaa adalqglqll
      361 ctdrgqlaaa hgdwgagrvp repvplamsf sasddtlapp gqhvvtiwgq wypyaladgg
      421 dwdaladtea rrlvaavdry apgfaasvre myvqtplale relslprgnv mhvemglasm
      481 fafrpapgls gyrvpglrgl ylagasthpg ggvsgnsgrt aartvlaerr alpraraaar
      541 ralrr
//
LOCUS       WP_284490972             202 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Blastococcus capsensis].
ACCESSION   WP_284490972
VERSION     WP_284490972.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 202)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..202
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21944
     Region          109..179
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtdtrpatri velpppwmre hmhevltvyg lamgydsgvv agrygyaiqh terpgfravg
       61 afaqtgtggg etaerlvgfg ygylvapgqw whdqvraald rrtakkwlpg afevcelhvh
      121 pdaqsqglgr rllhalvegl phpvallstp dadtkafrly radgfvdlar gyhfpgdsrp
      181 failgaklpl hppapsatns ra
//
LOCUS       WP_284491072             321 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Blastococcus capsensis].
ACCESSION   WP_284491072
VERSION     WP_284491072.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..321
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34582
     Region          60..308
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 msltrrqfla aaagvggaal tggvladqvw pllsredlvp grtpelvlps qawtttpdrl
       61 tfaavgdtgt ggrqavavat rmaqgyeqnp yglithlgdi cyygkienrf ddvflrpygp
      121 lieagvdvel aignhdgevy fsdarleeie telrllgtpa ryyrtthgpv dffyldsstp
      181 glfgsgasaq ldwlddalat stsqwkivcl hhppyssgrh gatpgaedml vpvlerhavd
      241 lvlaghdhny ertipldgit yvvsgggakl tpvrpsrita aaasvlqylh vevdgdrlta
      301 rcirpdgglv drftlrareg r
//
LOCUS       WP_284491141             181 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Blastococcus capsensis].
ACCESSION   WP_284491141
VERSION     WP_284491141.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..181
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=20322
     Region          23..132
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mskksqltdr vgrlvahrlv gtrpwsdavv egiarsstgm kvleigsgrq dmgheayslr
       61 rlfggsdefv qsdvnpafgh rvidvtdmdi dqefdlilcm yvlehvfdvg aavesmrral
      121 rpggrlvvav phlypyhdep idfwrftehs lrqlcsafss vevtrkgirr wpkallvvat
      181 r
//
LOCUS       WP_284491225             296 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Blastococcus capsensis].
ACCESSION   WP_284491225
VERSION     WP_284491225.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..296
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32111
     Region          86..190
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mrpssdldsr pgwhteadae vtprglralc spttltgglt elawvgahvl myplgtrmea
       61 lradphkrag aqpaavralf aadplaarvp vllvhglvdn rsvfavmrrs lrkrgftsvc
      121 swnyspfltd idqgatdlgr hierlcrqtg hdrvhvvghs lggliarhhv qrqggdrrid
      181 clvtlgtphr gsvlahllpt plirqlrpgs pllreldepa pecrtritav ysdldqmvlp
      241 tqsgrcdhpd laarnvlvrg vghmslpihr gvldevastl agvrqdsdtr plaava
//
LOCUS       WP_284491298             289 aa            linear   BCT 25-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Blastococcus capsensis].
ACCESSION   WP_284491298
VERSION     WP_284491298.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 289)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..289
                     /product="MlaE family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31016
     Region          23..279
                     /region_name="MlaE"
                     /note="Permease subunit MlaE of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG0767"
                     /db_xref="CDD:440530"
ORIGIN      
        1 mallspvdri rvgarrfarv vyrrpldtld dlgdqlgfyg ralgwaprtl rrykretfrl
       61 laevtfgtga laviggtvgv iaflsfftgt evglqgyaal dqlgtsaftg flsayfntre
      121 iaplvaglal satvgcgfta qigamrinee idalevmgvp slpflvttri iagfvavipl
      181 yvlglltsyf atrtiatqaf gqstgtydhy fnlflppedv lwsflkvlvf avviilthcy
      241 ygyrasggpa gvglavgrav rfsivainii dlflslaiwg stttvriag
//
LOCUS       WP_284491316             387 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Blastococcus capsensis].
ACCESSION   WP_284491316
VERSION     WP_284491316.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..387
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42419
     Region          104..357
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mggeaqgsrg wrrravasia krpdgtyrpr yrdengkeha rhfkrkvdaq rwldeqtaai
       61 vtgdyvdpaa gkitfkvwfk awsgrqvwer gttlaaqqaa dsvtfadvpm rqirpshvqq
      121 wvkvmsqpas srtsglapst irtrynyvhm alraavvdri iksdpsagvp lprarkasaa
      181 mtipaieevg ralsvapvwf rpfiavcafa glrlgetagl rledvdflrr tivvrrqlqg
      241 enrvttevva pkfgservvy vpaelvdlla qhvqragvqq gdwmianarq plnrnsaghq
      301 wrevrkaagl ggytlhdlrh fyasgliasg cdvvtvqral ghssatitlg vyshlwptae
      361 drtraaagdl maaalgasad slrtegl
//
LOCUS       WP_284491339             253 aa            linear   BCT 25-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Blastococcus
            capsensis].
ACCESSION   WP_284491339
VERSION     WP_284491339.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..253
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26508
     Region          12..250
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mtgvvpdplp gwltaatgit altgagistd sgipdyrgpd gvwtkdpdae klvtlsyyvr
       61 dpdirrrawl mrrdlgardl apnaghaalv dldrqgrlrt litqnvdglh qaagstperv
      121 leihgtvhev eclgcrartt mhealdrvaa gepdpaclvc ggilksatis fgqmldpevi
      181 eaavdaaadc dvflavgtsl tvhpaaglvd iavrhgarvv vvnaeptpyd dvadlvvrep
      241 igsalprlva ppa
//
LOCUS       WP_284491356             282 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Blastococcus
            capsensis].
ACCESSION   WP_284491356
VERSION     WP_284491356.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..282
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29225
     Region          9..225
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 meslaahprs sapaddgrtr drvsallleh gpqtatelag rlgvspaavr rhldallasg
       61 rveerqsrda hrgrgrparr fhltdagrsa fphayddlal talryvaasg gpdavravae
      121 qqlagleara ssavaqavda rpgqpvdraq alaaaltaeg yaatasaisg ggqlcqhhcp
      181 vahvaaefpq lceaetavig rlvgthvqrl atiahgdglc tthipgplvp gtgrgrehtr
      241 agnrsaparp vpgergvprp arertapsst ttptndrert pa
//
LOCUS       WP_284491415             222 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Blastococcus capsensis].
ACCESSION   WP_284491415
VERSION     WP_284491415.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..222
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=23840
     Region          <1..198
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mhvvvmgcgr vgsaiarrle eighsvavid qdpaafrrlg pdfsgrqvtg lgfdrqtlld
       61 agidsagafa avssgdnsni isarvaretf gvqhvvariy dskraevyer mgipsvatvp
      121 wtvnrllrel lsvkvselwr eptgkvllmr vtvtegwvgr kltaleaatg araawlvrfg
      181 eaqlptpttv lqdgdqlvva atdelttrvd eviergpqgg eh
//
LOCUS       WP_284491473             302 aa            linear   BCT 25-DEC-2024
DEFINITION  amidohydrolase family protein [Blastococcus capsensis].
ACCESSION   WP_284491473
VERSION     WP_284491473.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..302
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32202
     Region          4..286
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 msgidahchv fvadgvdmsr lvggaaydpp afdvhdhaeh lraagcdrgv lvqpsaygdd
       61 hrcllaalrt rpdalrgvac vapgtspqel aemhavgvrg trvqdgypgg vpveslvevg
      121 etvaplgwhv evwtdvrrhv drlgdavrrc papvvldhlg ylpsdvgldd pavrlvlell
      181 eedriwvtls glerllppgv daeaggaafa eawerheeai aarvralvev rpqnllwgsd
      241 wphvgvqlpv pdaagmrgrl erwvpdpavr havlvdnpar rygfgpagta spepvapgpg
      301 rv
//
LOCUS       WP_284491481             388 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Blastococcus capsensis].
ACCESSION   WP_284491481
VERSION     WP_284491481.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..388
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40973
     Region          12..367
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 msatgngrpa pplagirvld fstllpgpla tlllaeagae vlqverpphg demrsyvprl
       61 gessanyall nrgkrsaavd lkdpavrdrl lalapevdvv veqfrpgvmd rlglgyedfr
      121 avapgtiycs itgygqtgpa agraghdlny laesgllgvv vdergdphlp ptviadiagg
      181 typavvnill alfrrqttge gchldigmtp nlstlaygyl athagsgtwp epgrdlltgg
      241 spryhvyrta dgrhvaaapl eerfwrrfce lvdlpaelrs dagredevia avaeriaasp
      301 aaywserfgg edvcccvvat leeaarsqtl rtrsghrvag pgfdvsalpv pvvdqlrsap
      361 galpypplrt gpealtfdra atpsgspa
//
LOCUS       WP_284491510             299 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Blastococcus
            capsensis].
ACCESSION   WP_284491510
VERSION     WP_284491510.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..299
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=31177
     Region          12..265
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 msipegtrrp ltalvtgass gigratavql gergarvvlv argresleea aeevraagaa
       61 avrvcpadvl deeavagvva atvaefgrld vvvhsaqvma ygriedvpke vyervvatsl
      121 ngtatvarqv lpvfrrqhag hlvivnsllg tvttpllgsy tvakwgqlal arvlqqetrd
      181 epgisvsivq pggvdtpiyv qaatyagvhg sppppvysaq raagiilstl drprrvvqag
      241 llnplitagf rllpgvydll vepllrrlam adepvgpteg nvfrsnpagn avdgrsaar
//
LOCUS       WP_284491616             197 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Blastococcus capsensis].
ACCESSION   WP_284491616
VERSION     WP_284491616.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..197
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20757
     Region          55..194
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 msrpfsrrtl llaasaaagt lagcstggnd taaptgeyqf teptptatvi aedqrapapa
       61 fsgelldgtp fdssslasdv avinfwgswc vpcrvetpef qavhadvadr gvqflgidvk
      121 dqrqlaiafv eqlgvaypsv fdprgevama frgfpanvvp stilldrdgr vaavytgqvr
      181 ghdlrtavel llaedqt
//
LOCUS       WP_284491622             197 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Blastococcus capsensis].
ACCESSION   WP_284491622
VERSION     WP_284491622.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..197
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20677
     Region          56..194
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mparlaggll aaallagcat tteptttelt ttepaaaepa pavpaceqlp enttpagvda
       61 lppltlaclg pgpdvvlerl tgrptvinlw atwcgpcree mpllqeayar hgdqvrflgv
      121 dvqddpdaar wfldelgidy phavdrdgrl lrelgvrglp vtlaldaegr iagrsvgqlt
      181 geelerligt vlssegr
//
LOCUS       WP_284491654             593 aa            linear   BCT 25-DEC-2024
DEFINITION  IucA/IucC family protein [Blastococcus capsensis].
ACCESSION   WP_284491654
VERSION     WP_284491654.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..593
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=64082
     Region          7..580
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mnqspdvtts twqdagrllv akalselsye elfvpvpdgp ggwrlelpda pvyrfrarrg
       61 gfgtwrvdpa gvsrgdepav dpvrlvldar svlgfdgptt aevvreltat qaaearllae
      121 grpageladl pyaeleqhlt ghpvlvlnkg rlgfdaadld ryapeargtv alrwyaahrs
      181 vaayqgvpgl dqqrllaeel dpvtrerfaa tlagqvtdpa ayvwlpvhpy qdetvvrtlf
      241 agyladrrlv plgkgpvdyr pvqsvrtlva pghrdvktpl lmrntlvwrg lgtrataaap
      301 dvsawlatlp agdpelratg lgllgevasv vvahdrydev ddapyryrel lgavwrepva
      361 ahlrpgerar slaallhvdp agravltevv grsglaprew lrrlcdallp glllcltrhg
      421 vafcphgent vvvydtgdvp vrvlvkdfae dvtllpghay pglseradrv lvrwpaqema
      481 hsiisavlag hfrflagvae ehlglpedtf wsvvrdalls wradhpdlad afddlgllap
      541 everialnre hltgggfhdr adrdaapdvv hgcvanplat apvpaalpag vpa
//
LOCUS       WP_284491678             236 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Blastococcus capsensis].
ACCESSION   WP_284491678
VERSION     WP_284491678.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 236)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..236
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25258
     Region          46..217
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 masvwsspdr payphqalav vlqvraarlh vmlwrraaep fagawalpgg sllpeetlga
       61 svgrqlaskv evaqlahleq letrsdphrd prsrtvatay lglipsgldp vlpedtawhl
      121 vdglpetafd hgsivgsale rlraklsytn vafalapptf siaelreiyv aalgyevtat
      181 nlqrvllrrg aleptgemaa sgraggrpat lyrfgttgle vtdpfavlrp pssrgr
//
LOCUS       WP_284491689             217 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Blastococcus capsensis].
ACCESSION   WP_284491689
VERSION     WP_284491689.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..217
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22607
     Region          39..201
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(160..167,177,180..181,184)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mtlslyvprr svvhrlpaga kllalavlav vlfarpslpv vgaalagvla vglllarlpv
       61 atlarqartv lwwlvglfvf halfsdvata avtvlrllal vlaaavvtst trvtemvavi
      121 erlcaplrlv gvrpariglv ismalrfipv laeradrirq aqaarggsar gvrglrttvt
      181 pllvqllqma htvsealdar gaddvppagg rrapaag
//
LOCUS       WP_284491695             694 aa            linear   BCT 25-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Blastococcus
            capsensis].
ACCESSION   WP_284491695
VERSION     WP_284491695.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Shan,L., Mathews,I.I. and Khosla,C.
  TITLE     Structural and mechanistic analysis of two prolyl endopeptidases:
            role of interdomain dynamics in catalysis and specificity
  JOURNAL   Proc Natl Acad Sci U S A 102 (10), 3599-3604 (2005)
   PUBMED   15738423
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Polgar,L.
  TITLE     The prolyl oligopeptidase family
  JOURNAL   Cell Mol Life Sci 59 (2), 349-362 (2002)
   PUBMED   11915948
REFERENCE   3  (residues 1 to 694)
  AUTHORS   Polgar,L.
  TITLE     A potential processing enzyme in prokaryotes: oligopeptidase B, a
            new type of serine peptidase
  JOURNAL   Proteins 28 (3), 375-379 (1997)
   PUBMED   9223183
REFERENCE   4  (residues 1 to 694)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 694)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..694
                     /product="prolyl oligopeptidase family serine peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=74539
     Region          1..691
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mrypeaprld lvddlhghrv adpyrwledp ddprtqewsr vqdelaaqll pslplrerfa
       61 aslgdlvrsg avgvpvwrge rafstrrdpg qehavlrvre adgsvrvlvd pmtldpagtt
      121 tldawspswe gdrlayqvst ggdeesqlfv ldvasgelld gpidrcrysp vgwlpggeql
      181 fyvrrlapgl vpageeqfhr rvwrhrvgap adddvlvhge gsdpasyfgv rtsrdgrwlv
      241 vsrsvgtapr ddvwladlsg stlephpplr elqlgvdaqt aawvardgrl wlmsdrdapr
      301 wrlavadpad patwvperwr dvipqqegav lsdvalvdgp dgglqvlavh avdatdrlsl
      361 wagdgggrva evvapgagsi sgvsappegg psawvgytdy gtppsvlrwd agsstelapw
      421 eqadvagevp altvvethat sedgtpvhlf vlsgagtpdr prptvlygyg gfnvsltpay
      481 saqalawvaa ggiwvvanlr ggsehgeewh ragmrerkqn vfddfaaage hlvaggwtth
      541 qqlavmggsn ggllvgaalt qrpdlaaavv csaplldmvr yerfglgrtw ndeygtaedp
      601 velgwllgys pyhavregta ypavlfttfe sdtrvdplhg rklaaalqha tasdapvvlr
      661 retsvghgar avsrtvglaa dqlaflaaht glar
//
LOCUS       WP_284491714             184 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Blastococcus capsensis].
ACCESSION   WP_284491714
VERSION     WP_284491714.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..184
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18855
     Region          50..181
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 msrdrrapgr licflaalal vsagctpgtg sspaspgggt vadgrqqgaa tvlalsgttv
       61 dggkldaael aatplvlwfw apwctvcrae apevaevaae yagrvevlgv agrgdleamr
      121 afvdetgtgg frhlvdedgs lwqrfgviaq pafvfvagdg ttesflgslg gdqlramvee
      181 ldre
//
LOCUS       WP_284491739             316 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Blastococcus capsensis].
ACCESSION   WP_284491739
VERSION     WP_284491739.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..316
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35123
     Region          2..229
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mtpvvsvvti fldaerflde avesvfaqty phwelllvdd gssdgstaia rkwarrhadr
       61 vrylahpgga nrgmsaarnl gvahargdlv afldaddvwl pgklaaqvql agdhpeagmi
      121 cgptlywhsw raaagradel relgvptdtl idpprllpgl lreevnapat ctallrretv
      181 ervggfeesf rgmfedraff akvyrtvpvy vagachdryr qhadsasara vragtfspve
      241 lspahrvfle wfdgylrrag errpevtaam aaalwpyrhp lrararrwvh rgrsragrwr
      301 rrltagrgra gtgarr
//
LOCUS       WP_284491742             305 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Blastococcus capsensis].
ACCESSION   WP_284491742
VERSION     WP_284491742.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..305
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33814
     Region          2..>122
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mtppvsvvvv fkdeerflpe avdsvfgqrf dgwelllvdd gssdasaeia reqvgrrpga
       61 vrylqhpdga nlgisasrkl gmdaahgsfv afldgddvwl pdklgdqaal mrahpevglv
      121 ygpvqlwhsw saasavhdhf vdlgvppetl vpaprllpql ienryqsptt sgsmlrrdvv
      181 drvggvdvrf rgmyedqvlf tkllavsaty vsgrcwtryr qrpdslsarf edavpyhvgr
      241 lvylrwaedh laatgttdpe vwrslrrels aarhprltrl rhgvgarvrh glgarlrarr
      301 gggdr
//
LOCUS       WP_284491769             293 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Blastococcus capsensis].
ACCESSION   WP_284491769
VERSION     WP_284491769.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 293)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..293
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31976
     Region          17..279
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mprqqspnfs svadvskrls tagylpdaqi attvfladrl gkpllvegpa gtgktelaka
       61 latatgseli rlqcyeglde aralyewnyk kqllriqasq adggadwdtv hddifgeefl
      121 lsrplltair raeptvllid etdkadveve glllevlsdf qvtipelgti tatrrptvvl
      181 tsnatrelse alkrrclyla ldypsaerer eivlsrvpdl apgladqlvr tvralrglel
      241 kkspsisetl dwaqtllelg ldtldepama stlgvvlkha sdqtraaael rln
//
LOCUS       WP_284491839             205 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase [Blastococcus capsensis].
ACCESSION   WP_284491839
VERSION     WP_284491839.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..205
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=22020
     Region          2..201
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mvvradaahl lpglpdgcvd avvtdppwnl graygrhgdr ladeeyerwl railcecari
       61 srgpvvacig thnaarvprl ldgtglhaaa wlswhrepgs petvvvaaqa swevpgrrld
      121 tarrvlartp etrrrwghpv pkplavmaal vhlacppggv vldpfagvga tllaarrtgr
      181 rsigveleer fcrtaaarlt agprv
//
LOCUS       WP_284491804             104 aa            linear   BCT 25-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Blastococcus
            capsensis].
ACCESSION   WP_284491804
VERSION     WP_284491804.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 104)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 104)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 104)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..104
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11019
     Region          8..100
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 msastdamta aspdrfrtll qtqradcvqq reealaecat svpdpvaqrr sadlqrqiee
       61 idaaltrldg gtygrctgcg avipeerlel rpfastcvsc taaa
//
LOCUS       WP_284491866             492 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Blastococcus capsensis].
ACCESSION   WP_284491866
VERSION     WP_284491866.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..492
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52538
     Region          5..492
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 msvappptls lsdrffrelg elavpwraee apeprllaln eplatelgld paalrtpagl
       61 rllvgtevpd gatpvaqaya ghqfggfvpr lgdgralllg elvdaegrlr dlhlkgsgrt
      121 pfarggdgla avgpmlreyv iseamhalgi pttrslavva tgrqvrretl lpgavlarva
      181 sshlrvgsfq yaratddldv lrrladhaia rhevgtgggg aaraenpyla lfeavvsvqa
      241 slvaswmlvg fvhgvmntdn mtvsgetidy gpcafldafd patvyssidt ggryaygnqp
      301 lvaewnlarl aeallpllhd deaqavpvav ealrgfrpry eaawtagmrt klglagnsdd
      361 dtvaslavdl lellhrdhvd lttffrglaa aargdveptr llfldlagid gwlarwralq
      421 pdpdgmdrvn pvyiprnhlv eealdaatgg dlgpldrlle avtapydqrp gldryaapap
      481 qdfgvyrtfc gt
//
LOCUS       WP_284491867             304 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Blastococcus capsensis].
ACCESSION   WP_284491867
VERSION     WP_284491867.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..304
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32614
     Region          19..302
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mdphrgdypp avvrrpgatp aglaglldlt pveegvftaa prstvaghaf ggavaaqall
       61 aagrtvpaer avhsihghfl rpgdvtaptd frvapvrdgg sytlrsvvae qhgaavfvlt
      121 asfqapeegw rhqlpqldap apdelpplee aaattdgpvr qwldwlaerh afdfrfvgel
      181 praaaarget adprqrfwlr sreplpdkpl ahscgvayas dmlllgaala phattirapg
      241 vaaasldhav wfhqparvdq wlfydqessw agggrtlcrg rifdrsgrlv atvaqegmvr
      301 rrpr
//
LOCUS       WP_284491883             989 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Blastococcus capsensis].
ACCESSION   WP_284491883
VERSION     WP_284491883.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..989
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..989
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=106084
     Region          <2..960
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mrgspedaap rhraagttsp acpdgdattl vgpriaelpp vgrdgtlgtl melterlatg
       61 wsgicvltge pgvgktrvlr ellgrvraqg hhvlhgraqe ydssiayavl kdalastpra
      121 digarvrael dglvdamdrs vtgpegdevs rrqspyvmtt rllrsltder pcviavddah
      181 ladeeslaal claarhlrnr plllvfvlrs grpvpgtafa atvgrlveeg sgpvvhlapl
      241 seedtrtlic taldaspdpr lvqhvfaqsr gnplfawetl laltaqrair sahgrlylsg
      301 epgrglvsrr gallhrifqq dedarrlarv msafgrvhld qlslvaeltg ldeprvqraf
      361 daltesavla rvgsggfefa hplmaevlyd dlgpverrrv haaisaytda hpdpriglle
      421 raahaveaas pgdpvaieaa lqaaratrdt aplsaarwln ralelappgs gqageilaqq
      481 tqaywkgsrp dlaidagira sellpagrrr tstaltvina ayatgrlsea lelserlmpg
      541 ddapaamvaq rsllltyvgr aeeaaelaal awtrlrcgdp earavtyssl afvenmvgsr
      601 vraeqaldgl whlatdgada lpvgarlsal eswtyisrlt drtdetpvsr elieslsgrt
      661 gwldlggqav safarvqwlr gewdaaldti hsgvialefa glstnlawlr mlearillaq
      721 gapapaqevv dgvrlpeqsa ywcaqrdvlq arldvardpa gdgaerlaec lrsgvrtgwh
      781 dvvaeslgal vdramdrddp galessavlv rrlaeradsl plrlvravda aeallhrdpa
      841 savdvlrreq aagiplatar ahfllalldh daashlgaaa cgfealgara wsqrtqalaq
      901 argiplvrsr pvpedsaprl adidlqllql vrdglnnrei aeamhysrkt veaylsrlyr
      961 ktgstsrisl vltaeregwl sataagsrs
//
LOCUS       WP_284491911             274 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfite exporter TauE/SafE family protein [Blastococcus capsensis].
ACCESSION   WP_284491911
VERSION     WP_284491911.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..274
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27885
     Region          52..265
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mvdafpsdll padlsggvll llllaalaag widavvgggg llqlpalllv pgigpvqala
       61 tnklasifgt atsattfyrr vhpdlrtalp magialvgsf agasvaaalp asvfkpvivv
      121 alvgiaaftv lrpslgevta lrhsgrrhhg iaaavgaaig fydgilgpgt gsflvfamvs
      181 llgydflnas akakivnvat nvgallffvp hgavfwglgi lmglanmlgg ylgaraatar
      241 gtrfirvvfl vvvtalicrl gwdvwtenlr plla
//
LOCUS       WP_284491917             248 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Blastococcus capsensis].
ACCESSION   WP_284491917
VERSION     WP_284491917.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..248
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25144
     Region          5..226
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 maisemdlrr rwsegqpchg lwsmlpgavt geilartgad fvvvdlqhga rseaelpgva
       61 aaitaagsvp lvrtrsalfp dvgrpldlga rgvivpnvrd aeharevvac cryapgggrs
      121 igrlvggteg pltivmveta taledldavl avdgvdgvfv gpgdlglalg ltgadrrael
      181 rgvlssiivr agaagvpvgv yarsgeeaag yaaegativt agadaatlge amarhlgvar
      241 drpepers
//
LOCUS       WP_284492030             406 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Blastococcus capsensis].
ACCESSION   WP_284492030
VERSION     WP_284492030.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..406
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43335
     Region          146..394
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mpafrpevat rlaelaprll dqldamtdrm vdvlartepv yrelieqseq dlrlstrsnl
       61 englrslmaa asgggaphla saravgrrra aqgmpleavl rayrlggqvt wetlvavsrd
      121 gsghhdtlll evagpvwrtn daecgavaeg yrqeqrrldg vdeqerqqvl dglldgrgsd
      181 pafvrsatel lamplegrlm avvafpgpdg eaglqtpaet llkrglrsvw garseaqvgv
      241 vvlgasrpad llvllrtaar gpvgvsgvvd gaaaagaayr laetavrtlp agasrvvsid
      301 drlpeallsn speissrlvg qslggllelp ederevlldt laaflasdgs ptraadalyc
      361 hrntvmhrlr riesvtgrkl tdarsrllwq lallgtergq parrsa
//
LOCUS       WP_284492049             334 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Blastococcus capsensis].
ACCESSION   WP_284492049
VERSION     WP_284492049.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..334
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34528
     Region          1..334
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mrrfratapa llaasvlvlt acgddaaepe tdaggggdaa aadyptesit livpyaaggp
       61 tdlagrtigs cieeelgqtv vvenregasg svgmqamlag gndgytlsli avpasatnpl
      121 qddvgytned yvpiavvtei psalivgads qfstaeeffq yaeenpgeln vgvpgtttsq
      181 amelrrlaee ygvevtavpf tgnaemttai lggnvdavfi nssqdvleni eagsflplav
      241 spaepvdyid aptlaesgfp eltnsvsvfg laapagvpdn vvstleetvd tclqkddvre
      301 qlgeqyvpde fidsdafssr idsiieaygp ilqe
//
LOCUS       WP_284492072             290 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfotransferase family protein [Blastococcus capsensis].
ACCESSION   WP_284492072
VERSION     WP_284492072.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..290
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=32629
     Region          9..184
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mtprdlptfi vigamkagtt slyhylrnhe qifmpkikel dffaeggnws rgmdwyrqqf
       61 hgagdavarg eastlytkyp qydgvperia aalpdvrlvy lvrdpivrmr shyehrvalg
      121 aetappeial lenpiylays qyamqlerya ahfpreqllv vtseglrhdr avtvrevyef
      181 lgvdpslspp aletefykts qrrsyppivw sarrflkrhv pqakrakevv dsmlerraas
      241 sgagsaasgt asadtvitpe lrarlaellr ddvarlrpym spgfdgwgig
//
LOCUS       WP_284492074             421 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Blastococcus capsensis].
ACCESSION   WP_284492074
VERSION     WP_284492074.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..421
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=43479
     Region          143..376
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mavavaltpl vapkgpghga pidalmafgi favvlwalrs katlripyvi pmtalivvgl
       61 asamvssgpg sgvvagiqev fllvwaaala tmcrtpralg vvlrtwalsa tawavlliaa
      121 vvtgttavsg atgdggtrar llfdhpnmag nyfmisvfvv vasgvprrww lrvgaclllv
      181 lamlssgsna allsliggsv valflhlrar rgivtatavv amviavlgig wvevaqplit
      241 aaqqsdnpll rysvgrgars aeartnlfqs qfelfqqghl lgigpantra algdaaattv
      301 keahndylat lvergplgvl almgligavg aravritrrp lpravaaavp vpaalvgaca
      361 afaltavthe vlhyrwlwtl fallaavhll arsrsdpgpa gdaatttpag aelvrvqrrv
      421 r
//
LOCUS       WP_284492088             439 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Blastococcus capsensis].
ACCESSION   WP_284492088
VERSION     WP_284492088.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..439
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=47017
     Region          1..437
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mkisvigcgy lgavhaasma elghdvvgid vdeakiesls qakapfyepg feellartle
       61 tgrlrfstdf adaagsavhf vcvgtpqkrg eyaadmryvq gavesllgvl eagelvvgks
      121 tvpvgtaaal aelveakvpg allawnpefl regfavedtl hpdrlvyglp agadgdtara
      181 lldevyativ ergtpkvesd yataemvkta ansflatkis finamaelce atgadvklla
      241 daigyddrig rkflnaglgf gggclpkdir afmaragelg adqaltflre vdninmrrrl
      301 rmvelarevc dgsllgkrva vlgaafkpds ddirdspaln vaaqlqlqga vvrvtdpaav
      361 ensrrlwpql dyadtaeeaa eradavlvlt ewkqyrqldp vafgrivkqk rvldgrnald
      421 reawtaagws yralgrrag
//
LOCUS       WP_284492114             385 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Blastococcus
            capsensis].
ACCESSION   WP_284492114
VERSION     WP_284492114.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..385
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40811
     Region          11..381
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mtatssgtle rillsppdvg dreeqlvvea lrsgwiaplg pmvdafeegv aarcgrthav
       61 alssgtaalh lgllelgagp gtvvivptmt faatanavvy tgaepvfvdc egttgnldpg
      121 llerclgrlr aegvtvaavv pvdllgrcad ytsllaicer fevpvladaa esvgswhaer
      181 pagsfgrmaa lsfngnkimt tsgggmlltd savqadriry lssqarqpae hyehtevgyn
      241 yrlsnllaav glgqlerlds migrrravre ryvecfaglp gvrvfqrdgd eadncwltsv
      301 lvdearagws agelrralae adiesrplwk pmhlqplhag artwlsgase glfatgvtlp
      361 sgsalrpeev drvigtvtdf vrggr
//
LOCUS       WP_284492320             253 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Blastococcus capsensis].
ACCESSION   WP_284492320
VERSION     WP_284492320.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..253
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26672
     Region          38..190
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 msaqpvadgv pdylrrlver addlplrhrm pqatrtarrs avlilfgegp rgpdvliiek
       61 slhlrshagq pafpgggadp gedypvetal reaeeeagid pggvrvlatl pelflgpsdn
      121 lvvpvvawwd dprdvtvgdp revarvarvp ladladpanr frvrhpagfi gpafgvadmv
      181 vwgftaalld aileaaglar pwdasdvrpl retgvrpphl pgslgaggae daaaptvadp
      241 apdgaptrtv rpr
//
LOCUS       WP_284492408             471 aa            linear   BCT 25-DEC-2024
DEFINITION  class II fumarate hydratase [Blastococcus capsensis].
ACCESSION   WP_284492408
VERSION     WP_284492408.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Woods,S.A., Schwartzbach,S.D. and Guest,J.R.
  TITLE     Two biochemically distinct classes of fumarase in Escherichia coli
  JOURNAL   Biochim Biophys Acta 954 (1), 14-26 (1988)
   PUBMED   3282546
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..471
                     /product="class II fumarate hydratase"
                     /EC_number="4.2.1.2"
                     /GO_component="GO:0045239 - tricarboxylic acid cycle
                     heteromeric enzyme complex [Evidence IEA]"
                     /GO_function="GO:0004333 - fumarate hydratase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006099 - tricarboxylic acid cycle
                     [Evidence IEA]"
                     /GO_process="GO:0006106 - fumarate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49779
     Region          13..470
                     /region_name="FumC"
                     /note="Fumarate hydratase class II [Energy production and
                     conversion]; COG0114"
                     /db_xref="CDD:439884"
ORIGIN      
        1 maqqngapqd ggdfriehds mgevrvpswa kwraqtqrav enfpisgtpi ereligalaa
       61 ikgaaaavna dlgvldreia davteaagsv argdwddhfp idvfqtgsgt ssnmntnevi
      121 atlatealgk pvhpndhvna sqssndvfps aihiaatrav vatlvpalqh leaslerkae
      181 efaevvksgr thlmdatpvt lgqefggyaa avrygverlq aslprigelp lggtavgtgi
      241 ntppgfaaai ieklatqmal plseardhfe aqssrdslve asgqlktiav glikiandlr
      301 wmgsgprtgl geiqlpdlqp gssimpgkvn pvipeaviqv gaqvigndaa vtyagttgvf
      361 elnvtlplma rnvlesirll anvsrlladr cvdgivadve qcrtyaessp sivtplnkyi
      421 gyeeaakvak qslaeqktir qvvvergyve qgklteqqld ealdvlsmth p
//
LOCUS       WP_284492476             226 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Blastococcus capsensis].
ACCESSION   WP_284492476
VERSION     WP_284492476.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..226
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23692
     Region          38..158
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mppaatdfya aalkstgtgd apapepwsvr daagrtysla daldrwtgea ddvdrgfltr
       61 srgtvldvgc gpgrltaela rrgvhalgld isptalrlar rsgatvirrs vfepvvaegl
      121 wgttlladgn igiggdpaal lrrcralvap gglvlveter pgvgqrttrl rleragavsa
      181 wfdwahvgcd aiqqlaggag lrlteswedg grwfaalrrd ptpgis
//
LOCUS       WP_284492484             209 aa            linear   BCT 25-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Blastococcus capsensis].
ACCESSION   WP_284492484
VERSION     WP_284492484.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Niehaus,T.D., Elbadawi-Sidhu,M., de Crecy-Lagard,V., Fiehn,O. and
            Hanson,A.D.
  TITLE     Discovery of a widespread prokaryotic 5-oxoprolinase that was
            hiding in plain sight
  JOURNAL   J Biol Chem 292 (39), 16360-16367 (2017)
   PUBMED   28830929
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Fan,C., Li,Z., Yin,H. and Xiang,S.
  TITLE     Structure and function of allophanate hydrolase
  JOURNAL   J Biol Chem 288 (29), 21422-21432 (2013)
   PUBMED   23754281
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Wang,L., Grau,R., Perego,M. and Hoch,J.A.
  TITLE     A novel histidine kinase inhibitor regulating development in
            Bacillus subtilis
  JOURNAL   Genes Dev 11 (19), 2569-2579 (1997)
   PUBMED   9334321
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005226
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..209
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=21279
     Region          10..208
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 madlgdvvdv vrygdrallv eaagaatvpg lraalaatpl agqvdlvpaa rtllvvldrp
       61 ptdqdvaglr rlvpaapdag qtpapldlpv vfdgpdladv arltgrspaa vvaaltgtrf
      121 tvafggfapg fgyltglpsd lhvprratpr trvpagavgl agpyagvypr pspggwqlvg
      181 rtdavlfdvd rdqpallapg tdvrfrevg
//
LOCUS       WP_284492496             428 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Blastococcus capsensis].
ACCESSION   WP_284492496
VERSION     WP_284492496.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 428)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..428
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45244
     Region          30..326
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mssaastpte svpapsqapv ppsvdaarle rvlfeikrvi vgqdrlverm lvallarghv
       61 llegvpgvak tlavetlatv vggsfsrlqf tpdlvpadii gtriykagqd afdtelgpvf
      121 anfvltdein rapakvqsal levmaerqvs iggvthplpd pflvlatqnp iesegvyplp
      181 eaqrdrflmk vlvdyptaee ereiiyrmgs erpvaetvlg pdelrrlqrt asrvfvhhal
      241 vdyvvrlvva trsprehgme dvanwvsyga spraslglia asralalvrg rdyvlpqdvl
      301 dvtadvlrhr lvlsydalad gvpadhivkr ivqtvplpqv aprqgasggp gqpggpsvpt
      361 gpfygppqgm phgapwgqgg pqgpggpqyg pgpqghapha naphanggah madgegrhng
      421 tasgpqqa
//
LOCUS       WP_284492517             304 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Blastococcus
            capsensis].
ACCESSION   WP_284492517
VERSION     WP_284492517.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..304
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=30269
     Region          3..303
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mrdtprlllv vnraagtaqd daveaalael rtgadvavaa tgdaaeldev lerndgrrvv
       61 vlggdgsvha vvaaldrvgl ltpeepigiv argtgndlar slglpldpvd gaaavlagta
      121 rsvdllrddt ggvvvnavhv gvgaeaaaea vrlkgrlgaa ayplgaaiag lsgagwnlrv
      181 eidgriatsa ewaadgscav lmlgvcngat igggtplapd aepddglldv vistaigpva
      241 rvaygaalaa grhgdrpdvl vvrgrevrvs gaavavdadg eldeievart wrvdpaawsv
      301 lvpg
//
LOCUS       WP_284492588             217 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Blastococcus capsensis].
ACCESSION   WP_284492588
VERSION     WP_284492588.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..217
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22566
     Region          5..216
                     /region_name="Nnt1"
                     /note="Protein N-terminal and lysine N-methylase,
                     NNT1/EFM7 family [Posttranslational modification, protein
                     turnover, chaperones]; COG3897"
                     /db_xref="CDD:443104"
ORIGIN      
        1 mltvppefvr ahtrpvrpal vpevellvaa dvvalweame telgrtstdp pfwaaawpgg
       61 qalaryvldh pelvagrrvl dlgagsglvs vaairagaaa vlasdvdpfa ltavavnael
      121 ngtagitpvg dvlgdgppdv glvlagdvcy dremtdrvlp flaaaragga vvligdpgri
      181 ylpedrlial avydvpdtep sptqptsvrr ttvwrlp
//
LOCUS       WP_284492624             417 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Blastococcus capsensis].
ACCESSION   WP_284492624
VERSION     WP_284492624.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..417
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43246
     Region          20..>386
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mllaaagala llaaawsdwf rrlpvsepll alaigvllgp avlgvlplpa lledhawlht
       61 aarlllaisv msvalrypfh avrarrrpvl lllavvmpvm avvtaglaaw tlgvglgvaa
      121 ligaaltptd pvlastvttg epaeqdlpgr drqvlslesg andglalalv lialalagpl
      181 pmgdalletv wdvigalllg aflgwlggqa lkagadhgat dpgpelvfti vlafavlgvg
      241 glihvdgifa vfvcglvfna vstgreread vrideavnrf vvlplflafg ailpwaewrs
      301 lgwagllfav avlllrrppv vyllrrplgl prpdavhlgw fgpigisalf yltleserls
      361 idpvvlvags lvvavstlvh gltatpgrvl yrkvagpkgg dedahpdrpv ssssgdg
//
LOCUS       WP_284492663             961 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Blastococcus capsensis].
ACCESSION   WP_284492663
VERSION     WP_284492663.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 961)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 961)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 961)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 961)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..961
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..961
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=100851
     Region          280..935
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mtprgdagra qlrrtrpaad qtdvdlggrr wdagaplrfl dlpfappprs vvpaapvsaa
       61 pasalresrl flvllaalsl cggsvrvvlg trvelvlpll lgfaaaatav vvhrhsawld
      121 rrsrrpwrll avacgllatg qlvsvldpai gqaqsvaahv pqvlavplal aaclllsshd
      181 grragprell dgaivvvala llaglvlcqv vvgsrgaagf lltmgyplag alscgvalvv
      241 vsrtagsrrr pavwvlvamv gasvaavaga lapalgntss dlligvawag mlaaavravd
      301 tdpghlppqp eadtglplfg lvvshatayg vagivvavlg aghtfctfer iaigllvlct
      361 slrsllwvld ggrltrrlle teayfralaa saedvtvvld rdgtvrwvsg atlsqlgwtg
      421 qeltgrrlad lvdpadrpil arvvadvgra aattrpivrl rtseggqrdv klsgaaragv
      481 pgtalrdglv lhlrdvterr taqrelerma ftdyltglpn rarfmaalee araraaaghp
      541 scvllldldg fkavndgagh dagdqllvqv adqlragare qdlvarlggd efallvpggp
      601 deatglaerl vvaldrsfra stpgqdgtgp mfvvsgsigl aeldgsgdvp aivrqadlal
      661 raakaagkrc vrssgeaidd aagrrtrlar dlpaaieegq lrvlyqpvvg vhdrrvlgle
      721 alvrwehpll gtvppdefih laeedglivp lqrwvlevat rqaavlmadg wdvqmgvnvs
      781 vrhllagclv pdvaaalaaa qlpsgklile ltesvlldaa qdrlvadlet lrgmgvvlsl
      841 ddfgrgwssl aylarlpvqi lkmdrefvag ietdprgral vagvvelgrt lgmdvvaegv
      901 eneeqvaelr gmncrylqgy lfgrpmpfad lralldtfda avldvevsem dagvhlvgrd
      961 g
//
LOCUS       WP_284492685             267 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Blastococcus
            capsensis].
ACCESSION   WP_284492685
VERSION     WP_284492685.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..267
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28912
     Region          9..246
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mteqsaggra aarrpgrwat rgpissalwl cilviypvsa llfrlryrhg gripvrgpvl
       61 lvvnhlsvld placarlvfd hgriphflak eavfqglagt ilraagqipv aryssaargs
      121 ldaakedlra gglvviypeg svtrdsdwwp mrartgaahl alttdavvlp vaqwgpqrvh
      181 dyhakklhlr vrtptdylvg kpidlsarra evrggrpldg kllrevtdlm msrvrdqlae
      241 lreepapatf hpgpgrdrpg gvpgsaa
//
LOCUS       WP_284492688             262 aa            linear   BCT 25-DEC-2024
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Blastococcus
            capsensis].
ACCESSION   WP_284492688
VERSION     WP_284492688.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439579
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..262
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28269
     Region          20..235
                     /region_name="PssA"
                     /note="Phosphatidylserine synthase [Lipid transport and
                     metabolism]; COG1183"
                     /db_xref="CDD:440796"
ORIGIN      
        1 mhenaagtta tttaapgfsr rlrlagaavh lytasgsvlg llmvlaaveg dvvtalwlvl
       61 atlvidgtdg mlarwarvke tipwfdgarm ddivdyltyt fapvvllwat drlpggpvgw
      121 llaalpllas cyqfcrtdak tedhyflgfp sywnvaafyl ivldvgttgv avtlavltvl
      181 vfvpvkyvyp srtrtlrsln lalatlwlvs yavllvqypd phpvvvvlsl aylvyyagvs
      241 vwltvtgarr rpgsaesver ag
//
LOCUS       WP_284492746             452 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Blastococcus capsensis].
ACCESSION   WP_284492746
VERSION     WP_284492746.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..452
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48883
     Region          21..434
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mrdpsgvgqs aggtagalag vrvldftwsv lgptvtrtlt sfgaevikve wpkradpmrt
       61 tmysageerk gldngpffhn lntgkrsltl dvrspcgmei irrlvgvsdv viesfssqvf
      121 rrwgldypql reinprivyv sasgfghsgp yegydtwgpt aqafngltsi sglpghapag
      181 wgwsymdvag gamatvatla aihhqvatge gqyvdvsqve sglsltgpsv ldqnatrerr
      241 ggdtsppgnr aatggaspay gyrgewgapy gayptrgggh ndycvisvla deewvalreq
      301 mgrptwaldp sldtadgrva qqdgmdgria awtetydkqe lmrklqaagv rcgavqsaqd
      361 rtendaqlvh rgmfptlehp vlgehrfeat pirmsetdrv tppswpllgq dnqyvlgdll
      421 gmseeeirql drdgltwpad lprdvtvsrs lw
//
LOCUS       WP_284492788             446 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Blastococcus capsensis].
ACCESSION   WP_284492788
VERSION     WP_284492788.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..446
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=48427
     Region          2..423
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 mvlfalglmf siafheaghf wwarkfgmrv pqfmvgfgpt vfsrrrgete ygvkaiplgg
       61 yirivgmipp aeegeskrat rmrsfiaevr gqalndvrpt dgdrvfykkp wwqrvivmfa
      121 gpfhnlvlav vfftvvlvgf gipeistria qvpdcvlpag aetaraespc sipitpeger
      181 ceagapgcal psrspateag lrpgdtilal ngepvsqetd vgwtevqeai rvsagepvvf
      241 tvdrdgerld ltvtptenqv yaddegerte tvgfvgiqpa lpdvrqspae vpghlgtivv
      301 rsvdrlieip ervpqlfraa flgeerdplg pigvvgvsri sgevfafeef sagkkisyfi
      361 qllagmnmvl flfnllpiyp ldgghiagal yekvrsvfar lrgrpdpgpf diarlmpvay
      421 avaglfltls llllvadvvn pvrlgg
//
LOCUS       WP_284492833             426 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Blastococcus capsensis].
ACCESSION   WP_284492833
VERSION     WP_284492833.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..426
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45248
     Region          8..403
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 myvsdqvpqg altgvrvldl tqvmagaycs mlladmgadv ikierpeggd dtrrmsrgpd
       61 vehspafnam nrnkrgiavd lkdprgadvv rrlaedadvl venfrpglld rfglgqealr
      121 aanpalvycs isgfgatgpy agrggydlia qamsglmsmt gepgrppakv gvpicdlnag
      181 vfgaygvlsa yihrlktgeg qfvdtsllea giaytvweta mffslgdvas pmgsahrlsa
      241 pyealptadg wiaigaandr nwarlcaglg merllqdprf ennparmtyr felagelaat
      301 lrqrttaewl ealhaagvps gplydieqvy adphvqarem lvetqhprmg tvrhigapvk
      361 lsgtpsairr papllgehsr evlaeagmsa aeieelvsag vlvtpddhar ttgaaaspld
      421 stevpa
//
LOCUS       WP_284492859             138 aa            linear   BCT 25-DEC-2024
DEFINITION  Rieske (2Fe-2S) protein [Blastococcus capsensis].
ACCESSION   WP_284492859
VERSION     WP_284492859.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..138
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=14750
     Region          20..120
                     /region_name="NirD"
                     /note="Ferredoxin subunit of nitrite reductase or a
                     ring-hydroxylating dioxygenase [Inorganic ion transport
                     and metabolism, Secondary metabolites biosynthesis,
                     transport and catabolism]; COG2146"
                     /db_xref="CDD:441749"
ORIGIN      
        1 mseptaispa pvvdqpdtds wvhvaelkdl arrkrkqvtv gscpvalflv ddevlavddt
       61 cihqerslak gtllngqvic pghqwkfdpr tgeaedqdgr latyavqvte egavlvapqp
      121 vtpreattsd sathpagr
//
LOCUS       WP_284492899             335 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Blastococcus
            capsensis].
ACCESSION   WP_284492899
VERSION     WP_284492899.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..335
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37762
     Region          4..318
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mprpvtlftg qwadlpfeem crlasgwgyd gleiacwgdh ldveraandd syvqerlall
       61 ekhglqvfai snhlngqavc ddpiderhrg mvhprvwgdg dpegvrqraa eemkltaraa
      121 rnlgvdvvvg ftgskiwktv amfppvpesm iedgyrdfad rwnpildvfd evgvrfahev
      181 hpseiaydyw ttvrtmeaig hreafglnwd pshfvwqdld pvsfiwdfkd riyhvdckda
      241 kkqvgngrng rmgshlpwad prrgwdfvst ghgdvpweac frmlntigyd gpisveweda
      301 gmdrlvgape alefvrrlaf dppsaafdaa fasgn
//
LOCUS       WP_284492914             535 aa            linear   BCT 25-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Blastococcus
            capsensis].
ACCESSION   WP_284492914
VERSION     WP_284492914.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10594375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..535
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=57077
     Region          288..418
                     /region_name="SIR2_2"
                     /note="SIR2-like domain; pfam13289"
                     /db_xref="CDD:433090"
ORIGIN      
        1 msghvfvvga dltrlscddv lvptdrslrv argwrpllpd elitdhqddg dcvglswsgr
       61 ervlevpgdg prrtwlvdtv ddgghglswl ldgarealaa varreapepv hgrarrlvgl
      121 palgtgwgga agergallqe llpvlreaav qhgfdvalvl rgpsdlaaaq rvrrgqdgaw
      181 dlpehlcela eqlgerarrg qlalfvgagv saaaglptwe qlvhelatrs glddalregl
      241 sglppqdsaa llarelgseq leafvaerfg pgsyalahal ladlpvqefv ttnydplvel
      301 aaddigrqvr vlpyeeaepg rpwllklhgd aahpgsvvlt reeylqfgnt gaalagvlhs
      361 llltrhvlfv gtsmldddli riahqvrmaw qtqgsgtarr agtvlalred pararlwerd
      421 vetvamspad gspaeaarrl evvldligcl stpptgylld payrgmlnde eralagalrt
      481 vaetlppdas staalevagl lrrlghgsca adgdepppel asgprndraq eqrpg
//
LOCUS       WP_284492922             367 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Blastococcus capsensis].
ACCESSION   WP_284492922
VERSION     WP_284492922.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..367
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=38247
     Region          17..367
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 masraarrda lrataaergf davlvtnlln vryltgftgs ngallvrvdr adlfgtdgry
       61 ttqaatqvpd vevvvdratv aalareavrr gagrlayesh dltvdglhgl qrvltdaaag
      121 gtvpelasvr raveaqraik ddgeiealrr acavadqala elaaegalrp grtelqvgre
      181 ldarmlalga eapsfetiva tgvnsaiphh rpdatvlreg dflkidfgat vdgyhsdmtr
      241 tlvlghaadw qreiyelvaa aqaagraala vgadvvavds aardaiieag hgdhfphglg
      301 hgvgleihea pgigqlgagt laagmavtve pgvylpdhgg vriedtlivt ddapelltlt
      361 skellvl
//
LOCUS       WP_284492993             228 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Blastococcus capsensis].
ACCESSION   WP_284492993
VERSION     WP_284492993.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..228
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24112
     Region          53..156
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 msgvasepgt qppartgpts avdresydel yrsapavwsg rpnrqlvaea gdltpgrald
       61 agsgeggdal wlaergwrvt avdfspvalq raaarsrera vddrvewvha dldvwpppeg
      121 rfdlvtahyl haswsdragm frrlaaavap ggtllvvghl hgeerghghs hahgadamyt
      181 aedvaavldp gewpdvvtgt rdrdpgaaar tgnpvpdtvl varrsgar
//
LOCUS       WP_284493221             386 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Blastococcus capsensis].
ACCESSION   WP_284493221
VERSION     WP_284493221.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..386
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39832
     Region          6..380
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mpergtdvvv vgagiigaac alyaaragls vtvldrgsvg agttsrcegn ilvsdkgagp
       61 eldlalasrs lwlelaaeyg adrfeleekg glvvatgeag maslrrfavg qgaagvtaep
      121 vtpdglrahe pnlasglpgg vyypqdlqvq pvlaaaslla aardlgarvv tgtevtgaar
      181 gadgrltavh trdatypaga vvnaagtwgg dvgerlggsv pvlprrgfil vteplprvir
      241 hkvysadyve nvasddagle tsaviegtrg gtvligasre rvgfdetlsv evlrrlaaqa
      301 irlfpfladv rlmrsyrgfr pycpdhlpvv ghdrrvqgll hacghegagi glapatgrli
      361 adlltgahpl vdpgpfdpmr famedv
//
LOCUS       WP_284493233             377 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Blastococcus capsensis].
ACCESSION   WP_284493233
VERSION     WP_284493233.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..377
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=39167
     Region          91..369
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mrddlqdlvd evsrvlaapa tledadftll afcahddsga dpidavrtrs iltrgsapgt
       61 rrwfedfgia satrplrtpa epaagiltrl vlpvrhdgei rgylwllddg ridpdahgdp
      121 aleraqdlaa dagrmlagrp aadlgdalad vldgrpgarp paerrlaerl tgdgpqvlva
      181 lfpaggaapr gwrlpaagav aavvaggava vlvplpaaad lrpagaltaa slralpagss
      241 agvsavrrga aeladqwqea rtaariaaav erfspvalwe elgawrlaaq lpgpdpalqp
      301 lladpvltat aetfldcags aartaealci hrqtlyyrlg ritaltgldl adgdarllvh
      361 aglraarlrn atrpprs
//
LOCUS       WP_284493260             614 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Blastococcus
            capsensis].
ACCESSION   WP_284493260
VERSION     WP_284493260.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 614)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 614)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..614
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=63874
     Region          37..591
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mrrtrltlta avvaatsaal vagpttaaat hqaepnvpvq liamndfhgr isqttggdal
       61 qvtaagpdga ygtpddvedt vggsahvaat vqrltaefqa ahgaeaasvf vgagdlisas
      121 sfessvfkde ptievlnamg ldvtsvgnhe fdrgteelrr vsaatdgtyt ddvvacpetl
      181 ggeafragvd gcfgadehaf hgadfpflaa nvldretgrp mlppyqivdv gggermalig
      241 vvtestptiv spggvadvef ideadainrv vpellkqgvk aigvlvhegg fqqgpsaanp
      301 ngcddlggpl ldinqrthpq vdlivsahth sayncllpvp dsrdrlvtsa gyygrlvsdi
      361 rvmikpsngd vdrkatyaat nvpvlrtaad arvqsivdyw naraaearnr vvgtagadie
      421 raasrdqess lgnlvaqmql eavdeaqfgt pviafmnpgg lrtdiaagev tygelyavqp
      481 fgntvnvvtl tgadieevle qqfqadqarq stlmlgtseg faysfdpsra fgdrvdacsi
      541 tldgvridpa asyrvaansf ligggdsfta ftkgtspatg pvdvetavey fgqnspvspp
      601 aadhatlstv rgtc
//
LOCUS       WP_284493415             252 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Blastococcus capsensis].
ACCESSION   WP_284493415
VERSION     WP_284493415.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..252
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26781
     Region          1..236
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mslkklftnd gvalgmmlsg vsnpgvvsmi stagldyfil dmehgpfdws dmaamigiar
       61 gagirpivri peirretvlk pldagaagll vpmvdtveqa eeivrhakya pqgqrgtalr
      121 rghsdyakkp aveymarvne ettiaiqies reavknaeal aavpgidalf igpfdlsvdm
      181 gltgqasdpq mrevyrtvla aakasgkvag ihlfdtqlak slieegfqmv svssdidiiv
      241 dqtaanvsal rg
//
LOCUS       WP_284493541             457 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Blastococcus capsensis].
ACCESSION   WP_284493541
VERSION     WP_284493541.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..457
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=47516
     Region          108..457
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 msrtagrrgl rarivlgfaa stllvsavlv tttwllarsy vveqreqalt qqafadadvl
       61 rnrlstagtd vgrvlgelvp fgdaevvvrs gddwysssld vggrdvpral qevvatgaag
      121 alrvetadgp qlvvavpvvs agvefyevap laeletllrt lavvlgagav vatlagagfg
      181 awasrravlp leqvagaatr iaggelstrl patddpdlvg ivaafnsmvd alaarisrda
      241 rfvgdvshel rspltsltts vevlatrrqe lppraqqala lvegevarlr vtlddllela
      301 wfdgaghvpd avpvsmtalv revlegtgrp valldagpep ettvlgdksr leravrnlld
      361 nadrygdgpv rvgvrrcegs vavtvddagp gvapldreri ferfarapgs arrsvpgagl
      421 glaivaetta qhggaawcae spgggarfvl smpaart
//
LOCUS       WP_284493688             247 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Blastococcus capsensis].
ACCESSION   WP_284493688
VERSION     WP_284493688.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..247
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25075
     Region          17..215
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mpvdpvggga aapapelrav lfdmdgtlvq teeywgeamf eladalggrm saearaatvg
       61 tsmrrsmqvl yadlglvrte eqlqadarrv edrtgelmvt agiawrpgar dllagvradg
      121 latalvtttp rrladvvlas itadlgadpf dvtvcgdevp arkpdpapyl qaatalgvdv
      181 ascvvvedsl vgvtsglaag mavlgvpalq pvpaapgltl rgslegfgvp elavvlaags
      241 amaivgr
//
LOCUS       WP_284493711             450 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Blastococcus capsensis].
ACCESSION   WP_284493711
VERSION     WP_284493711.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..450
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48356
     Region          3..436
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtaagteltl rhpierftlg nglrvvlapd rsvpvvavsv yydvgmrnep egrtgfahlf
       61 ehmmfqgsan vakmeharlv qaaggtfngs thqdytnyfe alpaealera lfleadrmaa
      121 paiteenlrn qidvvkeeir vnvlnrpyga fpwlqlpqva fdtfanthdg ygsfvdless
      181 tvddatdffs ryyapgnavl ciggdldvae teklvhrwfg pvpardvppl phtgepspta
      241 vrsavvedal apapalaigw rvpdpvgdfd sylgtvllae llsegdasrl errlihddri
      301 aiaqssyvgl fgdpfdvrda tllttqvhhp aavpadrvma avheevaria qdgvetaelr
      361 rvqarveaql lqqadsvlgr tlafaaaelv hgraelagel aarlaavspe avrtaargld
      421 pgtaavlelr pagrppmsag gagsplevrr
//
LOCUS       WP_284493822             498 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Blastococcus
            capsensis].
ACCESSION   WP_284493822
VERSION     WP_284493822.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..498
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=52688
     Region          34..489
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mqtvlaatfd eqvdswfapi seritsvvfy avpldfvddg vvlplivvwl viagffftiy
       61 lrgfqfrafk haiqltrgdy ndprdagevt hfqalatavs gtvglgniag vavaislggp
      121 gatlwmiiag lvgmctkgve ctlgvkyrnv ypdgrvsggp myyltkgleq khprlgtfgk
      181 vlavlfcift lggavgggnm fqanqafsqa qsvtggedgp lgggaagaif glvmallvga
      241 viiggirsia rvtdklvpfm aifyvlaclt vlfanfteip nalwaivsqa ftpeagfggv
      301 vgvliqgfrr aafsneaglg saaiahsavk tnepateghv avlepfidtv victmtalai
      361 vitgtyades sapgvqttsa afesvvgwfp ivlaiavilf aystmlawsy yglkaatylf
      421 gesmlvdrtw klifclfvii gasstldavi gfsdsmiflm slpniiglyi larvvkreiy
      481 gyrarletge ivpvaert
//
LOCUS       WP_284493852             360 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Blastococcus capsensis].
ACCESSION   WP_284493852
VERSION     WP_284493852.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..360
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=40033
     Region          75..331
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 maeliktrtp gvyklhrgkg tvfvarwrev dpitgkarvr sktlpteaaa rqyrtsvvha
       61 qatgtyvppn vgkatvreia eqwlavaatq vrprtlekye rglrlrvlpt fgarridslt
      121 srdverwiad lgsvmpstvk haifplsatl nyarkhgliq snpcevvdrp krlptgrdkr
      181 agiflsraqv aavsanvaet epvygllvrf aagtglrrse iaglrvrdlr larrethver
      241 maertypggv wviqepksar srrrvpildd ellhdlgvyl aahprrhdfd aplwpakyrs
      301 gplnytgrrt vergqllqar lracggrrwa trrpaqrrpv srsaapaaas gsqmgttcsa
//
LOCUS       WP_284493858             872 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Blastococcus capsensis].
ACCESSION   WP_284493858
VERSION     WP_284493858.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus capsensis
  ORGANISM  Blastococcus capsensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 872)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 872)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 872)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 872)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..872
                     /organism="Blastococcus capsensis"
                     /db_xref="taxon:1564163"
     Protein         1..872
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=93189
     Region          177..849
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mtdtcpaslr rwswlttsrr iallvaamsm aavavfvivv rdlpgldapf glpwwawvaa
       61 faageilvvh vqlkrdshgf sltdlvlvag lylaepavvv ltqllgtgla lvlhqrqsgl
      121 klafnlaqyg ltgsvavvaf tvlagntdwd spwrwtaalv avavttlvad lclfaalsis
      181 egtlhvrelp hmlmlslpfa vgvaaiglla ayialqnptg llllvlpsvl lfsayraytk
      241 areqqnnlrl lhettsllyn sddaslaltn fltsvrgafr agvgelvllg edgvttvsrs
      301 rdgqeptall plphsadveq liesatatgv ltartgqvrg sgldqyagqr gfkdamvsvl
      361 rtenrvhgvl lvadrlgdva tfassdlall epfarhlats lergrlesdl rqvtelkekl
      421 rhqamhdalt glpnrtlfld rtqhavhlaa rnglwpavly idldgfkpvn dtygheagdv
      481 llqafserld gclrsadtaa rlggdefavl lhgpidrsgv ervldrirtq ldrpidlgag
      541 reatigasig vafadagtdv atlighadva mytakrngrh rsvfyeaglg daaperpdpa
      601 aelaaaldrg eltvayqplv dlragraiga ealvrwqhpv dgnrppdtfi plaeetglim
      661 eigefvlrda crqavrwvqs ssdpadllvt vnlsarqvtd artveavqaa ladtglephr
      721 lvleitetvl mqdrdaaatn ldrlkalgvr iaiddfgtgy sslaylcrfp ldmlkvaref
      781 vdglgrdpna dvvtraivel agalglrtva egvetdeqhq qlaelgcdla qgylfsrpvd
      841 aetvlalmag vdaeasttgp aagsstaela ia
//
LOCUS       WP_284493906             126 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Cupriavidus taiwanensis].
ACCESSION   WP_284493906
VERSION     WP_284493906.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 126)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 126)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 126)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..126
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12844
     Region          <49..118
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mdsfplsgaa wrraaagtlv aalvaapaag iaadapapar qaqlahwlrd dcgachgmtl
       61 rgglgppltr aslagkptdg lvatvlygrp gtamppwqpf mtqdearwli drlqagqppa
      121 vtpqgn
//
LOCUS       WP_284493942             308 aa            linear   BCT 25-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Cupriavidus taiwanensis].
ACCESSION   WP_284493942
VERSION     WP_284493942.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..308
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34450
     Region          28..307
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mttatahasv srqqsaplst vsanagnfei rpldaplgae vigldlsqpl sdadlarihr
       61 ahldyhvvvf rdqqitpaqq idfsrrfgpl qihvlhqfql pghpevlvvs nvvengkpig
      121 lgdaghfwhs dlsykekpsl gsllharelp aeggdtlfan mhlawdtlpa alqravdglq
      181 aehtylarya elqqrspwrp nltpeqiaqv rpvlqpvvrt hpetgrkalf vsehfttriv
      241 glpeqesrdl leqlfahsvk pahiyrhqwq phdlvfwdnr sllhlaagcp peqrrvmyrt
      301 tiegdvpr
//
LOCUS       WP_284494008             342 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Cupriavidus taiwanensis].
ACCESSION   WP_284494008
VERSION     WP_284494008.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..342
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=35473
     Region          22..330
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mdaratgptp dsvlqtrlta llgirhpill ggmhhlgtsg vvaavvnaga mgfitarsfe
       61 slddyradlr rcrtltgglp fgvnltmsrr edfnrlvpdw iriafeegvr lfesagsspe
      121 alvgpihegg gilvhkcpsv rhavtaqrlg vdavalvgle egghpganql safvngafal
      181 erldlplvig ggigsgrqia aalalgadgv vmgsrfmvas eiaahdalkh rivasdehcs
      241 ttilgslgdt wrvlandsar avqrleaqga sdhaafgdli lssrtrqrvy qrgeveagiv
      301 slgpaggfad aiepagriva rlvadaraac dalagrrvgl pa
//
LOCUS       WP_284494063             325 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Cupriavidus taiwanensis].
ACCESSION   WP_284494063
VERSION     WP_284494063.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..325
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33970
     Region          1..323
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mksfknafag lvlacgaala atpalaadef pskplrlvvp faagsgtdav arltakylge
       61 slqqpvvvdn kpgangtiaa efvakapadg ytlfmttntt hsanpslmkq lrydpvkdft
      121 pvsrmgnlpf mlvvnpalpv ktlrefvdya kahpgltyas gnstgivsga tlskmaglqm
      181 lhvpykstpp amtdvmggqv qamfvdfaag ianvrsgklr alavttaqrs allpdlppla
      241 svpelkgfdv tswngvfapa gvpapvvarl nrelvaiats kqhaaqfhal gfepfgstpa
      301 elsqfvvael qkwarlvkda giqpe
//
LOCUS       WP_284494163             481 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Cupriavidus taiwanensis].
ACCESSION   WP_284494163
VERSION     WP_284494163.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..481
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=53369
     Region          64..436
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mqavaprssl lageqstapt rpydpaydpl htptpghgre yaptywigta geppaddgpi
       61 thdidvdvai igsgftgltc aiflaqeygi katvleanrv swgcstrngg qaqcasgrlk
      121 rsqwiqrygl dtalrlhrev cdgmetfkgl irnidcdpqp gghlyiahrd kvmpalekea
      181 kllrevfnyd arildaatvr reyvddkeaa gamhepegig ihagklafgy lrrarelgar
      241 vhpsspvtgw etrngvhylr tpggivrara vgvatggyts qslhrelknr lfpilsnsiv
      301 trpltpdela acnfrttqvi tdtrilrhyy rlmpdgrlqi gsrsaitgnd apqdqykqkl
      361 iadmhrkfpa lqgiqvdysw wgwvdvshdm mpritqpdpa qsiyyamgyg gngvmysaqa
      421 gkrlaaliag kssalpelpi fgsplpfpnv remvesqmfa pfrrlgqrvl yhwyhwkddv
      481 f
//
LOCUS       WP_284494248             279 aa            linear   BCT 25-DEC-2024
DEFINITION  OmpW/AlkL family protein [Cupriavidus taiwanensis].
ACCESSION   WP_284494248
VERSION     WP_284494248.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006882
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..279
                     /product="OmpW/AlkL family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29050
     Region          25..279
                     /region_name="OmpW"
                     /note="Outer membrane protein OmpW [Cell
                     wall/membrane/envelope biogenesis]; COG3047"
                     /db_xref="CDD:442281"
ORIGIN      
        1 mktlrltlal glaalaslal pahaqkkgdn vvsagwfhiq thgqsdpltt slldvpinyp
       61 lglpssftap gssisssnad tlgltfshfv tdhiaitavg gippefklyg hgelippgpa
      121 galgrqslgd pslnpivtka rqwspaamvq yhflepgtrf rpflgvgvsy nfftnievnp
      181 afassvnnnl gailaagagi pgptsvsada ssswapvfnv ggtynfdehw gltaavtyip
      241 lkttstmtik aangtvlsts ktklepnplv ffvaasykf
//
LOCUS       WP_284494255             537 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Cupriavidus taiwanensis].
ACCESSION   WP_284494255
VERSION     WP_284494255.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..537
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=59743
     Region          26..469
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mnapaelppq laeqaqpaqp trqpappape htdiaiigsg faglgmairl rqrgehdflv
       61 fekagsvggt wrdnhypgca cdvqshlysf sfapnpdwsr mfstqpeira ylehctdrfg
      121 lrphlrlhhe lrhaawdesa qlwrlrmadg kevrarvlvs gmgglsrpay pdipgldtfe
      181 gecfhsqhwn hayalrgkrv avigtgasai qfvpqiapqv aqldlyqrtp pwimpkpdre
      241 vsaaerwlfr rlpftqtlvr tgiywmlesr vlgfvlhpki mkvvervarr hlarqvrdpa
      301 lraaltpdyt igckrvlisn dyypaltrdn vdvvttgiar verdavvlrd gtrrpadcii
      361 lgtgfhatdp lprgviagig gvdlvdawrd gaqaylgttv sgfpnlffvv gpntglghss
      421 mvfmiesqva yiadalrqmr ragvqavnvr epvqrrfndk lqarlghaiw saggcaswyi
      481 dprsgrnttl wpgftwqfrr atasfrmtdy dlypvrhalp denalqpsad iataaga
//
LOCUS       WP_284494317             329 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Cupriavidus taiwanensis].
ACCESSION   WP_284494317
VERSION     WP_284494317.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..329
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33650
     Region          30..327
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mafpfrsspl aaacvfsaaa lapaaaaaad typsrpirli vayptggisd tvaralgerl
       61 saqmgtsvvv enkagaggsi gidavakaap dgytlgfaat spltlnphvg rvnydpqkdv
      121 apvmsvmysp vlvvatsafs gksfadvvgq asakpgsvrw atsglgtvgh vvleqvkqks
      181 kadivlipyk gagqqmndal ggqfevmstn aspvlsqhmq agrlralavg apkrleslpa
      241 vptlaelgyp kanltstfgi fapgktpaai inrlnaelnk alaepevher llkggevptg
      301 gtpaqfakai reesaenari vreagikae
//
LOCUS       WP_284494381             742 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Cupriavidus taiwanensis].
ACCESSION   WP_284494381
VERSION     WP_284494381.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 742)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 742)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 742)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..742
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=82595
     Region          16..742
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mvtstdlagr vagipdtelv eralayvreh gagvalptge tvpshaegml rildglrvdd
       61 saraaaclfg laafvpetea eieprfgeev arlvngvrql lrigaiagnr peaesaapsk
      121 neaqarheqv ealrkmllaf aqdirvvlvr lasrlqtlrw laetkqaplp gvaretldiy
      181 aplanrlgiw qmkweledla frfeqpdtyk riarlldekr ieregyiaga iarlqselat
      241 agiraevsgr pkhiysiwkk mrgkeldfad lydvrafrvi vddikdcytv lgivhhiwqp
      301 iprefddyis rpkangyksl htvvigddgr afevqirthe mhhfaeygva ahwrykeags
      361 rgyagqfsas erydekiawl rqllawkdda dhsvahdesw eqikhaaidd hiyvltpqar
      421 vvalpqgata vdfayylhsd lghrcrgarv dgtmvplntp lkngqtveii avkqggpsrd
      481 wlnadlgyla ssrarakvra wfnamdsqet iaqgralidk tlqregrtav kledlatrlg
      541 fktpdelfaa vakdefslrh vehalrhpeg evqapvneed avtkksrats vargaksgvl
      601 vvgvdslmtq msrcckpapp ddivgfvtrg rgvsihrrnc htfqqlsara perviqtewg
      661 kkshaavypv dihveaidrq gllrdisevl srekinvtgv ktlsskgvar mqftaevsea
      721 tqlqrallli eevqgvlqak rk
//
LOCUS       WP_284494440             606 aa            linear   BCT 25-DEC-2024
DEFINITION  autotransporter assembly complex protein TamA [Cupriavidus
            taiwanensis].
ACCESSION   WP_284494440
VERSION     WP_284494440.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..606
                     /product="autotransporter assembly complex protein TamA"
                     /GO_component="GO:0097347 - TAM protein secretion complex
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=66820
     Region          46..606
                     /region_name="TamA"
                     /note="Outer membrane translocation and assembly module
                     TamA [Cell wall/membrane/envelope biogenesis]; COG0729"
                     /db_xref="CDD:440493"
ORIGIN      
        1 mpqdtantad sagraawhaa aralaalgvl lgvvlglaaa paqaaykvev eapkpireml
       61 eehldlaryk drtdlsqdqf dymvetvgeq vraftstegy fdpttttrve gegdqrvvhv
      121 vvdpgartli rnvdlqvtgp aatqspeqva emkakwglpa gepfrqddwd kakedalvtl
      181 qshtyygarl aasqarvepd elradlsahy asgpayrlga lkvtgtrryp eqiiynvnpl
      241 negepyrver llelqraiqn qpyfsnvlvd lepppdadqa pdgvvtapvs vrvreypvhr
      301 lnsgvgfttd tgaqvegrys yynlfnrawt fdsqarieqk rsylfaeaam ppsrgayrns
      361 vyssyertid ientdttslr aglkrsrsre kydvtmsldf yydkllpvgq asqiskalvp
      421 afawtrrdvd npvfprrgnv istqigvaaq nllsdatflr lygrirqyvp vgkrdlvvar
      481 lelgadlsgd saskipatlr fraggtdsir gysyqsigtp sgasvlpaky latgsleyqy
      541 wfkpdwgvav fwdagtaadn lrgvtiyngv gvgvrwrtpv gplqldvgyg iqeqqfrphi
      601 slgvaf
//
LOCUS       WP_284494453             335 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Cupriavidus taiwanensis].
ACCESSION   WP_284494453
VERSION     WP_284494453.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..335
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34249
     Region          29..333
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msdfrralai wmvlalaall afglslalgs valdarelwr alsgadtgta gaivhelrlp
       61 raaaafacgg llalsgalmq vllrnplaep yvlgvsggas taallamlal apwwgvqaaa
      121 aigallamvl vaslarrdll hpqvqgghre agarllltgv ilaagwgavi tlilsvapes
      181 rlrgmlfwlt gdlggtasyg galamlvaal llampmaral nvmllgetva qslgvrvgrv
      241 rlatfmlasl ciaaaittag sigfiglvvp hlvrlawgnd qrlllpaatl lggallmaad
      301 liartvvapa qlpvgvitgl lgvptflyll lrrpr
//
LOCUS       WP_284494486             327 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Cupriavidus taiwanensis].
ACCESSION   WP_284494486
VERSION     WP_284494486.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..327
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34042
     Region          5..325
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mryprtllgl lgitatmlaa vpaiagaqey psrpirlvvp fvpggvtdas arlvanklgq
       61 slgqnvvvdn rpgasgniga eivarsgadg ytlllgfdga lvtgthitrp rfdvlkdfap
      121 vtkigdatli fvtnpavpar sfselvaysr askgaglsfg ssgtgttchl agellreqag
      181 iqlqhiaykg gsqaltdvlg gslpvlctav asvsqyvkng qvraiavtgs hrvaslpevp
      241 tlmesgvknf svdswvgila pagtpaavvt rlqqeirkvl dqpeirskml elgitpvgnt
      301 pedfgrqihh dyarygevvk kagitln
//
LOCUS       WP_284494656             388 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Cupriavidus taiwanensis].
ACCESSION   WP_284494656
VERSION     WP_284494656.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..388
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40799
     Region          11..373
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 madassnesv rgalsglrvv dasrvlagpf cgqilgdhga dvikieapeg decrgfgppf
       61 vegasayfra vnrnkrslvi dmnlaadrev fwqlletadv lienfkpstl etwgidrpss
      121 iterfprlih critgfgddg plgrlpgyda avqamaglis ingepggnpv rlgvpvvdlt
      181 tgmnaamavl lalnarhrtg rgqladvsly dsavsvahpf mtnflasget prptgnshpn
      241 ivpydvfqta tcplfvavan drlfgklcqa lgaghlpdde rfatnrqrva hrealtaels
      301 rafatvdges fgkallarnv paapilsiad vaaaphtlhr qmvvrqgdyi gpgvpiklsg
      361 tpasirsgpp algglsgaag eaaslwkq
//
LOCUS       WP_284494660             410 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Cupriavidus taiwanensis].
ACCESSION   WP_284494660
VERSION     WP_284494660.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..410
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43537
     Region          17..408
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mtsfpsgtdg gsgaacadlp lsgltvldls iaragpaavr llsdwgadvi rveppppqdr
       61 gsvtgrrrgs deqnlhrnkr slcldlktpq gaevlarlvr radvvvenfr svvkerlglt
      121 ydhlsainpr vilasisgfg qdgpycerpg ldqivqgmsg lssvtgepgq gplrvgiais
      181 dttagmflgq gillallhra rtgrgqwvht sliegmlnkl dfqatrytvd gevptqqgna
      241 hptlvpmgty rcrdgvvnia astdrmwanf crtveagwll ddpafqtatg raaerqrlda
      301 ainqctaaft aaeltarlna agvpcgpvfd igqafedaqv rhlrmtrpae hpvlgplall
      361 rspinlsaap hperfaraap dpgehtdeil rglgyddagi aalreasvas
//
LOCUS       WP_284494676             168 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Cupriavidus taiwanensis].
ACCESSION   WP_284494676
VERSION     WP_284494676.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..168
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18375
     Region          45..162
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mmrsrrqlla aavaaaaaca llpgtanaad rvavfdsana sriaasqrgk pfvlvvwsld
       61 cvyckrnfda lgklrakhpg lrvvtlatds aealpqvqqv ldrvkltnha wmfghepqer
      121 lryavdpdwm gemprtyfyr adgqrqgvsg visegdwarh lrwagiag
//
LOCUS       WP_284494815             598 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Cupriavidus taiwanensis].
ACCESSION   WP_284494815
VERSION     WP_284494815.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 598)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..598
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64279
     Region          36..>403
                     /region_name="PMT_2"
                     /note="Dolichyl-phosphate-mannose-protein
                     mannosyltransferase; cl21590"
                     /db_xref="CDD:473917"
     Region          477..578
                     /region_name="Arnt_C"
                     /note="Aminoarabinose transferase C-terminal domain;
                     pfam18583"
                     /db_xref="CDD:465810"
ORIGIN      
        1 mphrsdrlaa epalglaqpa apwhaarvag vpaltlalva igfallwfgt lgvrhllgpd
       61 egryaeiare mlssgdwvti rydglkyfek ppfhmwmtav ayalfgigdw qarlcvalag
      121 avgtgmsmla aarwfgarag lmaglvlvsa pmwivaahfn tldmtlsgal acvlasllla
      181 qhpaataaar rrwmlacwaa mgvavltkgl vgvalpglvl vlytaatrdl alwrrlhapa
      241 gialmllvav pwywlvarrn peflrfffvh ehwqrytstv hartgapgyf vpllvggflp
      301 wlgllpgmvr avtqragvah atgtrppfqp almaalwavs ifgffslsgs klpgyivpif
      361 palgmlasva ltqassrawt rqlramlvvg aigllaspvv atldanntpn alyrdyaiwa
      421 alafalvmas aaaalwllrr qgrmasvtgy afgmllafsi allgheaigr sasgidlaap
      481 iervlrpgmp lygvgmldht lpfylrhplt mvaqadelaf gaaqeprkwl ptidafvdaw
      541 qhgpravall spqafaelga rvpmhviard wrrvavsnfp fagelqarrr vpdspaip
//
LOCUS       WP_284494842             255 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Cupriavidus
            taiwanensis].
ACCESSION   WP_284494842
VERSION     WP_284494842.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 255)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..255
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=26931
     Region          7..231
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mdsqfqwtsa actdvghara rnedacldrp aqalwaiadg mgghalgdva sqavvaalga
       61 lpaqgpledr vgathaalqa vnrelvdeaa rlgvrcigst vvvllatdgr cacvwagdsr
      121 lyrlrggqla rltrdhnyag qllatgwite eqarrhptrn titravgatp alepeqwldd
      181 vadgdifllc sdglsnevdd dsiaavlarh dvaqaapelv rlaldaggrd nvsvvvvraa
      241 radehscrrs mtcpk
//
LOCUS       WP_284494891            1496 aa            linear   BCT 25-DEC-2024
DEFINITION  NACHT domain-containing protein [Cupriavidus taiwanensis].
ACCESSION   WP_284494891
VERSION     WP_284494891.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 1496)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 1496)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1496
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..1496
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=166621
     Region          328..1102
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mqlpdidfas irlhrksqps afeelccqla sdeeldqerv sfirkglggd ggiecfatls
       61 dgtetgwqvk yywdiasais sldeslnkal vkhpkmtrfi aclpfdlsds rrddvktale
      121 rwttwkdkri anaassgrqi eidrwdafel kkrltastat aagrvaywfg qslltsewfr
      181 ssferaragl geryspenhv dlpirrviea taldtrlykd ladfseaiaq slartnmsds
      241 tavnaceaaa relaqaaevq gkpifvaavr eavsvardav lpwdqtqrna fppdhpnpqa
      301 saianlsstl nsiarelafp hwdhvgtral lvvgeagsgk shlladvcdh aiegerpavm
      361 vlsgklpdae pwaeilkdlg lprdllpetf lgalnaagqa lgvralvmid alnekngrai
      421 wperlaglvh dvgrfewisl vlscrstyeq vvipeelnsd rlprvkhegf serqarqylk
      481 krgislgeep nsaeefetpl flriccdala ldgqtvlths lggvteifnl ytkaivnrvn
      541 kqigataqrr fveraistla qemadtgree vlssraydli seffpavvsa eedilfqlqn
      601 egllsaqpsq edkdqeeyrf tfqrmsdhai assllhrsie ggnvvaafsg dtavrramad
      661 afwplsagvl ealavqlper fgvelndmpd lsdvwgvsea feaslltrnp kslsnrtwel
      721 ieqvggnelr yetlvalstd pgqdhnaeyl dgelrgmsmp qrdaiwsthl atnrraterl
      781 tdwvreadql aihserasla glqlcwflta sdrlvrdtat kalvvllagr pklaealwtr
      841 fkslddsyvt erlvaaiyga smqgrwsaed lsslvmvihs dilvsiefpa niltrgyalg
      901 lihfakskaa lpdsvdaspa nltfrspwpi eyvteaqies yertyrgnsr hhdeivsstv
      961 fdgdfaryqi dptlrdcsva tkasgkvptd aqlaqdwldr frsnasqeml aahdalvsam
     1021 segadrsyae krdiadraks afraavgeev yaqwsaeasn wrqsgmfqqf gnrrdapagf
     1081 nlawarrwvc krahdlgwse alhgafdssi rndrnthqve rigkkyqwia fyelcarmad
     1141 nlqplpgrda avdvlrlrni dpsllvarte ddgwrrfeep sfwvppqpel ppialdaale
     1201 wlganvdyvd gednievtnp tddkhwlvlk gfeswrggsk svkldtwrri acfvvrkrdl
     1261 kktldlikhk hfqadddvps arsagfhsyl gehpwswrtg dekvddewik gwsplrfdda
     1321 grvsirptta aylaesgsyd asitqtinln lpaawlmdgl glhltdgeti ryvdkdqvvr
     1381 fmdpsvaatg rsaalidrea flsflkkenl vavwalagek nvygeasrgf ggrwtytrif
     1441 hslgskival eryqthdapd dsqlaalraa aanidnndnd ddadddwtal adcdgn
//
LOCUS       WP_284494918             354 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Cupriavidus taiwanensis].
ACCESSION   WP_284494918
VERSION     WP_284494918.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..354
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=37759
     Region          21..352
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mkhhstapld ravqkrqkhe ptrrawllrh gsaiagacvl aalvgasqst laqdgypskp
       61 vtivvgfppg tatdtvsrvl aerlsqrlgq qfivdnrpga ggsiaagiga rakpdgytll
      121 vvgaasqain phlynkltyd akkdfapigq lawlpylfvv nkdnpakdlr qflaqakksp
      181 nsvtyastgv gtgahlvmsv llakagvqmv hvpykgsgqa qtdllggqvm csfdtmvsel
      241 amvksgklka laistprrse ifpdvptvae qgfpgfdlgv wlgligpagl paeiqnrlak
      301 evnlilaepe trtkliqlgt evrgtsspqe fgkiirtdye ywgkvvrdfn vkad
//
LOCUS       WP_284494928             322 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Cupriavidus taiwanensis].
ACCESSION   WP_284494928
VERSION     WP_284494928.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..322
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33869
     Region          6..320
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mkkptssirr avlicslvlp silhaqqsst vpvkiyvgyg pgggtdvvar avgeelskmw
       61 nrpvivenrp gangaiaska varaepdgss llvmpptsli idaalrpnia vdpgkeltlv
      121 sglvttplvv vtpasapynn ladlikaara angkfsygwg nlgmrvgiee laqktgvkma
      181 pigyksagqs vpaivsgeid mlmidmapia qlvkagkvka lavstpersh mlpnvptfke
      241 sgvdvqltgs ialyapakvs qtvikkmrsd vasvlkntel rsritgtgmd aydgsqdyfe
      301 aylmqrknsi eavikagdfk le
//
LOCUS       WP_284495015             253 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Cupriavidus taiwanensis].
ACCESSION   WP_284495015
VERSION     WP_284495015.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 253)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 253)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..253
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28483
     Region          4..253
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mtptaliadd eehlraylrg klqrlwpelq ivaeatngie aadaiarlsp svafldikmp
       61 glsglevaqg ietdtrlvfv taydefalda feraavdylv kpvseerlgr tierlrkalq
      121 eaaplpelaq llnqltrtqp raegggqlrw vrasrgntts hvpiqevmyf qsddkyvvvh
      181 trdgehlirt plaelmagld pevfwqihrs sivnmeyvag trrdesgrlf vrmrgsdael
      241 pvsraymhrf rqm
//
LOCUS       WP_284495157             548 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Cupriavidus taiwanensis].
ACCESSION   WP_284495157
VERSION     WP_284495157.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 548)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 548)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 548)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..548
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58609
     Region          3..543
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mllssrrrfh pltlatvama lliavpvlvi asavllpagd twrhlidtvl aeyvlntvwl
       61 lcgvaagvll lgvttawlvs tyrfpghavm ewalvlpmam payviayayt dalqfagpvq
      121 gwlreltgwr areywfpeir slggaivlfs lvlypyvylt araaflqqtq ntleaarllg
      181 hgtwsrlwrv vlplarpgiv agtalammet ladfgtvayf aiptfstgiy rawfslgdkn
      241 aaaqlsacml lfvaaillme rasrgraqvf gnqrraaawt ldgargwlal aaclvpvllg
      301 flvpalmlcr maltdgdaqf gprfvglvrn sfllasatal aavavalgvg yaaravngkr
      361 swlmrgltrv cgmgyalpgs viavgvlvpv arldnalsaw lqqqfgvsag llltggiaal
      421 vyallvrflg valqavnagl gkitpsmdaa arslghgpga tlrrvhlpml rgslltaali
      481 vfvdvmkelp atfvmrpfnf dtlavqaynl aaderlteaa taslvivavg llpvivlsrt
      541 irrqaqpr
//
LOCUS       WP_284495237             143 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Cupriavidus taiwanensis].
ACCESSION   WP_284495237
VERSION     WP_284495237.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..143
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=15462
     Region          <2..141
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mhipykgsne svlamlggei davfggwglt stqvnagkvr vlavtspqrs pmlptvptlr
       61 elgipfglns wyglvapsgv apdtmkrlee slrkavgqpe ianrlrnmgm qpqsstsael
      121 rdrirsdydi wgkkiaetgv qkr
//
LOCUS       WP_284495245             342 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Cupriavidus taiwanensis].
ACCESSION   WP_284495245
VERSION     WP_284495245.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..342
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=35921
     Region          41..340
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mkhnmgrasv tatplpdprr rallrglaal glgaagsply asnawparpi rlvvpappgg
       61 gtdlfartla aalgkalgqt ivvdnkpgat giigndavak aspdgytllf tyaaavvinq
      121 tlqprlpydg lrdlvpvaqi gaggnflvvt pdfpartlre fvdhvrkhpd aydygswgig
      181 sgghltmaal glqtgiklrh vpykgvapil adlqggvika afvdtssslp liragklral
      241 avsgtrrapa tpevptmteq gypfdtdswy glfapagtsa aivqrlnaev nrlmseapmr
      301 erflqlnmgm appktaeqfa qtvradvgvw gkviqanhit vd
//
LOCUS       WP_284495271             364 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Cupriavidus taiwanensis].
ACCESSION   WP_284495271
VERSION     WP_284495271.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..364
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38963
     Region          8..363
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mkpawsclnd vtiidvsqll pgphacsllr qlgadvikve qpgsgdtarq lgahvyaqfn
       61 rgkrsvaldl ktdagraafl dlvreadavv egfrpgvmar lglgydalaa vnpaivlcsv
      121 sgfgqtgpya shaghdlnyl alagywatpv qvhdavsrpr vrvsdyaasg yaalslavai
      181 msarqhgqgq hldvsihdam lswtahgawt araheaspha sptvmpendl fetrdgrhla
      241 mgilenkfwd nlcaalgdaf palrdprfat raarsghkve vndlmaavfr trdltewaaf
      301 fepldipfsp vlgagdlfed ahvrargvvr hvpggitvdf pvkfslglpe gedfvagvge
      361 hnqr
//
LOCUS       WP_284495278             397 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Cupriavidus taiwanensis].
ACCESSION   WP_284495278
VERSION     WP_284495278.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..397
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42561
     Region          8..393
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mseadsrpap agpldgirvl dltavvlgpl atqvladfga dvikvegpeg dlmrangvsq
       61 hagmssiyla lnrnkrsvvl dlktpdgaaa lraliagadv lvhnmrvaai erlgfgyaev
      121 arinprivyc matgfgqdgp hrdkpafddi iqagcglval gsasgerpey vpslladktt
      181 glalanavla allyrerhga gqlvevpmle tmtafvmaeh lggltfeppp agagyarllq
      241 ggrrpaptrd gwicalpyte rhwlaffrav grddlaeryd vadraqrnan iralyghlae
      301 ltparttgew mdlfesldip atpiygldal vdhphlravg lfqqthhpte gplrevrpaa
      361 rfsatplslr rhapalgeht aevlqelaia pdahqhr
//
LOCUS       WP_284495299             406 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal-phosphate-dependent aminotransferase family protein
            [Cupriavidus taiwanensis].
ACCESSION   WP_284495299
VERSION     WP_284495299.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Koper,K., Han,S.W., Kothadia,R., Salamon,H., Yoshikuni,Y. and
            Maeda,H.A.
  TITLE     Multisubstrate specificity shaped the complex evolution of the
            aminotransferase family across the tree of life
  JOURNAL   Proc Natl Acad Sci U S A 121 (26), e2405524121 (2024)
   PUBMED   38885378
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Koper,K., Han,S.W., Pastor,D.C., Yoshikuni,Y. and Maeda,H.A.
  TITLE     Evolutionary origin and functional diversification of
            aminotransferases
  JOURNAL   J Biol Chem 298 (8), 102122 (2022)
   PUBMED   35697072
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..406
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43531
     Region          12..395
                     /region_name="PucG"
                     /note="Archaeal aspartate aminotransferase or a related
                     aminotransferase, includes purine catabolism protein PucG
                     [Amino acid transport and metabolism, Nucleotide transport
                     and metabolism]; COG0075"
                     /db_xref="CDD:439845"
ORIGIN      
        1 mvhldfhpsg rhflqipgps pvpdrilram syptidhrgp efgalgrkvl agikeifktr
       61 hpviiypasg tgaweaaltn tcspgdhvlm fetghfatlw kkmaealglr peflglpgie
      121 gwrrgvqadm iearlredtg hairavcvvh netstgvtsd iaavrraida aghpalllvd
      181 tisglgsady rhdqwgvdvt vsgsqkglml ppgisfnals pkaiaaseha klprafwgwa
      241 eiieankngy wpytpntnll yglsealdmi lgegleqvfa rhqrlaqatr cavrawglei
      301 qcadpavysp vltgvmmpdg vdadavrkli yerfdmslgq algkmrgrmf righlgdcnd
      361 ltlmatlagc emglklagvp lagsgvaaam aslqahaelp vlkaaa
//
LOCUS       WP_284495371             320 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase, partial [Cupriavidus
            taiwanensis].
ACCESSION   WP_284495371
VERSION     WP_284495371.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..>320
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
     Region          17..320
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mthspstadr lpllrrlgir tpiiqapmag vstpalaaav tnagglgslg vgamdaeaar
       61 ksiretralt sgpfnvnvfc hapavadaar eqawlaylap rfaefgatpp atlreiyrsy
      121 vtddamhaml leerpavvsf hfglpdagri ralrdagivl lasatsldea raieaagida
      181 ivaqgieagg hrgvfdpaav deglgilalv rvlstqtrvp viaaggimdg agiaaalalg
      241 aqaaqlgtaf iacpetiadg pyrdallqrk rptvltrais grharglanr ftelgaapga
      301 patpdyptay dagkalhaaa
//
LOCUS       WP_284495384             336 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Cupriavidus taiwanensis].
ACCESSION   WP_284495384
VERSION     WP_284495384.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..336
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=35527
     Region          3..330
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 matlnrrrfl qhaglaagas vlsglpalaa dafpakalsl vvpypaggas dasarifges
       61 isksvrqqvv venygggtgl igankvlaap adgytffhgs inevflapll npaarykpqd
      121 fllaapisda nivlmvrngi aadsldkfie farqskgkal tyatvgidsi yhlmgdalga
      181 rlgvsflhvp ykggapalqg laggevdfai lpyqssfdsm qqqgrlkilt sfsralppal
      241 ksvplisqsr lvpdfeytig ggyfvrqgtp aervavlrka igealakpdi rakleaegrt
      301 vlqpidsqeq anrmfdqyla rvdklirsvg rktnag
//
LOCUS       WP_284495390             325 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Cupriavidus taiwanensis].
ACCESSION   WP_284495390
VERSION     WP_284495390.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..325
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34405
     Region          1..323
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mnpirrhwia aaialaispl agaqsagdwp arpvrlivpg ppaggtdila rllaeqlska
       61 fgkpfvienk pgangmigse tvahaapdgh tllfsyagam vvnpslyvra ldplksfepi
      121 aqigsfgnll vvspalpvhn lqeladyark rpgelnygtw gvgsgghltm eiflqrakvt
      181 mhhvpykgaa svatdvqggt lpvgwtdvts qiqqvragrl ralavsgtsr lpqlpevptm
      241 seqgypfett swyglfapar tpaaivdrln aevnriiatp efkarlamln lpaaptvsaa
      301 qfrnvvakdt vawravvqaa gvrpe
//
LOCUS       WP_284495403             322 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Cupriavidus taiwanensis].
ACCESSION   WP_284495403
VERSION     WP_284495403.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..322
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33824
     Region          4..320
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mqirsllvlg llawscagla qsyptrplti vvpgppggat dtlaralaed mgkrlgqpiv
       61 vdnkpggggv iavqaitrgp qngytlllth saplintphl ypsvpydvrr dlafvtevav
      121 gkvvlavrrd vpaanvqefl awaaknkgkv sfgsygvgsf phlvgahlnt trgldmthia
      181 ykgeapmaqd llagniawai gsvttlgphi ksgrlralav mgnkrikemp evatiaesgf
      241 adqelrapaw lgllarsgtp adilarlete arasvqspam qarlealale pvgnspaefr
      301 qefeatepam arlikasgak ae
//
LOCUS       WP_284495460             303 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Cupriavidus taiwanensis].
ACCESSION   WP_284495460
VERSION     WP_284495460.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..303
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=32326
     Region          46..301
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mqfawsaspy pagaatgtap llhaltalpp vflvaaaall glvvgsflnv vihrvprmme
       61 rdeanyiael rgdplpypgr ynlmvprsac phcghaiapw envpvlsyll lrgrcsacka
      121 pisvryplve lacavlsalv awrfgpgaqa laalvlvwgl laltmidadt qllpdqitlp
      181 llwiglllnv tglfvalpda vigaaagylv lwlaywlfrl lrgkegmgfg dfklmaalga
      241 wfgwqalpal vllssvagvv fglvnialrr qqrdtpfpfg pfialagvvv llfgpgvlpl
      301 faw
//
LOCUS       WP_284495581             391 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Cupriavidus taiwanensis].
ACCESSION   WP_284495581
VERSION     WP_284495581.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..391
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40822
     Region          15..384
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mvhsdpapag gkqfsadylv igagiagasv aywlaragsv ivleresqpg yhatgrsaal
       61 ylesygtpqv rgltmasraf ldappagfad hpvlsprgam mlarpgeqdq ldahwqvlag
      121 lgaraqrldr agacalvpvl rpelvlgavl epdaadmdvh alhqgylrgv rhhggllacg
      181 aeagaierrd glwhvhagad iyrapvlvna agawcdvvag ragvapvglq pcrrsafvfa
      241 ppegievsrw pmfygfdetw yvkpdagmll gspanadpvp phdvqpeeld iamgihqiea
      301 attltirrpa rtwaglrsfv adgdlvggfd paaegffwva aqggygiqts aamgeacaal
      361 aqgrplpahi adhgvsaaml sparlrgqag r
//
LOCUS       WP_284495590             387 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Cupriavidus taiwanensis].
ACCESSION   WP_284495590
VERSION     WP_284495590.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..387
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41394
     Region          1..384
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mlhralegir vldlsrilag pwctqnladl gaevtkvehp ergddtrgwg ppyldapagt
       61 egdprlsgyf iccnrgkrsv tidygtaega aqvrelarqa dvlvenykvg tlrrygldyd
      121 tlkainprlv ylsitgfgqs gpmadkpgyd yvfqgmgglm sytgqpdgap gagplrtgva
      181 vvdlstgmya tsavlaalyq rqatgagahl dialldvava mnanqaanyl vsgqnpqrsg
      241 nahpncapye vfrcadghli laigndsqfa rfcavagvpa laqdpryatn sariehldal
      301 rarltalfpt rtraawteaf daagvpwgpi htmdevfahp qvqhrrlmqv aqhpvmgrvp
      361 mvrnpmlagh egppaappll gqhsppr
//
LOCUS       WP_284495599             326 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Cupriavidus taiwanensis].
ACCESSION   WP_284495599
VERSION     WP_284495599.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..326
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34553
     Region          4..326
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(41..42,46,124,128,131,149,152..154,173..174,178,193,
                     217..218,239..243,264..267,314,316)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(136,232..233,246..251,259..266,269..270)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 manvvrmyet ggpevlryeq mevgdpgpgq vrirhvavgl nyadtyfrng typvplpsgm
       61 gveaagvvvs vgpgvtnvaa gdrvtytgfv ntlgayster lvpaaplirl pesiafetaa
      121 amtmrgltsa ylmrriypfs qgdtillhaa aggvglivsq wakllgltvi gtvsteakae
      181 varahgcdhi iqytredvar rvreltdgag vsvvfdsvgk ttfmasldsl krrgtmvcvg
      241 tasgpvppfd pvllamkgsl fltrpalady iadpaekqal agelfdhvga gririginqr
      301 yaledavqah qdlearrttg ssifvi
//
LOCUS       WP_284495665             289 aa            linear   BCT 25-DEC-2024
DEFINITION  arylamine N-acetyltransferase family protein [Cupriavidus
            taiwanensis].
ACCESSION   WP_284495665
VERSION     WP_284495665.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Zhou,X., Ma,Z., Dong,D. and Wu,B.
  TITLE     Arylamine N-acetyltransferases: a structural perspective
  JOURNAL   Br J Pharmacol 169 (4), 748-760 (2013)
   PUBMED   23517104
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Sim,E., Walters,K. and Boukouvala,S.
  TITLE     Arylamine N-acetyltransferases: from structure to function
  JOURNAL   Drug Metab Rev 40 (3), 479-510 (2008)
   PUBMED   18642144
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Sim,E., Westwood,I. and Fullam,E.
  TITLE     Arylamine N-acetyltransferases
  JOURNAL   Expert Opin Drug Metab Toxicol 3 (2), 169-184 (2007)
   PUBMED   17428149
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Sinclair,J.C., Sandy,J., Delgoda,R., Sim,E. and Noble,M.E.
  TITLE     Structure of arylamine N-acetyltransferase reveals a catalytic
            triad
  JOURNAL   Nat Struct Biol 7 (7), 560-564 (2000)
   PUBMED   10876241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..289
                     /product="arylamine N-acetyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31194
     Region          5..265
                     /region_name="NhoA"
                     /note="Arylamine N-acetyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2162"
                     /db_xref="CDD:441765"
ORIGIN      
        1 mttlnaaqld awlarlgiaa ppsptlqald avlaahlasi pfenvdpllr rpvridleav
       61 fdklvtrrrg gycfelntll saglgalgya vtplaarvrw gvpddvptmt shmllrveva
      121 hrsyladvgf ggptpframp lsepadddfp yrlapspaqa dasafhsydl qargdagwip
      181 iyrfdltpqp sidfeprswy vsthpdsifl rrlmaartda dgtrvtladg elaerapdgs
      241 vrrtqlqqad avvqalsdrf gilldqdlrd glmaalpall apatasagr
//
LOCUS       WP_284495710             130 aa            linear   BCT 25-DEC-2024
DEFINITION  tautomerase family protein [Cupriavidus taiwanensis].
ACCESSION   WP_284495710
VERSION     WP_284495710.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..130
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=14133
     Region          2..59
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
     Region          67..124
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mphivlhlsg qadadltcrs akaiadlter vlgkrrdvia vtvqyiphds wiigdaplse
       61 qgrnafhldi svtdetntka ekaqfiaavf etmsgllgnl hpvsyvhvid araaaygygg
      121 rtqeyrhqhg
//
LOCUS       WP_284495811             366 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Cupriavidus taiwanensis].
ACCESSION   WP_284495811
VERSION     WP_284495811.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..366
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38733
     Region          1..351
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mnpfryeram tveaalqsia aaqqaagvqs lgedraphfl aagtnlidlv kggmmhpaal
       61 vdvrqlplrm ieataegglk lgalasnadt aqhplvrgqy pllraailag asaqirnmat
      121 nggnllqrtr cyyfydpgvp cnkrepgtgc paatglarqh ailgasehci athpsdmcva
      181 laalgavvhv asasgrreip fpefhrlped rphidttlrp delithivlp pagefarhac
      241 ylkirerasf afalvsvaaa ldladdgtvr aarlalggva hkpwrdpeae aqlqgrpatt
      301 ehfasvarfl lrdarawggp avpeslpgns fkialaerai vralemavag vlsntgedaf
      361 seealp
//
LOCUS       WP_284495955             456 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Cupriavidus
            taiwanensis].
ACCESSION   WP_284495955
VERSION     WP_284495955.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..456
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49138
     Region          126..454
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mslkphwkss rpwrrlagva lvlasvpaws qpaasaasaa papaaaaitv aaalatdpnv
       61 qgwmqgfppp pdklithvpg gnrfprnrwl fshvrelvpt asvwrgpgpa salpraeqpi
      121 gaipftdadg trrtfdemla ltytdgilvm hkgkviyery fgaldshtph iamsvtksfv
      181 gtlaamlaae gkldpaapvt rylpemagta ygdatvrqvm dmtigvryse dyadpkaevw
      241 dyaraggmla rpanyngpgt fydflktlqk dgshdaafay ktvnaevlaw ivrrasgqsl
      301 akllsdriwq pmgaeqdayf tvdsigtesg ggglnttlrd larfgetirg ngrfngkqii
      361 pasvvadirr ggsreqfars gsasvlpgws yrdmwwvshd shgmfqaagi hgqriyidpq
      421 aeltivryas hpvagngann aitfrafrav aealsr
//
LOCUS       WP_284495972             390 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Cupriavidus
            taiwanensis].
ACCESSION   WP_284495972
VERSION     WP_284495972.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..390
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42012
     Region          8..383
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mtasappflp fvrpeidaaa iaevgkvlas gwitsgpkmq afeaalsdlf ggrpvrtfan
       61 gsatmeialr iagigpgdev ittpitwvat anvvvavgak pvfvdidprt rnldldavea
      121 aitprtraim pvylsglpvd merlyaiaak hnlrviedaa qaidsrwcgr rigafgdlvs
      181 fsfqanknit tieggclvmn tpeeavraer lrlqgvirtg mdgmdveepg gkfnltdvna
      241 avglaqlerl daitarrael adtyfrcaad sglqalgiel pqaldphaat tnwhmfqvvl
      301 ptarmqggpa qarhklmeam rergigtgvh yppvhlftyy rslgwregml phaerigrgi
      361 vtlplfpamq asdvervcat lsetckrlsq
//
LOCUS       WP_284496018             414 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Cupriavidus taiwanensis].
ACCESSION   WP_284496018
VERSION     WP_284496018.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..414
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44065
     Region          6..414
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 maggqaparg alagvrvldl srilagpwca qnladlgaev ikverpgagd dtrswgppwl
       61 pgadgqpsrd atyfaganrg kqsvtldias pqgqqivrel aaksqivlen ykvgdlkryg
      121 ldydslkavn psivycsitg ygqtgpsahk pgydfifqgl gglmsvtger ddlpgggpqk
      181 vgvavvdmlt gmyatvavla alrhaertge gqhidmalld avvavgatpi iaqrvtgkam
      241 prfgnahanm vpyhvfatad gymivaagnd gqwqaycrgi erpdlaader fatgpgriih
      301 rdtlvpllea hmrsrptahw vqaleaqgip cgpindygqv ledpqvrhre lqvdlvrddg
      361 svcptvkspl rlsatpvqyd appprlgqht eqvletvlgl saeriarlre qgvv
//
LOCUS       WP_284496037             318 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Cupriavidus taiwanensis].
ACCESSION   WP_284496037
VERSION     WP_284496037.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..318
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33899
     Region          16..316
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mkrpllaltl ltmafpvaas typdkmvrll vpsiagsapd iiarqvaerl antwkqqviv
       61 enkpggngiv amsalkqasa dgytlvlfha aaavttpvmy keakfdiqrd tevaatlayt
      121 pmmfvagpat pykslgevik eakgrpddvv igsptrgsvp hltaemmgql qnarfrqvsf
      181 sgttqaiqav vkgdipvyvd giaplvplvr ggrlkalavt sdtslpgleg iplakdvapg
      241 lvakgwftif apkgtpvsvl drvnsavnqt lrqqpfvdrl kdlgtypmpm srpegakfie
      301 aeklrwekvi adagvkpe
//
LOCUS       WP_284496041             149 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Cupriavidus taiwanensis].
ACCESSION   WP_284496041
VERSION     WP_284496041.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..149
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16299
     Region          10..147
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mirateyvls etpfvvrrtv rwgdcdpagv vytgrftdyl lgavglytsh maggdgrlgd
       61 vhgvgtpcka mrfefigtlw pddvidiacs veairtrsfd ircmarrpdg apvfdamfsp
      121 icvrldrreg tpipaslrav ltrflspal
//
LOCUS       WP_284496078             164 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Cupriavidus taiwanensis].
ACCESSION   WP_284496078
VERSION     WP_284496078.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..164
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17828
     Region          28..158
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mrapamllra llaaglllaa agaaalevgd tvrlpevrtl dgrtlsaaal agkplvveyw
       61 atwcpfcamq nprlqklyer trgtplqvla isidkdprea adymtkrgyt fpatmdspal
      121 qavfgkrkgl pelyvidarg rlvqkevgem leedvaaler yarp
//
LOCUS       WP_284496087             298 aa            linear   BCT 25-DEC-2024
DEFINITION  DODA-type extradiol aromatic ring-opening family dioxygenase
            [Cupriavidus taiwanensis].
ACCESSION   WP_284496087
VERSION     WP_284496087.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Vaillancourt,F.H., Bolin,J.T. and Eltis,L.D.
  TITLE     The ins and outs of ring-cleaving dioxygenases
  JOURNAL   Crit Rev Biochem Mol Biol 41 (4), 241-267 (2006)
   PUBMED   16849108
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Siegbahn,P.E. and Haeffner,F.
  TITLE     Mechanism for catechol ring-cleavage by non-heme iron extradiol
            dioxygenases
  JOURNAL   J Am Chem Soc 126 (29), 8919-8932 (2004)
   PUBMED   15264822
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..298
                     /product="DODA-type extradiol aromatic ring-opening family
                     dioxygenase"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016701 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31895
     Region          3..285
                     /region_name="45_DOPA_Dioxygenase"
                     /note="The Class III extradiol dioxygenase, 4,5-DOPA
                     Dioxygenase, catalyzes the incorporation of both atoms of
                     molecular oxygen into 4,5-dihydroxy-phenylalanine;
                     cd07363"
                     /db_xref="CDD:153375"
     Site            order(9..11,46,115,171,235,277..278)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:153375"
     Site            order(9,46,235)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:153375"
ORIGIN      
        1 mlpslyishg spmlaidpgp tgaafealga rlraqrprav lvisahwiys tlavtsrerq
       61 eawhdfggfp relyalryda pgspdlaarv kelvesaaip gagfvghdde rpldhgawmp
      121 mrhffpdadt pvvqlalnpy lspatqiaig ralaplrdeg vlvlasgsft hnlqevfggg
      181 rreqhgpqae pyveafrtwm aealdhtlat gdtrriadyr aqapyarrah ptdehllpff
      241 valgaalgaa pgpegaraal peparvsrva devtygvlam dsfvfegiga aaplraaa
//
LOCUS       WP_284496178              81 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome, partial [Cupriavidus taiwanensis].
ACCESSION   WP_284496178
VERSION     WP_284496178.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 81)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 81)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 81)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 81)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 81)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007114
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         <1..81
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          <1..78
                     /region_name="CytC5"
                     /note="Cytochrome c5 [Energy production and conversion];
                     COG3245"
                     /db_xref="CDD:442476"
ORIGIN      
        1 asaevgkkvy eqvcaachaa gvagapkfgd kaawaprlke gmdavhnfal kgkgvmppkg
       61 gyagpdadvi aasdymanaa k
//
LOCUS       WP_284496256             615 aa            linear   BCT 25-DEC-2024
DEFINITION  IucA/IucC family protein [Cupriavidus taiwanensis].
ACCESSION   WP_284496256
VERSION     WP_284496256.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..615
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=68393
     Region          33..605
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mqgkiedaga rrpaaelael aalaaarrce etllncycre vaapagqlrv gppaaqsdwp
       61 aaiamtlqra paqvlevqlp hshdrllavv ggawltgnyr ylspvfhkae nkpwalldwe
      121 alaalllrem aqqhelppnt elmeqirnsv avstevlsvp vpaaipadpv dayidseqsl
      181 tfghpfhptp ksrqgfsdad llryspelrt rfalawfavp rddiaqqsll dtscdqliaa
      241 napavsadrv avpvhpwqag ylrehplvrd alasgrmqdl gtqgadffpt ssirtlyqpg
      301 npyfyklsln iritncvrkn awyelesamh vnrvlrpllp elarqfpgla lmeepaflsv
      361 dlrhadieqn rqviegfgli lrqsvdtlra pdcvpllags lfgnhyygea rmqrlltala
      421 aragstvdam terwfsayva qliypvfhlf fahgvifeph lqnvvlglrq dmpaqlflrd
      481 fegvkltpsr hpassmsgvs erartslwyd eeqgwnrvay clfvnnlcev iaqlgagrqv
      541 mtarlwsvvr hhlhtyqhrh gnaasarrin gvlagrpfpa ktnfsnrffq radrastyvp
      601 vanpipfagm eaawq
//
LOCUS       WP_284496241             260 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Cupriavidus
            taiwanensis].
ACCESSION   WP_284496241
VERSION     WP_284496241.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..260
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=27621
     Region          26..209
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mtkfvsppfv pnrmecrdla aaafprripa plpqlslwqv eladpghara iaaadclcqt
       61 eqahcatlrq aadrrrftga rvalrtvlaq rldcapaalr lrtgshgkpy veaagapafn
      121 vahagdyawi alaeagevgv dieridpalg qaemheiaah cltprerawl allpahawpr
      181 afftlwtake allkalglgi adhlqhvsvv adgpggacrl avlrepgqla ghaaalarmq
      241 lyrvagpdgy aaamawvppa
//
LOCUS       WP_284496319             415 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Cupriavidus taiwanensis].
ACCESSION   WP_284496319
VERSION     WP_284496319.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..415
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45245
     Region          20..413
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mnqtrneivv igggavgvac alwlrrdghq vvllepedia sqcsygnast faeyacspia
       61 npsvwsnlps llfsqdspfv irwsrlpqll pwlmrfmgqc tqenaktntk rlarllrqty
      121 tgyeplldda psaralirtn gclyaytsek glrgaqadia lrrslgieqe vldsagieal
      181 epamagqsvg gvlfprschl rdtqgfiqal aapmiaegsl rrgratrlqs csdgvhihcd
      241 dgstlvadrv vlaagvwstk laasmgekip ldtergyhve felgrelltr ptcpvesafy
      301 mtplangrlr aagtvelgsl rdpinparir yieervrkvl nidapvshrw mgfrptlpdc
      361 vpvigpsred arvihafghq hlgitlagat gelvaahvrg qapewlgeys asrfh
//
LOCUS       WP_284496345             170 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Cupriavidus
            taiwanensis].
ACCESSION   WP_284496345
VERSION     WP_284496345.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..170
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18334
     Region          3..107
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mpptdftamp cpvarsmavl gerwailvlr eafygstrfd efernlgiap nilsarlktl
       61 vahgllarva peggarhvyq ltdkgrdffp ayvalkawad rwmtddkgpl tllqdrrtgt
      121 eiaepaltrv dgsaitlddl qvvpgpgags slrrrfgdta aavgtetghd
//
LOCUS       WP_284496362             584 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Cupriavidus taiwanensis].
ACCESSION   WP_284496362
VERSION     WP_284496362.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 584)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 584)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..584
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63906
     Region          14..584
                     /region_name="COG4986"
                     /note="ABC-type anion transport system, duplicated
                     permease component [Inorganic ion transport and
                     metabolism]"
                     /db_xref="CDD:444010"
ORIGIN      
        1 mmppadrraa qpapgfdsql lrappnrfdl allpmilavi vmiafaaqqm nvpfqpgqpl
       61 avhldvaylp yylmrtsirm laalaasllf slafaalask srtaekvlvp aldilqsipv
      121 lgflsitvtg fialfpgnla gvecaaifai ftsqawnmaf slyqsfrtip gdlleaaamf
      181 rlsawqrfwr levpyampgl lwnmmmsmsg gwffvvasea isvsghdirl pgigsyiala
      241 iqqqdlaaig waivamlvgi llydqllfrp lvawadrfrf etlaqdklpq swlldllrrs
      301 awvgallaqa talasrtlaw gartgapapa rpadprrarw pgrardaviv lvalaallrv
      361 gyfvhsevgw aeavhvlwlg tltmvrvivl ialaalvwvp vgiriglnpd lariaqpvaq
      421 flaafpanlm fplavmliar fglnpeiwls pllifgtqwy ilfnviagas giptelrlaa
      481 rnfglrgwll wkrflipavf pslltglvta aggswnasiv seyvtwgdrt ivatglgsyi
      541 aettargdfp rialgivvma lfvvgfnrfl wnrlyqlaqe rtrl
//
LOCUS       WP_284496388             286 aa            linear   BCT 25-DEC-2024
DEFINITION  TPM domain-containing protein [Cupriavidus taiwanensis].
ACCESSION   WP_284496388
VERSION     WP_284496388.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Sirpio,S., Allahverdiyeva,Y., Suorsa,M., Paakkarinen,V.,
            Vainonen,J., Battchikova,N. and Aro,E.M.
  TITLE     TLP18.3, a novel thylakoid lumen protein regulating photosystem II
            repair cycle
  JOURNAL   Biochem J 406 (3), 415-425 (2007)
   PUBMED   17576201
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..286
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29962
     Region          27..232
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrhpwrwcar hgwlaaallw laallgspal gadgfvavpp ltqrvtdltn tltpqqrgal
       61 envlaeyeqq rgsqifvlmv pttdpepida ysirvadawr agrqgiddgv ivliakdnpp
      121 glrkmrlevg rgvqgsltda mskrilqdvm aphfrqndfy gglaagisai qatidkegla
      181 apqrkaqqas aldqwlpall plaiivfffl sailrrrgpq ivttrrgrdv iagglgglgg
      241 ytigqdwgrr sggwggggds ggfgggggfg ggggggfdgg gasgnw
//
LOCUS       WP_284496433             632 aa            linear   BCT 25-DEC-2024
DEFINITION  ABCB family ABC transporter ATP-binding protein/permease
            [Cupriavidus taiwanensis].
ACCESSION   WP_284496433
VERSION     WP_284496433.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 632)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..632
                     /product="ABCB family ABC transporter ATP-binding
                     protein/permease"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69931
     Region          21..615
                     /region_name="ATM1"
                     /note="ABC-type transport system involved in Fe-S cluster
                     assembly, permease and ATPase components
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5265"
                     /db_xref="CDD:444078"
ORIGIN      
        1 mrrysttaep apdrasvklf pgqraprsdw qtvrnllpyv whykwrvmla laclvaakva
       61 nlgvpvlmkr lidsmnitag dprallavpv glivaygllr lsatlftelr eilfskvtqs
      121 avreialqvf qhlhalslrf hldrqtggms rdiergtrgi qslisyslys ilptlvemal
      181 vigffilhyd iwfaaitgca lvgyivftiv vtewrthfrr rmneldsran qkaidsllnf
      241 etvkyfgnea yeaqrydenl rkyrtaairs qnslsflnfg qqaiiavgli lilwratvgv
      301 vdgkltlgdl vlvntlmiql yiplnflgvi yreikqattd mdrmfvllgt hqevadapga
      361 palrvsgaqv rfrdvrfsye pdrlildgvd ftiaagstta vvghsgsgks tlarllfrfy
      421 dvgggaieid gqdiraitqd slrraigivp qdtvlfndsi yyniaygrpd atrdeviaaa
      481 qaaqidafir elpqgydtpv gerglklsgg ekqrvaiart llknppvlvf deatsaldsr
      541 teqaiqaelm rlaqnrttll iahrlstvvh adqilvmdhg rivergthaq lmraggryae
      601 mwdiqaraaa kggealgaqa laldvgdatq da
//
LOCUS       WP_284496930             762 aa            linear   BCT 25-DEC-2024
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Cupriavidus taiwanensis].
ACCESSION   WP_284496930
VERSION     WP_284496930.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..762
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..762
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=80716
     Region          63..>186
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          196..754
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mtatqlqppa qadaatpral rlalqqaagv llvtrapqpa arpapgqpga asdyvpalpd
       61 vfiavrdsge vlafnghvdl gtgirtalaq ivaeeldvpf ghvrmvlght eatpnqgpti
      121 asasiqisal plrraaaqar awlqaraarq lgvdaaavea qdgvfrvrgt qasigygalv
      181 agehvelpla edvltkpvea yrivgraapr vdipdkarga ltfvhdvrvp gmlhgrvvrp
      241 pyagrdsggf vgnsllevdr dsvrdvpgll evvvqgdfvg vvaereeyav qaarrlrvrw
      301 kpvpplpald dpepalranp atrrellseg elpaagagtv lqrryvwpyq mhgsigpsca
      361 vadwhedglt vwsgtqnphm lridlsrlcg lgedrieivr meaagcygrn caddvcadaa
      421 llsravgrpv rvqlsreqeh lwepkgaaql mdvsatlgad gallgydfts rypsndaptl
      481 alvltgavpn aprtlemgdr tavppyayaa rrigcddtpa ivraswlrgv salpnafahe
      541 cvidelalaa gadpvdfrlr hlpdaraadl lravaeaagw qrgaagsrgv pdaegrlrgr
      601 gvayaryihs rfpgfgaawa awvvdlsvda gtgriaidkv vvgqdtgmvv npdgvrhqvh
      661 gnvvqtlsrv lkeqvrfdad gvasrewgsy plltfpeipp idvvlmprqs epplgagesa
      721 slpgapaian alfdalgvrl rrppfvpetv laamasttst kg
//
LOCUS       WP_284496970             615 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)-binding protein [Cupriavidus taiwanensis].
ACCESSION   WP_284496970
VERSION     WP_284496970.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 615)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 615)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10602124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..615
                     /product="NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64989
     Region          <27..536
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          78..153
                     /region_name="NAD_binding_8"
                     /note="NAD(P)-binding Rossmann-like domain; pfam13450"
                     /db_xref="CDD:433218"
ORIGIN      
        1 mtitrrdfln gtalaiaagl apaqllraqp rapstlyppa ltglrgnhpg tytlahslar
       61 egakypavla reafdlvvvg gglsglaaaw fyrrrfgakr rilildnhdd fgghakrnef
      121 tvrgkrlvty ggsaempaga agdaavrell aglgldaaha pagaaaadpy aalgmgravf
      181 fdaehfgrdq wvagdpfgew idarssgrad gpdaaalsrf ldsaplpaad raalarlaag
      241 ttdylpalsg aeriaalram ryasflrdka giglagqrfl rsrshdayal dadgisvada
      301 iaiglpagan mpapagnarl gkspasrlwf adgnaslarl lvqglipava rigrpeevvs
      361 aafdysrldr egdpvrlrln staiavepdg pitrvtygfs gnlhrvearh vvlagynmmi
      421 pyllpslpaq qkailhneak aplvytkval dhwqafaalr trrihapama ytdlwleppa
      481 grapsdpavl hmlyvptvpd sgmpardrfr agralllgtp fdamerdira qldrmlghqg
      541 fvsqevirgi tinrwahgys ympdslagen vppgaawpgl agvgnisian sdnagspslt
      601 aavaqgkrai erlpg
//
LOCUS       WP_284497095             324 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Cupriavidus taiwanensis].
ACCESSION   WP_284497095
VERSION     WP_284497095.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..324
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33611
     Region          8..322
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mlkpafplvv saflalalis lpvaaqypqk pvrlvvpyap gggtdsiarl laeklagrlg
       61 qpvvvenkgg asgiigsdav akspadgytl llagvgplav spsliqkary qptkdfvpiv
      121 kvssaamvlv taskkpgegl kelveyarnk pgqltvanag dgspqhicaa mfarsagitv
      181 nhiaykgaan aitdllggtv qvlcdnvgtv rpfiqagklr plavstrkra ealpdvptfe
      241 aqglhgidfa lwfmlvapag tptevvtrln nevnailkqp dviqklhdng sepaggpvts
      301 anqflakena awlemvraig ltkq
//
LOCUS       WP_284497047             335 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Cupriavidus taiwanensis].
ACCESSION   WP_284497047
VERSION     WP_284497047.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..335
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=35427
     Region          21..328
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mpaaatdskr ttmktritel lgirypiiqg gmqwvgyaem asavsnaggl giltaltqpt
       61 pedladeirr cremtdkpfg vnltllpsin pppyaryldv iiesgikvle tagnnpkehi
      121 arakaagikv ihkcvavrha lsaerlgvda vsidgfecag hpgeddvpgm vlipqavrkl
      181 sipviasggi adgrgmaaal vlgaegvnmg trfcatreap ihdnvkqalv qaserdtnli
      241 frtlhntarv lrnavsdevv sierrpggaq fedvkhlvag vrgkaalkag etdggiisag
      301 qcvgliddvp sceeliarmv adcrehlsva sryfa
//
LOCUS       WP_284497266             239 aa            linear   BCT 25-DEC-2024
DEFINITION  pyrroline-5-carboxylate reductase family protein, partial
            [Acinetobacter baumannii].
ACCESSION   WP_284497266
VERSION     WP_284497266.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         <1..239
                     /product="pyrroline-5-carboxylate reductase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004735 - pyrroline-5-carboxylate
                     reductase activity [Evidence IEA]"
                     /GO_process="GO:0055129 - L-proline biosynthetic process
                     [Evidence IEA]"
     Region          <24..229
                     /region_name="ProC"
                     /note="Pyrroline-5-carboxylate reductase [Amino acid
                     transport and metabolism]; COG0345"
                     /db_xref="CDD:440114"
ORIGIN      
        1 lmfefaeevk fenqiilkqk qhevkkadiv vllldpkdlk ailaplkkwl adktivsmma
       61 gvniqqlmsi tgskkiirvi snppvltytg thvligsdyl epldkeviet iysatgrtyw
      121 ansesqsdai ialsgsgpay ffyildsmvk tgvsmgldkq faldlilqaa sgavemvrks
      181 nvqpselcgk vtlangites alrmfelgnl sddirlalka ayhrskeisl einaeikrh
//
LOCUS       WP_284497352            1078 aa            linear   BCT 25-DEC-2024
DEFINITION  type I restriction endonuclease subunit R [Escherichia coli].
ACCESSION   WP_284497352
VERSION     WP_284497352.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 1078)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1078)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1078)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1078)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1078)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1078)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1078)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1078
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..1078
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=122095
     Region          1..918
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 maahhevhfe qyiteqlvnn gwkeghschy dqqralypqd vmdwvkatqp dawhklnklh
       61 gvnaeqvlle rlekalsshk agsktggtin vlrkgftiag cgtiamgqrk pedarneeri
      121 aryehnilrv vrqlkycptr eweidlvffi nglpvatael ktdftqsles aiaqykedrl
      181 pvdpktkrke plltfkrgav vhfamsdtei amatklagen tyflpfnkgh dgstsdlpvh
      241 inlpgedgey pvsyfwqeia qkdnwlrify sfvyvetkev adsngkverk etqifpryhq
      301 laavnkmidd arqngagmqy lcehsagsgk tstiawtahd lirlrstdgk avfksviivt
      361 drtvldsqlq davqqmdhqy gvikaidrek sseskskqlt ealltgtpii vvtiqtfpya
      421 leailtnqsl aqsnfaviid eahtsqtgst akglraaltl nlspqeleqm siediltkvq
      481 earampknvs hfaftatpkh stkmlfgrpk dpnqpvsddn lpesfhlytq rqaidegfil
      541 dvlenythyd taykigennl dekrvdskqa rralarwmsl hpttvsqkve fiikhfkani
      601 ahllegeaka mvvtsgrpqa vkyklafdky ikkhgiegiq alvafsgkvp gkdlgdedsq
      661 dpleidfdke yteynlnpdt hgadlrhefe kteyrvmlva nkfqtgfnqp klvamyldkk
      721 isdveavqtl srlnrtypgk dttfvidfvn dpqtilnafk kydkgaqlne vqdvnviydi
      781 kdildeqniy nhqdlelfkq argksilgqs pdkkshahkk llaatqrptd vfnvklkelv
      841 daanhwdqqy nkahlagdek aanyaesqrs dftkqrealm rfksdlarfv khysymaqli
      901 efgdpelenf aafahllsrr lkgvtpenid lsalvlekfk ikydkeplpe afnqvlepir
      961 pnyndpadre qafladiirr lnelfgdvgd epgrrnfang titrvtqnpi vveqiekhdk
     1021 sialkgdlpq avkqavvqal lkegdiartl lkdpqvmasy velifdmmkq gaeqaavk
//
LOCUS       WP_284498642             114 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein, partial [Synechococcus sp.
            MU1655].
ACCESSION   WP_284498642
VERSION     WP_284498642.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. MU1655
  ORGANISM  Synechococcus sp. MU1655
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Synechococcus sp. MU1655"
                     /db_xref="taxon:2508355"
     Protein         <1..114
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
     Region          1..106
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 avglglavqg flalgpslsp lpdpkpkaal ittgvyghcr hplyravvic slgvvlakgs
       61 llhlglfvll vavlngkahr eeerlcnvhp dylqycahtp aivpgipgld wrkg
//
LOCUS       WP_284499454             255 aa            linear   BCT 25-DEC-2024
DEFINITION  MBOAT family O-acyltransferase, partial [Escherichia coli].
ACCESSION   WP_284499454
VERSION     WP_284499454.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Hofmann,K.
  TITLE     A superfamily of membrane-bound O-acyltransferases with
            implications for wnt signaling
  JOURNAL   Trends Biochem Sci 25 (3), 111-112 (2000)
   PUBMED   10694878
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004295
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>255
                     /product="MBOAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
     Region          <1..225
                     /region_name="DltB"
                     /note="D-alanyl-lipoteichoic acid acyltransferase DltB,
                     MBOAT superfamily [Cell wall/membrane/envelope
                     biogenesis]; COG1696"
                     /db_xref="CDD:441302"
ORIGIN      
        1 sgpitnydvi tnqlnsrdny fgkyfvpavf ifsvgifkkv vlssyfgsia dqgyanisal
       61 galeawitsl sysiqlyfdf sgytdmaigs allfgvvlpi nfnspyiatd lqdfwrrwhi
      121 tlstwlrnyv yiplggnrng vlrtylnlfl tfliggfwhg agwnflawga lhgaglvihr
      181 ywsqngfrmp svvgwfitfn yvnitwiffr tdnlndafsl lkkmfagyds lvsgfkyaqp
      241 fadsflyeas kggfy
//
LOCUS       WP_284499496             196 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase [Lysobacter enzymogenes].
ACCESSION   WP_284499496
VERSION     WP_284499496.1
KEYWORDS    RefSeq.
SOURCE      Lysobacter enzymogenes
  ORGANISM  Lysobacter enzymogenes
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Lysobacter.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Lysobacter enzymogenes"
                     /db_xref="taxon:69"
     Protein         1..196
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=20573
     Region          <59..160
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mkvfrllkka vvlslirlgw fikpglvtrl yawflrsega qieerpnyls akiwfdgtdy
       61 slirlgkgct issnvrilth dwaihtvake lglkfdrpqg rikpisigrh afigtgsiim
      121 pgadigagci vgagavvrga ipplsivvgn pgqvvgsvae yveratrgag vgpaeqaalk
      181 qaalahaaal agarag
//
LOCUS       WP_284499862             356 aa            linear   BCT 25-DEC-2024
DEFINITION  transketolase family protein, partial [Escherichia coli].
ACCESSION   WP_284499862
VERSION     WP_284499862.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Schenk,G., Duggleby,R.G. and Nixon,P.F.
  TITLE     Properties and functions of the thiamin diphosphate dependent
            enzyme transketolase
  JOURNAL   Int J Biochem Cell Biol 30 (12), 1297-1318 (1998)
   PUBMED   9924800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>356
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016744 - transketolase or transaldolase
                     activity [Evidence IEA]"
     Region          1..>356
                     /region_name="TktA"
                     /note="Transketolase [Carbohydrate transport and
                     metabolism]; COG0021"
                     /db_xref="CDD:439792"
ORIGIN      
        1 mssrkelana iralsmdavq kaksghpgap mgmadiaevl wrdflkhnpq npswadrdrf
       61 vlsnghgsml iysllhltgy dlpmeelknf rqlhsktpgh pevgytagve tttgplgqgi
      121 anavgmaiae ktlaaqfnrp ghdivdhyty afmgdgcmme gishevcsla gtlklgklia
      181 fyddngisid ghvegwftdd tamrfeaygw hvirdidghd aasikravee aravtdkpsl
      241 lmcktiigfg spnkagthds hgaplgdaei altreqlgwk yapfeipsei yaqwdakeag
      301 qakesawnek faayakaypq eaaeftrrmk gempsdfdak akefiaklqa npakia
//
LOCUS       WP_284501779             228 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein, partial
            [Actinotalea sp. C106].
ACCESSION   WP_284501779
VERSION     WP_284501779.1
KEYWORDS    RefSeq.
SOURCE      Actinotalea sp. C106
  ORGANISM  Actinotalea sp. C106
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Cellulomonadaceae; Actinotalea.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Actinotalea sp. C106"
                     /db_xref="taxon:2908644"
     Protein         1..>228
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
     Region          64..>226
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mtpgrtqvdv griphpfdap gvfgflaara vtgvevadls edrlryartl alphgpaaid
       61 vvaswtpgpg wqvqvrlels spedrgaala qvrrlldldt dpsavdaals edpvlaplvt
      121 rtpgirvpga vdphellvra lvgqqisvaa arthlgrlaa rvgsphvsrv tgldrlfpsa
      181 aqisaavpap vpgepldpdr plrlpgqavr slvatcgala dgtldlgg
//
LOCUS       WP_284501828              88 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein, partial [Actinotalea sp. C106].
ACCESSION   WP_284501828
VERSION     WP_284501828.1
KEYWORDS    RefSeq.
SOURCE      Actinotalea sp. C106
  ORGANISM  Actinotalea sp. C106
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Cellulomonadaceae; Actinotalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Actinotalea sp. C106"
                     /db_xref="taxon:2908644"
     Protein         <1..88
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
     Region          <1..77
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 gelhergvya vsrhpiytgl lvatagwavl rrrpepvvaw lallavldak trreeqrlva
       61 rfgdryvayr artprllalp grtaarrp
//
LOCUS       WP_284502800             808 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Caballeronia sp. AZ10_KS36].
ACCESSION   WP_284502800
VERSION     WP_284502800.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. AZ10_KS36
  ORGANISM  Caballeronia sp. AZ10_KS36
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 808)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 808)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20158983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..808
                     /organism="Caballeronia sp. AZ10_KS36"
                     /db_xref="taxon:2921757"
     Protein         1..808
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=88254
     Region          130..>394
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          307..774
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mksfvvrllv ttvaltavll lvmlalasan teffdryygw lyaanvaval ifmlivislt
       61 liivsrvrqg rfgtrllakl alifalvgvl pgaiiyvvsy qfvsrsiesw fdvnvetalt
      121 sgltlgrgml etsladfknr srqmsdqlas adpssltltl lrlrdqfgvq davvferprd
      181 qynredlnag gplqrvaalr tiaqasgnyy sllptnepts amlkeaqdrp fgaiegeidg
      241 dpksngpkga lrlrvitkip dpttttefqh vdrflqieqp vsqelarnad avqrayreyq
      301 ekrlgrtglr kmyigtltla lflatfiamm lalalgnqla rplfllaqgt kevaegdytp
      361 kreinsrdel gfltqsfnam trqlsearaa vennrialeh skaylesila nltagvfvfd
      421 rqfrlttanr gaerifrqpf ralqghsldq idvlaefgam vkkafaerda aaigsghptg
      481 drghwqqqva vtvpgendpl tllvrgtqll satesdteda ettgyvvvfd disdvisaqr
      541 svawgevarr laheiknplt piqlsaerlq mkladklapq daevlkrast tivnqvqamk
      601 hmvddfreya rtppavlgnl qlndlvgevl alygieegks pikvdlaklp virgdatqir
      661 qvihnllqna qdavadvpep rvlletrtve ygepdasgha rvavrlsvsd ngagfparil
      721 srafepyvtt kakgtglgla tvkkivdehg aridirnrsk tgdvvegaqi silflqladd
      781 taadgaapst paaakhgttk atvqtraa
//
LOCUS       WP_284504221             444 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [unclassified
            Caballeronia].
ACCESSION   WP_284504221
VERSION     WP_284504221.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..444
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=50161
     Region          33..425
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mqtlhdvvvr qpdvtllfpv qhsnaversa rrpltdvaik nakprdksyr mhdtgglyle
       61 lfpngsklwr wkyrfegrek rlafgkypev glkdarekrd darkllrtgv dpsgnkqlle
      121 aakqfqaast feavandwya rmmsdkaesh rvkvkarlek dlfpwlgqka itdikapdil
      181 eclrriegrg ardtahralq ncsavlsyav asgkaqenpa vhlkgalppa rpghfaaite
      241 pesvgpllrr mdavsatfpv kcalrllpyl fcrpgelrtm rweevhldaa ewryvtsknr
      301 lphivplpaq availrelqp ltgrgefvfp grddrtqpms natlnralqr agistreeqt
      361 ghgframart ilheglrfap eviehqlahr vpdalgyayn rtrflddrkr mmqqwadyld
      421 rlrdgvepga aaepglpigp regr
//
LOCUS       WP_284504446             335 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Caballeronia sp.
            ATUFL_F1_KS4A].
ACCESSION   WP_284504446
VERSION     WP_284504446.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. ATUFL_F1_KS4A
  ORGANISM  Caballeronia sp. ATUFL_F1_KS4A
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Caballeronia sp. ATUFL_F1_KS4A"
                     /db_xref="taxon:2921768"
     Protein         1..335
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35983
     Region          1..328
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mdmfqlsrar dmrdainaga lahtaqqgae vrflaggttl ldlmklnver pmrvvdisrl
       61 pldkieetkd ggvrigatsr nsdlahhpli rdryavlsqa vlagasvqlr nmattggnil
      121 qrtrcvyfrd ttspcnkrep gsgcsaiqgf nrmmaimgts esciasnpsd mcvalqalea
      181 tihvegtggk raipideffl lpgttpdren vldagdlvth vtlpppadga rsaylklrdr
      241 asyefalasa gvvigvkdgr ieharvalgg vgtkpwrsre aekelmnatp deatfkraad
      301 aaladakpqs engfkvelsk rcivhtlklv ttqts
//
LOCUS       WP_284505291             110 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: thioredoxin family protein [Streptomyces].
ACCESSION   WP_284505291
VERSION     WP_284505291.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..110
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11960
     Region          9..110
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 mikaagvsev rdadfgtevl radlpvlvef tadwcppcrq mgpvlsdlas eqegrlkvvq
       61 ldvdtnpgtt naykvlsmpt flvfrdgepv kamvgarsrr rlleeladvl
//
LOCUS       WP_284506731             103 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Caballeronia sp. GAWG1-5s-s].
ACCESSION   WP_284506731
VERSION     WP_284506731.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. GAWG1-5s-s
  ORGANISM  Caballeronia sp. GAWG1-5s-s
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Caballeronia sp. GAWG1-5s-s"
                     /db_xref="taxon:2921743"
     Protein         1..>103
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          1..>96
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mlshelrnpl apiesaievi rrsvpeqspa aaasnivkrq vrnlsvilnd lleadrtvrg
       61 mfsidpvpve msaiideavd airpaaaqng qtvtidgldr sat
//
LOCUS       WP_284506965             334 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Caballeronia sp. GAFFF1].
ACCESSION   WP_284506965
VERSION     WP_284506965.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. GAFFF1
  ORGANISM  Caballeronia sp. GAFFF1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Caballeronia sp. GAFFF1"
                     /db_xref="taxon:2921779"
     Protein         1..334
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35395
     Region          1..332
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 memfqlsrar dlpdaihtga tahtaqqgae vrflaggttl idlmklnveq parivdisrl
       61 pldkieatdd ggvrigatsr nsdlahhpli rerytvlsqa vlsgasvqlr nmattggnll
      121 qrtrcvyfrd taspcnkrep gtgcaaiggf nrtqailgts eaciasnpsd mnvalaalea
      181 tvhvegargq raiafddfhl lpgstpdret vlepgdlith vtlpppvagt rslylklrdr
      241 asyefalasa aivigvsdgr iahvrvglgg vatkpwrare aenellnaap deaafrraad
      301 aaladakpqs gnafkvelak rcivhalkla tqas
//
LOCUS       WP_284507061             807 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Caballeronia sp. ATUFL_M2_KS44].
ACCESSION   WP_284507061
VERSION     WP_284507061.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. ATUFL_M2_KS44
  ORGANISM  Caballeronia sp. ATUFL_M2_KS44
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 807)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 807)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20158983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Caballeronia sp. ATUFL_M2_KS44"
                     /db_xref="taxon:2921767"
     Protein         1..807
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=87799
     Region          134..>394
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          307..781
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mksfvvrllv ttvaitaavl lvmlalasan teffdryygw lyaanvavai vfmlivislt
       61 liivsrvrqg rfgtrllakl alifalvgvl pgaiiyvvsy qfvsrsiesw fdvnvetalt
      121 sgltlgrgml etsladfknr grqmsdqlas adpssltltl lrlrdqygvq davvferprd
      181 qynredlnag ggslrvpglr tvaqasgniy allptnepss amlkaaqdrp fgaiegeidg
      241 dpaskgpkga lrlrvitkip dpttttefqh vdrflqieqp vsqelarnad avqrayreyq
      301 ekrlgrtglr kmyigtltla lflatfiamm lalalgnqla rplfllaqgt kevaegdytp
      361 kreinsrdel gfltqsfnam trqlsearaa vennrialeh skaylesila nltagvfvfd
      421 rqfrlttanr gaarifrqpf dalvnqplds idvlaefgam vkkafaerda aavgsghpag
      481 drghwqqqva vtvpgendpl tllvrgtqll tgvesdtedt ettgyvvvfd disdvisaqr
      541 svawgevarr laheiknplt piqlsaerlq mkladklapq dadvlkrast tivnqvqamk
      601 rmvddfreya rtppavlanl qlndlvgevl tlygieegks pikvdlaklp virgdatqir
      661 qvihnllqna qdavaevaep rvlletrtve ygepdasgha rvavrltvsd ngagfparil
      721 srafepyvtt kakgtglgla tvkkivdehg aridirnrsr tadvvegaqi silflqlaed
      781 aadgatpsaa paakhgttka tvqtraa
//
LOCUS       WP_284507409             687 aa            linear   BCT 25-DEC-2024
DEFINITION  PAS domain-containing hybrid sensor histidine kinase/response
            regulator [Caballeronia sp. ATUFL_M2_KS44].
ACCESSION   WP_284507409
VERSION     WP_284507409.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. ATUFL_M2_KS44
  ORGANISM  Caballeronia sp. ATUFL_M2_KS44
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13751984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Caballeronia sp. ATUFL_M2_KS44"
                     /db_xref="taxon:2921767"
     Protein         1..687
                     /product="PAS domain-containing hybrid sensor histidine
                     kinase/response regulator"
                     /calculated_mol_wt=74470
     Region          171..257
                     /region_name="PAS_3"
                     /note="PAS fold; pfam08447"
                     /db_xref="CDD:430001"
     Site            order(174,178,184,198..201,227,232)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(195,199,207,210..211,239,241)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          <297..682
                     /region_name="PRK13557"
                     /note="histidine kinase; Provisional"
                     /db_xref="CDD:237425"
ORIGIN      
        1 mpeidpcptl ilapsgrdas iaaamltelk vlsqicrnve hlsslvsdrt ccvvateeal
       61 vdadlhrlst wintqpawsd lpfvvltrra svadrapavr lvktlgnvtl ierpfhpatf
      121 asvvgtairg rnrqfdartr ieqvhegear lqtaltagql gswdldlstg vlttsatcka
      181 ifgypadsaf tyqtllasih pddrdrmqat vkssvetgcd yiieyrnvwp drtihwvdir
      241 arvlsdeigr ayrlvgvssd vtarktaeeg mrqanealem kvtqrtaell qthqkvldei
      301 rqreqteell rhiqkletlg qlsggiahdf nnllmaiian lelarkevpq esrlmklidg
      361 afggarrgaa ltqrllafar qqelkvepva mssliagmsd lvqrsigssi elvirsdsts
      421 pqtmvdanqv elavlnlvin ardampnggt lsisvdtaea sgalelhagq yvrvtvsdtg
      481 tgmdpatlar atepffttke vgkgtglgls mvhglalqlg gslrlesspg rgthaslllp
      541 vseaqtshal ppvtlparqs evidplhera cvlvvdddpl iasstaflle dlghevvevh
      601 sgvaaldvlh ngkhidlilt dysmprmtgl elahaarglr pslpvviatg yaelpegadh
      661 tiprirkpyl qeqliaeirk alhprst
//
LOCUS       WP_284508340             335 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FAD binding domain-containing protein [unclassified
            Caballeronia].
ACCESSION   WP_284508340
VERSION     WP_284508340.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..335
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=36039
     Region          1..328
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mdmfqlsrar dmrdainaga lahtaqqgae vrflaggttl ldlmklnver pmrvvdisrl
       61 pldkieetkd ggvrigatsr nsdlahhpli rdryavlsqa vlagasvqlr nmattggnil
      121 qrtrcvyfrd ttspcnkrep gsgcsaiqgf nrmmaimgts esciasnpsd mcvalqvlea
      181 tihvegtggk raipideffl lpgttpdren vldagdlvth vtlpppvdga rsaylklrdr
      241 asyefalasa gvvigvkdgr ieharvalgg vgtkpwrsre aekelmnatp deatfkraad
      301 aaladakpqs engfkvelsk rcivhtlklv ttqts
//
LOCUS       WP_284509021             989 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: putative bifunctional diguanylate
            cyclase/phosphodiesterase [Caballeronia].
ACCESSION   WP_284509021
VERSION     WP_284509021.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 989)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 989)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 989)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 989)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..989
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..989
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=108939
     Region          276..940
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 masvipasls rfrrtgswid dalyavavya vpilillgti atlyflprqy etrgavplal
       61 hvvadksanm tpadalealq gaapvsryst rlsekpvwfs fttpsmsads stvvelpsrh
      121 aqtlacwnak tlaplgqadr egvtgemrvv kagfsiqvgr ikqaenvlcr gtfsgpaqin
      181 ayawewqglr nsaldfqess gliagglltl avfvfvtali nhewtyvifa vwlvgnlrlc
      241 anamgwdmqw lgrvlpadfm qplrqftfaa yylltaalfq qlfrrelrvv gyrwllrviq
      301 yvgivllaaa falpyalfip tlwiiagfgi cvllfflarl vwmarsrtvl wyvaslgvvl
      361 fstfsevlga afglkvlvgg vntvmaalss smmaafaiae qmraerdfrr qaqmelrnty
      421 evtpiglftl dadghfvran palramldlq ktdykvrhwn dyfeagawga lqalaskgsd
      481 gelemggspe rgtgerryll kairsngwie gslqdtters kaverlrfla ehdsltgsln
      541 rrgvekaisa qseetlpwal ayvdldrfkl vndlfghrsg devlrqvaar trahfarsyp
      601 vgriggdefv cvmhdtsied aiaqcrelis ilsdapyqvg nrafqvkasi glvecsqgvr
      661 vqdalshadr acreakkvah thlvtyrkga aafeeraeel klvetlgrnr lppglflvmq
      721 pimslsapte slnfevllrm rapdgatlpa gkvivaaees gniaaidrwv istlldwiev
      781 hqqqlgntqf icvnlsggsl ndeqfmedif alfaahqsiv hylcleites valhdlentq
      841 rfiarvhdmg gkialddfga gytsfkylka lsadalkidg efvrsmcahp adiaiveaiv
      901 alarnlgmrs vaewvedvdt lralqeigvd yvqgflvarp qdssailaas saasfvkdpe
      961 visfveglse pvqatvfdye wharasgth
//
LOCUS       WP_284509624             341 aa            linear   BCT 25-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Salinivibrio costicola].
ACCESSION   WP_284509624
VERSION     WP_284509624.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio costicola
  ORGANISM  Salinivibrio costicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Salinivibrio costicola"
                     /db_xref="taxon:51367"
     Protein         1..341
                     /product="metal-dependent hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36376
     Region          31..>94
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
     Region          76..>309
                     /region_name="Met_dep_hydrolase_A"
                     /note="Metallo-dependent hydrolases, subgroup A is part of
                     the superfamily of metallo-dependent hydrolases, a large
                     group of proteins that show conservation in their
                     3-dimensional fold (TIM barrel) and in details of their
                     active site. The vast majority of the...; cd01299"
                     /db_xref="CDD:238624"
     Site            order(92,94,269,289)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mvglmrylav asllvvtsvm aqseppkshv lfenvrifdg ksaqlsapah vlvegnkitq
       61 ishepinvtp ssntkvikga grtlmpglid ahwhamlatv svpqlltadt gyinlraghe
      121 aertlmrgft svrdlsgpvf glkqaidegi vagpriwpsg amisqtgghg yvasiilagf
      181 rmryevpaan naglsrgeat nggviadgva evrkrvreql mlgasqikla agggvasayd
      241 pidvaqysee efraavdaae nwgtyvtvha ytpkaiqtai kggvkvidhg qlmdeetaql
      301 maekgvwlsg qaflaneysn pvqgeakvkq qqsckrhrqr l
//
LOCUS       WP_284509728             196 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Salinivibrio costicola].
ACCESSION   WP_284509728
VERSION     WP_284509728.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio costicola
  ORGANISM  Salinivibrio costicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Salinivibrio costicola"
                     /db_xref="taxon:51367"
     Protein         1..196
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=22142
     Region          33..>196
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mkcdlmtnwv rrltivwltm lsfqvwsats dplnvcvgdg spwppytywq getrqqkadt
       61 ltgyatdlvl salesndity qlvfmpwarv qhelaresgr cdltwdasyk peraqysrlt
      121 tplysislgy lyigdpaanv rprlpvsdsv cgvngynyag fgdnpkprfe antlqqalrm
      181 leagrcrfla sdeysl
//
LOCUS       WP_284509780             304 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Salinivibrio costicola].
ACCESSION   WP_284509780
VERSION     WP_284509780.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio costicola
  ORGANISM  Salinivibrio costicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Salinivibrio costicola"
                     /db_xref="taxon:51367"
     Protein         1..304
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=32757
     Region          <3..301
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 malellpaga hiiamcgvyg gthrlfdklr arnnglsvdy vdlndldava aavkpstamv
       61 wietptnpll elvdiaaicq farehalltc vdntfatawn qtplslgadi vmlstskyig
      121 ghsdmiggal vtadetlakk idfakttvga iaspfdayla lrglktldlr mqrqcdnaln
      181 vatalenhpa ieavfypglp shpqhalcqt qmrsggavvt iqlkgtrves erflsrlryf
      241 ilaeslggve sminhsasms hgsmseeere amgvfdttfr lsvgiedsrd liddllyald
      301 qeas
//
LOCUS       WP_284509967             136 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Mycoplasmopsis cynos].
ACCESSION   WP_284509967
VERSION     WP_284509967.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis cynos (Mycoplasma cynos)
  ORGANISM  Mycoplasmopsis cynos
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13031057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Mycoplasmopsis cynos"
                     /db_xref="taxon:171284"
     Protein         1..136
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=15516
     Region          12..126
                     /region_name="SpoU-like_rRNA-MTase"
                     /note="SAM-dependent rRNA methylase related to SpoU-TrmH;
                     cd18095"
                     /db_xref="CDD:349968"
     Site            order(65,67,88..91,94,108..109,111,115..116,118,121)
                     /site_type="other"
                     /note="SAM binding site [chemical binding]"
                     /db_xref="CDD:349968"
ORIGIN      
        1 mleqllelqk yfnfdtviie nldvfndkvi rasqgalfkl niietndles eliklknnsy
       61 tiyetllnkn tqvlnsikfv edkmvivfgn eangirpniq klsdlniyip iefeslnvai
      121 sagivldkvy nrskde
//
LOCUS       WP_284512082             180 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Bacteroides sp. D20].
ACCESSION   WP_284512082
VERSION     WP_284512082.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. D20
  ORGANISM  Bacteroides sp. D20
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Bacteroides sp. D20"
                     /db_xref="taxon:585543"
     Protein         1..180
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21004
     Region          <80..179
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mekkrkeyea eqmqqnikmr eqehlitlqq qqlleaelsa kskdlasmal gvfaknevle
       61 klraavqefl vkgqygrknl esllklinen ietqefwdvf qnnfdlihek ffrnlreryp
      121 sltatdlrfc allrlnlstk diaqmtnlti rgveaaryrl rkkldipdgt glvdflidlk
//
LOCUS       WP_284512137             234 aa            linear   BCT 25-DEC-2024
DEFINITION  aldo/keto reductase family protein [Bacteroides sp. D20].
ACCESSION   WP_284512137
VERSION     WP_284512137.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. D20
  ORGANISM  Bacteroides sp. D20
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Bacteroides sp. D20"
                     /db_xref="taxon:585543"
     Protein         1..234
                     /product="aldo/keto reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27192
     Region          14..>226
                     /region_name="AKR_AKR1-5-like"
                     /note="AKR1/2/3/4/5 family of aldo-keto reductase (AKR)
                     and similar proteins; cd19071"
                     /db_xref="CDD:381297"
     Site            order(45,50,75,124)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381297"
ORIGIN      
        1 mdmqyiklnn giempqiglg tflipkdkle dtlikaydmg yrqfdtawry yneadiarif
       61 kkhgikredv fittkvnida lycggykygi hrilnrrnnv sieqavqksf dnldteyidl
      121 flihnpwkif mdmwkvlekf ykegriraig vsnflqphie alseisdvvp avnqieispl
      181 naqielikyc qdrgiavesm stfshfrsve prleiiehpl ilaiaknmvr apfk
//
LOCUS       WP_284512492             364 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Shigella flexneri].
ACCESSION   WP_284512492
VERSION     WP_284512492.1
KEYWORDS    RefSeq.
SOURCE      Shigella flexneri
  ORGANISM  Shigella flexneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Shigella flexneri"
                     /db_xref="taxon:623"
     Protein         1..364
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41385
     Region          17..359
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mavklfdeis piqlvdhgrn nqidgmrgfl aifvlihhaa iwhgylltgv wktpssnllt
       61 nlgqvgvsff fmitgylffs kirssdqdwv rlyisrflrl tpmfivslcl vllvigfksr
      121 wsvhvspasl tvslmrwapf talgmpning vkdsftinaa vtwtlvyewf fyfslpviaa
      181 lfkrrvsihm iiisvlvlvi flcypskkih visflfglla sysnnyvhrv akakitpimi
      241 iallsyemiy fpttyaplpl iicgvcfili asgcdfygil rlnltrklge ttysiyllhg
      301 vflycvmtwv ipsnysnyff imlisitafc vtllscitfk lielpfinit kqtamkirgi
      361 iknt
//
LOCUS       WP_284512849             764 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Rothia mucilaginosa].
ACCESSION   WP_284512849
VERSION     WP_284512849.1
KEYWORDS    RefSeq.
SOURCE      Rothia mucilaginosa
  ORGANISM  Rothia mucilaginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Rothia.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Rothia mucilaginosa"
                     /db_xref="taxon:43675"
     Protein         1..764
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=83436
     Region          23..764
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 msseslpqqs adssaaeklf aeqmaaerey varvyarlde lreetaekla avrknqavgg
       61 hqnrserdsf athyedrlaq lnavdsrltf grldmdrega davryigrig itdsnqqrll
      121 mdwrapeagt fyqatafhpm gvrrrrhlml egrtvvnied evfdsemlqd edtlhgegal
      181 laalnkkrtg rmgdivatiq aeqdaiirse lpgvrvvqgg pgtgktaval hraayllytn
      241 rerlskagvl vvgpsnsfmw yiervlpslg etgvvmasla tlypglravp endravaalk
      301 gdlrmvqvik ravanrqkvp aqvqrlnveg tdveltpemv rsarsrarst gkphnearet
      361 fvkillkelt aklddqlnra agrvverpyl qddvrasmdv rralnlawmp lspetllrsl
      421 fskphylesa trelskaere llarpadapf teadvpllde aaellgdfsk vtgaaaaara
      481 aaehranlen aakalenvhq sledigadgv itpeqiammn evrgermtaa aaasadrtwa
      541 yghivvdeaq elspmqwrll mrrcpmksft ivgdiaqass aaaasswsqa lepfvgerft
      601 leeltinyrt paqiaeaavs vaqaagyevs apravregqw pplvhevaae svveqtvavv
      661 seevahsgga ligvvcppsl yvqtaqavar ahadrtgtaq talenqvlvl tpweakglef
      721 dvvvivepqq liddadgavg dlyvsmtrpt qrlhmvgsrm pegl
//
LOCUS       WP_284513671             200 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Rothia mucilaginosa].
ACCESSION   WP_284513671
VERSION     WP_284513671.1
KEYWORDS    RefSeq.
SOURCE      Rothia mucilaginosa
  ORGANISM  Rothia mucilaginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Rothia.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Rothia mucilaginosa"
                     /db_xref="taxon:43675"
     Protein         1..200
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=20669
     Region          2..200
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mniaiigatg mvgartsaea isrghrvday trsgkapegt tahsidladt aalvnivnnh
       61 dvtivavpgg rgtsaqpiid ahraliaaap tgrllvlgga gsledgngnr fvdgegfped
      121 ykpeakafaq ildeyraseg lnwtmlspaf eiapgertgk yntaldtpag gfvsaedfav
      181 alideaeepk hagrrftvan
//
LOCUS       WP_284515488             196 aa            linear   BCT 25-DEC-2024
DEFINITION  STN domain-containing protein [Bacteroides sp. AM54-2NS].
ACCESSION   WP_284515488
VERSION     WP_284515488.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM54-2NS
  ORGANISM  Bacteroides sp. AM54-2NS
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10541884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Bacteroides sp. AM54-2NS"
                     /db_xref="taxon:2292955"
     Protein         1..196
                     /product="STN domain-containing protein"
                     /calculated_mol_wt=22254
     Region          69..119
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     pfam07660"
                     /db_xref="CDD:429580"
     Region          130..>193
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mriliiimll cttlvpnyly aishenysee sflfvgedym qenykvtlhl sgvsvstlfn
       61 eiqkqtkldf vyntelleti tpisvtaeke svfdvlnrlf ngtgfifkks gniitvnkke
      121 elqqddkflv tgevkddtge plvgvtiqqk dtrnititdm dgrysiqvss kaeafltfsf
      181 vgmktktvpl reeylm
//
LOCUS       WP_284515535             301 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Bacteroides sp.
            AM54-2NS].
ACCESSION   WP_284515535
VERSION     WP_284515535.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM54-2NS
  ORGANISM  Bacteroides sp. AM54-2NS
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Bacteroides sp. AM54-2NS"
                     /db_xref="taxon:2292955"
     Protein         1..301
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34603
     Region          <213..301
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mlranpcndg keivmitsgi qsfalshgeq ykhgrtslrd lsgklpfvan gctmllcveg
       61 ravvttntrk rtfrkgdllv lfsdtlfapl cvspsftaey islsleltge ifykmtspaf
      121 wdglyeypvc rlseaqysla dgvfkqmiwa mengdeesrk nilqnciynv flaldivfkp
      181 mfpdlgkcyq kdqsrvlfgk fmsllaknfh vkrdvryyad rlcittdyly kitckieqrt
      241 pkeiidlfvv telkryldnt eqsvkdlarl fhfedasylc rffrrtagcs vseyrnrlgr
      301 s
//
LOCUS       WP_284515541            1000 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM54-2NS].
ACCESSION   WP_284515541
VERSION     WP_284515541.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM54-2NS
  ORGANISM  Bacteroides sp. AM54-2NS
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1000)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1000)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1000)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1000)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1000
                     /organism="Bacteroides sp. AM54-2NS"
                     /db_xref="taxon:2292955"
     Protein         1..1000
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=110718
     Region          16..999
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mffflftpfv ysqsrkqitg svqdvqgnpl igvsiletgt sngtitdmng tyslnisstn
       61 atlrfsyigy eeqlikiqgr nvinvkmnee tsnldevvvv gygvqrksdl tgaissinaa
      121 etlkkmpaaq vadllqgria glsivnssga agavptlrvr gvnsikadgg plvvidgfpg
      181 gnlsainpad iksievlkda sstaiygsrg angvilittk spkegklsvd yngyvvagtp
      241 adkpsimpvn efarmandwn qayygkdlyt erqitnftng ydtydymgni indyaishsh
      301 disikggndk msflfstqyi hnkgiaghst ndrwnyrlkv danitkklkf ganfygmins
      361 aagnnfsgqy slltlaqqfp qtvlpydkeg nltqgtidnt giynpigfid eqkrnnnedm
      421 tfnnwlqayi syeiipgltf rneqqinign rfygttsskq smngflkgks latyydansw
      481 gwrmtntlny tkelnknnri natigveesl srsyimrqta egltsesigw knmmlaetsk
      541 lednevsktt aisyfgriny vlmnrymatv tfrrdgssll sydhrwdnfp sfslawnlke
      601 esflkninsl dqlklrygyg vsgnqavaay saytqydati gngqiaytlv pgnpilkwek
      661 thqhnygvda aflngrisft fdyydkktkd aintvvlpad tglssglrna aeisnkgfei
      721 tlgitpitak dfywkadisl ahnkakiekl gdidsdfmei gtgwgnsfyr yfvgepigai
      781 yglqstgvws teeynnpdik kptsptvrpg sykyvdqnds gtidaddyvi igngqpkfnw
      841 gmnnsftykn fdlnifligf hgfdiynypr arltsslspf pelaerwiag knenaiiagf
      901 gkdrdaitsp etvasstfve kgdfvklksi tlgynfskgl lskinlsaar vyfsiknvct
      961 itkysgndpe lsisnplrpg ldmgtypsqr eyllglnvsf
//
LOCUS       WP_284518577             108 aa            linear   BCT 25-DEC-2024
DEFINITION  thioredoxin family protein [Mycoplasmopsis cynos].
ACCESSION   WP_284518577
VERSION     WP_284518577.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis cynos (Mycoplasma cynos)
  ORGANISM  Mycoplasmopsis cynos
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Mycoplasmopsis cynos"
                     /db_xref="taxon:171284"
     Protein         1..108
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=12393
     Region          7..107
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 mrkevnmlre inaqeaknei ktgkkllvfh alycalrkmy kstleeladk ngveilrvni
       61 eenkefates gvraipytqv yqdgsmikdl vgyrtyddll seldsflk
//
LOCUS       WP_284519297             774 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-N-acetylhexosaminidase family protein [Mycoplasmopsis cynos].
ACCESSION   WP_284519297
VERSION     WP_284519297.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis cynos (Mycoplasma cynos)
  ORGANISM  Mycoplasmopsis cynos
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 774)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 774)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 774)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 774)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 774)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Mycoplasmopsis cynos"
                     /db_xref="taxon:171284"
     Protein         1..774
                     /product="beta-N-acetylhexosaminidase family protein"
                     /calculated_mol_wt=89160
     Region          40..183
                     /region_name="Glyco_hydro_20b"
                     /note="Glycosyl hydrolase family 20, domain 2; cl03741"
                     /db_xref="CDD:446174"
     Region          189..478
                     /region_name="NAGidase"
                     /note="beta-N-acetylglucosaminidase; pfam07555"
                     /db_xref="CDD:429533"
ORIGIN      
        1 msikktlkai islasasglv amlssnntat srqvvtnhke ykiypsvhsi eyynkhflit
       61 peinlvvedg idsavlerfe etlnlrkiky kisnkiisgk tnvliglkdn kdtfvddylk
      121 sknlmldtnl mnkidsyvln skdnvisiya sgedasyygv tslwhifnql ngleieefni
      181 ndyadiktrg aiegyygnpw slqdrinymr wgsyyklngy fyapkddpkh shkwrelyte
      241 seienlikpl aregnrtkvr yiytlhpffg trldndydqg vkdlknkflq viqagvrqig
      301 iladdvarnd igtqvrllid mvtwlkelkq tkyhdlkvvl pfvvneyagy gqsyfkrfpn
      361 evqivmtggk twgevspeft nkfysntnrg sllwinwpcs dnsknhlilg gyreflhknv
      421 dpkkvqgivl npmqqsepsk valfgaadyt wniwkddahi dqtysdafny vtnnsyqeta
      481 eskafrnlak hminqnmdgr vvaleesiel kkklakvrts letnnllvdn ikdlkvefee
      541 lyndaltikn svvnrdlyyq irywiessie lyqgltltlm eliklsqgdk tdfvlnlnka
      601 ktliqkartq htvdylgsiq yaevgvqhiq pfttwlldym snkilntnik nnnnkkdqvv
      661 gynleiakhs sindnaknnk ldyiidhnds tlawlssann gnvgkdqgie ihfesakeik
      721 sirilqdsnd kmeslkiqkl ynnqvidlen gtldfkdkke itytvpenvl ndwn
//
LOCUS       WP_284519673             143 aa            linear   BCT 25-DEC-2024
DEFINITION  DHH family phosphoesterase [Mycoplasmopsis cynos].
ACCESSION   WP_284519673
VERSION     WP_284519673.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis cynos (Mycoplasma cynos)
  ORGANISM  Mycoplasmopsis cynos
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Mycoplasmopsis cynos"
                     /db_xref="taxon:171284"
     Protein         1..143
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=16635
     Region          11..>133
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mqignlelvt kelikydsiv ifhhirpdgd clgsqfglre llrtnfpnkk iyvigdnknm
       61 fsfldfkmdd iptdeilkks lgvivdanfk eriehrfvld keifakliri dhhpndddlg
      121 dnttrwvdss ysawwndyrn sgc
//
LOCUS       WP_284520104             606 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-N-acetylhexosaminidase family protein [Mycoplasmopsis cynos].
ACCESSION   WP_284520104
VERSION     WP_284520104.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis cynos (Mycoplasma cynos)
  ORGANISM  Mycoplasmopsis cynos
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 606)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 606)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Mycoplasmopsis cynos"
                     /db_xref="taxon:171284"
     Protein         1..606
                     /product="beta-N-acetylhexosaminidase family protein"
                     /calculated_mol_wt=69969
     Region          40..183
                     /region_name="Glyco_hydro_20b"
                     /note="Glycosyl hydrolase family 20, domain 2; cl03741"
                     /db_xref="CDD:446174"
     Region          189..478
                     /region_name="NAGidase"
                     /note="beta-N-acetylglucosaminidase; pfam07555"
                     /db_xref="CDD:429533"
ORIGIN      
        1 msikktlkai islasasglv amlssnnpat srqvvtnhke ykiypsvhsi eyynkhflit
       61 peinlvvedg idsavlerfe etlnlrkiky kisnkiisgk tnvliglkdn kdtfvddylk
      121 sknlmpdtnl mnkidsyvln skdnvisiya sgedasyygv tslwhifnql ngleieefni
      181 ndyadiktrg aiegyygnpw slqdrlnymr wgsyyklngy fyapkddpkh shkwrelyte
      241 seienlikpl aregnrtkvr yiytlhpffg trldndydqg vkdlknkflq viqagvrqig
      301 iladdvarnd iriqerllid mvtwlkelkq tkyhdlkvvl pfvvneyagy gqsyfkrfpn
      361 evqivmtggk twgevspeft nkfysntnrg pllwinwpcs dnsknhlilg gyreflhknv
      421 dpkkvqgivl npmqqsepsk valfgaadyt wniwkddahi dqtysdafny vtnnsyqeta
      481 eskafrnlak hminqnmdgr vvaleesiel kkklakvras letnnllvdn ikdlkvefee
      541 lyndaltikn svvnrdlyyq irywiessie lyqgltlfld gliklsqgdk tdfvlnlnka
      601 ktliqk
//
LOCUS       WP_284521366             179 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Cytobacillus
            pseudoceanisediminis].
ACCESSION   WP_284521366
VERSION     WP_284521366.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus pseudoceanisediminis
  ORGANISM  Cytobacillus pseudoceanisediminis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Cytobacillus.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Cytobacillus pseudoceanisediminis"
                     /db_xref="taxon:3051614"
     Protein         1..179
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20560
     Region          <8..177
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mkycetsivf tksnqiiall vngrkrydqs laddiqrkvs raviglgrev altdmtdtyq
       61 eavealsfak nhqhktcity selgaerlwl ntdrsllnkf vsdkigsllk mepeylktmq
      121 aflannqshk qtaeemhihp ntlayrlkki eselqldfsr kedwitvvla fqvfdflnp
//
LOCUS       WP_284520879            1502 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-N-acetylhexosaminidase family protein [Mycoplasmopsis cynos].
ACCESSION   WP_284520879
VERSION     WP_284520879.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis cynos (Mycoplasma cynos)
  ORGANISM  Mycoplasmopsis cynos
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 1502)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 1502)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 1502)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 1502)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1502)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 1502)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1502
                     /organism="Mycoplasmopsis cynos"
                     /db_xref="taxon:171284"
     Protein         1..1502
                     /product="beta-N-acetylhexosaminidase family protein"
                     /calculated_mol_wt=173049
     Region          2..141
                     /region_name="Glyco_hydro_20b"
                     /note="Glycosyl hydrolase family 20, domain 2; cl03741"
                     /db_xref="CDD:446174"
     Region          147..436
                     /region_name="NAGidase"
                     /note="beta-N-acetylglucosaminidase; pfam07555"
                     /db_xref="CDD:429533"
ORIGIN      
        1 mypsvhsiey ynkhflitpe inlvvedgid savlerfeet lnlrkikyki snkiisgktn
       61 vliglkdnkd tfvddylksk nlmpntdlmn kidsyvlnsk dnvisiyasg edasyygvts
      121 lwhifnqlng leieefnind yadiktrgai egyygnprsl qdrlnymrwg syyklngyfy
      181 apkddpkhsh kwrelytese ienlikplar egnrtkvryi ytlhpffgtr ldndydqgvk
      241 dlknkflqvi qagvrqigil addvaradir tqvrllidmv twlkelkqtk yhdlkvvlpf
      301 vvneyagygq syfkkfpnev qivmtggktw gevspeftnk fytntnrgpl lwinwpcsdn
      361 sknhlilggy reflhknvdp kkvqgivlnp mqqsepskva lfgaadytwn iwkddahidq
      421 tysdafnyvt nnsyqetaes kafrnlakhm inqnmdgrvv aleesielkk klakvrtsle
      481 tnnflvdnik dlkvefeely ndaltiknsv vnrdlyyqir ywiessiely qgltlaldgl
      541 iklsqgdktd fvlnlnkakt liqkartqhg fdylgsiqya evgvqhiqpf ttwlldymsn
      601 kilntniknn nnkkdqvvgy nleiakhssi ndnaknnkld yiidhndstl awlssanngn
      661 vgkdqgieih fesakeiksi rilqdsndkm eslkiqklyn nqvidlengt ldfkdkkeit
      721 ytvpenaglm tgiritstkq tstwwkvksv diqeknvpdp syihtslkdk sklqalrsng
      781 smilsndlkn isknheipsk gyigvdlkdi kyitninidw ikndkfkfli svngfnwiel
      841 dqanfnkkvk frylrlvnss daiqilkftk lslniideiv pfgklietni dlknnwlddr
      901 kngggfdgdf nrytkfggsp lkgqyaiydl ggeldlkslr mytadntadf pryldiqvsn
      961 qkdsgyetvf sindsadsrd itpgqggfgn pdslhpnlrw wgnddikdkk vryikllvkk
     1021 dypsraiiin eivvnggkyl nlnidprfdg tnylesngky kpenifdnkl nssykpaekn
     1081 gkliinldaa ryankdikii teeepsnavv kaivydiktn keleivigal snpivsfslp
     1141 ndpekkvval kiewkdhipv iseiidiekq ngqkvdkskl ktllekpvvd lekwttssrq
     1201 nyiakkqsaq aindltsvtq eavadalkal ddainehklk vdksefdali knenlkndhf
     1261 iytnesfydy qlalekikyq nvddlgqsef nklkenletk kialefspyn mqislfnvek
     1321 fneinkdnyl sdsynklkak vdeikrkite nkiepseyik lnkeyeilys qlspkaksvl
     1381 iltyekyknd vvipfiakyk nkwpeeyaki ndvltknegk vsdqstdlsi neaindlknv
     1441 agsiiegvar kqkeirdiyi nrktnaylvy qddkytnydk fiselafmnn iqktwlvkni
     1501 mk
//
LOCUS       WP_284521399             319 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Cytobacillus pseudoceanisediminis].
ACCESSION   WP_284521399
VERSION     WP_284521399.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus pseudoceanisediminis
  ORGANISM  Cytobacillus pseudoceanisediminis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Cytobacillus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Cytobacillus pseudoceanisediminis"
                     /db_xref="taxon:3051614"
     Protein         1..319
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=35866
     Region          <1..305
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mlvgvlvltn glltylvsks iikpllrlke aandisrgnl dtkievsgkk delnelamaf
       61 dimrgrlkea adiqmqyekn qkeliasish dlktpltsik gyirgisdgv antpekmdry
      121 irtiektsde mesliselll yskldlpnvp ydmremdlvs yfdhyleelr fnlagqnvsl
      181 slecqpnqsy rvhadrgkln rvvanivqns lkymneekke lmfrlsskae eviveirdng
      241 agvskdelpy lfdrfyrtdv srnsatggtg lglsivkkii eghggtiwar ggtghglsiw
      301 ftlkkgvtig knlnyrrra
//
LOCUS       WP_284521756             302 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Cytobacillus
            pseudoceanisediminis].
ACCESSION   WP_284521756
VERSION     WP_284521756.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus pseudoceanisediminis
  ORGANISM  Cytobacillus pseudoceanisediminis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Cytobacillus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Cytobacillus pseudoceanisediminis"
                     /db_xref="taxon:3051614"
     Protein         1..302
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34329
     Region          1..287
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mkvglstysl vrelrdgnmt vldvidwiae nggehmeivp ygfsvvdnae lahqikkrae
       61 sagielsays lpanfvqptq eafeqeverl kehvdivnlm gikimrhdvt afqlkpeemt
      121 ihyfeehfdk lvegsrqiad yaaqygittt ienhgfnvqs sdrvqrvihe vdrpnfkttl
      181 dvgnflcide dplvgvkknl kyaatvhlkd fyirpyyenp gdgvwfrtvn enylrgaivg
      241 hgdlnireii rlikdsgydg yltvefegme dcrtgskigm dnvrrlwnev qavndtkpvl
      301 kg
//
LOCUS       WP_284521890             428 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Cytobacillus
            pseudoceanisediminis].
ACCESSION   WP_284521890
VERSION     WP_284521890.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus pseudoceanisediminis
  ORGANISM  Cytobacillus pseudoceanisediminis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Cytobacillus.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Cytobacillus pseudoceanisediminis"
                     /db_xref="taxon:3051614"
     Protein         1..428
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=48784
     Region          9..427
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mskkffedkh fhhmfnhlkd gifiadhngi alwindtssk qmgaprskvi grsvsdlekd
       61 glftpsitni vlekretvtk vqtskgrqyl atgyfveike dktqyvlvnv kditdtvrss
      121 lqlekaeill qkywdelqem kvkesekknn hiiignskkh eeildligri asldvtillt
      181 getgvgksmi asmihrrsnr tdkpfiqinc gaipetlles elfgykkgaf tgannsgkig
      241 lvekanggtl fldeigelpl tlqpkllqlv qeksffpigs telkqvdvri itathqslle
      301 mvqekrfred lyyrlnvvsi qipalrerkd diiplvfhyl elfktkyrks tvlgkelvdy
      361 lqnyswpgni relenmierl vvtakseiid ksdlsekvlr evqkkesafp pklngqslps
      421 yieeieks
//
LOCUS       WP_284522212             260 aa            linear   BCT 25-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Cytobacillus
            pseudoceanisediminis].
ACCESSION   WP_284522212
VERSION     WP_284522212.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus pseudoceanisediminis
  ORGANISM  Cytobacillus pseudoceanisediminis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Cytobacillus.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Cytobacillus pseudoceanisediminis"
                     /db_xref="taxon:3051614"
     Protein         1..260
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29669
     Region          23..259
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mfftalatvi sffgikkmts tthkmkkigh rgaagycpen tfpsydraie mgadyleidv
       61 qlskdgkivv ihdslvdrtt dhkgkvsdft fdelrkmdag swfsqkfrga cipsfeevld
      121 kyadrvglli elkkpslypg iekmiaeelk krnfhtkgdd hiivqsfete smkrfhelvp
      181 eipvailiny ppdtveikni aeyasylnpk wtvvnkrvid lihsnhmkai awtvrsrkea
      241 eklkhypldg ivadyldlie
//
LOCUS       WP_284522419             469 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Cytobacillus pseudoceanisediminis].
ACCESSION   WP_284522419
VERSION     WP_284522419.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus pseudoceanisediminis
  ORGANISM  Cytobacillus pseudoceanisediminis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Cytobacillus.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Cytobacillus pseudoceanisediminis"
                     /db_xref="taxon:3051614"
     Protein         1..469
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52763
     Region          <157..457
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mgeinekkls iklgivffli ifsleifmff flhsalvdsr ieeefislqa rgnahrdile
       61 khfdqdtish vslmeseant dvvitdmngr ilgssskssd iqdhinsads viprdgevvd
      121 gnwkegkfis tvspveidgd itakvfmfqe tesihslidr lnkhfiltgi favfltltvi
      181 iflskglakp likmkeatsq iskgdftvsl pknrndelgd ladsisrlas dlhylklern
      241 dflasishel rtpltyikgy adivhkrnls iedrdkylni iheeanrlsd likdlfdlak
      301 mdknsfviqk rpidltdfil kieqkfspaf qekemeldvi cpkeaviiad ptrleqiifn
      361 lldnaikysp pgaktilsvn nkkkdvyikv rdngkgipee dlpyilnrfy rvdksrtrsl
      421 ggtglglaiv kelvlahggt vsvrskegkg tefelvfkga dkiendtis
//
LOCUS       WP_284522517              95 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            aquatimens].
ACCESSION   WP_284522517
VERSION     WP_284522517.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium aquatimens
  ORGANISM  Corynebacterium aquatimens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Corynebacterium aquatimens"
                     /db_xref="taxon:1190508"
     Protein         1..95
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=10044
     Region          32..>84
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
ORIGIN      
        1 mrfdgshdha vtatvtwedg peetnppspq ptpelsgnel lafnalqaag temsssdvae
       61 aaglstqqay ralrklvdag hvtrsgetrm trysv
//
LOCUS       WP_284522619             151 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            aquatimens].
ACCESSION   WP_284522619
VERSION     WP_284522619.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium aquatimens
  ORGANISM  Corynebacterium aquatimens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 151)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 151)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Corynebacterium aquatimens"
                     /db_xref="taxon:1190508"
     Protein         1..151
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16104
     Region          23..>147
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msknsnpttl gsvetapaar vptalrglrl lelmqwgksf ttaelaaelg vsqssirkyi
       61 aqlrsanyti ksgpgfgamy wiargertyp lqltsdemet vllslsiysa angstdprsh
      121 matdlftris dvvpadiaea tsgasekwsg n
//
LOCUS       WP_284522824             278 aa            linear   BCT 25-DEC-2024
DEFINITION  indole-3-glycerol phosphate synthase TrpC [Corynebacterium
            aquatimens].
ACCESSION   WP_284522824
VERSION     WP_284522824.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium aquatimens
  ORGANISM  Corynebacterium aquatimens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Corynebacterium aquatimens"
                     /db_xref="taxon:1190508"
     Protein         1..278
                     /product="indole-3-glycerol phosphate synthase TrpC"
                     /EC_number="4.1.1.48"
                     /GO_function="GO:0004425 - indole-3-glycerol-phosphate
                     synthase activity [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29074
     Region          11..260
                     /region_name="TrpC"
                     /note="Indole-3-glycerol phosphate synthase [Amino acid
                     transport and metabolism]; COG0134"
                     /db_xref="CDD:439904"
ORIGIN      
        1 mlapsavndv vagvlrdvak reasvpfqei karsrtmpdp trdaraallr sgcgviaeik
       61 lnspvygptg varrdiagva raieeggahl iacqterlrf dgslhdmaqa raavalpmvc
      121 rdvivdpyqi hearcygada lplqvgileq arlialidra esigmaviae vrtpqeadra
      181 leagasiiav nswtfdtndl rpgtfaeiap glpsgvikis lggvtsvrdl mnaascgada
      241 vlaaeaimsg ddifaatrkl aaagqhppar rggrasrr
//
LOCUS       WP_284522833             698 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium aquatimens].
ACCESSION   WP_284522833
VERSION     WP_284522833.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium aquatimens
  ORGANISM  Corynebacterium aquatimens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Corynebacterium aquatimens"
                     /db_xref="taxon:1190508"
     Protein         1..698
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=74665
     Region          12..373
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mstprayqpa rpsgasayrv dldglrgyai alvvifhvfv grvsggvdvf lflsgyfflg
       61 gqlryamrpf pnlnpwwpfw rtvrrlvpal vvvlaatllg ilaltpelmn eglarqftas
      121 llyfqnwelt iqdaayaaas dttsplqhlw smsvqgqfyi fgiclatlia wlvstsktsk
      181 qsaqrlvvav lavitvasfa yaarfgfegt pqnyystfsr awelslgall afvpahwylp
      241 qrgswiaslt glvmitatgi iiptslafpg plallpitga aliilagnan pvstvlaskp
      301 mtwlgsvayp lylwhwplli ivtasggftt pppavgvavi laslalahvt ytlvekplrq
      361 hgkrplsfdt pvadaraslr taagagravg gaivaalfvc glaiqpvwdn rinqadkpld
      421 pakypgamal lgtdvpknkp kpnpqlisgi yppiglqecm iflpapadem prpdcafgdl
      481 naettvvmvg gshiepfgip ldilgqqhgf kvipfvrqec plviggedrf divsevcaew
      541 gervyqqild iqpdlvists trpggragaa gsaadavpda yanlwanfad qgipflglrd
      601 npwffdpfgn pmdpnvciva ggteescsmp aakaypepdp aagyldgmnn lfsvdtagwy
      661 cpgdtcprks atctctatrt tsptptraas phcygasw
//
LOCUS       WP_284522886             728 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Corynebacterium
            aquatimens].
ACCESSION   WP_284522886
VERSION     WP_284522886.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium aquatimens
  ORGANISM  Corynebacterium aquatimens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 728)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Corynebacterium aquatimens"
                     /db_xref="taxon:1190508"
     Protein         1..728
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=77051
     Region          36..560
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mfsfrrvgsl vaattatavi lsgvpvafad engnivdikv anftdfhgrl eykpstttkk
       61 daagnavkdd kgkdvkvetp kkgdemgaar vagiidylra qnenlivtns gdnqggsgfv
      121 sminekdqpt mdflqaigth gsavgnhefd qgysditgri mretavehqn vtsaddtkwk
      181 nqtqlganif lkgtdtrevn pynivdvdgv kvaligttst ltvtksapsn vaavdikdsa
      241 ewvnkeakal kdagkadvvi alihddaker adkldakyvd flfggdshvv yenadapvpy
      301 aqaweygktv idmdfqydkk akkvvgkpty nfidasqlad lkitpnvnve kivteakkna
      361 delgkevvat tkadfkrgsn pgaepgsnrg testannmla qsavqslsky mgreidfgim
      421 naggvrddlp kgeitykdav tvqpfgndis fakikgstlk emlenqwqte ektassgrpr
      481 ldmglsdnva ytynpeaarg qriqnlting anldpnkeyt faastflleg gddfldpski
      541 ierldigynd tqalidhlna dsievrkgqk dagvvlpegg lkagkneikl tslsyssege
      601 pkaqnvtvkv gkakatakvd nnvtdadkgy geqgratvtl nipagvtgaq tleittdagt
      661 kvtmpvtvag kggdtgtapg gntgdnttsg ssaskalagt iigtsiaili aiglggflvt
      721 nagfpias
//
LOCUS       WP_284522915             233 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            aquatimens].
ACCESSION   WP_284522915
VERSION     WP_284522915.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium aquatimens
  ORGANISM  Corynebacterium aquatimens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Corynebacterium aquatimens"
                     /db_xref="taxon:1190508"
     Protein         1..233
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23729
     Region          2..219
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 maertrsggg dtrravmaql lkrgpvsaad ladglglsaa gvrrhldalv aeglaetcsp
       61 nqvageeagr grppkhfrlt dagrdhfgts ydslaleavd likdlggega vrtfakgris
      121 kilggvrsaa egeaddveav vaevaaaled hgyaatvtra gggiqicqhh cpvsavaaah
      181 pelceaehea iaelvgrhiq plaliadghg icttniplsv tspagdtner sga
//
LOCUS       WP_284523095             139 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium aquatimens].
ACCESSION   WP_284523095
VERSION     WP_284523095.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium aquatimens
  ORGANISM  Corynebacterium aquatimens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Corynebacterium aquatimens"
                     /db_xref="taxon:1190508"
     Protein         1..139
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=15448
     Region          <2..135
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 msrserrrad vvfathfdpw vmtgdpeaml rapvnimdna akwsppngev kvrlvakpgr
       61 ailtvddagp gippdqrerv ferfyratet rstpgsglgl aitkqvlerh darvfveesd
      121 qggarfrvif pghkpdnrq
//
LOCUS       WP_284524235             162 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Mycoplasmopsis
            cynos].
ACCESSION   WP_284524235
VERSION     WP_284524235.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis cynos (Mycoplasma cynos)
  ORGANISM  Mycoplasmopsis cynos
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 162)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 162)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 162)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Mycoplasmopsis cynos"
                     /db_xref="taxon:171284"
     Protein         1..162
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=18963
     Region          <23..159
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mirlkkrygy higiiyvqwi rkklivfysg dsrcyiykkn gellqitrdh nllnrwideg
       61 ieqkniekny rvyryltsai ganletkidf ivlennfenp itkilltsdg inefltndqi
      121 hfilsnkkdt tlqklnslvt lslisesndn msailmeikn dk
//
LOCUS       WP_284524714             129 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Mycoplasmopsis cynos].
ACCESSION   WP_284524714
VERSION     WP_284524714.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis cynos (Mycoplasma cynos)
  ORGANISM  Mycoplasmopsis cynos
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13031057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Mycoplasmopsis cynos"
                     /db_xref="taxon:171284"
     Protein         1..129
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=14468
     Region          2..119
                     /region_name="SpoU-like_rRNA-MTase"
                     /note="SAM-dependent rRNA methylase related to SpoU-TrmH;
                     cd18095"
                     /db_xref="CDD:349968"
     Site            order(58,60,81..84,87,101..102,104,108..109,111,114)
                     /site_type="other"
                     /note="SAM binding site [chemical binding]"
                     /db_xref="CDD:349968"
ORIGIN      
        1 makafnfdtv iienldvfnd kvirasqgal fklniietnd leseliklkn ngytiyetll
       61 nknaqvlnsi kfvedkmviv fgneangirp niqklsdlni yipiefesln vaisagivld
      121 kvynrskde
//
LOCUS       WP_284525675             404 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Shigella flexneri].
ACCESSION   WP_284525675
VERSION     WP_284525675.1
KEYWORDS    RefSeq.
SOURCE      Shigella flexneri
  ORGANISM  Shigella flexneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Shigella flexneri"
                     /db_xref="taxon:623"
     Protein         1..404
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=45720
     Region          12..399
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mkhspgnpgr fkpddkplph ggitgltlhp ssvkgrgkwv fryvspvtqk rrnaglgtyp
       61 evsiaeaart arimreqlaa gddpleikka esekvviptf adaarrvhae lspgwenpkh
      121 vrqwlstlen yafpqlgakt ldsitaadva etlrpvwltl setasrvkqr ihvvmqwgwa
      181 hgfcvanpvd vvdhllpqqt rgrdehqpam pwrqlplfva tsvysdepyn vtralllmvi
      241 ltatrsgear gmrwaeidfh krvwtipaer mkarlqhrvp lsrqaiyile nirglhdelv
      301 fpsprkqqil sdmvltsflr kkkavsdipg rvatahgfrs tfrdwcseqg ysrdlaeral
      361 ahtlknkvea ayhrtdlleq rvpmmqawad yvmsqlaknt kefa
//
LOCUS       WP_284525849             451 aa            linear   BCT 25-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Microcystis panniformis].
ACCESSION   WP_284525849
VERSION     WP_284525849.1
KEYWORDS    RefSeq.
SOURCE      Microcystis panniformis
  ORGANISM  Microcystis panniformis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Microcystaceae; Microcystis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Microcystis panniformis"
                     /db_xref="taxon:513223"
     Protein         1..451
                     /product="metal-dependent hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48868
     Region          58..>102
                     /region_name="metallo-dependent_hydrolases"
                     /note="Superfamily of metallo-dependent hydrolases (also
                     called amidohydrolase superfamily) is a large group of
                     proteins that show conservation in their 3-dimensional
                     fold (TIM barrel) and in details of their active site. The
                     vast majority of the members have a...; cl00281"
                     /db_xref="CDD:469705"
     Region          81..430
                     /region_name="Met_dep_hydrolase_A"
                     /note="Metallo-dependent hydrolases, subgroup A is part of
                     the superfamily of metallo-dependent hydrolases, a large
                     group of proteins that show conservation in their
                     3-dimensional fold (TIM barrel) and in details of their
                     active site. The vast majority of the...; cd01299"
                     /db_xref="CDD:238624"
     Site            order(99,101,266,286,362)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mstsgsrdik rspssrlikt lkklttgett mtgtnstspn yvivtdqywd gladnplgat
       61 eiriengnit aiattvdhsn aqiielkght vtpgfidchv hitfcegdpt ipenpymvtv
      121 plmtlyslnp lktllmngft tvrevgcpdp efitvdlkka iangwiigpd llvaphlisa
      181 qgghgdftsl vafqfrpekf evadgtaeii rivreeirsg adwikfcatg gfssptddps
      241 qttysqeemn ilvstakdfg isacphaygg egvqravnag vrsiehgnla ssetlqlmee
      301 kgvylvptqy tvlekarnan npeywksrsp wqhakyqkya sqliacadnl aksnvkiafg
      361 tdagtfphid nwkefpamvq ngitplralk aattvaaell mqpnigalav gkfadiiamp
      421 gnpfedinvt gkvdfvmkrg viykqpsggq v
//
LOCUS       WP_284525718             418 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Clostridium sp.
            AF50-3].
ACCESSION   WP_284525718
VERSION     WP_284525718.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. AF50-3
  ORGANISM  Clostridium sp. AF50-3
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Clostridium sp. AF50-3"
                     /db_xref="taxon:2293021"
     Protein         1..418
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=49145
     Region          1..398
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mllshrtsvn irpeysniig hmcyaasklw nvcnyerrry kelglekypd wyyqkkahkg
       61 dlwyrqlpsq taqetckqld kawksfyalk ktggikdpnp prfkqdnipi tymqmgirhe
      121 kgsdqlrlsl skdlksymee tygihekfly lenkifrnmd hikqlriypp edgkcdlivi
      181 yeikepepls lnghylsidl gihnlmtcyd sgngrsfilg rkylsleryf hkeisrvqsi
      241 wyaqqmengi kyprsskhik riyrkkqnav kdylhkvtrw laeyckkeri scviigdirn
      301 irkgkdighk tnqkfhglpy nklyimleyk lklygisltk qeesytsqcs pfspelskry
      361 aeasnrkerg myitdgvryn adavgafnil rkylsgsgkq kelsvtglkn peiikvav
//
LOCUS       WP_284526338             238 aa            linear   BCT 25-DEC-2024
DEFINITION  trypsin-like serine peptidase [Staphylococcus aureus].
ACCESSION   WP_284526338
VERSION     WP_284526338.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     Protein         1..238
                     /product="trypsin-like serine peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=25548
     Region          61..234
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mnkniiiksi aaltiltsvt gvsttmveri qqtakaehnv tkitntsisp ykgilrvgaa
       61 tgfvvgknti ltnrhvvkdv qvgstvlahp ngendtggyy kvkkvipyag sadlaiveve
      121 edsvypknkk fsenteiltl aseakanerv aivgypapyk nkhhmyqstg tvlsingdkl
      181 vsdafaeggn sgspvfnnkn evvgvlysgd qighskkesy svyltpeikk fiadntek
//
LOCUS       WP_284526616             343 aa            linear   BCT 25-DEC-2024
DEFINITION  RHS repeat domain-containing protein [Shigella flexneri].
ACCESSION   WP_284526616
VERSION     WP_284526616.1
KEYWORDS    RefSeq.
SOURCE      Shigella flexneri
  ORGANISM  Shigella flexneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Shigella flexneri"
                     /db_xref="taxon:623"
     Protein         1..343
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38262
     Region          <4..237
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 meklvdkggy rplqwrykwd srsqltglet pdgerweyky dpfgrriskr ctshdkpgmd
       61 fhwngdqlte eipvgvdgkp edenairwiy epgdftpfar yekgqlnyav tdtvgrvqel
      121 ltedglivwk gkqqlwgree ginkgdaptc rlrfpgqyed tesglyynrf ryydcgtgqy
      181 issdpiglrg gikpygyvhs plnyidplgl anakvidnvl hivdkfgvng aapdtaasre
      241 laefvkrwne qivanggsma rrsvckevrk aaseaaaaer klnpslyang evaghipdvg
      301 wggkidgpfm plspkvnsyi ggltqavpvg ttytsvrivd iil
//
LOCUS       WP_284526721             402 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Shigella
            flexneri].
ACCESSION   WP_284526721
VERSION     WP_284526721.1
KEYWORDS    RefSeq.
SOURCE      Shigella flexneri
  ORGANISM  Shigella flexneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Shigella flexneri"
                     /db_xref="taxon:623"
     Protein         1..402
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=45525
     Region          1..392
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkrlqafkfq lrpggqqehe mrrfagacrf vfnralalqn enheagnkyi pygkmasrlv
       61 ewknatgtqw lkdspsqplq qslkdleray knffrkraaf prfkkrgqnd afrypqgvkl
      121 dqensriflp tlgwmryrns rqvtgvvknv tvsqscgkwy isiqtesevs tpvhpsasmv
      181 gldagvakla tlsdgtvfep vnsfqknqkk larlqrqlsr kvefsnnwqk qkrkiqrlhs
      241 rianirrdyl hkvtttvskn hamiviedlk vsnmsksaag tvsqpgrnvr aksglnrsvl
      301 dqgwyemrrq leykqlwrgg qvlavppayt sqrctccght akenrlsqsq frcrvcgyta
      361 nadvngarni laaghavlac ggmvqsgrpl kqeptemiqa ta
//
LOCUS       WP_284526735             230 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Shigella boydii].
ACCESSION   WP_284526735
VERSION     WP_284526735.1
KEYWORDS    RefSeq.
SOURCE      Shigella boydii
  ORGANISM  Shigella boydii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10150555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Shigella boydii"
                     /db_xref="taxon:621"
     Protein         1..230
                     /product="helix-turn-helix domain-containing protein"
                     /calculated_mol_wt=25831
     Region          143..199
                     /region_name="LuxR_C_like"
                     /note="C-terminal DNA-binding domain of LuxR-like
                     proteins. This domain contains a helix-turn-helix motif
                     and binds DNA. Proteins belonging to this group are
                     response regulators; some act as transcriptional
                     activators, others as transcriptional repressors. Many...;
                     cd06170"
                     /db_xref="CDD:99777"
     Site            order(144..146,159..161,169..170,172..173,175..179,190)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:99777"
     Site            order(155,157,159,190..192,195,198..199)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:99777"
ORIGIN      
        1 mskipvmqag lkevmrthfp eyeiissasa edltllqlrr sglviadlag esedprsvce
       61 hyyslisqyr eihwvfmvsr swysqavell mcptatllsd vepienlvkt vrsgnthaer
      121 isamltspam tethdfsyrs viltlserkv lrllgkgwgi nqivsllkks nktisaqkns
      181 amrrlaihsn aemyawinsa qgarelnlps vygdaaewnt aelrremshs
//
LOCUS       WP_284526265             293 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein, partial
            [Shigella boydii].
ACCESSION   WP_284526265
VERSION     WP_284526265.1
KEYWORDS    RefSeq.
SOURCE      Shigella boydii
  ORGANISM  Shigella boydii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Shigella boydii"
                     /db_xref="taxon:621"
     Protein         1..>293
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
     Region          11..264
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mrdllqrpdl fsintatlgy ktplpaiida caargigaia pwrrelqged lqqitrqlaa
       61 snmsvsglcr styytaptla erklaiddnr ralddaavln aacymqvvgg lptgtkdlye
      121 areqvkqgir qllphskdvg vpialeplhp mtaadrsclc tlrqaldwcd eldpdgefgl
      181 gvavdvyhvw wdpdlasqil ragkrilafh vsdwlvpttd lvndrgmpgd gvinipsirr
      241 lvenagfnga ieleifspyw wqkdinstgn dsnllivfyv qimpddlvmq lhr
//
LOCUS       WP_284526873             393 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Shigella flexneri].
ACCESSION   WP_284526873
VERSION     WP_284526873.1
KEYWORDS    RefSeq.
SOURCE      Shigella flexneri
  ORGANISM  Shigella flexneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Shigella flexneri"
                     /db_xref="taxon:623"
     Protein         1..393
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=45245
     Region          2..391
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 maltdikvkt akpkekpykl sdgggmylli ntngskywrm kyrfagkekm lsigvypdvt
       61 ladarekrse arkilaagcd pgetkkeeki alqmslkntf eavarewhqs kadrwslryr
      121 deiidtfekd ifpyigkrpi aeikpmelle alrkmekrga lekmrkvrqr cgevfryaiv
      181 tgranynpap dlasalatpk kvhfpfltan elphflndla gytgsiitkt atqiimltgv
      241 rtqelrfarw edidfetklw eipaevmkmk rphivplseq vialfkqlep iskhhplvfi
      301 grndprkpis kesinqviel lgykgrltgh gfrhtmstil heqgfnsari emqlahmdkn
      361 airgtynhaq yldgrremmq wyadyidsls eqi
//
LOCUS       WP_284527013             255 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Shigella flexneri].
ACCESSION   WP_284527013
VERSION     WP_284527013.1
KEYWORDS    RefSeq.
SOURCE      Shigella flexneri
  ORGANISM  Shigella flexneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Shigella flexneri"
                     /db_xref="taxon:623"
     Protein         1..255
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=28487
     Region          <1..251
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 meqkiklntr miyaespgtm tmqivdlqai aqlatrygii taidntwptp lfqkplslgf
       61 divihsctky laghsdvlag vvitrrelms iirdfshqll gavlspfsaw lllrgirtlp
      121 irmathqhna inviewlatr devenirhpl catdkekeii rrqmcgfsgl fsfelkgagf
      181 eevkcfidac rifkpgcswg gyesliispn rgynqsaldd aeiprglirl slgqenaall
      241 iadlerafds lrtkp
//
LOCUS       WP_284527052             812 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Microbacterium sp. T2.11-28].
ACCESSION   WP_284527052
VERSION     WP_284527052.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 812)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 812)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..812
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=90525
     Region          11..811
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtdpagrfar aeaarshplt tafadaqrfd ldpfqiagch aleagrsvlv aaptgagkti
       61 vgefavhlam qepgekafyt tpmkalsnqk frelqdvyge sevglltgdt ningsarivv
      121 mttevlrnml yadspalrgl ryvvmdevhy ladrfrgavw eeviihlppq vrlvslsatv
      181 snaeefgdwl dtvrgdtevi vsetrpvple qhvlvrgdll plfddragia taqvnqelmr
      241 irsvkgsnfd nnrrvqefrs sggyeaghrr phkggrrpvr sanvqrieri drpdvvellg
      301 ranllpaiff ifsragcdga vqqvrrsgvr ltsreerdei rqivdertrt mqdedlavlg
      361 fwewrenler gvaahhagll pafkeiveel fqrklvkavf atetlalgin mpartvvlek
      421 lekfngearv aitageytql tgragrrgid veghaviqwt egldpqavaa lasrrtypln
      481 ssfrptynma vnlidqfgrp rareilessf aqfqadrsvv glarqvkdae eslagytkam
      541 acdrgdfpey aqmrrelsdl eklnradrta paktrqqrqn qiqslrrrlq rhpchscpdr
      601 ekharwgery aklsrqidkl rhqietrtgt varifdrvvd vlaaldyvvv dadgtsrltd
      661 agatmrriyg erdllvaesl rrglwtglda pglaalaccl vyeprrddag dralprgafr
      721 aalsdtqelw avlddlerdh rlpgseppsa glaqamhswa rgvaldrvlv eadlaagdfv
      781 rwtkqtidll dqlsmvadpp vattarkald ae
//
LOCUS       WP_284527046             332 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Microbacterium sp.
            T2.11-28].
ACCESSION   WP_284527046
VERSION     WP_284527046.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..332
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36512
     Region          12..326
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 matestriap eerlvnlvva llatdqgltk dtiltsvsgy reqseagagk dalekmferd
       61 kenlrglgvp ietigdfadp ddlrearyri ptseyelpvd idftpaelav lnlaggvwse
      121 ssmsaqarsg lrkiralgne vdapiigysp rinlrepafa plqraieqar evefdylkag
      181 ddtpgrrrvr plalleyegr whvygfdrdq naertfllsr vaspvqvtkr afdpslrdga
      241 gekalsglha vaarqqalle vapgteaalr lsrrasvaeq girvpyvdvh vfadelasyg
      301 pevrvvepgd lrdevirrle rtlathtdgg lr
//
LOCUS       WP_284527666             480 aa            linear   BCT 25-DEC-2024
DEFINITION  protoporphyrinogen/coproporphyrinogen oxidase [Microbacterium sp.
            T2.11-28].
ACCESSION   WP_284527666
VERSION     WP_284527666.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Pawelek,P.D., Cheah,J., Coulombe,R., Macheroux,P., Ghisla,S. and
            Vrielink,A.
  TITLE     The structure of L-amino acid oxidase reveals the substrate
            trajectory into an enantiomerically conserved active site
  JOURNAL   EMBO J 19 (16), 4204-4215 (2000)
   PUBMED   10944103
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440906
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..480
                     /product="protoporphyrinogen/coproporphyrinogen oxidase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006779 - porphyrin-containing compound
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=47961
     Region          3..443
                     /region_name="HemY"
                     /note="Protoporphyrinogen oxidase HemY/PPOX [Coenzyme
                     transport and metabolism]; COG1232"
                     /db_xref="CDD:440845"
ORIGIN      
        1 mtvdlvvvga gigglavahd aaragldvvv leegdrtggm lrradlggva idigaesfat
       61 rttgvadlia daglglriva ptaggahlaa vgdhgvlrap lprrtvlgip adpladdvvr
      121 ilgeagarra aaeaamppgg relaepslad lvaersgpal lhrlvdplcr svysvpaaev
      181 rlsrlhpalw rafcdlgslt aaaaslaape ragaavggie ggmwrlaeel hraataqgad
      241 irtgarvrqi ateqgrvsva agdatlrarr vvlatgtaaa rsllatpaaa ppvvrvaaal
      301 vrapalddap vgsgviaaad vpgqakalth vtskwewvaq avppghhivr fsardgasrl
      361 gtaadvvrel dvlagvaldp advvavveqa wpdavaappv dparraalaa dgvllagaaa
      421 agtglasvvp harelaralv aelrgpspig pgtravpdpl aaaatltpnt pptsndrrta
//
LOCUS       WP_284527752             313 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Microbacterium sp.
            T2.11-28].
ACCESSION   WP_284527752
VERSION     WP_284527752.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..313
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34935
     Region          85..313
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          225..309
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 maerwrlrta gpdaveetwq tvvpssrlhr vdpqrfafdw tsstlegmtv vaydleasvr
       61 aavdavdqvm vcrvvtadgg awdehgpldt rhpwvsagrp irarwdgrar vhalvfdrrl
      121 velsarrisg ddslwlgpwd arpvsdaaar hwqrayryia emlladdegp gslaeaelrr
      181 havhatltty spaflersar saqrraapat vrramafiee hahepitvdd valaagistr
      241 glqyafrrav dttptewlrr arlsgahrsl sdpeggtvae iarrwgfehp srfaahyraa
      301 ygvnpaqtlr ahr
//
LOCUS       WP_284527823             330 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Microbacterium sp. T2.11-28].
ACCESSION   WP_284527823
VERSION     WP_284527823.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..330
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34942
     Region          2..326
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 miivgagqag lavaaalrae glepqrdfiv idgapslhlr swrdrratle llsdarhsaf
       61 pwrplpgdqr rriqademad ylsaveaalg vetrwnvrat svehsgsgtt lflstsagiv
      121 qtrnvvcatg atsrpaspsw asylavpgiv lhshdyrspd qiprgdvliv gggnagvrla
      181 helsathrvt latrtprvir adrgraprag rpprfapraa hrepvhgpnl aalrrsgvtl
      241 asgvvhadga rvrfadgsva sptsvvlatg yhpgdewlag atpqprratl tdipglfvag
      301 iprfgrpesv tiagvwndat iiaqhimgrp
//
LOCUS       WP_284527833             211 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Microbacterium sp.
            T2.11-28].
ACCESSION   WP_284527833
VERSION     WP_284527833.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..211
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22569
     Region          66..209
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 myrrhrgala rthfhrralp favisitall isgcapiggv dqgytppdga gvvsvdgrif
       61 eiaadergep vafsgtsehg daidsatfkd rvyvvnfwya acgpcrveap lleevwqkyq
      121 rekvgfvgvn iydqpgtaas faeqygityp svidvndgav klafaavtpi qatpttlvmd
      181 rqgrvaarii gelpsasild tlvkdllaeg e
//
LOCUS       WP_284527835             632 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Microbacterium sp.
            T2.11-28].
ACCESSION   WP_284527835
VERSION     WP_284527835.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 632)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..632
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=65346
     Region          4..613
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mpdelraaww rdlallpsal sgvfllvgyv lewsgvqvpa lvfqwlalla gaytfvpgal
       61 rrlmrrrlgv gllmtiaavg avllghvgea atlaflfsla ealedramdr akeglralls
      121 lipdtvrvsr lageatipav evreldilvv gagervatdg vvvegrssvd tsaitgesip
      181 vevgpgdava agsvngsatl rieatadgrd nsltqivtlv eqaharkger arladriarp
      241 lvpvvliaaa lvalfgfvvg dpetwieral vvlvaaspca laiavpvtvi saigsaskfg
      301 vviksgeafe rlgtiravaf dktgtltrne pavvevrtvd grsrddvlrw agaveaasth
      361 plasaiiaaa psstlavdvv edaghgirgt vdgrairvgn vrwldavtlr seadrmasqg
      421 itvvvveadg aiagligird elrpesaetv rmlhaqgidt imltgdnsat ahalardagi
      481 tdvraeqlpa dkaaaidtlt rtrptamvgd gindapalat atvgiamgvk gsaaaiesad
      541 vaftghdlrl ipgalaharr grrimtaniv lalaiivglf plalfgvlgl agvvlvheia
      601 evivilngvr aarrtapsas tvgvrpvphm va
//
LOCUS       WP_284527848             362 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Microbacterium sp. T2.11-28].
ACCESSION   WP_284527848
VERSION     WP_284527848.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..362
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36976
     Region          9..359
                     /region_name="Tdh"
                     /note="Threonine dehydrogenase or related Zn-dependent
                     dehydrogenase [Amino acid transport and metabolism,
                     General function prediction only]; COG1063"
                     /db_xref="CDD:440683"
ORIGIN      
        1 mtaaipatmr aavlhgrrdl rveevpspsp gpgelllevt avgvcgtdaa ewgngpkllp
       61 ievrhpvtgh lgpltmghef agrvvavgdg vdpawigrla ascgagpcge cdlcrigrsn
      121 vcrryaavgl hrdgalaryv sapaascvda galgidehea alvqpmsiav haarrsgvrs
      181 gdvavvqgvg gigaflihvl vdlgarvvav dldpgrlrla aelgatltvv gatattadel
      241 vaawgeelpv ffevtgsqrg ldlaieivpm gttivavgia kapapvdlgr vtvreitlvg
      301 tnamvretdl ddaarlvaar agrwdvvapa plpferlvdg alapiadgrp pavkslvlpp
      361 rp
//
LOCUS       WP_284527882             365 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Microbacterium sp. T2.11-28].
ACCESSION   WP_284527882
VERSION     WP_284527882.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..365
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38578
     Region          49..215
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 msdpqtapvp aggraradlr agldrlress tpilqivlaa taayafahfv lghaapllaa
       61 tvtisslglv rdarprrvle tvvgmvvgil iaelillvag vgwwqlaitl aaslavarfl
      121 spqpgfaiaa aiqsaivmvi pasvpflrlv dgvvggiaal lvtalvprnp vravtrdgha
      181 llaafdgavl tlvqalrrgd rmraerglqk aralqplvdr wqaslesgra iarispflrr
      241 qrfelerqdr vrvhidlavr nlrvigrrvv yvcddsrprp vaadllgela agarligdsl
      301 ddisfepaar eavravaarl dpatlaagrq sldqnlvgal rplavdlmta agmpsadara
      361 alprv
//
LOCUS       WP_284527977             243 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Microbacterium sp. T2.11-28].
ACCESSION   WP_284527977
VERSION     WP_284527977.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..243
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25711
     Region          12..241
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mtaaqlpdlt sydgvlfdld gvltptaevh mhawqtmfte lfadwgispp yterdyfeyl
       61 dgkkrydgva sllrsrdvev pwgdpsdppt adtvcgignr knevfsrilr segiapypgs
      121 ialvdrlrda gvpvavvsss knadevlraa girdrfevvm dgviaeregl pskpapdvfa
      181 egarmlgvdp arsaavedah sgvqsaaaag falvvgvdrg vgadillasg ahvvvddlsa
      241 flp
//
LOCUS       WP_284528055             281 aa            linear   BCT 25-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Microbacterium sp.
            T2.11-28].
ACCESSION   WP_284528055
VERSION     WP_284528055.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     BTLCP proteins: a novel family of bacterial transglutaminase-like
            cysteine proteinases
  JOURNAL   Trends Biochem Sci 29 (8), 392-395 (2004)
   PUBMED   15288868
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..281
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=30378
     Region          45..208
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mhrivtaeld ldlgspvdli fqiaaaqpap vvreeltfaq gdrvytptei idqsgsrlhr
       61 lqgeagllqv ryealidgqv spratsdlea itylrpsryc qsdevfsqar rqfrgmqgee
      121 litavsefva tsttytpgls qgtdsavttl mtgqgvcrdy ahvviallra mdmparyaac
      181 yapglrpmdf havaeayhdg twyvidatrl anrrslvria tgrdaadcaf lsyhgghvgl
      241 qrmrvdavvv pddtsdveai daaaaasdpa lddfgalvql a
//
LOCUS       WP_284528181             457 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Microbacterium sp. T2.11-28].
ACCESSION   WP_284528181
VERSION     WP_284528181.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 457)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..457
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=49328
     Region          14..456
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mttdavrmhe vsdeartivd lvldysrqrl laddtpldkp lsaaelsrla grtidergig
       61 arkalsvfeh vlapacittd dpqylsfips apskaaaafd lvvsasalyg gswlegagav
      121 haenevlrwl adefglprga ggvfvqggtl gnlsalvaar alrqaqaaeg prpdrwrvvc
      181 saeahssias aarvmdievv avppgddgvl raaavraald ehgdsvfavv atagstnfgi
      241 vddiagiaal kdrydfwlhv dgayglaaml sptarplfag vehadslvvd phkwlfapfd
      301 acaliyrdpe lgrrahtqha eyldtlteks dwspsdyaah ltrrprglpl wfslatygag
      361 vyreavtasl slaqriaeei drrpgltlvr rpqlsvvvfe regwskadyd awssrllddq
      421 hafvtpsshr grtnarfalv nprttfehlt aildtmd
//
LOCUS       WP_284528233             278 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Microbacterium sp.
            T2.11-28].
ACCESSION   WP_284528233
VERSION     WP_284528233.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..278
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29183
     Region          15..278
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 msqhsgfeqp gtavpgpall fcpadrperf ekalaradgv ildledavaa dakaaarghl
       61 idaqldpdrv vvrvnppgse dfdadmatls qtdfrtvmva kasspkrirr ldprfavial
      121 cetaagvaaa eklaaldnvv almwgaedlv aslggtssrk rgggyrdvar fararvllaa
      181 gaagkaaida vhldigderg lrreardaaa sgftatacih paqvpvvrda yrpdaatlaw
      241 argvlaasqg ergvfrhdgv mvdepvlrha ravlqrad
//
LOCUS       WP_284528240             340 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Microbacterium sp. T2.11-28].
ACCESSION   WP_284528240
VERSION     WP_284528240.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..340
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34822
     Region          21..327
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mtqtaplavv aipsrtaepg aarrrtagvt mavvsalafs ssgplvkpll eagwslsaal
       61 ivrmglaalv lspalvravl rergflrrhg lallafglip vagcqllffs amqrmpvava
      121 lliqylapvf lvafvwlrtr rapsrlvvvg savaiaglvl vvdisgarfd llgtllalga
      181 alcvcvyfvm sertgddlpp lalasggllv gavftavlaa igvlpfsapd itvafrgvev
      241 pgwlpllwvg avgttvgyal gvmavprtgs rlasfvglse vlfalmfawl llaetpapiq
      301 flggglilag vvlvrldada ppevtapvep lpgggapgtr
//
LOCUS       WP_284528299             278 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Microbacterium sp.
            T2.11-28].
ACCESSION   WP_284528299
VERSION     WP_284528299.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..278
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29239
     Region          7..266
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mpeldvtgat svitgaaagm gaevarelar rgarialvdr daaglaavaq slegdghtth
       61 vvdladdaav eaaaaeiaah hplvqtlitc agssmlgsid qltmaemrwl mdvnlwgtvs
      121 itqallpalr rapaahithl vsiyglaapa gripyamskf avrgftealr heledgsvtv
      181 gavypagvkt giilrgryaa aldpaiaqra aaaqakmyht epahaarriv eatvrrrprt
      241 migrearlvd vlarlaptry waamrrplra avdtttpi
//
LOCUS       WP_284528509             355 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family oxidoreductase [Microbacterium sp. T2.11-28].
ACCESSION   WP_284528509
VERSION     WP_284528509.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142552
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..355
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37203
     Region          19..278
                     /region_name="AR_SDR_e"
                     /note="aldehyde reductase, extended (e) SDRs; cd05227"
                     /db_xref="CDD:187538"
     Site            order(24,26..29,49,97..101,139..141,170,174,199..202,
                     213..214)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187538"
     Site            order(101,104,141..143,146,170,199..201,217,229,235)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187538"
     Site            order(141,170,174)
                     /site_type="active"
                     /db_xref="CDD:187538"
ORIGIN      
        1 mttdttptta greggpaplv lvtggsgyvg ahtvaallrq gyrvrttvrs adrsdevasq
       61 laaagvdasg lefavadlsa dagwgdavag adhvlhvasp fppagtvdnd deiivpardg
      121 tlrvlhaahd agvrrvvmts sfaavgygav prdlyteadw teptddntay irskaiaera
      181 awdlvagwgg steltvvnpv gifgpalgpk lsvslgfvka llegampvvp rqifgvvdvr
      241 dvadlhiram lhpraggerf lavsgmssfy gvgqilrrrl gdlaaavper eltddevrer
      301 atsdpalres vsqlgrtpvi ssekarrvlg wsprdvedti edsarslirl glvqg
//
LOCUS       WP_284528507             111 aa            linear   BCT 25-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Microbacterium sp.
            T2.11-28].
ACCESSION   WP_284528507
VERSION     WP_284528507.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 111)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 111)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 111)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 111)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..111
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11868
     Region          3..99
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mtrailearl reldtalarl daddaslrhd radataddeh dpegstlsge wqrvdalrra
       61 rlderaevla aldrveagty gicavcgrpi paarlevrpm attcvacaaa v
//
LOCUS       WP_284528568             553 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Microbacterium sp.
            T2.11-28].
ACCESSION   WP_284528568
VERSION     WP_284528568.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..553
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=58597
     Region          1..538
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msavldvrdl avayetrcgr vvavdgidir iepgeavalv getgsgktta alasigllpr
       61 gavrlrgtvr lgalditgws prrlerilgr dvglvpqdpt asldplktvg wqigevlrih
      121 gerdrariaq evegllervg ladtariars yphelsggqr qrvliagava lrpglivade
      181 stsaldvtvq rtvldllddl rredrsgllf vthdlavaae radriivleg gavqdagdvr
      241 tvlggaghra apytrrliad apalqparfr eappatgepp aievaglakv ftghrgrpdv
      301 aalrdvsftv argtthaivg esgsgkstva rialgfesps agtvkvagtd vsgtqghglr
      361 gaglrrfras vqlvyqspya sldpslsild tvseplrrfg glprrearrs aaellerval
      421 apalhdrrpr elsggqrqrv aiaraiaprp evlvldepvs aldvtvqaqi lallddlqre
      481 fgltylfish dlavvrrisd tvtvlshgrv eetgtardvf ecprsdytva lleaipvpsl
      541 apaplpapig gha
//
LOCUS       WP_284528580             249 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Microbacterium sp. T2.11-28].
ACCESSION   WP_284528580
VERSION     WP_284528580.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 249)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 249)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..249
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=26427
     Region          1..236
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 midvlvadde rpaldelvhl lradgrigei ltagsgadal rqlseravav afidihmpgl
       61 tglelapala aladppaivf vtaddaravd afdlraadyl lkpvrgerlr ravdrvvela
      121 aaapaetead evlpvtvgqs vrfvrrsdvr wvqaqgdysr lhgdgrddga ghlvripise
      181 leqrwasagf vrvhrsylvl aaavtearls gaepsvsvgp valpvsrrll pavrdalvgd
      241 arardggpr
//
LOCUS       WP_284528597             754 aa            linear   BCT 25-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Microbacterium sp.
            T2.11-28].
ACCESSION   WP_284528597
VERSION     WP_284528597.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     BTLCP proteins: a novel family of bacterial transglutaminase-like
            cysteine proteinases
  JOURNAL   Trends Biochem Sci 29 (8), 392-395 (2004)
   PUBMED   15288868
REFERENCE   2  (residues 1 to 754)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..754
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=80074
     Region          365..552
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mnrpivrlgi dlaavaalla vavigfgptf dgpqylvagf gaivvglaia wlgqwrrwgv
       61 lpvagvtlav yfllggalal phtaflgvip tietwrqlal gtvtsfktll ttvppvaasd
      121 ghlivpfllt lvaavlagsl alrvrpaawa llpalaltal qillgasqpa aplvqglvfa
      181 aiavvwlalr qtwdadsaaq ridnpaatps rplrarrlia ggavlaiaag vgigtaafat
      241 ppaqryilrd fvvppfdihq ypsplqswrg iirddadstl ftvgglpdea rvrlatmday
      301 ngivynvsdd gagsssaftp vrsnmsptat gtettvridi adyrgvwlpd vgavteiafd
      361 gdragelrrs ahfndatgtg ivtagltggd aytlqtrvse vpsdsalada qfapltmpkq
      421 egvpeslskl aaenlgdaet piervralqd wlstdgyfsh gladdvysps ghgaarisml
      481 fgneqmigdd eqyavamall arqlgiparv vmgwypdede adagvftatg dnlhawveva
      541 fdgfgwvpfd ptpdednepn dqntkpqanp kpqvlqpppp aqepadlppt iaddreqddd
      601 kepgvdwlgp illyggiglg laalmmapfi vlglikgarr arrraaerta drisggwdel
      661 vdnavdlrtp vvpgatraes aqivgtrfde prvatlatwa dadvygpgdp speevdafwa
      721 qvdelvggmr qqtpwwrrlg arlslrslrr grrs
//
LOCUS       WP_284528898             239 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Microbacterium sp. T2.11-28].
ACCESSION   WP_284528898
VERSION     WP_284528898.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..239
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24506
     Region          4..169
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mtwpdavlwd mdgtfidser awldgartla arsgvtlqra dldrlvgasm attaavlqaa
       61 gvagdadeii aeltervrig lvddlvfrpg alalaaevaa agipqaivsm snrrivdhvi
      121 avapvalasv agddvangkp hpeayltaaa rlgvaierci vledsatgla agvasgavav
      181 avpfylpvda saaaaewdal egrtltdlqr laprssppsi psddntallp tptliteer
//
LOCUS       WP_284528943             192 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Microbacterium sp. T2.11-28].
ACCESSION   WP_284528943
VERSION     WP_284528943.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..192
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=20268
     Region          1..>137
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mrvvivgagl gglvlahalr rradvvvldr dasaadtggy rialtpeavs vierhvpgsl
       61 vdriravsdg pdtfsqftia nsrlrpivia pepagqdrml sqrralrqil aeglrdelrf
      121 sstvvaadss ptqavvtryq sqvdewavpa iveslgpvrv iralrhpllq laagpalala
      181 gaagsaahrg rr
//
LOCUS       WP_284528945             392 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Microbacterium sp. T2.11-28].
ACCESSION   WP_284528945
VERSION     WP_284528945.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..392
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=40967
     Region          14..375
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mpdvvvvgag pvglllsael arrgldvltl erraergsrs raiglhapvl aalepsgite
       61 rllagavrvd rgecradgrv lgvvrfdals trfpfvatlp qpvteaalaq dappvrrgal
      121 vtgirtiagd grrrvrvqav tadgarewda avaivasgag grdlvyrpgg vaihayadry
      181 lmadadvdpr pdadvavvtl ardgvlesfp lpggrrrfva wdglgddpdt gpetrderlr
      241 aamrrrgeaa aaervtgats frvrravapr lrrgpvlvvg daahevspig gqgmnlglld
      301 avglaplvat wvrtgaapda elerwersrv rsarvaaaia svntalgrpr spvlhrvrss
      361 vlgaaisgpg grllahayam gfdsgrhpta ag
//
LOCUS       WP_284528950             180 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Microbacterium sp.
            T2.11-28].
ACCESSION   WP_284528950
VERSION     WP_284528950.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 180)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..180
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19820
     Region          14..95
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 madttdtrdd ganvpseaes ealaralssp lrlrmlrlca weartnkela dllevnpgtm
       61 lhhvrtlvdt gllaaepara gargarevpy ratgrswrap rvpnqsivll etmrqqivgv
      121 dpadiettwl glrlnqehvd elrdrlygll eefkqrgpdv dgetfslvtv lhpdlnppaa
//
LOCUS       WP_284529156              94 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Microbacterium sp.
            T2.11-28].
ACCESSION   WP_284529156
VERSION     WP_284529156.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 94)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 94)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..94
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=10659
     Region          34..85
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 msirllitrq edvmalvtdq dprssrevde sglelmsieq llellpgvsr gllaqwryeg
       61 hgpdfvklgr rplyvrksvq ewleanlhvq phgv
//
LOCUS       WP_284529489             367 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide)
            pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
            [Microbacterium sp. T2.11-28].
ACCESSION   WP_284529489
VERSION     WP_284529489.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Davies,G.J., Gloster,T.M. and Henrissat,B.
  TITLE     Recent structural insights into the expanding world of
            carbohydrate-active enzymes
  JOURNAL   Curr Opin Struct Biol 15 (6), 637-645 (2005)
   PUBMED   16263268
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   4  (residues 1 to 367)
  AUTHORS   van Heijenoort,J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit
  JOURNAL   Nat Prod Rep 18 (5), 503-519 (2001)
   PUBMED   11699883
REFERENCE   5  (residues 1 to 367)
  AUTHORS   Ha,S., Gross,B. and Walker,S.
  TITLE     E. Coli MurG: a paradigm for a superfamily of glycosyltransferases
  JOURNAL   Curr Drug Targets Infect Disord 1 (2), 201-213 (2001)
   PUBMED   12455415
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..367
                     /product="UDP-N-acetylglucosamine--N-acetylmuramyl-
                     (pentapeptide) pyrophosphoryl-undecaprenol
                     N-acetylglucosamine transferase"
                     /EC_number="2.4.1.227"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0050511 -
                     undecaprenyldiphospho-muramoylpentapeptide
                     beta-N-acetylglucosaminyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051991 -
                     UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-
                     glutamyl-meso-2,
                     6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol
                     4-beta-N-acetylglucosaminlytransferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0030259 - lipid glycosylation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=38617
     Region          13..367
                     /region_name="MurG"
                     /note="UDP-N-acetylglucosamine:LPS N-acetylglucosamine
                     transferase [Cell wall/membrane/envelope biogenesis];
                     COG0707"
                     /db_xref="CDD:440471"
ORIGIN      
        1 mtidpvpqra tttyllaggg taghvnplla vadglrardp eaqilvlgtr egletrlvpe
       61 rgyellfvdk vpfprrpnaa aarfparfar avaqvrahlr drqvdvvvgf ggyasapayv
      121 aasrqrvpyv vheanakpgl anilgargar gagivfegtp lrgarvvgmp lrreivtlda
      181 asrrpgaaas fgldpdrpvl lvfggslgar rlnealaggw eavtdagwqi lhaagernel
      241 vdpqhpdyri vpyldrmdda favadaivsr agaatvseis algipavyvp yavgngeqal
      301 naasavraga arlipdaeft adrlrtevvp llqdgsalaq mrerasgvgt rrgtenviem
      361 idaaigr
//
LOCUS       WP_284529517             264 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Microbacterium
            sp. T2.11-28].
ACCESSION   WP_284529517
VERSION     WP_284529517.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..264
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=27512
     Region          5..240
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mtfrlraavf sdvgphrdan qdaafaaswg aavadgvggg pagdlasaal vhrlvaggsd
       61 vgdadelevr irganwdlga hvrrdptlag mattftclwl drhgglllah tgdsrayllr
      121 dghlirqtrd dsyvqvlvdq givsaadams hprrniitas lrgddtdhvr vvdrlpvegd
      181 rwllcsdgvs dylpddviad lvgmdvevda aaqlivsaal eagsrdnvta vvcdvergap
      241 gveepswaga aadrfagdls glag
//
LOCUS       WP_284529590             333 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease, partial [Microbacterium sp.
            T2.11-28].
ACCESSION   WP_284529590
VERSION     WP_284529590.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         <1..333
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          24..329
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 grreivlavg vaavllsvll slafgsrpvs aaevvegita wvrgetptdi galavqsrvp
       61 rtvlallaga alalsgalmq aitrnpladp gilgvntgaa lavvvgiafl gitsmwsylg
      121 lalagafvta lfvyfvgsvg pggttpikla lagaattaal sslvsaillp rqsvmdefrf
      181 wqvgnvgraa wetmavvtpv lilgavvail casalnalal gddlavglgv rvgrvriiaa
      241 itgvalcaav tavagpigfv glmvphvvrl lsgadqrwll plsalggavl lvladtvgrv
      301 igspgeveag iitaflgapv liviarrarm kal
//
LOCUS       WP_284529745             221 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Microbacterium sp. T2.11-28].
ACCESSION   WP_284529745
VERSION     WP_284529745.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..221
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=22897
     Region          1..209
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mhvclastsp arlmlmrqag iepsaraprv deeaviaeve aregrtlppg ehvlllarrk
       61 aadvvaalae depgfeglvv ggdsmfeldg evlgkpytpe aatarwhamr grtgtlhsgh
      121 svflvvpgaa pveahavada evtfaadvtd aeidayvatg epllvagaft vdslggafit
      181 rvvgdpstvv gmslstvrrl aaelgvpwtr lwnrggtapa s
//
LOCUS       WP_284530001             508 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Microbacterium sp.
            T2.11-28].
ACCESSION   WP_284530001
VERSION     WP_284530001.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19448763
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..508
                     /product="helix-turn-helix domain-containing protein"
                     /calculated_mol_wt=53500
     Region          <36..125
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          235..503
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 miqptlrall srrelqlrle sddaalapda ldaplrwvhs sdlldptpfl aeellllttg
       61 tqfapdagad vftgyvtrlr trgvrglgfg tevardgipr llseacaaag mplfevpyrt
      121 pfialarana eaiaaqayar rtwaldaqra islaalrpdg lgatvaelar qlgtwvgmfd
      181 aagvltqrhp idgigeqvla hltaevgsvl rrgvragstl dvdgarftlq tlgrgghlrg
      241 aiviaggdld legrgvvtsv iamaglaleq nvglgkarga lraglvhsll tgdptlarrv
      301 srelwgalps apivvavaev sharadaavd wlelavtenr gtlfhgrgpd glvvvvaaer
      361 ravldefael feaaagvsdp vgyagfadah aqavtarrrs apgraadfae vaaggilgql
      421 dtvearalae srlaplrehd rtqgtqllrt vrtwleqdar idaaaealgi hrhtvrarva
      481 qaqallgvdl tsfparaelw aalvtadr
//
LOCUS       WP_284530157             493 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Microbacterium sp. T2.11-28].
ACCESSION   WP_284530157
VERSION     WP_284530157.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..493
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50903
     Region          1..475
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mqrratvvgs gphglvaavt laragyavrv leaadapggg arsaeltlpg frhdvasavh
       61 patlaspwfr afgiadrvew ivpeasfghp lddapaaiaw rslertadgl gadgprwrrl
      121 fepvrdhlad vvevtsdtll rvprhplala rfgaraaglg tpsanallrt eagralwagv
      181 aahapsrmps lagagagall aahahaphgw plprggaqai tdalladlaa hggsvecgvr
      241 vddlaaldvg dprrgdllfl agsprlietl pdvpprylra vrrfrygpgv akvdaaldgp
      301 ipwrdealaa vptvhvggsa heirtaesqv lsgrmpsrpy vlltqpsvvd dtrapagaav
      361 lwayvhvpag sdldpteavl dqlerfapgv rdrmlairst saarlavqnp aaiggdglgg
      421 altvrnllrr pvvsgtpwrt pvrgvylass atppgpsvng magwhaarta igdagggrpg
      481 lsdlfpggda pea
//
LOCUS       WP_284530162             508 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Microbacterium sp. T2.11-28].
ACCESSION   WP_284530162
VERSION     WP_284530162.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..508
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=53259
     Region          142..476
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mstpppapdr rlrmsvrtri vavitlvaai glisvgatvy lveravslea iedrlqdnld
       61 sarfivgegp ddtgtwpsad ealravvqrm spddntgalg ivdgravlrs gvdldldlts
      121 apgfvahvss evtgadpvig tyaeegvvwr ylaapiavvg gdaatgaevi ftmaydvsae
      181 lgeingtaqa ylvaagiall viavvativs trllrplrrm retaervsaq slgerlpvqg
      241 rddvselast mndmldrldg aldsqrqlls dvghelktpi tivrgnlevm daddpddvre
      301 tqalaidele rmdrlvqdls aaaalhgpsp vttarvdage lvqqivrkaq giegaevdag
      361 piadvvarvd pgritqamlq lsqngvthgg grieigsrvv ddtlelwvrd hgpgvpdadk
      421 avvfdrfhrg stahagsglg lnivqviara hggsvrvdda pcggalfvis lplaetpqpd
      481 dlvipprppl pplpeprptt ltttggga
//
LOCUS       WP_284530444             200 aa            linear   BCT 25-DEC-2024
DEFINITION  peroxiredoxin family protein [Microbacterium sp. T2.11-28].
ACCESSION   WP_284530444
VERSION     WP_284530444.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Schroder,E. and Ponting,C.P.
  TITLE     Evidence that peroxiredoxins are novel members of the thioredoxin
            fold superfamily
  JOURNAL   Protein Sci 7 (11), 2465-2468 (1998)
   PUBMED   9828014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003123
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..200
                     /product="peroxiredoxin family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21227
     Region          59..199
                     /region_name="Bcp"
                     /note="Peroxiredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG1225"
                     /db_xref="CDD:440838"
ORIGIN      
        1 mnrktretvs apartrrqsp rsrtriwvta savtvgavlv gygiysaipe aapvdveaaa
       61 dftlpatdgs tvslsdlrge tvvlyfnega gcgsctaqma aieknpgfae kditvlpivm
      121 npaaqiqadm dafgvttpyl lddgtvseay dvlgrgmhag lpghgfvlid aegnerwrgd
      181 ypsmwldpee llhevqealg
//
LOCUS       WP_284530629             266 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Microbacterium sp.
            T2.11-28].
ACCESSION   WP_284530629
VERSION     WP_284530629.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. T2.11-28
  ORGANISM  Microbacterium sp. T2.11-28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Microbacterium sp. T2.11-28"
                     /db_xref="taxon:3041169"
     Protein         1..266
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28788
     Region          26..128
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 maddythghh esvlrvhrqr tagnsaayll pelrpgmtvl dvgagpgtis tdlaaivapg
       61 rvraidasad vvahaeadrv algienlsya vddayalsse dgawdvvhah qvlqhltrpv
      121 dalrefrrvv apggvvavrd vdyegtiwwp rvpgldewre vylaahrgts gdpaagrqlk
      181 awaraagfae vrssasiwlf esaearawwg gawadralhs sfadnvlrlg iadraaleri
      241 seawrewaas edgwllmphg evlarg
//
LOCUS       WP_284532115             467 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284532115
VERSION     WP_284532115.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..467
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48459
     Region          254..447
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 maslqlvhlt idhsehaiad lasqatalts aallassgll yfdarttdne vvawlaaavl
       61 llglaggasi tlerpgggap qgwpaiyqav livvalglva lsgrpryagh plglgvlggt
      121 tstlvaltll dtgllprlpp tlewlapatl alayaaltir lyhlsslpgw frvqlgltaa
      181 llgvsqvaaq ggsghllads vtivggvvga aclwsgcsvl lqramseteq alvdvrtrvh
      241 elegsfradr armhevdatl agiasaadll hdaphlppqr rrvlqamvrs esarlvrqla
      301 edrggpprpv pvdavleplv erqrlrgvdv awsptgival aepgdlgdal svllenavrh
      361 apgstvrvec rragspldpt veilvsdsga gvapevrarl fdwgargpqs pgqgiglyya
      421 aqlvnrhhge lrladtpagg atfmirisaa rrasdghlns aiastgt
//
LOCUS       WP_284532131             470 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284532131
VERSION     WP_284532131.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..470
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=50425
     Region          215..>353
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mqrvsrwwhg rreipalwfl rgyvvlllav paqlilrplg apgtlanmvg lggllwwcga
       61 riagltprsp spvrlllgva faavlvsyaa gslagwyaps nmrqgtddvw tlvfptvdqv
      121 hgamvaaadr gllsfaawlg ialltldglr swrdldllvr wlcwvsaaya ltgiyqfytg
      181 tnlasyvrvp glsanaavga sltrsvlerv sstathpief avflacvlpf alhlaiyrtr
      241 rrdvvpvimi gfamplavsr sgilaagval limfcywpsa rrrralmlap avvvllrlav
      301 pglvgtiysl faslatdpsv tgrtedygvv lalyrdqpwf grglftfvpg yyrildnqil
      361 mlllelgmvg llvvlllyvg asgsalgarr ravaardshv slaiaagivg mlvasvtfda
      421 wgfaqagglt fllfgmagaa srlsyedraa arvearaear pletagvrhg
//
LOCUS       WP_284532194             211 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284532194
VERSION     WP_284532194.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..211
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23275
     Region          13..204
                     /region_name="HAD_sEH-N_like"
                     /note="N-terminal lipase phosphatase domain of human
                     soluble epoxide hydrolase, Escherichia coli YihX/HAD4
                     alpha-D-glucose 1-phosphate phosphatase, and related
                     domains, may be inactive; cd02603"
                     /db_xref="CDD:319790"
     Site            order(17..21,118..119,151,175..176,179..180)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            146
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mtgerlrfat peavvfdlgn vlidwdpfpa iaagvgpdea rrfleaedfd fwawnlgpds
       61 gdtwadaeda vrrshphwle halayrthfl eslvgevpgt advvrdlhaa evrlfaltnw
      121 shelyphape nfdvlalfdd vvvsgtekia kpdprvfriv aersglpldr llfvddkqan
      181 vdaaaalgmq ailftdaaal rtelrshglp v
//
LOCUS       WP_284532229             394 aa            linear   BCT 25-DEC-2024
DEFINITION  saccharopine dehydrogenase family protein [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284532229
VERSION     WP_284532229.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..394
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42189
     Region          8..394
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 madareldpd ydivlfgatg ftgrltaeyl vrhapaglrw alagrnpekl eavrrhlati
       61 dpaagdlpll hadvtdpasl advaartrvv ittvgpylah geplvaacae agtdyvdltg
      121 epefvdrmyl ahhataertg arivhacgfd svphdlgvly tvqqlaatgp vrvrgvvrss
      181 gtfsggtfhs algqfsrarq mratmqerrr veprpegrrs rtsggkphrd pvlgywllpl
      241 ptidpiivar sgaalpsygp dftyshyagt ktlryaagga aavtamftsa qvpplrrlll
      301 grikqgdgpd errrskswft vdfvgegdgr tihtrvsggd pgydetakml aesalclald
      361 dnpptagqvt taqamgdnll arlqaagmrf etld
//
LOCUS       WP_284532445             263 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Nocardioides
            sp. T2.26MG-1].
ACCESSION   WP_284532445
VERSION     WP_284532445.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..263
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28536
     Region          4..257
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mapriglstv svypessaha fayaaslgyd tvevmvgida lsqqssaiqq lsrhhgvpvs
       61 avhapcllft qrvwgtepwg klersaemaa algaevvvvh ppfrwqktya rdfvdgiaal
      121 eessgiafav enmypwrass srgmemylpg wdpsdepyan ttidlshaai arsdpvamae
      181 rlgdrlrhih ltdgtgsakd ehlvpgrgsi gaeeflrhla rvgfageivv eintrkcrdt
      241 aeretdlres lefarehsav gap
//
LOCUS       WP_284532515             120 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284532515
VERSION     WP_284532515.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..120
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13091
     Region          10..110
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mvtvrelqld tvcpdtrllv ehvtskwgvl vlltlddrtl rwselkreia gvsekmliqt
       61 lqtleadglv rrealpvvpp hveysltahg rvatgllapl vhwaqrhvqd gaglssaqgg
//
LOCUS       WP_284532665             456 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284532665
VERSION     WP_284532665.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466432
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..456
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=50234
     Region          4..452
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 mslvdrhiqf lealrgagls vslaedldai ralralewdd ratvragyaa tlvkkqsqrp
       61 tfdalfdlyf prmvgdgaaa atreqdpegg vrdnaealsg frdqvvdala egdrqamvel
      121 aadmvarfga mpgrgpglss wsaytalqrv apaeltdriv aallaagrpe ddgrreaarr
      181 igsfttlvea darrriaeek gpdhvagvav rptidrldft aarkadleem rreiyplarr
      241 latrltqehh arrrgpldfr rtvrasmstg gvpmithhkp krphrtelvv lcdvsgsvan
      301 faqftlllvy alrdqfekvr aftfidhvhe vtpyftpgad padvmadlaa stahaalwgr
      361 tnygralakf evnhadalgp kssllilgda rsnysdlnld vlkrlagsar hawwlnpehr
      421 rhwdtgdsaa trygdivpmv ecrnltqlge lvhdil
//
LOCUS       WP_284532689             386 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284532689
VERSION     WP_284532689.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..386
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43075
     Region          130..376
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mfeyftgpky vwnlgvcatl nnggaidevd racrpareaa dvnsgsrifm qswkavadql
       61 adqaraseaa ghlrtagqqw yrsglyvcqa ermlsntdpg rrafyqqald afakvfeiad
      121 pattrvevpf egttlpayfs dasrdgepvp cvimwnglds tkehmytsgw pqemrargis
      181 vlmvdcpgsg ealrvqdlka rietegwata cvdyletrsd vdadriglaa wslggyyapr
      241 aaafekrikl vavwganhnw gevqkrrlqr egenpvphyw ehvlwvwgfd dvekfieyae
      301 gihldgvvdq itcpfliahg endrqipvay ahrsydqavh spkrelrvft veegaaehvg
      361 ldhmphinaf vadwvddtfa ellggs
//
LOCUS       WP_284532845             265 aa            linear   BCT 25-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284532845
VERSION     WP_284532845.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..265
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29958
     Region          1..259
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mrpqvvahrg asyenaehtl gayvaaldag adavecdvrl tadghlvcvh drdlrrtart
       61 rglistmela eldqldfasw knpwadldde apprderldr vltlrtllet vadyerpvev
      121 aietkhptry gglverrlve elrrfgwdrp gspvrvmsfs wtalqrlerl apgirlvllv
      181 ehahhwpfvs rligddwlvg pgidelmehp rlgrritrsg hdmhvwtvnt paelerclel
      241 gvkavitdrp ayvhdlldkr daasg
//
LOCUS       WP_284532946             331 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284532946
VERSION     WP_284532946.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 331)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18123688
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..331
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36504
     Region          12..215
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          237..311
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 miqlrlsaav lartrfaysp laeaakslyv vhsgtihplh rgwydrvrgd lrrtdsdllr
       61 avvppgghva eflfvgatsi ettiedqlhl vatwphahfl seleqawrgv gvtpaarrql
      121 edpdapqrva eelerywqrv lapywprfra lldadvayrl drlarggiga llsdlhpslq
      181 vtdealhirs vtdsdidgdg ltlvpcvfvw prlwvelgll gepsltygar gigtlwaerp
      241 aepdredalg ellgrsraei lmglrlprst tdlayevglt aptvsahlsi lrrsglvtsw
      301 rsgrrvlyqr talasmmvsa gadddqteas g
//
LOCUS       WP_284532961             255 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284532961
VERSION     WP_284532961.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..255
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27541
     Region          2..208
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mrdltypsvi laaktgfrll gqrfvmtgte hvprsggvll acnhigyvdf vygglaanps
       61 grlvrfmakr eifdhpvgga vmrsmhhiev drgeglasfh tavdylrage avgifpeati
      121 sramvlkefk tgavriaaaa gvpvlpvilw gtqrmltkdh prdlsrgkti airvgeplhp
      181 tgadpvaeta elksvmagll detirsypaa eqppgswwlp asygggaptl eeaarldsee
      241 rrrraerkaq kqpgr
//
LOCUS       WP_284532987             522 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284532987
VERSION     WP_284532987.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..522
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=56034
     Region          <213..>476
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 meqqpeekrp trkpldrdpa pprpssiatv egrvldpata isvkgvrprp tvyvgprlvv
       61 sksvdfegal avlravaepl gwvvvpered prtanlkfgv rpvridigsn ratiapdgwt
      121 llqqtraqfg veavrgvgle hvlasttvva npiemshpie mshpiemshp iemshpaaty
      181 glpgrggrqp vafigarprr capkelngrr rpvvavldtg cgehpwldgv vrtdvrlagt
      241 pigyvddatn pelhpdqngp mdgsidptsg hgtfiaglih qacpdadils wrvvpsegpl
      301 vesdwivaia qvlelvrrft agepggrrid vlslsmgyyh etpddhlfdp elqniltelg
      361 rlgtivvcsa gndatsrpsf paafapwegt ipprdvvpvv svgaqnpnlr tdalfsnagq
      421 wvrawapgaa lvstvppfeg gllplarttd degrvrecid pddfrggfav wsgtsfaapl
      481 lagrlaaala prlpkkaaep qpvatvvnra wkvveeltpi rr
//
LOCUS       WP_284533091             371 aa            linear   BCT 25-DEC-2024
DEFINITION  lipid II:glycine glycyltransferase FemX [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284533091
VERSION     WP_284533091.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Rohrer,S. and Berger-Bachi,B.
  TITLE     FemABX peptidyl transferases: a link between branched-chain cell
            wall peptide formation and beta-lactam resistance in gram-positive
            cocci
  JOURNAL   Antimicrob Agents Chemother 47 (3), 837-846 (2003)
   PUBMED   12604510
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Hegde,S.S. and Shrader,T.E.
  TITLE     FemABX family members are novel nonribosomal peptidyltransferases
            and important pathogen-specific drug targets
  JOURNAL   J Biol Chem 276 (10), 6998-7003 (2001)
   PUBMED   11083873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006395
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..371
                     /product="lipid II:glycine glycyltransferase FemX"
                     /EC_number="2.3.2.-"
                     /calculated_mol_wt=41248
     Region          1..370
                     /region_name="FmhB"
                     /note="Lipid II:glycine glycyltransferase (Peptidoglycan
                     interpeptide bridge formation enzyme) [Cell
                     wall/membrane/envelope biogenesis]; COG2348"
                     /db_xref="CDD:441916"
ORIGIN      
        1 msvreisend hlellrsqrs asflqtpawg rvksewrres igwfrgdelv gaalvlyrql
       61 pkvkrflayl pegpvidwea ddlgawlspm aahlsgrgaf gvrmgppvvt rrwdaatika
      121 giaddavrrl gdlppterth sgarvtsqll dlgwraqtve ggfaagqpqy vfqiplagrt
      181 eedvlagmnq lwrrnikkaa kegvevvsta sgdeelkafh elymhtaerd hftprplayf
      241 rtmvealgae dpdrirlyta rhegtlvaat igirvgahaw ysygasstek revrgsnaiq
      301 wqmirdaiaa gadvydlrgi tdtldeddph qgliqfkvgt ggeaveyvge wdlplnraly
      361 aafamymkrr a
//
LOCUS       WP_284533131             118 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284533131
VERSION     WP_284533131.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 118)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 118)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..118
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13240
     Region          1..88
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 madelsrvfq aladptrrdi varlaadgda tvgdlaapyd vsvqavskhl kvledaglvs
       61 rrrdaqrrpv hleaevldlm tkwieryrrq aeeryrrlde vlaslddesr preqgaas
//
LOCUS       WP_284533317             149 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284533317
VERSION     WP_284533317.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469162
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..149
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16620
     Region          23..51
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(24,27..28,31..32,34,58,61..62,65..66,68..69,92,
                     95..96,99..100,103)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          27..143
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          56..86
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          91..117
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mndfdqqmdl qappvvfpgq tgpesayrta fdllarrapr ealeviepal adepgnsglr
       61 mlrawaflmr aqlqraeael gdlveenpad dwvrhalgrc lerqsryaea lphlrlaatm
      121 sgdpehevav lrverrlaet getsfdrlv
//
LOCUS       WP_284533267             226 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284533267
VERSION     WP_284533267.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..226
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24358
     Region          5..223
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mtgptladap tqlpgnrrae vlallrqadq pmsvaevaes malhvntarf hldglvedgl
       61 aerttepret pgrprilyss egptvgprsy ellaemltgf vssledsgpg tvelgkawgr
      121 hlieraapse rvdadeavar ldrmldavgf rpdsratesg vevrlqrcpf reiaekhtdv
      181 vcaihlglmq galeeldapv vatslqpfvt phlcvarlqp rtepaa
//
LOCUS       WP_284533335             101 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Nocardioides
            sp. T2.26MG-1].
ACCESSION   WP_284533335
VERSION     WP_284533335.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..101
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=11190
     Region          2..98
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mpvvkinais vppqareele krfanrahtv dgtpgflgfq llrpvrgedr yfvvtqwede
       61 asfeawrdgd aveahagerr spvstgadll efevvldvpr a
//
LOCUS       WP_284533365             268 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284533365
VERSION     WP_284533365.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..268
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=27465
     Region          7..240
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mlrfsgagvs dvglvrsdne dsafvgpyva vvadgvggaa agevasataa yavsatvlar
       61 mgdepealll dgieaartsi rrgiqedlgr lgmattltav acdgrravla higdsrayls
      121 rdgaltrltt dhtyvqrlva aghlraeevs rhpwrnvvlr sldgdpvheg vdllplavvp
      181 gdrlllcsdg lsdlvpesai aelvtlddph saaavltraa laaggrdnvt avvldvvdgp
      241 mvvgdgqllg avrdisnivd pgavrtgr
//
LOCUS       WP_284533377             489 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284533377
VERSION     WP_284533377.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..489
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=53349
     Region          4..444
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 msgprvvvig agfgglgvah tlrqvgvtdv tvleraddvg gvwrdntypg aacdvpsply
       61 swswatnpdw grryspqpei ldyirrtaad dglrdlvrtg vevsaieydd atstwqvttd
      121 tgtltadlvi pavgqlskpv ipsipgastf tgpafhsaqw rhdvdltgkr vavvgtgasa
      181 iqfvpgivdr vgsitvfqrs apyvvpkpdq aysprhhrlf hrlpaipage rrfvywlter
      241 lngalagesp itrpmiaalr aawrlqlrrq ihdpelrrkl vpdypigckr llfsndwypa
      301 ldrdhvevvt dritgiepag vrtadgelhe vdvliwgtgf aateflagid vrgaggvslk
      361 evwadgarah lgltvpgfpn lfcvygpntn lggssiigmm eaqagwiaqv arrvadgaah
      421 rvavrrdvwe aydremqgrl gesvwaacds wyvdgtritt nwpglvteyk rrtatvdwse
      481 leevgattq
//
LOCUS       WP_284533439             321 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284533439
VERSION     WP_284533439.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..321
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32178
     Region          13..321
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mtslahdetl pvaadsrlvs glgfaivsaa sfgmsgalas elldtgwspg aivlvrvgla
       61 alvvvpfgiv alrgrwgllr rnvgvigvyg alavagaqfc yfsavahmqv gpallieyta
      121 paavvvwlwl rhgqrpggvt vlgaaiaaag lvlvldllsg adlsvagvlw alaamvgaaa
      181 yfvisadeqn glppmalaaa glvlgaaala ilalvgllpm rastgaatya gatvdwwvpl
      241 vvlgvvtaal ayttgiaagr rlgsrlasfv allevvagvl fawllldelp rtmqlvggll
      301 ilagvvavkl geratvgvpv p
//
LOCUS       WP_284533517             270 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Nocardioides
            sp. T2.26MG-1].
ACCESSION   WP_284533517
VERSION     WP_284533517.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..270
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28702
     Region          2..218
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkvlvtgaag sigrvvtvgl vdrghtvvgl drvpqpdgde gawytvdatd pdavaavfee
       61 epldavvhla ghpgeaslpd slashvittg alldamvehd vrrfvyassn havgrtprag
      121 ladgvlrvda rprpdtfygv gkvaaealms lyadryglda vacrigsfle rpetvrnlst
      181 wlshddcvrm vdaaltatap gfavlygisr ntrawwdlep gralgydpqd daerfldsiv
      241 agewdeahga hvggpyatae ferpaldrss
//
LOCUS       WP_284533560             127 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284533560
VERSION     WP_284533560.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..127
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13696
     Region          19..115
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mvdtrtcarp eggegscgai admlarlgdk wsllivaslg egplrfnelr rhvgeisqkm
       61 lsstlkvler dglvsrtvia tvppqveyal tdlgrelrvp vshlaewttv ntprilaara
      121 efdsrag
//
LOCUS       WP_284533791             826 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-glucosidase family protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284533791
VERSION     WP_284533791.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 826)
  AUTHORS   Varghese,J.N., Hrmova,M. and Fincher,G.B.
  TITLE     Three-dimensional structure of a barley beta-D-glucan exohydrolase,
            a family 3 glycosyl hydrolase
  JOURNAL   Structure 7 (2), 179-190 (1999)
   PUBMED   10368285
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444920
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..826
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..826
                     /product="beta-glucosidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0015926 - glucosidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=87581
     Region          19..428
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          <576..692
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
     Region          748..816
                     /region_name="Fn3-like"
                     /note="Fibronectin type III-like domain; pfam14310"
                     /db_xref="CDD:433860"
ORIGIN      
        1 mpsavpsaap dldalvarlt ldqkvrlltg adfwalydep aiglrrivts dgpagvrgel
       61 wderdpsvni psptalaasw dpelvetlgr llahearrkg vdvvlaptvn lhrspyggrh
      121 feclsedpll tgdlgaalvr glqsqgvaat vkhfvandse tdrltvdarv dertlrelyl
      181 apfetivrda gvwavmaayn slngttmtes pllrsvlhee wgfdgvtmtd wyagrstgpa
      241 argaldlmmp gptgpwrral veaveagdvt eaevdakvrr llllatrvga ladgpdpqpv
      301 dpwtdaasdq lvrraassgf vlvrnepvdg rpllpvdagg vrrvavigpn arearflggg
      361 salvfppatv splagllaaf gpdvevtycq garghervsa adpellttpd gergilvefr
      421 gaggevlgrd rrlgsafnwn nafegvdpal iteigletvv tadltgeyri gasgvgrfrl
      481 rlddrpafde llelgpgadp veglmrppqe watvslnage sirvslthvv kdhragedll
      541 vslqvavdct vedddaalah avadaaaadl aivvvgttee vesegfdrds lalpgrqdel
      601 vhrvararpe tlvvvnsgap vllpwrdeva avllawfpgq efggaladvv lgavepggrl
      661 pttwptaegp alasttpvdg rlpyaeglhv gyrrflcehv apaywlghgl gfttwsydav
      721 taasapdgga vvevsltntg drggrqlvqv ylsrpvstie rpvrwlagha wveaapgatv
      781 ratvevapra fehwdvaagg warepgtftv evgrsagdiv lrgelg
//
LOCUS       WP_284533453             227 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284533453
VERSION     WP_284533453.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 227)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..227
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23824
     Region          2..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mhdtdlaavg aligdpsrar mldslmggra laagelarva rvgpstaseh larllagglv
       61 evvaqgrhry yriagpavge alealshvap prpvttlres gharalgyar tcydhlagrc
      121 gvalhdallq hgwltdaydv tpagaaalag wgvdveaarg lrrsfarpcl dwterrphla
      181 galgaglgaa lvdrgwfepr spdsralrlt drgrdelvgl gcdltrp
//
LOCUS       WP_284533837             252 aa            linear   BCT 25-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284533837
VERSION     WP_284533837.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     BTLCP proteins: a novel family of bacterial transglutaminase-like
            cysteine proteinases
  JOURNAL   Trends Biochem Sci 29 (8), 392-395 (2004)
   PUBMED   15288868
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..252
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=27270
     Region          <9..156
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mdvevgkadr vpaamtptag phleatffld hgsasvrdft qrvvagassp rerasllfaa
       61 vrdrvwydpy svsrdpahyr asyvleagra ycvpkavlla avlraagipa rlgfadvrnh
      121 lqtdtlravm ggtdlfvyhg ycsvhldgrw lkatpafnve lcerfdvppv dfdgqsdalm
      181 haftsdgtrh meyvrdhgsf ddlpldrilt aldqtygrmt pragvaddaf aapadtgeat
      241 ehaavdpsvs sd
//
LOCUS       WP_284533853             557 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284533853
VERSION     WP_284533853.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19448763
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..557
                     /product="helix-turn-helix domain-containing protein"
                     /calculated_mol_wt=58879
     Region          27..117
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          237..548
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mttapssrpr aslgrvlddl gatlldlvhg dpdaghdigg vvihdpvdap vlpphalvlg
       61 vglddpdhva glladlgrqg asglvlrapv rltdrlrdaa dtsgvallal srgapwahla
      121 amlrsllaeg dvgvaepesl gglpsgdlfa vanaiaslld apitiedrss rvlafsgrqd
      181 eadpsrveti lgrqvperya rilsdrgvfr elhrsdrpif iepaeseeaf smprvavavr
      241 agdevlgsiw aavpgplsee rtdalresak lvalhllrvr agadvqrrlr adllssaleg
      301 gagarealer lglagqslmv lavavskada dddpaastdg aaaaherqrl sdafamhlsa
      361 vhprsaaalv gdvtyglvpm pggmedgeer avriahdfld rvgermrpvv gigpvaqdla
      421 glvharastd ravrvlrggr ggrrvarlad iqvealmlel rdlatargdr ptgplarlid
      481 ydqahrsflv etlrawldaf gdvaaaadal yvhpntfryr lrrvsevgei dltdpearfv
      541 amlqlrvlaa rsggdpv
//
LOCUS       WP_284533968             808 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284533968
VERSION     WP_284533968.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 808)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 808)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 808)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 808)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11905783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..808
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..808
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=84470
     Region          1..805
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
     Region          136..407
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 maqtglwlrw swrdlrrrwp vvtaialvia lgtgtyagll stsawrtqsn dasfallnth
       61 dlrvalpsgs tteegrlaav vaslehagdv aaarerlvvp tqiagpgdll vtgelvgtdt
      121 lpgaavdgvh vtrgralgaa ddgagavvad esfadknhlt vgseltvsgg arlevvgrgq
      181 speyfivtgg qgglpfltqk gygvlfaslh tvqraagadg qvndlvltlr pgadrarvaa
      241 elsraleiaq pplaadlttr ddidayrvly ddidgdeqlw rivallvlvg aafasmnltt
      301 rvveaqrrei gigmalgvpt wrlavrpllf gaqiavlgvl lglgvgwavs iplrdvfvgm
      361 iplpiwrtpl qadvfaqaav lglllpfvai awpvwrallv qpveairvgh laargsglap
      421 llsrlrvpgr gyrqipvrnv lrtprrtllt afgiasaitt lvttvglldt fgatldraea
      481 emlhtapdrv svaldtfqpl dgdvvrtveq lpevgsleag lripavadpd gegvdllvdv
      541 lpagarwqpt lvdgqpdggl llaeeaaadl gvgvgdavtv ehpqatatgl rtvrttmvva
      601 glhpnpmrvf ayldpaaada lglagtanvm svtpaegrsa ddvrrallev phvasaqtpq
      661 aaidgmrttl defvgilnva alitlllall iafnttsiav dersrehatm lafglpvrtv
      721 lgmtavetvi vgalgtlggi gggylvlrwm sattisdvlp evgvtaslsa ttvvgalllg
      781 iatvglaplf tlrrmrrtdi psalrvme
//
LOCUS       WP_284534025             542 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284534025
VERSION     WP_284534025.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..542
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=59624
     Region          172..>198
                     /region_name="LicD"
                     /note="LicD family; cl01378"
                     /db_xref="CDD:470175"
     Region          340..>491
                     /region_name="SmtA"
                     /note="SAM-dependent methyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG0500"
                     /db_xref="CDD:440266"
ORIGIN      
        1 mveaftesev rgwvsvpads pptevelrlg smtvsrttat pdgamsasrk nakgsptpsl
       61 pppkgdrrns rgqirtftfa isqlwdyapk gtplrvvvgs qvlpihghgm flraprsggq
      121 tprdlqkrfd eghllgrtgv vqiskrldev wqsavsslye stralfaeef gydlfitygt
      181 llgaireggf lahdndydts fvssattgpe aademvsiak vliakgyrvg amggglhvyh
      241 parpqhridi fhiyfdadgv lqhpfgyaga rqitsadwkg treiefvgrp alvpvcaeel
      301 latfygedwr lpktafiwsv ekrgndrtgv mtssrltevy wadyyahnvh adastfarfv
      361 qdrlgsaplt vidvgcgdgr dsiyfatqgr kvlgldragv aieharekaa qggldgarfe
      421 vcdladgarl aevlddavdr plifysrfvl havdvrtqaa lldaidaqar tgdlfvaefr
      481 tdkdeervkv hpkhyrryqs aaafladlre rgwvidydve sdglapwgde dpvlcraiar
      541 qp
//
LOCUS       WP_284534176             284 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284534176
VERSION     WP_284534176.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..284
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32103
     Region          1..139
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
     Region          160..284
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mrhtyrcplr wadldllghv nnvvyvdylq earvdmlrth gpaavtgela egvvvvrhev
       61 sylaplafgf epvtieswit eiraatftia yeifheqpdg errvyvrakt vltpyvfase
      121 rprrltqaer etlavflepd drapqaplat trpdvavhap vqvrfsdvda yghvnnvkyf
      181 eylqearill tadlwqgldp islvvaqtdv dyrvpilfrp epydawswas rvgqrsatie
      241 slildgetvl ararvaivff dprtersvvp peayldglrs llvs
//
LOCUS       WP_284534244             325 aa            linear   BCT 25-DEC-2024
DEFINITION  ribose-phosphate diphosphokinase [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284534244
VERSION     WP_284534244.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Sinha,S.C. and Smith,J.L.
  TITLE     The PRT protein family
  JOURNAL   Curr Opin Struct Biol 11 (6), 733-739 (2001)
   PUBMED   11751055
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Becker,M.A., Smith,P.R., Taylor,W., Mustafi,R. and Switzer,R.L.
  TITLE     The genetic and functional basis of purine nucleotide
            feedback-resistant phosphoribosylpyrophosphate synthetase
            superactivity
  JOURNAL   J Clin Invest 96 (5), 2133-2141 (1995)
   PUBMED   7593598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..325
                     /product="ribose-phosphate diphosphokinase"
                     /EC_number="2.7.6.1"
                     /GO_component="GO:0002189 - ribose phosphate
                     diphosphokinase complex [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004749 - ribose phosphate
                     diphosphokinase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0006015 - 5-phosphoribose 1-diphosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009156 - ribonucleoside monophosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009165 - nucleotide biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34498
     Region          1..310
                     /region_name="PrsA"
                     /note="Phosphoribosylpyrophosphate synthetase [Nucleotide
                     transport and metabolism]; COG0462"
                     /db_xref="CDD:440230"
ORIGIN      
        1 mreivvfsgs ahrslataic qglgvplssv eltrfsndcl qaqlqencrq rdvyivqpls
       61 pptqehlmel llmvdaarga saaqitavip yyayarsdkk dasrlsiggr lvadlldaag
      121 vdrvitmtlh apqvhaffsv pvdhltalgv ladhfqgadp attvvvspdf gnaktasqfa
      181 rllglpvaag skkrladdqv vidaivgdva grkaivldde iatggsivel ldrlaeqgct
      241 eaavacthgl fvgkaierlr ehpmitevvt tdtvpppadw pelqvrsiad lfaqaierih
      301 agesvsslfd gvdpslgppq prlfd
//
LOCUS       WP_284534403             834 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284534403
VERSION     WP_284534403.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..834
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=83043
     Region          <2..703
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mnssgikrgl avsavsalav agipalassa saaagdtitv vstgparngg dlgadvvlrv
       61 kdgtvaagdl altatnsdav gsqnngsqna tidgvsgpvn dpadnayefl tvsievttaa
      121 dgdtaafrii dndgavagsl easearanvs vttagaaskl vvapatqsap qglesgayta
      181 tvqdsagrtt qllvgesiav tsdadvtvne sgnaitadei sggtdtftvt paaaaalgnh
      241 titlagpgtv dttatvnvtk satldanmvd ivtgadswdg fgggnfgapn tlvrvdqgtv
      301 kidikggaan anstvsltat gggltfggkg sttvatvlda sgngsltitp dagtiqdgdt
      361 iaiggsfpet lefdratvsd vvptadlyfs kvggstdvtv kvvdqfglpv tsgfvtaart
      421 gvnaaadatp qkkavgadgs ttftftdtka tdgttedvnv nyyadqfsat pdfsevgvat
      481 ikyttdgmga nfvtsldgnn teaadynagk tvvvpladtk addeagines adlvlttgge
      541 pgaamtisvd ngalilepgk tllsegkpsv tvtldgggll pagyriagtk sgvvtatlsa
      601 anrtetaalt vapetdvsta rnvtvsgpae vesgttqipf vavitdgfgn pvqgvpvwdl
      661 niqvtgpaqf qdsdartdan gqihlnvrvd agavgdvtik vdgmyeqfga aadqlyagsa
      721 ansakglpas aaeatatttv kaappvvtql pinlklsgrg akidkihana nnraaglkav
      781 lfkngkrvks hvlsasgdwt fkvkdtngmr ktkytvkvrp taatlgatks irik
//
LOCUS       WP_284534417             265 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284534417
VERSION     WP_284534417.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..265
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26420
     Region          20..262
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mtpalpaval vtlgvlglli gsflnvvihr vpaglslvsp gsacpacahp vrprdnvpvl
       61 swlvlrgrcr dcaapiaary plveltsgll fagvgwrfgs tpyaaaalvv aaagvalfvi
      121 dldhrrlpfa itgamavgtv ialaidtarh gaepvvpall aaglwlavyg giwlltagrg
      181 mglgdvalap vlglalgwlg wgpavvglgs gfvvgavvgi alllsgrara gsqvphgpfl
      241 lsgaaigmla geplaaaylr lvglg
//
LOCUS       WP_284534540             126 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284534540
VERSION     WP_284534540.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..126
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13738
     Region          3..111
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 makrprsgpy vcgidaaldv vsgkwkglvl welhahgvrr faelrrgipg vsekmlaqhl
       61 remeadglvq rrvyaevppk veysltdaga slnralgplg ewgrerlrrd gldttaasge
      121 patehv
//
LOCUS       WP_284534555              99 aa            linear   BCT 25-DEC-2024
DEFINITION  GroES family chaperonin [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284534555
VERSION     WP_284534555.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Hayer-Hartl,M., Bracher,A. and Hartl,F.U.
  TITLE     The GroEL-GroES Chaperonin Machine: A Nano-Cage for Protein Folding
  JOURNAL   Trends Biochem Sci 41 (1), 62-76 (2016)
   PUBMED   26422689
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Horwich,A.L., Farr,G.W. and Fenton,W.A.
  TITLE     GroEL-GroES-mediated protein folding
  JOURNAL   Chem Rev 106 (5), 1917-1930 (2006)
   PUBMED   16683761
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Levy-Rimler,G., Bell,R.E., Ben-Tal,N. and Azem,A.
  TITLE     Type I chaperonins: not all are created equal
  JOURNAL   FEBS Lett 529 (1), 1-5 (2002)
   PUBMED   12354603
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Fenton,W.A., Weissman,J.S. and Horwich,A.L.
  TITLE     Putting a lid on protein folding: structure and function of the
            co-chaperonin, GroES
  JOURNAL   Chem Biol 3 (3), 157-161 (1996)
   PUBMED   8807841
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11277705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..99
                     /product="GroES family chaperonin"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0044183 - protein folding chaperone
                     [Evidence IEA]"
                     /GO_function="GO:0051082 - unfolded protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=10654
     Region          1..85
                     /region_name="Cpn10"
                     /note="Chaperonin 10 Kd subunit; smart00883"
                     /db_xref="CDD:197951"
     Site            order(2,5,37..38,50,60,65,67,83..85)
                     /site_type="other"
                     /note="oligomerisation interface [polypeptide binding]"
                     /db_xref="CDD:238197"
     Site            16..29
                     /site_type="active"
                     /note="mobile loop [active]"
                     /db_xref="CDD:238197"
ORIGIN      
        1 mlhdrllvev dresgerrss ggivipataa mgarrlvwsk vvavgpnars vevgdrvlfe
       61 pedkaeveva gelyvvmrer dvhavaaerv gdqatglyl
//
LOCUS       WP_284534669             365 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284534669
VERSION     WP_284534669.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..365
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39793
     Region          9..343
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mtvidddlrp lngvrvidls llipgpwats mlaelgadvl hveppggdpl qammpgayri
       61 vgrgkkavrl dlksdggrrr lldlleesdv lvegfrpgtl qrlgfsldqi masfprlivc
      121 slngygsdga yrdrpghdln ylaasgllsv sgepsgrpyp gggvpladla gslfatqgil
      181 aalllrqqtg agsrlvvpla aaalklsepr maeyderggp akaelmsrga ydvfrcrdgs
      241 wlavacmedr fwrglcqvlg redwldreey ssyggrcrha erlngdlade faradrdewv
      301 drcvaadlpv navldfteis ddvhmrrwld rvpnggarsv rlpytllpar ptptthdsgr
      361 srwpt
//
LOCUS       WP_284534760             528 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284534760
VERSION     WP_284534760.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..528
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59272
     Region          2..527
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 misrrtvvgg alaslgvmst palaaaarpp llempmaarr rlrdpftlgv asgdpepdgv
       61 vlwtrlapqp lawdglggmp srevlvdwqv aedpgltrvv rggrvravpr fahavhvevd
      121 glqpgreyfy rfraeghlsg vgrtrtapay asspssltva aascaqyehg yftayrrlae
      181 etpdlvlhlg dylyemrnda yvayphnvrs vagpetvsla ayrqrhaqyk tdpdlqaaha
      241 aapwsvvfdd hevdgnwagl hqehrrrsdp sfrqrrasaf rayyenmplr rtslphgprm
      301 riyrrlqwgd latvhlldtr qyrddqvsrg hsrsarrarl dprrsitgdr qeqwllqglg
      361 dsdarwdvla qqvffaqrdr srrpglqvgm dgwdgyaasr hrilegfehr gvrnpvvltg
      421 dvhrhyandl rldfdrpstr pvgvelvtts itsggdgqdr sgemraerav nphirfasgr
      481 rgyvlarfer erlyadfktv pyvrrpgapv rtaasfvved rnpglqpa
//
LOCUS       WP_284534761             385 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284534761
VERSION     WP_284534761.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..385
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40956
     Region          1..383
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mtdgplsdlv vldltralag phaammlgdm garvikiepp agddtrgwgp pfvgaddere
       61 styflsanrn keslvldlks edgkqvlarl veradvlmen frvgvmdrlg fsaerlheln
      121 pglvllsitg fghdgpeatr agydqiaqge gglmsvtgts qptkvgvpia dlvagmngaf
      181 gvlaalhert rtgrgrvvrt sllagmvgvh afqgtrwtva revpglagdh hpsiapygmf
      241 atatapvqia cgseslwral caafgwdpee payatnalrv anrdgliari ealfadgpae
      301 qwlarlaeag vpsgkvrsmd dvysweqtls qglllsvdhp tqgelklpgs pirfddnpfs
      361 ggrsehlapp tlgqhdaair ewles
//
LOCUS       WP_284534797             487 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284534797
VERSION     WP_284534797.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..487
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51673
     Region          33..291
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mnrppyavre agavclvlvv glmllaphyg phrdelyfve agkhlawgyp dqpaftpfla
       61 rltdlvapss vtvlripsvl amvgvvllsv qaarllgaar agqaltavav glstivpglg
      121 hllstatfdm lfwtavlvvv gqalvddrpr lwllagavag vglnnkhava fcllgvlvgv
      181 alvretrpal gtrwpwlggl lalamwvpnl gwqaqhdwpv falsadiade yggvggritm
      241 vlealvifsp ligavwvlgl vqllrrpdwv rarplavafl vvlavflvtg gkgyylagai
      301 ppliaagcth laatrssrav vragawmvas aavaypavlp vlpastfggs fyadvndvql
      361 etigweeytd qvravvdalp pderrtavvf tgnygeagsl swygvgvpvy sghngyrewg
      421 pppasaapvi vvgwrdptad fdgctraatl dndadapnee qglpvwrcss vrgswterwg
      481 elshyda
//
LOCUS       WP_284534802             416 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284534802
VERSION     WP_284534802.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..416
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=46251
     Region          134..404
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mtitstrsts grwpgldaap tglrtevssr varrlfthav daldvtvhvg eetlgrggpa
       61 mtvhrpdelf arlgreglig fgeayltgaw taedltgflt vlaanvgdli pqrlqrarsl
      121 vqrrtprahr ttqdrtreli ahhydlsndl fglfldesls yssalfdgdl deallpaqhr
      181 kidrlldrag vragtrvlei gtgwgelair aaargatvht vtlsseqlal aerraaeagl
      241 adrvsielcd yrevrgeyda vlsvemveav gheywptyfr tidrllapgg raaiqailmp
      301 hdrmlatrgs ytwinkyifp ggflpsaqvi devterhtsl rvtdrlafgg dyaetlrrwd
      361 etflaaeddv rrlgfdetfv rmwhfylcys ragfasgyld vqqltlerpa svmitp
//
LOCUS       WP_284534811             191 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284534811
VERSION     WP_284534811.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..191
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=20060
     Region          9..190
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 maapevprvv vvdhhdsytw nlvhlvaavt gvlpvvvqhd evsaddvlgf shvvlspgpg
       61 hpdvvedfav grevlrratr pvlgvclglq glvttyggav grvdpahgdv avvehdgrgv
      121 faglppsfra vryhslaala vppclevsaw segvvmgvrh rtlplegvqf hpesilsehg
      181 arlvanflgv p
//
LOCUS       WP_284534872             409 aa            linear   BCT 25-DEC-2024
DEFINITION  fatty acid desaturase family protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284534872
VERSION     WP_284534872.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..409
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46373
     Region          26..362
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mtaiqkkpvs piehltpedi eqlgveldti rqdildsrge kdakyirtvi dvqrrlelgs
       61 ravllfssfp pawvvgtagl svakilenme ighnilhgqw dwmrdpkihs ttwewdmatp
      121 aeqwkhshne lhhtytnvig kdndlgygim rvdedqpwhp fflvqplwnf inacffeygi
      181 aaydlelgat ikkkqtkdpd fkrrvkgvlt kirrqatkdy vvhpalsipt gsflptlaan
      241 ftanvvrnlw shsvimcghf pegvetfekr siegesrgew yvrqmlgsan isgskamhim
      301 sgnlshqieh hlfpdlpsnr yaeiaprvka lfekydlnyh eaplpkqvys awhkvvrlsl
      361 pngwlattna knapqqlaml ykmstggpkv rraaqarlnq larktsaaa
//
LOCUS       WP_284534930             629 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284534930
VERSION     WP_284534930.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..629
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65302
     Region          62..613
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 msrtvhtrll paaaaltsla llvaagassa tatrehrpda katytqltka spakggakkd
       61 yvkvdllain dfhgqlepvp atsssgrinn tpaggaayla rllkqerars raagaapltv
      121 aagdligatp llsgafhdep tikamnllgl qvasvgnhef degwrelrrm qnggclddgp
      181 dganganscp gdqgfggadf rylaanvkwa dgqahardtl fpatkimkvk gqkvafigmt
      241 legtpdivta agvqglafad evktanalvp klrkrgirsi vvllhegvkp adttayndcs
      301 gvsgpaleia qklspaidav vsghthqayn clvkdpkgqp rlltsamsig rmltkihlli
      361 dptthdvvrp aeyadnliaq ngadvtpvpa vqslidtyka lvapienqvv ghiepgtsvs
      421 rtadadggds plgnliadaq vadgstveag asgrtavepv ialmnpggir adllenaagd
      481 vtygatftvq pfnnymvsmd ltgaqikall nqqwngtnea srkilqvsgl syawdtseaa
      541 avdadalvpg svmvdadgdp atpmvpidda atyrvvannf lygggdgfst ftestngyfg
      601 gldidalvky lqehdpvaas atdritqvp
//
LOCUS       WP_284534997             439 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284534997
VERSION     WP_284534997.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..439
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46852
     Region          20..196
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mrdqwrrrls relrrlrtgw rgavlwslri tmaavisyvv atlifpgtqp llapltamlv
       61 vqvtpvslla sgldrvvavv tgvslavafa avvplewwsl gllilisitl gqalrlrdnl
      121 ievaisgmlv lgvgslgaga aagqriaetl vgagigvaan llfpprvpts dagreiegla
      181 daisavlrrs adaleqltgd rgsvaaaaga wlgdarrith hdvprvgaal lhaeqgrrln
      241 vravgtpdlg pglrhglesl ehtaltvrsm yraladateg dpewleaega mdvllglalt
      301 frdladavda fgelvrleaa pagqadsadf ealresiqgl pearsrlegm taavadphlg
      361 elhgtilstv krvqreldle qrvrrqlqlr rpvrtwpapl rphpsrrrga alpdpgaeid
      421 ldaettalpr lsdddlder
//
LOCUS       WP_284535034             521 aa            linear   BCT 25-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284535034
VERSION     WP_284535034.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..521
                     /product="long-chain-fatty-acid--CoA ligase"
                     /EC_number="6.2.1.3"
                     /GO_function="GO:0004467 - long-chain fatty acid-CoA
                     ligase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56332
     Region          6..520
                     /region_name="FC-FACS_FadD_like"
                     /note="Prokaryotic long-chain fatty acid CoA synthetases
                     similar to Escherichia coli FadD; cd05936"
                     /db_xref="CDD:341259"
     Site            order(176,179..184,186..187)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(179,299..300,321..326,408,420,423,434,514)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(179,221..222,269,271..272,275,299..300,321..326,408,
                     420,423,431..434,495)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(221,271..272,275,299,431..433,489,495)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mttynlatll edgaasypdr taivlgdtrl syaevdtfan mvanllvsrg irpgdkvalt
       61 cpnlpyftvv yfgilkagat vvplnvllkg revgyhlads dakayfcfqg tpelpmgeag
      121 hagfnategc ehffvitagl gdpspiegve tmaqamggqp gtfetvatde ddtavilyts
      181 gttgqpkgae lrhrnmrdna llgeplfgae aakpdtylcv lplfhsfgqt vcqngafayg
      241 gtvvmlprfe ahaalelmlk eritffagvp tmywgllgal edgvdvsalr dnlrvavagg
      301 salpvevhke fekrfgitil egyglsetsp vasfsrygqp arpgsiglpv pgvemklidp
      361 rwqevegpge hgeigeiaik ghnvmkgyyn rpeateeviq dgwfrsgdla rrdedgwyyi
      421 vdrskdmiir ggynvyprei eevllthpav slaavigvpd eshgeeikav vikapgaeit
      481 eaelvawgke qmaaykyprh vefvdslpmt stgkilkrel s
//
LOCUS       WP_284535047             256 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284535047
VERSION     WP_284535047.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..256
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25902
     Region          <96..253
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mrrrsflalp plvglgtlaa cgsdgerpms aaaqriaygg dpaqygeltq pagtargvav
       61 vvhggfwkpa ygieyarplv pglaaagwav waveyrrgtg aadtladvra avdarpevdg
      121 pvvgighsag ghlatwaaag gglthvvsqa gvldlraahg lglgdgavea flghppgpad
      181 dgadpirqvp lgvpvwcvhg raddvvpisq srayvaaara agataelvev egdhfvvidp
      241 dstawartle ildalv
//
LOCUS       WP_284535094             120 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284535094
VERSION     WP_284535094.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..120
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13183
     Region          25..117
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msdetpktip pragrpvrgs rtgrpvmall dllgrrwtlr llwelhtags spltfraiqg
       61 rcedmsssvl sdrlgelrqa qliehdrggy rlsalgaelv glllpldawa trwggretnp
//
LOCUS       WP_284535105             214 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284535105
VERSION     WP_284535105.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..214
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23102
     Region          1..214
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 msraperggr ervlavlrga rqpmsiveia rrldvhantv rfhldtlteq grverveatn
       61 tgpgrppllf ritpgmdpag prnyemlagi lveglarepd adaraerfgd twgrglvasp
      121 pasqtpgeat dtlvamlddl gfaaerrggg trleiglrhc pflelsshrt dvvcplhlgl
      181 mrgvmgqlas gvsveslepy vepdlcltrl vlnp
//
LOCUS       WP_284535107             271 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284535107
VERSION     WP_284535107.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..271
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=28989
     Region          3..271
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mtamfryrap rrrdellell aeygerarvl aggtdllgdv rsglarpaav vdvklvpgfg
       61 elawsaaegl virpgvtidd vlrderarss ypllaacaqd lashqirnra tvvgnvvnas
      121 pcadmapall clgaraviss qdsrrevpft efftgakrtv lragelleei vvpaqsagar
      181 gsyrklkrik ghdlgivgva amakdgelrl gisscaptpl lvdglttrdp vdevvavara
      241 aispisdvrc tkeyrthmvg vyvrrameev a
//
LOCUS       WP_284535137             333 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284535137
VERSION     WP_284535137.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..333
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36453
     Region          23..314
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mpeqatettp pepmsvpeaa dlarrvldev eravvgkrda lmqvlaavla kghvlledyp
       61 glgktlaars lartlgidfa raqftpdllp adltgsfiyd qrrgefefrr gplftgllla
      121 deinrtppkt qaalleamqe rqitvegetf rlpepfhvla tanpieyegt fplpeaqldr
      181 fllrvsfgyp tphqeydvla rrmarrqeev dldvvtdgpg llamqaavet vvvdesvgry
      241 cvdlavatrh hpdvltgasp rgslglvlaa rafallrgrd yvvpedvkav arpvlahrit
      301 vkpelwmsda sgrrvvdavl gqvptpatrd alr
//
LOCUS       WP_284535160             212 aa            linear   BCT 25-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284535160
VERSION     WP_284535160.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Niehaus,T.D., Elbadawi-Sidhu,M., de Crecy-Lagard,V., Fiehn,O. and
            Hanson,A.D.
  TITLE     Discovery of a widespread prokaryotic 5-oxoprolinase that was
            hiding in plain sight
  JOURNAL   J Biol Chem 292 (39), 16360-16367 (2017)
   PUBMED   28830929
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Fan,C., Li,Z., Yin,H. and Xiang,S.
  TITLE     Structure and function of allophanate hydrolase
  JOURNAL   J Biol Chem 288 (29), 21422-21432 (2013)
   PUBMED   23754281
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Wang,L., Grau,R., Perego,M. and Hoch,J.A.
  TITLE     A novel histidine kinase inhibitor regulating development in
            Bacillus subtilis
  JOURNAL   Genes Dev 11 (19), 2569-2579 (1997)
   PUBMED   9334321
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005226
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..212
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=21542
     Region          1..200
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 mpvqlrpfgp tavlaevggp aaalalatwa rasgvaavei vpaaetvlfd gvddvatlaa
       61 tleswsptdp vppgdlvelp vtydgpdlef vaeawrtdva gvvrrhgeve yvasfcgfap
      121 gfaylaglpa elavprlasp raqvpagsvg lagvwcgvyp saspggwrli grtdarlwdp
      181 agdppallap gtrvrfrdas slgsstpgfg as
//
LOCUS       WP_284535216              67 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284535216
VERSION     WP_284535216.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 67)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..67
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7195
     Region          <9..59
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mgsasrpslk tleqdglvrr daeavipprv hysltdrghe vsallvplad wafqnadaiv
       61 ndqpsrs
//
LOCUS       WP_284535236             106 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284535236
VERSION     WP_284535236.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..106
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11660
     Region          6..67
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 malvvplpqd pflntedacg ylgvpkatll twrvrrpgyg pravkaggrl kyrlseldrw
       61 lrdheesfal dddnegadsa sdggrevrtr nranrvrgga lrtaqp
//
LOCUS       WP_284535286             264 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284535286
VERSION     WP_284535286.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..264
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27705
     Region          1..264
                     /region_name="COG4587"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443644"
ORIGIN      
        1 mrtyarlfva gfrrqstyrl aalgglvant tfgllkvall faavdaaggq lsgydvgams
       61 ayiwisqgll gsinlfgrtd mavrirsgdv avdflrpvdv hlatiatevg rsvfallprg
      121 lpsvaigafv vgmslpddpa ayvlgalsiv lgivvsattv ylvaatgfwl vetrgveily
      181 mvvsgffagl fvpirlfpdw lhaaatatpf psmmmypvdv isgrvdgaes aglvglqvfw
      241 lattiaagql atragrrrle vqgg
//
LOCUS       WP_284535382             344 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284535382
VERSION     WP_284535382.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..344
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36660
     Region          10..310
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 msgqsprspa evfsalarac edlgidawdw ygeggavrrl eddlverfgv eaaaffpsgv
       61 maqqaalrvh cdragslrva mpdlshllvh eedgprvlhd leilfltrgf evptaahvaa
      121 lpgrlgavlv elplrdagcl lptwdelrel sgacrergva lhvdgariwe aqpwfdhsfa
      181 eiaaqadsty vsfykglggl agaallgsad vvaearrwrr rlggttyrvt aeavaalvgl
      241 rdrlplipqt vawaqafaaa lpatitvqpg rpqtnqflly aagdadavne rtveaieahg
      301 vglpawwsar epgrvqtevv vtpaalgldl aamaaqlaqv ilad
//
LOCUS       WP_284535325             295 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284535325
VERSION     WP_284535325.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..295
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32648
     Region          8..286
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mtgeavraae elvalldler idadlfrgsq pdsararvyg gqvaaqalia girtadpaya
       61 vhslhsyflr ggdysvpivy dvertregrs fqtrrvvarq hgrpiyyqsl dlqraedgye
      121 hqdvmpevrp peegidlvev mrrggnadad algkewgald vrwlgnsrrg iepdpahpsr
      181 armwvrlkdg lgddpvvhla aftyasdvsl lgstlaahkv npssiqmasl dhtiwfhrpf
      241 radewwlydq espvaggarg lafgrvftqd gtlvatvaqe glirprndvs erppr
//
LOCUS       WP_284535487             367 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284535487
VERSION     WP_284535487.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..367
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=39015
     Region          9..359
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mrtaicdtfg idypifaftp sehvaaavsr agglgvlgcv rfndtdeler tlswlddntd
       61 gkpygvdivm pmkiptegts vdlksmipee hisfvertlq rlgvpplpeg egrdgvlgwl
      121 hsvarshldv alnhrpvlia nalgsppvdv iekchehgvl vaalagaakh arshvangvd
      181 iivaqgyeag ghtgeiasmv lqpdivdavg pdvpvlgagg igsgrqiaas lalgsqgvwt
      241 gsiwlgtaey qnlqsnagwt eaftratssd tvrtriytgk parllktkwt eawaeteape
      301 plpmplqnll vadahnrina sgdpdvismp igqivgrmne vrpvadvmad lvaefeqtvt
      361 rleairk
//
LOCUS       WP_284535639             267 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284535639
VERSION     WP_284535639.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..267
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28689
     Region          7..267
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 matlieitda adprladyrd lrdvelrkhl eaehglflae gakvvrrsle agftprsflm
       61 aarwldgldd vlsrsdapcy vvsealaeev tgfhvhrgal aslerrplps vdsvltsars
      121 vlvledivdh tnvgaifrsg aalgfdavll aprcadplyr rsvkvamgav favpwtrlpd
      181 wydalpllsa agfttvaltl apdavpieea vagldrvalv mgseghglsp hweqtadrra
      241 iipmregids lnvaaatava cyvtarr
//
LOCUS       WP_284535698             295 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284535698
VERSION     WP_284535698.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..295
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=31084
     Region          14..290
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mdrliqrlrh lddwargwgw asliangalv vtggvvrltg sglgcptwpr ctedsltphg
       61 aydihsvief gnrmltwvlv vvavgtfvaa wqsgrrdlrr ialvmalgip aqaviggitv
      121 ltdlnpwvvs lhmlcsmaiv alavfflerl drpapavppr gatlglawat fgaawavfyi
      181 gtvvtgagph agdsaskrng lsalqmsqlh adfvflfvgl tigllfaava tgapastrrv
      241 ivlllaievg qgtigfvqyf tdlpvvlvgf hmlgsaltsg avawalvrvr epaaa
//
LOCUS       WP_284535652             456 aa            linear   BCT 25-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284535652
VERSION     WP_284535652.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..456
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=48307
     Region          2..456
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 msaetytvin pataapvtdv hlasvaetdt aiegahgafp awkamppger atllrrfaav
       61 vdahveelae levrnaghtw gnarweagnv rdclnyyaga perlfgrqip vpggvdvtfr
      121 eplgvvgviv pwnfpmpiag wgfapalaag ntvvlkpael tpltairlge laleaglseh
      181 vltvipgkgs vvgerfvthp lvrkvcftgs tevgkrimag cadqvkrvtl elggkssniv
      241 fadadidaaa asapyavfdn agqdccarsr ilversvyde flaklqpave glrvldpgde
      301 ssemgplisa hqratvtgyl devevvfags tpggsvsegf wvppsvvtvd dpatriwree
      361 vfgpvvavmp fddeadavak andteyglsg siftrdlgrg lrvargveag nlsvnshssv
      421 rywtpfggyk qsglgrelgp dapmafteek nvfish
//
LOCUS       WP_284535762             841 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284535762
VERSION     WP_284535762.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 841)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 841)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..841
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..841
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=93274
     Region          3..832
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtdlldeita aatargltly phqeeailav lagdnvvlat ptgsgkslva aaahraalae
       61 drvsfytapi kalvsekffa lveefgaadv gmltgdasvn peapiiccta evlanialre
      121 gsaadvglvv mdefhfyaep drgwawqvpl lelpqaqfvl msatlgdmse iaadltrrng
      181 rettvvddav rpvpltfswv mtplietlee lvttgqgpvy vvhftqkdav eqatsllnag
      241 waaapreqrd llaerlagvr fgagfgktla kllrrgigvh hagmlpryrr lveqlaqagl
      301 lriicgtdtl gvginvpirt vlfsglakfd gsrqrvlrtr eflqiagrag ragfdtagyv
      361 vvqapehvie nekakakvaa rqaagkknsr aqlrkppegt vvwseqtfdk lvagepeplv
      421 srmkvdnsml invlardeda fpvlrrllmd nhedrrqqlr larravrlar sllrsgtltr
      481 laepdelgrr yvltvdlppd falnqplahf alaaldvldp eaetytldiv svveavlegp
      541 rqilfqqqhv argeaiaemk adgleyderm alleeitwpq plaelleaty eiyrerhpwl
      601 redalqpksi vremyeqgms ftdfvgryql arseglvlry ltdayrtlrq tvpdqhhtpe
      661 lgdliewlge tvrqtdssll dewealadpt hvrsdvahhe ppppprpisk qdrafrvmir
      721 namfrrvelv arddldglma meraaadrte ppvevvmtrs awdaaieeyy aehdrvllds
      781 dargpsllqv eeagrtwrvt qtlhdpeghh dwvveaevdl dasdeagelv lrttsmrrlg
      841 g
//
LOCUS       WP_284535903             489 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284535903
VERSION     WP_284535903.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..489
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=51706
     Region          160..488
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mirtawqrvr dalasltsrl vvttvllvll vsvligtatt favrsyltdq ldqdvhdaar
       61 ryafevtggp agvapdagtr iriagdgppg tlnaiwtsag easgqvgtqr stgeistkal
      121 pqktltalgn lrtneaatid vpgvgsyrve vvalsesvsi aaglptsdvd aavanviwwe
      181 vllallavta aggaalivvr rqlrplreva atahsvselp lesghidite rvpdhltdar
      241 tevgqvgaal ntllahvets laarhrseqq vrqfvadash elrsplatia gytelarrrp
      301 ddtagartal dkveeesdrm talvedllll arldagrple qapvdltrll leavsdarvv
      361 apdhrwrldv pddavdapye vtgdelrlhq vvtnllsnar rytpagttvt vtvrrdgfav
      421 hddgpgfppg lvehaferfa rgdaartrtg evgvglglal vqaivtahgg svrlssspgd
      481 ttldvrlpg
//
LOCUS       WP_284535906             280 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284535906
VERSION     WP_284535906.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 280)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..280
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29613
     Region          3..268
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mktledkvcv vtgagsgigr alalnlagrg allalsdvdd aglaatvdqv raaggrevrs
       61 dhldvadrda fasyaasvad hfgrvnvvvn nagvalagnl edleyadmdw iigvnfwgvv
      121 hgtkeflphl ihsgdghlvn isslfglvsm pgqsmynask yavrgmseav reemliaghp
      181 vgvtvvhpgg iktaiarnar vsaredkekt aklfdeklak mtperaaeii vrgilhnrar
      241 vlvgldahav hhlakltgsr yqdivaragk rvlpdhttvv
//
LOCUS       WP_284536003             519 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284536003
VERSION     WP_284536003.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..519
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56600
     Region          8..505
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mtdlgqplpr rtflragavs vagglalgaa sgslrpaaaa aglvsrrlel psgvatgdvt
       61 srgavlwars sdvgrlvadv rsgrttrrvr gpwatpdtdh takivldglt pgrdhdvrls
      121 fedehgrtge aqvasfttag trggatsfvw tgdscgqgwg inpdlggmvg yrtmhrtrpd
      181 fflhsgdtvy adgpiaatvt epdgqvwrnv vaegvdkvae eldefrgrhr ytrldanyra
      241 faaevpiigq wddhethnnw ypgqiltder yterrvdvla ararqawqey lpiagspsrg
      301 riyrkvergr hldvfcldmr tykdpntagt eaepthilgq eqtdwlirev rrsratwkvi
      361 aadlplglvv pdgpvnqesl anrdpgaplg keleiagvls afkrhgirnv vwltadvhyc
      421 aahhydpara gftdfdpfwe fvagpiaagt fgpndldatf gpevvftkha atpnesprrg
      481 nqffghvaid ddgrmtvslr dlsgavlfsq dlepqaerv
//
LOCUS       WP_284536177             253 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284536177
VERSION     WP_284536177.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..253
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=25975
     Region          6..250
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mdqvelhhga atdvgrvrqv nedaylaepp vfvvadgmgg heggdvasai vveefarlaa
       61 tgydphrgae avtdtldrca driaeyaaaq raagvargrs agttavvall veddhgaawl
      121 lanlgdsriy ryadgrlvqv svdhslvqel vdagqldpde aathpernvi tralgdasga
      181 rpdffelpva gaerlllcsd gvsgmvddvg latilgacad pedaaerlva aaveaggedn
      241 atavvvdvvg gmp
//
LOCUS       WP_284536203             284 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284536203
VERSION     WP_284536203.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..284
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=29378
     Region          3..284
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mipaafdyva pasvedalaa laehgddaki iaggqsllpv lrmrlnapem iidlgriesl
       61 rgvrddgdai vigamtphav vgsdplvaeh aslitkaveh ladaqirhrg tfggalahad
      121 pagdlgapal vlgaefviqg aggtrrvaad dffvdlfeta igedeiltev ripkhtgwga
      181 hyekfvrvah qwpivavaat vrvdggaiae arvgltnmgs tplrargvee alvgqpated
      241 avraaaarst egtnppsdln gdadyrrhla tvvtrravla aagg
//
LOCUS       WP_284536217             224 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284536217
VERSION     WP_284536217.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..224
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23877
     Region          21..222
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mknnplgprp grgprpltag raavlqllvd qptpprlaal aqtsglhpnt lrehlealva
       61 dgwvrrvrse pqgrgrpawr yeavddrghd eyaglatala asiaatspap tetarfageq
      121 wgrtlatdrg tdprtpeear aevvsmldel gfepevdadr pervrltrcp lldaahrypg
      181 vvcevhrgiv sgalasygvd pagtdlvpfa epgacllaip pttr
//
LOCUS       WP_284536303             598 aa            linear   BCT 25-DEC-2024
DEFINITION  Kelch repeat-containing protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284536303
VERSION     WP_284536303.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Shi,X., Xiang,S., Cao,J., Zhu,H., Yang,B., He,Q. and Ying,M.
  TITLE     Kelch-like proteins: Physiological functions and relationships with
            diseases
  JOURNAL   Pharmacol Res 148, 104404 (2019)
   PUBMED   31442578
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Gupta,V.A. and Beggs,A.H.
  TITLE     Kelch proteins: emerging roles in skeletal muscle development and
            diseases
  JOURNAL   Skelet Muscle 4, 11 (2014)
   PUBMED   24959344
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 598)
  AUTHORS   Adams,J., Kelso,R. and Cooley,L.
  TITLE     The kelch repeat superfamily of proteins: propellers of cell
            function
  JOURNAL   Trends Cell Biol 10 (1), 17-24 (2000)
   PUBMED   10603472
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..598
                     /product="Kelch repeat-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=62865
     Region          2..295
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          14..62
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          68..157
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          160..204
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          206..248
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
ORIGIN      
        1 mgswrqlaal petrweaaav fhggkvyllg gqrffsggss syqntmfiyd pagntwtagp
       61 plpatgpaya fstaadgihl vfpvtgahya idpadpvpvw avrtsapapt llraahftda
      121 sgrfylaggt lvgsgsslkv nrydpttngw taradlpanf dtgsttsegv lggdnkvylg
      181 gstaglavyd patdtwsttt apptggfgts agqvsrlpsg ivlsvgrrty sgllsrvdgy
      241 npatgtwtag vtpdfpasis dmsitaepgg qiyllggtvd satttestaq awaykqnepp
      301 tvatlltmts galvstastn rarhqfndpn agdsqskfdw ryrkvgdptw ttgtvispnp
      361 whdipagtlt pgnyerqilt ydaagepapa ftasgfftaa tppagpsity pingqtldqa
      421 ervdwsipaq dsyqvrrvad dgagapnpav iyydtlevvd tltrslplnf avngrtehvq
      481 vrvkdgglws dwvsvsgdvs ytpppaptft aypdptdgsl lvmianpdpt gaepaaaynd
      541 iyiteplpsg vvteerrvte hpantpwryr vpvgswdysg arirvvavaa ngttsssi
//
LOCUS       WP_284536437             781 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284536437
VERSION     WP_284536437.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 781)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 781)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 781)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 781)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..781
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..781
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=81388
     Region          14..754
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtqqttasdt vndielaivg mtcascaari ekklnkldgv tatvnyatek akvsyptnls
       61 pddlvtvvea tgytatvpar apsgdegvat tepddrdrea agwwqrlvvs avltvpvlam
      121 smipalqfdn wqwisltlas pvvvwgawpf hraavtnarh gaatmdtlis vgvtaawlws
      181 lwallfthag mtgmrmpfdl fpdgeadvhi ylevaaavtt fiiagryfea rakrqsgaal
      241 ralldmgakd vavlrdgaev rvpvsqlavg drfivrpgek vatdgvvedg tsavdasmlt
      301 gepvpvevgp gdsvvgatvn aggrlvvrat rvgadtqlaq marlvedaqn gkaevqrlad
      361 rvsavfvpiv ialslatlag wllsghsvta aftaavavli iacpcalgla tptallvgtg
      421 rgaqlgvlik gpevlestrv vdtivldktg tvttgrmelv evvpadgvdp adllrlvgal
      481 enasehpigq aiatgasqrv drqlpdvegf tstqglgvag vvdghavvag rpswlagews
      541 qpldahltqv idtaeqqgrt viaagwdgsa rgvvvvsdai kptsaqavae lkelglepvl
      601 ltgdneraar avaaevgiae viaevlpadk vavverlqre grtvamvgdg vndaaalats
      661 hlgiamgtgt dvaieasdlt lvrgdlraav dairlsrrtl rtikgnlfwa faynvaalpl
      721 aalgllnpli agaamafssv fvvsnslrlr rfqavstqst etphldhdst rtnpskveag
      781 r
//
LOCUS       WP_284536439             207 aa            linear   BCT 25-DEC-2024
DEFINITION  peroxiredoxin family protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284536439
VERSION     WP_284536439.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Schroder,E. and Ponting,C.P.
  TITLE     Evidence that peroxiredoxins are novel members of the thioredoxin
            fold superfamily
  JOURNAL   Protein Sci 7 (11), 2465-2468 (1998)
   PUBMED   9828014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003123
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..207
                     /product="peroxiredoxin family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22508
     Region          64..206
                     /region_name="Bcp"
                     /note="Peroxiredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG1225"
                     /db_xref="CDD:440838"
ORIGIN      
        1 mshkaaeqsr nerrqraeqa arasgrrrrl rimigtasal alvaavtamm ltsrpessda
       61 irtapeftlt dtggsehtla qhrgenvlly fsegagcqsc ivqmgeiekq aaafeklevt
      121 vlpivmntre qitadmtang vttpfllddg tvseaygtlg kgmhaglpgh sfvlidrqgr
      181 qrwygeypsm wlapqdllde vrsnlsa
//
LOCUS       WP_284536529             142 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284536529
VERSION     WP_284536529.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..142
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15595
     Region          45..102
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 metvketliv gghrmlaaqs eripddagad pdelrlterg rpaltpatmn iaqaaayigi
       61 akstlytwrt rrpgfgprav kaggalryrr sdldawieah aetldlqaet diddegrrsg
      121 sdqqptsrtl gsmsrrsrpr hr
//
LOCUS       WP_284536635             362 aa            linear   BCT 25-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284536635
VERSION     WP_284536635.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Rengstl,B., Oster,U., Stengel,A. and Nickelsen,J.
  TITLE     An intermediate membrane subfraction in cyanobacteria is involved
            in an assembly network for Photosystem II biogenesis
  JOURNAL   J Biol Chem 286 (24), 21944-21951 (2011)
   PUBMED   21531723
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Komenda,J., Nickelsen,J., Tichy,M., Prasil,O., Eichacker,L.A. and
            Nixon,P.J.
  TITLE     The cyanobacterial homologue of HCF136/YCF48 is a component of an
            early photosystem II assembly complex and is important for both the
            efficient assembly and repair of photosystem II in Synechocystis
            sp. PCC 6803
  JOURNAL   J Biol Chem 283 (33), 22390-22399 (2008)
   PUBMED   18550538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..362
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=39467
     Region          104..295
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          284..>353
                     /region_name="Sortilin-Vps10"
                     /note="Sortilin, neurotensin receptor 3; pfam15902"
                     /db_xref="CDD:464929"
ORIGIN      
        1 madrtllivg trkglwlgts deartdweft gphcdmeevy sclvdtrsdp prllagasss
       61 wlgpqirrsd dlgatwqetp ggairfpega datvervwql tpgvedgvvy agtepgavwr
      121 stdrgetfel eqglwdhphr pqwgagfggq afhtvlphpt dpqsvtvais tggvyqtsdg
      181 gaswaprnqg iraeflpegq qypefgqcvh kitrhpsrpe rlflqnhggv yrsddhggsw
      241 tyiadglpsd fgfaivvhpq epdtvfvfpn gsgdgryppg gkarvwrsrd agetweelgn
      301 glpdsfyvav mrdamcadgh drtglyfgar ngavwgsade geswrqivcd lpdvmvvraa
      361 ai
//
LOCUS       WP_284536676             353 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284536676
VERSION     WP_284536676.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..353
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35345
     Region          44..349
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 malllcaqpt staaaagser atsrrglaav vallgllala llaslmwgar eiapgqvwaa
       61 lvdpvsgdad hhvvrdlrvp rtliglvgga algaagalmq gvtrnpiadp gllginsgas
      121 lavlvaisal gvtsvsgyvw fafagaavaa vvvygaaslg wegvtpvkla lvgaaftata
      181 tsvitvvllt dqralddyrf wqvgslanrp igvltavlpf valglvlala agrvlnalal
      241 gddvarglgq dvvrgrllvv aavvllcgsa vsmvgpiafv glavphlarv lvgpdyrwiv
      301 vlsmllgpvl lltadiagrl varpgeleag lvvavvgapv llaivrrsrg iaa
//
LOCUS       WP_284536704             204 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284536704
VERSION     WP_284536704.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..204
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21029
     Region          10..200
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(29..30,32..33,36..37,74,78..79,82..83,107,110..111,
                     116,139,143..144,146..148,150..151,154..155,158..159,
                     177..179,181..183,185..186,188..189,193,196..197)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(142,146,149..150,152..153,188,191..192,194..199,202)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(163..170,176,179..180,183)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 msnpllvgvy qpgtsllhrl pvgaklgglg vlsltivavr daraavvfla vavalalvgr
       61 iglrmlartt rsvlliavia gavqwwvsgp akavetlldl vslalaaiav sattpvnail
      121 dslvrwispl rrigvdpdrv amtiglavqa lpgtvalale trdaarargl grhprayltp
      181 fvirvvarah etgdalaarg vgdd
//
LOCUS       WP_284536746             252 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284536746
VERSION     WP_284536746.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..252
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27221
     Region          10..228
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mtvrklqqrr gwawnlavpi ikplllattt rewiggenip esggfilaln hvshvdplta
       61 ahivydhgrl prylaksglf ksragawfft aagqipverl tknavgayda aveavrrgec
      121 vvvypegtit rdpggwpmtg ksgaariala tgcpvipvgq wgaqqllapy tkkpdlfprk
      181 kitmkvgtpv dlsdlvdqpr tgavvqqatd rimaaitalv edvrgetapa erfdmkkagv
      241 rqignpnkkd ra
//
LOCUS       WP_284536757             174 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284536757
VERSION     WP_284536757.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..174
                     /product="YceD family protein"
                     /calculated_mol_wt=18979
     Region          2..171
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mldtrelgrr pgsqreekrt vpapadlgie vlrvpegspv dldlrleavm egvlvtgsas
       61 aelagecarc lepiadeidv rfqelfvydd qdysseeddg vsmlegdlld lepllrdavv
      121 lalpfqplce ddcpglcpec garlaedpgh thdaaidprw gklqqlqqdt dpqq
//
LOCUS       WP_284536941             157 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284536941
VERSION     WP_284536941.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..157
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=16233
     Region          54..157
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mteptttprr lpvppvavlg aaaaaqhvls rrhghigaar glagaalalt aggfiagsvr
       61 efrraqttvn pvapdratsl vtggphqlsr npmyvgmagl lvahavargn waavlpalgf
      121 vavidrvqip aeegamaelf grdyaeyaar vprwlgf
//
LOCUS       WP_284536991             453 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284536991
VERSION     WP_284536991.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 453)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..453
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=48122
     Region          4..446
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 mtglfyllgv vifvvailas iglhelghmi pakkfggkvt qyfigfgptv wskrvgetey
       61 gvkaiplggy vkivgmlppg adqladevtv daegnqvvkv rksntgmftq lisdaraaew
      121 etiqpedsdr lfykmtwwkk vvvmaggptv nlliafaifw gifglygeht vepdagapvi
      181 egvsqcvlpy aeegrdctas dppspaaaag lrpgdvitsf ngapitgwdq lrtlirgndd
      241 gqavigyerd gqqltgttst tvearptset dqtlrqvgfl gvtptshevv tkggpiytae
      301 qmghmtvttv kalgtlpvkv wgvakaivgv eersidspvs ivgggriage tvshqdfpvv
      361 ektvyllgli agfnffigmf nfvpllpldg ghiagalwea lrrgfarlrg rpdpgyadva
      421 kllpiaygva aclmlmgvvl ivgdlvvplh las
//
LOCUS       WP_284537027             171 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284537027
VERSION     WP_284537027.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..171
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18863
     Region          21..127
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mavqtippri rwavdimdvq psdhvleigc gpgagaelic erletgklfa idrsesgvdr
       61 tkrrcarfve sgrltvrqid latlrvpvkr lnkvfsfnvn lfwvrsctee vallhervvp
      121 ggevflfyea nrpelvptiv kkasaalteg gfrvsvvdqk appvigiigr r
//
LOCUS       WP_284537031             130 aa            linear   BCT 25-DEC-2024
DEFINITION  VOC family protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284537031
VERSION     WP_284537031.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..130
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13430
     Region          10..124
                     /region_name="PhnB"
                     /note="Zn-dependent glyoxalase, PhnB family [Energy
                     production and conversion]; COG2764"
                     /db_xref="CDD:442048"
ORIGIN      
        1 mkvnataisl nvadvdasas fatthlgftq amaadgfvsl ahpsagvnvv flrtglstfk
       61 pegiagpagq glllalevdd ldtefarisg agarvvtppe tepwgerycq faddngivwq
      121 lvqwvaapge
//
LOCUS       WP_284537112             335 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Nocardioides sp. T2.26MG-1].
ACCESSION   WP_284537112
VERSION     WP_284537112.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..335
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34925
     Region          1..332
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 midlrsdtlt kptgdmraam aradvgddvy gedptvarle ervagllghe aalftptgsm
       61 anmlavrslv gpgqevlcea sahiaraelg ahgaytgltm rtwihprgqv dldairtifa
      121 pdmgpffvpt aaisventhn faggavlplq dlrdlreyat gvgvrvhvdg ariwnahvat
      181 gtplaeygai advmsvclsk glgapvgslm agsadaiaea riwrkrmggg mrqvgilaaa
      241 glhaldhhld rladdhahar llaeacgvdp atvdtnivvv rrsdasdfva aareegvlvs
      301 avgptavrlv thldvsrdda ekaaavlgrl agahq
//
LOCUS       WP_284537128             253 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nocardioides sp.
            T2.26MG-1].
ACCESSION   WP_284537128
VERSION     WP_284537128.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. T2.26MG-1
  ORGANISM  Nocardioides sp. T2.26MG-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Nocardioides sp. T2.26MG-1"
                     /db_xref="taxon:3041166"
     Protein         1..253
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26041
     Region          <41..139
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mphersserp serpserrsa artsvvwdal rpalegvamd vldigggtgg favrvaelgh
       61 rvtvvdpspd alaalgrrar elgvavtgqq gdlstlldvt gpaaadvvlc hgvlevvddp
      121 aaalatlrqv lrpggtlsll vgqrhaavva ramaghfaqa lalldptdas gvrdagtgrs
      181 grrftdtevt glleaagfrv davhgirvfa dlvpgslldl epgstaalvd lecavserpe
      241 frplaaqlhv lag
//
LOCUS       WP_284537305             325 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284537305
VERSION     WP_284537305.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..325
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34281
     Region          3..325
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(41..42,46,123,127,130,148,151..153,172..173,177,192,
                     216..217,238..242,263..266,313,315)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(135,231..232,245..250,258..265,268..269)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mvkaiviret ggpdvmsfed vevgapgpge vrlkhtaigv nfidtyyrkg lypapgglpf
       61 ipgaeavgiv ekagegvaqf rpgdrvayag svgayseari isaqklvrvp ddidgftvaa
      121 sllkgmtvqy llrqtfqvtr dhtvlfhaga ggvgqiagqw lkslgatsia tvsseekaei
      181 aracgythvi nyrtedfvar vaeitggakc dvvydsvgkd tfpasldclk prglfvsfgn
      241 asgpvsefnl gilsqkgsly vtrptlghyt atratldacs gdlfeqirne vltisvgqkf
      301 tlanavachk amearetvgs tlltv
//
LOCUS       WP_284537311             272 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284537311
VERSION     WP_284537311.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..272
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=30465
     Region          20..258
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 matkdewset rldidatage afvvdvdgfe gpldllltla rnqkvdlari silaladqyl
       61 afierlgerr lelaadylvm aawlaylksr lmlppdetpg depsaeelag mlamrlkrle
      121 girilagrlv drsrlgrdvl prgapeemgl vrrslweasl fdlldaygrq rqrdmvrvht
      181 vrkrqvwala dardllerli gaipdwapie dylirymtgp esratvrasa fsaslelvre
      241 grmelmqsap faplymrkgk gvagvpdeeg dq
//
LOCUS       WP_284537354             736 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284537354
VERSION     WP_284537354.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 736)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..736
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=82611
     Region          1..736
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mmrqyelver vqrynpncde gllnrayvya mqkhgtqkrd sgdpyfshpl evaailtdlk
       61 vddativial lhdtiedtda trqeidqlfg veigqlvegl tklqkldlvs krtaqaenlr
      121 klllaiaedl rvllvkladr lhnmrtlhfa peskrgriae etmeiyapla grmgmqdmrd
      181 elediafktl hpdafsaiqa rldemealqk dliadiekel renlevrgiv atvkgrrkqp
      241 ysifrkmidk qlgfeqlsdi ygfrvlvddv dtcyralgvv hqlwrtvpgr fkdyistpkp
      301 ngykslhttv vgphrqrvel qfrthdmqqv neygiaahal ykdkisesgh lpqladdtaa
      361 yawlrqtvea lsegaspeef lentklelfq dqvfcftpkg llialprgat pidfayavht
      421 nigntcvgck ingritplvt elkngdevei irskaqvppp twetiavtgk araairratr
      481 eatrkqfasl grqvletvfs regreltdtl leqalprlsq ptvpdllaav graevpstdv
      541 lkacfpdyre eraarqtatq rqeggwfsfa aqagikfhgd sdsirahglp irtvaadlpv
      601 rfapdggavp gdrivgivep dvgitiypiq spalvvfedk pdrwldvrwd idsedpirfp
      661 arisiqsfne pgslariaka isdsdgnidn igmarrtpdf heivvdlevw dikhltqiln
      721 elrvlpnvsk vervng
//
LOCUS       WP_284537494             199 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284537494
VERSION     WP_284537494.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..199
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=21457
     Region          <9..174
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mfpdgcrdvl ilrgpegtrd vvltefdfgp rpaklrpgte ivgyrlrpga dvsrrvveav
       61 aanpdlveai lgeacggwnd lddaiaaltl pgatvaavsr dlgvsirtmq rhflsrslpp
      121 pdfwrllars rqaarlldva splaevaaec gfsdqahmtr dfmrwfgltp aqvrgsapll
      181 nvlsqpalgn wtgeqistr
//
LOCUS       WP_284537589             927 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284537589
VERSION     WP_284537589.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..927
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..927
                     /product="class I SAM-dependent DNA methyltransferase"
                     /calculated_mol_wt=103881
     Region          20..915
                     /region_name="YeeA"
                     /note="Type II restriction/modification system,
                     endonuclease and methylase domains [Defense mechanisms];
                     COG1002"
                     /db_xref="CDD:440626"
ORIGIN      
        1 mnpveieeai salaeqpfda eefpyaflea fgnkettlrr lrkgesnksd lggvlqtnni
       61 hiatckpgdv trtlgalkas paterakarf vlatdgdlfe aedrttddap isctysdfpn
      121 hfgfflplag ittvkqvres sfdiratsrl nrlyvellkd npewgtaqrr hdvnhfmarl
      181 ifcffaedte ifdssaafts aietmsakds snthevisel framntkaea haaagvprwa
      241 grfpyvnggl fsgstdvprf sriarsyllh igsldwkkin pdifgsmiqa vadddergal
      301 gmhytsvpni lkvlnplfld dlsekldeag dnarmllnlr krmskirvfd pacgsgnflv
      361 iaykemraie aeinrrrdea drrseipltn frgielrdfp aeiarlalii aeyqcdvlyr
      421 gqkealrdfl pldaqnwitc gnalrldwls icpptgtgvk hhaddlfhtp lnqaqidfen
      481 eggetyicgn ppykgsqgqt ddqksdlkai fdsrtanwks ldyvsgwfmk aadygtktta
      541 asafvstnsi cqgrqvdtlw slifatmhei afahtsfkwa nlashnagvt vvivgiardl
      601 pafrrlystg greetilrel eninpylvgg pnimvqpspk plsdlndmsf gnmpneggyl
      661 llnqaeaeea varhgvrrcf irpflgsqef irgqerrciw vtdaeyaeak kndwladrfe
      721 svraqraasn rsttkqlakv pyrfgevrqr gdetaivvps vssetreylp vgylppgali
      781 snlafalyda pvwnmalias rlhlmwiatv cgkmktdfry sntlgwntfp vptlteknka
      841 dlthcaedil ltreahfpat iadlydpdam padlreaher ndevleriyi grrfkndter
      901 leklfelytk mtanpnktsk arqgtsa
//
LOCUS       WP_284537594             422 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284537594
VERSION     WP_284537594.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..422
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=46869
     Region          10..351
                     /region_name="PolY"
                     /note="Y-family of DNA polymerases; cd00424"
                     /db_xref="CDD:176453"
     Site            order(13..14,17..18,53,56,110..111,164)
                     /site_type="active"
                     /db_xref="CDD:176453"
     Site            order(108,111,195..201,231,253..258,285,313..317,319)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176453"
ORIGIN      
        1 mrqpetierl yldfdgffas veqaanrklr grpvgvvpye gggdramlia vsreaknagi
       61 tslmsvgeal akccdlvtvp qkpdlyrrah nallseieti ipidtaksid eltcvlaedg
      121 rqhpedlawr vkttirdhvt pvitstigfa anrqlskmac kagkrsrgsy gdgmavwhpk
      181 dmpaplfkvg lddipgvgsr lafrlkgmgi ytaedlynlq pkhmrkiwrs vvgermwyal
      241 hgydiqapts qrgmfghgrv lppesrtrtg akdisrlllt kaarrlrres yyagalslwl
      301 slregswfrq lplpvvhddq ailsalallw qafdsehper lsvfrigvtl leltpanerq
      361 ldflladdtr rkcweaasva vdalnakyag tvvslgtwkp pkggnvggki sytrvptsed
      421 fw
//
LOCUS       WP_284537651             202 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284537651
VERSION     WP_284537651.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..202
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21142
     Region          2..185
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 mivvldnyds fvgnvarylv elgeevtvlr ndalavadla tlgaealvis pgpcgpgeag
       61 istdavrmls gqlpilgicl ghqcigeafg grtvrarepm hgrsspithd rtglfsglpn
      121 plrvgryhsl avevpagtpl rvtarseggd vmaiehadhp tfgvqfhpes vlteggyrvf
      181 anflsclpgr agrhaaipps pf
//
LOCUS       WP_284537707             269 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284537707
VERSION     WP_284537707.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 269)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 269)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14398439
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..269
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30149
     Region          29..122
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          <159..264
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mprnvadtpf fepspvsyii dparpllirs qtliagrivr phahprgqya wakkgvlriv
       61 sdhcvwivpp thavwipggt rhqvvsetpa evrhvfvdps ravrtgsqrp drcavlavtp
      121 lmreltlrle tllveeldea rrlrfcdvmi deldrlaeap lslpggrdpr lvrltrhlge
      181 hpedrrplae lasfvgastr tlerlfvaet gltyrrwrar lrllaaierl ergesateva
      241 ltlgfsspsa ftasfreafg epprtflqg
//
LOCUS       WP_284537842             829 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284537842
VERSION     WP_284537842.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 829)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 829)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20158983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..829
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..829
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=89085
     Region          106..>402
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          286..700
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
     Region          710..>792
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mstpatlsvr vrlqsalail alltcfagai awitleggqn rlktlntgtl aevddalrls
       61 sdaadlatrm pfllaldspf rvhqegehil glianienrp dlqpgiaadl mrmrlavfdl
      121 lsatqsrsal ldrilrlnae vareerrlal lsatggqsld esgewltlqr vasallgagr
      181 aenliglgef qrefygltrr lppvatesgr eardrlaafa egddglfelr rrelahrvaa
      241 analvririg aeivssyaaa vtataqkeia seltstttmi svakstilvv mligtaialf
      301 taqfvaryvt anlsaiadgm mrlaagdrts slprsygksd eigkllrafr vfranairld
      361 rahrqrirqt alletmvrgm sdgvavfasg ggitaandrl aevldlplss ltgpidldrl
      421 lrakgwrsta taagyaeltd pegrtierrd ralpaggava lfsdaterrq lqdrmqqiqr
      481 ieglakisge vahdfgnils tisssmhmle aaspergrel rrsvasavev gtsltqrlla
      541 farrqhlepe lielnelveg ltdliyltlr eniglsvqpa dedlvvrvda gqlesaiini
      601 clnaaqaipg sghitialap sedghailti edtglgmtpn vlahamepff saradgkgtg
      661 lglamvygfi rqsngdvqie sqegvgttvr lilprsepaa glpapslpwr sillveddpa
      721 darqsldlls kagatvqlcs tadaafdcla gerrfeavit dlhlgtetag wqvaeqalnr
      781 dpdvvvfvvs ghlpeispfg nrygnrlrls dkpltldtls descsqlkh
//
LOCUS       WP_284538150             504 aa            linear   BCT 25-DEC-2024
DEFINITION  FGGY-family carbohydrate kinase [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284538150
VERSION     WP_284538150.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..504
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=52742
     Region          2..448
                     /region_name="ASKHA_NBD_FGGY_FK"
                     /note="nucleotide-binding domain (NBD) of L-fuculokinase
                     (FK) and similar proteins; cd07773"
                     /db_xref="CDD:466793"
ORIGIN      
        1 msllgidvgt tgckavvfda agrplatarr eyalanpheg fweldpeqvw qqvlsairei
       61 taiaganvta laisalgeav lpvdrdgvpl aggaisadlr aaaeidelrd nlgaatiyai
      121 tgqpatayys lpkmmwwrrn apdlyahtyk facfgdyvlm rlglestida tmaartlayd
      181 inrndwsevm leaagidadk lptvvvsgss igrlgrrgaa ltglsadvev vaggfdqaca
      241 alaagvvaeg sgfyglgtte alalamrhpn palsrlnvav iphavpgvll gmsgsqtggr
      301 llrwcrdelc aeerlaatar gidaydlmla gltadpgplm ilphfagsgs ldsdadalga
      361 ilglsfdtrr adivkavleg vtyeqalsll hldaegvspa rlavvgggar sdlwmqikad
      421 iigrplvrqe ifdasclgaa llagiatgvy aspqaavdav krpasvfkpd errhalhqrr
      481 laaygrlhad laelnallra ttva
//
LOCUS       WP_284538238             257 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284538238
VERSION     WP_284538238.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..257
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26712
     Region          2..240
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mmerpslraa lagarplrvg wsclpdplaa etmaragfea vlidlqhgvi dmgvapamla
       61 airaagdyal aripvgeyqs asrlldwgae mvvapmietv edarafvsfm kyppdgqrsy
      121 gparavqlsg lsadayrtsa ngstlavvmi etrsalanld ailavpgidg vfvgpydlsi
      181 alspdgepgl drpdtiaame rvvrqakaan kvcgafgana alvrrylglg ftfatlstdm
      241 dliaaatkaa iaevegs
//
LOCUS       WP_284538260             373 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284538260
VERSION     WP_284538260.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..373
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39835
     Region          2..371
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mgrtgqfsrl dtvvdnaigr tivganilik lkgelvysrq agfldreadr pmrsrtlfrl
       61 asvskpmvsv aalamveagk frlddpvthy lpdfrprlad gsaptitish lmthtsglsy
      121 dldigngkpa sggtgpsdfd laenvarisa lplafppgtg wrysvaidvl gavmeaaegr
      181 slqeivkayv tdplgmadta frpldpsrla vayadgtppt rmgeiervkd gegfvefwsg
      241 rafdetafps ggagmigsae dfltfleamr kggapilsaa smallteart vdldpapsgq
      301 gyshgwsiyr dpslqkmpck pgtwawggiy gnqwyvdpet gltivsftnt avegcngafp
      361 kdifravyad lgh
//
LOCUS       WP_284538334            1256 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284538334
VERSION     WP_284538334.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 1256)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 1256)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1256
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..1256
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=134065
     Region          761..1026
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
ORIGIN      
        1 mrirssvrhv avaaalclat igapdmtmaq attpqttaep vnvdfrsgpd fgrmvltfpn
       61 lnllpphkvt sdsgvlviqf dqpvslnaea avtrlanyvl ivrtdpdglg vrmalarsvk
      121 vnvmeagpql fvdflpatwk gepprlpdev vaalamkade makaaaaaqk liaetekpir
      181 vdvtaakapt fsrlnfkwnv pfdvdfrrtd lgvdlrfnrv gmpdlsmirs dpppfvndit
      241 aeqgeqglvv hiltdsvadv raykdddsyv vdvrgpdnpa tmtpldralq aavaplpavp
      301 agatqavsag ghdapaavpa apvadpaapa asvadhaapa adpaaphadp sstiaapdap
      361 ttahdvaava kpdatpehpa piaesaiaap qqpdaqpata parpvvvasa dkprtdlael
      421 penavaralv dgvirveser vgqavhitfp ykkevgaalf mrdstlwlvf ddaapidaat
      481 lqdafvgfar siepttldga qlirvdmidr yvstmspdgp kwvmtigelv tdptrplsig
      541 rqvhpdgsks ldipfgpvsr ihrltdpsse dtvivvtgkg qarglvkphs fteldalasi
      601 hglallpkvd dlavtsdgil vsigrpggla vstlaeekka tlfdlpaalg ssvarkaavi
      661 dfgdarnvdp ggywqarhkl mtdvtqardl pervdrwyka atfalaqglg pettgildli
      721 gklapeetvs drmaalragg eyftyrpeqt lkqldrrefa dspdasvwka malsdlgrhd
      781 eaaaefakgd avigayppvi qrryalshia saidlkdytt ardllarldp nsvsagehar
      841 ldllnalard aaghamdavt llsnivredk gpvaaeatyr lvqlqrregl itlaqaidrl
      901 eqlavswrgd elelktlrll gqysiengdy rrafevmrva eqvnpnstts rqmteemqva
      961 fsqvfldnkn snlspvqals lyydyreltp sgrrgdamvr kladrlvgvd llpqaaslle
     1021 yqvknrlrga araqvaadla lvyllddrpd kamftlsttr qaslpvaier qrrtveakam
     1081 aesgnpdgal evlapldgve igrlkadilw sadryadagt ayertlggrw tdamplsdse
     1141 qlavlkagia ytlagdrmsv drlrskytek maptangsaf davtgpivas gsdfqsivks
     1201 iadadtmksf ladyrkryld vgngdkpdmv tspdgtapkp pesnasvdag gatsag
//
LOCUS       WP_284538486             367 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284538486
VERSION     WP_284538486.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..367
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39044
     Region          10..364
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mtpetqarla alrermvate tglvavapgs hmqwllgftp asderpclll vspggtaflm
       61 palnaddvrq htdidffrwt devgphvalc qalaaigana pdrvaidetm radfallvld
      121 alpsgvlrtf tadtlgglrm rknereydll kmnagiadra ieaavaalkp gmtenelasi
      181 irshflqega apsfwivgsg pngafphhta sdrhivegda vvidiggiks afpsditrva
      241 ivgrppegfa eihaiverav qaalaaakpg vrardvdaaa rtviteagyg kffthrtghg
      301 mgidgheppy itatsetvle egmvfsiepg iyvsgrygcr leeivilrkd gpeilsglsr
      361 dilvakg
//
LOCUS       WP_284538490             534 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284538490
VERSION     WP_284538490.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..534
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=57256
     Region          2..520
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mivtalfvgv ylticgklal iglqvspeee vstldrtvar pdivdrngai latdlpvlsl
       61 faeprkvvda deasealaga lgnmtreeiy krlksrasfv wlkrgltpdq aneikqlgip
      121 aigfrgevrr fypqgretsh vigltdidng gisgferwld qssfgalrks gmmngaqvqa
      181 sqltidarvq havhevldka meqyhpaaag avilnaktge vislvslpdf dptipseaae
      241 kdrlnrvsgg vfemgstikt fttamalelg naklttiyda shplvigsqv ihdshsrgkp
      301 lslvdvflqs snigsareal svgmenhkaf lertgllski afelpevatp vsprvwrqvn
      361 sltsafghgf attplqtavg iaaimnhgrl vpptllprse eearalavqm vsektsddmr
      421 ylfrlnavkg sgrkanvagf rvggktgtae kvidgrysht nnfnafaaaf pmedpafvll
      481 vfiddprpef pgagitsaan avpiagaiie rsallldvqp vfddpadiaf afsd
//
LOCUS       WP_284538575             544 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Pleomorphomonas
            sp. T1.2MG-36].
ACCESSION   WP_284538575
VERSION     WP_284538575.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..544
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57284
     Region          24..519
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mtkrlaigil sagalalsag taladfqlti lhindfhsri eainkfdstc sakesdagec
       61 fggiarvksa iddkrkeldg anllvldagd qfqgslyyst fksapvaefm ngigfdamai
      121 gnhefddgpa eldkligavk fpiisgntvs akgslldgky kgyiikeigg ekvavvsvla
      181 kdtsetsspg kditfedeit ylqkavkeie aegvnkival thvgyvkdqe iaakvdgidv
      241 ivgghshtyl sstddkasgp yptlvknpsg ievpivtaya yskylgdltv nfddrgvvta
      301 tkgapillda svtpdegyae rvkelgkple elkakvvgsa adaidgdrks cravecsmgn
      361 lvadaaldrv asqgitisia nggglrasid agdvsmgevl tvlpfqntia tfqidgagik
      421 ealengvsev degagrfpqv sglkytfdrs kpvgsritsv evkdgdgfvp ldpaktygvv
      481 tnnyvrgggd gfktfadkav naydfgpnle dvvaeyltth npykpytdgr itdatpadyv
      541 ppkk
//
LOCUS       WP_284538698             421 aa            linear   BCT 25-DEC-2024
DEFINITION  cytochrome b [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284538698
VERSION     WP_284538698.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Tolkatchev,D., Yu,L. and Yu,C.A.
  TITLE     Potential induced redox reactions in mitochondrial and bacterial
            cytochrome b-c1 complexes
  JOURNAL   J Biol Chem 271 (21), 12356-12363 (1996)
   PUBMED   8647838
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Howell,N.
  TITLE     Evolutionary conservation of protein regions in the protonmotive
            cytochrome b and their possible roles in redox catalysis
  JOURNAL   J Mol Evol 29 (2), 157-169 (1989)
   PUBMED   2509716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..421
                     /product="cytochrome b"
                     /GO_function="GO:0008121 - ubiquinol-cytochrome-c
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=47215
     Region          5..408
                     /region_name="QcrB/PetB"
                     /note="Cytochrome b subunit of the bc complex [Energy
                     production and conversion]; COG1290"
                     /db_xref="CDD:440901"
ORIGIN      
        1 msghstyvpr taigkwfear lpvvrllhdt avsyptprnl nalwtfggil ammlvvqivt
       61 givlamhyaa estvafrsve simrdvnwgw lirylhanga smffiavyih ifrglyygsy
      121 kapreilwil gviiyllmma aafmgyvlpw gqmsfwgatv itnfftalpf vgqpiqtlli
      181 ggfsvdnatl nrffslhyll pfliagvvvl hvwalhvvgq nnplgidvks ekdtvpftpy
      241 atskdvmwiv lfmifygwfv fyqpnflghp dnyieanpls tpahivpewy flpfyailra
      301 idfnigpids klggvlamfg aiavlaflpw ldtskvrsgr frpifkvafw vfgvnalflg
      361 ylgsvktddi igglqavswa klstfyyfay flvilpvlgy iekpkplpvs indailaksa
      421 h
//
LOCUS       WP_284538808             296 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Pleomorphomonas
            sp. T1.2MG-36].
ACCESSION   WP_284538808
VERSION     WP_284538808.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 296)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..296
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=32630
     Region          4..295
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mgskivftgg sgkagrhvvp ylkdkghdvf nldlkpldcp gvttlacdlt dagqvysals
       61 mhfdfdslas gsrpvlpdav vhfaavpril ltpdnhtfet nvlstynvie aamklgirkv
      121 iiassettfg vcfaegdkdf hefplteeyd tdpmdsygls kvvnektara famrynadiy
      181 alrignviep heyvnfpgfm edpltrkrna wsyidardlg eivhlaigkn glgfqvfnav
      241 ndtitarept eaflkkacpn tphsrplvgn eapisnekir tvlgfkeqhd wrtyvs
//
LOCUS       WP_284539055             267 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284539055
VERSION     WP_284539055.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 267)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 267)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14398448
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..267
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29056
     Region          25..119
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          186..261
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mpilteqrht tdwldpdtvh rpvviygfva drfsdielpp hshakgqfil vqggaltcev
       61 daglwivppr saiwipggmr havrmsgmle gynafvdpal glglppacca vsvtpllrel
      121 mtrgarlppl yeeggvntrl lavlidemaa asvedlnlpm padpalrrla damlatpadr
      181 aplatwarra glsertlarr iaaetglsfg rwrqrlsiml avqwladgtp iqhvaanlgy
      241 eslpsfvtmf rktlgmapgr ymaerfg
//
LOCUS       WP_284539097             157 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284539097
VERSION     WP_284539097.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..157
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17356
     Region          16..147
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtehsrtpag daltgliltl frannltltw gdrmvaplgl tsarwqmlga iayarrprpv
       61 awlardlgan rqnvqrivne lekdglvafe pnphhkrahl vvltdkgrqa yekalrlytp
      121 raaaladgla tediatarrv ldtlrarlea edegter
//
LOCUS       WP_284539172             122 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284539172
VERSION     WP_284539172.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..122
                     /product="YybH family protein"
                     /calculated_mol_wt=13987
     Region          1..121
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mqpqehlkly easlarqcfd evapllsaea vfwftdgshr gidairaafe dtwrrlrnet
       61 ywledvdwia vgdtaascty rfrwtaeidg tpcagegrgt tvlrkeegqw kivhehlsrf
      121 pk
//
LOCUS       WP_284539352             262 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284539352
VERSION     WP_284539352.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..262
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27456
     Region          7..229
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mshapavlit gastgigaty aerfarrghd lvlvardaar mealasrlrq dsgvaidilp
       61 adltqasdla rvetrlreda rigilinnag taiggsfveq stddmarlva lnatalvrla
      121 gaiaprlaea gngaiinigs vvglapefgm tvygatkafv lflsqglale lgpkgvyvqa
      181 vlpattrtei wqhvgtdvda mtnvmevgdl vdaalvgfdr repvtipplh ddgqwnalea
      241 arkamlgniv narpaeryrs pa
//
LOCUS       WP_284539408             436 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284539408
VERSION     WP_284539408.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..436
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=46987
     Region          1..434
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mkivmigsgy vglvsgtcfa dfghdvvcmd kavekieale rgeipiyepg ldalvaanvk
       61 sgrltfttdl agpvadadvv fiavgtpsrr gdghadlsyv yaaareiaaa vkgftvvvtk
      121 stvpvgtgde veriiretnp nadvavvsnp eflregaaid dfkrpdrivi gyederarev
      181 mtevyrplyl nqapllftkr rtselikyag naflamkitf ineiadlcek vgadvqqvar
      241 gigldgrigg kflhagpgyg gscfpkdtla lvktaqdyds pirliettva vndtrkrama
      301 rkvvqavggd vrgktvavlg ltfkpmtddm rdspaisiiq alqdagakvr gfdpegmdna
      361 kkliegiayv gsayeaakga dalcivtewn efraldfprl kavmkapvlv dlrniyrpee
      421 vekhgfsyvs vgrsqt
//
LOCUS       WP_284539406             319 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Pleomorphomonas
            sp. T1.2MG-36].
ACCESSION   WP_284539406
VERSION     WP_284539406.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..319
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=35309
     Region          4..239
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 maekvivfgg sgfigthltr rlvaegvevi svdikpqret lpgvdyriad vrdlsgfwvd
       61 gaisriynfa aihttpghpi heyyetnilg alsitdfaar ngvseivfts sisvygpsee
      121 mkteqtppap esaygyskli serihrqwfe sssgrkltiv rpavvfggge ggnftrlatl
      181 lkkgffiypg rkdtikaciy vedlldaief arnkaepfil fngaypqryt leqiisamis
      241 ghfpkartfm vpkalvlaga rllkvldafh igihpdrvmk lvrstdiypg wltsqgreyp
      301 naietalmrw saesggrfn
//
LOCUS       WP_284539462             769 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284539462
VERSION     WP_284539462.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 769)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 769)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 769)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 769)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..769
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=83125
     Region          105..764
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mreliktrlg ahsgispvev vilvidalli lfiavatlsa aaqlsadavd kqlriqsnia
       61 dvmsdeinhs fqamelvlig vsdylkskgv ndqvalvset tsqpafemlr armsglafld
      121 altitdetgr vlastrtwpa peayfgdrpy fkamqsmvgp ptylsrpiig riagrpnlvl
      181 shrmtssags flgvvnaasd qdyfanrlar vdvgadsvia fvlndgtvma qspalvldka
      241 seanppkhda ealfalpstg glapagvlgd reryvavrrl gnfpaaivvg vaagtvndev
      301 rraviplaia sfvvcavivl vtglwsrqlr rdrrqsarqy vqartdvvtg lsnrlcfvew
      361 lealdkgggt apyalyfadl dnfktindtl ghdigdklla avaerlvdnl gsddrvarlg
      421 gdefaficmd vtdegnalri adivvsairq pflieghhln itssigislc prdgrdlvsl
      481 lknadlalfk akadgrgltr vfsedlasim atrrelqadl eeawtlgqfy lvyqpiyeat
      541 grrlsgfeal lrwkhpirge vrpdafipia eetglinrlg awvlekacad amawpaplfv
      601 svnlspvqfr egaieaqvhr alrlsglpne rleleitest llqkeggvqs ilanlrgari
      661 nialddfgtg ysslrylidf qidrikvdry fvegltdkss sqaiiqaila lastlglqct
      721 aegieteeqa eilgtggcsh lqgyllgrpl lpdqakalar aaerhvaag
//
LOCUS       WP_284539842             875 aa            linear   BCT 25-DEC-2024
DEFINITION  S1C family serine protease [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284539842
VERSION     WP_284539842.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 875)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 875)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 875)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 875)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 875)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..875
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..875
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=93915
     Region          672..>840
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mflsvplgaa lhptihfrgp iarrlwlgwa msllfcallw atetplraet fapppgahwi
       61 avastqdidt aigiarlfgp tarvirsksg wlavsleprk gslqqiaqti twpplpgdal
      121 lssgrdyvet iwkapvaqqa sakvkrdkpg visfaalevm vtrepaaqgw tahvtaqrag
      181 kqvldvrhtf aegepdyess vmvaevdggn dtpeifiday sggahcctrt valdaagpte
      241 wttvdlgnrd gegieledvd gdgeaelilp ddsflytfdc yacstqpiri skigkatvrd
      301 vsgdkkfrhr liqevrgmef lakvmpdrwh sngflaawva aknrigegqa awaamtglyd
      361 rnsdfgvyac rkpqpietcp tdqqyrlsfl dglrrhmeeh gygsitldae dtgasppvqv
      421 sledaraafm ampverrrdi qlllaslghw pavagdgfgk nlwqaikdfq nangkvsngv
      481 lsvgdydell raaspflsmw dlsrvthpvt gtplwiprgl akstlatntg vrfgaasega
      541 ivdldyypgv slqalygitq evvrshvtdy qtikskffvi nshgeaatqy trfedigtgv
      601 vgftliwpsv aefhgdrlat vmsdlfrsev elgiprspps pvapiasvps mpaaispspp
      661 paavpekerv vssgtgffva adrlltnahv vagcekvnvl idgkgvegvv rgrdttndla
      721 ivetndyrsa tfakmrpgvr lgedvaafgf plsgelassg nftrgavtat aglrddiahl
      781 qtdaavqpgn sggplidvyg nvvgvvdskl nslvatvann dipqnvnfai kasmatmfle
      841 aqsipfemgs vgtpvswpdl adrakaiaae itceq
//
LOCUS       WP_284540139             730 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284540139
VERSION     WP_284540139.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 730)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 730)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 730)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..730
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=80371
     Region          73..724
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mkrqlalffs rvvasslamv valsaigafl vwvtrsvdre dierqaeiag yalreirsnl
       61 ahnqesstfw deavertaag gnedwiddnl gswmhtffgi deayildgrd lpvyafaete
      121 lkspaffesr rdllrpylqa lrsklasges paresteesi gitdyayvag hpaivslkpi
      181 msdtgrveqp lstislhivv qylegaiidk igqahvltdl kyvptserks gtasvaltsd
      241 agdvaiefhw kpfepgrqll tslspvlvlm gsallagtli istasyrrkl drtrndehir
      301 ylashdpltg lhnrsayera adelieqfsy hqqsdplafl fmdldrfkqv ndilghqvgd
      361 avlvefarrm teilpanapi yrvggdefaa lipnrtrrei ealcgriies laepmeiggr
      421 rafvgvsigv smapydgtdr qelnrkadva lyhaktagrr rfsifgtqmd daiqnraaie
      481 selrealrtk aalsvvyqpk yagdgsrmlg tealvrwdhp drgaippslf ipiaeeagfi
      541 adlglwvlei acrdaigwpv dhlavnvspv qlcaigfaet vlatlrkldf pptrleleit
      601 etdfagteev gmlnikalna agiaiaiddf gtgsstferl rdidfdriki dqsfvksite
      661 segdaeivra mismahakgl kttaegveta eqrevlrsfg cdelqgyllg rpmpahqlse
      721 vlnaaetaal
//
LOCUS       WP_284540389             309 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284540389
VERSION     WP_284540389.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..309
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32507
     Region          1..299
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(34,247,250)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(186,217,245,248..249,252)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mllacgdali dfvpvksadg rdayvpavgg sclniavams rlgaltgfvg gissdmfgtm
       61 iadhlaasga slryvrrsdd ettlafvrfv gnephyafyd ettaarlwty qpgsipfpai
      121 evlhvgsttl inepvaseyl amfkaakgkt tlsfdpncrp tlthdkaayt armaefakta
      181 divrmsdmdf dflfggndfe akaqeilagg aalvivtrgg dgviawhata grvevpapat
      241 kvvdtigagd tfqgsflval keagriarpa leaisrdela aalafgtrca aitcsragan
      301 ppwraelke
//
LOCUS       WP_284540427             793 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284540427
VERSION     WP_284540427.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 793)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 793)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 793)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..793
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=86827
     Region          123..787
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 maivglmlvv lqlavgvtet arqldgiksd amyrakagld llaaipagta etgqngpdae
       61 aalsslrsia diyarnhpge tiqietggpa sdqaaiasdd ivawgdndlg vrrgfvlddg
      121 akrisgffsa ridlsgdyvg whrsildriq laafivlsvl mlavllmrvi vvsplerlsg
      181 ltrrlaagel vevpepvdha reicdlseal vvfrnnlaqk nkleatneva lrkleratgn
      241 ldmalramtq glalfdaqyr lllvnerfle ifdlaedpfg atlsaqdved liakqiaaap
      301 dlkhhfstae lfgrhlgrlf tqaepvsged tfgdriisft hvitgeggwv ttvedvterr
      361 aqearlayls rfdaltglpn rtqfndrlal dlawaadnsi klaaigldln qfkeindqrg
      421 hsagdavlve igrrlertaq dgefvgrigg deycalkkfr lqtevgeflg rlercfqapi
      481 rveendisvs vsigvaiypd daidaeqlvn nadlakyrak rsvtqnvcfy eadmdeasre
      541 rrtmardlwd aldreefhlt yqvqknirsr etigyealir wthptrgaip pdvfipiaee
      601 cgailpigrw vlkracldam awsdglrvav nlspvqiand divklvhetl lesglapqrl
      661 eleitestii gdkahalhvl rqlkalgitv alddfgtgys sldtlnsfpf dkikidrsfl
      721 seaeekedsr aivkavvalg rsldvpvlae gvetagqlsi leeegcqeaq gflfgrparl
      781 tgeevlksig rga
//
LOCUS       WP_284540553             122 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Pleomorphomonas
            sp. T1.2MG-36].
ACCESSION   WP_284540553
VERSION     WP_284540553.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..122
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13576
     Region          6..109
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mnpaydvfdd rcptrlvldr ladkwallvl drlqdgpvrf nhlrrdirgl sqkvlsqtlk
       61 rlerdglvkr tvhptvpvsv dyaltslgrt ltetvaafah waevnmdavl aaqtaydsam
      121 tg
//
LOCUS       WP_284540614             145 aa            linear   BCT 25-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284540614
VERSION     WP_284540614.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Schwartz,C.J., Giel,J.L., Patschkowski,T., Luther,C., Ruzicka,F.J.,
            Beinert,H. and Kiley,P.J.
  TITLE     IscR, an Fe-S cluster-containing transcription factor, represses
            expression of Escherichia coli genes encoding Fe-S cluster assembly
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 98 (26), 14895-14900 (2001)
   PUBMED   11742080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..145
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=15169
     Region          1..144
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mltkkgkygl kalvhlarse pgkavqvaei aareniskkf ldaimrdlkn agfvrswkgp
       61 gggfalsrpa seivvgpvvr aldgplapia casrtafqpc ddcgdlstcs vrivmtevrd
      121 aiaevldrtt ladmlekssa aalas
//
LOCUS       WP_284540625             392 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284540625
VERSION     WP_284540625.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..392
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=42096
     Region          12..392
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mtyqpprinh rlafstrtih ggqshdpttg avmvpiyats tfaqsspgvh kgweygrthn
       61 ptrqaferai adlesgtagf afasglaaia niletldhga hivasddlyg gtfrlidkvr
      121 rrsagldvsf adfrdpaaie aairpgtkli wvetptnpml kivdlqaiaa igrkrgivtv
      181 adntfaspai qrplelgidl vvhsttkyln ghsdmiggav vvgdnaelre rltflqnavg
      241 avsgpfdsfl alrglktlal rierhssnal aiarylegrr gvrrviypgl eshpqhalak
      301 sqmsafggiv sveldrdleg tkrflentrl ftlaeslggv esliehpaim thasipaeqr
      361 aklgisdgfv rlsagiedsg dliddlraal da
//
LOCUS       WP_284540674             479 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284540674
VERSION     WP_284540674.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..479
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=53038
     Region          9..479
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 msvedslaap vivwfrddlr lsdhpaldaa kasgrpvicl fvfeegterr slgaasrwwl
       61 dkslasldgd lrrlggrlvl rrgdprlvlp diaastgatg lyfnrrydre gsgidetvat
      121 elrrqgvais shaawllfep gtirtktggt frvftpfwka hrphlsprsa lhrrpdalsf
      181 fggmvvsdpl aslglhptrp dwsgglaasw apgeagatar latfldggls ryfaerdfpa
      241 ieassrlsph lrfgeiavar vahevlkaqa agsasdeaae kflaeigwre fawhllvafp
      301 dlarrnyqag fdsfpwqdda salkawatgq tgypivdagm relwqtgfmh nrvrmiaasl
      361 likhllihwr qgeqwfwdtl vdadlasnpf gwqwvagtga daapyfrvfn ptaqgekfdp
      421 egsyvrrfvp eiadlpnrll hcpwetppll rpdpslyppp ivdhdtgrkr alaafaqcr
//
LOCUS       WP_284540926             192 aa            linear   BCT 25-DEC-2024
DEFINITION  DedA family protein [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284540926
VERSION     WP_284540926.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..192
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=21094
     Region          7..184
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 miehaelvsm mssyglwvlt plavlegpiv tviagylasl silslwlivp cviiadivgd
       61 clmyllgrla lgslsprwrd rlglsrrrlf hlmrgfrrng trilvaaklt haagfaalta
      121 agaarmpfme flvantlasi pkslffvvlg ylfgsayeti akwlsgeaal imlalvlglf
      181 tiiylrrrrv rr
//
LOCUS       WP_284541090             612 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284541090
VERSION     WP_284541090.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 612)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 612)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..612
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=66341
     Region          4..580
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mpcqgalade taahdlgkvv fsanrtptee aavgssvtvi grkeiersge ttvldllarv
       61 pglgfsqagp agstttmqmr glgaryvlvr vdgidvsdpt qpqagpsien lllgdverie
      121 vlrgsqsaly ggtavagvid ittrtadekg vhhsasvggg sygtksvryg vsaatdalem
      181 gasfqrfqts gfssaerdng nteadgygns tasinasyra nealrlfaaa rytyrrsnyd
      241 dfsydwmtgf gqpidetgal rfhtigrevg arvgadfnll dgrlkntiav qhydltrevy
      301 dsspgrydgr rtkieylgnl altetiglsa gldyttedar ttggvdagmn nagvfaqasw
      361 kpitdvtlta alrddhhssw gdhptgrvta aweatqstkl rtswgtgfrp pslyelhapt
      421 ygnanlkpee srsfdigidq qvwdnrarls ltyfnidtdn lisydtstwa ytqiegtsks
      481 qgieftgrlk lldnltldag ytfteavdan dsrlmrvprh kvttgatlka ndrttltlrg
      541 twvgdsidtd ysvgqirqlp nyflldaglt wdwtdnvsls ltgknlldek yqtiwgygta
      601 gravyaelka ry
//
LOCUS       WP_284541167             291 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284541167
VERSION     WP_284541167.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..291
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=31026
     Region          8..280
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mpheaapilv vanpvagnfn yrhlmrlaer ldrlglksdi wltrysgelt diaaelspsv
       61 rtlvvgggdg sineaitgiv rqggdgpals ilpfgtanvl ahelglpssp ekiaeriaad
      121 rktplhlgmv gerpfalmvs agfdadivha vdapfkrrwg klaygwrglt lalaqkgrdv
      181 ivtadgetir criavvttar fyggpltitr htkatepglr lvtladdrpa tllraatala
      241 agrldrlaav qdravsevrf csegirmqid gdkmetsdav vragrvidvv a
//
LOCUS       WP_284541447             187 aa            linear   BCT 25-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284541447
VERSION     WP_284541447.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..187
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19704
     Region          7..168
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mskiysvavl vgslrkgayt rmlanalkki appsialsiv eigdlplynp dlddagapaa
       61 wtrfrnevks snavlfitpe ynrsvpaalk naldvgsrpy gasvwpgkpg aiisltpgsl
      121 gafganhhlr qslvfldvpt lqqpeaylgn agsmfdvagg fadasteahm kayldafadw
      181 itrtaka
//
LOCUS       WP_284541479             106 aa            linear   BCT 25-DEC-2024
DEFINITION  HesB/IscA family protein [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284541479
VERSION     WP_284541479.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Lu,H.M., Li,J.D., Zhang,Y.D., Lu,X.L., Xu,C., Huang,Y. and
            Gribskov,M.
  TITLE     The Evolution History of Fe-S Cluster A-Type Assembly Protein
            Reveals Multiple Gene Duplication Events and Essential Protein
            Motifs
  JOURNAL   Genome Biol Evol 12 (3), 160-173 (2020)
   PUBMED   32108236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..106
                     /product="HesB/IscA family protein"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=11098
     Region          1..105
                     /region_name="IscA"
                     /note="Fe-S cluster assembly iron-binding protein IscA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0316"
                     /db_xref="CDD:440085"
ORIGIN      
        1 mieltenaad avrtalaaad gqaeglriiv eaggcaglry rmgletderp gdlvveqggv
       61 rlyldlltqr hvdglvvdfv dgvdqsgfvf dnpnaashcs cgksfc
//
LOCUS       WP_284541492             289 aa            linear   BCT 25-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284541492
VERSION     WP_284541492.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10594375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..289
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=31503
     Region          120..276
                     /region_name="SIR2_2"
                     /note="SIR2-like domain; pfam13289"
                     /db_xref="CDD:433090"
ORIGIN      
        1 msallaggrl dvlsgeaard alshqrtell adrlvpylgp glltlegpaa vpaspediat
       61 alqkrvpvpg rirgnmwava qyieshrhrr tlkklmadvf aveptpsafh rflaelplgl
      121 vvdswydgvl vaamaeagrt dvvdvqgqsr aaigesrwhr afdllghpte pdkartllyr
      181 phggmrpdgd vlvsdsdyve vlteidiqtp ipeevrtrra trgflflgcr fhdqmlrtya
      241 rqilkrsags hvcvaeasal tvnerrflaa egillldlpl aeaaqilag
//
LOCUS       WP_284541498             301 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284541498
VERSION     WP_284541498.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..301
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33092
     Region          43..295
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 malgafmels latsendgis lacrltpvia gqrsvreipp gfrlfiylrg wqrfeidgqr
       61 fdvsadagpv alalslvrpa rlvqlawsed rmsklmitap sdwtatldld gaghgdalat
      121 flaghgnhhl wrldddsvri arlaaeppaw vprealplyr raraldlvcl tlstlalrre
      181 entlprpaqs vlgeririfl ldhlneplti davaqavgas vsvvqrcfke lygmtvfdfv
      241 rrrrldaard aldnrgvsia caafiagysa pssfatafkk aygvppklrr rqampfreaa
      301 e
//
LOCUS       WP_284541571             206 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284541571
VERSION     WP_284541571.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 206)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007442
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..206
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21066
     Region          97..198
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
ORIGIN      
        1 mslqpnkilg avlavavvaf aidfvsdqif akqdlktpgy vvdmnaapav aateapapaa
       61 vapdpnapaa vatqqaaaap aaagsdvapi adrlkaadva agektskvct achsfadsga
      121 nkvgpglwev vnrkpgtheg fkyspamvtf gethtwdyat ldiyltnpkt evpgnkmafa
      181 gvkkpedran liaylrslsa npaplp
//
LOCUS       WP_284541598             481 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284541598
VERSION     WP_284541598.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 481)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 481)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..481
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52613
     Region          156..474
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 maqtdssggt akphfptkht fslsfkllif tilfvmfaev llfvpavanf qrtyieskir
       61 tagivahtlt typetalprt iqadllnrld ayavavrseg mkqlvamada pptvtrsidf
      121 dsqrthgivm eamdtmlfgg drtirvtgdy dgegevevvf sethlrdeil hfagrlllvs
      181 flisafvgvl vffsiqylmv ipmrrlgksi ykwsqepesd aylvryggrt deigraefaa
      241 atmqqriqel fkqqkrlvel glavskinhd lrnllasaql isdrltaipd psvqrfapkl
      301 vsaidrainy cqsvlaygka qeapparrll slsrlctdva emtglihhas iewvnsvpdd
      361 levdadsdql frvllnlvrn asqaleqckd dalvrrltvs aerdgtkvsi rvsdtgpgls
      421 ekareslfkp fsgsvrsggt glglaivael vrahggtisc ldggpgatfv idipdrpala
      481 a
//
LOCUS       WP_284541750             146 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Pleomorphomonas
            sp. T1.2MG-36].
ACCESSION   WP_284541750
VERSION     WP_284541750.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..146
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16028
     Region          10..111
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 makvrhsrfd capgcaveaa iglidgkwks vilfhllert lrfgelsril asvtprmltn
       61 qlreleedgl vvrtvypqvp pkveyslspl grsmepvlma lkvwgdanig rfgkpkavge
      121 kqnppaptgq tagghqwary dpepie
//
LOCUS       WP_284541765             225 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF2161 domain-containing phosphodiesterase [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284541765
VERSION     WP_284541765.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009341
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..225
                     /product="DUF2161 domain-containing phosphodiesterase"
                     /calculated_mol_wt=24653
     Region          1..220
                     /region_name="COG5482"
                     /note="Uncharacterized conserved protein, DUF2161 domain
                     [Function unknown]"
                     /db_xref="CDD:444233"
ORIGIN      
        1 metdlylpvk rhleslgltv kgevkgcdlv glsdgepelv vigelkraft lelvlqavdr
       61 taaadevwla igaskrgrgr egdprvrklc rflgfgliav tptglveviv epapwkprrd
      121 grrrsrivee frrrrgdpip ggstrlpqmt ayrqqalava salrdgplrp rdlkpiapda
      181 akilqadvyg wfervergiy rltdggkaal vawaaylpae epvaa
//
LOCUS       WP_284541770             310 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284541770
VERSION     WP_284541770.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 310)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 310)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..310
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34381
     Region          15..102
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mnrnfltlha adshatlkgi ssptrldilr llhgkgpmnv neisaelslp qstvamsvqa
       61 leeaelidtk tvkakkghqk icsarydeiv irfddsgalp rdetievsmp iglytscdvr
      121 apcglcsndg viglldvpnf fldpnrmqag llwfgrgyve ykfpnnakvl neeisavefs
      181 melssevpgt nadwpsditl wvnnvlagtw tspgdygdkr gvytprwwkl egsqygklkt
      241 wtisergtfi dgirisdvkl adldldnhhs irmkigisde akhpgginif grgfgnydqd
      301 ivmrlyrsen
//
LOCUS       WP_284541972             718 aa            linear   BCT 25-DEC-2024
DEFINITION  GumC family protein [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284541972
VERSION     WP_284541972.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 718)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 718)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..718
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=78089
     Region          1..715
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mdssefdvrn aiglvrrqiw lilstvliiv glaavyvflq tptytastli lvdprqknal
       61 dpesqmsllp tdnarvesev eilkspstqi gaisrlglvk dpefgvklst vdrlmvffki
      121 kstenlladt daqlravltr fsnnvtiarr gltyvisvsa tssdpakaal iantlsstyi
      181 daqvdakisn alsvrdalnr rlvqasttin enenridafv neniekvsne stradisamr
      241 ssleslkaes isaqslqasv stlaankdwd giaaqlrsdt vsqikaerdk vladignaaa
      301 gsnresnlra slsqldkrla dqvnvelgtl sdrvktaqqe qdrlrtsird tvlssnltnd
      361 vmvkiyelqq essvaktlyq dllqrlrgve tqadlqlads rivssalppd apsapktkli
      421 lmlalvaglg lglglaflne nfiggftsdq qfeavlgvpv issipllsra grsitersqv
      481 aselldhplt aysesirrir lglenmlrrk lqdksreggl ivmvgsaipg egktttaiai
      541 arafalsgkr vllvdcdlrr psiapalslt penglsdylt lsldsqsirq fvtkdkvpgl
      601 dmivgknthr tstdslieta qfnllmelak erfeiivldt ppilpvvdaq ylatradivt
      661 lvvhwastsq rdvrsaindl rttagedlpi aavlskaelg vgsyrnkyns yyyyapes
//
LOCUS       WP_284542078             439 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284542078
VERSION     WP_284542078.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 439)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..439
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47286
     Region          56..428
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(132,134,286,288,323..325,366)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mtrlrtllts aalfaalgvt gamaevtvlg wpggpeeagl rkaadaynat aadadkvkli
       61 ffnrdgffdk laadlaagst dfdinllaty algryapfmd pitlpdaska tfpekvlatm
      121 qydgkqygip tdlslhfmyy rsdlieklls dadwkakyge isekylgkkl dpkdpdawtw
      181 edwmatalff tksinsdspt rygtvlqmkn llfnmmvwqs varahggdwm ndkgeitvds
      241 payrtaldiy kklydegtsp kdsttyefae snaafgagqv atmvqwnaaf gdldnkdktp
      301 avagkigtva ppagpegrft hihglglgin kasknkegav kflnwlgapd ameiyakagg
      361 spalsdavva kvsaerpdlv klgqfagayg fvmhggtaak alqvyelqak eftaywagdk
      421 slddalaatk sgmadllkp
//
LOCUS       WP_284542110             746 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284542110
VERSION     WP_284542110.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 746)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 746)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 746)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 746)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..746
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76652
     Region          11..737
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtetagnsvr sfdirgmtca acsarlervl kktpgildar vnlaleradv aveasvtpea
       61 vvaavdgagf satlrsddpv iaraereare veaagtrrlt gwllvvcall tlpfivamva
      121 mmagfghvlp tyvqlalata vqvlagrrfy rgawnalrgg ganmdvlvsl gttaawgfsv
      181 ymmatvhhmv eehlyfeasa ivltlvllgk fleerakast travrslmal rpetatklae
      241 dgsqtvvpvt gllpgdrvlv rpgervpvdg tilngeshfd eavitgeslp vrrqtgepvv
      301 tgavngegav tvevgavgee stlgritrlv esaqsgkapv qrlvdriaav fvptvvavaa
      361 iafvlwlalg ggleqalaaa vavlviacpc alglatptal vagtgaaara gilikdievl
      421 eraahigavv fdktgtltvg hpellevvta qgvepaqlla lsaavqggse hplaratlar
      481 aaaegvapsa aedvkavpgk glvgrvdgad vligtaalms ehgidhtdid kaglgrlqpe
      541 mtlayvaeng raiglfgyad alrpeapaai delrrrgirt llltgdrapa araiagaagl
      601 ddwradvlpe akaaeveglr aaggrlamvg dgvndapala aadvgiamgs gtdvametag
      661 itlmrpdprl vaaaldiaaa tslkirqnlf wafiynvigi plaafglltp alagaamams
      721 svsvvtnagl ltqwtpklpp vgstkr
//
LOCUS       WP_284542138             321 aa            linear   BCT 25-DEC-2024
DEFINITION  cell division protein FtsX [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284542138
VERSION     WP_284542138.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..321
                     /product="cell division protein FtsX"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=33215
     Region          36..317
                     /region_name="FtsX"
                     /note="Cell division protein FtsX [Cell cycle control,
                     cell division, chromosome partitioning]; COG2177"
                     /db_xref="CDD:441780"
ORIGIN      
        1 mktsilkpkk gasarkarpg gdmaiaspiv ppqaiagrtl vlviaimtfl agftiavvsv
       61 idraadawas digrevtiei rpldgvaida evekavalaq efpgvggarg isdaetqrll
      121 epwlgpgidl salpvprlvv vsidnaaafd akalaeavgr dirggsvdnh alwvdrlsam
      181 assmvfagig lmtlmlvali lsvvfatraa magnrdviev lhfcgaedrf iagqfqrrfl
      241 lfgveggaig galallammi tawaiggsag rpgadqieal fgrfelpgta yvlvlalvva
      301 valltaltsr lavrrslsal d
//
LOCUS       WP_284542156             134 aa            linear   BCT 25-DEC-2024
DEFINITION  bleomycin resistance protein [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284542156
VERSION     WP_284542156.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..134
                     /product="bleomycin resistance protein"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=15486
     Region          6..131
                     /region_name="BLMA_like"
                     /note="Bleomycin binding protein (BLMA) and similar
                     proteins; cd08349"
                     /db_xref="CDD:319937"
     Site            order(6..8,38,45..47,49,74..79,84..85,88,129)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319937"
     Site            order(30..31,38,49,51..52,76,111,118,120,124..126,128)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:319937"
ORIGIN      
        1 mtvklvpeln vdnleralaf yvglagfrir yqrpedrfay ieregaelmm eetfgpgrrw
       61 hpaplehpyg rginfqieit nvtelytrlr eagcafvldl eekryrvgdr segqrqfvvv
      121 dpdgyllrfc eaig
//
LOCUS       WP_284542220             490 aa            linear   BCT 25-DEC-2024
DEFINITION  xylulokinase [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284542220
VERSION     WP_284542220.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437490
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..490
                     /product="xylulokinase"
                     /EC_number="2.7.1.17"
                     /GO_function="GO:0004856 - D-xylulokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0005998 - xylulose catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0042732 - D-xylose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51242
     Region          4..483
                     /region_name="XylB"
                     /note="Sugar (pentulose or hexulose) kinase [Carbohydrate
                     transport and metabolism]; COG1070"
                     /db_xref="CDD:440688"
ORIGIN      
        1 mmtpllvgid vgttsvkatl fdaggtalra fadpypmlrp apglaeqdpa dwtrrvsaal
       61 trlsdgltdg avaavgltsq vnthvfvgmd gaplmpaitw qdgragaeaa eldaqissee
      121 rigwwgaplp idashplara lwlkrhhpdl wgrtrwmmap kdyclfqltg eptadpmtaf
      181 gvidqslayv prlldlvpgi adrlpplrsf tqsagrirag lplagapmvt gamdawagli
      241 gtgalgngec mylsgtseiv glvssvrhpa agviafptce gitmhagptq aggaslawls
      301 nltgrspsel salvaasdph rptplflphl qgerapiwdi gargafvgld gsmgpaeltr
      361 avfegvassv rwllealeas agraatgfsm aggggasdpw cqiradmldr pirrlktlda
      421 gvlgaailag vgagcfpsid aaasslvvtd rlfepdpsrr drmdflygey ralyaalkpf
      481 naaraafsgw
//
LOCUS       WP_284542268             344 aa            linear   BCT 25-DEC-2024
DEFINITION  sialidase family protein [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284542268
VERSION     WP_284542268.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..344
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016997 - alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37898
     Region          2..339
                     /region_name="COG4692"
                     /note="Predicted neuraminidase (sialidase) [Carbohydrate
                     transport and metabolism, Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443727"
ORIGIN      
        1 msnhasnlme lgngdllcaw fggsmegssd isiymarydh grdawldpvr msddatrseq
       61 npalfrhpsg elwllytaqe kadqgtavvr lrrsadegrt wsetvdligr pgtfirhapv
      121 vnpagllllp iwrsdmrnaf gddssfvqvs adggrswdvm avpdsrgcvh mdilencrva
      181 ffrrrqsdfi frcvsedggl swsaphpttl pnnnssiqar elsdgrlavv yneiaaagrp
      241 sesavppwik dreaflsacg tiengaiwgv prnplvlsts tdlgltwrkd lvleadatlr
      301 sahdergafv gdysypsiiq tsdglvqvty sylrdyikhe tlaa
//
LOCUS       WP_284542297             449 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284542297
VERSION     WP_284542297.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..449
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47069
     Region          70..439
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mpletrrpgv crlviaaila vlpghavsqd slpaeatafa patvmttpaa lsgntagteq
       61 meaeralkdq elaklrgame lsaekqaeia aeiaglsrdq qalsdqlvts aarvqaleqs
      121 itdseerlar gadnearirv slaarrdvli avlstaqrig rqpppalvvs pedalkavrs
      181 avvlgavlpe irieaealqs dldalvaert raaaerdrlr adaaaiaeer qrltllidkk
      241 kadsearaad laaekakaee laknarsled liagmkkalp aarpespaat apapgsrlgp
      301 aiafadakgr lippvrgvnl qsygddnglg glsqgqaiat ragarvvspa dgrvvyagpf
      361 rsygqllild agddyhvvla gmeridvqld qfvltgepvg vmgnqrlasa avldasvtqp
      421 vlyvefrkgg tsidpspwwv asqdrkvsg
//
LOCUS       WP_284542328             223 aa            linear   BCT 25-DEC-2024
DEFINITION  LolA family protein [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284542328
VERSION     WP_284542328.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Tajima,T., Yokota,N., Matsuyama,S. and Tokuda,H.
  TITLE     Genetic analyses of the in vivo function of LolA, a periplasmic
            chaperone involved in the outer membrane localization of
            Escherichia coli lipoproteins
  JOURNAL   FEBS Lett 439 (1-2), 51-54 (1998)
   PUBMED   9849875
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..223
                     /product="LolA family protein"
                     /calculated_mol_wt=24633
     Region          21..221
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mfqtlrigrr aflsgiagag vtlalataav plattealak pnlanlspeq latvqavnry
       61 fnsittfegk flqtapdgge ttgyfvidrp gkmrfryypp aqlditvdgr tvavddkamq
      121 sqtlyllset plrflldkni nlleeavvqs vsadsdfivi rlqdpgtfvt shltlyfdar
      181 ttelkqwtvt ddqgfdttva iyetkvgnpt npewfqinys kyk
//
LOCUS       WP_284542405             672 aa            linear   BCT 25-DEC-2024
DEFINITION  transglycosylase domain-containing protein [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284542405
VERSION     WP_284542405.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..672
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=71876
     Region          16..623
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mterrprrkp skrqsrrnrr sgmgllgrlv ywgvvlciwg ligvagiigy tvatmpqidd
       61 wkvptrppnv eivdasgtii anrgdtggee vslsdmspfl peavvaiedr rfyhhfgvdp
      121 iglsralvtn lfagsvvqgg stltqqlakn lflqpdrtle rklqeavlal wlewrfskde
      181 llemylnrvy lgagaygvda asrryfgksa revnlaeaat iagllkapsr yaptnspkla
      241 adrakvvlaa mvdqgyvsgd eaaratavga pslpakngsa anyvadwvmd llpgyvaryr
      301 tdlvitttid arlqaaaena vrttldkegv kykasqgalv aidndgavka lvggkdyaas
      361 qfdraiearr qpgsafkpfv yltaiehgfs pdsivvdepv singwspkny eneylgpvtl
      421 ttalarslnt vaarltatlg pdnvvqtarr vgivsqlhdn psialgtgev tpleitaayv
      481 pfanggwgii pylvedirtk dgkvlfhrqg dgpgrvisev avgtmnrmms tvvtdgtgqk
      541 allsdrpvag ktgtsqdfrd awfigytngl tagvwlgndd ntptkkatgg altallwnrf
      601 mtdatrglpa rplpgvelvp pptnvgvsfa etdglpmqgp qlpgatpapp lnvpvteasp
      661 aekgllqrlf gn
//
LOCUS       WP_284542544             429 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284542544
VERSION     WP_284542544.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 429)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..429
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47013
     Region          28..413
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(138,140,272,274,304..306,347)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mgnrllstlv attalmalag vadaktvvrm mhqgdpgwva lygkvaqrfe aanpdvdiel
       61 iyaphdayne kfssavmskq lpdimeldap flanyvwsgy lkplksyidq dllddmtasn
      121 vaqgtypidk elyaigltds svvlygnkky lekigaripk svddawtrae fedylaklak
      181 vdgvkwpidt frgygiktew vtyayqpiln sfgcdlidrt twtatgtlds qpcvdaltmm
      241 qtwvkngwvv pmssgtnqfy adgepaalaw gghwfyaeaa akmkddvvvm plpkfgdksa
      301 spdgtwiwai ttqsehpdia gkflsfllkd kdyrdfavsq saypglksfa aesplyaegg
      361 pmtvafeqas kvavprpphp ayptitsafm qavdqifnge daqkaltaaa kkidediadn
      421 dgyppfdgn
//
LOCUS       WP_284542590             211 aa            linear   BCT 25-DEC-2024
DEFINITION  transketolase family protein, partial [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284542590
VERSION     WP_284542590.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         <1..211
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
     Region          <1..207
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 vklcgqspgi gygelgpthh siedlawlrp lanlltivps dpweteqair faaahegpvf
       61 irvsrypvpa lahrldriep gkaevmrega dvailangvm lhkalgaaqv laesgvsarv
      121 vnmawmnpld veaivdaast gavvtveeas vrgglggava etlalhrpvp memlgfpgfv
      181 ptgsvdflfd hfgltengia daanrvlkrk s
//
LOCUS       WP_284542747             248 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284542747
VERSION     WP_284542747.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..248
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26880
     Region          <23..141
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mdiprifnit esvhrihnpm tadklatlga alrlepgarv ldlgsgsgem lctwardhgi
       61 vgtgvdlsrl fteqakrrav elgvadkvef ihadaaghvs aepvdvaacv gatwiaggvg
      121 gciellsrsl rsggimlige pywrqrpatd eiargclaha vsdflvlpel vasfgalgcd
      181 vvemvladqd gwdryeaakw ltmrrwldan pddelagevr amltsepery atytrdylgw
      241 gvfalmkr
//
LOCUS       WP_284542800             259 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284542800
VERSION     WP_284542800.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..259
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28936
     Region          1..>99
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mrdltvcita itrpevlklt lrsfakrcfc rydgihiian vdplgsdtas rddvvrllna
       61 fdsrgqaqvn tpetggfara vkwvwsqvda pyflhleddw flnrpvdvdr vsrlilggea
      121 divrlylrry apppstgefs lnpffmtgsa ahdlasrmnd qadpekqirg lffggadnlp
      181 riafhgkpgd padvtdigtl wrkshslkks yvpaddgsga hsvwqktvas slrvrlsdls
      241 yaarfnfsll ryrmrlfgd
//
LOCUS       WP_284542760             175 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284542760
VERSION     WP_284542760.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..175
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19219
     Region          33..164
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 maainfpfda thpsekpate rpggggaegl dfeliellff ayrdfvgead hileaigygr
       61 ahhrvvyfvm rnpglrvsdl ldilqitkqs lgrvlkqlid egyieqrpgp vdrrerllya
      121 sekgerland lsarqharmv ralatlppgs raivrdflgn midarapgaa lgeeg
//
LOCUS       WP_284542799             209 aa            linear   BCT 25-DEC-2024
DEFINITION  D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase
            [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284542799
VERSION     WP_284542799.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..209
                     /product="D-glycero-alpha-D-manno-heptose-1,7-bisphosphate
                     7-phosphatase"
                     /EC_number="3.1.3.83"
                     /GO_function="GO:0034200 - D-glycero-beta-D-manno-heptose
                     1,7-bisphosphate 7-phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22400
     Region          32..208
                     /region_name="HisB1/GmhB"
                     /note="Histidinol phosphatase/D-glycero-mannoheptose
                     bisphosphatephosphatase, HAD superfamily [Amino acid
                     transport and metabolism]; COG0241"
                     /db_xref="CDD:440011"
ORIGIN      
        1 msrravndpr lsgadpglwv evaedaarfa grpalfldrd gvinedtgyp srpehirile
       61 eivepirran algwpvvvvt nqsgvaqglf gwddfadvta hidaelatrg arldlvlacg
      121 yygngrppln vadhamrkpn sgmfveagrl tgldfkrslm vgdrdsdfqa aigaglsrlf
      181 spapdyiglr laptaepvrp laeaaelig
//
LOCUS       WP_284542598             395 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284542598
VERSION     WP_284542598.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..395
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41205
     Region          18..395
                     /region_name="FucP"
                     /note="Fucose permease [Carbohydrate transport and
                     metabolism]; COG0738"
                     /db_xref="CDD:440501"
ORIGIN      
        1 mtapssspsv papirrdrlt waaylalaqf tfflniqgni ipflkdefdl syrvvtlhpa
       61 avaaglivsg lfgerltrry grklsvsigl vgmlvgalai iaaphpavsi fgcflmgavg
      121 cliliivptl laewhganrs vaigeangis yvasltaama vglfaaiglg wraalllgvv
      181 lagllivflr gvpvpeaakp vaptvngkpg grlpvvywfy wltiiafvgv eqsvlvwate
      241 fmtrvkglpv assaviagaf sfgmlvgrls sslilkrmta slalylsaiv tlpafflfwg
      301 asslplavfg lfalglgcsl qypltltkai vtagpygela taraslasgl simiipwlvg
      361 atadqvglsg aiallpiltv vavgflfvge rvvrr
//
LOCUS       WP_284542930             445 aa            linear   BCT 25-DEC-2024
DEFINITION  S1C family serine protease [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284542930
VERSION     WP_284542930.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..445
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47289
     Region          <102..>156
                     /region_name="PRK10461"
                     /note="thiamine biosynthesis lipoprotein ApbE;
                     Provisional"
                     /db_xref="CDD:182478"
     Region          234..>408
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 msvlshrapl vasvllvlag saqamssdnf fiddvyadae kwtvgvnlar kscvmdmefv
       61 gnteiqigkd angssdqyym mfanpgwtye eggdyavtvk fnqvstwngd gvgmrlhkyr
      121 gvslegikrg videfasmrt lslrigktny gtfnltttgk gvakleecar avasgnisla
      181 siaeriaans saagpaapnd dnrfskppar edsppeanrp eanrdqdegr vgystgtgff
      241 insdgylltn ahvvegcgda mvrralsgpv parivarekt ndlailkide kpeafgtfrg
      301 apqirlgdsi vvfgypltgl lsstgnlstg lissltgagd dvsklqisap vqsgnsggav
      361 vdqsgrivai vvakaniqar gteekpdiev iqnvnfaika gmaqffldan qvnytveppg
      421 edlktpdvae iarkftaqvi cevrr
//
LOCUS       WP_284542937             263 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284542937
VERSION     WP_284542937.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..263
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28457
     Region          29..137
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mtaidrsfgr qafglnpaay haarpeyqdw vydrlvrcgl gpgarvfeig agtgkatrrl
       61 iergadplva iepdarladf leaslrhpal tvvrapfeea alaeggfdlg vsatafhwld
      121 eetalekvar lirpggwwaa iwhvfgdagr pdpfheatqs llsgyaspsa geggipfgld
      181 vaartqalkr tgafdvveyk ivpwqlvlta detvalyaty sdmaarpnma avltelgria
      241 reefgnrver nmttslfvar rga
//
LOCUS       WP_284542952             276 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284542952
VERSION     WP_284542952.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..276
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31203
     Region          28..276
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          190..273
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mrtpdcsili adcafhedrh yevsdggrvr fhfnfdvsie sranetavae ivdhsagilm
       61 mspdqmivdr vprrrhqhfv tiacdprwla dffnlrlldh vdtgdgdgsp flyreltftq
      121 pirsvinala sqpidglgga riatlaqkal llsleslved qrlrptrlsp sdisaivhar
      181 dilienlaap pnmqklsrlv ginrtklqyg frdmfgmsam qfsekqrmer ahallletdm
      241 svsaiavelg yehpssfstr frhyfgrspr liriqr
//
LOCUS       WP_284543063             244 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284543063
VERSION     WP_284543063.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..244
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27897
     Region          34..143
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 maqniydnpe ffsgytqypr qvigldgate wpavramlpp iqgkrvadlg cgfgwasrwm
       61 rsqgaasvqg fdlsekmiar ahedtddpai dyriadletl elpeaafdlv ysslafhyvk
      121 dirrlmrtih dalvpngdlv fttehpiyma pahprwlvde dgrkiwpvns ysiegerrte
      181 wfvkdvlkyh rtmattlntl ieegftlrrl refgptpeev srspdlseee verpmmllva
      241 vhrp
//
LOCUS       WP_284543177             448 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284543177
VERSION     WP_284543177.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 448)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..448
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=47441
     Region          134..430
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 makrllprsl rarlaiglsv sltllwigas lfaahvfrhe tdevfdstlr evaerilpla
       61 yeqmladedg gdgglrlppv gghefisyvv rdgagrellr ssaadnmhip aglapgfatt
      121 etlrtyteta vqgtivvtta eyldhrrhvf ggalwafvwp lvallpltal vvwlaillsf
      181 rpviafrgai eqrgrgnltp vdggglpsel spvaaavnal larlrsalea ersftansah
      241 elrtpiaaal aqtqrliaem pdanrerars iesalrrltr lsekllqlak aegggllaeq
      301 psdlaavlgl vvdeatrssd eddridlvtp ddgvpsdvdp dafavlarnl ienalkhgap
      361 dasievflda dsltvrnhgp vvaaseverl mrpfergssr sdgsglglai vaavcrgagl
      421 elsiaspveg wadgvsarvt glavakga
//
LOCUS       WP_284543189             266 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Pleomorphomonas sp.
            T1.2MG-36].
ACCESSION   WP_284543189
VERSION     WP_284543189.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 266)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..266
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28382
     Region          4..259
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mgqmypdrgi avitgastgi gfelarcaaa dgydlviaad epeihdaadl lgeygvsira
       61 veadlstpeg iarlvdvisd dgrpvellma nagrglghgf ldqsfddirr vvetnvmgtl
      121 dlvhrvgrqm reqgfgrilf tgsiagympg afqavyngtk afvdsfayal reeltdtgvh
      181 vtvlmpgpte tefferanlm dtemgqgekd dagyvahagy ralmageadi vtgwsnklqt
      241 amagfmspet larrhrklae pgsgls
//
LOCUS       WP_284543196             411 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284543196
VERSION     WP_284543196.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..411
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=45390
     Region          138..401
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mtslsistli psivglalpa rlrvslverm lghvergrls vtlpdgtqls atgrepgava
       61 dlhilrwrav srlltggdvg faeayvdgdw dtpdlvaflt lcadnldklt dvskaslpvr
      121 laqrllmlmr rnskagsrrn imahydlgna ffaewldrem iyssalyeeg ddleaaqrrk
      181 lqriaamlgl dgdpsvleig cgwgglaayl adagarsvrg itlspaqlav geqkmrargi
      241 dgqvslelcd yrdvegqydr vvsiemfeav geaywrgyfd klrqvlkpeg ravlqvitia
      301 ddrfehyrmh pdmiqtmvfp ggmlpskaif aevaakagfa ltesldfgls yartladwrq
      361 hfeaawpris elgysaafkr lwsyylayce agfrtgridv slytlepvgs s
//
LOCUS       WP_284543431             106 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Pleomorphomonas sp. T1.2MG-36].
ACCESSION   WP_284543431
VERSION     WP_284543431.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas sp. T1.2MG-36
  ORGANISM  Pleomorphomonas sp. T1.2MG-36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Pleomorphomonas sp. T1.2MG-36"
                     /db_xref="taxon:3041167"
     Protein         1..106
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=10712
     Region          2..106
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mawiylliag llevvwaygm klsagftqig asvvtivaml msfgllaiam kslplgtayt
       61 vwtgigavgs faigivvlge avtatrllaa alilaglvlm klsspa
//
LOCUS       WP_284543769             303 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Rothia mucilaginosa].
ACCESSION   WP_284543769
VERSION     WP_284543769.1
KEYWORDS    RefSeq.
SOURCE      Rothia mucilaginosa
  ORGANISM  Rothia mucilaginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Rothia.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Rothia mucilaginosa"
                     /db_xref="taxon:43675"
     Protein         1..303
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32063
     Region          1..300
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 msnpqadrvr diaklrtraa rtkkgqflve gpqavrealk ahlkkpilda vyvteaafdr
       61 hediaelleq vygtptpeeg rrvfmrvvtd evleamadsv spqgiiavsf mvdasfsllw
      121 gegalnpkli avmsrvqdpg nagtilrvad aagadlvitt kgsvdlynpk tvrstagslf
      181 hvpiiqgvql edfaedvksq gtavlaadgy gavnlqelse ytaarragve asapsgvkgn
      241 fdlskptmwl fgneaqglna eekaaatmrv avpvygsaes lnvgtaaavc lyasamaqrg
      301 vsr
//
LOCUS       WP_284543849             114 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Mycoplasmopsis
            cynos].
ACCESSION   WP_284543849
VERSION     WP_284543849.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis cynos (Mycoplasma cynos)
  ORGANISM  Mycoplasmopsis cynos
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 114)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Mycoplasmopsis cynos"
                     /db_xref="taxon:171284"
     Protein         1..114
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=12967
     Region          7..>104
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mikidkisek gnqrtnnedr vgyfiknniy lgilcdgmgg hkngdhaani aleilsmdfm
       61 nfftytnied lksfifnsim niknemkkia idspekkdmg ttlvsfmyne lekn
//
LOCUS       WP_284543911             253 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD-IIB family hydrolase [Mycoplasmopsis cynos].
ACCESSION   WP_284543911
VERSION     WP_284543911.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis cynos (Mycoplasma cynos)
  ORGANISM  Mycoplasmopsis cynos
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01484.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Mycoplasmopsis cynos"
                     /db_xref="taxon:171284"
     Protein         1..253
                     /product="HAD-IIB family hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=28327
     Region          7..253
                     /region_name="Haloacid Dehalogenase-like Hydrolases"
                     /note="The haloacid dehalogenase (HAD) superfamily
                     includes carbon and phosphorus hydrolases such as
                     2-haloalkonoate dehalogenase, epoxide hydrolase,
                     phosphoserine phosphatase, phosphomannomutase,
                     phosphoglycolate phosphatase, P-type ATPase, among others.
                     These...; cl21460"
                     /db_xref="CDD:473868"
     Site            order(10..14,49..50,196,218..219,222..223)
                     /site_type="active"
                     /db_xref="CDD:319763"
ORIGIN      
        1 mkkpkiifid ldgttldgpg ekfwekepte ytksvinrlq sqipvvvstg rgvndktlni
       61 vrklgsetyi awngaqtven gvvvkkhiid kdisqelfne ikknkcfvvy nsnvkyyafv
      121 knwfykllmg fgkksakkyn eykndfdvyk aliwslsktk ikklaekwgk mfegklevsl
      181 sgsnnvleit aanvskgsae vdfclskgid pseaihfgds mndssakgki gkliamansv
      241 eelkqmaddi teh
//
LOCUS       WP_284543965            1713 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-N-acetylhexosaminidase family protein [Mycoplasmopsis cynos].
ACCESSION   WP_284543965
VERSION     WP_284543965.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis cynos (Mycoplasma cynos)
  ORGANISM  Mycoplasmopsis cynos
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 1713)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 1713)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 1713)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 1713)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1713)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 1713)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1713
                     /organism="Mycoplasmopsis cynos"
                     /db_xref="taxon:171284"
     Protein         1..1713
                     /product="beta-N-acetylhexosaminidase family protein"
                     /calculated_mol_wt=197540
     Region          40..183
                     /region_name="Glyco_hydro_20b"
                     /note="Glycosyl hydrolase family 20, domain 2; cl03741"
                     /db_xref="CDD:446174"
     Region          189..478
                     /region_name="NAGidase"
                     /note="beta-N-acetylglucosaminidase; pfam07555"
                     /db_xref="CDD:429533"
ORIGIN      
        1 msikktlkai islasasglv amlssnnpat srqvvtnhke ykiypsvhsi eyynkhflit
       61 peinlvvedg idsavlerfe etlnlrkiky kisnkiisgk tnvliglkdn kdtfvddylk
      121 sknlmpntdl mnkidsyvln skdnvisiya sgedasyygv tslwhifnql ngleieefni
      181 ndyadiktrg aiegyygnpw slqdrlnymr wgsyyklngy fyapkddpkh shkwrelyte
      241 seienlikpl aregnrtkvr yiytlhpffg trldndydqg vkdlknkflq viqagvrqig
      301 iladdvarad irtqvrllid mvtwlkelkq tkyhdlkvvl pfvvneyagy gqsyfkkfpn
      361 evqivmtggk twgevspeft nkfytntnrg pllwinwpcs dnsknhlilg gyreflhknv
      421 dpkkvqgivl npmqqsepsk valfgaadyt wniwkddahi dqtysdafny vtnnsyqeta
      481 eskafrnlak hminqnmdgr vvaleesiel kkklakvrts letnnflvdn ikdlkvefee
      541 lyndaltikn svvnrdlyyq irywiessie lyqgltlald gliklsqgdk tdfvlnlnka
      601 ktliqkartq ygfdylgsiq yaevgvqhiq pfttwlldym snkilntnik nnnnkkdqvv
      661 gynleiakhs sindnaknnk ldyiidhnds tlawlssann gnvgkdqgie ihfesakeik
      721 sirilqdsnd kmeslkiqkl ynnqvidlen gtldfkdkke itytvpenag lmtgiritst
      781 kqtstwwkvk svdiqeknvp dpsyihtslk dksklqalrs ngsmilsndl knisknheip
      841 skgyigvdlk dikyitnini dwikndkfkf lisvngfnwi eldqanfnkk vkfrylrlvn
      901 ssdaiqilkf tklslniide ivpfgkliet nidlknnwld drkngggfdg dfnrytkfgg
      961 splkgqyaiy dlggeldlks lrmytadnta dfpryldiqv snqkdsgyet vfsindsads
     1021 rditpgqggf gnpdslhpnl rwwgnddikd kkvryikllv kkdypsraii ineivvnggk
     1081 ylnlnidprf dgtnylesng kykpenifdn klnssykpae kngkliinld aaryankdik
     1141 iiteeepsna vvkaivydik tnkeleivig alsnpivsfs lpndpekkvv alkiewkdhi
     1201 pviseiidie kqngqkvdks klktllekpv vdlekwttss rqnyiakkqs aqaindltsv
     1261 tqeavadalk alddainehk lkvdksefda liknenlknd hfiytnesfy dyqlalekik
     1321 yqnvddlgqs efnklkenle tkkialefsp ynmqislfnv ekfneinkdn ylsdsynklk
     1381 akvdeikrki tenkiepsey iklnkeyeil ysqlspkaks vliltyekyk ndvvipfiak
     1441 yknkwpeeya kindvltkne gkvsdqstdl sineaindlk nvagsiiegv arkqkeirdi
     1501 yinrktnayl vyqddkytny dkfiselavy eqhpenltse kyneiikkke ivekelvfnt
     1561 dldkvkskar siinilddkk eydkeiknan sieklsaiid qmiqqykdqe akkikdkkia
     1621 lleilkdldd kkqkdyltnk vnkitllsda kliefeidqt mmlnykkkir laindikdqk
     1681 lreksnsefn sndnkeelks fllklekles hwi
//
LOCUS       WP_284544530             616 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Acholeplasma laidlawii].
ACCESSION   WP_284544530
VERSION     WP_284544530.1
KEYWORDS    RefSeq.
SOURCE      Acholeplasma laidlawii
  ORGANISM  Acholeplasma laidlawii
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Acholeplasmatales;
            Acholeplasmataceae; Acholeplasma.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 616)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444863
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Acholeplasma laidlawii"
                     /db_xref="taxon:2148"
     Protein         1..616
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=68222
     Region          51..>419
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          407..612
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
ORIGIN      
        1 mrrklltiii iiffviiivs cddtppviqe ndypdanltl nekinwwldk ltiaekagqm
       61 vqgersnnng asgvrptdvk dlnlgsvlng ggnrpssntt fgwismyenm lnaslesssk
      121 ipiiygvdav hghnnlygat ifphniglaa annkelmkei gmitayemsq tgmnmnfsps
      181 iglikdkrwg rtyetlgesp dialnlipsy iegiqsygvi gsakhfvgdg yttfgtgldn
      241 kldrgnsiis kedletihfp lyeaaieagv ksimvsyssl ndvrmhenke litdilkdqm
      301 gftgfvigdy ngiddihant fyervikgvn agidmlmqph nfkevidaii rgvnenridi
      361 erindavsri lrvkyemglf edkepvdndl rsenalnvar rdvresmvll kndqnilpfk
      421 kdlnllilge gshnigiqsg gwtidwqgsd qlnipgttiv dafksvtngq iytdindidk
      481 adqiiivfse kpsaemmgds lalsltddts yasnqalidi akqankpvig lllsgkplii
      541 eevipyldaf vmlflpgseg lgitdvlygd ydfkgklpft wpksisqssh tildenyess
      601 dyrypfgygl sytilq
//
LOCUS       WP_284544664             160 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Acholeplasma laidlawii].
ACCESSION   WP_284544664
VERSION     WP_284544664.1
KEYWORDS    RefSeq.
SOURCE      Acholeplasma laidlawii
  ORGANISM  Acholeplasma laidlawii
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Acholeplasmatales;
            Acholeplasmataceae; Acholeplasma.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 160)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Acholeplasma laidlawii"
                     /db_xref="taxon:2148"
     Protein         1..160
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18672
     Region          4..158
                     /region_name="NUDIX_MutT_Nudt1"
                     /note="MutT homolog-1 and similar proteins; cd18886"
                     /db_xref="CDD:467596"
ORIGIN      
        1 mqflytlcfi krgnsilmln inkspwfgiw ngvggkrnqd etpldcihre ileetkikvd
       61 kaaiydrgiv twngefntps lglhlyfvev pkdfnyltpi etregilawk eidwianken
      121 lgvsynipyf imnviqdekr yhyycefkgn ellsvevkvl
//
LOCUS       WP_284544972             541 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Acholeplasma laidlawii].
ACCESSION   WP_284544972
VERSION     WP_284544972.1
KEYWORDS    RefSeq.
SOURCE      Acholeplasma laidlawii
  ORGANISM  Acholeplasma laidlawii
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Acholeplasmatales;
            Acholeplasmataceae; Acholeplasma.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Acholeplasma laidlawii"
                     /db_xref="taxon:2148"
     Protein         1..541
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=61945
     Region          <94..540
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mlnnflnkns kftyspftkw llillmvvvv alvvyifggs rysythlmyi piliagyalg
       61 fwqtliiali sglvlgpfmp qdvqaglmqp pttwifravi fiaigainal lnkqikayqk
      121 lelerlyvss itnypnlnkl kydldefies ktpfsllgfr ivnmnsirqn mtyeigtkvl
      181 ikisemlsdn hknmvysiya nevaaiipts dfnkayeigl nllnkmadsi aidryqigil
      241 lngsivqypl hikdaqdalk ksamildqtt ndfglhefdd emerrsklhg elipellhai
      301 kenefhlvyq pkisldgseq lsveallrwh hpykgmispi vfipvaeesg lineitktvi
      361 rkvieqsllw kekgldvkts inishrdfnh kdfltyihks maecqidpsf iefeitergv
      421 lerndniikl ftnlrdmgik isiddfgtgy nslihlvqvp mdfvkldrsf iinitkpkyq
      481 kmiqrlisla hdldikviae gvetkeqldi lkdmncdivq gyylskplea daleafyknr
      541 v
//
LOCUS       WP_284545157             100 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Acholeplasma
            laidlawii].
ACCESSION   WP_284545157
VERSION     WP_284545157.1
KEYWORDS    RefSeq.
SOURCE      Acholeplasma laidlawii
  ORGANISM  Acholeplasma laidlawii
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Acholeplasmatales;
            Acholeplasmataceae; Acholeplasma.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Acholeplasma laidlawii"
                     /db_xref="taxon:2148"
     Protein         1..100
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11335
     Region          2..100
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mqscsverav nlfgdkwkfl iirdlmdgkm rfselknsig nisqkvltqn lrslesngll
       61 trtvypvvpp kveyeltelg yslklvidal rkwgeiyaka
//
LOCUS       WP_284545469             685 aa            linear   BCT 25-DEC-2024
DEFINITION  elongation factor G [Acholeplasma laidlawii].
ACCESSION   WP_284545469
VERSION     WP_284545469.1
KEYWORDS    RefSeq.
SOURCE      Acholeplasma laidlawii
  ORGANISM  Acholeplasma laidlawii
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Acholeplasmatales;
            Acholeplasmataceae; Acholeplasma.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Margus,T., Remm,M. and Tenson,T.
  TITLE     Phylogenetic distribution of translational GTPases in bacteria
  JOURNAL   BMC Genomics 8, 15 (2007)
   PUBMED   17214893
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 685)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Acholeplasma laidlawii"
                     /db_xref="taxon:2148"
     Protein         1..685
                     /product="elongation factor G"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=76843
     Region          1..685
                     /region_name="FusA"
                     /note="Translation elongation factor EF-G, a GTPase
                     [Translation, ribosomal structure and biogenesis];
                     COG0480"
                     /db_xref="CDD:440248"
ORIGIN      
        1 mkeyktknlr niallghlgs gktsltesll nvtgvtnvkg everkntksd flveeqtria
       61 smqtslipie ahdcklnfld vpgndelise lyhalevvkg avilidatkg vevgtervwn
      121 eirrrripav lfinkmdkdn idyealledi rtklgkravp ftypigrked fegfvnvvem
      181 kariyngntc edaeiwdekk pkveqlremi mesvaetsee llekyfggee itneeithal
      241 nhaiingelt pvlvgsvlkn igvntllkml tdflpspdml releatkvgs deklqvktld
      301 eepfsgfvfk tmidpfvgti sfikvnsgil kvgdevyhaq sdstikintl mtligkdqip
      361 mdlahagdiv vttklealkt ghtitdpkrk ivfdtvklpt pviyqaiepd nekdedkism
      421 altklniedp sfdiqrnket gqlliggygi shikyitdrm knlykvsvsf edqkivyret
      481 ikkkgvgegk hkkqsggagq fghvwirfep tdklfefsee vfggavprsy fpavekglir
      541 afekgplagf pvihvkatly dgsyhsvdsn eisfvmaadl afkaalpeiq ptilepilhl
      601 titvkesyvg dvmgdmnkrr grilgmdqad gytvinayvp eaevttyaid lkamtqgsgq
      661 ferrfdryee vpqqfqskii eqykk
//
LOCUS       WP_284545611             486 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Acholeplasma laidlawii].
ACCESSION   WP_284545611
VERSION     WP_284545611.1
KEYWORDS    RefSeq.
SOURCE      Acholeplasma laidlawii
  ORGANISM  Acholeplasma laidlawii
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Acholeplasmatales;
            Acholeplasmataceae; Acholeplasma.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18609803
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Acholeplasma laidlawii"
                     /db_xref="taxon:2148"
     Protein         1..486
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=54184
     Region          48..361
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
     Region          322..483
                     /region_name="DUF3520"
                     /note="Domain of unknown function (DUF3520); pfam12034"
                     /db_xref="CDD:432277"
ORIGIN      
        1 mkkiltiifl sslliflvac sgkynggylq denynyifnd dehqeiienp fidvsvnnks
       61 nislsantas ysfirsqins gravdrnavr ieemvnffny nynqpetdkt fgfkseliqt
      121 pwnnethlll igletkqvdl gdipsnivil ldvsgsmsat nklslakkam ellieqmkpn
      181 dvislvtyss gekvvfkgks iddmaymtsq irllkasgat agkkgldmay evaeeyfieg
      241 gnnriilatd gdfnvgisst dmlieyisek resgiyfsay gfgygnfkde klervakagn
      301 gtyhyiddii sarkafvdni dgvlytvard akaqiafdas avleyrligy enrqltddef
      361 ddgttdagei gtglqvtaiy elklnegasd vgsltirykn hditddtqle eaftvlnain
      421 enpsvdakfi ssvvefglil mdskykvdad lgavleriet esynledyyr ndfidvlkty
      481 kdmtts
//
LOCUS       WP_284545755             261 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Acholeplasma
            laidlawii].
ACCESSION   WP_284545755
VERSION     WP_284545755.1
KEYWORDS    RefSeq.
SOURCE      Acholeplasma laidlawii
  ORGANISM  Acholeplasma laidlawii
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Acholeplasmatales;
            Acholeplasmataceae; Acholeplasma.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Acholeplasma laidlawii"
                     /db_xref="taxon:2148"
     Protein         1..261
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30400
     Region          35..246
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 madnnkkvdh dfqllknvke vklakdynff nhnpffkfls fftvfvikml vfyvfgvvfr
       61 glrikgkknl khlkkerfil vsnhlhvlda iwigtlifpr kiyvtmlqsn lglpfvgkil
      121 rvaggipipe tkelmvhfld elktelskkt pvlvmpeasi kpyhvgirkf lsgafrfaad
      181 adakilpfvy iyknpnfiqr lymkkprihl hilepievih getkqqtltl tknkvhqims
      241 dyfnkhsdlk eenynetaei d
//
LOCUS       WP_284545988             264 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Salmonella enterica].
ACCESSION   WP_284545988
VERSION     WP_284545988.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14398449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..264
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29738
     Region          32..112
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          175..255
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 miglrldgyd pdlhhdaava fcirarddel fsprhqhrkg qlilalhgai tcevenamwm
       61 vppqyavwlp gslphsnhvt agaelcflfi epaavvmper cctlkisplc relilslarr
      121 tdperaqmpt qrliqvlfde lpqqpqeqlq lpvsghpkir qmvetmaqep arwntlgqwa
      181 svfamsernl arlvvketgl sfrrwrhqlq lilalqalia grnvqqtaqm lgydsitafi
      241 tmfkkglgqt pgqyltgell lphn
//
LOCUS       WP_284546264             443 aa            linear   BCT 25-DEC-2024
DEFINITION  KAP family NTPase [Salmonella enterica].
ACCESSION   WP_284546264
VERSION     WP_284546264.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10542449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..443
                     /product="KAP family NTPase"
                     /calculated_mol_wt=50754
     Region          15..318
                     /region_name="KAP_NTPase"
                     /note="KAP family P-loop domain; pfam07693"
                     /db_xref="CDD:462231"
ORIGIN      
        1 mletlsfter defqrrniae niikllkpea displvidga wgtgksefsi klknliieqe
       61 teskvvyvda fkgdhaespl llitsaiasi lpeeekqnfi krslpairfg lktvlkagag
      121 wflrqeasev aeefqdamkk asnaaidgti eniledhmes ekninslksc iediskkqki
      181 viiideldrc kpsfstniie tikhifdinn vffilvtnte qlkasinhiy gysinsqkyl
      241 dkfikytitl pdtclinghn vcktsviywd hlvgettlln kinslvgsfi cdliqrtnls
      301 lretqtfsrn lnifrllndn ecksndpfin mivvvavfih cfgdkeklkq eitaesisyl
      361 adllnikeip ysyerrsqip eisiiffgii kdsitlnerf apksdeelkk ftnvytdyeh
      421 lkfwsttpre lmikyinqms fiq
//
LOCUS       WP_284546391             535 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Metapseudomonas otitidis].
ACCESSION   WP_284546391
VERSION     WP_284546391.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..535
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=59461
     Region          <18..517
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mpdthdrpar prtgrmkrdi vlillfalvs lallvhfdvg dllqraavrh ehweldeill
       61 mlslvgwcgf ifgvrrlmem rweaqarrsa elkvtrlaeh dmltglpnrr glrshlepcl
      121 gvsdspfyfa lvdldgfrlv ndlhsheagd hllqvlarrl atalpegdli grsgadeftl
      181 vlhsqkshta asallealle lirqpvqhed arievsatlg varypddgrr lddlmaraaf
      241 cvqsgkregr nmvvfyepgn dteleqqtrl vklldegmka gylrvdyqpi valesgeilg
      301 fealarldhp eagslgpaqf ipaaerlgyi tritrellqr aceearqwpt gvflsfnlsa
      361 idladeslpf hvsrilnkvg fpprrlelev tetavidhve rananiqalq amgirvsldd
      421 fgtgysslah isrynfdklk idrqfvaald ngskdesilr amlglsqelg iptvaegiet
      481 qrqlewlqsv gcrqgqgyyf sppvstaqat amvargpcll gpvprpsarp hstes
//
LOCUS       WP_284546419             456 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Metapseudomonas otitidis].
ACCESSION   WP_284546419
VERSION     WP_284546419.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..456
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=50697
     Region          <191..453
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mpasqpffkr lkqlwlahdl aligqrrerr mrllaslvml vigvlwgavf aarsawliva
       61 mdlllvlcgi gvlaltlrnr arsanlllfa vlvvvisist llldepspaa prashlyllp
      121 vsvaalmafr depmwlrygv slfclalftv mastswspgl gyglpdelrv igswvqsiaa
      181 avmlflllhi lqtdaaerse ldrdlrtalr eqqfvlhyqp qldiegrvlg aevlirwqhp
      241 qrgllapaef idhaektgli ipigqwvlhe tcaqlatwka iplfrelhla vnisqnqfrq
      301 atfvndvlgl iqrsgieahn leleltetli vqdmedlsrk mtalvehgvr fslddfgtgf
      361 sslshlkrlp ldklkidrsf vcdvltdsss etivrtvial gqsmgmsvia egvetqaqqr
      421 fladsgclqy qgylfsrplp lqafqafvse raaqac
//
LOCUS       WP_284546437             250 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Metapseudomonas otitidis].
ACCESSION   WP_284546437
VERSION     WP_284546437.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..250
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28437
     Region          29..249
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mrflsaflil lfpafalaga dtlrvdlrdr ppemwsidgr ptgplvkvle vaaeraglhl
       61 ewryapfars ladlregrid lvprvlpdpe rdrylhylps igtqdkdilf airptqqver
      121 yedlaplrig vkrsslyfpr fdadtalhkq pavdddilvr mfragridai avldkaaidt
      181 afdnirfrdy ayaglrepir ienrfaasqk lydsgraaly drlgreldam rrngdvvsiy
      241 reqgvepptp
//
LOCUS       WP_284546447             315 aa            linear   BCT 25-DEC-2024
DEFINITION  FecR family protein [Metapseudomonas otitidis].
ACCESSION   WP_284546447
VERSION     WP_284546447.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20752687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..315
                     /product="FecR family protein"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0016989 - sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34145
     Region          19..58
                     /region_name="DUF4880"
                     /note="Domain of unknown function (DUF4880); pfam16220"
                     /db_xref="CDD:435227"
     Region          68..313
                     /region_name="FecR"
                     /note="Periplasmic ferric-dicitrate binding protein FecR,
                     regulates iron transport [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG3712"
                     /db_xref="CDD:442926"
ORIGIN      
        1 mnddlqpltd pdgrhplrde ahawllrlts geaagrdaea frqwcarsta haaafrqvhg
       61 lwqalgpave rlaspaapvi plpsrrigrr aflggaiaas valvmlrpal hdrgdystav
      121 geqrrieage glvlelntdt rikrqatgag rvnlevlege vdvlarvpvr ilaaggtvda
      181 qgarfnlrar egqvcvtcla gnlslvlqgn alvlpagrql rydpqqwgep qpfdaeqvta
      241 wrrqmlvfdd tplaevidei nryrpgmill lnaqlgqrrv qarfrldqla qvaglirday
      301 garvaelpgg vllvg
//
LOCUS       WP_284546575             330 aa            linear   BCT 25-DEC-2024
DEFINITION  FecR family protein [Metapseudomonas otitidis].
ACCESSION   WP_284546575
VERSION     WP_284546575.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20752687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..330
                     /product="FecR family protein"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0016989 - sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35635
     Region          15..55
                     /region_name="DUF4880"
                     /note="Domain of unknown function (DUF4880); pfam16220"
                     /db_xref="CDD:435227"
     Region          85..316
                     /region_name="FecR"
                     /note="Periplasmic ferric-dicitrate binding protein FecR,
                     regulates iron transport [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG3712"
                     /db_xref="CDD:442926"
ORIGIN      
        1 msmpqaepqa rrdialdwll rlqqapadaa leaacrawrq aependaafr kaerlwhltg
       61 qlpattrpdw palppaaeag arvialparp pqrrrwlaga iaaclvlglg aglrtplead
      121 yrtargelkt veladgsrvq ldgdsaiava fssgrrevrl lrgqaffdva rdrerpfhvr
      181 aaaldvqvtg tafnvdlgaa rpavavahgs vrvvdqevgr elaaglgagq tlvldadhha
      241 rqgsqpvgqv aawrdrrlia dnarladmve rlepylpgvv llrdaelaer ritgvydlrn
      301 peaalramaq phgghvasws pfllvisrge
//
LOCUS       WP_284546686             319 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Metapseudomonas otitidis].
ACCESSION   WP_284546686
VERSION     WP_284546686.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..319
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=35493
     Region          25..248
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mkrclpllla cvactvgaae rlvypmhshg adpeayvvel lrlaldhsgg dyrlepslep
       61 vpqsraqysl eqndgnfqvm wtmttrerea vlapiripiy kgligwrvpl vradqaqrla
      121 avtsldalka lrigqrhdwp dtailrangl tvltspsyeg lfrmlqagrf dlfprevvva
      181 wdeekrareq gldlavdehl vlhyptafyf ftskarpdla aaierglega iadgsydalf
      241 qrthgesirr arldqrrvie lqnpdlpdtv plgraelwyd plarpasarn amadgksreh
      301 parlqapntt apvhtpgvp
//
LOCUS       WP_284546808             366 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Metapseudomonas
            otitidis].
ACCESSION   WP_284546808
VERSION     WP_284546808.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..366
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40805
     Region          <22..332
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mhlltlppsp tlatsirata qvfedprsqa llahlqqvap seasvliige tgtgkelvar
       61 hvhnlsgrrn gpfvavncga fseslveael fghekgaftg alaakagwfe eanggtlfld
      121 eigdlpmpiq vkllrvlqer evvrlgsrks ipinvrvlaa tnvhlekain aghfredlyy
      181 rlnvvslqlh plrerpgdil plarhfvaey srrlgysdvt lsedaarrla sydwpgnire
      241 lenvihhtll icrdrlirae dlhlsnlrie rqddsrpree saddllqraf erlfeeqsga
      301 lhekvedall raayrfchhn qvhtasllgl srnitrahli rigelvvnkr rpaqsaqggr
      361 vinlsi
//
LOCUS       WP_284546833             791 aa            linear   BCT 25-DEC-2024
DEFINITION  efflux RND transporter permease subunit [Metapseudomonas otitidis].
ACCESSION   WP_284546833
VERSION     WP_284546833.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Sandhu,P. and Akhter,Y.
  TITLE     Evolution of structural fitness and multifunctional aspects of
            mycobacterial RND family transporters
  JOURNAL   Arch Microbiol 200 (1), 19-31 (2018)
   PUBMED   28951954
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Hand,N.J., Klein,R., Laskewitz,A. and Pohlschroder,M.
  TITLE     Archaeal and bacterial SecD and SecF homologs exhibit striking
            structural and functional conservation
  JOURNAL   J Bacteriol 188 (4), 1251-1259 (2006)
   PUBMED   16452406
REFERENCE   3  (residues 1 to 791)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
REFERENCE   4  (residues 1 to 791)
  AUTHORS   Arkowitz,R.A. and Wickner,W.
  TITLE     SecD and SecF are required for the proton electrochemical gradient
            stimulation of preprotein translocation
  JOURNAL   EMBO J 13 (4), 954-963 (1994)
   PUBMED   8112309
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..791
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86876
     Region          11..774
                     /region_name="MMPL"
                     /note="Predicted exporter protein, RND superfamily
                     [General function prediction only]; COG1033"
                     /db_xref="CDD:440656"
ORIGIN      
        1 msnhhqdkat flerlifnnr pgvivicllv siflfwqatq vrpstsfekm iplhhpfiqk
       61 mmehrndlan lgntvrisve akdgdifskd ymetlrqihd evfyipgvdr sglkslwsps
      121 vrwtevteeg faggevipqt ydgsadslee lrnnvlksgq igrlvannfk ssiidvplle
      181 sypdpndqgk llkldyrqfs heleekirdk yqaqnpnvqv hivgfakkvg dlidglimvv
      241 affgiafltt lvllywftwc irstiavlst tlvaviwqlg lmhsvgfgld pysmlvpfli
      301 faigishgvq kingialqss dadnaltaar rtfrqlflpg miailadavg fitlliidig
      361 virelaigas igvavivftn lillpvaisy vgiskkaidr skkdatrehp fwrllsnfah
      421 ptvapisvvi aimafggglw ygkhlkigdl dqgapelrpd srynkdnnfi isnystssdv
      481 lvvmvktkpe gcsthealap idelmwtmen tqgvqsaism vtvskqvikg mnegnlkwet
      541 lsrnqdvlnn sisradglyn tdcslapvlv flndhkaetl qravkavqgf aqehnkdgle
      601 fllaagnagi eaatneviaq teltililvy icvaamclit frsipatici vipliltsvl
      661 gnalmaflgi gvkvatlpvv algvgigvdy giyiysrles flragltlqe ayyqtlkstg
      721 kavlftglcl aigvatwmfs aikfqadmgl mltfmfivnm fgalwllpal arflikpekl
      781 agktggslla h
//
LOCUS       WP_284546864             339 aa            linear   BCT 25-DEC-2024
DEFINITION  MraY family glycosyltransferase [Metapseudomonas otitidis].
ACCESSION   WP_284546864
VERSION     WP_284546864.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Anderson,M.S., Eveland,S.S. and Price,N.P.
  TITLE     Conserved cytoplasmic motifs that distinguish sub-groups of the
            polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase
            family
  JOURNAL   FEMS Microbiol Lett 191 (2), 169-175 (2000)
   PUBMED   11024259
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Lehrman,M.A.
  TITLE     A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P
            transferases
  JOURNAL   Glycobiology 4 (6), 768-771 (1994)
   PUBMED   7734839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10160628
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..339
                     /product="MraY family glycosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=36858
     Region          30..286
                     /region_name="GT_WbpL_WbcO_like"
                     /note="The members of this subfamily catalyze the
                     formation of a phosphodiester bond between a
                     membrane-associated undecaprenyl-phosphate (Und-P)
                     molecule and N-acetylhexosamine 1-phosphate, which is
                     usually donated by a soluble UDP-N-acetylhexosamine
                     precursor; cd06854"
                     /db_xref="CDD:133464"
     Site            91..92
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133464"
     Site            208..211
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133464"
     Site            order(257,268..271)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:133464"
ORIGIN      
        1 mnfllllpfl alaaflltgv mrryalsrsl mdvpndrssh klptprgggv avvlcffisl
       61 calltvglie wsifvafmga gtstallgfl ddhghiaarw rllghfaaaa walfwlggfp
      121 pltimgveld lgwighllaa fylvwmlnly nfmdgidgia sveavcacgg galliwfaas
      181 ptlpilplcv afsvvgflfw nfppakifmg dagsgflgit lglltiqaaw ldmhffwgwl
      241 illgvfitda tftlirrlln gekpyeahrs hayqyasrly grhlpvtlav mainiiwllp
      301 lallvgtgnl ndlvglalay aplvllciky ragvkersa
//
LOCUS       WP_284546976             191 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Metapseudomonas otitidis].
ACCESSION   WP_284546976
VERSION     WP_284546976.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..191
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21216
     Region          10..128
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 madrlyydrt qgappwpell kalellgrtd glaidlgcga grdslellrr gwqvlavdka
       61 aealerlqaq ldpawaprlq trcepfehte lpaarlvnsa falpfcapah fpglwqrier
      121 alaggglfcg nllgerddwa spevctftrt qleallagwe vlhleeidrd gttargrtkh
      181 whlygliarr p
//
LOCUS       WP_284547032             504 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Metapseudomonas otitidis].
ACCESSION   WP_284547032
VERSION     WP_284547032.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..504
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=54515
     Region          3..369
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mkktftqsma wlhtwgglla gwllfavflt gtlavfdqei dhwmhpevrd tpvptaeaae
       61 rglaylrqhh pearawtlnl pterspglsv sagerrhggg valdpatgev lpqrdsaggl
      121 fffrfhftld lprmlgiwvv gllalgmlva lltgivihkk ffkefftfrp gkgqrswlda
      181 hnatavlllp fhlmiaytgl aiflliympa aldslfdgdv eayfhaqsgt eeahpprgqv
      241 qpaplaalap mlaeaerqmg pvggvvirhp grsdarvevr rvlgnrialt kgqnmvfdgv
      301 tgallqappa mrasvlthrv imglhfaqfg gypmrwlyfl cglggcvmia tglllyevkq
      361 rrqaspgvga rlvaalnlaa vaglgvacvg llwanrllpl elagraqwev rvffllwlas
      421 lvhavwrpga rgwseqlgcg aalclgvpll gwatgsgagd ftrgmlevta vaiglllagc
      481 awrvqqpaav rparvrrpka evqg
//
LOCUS       WP_284547107             604 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Metapseudomonas otitidis].
ACCESSION   WP_284547107
VERSION     WP_284547107.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 604)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..604
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=64320
     Region          6..513
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mdetrillal ggiglaalcs qwlawrlrlp ailflllsgi lagpvlgvld pgalfgpllf
       61 pltslavali lfegsltlhl sewreigsvv rrmvtlgala twvviavath lllgfswela
      121 vlfgsltlvt gptvivpmlr vvrprasvan ilrwegivid pigalaavvt fsfivsrdqg
      181 gwsqslatfa gvigcgtllg vlggwalgvv lrrhwlpeyl hnlaalaavl gvfiasnllv
      241 hesgllavtl mgmwlanmrg vdvkpilhfk enlsvllisg lfillaarld lkallalgpa
      301 tlallaviqf iarplnigls tlgsalgwre rallawiapr givaaavsai falrlqehgd
      361 pnaqllvplt flviigtvvl qsatarplar llgvaepapa gfliiganpv aralgkalnq
      421 lgsrvlltds sweniraarm dglptyfgnp tsqhadahld lvglghllal spssemnala
      481 cmrfrhdfae prrftlpsga dsrrsdkhrs seqvrgrelg lpaltypqfa srlgrgaeir
      541 ittlteafdw aayqalhgnr atlllardtr gwvhiagpsq alepqpgwsl valvdadtvs
      601 daes
//
LOCUS       WP_284547204             452 aa            linear   BCT 25-DEC-2024
DEFINITION  spinster family MFS transporter [Metapseudomonas otitidis].
ACCESSION   WP_284547204
VERSION     WP_284547204.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..452
                     /product="spinster family MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006869 - lipid transport [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48315
     Region          18..421
                     /region_name="MFS_spinster_like"
                     /note="Protein spinster and spinster homologs of the Major
                     Facilitator Superfamily of transporters; cd17328"
                     /db_xref="CDD:340886"
     Site            order(28..29,32..33,36,69,119..120,122..124,127,147,
                     150..151,154,243,246..247,250..252,255,284,288,340..341,
                     345,349,369,372..373,376..377,380)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340886"
ORIGIN      
        1 mqnnnngyps glrawttvai lmvayvlsfi drqilnllvg pirrdlvisd tqmsllmgls
       61 falfytvcgi plgrladtrs rrgliaigvl fwsaataacg laklywqflv crigvgvgea
      121 alspaaysli adsfprerra taisvysmgv ylgsglaflv gglvikfasa qgdvhlpllg
      181 dvrpwqlifl ilgaagvlft llmlavrepe rrgvgsgvav plsevgrylr snrrtvlchn
      241 lgfaglsfag ygsaawipty yirthgwdag hvgvvygslv avfgclgvvf ggrladwmak
      301 rgrsdanmrv gllaalgalp lvilfplldd aawvtvvmap tvfclsmpfg vapaaiqeim
      361 pntmrgqasa iylfvitlig lglgptaval vtdfvfaddq alrwsllivt tlavgssvvl
      421 lwmglkpyre sverlkqwva psvmptaklv da
//
LOCUS       WP_284547269             247 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Metapseudomonas
            otitidis].
ACCESSION   WP_284547269
VERSION     WP_284547269.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..247
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27774
     Region          5..172
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mssnalytdl sayydlmcad idyqaqshcv rrlhqlfgts grrhldlacg tgphvrhfld
       61 fgyasagldi nqpmldlaql rcpeaqfsrq dmasftvdap qdlitcflys lhynpglapl
      121 qaclervhga laaggvfcfn tvdkrqidnq sfvrhsvehe gsaftfgsgw fyrgegeqqa
      181 lrlciekttd gvtqrwedeh pmvatgfdel qqllaprfev qvfehdyeri tpwdghsgna
      241 lfvcvkr
//
LOCUS       WP_284547282             199 aa            linear   BCT 25-DEC-2024
DEFINITION  IMPACT family protein [Metapseudomonas otitidis].
ACCESSION   WP_284547282
VERSION     WP_284547282.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Park,F., Gajiwala,K., Eroshkina,G., Furlong,E., He,D.,
            Batiyenko,Y., Romero,R., Christopher,J., Badger,J., Hendle,J.,
            Lin,J., Peat,T. and Buchanan,S.
  TITLE     Crystal structure of YIGZ, a conserved hypothetical protein from
            Escherichia coli k12 with a novel fold
  JOURNAL   Proteins 55 (3), 775-777 (2004)
   PUBMED   15103642
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Okamura,K., Hagiwara-Takeuchi,Y., Li,T., Vu,T.H., Hirai,M.,
            Hattori,M., Sakaki,Y., Hoffman,A.R. and Ito,T.
  TITLE     Comparative genome analysis of the mouse imprinted gene impact and
            its nonimprinted human homolog IMPACT: toward the structural basis
            for species-specific imprinting
  JOURNAL   Genome Res 10 (12), 1878-1889 (2000)
   PUBMED   11116084
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..199
                     /product="IMPACT family protein"
                     /calculated_mol_wt=21278
     Region          1..192
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 mpftlagpce yheeirksrf ialaapvtsa aeaqafiath sdpaashncw awkvgaqyrf
       61 sddgepggta grpmlaaieg qdmdrvavlv irwyggiqlg tgglaraygg saakclqgge
      121 rtellalqrl rghvafaela pfkarlaehq arledeayda egawlelalp aerqaalqqv
      181 ladlsrgrsq lqpveevap
//
LOCUS       WP_284547286             274 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Metapseudomonas otitidis].
ACCESSION   WP_284547286
VERSION     WP_284547286.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..274
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30752
     Region          53..155
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mngyldlnra nwddraplha asadyqverf vrdpghlsdv vrfdqprlgd ivglrgvhlq
       61 chigtdtlsl arlgarmtgl dfspaslkqa relarrcdap lefveaevca adqalprasf
      121 dfvytgigal cwlpsirdwa rtvaallkpg gwlfirdghp mlwtvneert dglvieypyf
      181 erpepmiwdd assyvetdrp ltatrthewn hglgeiital lengmtltgl eehrslpwea
      241 lpgrmhrvsg gewrlieapd rlplsytlqa vkrg
//
LOCUS       WP_284547318             360 aa            linear   BCT 25-DEC-2024
DEFINITION  fatty acid desaturase family protein [Metapseudomonas otitidis].
ACCESSION   WP_284547318
VERSION     WP_284547318.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..360
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41701
     Region          9..358
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mrhdrpldae aarafgeeld alrqrtladl getdaryirr vrsiaraccw sgrallmlgw
       61 fpptwllgsl mlglgkiien melghnvmhg qydwmndpef agrtyewdiv gpadfwrhth
      121 nhihhtytnv lghdddvgyg lvrlfpeqrw kpffrwqplw vtlqallfqf avavqhlrld
      181 kylkgrmtle elrprlrtfn akvlrqlvkd ygvfpllall lganawavla gnalanlirn
      241 lwtftvifcg hfteraavfp pevlegetrg qwylrqlrgs snleggpllh fmtgnlshqi
      301 ehhlfpdlpa rrygqlavev reiarrygqe yntgrlsrqf atvlrriwvy rrpetalpaa
//
LOCUS       WP_284547503             428 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Metapseudomonas otitidis].
ACCESSION   WP_284547503
VERSION     WP_284547503.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..428
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45564
     Region          30..403
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mnapqttlpa slwaatatpa patpalaeda rvdvaivgag ytglvtalhl aaagtrvcvl
       61 dagepgwgas grnggqvipg lkydpdalrk rfggaeaerl idvaggaade vfalierhai
      121 dcdatrrgwi qpaaspaalr tiegraeqwr rhgvpvelld reqvtrrigs phylgawvdp
      181 ragsvqplsy arglvraaqa egarihghsr vtglsaqsgg wrlatagghs vhaervllat
      241 ngytdalwpg lrqtvlaans fivatrplpe alrrsvlpgg evcsdarrll lyfkqdaqgr
      301 lllggrgpfa eprqagdwah leqslthlfp qlagapidyr wsgrvaltqd flphlhepap
      361 glsillgyng rgvalatalg rrmaqrmlgs eeafpfpasp irriplhglq rlylgagiaw
      421 yrlldmlg
//
LOCUS       WP_284547549             478 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Metapseudomonas otitidis].
ACCESSION   WP_284547549
VERSION     WP_284547549.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..478
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50614
     Region          40..477
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mytrlldalg vsrrsllrlg gaalltglar ggqaspggpp drqvdvvvvg aglsglvaar
       61 rlvaagcrvq vlearervgg rtlnqplgeg ievdgggqwv ggsqqavmrl agelgvplvp
      121 qytqgemaal iqgqrytfpp egpgpkaral mdrleamaar vppeapwkap raeawdamsv
      181 aawlkaqrad eeaveavatt lsttlasepg rvsllwflfy lrsaggftal ddqaqqyrlr
      241 ggaqrlslll aeplgdslit gspvsridgw legplrvhse ravisaeqvv vammpadvsr
      301 igfspalppg realqrnwaa sggikvhlry papfwraagl sgaglvtdgl vqmtvdstpe
      361 gqgdgvllaf ldparaggdp arrrkrvlre lsrllgdeaa rplayveqdw sqerwsagcv
      421 splppgvlar nghwlraplg rlhwagseas piwcgylega vragervaqe vlvalgra
//
LOCUS       WP_284547602             658 aa            linear   BCT 25-DEC-2024
DEFINITION  BCCT family transporter [Metapseudomonas otitidis].
ACCESSION   WP_284547602
VERSION     WP_284547602.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..658
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=72495
     Region          2..510
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mearssspst lnppvfygsa vlvialvlys tlardqaqwl fgqiqqwivl naswfyvlsv
       61 alilitvvfl avsrfgdirl gpdhsrpdyg ngtwfamlfa agmgiglmff gvaeplmhyv
      121 nppvgdphtv aaakeamklt ffhwglhaws iyaivalila ffcfrhdlpl tlrsalypli
      181 gdriygpigh avdifailgt vfgiatslgy gvlqingglh hlfgvpvstp vqlaliagtc
      241 glatlsaasg lnkgikvlse lnlalatllm llvlvlgptv fllqtfvqnt ggylseivsk
      301 tfnlyayept dwiggwtlly wgwwlswspf vglffarisr grtirefvcg vlfvpagftl
      361 lwmtifgdta ihmvlnqgyl dlvetvqqds slalfafldh fplstllsll avamvvvffv
      421 tsadsgalvl dmlasggken tplwqrlfws iltgvvamal lladglkalq tatiasalpf
      481 aavllaatwg llkalrldat krgiryqala lsrpaqqqlg gwqrrlrnil mfprrshvtr
      541 fidevvrpac levadelrkq gcavavlnge dgrcklnvgh geevdfsyev rprslllprf
      601 mareggeeng darkyfraev ylreggqdyd vmgwsreevi gdlldqyekh lhflhvvr
//
LOCUS       WP_284547777             262 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Metapseudomonas
            otitidis].
ACCESSION   WP_284547777
VERSION     WP_284547777.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..262
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28824
     Region          1..255
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mpryalitga ssglglalae alarrgrhli lvarqrdale siayeltqrf gvevlyrtcd
       61 laeplqlsgl lhelnqggrq idllvnnagi gsaglyvqqp wgreqeliel nilalarlch
      121 eiggamagrg egqilnvasv agfqpggwms nyyaskayvl hfseglreel krhgvkvsvl
      181 cpgpvrtaff rharmagekl egspllmsae evalytvral eknraiiipg wrnrlaakaa
      241 rfmprwltrr ltarinrrfv tg
//
LOCUS       WP_284547787             403 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Metapseudomonas otitidis].
ACCESSION   WP_284547787
VERSION     WP_284547787.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..403
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=44513
     Region          27..378
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mrplivllhr ylglatalfl alagltgsll afqheidewl npafyhapar gpllspgelv
       61 qrieqaeprl qvwymevpde aghsalmaav prtdpatgap ydlhhrviyl dpvsgaelgi
      121 rqwgacclqa qnlipfllef hytlalpgnw glilmglvai lwvidcfaga wltlprgrpf
      181 lkkwwtawtl krgagryrrt ldqhragglw lwllllpvav ssvamnlpep vfkpvvslfs
      241 eappstyqqr sqmprealge trldyqqvyr laqaegarqg ieggigelyy sveynffgag
      301 fgghdanple kswlffdgtd grligaevag rgtpgerfyr lqapihggri aglpgrivia
      361 llglaiagls vtgvviwwrk rqarrasaar aregrraafg qnl
//
LOCUS       WP_284547809            1637 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Metapseudomonas otitidis].
ACCESSION   WP_284547809
VERSION     WP_284547809.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 1637)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1637)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1637)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1637)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1637
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..1637
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=178608
     Region          39..1634
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mssykgllla lslgllaacd sstpehtaek aaaepaaqvq aprapvdtaa lakryagrel
       61 kvvdisevql dgasalsvtf svpldpeqpf aerlhlvdka sgkvdgawel ddnlmelrlr
      121 hlqpkrdlel tidaglrgvn darlasasvs qlrtrdlqps vgfasqgsll psrlaeglpv
      181 ialnvdavdv dffrvrpael pkllarwgrr sqmsywdsda llrtadlvys grfdlkpapn
      241 trenlllpia gieplkpagv ylavmrragr ysysnpatlf tlsdiglsah rfggrldvfa
      301 qaleggkpqa evnlqlldpe gtvlaegktd dkghlqlplt dkgrvlvghq gdqisllrld
      361 tpaldlsefd iagpaqqplq ffvfgprdly rpgetvllna llrdrdghal apqpvnvevr
      421 rpddqvsqsf vwspdangly qhqlalsgda ptgrwqllid lgnghkqlye fqvedflper
      481 maleikgsdt plesgdvarf qvqgrylyga paagnrltgq lyvrplreav kalpgyqfgs
      541 vteeelsqdv eldevkldea gkgalelesr wasarsplsl tlqasllesg grpvtrrleq
      601 pvwpaarlpg lrgvftddqv dmngmaevel liadpegnkl aaqgvkvrlv rerrdyywsy
      661 dddgwnyhyn ekflisderl vdvaangttr vsfpvqwgpy rvevedpqtg mvsslrfwag
      721 yrwqdntegg avrpdqvkla ldkpaynegd varisvtppa agsgyllves adgplwwqsi
      781 dvpaegrtfe vpvgrewarh dlyvsalvvr pgerkervtp kravgllhlp leraprklal
      841 tlraaekmrp nqplavhvqa knadgtparq ahvlvaavda gilsitdyat pdpfaalfgr
      901 kaygadqldv ygqlieagqg rlaslafggd aglaaggkrp pskvrlvalq svpvtldeqg
      961 egdvsldipd fngelrlmaq vwtderygma egktvvaapl vaelaaprfl aggdetsval
     1021 dltnlsgqpq aldvkleadg llrlaeapag qttplqladg qrttlrvpvr alsgfgqgsi
     1081 rvtvnglalp gealapltrd wtlgirpawp aqtrsfravl kgdswslpag tlaafetigr
     1141 earlsvsarp plniaehira lraypygcae qttsglyasl yldaatrqrl gledepdeqr
     1201 rkaiaigigr llgmqrfngs fglwsnesde epwltayvtd flqrareqgf dvpaaalaka
     1261 nerllrylqd rnqidvnytd nsdysrfavq ayagyvlart qqaplgalrs lferraesrs
     1321 glalvqlava lkamgdqpra dqaleaglaa qavrgdgwya dygstlrdea lilalleesg
     1381 lapdqvdarl fplsdrlagr dwlstqerna lflagrhlig kpepdwqasl diagqartld
     1441 rdhanlrfde qalaepltlt srspaplyqr ltlsgyptea pkaggenlsi qrdylgldgt
     1501 pvdirdlrsg qlvlvhlsvq arertpdalv vdllpaglep enqnlahsaa slqdasqevr
     1561 glqesmqgaa ikhqefrddr yvaavdvsgy dtthllylar avtpgtyrvp ppqvesmyrp
     1621 qwqalgdape vmvihdr
//
LOCUS       WP_284547904             276 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Metapseudomonas otitidis].
ACCESSION   WP_284547904
VERSION     WP_284547904.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469162
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..276
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=31381
     Region          <156..257
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          227..253
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkriikriit ltiiihtkts lahtsinfye snqgiislsk tentytllai aggrpaggat
       61 agnciimakl kdtekvikgk lypfkssyfs ydeassntpp itlekrskst ifievdtfgi
      121 cglgvtftdi yslqeahtrs ykenfletlk itheiaqnly qkgdkqgait imkpyaenmp
      181 mhwiensasg neicdfieky asflqlsgqp etainflrki leerpertaa wlnladtyws
      241 akkfkeares yrkyrilmst ekrektipqr vyersp
//
LOCUS       WP_284547939             360 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Metapseudomonas otitidis].
ACCESSION   WP_284547939
VERSION     WP_284547939.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..360
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38972
     Region          13..357
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mhigivgggv igllsayfla kegvkvsife kgnigqessw agggivsplf pwrypdavtn
       61 lsnwskefyn slsthlrdtt aidpevyqcg iywldlddiq paihwaetqs lkaslikkge
      121 lrarlpalsy nysnalfspl ianvrnpkls qslkaylsrk gvslfessai kniatkgehw
      181 vlrtdassvq ldkilitaga wsgellatlg lslpvepvkg qmilykcepg flpsmvlakg
      241 ryaiprrdgh ilvgstlehe gfdktptdva reslqasaee lipalarqpi vghwaglrpg
      301 spdgipfigp vpgfeglwln cghyrnglvl apascrllad lmlghepivd ptpyapsarl
//
LOCUS       WP_284547969             753 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Metapseudomonas otitidis].
ACCESSION   WP_284547969
VERSION     WP_284547969.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 753)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..753
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=82680
     Region          63..753
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mkrlalrpqp gprtllavgi glaagplvaa epprssasle letlhveerr sdgyrtersa
       61 saknavplld tpqtitvvpa evmrdqqals lrevlsnvsg itfnageggg gsgdnlnirg
      121 fsastnlqid glrdsaqnnr tdtfnieqve vikgpnsvfg gagttggsvn qiskqpgfea
      181 fsrlglglgs dhyrrltldt nqplqelgsg safrlnlmah ddeipgrkrl ererwgiaps
      241 lllglgedts ltlsyfhqrd dndpdygvpa fdgkrvagvk rnayfgwrnl dreridsdaf
      301 tvrlehrfnd qlslqnltry severdtvis aahinldrrr gggapgpvla pgqylpagpq
      361 aygrdvtsrm winqtnltae fdtlgightl vtgaefsret yhrttydygl kfpdegypla
      421 dppgywsgpa qrsnsgylat rlydralyaf dtlalspqwd lnlglrydwl dgdarnnslt
      481 kgtwvatdnr ssdehlsgra glvykpveng rfylaygtsf npsaeniats gaglsaatek
      541 ldpeknrtwe lgtkweller rlqldaalfr veklnartql tdgttilagn qrvqglelgl
      601 tgelnerwkv fstftfmdse tlkavnervg vsakgqalan tppqsfnlws tydfdggwrv
      661 gygaryvsqr nltasddgvk laaywvhsam lgyrvsdsfd lqlnldnlfd rqyvervrtq
      721 lgtqqgtgsq garssaieyg daraatlnat lsf
//
LOCUS       WP_284548096             261 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfite exporter TauE/SafE family protein [Aestuariimicrobium sp.
            T2.26MG-19.2B].
ACCESSION   WP_284548096
VERSION     WP_284548096.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..261
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27054
     Region          19..256
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 melalhvvll lvlaafvagw vdavvggggl iqlpslligl padtsvaais gtnkvssaag
       61 tlvatttylr kvrvdwwiav plmvfaylgs tsgarlvnfl pkqwftpivl valvgvglyt
      121 vrrptlglhh evrrhgwaaa ataagigavv glydgflgpg tgsffvialv gllgygflqa
      181 svlaklanlt tnvaaisvfs iqgviiwkla lamaaanlsg gfigaqmavr hgsafvrrvf
      241 lvvvgililk lgwdslrifi g
//
LOCUS       WP_284548117             344 aa            linear   BCT 25-DEC-2024
DEFINITION  lactonase family protein [Aestuariimicrobium sp. T2.26MG-19.2B].
ACCESSION   WP_284548117
VERSION     WP_284548117.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..344
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=36142
     Region          3..324
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 mstllvgcft desgvgglql fgvdghqltp iaqaavpspt wlveagdhvv aashtqgspl
       61 vrldvnadgi tvgsrrdtsg ldgchaslsp dgsavaiahy ssgslavvpl veggwgdatv
      121 vrfggqsgvv pdrqeaphah qavwldeehl lvcdlgadai rvvswldghl rqvgkitttp
      181 gfgprhlvvr rvngphgaqt qvavggeldg nvasyrhhdg tggspdwttg wervsqvqgt
      241 lvgeaqpsal rlldeqtlvv anrrintlgv lewhesgqlv ladefdcggd hprdvvvheg
      301 diwvanqgtg dvccftrrgl dsetcswrla srtsveapga llfr
//
LOCUS       WP_284548147             569 aa            linear   BCT 25-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Aestuariimicrobium sp.
            T2.26MG-19.2B].
ACCESSION   WP_284548147
VERSION     WP_284548147.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Pereira,J. and Lupas,A.N.
  TITLE     The VCBS superfamily forms a third supercluster of beta-propellers
            that includes tachylectin and integrins
  JOURNAL   Bioinformatics 36 (24), 5618-5622 (2021)
   PUBMED   33416871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..569
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=59032
     Region          475..534
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 msirlraltv avasslvvvt lagtapsara eptsqsrpri lsagsstvsp qssgsqglap
       61 qtvttqaavd palsslnelr srvgssslav tsatqsavsa havylelnkd danlnpndeq
      121 lgkpgysaeg daiapftvtv aeanthaial dvamtdpwar stlllnprat saafahtatf
      181 tviglpvats avstswpkvf pakashrgla wtssgasyyt sqcsqnpvqw gypisvqldd
      241 trihqvlgaq atltedgqpv etcvvsdagf tgvdglvlvv ptrplvpgai ysgrvrgtav
      301 tdqgasqnld aaisfttaat argngdqtgd gvadllavdt agtlqmikgq agagfgarwp
      361 igrgwgttiw vghvpdldgn rtdellavrs dgsmwlylgs gmggyasgrq vgrgwntvrn
      421 itvigdmthd stpevvaiss sgdlvrytlt rsgftstnki grnwqaisft vglgdfnrdg
      481 wndlvavsrq gdliayyvrn giivqaakvg rgwsgwtavf tpgdlsgdgv pdlvgrnssg
      541 tlyayqtgwv sfsparlvgt gfggyrlfa
//
LOCUS       WP_284548224             349 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Aestuariimicrobium sp.
            T2.26MG-19.2B].
ACCESSION   WP_284548224
VERSION     WP_284548224.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..349
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35971
     Region          3..348
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mtaidlrsdt vtrptaqmrr vmldapvgdd vygedpsiae fearvadlcg kpaalfcatg
       61 slsnllgvqt lvapgtevlc easahiarae mgahgalhgv tmrtwvagrg egrtaglatt
      121 vqieellspd agpylvstaa velenthnfg ggtiqpiehl revsamcraa gvglhldgar
      181 lwnahvetgv piadysalfd tvslcfskgl gapvgsvlvg sdeaiaqarv qrkrlgagwr
      241 qagmlaaaaq faldhhvdrl vddhaaaraf aervalaapg avdpervptn ivvvktgsrp
      301 aqdvaaaaaa qgvrvsvvga rlvravthld vdaadcraag dvvgrllap
//
LOCUS       WP_284548380              86 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Aestuariimicrobium sp.
            T2.26MG-19.2B].
ACCESSION   WP_284548380
VERSION     WP_284548380.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 86)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..86
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9457
     Region          <20..62
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(20,31,34,38..39)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mpwvttfgrq paadrifkkq qvaaqvgipy rrlsniltgs swgspgdlqr iadwigapve
       61 klfteelrna prptkgqrpn deavak
//
LOCUS       WP_284548418             105 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Metapseudomonas otitidis].
ACCESSION   WP_284548418
VERSION     WP_284548418.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..105
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=10630
     Region          2..101
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mawtyllvaa vfevlfamgm kyaegftrpl psasvivaav agiyfltlsm rvlpvsvayp
       61 vwtaigslgt vilgvvllge sftpvkglsv vlivagvagl kggag
//
LOCUS       WP_284548530             235 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Aestuariimicrobium sp.
            T2.26MG-19.2B].
ACCESSION   WP_284548530
VERSION     WP_284548530.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..235
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25339
     Region          73..187
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 maaeqnpptq ptstqptsiq pterrpsqaq pepgspepsq wvritsadpd hshryiqrfk
       61 tmasngadlh getrmidamv qrnahildag cgpgrvggel qrrghrvvgv dvdpvlidea
      121 rrvnpeatwv vsdlalldlp avginegfda ivcagnvmtf laastrvgvl rafarhlapg
      181 gravigfgqg rgyefadfir daheaglrlq lglstwdlkp feeestflva vfgrg
//
LOCUS       WP_284548755             451 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Metapseudomonas otitidis].
ACCESSION   WP_284548755
VERSION     WP_284548755.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 451)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..451
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=48063
     Region          5..448
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mdterqlled adrralayld gipgrrvfpt pdaiaalagf eeplpqqgrs pegvlrqlde
       61 lgspattasn ggryfgfvig atlpaaaaae rlvlawdqca stfdnspaad riekaaarwv
      121 leslglpaes avgfgtsata ctlaclsaar rallarkgwd ydgdglmgap evrvvasasv
      181 hitvkkalri lgfginrllv apvdelgrid paqlpplddm tvlclqagev ntgefdpfaa
      241 lipraraaga wvhvdgafgl warassaaal aegveqadsw ttdghkwlnt pydgamaicr
      301 daealatamn sdaayasasc daqknlnlef srrargvpiw aalaslgrdg lralidrhlr
      361 qathlaerlr dagyqvlnrv vlnqvlvrad sdeqtlairl aaqatgevwf gptlwqgrpa
      421 frlsvsswrt tdadierlad llitlkaqhp g
//
LOCUS       WP_284548861             618 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Aestuariimicrobium
            sp. T2.26MG-19.2B].
ACCESSION   WP_284548861
VERSION     WP_284548861.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 618)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..618
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65618
     Region          45..591
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mnptlkrrql lagavvggag lfagplspea qarptdptag aaagknvrlt vlgttdlhgn
       61 vhnwnyfsna aysdgkgnqi gvakcatlir hlraergadt citldagdti qgtplayyya
      121 kidpitqgsk hpmalamnai gydaaamgnh efnygldtla afadqldhpl lcgnalqvvd
      181 gqntdrpayp thtlktiklk gqqpitvglv glvtpgvsiw dknnvegklw fngiveqakv
      241 lipqvkraga dvvivschsg attssswgda lpwpenastl laeqvpgida ilvghahlev
      301 pqrfvtnqtt grqvllsepl ywgmrvsvmd lnltmvkgkw qvtsssatll nantvdedpe
      361 vaaviepahr tvlayvnsvi grsladmtga tacwedsaav dfinyvqaqa vkaglvgtad
      421 ettpvlsiaa pfsrtavipa gdvtvrdvag lyiydntlfg iamtgaqvka yleksasyfk
      481 qvssagplpa aqvtnavtss apngtpdyny dvmggldaal tydidlsvpa gdrirnlayd
      541 gtpvadekrf viainnyrqs gggnfpgvtt aevvynrqne irqliidwvt ahqvidpaqf
      601 hrvdwklvwg ttpitvta
//
LOCUS       WP_284548816             278 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Aestuariimicrobium sp. T2.26MG-19.2B].
ACCESSION   WP_284548816
VERSION     WP_284548816.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 278)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..278
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28961
     Region          21..278
                     /region_name="COG4587"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443644"
ORIGIN      
        1 mtagartsva rgvhdtvgra wamvrlgaan alvfranvvv smlsvalqtv llvtvwravy
       61 sgrhsvagvt geravsyavl glvlghlalp wrlsslperv regtvatdii rpvgvvgqsl
      121 lqsigaavga lpgvatalll gallggltmp atvsaafgfm ltaalgwlia tllnlvvsmv
      181 afwttdtrgp fyvyravasf asgalvplwf mpdwlrptle alpfalqvfa plqlwfseqp
      241 lggvggvvla qvgwlvvaal ltalvswral rtvvingg
//
LOCUS       WP_284548916             612 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Aestuariimicrobium sp.
            T2.26MG-19.2B].
ACCESSION   WP_284548916
VERSION     WP_284548916.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..612
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66794
     Region          1..601
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mtsaldlitt dhlwqlfdta adqhadrlat rvkrggvwdd ltygqlrdla rsvaralvrq
       61 gigvgdrval fapnlpewta idlavnlaga vlvplyatst peqishivgd sgarlmvigg
      121 ekeagrvlas rdqinaewpv isidgqvrdg iiglrgwlda etpdertegd aeldrrvaea
      181 raddltaivy tsgttgdpkg vmlthggmva qcravgdlfe fspedhslsf lplshalera
      241 wqfiviaygc rntycpnpre vagmltevrp tllvsvpkly etvyrvahek advspvkqtv
      301 fswavrvggq mqhsyrkgrr psivwraqlg ladklvlkni rdamggtktv lacggaplrr
      361 eveeffsaag mpiftgyglt easplvsfns psafkvssag rvmgggelri gaesevlyrg
      421 pnlmagywnq peasaqvide agwlhtgdag yvdgdgflfi tdrikdiivt lggknvapqp
      481 ieglvladpl fehavligeg rptltmlvrp slphleelae klqlpkgspa dlvnhpavve
      541 efkarvaalt aklpsheqir dlrasieeft mdnglltptl kvrrrevekk fsnlidemya
      601 riaefrkhrs de
//
LOCUS       WP_284548940             363 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Aestuariimicrobium
            sp. T2.26MG-19.2B].
ACCESSION   WP_284548940
VERSION     WP_284548940.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..363
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38839
     Region          5..356
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mtaefippak pligdeeraa vdrvlrsgmi aqgpevaafe aefsehfklg racvavnsgt
       61 sglhlgllsc gigagdeviv psftfaatan svaltgatpv fadiergsfc ldpasveasi
      121 tertkaimpv hlyghpanmv alreiadkhg lklfedaaqa hgaslngipv gafgefgmfs
      181 lyptknmtsg eggmvtaand tiernlrlyr nqgmlqqyhn evvglnnrmt dihaaigrvq
      241 ltkvdawtkt rqqnadylss hlegvtappv aegavhvyhq ytirvaddrd glakalkdey
      301 nvgsgmfypv pnhrlkpfqs pvelpetera aleclslpvh psvtqehler ivtavntlak
      361 aga
//
LOCUS       WP_284549046             519 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Metapseudomonas otitidis].
ACCESSION   WP_284549046
VERSION     WP_284549046.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..519
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58201
     Region          8..451
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mnapvtptpp arhckiaiig sgfsglgmai rlkqtgendf lmfekeagvg gtwrvnnypg
       61 cgcdvqshly sfsfepnpew trmfakqgei kaylercwek yrlqdktlle teikrlawsd
      121 eqeiwqieda agnhytaqfv vsgmgalstp siphlpgmen ftgksfhsqq wdhdydltgk
      181 rvavigtgas aiqfvpqiqk qvahldlyqr tapwvmpkpd raiserernr frsfplaqkl
      241 wrgliytvle srvvgfaltp kvmklaelya khyikrkind palrakvtpd ytmgckrvli
      301 sndyypalnq pnvdvitdgi qeiransivt rdgqeravda iiygtgftps dplprgvvfg
      361 rggvdlldtw pqgpeaykgt ltagfpnlff lmgpntglgh nsmvymiesq ihyvlgaldl
      421 letrhlqsle vkrdvqdrfn gklqgslgnt vwnaggcmsw yihpvsgrnc tvwpgftwrf
      481 rlltrnfdpa ayhfsrqqpv hagqgplafq naapqevta
//
LOCUS       WP_284549177             251 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein
            [Aestuariimicrobium sp. T2.26MG-19.2B].
ACCESSION   WP_284549177
VERSION     WP_284549177.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..251
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27868
     Region          4..250
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 msnlslqlyt ireelerdae haldvvagtg itevepfgit qfrewlpaal akrglkvttt
       61 htdllgdfdn svaalkevgg ttlvqpffdp qkwttkegiq elatqlneaa rkaapeglkv
      121 gyhnhhfeff tdfdgvnsyd yfvslldpev vleidtywvs vagldpvelv qrlgdrvthl
      181 hikdgpapvt refsrekhde qpanvvlgqg smdldtllga tenktwvvef dktdgdilde
      241 vvasiaylqn r
//
LOCUS       WP_284549195             310 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein
            [Aestuariimicrobium sp. T2.26MG-19.2B].
ACCESSION   WP_284549195
VERSION     WP_284549195.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..310
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33314
     Region          1..307
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mrvgfssysf hqylgtgrms lpevfdwake agaahieiaa gfasdnpmsd lsdlpnnrpl
       61 vdaikaaqdk tglpiaqial patfwtkpet adgqapgagg qsssargiea eldrvrahid
      121 lcaelgvgll rhdvshgnhs gddlplfeqa lpvivehskt iaqyaatkgv rtsienhgff
      181 vqgservrrv ihavdepnfg ttldignflc ldenpvvatk nniayanivh fkdfyirqtn
      241 pglgffgtrg gqflrgaivg qgdidipava kvvkesgydd fitiefegie dalpackaal
      301 entrrildea
//
LOCUS       WP_284549257             216 aa            linear   BCT 25-DEC-2024
DEFINITION  peroxiredoxin family protein [Aestuariimicrobium sp.
            T2.26MG-19.2B].
ACCESSION   WP_284549257
VERSION     WP_284549257.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Schroder,E. and Ponting,C.P.
  TITLE     Evidence that peroxiredoxins are novel members of the thioredoxin
            fold superfamily
  JOURNAL   Protein Sci 7 (11), 2465-2468 (1998)
   PUBMED   9828014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003123
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..216
                     /product="peroxiredoxin family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23268
     Region          75..199
                     /region_name="Bcp"
                     /note="Peroxiredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG1225"
                     /db_xref="CDD:440838"
ORIGIN      
        1 mttssrrtrr anresaalta retlrnqram edahrarwrl vsrvatvvvl vviaglvtvg
       61 llnsratdss vsrqapafsl rttagttvsl sdyrgkpvll yfnegagcgs ctqqmaeiek
      121 dpgfakagit vlpivmntke qiqpdldqfg vrstylldeg gsvskaygtl gtgmheglpg
      181 hgfvlidasg vqrwqgdyps mwiapaqllk eaksrl
//
LOCUS       WP_284549260             740 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Aestuariimicrobium sp.
            T2.26MG-19.2B].
ACCESSION   WP_284549260
VERSION     WP_284549260.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 740)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..740
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77201
     Region          11..739
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mttdtvrdtr qsieldidgm tcascaarie kklgkvegvd asvnyatdka lvlaptglta
       61 adlikvveea gygahlpepd stppdragay rrrlivaavf avpvillamv pslqfpfwqw
      121 vslvltlpvv twaawpfhks awvnarhaat tmdtlismgt saatlwslya lvftsaghpa
      181 yrhdfgftld rhhagtatyf eaavgiitfl llgrwiears rrdagaalra lltmgakeas
      241 ivrdgvetrl pidqlvvgdh fvvrpgekva tdgevvegns avdaslitge svpvevgpgs
      301 lvvgatints grllvrasav gsdtqlshia rlveqaqtgk aavqrladri sgifvpivig
      361 lalvtligwl vagaevgfaf taavavliia cpcalglatp tallagtgrg selgivirgp
      421 evleqarsid tvvldktgtl tegqmsvast hpaagttesq ltlvaaalen hsehpiarav
      481 vaaagtrglp evsnfsnhpg rgvvatidgv vhlvgnqrll ednglalgae vedaaqaasg
      541 rgetlvfvat ehevlgvigv adtikttsae girqlkalgl tpvmvtgdhe aaarvvadsl
      601 gidevrasvl pankvdivre fqaqgrrvam vgdgvndaaa ltqadlgmam gsgtdaaiaa
      661 sditlmrpdm vlaadavrls ratlrtikin lfwaffynvv alpvaalgfl npmiasaama
      721 fssvfvvlns lllrrftpra
//
LOCUS       WP_284549386             448 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Aestuariimicrobium sp.
            T2.26MG-19.2B].
ACCESSION   WP_284549386
VERSION     WP_284549386.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..448
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47536
     Region          3..448
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mldcivlgag laglsaatel vakgrsvvvv eardriggrv eagvlgdgqv vdfggqwiad
       61 ghtrmhelva rlhlelvaps agdvavrmgg nvsklptrde laaslnpfel adlgeglarf
      121 rhlaeriadd pawaegnvkw lsralvrwvn snlrtpaaqq wflrvfrasf rvepdqislt
      181 ealhransgt dmetmiavng gvrqrrvagg aaaicerlaa dlgdairlgc vvtgvaqsde
      241 wvtvtlasge qlqarsvvnc lppklavglv hepalpewrl dlaakvpagn vikaflvypt
      301 pwwrerghsg qmgsdagpvr vsfdssqegg rgvllgffsg pdadgwgtks vylrqraftd
      361 avtaafgpap depleyvdrd wsseeftrgc hgahfapgvw tasgpalaep ngreffagae
      421 fattfngyme gavrsglaga aqvlqala
//
LOCUS       WP_284549391             160 aa            linear   BCT 25-DEC-2024
DEFINITION  SixA phosphatase family protein [Aestuariimicrobium sp.
            T2.26MG-19.2B].
ACCESSION   WP_284549391
VERSION     WP_284549391.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..160
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=17371
     Region          4..157
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mptlfllrha kteavhsggd kareltdrgr adaravgaql rqrgidlvlc ssavrtrqtv
       61 eelgldarve smdalyncdv etmlqriget ddsvshllvv ghsptipaaa aelvwasqpr
      121 eadqlacsfp taawaeitfe gtwadlerar laavhrprdv
//
LOCUS       WP_284549531             999 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-mannosidase [Aestuariimicrobium sp. T2.26MG-19.2B].
ACCESSION   WP_284549531
VERSION     WP_284549531.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..999
                     /product="alpha-mannosidase"
                     /calculated_mol_wt=110099
     Region          249..996
                     /region_name="MngB"
                     /note="Alpha-mannosidase [Carbohydrate transport and
                     metabolism]; COG0383"
                     /db_xref="CDD:440152"
ORIGIN      
        1 mhdfvarteh rltrfinerl rqqlyrdrar vevthweapd epvsfaeata qtfapfevgt
       61 pwgppwgtvw fhvtgtvpvg wgkeadtrpe lhvdlgfagg gtgftceana wsaqgtlika
      121 lepmnryvtl dagpgesfel fieaaanpvv psfnwyqptp vgdkatagtd piyvvntlev
      181 alldtgvwel sqdvdalrgl mlvlpaestr rhqilsaled mmdavdphdl agtaargrev
      241 lrpalespag rsshvvhatg hahidsawlw pvretirkcs rtfsnvialm dedpdltfac
      301 ssaqqyewvr dhypelferi rekvaegrfv pvggmwvesd tnmpgseamv rqfvlgtrff
      361 idefgfepkd vwlpdsfgys gampqiaraa gkdsfltqki swndtntfph htfwwegidg
      421 srifthfpps dtynshlsae elarserqfr ekgrathalv pfgwgdgggg ptremmaaar
      481 rkadlegspk vvvdtpaeff aaakaehghl dtwtgemyle yhrgtytsqh rtkagnrrse
      541 hllreaelww ttavvregat wpkeqfdrlw kqvllqqfhd ilpgssiawv hheaeqhyga
      601 iaaeleelia eagrillgag etpfvlnarp fadhgvpalg vaaatepria evassgdgft
      661 lsneallvel danglvtrlf drragrdllp pgqvsnllql hrdipnewda wdinshykqv
      721 trdltevvsi atvpggvvie rstgassite tvtldeaglh ldfdidwhdr qkllkltlpf
      781 alhareatse iqfghlarpt svntswdaar fetvahrwlh vsepgygval ansctygydt
      841 lrttdgdgns vttvrpsllr apmfpdpdad qghhqlsfll vpgaevgdav eagyaenlpt
      901 rvlagahgvd plvtidnpav vveavklaed gsgdvvvrly esrggraaav lgvgfehgpv
      961 vatdllerpl atgtrsplvg qdrlelrpfe ivtlrigra
//
LOCUS       WP_284549596             527 aa            linear   BCT 25-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Aestuariimicrobium
            sp. T2.26MG-19.2B].
ACCESSION   WP_284549596
VERSION     WP_284549596.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..527
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=55942
     Region          2..523
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mltgasvadg lgnpleirdv avadglvvpl eqaddtwprv dlsglvlapg fvdihthsdl
       61 tllssplahs avrqgvttqv vgncglgmsp qtevtshddl rgvnsyldhd ptvdthwqrl
      121 adelrawrea rpsinvatla ahiplhaata gladqpadag qveamvglah qaiddgavgl
      181 stglvysplc faledellal grvaadrgvv fawhirdyid dllpsleqal rvarltgcrl
      241 qishlqvvgr rnwssfdaai amidearaag ldvafdmypy lagnsmltqv lpswvqsggd
      301 vgvrralvra dsrarvrael lsepgmafgw devliasapd psvvgrtvdw iatdrgrepv
      361 daaldliaeh gtevlmtafg rsaevlrgtl ahpacivasd gqaidpdgpt ghqqphprsy
      421 gcfphflaas flddlglslp eairrctsap sdrvglvdrg riaagfpadl vafdplliad
      481 rasytdpqvf pagiervwvs gqetvrggeh lgtragavlt rpatdrp
//
LOCUS       WP_284549879             215 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Aestuariimicrobium sp. T2.26MG-19.2B].
ACCESSION   WP_284549879
VERSION     WP_284549879.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..215
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22483
     Region          1..206
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(24..25,27..28,31..32,69,73..74,77..78,91,95,102,
                     105..106,111,134,138..139,141..143,145..146,149..150,
                     153..154,174,176..178,180..182,184..185,187..188,192,
                     195..196,202,204)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(137,141,144..145,147..148,187,190..191,193..198,
                     201..203)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(158..165,175,178..179,182)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mlslhvpghs lvhrlpagak lltilvfgtf affvdslvvl gscvgvvaaa ylvarvppar
       61 awqllrgvla mvalivlaqg flgdwttaaq vglrvlavvl lanlvtlsta qtalvdavvw
      121 aagplrrvgv dpdriglmia lvfrfipvia eeaskvreah aargvrpglf glgvsylapl
      181 virtlrmadg lgealevrgv gtrpappdrp akvpf
//
LOCUS       WP_284549950             206 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Aestuariimicrobium sp. T2.26MG-19.2B].
ACCESSION   WP_284549950
VERSION     WP_284549950.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..206
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=21878
     Region          1..199
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mrvilasksp arlaalrsag ldpevwvsha dedslqrstt qaltialael kgsvvaaelp
       61 ddedwaliac dsllelggqr hgkpgneaea iarwytmrgt tgvlwtghhv ivhragpdgg
      121 vslrasrggq srvtfadlsd aeiaayaatg epervaggft idglgaafvt riegdphnvv
      181 gislslvrqm lldlgvewht lwrldr
//
LOCUS       WP_284549999             201 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein
            [Aestuariimicrobium sp. T2.26MG-19.2B].
ACCESSION   WP_284549999
VERSION     WP_284549999.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..201
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=21535
     Region          7..>125
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mdtplpptsp prdttthvww tpltlasieq ldvldepera rleriappad rarvmlgaal
       61 lrhaiaglsg lapdlvevdr tceecgrqhg rpvlvgqpwq asvshsgllt vvalclepig
      121 idvqrrtggq rgaggdgrvd vdgevdvedw vrrearfksg lvapsfvdlh ppapghvail
      181 arsgngpvve hdgaellrrr p
//
LOCUS       WP_284550033             639 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Aestuariimicrobium sp.
            T2.26MG-19.2B].
ACCESSION   WP_284550033
VERSION     WP_284550033.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..639
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69319
     Region          34..635
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mtpepaeptp ssaransafg dlaerdrlla acsqnlgtml adrtratphk vaflvpdrap
       61 vganqwhelt wtqtqqrahv iaagliglgl qpedrvaiam ttriewvltd lgiacaggat
      121 ttiypntnvd dvthivadsd shivvvensa qldklrkate ldhvvrhivi ldddrsleds
      181 dervitfadl eeagrralhg dhdlvtrtva aiapdqlstl iytsgttgrp kgvelthrsw
      241 tyegvamqat givreddlqy lwlplshvfg kcllavqlts gfasavdgrl drivtglgev
      301 rptfmcgapr ifekvrsavm tkaapgstvd kisrwafavg rdsrqyrlag rrlpvglklk
      361 yaladrlvfs klkktmggri rffmsgsakl sekvqawfys agitvvegyg atetsaiafv
      421 ndpatphfgt vgkvtpgmev qiaddgelll rgpviargyh grsdataasf ddegwyhtgd
      481 mgvldddgyl sitdrkkdli ktsggkyvap qkvegavtaa splvsqvval genrkyvval
      541 ltldeaavkt waerhghags thadllaspd lratlddqia hanstlerwe tvkrfevlqr
      601 efsvddggvt pnmkvrrnvv esqyadviag lydedpadl
//
LOCUS       WP_284550034             294 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Aestuariimicrobium sp. T2.26MG-19.2B].
ACCESSION   WP_284550034
VERSION     WP_284550034.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..294
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32817
     Region          1..131
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
     Region          152..289
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mtttmrvevp lrwgdmdaqa hvnngmvaey lqearvdflh aagvtemlet gvvvishqie
       61 ylapityspr pvvvdlgith iggarfevay llshdgveca rarsvlcpfd lasqqvrrls
      121 agergwferh rievepfrdl qapallgrgv phplrprwsd vdrfghvnnv rlfdyvqear
      181 iaasswvdas mlrhgssldp ahaaeehslw lvarqdveyl aqipyrvepy rvdtgvarlg
      241 nssvtfaaev vdplaedqvl vrartvlvca ddegrpkqlp tttrsrlgre lvrd
//
LOCUS       WP_284550054             241 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Metapseudomonas
            otitidis].
ACCESSION   WP_284550054
VERSION     WP_284550054.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas otitidis
  ORGANISM  Metapseudomonas otitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 241)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Metapseudomonas otitidis"
                     /db_xref="taxon:319939"
     Protein         1..241
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=26201
     Region          7..240
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mmpgaawtsa arthpgkvra rnedafldsp gqglwvvadg mgghhagdra srlvveslae
       61 lpatgdfanr lqhlrrhlhr lnrrladelt vtdgqrrimg stvaallveg sraacvwagd
      121 srcylwrwgc lyqltrdhsl lrelieergm speqasrhps ahaltralgg dgdfaldvle
      181 lelhpgdtfl lcsdglyrel devalsqals laspvatleq lfeqalqgaa pdnltavvar
      241 r
//
LOCUS       WP_284550093             276 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Aestuariimicrobium sp. T2.26MG-19.2B].
ACCESSION   WP_284550093
VERSION     WP_284550093.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..276
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=29879
     Region          97..244
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 msgrkvspps qptrreqlra ereaqlrrsd rrmriiwlva avvvvaiiat vatvvvrnrs
       61 aghrltdqql aaqvsppnln aagsaivenp rttadvptit vyldfqcpac ksfnetygpv
      121 lnqlagasei klefsiltvi gkrlgnedas eragraamca dvvgvyptyh dalfagqpeq
      181 egagftdeql rvtfanqagl qnpelakfqq cydqratana lasqqekalp sfdgstpqvs
      241 ingknpmvna dgkqvawwqv ldpssaaweq aiaqyk
//
LOCUS       WP_284550119             595 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Aestuariimicrobium sp. T2.26MG-19.2B].
ACCESSION   WP_284550119
VERSION     WP_284550119.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 595)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 595)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 595)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..595
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=62278
     Region          23..578
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mansttrlna lllvmlltla awagrafylq aydaqanaam aanrmtytkt lvaqrgtisd
       61 rngvvmasse qavkivadpi misrngidtr vemtpgqkkr aataardisv vlakylggse
      121 adylpvlsdl grkhyvvvks qvpawtyeqi rrdlaaandg iglhglaked dpirtypagd
      181 vaanvigfmn sagegaggle ysleaslagt dgkesyatsa ngriplantt lvpavdgtsy
      241 tltldtemql manqalaagv tragakngta ivmnvktgel lalsttpgfd sndpagadpa
      301 nlgnravsap yepgsvekvl tmaaladqgl vtadtrvevp srvvsgdgki kdafehgtlh
      361 ltargvians snigtvlltr qmnkqklrqy lldfglgkkt glglpgesag wlppaslady
      421 srdqisfgqg lsvtavqeas aiaavanggl ynaptlvkat vdgdgkavpv ekaeprrvis
      481 aaasaqvldm mesvvmlkks rsipnyrmag ktgtaqrvdp qcscyrgyta sfvgvapved
      541 pqllvyvvvd qptrgtdgst lalpvaqqim slalprygvl psttkpterp ltyvp
//
LOCUS       WP_284550165             934 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Aestuariimicrobium sp.
            T2.26MG-19.2B].
ACCESSION   WP_284550165
VERSION     WP_284550165.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 934)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 934)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 934)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 934)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11970876
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..934
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..934
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=98040
     Region          <1..897
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          872..927
                     /region_name="LuxR_C_like"
                     /note="C-terminal DNA-binding domain of LuxR-like
                     proteins. This domain contains a helix-turn-helix motif
                     and binds DNA. Proteins belonging to this group are
                     response regulators; some act as transcriptional
                     activators, others as transcriptional repressors. Many...;
                     cd06170"
                     /db_xref="CDD:99777"
     Site            order(873..875,888..890,898..899,901..902,904..908,919)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:99777"
     Site            order(884,886,888,919..921,924,927)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:99777"
ORIGIN      
        1 mvgrsaqlav iddavaaasa grgglvlvtg eagigktmlg lagieraaav glrtahgfav
       61 ddtgapalwp wsrlarqlpe ldtvvvavkq adldndagrf gvaeavvdal tqaaepsgll
      121 vlledlhwad slsvavlrhv afdlphsrvv vlatarddaa tafgralpdl lrgggsvlvr
      181 ltgldagava qwlssdpslt gwgalvhelv crtdgnpffi havtsqappa sgdlddvlae
      241 rqdirgllaa pllqltdear dtlitaalms erlsptllaa acgrtvaqvt dhiaqgcrag
      301 llqhratgls fthalvrdav iadteahhrs areasiaaam qssgdellvg psavhwdrae
      361 ghaasvncrd aaraaaaraa avhaheeava farmcvrhtr rldhddaela eclvelagye
      421 wlanqvpaav dscveavdva eaadrpdrma raalvpqgig srevarvvag lcrralsrvp
      481 pedlttrarl tsqmavaaae davdgsadal svaaltlarr shsptaelda iaarhlvlsy
      541 pqtidervpl aeravelgrs sttamgtlwg hlwqadialq rgdlvaldda ivqiarvagr
      601 rsspvarwhe hrlrglvaav lgdfdgartq aeaglriadr tgdrsligmy hivcvqmall
      661 rgdpgeitep glrvleeatg iplvraslar alalagdrgr avallatlad lpervpvgpr
      721 wmgtlgqigl aaaalddpdl arrchallap tapwygadgg gtpfysgsne yplgviavaa
      781 gqrdvaadhf sraitenqri garpyvalar lglaeclehd papsaghrsg tptvrelaaa
      841 aaeefrlldm pgpllgaerl larpaptdap llttrelqva rlvgqahtnr qiadqlvvsv
      901 rtveshvrsa laklgfstrt elalwvrars dgrp
//
LOCUS       WP_284550234             281 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Aestuariimicrobium sp.
            T2.26MG-19.2B].
ACCESSION   WP_284550234
VERSION     WP_284550234.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..281
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=30825
     Region          19..260
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 mttaaatdet alpssegrpg ftlhldnfeg pfdlllhlis khkldvtevs lsrvtdefia
       61 fvkaggevwd ldqtssfllv aatlldlkaa rllpqgeved eddlallear dllfarllqy
      121 rafkivsall adrlgeqakr farpgglepr faalmpevnl pspealaqaa aralspqpaa
      181 lvglehlhqs tvsvqeqarl vvarlrakrv ltfrelvada drittvarfl sllelfreqv
      241 iafeqltalg eltirwtgde esdlqisdef dapppqpeet p
//
LOCUS       WP_284550320             290 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Aestuariimicrobium sp. T2.26MG-19.2B].
ACCESSION   WP_284550320
VERSION     WP_284550320.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..290
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32054
     Region          4..284
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mpattaelvd llsleeielg lyrgshprtt wqrtfggqvl aqalmaaygt mpaerichsl
       61 nayflrpgst dapiiydver trdghtfsar rvlarqrgtv iftlsasfhe leeglehsdp
      121 apvnvpapeq crrlsevmse rfgsesslfh ewdaldvrfa gdsgrsgeis psshrahmrv
      181 wvrtteglpd dhrlhqavta ylsdmtllgv stvphevafl saqlqaasid hamwfhrpir
      241 adqwilydqv spsasnalgf smgrllqdgl qvatcnqegl irvvpgtarh
//
LOCUS       WP_284550330             164 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-class carbonic anhydrase [Aestuariimicrobium sp.
            T2.26MG-19.2B].
ACCESSION   WP_284550330
VERSION     WP_284550330.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130171
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..164
                     /product="beta-class carbonic anhydrase"
                     /GO_function="GO:0004089 - carbonate dehydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17274
     Region          30..161
                     /region_name="beta_CA_cladeD"
                     /note="Carbonic anhydrases (CA) are zinc-containing
                     enzymes that catalyze the reversible hydration of carbon
                     dioxide in a two-step mechanism in which the nucleophilic
                     attack of a zinc-bound hydroxide ion on carbon dioxide is
                     followed by the regeneration of an...; cd03379"
                     /db_xref="CDD:239474"
     Site            order(36,38..40,52,55,74,79,89,92,153)
                     /site_type="active"
                     /note="active site clefts [active]"
                     /db_xref="CDD:239474"
     Site            order(36,38,89,92)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:239474"
     Site            order(37..40,46..47,52..54,56,58,69..70,73..74,153,
                     155..156,158,160)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239474"
ORIGIN      
        1 msdfddllaa nqsyaqgfsd ggfdgiarag vavvtcmdsr ieplamlglk lgdakilrtp
       61 ggritpdali gcilgvhvln vdrimvvpht rcamasgtda diaeriltqn gvdirgmtlg
      121 anpdqertld fdvrllashp lidgraqvgg flydvdsgll tqlh
//
LOCUS       WP_284550436             120 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Aestuariimicrobium sp.
            T2.26MG-19.2B].
ACCESSION   WP_284550436
VERSION     WP_284550436.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 120)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 120)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..120
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13429
     Region          6..97
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mpqswtarpl yevkaglfqg lthpyrilil elladgqeht vselglhtql eashlsqhla
       61 vlrknrlvvs errgshvfyr qfspavaell tvarrllkdl aadaslqwde vaslpeipsr
//
LOCUS       WP_284550628             436 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Aestuariimicrobium sp. T2.26MG-19.2B].
ACCESSION   WP_284550628
VERSION     WP_284550628.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..436
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47224
     Region          13..418
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 massglhydl idhtldnglr vvvnpdpssp gvavnlwyqv gsrdevaqrt gfahlfehlm
       61 fqgtwtgvgv gehlaaiqat ggganattsf drtnyfetvt pgaldlalwl eaqrmealkv
      121 dqtnldtqre vvkeekrqry dnqpygdtfe lltslafgad hpyghtpigs madldsadla
      181 dvqafydhwy cpsnavlvla gqitadealt raqhhfgaip arerptratv glpqvdlrga
      241 rhvvhrdvpr dtvhlvwpvp pqhsgddlal dvalgllsgg qsarlhqrlv relevaegvs
      301 astlglvagt nlalvsarvr pessaaqvrd lllaeivala tegptdeeld radaqterew
      361 leelatvear adeinqwtst tgdptainrh ladlsavnad dvsralgthl apedvftldy
      421 ltasnplpas ekearr
//
LOCUS       WP_284550698             323 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein
            [Aestuariimicrobium sp. T2.26MG-19.2B].
ACCESSION   WP_284550698
VERSION     WP_284550698.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..323
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=34822
     Region          2..309
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrivviggsg higsfliprl vrgghevvni srgtstpyvd ppewqlveqv vadrqredae
       61 gsfpdrvlgl ggevvidlvc ftlasagafv erlrgrtghy lfcgsiwsag asrvipmsee
      121 nttepfgeyg igkyeiarll rqetasgglv ttslhpghis gpgwapigpt gnldptvwtr
      181 lssgepvrip glgaetmahv haddvaqsfe cavehrdqas gqefyitaad alnvrgyatl
      241 aaswfgrppv lesvsweafr eglapehada swehlvrsqs ftmqkaqrll gyapkysage
      301 tvqeavrwlv dhgrievasp lvv
//
LOCUS       WP_284550797             210 aa            linear   BCT 25-DEC-2024
DEFINITION  peroxiredoxin family protein [Aestuariimicrobium sp.
            T2.26MG-19.2B].
ACCESSION   WP_284550797
VERSION     WP_284550797.1
KEYWORDS    RefSeq.
SOURCE      Aestuariimicrobium sp. T2.26MG-19.2B
  ORGANISM  Aestuariimicrobium sp. T2.26MG-19.2B
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Aestuariimicrobium.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Schroder,E. and Ponting,C.P.
  TITLE     Evidence that peroxiredoxins are novel members of the thioredoxin
            fold superfamily
  JOURNAL   Protein Sci 7 (11), 2465-2468 (1998)
   PUBMED   9828014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003123
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Aestuariimicrobium sp. T2.26MG-19.2B"
                     /db_xref="taxon:3040679"
     Protein         1..210
                     /product="peroxiredoxin family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22391
     Region          69..192
                     /region_name="Bcp"
                     /note="Peroxiredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG1225"
                     /db_xref="CDD:440838"
ORIGIN      
        1 matrhhptvt gatarqqlqq qlirekardv irrrvigflg galvvavaal vafglwsars
       61 tdsnvsrqap afsltttagt tvslsdyrgk pvilyfnega gcgsctqqma aiekdpgftr
      121 sgitvlpivm ntaeqiepdl atfgvktpyl lddgtvskay dtlgkgmheg lpghgfvlid
      181 adgnqrwqgd ypsmwiapgd llkevtgrls
//
LOCUS       WP_284550961             274 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Cutibacterium
            acnes].
ACCESSION   WP_284550961
VERSION     WP_284550961.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..274
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=30391
     Region          <94..201
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mtslvihaev tchllhelvy lligphkred qkliyisrvs ldkfpksalp qlmerasper
       61 rdrarryvri ddclrcliad elrayslkld ykvpvqsevs knafgkplla nrdgpkfnls
      121 hdgkwivcat sphpvgvdve avaepglavv sndfsveeve alrttatapl siaramiwtr
      181 keaylkylgl gltvqldsfs vidqtllspa egmtdgiqfy swcdadnshv isvcghgeev
      241 viscvsgqel ldglppshcs eepqeqlrwl pnls
//
LOCUS       WP_284550964            1697 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Proteus vulgaris].
ACCESSION   WP_284550964
VERSION     WP_284550964.1
KEYWORDS    RefSeq.
SOURCE      Proteus vulgaris
  ORGANISM  Proteus vulgaris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Proteus.
REFERENCE   1  (residues 1 to 1697)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1697)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1697)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1697)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1697
                     /organism="Proteus vulgaris"
                     /db_xref="taxon:585"
     Protein         1..1697
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=188789
     Region          122..1691
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mdmnqnqfrq ytekrgyrwc slavvlasal alsgcddkad esssstdkaq nvqtteqknt
       61 aqntpdtatq tsersavttk tnnetalksk evrdelamrf agkdvtvlda selqrdgast
      121 mvvtfsvpld pdqkfdnvih lvdtkkgkle gawelsdnlm elrfrhlpps telnltiddk
      181 ikginertlt tpfsqkltte eifpsvgfts kgsllpfdaa eglpiialnv dqvdvnffrv
      241 kdeqlaqflt qwesrsniny wesdeflsqa dlvytgrfel ntekntrenv llplksidal
      301 kkegayiavm qqagkysytv patvftfsdi glsmhsylds ldvftqslkn gsalneveir
      361 lldekgglis kaqtdsqgha tleksdkarl lmairdgqts midlrkpald lsefdiggpq
      421 gyskqffafg prdlyrpget livnallrdg dgnpikeqpv kvdllktdgq vsrsfvwqpe
      481 nglyqlklai padentgtrt lrfdigdgtp rfyefqvedf mpermalvit gkkgillsgn
      541 dayfdlegry lygapaadnr lqgqvflkas reavsklpgy efgtvkdenf srlldefeln
      601 ldsdgqgels vdsdryaelk spiniilqts lleaggrpvt rryqqavwpa thlagirpvf
      661 pkkevydyrt dkyksgysvd ensmaefeiv ytdqdgkklp andlkvkfiy erhdyywrws
      721 ssngwesgyn ekdlqmdeqt ikiakdgtak vafpvewgsy rievvdpkte lvsslrfwag
      781 yswmdntggt gavrpdqvkl kldkegylpg ekvklnivap hpgkgyvlle ssngplwwqe
      841 idvpekgldv evpinkewar hdlyltsvvv rpgdtskqat vkravgilhl plqdknrrid
      901 isldapekir pnqdlkirik anpvagqplp eninvlvsav dtgvlnitey ktpdpydaff
      961 grkrysidqy dvygqliegq grlanlrfgg dggeaaalsr ggkkpltdvq iiaqqtapvk
     1021 lnaqgegevs lpipefngev rlmaqawtad kfgsqegkvv iaaplvtqls lprfmaggdn
     1081 allsldltnl tddaqsitln ytasglvglg gaesktvslt kgertqvqip vkakhgfgqg
     1141 efslsiygik vpgeeikpyh ntwnigvrpa ypaetlhyas tlqdgetwsl ptdvlnrfnn
     1201 stlegelllt srpplqiary vrelfaypyg cleqtvsgly pslystekel kqlgiktqtd
     1261 adrkvaiekg iahlltmqka eggfslwnqd greeywltay atdflfrasq qgyavpaepl
     1321 krandrllry lqdkslvnye yavnqdaarf sarayaalvl anqqkaplge lrrlylernd
     1381 agsglalvql gialklmgdn sraegliaeg vtttrkynyg lgdygsvird qaliiallse
     1441 nnletqsrda svitlsdnlt srewfstqes nslylagrff inmseqpwev avnrqipais
     1501 sdravnetlt stqlqeglel nnrggaaiys rmnivgypkv apapysnvln vhrsyydlkg
     1561 nrvhpnrlqs gemlvvklev sadrdvpdal vvdllpagle ienqnlasss aslsdsaadl
     1621 qefiddmgqa nikhleyrdd rfvaavsvdr yrpttllyla ravtpgsyqv pppqvesmyv
     1681 pywraigste tkidivp
//
LOCUS       WP_284551168             495 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Cutibacterium acnes].
ACCESSION   WP_284551168
VERSION     WP_284551168.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..495
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52686
     Region          17..472
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mvsapnsaqd evrhgntapt asgagrgvek rtidmvpdge rhgtpksqft lwfgvnmqit
       61 avvngalaiv fgadvvwaii glfigqvigg avmalhsaqg palglpqmis sraqfgvyga
      121 alplflvlll yfgfaatgtv lagqainnaf gvqsrwigil vfaaltaiia mfgydlihkl
      181 gkvsstigll gllyvavrlf qvssfgpqlt hvhflvvpfl lsialaagwq ltyapyasdy
      241 srylprdtkf gsawfgpfag svlgatismt lgvfiaaagg qafigdqvgf mgnlaqnrvl
      301 ailvfisivi gkltintlna yggvmalsta lsgftgkssv spktrfgfvi gfnvvvvlta
      361 laassdflqv fksfiltllm fflpwsainl lnyylicrrc idipalytpr grygklhwpt
      421 ivvyllgvvv qipfisqafy vgpvaaamgg adiswlvglv vtalvyfplg rrafdyplei
      481 vypkdveldp sivsr
//
LOCUS       WP_284551183             752 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Cutibacterium acnes].
ACCESSION   WP_284551183
VERSION     WP_284551183.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 752)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..752
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77817
     Region          20..746
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mstpthpdaq selkdatept sinlditgms cascaariak klnkvdgaqa tvnyatskah
       61 vlttkpigvd dligvveaag ygasvptpaa ppedhaakir arlivaiila vpvmllsmip
      121 alqfdgwqwl alalslpvvf wcgegfhraa wtnlrhgats mdtlislgsl vslgwsvwal
      181 mwgsaghvgm rhrmtwaler tdpssalyle asvgvitfil igrwiearnr aeagsalqal
      241 lrmgaksvrm irdgqevtvp iealtvgdhf vvrpgekvat dgrvaegssa idaslvtges
      301 lpvevavgde vigatvntsg rlvveatavg sdtelsriat lveaaqtsrs ktqdladkvs
      361 sifvptvlii saltmivwav lgqgvtaaft agvavliiac pcalglatpm allagtgrga
      421 rlgivikgag slerargidv mamdktgtlt tgrmavvavw desgrvvnis dnppalavta
      481 alevgsehpi sraiveacpg vapaedfral pglgvsgtvn glpakagrvs lfdaipdtls
      541 knveraqaeg rtvlvvgrgd dilgaiavsd eikpeavvav krmvqagvrp vlvtgdnsga
      601 aahvaselgi devmsevmpa dkvdvvtrlr sdgsrvammg dgvndaaalq tadlsiamgt
      661 gtdvavaasd iictrgdprl avdalslaha tdrtirqnlf wafaynviai pvaavgllsp
      721 viaaaamafs sifvvtnsmr lvrwhpgmsd sn
//
LOCUS       WP_284551834            2348 aa            linear   BCT 25-DEC-2024
DEFINITION  amino acid adenylation domain-containing protein [Pseudomonas sp.
            T2.1D-1.1].
ACCESSION   WP_284551834
VERSION     WP_284551834.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. T2.1D-1.1
  ORGANISM  Pseudomonas sp. T2.1D-1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 2348)
  AUTHORS   Konz,D. and Marahiel,M.A.
  TITLE     How do peptide synthetases generate structural diversity?
  JOURNAL   Chem Biol 6 (2), R39-R48 (1999)
   PUBMED   10021423
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01733.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2348
                     /organism="Pseudomonas sp. T2.1D-1.1"
                     /db_xref="taxon:3041168"
     Protein         1..2348
                     /product="amino acid adenylation domain-containing
                     protein"
                     /calculated_mol_wt=258955
     Region          4..>2068
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
     Region          2073..2337
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mvrfarlpls pyqrdiwvaa aqfpeldqyt ifsydrftge vdtqaleral lqaardteaf
       61 rlrlgetdgt pyqwldadae fearhvdlra eaavrswlrd afrhaypldg rslvdlallh
      121 sdqalyvyvr thhivsdawg lqlflsrvra gylgelgepq aqmptaslla qletddysgs
      181 eqyrgdrayf aealeglepa lftrrrpagl rrtarhrltl ertlldaird rgespflfls
      241 aavalylari hqnddvvlgv pvlnradraa kqvvghfant lplrirtape qtvdeflaql
      301 reatrtllrh qkmplgdllr gasplfdttl symrwpaaqa ipnasvetva qthahdpdal
      361 aiwvsefdgh sdaqvdfeya cdvfdadfpm daaarhietf lralvegger rlgeldplsa
      421 aereelihtr natdqafpeq atlptlfaeq vartpqrtal leadggtlsy aeldakvqav
      481 adalraagvr tdervallva rgphllpail gvqraggayv pinpdhpler vrllledcga
      541 rvvlvderaa tlgeslgetr vlhlerlpqs tgdlpaanva pgdlayviyt sgstgmpkgv
      601 mvehrsvvnr lnwmqrrypi gerdvllqkt pvtfdvsvwe lfwwsftgar lsllppgaek
      661 dpremlrsiq rdavtvihfv psmltpfldl lngdptaraa asslrlvfcs gealaplqvt
      721 rfrrlfgdav rlvnlygpte atvdvsdhec asdnptrvpi grpidnlrly vldralrpqp
      781 lgavgelyig gvgvargyln rpelnaerfl vdpfvaggrl yrtgdlarwl adgnleylgr
      841 addqvkirgn rvepdevrdr laalpgvrda avvardsavr gthlvgyyva aaeldpgqlr
      901 aglsatlpdf mlpaffvrid slplsangkl drrqlpappe qvaavaprta teaelaavwa
      961 dvlgvaevgv hddfyalggd silmlriraa aqrrglgfel adlmrnptva glaerlvrpl
     1021 aersyqpfel vsevdkprle gledafptsr lslgllfhsr qrpdssvyhd vfhyrfdlaw
     1081 deaafrhald rvvaaypalr ssfdlsgase plqlvhtqar seplildlrg npeagtvlde
     1141 hirqrrfhry slqqpglflf aafvredgld lvfsfhhail dgwsvanliv alvaayrgep
     1201 lpgpapalac hvreelaala spaavgywte llegarmtrl dgfgahepqa aqgpashret
     1261 lpdgllerlk ataaqrglpl kslllaahcl tlhlfsrsds vvtgaisngr pelpdadrmv
     1321 glflntvpvr seiaghswie vadalfrqer dghahrrypl saiqqivgde lssafnyvnl
     1381 hvleplwqlr dfhvweetnf allvnviatp sdgmylrids dgrgisrsqa aligatfvel
     1441 lwrlaehpde aadfaflapr rdaasqpepl vdvvslferq vealpgsaal afeeqrwtyr
     1501 dldhvarcva trlvragarr gdaigvalnr spemiatiwg ilraglvcvp ldvsypaqrl
     1561 aliletaqpf rvvahpehah vaaaervlpv eelvadiepe tfaapqldel amllftsgst
     1621 grpkgvelsh rmwanytqwq lrvasgvpgl rtlqfaplsf dmafqeifst lcgggelqli
     1681 snrermdpsa llhvlerrqv qrvllpfval qrlaeasntl gvrpgalrvv vssgeqlrit
     1741 edvrafcaam pglllenqyg ptethqvtyh slsgdpahyp dlppigrpld gvevqvldaa
     1801 lrpvpvgvtg elyfggdcla rgyhrapelt aerfvehpwr pgarlyrtgd lgrilgngei
     1861 vwlgradtqv kvrgfriepa evelaimrqa erqpglrgaa vvarerqgnd aflaafllge
     1921 peavdlaelk qalrselpeh mvpahfawvd gfaltpsgkr ddaalralpl ehgtnieyla
     1981 prddyertla gllgelldrp rvgirdsffd lggtslsamr fmlliekryg vdlpmaalie
     2041 tptveglaer lrersavraf dplvpiragg srpplflvhp lgghvlcylp lvralppdqp
     2101 vyalqaagtg qgstplavle diaasylaai rrvqpegpyy lggwsfggfv ayemarqlra
     2161 ldpqavaqli vldsitvdrn hagsasdeal llffywelvw fersdeevep lpegasleqk
     2221 ldhiveraie agvlpagtpr atvqrlyelf raswqaligy rpevsdqdmt llradgplpl
     2281 alkpmhdaag thygdpkngw qhwtsgrldv idvpgdhlvl mkepyvetva aeiaalleps
     2341 tssertrp
//
LOCUS       WP_284551922             106 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Caminicella sporogenes].
ACCESSION   WP_284551922
VERSION     WP_284551922.1
KEYWORDS    RefSeq.
SOURCE      Caminicella sporogenes
  ORGANISM  Caminicella sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Caminicellaceae; Caminicella.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Caminicella sporogenes"
                     /db_xref="taxon:166485"
     Protein         1..106
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11875
     Region          8..82
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(11..12,14,17,20..21,24..25,28,58,80..81,83..85,
                     87..89)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(12..13,17..19,32..34,43..46,48..49,52..53,55..56,
                     62..64,69..71)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(32,35,80)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mnllnmevdi lkalahptrl qivkklakgt lcvcelnqdi elsqsnlsqh lkilrdanil
       61 vqerdgtrin ysikdkeile ivkiveklve eeikkiasqi ggmkda
//
LOCUS       WP_284552024             342 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Caminicella sporogenes].
ACCESSION   WP_284552024
VERSION     WP_284552024.1
KEYWORDS    RefSeq.
SOURCE      Caminicella sporogenes
  ORGANISM  Caminicella sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Caminicellaceae; Caminicella.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Caminicella sporogenes"
                     /db_xref="taxon:166485"
     Protein         1..342
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=40231
     Region          86..340
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mlqkkvsnlf sdiisnidie vnliddsgyi iestkkdkvg lidkfiankk iirdeviege
       61 nyiyyvncda kkvisfkece gtnrnlielm gkmilqeiki qltkkdflvd likekfdede
      121 iikycnyydi ninndffvvl ieidenlhde vekmiieayd evevlkfskn killilnsdi
      181 eiyekvlniy ndiyvelinn ckigigtkve sifmlstsyk kallalkygk ifyehkdiyf
      241 ynsmmipfli dnmeyktlke lsenindkle kiiknselis taqkffennl nitdtakqlf
      301 ihrntliyri nkiqkitgyd lrkfedamnf mialfivkyi ns
//
LOCUS       WP_284552096             195 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II [Caminicella sporogenes].
ACCESSION   WP_284552096
VERSION     WP_284552096.1
KEYWORDS    RefSeq.
SOURCE      Caminicella sporogenes
  ORGANISM  Caminicella sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Caminicellaceae; Caminicella.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Caminicella sporogenes"
                     /db_xref="taxon:166485"
     Protein         1..195
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21887
     Region          2..190
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 milmidnyds ftynlvqyle clkeevlvyr ndeitlkeik kiapdmivls pgpctpneag
       61 icidlvkkfk gqipilgicl ghqtigqvfg akilkavrpv hgkvypiihn nkgvfrglkn
      121 plnvtryhsl ivdkaslpdc feitaetseg eimgirhkey liegvqfhpe ailtemgmel
      181 lenflksakd fkvsr
//
LOCUS       WP_284552125             425 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Caminicella sporogenes].
ACCESSION   WP_284552125
VERSION     WP_284552125.1
KEYWORDS    RefSeq.
SOURCE      Caminicella sporogenes
  ORGANISM  Caminicella sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Caminicellaceae; Caminicella.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Caminicella sporogenes"
                     /db_xref="taxon:166485"
     Protein         1..425
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=49995
     Region          <8..425
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mlvkntdayf dyltglynrl ylfenfseni nefivvfldi ddfkyindty gyeigdeflk
       61 kfvrrlskiv gnrgkvfsyn adkflvlfpk enfkdiyekv ellfqklkei iivgdieiac
      121 sisigiyite kddkiddaik kaeiamqeak qkvkgqyvfy khqiekekmr kaniltelkk
      181 silrnelyil yqpilsvkgn kiqeveallr wnneklgevs pvefipiaee tgfiremgfw
      241 vieevcrqik ewkkknldlk vainispnqf kdkmffenyk yivknnnvef skikfeitet
      301 qifkteektv enlleimklg tkislddfga gyssmknmil ipcseikidk ifidyitkdt
      361 kiqnliasii htahrlgydv iaegveykeq ydklleydce kiqgyfisrp igekdiikfi
      421 krrss
//
LOCUS       WP_284552268             555 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC1 kinase family protein [Caminicella sporogenes].
ACCESSION   WP_284552268
VERSION     WP_284552268.1
KEYWORDS    RefSeq.
SOURCE      Caminicella sporogenes
  ORGANISM  Caminicella sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Caminicellaceae; Caminicella.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Caminicella sporogenes"
                     /db_xref="taxon:166485"
     Protein         1..555
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0004672 - protein kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=63901
     Region          6..470
                     /region_name="AarF"
                     /note="Predicted protein kinase regulating ubiquinone
                     biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport
                     and metabolism, Signal transduction mechanisms]; COG0661"
                     /db_xref="CDD:440425"
ORIGIN      
        1 myqirksykn mkrykeiaev lvkygfgffv kklhenklvp syvlkrkgni tlsteerirk
       61 iceelgptfi klgqiastrs dlfseelike lsklqenvki vsyeeissvf kdefkidled
      121 afikfdkkpi asasigqvyk atlysgeevi vkiqrpgikk iierdidill smsrlfdehf
      181 kdmfsfslyd immeltraik yeldytkear nterffenfk nnsnvyipki fwqytskkvl
      241 tqewidgisv snidklkekg wdikniakig aksflkqvfi dgffhadphp gnilvaneet
      301 iafidfglcg yldkskvsli tdlfiagakk dvekivella qidaisdetn ttrlkedllf
      361 lvshyynmpl kkinisdivs eflrityenn irlpsqftvl ikailtiegt grilnpefsi
      421 sstlrefsad iikhkyninn imdiavdfad dlkyglkifp nqirkilkil ednqikiaie
      481 dirfkalere lkqfsnkisl slivssliig sslvlnvktg pklfniplig figyfvasil
      541 gfflmisili skmkd
//
LOCUS       WP_284552320             441 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Caminicella sporogenes].
ACCESSION   WP_284552320
VERSION     WP_284552320.1
KEYWORDS    RefSeq.
SOURCE      Caminicella sporogenes
  ORGANISM  Caminicella sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Caminicellaceae; Caminicella.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Caminicella sporogenes"
                     /db_xref="taxon:166485"
     Protein         1..441
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50319
     Region          54..438
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mkvnyinekk msllaqssii ssrlsyyipq vnikyannmv hnivkdlsed lnsrimitdi
       61 ngkvivdsfn ilegqrlnne elalaligks taeqyiipky grvmyvavpi tnkgriigav
      121 fissslediy knikeimkkf milsllsmvi tgfisfvfad iistpierlt eavkrmaqgk
      181 fnqkveisgn deisnlgkaf nlmttkleqv dkqrrefvan vshelrtpls sikilaesli
      241 hqekveekiy keflkdidse vdrlnriids llslvdleke nlnldyqity vnyliekvin
      301 slkpladkkn ikiyyierek iqimldqfki qqslinvign aikytpenge ifvelysnsd
      361 eiiikvrdtg igipkedipf ifdrfyrvdk ararktggtg lglsitqqii alhqgrieve
      421 srinegttfy iflpkkaavn i
//
LOCUS       WP_284552325             237 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase [Caminicella sporogenes].
ACCESSION   WP_284552325
VERSION     WP_284552325.1
KEYWORDS    RefSeq.
SOURCE      Caminicella sporogenes
  ORGANISM  Caminicella sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Caminicellaceae; Caminicella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Caminicella sporogenes"
                     /db_xref="taxon:166485"
     Protein         1..237
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=27232
     Region          5..233
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mnsitlinnd tfkiintipd nsidliltdp pynlsqystg niklpwrsel nndiaewdki
       61 efspellvkd flrilkptgn ifaftsynli gkwhqafdkh fdtfqfmvwh ktnptpkvfk
      121 agflnsceli vcmwnkghtw nflgqnkmhn fiespicmgk erlknpkhps qkpikilkhi
      181 ikiasnegdv vfdpfmgvgs tgvaalelkr nfigieinke yfnaskkrln niqlslf
//
LOCUS       WP_284552365             410 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidase U32 family protein [Caminicella sporogenes].
ACCESSION   WP_284552365
VERSION     WP_284552365.1
KEYWORDS    RefSeq.
SOURCE      Caminicella sporogenes
  ORGANISM  Caminicella sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Caminicellaceae; Caminicella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787090
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Caminicella sporogenes"
                     /db_xref="taxon:166485"
     Protein         1..410
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=47421
     Region          1..307
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
     Region          325..404
                     /region_name="Peptidase_U32_C"
                     /note="Peptidase family U32 C-terminal domain; pfam16325"
                     /db_xref="CDD:465094"
ORIGIN      
        1 mnkvellapa gdleklryai iygadavyig gqtfglrtsa knfsfeemne gikfahdrgk
       61 kvyvtlniip hnddlrqlpe ylkklstmdi davilsdpgv lmyvrehapn leihlstqan
      121 ntnfmsanfw ykqgvkriil arelslkeis eirkntpedl eleafihgam cisysgrcll
      181 ssymanrdsn rgecahpcrw kyylveekrp geyipvfede kgtyffnskd lcmvnyipel
      241 ikaglgslki egrmksiyyv antvrvyrka iddyyklgen ykidsewiee lgkvshrkft
      301 tgfyfgkpne eaqlyasssy irdydflgiv ldydestgya tieqrnrmfk gdfieiigpd
      361 yklikqkinv mlddkgheid vaphaqqkik ilmdkpvdky filrrkrkdd
//
LOCUS       WP_284552380             765 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Caminicella sporogenes].
ACCESSION   WP_284552380
VERSION     WP_284552380.1
KEYWORDS    RefSeq.
SOURCE      Caminicella sporogenes
  ORGANISM  Caminicella sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Caminicellaceae; Caminicella.
REFERENCE   1  (residues 1 to 765)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 765)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 765)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455327
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Caminicella sporogenes"
                     /db_xref="taxon:166485"
     Protein         1..765
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=86762
     Region          <56..>200
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
ORIGIN      
        1 mkkntaivii lflmlgcifp stdyalsyqk pnvkapvnmv rsveksqvlv gkefkvrykf
       61 qpqpipagqi spdvylkdke ivlvmdtsgs mnrnlyggny gqsrmeiakk aakhfvdklk
      121 hdpsvkisli eydnfasvkq slvkltdkyn klnrqidnln agggtnigdg lrkayytlln
      181 sgsdnarkyi vfltdgepta fsfndieyrk kwiwdiwtps igelvgdnys imvsailnpi
      241 ykmdndssin yfvnwgtndy nnysleyakk vsnmignsdt pidaffiafs rdsnsnklke
      301 ianecngyyk kavddkalde vydklsqqia sdlpihsiyf eetfpdniei vnvpqnmeir
      361 gqkvigdigs inynlnketn qfeaepfefe itlraketgr fvlgendtsf irytdidgtv
      421 ntikyfpkse isvyenqppe ikakisnsfe sdkiyklnid idepaqieim dvngnslgky
      481 trntkgsfdi klnkedlvgn yiivkatdyf qneveekvpl iqineidisd ninennnreg
      541 nikivtqens iireitlndi llgenrltdn geyvqqveli hgmnslkivv vneynniael
      601 yckimsdnts lkiyskynnn qtkimqktve dikfnfkinv pvndlefvld ltknadsdin
      661 lntisifddn vkiiktdtgk niedinvmst inqngnliis idkdspiesg eytilvpikv
      721 ndnelgnsse fnlniikyki ngsevdlkds pveinikvvk lpgll
//
LOCUS       WP_284552516             256 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Caminicella sporogenes].
ACCESSION   WP_284552516
VERSION     WP_284552516.1
KEYWORDS    RefSeq.
SOURCE      Caminicella sporogenes
  ORGANISM  Caminicella sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Caminicellaceae; Caminicella.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Caminicella sporogenes"
                     /db_xref="taxon:166485"
     Protein         1..256
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30682
     Region          1..256
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mqgyekfkel iykktginls fykerqmkrr ieslikrnny nsyeeyynai ckdkklydef
       61 inyltinvse fyrnpeqwkv lkdeiipylm kdkkklkiws aacstgeepy slvmvlsnff
      121 plreieiiat didkealnka rvglyseksi enipsefkrr yfepvgnsyk isseikncvk
      181 fkqhnlledk ypdkcdlivc rnvmiyftee akefiyknfn kalnqngilf vgsteqiilp
      241 hrynfkplrt ffyqki
//
LOCUS       WP_284552987             209 aa            linear   BCT 25-DEC-2024
DEFINITION  LolA family protein [Caminicella sporogenes].
ACCESSION   WP_284552987
VERSION     WP_284552987.1
KEYWORDS    RefSeq.
SOURCE      Caminicella sporogenes
  ORGANISM  Caminicella sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Caminicellaceae; Caminicella.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Tajima,T., Yokota,N., Matsuyama,S. and Tokuda,H.
  TITLE     Genetic analyses of the in vivo function of LolA, a periplasmic
            chaperone involved in the outer membrane localization of
            Escherichia coli lipoproteins
  JOURNAL   FEBS Lett 439 (1-2), 51-54 (1998)
   PUBMED   9849875
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Caminicella sporogenes"
                     /db_xref="taxon:166485"
     Protein         1..209
                     /product="LolA family protein"
                     /calculated_mol_wt=25361
     Region          23..207
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mkykiflisi fiililvgcr eksdeqlfyd vqkfitslds ytctayitiy gnkepetyiv
       61 kqwykapdky ridiekpeel rgkttiyngn kvlirhpkig qgwimenykn tveqkmflgy
      121 fihnylnnen gkikkqtikk idyllfetei pgehpyfnre klwfeikkyy pyrlqildin
      181 dkirvdikyr nfeynqkikd dvfkihikn
//
LOCUS       WP_284553005             349 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Caminicella
            sporogenes].
ACCESSION   WP_284553005
VERSION     WP_284553005.1
KEYWORDS    RefSeq.
SOURCE      Caminicella sporogenes
  ORGANISM  Caminicella sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Caminicellaceae; Caminicella.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Caminicella sporogenes"
                     /db_xref="taxon:166485"
     Protein         1..349
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40784
     Region          34..349
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mkkklenkyi vekmiieekn nysflnfigv vvvmskvgna lkmliilqsr gkmkvcdlar
       61 elevderqir rykddllqag iyiksetgky ggysiednny llglnltnee ymsllmanee
      121 lkkmghlalk dyslamdkin ivykrenlnl lgncnymvks aranvnfeve rrklvdihaa
      181 mltrnkirik ytsltsgete rvvrpyatfq ykgdmyfigf cerkngilef klcrikeysi
      241 leekfemdns fsledymanc fgifkdeein vklkiyhpis qivkekiwvd nqkiieneed
      301 nsiifeatmk glkeikswil smgssvkvlk pqklideikn eidkikely
//
LOCUS       WP_284553287              61 aa            linear   BCT 25-DEC-2024
DEFINITION  FmdB family zinc ribbon protein [Caminicella sporogenes].
ACCESSION   WP_284553287
VERSION     WP_284553287.1
KEYWORDS    RefSeq.
SOURCE      Caminicella sporogenes
  ORGANISM  Caminicella sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Caminicellaceae; Caminicella.
REFERENCE   1  (residues 1 to 61)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10021090
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..61
                     /organism="Caminicella sporogenes"
                     /db_xref="taxon:166485"
     Protein         1..61
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6425
     Region          1..46
                     /region_name="CxxC_CxxC_SSSS"
                     /note="putative regulatory protein, FmdB family;
                     TIGR02605"
                     /db_xref="CDD:274226"
ORIGIN      
        1 mpifeyvcek cgykfeklvr ssdsdkkqkc pecgsentkk vfstfacggn sggfsapscg
       61 g
//
LOCUS       WP_284553229             216 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Caminicella sporogenes].
ACCESSION   WP_284553229
VERSION     WP_284553229.1
KEYWORDS    RefSeq.
SOURCE      Caminicella sporogenes
  ORGANISM  Caminicella sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Caminicellaceae; Caminicella.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 216)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Caminicella sporogenes"
                     /db_xref="taxon:166485"
     Protein         1..216
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=23263
     Region          <2..201
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mkqfliigag rfggsiattl ynmgndvlii ddseeainqi sgsvthaiqg naaderlist
       61 igannfdvcv iamgsdiqss ilvaimlkea garyivakaq nelhakvlyk vgvdkivfpe
      121 rdmgakiaqs lvssnimdyi elspeysive itaikewigk nllelnmrak yginimaikk
      181 gasinispta ltvieegdvl ivighnsdlk rlekkv
//
LOCUS       WP_284553455             235 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Caminicella
            sporogenes].
ACCESSION   WP_284553455
VERSION     WP_284553455.1
KEYWORDS    RefSeq.
SOURCE      Caminicella sporogenes
  ORGANISM  Caminicella sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Caminicellaceae; Caminicella.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Caminicella sporogenes"
                     /db_xref="taxon:166485"
     Protein         1..235
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26047
     Region          10..233
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 msillnalak taniipknir knltskvidy slkkyaqiev vnldivekrk siptiyignh
       61 lsnidgvvln kflknnniaf magvklsknp ltnlvletvn tilitpnsad kkaiksavnh
      121 lknggsifif pegtrsrtgs likakkgfil lakmanveiv pvalegtekl lpindanmgk
      181 ekfnygkvki tfgkpfcipe ktkenkdywt dfateysmkk iaellsskyq gvyri
//
LOCUS       WP_284553668             411 aa            linear   BCT 25-DEC-2024
DEFINITION  MDR family MFS transporter [Bacillus pumilus].
ACCESSION   WP_284553668
VERSION     WP_284553668.1
KEYWORDS    RefSeq.
SOURCE      Bacillus pumilus
  ORGANISM  Bacillus pumilus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023665
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Bacillus pumilus"
                     /db_xref="taxon:1408"
     Protein         1..411
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44157
     Region          13..388
                     /region_name="MFS_MdtH_MDR_like"
                     /note="Multidrug resistance protein MdtH and similar
                     multidrug resistance (MDR) transporters of the Major
                     Facilitator Superfamily; cd17329"
                     /db_xref="CDD:340887"
     Site            order(22..23,26..27,30,63,113..114,116..118,121,141,
                     144..145,148,221,224..225,228..230,233,263,267,316..317,
                     321,325,341,343..344,347..348,351)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mknnlrtlhp lswtiiigti fgrmatsmsi pflavyltqv kgasassagl iiavssligi
       61 vasfyggyis drigrkkvml lsifgwtlvf vgfafadaiw vlfimnalng lcralfepts
      121 kallsdvtps sirlfvfnlr ytainigvif gpllglylgs skttfpflva afiyllyglt
      181 lawqfqkhpv aapestkqig vkkalsiiqk dtvfsiilig vtlcsfgysh lsstlpqyls
      241 aspmiedgpk lfgyllslna vvvivvqypl imiakrysti lslttgnvll agslfaiafs
      301 qslgmlafii vvftigevll fammdlfvdn vakpevkgsy fgamgfsqlg svigpfvggl
      361 cidyfgaahp fsifsvlsii tiagvpflli gyyrlkkrsa atvavkvsgg h
//
LOCUS       WP_284553801            2382 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: amino acid adenylation domain-containing protein
            [Bacillus].
ACCESSION   WP_284553801
VERSION     WP_284553801.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 2382)
  AUTHORS   Konz,D. and Marahiel,M.A.
  TITLE     How do peptide synthetases generate structural diversity?
  JOURNAL   Chem Biol 6 (2), R39-R48 (1999)
   PUBMED   10021423
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01733.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2382
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..2382
                     /product="amino acid adenylation domain-containing
                     protein"
                     /calculated_mol_wt=266571
     Region          6..>2106
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
     Region          2132..>2299
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 msiqsvdsfp ltgaqagiwy aqqldpsnpi fntaeyidik gpidpihfea airktvlead
       61 slymrfvegt dgpkqwfssk keipfqlinl qnekqpfdaa iawmradlst pvslekdvlf
      121 revlfqladd rfiwyqrihh iaidgfafsl iarrvaevys alskgtpvpp qtfgslhdvv
      181 qeeityqqsn rydddrafwk nrfadqpeiv slaelaprts dhfirktasy daekvsimkk
      241 naqafggtwh emilaasaly mhrmtgahdi vlglpvmmrl gscalqtpgm vmnlvplrlt
      301 ckpemtlsal vhqvseelkt irphqryrhe dmrrdfklig rnqrlfgpqi nimpfdydlk
      361 fdqsigqahn lsagpvddis iniydradgn gfqidfdanp aiykeqavda hqqrflqlle
      421 eitgleqdqt isqfnlllsk ekenilkhwn dtkrklpkes lrelfekqvs ntpqakalqf
      481 egitltyeel nqranqlahy lkkhgigpeq fvaialprsi nmvvsllavv ktgaaylpid
      541 pdypndrvty mledakpacl ltiketadgl dhphivqldd atvhqeiags phlnptwseg
      601 sphhpayily tsgstgkpkg vvvtkrnvin filsmqdsfl ldqedqllav ttiafdisgl
      661 emflpllhga aillakketi qepaklsdmi rshhvtimqa tptlwhalad eypdvitgmr
      721 vlvggealpa sllhtlqslh cditnlygpt ettiwstmen vtahrensgp aigkpiwnts
      781 iyildeglnp vpagsigely iagegvsrgy lgrydltaer fvadpfgtkg trmyrtgdla
      841 rwredgsidy isradhqiki rgfrielgei etvmmqhqsi khtsvivred qpgqqllcay
      901 vvltdgsslh pselrqfvas llpdymvpsa vvvlpelplt pngkidrkal papnmslvss
      961 ertprtpqed mlcslfaetl alsqigidds ffdlgghsll aarllrrird tlgadlsmrt
     1021 ifesprvael aqhidkakdi rpplqvedkp deiplsfaqk rlwflhcleg psptyniplv
     1081 iqltgtldqt aligaladit ekhetlrtif pnkngmprqv ilhpksvqpe lhvtastdqh
     1141 ienqlneair ysfkieeepa lraelftlda nrsvlllllh hiagdgwsla pltrdlaaay
     1201 eariqgksis lpaepvqyad yaiwqqkllg seeetnslfa kqlsywkgal hdlpeelelp
     1261 ydfprpqegs fngatidfsi epalhqnlle lakqhqvslf mvlqaslaal mtrlgagtdi
     1321 pigspiagrn ddalddivgl fvntlvlrtn tagnptfsel lrrvrdvdla ayehqdlpfe
     1381 rlveilnpnr srsrnplfqv mlafqntpka emkltqldsd lyvkpvgsak fdltielteq
     1441 ktetgsaagl tglfefstdv fkqstiraia drmkrfltev aeqphvpigq vniltdkerh
     1501 tflpdkktfa qldqahrlpa lfektaqqyp drvavtygnr qltygelnnk anrlahlliq
     1561 rgvgpeqfva lalprsidml vsllavhkag aayvpldpdy padrlaymiq dakpvcsitt
     1621 kvnavhlpad cdlilldeke tsdqlltmpn hnpadidrie plsslhpayi iytsgstgkp
     1681 kgvviphqnv irlltstehw fhydeedvwt mfhsyafdfs vweiwgplly ggrlvivpht
     1741 isrspeemlq llveegvtvl nqtpsafyql mqidkehqtl gqalslryvi fggealelsr
     1801 ledwysrhsd ckpklinmyg itettvhvty nelnrdmitk nsssligepi pdlhvyvlde
     1861 ylqpvppgtt gemyvagagl argylgrpdl tsdrfpadpy gapgtrmyrt gdlarwteeg
     1921 aldyigradh qikirgfrie lgeieavlar hdavaqvavm mredqpgdkr lvayivttee
     1981 drfdtealrh faaaslpdym vpaayvqida mpltangkld qkslpapqlh lqqadgrgpr
     2041 npkeeilchl feevldlpki siddrffdig ghsllavrli srirdalgvk lsigtlfeap
     2101 nvaslaekle tgsdenaldi llplrtnger yplfcvhpag glswcyagll ntlekdipiy
     2161 glqargiark ddyphtlddm aadyikhiqt iqpkgpyhll gwslggnvvq amatqlqqqg
     2221 eeialvamld aypnhflpik aapdeeeali allalggydp dtltgepltm ksavdilkkd
     2281 gsalaslsen airnlketyv nsvrllgeyq pktyqgdilf frstiipdwf tpidpeawap
     2341 yingtieqhd ihcrhkdmcq pkplaeigvi ldnalhrvkq kh
//
LOCUS       WP_284553814             336 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Bacillus pumilus].
ACCESSION   WP_284553814
VERSION     WP_284553814.1
KEYWORDS    RefSeq.
SOURCE      Bacillus pumilus
  ORGANISM  Bacillus pumilus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Bacillus pumilus"
                     /db_xref="taxon:1408"
     Protein         1..336
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37993
     Region          37..298
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mkkriwliiv ataficiaaf vfyennfamn vkevvmeten galsgimttp kkapikgivl
       61 fvhgdgpqna tydggyrplm erfakqgyas iswdkpgvgq segnwlhqsm ddrakevgnv
      121 ikwakkepdl qskqiilwga sqagwvipkv madrtditas ilvgpsvnwm rqgryntlqt
      181 lketnasqeq iqktiekede qnklleegaa frtyhkktsd qemikdryef iqknmkadat
      241 sdikriqspi ylvlaqndrn vdsaetkriy ekevapkwlh vqtirgvehs mlnplihhsn
      301 alitlaaiaa pkdfllsqay ldhcehileq lktpsh
//
LOCUS       WP_284553986             308 aa            linear   BCT 25-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase, partial [Escherichia
            coli].
ACCESSION   WP_284553986
VERSION     WP_284553986.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10594375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>308
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
     Region          117..253
                     /region_name="SIR2_2"
                     /note="SIR2-like domain; pfam13289"
                     /db_xref="CDD:433090"
ORIGIN      
        1 mseyvelaya aatsrlclft gtgfskavsn geaptwkell kkvcskvhna kkledtlfpd
       61 dkppalslee aaqilslkln iegksiydei vdiispiqlg edisnikdff qknsfrvitt
      121 nydklaeclv gdesvqsitp glpipkypsk vkiyhvhgsi dspknmivts ddyfrfinsd
      181 tyfsrklstm lhentvailg yslsdtnlka iindykkfsk nnalcsnifl isrnkvsqdm
      241 kdyyfycfgi rvidnteidc ffsrlsykis likdiierar enirkvvsga ytykneylkl
      301 edsfyqii
//
LOCUS       WP_284554110             495 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Citrobacter].
ACCESSION   WP_284554110
VERSION     WP_284554110.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..495
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54275
     Region          113..351
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mknlfrrvkw vssgllalvk hvvltllvvl ivflgvrvyq tesgpdlhlw htwhgnemsa
       61 aaldnatfaq yqaqeemlfa dlqkqvgdkl sadeqtpinr fwsgsrvypa qftpngnrsf
      121 vlmpqgkprg vavmlhgltd spyslkylaq iyqrqgfiav vprlpghgta pgaltavdwe
      181 awlaatrlav reatrlagte vplhlvgysn ggalalkytl dsldddalrr prqlvllspm
      241 igvtsfarfa glaglpalfp afakaawlnv tpeynpfkyn sfpvnaarqs ylltkalqqq
      301 ivqdaqntrl hdlppvltfq svmdstvstq avvdslyryl gpngselvlf dinqaanlrp
      361 llrsasytaa atllpsvpra yrttvvtnat aetvavvard tlagtrevqi qplreawpqe
      421 myslshvavp fpltdslygl kpdalnrygv sigtialrge tatllvgldt lmrvtsnpff
      481 pylqerveav vggqr
//
LOCUS       WP_284554165             119 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 4 protein, partial [Citrobacter sp.
            T1.2D-1].
ACCESSION   WP_284554165
VERSION     WP_284554165.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. T1.2D-1
  ORGANISM  Citrobacter sp. T1.2D-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10601751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Citrobacter sp. T1.2D-1"
                     /db_xref="taxon:3041164"
     Protein         1..>119
                     /product="glycosyltransferase family 4 protein"
     Region          <1..111
                     /region_name="Glyco_transf_4"
                     /note="Glycosyltransferase Family 4; pfam13439"
                     /db_xref="CDD:463877"
ORIGIN      
        1 mykkfsfnpl dqinlgrfik klkpdlvhfa mtpqepvfyr gkrittthdl tmlrftragr
       61 hsmlvhwvrm mgyrwlfwes hrrskaiivp teyvkadlik lspatkdkii vtleaaepp
//
LOCUS       WP_284554216             171 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Citrobacter].
ACCESSION   WP_284554216
VERSION     WP_284554216.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 171)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11970396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..171
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19711
     Region          1..149
                     /region_name="PRK11475"
                     /note="DNA-binding transcriptional activator BglJ;
                     Provisional"
                     /db_xref="CDD:236915"
     Region          105..150
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mtsvpwqvmv dysaryrhrl mifniisheq syadfvsyln ksrfklydna vvviadsrla
       61 alciellyve kaivltdksp lrdfgrlttl teecwnprvf rsqkrlsdre qqilsllvsg
      121 yspneisdli svsyktiqth kmriivklgl ahstalnkqi vrfnhplsfl s
//
LOCUS       WP_284554273             212 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Lelliottia sp. T2.26D-8].
ACCESSION   WP_284554273
VERSION     WP_284554273.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia sp. T2.26D-8
  ORGANISM  Lelliottia sp. T2.26D-8
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Lelliottia sp. T2.26D-8"
                     /db_xref="taxon:3041165"
     Protein         1..212
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=22971
     Region          4..212
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mrmkkdepis srikriresk glsqkalael cgwasqsrig nyeagsrsvs vddaeviara
       61 lgisapellf gdnfaghytp gvkypliswv sagawseate pytlkeidew yesdahiegs
      121 afwlrvqgds mtspvglsip egmmvlvdtg keaqngslvi akltdaneat fkklvidggh
      181 rflkglnpiy plipingnck iigvavqtmm kl
//
LOCUS       WP_284554386             420 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lelliottia sp. T2.26D-8].
ACCESSION   WP_284554386
VERSION     WP_284554386.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia sp. T2.26D-8
  ORGANISM  Lelliottia sp. T2.26D-8
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Lelliottia sp. T2.26D-8"
                     /db_xref="taxon:3041165"
     Protein         1..420
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=47519
     Region          2..407
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 malsdvkvrs akpeekaykl tdgdgmvllv hpngskywrl ryrfggkekm lalgkypevs
       61 ladararrde arkqlangvd psenkkavkv eqeqeaitfe vvardwhasn qkwstshsar
      121 vlkslednlf aaigkrniae lktrdllvpi kavessgrle vaarlqqrtt aimrfavqsg
      181 lidynpaqei agavatakrq hraalelnri pellhridhy sgrpltrlav eltllvfirs
      241 selrfarwae vdfetamwti pgerepldgv khsqrgskmr tphlvplshq alailekiks
      301 mngnrelifv gdhdhrkpms entvnkalrv mgydtktevc ghgfrtmacs slieaglwsr
      361 daverqmshq erssvraayi hkaehlgerr lmlqwwadyl danrekgvsp fdfgktnnet
//
LOCUS       WP_284554448             245 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Lelliottia sp. T2.26D-8].
ACCESSION   WP_284554448
VERSION     WP_284554448.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia sp. T2.26D-8
  ORGANISM  Lelliottia sp. T2.26D-8
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Lelliottia sp. T2.26D-8"
                     /db_xref="taxon:3041165"
     Protein         1..245
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28764
     Region          1..242
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mkviivedei laqqelswli kehsqieivg tfedgldvlk flqhnkvdai fldinipsld
       61 gvllaqninq fahkpfivfv tawkehavea feleafdyil kpyqesrivs mlqklemawq
      121 qqnhsavsts pvitrendtl nlikderiiv tpmddiyyae ahekmtfvyt rresfvmpmn
      181 itefcsklpa shffrchrsf cvnlnkirei epwfnntyil rlkdldfqvp vsrskvkefr
      241 qlmhl
//
LOCUS       WP_284554580             262 aa            linear   BCT 25-DEC-2024
DEFINITION  TPM domain-containing protein [Escherichia coli].
ACCESSION   WP_284554580
VERSION     WP_284554580.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Sirpio,S., Allahverdiyeva,Y., Suorsa,M., Paakkarinen,V.,
            Vainonen,J., Battchikova,N. and Aro,E.M.
  TITLE     TLP18.3, a novel thylakoid lumen protein regulating photosystem II
            repair cycle
  JOURNAL   Biochem J 406 (3), 415-425 (2007)
   PUBMED   17576201
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..262
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28760
     Region          18..223
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mkkfiillsl lillplvats kplipimntl ftdvtgtvpd aeeiarkael frqqtgiapf
       61 ivilpdinne aslrqngkam lahassslsn vkgsvlllft treprlimit ngqvesgldd
      121 khlgllienh tlaylnadlw yqginnalav lqaqilkqpt ppltyyphpg qqhenappgs
      181 tntlgfiawa atfilfswif cyttrfiyal kfavamtian mgyqalclyi dnsfaitris
      241 plwagligvc tfiaalllts kr
//
LOCUS       WP_284554619             125 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_284554619
VERSION     WP_284554619.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..125
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          <10..115
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 aagtvsqpgr nvraksglnr sildqgwyem rrqleykqlw rggqvlavpp aytsqrcayc
       61 ghtakenrls qskfrcqvcg ytanadvnga rnilaaghav lacgemvqsg rplkqeptem
      121 iqata
//
LOCUS       WP_284554716              54 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator, partial [Escherichia
            coli].
ACCESSION   WP_284554716
VERSION     WP_284554716.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 54)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 54)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 54)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..54
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..54
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          1..53
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mafitqltgl tdkwfyklik dgafpapikm grssrwlkse veawlqaria qsrp
//
LOCUS       WP_284554762             263 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase [Escherichia coli].
ACCESSION   WP_284554762
VERSION     WP_284554762.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..263
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=28771
     Region          27..262
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mtvgiaiqhq pahtpehtkv yqtdnatlcr gnaleilpli epesidalit dppyssgath
       61 kagrtnqgsh akylngeslh rfdgfagenm darswaywtq lwmaqahrav rpggyalvft
      121 dwrqlpaltd afqasgftwr giiawnkgrg srtphtgyfr hqceyivwgs kghldkspsg
      181 pfdgcmtfpv ipskkmhptg kpeelmaelv rtansggtvl dpfmgsgttg vaalkagrkf
      241 igietsdhyf dvatqrlkta ies
//
LOCUS       WP_284554827             258 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: dimethyl sulfoxide reductase anchor subunit family
            protein [Atlantibacter].
ACCESSION   WP_284554827
VERSION     WP_284554827.1
KEYWORDS    RefSeq.
SOURCE      Atlantibacter
  ORGANISM  Atlantibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Atlantibacter"
                     /db_xref="taxon:1903434"
     Protein         1..258
                     /product="dimethyl sulfoxide reductase anchor subunit
                     family protein"
                     /calculated_mol_wt=26932
     Region          3..253
                     /region_name="DmsC"
                     /note="DMSO reductase anchor subunit DmsC [Energy
                     production and conversion]; COG3302"
                     /db_xref="CDD:442531"
ORIGIN      
        1 mhelplvfft vltqsavgaf illligsalg hieprrlaig lfvsvcvfga gvvmgifhvg
       61 qplrainmlf rvghspmsne ivlsavfgav aglaalglll nrgatrlftv lawiaavigv
      121 vfifaipriy qlptvaawrt swttammvlt pfigggalaa aigarrlgav vsllaiavsf
      181 clrpgylsei vmadgalasa qsswftaqav lliagaiaal lylrsksapt llfataslvi
      241 aaellgriaf ynlwaipm
//
LOCUS       WP_284554859             654 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidase U32 family protein [Atlantibacter hermannii].
ACCESSION   WP_284554859
VERSION     WP_284554859.1
KEYWORDS    RefSeq.
SOURCE      Atlantibacter hermannii (Escherichia hermannii)
  ORGANISM  Atlantibacter hermannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Atlantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Atlantibacter hermannii"
                     /db_xref="taxon:565"
     Protein         1..654
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=72717
     Region          6..304
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
     Region          438..505
                     /region_name="DUF3656"
                     /note="Collagenase; pfam12392"
                     /db_xref="CDD:463557"
ORIGIN      
        1 mrlhphhlel lspardtaia reailhgada vyiggpgfga rhnasnslrd iaelvpfahr
       61 ygakifvtln tilhddelep aralihqlwe agvdalivqd mgvleldipp ielhastqcd
      121 irsvekakfl sdvgfsqivl arelnlnqik aihdnvdati effihgalcv aysgqcnish
      181 aqtgrsanrg dcsqacrlpy tlkddqgrvv ayekhllsmk dndqsanlaa lvdagvrsfk
      241 iegrykdmsy vknitayyrq lldevmeqrg dlarasagvt qhffvpspdk tfhrgstdyf
      301 vnarkidiga fdspkfiglp vgevmkvakd hldvdvtepl sngdglnvlv krevvgfran
      361 tvenlagnry rvwpnempda lktlrphhpl nrnldhnwqq allktsserr vavdielggw
      421 qeqliltmts eegvsvtrtl dgefneannp ekaynslrdg vtklgqtmyy aravninlpg
      481 alfvpnslln qlrretsdal dearlaayqr atrkavsepa pvypdshlsf lanvynhkar
      541 efyhrygvql idaafeahqe kgdvpvmitk hclrfafnlc pkqakgsiks wkatpmqlih
      601 gdevltlkfd crpcemhvig kiknhilkmp lpgsgvvasi speellktvp grka
//
LOCUS       WP_284554880             371 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Atlantibacter
            hermannii].
ACCESSION   WP_284554880
VERSION     WP_284554880.1
KEYWORDS    RefSeq.
SOURCE      Atlantibacter hermannii (Escherichia hermannii)
  ORGANISM  Atlantibacter hermannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Atlantibacter.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Atlantibacter hermannii"
                     /db_xref="taxon:565"
     Protein         1..371
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40223
     Region          31..356
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mskchfrsra rllaasavfi aliaagiylq pgfstpsprq tgdaslvsfl tpllkgsrgs
       61 vaaalitprg vqyalwdsdy nqqyeiaslt ktmtssllid afrrgeataq trvgdlipei
      121 sgpareitle qlashrsglp plasslrqki rvirqiilre nfweydeksv iemvnntrla
      181 tparfdysnt gyallglals raahqtfnsl lqtrvfaqak mtnsvvaeal tpgtptfhhg
      241 wavsgfaeap wiqnaftpaa gvrstivdma hyaqallagk lagnaamqpr fatddadsrv
      301 gyawfttrir grditwhdge ssgfasaiav dpqqrsavvi lsdtawpvig pamrllltqt
      361 panteahhel d
//
LOCUS       WP_284555325             386 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Bacillus toyonensis].
ACCESSION   WP_284555325
VERSION     WP_284555325.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..386
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42158
     Region          39..384
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkkhcqitst glvllmtgss llyttpssiv kaesdqnvss slqtntqrdr tsvkkamrdt
       61 lqlgypgila kvskdrktws yaagvadlrt kkpmkadyrf rigsvtktfi atvllqlsge
      121 nrlnlddsie kwlpgviqgn gydgnqitir qllnhtsgia eylkskdydi mdtkklytae
      181 elvkmgislp pdfapgkgws ysntgyvilg mliekvtgns yaeevenriv eplelsntfl
      241 pgnstvipgt nhargyfqld easepkdvty sypgnsdgdm istaddlnkf fsyllsgkll
      301 keqqlkqmlt tvptgtevid gyglgiyekk lsngvsiwgh tggspgfstf aggtiggkht
      361 lainlngnkv nrsdpfknil laefsk
//
LOCUS       WP_284554928             338 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Atlantibacter
            hermannii].
ACCESSION   WP_284554928
VERSION     WP_284554928.1
KEYWORDS    RefSeq.
SOURCE      Atlantibacter hermannii (Escherichia hermannii)
  ORGANISM  Atlantibacter hermannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Atlantibacter.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Atlantibacter hermannii"
                     /db_xref="taxon:565"
     Protein         1..338
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=37268
     Region          2..331
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkilvtgats glgrnaveyl rqqnisvvat grnrlageel tregavfvpl dlaqanheqc
       61 vslmagcdav whcaaksspw gdrdafwqdn vnatstlaka agslgiprfv histpavyfd
      121 fqhhydvpet ylastfsshy asskreaerv iadaaacfgs ttfiilrprg lfgphdnviv
      181 prllrqlhqd ggvlrlprgg ealldltfvq nvvyamerat ysetlssgsi ynvtnhqpqr
      241 ladmldallr qqlglnytir svpwplmslv arcmelkgkc inkeppvtry sagtvcfdmt
      301 lstkkaveel gyiprfsmeq gialtgewlr nngknyri
//
LOCUS       WP_284555465             299 aa            linear   BCT 25-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Bacillus toyonensis].
ACCESSION   WP_284555465
VERSION     WP_284555465.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Rengstl,B., Oster,U., Stengel,A. and Nickelsen,J.
  TITLE     An intermediate membrane subfraction in cyanobacteria is involved
            in an assembly network for Photosystem II biogenesis
  JOURNAL   J Biol Chem 286 (24), 21944-21951 (2011)
   PUBMED   21531723
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Komenda,J., Nickelsen,J., Tichy,M., Prasil,O., Eichacker,L.A. and
            Nixon,P.J.
  TITLE     The cyanobacterial homologue of HCF136/YCF48 is a component of an
            early photosystem II assembly complex and is important for both the
            efficient assembly and repair of photosystem II in Synechocystis
            sp. PCC 6803
  JOURNAL   J Biol Chem 283 (33), 22390-22399 (2008)
   PUBMED   18550538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..299
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=33407
     Region          53..>134
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
ORIGIN      
        1 metmlsatai tklrdgklml attydglfie qdgewkqiln gfqkrirdlh svdnivygvg
       61 degtfirsmn ggenwtiqrf ptkatswnvc sniqgtviah gdktlylsnn fgstwetihp
      121 fldygsdaps irslflykhy lfigtkihak yggvwlfdle krklkrikia mnqmisaltl
      181 hnsylvaasg sckgiggnis fckidesien eklywhtcqs eqkassyldl svdqhvlytt
      241 stqnkagvst vcrvhlnegi vtvcdsvkgh gwrivnqkeg yvvagsgesk amqwkkkvv
//
LOCUS       WP_284555586             457 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Bacillus toyonensis].
ACCESSION   WP_284555586
VERSION     WP_284555586.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..457
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=50416
     Region          3..438
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mykiavagtg yvglvagvcf aevghqvtcv didekkvelm ksgvspiyea dleelmqkny
       61 gagrinyttd yksaykdada ifigvgtpeq adgsanlsyi atvakqiaes vekdclvvvk
      121 stvpigtndk veqfiqdflv nnvkvevasn peflaqgsav hdtlyaeriv igteskwaee
      181 vltnlykpfh lpivsvnrrs aemikyasnd flalkisymn dianlcelvg adiqdvakgm
      241 sfderigskf lnagigfggs cfpkdtkale ylarqngyel rtvkaaidvn kdqktllykk
      301 asqrlitfdg lkvavlgltf kpgtddlrea asleniplll eqgadiyafd pvgannfakv
      361 yregsnkhgn ityvtnieqa leganvcfif tewgevkalt pemykklmrt pliydgrniy
      421 diqsmqeagi eyhsigrkst srdrmkelyn ielqtsk
//
LOCUS       WP_284555944             112 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Bacillus
            toyonensis].
ACCESSION   WP_284555944
VERSION     WP_284555944.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..112
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12673
     Region          10..108
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mdlqepklkg viatlqiigg kwkplilfil ltdgtqrfge lkrlipdisq gtlakqlrel
       61 eqdqlikrem yqeippkvey slsehgktvs tvldsmcgwg kghlefidkn rl
//
LOCUS       WP_284556002             161 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Atlantibacter hermannii].
ACCESSION   WP_284556002
VERSION     WP_284556002.1
KEYWORDS    RefSeq.
SOURCE      Atlantibacter hermannii (Escherichia hermannii)
  ORGANISM  Atlantibacter hermannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Atlantibacter.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Atlantibacter hermannii"
                     /db_xref="taxon:565"
     Protein         1..161
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=17490
     Region          <1..144
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mtfafvllyi vlcgclcwhd wcttllpdrf tcpllwggll fntllspasl pdavlgavmg
       61 ygtfsifywl yrlmrgyegl gygdikllaa lgawhgwqsv stivliasls glilggllff
      121 kgadrnkktp lpfgpflvaa gfctswptfg plimvtikpa l
//
LOCUS       WP_284556231             417 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Atlantibacter hermannii].
ACCESSION   WP_284556231
VERSION     WP_284556231.1
KEYWORDS    RefSeq.
SOURCE      Atlantibacter hermannii (Escherichia hermannii)
  ORGANISM  Atlantibacter hermannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Atlantibacter.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Atlantibacter hermannii"
                     /db_xref="taxon:565"
     Protein         1..417
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44291
     Region          8..416
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 mekanfprrv avtgygaitp lgmsaseswa simdyrpgya fhptssqeig ahvfglvdke
       61 pdlralpsai rrrlprfarm vmgaaneavt mafhgqsplr whsalksgvv igtgwagqde
      121 sysyydefle agmgnvfscf hampsvataa csinwglrgy qntpvaacat gsiaigdafe
      181 aircgrttmm lagageslrs taaiwnidvl galtgetedl akaccpfsld rngfvlsega
      241 avvcleeyev avargatilg eikgygnfsd aydftapapd cearvhsitq alrqagmrgq
      301 didyinahgt stplndlnet qaiklalgeq aykipvsstk swsghliaaa gsfetivclq
      361 aiqhqimpat ahlthpdpec dldyipgthr qgqvkntlnl sfgfgganaa lvigqaq
//
LOCUS       WP_284556414             356 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Atlantibacter hermannii].
ACCESSION   WP_284556414
VERSION     WP_284556414.1
KEYWORDS    RefSeq.
SOURCE      Atlantibacter hermannii (Escherichia hermannii)
  ORGANISM  Atlantibacter hermannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Atlantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Atlantibacter hermannii"
                     /db_xref="taxon:565"
     Protein         1..356
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38447
     Region          1..354
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mmkthvaivg aglsglyaaw lleqagtdyv vlegrnrvgg rilpidstgv dlgatwlwpa
       61 iqpglcella qlglatfthq etgdmlfera tdaasrypgf vsapaaarvh ggmsqltdal
      121 larlapgrvi tgvqvmqvee hhgmltvhgr saaqqsvtlh arhlllalpp mlasriaftp
      181 alpqslrqaw rntgtwmaph akyvaryshd fwkrsglsge arssigpmve ihdvsetdrl
      241 salfgfiglp fharqengdd alrqqcraql vrlfgpdaah peaeflkdwa adpftatsrd
      301 rvlqpghfvp pawcaegvwr dvmtgiasew spafpgylag aidaaatgiq riikea
//
LOCUS       WP_284556418             170 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Atlantibacter hermannii].
ACCESSION   WP_284556418
VERSION     WP_284556418.1
KEYWORDS    RefSeq.
SOURCE      Atlantibacter hermannii (Escherichia hermannii)
  ORGANISM  Atlantibacter hermannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Atlantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Atlantibacter hermannii"
                     /db_xref="taxon:565"
     Protein         1..170
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=19168
     Region          49..160
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mtrwrdglrk gmpppvllfl fllfdvwssw palihpeqlv ilswrtcaav viggvslcla
       61 lsglfmlisr kttlnalfpe rtrvlvtegc yrysrnpvyl gfvglhiaaa llldsvigil
      121 atpvlvtllt llhiqveeag mrqrfslqwq qycdktprwl sgkslfrrls
//
LOCUS       WP_284556466             654 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Atlantibacter hermannii].
ACCESSION   WP_284556466
VERSION     WP_284556466.1
KEYWORDS    RefSeq.
SOURCE      Atlantibacter hermannii (Escherichia hermannii)
  ORGANISM  Atlantibacter hermannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Atlantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Atlantibacter hermannii"
                     /db_xref="taxon:565"
     Protein         1..654
                     /product="PhoX family protein"
                     /calculated_mol_wt=70971
     Region          26..648
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 msrplkplfk qehsdeisnr sanpvfsdva saflsrrrfl qmgvvagaav sfpallkspa
       61 awavesaisr psslgftsia vstddtvrvp egyvarpfyr wgdavglkgn lpefktdgsn
      121 ttdeqaaqag mhhdgmawfs lplggddphh gllamnheyi dngllfkdgv anwnldkvrk
      181 gqnamgisvi evkkegdswt vvrpsefarr itvntpmklt gpakhhalmk teadpqgetv
      241 lgtmqncang htpwgtyltc eenwsdifvk kaapnalekr ygisdsdesy rwnevdprfs
      301 vdatpnepnr fgwvveidpy npqstprkht algrfkhega aitlaadnrv vaymgddqkf
      361 eyiykfvsan kydasqreaa mdllsegtly vakfngdgsg twlllvygqg gldesngfas
      421 qgelliktrl aadvvgatkm drpewiavdp laagsvyctl tnnsdrgkeg kapvdaanpr
      481 annvyghimh wteenndpas gafkwdilvl ggkpdsadek akgsmngaef gsadglsfdh
      541 rgvlwiqtdv ssstinkkay egmgnnqmla tvpgtneyrr fltgprgcei tgiaftpdnr
      601 tlfiniqhpg epgddisdpa nptavstwpd gdkngrprss tvvivkadgg iigs
//
LOCUS       WP_284556610             400 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein, partial [Escherichia coli].
ACCESSION   WP_284556610
VERSION     WP_284556610.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..400
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
     Region          153..392
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 llyligllfv pidlnittki inatgafslf llivnkkhny nknviililg llllgamnli
       61 wyefyktedv vyrnayrgyl esgkllvfss ltflllsknk frqneklhfi sailvqiiml
      121 crayyqgiyl hadriplsam ngnigqmgaa tiaayvitft tlyssivfik mqskykwflf
      181 yanfalsfaa vmmtgtraai ftfplmimvi lflqhrdqkv flfkglsgvf illlacglif
      241 nkeidrrins lkadvisyat knnsqssvga rfamvnagik gspdgfnwqs leqraekika
      301 lsaenniysg allfldvhmh neiveslstk gkigllvlim fyvamiyyci rekkyillvf
      361 pasimlfgis dvithakpip aswivclfls isflsknepq
//
LOCUS       WP_284556701             389 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Bacillus toyonensis].
ACCESSION   WP_284556701
VERSION     WP_284556701.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..389
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41610
     Region          75..387
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mktrsqitca slalliagsa llytsptsiv kaaptqnvss ssqtstqrdr tsvkqamrdt
       61 lqlgylgila ktseggktwg yaagvadlst kkpmktdfrf riasvtktft atvvlqlage
      121 nrlnlddsie kwlpgviqgn gydgnqitir qilnhtsgiv eyarskeidf ftntkksfta
      181 eelvkiglsm ppefapgkgw sysntgyvll giliekvtgn syaeeienri ieplelsntf
      241 lpgnssvipg tkhargylqp dgaselkdvt yynpsigssa gdmistaddl nkffssllgg
      301 kllkeqqlkq mlttvptgia etggyglgiy etklpngvsi wghsggipgf stfaggtlgg
      361 khtlavnlnn lkadspdpfk nillaefsk
//
LOCUS       WP_284556689              95 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Bacillus toyonensis].
ACCESSION   WP_284556689
VERSION     WP_284556689.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 95)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 95)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 95)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..95
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=10597
     Region          4..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlnyekdaev fkalahpvri eilkeliirg acnvtqivgi lgipqstvsq hlakmksqkl
       61 irndrkglev yysaqnkain siveilldyk stnck
//
LOCUS       WP_284556702             389 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Bacillus toyonensis].
ACCESSION   WP_284556702
VERSION     WP_284556702.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..389
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41824
     Region          34..387
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkirsqitca slalliagss llyttpasiv kaeptqsvss slqtstqrdr nsvkqamrdt
       61 lqlgypgila ktseggktwg yaagiadlrt kkpmktdfrf rigsvtktft atvvlqlvge
      121 nrlklddyie dwlpgviqgn gydgnkitir hilnhtsgia eysrskdadf tdtkksytae
      181 elvkmgvslp pdfapgkgws ysntgyvllg iliekvtgns yaeeienrii eplelsntfl
      241 pgnssvipgt nhargyvqpd gaselkdvty ynpsagssag dmistaddln kffsyllggk
      301 llkeqqlkqm lttvptgkeg idgyglgiye tklpsgvsiw ghsggilgft tlvggtlggn
      361 htlvvnwnsl grtgspnpfk niliaefsk
//
LOCUS       WP_284556990             335 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Bacillus toyonensis].
ACCESSION   WP_284556990
VERSION     WP_284556990.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..335
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35417
     Region          26..330
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mqktnavpvt ilciapilil atvilsilyg aksidaetvw nalfhfdssd vnhniiitsr
       61 lprvvaallv gaflaisgal mqgmtrnyla spsimgvtdg aafvitlcmi flpgmssigm
      121 vlcsmigsal gagivfgfgs llqnglspvr laiigtvigt flssvsaama syfqisqnvs
      181 fwfnakldqv dpniikitip fgiigivlal liaksitils lgeevsinlg qrtklvkama
      241 ilsvifltgt avalvgkvgf vgliiphitr fiigvdykwi lpcvgviggv flalcdllsr
      301 fvnypfetpi gvvtsligip fflylirtrg gerha
//
LOCUS       WP_284556953             321 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Bacillus toyonensis].
ACCESSION   WP_284556953
VERSION     WP_284556953.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..321
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34594
     Region          2..321
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(40..41,45,122,126,129,147,150..152,171..172,176,191,
                     214..215,235..239,259..262,309,311)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(134,228..229,242..247,254..261,264..265)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mkalcfeqfg npdvlqykki hdpiinsnei lvrtkaigln fadiyrrrgd yhlagnppyi
       61 lgyegagive qvgadvttin pgdriafadv pfanaelvav psekaillpd sisfetaasv
      121 llqgltahyl tkdsyqikqg dtalvhaaag gvgqlliqii kllggkvigl tsskekakva
      181 tlagadrvfl yteewhtkvl evtndagvnv vyesvgstle esfkvtkvgg tvvfygmagg
      241 npvpvdprml mdtsktltgg dlwnvlttfe erkqrstqlf dwittgkvni aspttfslqn
      301 garahelles rkstgkilli p
//
LOCUS       WP_284556991             303 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase 2 [Bacillus toyonensis].
ACCESSION   WP_284556991
VERSION     WP_284556991.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11650847
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..303
                     /product="DNA-3-methyladenine glycosylase 2"
                     /calculated_mol_wt=35085
     Region          16..133
                     /region_name="AlkA_N"
                     /note="AlkA N-terminal domain; cl05528"
                     /db_xref="CDD:446705"
     Region          83..300
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mtaeynnalt laapkefnfq enlrylsrsn necmfhiedn kiykvipveh vnplveisin
       61 tdeniqirfl gesynsekwv cdavanyvie wfdfttdlap fytlakhdpl lqgpiqdyyg
      121 lrtlgipdlf ealswgiigq qinlayaytl krrlveqfgs yvewndrkhr ifpspetian
      181 lhvedlkklk mttrkceyli giaklitegk lskesllqtq dvkiaekqlt aihgigpwta
      241 hyvlmrclrf psafpiddvg lhnaikfitg sqnkptknei kdfaanwtnw esyatfylwr
      301 vly
//
LOCUS       WP_284557196             433 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Bacillus toyonensis].
ACCESSION   WP_284557196
VERSION     WP_284557196.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..433
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47093
     Region          25..432
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(35..36,39..40,43,77,127..128,130..132,135,155,
                     158..159,162,264,267..268,271..273,276,303,307,356..357,
                     361,365,381,384..385,388..389,392)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mqpsapphle stetifsssi tklvvficwl ailadgydlg iygavlpkll ednswalspa
       61 qagtiasyal fgmfigaili gtitdligrk wtlicclalf sitmglaaia pspelfglsr
      121 figgiglggv iptasaltve ysskkrqsfi yalmftgypl givlgailsm fmledfgwri
      181 mfgigmipll lipfiilylp esiqfllsrn rqeevnkiln rfqiefhvkd eiseapsniq
      241 kkngfltlfs keyikatllf wityimgmfl iyglntwlpq mmrqagyplg sslsfllmln
      301 itaaigalfa gaiadrigtk ivisisylma aiciglltik psvtiiylli glagigsvgi
      361 tqilnayvtq yfpshirats lgwglglgrv gaiagpilvg iimtmqydla wnfylfsfag
      421 liaaisvffi ptk
//
LOCUS       WP_284557230             324 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Bacillus toyonensis].
ACCESSION   WP_284557230
VERSION     WP_284557230.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..324
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37362
     Region          13..323
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msclkrkkvi hlskakrlld ilifasakkt ftaqeiadef nisvrtvhry ildlgdmglp
       61 iyaaqgrngg ykvltnrvip pilfteeeav siffafqsls yyrdlpfnte insvthklys
      121 slqneakakv dkirsyiafw npkrtietpl lnevltaaie nknlhfqyes ksgiktkhvh
      181 pigvyahdgl wylpsydydr kkvllyridr ilsilsteen edtfmnleew fasnsnvvhs
      241 ptqlhvlltt egvrqcksvp yleefvevne dgtgyihsti dkgeihfitp lfyrlgkdar
      301 vleprelidg lrirakeilh myed
//
LOCUS       WP_284557447             226 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Bacillus toyonensis].
ACCESSION   WP_284557447
VERSION     WP_284557447.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..226
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25649
     Region          22..142
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mtkfnwhesa ekkwdssaey wkqnsqemwd sgsrstiipf feqyvekeaq vldvgcgdgy
       61 gtyklsrvgy kavgvdlsei miqkgkerge dsnlsfvkgd lsalpfeneq fkaimainsl
      121 ewtenplqal neikrvlkkg gyaciailgp takprensyp rlygkdvvcn tmmpwefeql
      181 akeqgfevvd gigvykrgvn ekmlgqlpte lqqsltflwv fmlknv
//
LOCUS       WP_284557454             320 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Bacillus toyonensis].
ACCESSION   WP_284557454
VERSION     WP_284557454.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..320
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35902
     Region          12..301
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 marldslhpi vekiinniek lmvgkrketi ltmtallaeg hvlledvpgv gktmlvrtls
       61 ksidadykri qftpdllpsd vtgvsiynpk elqfefkpgp imgnfvlade inrtspktqs
      121 allesmeegt itidgitrsl pkpffvmatq npveyegtyp lpeaqldrfl lkltmgyptp
      181 eeefeilnrm ektnplshlq aittieelly lqqsvrevsm dkaikhyivk lvnqtrsyss
      241 iqlgasprgs ialmkasqay afihgrnyvi pddvkflapy vlahrlilkm earfegitge
      301 qviakiiart tvptqrtknl
//
LOCUS       WP_284557466             533 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Bacillus toyonensis].
ACCESSION   WP_284557466
VERSION     WP_284557466.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..533
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58684
     Region          57..174
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mrlmrrcval liiffimaps istnvraevv kelgkgfpdt evftpgdwfl gqkptnyden
       61 kppilfvqgr ngnadswygk tvyhdindmy dyalkagyqt vfiqlydaag kgsasqwdng
      121 kllaqkleei ynhfgkkvti vahskggidt qvalvgygan rfvgnvitla tphhgsnlad
      181 lsyswwagwl asilgqkddg tyalqigema kfrstidnnp avklnryyta tgtswgpvfs
      241 alsmgglyls sygsndglvn ewsaklpygt hlftdskfdh dnirkgsavf ariepylrta
      301 nvgvpplvap snsseenieq lnttsnqnil ggelpqsqwi eqavavdkka egmvsvltaa
      361 sdveiqlisp kgkvytnkds tittgegesf fngatistfk fdkmdvgewr vkmmakqskd
      421 aylivsdhks gapfvlqmpt kvkinkseyk lkkspaapem kgnlsitvrv vnkegklvse
      481 fnelqnvntn tftgalkdik qpgvynvtmd ikginkegkp ynrtivksvy vek
//
LOCUS       WP_284557475             262 aa            linear   BCT 25-DEC-2024
DEFINITION  dimethyl sulfoxide reductase anchor subunit family protein
            [Enterobacter cloacae].
ACCESSION   WP_284557475
VERSION     WP_284557475.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..262
                     /product="dimethyl sulfoxide reductase anchor subunit
                     family protein"
                     /calculated_mol_wt=27789
     Region          1..259
                     /region_name="DmsC"
                     /note="DMSO reductase anchor subunit DmsC [Energy
                     production and conversion]; COG3302"
                     /db_xref="CDD:442531"
ORIGIN      
        1 mhelpllift lflqgsvgvt lwlalgdaqa sprnallpaa gafvlaclgl lastlhmgyp
       61 lnalnalrhv ssswlsreiv faslylaalg latllmfakk pgwkpllava glvglvdvfc
      121 maqiyihtsv vtwqhintlv lfigsvgiig sacvavgaps rinlraavvi itllvlvrlv
      181 mqpvwladit amdntvvtfp haplrmleql rtmhllswcv svagmlcfaa gglkaargpv
      241 llgsallivg elmlrfvffs ig
//
LOCUS       WP_284557497             436 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Bacillus toyonensis].
ACCESSION   WP_284557497
VERSION     WP_284557497.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..436
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47780
     Region          1..425
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mkkfdvaivg gglagltasi ylakagkkvi vlekssrfgg rgmtinkngi cmnlgahaly
       61 rggaafltfn elgmnlpggi pttkahgiwk gdiftiptdf rsilstplls wsakvqfsrl
      121 mirlgnldvg evpkmsltaw aeneikdpmv rnifyalcrt ttytfaptiq lassvlkqtq
      181 lsmkegvlyv dggwetiitk lrdiannvgv qflakkhvle iehdedkqri hcfddevfev
      241 gtvivttppk eackiikgte gtslhrwseq svpvtvaald iglrqlpnpt hqfalgldqp
      301 ifftnqsraa klsedgsiav slikyhnpal emnhihedke qlesamellh pnwkrevvaq
      361 qylpkitvay dfphiervet pgpnipempg vyvagdwtgq delladaava sgkraalhil
      421 kqlesegvhh gngavi
//
LOCUS       WP_284557736             107 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Enterobacter
            cloacae].
ACCESSION   WP_284557736
VERSION     WP_284557736.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..107
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12135
     Region          1..91
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 miavifeaka apahqarylq latelkplla didgfidier fqslttdgki lslswwrdee
       61 airnwkqnvf hqaaqaegre siftyyrirv aqvvreysae ngghadv
//
LOCUS       WP_284557809             727 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Enterobacter cloacae].
ACCESSION   WP_284557809
VERSION     WP_284557809.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 727)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 727)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..727
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=78695
     Region          68..727
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mnntrmhktl lalavgavth aalaaeakse dtmvvqsatg pdftpggdql vpafldgqva
       61 nggrlgmlgq qnamdvpfni isytsklved qqaktiadvv andagvqfvq gygnsaetfr
      121 irglkfdgdd mtfgglsgvl prqvvdaqmv drieifkgan slmngaassg vggminlepk
      181 hagdvpqakv gvdytsdsqi gttldagrrf gdndqfgarv nlvhregetg vpndrrrttl
      241 lstgldykgd nfrtsldlgy qkktfhgspt svnisavdfv peppkndrnf sqkwaysdie
      301 nefgmwrsey ditdnwtayt glgaqhahee giysapklvd ksgkatvsrl dtnrisdsvs
      361 gmagirghft tgfvshkvnv gysamtknek iawkmsatad npttniyhnt gvampdssnf
      421 ngsggkysdp ltsgrtrtqg wllsdtlgvl ddkllftaga rhqkvvirgy nkitgaenda
      481 dgfdgsrwmp tygvvykpwe eislyanhte alqpgktapn tttnyyqstg ivhskqnevg
      541 vkadfgrvgg slalfeikmp sailddsghy gldaeqrnrg velnvfgepm lgmrlnasat
      601 wlqaeltktk ngvnqgndai gvpnfyavlg aeydikpieg ltatarvnhs gtqyadlans
      661 kkldsyttld lgmryrfavn hnenqmtvra gidnvtneny wssvddsgty itqgeprtfk
      721 vsvgyef
//
LOCUS       WP_284557756             281 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family transcriptional regulator [Escherichia coli].
ACCESSION   WP_284557756
VERSION     WP_284557756.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Nazaret,F., Alloing,G., Mandon,K. and Frendo,P.
  TITLE     MarR Family Transcriptional Regulators and Their Roles in
            Plant-Interacting Bacteria
  JOURNAL   Microorganisms 11 (8), 1936 (2023)
   PUBMED   37630496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Will,W.R. and Fang,F.C.
  TITLE     The evolution of MarR family transcription factors as
            counter-silencers in regulatory networks
  JOURNAL   Curr Opin Microbiol 55, 1-8 (2020)
   PUBMED   32044654
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Grove,A.
  TITLE     Regulation of Metabolic Pathways by MarR Family Transcription
            Factors
  JOURNAL   Comput Struct Biotechnol J 15, 366-371 (2017)
   PUBMED   28694934
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10581578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..281
                     /product="MarR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30768
     Region          30..97
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
ORIGIN      
        1 mlakvtflsc ktmsdftfsg yelacfvths glsrsaghil sqcanlaatt seyfihkphr
       61 liaaetgysq stvvrafrea vnkgilsvei vigdhrerra nlyrftpsfl afaqqaknal
      121 iesklkissa atkvkavlak tlalfnflst ppcqndtpsp cqddvaiknk ksqvkktkrs
      181 vsggagttrl kkltswiaea kakadnlrls kkraqkhefk qkveaaarky aylknkrspd
      241 iggvsnfdnl phcmtvneal navlaknkdn eqwgipagfr g
//
LOCUS       WP_284557902             398 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Enterobacter cloacae].
ACCESSION   WP_284557902
VERSION     WP_284557902.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..398
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=44276
     Region          4..387
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 miktrhsslw rwicarilal aigsviviaa cmwlryavqn ywimgkmpaa vrqefltlsq
       61 npqsnparfh divdswwgls ystpsiasad wvtvallvlv mipfivvmgl kharplalqf
      121 sclrdaakdv adgqfgrqae lvkdapaemi sfaadfntmt gqlaryekel rashvamahe
      181 lrspltaaig rlqgmmdgvf datpeqlgmv mkqlqhlnrl tdelhllsla dagnlvledr
      241 pfrldeliqe radwitpqad ahnftitlrn prpcpfrgda frmgqvftil menslrygre
      301 gghlevtlhy tqgqytlefa ddgpgvskhf lpdmfkrfsr eeqsrarhsg gsglglsiaq
      361 aicqahggsi saslpetggl lvciqlpwra cdeensrs
//
LOCUS       WP_284558022             502 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Bacillus toyonensis].
ACCESSION   WP_284558022
VERSION     WP_284558022.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..502
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=56621
     Region          50..376
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mknrqkasii cksilclmic ifitnevwft nvvraesgtl tnrsienfkk kmdeqvpkwq
       61 enyevpgvai givhegriay tlnygyvdkk tkkavsddtl fqagsisksl tawgilhlvd
      121 egrlslddpv gkyltkwklp nsefnnnevt irrllshtag lsahkgylgv apgkhldsie
      181 eslsgkgwln elvevtnkpg setiysgggy tilqlvieev tgipfdryme eqimkplgik
      241 sssflqrpen hnlskaygyf geelpsyqft eqaaaglktn vtdmmtlila smdannkgng
      301 viksehveem qklvlgengl gifekklsnq wkllyhsgdn rgwhsfygfi pntkdglvil
      361 tngeggidlr qdiyhawiey etgklpesyf slaeqrknns itsivigatl glylllfvir
      421 lykgrrtfif kqekrsyigl vvrtflliit ailvfcaayl wrvfslnsgn tinfilimvw
      481 iitllisgff pkiksnkkqr mk
//
LOCUS       WP_284558425             974 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Bacillus toyonensis].
ACCESSION   WP_284558425
VERSION     WP_284558425.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 974)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 974)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 974)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 974)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 974)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 974)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 974)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18767243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..974
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..974
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=114040
     Region          1..967
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          1..196
                     /region_name="AAA_27"
                     /note="AAA domain; pfam13514"
                     /db_xref="CDD:433272"
ORIGIN      
        1 mrmeklhiyg ygklenvemd lsmltvlyge neagkstirs fmksilfgfp trgqrryepk
       61 eggkyggavt vqtekygrlk ierlpktaag evtvyfedgk tggeeilhdi lsgmneslfe
      121 svfsfdmhgl qnihqlgead ignylfsasa vgsdallqld kklekemdqr fkpsgrkpei
      181 nmslqemkkl eekmkewqgk igtyekqveq lkedeeklas vraekenaek rkqdyeilaa
      241 leplviekha hekvleyekr qfpvngtary eaikakmepl qlqvdslhkk ietvqseias
      301 iqideeflqk esyveelrmq hmsyenarqe mrdmtgnian ikeeiaeleq qigatfeket
      361 vlsfdmslat kelitqtvqk areletqkaq lddrfkvaqe qleeqeenir qikkqmlade
      421 eratlaekek sfqdaafigm gadrmkrkye ekvgvatqkk kqwqrvclll llintgvlft
      481 slfidnrqll fisvivfvgi vlalvlykdp ssglqeellt lqqsaggrqs eeamsvryql
      541 ekdeeirklf eresyklqqm eraydkvvss yeeweretfr ageqvdayks rymfpefyty
      601 ahilpafers ekmqqlyrev ekqstrkssl yemishfehk letvigsaey nklheaqsrm
      661 qnekekrqtc kqlkekltew qeeyefmqgq lkqllverds lwhiaeatde emfleagkla
      721 ekcedaekqv grllpqiell eqrltslsla ehyeaegyee klkremtvvr nclakekelt
      781 eriakhrmei enleegstyg dlmhewemkk aqvreqvkkw aayaaaktvl tktkqyyhev
      841 hlprilqkse eyfvyltggr yskifspsea epfiverndg irfyshelsq ataeqlylsl
      901 rfalaktfeh dypfiiddsf vhfdvvrtnr tielikeiak drqvifftch ahlltyftee
      961 riiklthkrk enel
//
LOCUS       WP_284558464             233 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Bacillus toyonensis].
ACCESSION   WP_284558464
VERSION     WP_284558464.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..233
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=27296
     Region          60..>115
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mndktwndyl awraqqglvg lsteeeynef mdsytkeete kltkqeanel eiifkdvlat
       61 pkeqatfdvm kdkltggfea tytelaelag vsertakrhi ealarkgylt atrtqkanry
      121 nwgvdmktke qiviypvaft qwdeffeevk erlglieidt rsiaihtkyd yvsadeqlrl
      181 qvnksiknfw ftgnelseea ykqfdrynyd lmltiynnfe eathkaieie sfk
//
LOCUS       WP_284558504             260 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Bacillus toyonensis].
ACCESSION   WP_284558504
VERSION     WP_284558504.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..260
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30957
     Region          1..260
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 miieqdydhf iasfkqqynm diasykqdrm rrridafisr kgfdnyanfl nhlradqnlf
       61 lsfidyitin vseffrnker wqtletkalp klleqnngkl kvwsaacaag eepytlslil
      121 skhlspfrye iqatdldfhi letakrgqyt erslkelpia lkerhftken dtyslhqnik
      181 qnvsfkqhdl lmqsfdtnyd liicrnvmiy fteearvkly ekfsrslrkg gvlfvgsteq
      241 iltperynlq rfdtffyeki
//
LOCUS       WP_284558505             575 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Escherichia coli].
ACCESSION   WP_284558505
VERSION     WP_284558505.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13939702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..575
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=63563
     Region          110..430
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
     Region          392..569
                     /region_name="DUF3520"
                     /note="Domain of unknown function (DUF3520); pfam12034"
                     /db_xref="CDD:432277"
ORIGIN      
        1 mrnkniimll msslilsgcg pqpenkesqq qqpstpteqq vlaaqqaaik eaeqsaaaak
       61 alaqqevqqy sdkqalqgrl qeaptfaraa kakathianp gtaryqqfdd npvkqvaqnp
      121 latfsldvdt gsyanvrrfl nqgllpppda vrveeivnyf psdwdikdkq sipaskpipf
      181 amryelapap wneqrtllkv dilakdrkse elpasnlvfl idtsgsmisd erlpliqssl
      241 kllvkelreq dniaivtyag dsrialpsis gshkaeinaa idsldaegst nggaglelay
      301 qqatkgfikg ginrillatd gdfnvgiddp ksiesmvkkq resgvtlstf gvgnsnynea
      361 mmvriadvgn gnysyidtls eaqkvlnsem rqmlitvakd vkaqiefnpa wvteyrqigy
      421 ekrqlrvehf nndnvdagdi gagkhitllf eltlngqkas idklryapdn klaksdktke
      481 lawlkirwky pqgkesqlve fplgptinap sedmrfraav aaygqklrgs eylnntfwqq
      541 ikqwaqqakg edpqgyraef irlieladgv tdisq
//
LOCUS       WP_284558543             253 aa            linear   BCT 25-DEC-2024
DEFINITION  DODA-type extradiol aromatic ring-opening family dioxygenase
            [Bacillus toyonensis].
ACCESSION   WP_284558543
VERSION     WP_284558543.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Vaillancourt,F.H., Bolin,J.T. and Eltis,L.D.
  TITLE     The ins and outs of ring-cleaving dioxygenases
  JOURNAL   Crit Rev Biochem Mol Biol 41 (4), 241-267 (2006)
   PUBMED   16849108
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Siegbahn,P.E. and Haeffner,F.
  TITLE     Mechanism for catechol ring-cleavage by non-heme iron extradiol
            dioxygenases
  JOURNAL   J Am Chem Soc 126 (29), 8919-8932 (2004)
   PUBMED   15264822
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..253
                     /product="DODA-type extradiol aromatic ring-opening family
                     dioxygenase"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016701 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28517
     Region          3..253
                     /region_name="45_DOPA_Dioxygenase"
                     /note="The Class III extradiol dioxygenase, 4,5-DOPA
                     Dioxygenase, catalyzes the incorporation of both atoms of
                     molecular oxygen into 4,5-dihydroxy-phenylalanine;
                     cd07363"
                     /db_xref="CDD:153375"
     Site            order(9..11,43,109,165,219,245..246)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:153375"
     Site            order(9,43,219)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:153375"
ORIGIN      
        1 mmpslflahg spmlaiqdtd ytrflktlge tykpkaivif tahwesevlt isssdnayet
       61 iydfggfppe lyeikyrakg sssiasmlet kfknkgisvh hnmtrgldhg swtllhrmyp
      121 eanipvvqis vnpflpakeq feigealkgl gqedilvigs gvtvhnlral kwnqttpekw
      181 aiefddwimk hmqnndkdal fnweknapha qlavpraehf vplfiamgsg esdgkvihrs
      241 yelgtlsylc lqf
//
LOCUS       WP_284558604             436 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Bacillus toyonensis].
ACCESSION   WP_284558604
VERSION     WP_284558604.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..436
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47988
     Region          1..425
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mkkfdvaivg gglagltasi ylakagkkvi vleksrrfgg rgmtinkngi cmnlgahaly
       61 rggaafltfn elgmnlpggi pttkahgiwk gdiftiptdf rsilstplls wsakvqfsrl
      121 mirlgnldvg evpkmsltaw aeneikdpmv rnifyalcrt ttytfaptiq lassvlkqiq
      181 lsmkegvlyv dggwetiitk lrdiannvgv qflakkhvle iehyedkqri hcfddevfev
      241 gtvivttppk eackiikgae gtslhrwseq svpvtvaald iglrrlpnpt hqfvigldqp
      301 ifftnqsraa klsedgsiav slikyhntvl emnhihedke qlestmellh pnwkrevvaq
      361 qylpkitvay dfphiervet pgpnipempg vyvagdwtgq delladaavt sgkraalhil
      421 kqlesegvph gngavi
//
LOCUS       WP_284558770             388 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Bacillus toyonensis].
ACCESSION   WP_284558770
VERSION     WP_284558770.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..388
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42378
     Region          39..386
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkkhcqitst glvllmtgss llyttpssiv kaesdqnvss slqtntqrdr tsvkkamrdt
       61 lqlgypgila kvskdrktws yaagvadlrt kkpmkadyrf rigsvtktfi atvllqlage
      121 nrlnlddsie kwlpgviqgn gydgnqitir qilnhtsgia eylkskdydf mdtkklytae
      181 elvkmgislp pdfapgkgws ysntgyvvlg iliekvtgns yaeevenrii eplelsntfl
      241 pgnstvipgt khargyeryd gesepkdvty sypgnsdgdm istaddlnkf fsyllsgkll
      301 keqqlkqmlt tvptgivgmd gyglgiyenk lsngvsiwgh sggspgfstf aggtlggkhi
      361 lainlnghki sysnsdpfkn illaefsk
//
LOCUS       WP_284558814             468 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Bacillus toyonensis].
ACCESSION   WP_284558814
VERSION     WP_284558814.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..468
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52236
     Region          95..447
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mleiifvavl llssitpifi ergltkkniv illinyvflf aiiiviganw rmipsyfllf
       61 vltlqvflkp kttavskklv mkvlkglgii vtaiamftlp llfpiitlpe ptgkytvgtk
      121 afhlidtnrk ettvpnnhgn relmiqvyyp aekgsgnpsa yfeniselae qlavtngapy
      181 ivtthlgltk thsyqdakpl qdkekfplll fghgmglygq qntfqleela sqgyviiain
      241 ftgyaattif pngnrvdsip ieytptalnt ivqkweqdtt fvlnkviegn fdesfktiad
      301 linydkigmf ghsfggatsa qmlvkdtrik aaidmdggly gdpmpkdgpq kpfmlmnaea
      361 tihymkeaen qkttgiqnel leisylrnkt iekpgmytvv ipkanhtsft dlaafspiin
      421 epdedvaany tlinklvtsf fdqnlkgink nhleeikkqy pelhlikh
//
LOCUS       WP_284558867             345 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Bacillus toyonensis].
ACCESSION   WP_284558867
VERSION     WP_284558867.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..345
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38563
     Region          34..344
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mnnsynekth tsikqllknf sskapgftyi ssfdsgvtyk gavglasiek nlpmttktvf
       61 niasvskqft afsillleqe rklslddsil kfvpsigaya epvtlkhlih htgglvdyme
      121 laeaanikyt dtltvkesle qlkshqmarf pvgtkfeysn tgyfllslvv ekvsgkslrq
      181 fakerifdpl hmkdttivdc ypttisiang ysrneqgtyk iyespwehtg dgavhatved
      241 lvkwgenltk gtvggkdlvk rmseigpkis ptgetiidne dyafglrlae gfnckylehs
      301 gswagyrshf mrfpevylsv vvlsnydefd skkyaneiae ivlek
//
LOCUS       WP_284558987             687 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Bacillus thuringiensis].
ACCESSION   WP_284558987
VERSION     WP_284558987.1
KEYWORDS    RefSeq.
SOURCE      Bacillus thuringiensis
  ORGANISM  Bacillus thuringiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Bacillus thuringiensis"
                     /db_xref="taxon:1428"
     Protein         1..687
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=59366
     Region          63..>661
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 msswlnntng ycscnnqngv hvdsccfscd gtvpklgptg ptgstgstgs tgstgatgst
       61 gptgatgstg ptgstgatgs tgstgstgat gptgatgitg atgptgatgi tgvtgptgat
      121 gstgatgptg ptgatgstgs tgptgatgst gvtgptgstg atgptgatgs tgatgptgat
      181 gstgatgstg stgstgstgp tgstgatgpt gstgpigatg ptgstgptgs tgptgatgpt
      241 gstgatgstg stgatgptga tgstgstgpt gatgstgvtg ptgstgstga tgptgstgst
      301 gptgatgatg atgptgstgp tgstgpigat gptgstgptg stgptgatgp tgatgstgst
      361 gatgstgstg stgptgstgp igatgstgpt gstgatgptg stgstgptga tgstgatgpt
      421 gatgptgatg itgatgitga tgitgstgit gstgstgptg atgstgptgs tgatgstgpt
      481 gstgstgptg atgitgatgi tgstgitgst gstgptgatg stgptgstga tgstgitgst
      541 gstgptgatg tsitatyafa nntsgtaisv vlggtnvplp nnqnigpgit vsggntvftv
      601 anagnyyisy tinitasllv ssritingga lagtinapav attsfsatii ttlaagdais
      661 lqlfgllava tlstttpgav ltiirls
//
LOCUS       WP_284559011             317 aa            linear   BCT 25-DEC-2024
DEFINITION  TRM11 family SAM-dependent methyltransferase [Bacillus
            thuringiensis].
ACCESSION   WP_284559011
VERSION     WP_284559011.1
KEYWORDS    RefSeq.
SOURCE      Bacillus thuringiensis
  ORGANISM  Bacillus thuringiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Kozbial,P.Z. and Mushegian,A.R.
  TITLE     Natural history of S-adenosylmethionine-binding proteins
  JOURNAL   BMC Struct Biol 5, 19 (2005)
   PUBMED   16225687
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437146
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Bacillus thuringiensis"
                     /db_xref="taxon:1428"
     Protein         1..317
                     /product="TRM11 family SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=35712
     Region          159..316
                     /region_name="Trm11"
                     /note="tRNA G10 N-methylase Trm11 [Translation, ribosomal
                     structure and biogenesis]; COG1041"
                     /db_xref="CDD:440663"
ORIGIN      
        1 mnnhsktpac iytyafreee ralcylemrs ffgmeshvni lksdvkidps rsafikerie
       61 vmyegddles ilkqveqidl agatfkvifv kindlvgenk ieygerrlie rdlgmhiege
      121 advrnpervf givplggrwy fgyyvesepv wyhhikkphs ystslstrva rsvaniavpn
      181 pegvraidpc cgigtvvvea lsmginivgr dinplvvlgt rkniahfgfe gtvtkgpiek
      241 itenydvaii dmpydlftha tpedqlsils sarriakkvv vvtmetmddm iheagfeitd
      301 rcitrkgsft rqilvce
//
LOCUS       WP_284559040             475 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Bacillus
            thuringiensis].
ACCESSION   WP_284559040
VERSION     WP_284559040.1
KEYWORDS    RefSeq.
SOURCE      Bacillus thuringiensis
  ORGANISM  Bacillus thuringiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Bacillus thuringiensis"
                     /db_xref="taxon:1428"
     Protein         1..475
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52875
     Region          27..365
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkkiivfvlt ifilfsgfat qsyalsdsqs aaiqalldda crisgvpgms isiladdevf
       61 yfssgyadre kglsasentl yelasvskaf tgmsimllee qgllsmtdpv qkylpwftlk
      121 yqgkpvdmqs ltlnnflhht sgltnirhlq nipqgntpdm lqktvemlvd aelafppgeq
      181 ynygtvnydv lglvieivsr qsyedfmkeq vfqplglhqt yvykedaqat gqlaqgyrss
      241 ffmttpfkap dyagnkpagy iisntkdmar wmgiqmgivq dipeifhtvi ekshrgdmsv
      301 savngmyyaa gwsvnaeqti iehtggnpnf rtevvilpne rtavsllsng tntntnmvlk
      361 vkdilegnlt qsyeisgtql ldiilssiti ifcllavllf llglrrrrtn erqpmtkkri
      421 tvtvifliat ialgilccaf dwstilmwqt ysvltaliss alltasitwf vythr
//
LOCUS       WP_284559110             315 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Bacillus
            thuringiensis].
ACCESSION   WP_284559110
VERSION     WP_284559110.1
KEYWORDS    RefSeq.
SOURCE      Bacillus thuringiensis
  ORGANISM  Bacillus thuringiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 315)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Bacillus thuringiensis"
                     /db_xref="taxon:1428"
     Protein         1..315
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=36580
     Region          9..304
                     /region_name="PobA"
                     /note="Chlorophyllide a oxygenase/letal leaf spot protein
                     [Coenzyme transport and metabolism]; COG5749"
                     /db_xref="CDD:444459"
ORIGIN      
        1 mtlninrvfp rnwyavsyak dikkipvkkr fagkdfvlyr dekgevqals pycphrgadl
       61 slgqvvngkl vcpyhgwefd scgtcvrips qpnkpipkfa htlsypvkek igliwiypdn
      121 eetppewqtf hvmentpfkl sffhatwnah ltrsiesvld iahlayvhkk tigrktkaes
      181 tnykpegtld qfifsngday leykfphqwm lhsgkqenes fiqyitftpi deeetlimgy
      241 tgrtflkyfp lldqilakfs lrvlkedqii vesqhprpip ealkmeahvh admaqvqfrk
      301 rwfqflqngs cfsld
//
LOCUS       WP_284559231             496 aa            linear   BCT 25-DEC-2024
DEFINITION  RecQ family ATP-dependent DNA helicase [Bacillus halotolerans].
ACCESSION   WP_284559231
VERSION     WP_284559231.1
KEYWORDS    RefSeq.
SOURCE      Bacillus halotolerans
  ORGANISM  Bacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Larsen,N.B. and Hickson,I.D.
  TITLE     RecQ Helicases: Conserved Guardians of Genomic Integrity
  JOURNAL   Adv Exp Med Biol 767, 161-184 (2013)
   PUBMED   23161011
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Rezazadeh,S.
  TITLE     RecQ helicases; at the crossroad of genome replication, repair, and
            recombination
  JOURNAL   Mol Biol Rep 39 (4), 4527-4543 (2012)
   PUBMED   21947842
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 496)
  AUTHORS   Bernstein,K.A., Gangloff,S. and Rothstein,R.
  TITLE     The RecQ DNA helicases in DNA repair
  JOURNAL   Annu Rev Genet 44, 393-417 (2010)
   PUBMED   21047263
REFERENCE   5  (residues 1 to 496)
  AUTHORS   Chu,W.K. and Hickson,I.D.
  TITLE     RecQ helicases: multifunctional genome caretakers
  JOURNAL   Nat Rev Cancer 9 (9), 644-654 (2009)
   PUBMED   19657341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Bacillus halotolerans"
                     /db_xref="taxon:260554"
     Protein         1..496
                     /product="RecQ family ATP-dependent DNA helicase"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0043138 - 3'-5' DNA helicase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=56597
     Region          1..475
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
ORIGIN      
        1 mtklqqalyq ffgfhsfkkg qediirsvls gkdtiamlpt gggkslcyql pgymldgmil
       61 ivspllslme dqvqqlkarg ekraaalnsm lgrqerhfvl ehihrykfly lspealqssy
      121 vleklksvpi slfvideahc isewghdfrp dysklgqlrk klghppvlal tatatkdtlh
      181 dvmnlldlqh aeqhlnsvnr pnialkvent adtaekidrv vqlvenlqgp givycptrkw
      241 aeelaeeikn ktssrvdyyh ggmdsgdrml iqqqfinnql dvicctnafg mgidksdiky
      301 vihfylpqta eafmqeigra grdgkpsvsi llrapgdfel qeqiiqmesl tdgeianvir
      361 vleeteerde rklrelfmqy gitetqsrmi ihqfmqgkts idlikreity rmelkldkmr
      421 hvsallhrdg clrqsllayf detyepdkgs mpccshcgid lslyeqkeer vqialldgwr
      481 selhrifsle tvgepn
//
LOCUS       WP_284559451             248 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Bacillus halotolerans].
ACCESSION   WP_284559451
VERSION     WP_284559451.1
KEYWORDS    RefSeq.
SOURCE      Bacillus halotolerans
  ORGANISM  Bacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Bacillus halotolerans"
                     /db_xref="taxon:260554"
     Protein         1..248
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26442
     Region          1..243
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mipilfvlgl ilgsfyytvg criplhisii sprsacsfcr rtltptelip vlsfilqkgn
       61 ckscgqklsl mypaaelsta slfaaagfrf glswelival vflslliivs vtdihfmlip
      121 nrillfflpf laagriispl lswyesfiga aagflllafi avithggigg gdvklfavig
      181 lvlgvkmlaa afffsvfiga lygaaavlfg rlarkqpipf apaiaagsif aylygdsiis
      241 fyvktalg
//
LOCUS       WP_284559672             554 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Bacillus halotolerans].
ACCESSION   WP_284559672
VERSION     WP_284559672.1
KEYWORDS    RefSeq.
SOURCE      Bacillus halotolerans
  ORGANISM  Bacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 554)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Bacillus halotolerans"
                     /db_xref="taxon:260554"
     Protein         1..554
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=63776
     Region          7..468
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(21,23,25,29)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(60,63,100,103,144,163,167,199,256,411)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(199,256,326)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          476..550
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; pfam16657"
                     /db_xref="CDD:435493"
ORIGIN      
        1 mkkawwkeav iyqiyprsfk dsnsdgigdi qgirsklpyi kelgadviwi cplydspnad
       61 ngydirdykn ilsdfgtmad fdqllhdihe lgmklimdlv vnhtsdehpw fiesraslqs
      121 qkrdwyiwkd gkdgkepnnw esifggsawq ydqqtsqyyl hlfdkkqpdl nwenqevrna
      181 vydmvnwwld kgidgfrvda ishikkkegl pdllnpkgls yvpsfpyhmn aegildflte
      241 lkentfsryp imtvgeangv aakeaaewag eesgifsmif qfehlglwdi einesidiaa
      301 fkriltewqn slegigwnal fmenhdqprs vsvwgndgns lkesakalav vyflmkgtpf
      361 iyqgqeigmt nvafpsiedy ddvamkrlyd ietakgashe evmkivwkkg rdnsrtpmqw
      421 nasphagfsd akpwigvndn ytwlnaeaqi ndntsvyhfy ksliklrqty dvfiygqyel
      481 ilpedqqifa ylrknesqta liaanltgap afcrypalpl ssdklllsnm etephkhtts
      541 lllkpyearv ylwq
//
LOCUS       WP_284559684            2379 aa            linear   BCT 25-DEC-2024
DEFINITION  amino acid adenylation domain-containing protein [Bacillus
            halotolerans].
ACCESSION   WP_284559684
VERSION     WP_284559684.1
KEYWORDS    RefSeq.
SOURCE      Bacillus halotolerans
  ORGANISM  Bacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 2379)
  AUTHORS   Konz,D. and Marahiel,M.A.
  TITLE     How do peptide synthetases generate structural diversity?
  JOURNAL   Chem Biol 6 (2), R39-R48 (1999)
   PUBMED   10021423
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01733.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2379
                     /organism="Bacillus halotolerans"
                     /db_xref="taxon:260554"
     Protein         1..2379
                     /product="amino acid adenylation domain-containing
                     protein"
                     /calculated_mol_wt=263670
     Region          11..>2105
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
     Region          2131..>2285
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mpdtkdlqys ltgaqsgiwf aqqldpdnpi yntaeyiein gpidislfee alrhvikeae
       61 slhvrfgedn dgpwqmmnps pdvqlqvidv ssepnpekta lnwmeadlak pvdlqhdplf
      121 realfkagpq rffwyqrihh iaidgfgfsl iaqrvahayt alaggrsadd rsfgslqdil
      181 aedadyrssd tyeedrqfwl nrfadrpevv slaeraprts ksflrqtsyl ppsdvnalke
      241 aaryyagswh evviavsaay vhrmtgsedv vlglpmmgrm gsaslnvpam vmnllplrls
      301 vspsmsfsel vlqisreirs irqhhkyrhe elrrdlklig enhrlfgpqi nlmpfdygld
      361 fagargtthn lsagpvddls invydrtdgs glridvdanp evysdseika hqqrilqllq
      421 tasagedmli gqmefllpae karvisewne takserllsl pdmfqeqadr sperialicd
      481 hsqlsyqeln eqanrlahll iekglgpeqf valalprsse mvaamlavlk tgaaylpldp
      541 efpadrisym lkdakpscii tteeiadtlp ddltapqlvl dlpvtkeivk rysadnpnvh
      601 vslahpayii ytsgstgrpk gvvvtmksls nfllsmqetf slneqdrlla vttvafdisa
      661 lelflplisg asivvaqket trepqalakm ieyfditimq atptlwhalv tnepeklrel
      721 rvlvggealp sgllealhal dcpvtnlygp tettiwsaaa flekgvqgvp pigkpiwntq
      781 vyvldnslqp vppgivgely iagtglargy lgrpdltaer fvadpygppg trmyrtgdqa
      841 rwradgsldy igradhqiki rgfrielgei davlakypqi eqaavvvred hpgdrrlvay
      901 lvvssaldia elrryvgvsl pdymvpaafv eidelpltpn gkldrkalpa pdfsasvtdr
      961 gprtpqeeil cdlfaevlgl arvgiddsff elgghsllaa rlmsriretm gaelgivklf
     1021 deptvaglaa hldqaqsvrp alqraerpen iplsfaqrrl wflhclegps ptynipvavr
     1081 lsgelnqeal qaalydlisr heslrtifpe sqgtsyqril dadqarpdly vtemkkeels
     1141 erladaarys fdlaaepsfr aelfvigpde yvllllvhhi vgdgwsltpl trdlaaayaa
     1201 rchgrapewt plavqyadya lwqqsllgse hdpdsliagq lafwkerlkn lpdqlelptd
     1261 ysrpaepshq gdtihfhids klhsrllela ranrvslfmv lqsglaallt rlgagtdipi
     1321 gspiagrndd alsdlvglfi ntlvlrtdts gdpsfrelld rvrevnlaay enqdlpferl
     1381 vevlnparsr athplfqvml afqntpdael slpgtesslr ihsvgsakfd ltleisesrl
     1441 ddgtpngleg lleystdlfk retvqaladr llrlleaaea dpdqeigrld ilapeersit
     1501 vtdwqsvsek ipqaclpdlf ekqaalspds iavvyedkam symelneran rlarlliskg
     1561 vgpeqfvala lprsldmtvs llavlkagaa ylpldpdypa driafmlsda rpafiitssq
     1621 aenqippaen vqnivlddpe lreklktysp lnpdntdrir plspystayv iytsgstgvp
     1681 kgvmiphqnv trlfgatdhw fhfgsddvwt mfhsyafdfs vweiwgpllh ggrlvivphd
     1741 isrspeaflr llvkegvtvl nqtpsafyqf mqaereqpdl gqalslryvv fggealelsr
     1801 ledwyhrhpe qapklinmyg itettvhvsy ieldrniaal ransligcgi pdlgvyvlde
     1861 rlqpvppgva gelyvsgagl argylgrpgl taerfiadpf gppgtrmyrt gdvarrradg
     1921 sldyvgradh qvkirgfrie lgeieaalvq hsqledaavi vredqpgdkr laayvipsse
     1981 etfdtaelrr yaaerlpdym vpsafvtmke lpltpngkld rkalpapdfa aavtgrgprt
     2041 pqeeilcdlf mevlhlprvg iddrffdlgg hsllavqlms rirealgvel signlfeapt
     2101 vaglaerlem gssqsaldvl lplrtsgdrl plfcvhpagg lswcyaglmt slgtdypiyg
     2161 lqargigqqe alpktlddma adyieqirti qpkgpyhllg wslggnvvqa matqlqkqge
     2221 dvsllvmlda ypnhflpike apddeealia llalggydpd slgdkpldfe taieilrrdg
     2281 salasldesv ilnlkntyvn svgilgsyap ktfrgnvlff rstiipewfd piepdswkpy
     2341 idgqieqidi dcrhkdlcqp eplavigrvl aakleemnq
//
LOCUS       WP_284559714             372 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Bacillus halotolerans].
ACCESSION   WP_284559714
VERSION     WP_284559714.1
KEYWORDS    RefSeq.
SOURCE      Bacillus halotolerans
  ORGANISM  Bacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Bacillus halotolerans"
                     /db_xref="taxon:260554"
     Protein         1..372
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39635
     Region          1..368
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mksyiivgag ilgastayhl aksgarvtvi drnepgqatd aaagivcpwl sqrrnqdwyq
       61 lakggaryyn dlikqleedg etdtgykrvg aisihtdsvk ldkmeerayk rrehapeigd
      121 itrlsasetk klfpiladgy esvhisgaar vngralcrsl lsaaekhgav ivkgnasllf
      181 engrvtgvqt dkqqfeadnv ivtggawane lmkplgihfq vsfqkaqimh feipgadtgs
      241 wpvvmppndq yilsfddgri vagathenea dlkdlrvtag gqhevlskal aaapvladst
      301 vietrvgfrp ftpgflpvvg avpnvqglya anglgasglt mgpflgsela klvlgkptei
      361 dlspydlaga la
//
LOCUS       WP_284559912             389 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Bacillus
            halotolerans].
ACCESSION   WP_284559912
VERSION     WP_284559912.1
KEYWORDS    RefSeq.
SOURCE      Bacillus halotolerans
  ORGANISM  Bacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Bacillus halotolerans"
                     /db_xref="taxon:260554"
     Protein         1..389
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43100
     Region          8..384
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mvqkrnhflp yslpligkee iqevtetles gwiskgpkvq qfekefaafv gakhavalns
       61 ctaalflalk akgvgpgdev itspltfsst antiihtgat pvfadidekt lnidpkklet
      121 avtprtkavv pvhfggqscd mdailaiaqk hglfvledaa havyttykqr migsigdata
      181 fsfyatknla tgeggmlttd deeladkirv lslhgmskga wnryssngsw yyevespgyk
      241 mnmfdlqaal glhqlkrldd mqkrreeiag qyqaafqqip glitpfvhne grhawhlyvl
      301 qvdekqagvt rdemitalkd eynigtsvhf ipvhihpyyq kefgfketdy plamkyykrt
      361 lslplypsms dedvndviea vrdiakgag
//
LOCUS       WP_284560118             293 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Bacillus halotolerans].
ACCESSION   WP_284560118
VERSION     WP_284560118.1
KEYWORDS    RefSeq.
SOURCE      Bacillus halotolerans
  ORGANISM  Bacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Bacillus halotolerans"
                     /db_xref="taxon:260554"
     Protein         1..293
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33589
     Region          13..>104
                     /region_name="PRK15121"
                     /note="MDR efflux pump AcrAB transcriptional activator
                     RobA"
                     /db_xref="CDD:185076"
ORIGIN      
        1 myyekavqqt idwleshlhe pisgkdivsv sgfskfhfhr ifqkevgmsv asyirlrrla
       61 naaaallytd vriidialhy qfesqeaftr afkkmyhmpp gayrtfmkrf takkeeswme
      121 kkmkgwvlsg shpfqfeigv drenvhqgka sgylkstmvh diaefatmmq qfkadrylgk
      181 rlrlssfikt kgvkhfaslw mrvdsaaedv lqfdnmsnrp itgttnwnhy avvldvpens
      241 avisfgvqls gpgqvwmdhv vfeevdesvp stnlempgel ldepvnlsfe eel
//
LOCUS       WP_284560132             244 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Bacillus halotolerans].
ACCESSION   WP_284560132
VERSION     WP_284560132.1
KEYWORDS    RefSeq.
SOURCE      Bacillus halotolerans
  ORGANISM  Bacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10562492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Bacillus halotolerans"
                     /db_xref="taxon:260554"
     Protein         1..244
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=27784
     Region          24..222
                     /region_name="vWA-TerF-like"
                     /note="vWA found in TerF C terminus; pfam10138"
                     /db_xref="CDD:401947"
     Site            order(32,105,136)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238119"
ORIGIN      
        1 matidlqkks vkivlekkql tkvtarvglv lditgsmrtl ykngtvqkvv erilavadqf
       61 ddnglldvwv ydnefsrlkp vneidfsgyv dreilnnell hkfgrndepp vikdvlhkyv
      121 veepssypaf ivfindggck ksikpiieaa sdkpvfwqfv gigngnfdfl nkldtlegrv
      181 vdnanflhie edierisdde lydalltefp fwlqevkekg ilieqepeaa kpekkgffsr
      241 lfsk
//
LOCUS       WP_284560216             368 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Bacillus halotolerans].
ACCESSION   WP_284560216
VERSION     WP_284560216.1
KEYWORDS    RefSeq.
SOURCE      Bacillus halotolerans
  ORGANISM  Bacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Bacillus halotolerans"
                     /db_xref="taxon:260554"
     Protein         1..368
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43539
     Region          61..366
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msirktkdgr yridvslgfd pvtgkrkrkt mtlktkkhae emyhaikkah sdglltshke
       61 vsfstlvsly leqcklhhkp nyyniekyti ekhiiphfen civkkvthne vqdfqkslid
      121 kglenktinn imiilskifd igivedvlik npcakvknls vvkkqmkfwt pdqfkefisl
      181 ikkdefifkv fyttdyltgm rlgeilalqw kdldkfrrei nvykaltyin qeyiitspkt
      241 knsirrisin sklitlldew rrqqkeifde lrihqseety mfqykdrppt kdifsrkikq
      301 icqrgnvdpi rfhdlrhshv allihqgedy lvikerlghs svsftmntyg hlfpnkqket
      361 adrlddll
//
LOCUS       WP_284560280             322 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Bacillus halotolerans].
ACCESSION   WP_284560280
VERSION     WP_284560280.1
KEYWORDS    RefSeq.
SOURCE      Bacillus halotolerans
  ORGANISM  Bacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Bacillus halotolerans"
                     /db_xref="taxon:260554"
     Protein         1..322
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34345
     Region          6..307
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(41,257,260)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(197,228,255,258..259,262)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mrsqsvvcig ellidffctd vdvdlkkgrq flksaggapa nvsaaiaklg gdaafagkvg
       61 kdpfgyflkq tldavhvdts mlvmdekapt tlafvslknn gerdfvfnrg adalftiedv
      121 dqdkmnqaki lhfgsatall sdpfctaylr lmtiakdkgq flsfdpnyrg dlwkgrvsef
      181 vsaakraial sdfvkvsdee leiitgakdh eegvnilhgi gakmvavtlg kngtllsngk
      241 eheiipsipv tsidstgagd afvgaalfkl agtdkiqsae tefeklrdiv sfankvgalv
      301 ctkigaidal prmeeieasl sl
//
LOCUS       WP_284560320             318 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Bacillus halotolerans].
ACCESSION   WP_284560320
VERSION     WP_284560320.1
KEYWORDS    RefSeq.
SOURCE      Bacillus halotolerans
  ORGANISM  Bacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 318)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Bacillus halotolerans"
                     /db_xref="taxon:260554"
     Protein         1..318
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36276
     Region          6..318
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 metvpkkgna pvlaagkgis wmtalkrdkw lylllipgll yflifkylpm wgvliafkdy
       61 spylgfwkse wvgldyfkdf fmnpdffrll rntlmlasld llfafpapli lalllnelrk
      121 avykrciqtl iyvphfvswt ivvsitfvff tvdtgvinkm vmsltgnqis flsdadwfrp
      181 mivmqsiwke tgwgtilfla alatvdqeqy eaaimdgagr frrmwhitlp airstiivll
      241 ilrigsflni gfeqvylmtn slnrsvadif dtyvymmgit qgaysystav glfksvvgii
      301 lifganyiak kfdqeglf
//
LOCUS       WP_284560344             471 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Bacillus
            halotolerans].
ACCESSION   WP_284560344
VERSION     WP_284560344.1
KEYWORDS    RefSeq.
SOURCE      Bacillus halotolerans
  ORGANISM  Bacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Bacillus halotolerans"
                     /db_xref="taxon:260554"
     Protein         1..471
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=50549
     Region          1..444
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 meqllewver isdwlwgppl iilltgtgly ltillkffqf ryplyilkqt igsvgkkpkg
       61 egtvtplqal tsalsstiga anivgvpaai mfggpgavfw mwlvalfama ikfsesvlav
      121 hyrekneqge fvggpmyyit kglrmkwlgv ffsvalivel ipsimvqgns vsvslaetfs
      181 fnkiyagigi afliglvvig gvkrigkvte fvvplmagay agagllivlm nlssvpaffs
      241 lifsnaftss saaggfagaa laetirwgfa rglysneagm gtapiahaaa mtdhpvrqgf
      301 wsvigividt liictttafv vlasgvwtgk nassdpaalt taafhhyfgs gggyfvsisl
      361 vffvvstimv vifygvkqae flfgrlsghv ikfvylaaii igaaggakai wgfldlalvf
      421 ilvpnviall llskkvkaly tefftseqyy lkdrrktkqs avyqtkeaen s
//
LOCUS       WP_284560575             704 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Bacillus
            halotolerans].
ACCESSION   WP_284560575
VERSION     WP_284560575.1
KEYWORDS    RefSeq.
SOURCE      Bacillus halotolerans
  ORGANISM  Bacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 704)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 704)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 704)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 704)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..704
                     /organism="Bacillus halotolerans"
                     /db_xref="taxon:260554"
     Protein         1..704
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=79205
     Region          9..668
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mteigrepkk krkgnrairm nlyflavfvl ftalifklgv vqivegeqhe enaekanakt
       61 ayypaprgkm ydrnekvavd nqsvpeivyv stsstktedk iktakrlaal ididteflkd
      121 rdlrdywlas hpkkalgllk esesnlkgtq ayklqvervp aeelkaiqrd deemqtaaiy
      181 trfssgnaye pqivkamdpn dsngngkngs lldekknssq rpkndltyde isivsehlee
      241 lpgidvvndw trkypydktl ysvfggvttp dqgllsdrkd fyvtrgyasn drvgksyley
      301 qyedylnshk ekveyvednk gnvvsqktid kgsrgydlrl sfdmelqakv ekiveeevrn
      361 srargnymld rafvvmmdpn ngdilsmagk kielktnkie dyaigafttq yemgsavkga
      421 tvlagyqdgi phykyfhdap mylgtnlikk sytnmgtine ltalqkssnv ymfnvamhia
      481 gvtykprgpl padqkdllkm rnyysqfglg vktgvdlpqe sagmqttpdv vgglildlai
      541 gqydtytplq maqyisvian ggyrvqpriv tsihepgkkd elgkaieqrk pkvlnkinns
      601 qsdlqqvqtg mklvtssgta kntftedvsg ktgtaetyyy gtnrnwwgkk tynltfvgyy
      661 psknpkvafs vvvpsvdddd kinkiiakra ihayaelekk nsek
//
LOCUS       WP_284560444             400 aa            linear   BCT 25-DEC-2024
DEFINITION  MDR family MFS transporter [Bacillus halotolerans].
ACCESSION   WP_284560444
VERSION     WP_284560444.1
KEYWORDS    RefSeq.
SOURCE      Bacillus halotolerans
  ORGANISM  Bacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023665
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Bacillus halotolerans"
                     /db_xref="taxon:260554"
     Protein         1..400
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44161
     Region          16..383
                     /region_name="MFS_MdtH_MDR_like"
                     /note="Multidrug resistance protein MdtH and similar
                     multidrug resistance (MDR) transporters of the Major
                     Facilitator Superfamily; cd17329"
                     /db_xref="CDD:340887"
     Site            order(26..27,30..31,34,67,117..118,120..122,125,145,
                     148..149,152,220,223..224,227..229,232,260,264,313..314,
                     318,322,338,341..342,345..346,349)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mfilfqsiks rytapvwlrf fgemltsltg ammgpfmvly lheqlngsvm lpmliislqp
       61 fadicltlia grvtdqlgrr tailtalllq taamagfvfa hdayffafly ilngigrsly
      121 ipasraqiae stpesrrsev favinaiysa gltagpllgl llyahdpvwi faldaaalfi
      181 yfliaafklp etkplkadhp aalsarftry rpvlilllls lpismlyaqt ettyrlfsks
      241 mfpdylsmla iysaakalls fvlqvplvkw tekfpmktil lityisysla aagfafstsl
      301 tllmltaavm tvgesiglth iqtfisrlap phmlgrfyai yglhwdisrs igplagglil
      361 tsfggeimfy slsacllaag flqshimeri eykvirkvng
//
LOCUS       WP_284560639             392 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Bacillus halotolerans].
ACCESSION   WP_284560639
VERSION     WP_284560639.1
KEYWORDS    RefSeq.
SOURCE      Bacillus halotolerans
  ORGANISM  Bacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Bacillus halotolerans"
                     /db_xref="taxon:260554"
     Protein         1..392
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43538
     Region          77..389
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtsptrrrta trrrrklnkr gkllfgmlaa iicftiwnai hredeeaeps qeaaavsdtg
       61 qkqadqkknk akkteeqika vdrnqkissy lkeigfsgta mivrngevvi nkgfgyadre
      121 hhiknnpats fyvgssqkal iatailqlee kgklqtsdpv stylshfpng knitlknllt
      181 htsginghve gngeitpddl ikdieqqgik rqpgiwdyqd snytvlayiv aevsgesyeq
      241 yitnhifkpa gmthsgfykt ydkqpypavg yklkgsravt pympdlsqly gagdiymsaa
      301 dmykfdkali dgklysqesy ekmftpgsss tygmgfyvap gsysnhgvmp gfnvlnsfsk
      361 sgqtvvvlls niqnnaklgq vnnkiyqlln qk
//
LOCUS       WP_284560900             210 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_284560900
VERSION     WP_284560900.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..210
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          <1..200
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 sdgtvfepvn sfqknqkkla rlqrqlsrkv kfsnnwqkqk rkiqrlhsci anirrdylhk
       61 vttavsknha miviedlkvs nmsksaagtv sqpgrnvrak sglnrsildq gwyemhrqle
      121 ykqlwrggqv lavppaytsq rcaycghtak enrlsqskfr cqvcgytana dvngarnila
      181 aghavlacge mvqsgrplkq eptemiqata
//
LOCUS       WP_284560762             454 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Bacillus halotolerans].
ACCESSION   WP_284560762
VERSION     WP_284560762.1
KEYWORDS    RefSeq.
SOURCE      Bacillus halotolerans
  ORGANISM  Bacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 454)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 454)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Bacillus halotolerans"
                     /db_xref="taxon:260554"
     Protein         1..454
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50699
     Region          30..143
                     /region_name="ArlS_N"
                     /note="ArlS sensor domain; pfam18719"
                     /db_xref="CDD:465847"
     Region          173..227
                     /region_name="HAMP"
                     /note="HAMP domain; pfam00672"
                     /db_xref="CDD:459898"
     Region          <232..446
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mklktkihly tsiwllillv lvhtavylif ssaltskdaa rladetdnia ealhtaetqg
       61 valqdmlqay lpangmvrvl sadrkavmti tkekaykdfp lsfhsgettd vtkhegklfa
      121 aaavpviwtd gqvvslqlve rlehteesll llriiliaas aavciasffa gsllarhiin
      181 pirqlvttmk diqrekafkt islegqshde lyqmgltfne masmlkehyd kqqqfvqdas
      241 helktpitii esysnlmkrw gakkpevlee sieaihseav hmkkltnqll tlakthkele
      301 ldlktvdlie vsraviqtlq pvyirdifle tdkenllvta deerikqllt illdnaikys
      361 dkaivisagt nnrrpflsvr degigipedh iprlferfyr adearnrktg gtglglsiak
      421 hiadehgidl svkskpgqgt nvtmqfkeqn ggal
//
LOCUS       WP_284561051             349 aa            linear   BCT 25-DEC-2024
DEFINITION  C45 family autoproteolytic acyltransferase/hydolase [Bacillus sp.
            T2.9-1].
ACCESSION   WP_284561051
VERSION     WP_284561051.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. T2.9-1
  ORGANISM  Bacillus sp. T2.9-1
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   True,J.R., Yeh,S.D., Hovemann,B.T., Kemme,T., Meinertzhagen,I.A.,
            Edwards,T.N., Liou,S.R., Han,Q. and Li,J.
  TITLE     Drosophila tan encodes a novel hydrolase required in pigmentation
            and vision
  JOURNAL   PLoS Genet 1 (5), e63 (2005)
   PUBMED   16299587
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Tobin,M.B., Cole,S.C., Miller,J.R., Baldwin,J.E. and
            Sutherland,J.D.
  TITLE     Amino-acid substitutions in the cleavage site of acyl-coenzyme
            A:isopenicillin N acyltransferase from Penicillium chrysogenum:
            effect on proenzyme cleavage and activity
  JOURNAL   Gene 162 (1), 29-35 (1995)
   PUBMED   7557412
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Tobin,M.B., Fleming,M.D., Skatrud,P.L. and Miller,J.R.
  TITLE     Molecular characterization of the acyl-coenzyme A:isopenicillin N
            acyltransferase gene (penDE) from Penicillium chrysogenum and
            Aspergillus nidulans and activity of recombinant enzyme in
            Escherichia coli
  JOURNAL   J Bacteriol 172 (10), 5908-5914 (1990)
   PUBMED   2120195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF040521.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Bacillus sp. T2.9-1"
                     /db_xref="taxon:3041163"
     Protein         1..349
                     /product="C45 family autoproteolytic
                     acyltransferase/hydolase"
                     /calculated_mol_wt=39926
     Region          12..304
                     /region_name="C45_proenzyme"
                     /note="C45 family autoproteolytic
                     acyltransferase/hydolase; NF040521"
                     /db_xref="CDD:468523"
ORIGIN      
        1 mkqvysdfiq frgnhydfgy mqgqllkesp ilpnrikhwt skrkryftin ekesiqllnk
       61 fipgmlaein gladalhwkl edalrefggh yveyarsgcs ilagsnylir nydshpgsye
      121 grymiyqptd tgyavigpsm qitgridgmn ekglvmgynf inrvgsgdgf icnmigriil
      181 etcanveeai allkeiphrt sfsyvlldnc geayvveatp rsviarksni stnhfeilke
      241 enqyqmddsi rrkqiiegqq gsysnvyeaf rilndkdkev fsnkynawsg tlhtaaylph
      301 ekkawfaigs drmpliidld sflkgeklnl krikgqlefd tpfinmeil
//
LOCUS       WP_284561091             243 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Bacillus sp. T2.9-1].
ACCESSION   WP_284561091
VERSION     WP_284561091.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. T2.9-1
  ORGANISM  Bacillus sp. T2.9-1
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Bacillus sp. T2.9-1"
                     /db_xref="taxon:3041163"
     Protein         1..243
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28265
     Region          9..148
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 maykgssvyd nvqffenyrs rrnhdsspnn sierpifyel leemkgksil dlgcgdanfg
       61 lellgkgaes yigvegskrm fdeasrhvng ttasvyhskl edwdfmnskv divvsrlvfh
      121 yikdlhtifh giynqlkedg kfvfsvqhpl llstiesads skkrtnwivd dyfsmgerte
      181 pwigedvvky hrtieeyfrl lkeagfkvtd lregmpkqen feqkedferr kriplflils
      241 cek
//
LOCUS       WP_284561107             444 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Bacillus sp. T2.9-1].
ACCESSION   WP_284561107
VERSION     WP_284561107.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. T2.9-1
  ORGANISM  Bacillus sp. T2.9-1
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 444)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Bacillus sp. T2.9-1"
                     /db_xref="taxon:3041163"
     Protein         1..444
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48912
     Region          35..429
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(152,154,283,285,315..317,361)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrkvkillss mlifsmlllg acssgssgea dgkkeitfmf rggpdektay teaikkfees
       61 hegvsvkiin tdadqyatkl saavsggnvp dvfyldsgsi anyvdngiia diteeveaan
      121 fdldsiwkfg vdiyrydget pgkgalyglp kdvgpfalgy nknifeeagi plpdkdkayt
      181 weefleisqq ltkdtngdge vdqwasgfna twtlqsfays ngasflneag dkitvdtpef
      241 adslqfladl tnkyhttpss sqaetldtyq rwmngelaff pvgpwdmsty akldfeydlm
      301 pwpsgstgks vaytgslglv vsastknpdl atelaiylca deeaqqtlld aqvqipnlid
      361 maeewasdte svpsnkqefl diiqdygvpy ptyatynsqw ldefwanitp vmqgeqtane
      421 flaeiqpkmq klldeaneqa kmsk
//
LOCUS       WP_284561166             130 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Bacillus sp. T2.9-1].
ACCESSION   WP_284561166
VERSION     WP_284561166.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. T2.9-1
  ORGANISM  Bacillus sp. T2.9-1
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 130)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140359
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Bacillus sp. T2.9-1"
                     /db_xref="taxon:3041163"
     Protein         1..130
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=14466
     Region          3..121
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04669"
                     /db_xref="CDD:467553"
ORIGIN      
        1 mrdrgsviie dnkvglikrv reeavyyvfp gggieegets ieaakreafe elgvevkike
       61 ciakvefngi qyfflseiik gtfgtgqgee ytdkerdrgt ylpvlvdiks lssidvipke
      121 valkvqslfk
//
LOCUS       WP_284561278             254 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Bacillus sp.
            T2.9-1].
ACCESSION   WP_284561278
VERSION     WP_284561278.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. T2.9-1
  ORGANISM  Bacillus sp. T2.9-1
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Bacillus sp. T2.9-1"
                     /db_xref="taxon:3041163"
     Protein         1..254
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28865
     Region          4..250
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mknipiaiqm ytlreeceqd frgtlqkvas lgfqgvelag yggisvaalk elldelnlqv
       61 aashvpladl esnltqvvqd qlvlgskflv cpyllpdkrt eadyesliaf lnmagaecqk
      121 egislcyhnh dfeldrlydg rtaldtimee tdsklvfael dvywlskrey dpaqwidtyk
      181 nrtklvhlkd mttdeerffa evgtgsidfq ailekgeead iqwwiieqda trrtpfesie
      241 islnnlrkil geqk
//
LOCUS       WP_284561398             224 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Bacillus sp. T2.9-1].
ACCESSION   WP_284561398
VERSION     WP_284561398.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. T2.9-1
  ORGANISM  Bacillus sp. T2.9-1
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Bacillus sp. T2.9-1"
                     /db_xref="taxon:3041163"
     Protein         1..224
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25634
     Region          10..>104
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
     Region          127..>187
                     /region_name="CcmA"
                     /note="Cytoskeletal protein CcmA, bactofilin family
                     [Cytoskeleton]; COG1664"
                     /db_xref="CDD:441270"
ORIGIN      
        1 msdkegeinm tcstkifsym hqyldeeiee vhlkelkehl dqceecaahf helkktialv
       61 qstshiqapm nftenildrl peepkqvrvk rwlrhhpmla aaslflilmv sslmsawned
      121 hqfsvskqpn ilvenntaiv pegetvkgdi ivrngdikie gqvegnvtvi ngkkymasan
      181 qvtgeikevn evfewlwyhi kktvtdftel ftkdnkeens lpai
//
LOCUS       WP_284561517             482 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Bacillus sp.
            T2.9-1].
ACCESSION   WP_284561517
VERSION     WP_284561517.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. T2.9-1
  ORGANISM  Bacillus sp. T2.9-1
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Bacillus sp. T2.9-1"
                     /db_xref="taxon:3041163"
     Protein         1..482
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=55540
     Region          56..481
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mgdnmighsl ktimvfvgvy llyiviscvv vpyfyhpkad pfwkpatkln qndkkvvspd
       61 kvvllqdred sglarlqlik nakksvdist yaihkgpyad lffgclfdaa nrgvkvrlll
      121 dgivnqfnkd lrlysyaift hpnielkyye plhlgkpwtw nnrfhdklfi idselaivgg
      181 rnigdkyfsa agtkgasndr dvivfteeqk dtsvlmkidd yyqyvwehpf sknavkkish
      241 rkiqlgkeka eeamdlltha kdvyplpidk aidwkkdays tdkvfllhnp hqrvnkdpli
      301 wkelislteq stksiylesp yivptkkmle yvkpekikvd hwkvltnsaa stpnmvafsg
      361 ywsnrhyiin wvdelfeyqe kteslhgkty ifdekislig synvdarstf lntetmllid
      421 seefahflqk elnktvdnhs lqvsedgsyk akedveqadv afwkriaikt lapiiklfaf
      481 lv
//
LOCUS       WP_284561644             244 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Bacillus sp. T2.9-1].
ACCESSION   WP_284561644
VERSION     WP_284561644.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. T2.9-1
  ORGANISM  Bacillus sp. T2.9-1
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Bacillus sp. T2.9-1"
                     /db_xref="taxon:3041163"
     Protein         1..244
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28632
     Region          <123..244
                     /region_name="PRK10572"
                     /note="arabinose operon transcriptional regulator AraC"
                     /db_xref="CDD:236717"
     Region          188..>234
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msstklllen nngvflykkd fgqesnwrsd nyykfiyslm gtidyqtnrs qltlhnqhfi
       61 lfnpldehkq laiddrkfli elnpsflnev sqalypvhnd iqfathiqkn sqisnwvrfv
      121 ldfvqlekdd tksmeifleh sftqlalmll ksavgthtqd inlntyktid pqiyktilal
      181 kedyqhswtl nemakvanls kfqfahyfkd ilgispyswl qtyrvvksqe mlkknlhgtt
      241 ntmi
//
LOCUS       WP_284561665             374 aa            linear   BCT 25-DEC-2024
DEFINITION  MDR/zinc-dependent alcohol dehydrogenase-like family protein
            [Bacillus sp. T2.9-1].
ACCESSION   WP_284561665
VERSION     WP_284561665.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. T2.9-1
  ORGANISM  Bacillus sp. T2.9-1
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Gonzalez-Duarte,R. and Albalat,R.
  TITLE     Merging protein, gene and genomic data: the evolution of the
            MDR-ADH family
  JOURNAL   Heredity (Edinb) 95 (3), 184-197 (2005)
   PUBMED   16121213
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Bacillus sp. T2.9-1"
                     /db_xref="taxon:3041163"
     Protein         1..374
                     /product="MDR/zinc-dependent alcohol dehydrogenase-like
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41332
     Region          20..367
                     /region_name="Zn_ADH2"
                     /note="Alcohol dehydrogenases of the MDR family; cd08256"
                     /db_xref="CDD:176218"
     Site            order(56..58,61,175,179,199..204,223..224,228,251,
                     267..268,270,290..291,315..317)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176218"
     Site            order(56,87..88,175)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176218"
     Site            order(117,120,123,131)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176218"
ORIGIN      
        1 mntntvinee fkevvipktm kaivayepgd yrleevavpe itdeeilikv eacgicagda
       61 kaydgapsfw gdekqpayik apmipghefi gtivavgnkv egykvgdrvi seqivpcwdc
      121 rfckrgqywm cekhdlygfq nnvnggmaey mkftkeainy hvpeelpiek ailiepyacs
      181 fhavqrakiq lgdivvlaga gtlglgmiga ikksgpgklv vldlfddrle lakkfgadlv
      241 lnplrddvtk iikemtdgyg cdiyieatga qksveqgltl irklgtfvef svfkepvtvd
      301 wsiisdrkel dvlgshlgpy cyplviegim ngdlptegvv thklpleefe kgfklvkdgk
      361 eslkvilipn yqae
//
LOCUS       WP_284561711             479 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Bacillus sp. T2.9-1].
ACCESSION   WP_284561711
VERSION     WP_284561711.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. T2.9-1
  ORGANISM  Bacillus sp. T2.9-1
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Bacillus sp. T2.9-1"
                     /db_xref="taxon:3041163"
     Protein         1..479
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=54136
     Region          222..467
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mgnnrtgskt igftvlfigc ltvlyvttmy kltwilpivs iwisiqlgvy lksvmtldql
       61 frkvmyalll stflnqsvis vnvgafslfl yrillllaii myvctalynk rltvdfnrsg
      121 lsyiwlffgg wllygilsvl wslsimasik ylsllmmgia fvylasmtfk trlqlkffla
      181 gwlgmtvvlv gigfvnyffa iqlpssglyg asvhkltypt avffnqndfa vylgisffff
      241 lavaknakrt mlkgstflls vmvlmllylt esraamlavv ggglvylfll ipkrwkklml
      301 ltlfglfvlg sllfanrgia kvhllmdsag eygfdevlps nlarinllrn tfyylldsyg
      361 fgigagnipy ylehesyfpt gnvyqvhnwf aeiagnfglv illgylfvwi yafigfyriy
      421 qrtnsstdkm lleasmigmv sflissisps svmnlyfhwv flgfilstls vyknkkles
//
LOCUS       WP_284561770             328 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Bacillus sp. T2.9-1].
ACCESSION   WP_284561770
VERSION     WP_284561770.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. T2.9-1
  ORGANISM  Bacillus sp. T2.9-1
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Bacillus sp. T2.9-1"
                     /db_xref="taxon:3041163"
     Protein         1..328
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=35657
     Region          31..323
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mkkylisiis iililslsac ssssssssks edfptkpvkl vipyppgggt dvlfrlvaqy
       61 aekhlgqtiv ptnmagatst vgsrfvkdae pdgytilgth qvvataehtg vvdygfstfd
      121 pivlmtstph ipsiskkfse enniktmndf ieyvkagnkv nwaytvased hysiaamlda
      181 agvdpkslny ihydgtgpqy aailanqadg miadyasgkg yyddgtlvpl gmvfdernpf
      241 lpdvptlkeq gidfsvtvdr gilapkgtds erikvineaf kkaledpelq kkieelgsfp
      301 hymtseeysn hvneldsemg klapkmef
//
LOCUS       WP_284561843             262 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_284561843
VERSION     WP_284561843.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>262
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          6..>262
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkqqvsfkfr lkpdgqqehq mrrfagacrf vfnralalqn enheagkkyi pytkmaswlv
       61 ewkkdtetew lkdspsqplq qslkdleray knffqnraaf prfkkrgqnd afrypqgvkl
      121 dqensriflp klgwmryrns rqvtgivknv tvsqscgkwy isiqterevs tpvhpsasmv
      181 gldagvakla tlsdgtvfep vnsfqknqkk larlqrqlsr kvkfsnnwqk qkrkiqrlhs
      241 rianirrdyl hkvtttvskn ha
//
LOCUS       WP_284562133             326 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Escherichia
            coli].
ACCESSION   WP_284562133
VERSION     WP_284562133.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..326
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36889
     Region          37..262
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mmtinnarki lqrvdtlply lhayafhlnm rlervlpadl ldiasennlr gvkihvldge
       61 rfslgnmddk elsafgdkar rlnldihiet sasdkaside avaialktga ssvrfyprye
      121 gnlrdvlsii andiayvret yqdcgltfti eqhedlkshe lvslvkesem eslsllfdfa
      181 nminanehpi dalktmaphi tqvhikdali vkeqgglghk acisgqgdmp fkallthlic
      241 lgddepqvta ygleeevdyy apafrfeded dnpwipyrqm setplpenhl lnarlrkeke
      301 dainqinhvr nvlqqikqea nhllnh
//
LOCUS       WP_284562242             384 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Kocuria rosea].
ACCESSION   WP_284562242
VERSION     WP_284562242.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..384
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=38407
     Region          34..382
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mtptpttpit htggatghgt aatttaplpa rrfrsvralr agpvslrvhp rslligvill
       61 vavavtaaah lavggtpipy pqvlaaltgg ateasvylav tefraprmva ailvgaclaa
      121 agaitqtvar nplaspdilg vtagasagav avlilaedga aglsglaatv gmpvaaftag
      181 lisgvaayll ayrngidsyr lilvglgisg fataittwml tlgdvtsaaq altwmmgsln
      241 gkdwilvrpm aavavlllga avlsgrwlll aaldedtaig lglrlglirv valtlavlla
      301 avatvvggpl vfvalaapqi arlltrspvp pvtvsaltga vfvlvadtaa anllatplpv
      361 evatavlgap yliylvirsq rrpr
//
LOCUS       WP_284562325             341 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Kocuria rosea].
ACCESSION   WP_284562325
VERSION     WP_284562325.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..341
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=36449
     Region          22..312
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mnrasdpsdv dvrehgggll psritpwvrw lavaslvans vliltgglvr ltgsglgcpt
       61 wprctdeswt ntpemgmhgl iefgnrlltf llaavavltf lavlrlrheh rdlfrialll
      121 glgiplqavv ggitvltgln pwivgihyli sgamialatv lvnrtrrrsl pavrdaerpg
      181 qaygqrrtvr glmvslgvlt alilylgtlv tgtgphagdd ttarhafday lvtrahavpv
      241 ylivaavvlg lvltrrhrwp vplasglnvl laalvlqali gyyqyfngvp ivavalhlvg
      301 savliwatar tvekgfavtr tpapvlrstd raqpaeapsr g
//
LOCUS       WP_284562344             333 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Kocuria rosea].
ACCESSION   WP_284562344
VERSION     WP_284562344.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..333
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37379
     Region          5..318
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mghhrytlft gqwadlplee vaelaagwgy dgleiavsge hldawrwddd ayvrdrldil
       61 erhglgvwai snhlkgqavc ddpidfrhes ivgprvwgdg tpegvrtraa eelqhtarla
      121 rklgvdtvvg ftgssvwqyv amfppvpqev idagyqdfad rwnpildvfd ecgvrfahev
      181 hpseiaydyw sthraleaig hrpafglnwd pshflwqqid pvafisdfad riyhvdckdt
      241 kmrtgggrng vlsshlpwgd prrgwdfvst grgdvpweds fraltaigyd gpisveweda
      301 gmdrlrgape alaflkrfdf apsgasfdaa frq
//
LOCUS       WP_284562395             431 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Kocuria rosea].
ACCESSION   WP_284562395
VERSION     WP_284562395.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 431)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..431
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45357
     Region          16..380
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mpsdryrahe pgkdsrrayl vfaigtfayf savaqrtsfg vasvdaaerf gtaasalsmf
       61 slmqvlvyaa lqipvgvlvd rfgsrvmvaa gallmtagqv qlaladtvge gvaarvlvga
      121 gdattfvcvm rlipawfsal rvppltqflg vvgnlgqlvs vipfawllel tgwfpsfaal
      181 aslallaavl aatllrnapp gvevlnpalg lrrtgrvlre svaepgtrlg fwvhfttqfa
      241 gntfvlmwgy pyleyaqdls dttislvmts fvvtnlaval glgglsarhp hrrvrlslgv
      301 tavifaawtv lliwpgtapv pvvlaavcvi aismpasmia fditrsfnpa rrsgtatgiv
      361 nvggftasvl aifvtgfvld vlhaagfrde lyapdafrva iaaqflvaaa gaagvlatvr
      421 rvrrqhghda a
//
LOCUS       WP_284562474             138 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Kocuria rosea].
ACCESSION   WP_284562474
VERSION     WP_284562474.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 138)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 138)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..138
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15223
     Region          9..104
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mvvrneltdd evdrifqala dstrrdivvr vlrqeqsvsa laahyrmsfa avqkhvavle
       61 raslvtkerr greqvvhagv atlsraaall adyeqiwrgr araiedllae etppgspgaq
      121 eegsmtcrss tctrtprh
//
LOCUS       WP_284562479             597 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Kocuria rosea].
ACCESSION   WP_284562479
VERSION     WP_284562479.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..597
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62397
     Region          13..477
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          531..596
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(553,562..564,571)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            563
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mtgknpadga irpitkvlva nrgeiavrvi raardegias vavyadpdrd alhartadea
       61 yglggstaad sylvidkild vaarsgadav hpgygflsen aefalavlea gltwigpppa
      121 aiaklgdkva arhiaekvga pqvagttdpv gsaeevlafa dehglplaik aafggggrgi
      181 kvvrnrddip elyesavrea taafgrgdcf verfldaprh vetqcladah gnvvvvstrd
      241 cslqrrnqkl veeapapfls eeqnrllyas skailreagy qgagtceflv gqdgtitfle
      301 vntrlqvehp vseevtgidl vreqfrlarg ealgyddpev rghsiefrin gedpgrhfmp
      361 spgtiaaldl pggpgvrvds gvqagetvgg nfdsmlakli vtgatrqqal ersrralael
      421 riegmptvvp fhravvadpa fapadgapfs vhtrwietef dntippfegv pqagpeaeer
      481 qaivvevsgk rlevvlpalp gtakpngaaa kprksrsarg ggtaaasgds lsspmqgtiv
      541 kiavdngdev aegdlvlvle amkmeqplta hksgtvsgls vspgdtvsag avlatis
//
LOCUS       WP_284562530             367 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Kocuria rosea].
ACCESSION   WP_284562530
VERSION     WP_284562530.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..367
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=39014
     Region          115..349
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mneilgvail misfvymvrn gagagtftii vaclalsnai avfgsapdaf gelirtasvl
       61 svfffvksfq siftvshvvw imhivcilsm aftvfqllts sgmivegvpr iagamahpns
      121 aallyalglt latafflngy hrvvnmllil ayasgilltg slggiaaalv mimvlglrsr
      181 rlsvaarlga vsgiaimivi ffntpvgrer lsqlsgfdla arsaesnsle wrigrwsell
      241 fywyespfvg qgygssttgs flngyvphse yvrilveggl vgtcvlllav vsvfrglirv
      301 eklnirasiv gsagiamvsg llvnataent flysvpgyll alvlglgwgh lrafnlqthp
      361 tvmarsa
//
LOCUS       WP_284562539             333 aa            linear   BCT 25-DEC-2024
DEFINITION  GDP-L-fucose synthase family protein [Kocuria rosea].
ACCESSION   WP_284562539
VERSION     WP_284562539.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..333
                     /product="GDP-L-fucose synthase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36341
     Region          28..325
                     /region_name="GDP_FS_SDR_e"
                     /note="GDP-fucose synthetase, extended (e) SDRs; cd05239"
                     /db_xref="CDD:187550"
     Site            order(31,33..36,57,60..63,83..85,87,107,126..128,157,161,
                     184..185,187)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187550"
     Site            order(104,128,157,161)
                     /site_type="active"
                     /db_xref="CDD:187550"
     Site            order(128,157,186,205,222,230)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187550"
ORIGIN      
        1 mtadttekaa daiasftpgp ldrtapfyva ghrglvgsai wrrlqaegft dligrssael
       61 dlkdrdavfa ffartkpryv vlaaakvggi lanntypvdf lsenlriqvn vldaalehgv
      121 ervlflgssc iypklapqpl keeylltghl eptndayaia kiagilqiqa vrrqyglpwi
      181 samptnlygp gdnfsptgsh vlpamirrye earlsgaesv tnwgtgsplr eflhvddmae
      241 aclhllehyd gaehvnvgtg tdvtikelag lvaeavgyeg riewdttkpd gtprklmdvt
      301 klaaagwtar iplteglrtt vdwfrehqdg irq
//
LOCUS       WP_284562712            1209 aa            linear   BCT 25-DEC-2024
DEFINITION  TM0106 family RecB-like putative nuclease [Kocuria rosea].
ACCESSION   WP_284562712
VERSION     WP_284562712.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03491.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1209
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..1209
                     /product="TM0106 family RecB-like putative nuclease"
                     /calculated_mol_wt=131593
     Region          1..533
                     /region_name="COG2251"
                     /note="Predicted nuclease, RecB family [General function
                     prediction only]"
                     /db_xref="CDD:441852"
     Region          380..1202
                     /region_name="DNA2"
                     /note="Superfamily I DNA and/or RNA helicase [Replication,
                     recombination and repair]; COG1112"
                     /db_xref="CDD:440729"
ORIGIN      
        1 mfllgpeadl vfsasdlvra aecpyaslcv ldeklgrapr raperdamla rtaelgdahe
       61 hrvlaahlaa fgpwdaatgr gvheveparr mdrdeltakh aesldalrag advvfqasff
      121 dgafhgradf lvrrpdgaya vhdtklarha kvtallqlaa yadqleragv dvapevtlvl
      181 gdqreavfpv sehlavyrer rerfvaaaaa hrartgpvdw qdddvarcgr cehcaravae
      241 hrdllltagl svrvrrtlrd rhgvrtvdel alledrrlpa alrrlrdqaa mqtgrggedg
      301 sveyrkdggt rrvayrvtat dpvrrlpapd agdvffdfeg dplwqdpgdp tswgleylfg
      361 vveqppepga apvfrpfwah sraqerdalr afldyvaerr rrfpgmhvyh yanyekaalr
      421 rlslvhavge davdellren vlvdlydtvr gslrlsessy sikkleplym gehlrtgdvv
      481 dagasvvaya dwctaraagr eedaarllag iadynaydcl stlrlrdwll glagispdpa
      541 dhpprpaqer lelpgelpda gmtsaeqrlh ehlddpaard vlteeqrtav amvasatgyh
      601 rrerkqywws hfdrlegpve dwedtrdvfv vrraevledw akdpgkrssa aptrllrlag
      661 rfgegstpkp gtaglflmyg apvpahlaed aaprgsgrag dwtaalehve ehedgtavlt
      721 vrerlkkprd apapepwael pialgpaqpi atrsleeslq tlaartadal pelprqpgle
      781 llqrraprpa dgsplprphd gpdgtidavv ralrsldrsf lavqgppgsg ktflgshvig
      841 rlveagwrig vvaqshavve nlltgvlekg gvapervgkk ppsgrpadre tpwrdvpgkd
      901 faafladgga vvggtawdfs nakhledeal dllvvdeagq yslantlavs raarrllllg
      961 dpqqlpqvsq gthplpvdes algwlshgsp tlpaehgyfl drtwrmhpal cepvselsya
     1021 grlgsapaag rreltgvapg lrtcyvehtg nrtaspeear rvvelvhefa gtpwrsgpga
     1081 ppvplapedv lvvaaynaqv dligrelaaa glrdedgggv rvgtvdrfqg qeapvvivsm
     1141 aasaadgprg mefllspnrl nvavsrgqwc avvvrspalt dylpatpeal qvlgrftrlc
     1201 rrgrpaglp
//
LOCUS       WP_284562783             485 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Kocuria rosea].
ACCESSION   WP_284562783
VERSION     WP_284562783.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..485
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51745
     Region          10..479
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 msrvvvvggg iggltsavll ghaghrvtll eaadhlggks rrleaegqrl dtgpslftfp
       61 gvweellrrl drlrdagtar agapraedta glelerlpav gtyyyrgtrc elpvppghpw
      121 haawtrfeae hgvlgpditr llttdvldra aypalgrlgr lygrrlttrd yldsltwmpe
      181 glreviaiht lnagvgpart palyasmpav mardgvwipr ggvyelveal rrlavdagve
      241 lrtgepvtsv arrriltarg aypadavvsg ldahrldgll agrapraprr lscsaiavya
      301 vldhelpegt prhgvimpdr padlyaalea gtepeqtmaf anhypahagh pnsaatlall
      361 ltapangksy tledpfvare lertaralgl pgpitdrfrs teildpayfa ahgsaggaly
      421 gavrpawrsg pfhapahtsp lrpwlwrvga svhpggglpa vlggamistg kllerlarae
      481 grrpg
//
LOCUS       WP_284562853             360 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Kocuria rosea].
ACCESSION   WP_284562853
VERSION     WP_284562853.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..360
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38004
     Region          1..178
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mqtirgaril lalktslava lswvvaqrmp gvidqypyya plgaisamyp tvlgsvragl
       61 qtvagialgi llaagvllvg epnlvtvava vglgvllagi rrlgagaeyv pvgalfvliv
      121 ggqdaegfsa gflvqmsvgv aigllvnvtv fppldfrtar lqldrlqnvv vdyledvage
      181 laepgttggr dwrrrnhslv ritgevreav desarsargn prmvlrrrrr paadpgdpgy
      241 dsllklenvi fhlrgftdav rglydhqahd wlvpaaltar lgeavqsaad avrawaaged
      301 peeaaervrs lvgrlhsdlt dpsrtedrlv maaaqdlarl vavldpptap tagssavtrg
//
LOCUS       WP_284562861             411 aa            linear   BCT 25-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Kocuria rosea].
ACCESSION   WP_284562861
VERSION     WP_284562861.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Pereira,J. and Lupas,A.N.
  TITLE     The VCBS superfamily forms a third supercluster of beta-propellers
            that includes tachylectin and integrins
  JOURNAL   Bioinformatics 36 (24), 5618-5622 (2021)
   PUBMED   33416871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..411
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=43515
     Region          55..120
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          110..175
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mkrsptarll tglsaaalat tgialagpah avstqgflsy vdgwrvgqhv reladvngdg
       61 radvvafgdp gvfvaqgqad gtfaapvlrv rdfgtaqgwr tdrhprtvad vdgdgrddlv
      121 gfgnagvivs yaqpdgsfta pqlkvrdfgw nqgwrvdqhv reladlsgng tadivgfgys
      181 gvtvshgrad rtfdgtgkri dsygwdrgwr idknprmlad mdgngtadiv gfgdagtyvs
      241 yfsalgdtft qpaleirdfg yaqgwrvdqh prvvgnvsgh lppdvvgfgh rgalaaysrp
      301 sapgepryqp vsleladfga aqgwrtdrhp rdladingdg ildvvgfgna gvlvaygddd
      361 fltgpeltss sfgwsagwdp aryprllgdv dgdgrddvvg fgysatyvgl s
//
LOCUS       WP_284562901             471 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Kocuria rosea].
ACCESSION   WP_284562901
VERSION     WP_284562901.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..471
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49240
     Region          76..>177
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mvrsprfrrt alvpvaalat vlattagilp avatpaasvv assgtaasaa ptvatgtldn
       61 gaawraevpa dwngkvvlfa hgfrpgpanp awdagfdpta qelirrgyav asssyaatgw
      121 aletavqdql dtlaafeqrf geadrviamg rsmgglvtsl maevpgadid gavstcglvg
      181 ggvalnnyql daahaaaell lpgedlqltg ftapgqsdat iaalrealde argsaegrar
      241 ialvaallht pteldgvdae dpealaaaqa elvlqtlptv ierrhtivea aggdsgwtag
      301 vdyarllrss dqrhqvrhly rlagldlatd lgtlsrsadi apdedglewm lqtstptgel
      361 qvpvlathtl vdllapveyq eeyaetvrra ggqslfrqaf vdreghcaft vaenvaavea
      421 mderletgrw gslartsslq rsaeslgldg aafvdhrpde fvgdrtwyaa p
//
LOCUS       WP_284562871             354 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Kocuria rosea].
ACCESSION   WP_284562871
VERSION     WP_284562871.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..354
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37737
     Region          11..337
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 msaperaekr rrvlrvldah gvdavllqsh savswyldga rvhvslagpp vaavlvhrdg
       61 devvtsanea arlvaeelpk gvrlhevpwh gsltapedwf pgaramavaa eecvaaplra
      121 arasllpgea qryaqlcrda aavltgaltr atprtterel aaeltaglvr agaeplvvlc
      181 ggadrlphrh plptagplgr ramavvcarr gglianatrw vrfgpaepae tdaeariaev
      241 eadvldalrp glpladllpv lrhayprhgf daeewtrhhq ggpagyagrd prlapgvpdl
      301 vhehqaftwn psapgtkied tvllgpggvv plsvdprwpv vrvrgrdrpa vler
//
LOCUS       WP_284562995             563 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Kocuria rosea].
ACCESSION   WP_284562995
VERSION     WP_284562995.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 563)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 563)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 563)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 563)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 563)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..563
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58850
     Region          78..532
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mtepavlapt rtsarrprra pgsgrpawsa lvvlvavvva tpvlalvvdg lgslgsaapp
       61 rdlgrmvltt lllmlgvgag tlvvggglaw lvtafrfplr dvlvwllvlp lampayilgf
      121 vflsvfdvag pvqgalrsvl gpdvwvpevr slpaavlvms ltlypyvyll arsalveqtt
      181 gtydaartlg agrgralrrv lvplarpsla aglalvmmet ltdfatvqyf nvqtvsvgvy
      241 lvwkgtfdfh satqlavlvl lfavavltge rllrgrarfh qrggrgqglq pqrltgwraw
      301 gatllalaal sagflvpvlq llvwavgeav gnpaslsdpr faqylgnslv vagiaavacv
      361 alslavahgv rmgggravaf aaqlttfgya vpgavvgigv liafagldta leragvpggt
      421 gllvtgsvlg ilyayvirfl apayqavdas lakisptvtf saqslgaspl rvltrvhlpi
      481 arpgvatalv lvmidavkel pivlllrpfg fttasvwvye larenfweka alpalvivaa
      541 avvpvfflvr qahradrhgk vss
//
LOCUS       WP_284563151             841 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Kocuria rosea].
ACCESSION   WP_284563151
VERSION     WP_284563151.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 841)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 841)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 841)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 841)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 841)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444898
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..841
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..841
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87969
     Region          42..458
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          <592..731
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
     Region          765..>816
                     /region_name="Fn3-like"
                     /note="Fibronectin type III-like domain; pfam14310"
                     /db_xref="CDD:433860"
ORIGIN      
        1 mtdatrtsgr aarltelvdr lslaekvhll tgetdftlpg neriglaala fsdgptgvrg
       61 ltfvggdava lfpsatliag afddgiaeev grmlaeeaqr qhihvvlgpt inlhrtplgg
      121 rlfeaysedp yltgrtaaay vrgmqergta aclkhlvane setlrnfmds rvpetalrel
      181 yllpfemavq dagawsmmaa yndvngvaat ehdhvqngiv kgewgwdgli msdwfatkrt
      241 aasaqggldl vmpgpggpwg erlvtavrag evaeetiddh vlrllhlaer iggltppgrq
      301 srpwaqdlpa vdspqrkeql rriavrgmtv vandgvlpla vegdagqdva ligrhaidtv
      361 dmgggsavvn ppyrstiaeg laallgdrvr vadgpavrtr pvpadpaflt dpatgtpgmq
      421 vvllgadgte ltryhsdspa isldghddlg evpatavltt ilandagpvr lgavgagrwd
      481 lvaegqelsa elrlegqdpg eamlrppafa etvelpaaat ltatvapapv dwrevllgdp
      541 glglaeeshl lqmttagkta lvaapaprpd ddllaaaeaa aaaagtavvv vglteeqete
      601 aadkttlvlp grqdelvrrv ataaertvvv vnaatpvlmp wldqvdavlv aglpgqeggh
      661 avaaaltgal eptgrlvtsw paadgaapaw dvvpdgdral syddgtfigh rgyhaghapa
      721 plfwfghglg ygtweygtvr arageggpvv dveltntssr asretvqvyl dpaeddqpir
      781 ligyqgvdvp sgataavrvr cddrllrrwd daagtwapla gggelvlarg lgdvrarvpl
      841 a
//
LOCUS       WP_284563153             379 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Kocuria rosea].
ACCESSION   WP_284563153
VERSION     WP_284563153.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..379
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39147
     Region          1..365
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtrtavvgag ivglaaahal rargadvtly esgppgggqs agqgrifrha hedprlvalv
       61 arsrtlwrew eqefgvelvs pdgavaigdg vedklralep fedvpvrrls paelherlpl
      121 ladwtgpaml dvrggairtl aavaalsrrl egsmlrehvl avrrtgtgav evrtgttget
      181 ydhvvlcagr gtaplargag lglpvevgah vrltfavapd gpahhgpvpd gappgaargl
      241 ptfqdgsgaf getgvyaapy pdgrhfsvgl sadtpahpdg gladpaalaa ladrtvsyvr
      301 ralpgldprp vdhvhcwvtr lpwgddgvgi wsedgltala ghnlfkqapa lgealagtvl
      361 tgtvpghlhh gerlgrsag
//
LOCUS       WP_284563202             515 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Kocuria rosea].
ACCESSION   WP_284563202
VERSION     WP_284563202.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..515
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=56736
     Region          18..442
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mrapstasep preipggtdh rdvvvvgagl sgigaayrlq terpelsyav learddlggt
       61 wdlfrypgvr sdsdmftlgy sfkpwrdpqa ladgpsilay ihetaeefgi drhlrlrtrv
      121 vsadwsgaeq rwslglevrd edgavhrrsm tcsflyscag yydydrghda alpgledfgg
      181 rvvhpqfwpe dldwagrrvl vvgsgatavt lvpamartaa gvtmlqrspt wisavpgrdr
      241 radalrrllp aglahrvira knilfstavy qfcrrrpaaa rafftsraar ilgseelvae
      301 hftpsydpwd qrlcavpdad lfkalkrgra evvtgtidtf vpegvrlsgg rvleadlvvt
      361 atglrllpfg givltvdgtp velaeqfvwn gamltgvpnf alcigytnas wtlradlthr
      421 lvcrvlrhle rhdagavvpr aprgmaeqpl ldlssgyvrr aigafprqgd rhpwrvrqny
      481 lldsattlrt plsrtldlip rtaarrgarp qetha
//
LOCUS       WP_284563254             494 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Kocuria rosea].
ACCESSION   WP_284563254
VERSION     WP_284563254.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..494
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51956
     Region          1..452
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 melvtdlvgt lggwvwnvvf ailigvglyl tvrtgvvqlr lvpemfrvln dkpglaedgq
       61 kgisafraft vsaasrvgtg niagvaiais lggpgavfwm wviagigaas aftesllgql
      121 ykikaptgyv ggpayymerg lgarwmgllf avvitltygf vfnsvqsnsi vdalggslgv
      181 diaaaealwf rilvgavlvg ltaaiifggi rrisavseiv vpimavlyll lgllvvflnl
      241 gevpavlgqi legafgiref vtggligvii qgmkrglfsn eagmgsapna gatasvshpa
      301 kqgflqalgv yfdtwlicsi tafivllsnp efggregasl tqsalalqlg swavhfltva
      361 iflfaftsvi gnyyygesnv rfltgspaam tayrvlvlvf vfggavlald lvwsladlfm
      421 avmatinlva lvllagvavr vlrnyeaqrk qglepifhsg dvpglsglga wdgtdvvttr
      481 gyweelaqkp trtr
//
LOCUS       WP_284563320             365 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Kocuria rosea].
ACCESSION   WP_284563320
VERSION     WP_284563320.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..365
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=39341
     Region          16..342
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mattlrdrlg drhnrlnalr lglaslvivg hawpltgadg pslellsdva vngffvlsgy
       61 liaesrvrtt lvpylwrrfl riypaflvsl lvvaavfapl aaalegtsld lasaagfvln
      121 ngdlrisqwg idgtlvrvpa pdswngslwt lfhealayvl iglvlslava vrharwvlpg
      181 lflvvlvlrp lvegplevts hlwlngarlv gyflagaavw awagtwrptw vhvagagvvy
      241 avltdqgwad lygqlplavl llglgaapsr nwttrtdlsy gvyiyaypvq qllvllgtas
      301 wgvaansllv vlltlplall swtlvekpal rakawldprd rpdrrvptag aqapspaave
      361 grrpe
//
LOCUS       WP_284563328             313 aa            linear   BCT 25-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Kocuria rosea].
ACCESSION   WP_284563328
VERSION     WP_284563328.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..313
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33535
     Region          1..285
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mrpivyahrg asadlpehtr aayvqalldg adgvecdvhl srdghlvlhh daqlgrtsdg
       61 rgpvsartla elrrldwtsw kgvrippghg apgrqlltlp elldllrgag rpvglavetk
      121 hpspfghrle eevlgllmre gwdpetgrld dvtvslmsfh pdavrhflet vparhvcqlv
      181 gtttrrtvgd slrvgrtaaa vlhagmrfvv ppalpvisag lvdlvgpgld lvrarpdlvr
      241 qwradgrvlr vwtvdtardv dlcralgvqq lttnrpadvl rwarapsgap lgvpaggpaa
      301 vtgrsrcast tvg
//
LOCUS       WP_284563357             265 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Kocuria rosea].
ACCESSION   WP_284563357
VERSION     WP_284563357.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..265
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26703
     Region          11..243
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(73,77..78,81..82,112,116,123,126..127,132,148,
                     152..153,155..157,159..160,163..164,167..168,192..193,
                     195..197,199..201,203..204,206..207,211,214..215,221)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(151,155,158..159,161..162,206,209..210,212..217,
                     220..222,225,227)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(172..179,194,197..198,201)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 msagaiapsa rtsllgrtna vvkltgalll tvvlllsadp vtsgtvllge vlllalagqr
       61 plallrrawp vvvaalvsgw gaallaedsg pvlldlgvtg issgsvaaga aialrglala
      121 lpglmlvltt dptdladgla qtlrlparfv laslaalrlv gvmvsewatl amarrargtg
      181 sghgpvgalr efggqaftll vqslrratrl svtmeargfg agprtwarvp gyswrdaavl
      241 tgcaaaaaag pavsvllgth rfiwa
//
LOCUS       WP_284563368             523 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Kocuria rosea].
ACCESSION   WP_284563368
VERSION     WP_284563368.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..523
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=55149
     Region          19..366
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mterstscaa vpvavlrsps prtahrpdlq glrgvavllv vvfhvwtekv sgevdvffvl
       61 saflltgsfa rriehgrpla lpaywartfa rllgpvavll lavlaavflw fppsrwaell
      121 aqawgsliyv vnwvladqav dyyagnsaat tplqhmwsls vqgqvflvwp lllagaavta
      181 rrtgtgfrpv awvvfaavfa gslawsvvat aagpeaayfs tltrlwefal gsmaalalag
      241 sgtartasrr rraparvtgv vlgwaglaai latpfligpd trfpgtvala ptlgaaaill
      301 ggalapdart gaarllsarp lqwfgdrayg iylwhwplli tyllltardt vpvpaglgil
      361 aasvvltrvt allltgwral pgirarsgir liatallvav pltgahqytv lrdptagver
      421 taqnypgaav lrgeasevpd vpiipteder dqewgdtgdp cppertppgi aelgecriia
      481 pdpdpaggtd pggtdpgltl vvlgdsharq lltpihrvad aqg
//
LOCUS       WP_284563425             599 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Kocuria rosea].
ACCESSION   WP_284563425
VERSION     WP_284563425.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 599)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 599)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..599
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=66851
     Region          30..508
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(82,85,122,125,173,192,196,228,291,451)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(228,291,365)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          516..>569
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; pfam16657"
                     /db_xref="CDD:435493"
ORIGIN      
        1 mstrtqqqdi taqrpgtgsg agetpawwtn avvyqiyprs fadsdgdgig dlggiiahld
       61 hlqdlgvdvv wlspiysspq ddngydisdy qdidpvfgtl eqfdellgav hargmklvmd
      121 lvvnhtsdeh pwfvesrssp dspkrdwyww raprrgmeag apgaeptnwq sffsgstwey
      181 deasgeyylh lfsrkqpdln wenpevrqav hammrwwldr gvdgfrmdvi nmiskdvaed
      241 ghlhdgppvd gtpwgdgsas flcgprihef lqemhrevfa grdaelitvg empgvtveqa
      301 qlftdparae vdmvfqfehv gldhgpggkf dpeplrltdl kaslgrwqeg leevgwnsly
      361 wnnhdqprav srfgddspeh rvasatclat llhlhrgtpy vyqgeelgmt napfetiedf
      421 rdiesvnhyr havaagadpa gvlrglrwss rdnartpvqw taganagftt gtpwiavnpn
      481 hdevnaeaar aephsvfhhy rrlielrhte pvialgdftm laphheqlya ftrrlgdvel
      541 lvlanvsgee vrtdlpegwa gaellignrp dgvvpgdegl lrpwearvhr rtrgaatqg
//
LOCUS       WP_284563447             732 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Kocuria rosea].
ACCESSION   WP_284563447
VERSION     WP_284563447.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..732
                     /product="PhoX family protein"
                     /calculated_mol_wt=79021
     Region          79..676
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mtetakrtvl pllghtrgkr spvtcqlkcg sacagpecnt sgngyfrdia saalsrrsal
       61 glgaaaavtv gvvgatpeaa qahgrgrsgl sfapiapvpn tvddltvpeg fdwspiirwg
      121 dplfedspef dplrqtpesq aaqfgynsdy ldilqdrggr sgvlvnnhey tnenlmfpae
      181 qqddlqrvar vamaahgmsv veiartgpgr pwsyvrggar nrritlstpf avdgpaagsa
      241 llrtqddptg tvvlgtqnnc aggttpwgtv lsgeenfnqy fkgngsaeqk rygiaaeaps
      301 rrwhevdprf dstlpgyene pnrfgwvvel dpqdpastpv khtalgrfkh eganvrvaed
      361 gtvvaysgdd erfdylykfv saqkyvegdr ahnmtllseg nlyvakftgd taaeidgsgr
      421 lpsdgafdgs gewlplvvdg esavagmsve evlvftrlaa dqvgatkmdr pedvepspht
      481 gkvyvaltnn tdrgtpgkag pdeanprtqn rdghvieite rhhradatef gwnillvagd
      541 paknastyfs gypvekvspi scpdnlafds egnlwistdg apgtigyndg lfkvglsgre
      601 rgnveqflav pqdaetcgpv irdrermvyv avqhpgedgs feeprsyfpd yvvetrqgeg
      661 ewslprpsva qvfavdrage pefpgaihdr pgrgrnqhkr rkngergpry rgykgkatae
      721 tkaaartasr sy
//
LOCUS       WP_284563449             462 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Kocuria rosea].
ACCESSION   WP_284563449
VERSION     WP_284563449.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..462
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48632
     Region          24..433
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(33..34,37..38,41,77,127..128,130..132,135,155,
                     158..159,162,264,267..268,271..273,276,302,306,355..356,
                     360,364,380,383..384,387..388,391)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mnrphtiiae nplleqrtar fvafiiclal lfdgydlviy gvvlpgllad ptqigtlepa
       61 vaglvgsyal igvligslvc gaigdffgrr rllitgvawf svgmfvtalt tsvlafgamr
      121 fltgiglglv iatagatmae fapagrrqfy ngivysgipa ggvfaalvgi afladlswrg
      181 lfmigalpll llvplmlwkl pesprwlltr geteraeava lrtgvpliee qviqtvgaap
      241 rrtgyaavfs rqfalasill gfmsfcglll tyglntwlav imngyghsis plyfvlvlng
      301 salvggllas rladrtgpqr miattfalaa ialvlmtfsf plpllflfia vagvgtigtq
      361 vlvygfqsny yttnaraagv afcasmgrfg gifgpiiggw laaagfggpq afyvfagval
      421 lgalvtlvvp hqrgleeaeh rveelaghpq apaereaptv rg
//
LOCUS       WP_284563590             370 aa            linear   BCT 25-DEC-2024
DEFINITION  MraY family glycosyltransferase [Kocuria rosea].
ACCESSION   WP_284563590
VERSION     WP_284563590.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Anderson,M.S., Eveland,S.S. and Price,N.P.
  TITLE     Conserved cytoplasmic motifs that distinguish sub-groups of the
            polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase
            family
  JOURNAL   FEMS Microbiol Lett 191 (2), 169-175 (2000)
   PUBMED   11024259
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Lehrman,M.A.
  TITLE     A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P
            transferases
  JOURNAL   Glycobiology 4 (6), 768-771 (1994)
   PUBMED   7734839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10160628
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..370
                     /product="MraY family glycosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=37843
     Region          61..306
                     /region_name="GT_WbpL_WbcO_like"
                     /note="The members of this subfamily catalyze the
                     formation of a phosphodiester bond between a
                     membrane-associated undecaprenyl-phosphate (Und-P)
                     molecule and N-acetylhexosamine 1-phosphate, which is
                     usually donated by a soluble UDP-N-acetylhexosamine
                     precursor; cd06854"
                     /db_xref="CDD:133464"
     Site            124..125
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133464"
     Site            232..235
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133464"
     Site            order(280,291..294)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:133464"
ORIGIN      
        1 mspapvvllp agldltdpga apdpeelrrl gelvltvgvp alvlslllpl avkpllarwg
       61 vldipnerss hhrtvvrgmg lavalavlaa ygsalltgai evdrsvalvv lavtglfaal
      121 gwaedyrgvs vrarlaaqlg iglaatavlv avlgtsawwl pvgtlaiaay vnmanfmdgi
      181 ngisglhgla agllyawaga sndlpwmiaa glavaggfag flpwnlgrgt vflgdvgsyl
      241 lggslagiav aaflsgvyve yllpplavyv adtsvtllrr vrageawyrp hrqhvyqqlt
      301 dvglshtgsa lvvtaatvlv svasvvglrt gpvatavaga fvlavlalyl vlpallgrra
      361 gvrsrtgtrp
//
LOCUS       WP_284563603             274 aa            linear   BCT 25-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Kocuria rosea].
ACCESSION   WP_284563603
VERSION     WP_284563603.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     BTLCP proteins: a novel family of bacterial transglutaminase-like
            cysteine proteinases
  JOURNAL   Trends Biochem Sci 29 (8), 392-395 (2004)
   PUBMED   15288868
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..274
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=29227
     Region          75..217
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mpttrrtvsa evdfasetdh lavfslaaar pgggarpgeh lslrvdgtev aleeaedlhg
       61 trlhlarvpg gtqctvsyal eldgpagspp paepvdfvry trpsrfcpfd emagtpdalf
      121 pgargggyet lqrvrdwvhe hldyvvgsst atdtavhtfl trqgvcrdya hllitllrgl
      181 gvparlasvy apglspmdfh avveawhdga wyvldatgla prtefvriat gadaseaafl
      241 ttlqgeitlg gmrvsaessv rgredprarv vlpl
//
LOCUS       WP_284563631             424 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Kocuria rosea].
ACCESSION   WP_284563631
VERSION     WP_284563631.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..424
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45882
     Region          172..407
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 magqdgnttt rwlrpsrrrs tdrhrpvapp hprtlenlka nlgaistvat rrletdlgwf
       61 eelraderse lglvaqrgis sfvrwyedpe eplwvltqvf rgaptdltrs islqhalqll
      121 rivvdvveek vpelakhhde aalreavlry sreiafaaad vyaraaenrg swdarleslv
      181 vdgilrgehs dalrsrvaal gwastgpvtv ltgsapeaag pstvarlrrl agrhaqdslv
      241 siqgdrlvli lgglsdrdla leklaaafgp gpvaygpesp tvfaagrsar lahaalsvap
      301 awpaaprpvh sedlwperam agdesartam vesvyrpltr satglvetls ayvsvghsle
      361 atarelfvha ntvryrlrri sdltgwdplv prdafvlhca lvagrladsc apidtstpav
      421 gpvl
//
LOCUS       WP_284563717             393 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Kocuria rosea].
ACCESSION   WP_284563717
VERSION     WP_284563717.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..393
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42300
     Region          39..382
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 masdrcdvrg vahlgdamhs hpsenhadds vaepgetpew laeavmtmmr sgripglslv
       61 vvdsqrslya ggfgtadlat gtpatpatvy lwfsmtkivt ataamtlved grleldapva
      121 dyvdclrapr asqptvgqll thtaglsnpl plrwvhpaeq eapavedllr svmsrprayr
      181 hapghraryt nigylalgqi ieavsgmpvt sylrqsvldp vgmtstgfty rpeapvatgc
      241 vrapraadpl lrrllppgva gtrhgaylgl rpfyvdgaay gglvgdvada grflrlhlgd
      301 gqieghrils aetarsmrvi ehpgkpfghg igwfrrptqe tgqwvehfga gagfwnvmrl
      361 ypehglgiav mtnnttsydf eplfarltta sws
//
LOCUS       WP_284563862             122 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [Kocuria].
ACCESSION   WP_284563862
VERSION     WP_284563862.1
KEYWORDS    RefSeq.
SOURCE      Kocuria
  ORGANISM  Kocuria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 122)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 122)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Kocuria"
                     /db_xref="taxon:57493"
     Protein         1..122
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12750
     Region          1..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mrilspvavm srfgkaladp traavllqlq qgpavpsela arigvsrqil snhlaclrdc
       61 glvvgvpvgr nvryelsdpk lahaledllg tiltvepvcr cgtpecaaea laddattqei
      121 pv
//
LOCUS       WP_284564415             267 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_284564415
VERSION     WP_284564415.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>267
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          1..>259
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 emrrfagacr fvfnralarq nenheagnky ipygkmaswl vewknatetq wlkdspsqpl
       61 qqslkdlera yknffrkraa fprfkkrgqn dafrypqgvk ldqensrifl pklgwmryrn
      121 srqvtgvvkn vtvsqscgkw yisiqtesev stpvhpsasm vgldagvakl atlsdgtvfe
      181 pvnsfqknqk klarlqrqls rkvkfsnnwq kqerkiqrlh srianirrdy lhkvtttvsk
      241 nhamiviedl kvsnmsksaa gtvsqpg
//
LOCUS       WP_284564677             224 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Citrobacter braakii].
ACCESSION   WP_284564677
VERSION     WP_284564677.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter braakii
  ORGANISM  Citrobacter braakii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Citrobacter braakii"
                     /db_xref="taxon:57706"
     Protein         1..224
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=24812
     Region          <65..214
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mktiqeirrl narklrdgvg gnsyfanmid reptqtsrfm gegatkgigd amarhiekcf
       61 dlpqgwldte hqttniaksp dvsdvnrsit mvpviswvqa gawtdagyae vdlssvetyp
      121 cpvpcgpmty ilrvigdsmi deyrpgdmif vdpevaashg ddvialmhds gettfkrlie
      181 dsgerflkal nanwpepyir ingncsiigt vvfsgkprrh rhkp
//
LOCUS       WP_284564707             391 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter braakii].
ACCESSION   WP_284564707
VERSION     WP_284564707.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter braakii
  ORGANISM  Citrobacter braakii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Citrobacter braakii"
                     /db_xref="taxon:57706"
     Protein         1..391
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=44421
     Region          1..391
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mltdaklrvl akpngnkhpi kvadrdglcv vvtpkgsvtf tyrfrwlgkq qnvglgkypl
       61 mslvearqkh decrrwvaeg kdprsqlala rqaniealtv gqmldnwlsd tnrkdvndlr
      121 rtfakhipke fmrltaddvg attwkrllkd vaegkrhkpa pvaagfllqn irlamnyaks
      181 erlmtssale hievkhvgkk qaerervlda keirdllaws ddirhpfyyr avvkllltfg
      241 srtqeirlst vgewdlldkv wkcpvenskn gevitrpipd evmpliqvli dnahqtgsel
      301 llseskphtt vagygsrlpe klghekwtfh dlrrtfashl addgadltii dvllghklpk
      361 iqriynrstl mtqkrevmdk wvgilkgvqn g
//
LOCUS       WP_284564838             139 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Bacillus altitudinis].
ACCESSION   WP_284564838
VERSION     WP_284564838.1
KEYWORDS    RefSeq.
SOURCE      Bacillus altitudinis
  ORGANISM  Bacillus altitudinis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Bacillus altitudinis"
                     /db_xref="taxon:293387"
     Protein         1..139
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16207
     Region          <30..137
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 metqilkwpe hlpwihssqq rclpeghtql lyfwsvncph ceeltdhilh nvdqlsihlt
       61 cvhvpyteee ksievvskya eeknliapiv ldqdyeivtk ykiqglpsfc lidkegqlid
      121 rkmgdtgwek ilkklekrs
//
LOCUS       WP_284564607              61 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Citrobacter braakii].
ACCESSION   WP_284564607
VERSION     WP_284564607.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter braakii
  ORGANISM  Citrobacter braakii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 61)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 61)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 61)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 61)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..61
                     /organism="Citrobacter braakii"
                     /db_xref="taxon:57706"
     Protein         1..61
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=7148
     Region          <1..43
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mfnkvidlar sqgkkylwle vleqneraqk fykkqgmkhi sdiifetnsq rsilklmgmc
       61 i
//
LOCUS       WP_284564885             178 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Bacillus altitudinis].
ACCESSION   WP_284564885
VERSION     WP_284564885.1
KEYWORDS    RefSeq.
SOURCE      Bacillus altitudinis
  ORGANISM  Bacillus altitudinis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Bacillus altitudinis"
                     /db_xref="taxon:293387"
     Protein         1..178
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20907
     Region          81..165
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mltirriyqk nypkgkqvyy qytsekyydi hmetshngwn islteeefea pvkknlkeei
       61 fdpykegsev yvsemngeet giiviqhmkw nntllihdly vdkqfkrkgi gstfikmakk
      121 rarelgvrmi vletqssnfp aiqfylkngf qliglnvnsy snedikkkei riemgcli
//
LOCUS       WP_284564844             202 aa            linear   BCT 25-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Bacillus
            altitudinis].
ACCESSION   WP_284564844
VERSION     WP_284564844.1
KEYWORDS    RefSeq.
SOURCE      Bacillus altitudinis
  ORGANISM  Bacillus altitudinis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     BTLCP proteins: a novel family of bacterial transglutaminase-like
            cysteine proteinases
  JOURNAL   Trends Biochem Sci 29 (8), 392-395 (2004)
   PUBMED   15288868
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Bacillus altitudinis"
                     /db_xref="taxon:293387"
     Protein         1..202
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=23358
     Region          <25..137
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mnltceskkf ndylcelaev dyshplirak anelfnplqt eiekakaaye fvrdeishtw
       61 diqskrvtch asdvltfkeg icyaksnlla allrsqgipt gfcyqrlmlf dtpdkgycih
      121 alnavffhsl nrwirldsrg nktginaqfs lnherlafht qqkldevdyp liyvrphpkt
      181 msilkehtda iemykhhlpe ki
//
LOCUS       WP_284565032             708 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Bacillus
            altitudinis].
ACCESSION   WP_284565032
VERSION     WP_284565032.1
KEYWORDS    RefSeq.
SOURCE      Bacillus altitudinis
  ORGANISM  Bacillus altitudinis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 708)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 708)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Bacillus altitudinis"
                     /db_xref="taxon:293387"
     Protein         1..708
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=79657
     Region          13..676
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mgekqhqgaa eqkkmkrrna wrinlfffav fslfaglvik lgvlqivnge dykkqanrte
       61 vktasypspr gkmydvrgrv vvdnesvpai vytsesgvka edkikvarkl atyikmdtdf
      121 lrerdirdfw lashpkeadk liskaeqknl kakdvyplqv ervpkkevka iekdaeekav
      181 aaiyrrftgg yafepqivka mdpneekkgd ekvalldetk eskqtssvsl tyeeislvse
      241 hldelpgvnv indwtrkypy ektlynvlgg vttpeqgiik eredyymarg ysrndrvgks
      301 yleyqyedfl npekatvqyt qvggklldei krtegrrgld laltfdmelq kevdkivese
      361 lrsasarnym mdrafvvmmd pntgdvlams gkkmdgrdvt dyaigtfttq yemgsvvkga
      421 tvlsgyqdgm shnqsyldtp lyfagsggkp kqsykvlgwv ndlqalqkss nvymfqvamr
      481 magityqkdg plrarpehlq kmrnyyaqfg lgvktgidlp qessgmqthp qtvgglllde
      541 aigqydtytp lqvaqymsti anggnriqpr vvksvhfptn keevgpvvkk yepkvlntin
      601 nskadidrvk mglkmvtstg gtaagrfgqh dvagktgtaq tfyyganrsw wgnatynltf
      661 ggyypssnpk vafsvvtpyv sdkdpvikti pskivdkyve lqkkyekq
//
LOCUS       WP_284565130             420 aa            linear   BCT 25-DEC-2024
DEFINITION  Kelch repeat-containing protein [Bacillus altitudinis].
ACCESSION   WP_284565130
VERSION     WP_284565130.1
KEYWORDS    RefSeq.
SOURCE      Bacillus altitudinis
  ORGANISM  Bacillus altitudinis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Shi,X., Xiang,S., Cao,J., Zhu,H., Yang,B., He,Q. and Ying,M.
  TITLE     Kelch-like proteins: Physiological functions and relationships with
            diseases
  JOURNAL   Pharmacol Res 148, 104404 (2019)
   PUBMED   31442578
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Gupta,V.A. and Beggs,A.H.
  TITLE     Kelch proteins: emerging roles in skeletal muscle development and
            diseases
  JOURNAL   Skelet Muscle 4, 11 (2014)
   PUBMED   24959344
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Adams,J., Kelso,R. and Cooley,L.
  TITLE     The kelch repeat superfamily of proteins: propellers of cell
            function
  JOURNAL   Trends Cell Biol 10 (1), 17-24 (2000)
   PUBMED   10603472
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Bacillus altitudinis"
                     /db_xref="taxon:293387"
     Protein         1..420
                     /product="Kelch repeat-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=47016
     Region          28..301
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          39..83
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          87..131
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
ORIGIN      
        1 mkkwffifil lfsalsyplq sikaetlewe kreelpdarv gavsevydgk iyviggtgps
       61 kaysnttyvy dpkldkwsek agmktgrmga asvivderiy vmggrteqgs tnsvevynik
      121 tdtwensedl pfelkisayn lyagvidnki yvvgynsslk perynntfsy dtktkewtkk
      181 kkftneatag navviknkly vlagseligp ktfeydplld qwtvlgsgai apyhdalnfe
      241 dyiirtggts rvtlfdieam ksktipntsa pyrmghvsal vddtlyvigg veqsssaptn
      301 aranfktnls islkslknte teppgdkdpe pttppkddat dedgdallii tmvnglqkey
      361 dlsmkevnaf lswykkrdag egpgfyeide hdnnkgpfes kkdyvvfnni lmfevnkykk
//
LOCUS       WP_284565281             207 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Bacillus altitudinis].
ACCESSION   WP_284565281
VERSION     WP_284565281.1
KEYWORDS    RefSeq.
SOURCE      Bacillus altitudinis
  ORGANISM  Bacillus altitudinis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Bacillus altitudinis"
                     /db_xref="taxon:293387"
     Protein         1..207
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23648
     Region          25..199
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mfidqlksdl hqsqplfige etafkaavlv plvqvdgewh vlfevrsltm rkqpgdisfp
       61 ggkldggetv qeaalretye elgippesvk vlgqlspyia spsfvvypfv giideqqvkh
      121 sfnqeeveet ftvplswlsq yepylhhvsv qptpgedfpy ekimngekys wgsrsieewf
      181 ydydrytiwg ltarilkhfv mvakrns
//
LOCUS       WP_284565318             391 aa            linear   BCT 25-DEC-2024
DEFINITION  sialidase family protein [Bacillus altitudinis].
ACCESSION   WP_284565318
VERSION     WP_284565318.1
KEYWORDS    RefSeq.
SOURCE      Bacillus altitudinis
  ORGANISM  Bacillus altitudinis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Bacillus altitudinis"
                     /db_xref="taxon:293387"
     Protein         1..391
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016997 - alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44032
     Region          6..386
                     /region_name="COG4692"
                     /note="Predicted neuraminidase (sialidase) [Carbohydrate
                     transport and metabolism, Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443727"
ORIGIN      
        1 mtnedimiki dgklrqneqd aarkeaflpt dcvqnhaanl ieldngdllc vwfggtqegi
       61 pdisiymsrl kqgsnqwtka vklsddstrs eqnpvlfqek ngrlwllyta qlsgnqdtav
      121 vryrlsedrg etwgeigtlf dqpgtfirqp ivvldnddwl lpvfycktip gvkwtgnrdv
      181 savkissdqg ktwkevtvpn stgcvhmnig kcadgsllal frsrfadsiy msrsvdhgrt
      241 wsepratelp nnnssiqftv lhnghfalvy nhinaddqte rraslydeie degdtrtavd
      301 tearpafwgt prapmtlais tddgatwpvr rnleigdgya mtnnskdkln reysypsite
      361 gkdgslhiaf tfyrqaikyv cvceewthht s
//
LOCUS       WP_284565319             325 aa            linear   BCT 25-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Bacillus altitudinis].
ACCESSION   WP_284565319
VERSION     WP_284565319.1
KEYWORDS    RefSeq.
SOURCE      Bacillus altitudinis
  ORGANISM  Bacillus altitudinis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Bacillus altitudinis"
                     /db_xref="taxon:293387"
     Protein         1..325
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=36406
     Region          3..312
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(9..10,12,52..54,73,101..102,105..106,108..109,112,
                     116,118,126,128,130,132..133,136..140,141..145,163..164,
                     168..169,267..268,276,282..288,290..293,295)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(53,74..76,99,238,286,289)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240626"
     Site            order(75..76,103,153..157,176..178,181,208..210,214..215,
                     236..238,262..263,286,288..289)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 mkphifvakp lpasfedmlk ehctyevwqs kdpiprdllf eklqkadgll tsgtkidqnl
       61 ldhapqlkvv snnsvgydnf dleamrqrgv igthtpytld htvadlafsl ilssarriae
      121 ldrfirkgkw tkfvqeedif gidvhhqtlg iigmgrigeq vakraahgfd mnvlyhnrsr
      181 nekaesayga vycalddllk qadiivlitp ltdetyhmig erelklmkpt alfvnisrgk
      241 tvdeksliqa lqegwikgag ldvydqeplq edhpfkemdn vtlvphigsa tettrdlmlk
      301 raihnvihgi dgkasvdivk elass
//
LOCUS       WP_284565400             149 aa            linear   BCT 25-DEC-2024
DEFINITION  STN domain-containing protein, partial [Escherichia coli].
ACCESSION   WP_284565400
VERSION     WP_284565400.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10659146
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>149
                     /product="STN domain-containing protein"
     Region          51..102
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
ORIGIN      
        1 vfrkttplvn airlsllpla glsfsafaaq vniapgsldk alnqyaahsg ftlsvdaslt
       61 rgkqsnglhg dydvesglqq lldgsglqvk plgnnswtle papapkedal tvvgdwlgda
      121 rendvfehag ardvirredf aktgattmr
//
LOCUS       WP_284565431             200 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Bacillus anthracis].
ACCESSION   WP_284565431
VERSION     WP_284565431.1
KEYWORDS    RefSeq.
SOURCE      Bacillus anthracis (anthrax bacterium)
  ORGANISM  Bacillus anthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Bacillus anthracis"
                     /db_xref="taxon:1392"
     Protein         1..200
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22963
     Region          <43..137
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mnnfwndryk sdeyfygeep nvfikeqafr linhnkviaf aegegrnaif lakqghkvta
       61 idysedglek tkklakkhnv evhtkkvdll adslpvdeye aaimvfghfh ndyqkmildk
      121 miqtikpggl imfevyskkq inyrtggpkd vdmlydpidi ltwceenevi hffngeqerv
      181 egkghtglad viqvvisksm
//
LOCUS       WP_284565511             513 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Bacillus anthracis].
ACCESSION   WP_284565511
VERSION     WP_284565511.1
KEYWORDS    RefSeq.
SOURCE      Bacillus anthracis (anthrax bacterium)
  ORGANISM  Bacillus anthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Bacillus anthracis"
                     /db_xref="taxon:1392"
     Protein         1..513
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=57952
     Region          50..374
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mknrqkasii cksilclimc ilitneawft nvvraesgil idrsiedfkk kldeqvpkwq
       61 enyevpgvai givhegriay tlnygyvdkk akkavsddtl fqagsisknl tawgilhlvd
      121 egrlllddpv gkyltkwklp nsefnnnevt irrllshtag lsahkgylgv apgkhldsiq
      181 qslsgkgwln eavevtnkpg setiysgggy tilqlvieev tgipfdryme eqimkplgmk
      241 sssflqrpen hnlskaygyf geelpsyqft eqaaaglktn vidmmtlila smdannkgng
      301 vikserveem qkpilgengl gifekklsnq wkllyhsgdn rgwhsfygfi pntkdglvil
      361 tngdggidlr qdiyhvwiey etgnlpesyf slaeqrktnf itsivigatl siylllfvir
      421 lykgrrtfif kqekksyigl vvrtfllvvt avlifcaayl wrvfslnsgn tinfilimvw
      481 iitllingff pkiksnkkqr mkrkdltskf tcm
//
LOCUS       WP_284565586             488 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Bacillus anthracis].
ACCESSION   WP_284565586
VERSION     WP_284565586.1
KEYWORDS    RefSeq.
SOURCE      Bacillus anthracis (anthrax bacterium)
  ORGANISM  Bacillus anthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Bacillus anthracis"
                     /db_xref="taxon:1392"
     Protein         1..488
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54904
     Region          5..488
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mtknneagwn ldhsyttlpq sfyteipptp vsspelvkln hslaislgfn peelkkeaei
       61 aifagnalpe gahplaqaya ghqfghfnml gdgrallige qitpsgkrfd iqlkgsgptp
      121 ysrrgdgraa lgpmlreyii seamyaldip ttrslavvtt geptyretkl pgailtrvas
      181 shirvgtfqy aaargsiedl qsladytikr hypeieahen rdtallqevi kkqasliakw
      241 qlvgfihgvm ntdnitisge tidygpcafm dnydqgtvfs sidtqgryay gnqpymaawd
      301 larlaeslip ilhedeeeal kiaqdeiskf svqyekqwfl gmkrklglfc ndeqdqslie
      361 qllkmmekfk adytntfrsl tlntiental fespefkewy klwqsrlerq eeskenayem
      421 mknnnpsiip rnhrieeale aavtngdysv mekllealan pyaystdqed ycappaptnr
      481 pyrtfcgt
//
LOCUS       WP_284565625             527 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Bacillus
            anthracis].
ACCESSION   WP_284565625
VERSION     WP_284565625.1
KEYWORDS    RefSeq.
SOURCE      Bacillus anthracis (anthrax bacterium)
  ORGANISM  Bacillus anthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Bacillus anthracis"
                     /db_xref="taxon:1392"
     Protein         1..527
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=59833
     Region          7..511
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mnpnqivtln illtsdihgt vypihyqdns kaeiglakis tlikkerskn gnvllidngd
       61 fiqgtpftyh yatyeknkkn pmsllanylr ydaavignhe fnygmdvlnn vistanfpyl
      121 sanildknsk kpyfgkpyti khiesnikia ilgvtthyip nweqpdhikd lqfedalett
      181 qnwvsyireh ekpdllvvay hggferdlqt gvptevltge nqgyamchei egidilltgh
      241 qhreiahtvi ngvtvlqtgc nghfvgkvti tfekteqswi kkesysqllp vqgiatdqdi
      301 lslvtdyeek tqnwldqpig liygdmqisd amqtrlqdhp fiefinkiqm dianvsisct
      361 slfhntspgf skyvtmrdiv snyiypntlk viritgadik dalelsasyf tlkadgtiiv
      421 npsyiepkpq hynydmwegi syvlniskpi gerveslqyk gtplnmneey evvmnnyras
      481 gggnffmfqn kpvikhiptd mselianyil khkkieatvn nnwkvin
//
LOCUS       WP_284565636             613 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Bacillus anthracis].
ACCESSION   WP_284565636
VERSION     WP_284565636.1
KEYWORDS    RefSeq.
SOURCE      Bacillus anthracis (anthrax bacterium)
  ORGANISM  Bacillus anthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 613)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10141189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Bacillus anthracis"
                     /db_xref="taxon:1392"
     Protein         1..613
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=67704
     Region          186..465
                     /region_name="Peptidases_S8_11"
                     /note="Peptidase S8 family domain, uncharacterized
                     subfamily 11; cd04843"
                     /db_xref="CDD:173792"
     Site            order(207,238,339,424)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:173792"
     Site            order(207,238,424)
                     /site_type="active"
                     /note="putative catalytic triad [active]"
                     /db_xref="CDD:173792"
     Region          534..598
                     /region_name="PPC"
                     /note="Bacterial pre-peptidase C-terminal domain;
                     pfam04151"
                     /db_xref="CDD:427748"
ORIGIN      
        1 mkifqkmcas tviittllgi ggtvnsvhad sieqqsklgi dqetdkqiiv kfkadlkfpy
       61 edgiekqiqs qtndkvledl lveypdvtft rlftsvspee iedlevkapn nvstsllnyy
      121 ilqtqngeqk eelvdrlkks sliedvymkk qekitppevq pssvslspnn nprfkqqgyl
      181 eaapyginap fawevqggkg ngitfvdmey gwllnhedlv hqnielmsgi nidqhvghgt
      241 svlgivssed nevgnigiap kakakvisqi rdngqyntad ailsavnqle agdvllleaq
      301 asfdgygdky lpvevqpdif dairagtdkg vviieagang wndldqfkdr ngkqilnrns
      361 kdfkdsgaim vgassssfph ermwfsnygs ridvygwgen vdtttaeqsr savnlytssf
      421 sgtssaspii agaatlvqii akenlgqpyr pselrailsn entgtkskdp yadkigvlpd
      481 lksilvnlgy gqrkpnggne lqvtenepnn eriqankvnf htpmkgtlhn sdrvdvftfq
      541 idspenitis llneqnigmt wvlhhesdln nyvaygeneg nvvkgtynak pgkyylyvyk
      601 yenkdgsyvl nik
//
LOCUS       WP_284565707             917 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Bacillus anthracis].
ACCESSION   WP_284565707
VERSION     WP_284565707.1
KEYWORDS    RefSeq.
SOURCE      Bacillus anthracis (anthrax bacterium)
  ORGANISM  Bacillus anthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 917)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 917)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13717732
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..917
                     /organism="Bacillus anthracis"
                     /db_xref="taxon:1392"
     Protein         1..917
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=98955
     Region          63..158
                     /region_name="Inhibitor_I9"
                     /note="Peptidase inhibitor I9; pfam05922"
                     /db_xref="CDD:428674"
     Region          195..590
                     /region_name="Peptidases_S8_subtilisin_Vpr-like"
                     /note="Peptidase S8 family domain in Vpr-like proteins;
                     cd07474"
                     /db_xref="CDD:173800"
     Site            order(204,237,295..297,327,531)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:173800"
     Site            order(204,237,531)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173800"
     Region          381..497
                     /region_name="PA"
                     /note="Protease-associated (PA) domain. The PA domain is
                     an insert domain in a diverse fraction of proteases. The
                     significance of the PA domain to many of the proteins in
                     which it is inserted is undetermined. It may be a
                     protein-protein interaction domain. At...; cl28883"
                     /db_xref="CDD:333703"
     Site            440..442
                     /site_type="other"
                     /note="PA/protease or protease-like domain interface
                     [polypeptide binding]"
                     /db_xref="CDD:238300"
     Region          <734..>813
                     /region_name="FLgD_tudor"
                     /note="FlgD Tudor-like domain; cl29105"
                     /db_xref="CDD:452922"
ORIGIN      
        1 mkkttstlls malvfssfga lsahaeslqk ekqfspqlka nieqwgenki aqnvetktsk
       61 eisvivelqh aplasqsniq hapdlqnnna qsyhtelkka qedttkkike kapgakikev
      121 yntlfsgfsi svpgdqital aslpevkavy pnltyklhet sksttneeap niggptigat
      181 eawnlkdpsg kpldgkgmkv aiidsgvdyt hpdlkanyig gydtvdednd pmdgnvhgth
      241 vagiiagngk ikgvapnasi layrvmndgg tgttediiqg ieraiqdgad vlnlslgqsl
      301 ntpdqpvtlt leraaklgvt avvsngndgp hpwsvdapgn assvisvgas tvsipfptfq
      361 vagssktyqg lplsksdfpi gndfplvyvg ygnpsdyakq dvkgkfalvl qgtsstlvka
      421 eqakqagavg vlfistekei nimpeyfmre nlalpvmqls nvhgeelknl itkrkkniki
      481 gqpnptelia nfssrgpsqg swlikpdiia pgvqimstvp rggyeshngt smaapqvaga
      541 vallrqmhpd wtteqlkasl antaktlkdv nentypimtq gsglinipka aqtdvlvkpn
      601 nvsfglikpn sgkvkltqni tlqnlsskkk sfstrvelld tntktkvkts vpssisiqpn
      661 sstekpftit vdsslpqgvy tgnvyikeqg kkeetripft fsidpkdykr idgleiinst
      721 fspngdqild dnlinyylva pvddvtlhan lvtkehvtyq giihqaknet agykpfkwng
      781 tkadgtplad glyqieavas nsggetkqta avfldrtapk ltyeidqenl vitgkvddil
      841 ldwmtesgwv apgipvrlqy eingngvwes aflnpwekny giyldrtqlq edkntihiva
      901 tdaagntsnl nidldvk
//
LOCUS       WP_284565731             265 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Bacillus anthracis].
ACCESSION   WP_284565731
VERSION     WP_284565731.1
KEYWORDS    RefSeq.
SOURCE      Bacillus anthracis (anthrax bacterium)
  ORGANISM  Bacillus anthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Bacillus anthracis"
                     /db_xref="taxon:1392"
     Protein         1..265
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28986
     Region          15..256
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mirqeereih imknidsvqn prvkqwkklq tkkerdkkgl ffvegfhlve ealkagvvte
       61 livsdqtdlp kdwtvndvem yivpeaivkv lretettqgv favcekhese aaltdgkfll
      121 ldglqdpgnl gtiirtadaa gihavvlgeg cvdaynskvl rstqgsifhl pivkgnleew
      181 vdklkennvp vygtalengv pygevtpags falivgnegn gvrqeilakt dqnlyipiyg
      241 gaeslnvava agiltyylqs pvank
//
LOCUS       WP_284565768             617 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Bacillus anthracis].
ACCESSION   WP_284565768
VERSION     WP_284565768.1
KEYWORDS    RefSeq.
SOURCE      Bacillus anthracis (anthrax bacterium)
  ORGANISM  Bacillus anthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Bacillus anthracis"
                     /db_xref="taxon:1392"
     Protein         1..617
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=71217
     Region          289..616
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrkgivlklf tlttalcmli latifigqti ffkqyyanrk vedikvnlns feknylnyag
       61 nteeikrleq dflrenntwi ttldqngnlk haddfyfevt idrkqqksfg qqifkiplyn
      121 linieeidnk sstpflgqei yfsgvkkees fipfsislgk qnlngfnkpl ekafnekmsk
      181 ldqekkkaae eqfgkekkpa vqeqaaqepd ihiggrvtkv qlpdvtgpin piyknsifld
      241 nikefqtdll lkeskpiqst tqtmdyeknd ikykllikpi kekdgsvtyi yamaslqpvd
      301 eavqmvqdyy iyiiafvvvl iflasfyysk qiakpllkin dttkkiahld fteqipitsk
      361 deigdlskni nvlsnklhsh igqleqdiek erklektrke fisgvshelk tplsimksci
      421 silkdgvaeh kkeyyfqame revdkmdtli ldmlelakfe sgtykmkkds fyidtvmedi
      481 cenlsveiek kelrvhkhig pfevvanqgr ieqvivnfit nairytpnke diiistidek
      541 drikvcienk gthieeeqld kiwdrfyrvd aarqrsqggt glglaiskni lelhdaeyga
      601 entedgvlfy fylpkka
//
LOCUS       WP_284565785             368 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Bacillus anthracis].
ACCESSION   WP_284565785
VERSION     WP_284565785.1
KEYWORDS    RefSeq.
SOURCE      Bacillus anthracis (anthrax bacterium)
  ORGANISM  Bacillus anthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Bacillus anthracis"
                     /db_xref="taxon:1392"
     Protein         1..368
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42281
     Region          7..365
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mdnmmksfrf kmialfalsm vlaatvtyii ykglqlyykt mvryeeplaq frsivrefgd
       61 inffliffip lsiifffflt kpylkyfsei sngihhlang nftnrvqvss ndefgdiare
      121 invaseklke avergdfaes skdqlvvnla hdlrtpltsv lgyldlilkd enltkeqikh
      181 fstiaytksq rleslidelf eitrmnygml qlnkkpidis elliqleeel ypllekhhle
      241 arlnvdphlp ingdgkllar vfenlltnav rygydgqfvd lngyidnkev vvqvmnygds
      301 ipeedlpylf dmfytgdkar senrggtglg lfiakniveq hngtisaesn ivrtmfevrl
      361 pkdenvii
//
LOCUS       WP_284565894             385 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Bacillus
            anthracis].
ACCESSION   WP_284565894
VERSION     WP_284565894.1
KEYWORDS    RefSeq.
SOURCE      Bacillus anthracis (anthrax bacterium)
  ORGANISM  Bacillus anthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Bacillus anthracis"
                     /db_xref="taxon:1392"
     Protein         1..385
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=44510
     Region          1..377
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkraylieik ptteqiskir qsigvcryvy nlyisknkea yesegkflsg ydfskwlnni
       61 htkecdqwik evsskavkqa imngdkafkr flkglskfpr ykkkkkqdvk cyfpknnktd
      121 wtverhrvkv ptigwirlke ygyisknttv ksgtvyqkag ryyvsilyev kggkpnatln
      181 avglgidlgi kdfavrsdgk thkninktvq vkkiekrlkr eqrslarkfe nlkkrgeksv
      241 tnkrvnidkn vlrvqklhar lanirlayvk sivndvvktk ptfitvedln vkgmmknkhl
      301 skavaqqcfy afktwlltkc reygielrqv drfypssktc sccgqkksdl klsdrvytcd
      361 cgnvidrdln asinllqakk ytilt
//
LOCUS       WP_284565990             285 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Bacillus anthracis].
ACCESSION   WP_284565990
VERSION     WP_284565990.1
KEYWORDS    RefSeq.
SOURCE      Bacillus anthracis (anthrax bacterium)
  ORGANISM  Bacillus anthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Bacillus anthracis"
                     /db_xref="taxon:1392"
     Protein         1..285
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=33330
     Region          14..284
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 menkyynfdp svdmdkrtnl eiellleavf klsgfdfrqy artsiyrric nrmqisnipt
       61 iskliekvih eegvleqlln dfsinvtemf rnpiffkalr ehvipelrkh peiriwhagc
      121 atgeevlsms illheeglse kaiiyatdmn tdvlekakqg ilplnkmqty tknylqaggt
      181 qafsnyystd srfayfnpsl lqniifaqhn lvtdqsfnef hiilcrnvli yftsklqnqv
      241 qqlfyeslsh ngflclgnke tlrfsdimph ytqfnpheqi yqkiq
//
LOCUS       WP_284566048             423 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Bacillus
            anthracis].
ACCESSION   WP_284566048
VERSION     WP_284566048.1
KEYWORDS    RefSeq.
SOURCE      Bacillus anthracis (anthrax bacterium)
  ORGANISM  Bacillus anthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Bacillus anthracis"
                     /db_xref="taxon:1392"
     Protein         1..423
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46769
     Region          16..422
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mkkkfaafsv laagtifvsp llspayaetn qdklsniqse legkqndlqn ksaekeqiek
       61 eiqelqkkid dlttsinkne aelnntkkei sktqqiiaek kkhieqlqtn idtrqevikq
      121 rlqsmqekpr tniitevltt stniadlvdn mysvslilnn dtdivkkqtt dqnavtkeke
      181 avekkeqelk eaeqklvqkq qelqtnqqqq qtfisdlhtk vakvdseieg leeskgilen
      241 qrqavqkaie eekraeeark aeearkaeea rkqattsaqk aqaaptphdt niggfikpaa
      301 gsktsgfgvr sidnhkgidi aasgtvpiia aadgvvirse lsssygnvvy lshringkty
      361 ttvyahmssr svsngqtvkq gtqlgfmgnt gqsygqhlhf elhlgewnvg ktnavdpspy
      421 igl
//
LOCUS       WP_284566087             403 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Bacillus anthracis].
ACCESSION   WP_284566087
VERSION     WP_284566087.1
KEYWORDS    RefSeq.
SOURCE      Bacillus anthracis (anthrax bacterium)
  ORGANISM  Bacillus anthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Bacillus anthracis"
                     /db_xref="taxon:1392"
     Protein         1..403
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47056
     Region          1..69
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          283..400
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
ORIGIN      
        1 matlggkira lrkekkltqt elagseltks mlsqiengka tpsmktlqyi aeklgcetsf
       61 lleedddeiv vliqkmerli knkcdevyet llpivqkelp stlntarlyk qfitaaavmn
      121 dynieyyvet avsifekytl yrestetkll fyymlfkqkk ykeclqmiat irdeykaknl
      181 emdlithiql ylkeaiilla ygnyekcekv ildalafskk hqvyyktdef yrilsyqkii
      241 ttdkeqylyy ikkseqfaif tedtlsaanv dilkayyynt vtneytiale hleqfreklk
      301 ndpifqddgl yylekgksly glkrykeale tlkhatipdy mnhpldqswv ltagsyralc
      361 yielqdkksa lteakeavqa idsypdsift sfiketlqii qkl
//
LOCUS       WP_284566091             556 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Bacillus anthracis].
ACCESSION   WP_284566091
VERSION     WP_284566091.1
KEYWORDS    RefSeq.
SOURCE      Bacillus anthracis (anthrax bacterium)
  ORGANISM  Bacillus anthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 556)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 556)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 556)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 556)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 556)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Bacillus anthracis"
                     /db_xref="taxon:1392"
     Protein         1..556
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=61574
     Region          1..533
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mvnrfvlvrq vgmtvalllv amliviplfl illssvyens swnflkpfev mqsgglagif
       61 lnsmllgvlv vigatifafp lafimsktdv gkhskldivf mipfmtppyi gsmgwilfmq
      121 pngyfeqffp mlktisssff slggmvlims lhlfpflyfm lkntllqigs skeeaaavhg
      181 grffyrlrki ilpllvssyv mgallifvkt iaefgtpatf grrigfhvlt seihkfissw
      241 pidfssatal sslllsacml iwymqnvlnr kysyamvsgk gvkskrytls ifvrvvawfy
      301 vigllivsig ipyfsilias lsklrggglh vnnfttshye alftigspgl ealwnsflfs
      361 litaiiavmi gvflalmirk gkkssekwld mcgmlpnmvp givmvvglil fwnspympls
      421 iyntpvmviv tyvvlflpyt vqyvkaslgq iddslvqags ifsgnyiyif rkiifpliip
      481 gilagwamtf tisirelvas llvlppsvet satfilaqfe qgevsigmam avvsvglttl
      541 cllllqhmeq krkgva
//
LOCUS       WP_284566119             460 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Bacillus anthracis].
ACCESSION   WP_284566119
VERSION     WP_284566119.1
KEYWORDS    RefSeq.
SOURCE      Bacillus anthracis (anthrax bacterium)
  ORGANISM  Bacillus anthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Bacillus anthracis"
                     /db_xref="taxon:1392"
     Protein         1..460
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51343
     Region          174..425
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mnkkkkiqks vlsftllfsl gissfpltta ihadtreeqs vekkrvslte rtslffeylq
       61 qdkyakalql tsaafqskft antlqnwwtq sgwsaiksmg ipvikeqnlv hqtveisgtt
      121 qgttiplllk ftpggkvdei gvrtppesyi ipqptydqpa syqereivig nstyplpatl
      181 tipkhkpgek vpvvvlvhga gihdrdstyl gtkilrdlav glssngiavl ryekrtleha
      241 lkmsaepvtl drdttddaiy aaksaaqqeg idpnnifilg hslgagampr ilskspsslv
      301 rgsillappa rpltdiaidq nqylgapkev idelkrqvaf iqdptfnpdh ppagynfasp
      361 hfmydvsrwr pveearlrte pllilqgard hqvtvkneyt kwqeglsnrr nvqfnkypkl
      421 nhfftegdge lslpseyeip anvpeyviqd iikwvnetkk
//
LOCUS       WP_284566278             436 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Bacillus anthracis].
ACCESSION   WP_284566278
VERSION     WP_284566278.1
KEYWORDS    RefSeq.
SOURCE      Bacillus anthracis (anthrax bacterium)
  ORGANISM  Bacillus anthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Bacillus anthracis"
                     /db_xref="taxon:1392"
     Protein         1..436
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48091
     Region          1..425
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mkkfdvaivg gglagltasi ylakagrevi vlekssrfgg rgmtinkngi cmnlgahaly
       61 rggaafltfn elgmnlpggi pstkahgiwk gdiftiptdf ssilstplls wsakvqfsrl
      121 mirlgdldvr kvqkvslttw aeneikdpmv rnifyalcrt ttytfaptiq lassvlkqiq
      181 lsikegvfyv dggwetiitk lrdianhvgv qflakkhvle iehyedkqri ycfddevfev
      241 gtvivttppk eacniikgae gtslqrwseq sipvtvtald iglrrlpnpt hqftlgldqp
      301 ifftnqsraa klsddgsiav slikyqnpal emkhthkdke qlestmdllh pnwkrevvaq
      361 qylptikvvy dfphinrfet pgpnipempg vyvagdwagh deiladaava sgkraalhil
      421 kqleseavhh gngaii
//
LOCUS       WP_284566332             338 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [Bacillus].
ACCESSION   WP_284566332
VERSION     WP_284566332.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..338
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38655
     Region          5..332
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mytydklisw venikeqnhs saaalcimkd nkivlehysg yhsntssnei vsassqfnva
       61 sarksylglm iayalyegki nsiddeaiky fkdfdhallg kttirhlvth shglgetndg
      121 kifrefepgq swayrdinvr mmthliyqly rksfpellke rvfkpanfqe tgwriqqddn
      181 lvavvddpnk daireigtvd dgteknlfis arefaqwgnl hlnqgmihdk qivpkeviki
      241 atslqsptyv nkelpqnglf wfvqnepaql selgervpkg syqilgitgp tilvipaynv
      301 vvakmynkry nyggdnylyy lrefsnlvvd tfrnsnra
//
LOCUS       WP_284566344             371 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Bacillus].
ACCESSION   WP_284566344
VERSION     WP_284566344.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..371
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39886
     Region          1..367
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mksyivvgag ilgastayhl akaganvtiv drqqvgqatd aaagivcpwl sqrrnkawyk
       61 ivkggaryys sliqqleedg etdtgynrvg aislhtdekk ldqmeerayk rredapeige
      121 itrlsaeetk klfpalseey ssvhisgaar vngrllrnal isaakkhgat fikgdavlvh
      181 egnhitgvkv ndetilaekv ivtagawane ilnplginfl vtfqkgqivh lqmentaten
      241 mpvvmppndq yiltfdnghv vigathendt gfdhrvtagg lhevfhkalt vapglenatm
      301 letrvgfrpf tpgflpvigp lpnfegilva nglgasglta gpylgselak laleqpield
      361 lndydvagai e
//
LOCUS       WP_284566539             374 aa            linear   BCT 25-DEC-2024
DEFINITION  sialidase family protein [Escherichia coli].
ACCESSION   WP_284566539
VERSION     WP_284566539.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 374)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..374
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016997 - alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40859
     Region          26..369
                     /region_name="COG4692"
                     /note="Predicted neuraminidase (sialidase) [Carbohydrate
                     transport and metabolism, Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443727"
ORIGIN      
        1 msvalirdgv irpsendshv ltamlpsscp qnhaanilpl pdgalmcvwf agtqegiadi
       61 svwgsrlpag gmqwsdaakl shddtrseqn pvlflapdnv lwllwtaqis gnqdtaivry
      121 rksddlgqtw geiatlldkp gtfirqpitv ldngnwllpv fycrtqpgek wvgnddisav
      181 kisadgghsw rdvevpqslg cvhmnitmlh dgtlvalfrs rwadniyish svdngeswsv
      241 pqatelpnnn ssiqvttlas gelalvynam saagaverra slydeiddgd dsrkeptavg
      301 rsafwgapra pmtvaisadg gkswswrrnl degdgycmtn nsleklnref sypsikqspd
      361 gtlhiaytww gqas
//
LOCUS       WP_284566573             371 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Weissella paramesenteroides].
ACCESSION   WP_284566573
VERSION     WP_284566573.1
KEYWORDS    RefSeq.
SOURCE      Weissella paramesenteroides
  ORGANISM  Weissella paramesenteroides
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Weissella.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Weissella paramesenteroides"
                     /db_xref="taxon:1249"
     Protein         1..371
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42821
     Region          70..371
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msigipifan fskgwyrimp vkhvgnkwqi dvytkgarrr isgfvtkkea lqfervllne
       61 sdglpdstgi tvnnlweewh eaylaggvte stqykvdgff grhiqptfgk rdiatitsqe
      121 lqawinkgsl kwrsfnknah yfkrifdyai kieylennpf dkvsmprkks tpeksvwtse
      181 eyeqwlnyll tdlwkkskqq svylvlltkt gmrrqeisal nvkdinfkkr tlsinkalky
      241 gksgmylget ktkdskrdig ldkntiemlk vylrdreyah qklfttgsed vymsfnrpyk
      301 wfkqaikeag vtdigglhal rheyatmaik kgispklvqk qlghsdvait mdiynhvsnn
      361 evigiadkla d
//
LOCUS       WP_284565577             338 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Bacillus anthracis].
ACCESSION   WP_284565577
VERSION     WP_284565577.1
KEYWORDS    RefSeq.
SOURCE      Bacillus anthracis (anthrax bacterium)
  ORGANISM  Bacillus anthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Bacillus anthracis"
                     /db_xref="taxon:1392"
     Protein         1..338
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35621
     Region          30..338
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mkkilntdkk raitvttifg cigiavilis lntgtlsiap lkviqtlfgy gdfesatvly
       61 dyrmpriiit mlagiglgis gailqglsrn aladpgilgl hsgasfgliv fvtlfhsine
      121 sasiliplft fgggvlaafl iillasdrsk gllpirlilv giavsagfsa itlffslkln
      181 detytfasrw lvgnvwgrdw ihvlallpwi filtpyawlk sktlnalslg dsvaaglgvs
      241 vqkerlllla tavglscgsv siaggigfig lvaphiarkl vgttyqhflp lagiigmiil
      301 vladtigrsi fepnsipagv vvaalgapyf lylltktk
//
LOCUS       WP_284569717             456 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Staphylococcus warneri].
ACCESSION   WP_284569717
VERSION     WP_284569717.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus warneri
  ORGANISM  Staphylococcus warneri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Staphylococcus warneri"
                     /db_xref="taxon:1292"
     Protein         1..456
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=53984
     Region          1..456
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mkvgvilnrv frihhnplla yicnqldttd tcvliipkek fgdeaqlkas fyhgtlnafi
       61 ntlnhyqiqt nvidydylie fcinqqldkv vmasdimsyh hesydyphqk qrfhdagihv
      121 dalrvqhyfs prktfnnqge pykvftsfyk kwrpyvmqrh rahyelsdis kivepayapt
      181 qindshsglt ekevqqqwqs flnndiqnye snraylpevl tsqlsialay glidilqvfn
      241 dllqgyesde snyeafirel ifrefyyvlm tqypetahqs fkekyrnidw vndkqqfnkw
      301 kngetgypiv daamqelnqt gymhnrmrmv tsqfltkdll idwhwgetyf kdklidydna
      361 snvhgwqwsa stgtdavpyf rmfnpikqse rfdqnalyik qwlptfnnvd shllhdtkkh
      421 mqllkqqgie lgidypepmv nhsdsrqrvm slfksl
//
LOCUS       WP_284569728             197 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II [Staphylococcus warneri].
ACCESSION   WP_284569728
VERSION     WP_284569728.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus warneri
  ORGANISM  Staphylococcus warneri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Staphylococcus warneri"
                     /db_xref="taxon:1292"
     Protein         1..197
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22388
     Region          2..191
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 mivvidnkds ftynlinyfk matqetvnvv dvedinieel kelkpkaivi spgpgrpsdy
       61 pilfkvmddf yqripilgvc lgfqmiyqyf ggtiihrdrp ihghttllrh ngegvfkglp
      121 dsfsvmlyhs lkadescvpn elkvtaeged yvimglqhek ypiyglqyhp esilseqgqn
      181 qiqnfidivg ensdyqi
//
LOCUS       WP_284569754             160 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase [Staphylococcus warneri].
ACCESSION   WP_284569754
VERSION     WP_284569754.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus warneri
  ORGANISM  Staphylococcus warneri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Staphylococcus warneri"
                     /db_xref="taxon:1292"
     Protein         1..160
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=17788
     Region          58..159
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mrklkphrgy qatnmnplwh iyrlvkfpkv lrqtiiieic rympnlklks hmyrqllgmd
       61 ignhsvfafk vvpdlfypel itvgnnsvig ynttilthei lvdefnigkv tigshtliga
      121 nvtilpgvti gdhvkigagt vvskdvpnns vafgnpiqiq
//
LOCUS       WP_284570063             689 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Staphylococcus warneri].
ACCESSION   WP_284570063
VERSION     WP_284570063.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus warneri
  ORGANISM  Staphylococcus warneri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 689)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 689)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 689)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 689)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..689
                     /organism="Staphylococcus warneri"
                     /db_xref="taxon:1292"
     Protein         1..689
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=77189
     Region          13..682
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mlkrlkeksn dekvrntmnr rinfifglvv fifaimvlrl gylqiaqgsh ykqliknden
       61 itvnesvprg rivdrngkvl vdnaskmait ytrgrktsqk emletakkls slinmdtdki
      121 ydrdkkdfwv tlhpqkakdl mkkeqsmled gsisqeqyde qqrkkigkkq lselskkdlq
      181 ilaiyremna gstldpqiik nedvtekeya avsqqlsklp gvntsmdwdr kypykdtlrg
      241 ifgdvsmste glpkelteqy lskgysrndr vgksyleyqy edvlrgkkkq mkyttdksgk
      301 vinsevinpg srghdlqlti didlqkkves lldkqiaklr sqgakdmdna mivvqdpkng
      361 dilamagkqi skngkltdyd ignftaqfav gssvkggtll agyqnnaikv geqmvdeplk
      421 fqggltkrsy fnkngrvtin dkealmhssn vymfktalkl agdpyysgmp lpsdismagq
      481 klrkglnqvg lgvktgidlp netngqiepl tnnpgnyldl sigqydtytp lqlsqyvsti
      541 anngyriqph iglsihdatn kdelgpvkrk vkgnvlnkvn nsqkeidevq dgfkmafnek
      601 dgtgyasfkd tvvpsagktg taevfqdgep rvnstyvgya pikdpklafs ivytnqpvpp
      661 pwlnggdlgr dvinyyfkdk dkngdstek
//
LOCUS       WP_284570130             501 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Staphylococcus warneri].
ACCESSION   WP_284570130
VERSION     WP_284570130.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus warneri
  ORGANISM  Staphylococcus warneri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Staphylococcus warneri"
                     /db_xref="taxon:1292"
     Protein         1..501
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56711
     Region          3..497
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mniavigagv tglasaarla ahghqvtlye kndqiggrmn qfkkdgftfd mgptivmvpe
       61 vykavfeacg erfedyidme qlpyiydvyf dkedkvrvpt dlaelhdtle qiepgtthgf
      121 mkfladlygr yeiarkyfle rtyrkpsdfy nltsliqgyk lktlnhadnl igqyvknekv
      181 qkllafqmly igidpkqgps lysiipmiem mfgvhfikgg mygmvkgleq lnlklgvdiq
      241 cnanieeiii dpkykqadgv rvnglvkrfd kvictadfpy aaqqlmpqha pvkkyppqki
      301 dqldyscsaf mmyigidkdi tedvllhnvl fsnhfrqnid eifngdised pslylyvpkv
      361 gdatlapegq tglyvlmptp elktgplewe npqfiksvke hiyrklatip alehvqdyvi
      421 setiftpkdf eqtfnakfgt afglmptlaq snyyrppnvs rdykdlyfag asthpgagvp
      481 ivltsakitv deiikdinnh i
//
LOCUS       WP_284570195             106 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Staphylococcus warneri].
ACCESSION   WP_284570195
VERSION     WP_284570195.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus warneri
  ORGANISM  Staphylococcus warneri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Staphylococcus warneri"
                     /db_xref="taxon:1292"
     Protein         1..106
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12217
     Region          3..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msyqqlasil kvlsdenrle ildllscgel caydllqhfe isqptlshhm kvlvtyqfvt
       61 trkvgnkrfy qlnhefytqi idnlnlintt hdqcvcqsvk rgdhsc
//
LOCUS       WP_284570264             232 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Staphylococcus
            warneri].
ACCESSION   WP_284570264
VERSION     WP_284570264.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus warneri
  ORGANISM  Staphylococcus warneri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 232)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Staphylococcus warneri"
                     /db_xref="taxon:1292"
     Protein         1..232
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26642
     Region          1..>203
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mnklerqnrl iteiqqsnki tatelakrfn vskrtilrdi ddlenqgvqi hashgsqggy
       61 kiqdaqskis ltltdsqlsa lfltlnesqs ystlpytkei qeilkqcltl pqtrvrkllk
      121 kmdyyikfed taqitlpnif sdiliycter nvmlvdffee dqtiaenvif igllckdgqw
      181 havvfeiglg strelpikdi qdisysfekt intqditidn yqqflnptdl hv
//
LOCUS       WP_284570307             651 aa            linear   BCT 25-DEC-2024
DEFINITION  IucA/IucC family protein [Staphylococcus warneri].
ACCESSION   WP_284570307
VERSION     WP_284570307.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus warneri
  ORGANISM  Staphylococcus warneri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Staphylococcus warneri"
                     /db_xref="taxon:1292"
     Protein         1..651
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=74984
     Region          44..650
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mnsikiakdn kfnltkdeqd ayqflsqshp ewsqyfienv nigrdkvtqr lvtsihrenl
       61 vngndhsril kskdieglss hrpevleief kashkklyap isgkhafnrv dvegpfyyqs
      121 indsifyrve hpndilewvl ieapeldnea sdqfkddltn saanmifais yqaysmkdes
      181 rplfdiiknh ddsylrseqs vieghplhpg aklrkgmnss etfkyspefa qpinlkiili
      241 hhqfsrvqsl aksyndmmnq lfpkmyqqlq devkeyhdis lddyhvmivh pwqydevlar
      301 dyskeldqhl iikthctlpy yaglsfrtlm pkapnedphi klstnvhitg eirtlseqtt
      361 hngplvthil nqilvndmtf ksyassvide vagihfyngn dqdpiqters eqlgslfrtn
      421 inihlkekgl tsmipsslva qypyhpeppi vsliklyqnh ndftsydeaa qawmkdysha
      481 llglvvpllt kygialeahl qnaiahfned gslnhlyvrd feglridqar lnsmgyatnq
      541 fheksrilte skdsvfnkaf ystvqnhlge lilnvvqsan qddledliwn dianiihqil
      601 dtitdvsner iseiqnvifa ksidykcvtt mrledeahey tyikvnnplh s
//
LOCUS       WP_284570335             157 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein
            [Staphylococcus warneri].
ACCESSION   WP_284570335
VERSION     WP_284570335.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus warneri
  ORGANISM  Staphylococcus warneri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Staphylococcus warneri"
                     /db_xref="taxon:1292"
     Protein         1..157
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=18828
     Region          44..>117
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mllndyykty kmnesedtfm ieknndaqyy dilesinels ndtfcvlnhl yvnedkesqf
       61 edkflgrqkh lqdvpgfkal rflrpqakhk hyiivtlwqs rqafydwqks sayaqthckr
      121 gtkrgvdnli vnrdlsynir ieledmtnqf lnyedif
//
LOCUS       WP_284570428             468 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Staphylococcus warneri].
ACCESSION   WP_284570428
VERSION     WP_284570428.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus warneri
  ORGANISM  Staphylococcus warneri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Staphylococcus warneri"
                     /db_xref="taxon:1292"
     Protein         1..468
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54748
     Region          12..199
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkvikskein hrpkvsvlis tynkekfist tldsvlkqtm nmkdfevivv ddcstdqtfd
       61 ivgqkiegfa nykfvqldqn sgtpvkprnl sielskgkyi ifidgddwlp edalkklytl
      121 lktnktdyat gltkyvhsdr iarsgvalsk laynkadlky frksfyhlap agrmikasvi
      181 kknhiqfpem ifgedlqffa evffntkris ttqdvvycan ryddnislvk sesstninrm
      241 kwqgeaykhl mnkykhnklm pnllyriink dileakfykk rfinninell pifqniiqmi
      301 eenfnpldyv dddlnrraie lirkgdkeai lnfvnfylkk dekplheknd iyyysfkgkh
      361 ykkrmhptll kieqehdkif lkllsknadl kylevknrkd ptqfividik ksrfksgeys
      421 vqfktdhlpk gklaltvydk dlngsviksg mrfdfyetvg gnlgyikk
//
LOCUS       WP_284570612             349 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Staphylococcus warneri].
ACCESSION   WP_284570612
VERSION     WP_284570612.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus warneri
  ORGANISM  Staphylococcus warneri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Staphylococcus warneri"
                     /db_xref="taxon:1292"
     Protein         1..349
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=40753
     Region          65..339
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 masftitkrk nknstswqyd vkhpffksgk krksgfktka eatnaaqqli rdlqdgnnie
       61 enkkfidyyn dwlkiknkkq lsskqfywye raiklfseyf genmlvknit rseyqkflnq
      121 yaqghtdetv rkvngclarc ikdalydgyl kkdptynvni kgtekakdek fkyitikdyl
      181 nlldyfkkrd eesyiilyll gitgarysdv inmtykdlnk angiihlpgt ktknskrdve
      241 vnskdimhin sklariprri dgklfsvsht svskafrkak eaiglndnni tpyslrhtht
      301 syllskripi eyiskrlgha tisqtlntys hlleehkkeq gqrvreifs
//
LOCUS       WP_284570749             407 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Escherichia coli].
ACCESSION   WP_284570749
VERSION     WP_284570749.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..407
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=46893
     Region          14..399
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 malsdawlrs vvgkerdkvl vksdrdglsv rvspkgrvvf qyryqwagkg erldigtypa
       61 tglkeareev irlrgelesn rnprlvkqae krkateamtv esvirawyea ycvknkkgsv
      121 qilrsfelhl fskigniphd aatlhdwlev leplstktpa iadrllinak qahvwaykrk
      181 lietrplsdi tgkdmdirkg qkkrflthde ikilyaaidg srmvpkyraf iklllhfgcr
      241 sselitarvd dfdfinkvwt vpperhktge itgeplkrpi iepveeliky aismnngsdm
      301 lftkegsrep vgrtslqslp ynlmqyawrr lgyqfphwsl hdlrrtartn fsdltaphia
      361 eimlghklpg vwqvydksdy leeqrkayqa wwervesivt csgsdtn
//
LOCUS       WP_284570901             584 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284570901
VERSION     WP_284570901.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..584
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=63181
     Region          59..391
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(60..61,64..65,98,101,155..156,211)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(153,156,236..242,271,296..300,331,355..359,362)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mtatvpsriq pqvefrsgtq qserrqqsdh sqrshqnasq strhnfgysh sagnriavlw
       61 fpdwpvqaal leetrrgisp espaialasn hritaccdka raqgvrrgmk lraaqalcps
      121 mvvrdadpqr dgrlfssive elddvsasle vlrpgmvaln ltaatrfygs eqaalerfid
      181 aaahegidat agaadelpta iiaarhrvlg avvqpgdsva flyqqplsvl laepalgcqk
      241 dtvetlaglg istlgeltel pttaistrfg saglhchria saqqqrkvap gaveldlsas
      301 itpeapitrv deaafiarml adqvhqqlat qglncvriki aaetddgtti skiwrtttal
      361 tehataervr wqldgwlssg gagaivelsl tpletqiptn tgsiieadta vaeettvtvv
      421 srlqsmlgfd avqqphavgg rgvadrvrfl pygqaaenir elgrrnaewi gaipsplptr
      481 lgggldhpas rvrlvdkhgn pvfvtaeall sadpagmswg kkkfqvlgws vpwpvdtgww
      541 eseifdesqr larmqlvgkn agdqhpkawl lvwqhrawri eamy
//
LOCUS       WP_284570914             340 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284570914
VERSION     WP_284570914.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..340
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34498
     Region          28..336
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mqapalfarr tlgmlailaa ivvmicfsia lganplpwge vwngllardn seaaiivwtl
       61 riprtvvaia tgaafgvaga liqaltrnpl adpgilgvna gagfavtlgv gffgltsisg
      121 yiwfaflgaa ittvvvyfig sgaslgasgk anpatlvlag valaavlsgi tqfltlidpd
      181 tfqairnwsl gsvaradlsd talvapflpa glvlalaiss slnsialgdd laaslgtkvv
      241 rtrvlgiiav tllaggatal tgglafvglm vphvvrwivg pdqrwiiiys alaapvlvla
      301 sdvigriiar pgeievgiit avvgapvlim lvrrrkasgl
//
LOCUS       WP_284570916             517 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284570916
VERSION     WP_284570916.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..517
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55013
     Region          15..514
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mssgfarssf ahngkarvav igagpnglta aavlaqagcr vevfesadhi ggsarthpaf
       61 gagsavdfga aahpfgvvsp vfrqlgleny glewkhpqyp mahplvdapa vilhrdlktt
      121 aaqfsdhdrr vwnhlhkplv ddvgklvnsv lpvrprypla larlglrgvw parsltsrll
      181 vdeaarallv gsavhairpp sqpgtaafgl lfnslgmttg wpvvsggsgk lvralarvie
      241 hyggtiktga kvqdlsgfvt ydavvatqtp rqllalqgld lsrlrsrslr rwkygtavyk
      301 vdylvngpvr wndprvagag tvhvggtvse mqlaesqaaa gmlperpfvm vcqqqtadpt
      361 rfsgswrslg vgrvlsaqid agripedarq philwayahv phgyqekfpg evaglietqi
      421 sryasgfsaq iiehheaspv qlqeananli ggdiaggamn laqmlrqrqy vgtltmnpev
      481 pvvqasgasl pgagvhgmag wraaqtilrr fgatefs
//
LOCUS       WP_284571272             428 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284571272
VERSION     WP_284571272.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..428
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46917
     Region          157..263
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mtdrkrgakr srkhgteqnt gqstesftes vsnsltrlkn slrrhlsqqw teltspsfsv
       61 pasklpepla hhatevsast ipesvvaeia eslnlrgkhd hhhaatdqes enapepedgp
      121 qtaeksdynf dssrhlplga rfkprgvfed dwsarpsadk pwpvilihgt vdtkgvwqel
      181 gtelradgwc vfapdygkrg taameesavq lgayieavrt itgaeqvili ghsqggllar
      241 ywmrtsgqar yvkhlvslga pnhgttmggi lsplvtnnlt enimhsliqh wfgpvgfqqi
      301 tgseifavfn ngaddrdgdg nsddssgtnt hgsgeledgv dytciasrqd tvvqppetcf
      361 lngpahqvrn vwvqdiipra nvqhqdlpmn khvraiirtg lkkganeenl kcktqntepk
      421 trrlehgv
//
LOCUS       WP_284571148             446 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284571148
VERSION     WP_284571148.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..446
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46521
     Region          17..427
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 msrtggsaph prevvtrral vvwvagvacy ivaitgrtsf gvagveaiar fdvdasriav
       61 faavqlgvya laqiptglgi drfgpramvm fgavvmglgq fllalttsyp laivarvlig
      121 agdasaflav mrllpywfpl rktplftqlt gaigqtgqfi savpflallg sagwtgafvt
      181 lgatsillag laglaikdlp dvdrraadap esgtaasgrd slrarmrtll rtpvawqgff
      241 mhysclmfql vflmmwgfpl mtlgmglsak qagavlaint vvtvfsgplh gifsarigaa
      301 rhwavvgfsv tivltwvvff asatprglaa ivvvnvival cassanygfd nvregvsrev
      361 vatatglanm ggflagmaas qgigvvldis saggeytwgd fqvaalaagv vwavgvigll
      421 vasawrkypg pahrilphrl ralrsh
//
LOCUS       WP_284571325             239 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284571325
VERSION     WP_284571325.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..239
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25480
     Region          76..221
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mskkvtnpnq kssagfigai aavlaivvav iayivingqg akaekfanwe ikqvsaetsf
       61 dgntltfgaa dkaphvdlye dfscphcahl aeatdaeale einagnlavs ihpmtfldnq
      121 gdghstqava allalaehdd vnalwnlrea mfenqqdiar swgpddfada aaqmeasdea
      181 vedirngkfl ekareagean gkdleskvgr vstprvlmdg kdlevedind wvkvavask
//
LOCUS       WP_284571429             413 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284571429
VERSION     WP_284571429.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 413)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..413
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=45704
     Region          49..344
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mrgriraklr rfeltslpny aledvihipe gmrthpffli lrrfmlaaai vtgvaavvyi
       61 gqdgynekln lidalyysti sltttgygdi vpvttgarlt nillvtparl mflillvgtt
      121 lsvltersrk tfqiqqwrkh vhdhtiiigf gtkgqsamqa llddgtdvrn ivvvdperac
      181 lrvaeaqevv tvqgsgtksd vlkiagiera knvvvatnsd dtnvlatlsa remnkkakis
      241 aavrevenrh lllqsganst vvssetagrl lglststpsv vkmmddllsp segfsvaerp
      301 vasyevganp rhlsdivlsv irndrvyrvd mdetlelraq drllyirksd eterkkqnek
      361 remerlggka kqvkdkshre sksrevtdts gdchgrhide qrelkskesg gna
//
LOCUS       WP_284571463             292 aa            linear   BCT 25-DEC-2024
DEFINITION  indole-3-glycerol phosphate synthase TrpC [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284571463
VERSION     WP_284571463.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..292
                     /product="indole-3-glycerol phosphate synthase TrpC"
                     /EC_number="4.1.1.48"
                     /GO_function="GO:0004425 - indole-3-glycerol-phosphate
                     synthase activity [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30677
     Region          3..279
                     /region_name="TrpC"
                     /note="Indole-3-glycerol phosphate synthase [Amino acid
                     transport and metabolism]; COG0134"
                     /db_xref="CDD:439904"
ORIGIN      
        1 mttvlaadai vaeiladvaa rearvsfadi kalsrsvpsp rpvvsellrp gcsiiaeikr
       61 anpvphvhgg ndcvvradap rlldfdtvss ladvaglaqg faqagvaava cqteqlrfrg
      121 sledmatara assvpmlcrd iivdpyqvhe arffgadmvp lqvellaqar lvalvdries
      181 lgmtvlaevr speqaqcava agvkvvgina rglhsrhlnp hrfsaivphl psdvvriglg
      241 gvvsarevwr yagwgadavl vgealmaapr pavlardlva aglhpacpvw rs
//
LOCUS       WP_284571580             460 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284571580
VERSION     WP_284571580.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..460
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48536
     Region          4..460
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mtenmkvdvl vigfgkagkt iamkraaagd rvalveqssa myggtcinig cvptkalltd
       61 aeshhakptt ddaaafaeai qrrgtltskm nqanldlaeg kgvivvdgha sfisektvev
      121 tggddrmeit getviintga epvvlplpga dlervinstq aqqlderpds llivgggpig
      181 mefatyfakf gtkvtvvdtv dkpfanfdrd iaehvgtimd nlgitwitga qvtefrenga
      241 davttvwkdg dgneqtadta qvlvavgrkp atkdlgldka gieltergav avdkhlrtnv
      301 egvyaagdvn ggpqftyvsf ddhrvilsdr wgdgsrttdn rvvptttfid pplatvglge
      361 daareevear gntldvkaad ikdipimprp kilgkpegra kilveretdr ivgatllcvd
      421 aqelintlal amsaeipast vgggiythps ssevfnallg
//
LOCUS       WP_284571603             416 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284571603
VERSION     WP_284571603.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..416
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45503
     Region          1..411
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mkdivvigag aigmasafrl akeghnvtiv dpvapgskas shnagwvvpt msepvpapgv
       61 ltkamkwlwk kdsplyisps adwrfytfll rmlqhtsekr yaagtetliq lsketfstfd
      121 efvdegvdvg lefttmrtlf kdtsgmdarl delahfaenf pglsyrrmdd aelrdfhpkl
      181 sedvqggies rgdahldptk ftaalhkacq eagvefvasr awlrdrgsgk arvivdgafm
      241 dpdhvvvaag awtgevvkql gqrislqagk gygfdfpvrq gwltdtlymt dakvvatpmg
      301 dhvrvagtmg fseidesldh vraggilkgv qsffpdwpvn efdlepwqgm rpmtpdglph
      361 igalrkfpnv vvatghamqg islaprtaql vsgviagetm pdwmtkihpe rftrlg
//
LOCUS       WP_284571612             464 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284571612
VERSION     WP_284571612.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..464
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=48803
     Region          1..463
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mhltvfglgy lglthaacma eaghevlgvd iaparvaqlq aarvpfyepg laelvargve
       61 sgrlrfscdy rqaaefaqlh fiavgtpera dspaadtsav eavvdqlapl lrgkhvlvgk
      121 stvpvgtaar lqeraanisr atvdilwnpe flreghavad tlrpdrivvg tgaestpngv
      181 ssapalqklr evyraplerg tpflvmpwas aelvksaana flatkisfin aiaevceavg
      241 gdvaavaeal gyderighqy lgaglgfggg clpkdvrafr aradecgagd alaflgqvel
      301 inarrrqrvv qlaselvaqs pkvaqpskva epagsarpgl sgavitvlga afkpnsddvr
      361 dspalhvaae lalrgarvrv cdpqavenar rvypgleypa sladgvagad lvilatewpe
      421 yreldpvwaa elvaepvvld arnaldlarw rsagwqvhgl grgs
//
LOCUS       WP_284571617             246 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284571617
VERSION     WP_284571617.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..246
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25801
     Region          11..243
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(29..30,32..33,36..37,74,78..79,82..83,107,111,118,
                     121..122,127,142,146..147,149..151,153..154,157..158,
                     161..162,181..182,184..186,188..190,192..193,195..196,200,
                     203..204,210,212)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(145,149,152..153,155..156,195,198..199,201..206,
                     209..211,215,217)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mkqstastaq vpvgkpmhfl hpltviiigv sawvaalsis wpllhaalia lgwlagiags
       61 rslavpatsi alsipaglsm llvhaphgeh qiaplltsdg lvtagelalr fcalmtslla
      121 amanvhipdl lkalqhvglh hsvvyvlgas lqllpqasal isevaaanrl agrkvtlttv
      181 iprmiipvit rlltrgadrg ialqgmgyda pgrrtvlypv rahrweillr lifpaaaigl
      241 vvlawi
//
LOCUS       WP_284571663             325 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Corynebacterium propinquum].
ACCESSION   WP_284571663
VERSION     WP_284571663.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..325
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34487
     Region          2..319
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(40..41,45,118,122,125,143,146..148,167..168,172,187,
                     210..211,232..236,257..260,307,309)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(130,225..226,239..244,252..259,262..263)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mkaiqieqtg gpevlqlaev aapepsdgqi lvdvlvagvn yidtyyregi ydaetpftpg
       61 fegvgrvrhd pqgeiapgtm vawntafgsy aeqvcvdrdk vvavpndfdl ptaasmllqg
      121 itahylthgv yelgegdscv itagaggvgl vatqlaaaag aivytvvssa ekeqlsydag
      181 atrvlrygpd lveqvrdltd grgvdvvydg vgkdtfaqsl dmvrgrgvvc lfgaasgpvd
      241 pinpqvlnqk gsifltrpsv agwtsregef qmraqavvqa vvdgdlrfrv snsyaledaa
      301 qahrdlqnrk ttgsivlrvq edeya
//
LOCUS       WP_284571868             350 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Corynebacterium propinquum].
ACCESSION   WP_284571868
VERSION     WP_284571868.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..350
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38477
     Region          36..345
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 malekdsply ispstdwrfy tfllrmlqht sskhyaagte tliqlsketf stfdefvdeg
       61 vevdldfatm rtlfkdtsgm darldelahf aenfpglsyr rmddaelraf qpklsedvqg
      121 giesrgdahl dpakftaalh kacqeagvef vasrawlrdr gsgkarvivd gsfidpdyvv
      181 vaagawtgev vkqlgqnisl qtgkgygfdf lveegwltdt lymtdakvva tpmgdhvrva
      241 gtmgfsgide slnqvraggi lkgvqsffpe wpvneydlep wqgmrpmtpd glphigalrk
      301 fpnvvvatgh amqgislapr taqlvsgvia ggtmpdwmak ihperftwlg
//
LOCUS       WP_284571781             295 aa            linear   BCT 25-DEC-2024
DEFINITION  indole-3-glycerol phosphate synthase TrpC [Corynebacterium
            propinquum].
ACCESSION   WP_284571781
VERSION     WP_284571781.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..295
                     /product="indole-3-glycerol phosphate synthase TrpC"
                     /EC_number="4.1.1.48"
                     /GO_function="GO:0004425 - indole-3-glycerol-phosphate
                     synthase activity [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30735
     Region          9..274
                     /region_name="TrpC"
                     /note="Indole-3-glycerol phosphate synthase [Amino acid
                     transport and metabolism]; COG0134"
                     /db_xref="CDD:439904"
ORIGIN      
        1 mvttaltakd ivagiladva arearlpfad ikalsravpa prpvapllsq pgcsviaeik
       61 rakpaarydd afgtcatgag htdslidfga vdtladvasl ahdfesagvv viacqterlr
      121 frgsledmat araassapml crdiivdpyq ihearffgad mvplqvelle qarlealvdr
      181 ieslgmtvla evrspeqacr avsagvsvvg inarglesrt ltpdrfaaiv phlpesviri
      241 glggvlgare mwryagwgad avlvgealms apnpaatara lvaagrhpac pavrg
//
LOCUS       WP_284571951             103 aa            linear   BCT 25-DEC-2024
DEFINITION  FluC/FEX family fluoride channel [Corynebacterium propinquum].
ACCESSION   WP_284571951
VERSION     WP_284571951.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   McIlwain,B.C., Gundepudi,R., Koff,B.B. and Stockbridge,R.B.
  TITLE     The fluoride permeation pathway and anion recognition in Fluc
            family fluoride channels
  JOURNAL   Elife 10, e69482 (2021)
   PUBMED   34250906
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Li,S., Smith,K.D., Davis,J.H., Gordon,P.B., Breaker,R.R. and
            Strobel,S.A.
  TITLE     Eukaryotic resistance to fluoride toxicity mediated by a widespread
            family of fluoride export proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (47), 19018-19023 (2013)
   PUBMED   24173035
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Stockbridge,R.B., Robertson,J.L., Kolmakova-Partensky,L. and
            Miller,C.
  TITLE     A family of fluoride-specific ion channels with dual-topology
            architecture
  JOURNAL   Elife 2, e01084 (2013)
   PUBMED   23991286
  REMARK    Erratum:[Elife. 2013;2:e01700]
            Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..103
                     /product="FluC/FEX family fluoride channel"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:1903425 - fluoride transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:1903424 - fluoride transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=10752
     Region          17..102
                     /region_name="CRCB"
                     /note="CrcB-like protein, Camphor Resistance (CrcB);
                     pfam02537"
                     /db_xref="CDD:460582"
ORIGIN      
        1 mnldisltea llstasvaag afaggllrgl lsklrgrytg tacsnmlacf algimlarvd
       61 lgalvhlpyw eiafgtgfcg alstlatlar elgnltyera wir
//
LOCUS       WP_284572023             372 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium propinquum].
ACCESSION   WP_284572023
VERSION     WP_284572023.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 372)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..372
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=38747
     Region          27..368
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 msadntpath gtpqsgtvlp efthgyrrlv irnqwvslhf ptrvlvtalg llllaligav
       61 aaitlgeypl slgevfsalf srgggfdtti mrewrlpiav aavafgallg iggaifqslt
      121 rnplgspdvi gfdagaytav vitmlvvgas nfwaiagasi vggiitalvv yllawrkgvq
      181 gfrliivgig vsamltsins ylitradvee giqvgfwaag sitkvtwqgl vptmllgiiv
      241 viaaagysra lrhlelgdda attqgfavnr arlglivigv attalvtaaa gpisfialva
      301 pqiarrimrt agvsllgaaa mgatlltgah ilslviatfy rqipvglitv vigglymlwl
      361 llrestrryg tg
//
LOCUS       WP_284572100             319 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium propinquum].
ACCESSION   WP_284572100
VERSION     WP_284572100.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..319
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=34498
     Region          143..301
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 msssrnafqr kpallwtlia lvvalavlvv vavvrsgddd spsasdqdav hgpqapdsan
       61 sgstskssan sgsdaashdg eyspekarel aekvepgtnf aqpkspdatv igpgkeitsn
      121 ddilnvhrrn aedpfamgal dapvvlsefs dfecpfctrf avetapklke kfvdtgllri
      181 ewndlpvngp haetgaqagr aagnqgkfye fhdvlynnty dnqtgghpgy diadyvrfae
      241 eagiqdleqf rseieneqyr dvvrqalhya ssigmrgtpa filgdrfisg aqpyevfede
      301 vyrqlakvad gtvprpetq
//
LOCUS       WP_284572160             516 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium propinquum].
ACCESSION   WP_284572160
VERSION     WP_284572160.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..516
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=55587
     Region          35..454
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mtlrqdrpaq asttmpagav detsarnkrg arkpnalval lrrlhfyagm figpflliaa
       61 isgalyavap taeklvyqdv ltvtpppgse gvintislee qvtqaheafp dldiaqvwps
      121 sepgettrvl lidetideae lrsvfvnpyt gavvgdepsy sglgelplrr wishlhesmh
      181 lgpvgelyse laaswlwffa lgglvlwasr nkkvqqlfgf gnartgkeak nkgsgrrrlv
      241 nlhgvtgtwm ligmlalsvt gitwstyagg nvnrtvealq wradpittel sgesteaadp
      301 haehaghggg aasesearaw tpeeiaeqsd qvlatareeg ltgslrmypg esvehgwqas
      361 erwtewrtts daisvdgetg evidrlpfse lplfskltsw giylhmgimf glplqilllv
      421 talaiaglvv lgyliwwkrr ptpgatagip gprtklstkq wiivavflva vggflplfgi
      481 slaamlladv vlskraghaa haghetrraa vdgara
//
LOCUS       WP_284572178             259 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Corynebacterium propinquum].
ACCESSION   WP_284572178
VERSION     WP_284572178.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..259
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26982
     Region          8..243
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mpipvklprt faqqlqqesg pqvgawissg spvaaeivas agfdwllvdg ehspysletv
       61 tdllratday gatrvvrvpv gdtalikqyl dlgaqnlmvp mvdtaeqard avaamhyppr
      121 gvrgvgaala rssrwnaved ylqnasdlvs ltiqlesvta vdnaaeiaav dgvdqlfigp
      181 sdlaasmgvl gqqthpdvld avsramkacq dagkpvgvna fnleqaqayl dagasfvlvg
      241 advqllagaa rgladkfvk
//
LOCUS       WP_284572376             333 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium propinquum].
ACCESSION   WP_284572376
VERSION     WP_284572376.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..333
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=34455
     Region          25..332
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mapsgnnsaa tasvdkvatn tagvsvddpv fadirllnhp rlrpdrqprl avgvkgeyvp
       61 akrspvvlad galplarmca qdavvaptai fgrreklaqf aadypgewda ivaaeipvyd
      121 vpaallrevv gfdlhrglls vaprpaipdl qqlsgratsg peissasgil hgartvvile
      181 gvgdpdniga ifrsaaslga dailvgagcs dlwdrrvirv slgqalrvps iriaggpndw
      241 hhglaglqeg gfhvvalspg hgsvelrqsl vhddgtgrek vafllgaegp glsshamaaa
      301 dsravipmaa gadslnvatt aacclyerwr ard
//
LOCUS       WP_284572599             405 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Corynebacterium propinquum].
ACCESSION   WP_284572599
VERSION     WP_284572599.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..405
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42908
     Region          3..392
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mklddlatqr leswkqqgll rtpvefagpq drrarlhghs dkrillsssn ylglathpev
       61 iaaarsalet fgagsggsrl ttgsttwhrr veedlagfvg fddavlfatg yqanisvlqt
      121 latpdlqifs dslnhaslid girlagasga qkniyphldy aaleqqltks tsphklvvsd
      181 gvfsmdgdia dlavlreicd rhgawlmidd ahgigtvgkh gigaievhat rpdilivtas
      241 kalgaeggfa acstpvahml rnqargyvys tacsapncaa isaalriiqq pltdhhpvvr
      301 lqqrvaalrt iagtrsngsd svsgdspiip lpvgaesaam elaaalaqrg fhvpairypt
      361 vargqailra tamatleldd iaefgttlkn lgwrrrdaag tkpkn
//
LOCUS       WP_284572593             505 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Corynebacterium
            propinquum].
ACCESSION   WP_284572593
VERSION     WP_284572593.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..505
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=57981
     Region          5..504
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mstpqpalmw frddlrlrdn saldwiaqqg pviavvieed pettrtrelg aaarwwwqrs
       61 vhqlknslaa hgvpllyysg dpreiipaiv eefgvsavgw srryheplre ldaeikqmlh
      121 ergvtarsfa ghlltepwev ltqqgkqykv ytpfaktart iaevnvasyl nnvndqapsp
      181 tghdelspig lagpgtdfpa ssplpdwnep dwthtlaqhw lpgenaawki aeefldqlaa
      241 aarkqaphya adrdrldkqa tsrlspylrf geisihrlwa lvteasntgr iagedasafl
      301 nellwrdfaw hrlyhlpelh rrnvrqqfdh fdwhwdetea qrlsttrrdp rcaeatedlp
      361 tddfrrvfsa wragqtgiav vdagmrelwe tgtmhnrvrm vvasfltknl gihwrhgeaw
      421 fwdtlvdadp asnpfnwqwa agcgddaapy frifnpdsqa krfdphyryi rhwvpefgtp
      481 mypqplvdlk esrrqalaay devkn
//
LOCUS       WP_284572743             369 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium propinquum].
ACCESSION   WP_284572743
VERSION     WP_284572743.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..369
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=38154
     Region          14..365
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mtnsphllsr pvvpgrpalr kgcvslvwrp wvlfstismi caaviifaas iaigdypltv
       61 pevlriiflg dgsrieriav fdwrmpralt altvgfalgl agaltqsvtg nplaspdilg
      121 itsgasaaav tvltfgggvg afaavagkva tfglplaala gglitgavvw ilssrgsfda
      181 yrlvlfgiii talmnayigf lmtraelrda ataqqwlags lnstnwdrav pvalvilicv
      241 plfawmaytl taavlgqdla aalglrvsrt qltflviavt lasiavaaag pigfvafvap
      301 qlavritkls tpplvasafm gailllgadl vvrtnipvdl pvgivtsafg gvfllyllis
      361 snlkrsrss
//
LOCUS       WP_284572944             239 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium propinquum].
ACCESSION   WP_284572944
VERSION     WP_284572944.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..239
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25424
     Region          76..221
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mskkvtnpnq kssagfigai aavlaivvav iayiviagqg akaekfanwe ikqvsaetsf
       61 dgntltfgaa dkaphvdlye dfscphcahl aeatdaeale einagnlavs ihpmtfldnq
      121 gdghstqava allalaehdd vnalwnlrea mfenqqdiar swgpddfada aaqmeasdea
      181 veeirsgkfl ekareagean gkdleskvgr vstprvlmdg kdlevedind wvkvavask
//
LOCUS       WP_284573041             406 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium propinquum].
ACCESSION   WP_284573041
VERSION     WP_284573041.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..406
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43997
     Region          44..163
                     /region_name="Creatinase_N"
                     /note="Creatinase/Prolidase N-terminal domain; cl46291"
                     /db_xref="CDD:480631"
     Region          46..405
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 msshnnstaa dsaadasaes aagaahaaah stynpvtadh frarlakaek ivaeqnlagf
       61 lvspgpefqy ltgstfsshe ratflvlrag kdpvavcpet dvltlqqenl delgfrfeaw
      121 rdgqspyeit rrlleenseh kavavanamt adhvlrldaa lpnhsielgs damsqlllak
      181 geeeisqlaa aaaaidrvhe qvpallrdgv terevadklh dlilqehhsi dfiivgcgen
      241 ganphhsfsd rvlhtgepvv vdlggafgdg yrsdstrtyv vdgavdkapq efrdayevvt
      301 rafhaareva kpgataesid raareiitea gygenfshrl ghgiglsthe dpfylegnkq
      361 qvqegftfsi epgiyvegkw gmrledivvl eadgprhlnq qprelr
//
LOCUS       WP_284573064             436 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Corynebacterium
            propinquum].
ACCESSION   WP_284573064
VERSION     WP_284573064.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..436
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=48895
     Region          238..340
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mgnirkiidg svasifggwl vatllsqhpe snldrirrld drfgntiipn wkffapnpav
       61 edvhvlyrlv sedlseyspw eechtisprk msqafwfprr rfekgifdth qalvvglasl
      121 gkgeendavl rrsisdtaem lnnyirhnyt rsiskteknw ywqqlmlvrf aghdgaakpi
      181 ydlilnyqai nteqdsnisp afycddyfne yydevmktvd pnvdhaewis aavsgqlpqr
      241 ildigagtgr vlaqvasrfp naklfaiepd ekfsqsfadi danffsgtve eaftaeatmd
      301 idlafvtygs lqyisslsel teslktvrrm mtrggiiave lfaseiyhap vqpspmslkl
      361 geephtisms slqyphgiva vttqikrqsd gktgvmkecv fpvtrqeave alhaagfssv
      421 qvnlkgaylr ctaknm
//
LOCUS       WP_284573140             120 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_284573140
VERSION     WP_284573140.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..120
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          <5..100
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 sqpgrnvrak sglnrsildq gwyemrrqle ykqlwrggqv lavppaytsq rctccghtak
       61 enrlsqsqfr cqvcgytana dvngarnila aghavlacgg mvqsgrslkq eptemiqata
//
LOCUS       WP_284573194             282 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase, partial [Corynebacterium
            propinquum].
ACCESSION   WP_284573194
VERSION     WP_284573194.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         <1..282
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          <1..259
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 thplaaaita atpqaptaqq vseaagqgit gildgsriav gsprwlspgp lagqvetlee
       61 qgmtvvivhr ddrpvgavgv rdelrpetpq viksladegf gitmltgdnt rtatalarea
      121 gitdvraelr pedkatavag lgtrgpvami gdgindapal asadigiamg akgsdaaies
      181 advaftgddl rlipralhha rrgraiinqn iilslaiiiv llplaitgvl glaavvlvhe
      241 vaeviviang lraartqhpd lkpveaatvt adedadgrsr vs
//
LOCUS       WP_284573310             319 aa            linear   BCT 25-DEC-2024
DEFINITION  S1 family peptidase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284573310
VERSION     WP_284573310.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Perona,J.J. and Craik,C.S.
  TITLE     Evolutionary divergence of substrate specificity within the
            chymotrypsin-like serine protease fold
  JOURNAL   J Biol Chem 272 (48), 29987-29990 (1997)
   PUBMED   9374470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475742
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..319
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32794
     Region          1..233
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
     Region          <226..>296
                     /region_name="PRK10263"
                     /note="DNA translocase FtsK; Provisional"
                     /db_xref="CDD:236669"
ORIGIN      
        1 mrkivalaaa sllgvtgtsg vlgagtaval tngtpvsped etatgvvqva sctgtvvapq
       61 wvltaqhcve vpnlqrtvyt gttreqqhre enkftsdyav waphgdvalv hvtdalpqrl
      121 vrevrrtpvs fgeqgrvygw gagtgetlqy araavgktss gvrpqenqhg aflvqyldea
      181 tagrgdsggp lfidgkvagv tsfkapqggg ryslfaslhg lgdwiaqtta apaqpstdna
      241 pvetaphhng pvakpeqpst esvppvakpk npnsknpqpq nsqaqnpqse qprgpqatpg
      301 rggtgtggag gsslglssy
//
LOCUS       WP_284573359             180 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284573359
VERSION     WP_284573359.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..180
                     /product="YceD family protein"
                     /calculated_mol_wt=19134
     Region          1..180
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mtspfvfdvk alltqqqgpe qithtgpapr rigaemlaie egaevtvdav lhslgsgvma
       61 dagvsavlrg ecsrclsple rptefrisqv faaddefisg daeddedags gdeipqvshe
      121 dtidllqtvt delvvalpfn pvcedgcpdd vptpapdgvs geeteervdp rwaglekfrd
//
LOCUS       WP_284573632             391 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284573632
VERSION     WP_284573632.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..391
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42679
     Region          29..148
                     /region_name="Creatinase_N"
                     /note="Creatinase/Prolidase N-terminal domain; pfam01321"
                     /db_xref="CDD:460159"
     Region          31..390
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 msshnnstaa dsaanstyip vtadhfrarl akaekivaeq nlagflvspg pefqyltgst
       61 fssheratfl vlragkdpva vcpetdvltl qqenldelgf rfeawrdgqs pyeitrelle
      121 ensehkavav anamtadhvl rldaalpnhs ielgsdamsq lllakgeeei sqlaaaaaai
      181 drvheqvpal lrdgvterev adklhdlilr ehhsidfiiv gcgenganph hsfsdrvlht
      241 gepvvvdlgg afgdgyrsds trtyvvdgav dkapqefrda yevvtrafha areaakpgat
      301 aesidraard iiteagygen fshrlghgig lsthedpfyl egnkqqvqeg ftfsiepgiy
      361 vegkwgmrle divvleadgp rhlnqqprel r
//
LOCUS       WP_284573650             458 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284573650
VERSION     WP_284573650.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..458
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=48277
     Region          1..457
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mhltvfglgy lglthaacma eaghevlgvd iaparvaqlq aarvpfyepg laelvargve
       61 sgrlrfscdy rqaaefaqlh fiavgtpera dspaadtsav eavvdqlapl lrgkhvlvgk
      121 stvpvgtaar lqeraanisr atvdilwnpe flreghavad tlrpdrivvg tgaestpngv
      181 ssapalqklr evyraplerg tpflvmpwas aelvksaana flatkisfin aiaevceavg
      241 gdvaavaeal gyderighqy lgaglgfggg clpkdvrafr aradecgagd alaflgqvel
      301 inarrrqrvv qlaselvaqp skvaepagsa rpglsgavit vlgaafkpns ddvrdspalh
      361 vaaelalrga rvrvcdpqav enarrvypgl eypasladgv agadlvilat ewreyreldp
      421 vwaaelvaep vlidarnald larwrgagwq vhalgrgd
//
LOCUS       WP_284573695             376 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284573695
VERSION     WP_284573695.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..376
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39209
     Region          63..370
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtqnsnkttt apsaaraatt arhrrenpra pqqhhdvfaq rhrlrvgtfv alivllvgsv
       61 llstalgqyy lslpdllsil tsgpraetdi aasvvwdirl priflgflvg aalgvagclm
      121 qavfanplae psivgvtsga gvgaalvivf evsflgtftv paaafltsli vtaiiyrlah
      181 nrgkvavvnl iltgiavnav cgalisfmvy lapttsreqi ifwqmgslng sqwkhvwvvl
      241 pivivgfaia srlgaqldvl algekaaght ginvaalrmv aivasavlta aavsfaglig
      301 fvglivphvl rtivgpenki llpasalaga llialadvaa rtlipfadlp igiftalvgg
      361 ptffillrrm mrkgsv
//
LOCUS       WP_284573698             415 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284573698
VERSION     WP_284573698.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..415
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45381
     Region          157..263
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mtdrkrgakr srkhgteqnt gqstesftes vsnsltrlkn slrrhlsqqw teltspsfsv
       61 pasklpepla hhatevsast ipesvvaeia eslnlrgkhd hhhaatdqes enapepedgp
      121 qtaeksdynf dssrhlplga rfkprgvfed dwsarpsadk pwpvilihgt vdtkgvwqel
      181 gtelradgwc vfapdygkrg taameesavq lgayieavrt itgaeqvili ghsqggllar
      241 ywmrtsgqar yvkhlvslga pnhgttmggi lsplvtnnlt enimhsliqh wfgpvgfqqi
      301 tgseifavfn ngaddrdgdg nsddssgtnt hgssgeledg vdytciasrq dtvvqppetc
      361 flngpadqvr nvwvqdiipr anvqhqdlpm nkhvraiirt glkkganeen lkhki
//
LOCUS       WP_284573911            1175 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284573911
VERSION     WP_284573911.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1175
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..1175
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=124999
     Region          244..390
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <646..1119
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 msvkstsprn prgggernka ranstrpapr tgpgraagkk lspgmsgktg gdpaksreen
       61 sdsanletvv fgsaqraant shertgsafr avgsgiataf sktsdalkrf gnigqadddy
      121 deyadyddli ddadtdagat emgrktadkn kklknspagl dedlysadmt gkkakakkgq
      181 rssgamaqsr gkrrstdthv sdddldqhgd dahaeqtegd evaasesalp aakpevgvps
      241 srsdaialtl igvaivlgas vwldiagfig raiatathav lgagafiipv alviaasalf
      301 sgrrvavehr arvsigttli vismlglihl fsgapaewpe rfvaggalga wtggalaagf
      361 spyvavpllf lviiygalkv tgitvkefte ylrnvisgns sknldadpdr esvgghneyg
      421 daygrandei aaiasgaqrt prrraplrtn pvashsnrqg ftttqssnag thdvvanrkk
      481 stglfprteq ppqvehtevl ysndsrehqe qvsktaagle naptasdtde fpavldsptr
      541 srsartepev ekteqlplap edavdqaqsg lqqkqaaenp rtvdtkhldt aretrvpgvk
      601 pqsdarqpva qqatqvdlas qindgpredt gatqqaskla teytipsagl lepgrapktr
      661 teindrtiea idacfaefkv daqvtgftrg ptvtryivel gpgvkvskit nlqsnlayav
      721 atgsvrilap ipgksavgie vpnsdreivr lrdvlesevi agdedptlvg lgkdiegefi
      781 sssiqkmphl lvagstgsgk safvnamlvs lltratpddv rlilvdpkmv eltpyegiph
      841 litpiitqpk kaaaalqwlv eemeqryqdm rsarvrhikd fnhkvrtgev qapagserkm
      901 epypfivcvv deladlmmta pkeieesivr itqkaraagi hlvlatqrps vdvvtglikt
      961 nvpsrlafat ssstdsrvil dqtgaeslig mgdglfipqg grpvrmqgaf vsddevyavv
     1021 eaakeqgepd ytegvtedkq aeakkaiddd igkdmddlle avelvvtsgl gstsmlqrkl
     1081 rigfakagrl mdlmetrgiv gpsegskare vltkpeeldt tiwmikgadp adaprevqeq
     1141 qnqgqpdnvv edsagdtdgs ahitkatynp tsqaf
//
LOCUS       WP_284569790             439 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Staphylococcus
            warneri].
ACCESSION   WP_284569790
VERSION     WP_284569790.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus warneri
  ORGANISM  Staphylococcus warneri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Staphylococcus warneri"
                     /db_xref="taxon:1292"
     Protein         1..439
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49879
     Region          1..436
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mkltiyhtnd ihshlneyar iqsyltehrs klqhpslyld igdhvdlsap itqatlgkkn
       61 iellneakcd iatignnegm tishealqnl yinaqfevic anvfdeegrl pnriassyik
      121 eidgvrilfv aatapftpfy raldwvvtnp lesikdeika ndgqydvliv mshvgvffde
      181 klcqeipeid lilgshthhh fdhgqmnngv lmaaagkygh ylgevnltie nksitrktac
      241 lhpletlpev qtnfdeegka mmrtpvvnhp lkldnktdvi tktsyllaes vyeftnadct
      301 iinaglivkg ieadeitefd ihrmlphpin vvrvkltgee lkevivksqk qeymhehaqg
      361 lgfrgdifgg yilyrlgfie segryfidgk eiqndehyil gtvdmytfgr yfpslkgllt
      421 eyimpeflrd ifkqkllef
//
LOCUS       WP_284574031             213 aa            linear   BCT 25-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284574031
VERSION     WP_284574031.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..213
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=21986
     Region          8..>126
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mtttattakd lfltamdrrf apevgqgdls lalagaelld llgaraltld gdrvvpgaaa
       61 algdglldea saalvrqppy eqvedwlwrr grglaaayrr aleadgglsa rrsgrlglga
      121 vrvepvdspa reraaarlea aepvlgalaa aigigiaadt eagqaavpaa aaledepvtt
      181 vlaavmdavm eleavrrrrs ieeaafaniw rap
//
LOCUS       WP_284574067             125 aa            linear   BCT 25-DEC-2024
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Streptomyces sp.
            2P-4].
ACCESSION   WP_284574067
VERSION     WP_284574067.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..125
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=13060
     Region          1..123
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mrtrpvlvyd gdcgfcttsa rfaerrvrpr cdvvpwqsad lgalgvsrdr aayevlwvtp
       61 sgavhggara vakallsagg awpvlggvlg lpgvrraada vyrvvaanry rlpggtaaca
      121 lprdr
//
LOCUS       WP_284574028             348 aa            linear   BCT 25-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284574028
VERSION     WP_284574028.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..348
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37118
     Region          8..341
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 marriedlri gfighgrhar anlypalgla ggrltsiatr draaaaraaa lhgaarghgd
       61 hrrmlaedgl davfvsvape dqaavtedcp ragahvfaek plgmdeaear rvadtaeqag
      121 rsvavgfmkr hapayrrlag lmadeaafgr vlsfhaffaf spwtdtlrdd tylkfgavhm
      181 vdlvrwlfge vaevsgltns rgsdismaat lrfrsgvvgs ltlagvpaws reqeeltvtg
      241 qrgfarvenl savayhharr agagrgeawq eldedtvvvr svnspasggh qdlylrgfag
      301 evrhfleava ngtpqaasaa dntatmalcd ellrslrpag rtgrgpnl
//
LOCUS       WP_284574271             463 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces sp. 2P-4].
ACCESSION   WP_284574271
VERSION     WP_284574271.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..463
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49241
     Region          14..414
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mpeseleslk rsgrivvvga slaglraaet lrekgfkgtl tmvgdepyep ydrpplskqv
       61 llgmaraent alprrraiea ewrlgvpasg ldmagrrvkl adgdevpydr lliatgvrar
      121 pwpneaegel dgvfvlrtra dgaglarrle agprrvlvig agftgseias acrerglevt
      181 vaeradaplv galggvigav aagmhrehgv dlrtgvmvtr legdaggrvr aahlsdgavv
      241 ecdvvvvclg aqrntewlag sglgagprgi acdagcrafg itgivtddiy vagdvarsph
      301 plfgyqflsl ehwgnavsqa etaahnmlsn sagrrphiwv pafwssqfgv nvksvgvptm
      361 gteimitqgs lgerrfagvy gyqgriigav tfdnarwldf yqrqieatap fppeftnvdr
      421 rpegsrpvpa efpdpsipth gptvtlsgys padrrmtftp agn
//
LOCUS       WP_284574266             346 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces sp. 2P-4].
ACCESSION   WP_284574266
VERSION     WP_284574266.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 346)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..346
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37453
     Region          <282..337
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 misfelgved lahtrfalsp lgetvlslrv lrdpgvsvlh lpwrrsvlar iaglgggldt
       61 glllslvadl ltlpdfltpr pavfephfed elavvrstpp drvrrdllaa haphplpapl
      121 haatapgdgp vtalrdtvce llhryweiai rpvwpqirlv aeadmtyrar qlarggarll
      181 fadmhpqlrw edagsrgflr vhrtiggyea kacgrglllv psvfahkcap pvcpdeppsl
      241 lypsrgaatl weaepepvlr ngadaagraa gdalvlllga prarllrmla epaataelar
      301 rlrvtpsavs qhlrvlhaag latrtrhgrq vlyrrsrlgd rltagg
//
LOCUS       WP_284574306             387 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284574306
VERSION     WP_284574306.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 387)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 387)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 387)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10543770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..387
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41037
     Region          99..242
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
ORIGIN      
        1 mtttatqepp aparqtlpae eryadelafl aaqdtgprpp gwaltpravv tfvcgsdgee
       61 ltlrgrrtgl pakmkiapkf vgeralverc vvtlagergl lltgepgtak smlsellaaa
      121 vsgtssltvq gtagttedaf rygwnyalll aqgptpqalv dspvvsamrt grvvrveeit
      181 rclpevqdal vsilsdrrvs vpeltateda vvsaapgftv iatanlrdrg vsemsaalkr
      241 rfnfetvdpi adadaeatli rrqavaavqr agasfgvdda vldalvtvfr dlrsgrsaeg
      301 wdverpgtvm staeavqvaa slgvaaaylp ggdvldllpg hllgvvrkdd padhgrllgy
      361 wdgpvrrrae dgsamwrrlw dlrgslr
//
LOCUS       WP_284574404             327 aa            linear   BCT 25-DEC-2024
DEFINITION  1-phosphofructokinase family hexose kinase [Streptomyces sp. 2P-4].
ACCESSION   WP_284574404
VERSION     WP_284574404.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..327
                     /product="1-phosphofructokinase family hexose kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008443 - phosphofructokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33385
     Region          16..322
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 mstgagpdas aagpdvvtlt lnptvdlcwe vdrleytgkn rarvrsvaag ggginvarhi
       61 arfgaratav htaggevglr ltrlldeegm hhvavgiaed trealvlfet vsrrschvvp
      121 pgpqlregeg erclealerf lggrpyvvas gslpgglpdd yyatvarlvr eagarlvldt
      181 sgpalragla egvflfrcnr teaesltgrp vdsfddaral nghllatgaa eiavttlgal
      241 gavcstgngh telhapplpg eplsdagagd smvaaltael aggadpvgac tlgvataaaa
      301 mltpstesfd vrvarslrgq vravsrg
//
LOCUS       WP_284574510             348 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284574510
VERSION     WP_284574510.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..348
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35851
     Region          35..340
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mdrqrtqqvl rtrnrnrvll fvvlvfvlvs gtiaslvigq ytipigelpr ilavgplgvs
       61 amdesviwqi rlprlvlgll vgaalgvgga lmqavfanpl aepsvigvta gagvgaslai
      121 vlgiswfgat tvpvfaflsg llttwlvyql arfggrirvi nlvlvgiavn avagalisff
      181 ifiaptssre qvvfwqmgsl sgakwahisv vavlvgagia lalllvgkld vlalgdraag
      241 hvgidvarlr vlalllatll tagavsyagl igfvglvvph iirtvagpsn vvllpasalg
      301 gaalivladt aarsiidfad lpigiftalv ggptffillr ammrrgav
//
LOCUS       WP_284574515             177 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF1990 family protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284574515
VERSION     WP_284574515.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..177
                     /product="DUF1990 family protein"
                     /calculated_mol_wt=19068
     Region          3..160
                     /region_name="COG4762"
                     /note="Uncharacterized conserved protein, UPF0548 family
                     [Function unknown]"
                     /db_xref="CDD:443794"
ORIGIN      
        1 mtrlsgaarp altypergat aslplpdryh hlrhrirlgr gravfeaaga alttfgahra
       61 agaavrcghg avrpgsrvav glgwgplrie apcevvwtay epartgfayg tlaghpeege
      121 esflvlldrd gsvwfevtaf srparwytra agplvplfqr cyarrlgral rrlaapa
//
LOCUS       WP_284574526             529 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Streptomyces sp. 2P-4].
ACCESSION   WP_284574526
VERSION     WP_284574526.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 529)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 529)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 529)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..529
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54657
     Region          52..503
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mhstdpvaaa dpavrpagat apagrlragr rppaalllpa alaavfallp lgylavrsle
       61 rgpafawdai adertaqllg rslglaavvv saslvlgvsl awltartdlp gartwavlvt
      121 lplavpsyva aftwlsvfpg lagfggsala ltlvsfpyvy lpvtavlrga dpaleevsrs
      181 lghgplrtfl rvtlpqvrpa aaggsvlval yvfsdfgavs lmrydtftrg iytsyrasfd
      241 rtpaaalsvv lvvmtillva aeartrgrag qartgtgtar paapaplgrw rmpaltwcta
      301 vaaiavlmpl atlgywlavg nsatwdpaal ldtagttlgv aaagavlttl lalpvgviaa
      361 rhrgrtahll eqsayaghal pgitvalslv ffavryadpl yqelpllvca yavlflpvsv
      421 aatraavlqs ppvledvars lgrsplrvlr eitvplaapg vaagaaltfv vcmkelpatl
      481 llrptgmdtl atrlwtetgt gsfaaaapya aalillaaip syllgrhrt
//
LOCUS       WP_284574575             477 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Streptomyces sp. 2P-4].
ACCESSION   WP_284574575
VERSION     WP_284574575.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..477
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50895
     Region          10..413
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 msmgtkggeh avvlggsigg llaarvlada ydrvtvidrd dltgagmglr paiswahhih
       61 allergrtii edlfpgfldd llalgvpvgd fgmtchyyfn grmmvpaetg macvaanrpv
      121 lenrirtrva alpgvtlrer tdilglvass drrritgvrv qgrdpddgga pgaeeaidad
      181 lvvdatgrat rtprwlgelg yerapeerir mdltyttmdf tgplpfdplg ddialvptat
      241 palprgaifa rladryaltl tgilgdrapt dregflayaa slpvpqihea vrdaeqrgpa
      301 hsfrfpasvr fhyerlsrfp agylvlgdaa cifnpvyaqg mtvaamgatv lakhvgkgae
      361 prsadyfrdl srvidapwam saaadlgypa vrgrrtvatr manlymprvq aaaahdpvva
      421 rgfirtaslv dppqslmrps mvgrvlfgrk paapaapaap aapaaprvpa psseepr
//
LOCUS       WP_284574529             383 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284574529
VERSION     WP_284574529.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..383
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40516
     Region          51..360
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mgrepglpvv ivaglhaear aevvdrllna vpgsvalhhd lagasdgtvl rlirdaagtv
       61 srgetplvnd caccalredl vpelerladg gltrlavvel wdsvepkama eviaghggdr
      121 ltltnvitav dpalvlpclv ngddlseagl aaaatdqrtv gdtwarqley apvlavvdnd
      181 eaddedrall aqlhptarrv padsgelaea alagfdveaa aaaqhpacal lpqeadeagv
      241 ttfvwrrhrp fhperlyqal edlccaaars rgrfwladrp dtllawdaag galcvenagp
      301 wlaslpdaaw emvppmrraa aaldwhpdhg dccqhlvfts pgldrdglgr lldsclltda
      361 eyasgreawk hlpaafdall daa
//
LOCUS       WP_284574583             327 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284574583
VERSION     WP_284574583.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..327
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33819
     Region          22..326
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mrktwtiagi saaallvalv gsltvgsssm sfseliglvv psqpspsplr tsiltelrip
       61 rilmaafvga ilavcgvamq avthndlaep yllgvssgas tgaviailfs twqygiifga
      121 tigslasfal lmlllrntgg datkvvltgv ligflfqslt slvvtasgda estrsimfwl
      181 lgvlgaarwp tlfavmivgs igmlvlwals rhldalslgg dtastmgvpv ialryivlic
      241 vslmtattva svgaigfvgl iiphavrmln vpkhaslipl salvgavtlv iadafarsif
      301 apqelpvgvi taligvpmff lilrrkh
//
LOCUS       WP_284574653             305 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces sp. 2P-4].
ACCESSION   WP_284574653
VERSION     WP_284574653.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..305
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31865
     Region          44..287
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          200..283
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkptgrsaae lplhrlqvpq phllpfavgs fdaigplsra gfphrhtfhe iahvtggagr
       61 hvldlvpgpl appvlcvitp gqvhhwegae glagqvvlfh edflgghped aralrrlagr
      121 ptvplgahap rvaglvdame eeyralrsgy agvlraylhi lvveaaraae agappavpad
      181 rgdslaeafa kitarpggaq ltvaacarel gvstghlhaa vkqatgltpg glirraqtle
      241 akrllagtdm tvrqvaqqag fadpsyfcrf frretgltpg gfraglagnh hdpripsiaa
      301 pdsgp
//
LOCUS       WP_284574668             353 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284574668
VERSION     WP_284574668.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..353
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38341
     Region          51..309
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 masrrstrrr rvvravlaal aalavaaagl gglvvwqhty dlreeavtvr rdgrtldgvl
       61 alpeqgkgpf plvvfvhgdg pvdathdtfy rpiwesfara gyaslswnkp gvggspgdwl
      121 dqsmddraqe avdaiawarq rpdvdsrrig lwgasqagwv lpkiaaknpg irfviavspa
      181 vnwhrqgryh llaelrrdga sdaevaaalr rretglellg rgapyeeyvr avgdpqgmta
      241 arwrfvsknh tadasadlpa lrgvpvllvl aghdmnvdta dteaayrrll pgpalrvgry
      301 pdathglvrq dvensalrlt ltalcapral fadgfledqr kflasveteg ptr
//
LOCUS       WP_284574669             773 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284574669
VERSION     WP_284574669.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 773)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 773)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 773)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..773
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=80346
     Region          19..757
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mptprstssp ipapstaast ielnisgmtc ascaarvekk lnkhdgvhae vnyatekati
       61 tgdtdaldad aliatvektg ygaeltpest tagtqapqda maeaeldslr rrlivsavla
      121 vpvialamvp awqfdywgwv slaltlpvvv wagwpfhrat wqnlrhgsvt mdtlislgts
      181 salvwsmval ffgsagdpgm rhgfdftvsr gdglshiyle vaagvitfil lgryfekrsk
      241 rtagsalral ldlgasevtv lrdgaettin ineltvgdef vvrdgekiat dgvivsghst
      301 idtsmlsges vpveagpdda vagatinvgg gklvvqatkv gkdtqlaqma qmvedaqsgk
      361 asaqrladki sgvfvpivia vslltliawl lidgdwaaaf taavavliia cpcalglatp
      421 tallvgtgrg aqmgvlikgp evlehsrgid rvildktgtv ttgvmeladv vtaegfdrde
      481 vvhlagsleh esehpigrai araatnqrad gtlsevsdfe sirsagvrgv vegrrvavgk
      541 psladnadlg alqqpflsaq tqghtalvvl vdgtpaavlm vadqvkttsa aaiqqfhelg
      601 ietmlltgdn qavaetvaae vgiehvraev mpedkvavia dyqdrgykva mvgdgindap
      661 alaqadlgma mgtgtdvame saditlvrgd lraatdairl srrtlgtikg nlfwafaynt
      721 aaiplaalgl lnpmlagaam alssvfvvsn slrlrgftst agvgvdatvr atv
//
LOCUS       WP_284574790             564 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces sp. 2P-4].
ACCESSION   WP_284574790
VERSION     WP_284574790.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..564
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=58356
     Region          172..366
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mvraavlpal aaglsgtaav iftlqlgggs ghrdprlwpv lvgcallvag alaaaflgae
       61 rsakavrdrc ealrrssirg rqelrtaaer lergeapnrp vrggptgppp gtdpgrvdef
      121 wllaqelrga reqahtalvr vagpaapsds drkvevfmnl arrlqslvhr eitlldgled
      181 tvedpdllke lfhvdhlatr irrhaenlav lggaasrrqw trpidlgevl rsavaeveqy
      241 trvkvvppag gtvrghavad vvhllaelve natvfsapdt dvvlraervt agiavevedr
      301 glgmpaaelh rmnalladpd qvsvrhllad griglfvvsa larrhgiave lktniyggld
      361 avlvlpqdll gaqasgageg qggsratswg tgngpltgpt tgngapaapp leparvavpr
      421 peapaappaa aparmqapaq tgpyadprlp apavpeprep arpapepara agpplpggpa
      481 paaapaaapw rvppgnpapa papwpvppgp daagvpvpag raaaaagrpp lprrraqshl
      541 apglrdtphr parphpisps ttrt
//
LOCUS       WP_284574965             330 aa            linear   BCT 25-DEC-2024
DEFINITION  trypsin-like serine peptidase [Streptomyces sp. 2P-4].
ACCESSION   WP_284574965
VERSION     WP_284574965.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..330
                     /product="trypsin-like serine peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=33029
     Region          126..>289
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mvstsrsgsg rrprrlrvrl lvgagaalla aggaayawgl pgilahsatg drargsyaad
       61 padgdraaaa llaggvrqvp aagrsgpgea pgpaeapgaa agggqsagqa psgplaarpa
      121 aaepaigalf spggdgdgph hcsgvvvhap ggdlvataah cvhrpllgfr tnlvfvpgyr
      181 dgqaphgvwv ptrihvhprw aasqdpdhdi aflrvrrpgr pgerledtag aypvrfgagl
      241 plparlvgyp ggaeqpldcs ttavaesatq lrldcadvpn gtsggpvlag grtligvigg
      301 rdgggdewts ysirfgdatr elyeratrag
//
LOCUS       WP_284575055             324 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284575055
VERSION     WP_284575055.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..324
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33767
     Region          1..289
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 massanpisv lciigscisl qlgsalavkl fddggtwgts avrllvaavv llaitrprvh
       61 ewnrqqwagv lglglslglm ngffyagidl vplgpavtie flgplllaaf lsrslrdgic
      121 vvlamtgmal lgldafngnp lnplgvafll gaalfwaiyi lanknagalv pgqgglavaf
      181 vvggvamlpm gadgawnlis stntlwfaig tgilgslvpy slelialrgl apnvfsilis
      241 lepafaaffg wlllaqnist lklvaigvvi aasvvqtvgp krsgedgepr aklkklqdig
      301 kkvatkrtek rlrtearsrk knld
//
LOCUS       WP_284575011             182 aa            linear   BCT 25-DEC-2024
DEFINITION  glycine-rich domain-containing protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284575011
VERSION     WP_284575011.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..182
                     /product="glycine-rich domain-containing protein"
                     /calculated_mol_wt=19274
     Region          49..158
                     /region_name="COG4278"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443419"
ORIGIN      
        1 mtcnntppga ppppctvkpa ggaapsprrl ltdaqfndvr atvldnnpgm apdmatrivv
       61 ealkfvvaas lfptvriapt revdegwhal ilhthlyatl csrlgrtvhh yperpdesrh
      121 dpdvltrtva lieqagyspd aelwpgpers lvsvavscsh tpvpggcgpi rpgqcathgg
      181 de
//
LOCUS       WP_284575132             240 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284575132
VERSION     WP_284575132.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..240
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=25989
     Region          <28..225
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mgnylhslrr rrrkrlldsd ilaagdqrva viglgrfgss laneltrrgw dvlgidtdaa
       61 lvqkhsdift htavadctdp evlrqlgvgd fpsvvvgigt dieasilvas nlleegvpni
      121 wakaisrqhg qilerlgvhh vvlpehemge rvahlvtgrm ldfiefdddy alvktitpdt
      181 itgvplgqsa vrtkygitvv gikrpghdft hataetvvak gdviivtgrt rhveafaelg
//
LOCUS       WP_284575155             519 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284575155
VERSION     WP_284575155.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..519
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=59180
     Region          9..512
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mpsekdapqp almwfrddlr wqdnaalawv akqgpviavv idedatvtga ralgaatrww
       61 wqrsvhqlqh klhahgvpll yyqgdpraii pavveefgvs avgwsrryhk plreldaqlk
      121 rllqekgvaa ksfpghllte pwevqtqqgk qykvytpfak targvaadnv asylnngnah
      181 sssptshdel gpigfaspga dlasahplpd wdeadwtlsl aqhwspgena awqlaeefls
      241 qlaaaskqra phyaadrdrl dkkatsrlsp ylrfgeisih rlwalitqas dsgritnedt
      301 saflsellwr dfawhrlyhl pdlhqrnvre qfdhfdwhwd enearriast rrdprwpete
      361 kdipeiatad dfrsvfsawr agqtgiavvd agmrelwatg tmhnrvrmvv asfltknlgi
      421 hwrhgeawfw dtlvdadpas npfnwqwaag cgddaapyfr ifnpdtqakr fdpdyryiqh
      481 wvpeyatpiy pqpvvelkas rrqalaayee mknfhprpe
//
LOCUS       WP_284575282             491 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Streptomyces sp. 2P-4].
ACCESSION   WP_284575282
VERSION     WP_284575282.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..491
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50331
     Region          4..>188
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 maaiviaggg taglatalal grrghrvrvl erggpppdgp avesaqrwrr pgvpqavhdh
       61 ilnalgvrml rrhapdvlgs llahgarlld ltaaapggpa gpgeeelvtl varrslldvv
      121 lhraaaaapg vsfshrtaaa glltapagps ghrvagvvad sgeriparlv vdatgrrsas
      181 rswlaaaglp vaddlsgpsr lhaygrfyrl rrpcgplpgp lnrgnaaggi wghysavlhp
      241 adndvfaitl galpgdpala alrgagafta acrlspylap wveedaaqpl gpvratgmpp
      301 nvlrgtatdr qrpvrgllqv gdaacttdpm fgrglslala hafglaglvd grpepddrla
      361 rdaaglaagl lrpwfdkgvh dsrlrvrqwr eatgaaagpe pagppeppap pvparlwaaa
      421 taaaaadrav wrgltriqts latpaevfad pafldrvraa dtarpgaaap dgprpptpae
      481 lrhaltareg g
//
LOCUS       WP_284575207             440 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent RNA methyltransferase [Streptomyces sp.
            2P-4].
ACCESSION   WP_284575207
VERSION     WP_284575207.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..440
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=47705
     Region          13..437
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 mteqnekqsl vgeeyevevg pvahgghcia rtadgrvlfv rhtlpgekvv akvtegdtds
       61 rflradavtv ltaskdrvea pcpyagpgrc ggcdwqhakp gaqrrlkgev vaeqlrrlag
      121 ltpeeagwdg tvapaegdkv pagqvpqwrt rvqyaidaeg raglrkhrsh diepvdhcmi
      181 aapgvselgi ekrewpqmat veaiaatgsh drqvvltprp ggrlplveld kpvsvlrvee
      241 kdgathrvhg rpfvreradg rtyrvgmggf wqvhpqaadt liravmqglm prkgemaldl
      301 ycgvgifaga laerlgetga vlgiesgkra vedarhnlad fprvrieqgk vetvlprtgi
      361 tecdlvvldp pragagrqtv rhvaslsarr iayvacdpaa lardlsyfae agykprtlrv
      421 fdlfpmtshv ecvavlepvr
//
LOCUS       WP_284575266             311 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284575266
VERSION     WP_284575266.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..311
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32969
     Region          18..310
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mlepqapqvi tladaqvddp rladirqlnh prlrpdrqpr leldssgdyi pasrpsvila
       61 dgalpiarmc gtdsavtpaa ifgraeklqk fatdypeqws riaqlgipvy elpavllrdv
      121 vgfelhrgll avalrpdsve lgtksaeeil apartivvle gvgdpdniga iyrsaaslga
      181 dalvfgagcg dlwdrrvirv smgqalrvps vripggfsnw hhgltdlrnq gfyvtalspg
      241 aqavqlrdal vgpsgnrrek valllgaegp gltphamnaa dacavipmaa gadslnvavt
      301 aacclyerwr g
//
LOCUS       WP_284575392             323 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284575392
VERSION     WP_284575392.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..323
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34273
     Region          2..319
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(40..41,45,118,122,125,143,146..148,167..168,172,187,
                     210..211,232..236,257..260,307,309)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(130,225..226,239..244,252..259,262..263)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mkaiqithtg gpevlqiaev esptpsddqv lvdvlvagvn yidtyyregi ysattpfipg
       61 fegvgrvlhd pigkiasgtm vawntafgsy aeqvcvargk lvavpndfdl staasmllqg
      121 itahylthgv yeladgdscv itagaggvgl lttqfaaaag anvytvvssd ekeelsyqag
      181 athvlrygpe lanqvrelta gkgvdvvydg vgkdtfeqsl dmvrnrgtvc lfgaasgpvd
      241 pidpqilnek gsifltrpsv agwisregef qmraqavvqa vvdgdlkfrv sdsypleeat
      301 qahrdlqdrk ttgsivlrvq eai
//
LOCUS       WP_284575433             226 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Streptomyces sp. 2P-4].
ACCESSION   WP_284575433
VERSION     WP_284575433.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..226
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23277
     Region          3..>79
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mtptptptlv ardwaeiqer mlvplyetvy drlgvgpgdr llgldcgagl alllaegrga
       61 aatgveadpe rralarerll dvlpaapapg grpydvlfaf apsraalaaa lpslrsgaav
      121 vlagwgpaer ctvpsvpggg papqdlealv saaglrpdgs grvfcpfgya dadsavrgll
      181 stglygsagd tgqvekelae alhpyersdg svwlpnilry vlarvp
//
LOCUS       WP_284575476             936 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284575476
VERSION     WP_284575476.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 936)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 936)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..936
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..936
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103430
     Region          2..934
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtsthfetfr sqltyeldpf qvqgcraven grgvlvcapt gagktivgef avslalsrgt
       61 kcfyttpika lsnqkfhdlv aihgedavgl ltgdvsfqpd adivvmttev lrnmiyaksp
      121 aldrlthvvm deihfladqa rgavweevil nleehisiig lsatvsnsee fgrwlstvrg
      181 dtevivsehr pvpleqwmli gqkvyplfap gtpaiegttt sepagvnpel qrrvarleag
      241 daadgrddfr pgqgfrsrtt agtgnsrsgn vrpqdryrpl grpevlrilq gqnmlpaiif
      301 ifsragcdga lhqclrskmv ltdedeqrii aevidagveg iphedlevlr fsqwrkalir
      361 gfaahhagml pafrhivekl fvrglvravf atetlalgin mparsvvlek lvkfngeahv
      421 dltpgqytql tgragrrgid tlgnaivqwa pamdpqrvag lastrtypli stfepgynma
      481 inllnnlgmd dslrlleksf aqyqadgsvv eetreierav hrveklreql neaiaafapp
      541 stddqdpaql lseyvelrkr lsveekslks rakdergdet railaklqpg dvialpskkr
      601 pvlavvntpa nqtadprpwi ttekgwsari dasgfdnppa lvgkmklpgk alknprrhnh
      661 ivvdkfared yprpkkmklr arirdterik dlrtqmkkhp ahawpamere qltqlaqkyl
      721 rrkgeldklr atvdkatetl gdmlrrivdl lteldyvdiv dgepvvsieg eklaqvhnas
      781 dlliaqclkr giwqeldpae lagvvslctf enrratggql fdgvtdamts amentlrlwe
      841 elisdesrhg lphtrepepg fsiaihqwca gaplgyclaa aaesgaeltp gdfvrwcrqv
      901 idllqqvakt gysseikrta gqaiasinrg vvaigs
//
LOCUS       WP_284575532             361 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284575532
VERSION     WP_284575532.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..361
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37151
     Region          35..353
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mdrqrtqqvl rarnrnrvll fivlvfalvs gtiaslvigq ytipigelpr ilavgplgvs
       61 amdesviwqi rlprlvlgll vgaalgvgga lmqavfanpl aepsvigvta gagvgaslai
      121 vlgiswfgas laivlgiswf gattvpvfaf lsgllttwlv yqlarfagri rvinlvlvgi
      181 avnavagali sffifiapts sreqvvfwqm gslsgakwah isvvavliga giavalllvg
      241 kldvlalgdr aaghvgidia rlrvlallla tlltagavsy agligfvglv vphiirtvag
      301 psnvvllpas alggaalivl adtaarsiid fadlpigift alvggptffi llrammrrga
      361 v
//
LOCUS       WP_284575723             219 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284575723
VERSION     WP_284575723.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..219
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22243
     Region          11..>74
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mtgvspspae qhlgdrlaal vdgelshdtr ervlahlatc pkcraeadaq rrlkamfves
       61 appplsagll arlqglpgeg pagppggdlf gyrvpeppqe gfriaevgrp rrrlafvaag
      121 avslaaialg gtyplntiep nvrgespatr pgtavpaapa sgsgpapgsa pggavsvada
      181 vvrdrarrpg ptadpqeegp lpplhpsaht psrpvsllr
//
LOCUS       WP_284575796              87 aa            linear   BCT 25-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Streptomyces sp.
            2P-4].
ACCESSION   WP_284575796
VERSION     WP_284575796.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 87)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..87
                     /product="type II toxin-antitoxin system RelE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0017148 - negative regulation of
                     translation [Evidence IEA]"
                     /calculated_mol_wt=9897
     Region          4..86
                     /region_name="RelE"
                     /note="mRNA-degrading endonuclease RelE, toxin component
                     of the RelBE toxin-antitoxin system [Defense mechanisms];
                     COG2026"
                     /db_xref="CDD:441629"
ORIGIN      
        1 mseyrtafrp eaqaelrkip rdvalrilak lteletdplg fnttalasqp errrlrvgdy
       61 rvvytidnge laiwvvhvgh rstvyet
//
LOCUS       WP_284575804             759 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium propinquum].
ACCESSION   WP_284575804
VERSION     WP_284575804.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 759)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 759)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..759
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=84112
     Region          23..752
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 msprfsrghe stasqkaqrv hhsefsaela aeqsyldalf gildsdvsna rqrladaqlt
       61 idpanadsda llrreteyhr lqekldqlnl aqiglvfgri dvdadgenpt pdgldrryig
      121 riglmdrddd yrsllidwra pmarpfylat tahpegvrmr rhirtadrvv kdiddellsg
      181 tapddaarad vageaallha mntargehmq sivetiqreq daiirdatrg vlvveggpgt
      241 gktavalhrv ayllytwreq lsrtgvliig pnptflnyis qvlpelgetg vvlstigrly
      301 pglrptlhed aetrrvkgsl qmvdvlkaav kayqqvpkhn rdvvlegtrv eltpamvksa
      361 rtrarrsrkp hnearevfte qlrselahgl aaiighdpld ggnlldsadi aalredisde
      421 aiieelvdef wpqlgprqvl relltdhtal haacrgngge efvsallrna dssahswaes
      481 daalldelaq llgsgddeqq aaaderewqe aleeaegald ilatsestdn ddvfdseils
      541 ahhvidaetl arrqqardyr ttaeraegdr twafghvvvd eaqelsamew rmvfrrspnh
      601 wmtvvgdpaq tsspagcdnw sealepfvgk ryrqhqltin yrtpveiael aeaivrkyqp
      661 datvaqairn reaavrwlps gtspesvreq lqadeqqrsc aiitaqnasq hkgleydhvi
      721 viepaeiiaa tprgwqdlyv actratqtls iigelnlae
//
LOCUS       WP_284575866             331 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NUDIX hydrolase [Corynebacterium].
ACCESSION   WP_284575866
VERSION     WP_284575866.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 331)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18950610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..331
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=36443
     Region          40..163
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
     Region          177..318
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mvkksqmsea dkdnqsgfnl saryhqigkn pgaeyrkptl aagavlwrrg dngtaevavi
       61 hrpryddwsl akgkvdpges lasccvreia eetgyqvqlg sllgsvnypv qgrtkvvfyw
      121 nanitggkfq kneevnklrw lsvneahekl tydtdrrvle qaairhddai dtrvlyvrha
      181 kahdrktwsg ddnlrplhkk grrqaeflvp mlsaykptal ysaeparcqs tiaplsdals
      241 lpvtteqivg dagldnlaea tarfreiatg ggvpvivsqg gmmpeiietl aaeaefdiep
      301 refkkagtwv lalregklvg adylasplpv r
//
LOCUS       WP_284576101             609 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Corynebacterium propinquum].
ACCESSION   WP_284576101
VERSION     WP_284576101.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..609
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65592
     Region          11..609
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mreafspaky tiepgqtllp ltidavkaqp kaemftrpkn htwvpvsrqe fldevyavak
       61 glldagvehg drvalmantr yewmllnyai waagavvvpv ypssslsqvq wiiensgavl
      121 gigetqehse ilrmlqladd geprvkdsts qmrafyeind gavaalqaag kdidddavdk
      181 riaattsddl aslvytsgtt grpkgcmlth rnwtaqvlgl ltnpiggiah agnhvltflp
      241 lahvlafsvs aaaiisgptq nfwadfaslp tefqrskpnl ilgvprvfek vrngarakah
      301 dsgtvqgklf draeataiay sraldtedgp slalrgahki mdklvlskir agmggevdyc
      361 isggsamspe vmhffrgigv piyegyglte taaaatvdfe nqkigtvgpp lggtrvriap
      421 dgelqlagdl vfdgywrnae atdeafdgqw yctgdlgeil psghvkivgr kkdlivtagg
      481 knvapggled glcshplisq alvvgdgkpf vavlvtldeq algrwksqhn ipasrsvdel
      541 ahdatlraei qdainavnst vshaeaikkf yildkdftee sgeltptmkv krnvvvqrys
      601 evleklysr
//
LOCUS       WP_284576313             427 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Devosia
            rhizosphaerae].
ACCESSION   WP_284576313
VERSION     WP_284576313.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..427
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=47066
     Region          58..427
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 marffskslg valalviagv fgtiaavili pephelagpv etelvagspe fvrsmfalhg
       61 gnlyesntia tlqngeeifp amldaiasaq rsinfetyvy wsgsigsrfa ealaeraaag
      121 ievnvlldwq gsvsmedeli etmvaagatv krfrpiewyt ldrfnarthr kllivdgtvg
      181 figgvgiadk wlgdasspde frelhyrvqg pvvasmqgaf afnwleatgr plqgdlyfpp
      241 vadsgplvtq lvyssigsrn vmhvmlmtal aaaqdhirig tayfvpdeia iaqllaarqr
      301 gvtvdvlvpg khtnkdfvra asrhfwgdll eagvnfyeye ptmyhakiti vdeswtsigs
      361 anfdersfrl ndeanlnvyg gdfadqqiri feqdlerstl itlehwesrp awqkltdwla
      421 stlrvql
//
LOCUS       WP_284576321             110 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Devosia rhizosphaerae].
ACCESSION   WP_284576321
VERSION     WP_284576321.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 110)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 110)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..110
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12172
     Region          5..86
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mvsfdldatf tsladptrra mllalkggek siaelaqpha mtragaakhl amlekaqlie
       61 rhkvgrkqmc rlrpeplrha ggwlhqweaf wneqldslea alqedasgqd
//
LOCUS       WP_284576394             438 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Devosia rhizosphaerae].
ACCESSION   WP_284576394
VERSION     WP_284576394.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..438
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47309
     Region          17..>418
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mldweadpyi vvmtgsglli alvawlplal rrlwislpiv clviggvvfn lprigtnvsp
       61 vdfpviterv telvviialm gaglkidrif kfsdwqvtwr llgitmplgi laitvlgmnl
      121 lnlsvfgall laaclaptdp vlasdvqvgp pheggedtvr faltseagln dglafpfvhl
      181 aivlsavlat gepwlvhwtg yyliwkilag ifcgwvvgqv fgwltfkmpg dslartgdgl
      241 iaiaatfvsy gvsellqgyg flgvfitala lrqvhhdhdf hrdmhditeq verlvmmvll
      301 lmfggalaag llrdvgwvev taavvillvi rpltglvami gikatlsekl visffgirgv
      361 gsfyylaygl nhgefleanr lwtivalvvv lsilihglav tpimhwvdrl qgrdpdaega
      421 vpppglqgpa apnnheeq
//
LOCUS       WP_284576545             536 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces sp. 2P-4].
ACCESSION   WP_284576545
VERSION     WP_284576545.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..536
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=59487
     Region          122..489
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mkgstyrrcs crdpksgkel gascpkrnsr nhctysirqe lppredgsrr sfarggytna
       61 kaaqadldhv rallglaead dpegtqllae mlaevsgekl plpdveetrr rlkagqdlvg
      121 sltvaewldr wlagkrirks gisryetdir vhlkphighr rldrlrvshl semftaiadg
      181 naeileqnaq rraavkelat ipwkgaenra rrkalkeaid ampafrrvtg patrqhvkat
      241 lraslndaig qqiitfnpaa hveidpvrkp kalvwtderv akweqtgekp spvmvwtpeq
      301 tgafldfvad drlyamwhli afrglrrgea cgqpwsetnl drhsltvtgq lvqdgwevea
      361 sepktdsgfr vvaldddtvg vlerhrmqqe adrlewgsaw vntglvftqe dgswlhpgkv
      421 tdlferlvaa sglppirlhd lrhgaatlml aadidikivs dtlghsdtri trdiyqsvlp
      481 hvgksaaeat aklvplqrka eqeeqarkaa kkakqaakak akgkkkakak kaakkg
//
LOCUS       WP_284576562             263 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Devosia rhizosphaerae].
ACCESSION   WP_284576562
VERSION     WP_284576562.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..263
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28297
     Region          1..256
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 maeraklavv tgaslgigle lakqciehgy dliiasdtee iqeaaavlrg lggtveavqa
       61 dlatrigidq lyttvarqgr pvdvlmanag rglgeafvdq dfadiqrvid tnvfgttyll
      121 hrflrdmrnr negkvlitgs iagampgafq avynatkayv dsfayalrne lkdtditvtc
      181 lmpgptdtdf fetadmldtk vgtdkkddpa mvakkgfdam mrgeghevtg fankmqamma
      241 nimpddalae mhrkmaqpgt akh
//
LOCUS       WP_284576637             172 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284576637
VERSION     WP_284576637.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..172
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18559
     Region          5..66
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mipngtaika lrevqsmslr dlarlaqtsa gqlsriergk agagedllfr laealavpva
       61 ditrgemvti taeptadvve nkrpkrvpkq atrdvpypgt pegavfhysp eeaarflpws
      121 alqlkrkaya reipfndgas rvtftgmdir eisamtavrp lsetarptsv as
//
LOCUS       WP_284576689             193 aa            linear   BCT 25-DEC-2024
DEFINITION  NuoB/complex I 20 kDa subunit family protein [Devosia
            rhizosphaerae].
ACCESSION   WP_284576689
VERSION     WP_284576689.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Yu,H., Schut,G.J., Haja,D.K., Adams,M.W.W. and Li,H.
  TITLE     Evolution of complex I-like respiratory complexes
  JOURNAL   J Biol Chem 296, 100740 (2021)
   PUBMED   33957129
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Parey,K., Brandt,U., Xie,H., Mills,D.J., Siegmund,K., Vonck,J.,
            Kuhlbrandt,W. and Zickermann,V.
  TITLE     Cryo-EM structure of respiratory complex I at work
  JOURNAL   Elife 7, e39213 (2018)
   PUBMED   30277212
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Walker,J.E.
  TITLE     The NADH:ubiquinone oxidoreductase (complex I) of respiratory
            chains
  JOURNAL   Q Rev Biophys 25 (3), 253-324 (1992)
   PUBMED   1470679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..193
                     /product="NuoB/complex I 20 kDa subunit family protein"
                     /EC_number="1.6.5.9"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=20815
     Region          28..187
                     /region_name="PRK06411"
                     /note="NADH-quinone oxidoreductase subunit NuoB"
                     /db_xref="CDD:235797"
ORIGIN      
        1 mglssqtgtm vapqptglvd phtgkpagse dpfftgmtde ladkgflvst aahlinwart
       61 gslmwmqtgl accavemmqm smprydverf gtaprasprq sdvlivagtl tnkmapalrk
      121 vydqmpepry vismgscang ggyyhysysv vrgcdrilpv diyvpgcppt aeallygill
      181 lqkkirstgt ier
//
LOCUS       WP_284576726             223 aa            linear   BCT 25-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Devosia rhizosphaerae].
ACCESSION   WP_284576726
VERSION     WP_284576726.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Niehaus,T.D., Elbadawi-Sidhu,M., de Crecy-Lagard,V., Fiehn,O. and
            Hanson,A.D.
  TITLE     Discovery of a widespread prokaryotic 5-oxoprolinase that was
            hiding in plain sight
  JOURNAL   J Biol Chem 292 (39), 16360-16367 (2017)
   PUBMED   28830929
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Fan,C., Li,Z., Yin,H. and Xiang,S.
  TITLE     Structure and function of allophanate hydrolase
  JOURNAL   J Biol Chem 288 (29), 21422-21432 (2013)
   PUBMED   23754281
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Wang,L., Grau,R., Perego,M. and Hoch,J.A.
  TITLE     A novel histidine kinase inhibitor regulating development in
            Bacillus subtilis
  JOURNAL   Genes Dev 11 (19), 2569-2579 (1997)
   PUBMED   9334321
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005226
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..223
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=23416
     Region          8..222
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 miawpklptp tvlpigdaal lvrfatvvde qanaaaialt teldadplpg vvelapnlvs
       61 vllrydplrt dparvagelr lrmirlggae aapstdwvip atfggeggpd lqevadslgm
      121 tpsdfaaahn asdlkvlatg fapgfvylgl hsqhlylprr ssvrakvsag sllfaagqta
      181 iaatemptgw hvigwtefsn fdarsdpptr lgagdrvrfe vvp
//
LOCUS       WP_284576770             372 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Streptomyces sp.
            2P-4].
ACCESSION   WP_284576770
VERSION     WP_284576770.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..372
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39833
     Region          19..365
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mttrtadlsr lrerrwpppp smsadravtm alysgtwtsg pythdveeam keltgapyav
       61 afqsctaaih atllahgvra gtplhtpafg fagtltgaah igarllyhdv dpdtgnsidp
      121 lpapgavvlt pdlhgvphtl prdqvitdac qslgtlvngr hlgaagthcw sfsatklvsa
      181 pdggavttdn edladdlrql rdygaepghp ranalitrpg hnwrptelsm aiavdeirfr
      241 lplvaprard vgarlretla dtglwhqqvp agtepafhki rtglpgtpps ryralrtalr
      301 danvpthdwg tiplpahptf atgpglgphv paavtladwt fclgteqcpp wtwtdeetdl
      361 vahtlemime sl
//
LOCUS       WP_284576814             368 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Devosia rhizosphaerae].
ACCESSION   WP_284576814
VERSION     WP_284576814.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..368
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39262
     Region          2..364
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 manmqatdst ideaiasgkl vgtvvmvakd getiyarkag ladreaqkpv eldtvfraas
       61 ltkpivaati lamadhgllr idepvrrylp yfrprmadgt epvitlhhll thtagltydy
      121 srdprisggl tnsdmaldev lrliaeqpla yppgtswqys vaidvlggvv aavnggqlsd
      181 avahyvtgpl ampdtvfsls essrlatpya dgedeparmr dphaannpwg gvtsfspsri
      241 fnstafqsgg agmattaadf lrfleamlhg ggpvlapata analrnqmgy erepgqafsf
      301 lgsytvdpek aghpwaagtn nwggiyghvw sidptnrism vslsntafyg geldypralr
      361 ravytdlv
//
LOCUS       WP_284576924             157 aa            linear   BCT 25-DEC-2024
DEFINITION  HIT family protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284576924
VERSION     WP_284576924.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..157
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17979
     Region          16..129
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 midtdwrsdr igsahrgenp tvmrrldqgf avigdrqflp gysvlltddp svtrlsdlpr
       61 prraayladm erlaeavela crrldpafrr vnieilgntd pylhahvwpr ydwepadlvr
      121 lpvwlygeeh wrgtehelgt rheglrtaig geldrla
//
LOCUS       WP_284576973             254 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Devosia rhizosphaerae].
ACCESSION   WP_284576973
VERSION     WP_284576973.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..254
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27907
     Region          24..249
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtlrpgvawv igggsgigaa vaillaqrgw tvaisgrred klnsvangqs sirpypldvt
       61 dsvaiaenmn qvvaelgrid lfifgaaawq pmkvgnydfe qfhrvvdtny lgfvrmlapl
      121 vtqmerqggg hlaaiasvag yfglprsaay sstkagminl letmraelap knivvrmiap
      181 gfvkseltek ndfpmpflle tddaarrivd gltqsdrfei afprrmvwlm ktirwlpyga
      241 ffrltgrmlp rdnp
//
LOCUS       WP_284577013             557 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase [Devosia rhizosphaerae].
ACCESSION   WP_284577013
VERSION     WP_284577013.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..557
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=60324
     Region          80..210
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 meagtptsgp vvgngadvhe hgqwhrrrle fltwdrtped iagadhqarl klleevagaq
       61 faptayiaae aaiytthlvl gerswiagha lvrgdvefga hctvnsyami sgkvrcgdgv
      121 riashsslvg fnhgfddpgv pihvqrhetl gitieddvwi ganavlvdgv rvgkgaviaa
      181 gavvsrdvpp laivagvpak vvryrgqsgk sdvaavlerl gaaakgqwkt ilaryerage
      241 ylsreadgte rrsirhlcda ieiaaafget pprldriatv arlqavqeat tglfpdpfqp
      301 prsgealren glalynvlav gyalealgsh plhriaaved ltaielcswl enlpwreraw
      361 sagsvvdaig talyfnaryf qtarsretlf gwlalkqdrg tglwgaptae qgllqpvngf
      421 yrltrgtyaq wglpvpnaer aidsvllnyr nyggfsdaty tacnlldtih plwlclrqtd
      481 hrraeaeaia raiitrager wvedqgfafa dgqfpslqgt emwlsvvhla akllgvetsf
      541 tfvpkgvhrt eavglgl
//
LOCUS       WP_284577032             269 aa            linear   BCT 25-DEC-2024
DEFINITION  inositol monophosphatase family protein [Devosia rhizosphaerae].
ACCESSION   WP_284577032
VERSION     WP_284577032.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..269
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=29153
     Region          8..263
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mtidydlild emvaiardag tltlehfrdf raleigikgp gdfvsdadre aeqlirkrlf
       61 ainpdwsltg eefapvdgad pehrwlvdpi dgttnflngq hytitialrr gqetlcglvy
      121 npvademfta skgggawlng drvhvsrste vglmcvgtgl ptpglqlypg ayqrldmirs
      181 nigavrvvgs aanscayvaa grltgyyeet gfvdtaagil lveeaggivt dwwgrgpevf
      241 ertgalivan pathaflleq lrsvprkep
//
LOCUS       WP_284577071             607 aa            linear   BCT 25-DEC-2024
DEFINITION  GumC family protein [Devosia rhizosphaerae].
ACCESSION   WP_284577071
VERSION     WP_284577071.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..607
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=65321
     Region          9..604
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mqelvqnwsp slrqrllefl rldsaeplsa geavtaalqt lrealtvqrv gltyvvsvqa
       61 rspdperaae lanavaqayv deqlrskidn vlsarqimqe qvadarqniv asegafdlyi
      121 esnmarivad tgrtdlarmq aeigqlsear tqsavradsl easlaednfa givqnlqnqa
      181 aielgqrrqr lsqqittasp avaldleael asideqiraa avnevnalea qvaqnqeeeq
      241 qtrqqlrsai assglsadil telfdlqqga dlsrqqyqrl lslerdlatr aslqvadsri
      301 vspalpsarp vfpnpalila saglaafglg vllafvyenl iggftraeqa eavlkarmps
      361 aiprqkgtaa eisamivhap msafaeavrr lraaidqwrp pmnasstakq sqvimvtste
      421 pnegktttav slarsyatgg rrvllidadl rkpgihrqvg vdpsmglley lsaapedape
      481 iaavitsdpl snatlllgsn rsgvptddlv slpaferlie dskrtfdiiv vdtppvgpvv
      541 dalyiaplan tvvfvtkwas taqrdaksal dsirvsapda qalvvlnqvs esrlayrrky
      601 ggyyaqv
//
LOCUS       WP_284577093             276 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Devosia rhizosphaerae].
ACCESSION   WP_284577093
VERSION     WP_284577093.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..276
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30104
     Region          95..272
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mhkeflairt asenvvgavv hrsgprqlvl eiryekndpd arrvvrrtle vltphivrvv
       61 elvrerqata legqsgdall efipvpafal daccvvrarn dhaesmirhm dclilgadgv
      121 lhardanldl qiksfvstgg gefrrparcv lttlssdggr ifasmhtvpp sgtrpglihg
      181 msqeegwrcl lvlddaskpi rmnadvlwka lgftagetdl vqgliggnti gdcaaarras
      241 kqsmrnllls vmrktgthrq tqlvslltrl alhara
//
LOCUS       WP_284577121             330 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Devosia rhizosphaerae].
ACCESSION   WP_284577121
VERSION     WP_284577121.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..330
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36247
     Region          15..327
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msrldqklel afaplatavq tgripggvlg ivdnagnrvm rslgaaqlvp qhremtdntw
       61 fdlasltkvi fttqrilala dagridldap lisalpdfrq ynpdnwerrv tfrqclghqt
      121 pfpavfplyt ygrdpqllra fllqhqweag pavysdinfm llglalerie rqgirqmdpg
      181 pgfawsadpa qsaateddsw rhrvlvgevh ddncsalega ghaglfgtad avldfardrl
      241 adtgpdapir tplsarrthg werpyegwsg gelcspasig htgftgtglw idfergcawt
      301 lltnrvhptr hfdsgivalr ravgdlinsd
//
LOCUS       WP_284577265             395 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Devosia rhizosphaerae].
ACCESSION   WP_284577265
VERSION     WP_284577265.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..395
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=40619
     Region          133..382
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mvaglslptv lpevanvtvl almgvglilv fvqpsgrgvi rqpavllpla agailalalv
       61 ftattpnhvl avlvlaplfl vgplasllqk lgreltptlv gifalvgaag afavavydva
      121 vrglsrggys vnnvihfadl altigfvali gvfgtkgrsr fifvigpvlg liavvlansr
      181 gpilaavpvs iaaaamisgm llprrwvlpa aaatlvvlig ggylayvlgf aqrlerlgsv
      241 vtlfssgttg dssvgerfhm yisawnafqa spifghglid ythaaaqyap pgpvqykpsq
      301 hlhndiadfa viggslglls yvlylaapla galatrgrwr naalylgvvm pvgyfamglt
      361 namigiltqt vlyavvlali aaldvnssps sthes
//
LOCUS       WP_284577303             425 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Devosia rhizosphaerae].
ACCESSION   WP_284577303
VERSION     WP_284577303.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 425)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 425)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..425
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45374
     Region          42..420
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mtaqtksppl seltarqvqw iaggyamafa tipgqtifia qfntairtqf elshgafggi
       61 ytiatlasav clvwagglad rigaralaia savglglval amsvqnhivt lvltlaalrf
      121 fgqgmlshia mttmsrwfnr frgraislag lgtatgdalt pfmitlailt fgwrevwfgt
      181 altlflvicp iiwfllrdpp dgkravargq vnpdgetggs ltgsqwnrgr vlrdplffmi
      241 ipgimappai gtlymfhqah lvelkgwdlt fftasyplla ltvvvtslla galvdrfgaw
      301 rlmpvfllpe gigclvlgli epqwsnplff ilfgltagmm spvvgalwae vygtrhigai
      361 ralataalva asalgpgiag ylidigidld lqsfgyaayc fggaalffal rvpfkrriae
      421 targe
//
LOCUS       WP_284577344             321 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284577344
VERSION     WP_284577344.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..321
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31670
     Region          15..>73
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mtpaadtirh pdvseisdla egllsparsa qvrrhlaecp lcadvlasle eirsllgtlp
       61 gpprmpadia gridaalaae alldsttpra gaavgaeadg aeadaaaqpg asgasgaaaa
      121 rpggrrpsgh pdgatgpgrr rarrriavva alagaaacav gillagglfg sgspdtaart
      181 sdprttaqap aggtytaqgl qdsvrrllgp adgakkatpp egnstfgaen apqsqglapg
      241 dravgtdaad vpacvlgatr rteaplaaer gsyqgrevfl lvlphpgdag rvdayvvgtg
      301 ctatpsggag eplltrtypr s
//
LOCUS       WP_284577363             810 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Devosia rhizosphaerae].
ACCESSION   WP_284577363
VERSION     WP_284577363.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14311963
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..810
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90440
     Region          11..>633
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          727..798
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; cl38983"
                     /db_xref="CDD:476840"
ORIGIN      
        1 mtltrrvlet dwtltcarpv gapelpdaip atvpgtvhtd llaarlipdp yldlneiavd
       61 wvgrcdwryd lafdwhdnga gqvdlvcpgl dtfarlslng tligetanmn rtfrfdvsal
      121 lregentlsi lfesawtrge qlasqyeprp nnypgpanlm rkmacnfgwd wgptlvtagi
      181 wqsitlesws earlasvrpe itvhgadghv risaeivggt pgavlrgtva gvtselpveg
      241 lasfdllvpe pqlwwphglg gqplydltve llrgeevldt wsrrigfrsv rldtgsdahg
      301 taftivvndv pvyvcganwi pddcflprvt pdryrarvdq akraninllr vwgggiyetd
      361 afyeacneag mlvwqdflfa caaypeegdl paeieaeard nivrlmphpa lvlwngnnen
      421 iwgwvdwgwq aalegrtwgl gyyldllprl vaeldptrpy wagspysgsm dihpnnpahg
      481 cthiwdvwnd igyehyrgsi prfasefgwq apptwatlsq svhdqpmtpt spgvwhhqka
      541 tigngkllrg laghlpspqs mddwhfatql nqarairlav ehmrshrpvn mgaivwqlnd
      601 cwpvtswsai dgygrlkplw yamravyaph lltiqprgee lylfaanert lfwrgpvtik
      661 rlrfdgtvla ewthwrlcad rldigslaip aavatpgdpa relliatmhd stayhyfaed
      721 ialdlpkpkv eidvegegqq wrvtlrartl lkdlclfvdr thpdaeiddm lvtllpgetr
      781 sflvtspvpl taeilsskpv frcandlvqg
//
LOCUS       WP_284577569             365 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Devosia rhizosphaerae].
ACCESSION   WP_284577569
VERSION     WP_284577569.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..365
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=38927
     Region          10..361
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mnahlstrma nlrarmeatg tdlvaigpss hmlwladlsp hgderpvlll vsqsfagilm
       61 palnvdsarq htdlpffpwa dadgpqpale elidaagvpr ispsivldet mradfallll
      121 dalpgasrrf tedtvgylrs rkdadeyerl kasallndra meagfaalrp gitetevatv
      181 irdfykanga ttefcsvcfg angafphhht gntklapgda vlidtggrig gypsdmtrvg
      241 ylgsapkgyq evhsilerav naaikaakpg vpasvvdkaa rdiitaagyg pnflhrtghg
      301 lgvdiheapy itassetvld egmvfsiepg iylqgrfglr leeiviirng vaevlsempr
      361 ttvsa
//
LOCUS       WP_284577125             383 aa            linear   BCT 25-DEC-2024
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284577125
VERSION     WP_284577125.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..383
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38170
     Region          87..340
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mprspraprt trtrrssgaa apalalaala llaaapapas aipppppaaa paadpapadp
       61 aptgpsafrl sdprviahys hedgqtpeni aldpdgsayl tfalarqvah adagghtrvi
      121 atlpeaappg tpgagaaavt givrthdgsl yvpyvtgtdr tgihrirpdg tvglfarlpa
      181 dghanglald krhgllyaad srlgtiwris lhdasvtawa agaplepvts agangikvhh
      241 gavwvsnsdr gtllripvre dgtagaveth atglagiddf afagdgmtvv aalpasdevv
      301 lvrpdgtrst mltrrdglsg ptsvavrdgr vyvasassla tdkdpnllva aiegagrges
      361 aasgpgaahs gaaaagadea sat
//
LOCUS       WP_284577600             631 aa            linear   BCT 25-DEC-2024
DEFINITION  ABCB family ABC transporter ATP-binding protein/permease [Devosia
            rhizosphaerae].
ACCESSION   WP_284577600
VERSION     WP_284577600.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 631)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..631
                     /product="ABCB family ABC transporter ATP-binding
                     protein/permease"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69851
     Region          22..614
                     /region_name="ATM1"
                     /note="ABC-type transport system involved in Fe-S cluster
                     assembly, permease and ATPase components
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5265"
                     /db_xref="CDD:444078"
ORIGIN      
        1 msadsvekkp svsadegsvv stirnlwsym wpadrpdlrl rvalaigall lskvattlip
       61 faykgiidsl egsspdpavi lglavpiilv iayalgnvid agfqqlrdvl fasvgqnavr
      121 klalqtfhhm hrlslrfhla rrtgglsrvi ergtkgietv vrfamlniap tiiefvivav
      181 ifvwmfgvsy lgvlvlmiwg ylyftikasn writirrdmn esdtdangka idsllnyetv
      241 kyfanermea qrydasmagy ersairiwts lgflnfgqal ifyggflvis vmavlgvmdg
      301 tltlgdfvll ntflmqiyrp lnfigfvyre lrqgltdiee mfklldqdpe iedkvgatpl
      361 kitgpvirfe dvhfaydedr qilkgvsfev pagktvaivg ptgagkstis rllyrfydvt
      421 ggaitidgqd lrdvtqeslr asigmvpqdt vlfndtigyn irygrpdatd eevrtaasma
      481 qvgpfieslp kgydtpvger glklsggekq rvaiartilk apsvlildea tsaldtkter
      541 diqsaldevs kgrttvviah rlstvvnahe ilvlregqia ergnhatlle qggiyaqmwn
      601 rqrevteaee qlrqktadpd gyfkrkeeaa e
//
LOCUS       WP_284577601             106 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Devosia rhizosphaerae].
ACCESSION   WP_284577601
VERSION     WP_284577601.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..106
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11371
     Region          2..86
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mrdddianim ralghpvrln ilrilatqqq gqcccadvte slplaqstvs qhikvlldag
       61 liqrqprgtr ncyivqhdrl qalgeaysgm iagfspsgak ltaeta
//
LOCUS       WP_284577771             456 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Devosia rhizosphaerae].
ACCESSION   WP_284577771
VERSION     WP_284577771.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..456
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=49865
     Region          206..440
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 msrrrwmptr flvasvamai lfallvaasv rlvasenelg gdvaedmvwl ssqaqyeavr
       61 faeaaahhaa gglpldevql rldvlasrls vleqgeprrq igalgfsedl aghrailada
      121 aerialiadd arqlewiren ilalaqtlrg tanaallaer qqdvvlrdqr krmlleilga
      181 laatmltgll lavilvrdqr nianaeaale rerqvsklhr sfisvvshqf rtpiaivdas
      241 aqrmirrgas msveeisvra qkmrdaclrl trlmestlda arleegeirf nplpcdvgql
      301 lhrvcdtrpd feqgrielri adlpssalvd etlleqavqn lvsnalkysp qdtsitvegg
      361 kareelfirv rdrgvgipad elgslfqrff rartaanvag tgiglsfaah ilklhggtve
      421 veseegrgst ftlrlpyrpa eapsspsdva vselal
//
LOCUS       WP_284577780            1065 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-mannosidase [Devosia rhizosphaerae].
ACCESSION   WP_284577780
VERSION     WP_284577780.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..1065
                     /product="alpha-mannosidase"
                     /calculated_mol_wt=120056
     Region          248..1065
                     /region_name="MngB"
                     /note="Alpha-mannosidase [Carbohydrate transport and
                     metabolism]; COG0383"
                     /db_xref="CDD:440152"
ORIGIN      
        1 mtysnplssk lglldddlkm egkllrlcad lqqkiltpid kfpwqwhvqr admsaadala
       61 avwhqweafg shsvwakkqg htwfaaevei pegargktfl lrftsqwqdr pgstdpqcla
      121 yldghivqal dgnhtelvie rdakpgnrht llvnaftffd rplvgfgvea fvrneraekl
      181 yydlqtplev airlhqsdpr rhailnivdr alraldrrga yteafeaslg gaeqiareiy
      241 elvdtevqpq itavgsthld vgwlwrvlht rdktarsfat vlnlmeeypq fifmynqsvl
      301 fdflkqdype lwermlarvk sgqfeiegam wvepdvnivs geslvrqimr grrfhldhfg
      361 vdpktvwlpd tfgysanlpq imeksglqyf vtsklswndt drhpydtffw rgidgtvtka
      421 qlitaqrfen eaiyttyngd lsvsetmgaw kryepkaahn evvmsygygd ggggptrami
      481 ergtrlergi pgapkvkleg ivpfldrlgk kmdavpgkfp twngelylqy hrgtltsvak
      541 nkannrrser llreleflgi mamtqagasy psetlaefwe lvlinqfhdi lpgtsipevy
      601 vdsdvdygri fstlssangp whaaaqafaq pgkdqlrlln ftsqsrsdfv hfraesvqeg
      661 vslacggtvl plqtitradg sseqmapvsv vplgwtagqv vagaaalpaa slsvsethle
      721 nellritfds aveitsifdk tsqretlaag ekanrliaye dkpmewdawd idryfeeqfw
      781 pladeqaeis vvetgphraa iriarkyqns slvqvislaa gqrqiefdtf idwqersivi
      841 ktlfpfdlna tevrseiqfg hvtrpthrnt twdrarfeas mhrwvdmsea dfgvallndc
      901 kyaydahdqt irltlvrgsn fpsadadlge hrlryalfvh egladlaevh raaerfnnpi
      961 avigstepsp gtssqeanfs fvqvdqanvt ietvkkaers davvlrifen aniranatly
     1021 fgvpvksvra vnlmeegegr lfelrnnsie lslhpfeiat lliel
//
LOCUS       WP_284577816             565 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Devosia rhizosphaerae].
ACCESSION   WP_284577816
VERSION     WP_284577816.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 565)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..565
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=61462
     Region          1..551
                     /region_name="COG4425"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:443540"
ORIGIN      
        1 mspnpttler lrqlvpmggv flgliffsla ltpsliprnf vlqgilcgva faagygigaf
       61 iewlwgfmgl gfpnkrlsra vligglaaaa lvalvflwqs tgwqnavrei mglppvesnq
      121 pvwvtiialg paailiilgt iitagvravs rflaqaippr valvgsliiv gvltniling
      181 vlarsvlsaa drfyaevdal agqyedpplh plqsgsaasl idwdtigqea rayvesgpsa
      241 eeiaaitgkp avmplrvyvg lrsadtvder aqlalaemqr igafdrsilv limpvgtgwv
      301 dppaidtlem lhggdvasva vqysyltswl slvsepevgt dtaralfstv yrhwtelprd
      361 grprlylhgl slgayasqas vspyailsdp fqgalwvgpp fesdvwrwat ssrepgtpew
      421 lpqfedrsai rfvnqhrgle dydqgwgpvr lvylqyasdp vvffepsily rppawlegpr
      481 ardvspllsw ypvvtfmqvl ldmvlaqtsp vgfghvyapq dyldswvavt apagwtesel
      541 dmlrtrltrh gdltslsggw frsip
//
LOCUS       WP_284578083             293 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Devosia rhizosphaerae].
ACCESSION   WP_284578083
VERSION     WP_284578083.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..293
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=33044
     Region          19..293
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mslltrpapa adhadadhls hrdygrisql igdetgiklp pakrlmiegr lrkrvralgl
       61 rglddyshfl fqrgglaaer vhlidavttn ktdffrepeh fnllerklvp dllelrnger
      121 qplikvwsaa sstgaeaytt amvladlaaq rrdfrfailg tdistsvlkq aeravyptef
      181 vapvppekng rylmharkqg lrpevrivpe lrrlvqfarl nlmdtsypfd rdvdviflrn
      241 vliyfdkadq ekvilrligh lrcggylilg hsesmigtav tmrqvapavf qkp
//
LOCUS       WP_284578141             181 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_284578141
VERSION     WP_284578141.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>181
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          1..>181
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkrlqafkfq lrpggqqere mrrfagacrf vfnralarqn enheagnkyi pygkmaswlv
       61 ewknatetqw lkdapsqplq qslkdleray knffqnraaf prfkkrgqnd vfrypqgvkl
      121 dqensriflp klgwmryrns rqvtgvvknv tvsqscgkwy isiqtesevs tpvhpsasmv
      181 g
//
LOCUS       WP_284578158             459 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces sp. 2P-4].
ACCESSION   WP_284578158
VERSION     WP_284578158.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..459
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=49078
     Region          29..409
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtinggisfw haadpgatpp arapltgdtt advvivgggy tglwtayhlk taapdlrvtv
       61 leqktcgyga sgrnggwlyn giagrnryar lhglpaarrl qqamnatvte vietaakegi
      121 dadihhggvl evartpaqla rlkafheaea afgetdrlll gaaetrarid vadavgatwt
      181 phgarihplk llrglatace rlgvtlhest pvtglaprra ttpygtvrap fvlrctegft
      241 asltgqkrsw lpmnssmivt aplpestwqr igwdgaetlg dmahaymyaq rtadgrialg
      301 grgvpyrfgs rtdndgstsa stitsltrll taffpalagv eithawsgvl gvprdwcatv
      361 sldrttglgw aggyvgsgva tsnlagrtlr dlvlgdttel talpwvnhrv rrwepepfrw
      421 lgvhalyaay readrretat htptttplar lanriagrh
//
LOCUS       WP_284578182             426 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Devosia rhizosphaerae].
ACCESSION   WP_284578182
VERSION     WP_284578182.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..426
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=46266
     Region          66..426
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mdepsssqps hrlstlaarm vaqaglvagl ggiffalalf gdlsvggavv gfiasaaaia
       61 vipsgivtit rtierqreqq pqqpaitdfa daltepcmil drravvvhan aaavrqfpav
      121 traipitlfl rnpellqaie avvrngetrs velhetvpse twdkvmvapl rragvewlnd
      181 dnrqlvitvq sltelkrvda lrtdfianas helrtplasl lgfidtllgp aakdavarek
      241 flgimrgqae rmskliddll slsriemhqh vrptatidla gllrevregl siqakasdve
      301 irltlfegpt tttgdrgqly evfenllena ikyggegkpv eislepagkp gfqhqvtvid
      361 hgpgvepehv prlterfyri dadasrkkkg tglglaivkh ivqrhrgqlt ikskpgeglr
      421 vevllp
//
LOCUS       WP_284578225             311 aa            linear   BCT 25-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Devosia rhizosphaerae].
ACCESSION   WP_284578225
VERSION     WP_284578225.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Kutner,J., Shabalin,I.G., Matelska,D., Handing,K.B.,
            Gasiorowska,O., Sroka,P., Gorna,M.W., Ginalski,K., Wozniak,K. and
            Minor,W.
  TITLE     Structural, Biochemical, and Evolutionary Characterizations of
            Glyoxylate/Hydroxypyruvate Reductases Show Their Division into Two
            Distinct Subfamilies
  JOURNAL   Biochemistry 57 (6), 963-977 (2018)
   PUBMED   29309127
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10187381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..311
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=34016
     Region          2..309
                     /region_name="GDH_like_2"
                     /note="Putative glycerate dehydrogenase and related
                     proteins of the D-specific 2-hydroxy dehydrogenase family;
                     cd12164"
                     /db_xref="CDD:240641"
     Site            order(46,65..67,90,226,274)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:240641"
     Site            order(66..67,84,90,94,138..142,160..163,165,192..194,
                     198..199,224..226,250..251,274,276..277,309)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240641"
     Site            order(93,95..97,99..100,103..104,107,109,112..113,
                     115..116,120..121,123,126,129,153,248,252,255..257,259,
                     263..264,266,269,271..273,275..276,280)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240641"
ORIGIN      
        1 mlllhlsdvd easwadklaa alapypvvrr gdafdpaevh yvfvwkpkpe afdgltglka
       61 ilslgagvda llkhpklpdv pmvrfvdtdl sqrmsdyvva qvtmhhrlyt rfradqkarr
      121 wsqlyppaas etsvgimgmg vlgqdaakrl lplgftlrsw srtpkslegv egfagdaqfd
      181 aflrgtdilv nllpltpett gvlnyetfgk lrrkldggpv ivnaargghq keadivrale
      241 dgtlgaasld vfeteplpqd splwdiency itphiaaisd eksgvsyyag iirdheagkp
      301 lpnvvdrqrg y
//
LOCUS       WP_284578297             348 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Streptomyces sp. 2P-4].
ACCESSION   WP_284578297
VERSION     WP_284578297.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..348
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33731
     Region          62..343
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mpvppagppa assaphsapa rpagreagpa gthagpavpa gpepeaaaaa asaraagrga
       61 rlgpvalvva agvsvqfgaa lavvimprag asgvvalrla aaalvllllc rpkvrgytra
      121 dwgtvvafgm amagmnglfy qaidriplgp avtlevlgpl vlsvvasrrl anllwaalal
      181 agvallaghg gggfggldpl gaafavgaga mwaayivfsa rtgrrfpqad glalamavaa
      241 vlvlplgvae agsallepst lalgagvavl ssvlpytlel lalrrlpapt favlmslepa
      301 iaatagflvl gqalgaldal aialviaasm gavrsragag agarerta
//
LOCUS       WP_284578345             357 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Devosia rhizosphaerae].
ACCESSION   WP_284578345
VERSION     WP_284578345.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..357
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36954
     Region          46..349
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msrshsprqy wvwrafdeql alrlprralf claglfllla tifaisvltg sygvpwgdvf
       61 atltgatvtt aidnvvwefr lprmlvaamv gammalsgaa lqnvtrngla dpslvgvsqg
      121 aalavvslvi afpevspslr pisafagama aailvqflst ggrrhgssir fillgigvaa
      181 fissittall tygdiqrasa altwmagsin aaswsdvwll agallvllpv llgisrqiaa
      241 lqmgedlavg lgapvrfary alitlavama aiatavvgpl afvgliapha arrlahagig
      301 ltliitamtg avlvsgadll gralfaplqi pagivtavig vptfvyllwg qaahgrr
//
LOCUS       WP_284578414             339 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces sp. 2P-4].
ACCESSION   WP_284578414
VERSION     WP_284578414.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..339
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36328
     Region          16..313
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtdtparllt llsllqtpre wpgselagrl rvstrtirrd idrlrelgyp veatlgaegg
       61 yrlvagaamp plllddeeav aiavglraga ghaiegveea svralakleq vlpgrlrhrv
      121 galqsatiav trgdgatvdp rtltamaaav agperlrfay rdrdgahtkr lvepyrlvst
      181 gsrwylvayd lerddwrtfr vdrvadpfpt garftprelp mdavdfvrrg lrgretyeve
      241 vsfgvpaqel pqwlqthaev spepgdagrc rarfesgdaa ewvaarlalt glpftvhgpa
      301 slaaaargla drlaagagtg agtgagtgqe rrgttrpda
//
LOCUS       WP_284578417             412 aa            linear   BCT 25-DEC-2024
DEFINITION  PAS domain-containing protein [Devosia rhizosphaerae].
ACCESSION   WP_284578417
VERSION     WP_284578417.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Imamoto,Y. and Kataoka,M.
  TITLE     Structure and photoreaction of photoactive yellow protein, a
            structural prototype of the PAS domain superfamily
  JOURNAL   Photochem Photobiol 83 (1), 40-49 (2007)
   PUBMED   16939366
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   6  (residues 1 to 412)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11451328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..412
                     /product="PAS domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=44592
     Region          15..306
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          <292..>335
                     /region_name="PRK09776"
                     /note="putative diguanylate cyclase; Provisional"
                     /db_xref="CDD:182070"
ORIGIN      
        1 mrppagpppe ailfrassls avdlfgvfna spnpyvildl eltivgcnda ylrvtgrtrd
       61 divgrnmfda fpadpgtpgg rllraslakv iaegepdeia lipydtsrpg eapamrywsa
      121 thtpirdgeg rlafilqhtt dvteverlrs asaaqneagi lnraaavqae nvalsqqssq
      181 lrrlfqqtps fmamvegpdh vftlvndays glvghrpdli gkpaaqalpe vveqgfiall
      241 dqvrttgepf igraapillq qgsgglperr yldfiyqpir epdggvsgif vqghditeqk
      301 vaqselerqr eilrlaqeag gvgtfvwdlv sgyiagsetl ygdrqlqmgl tsapsgafky
      361 rrsilagpfa rrgsranpvh lifgqgictc smiplaadtd pedetilqrr ly
//
LOCUS       WP_284578461             217 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Streptomyces sp. 2P-4].
ACCESSION   WP_284578461
VERSION     WP_284578461.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..217
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24126
     Region          1..182
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mvladgavtl rpirqrdhsa wrevnrrnre wlrpweatip ppapwgpvve rptyrqmvrh
       61 lraeanagrm lpfvveyegr lvgqltvagi twgsmcaghv gywvdrevag rgvmptaval
      121 avdhcfrkvg lhrievcirp engpsrrvve klgfreeglr prylhidgaw rdhlvyalta
      181 eeipegllar whrtrgqrng tgtgtgtgat gagpaap
//
LOCUS       WP_284578628             227 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Devosia rhizosphaerae].
ACCESSION   WP_284578628
VERSION     WP_284578628.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..227
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25067
     Region          12..219
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mnaphdtlsl dpfqavifdm dgtildtetv frsivfevca dlgfemsdlv hlsmvgsshe
       61 rtqqllveay gvafpytlfd ercrsimrer mhaevpvktg arelllelre rgvptaiats
      121 srqphahthl gtaglfdmfe tivtrddvvn pkphpepyll aaerlgvdpi hclaledsys
      181 gvraahaagm qtvmvpdlvh pseeiralgi aimesldhvr iaafpqr
//
LOCUS       WP_284578725             240 aa            linear   BCT 25-DEC-2024
DEFINITION  HesA/MoeB/ThiF family protein [Devosia rhizosphaerae].
ACCESSION   WP_284578725
VERSION     WP_284578725.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..240
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24787
     Region          7..240
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mssealspde trryarhlvl kgmggagqqa lkrarvlvvg agglgspvia ylagagvgtl
       61 gvvdhdsvsl snlqrqvihr teddgetkaa saarfvgeln phvrvnqhae rlapanaqai
      121 lsaydlvldg tdnletrrvv atsaevlglp lvsgavsmfd gqvtvfatgg prfadlypaa
      181 asdaelpsce atgilgpltg vigtlmamea iklitgigep ligrvlvydg kdarfseftl
//
LOCUS       WP_284578729             278 aa            linear   BCT 25-DEC-2024
DEFINITION  arylamine N-acetyltransferase family protein [Devosia
            rhizosphaerae].
ACCESSION   WP_284578729
VERSION     WP_284578729.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Zhou,X., Ma,Z., Dong,D. and Wu,B.
  TITLE     Arylamine N-acetyltransferases: a structural perspective
  JOURNAL   Br J Pharmacol 169 (4), 748-760 (2013)
   PUBMED   23517104
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Sim,E., Walters,K. and Boukouvala,S.
  TITLE     Arylamine N-acetyltransferases: from structure to function
  JOURNAL   Drug Metab Rev 40 (3), 479-510 (2008)
   PUBMED   18642144
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Sim,E., Westwood,I. and Fullam,E.
  TITLE     Arylamine N-acetyltransferases
  JOURNAL   Expert Opin Drug Metab Toxicol 3 (2), 169-184 (2007)
   PUBMED   17428149
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Sinclair,J.C., Sandy,J., Delgoda,R., Sim,E. and Noble,M.E.
  TITLE     Structure of arylamine N-acetyltransferase reveals a catalytic
            triad
  JOURNAL   Nat Struct Biol 7 (7), 560-564 (2000)
   PUBMED   10876241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..278
                     /product="arylamine N-acetyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30641
     Region          4..257
                     /region_name="NhoA"
                     /note="Arylamine N-acetyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2162"
                     /db_xref="CDD:441765"
ORIGIN      
        1 msqkvnlkay ferigfsgsi aptaatleal halhpaaipf enldsllgrp isldylaier
       61 kllserrggy cyehnlllma mlreldytvk glaakvlwsn peatdvaphh mllaveiggt
      121 tyiadvgfgg lsltaplklr aeveqetphe tfrllggdpi wrleakvaed wrvlytfdma
      181 ektlehygps ntwlssdpts pftselrval sppgkrlalk dnrftiytvg eppetreltt
      241 lkemrevlst tfgitlpgae lldpalervl tklqpaag
//
LOCUS       WP_284576998             641 aa            linear   BCT 25-DEC-2024
DEFINITION  multicopper oxidase family protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284576998
VERSION     WP_284576998.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 641)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 641)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 641)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..641
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=70291
     Region          35..633
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 malpkgtgaa pgagavgtfp aptldpttip kyvtdlvipp vmpkarhqqr hgldtyvigv
       61 rqfsqqvlps tlpattvwgy gslgddstfn ypsftieakt drpvrvtwvn dlvdsqgrfl
      121 phllavdptl hwanppggts grdsrptfts tpgpytgpvp ivthlhgghs teesdgytea
      181 wylprannip agyatvgsfy nefrdkfada hglkwdpgta tfqyandqra stlwfhdhtl
      241 gltrlnvyag pagfyllrgg esdlpkgklp gpapaygdrp gtryheiplv iqdrsfnsdg
      301 slfyptsref fdgfagpyip ttdvspiwnp effantmvvn grtwpkleve prryrlrfln
      361 gcnarflilk iansptarpa qsavpfwqig neggflpapv rlerlllana eradvivdft
      421 gipegtelyl inegadepfg rgepgvafpv adpattgqvm kfvvgplask dtsippdrlr
      481 lprirplgsa svtrrlslte ansssplvpp gtpvqnllgt ldaagnpval awadpvtenp
      541 rlnatetwel hnftvdahpi hihevtfevv drqpfngapi ppdswergfk dtviaypgei
      601 trvkarfdhp grfvwhchiv ehednemmrp fqiggrskqd h
//
LOCUS       WP_284578755             317 aa            linear   BCT 25-DEC-2024
DEFINITION  thioredoxin family protein [Devosia rhizosphaerae].
ACCESSION   WP_284578755
VERSION     WP_284578755.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..317
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33016
     Region          23..128
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
     Region          179..206
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          227..316
                     /region_name="TPR_20"
                     /note="Tetratricopeptide repeat; pfam14561"
                     /db_xref="CDD:434039"
     Region          247..278
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          283..315
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
ORIGIN      
        1 mstpfngtat gaspaappas alikessdra fkadvidasv eapvlvdfwa pwcgpcrqlt
       61 palekvvnek agkirlvkin idehpqiagq lgvqsipavf afaggrpvdg fmgampesev
      121 rrfadrviaa apasaapsds mdaqiaeava aaeealgagd lsraaqifgm vlqhqpehaa
      181 sliglsrvyl aagegaqaea tlsmvpeger kgdaytsvan sirllseaan lggtaalaaa
      241 vesnpddhqa rydlalalna egkrieaaea lvasfkrdrt wnddaarkkl leffeawgsk
      301 dpatikgrrl lsaalfs
//
LOCUS       WP_284578909             493 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Streptomyces sp. 2P-4].
ACCESSION   WP_284578909
VERSION     WP_284578909.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 493)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..493
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=53838
     Region          14..483
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mrshllnett aelyrrsvte gvervaakla stqrphtgis vdelapvvng idldrpledp
       61 aavldeleev ylrdavyfhh prylghlncp vvipavlgea vlsavnssld twdqsiggtl
      121 ierrlidwta ariglgpdad giftsggsqs nfhslllard eacrkamqaa drplaksevl
      181 prlriftsea shfsvkksaa mlgmgyeavi avpvdrnrrm dtsvlalele ecaseglipm
      241 avvatagttd fgsidplpei arlaaehgtw mhvdaaygcg llvsptrrhl ldgiehadsv
      301 tvdyhksffq pvsssamlvr nrdtlkhaty hadylnprrm aeeripnqvd ksiqttrrfd
      361 alklwmtlrt mgadgigslf devvdlaaag wdiidadpry evvvrpqist lvfryvpade
      421 vrpdlvdean lharkalfas geavvagtkv dgrqylkftl lnpqtttadi aavldllash
      481 aeqylgesla vvs
//
LOCUS       WP_284579140             317 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Devosia rhizosphaerae].
ACCESSION   WP_284579140
VERSION     WP_284579140.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..317
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33022
     Region          1..315
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mkkslftlal saamvlgaas ahaqvnvmlp anpgggwdst grqafaamne agiytdgvnf
       61 snvggaggti glaqfqstss gqedalavfg aitvgsiiln dspidlseyr plarltaehl
      121 vvavaadsei etleelvaam qenpgavpvg ggsaggvdhi alallaqead vpvaeinyip
      181 qasgaetvtg ivngtltagi sgisefqqfa dqgririlgi tsaermegld aptfqeagyd
      241 veianwrgil gapgmpdeny qtwvdrftql neseawqdvl etqgwdqyfl ageefgefia
      301 nereriagil edaglae
//
LOCUS       WP_284579228             309 aa            linear   BCT 25-DEC-2024
DEFINITION  cell division protein FtsX [Devosia rhizosphaerae].
ACCESSION   WP_284579228
VERSION     WP_284579228.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..309
                     /product="cell division protein FtsX"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=32136
     Region          25..305
                     /region_name="FtsX"
                     /note="Cell division protein FtsX [Cell cycle control,
                     cell division, chromosome partitioning]; COG2177"
                     /db_xref="CDD:441780"
ORIGIN      
        1 mierllaylp rrggtapivp ersvagrtll lmitimsfls avtlggvvlv qksaiawsad
       61 vgrevtiqir pvdgevmetn lrtavslaqs tpgvtsaral tieesqalle pwlgsgldlt
      121 aieiprlvvv qladpteadv eglarnlqsv ngasldthaa wrqqlntmag tivisgllvl
      181 iligaatvla iifatrgama tnreivdvlh yigasnkfia gefqgrflsi glqggllgvv
      241 aallffalig taagnmlsne agaqvgvlfg rfalgidgmi giaavvpvia altaitsrma
      301 vrqflsqts
//
LOCUS       WP_284579243             230 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Devosia
            rhizosphaerae].
ACCESSION   WP_284579243
VERSION     WP_284579243.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..230
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=24610
     Region          <29..218
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mgeildtgev yrrqaaaspr ldsaelvqah ieclvlldpr larvrdiaga vpprltppgf
       61 pgivkvicgq qvsvasaaai wgrfeqlpga ldpgtflsls eeqvrgagfs sgkfrtaral
      121 aeamvdglld fehveslpae eairaltahk gigpwtaevy lmfcaqhpdv fpagdlallk
      181 avqhglglda rpsikdmigi asawaphrsa aallfwryfa vlrdregill
//
LOCUS       WP_284579339             818 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-glucosidase family protein [Devosia rhizosphaerae].
ACCESSION   WP_284579339
VERSION     WP_284579339.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 818)
  AUTHORS   Varghese,J.N., Hrmova,M. and Fincher,G.B.
  TITLE     Three-dimensional structure of a barley beta-D-glucan exohydrolase,
            a family 3 glycosyl hydrolase
  JOURNAL   Structure 7 (2), 179-190 (1999)
   PUBMED   10368285
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444920
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..818
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..818
                     /product="beta-glucosidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0015926 - glucosidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=87837
     Region          11..429
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          313..672
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
     Region          730..799
                     /region_name="Fn3-like"
                     /note="Fibronectin type III-like domain; pfam14310"
                     /db_xref="CDD:433860"
ORIGIN      
        1 msriealada mtleeqvsll ssqdfwsvgg mehlgigtlr vtdgpngarg ggglvggvks
       61 asfpvgialg atwnvdllrq vgdalaeetr skgahvllap tvnlhrsvtn grnfecysed
      121 pvltaklava yikglqsrgv gatikhfvgn eseiertsis sdideralre lylvpfeaav
      181 kegktwavmt aynklngtfa senerilndi lrgewgfdgl vmsdwfgshs taetvnagld
      241 lempgptrdr gqklvdavta gqvsretvra ralsvlrlme rtralddrrp paeyaddkas
      301 hralirkaga eamvllknvg vlplpasigk vavigpnakt aqimgggsaq lnphyrispy
      361 dglhvalgdd rviyaegatn hrfqpllegs fiaeffante lagqavhiee henaeafwvg
      421 gvgdgkvdpq sfsarvtgsf vpkksglhql glfsagfsrl lvdgevvvds wtnwtpgstf
      481 feegndevvg aawleagqsy rlaiefatkp prwlglaafr agiglplgde aiaeaveaar
      541 qaevavvcig rtgewdtegs dlpsiqlpgr qnelvaavaa anprtvvvlq tggpvempwi
      601 ddvaavveaw ypgqeagnai advltgraep ggrlpqsfpv rwtdnpthsq drevypgldg
      661 hvryeegvfi gyrhyekvgv aplfpfgfgl sytqfelsef vvdtsrfeae grvavrikvt
      721 nvgaragstv vqlyvgeasp svprpqkelk afekgrlaag egatvtlnle prdfaffdle
      781 agnwrvnpgt fhlmvgtssa diayqaeivr keglairp
//
LOCUS       WP_284579367             347 aa            linear   BCT 25-DEC-2024
DEFINITION  ParA family protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284579367
VERSION     WP_284579367.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..347
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38282
     Region          4..286
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 msvvisffnn kggvsktttc fnlgwmlaer gkrvlivdad pqcnltgmvl dlsnnnalds
       61 fyannpqrnl kdalepafas rpkplepvdc vpvpgreglf lipghvglae yevslgiaqq
      121 lsesvqalkn lpgsfnylfe itaekyeady ilvdlspglg sinqnlvata dffvvpaspd
      181 vfsvmaidsl srviprwirw aesaaqleal stadypfpep klkflgtiiq ryrlkggept
      241 eafrtyfeel dsaidnvlap afrkagvlla dttyeeagld aylrlasipd fntliansqq
      301 arkpvfmltq edvgrrgfvw atqkksiesf rqvfeqlaer vevlavq
//
LOCUS       WP_284579435             479 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Devosia rhizosphaerae].
ACCESSION   WP_284579435
VERSION     WP_284579435.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 479)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 479)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..479
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=51518
     Region          8..472
                     /region_name="COG3920"
                     /note="Two-component sensor histidine kinase, HisKA and
                     HATPase domains [Signal transduction mechanisms]"
                     /db_xref="CDD:443125"
     Region          <249..472
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 magmkakrsv lpgrfsglsi kliatimgvi llvevvvylp slaifranwl edrlrvgvva
       61 arvldavpdv malprnltdr lltsagayai vyrregqsql ielaepvtpa avvtadmrqr
      121 dlfsliggaf dtlfagpgrt lrivgegdin asmvellmpe wplrqdmlay srqiawvsla
      181 iaaitavaly llasslfvhp irrltanmla frqapenaal iidpshrrde igiaeqelaa
      241 meaelfsmlr qrrhladlgl avakinhdlr ntltsaqlls dqvatlddpk vqrlaprlvt
      301 tldkaigfaq svidygreta alpvlapvgm ralvddaafd arlvghpdir fanmvpeelv
      361 lnidagqlgr vfvnllknar ealegaagnl tdavvtvgfa egedrlvlfv adtgpglppr
      421 ardnlfvafe gsaraggtgl glaiareite ahggqlslae vergtrfels lpsglrvve
//
LOCUS       WP_284579406             452 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Devosia
            rhizosphaerae].
ACCESSION   WP_284579406
VERSION     WP_284579406.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..452
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=49330
     Region          6..446
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 msepiilivd deemmrvale qwlrlsgfta hvatnateal allddvrphv vltdvrmpgl
       61 sgmdllravr eraiatevil itghgdvpma veamragafd flqkpyvpeq lvktlrraae
      121 qialkrevse lrrkldgges elatrligts rlmddlrhlv relaaiptdv illgetgtgk
      181 evvarclhdf spraagpfva vncaaipael ieselfghea gaytgardkr igkfeftngg
      241 tllldeiesm pllaqakvlr viqeraverv gsnrlipldi riiaaskadl raeseagrfr
      301 adlyyrlnma tiplaplrdr gddcvllfhh flaeaarrfd kpapslhpad vnalmvhswp
      361 gnvrelraaa erfalgldap grslgnllga easpapaaas laervaayer hvieaelarh
      421 ndsiaavvda lqvprrtlse kmsrlgvrrq sa
//
LOCUS       WP_284579464            1124 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284579464
VERSION     WP_284579464.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1124)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1124
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..1124
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=119662
     Region          118..1075
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          878..906
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(879,882..883,886..887,889,919,922..923,926..927,
                     929..930,959,962..963,966..967,970)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          917..947
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          958..986
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mryailgsvq vvrgdgtpva vggarlrall talalragra vpvhllvadv wageppadgp
       61 aalqalvgrl rralgrsavr seeggyllaa aredvdayrf erlvraaaaa vgadpaqaaa
      121 lydealalwr gpaladlpep gaeaarweav radarrgrla aalglgeaer alpelaelcg
      181 rhpldeplqa lriralrdag raaealaaye evrqelaarl gtdpgpalra lhaellappp
      241 gppgpaavpe arpgnlkarl ttfvgreedi raigadlgra rlvtllgpgg agktrlsqea
      301 aeahaagaag rqrwpdgvwf aelapvndpd dvpeavltal garetklrga saeelralte
      361 ragdeplarl tehcarrgml lvldncehva gaaaelaerl lthcpgvril atsreplgvp
      421 geflrpvepl pdhaalrlld drgaaarpgf tvaedpdaaa eicrrldglp laielaaarl
      481 rlltprqiad rlddrfrllt ggartllprq qtlravvdws welldaaerr vlarlsvfag
      541 gcdlpaaeav cadpgpgpgp gpgpdpdsgr gpgaggrgga vvrtgdvasv vgslvdkslv
      601 iaapgpggmr yrmletvaey arerlaaesg eagaaerrhl vhyrefarat epllrgagqr
      661 eagerlaady enirsalrra vaardageal clvhclvwyw qmhdlraecr hwanavaelg
      721 pdpfrapvap agpvpdriad tpppyrgeal teawrgirll qlaardqnse nwnspevrpl
      781 iegvlaayrp glpqtcrapg slwiyavmig gdaemlrrti datvetaraf dyrwelaval
      841 qlranvlanr aawagdasrd aeeslalfta lgddwgcaea lsaraearek hglyalaadd
      901 fraairhaer lgapsqvtvl rvrmagvlme sgryaeaedl ladvlrampr sygneampaa
      961 hlfmavclgr rgriaearah irrlreefam gayavfdcyl latmawldnq dgchkqalav
     1021 lrqalesard pladmvapql pavyvltaar araglggree alraarllga yrallpdghv
     1081 pvateredra raeelvrgel ddaaygaaya egggltleea aali
//
LOCUS       WP_284579567             228 aa            linear   BCT 25-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces sp. 2P-4].
ACCESSION   WP_284579567
VERSION     WP_284579567.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..228
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24145
     Region          21..179
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrsprpyslr tgpaaaqslt errkaatqld iaraacalfa ehgpdgttae diahragval
       61 rtfyryfrnk qeavapllat ggdtwramla eeapgtpvae aleraitrtl tapqavaegl
      121 evtrgllraa atdpalravw yrvnqdseea lvpvltrlts etadplsirl laaaatdair
      181 ialelwsttd tpctgpdspr elavrslral tpaiplppgp ggtprptp
//
LOCUS       WP_284579778             275 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Streptomyces sp.
            2P-4].
ACCESSION   WP_284579778
VERSION     WP_284579778.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..275
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28645
     Region          4..267
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 miltwlyapg dhqdtvakal hcgadavivd ledavpasrk eyaraatael laerppvpvy
       61 vrvnapdspw agadlaalag lrglagvrlp kvtapeqvvq vaertggval yallesalgv
      121 erayeiarah palrglalge adlcadlgcg teegldwprs rvvvaaraag lappaqspfp
      181 dirdlealaa scargrtlgf lgraaihprq lpvieraylp gpeevgaaqe vvtaarrnpg
      241 aavlpdgrfv daavlavaer vvalsrretp vrlps
//
LOCUS       WP_284579791             495 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Devosia
            rhizosphaerae].
ACCESSION   WP_284579791
VERSION     WP_284579791.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..495
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=53656
     Region          1..484
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mtrvlvvddd pvqlrltaev anhagfrpit atggeqalai lrddrnigam ildlvmpdvd
       61 gmgvldamrr eglttpviiq tsnasletvv samrngaady fvkpvaperl ivslrnvmkl
      121 daleatirae rarrtgtfts admvarapam arvlslcska artpipvlie getgvgkelv
      181 ariiqgtsdr agkpfitvnc gaippnlves vlfghkkgaf tgavadqagk faeahngtlf
      241 ldevgelphe mqvkllraiq egeiepigaa rpervnvrli satnrrllnl aksgefredl
      301 yyrlnvfpiy vpplrermed mpalvslfva rfaaeagkrv lgaspaalnl lmaydwpgni
      361 rqlqnvvyra vvladgafle pmdfpqivaq angrevarla vetaiqpaap mhidmaparp
      421 rqfedvvpaq drfldangdi aalaeieraa ivfaiehhgg rmsrvaralk igrstlyrkl
      481 heyglaqdli hdaaa
//
LOCUS       WP_284579949             328 aa            linear   BCT 25-DEC-2024
DEFINITION  MDR/zinc-dependent alcohol dehydrogenase-like family protein
            [Devosia rhizosphaerae].
ACCESSION   WP_284579949
VERSION     WP_284579949.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Gonzalez-Duarte,R. and Albalat,R.
  TITLE     Merging protein, gene and genomic data: the evolution of the
            MDR-ADH family
  JOURNAL   Heredity (Edinb) 95 (3), 184-197 (2005)
   PUBMED   16121213
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169633
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..328
                     /product="MDR/zinc-dependent alcohol dehydrogenase-like
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=35277
     Region          16..325
                     /region_name="Zn_ADH9"
                     /note="Alcohol dehydrogenases of the MDR family; cd08269"
                     /db_xref="CDD:176230"
     Site            order(47..49,52,127,131,151..156,174..175,179,206,
                     219..220,222,242..243,267..269)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176230"
     Site            order(47,71..72,127)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176230"
ORIGIN      
        1 mnvavvkpav mqaavvtgpg avvvesrplp epgagqvrvr legcgvcasn ltpwagpewm
       61 kfptepgglg hegwgiidav gedvaefaig drvaalsyhs yathdiaead avvklpdela
      121 gmpfpgeplg camnifkrad iqagqtvaiv gigflgallt qlavkagarv iavarrpfal
      181 elakkagaae viamndqwei ieqvkqltgg rfcdrvieav gkqwpldlaa eltmergkli
      241 iagyhqdgpr qinmqmwnwr gldvinaher dpkiyiqgir daieavqegr ldasalytht
      301 yrldqldeal natrdrpdgf mkalvlyp
//
LOCUS       WP_284580056             348 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Streptomyces sp. 2P-4].
ACCESSION   WP_284580056
VERSION     WP_284580056.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..348
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=36842
     Region          88..329
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 mpspaeagrp prrtlgrgpg aspapeatep apaepqeals gpaapgpapd apaaptaphg
       61 ppeaapravp gpeagapaeg aegghgrftl rldnfegpfd lllqlisrhk ldvtevalsr
      121 vtdefmahir amgpdgdldq tteflvvaat lldlkaarll paadvedead lalleardll
      181 farllqyray kriadilaer aeseglrhpr tvgledhhaa llpevvlgig aegfarlaar
      241 amqpraqpqv yvdhihaplv svreqaavlv avlrergaat fddltrdtdd tltvvarfla
      301 llelyrekav aleqeealrt ltvrwtggga gampavtdef driaeaae
//
LOCUS       WP_284580094             408 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284580094
VERSION     WP_284580094.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..408
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42606
     Region          12..408
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mashtqgvha rpadplpleg vtvvaveqav sapfatrqla dlgarvvkve rpdggdfarg
       61 ydtaarglas hfvwanrgke slaldlkdpr glevlhglla gadvfvqnla qgaaarlgld
      121 saalcarypr lvavdvsgyg pqgpyahkra ydmlvqceag lvsvtgtper pvkagipaad
      181 iaaamyafsg vlaallrrgv tgrggrvevs mldalaewmg hplhhtmhgg eqpsrtglah
      241 aviapydaya tadgdrvlls vqndrewrrl agqvlerpel addpayatna artrgrektd
      301 avvaealgrl daaeavrrle gagiacarln svaqlahhpq laardrwrev gspagplral
      361 lppiglpgga aprmgavpal gehtdallra lgmsgaqiat lrrdgvia
//
LOCUS       WP_284580110             416 aa            linear   BCT 25-DEC-2024
DEFINITION  cytochrome b [Devosia rhizosphaerae].
ACCESSION   WP_284580110
VERSION     WP_284580110.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Tolkatchev,D., Yu,L. and Yu,C.A.
  TITLE     Potential induced redox reactions in mitochondrial and bacterial
            cytochrome b-c1 complexes
  JOURNAL   J Biol Chem 271 (21), 12356-12363 (1996)
   PUBMED   8647838
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Howell,N.
  TITLE     Evolutionary conservation of protein regions in the protonmotive
            cytochrome b and their possible roles in redox catalysis
  JOURNAL   J Mol Evol 29 (2), 157-169 (1989)
   PUBMED   2509716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..416
                     /product="cytochrome b"
                     /GO_function="GO:0008121 - ubiquinol-cytochrome-c
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=46961
     Region          5..403
                     /region_name="QcrB/PetB"
                     /note="Cytochrome b subunit of the bc complex [Energy
                     production and conversion]; COG1290"
                     /db_xref="CDD:440901"
ORIGIN      
        1 msehstytpn sgvekwlder lpiirfskeh lmdfptpknl nywwtfgail vmclaiqivt
       61 gvilamhytp nvamafdsve hirrdvnggr miqafhavga smffaalyih mgrnlyfgsy
      121 kapreilyii gvlifvtvma tafmgyvlpw gqmsgwaatv itnifaaipv igtpllellr
      181 ggfavgnptl nrffslhyll pfvvaalval hiwalhvpgn nnpvgvdvks srdtlpfnpy
      241 ytvkdafamv vflipfcwfa ffapdilghp dnyiqfdsqv tpahivpewy flpfyailra
      301 idfnilfids rlggviffag sililffvpw ldtskvrsgg frpifkwfyw lfiinflalt
      361 ylgaapaegi yvvfaklcta yyfiyflvvl pvlgriekpr plptsisenv lartha
//
LOCUS       WP_284580281             327 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Devosia
            rhizosphaerae].
ACCESSION   WP_284580281
VERSION     WP_284580281.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..327
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36423
     Region          50..289
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 maqrfgagiw hfatyldrya tdgygvprni ieaidlagrv edlsvvdlnw pyfggeysda
       61 qikealernk lgvigitpei ytrdfvkgaf tnpdagirrk ahelitsacd vvrfhkadyv
      121 klwpgqdgwd ypfqvdystq wqrsldgvgq lasenpdlkf vieykprepr vrmsfgsvar
      181 tilgiekigl pnvgilldfg haimggesaa dsaqlaldhg rlfgmdvndn yrswdddlva
      241 gslhpielfe ffyvlkknkw egvwqldqfp fredsvatat haidflkaaa kgldaldvda
      301 lqeaqsrhda isalkiaqka lfgamge
//
LOCUS       WP_284580282             499 aa            linear   BCT 25-DEC-2024
DEFINITION  FGGY family carbohydrate kinase [Devosia rhizosphaerae].
ACCESSION   WP_284580282
VERSION     WP_284580282.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Yeh,J.I., Kettering,R., Saxl,R., Bourand,A., Darbon,E., Joly,N.,
            Briozzo,P. and Deutscher,J.
  TITLE     Structural characterizations of glycerol kinase: unraveling
            phosphorylation-induced long-range activation
  JOURNAL   Biochemistry 48 (2), 346-356 (2009)
   PUBMED   19102629
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426119
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..499
                     /product="FGGY family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=51639
     Region          6..488
                     /region_name="GlpK"
                     /note="Glycerol kinase [Energy production and conversion];
                     COG0554"
                     /db_xref="CDD:440320"
ORIGIN      
        1 mtasgfvlav dqgttntkal lvnangeivd qasvpnmvsy pqsgwaeqsa talmegvlka
       61 iedvlsksgs rqevaavais nqresivvwd aetgvpvgpc itwqcrrsap kcealhaagf
      121 shmveqktgl tldplfpaak iawlldnveg araraengkl ragtvdtwll wnltggtvhc
      181 tdhsnasrtq lfdtaalrwd eelsrlfsvp lsmmpevrps nslfgcvaag vsalpagtpi
      241 hamigdshaa lyghgvrttg avkatygtgs slmaltgarv lssrgissti awstadgpvy
      301 alegnisvsg qsaafmaell glkdaaqlsd lassvpdsng vvfvpalvgl gaphwradar
      361 gtltglslgt kpahlaraai eaiafqvtdv faamehdsga slsdlradgg asrnsvlmqf
      421 qadmigrpva tsaaaevsal gaaalafsgf gqfleavpfa srfapqmsdt araanllrwq
      481 haiaqtltgs akhpttggf
//
LOCUS       WP_284580312             220 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Devosia rhizosphaerae].
ACCESSION   WP_284580312
VERSION     WP_284580312.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 220)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 220)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18445957
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..220
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24151
     Region          6..96
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
     Region          120..220
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mssdnpkrvl yshfaalarl lasehrleli ellaqgeqpv erlvqltglp fanvsqhlqq
       61 lrkgglvigr rdgkniiyrl qdgpivetvv alrklaarnv aavqeivdty ftdpdelvpv
      121 staelldrmq sdsvtvldvr padefaaghl pgamnietgd lesrlselpp srevvaycrg
      181 pycvlshqai aalrakgyqv rrmaegfpew kaagypvrta
//
LOCUS       WP_284580415             299 aa            linear   BCT 25-DEC-2024
DEFINITION  TolB family protein [Devosia rhizosphaerae].
ACCESSION   WP_284580415
VERSION     WP_284580415.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..299
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=32380
     Region          11..142
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          153..295
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 mtfafprrgr tlaagqrsel tvidlqgnke vlltvnaaie apnwspdgkw lvfnaggciy
       61 rmptdasagp eqidagrlid lnndhvispd gstiyvssdd ghiyavpfsg gaprrvsneh
      121 stpfhyylhg ispdgrtlsy vavekkgper rvnvftipsa ggpdlqlthm svpndgpeys
      181 pdgrwiyfns elaasqpgha qifrmhsgdg sgleqltfda cvnwfphvsp dgqhvvflsy
      241 pagtighpad kevklrlmtp dgddqrelvs ffggqgtinv nswapdsarl ayvayplst
//
LOCUS       WP_284580363             247 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Devosia rhizosphaerae].
ACCESSION   WP_284580363
VERSION     WP_284580363.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..247
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27440
     Region          <120..212
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mlalgaarea lhrkehwvsl ltsgmvryit eqfqfvdlrg qiaslrqiyr dflehlaeep
       61 eeaverhhgr llewtrtqla vvgalelvrg tgfrpvcsny spelqlqvlg irseeikepv
      121 ldlgcgdgsl vrylcdrglt atgidrnapd gllsgewfda plgsgqwgti iahqsvslhf
      181 rsahhasasr asdyarlylr ilhalrpggr flyapslpff ehvlpseflv shssafpgae
      241 stmvtri
//
LOCUS       WP_284580432             497 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Devosia rhizosphaerae].
ACCESSION   WP_284580432
VERSION     WP_284580432.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 497)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 497)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 497)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 497)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..497
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=54640
     Region          3..486
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mpisnhafir ttvlllfvgf lalagivgtt iwlveqnsrw fdettearta rvavvglrna
       61 lqtaessqrg ylltgeehyl dpywealpsi pqyldtvvlv lrpypqaada vatittaveg
      121 klaemartid laqtgdtaaa lamirtdtgq elmaeattff dgiiaaadqr tadgiqnqrg
      181 atnalrwitv igavvifavv agsvwivlsy mrelgiarre ieeanqslee rvrertsdlg
      241 raneeiqrfa yivthdlrap lvnimgftse letsvatlst ymaeqqgedd pafkeaklaa
      301 tedlpeaitf iraatrkmdg linailkisr egrrqlrpqq inlqelvens vsaiqhqvte
      361 dggsvttdit vprlvsdrls leqalgnlld navkyrepgr pleisvrarq aagnrieiei
      421 edngrgiapt dhervfelfr rsgtqtqqge giglahvrtv vrslggditl rselsvgttf
      481 iitlprdlrs ylgtrtq
//
LOCUS       WP_284580436             569 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Devosia
            rhizosphaerae].
ACCESSION   WP_284580436
VERSION     WP_284580436.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 569)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..569
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=62009
     Region          17..550
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mallteplgg tialegarkv rgnltqarir wmilamvlgf glvggrlvql gmvvpdhsie
       61 gqtrdvitat rppildrngl emavdirvps lfaeprriid veeavrdlrt vlpdlkedwl
      121 rdrltgdkgf vwvqreltpa iqervmrlgi pgvdfitesk rfypamseas hilgstnidn
      181 qgiagierhm dsenvallqd lglargnala pvelsvdmrv qhvmheqlsd amtryqaiaa
      241 agvmmdvhtg eivamaslpd fnpnepatal vkdtfnrvts gifepgstfk tvtvagalds
      301 gavsltdqfd arfgirfgrf tigdfhgkhr ilslpevfky ssnigtirim qamgkdnfre
      361 fltrmgfder vpfelpemrl pavpetlsev gaatvsfghg lsvsplhlvt ayaafsnggn
      421 yvpptlykrd ateaqqlyrr vvspqtseai rylmrlnale gsgsqmnkaa agyraggktg
      481 taekvvdgry ssnkvtnffa safpldnpry amvimvdepk aenpqsgtta gwnagaitgr
      541 ivqrvapmlg iapdfseaid lnlvppalr
//
LOCUS       WP_284580446             277 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Streptomyces sp. 2P-4].
ACCESSION   WP_284580446
VERSION     WP_284580446.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..277
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=29434
     Region          1..270
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mlrvlavdde kplleellyl lrsdarvlsa egasdatgal rritraletg pdgpdgidvv
       61 fldihmaglt gldiarllag farpplvvfv tahegfavqa fdlkavdyvl kpvrperlae
      121 avrracdqlg rtaagpagag gglpapaapt rhgagagaap aggtpdraae iavelggvtr
      181 fvpvadiryv eaqgdyarlh tdagshlvri platleerwa ergfvrihrr hlvalgriee
      241 lrldsgttsv rvgsaelqvs rrharqlrdl lmrratg
//
LOCUS       WP_284580600             660 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Devosia rhizosphaerae].
ACCESSION   WP_284580600
VERSION     WP_284580600.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..660
                     /product="PhoX family protein"
                     /calculated_mol_wt=71258
     Region          25..654
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mtdkptfptq gletaefdpt ntsqnrtmge iiaarfsrrg flqgslavsa iaatvgpaal
       61 lsapraeaqe gssafsfpev tagvdanhhv aegydakilm rwgdpvvsga pefdpenqta
      121 eaqagqfgyn ndyvgyipld gsdehgllvv nheytnphlm fpglveivdg eavqgdlsee
      181 qvdielaahg gsiieiekvd gqwrrvadsk ynrritgttp tlvtgpaagh drlktsadat
      241 gtevlgtlnn caggvtpwgt ylmaeenfhg yfagelpegh aeaanyerlg gpggwyqwhn
      301 yhdrfdvske pnemnrfgyv vevdpmdpns vpkkrtalgr fkhegaasiv apngqvvlys
      361 gdderfdyvy kfvtagtyna ddraanmdll degtlyvakf eedgtmewmp mihgegplta
      421 engfnsqadv vietrraadl lgatkmdrpe diqpnsgsgk vyvmltnntr rteeevnaan
      481 praenafghi ieiaeddgdf aatsgtweil lkcgdpsiae vgatfttdts engwfgmpdn
      541 aavdadgrlw vstdgnnptd tgrtdglwav dtegnargts rlffrvpvga emcgpvftgn
      601 getlflavqh padggedweg hgrpsyyedl strwpdfndn mpvrpsvvvv tkqgggkiav
//
LOCUS       WP_284580677             317 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284580677
VERSION     WP_284580677.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..317
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32955
     Region          8..308
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(42,256,259)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(196,227,254,257..258,261)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mnpvprgvtv igecvadaft dparsspsrl aldvlpgggp antavalarl gtptrflarf
       61 sddvfgtlfr nhlsdsgvdl tgsvrapeps tlaianldet gqaaysffad gaadwqwtad
      121 elsaampegq taavhtgsla lirlpggrhi edyltkareh ttisidpnvr sllvpptvyh
      181 qrlhhwctla dilrlseddl alllpgatpe eacdtwhaag arlvvitlgg rgalasldgv
      241 rvtvpapavd vvdtvgagda ftagllhrla elghlgrrld tltledtada csfaarvaal
      301 tcsvpgadpp raeavgt
//
LOCUS       WP_284580699             185 aa            linear   BCT 25-DEC-2024
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Devosia rhizosphaerae].
ACCESSION   WP_284580699
VERSION     WP_284580699.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..185
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20040
     Region          9..179
                     /region_name="YdeN"
                     /note="Predicted esterase of the alpha/beta hydrolase fold
                     [General function prediction only]; COG3545"
                     /db_xref="CDD:442766"
ORIGIN      
        1 mkiseadili lpglggsspg hwqlrwaerm anagiveqad wdepelddwa dtieqavrla
       61 trpvvlvahs lavialahaa prladtnarg aflvaapdie lhpdvpeatt afrpiprnpl
      121 pfpsmlvast ndpycsvdra vefstcwgsd fhqagdaghi nvesghgpwp egllmftrlm
      181 qrlrp
//
LOCUS       WP_284580843             310 aa            linear   BCT 25-DEC-2024
DEFINITION  trypsin-like serine peptidase [Streptomyces sp. 2P-4].
ACCESSION   WP_284580843
VERSION     WP_284580843.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..310
                     /product="trypsin-like serine peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32438
     Region          117..310
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mtngphtavs nqpveltapa aeqaffegps egaqggspaa ftsdgleqva grtralsesv
       61 paeawtapsa plpdigeasf gppdlletvh gpddrvqitd taaypwrvna sllvtaadns
      121 qwigtgwfig phtlvtaghv vhikhsgvpg rdgwvksiqv mpgrngtflp fgavtstnfr
      181 svtgwtadgd enfdygalii ptelgattgw fgfgswpdad llktsvnisg ypgdqppgtq
      241 wydgrgvssv nplkvfydid taggqsgsav yrihnggryg iavhaygglt tnsgtritka
      301 vfdnlvlwka
//
LOCUS       WP_284580938             468 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Devosia
            rhizosphaerae].
ACCESSION   WP_284580938
VERSION     WP_284580938.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..468
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51494
     Region          25..468
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 msssirsyep thrlasieqa vdafsllrdf fegaiivdaq tritwmdtry rellkldpaf
       61 nplglpvedv iphsllrrvv etgrpilldi mdfddrqfvv criplkdddg qvegavgfvf
      121 ydnvdylapi lekfaslqkq ltraqaaltr erqtkytlss fvgvsdsvre lkamvrrfal
      181 rdgaaliege tgtgkellah amhqqsdrad gpfvavnvaa ipdslleaef fgvapgaftg
      241 adrkprkgkf elahggtlfl deigdmpapl qakllralqe geieplgsnt vkkvdvriia
      301 atsqdlqtrl aeksfradly yriavltiqv pplrdrledv gpiaealleq ipraqdqrgw
      361 ilqvdavqal vrydwpgnvr elrnvleraa aiapsevids glvtralpkr aaspatfrsg
      421 glsttlaate rqalidaiaa sngsksaaar rlgvsrsqfy eklkrhai
//
LOCUS       WP_284581001             223 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Streptomyces sp. 2P-4].
ACCESSION   WP_284581001
VERSION     WP_284581001.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..223
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=23592
     Region          4..215
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mngelfprer teiapgavhv pdwlgperqr sllaacrtwa rppaglrtvr tpgggtmtar
       61 qvclglhwyp ygyartavdg dgapvkpmpa wlaelgreav gaaygtappa ageapydial
      121 vnfydgdshm gmhrdaders aapvvslslg dtcvfrfgsa asrgrpyrdv llrsgdlfvf
      181 ggparlayhg vpkvhpgtap pelgltgrln vtlrvggldl prg
//
LOCUS       WP_284580987             306 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Devosia rhizosphaerae].
ACCESSION   WP_284580987
VERSION     WP_284580987.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 306)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 306)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..306
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32079
     Region          <65..130
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          147..233
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mtvrlthigv gaallalvsl plpvasqgpl gdlgtdspda vsiddvnhgr ftamggifgd
       61 qridcirchg ldgmgnssga fprlagqnaw ylyktltdya agrrpsevmv piarsmtdqe
      121 mrevaayyas iveerpyepp eadmqvlqig gaiaavglpr qgvpacssch gangeglppv
      181 npalagqfap ylehqlllwk qglrggdpmd vmariassmt eeqiravsly ygsvvtadwl
      241 tdaeaealap vvaeeitpvi pvvplvpeta apgagfapnv lppylpvfed evpsapaemp
      301 eplagq
//
LOCUS       WP_284581028             483 aa            linear   BCT 25-DEC-2024
DEFINITION  argonaute/piwi family protein [Devosia rhizosphaerae].
ACCESSION   WP_284581028
VERSION     WP_284581028.1
KEYWORDS    RefSeq.
SOURCE      Devosia rhizosphaerae
  ORGANISM  Devosia rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Thomson,T. and Lin,H.
  TITLE     The biogenesis and function of PIWI proteins and piRNAs: progress
            and prospect
  JOURNAL   Annu Rev Cell Dev Biol 25, 355-376 (2009)
   PUBMED   19575643
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Hutvagner,G. and Simard,M.J.
  TITLE     Argonaute proteins: key players in RNA silencing
  JOURNAL   Nat Rev Mol Cell Biol 9 (1), 22-32 (2008)
   PUBMED   18073770
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Hall,T.M.
  TITLE     Structure and function of argonaute proteins
  JOURNAL   Structure 13 (10), 1403-1408 (2005)
   PUBMED   16216572
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Carmell,M.A., Xuan,Z., Zhang,M.Q. and Hannon,G.J.
  TITLE     The Argonaute family: tentacles that reach into RNAi, developmental
            control, stem cell maintenance, and tumorigenesis
  JOURNAL   Genes Dev 16 (21), 2733-2742 (2002)
   PUBMED   12414724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Devosia rhizosphaerae"
                     /db_xref="taxon:3049774"
     Protein         1..483
                     /product="argonaute/piwi family protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52975
     Region          19..470
                     /region_name="Piwi_piwi-like_ProArk"
                     /note="PIWI domain, Piwi-like subfamily found in Archaea
                     and Bacteria. RNA silencing refers to a group of related
                     gene-silencing mechanisms mediated by short RNA molecules,
                     including siRNAs, miRNAs, and heterochromatin-related
                     guide RNAs. The central component...; cd04659"
                     /db_xref="CDD:240017"
     Site            order(174,178,189,190..191,194,204,207,211,215,444)
                     /site_type="active"
                     /note="5' RNA guide strand anchoring site [active]"
                     /db_xref="CDD:240017"
     Site            order(239,241,322,460)
                     /site_type="active"
                     /db_xref="CDD:240017"
ORIGIN      
        1 mvrspalskm ppfslleepl lvfsptdqth vdvhplrgla kfgpyskgsf gkyasriria
       61 tvgpesafrq rgalmaslrs sysptdrsey vppypgfeql yrvalesapp eahvrwpddl
      121 dklpgdglpq qrlsdamdaa lrrldavrte fdvvlvhfpd twlsasrgay fdahdtlkam
      181 gagyniptqv lndsafsfah kaslawrlst alyvkaagip wklaplkgvp edtayiglay
      241 alrgdqrdah yvtccsqvfd mdgggmqfva feardpvadv seaqrnpfls rddmrtvlar
      301 slelyqarng gvlprrlvvh kttafkpdei egafdalagi pevecvevgs asgwravwli
      361 esgqqkpptk psgypvprgt vvirsgssal vwvagnapqv ssksdyfqgg ksiprplqiv
      421 rhaghgsldl tahevlaltk mdwnndalyd pvpvtirysq rlartianvp ylpgkaypyr
      481 lfm
//
LOCUS       WP_284581172             921 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces sp. 2P-4].
ACCESSION   WP_284581172
VERSION     WP_284581172.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 921)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 921)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 921)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 921)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20665399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..921
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..921
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=96121
     Region          10..166
                     /region_name="AAA_16"
                     /note="AAA ATPase domain; pfam13191"
                     /db_xref="CDD:433025"
     Region          <284..802
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          <874..915
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 maagranatv ghgelikave qalaehgral ltapagagkt elagaiaaaa earqdtvlrl
       61 apeaadrwip easaaallas vpcaaletls gpqrtaiahl rretdtprag rdhvalrlav
      121 vevlrtlaar spvllvvdna qwldpestdl lrfalrltpp rvrvlvaecv qggvpvaapl
      181 cgpgtpairi pplgadevae llvrhglpar lagrvhqasg gnprlalalg hslaeaagsr
      241 dgaahhadtl plsgqareva rrllaeapar trrtlllaal aarpttallr ragrpdaeae
      301 laeaeraalv tvgedgtvaf tagalpmala adagwperaa ghaalaaavd dpvqavrhra
      361 lavdtpdewl aaeitraaad crrrgqrala aelgllaaer tpgdrpgeel arlvaaaeda
      421 gwagradlar ratravlard asrsdrvrar lavidaagqa lgtldetfay amddaegdpa
      481 lqaavrlrva wkhnlsdgdp vrardeaaea grlaaiggdq vaeamaltvr armgrilgdp
      541 daeeilaeal alpapevplg mrnapqylav rhalfddrla darrellall pavrrtgsae
      601 dvfevlrslt evelrrgrcs tasdharral eltieaglsp gpawyvaama evtggsfara
      661 agyarrgiqa seeerdqvfl srslyalglv elatgeaaka vatlrrvagl eaaqqvvdps
      721 ilrwhgelae alvaadapae avelidevga varslgrgtv vaaldrargs alsvlgeada
      781 avelltrtaa gfqafqlpve rgrtllalar aerrrrrkap araalraaaa vfeqagarpw
      841 aqlaaegpep vpaeagpava laalteaear lallvaqgas nqeaaarlfv svktvearlt
      901 riyqklevrs raqlatalra p
//
LOCUS       WP_284581231             281 aa            linear   BCT 25-DEC-2024
DEFINITION  C40 family peptidase [Streptomyces sp. 2P-4].
ACCESSION   WP_284581231
VERSION     WP_284581231.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..281
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=29469
     Region          <93..192
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mlrrsgpvgt liallavllw apapaaaaad dscrvlapga saaaeravaa aceqvaadvw
       61 ytwggghgpe pgatygqvdp ddpasehdpe rlgfdcsglv ryayaratgs dilngvasaq
      121 yythraagrf taaqglaplv pgdllvwgtp rhlhhiaiyl gagkmaearq sgtklmvsdv
      181 rlgsgyhgav rvnpgpvegp lfrtwgtgvw tkaepklsaa rvyafpgptt irvgcqkhae
      241 kvtsdgytnd vwsylpdyda wmtniyiqgp awldgvpacg t
//
LOCUS       WP_284581238             272 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Streptomyces sp. 2P-4].
ACCESSION   WP_284581238
VERSION     WP_284581238.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..272
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29539
     Region          37..188
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mdahlptqqs gpdyrferfr trlliddmtf grdalgpggr lpefdlptld ggrftsralg
       61 rrpvlmvfgs rtcpvtesav pvlkrlhtrf gervrfvlin treahpgqti rqpataaekh
      121 rhaqqlrdhh dipfevavdd idgtlhraft pkpnsaylid atgtitfrah wandetalhr
      181 aleqaasgnt vhgrsramar pllravghlp giitaagsrt ghdvwraapp lailgalsrl
      241 fprlpadrrg paaaatalia caatvglvvv lv
//
LOCUS       WP_284581445             376 aa            linear   BCT 25-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284581445
VERSION     WP_284581445.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..376
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40255
     Region          31..369
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkgtakdtaq qqareaapdg apagrepaph eplgvavvga gywgpnlvrn fqaspafrlr
       61 wlcdldadra rkvlggystv qatsdyeavl adpavdavav atpagthldv alaalragkh
      121 vlvekplaat yedglrlvte aeergltlmc dhtycytpav arirelvrsg elgeiqfvds
      181 vrinlglvqr dvdvlwdlap hdlsvldsvl pdnvrpvava ahgadpigag qscvayltlq
      241 ldtgaiahvh vnwlspvkvr ttmvggskrt lvwddlnpsq rvavydrgvd ltapqelred
      301 qrrdalvsyr tgdmvapalg ekealrtmve efaaavrhrr paltdgragl rvldileaas
      361 rslafhgavv glrtgr
//
LOCUS       WP_284581509              66 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Escherichia coli].
ACCESSION   WP_284581509
VERSION     WP_284581509.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 66)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..66
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=7615
     Region          <29..66
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mgftdnrpsa dslidmklit sdclftdkwi yklislgrfp kpiklgrmsr wragdyyawr
       61 dshsse
//
LOCUS       WP_284581611             398 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Streptomyces
            sp. 2P-4].
ACCESSION   WP_284581611
VERSION     WP_284581611.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..398
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43862
     Region          26..389
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
ORIGIN      
        1 mphreldlll edltrlaalp lergetlpar aytsedfyrl erdrvfradw lcaghvnqva
       61 epgdylrtdv lgepvvitrd edgslhalsr vcrhrfmdvl ppettpeqgs lkrltcpyht
      121 wtyrlngeya gqlagaplmn kvdfdraacr lpgyrlevwn glimicadad apalgpqlde
      181 ltaklacyrl pdlvvaysav wqgvaanwkv alengsenyh hmgshaatld pvlpgrdtvv
      241 ddcdgrwftm ytpfaadglq tadgaagtas alipglgere lsgmtiagvf phlvlallpd
      301 svtfarwipt gpethdahft vlvppeartk pgfdayvdas rqqletiqse dtvairgvqr
      361 glatnpgpsg grfshlerpl wqfqryladc lahrsrlp
//
LOCUS       WP_284581777             248 aa            linear   BCT 25-DEC-2024
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Streptomyces sp.
            2P-4].
ACCESSION   WP_284581777
VERSION     WP_284581777.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..248
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=25936
     Region          137..229
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mlrteallvl alslgasavs slisfigalt kpgalkdqaa tlngsyapgr pwldlawqlf
       61 gittalvpvl lvahlltreg vpglrvlgfd rtrpggdlar galvaagigs aglafylaaq
      121 aggfnltvqp ealpdvwwkf pvlmlsavqn avveevivla yllrrldqlg wspwgalaas
      181 svlrglyhly qgiggfvgnm vmgavfvlay rrwgrvgplv vahslldiva fggyallagk
      241 vgwlptpg
//
LOCUS       WP_284581799            1029 aa            linear   BCT 25-DEC-2024
DEFINITION  NACHT domain-containing protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284581799
VERSION     WP_284581799.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..1029
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=111501
     Region          340..1018
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mlslsdalvl lggdppalaa ldralggalg aatggigdgl lriadargsl valgrdavhg
       61 lgrrlghvqg raertallha ahtvivvvaw fealdaselp fgvddleltr geqlalagap
      121 ernargaafa halaaadapr paphrpsedv aaellrwyga lsdrflsfae glhlwsaltp
      181 sersaavral gadlaprava ryeelyarla qeapefgfwt aqvehqatrd rirlalagie
      241 ellsgaargm rppadvaaal araaeavlar pvldassapd girvpalrdm yldpdfrvra
      301 adgtggpate awweeapvrr dltgylagal tdpggahapl lvlgqpgagk svltrvlaar
      361 lpsagflpvr vplrdvraed dlqeqleqav raatgervaw pdlvrsagga vpvllldgfd
      421 ellqttgvhh sdflvrvarf qqreaeqgrp lravvtsrta vadrtrypeg lvalrlepfr
      481 paqirrwldl wnganaagla arglrplpwd avarhaplag qpllltmlal ydaadnalpr
      541 sadrpsgtga dggdpldeae lyeelltsfa rrevdktagg slpeegladl aerelqrlsl
      601 vafaqlnrrr qwvsaaelda dltallgrpa aesagfrapl gaaevalgrf ffvqraqslr
      661 dgrmlstyef lhatfgeylv vrlalhvlts lladrpalsa gasridddla yallshapls
      721 srqilrfggs marripqger erlgrllvrv fhqhgtrtdd phpayrpaan rtssrhgtyg
      781 anlvlmllll cgrttadrlf pdasdpasaw hrsvllwrss fneqqwtdfv lsvsvhrgwt
      841 dsgrslevrl rdeaqrapep ldmhwlyrrp qhdtvlwsrt ywddvwhkmd vtggttdllv
      901 rhavdpvmel lgpavtlfts sreggpatsl ahdllrllig gstglpvdel adlyrrvgra
      961 lvllpddapi repvtrllad alrrdgavlp gstllhldra glregrlrer laeavrthhp
     1021 hllrmlldh
//
LOCUS       WP_284581805             691 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional polysaccharide deacetylase/glycosyltransferase family
            2 protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284581805
VERSION     WP_284581805.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11679047
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..691
                     /product="bifunctional polysaccharide
                     deacetylase/glycosyltransferase family 2 protein"
                     /calculated_mol_wt=74955
     Region          70..262
                     /region_name="CE4_SF"
                     /note="Catalytic NodB homology domain of the carbohydrate
                     esterase 4 superfamily; cl15692"
                     /db_xref="CDD:472828"
     Region          304..681
                     /region_name="BcsA"
                     /note="Glycosyltransferase, catalytic subunit of cellulose
                     synthase and poly-beta-1,6-N-acetylglucosamine synthase
                     [Cell motility]; COG1215"
                     /db_xref="CDD:440828"
ORIGIN      
        1 mplsllacll allvlrglat neafhdsria vsvdkttvpd hllkggpvid argdrnehpv
       61 syripdrtav lsfddgpspe wtpkilevla ardvradffv tgamatrhpe lirqivadgh
      121 elgvhtfthp dlvyqshari swelaqtqla lagvagvhsa lfrppyssda tamddwnypv
      181 ikyvgargyl tafidrdtdd wkrpgvdsiv kaampakpga galillhdag gdrsqtlaal
      241 vqiidrlqaq gyrfttvsea lgassatvpv hgfqlwagkg fvwatgvavl tlpvlvglla
      301 vvgflnfgrf almlvlaplh arrsrrgnaw gppvtepvtv lvpaynerec iantlrslaa
      361 sdhpievivi ddgstdgtad iveemalpfv rlvrqanggk ssalntgiaa asydlvvmmd
      421 gdtvfepstv relvqpfgdp aigavagnak vgnrdsliga wqhieyvlgh nldrrmydml
      481 gviptipgav gafrkealrr vggmsddtla edtditiavl cdgwrivyae rarawteapa
      541 slqqlwsqry rwsygsmqam wkhrgavtsr gpagrfgrlg lplvvmfgvv apllaplvdl
      601 fllygvlfgd apitltswgg fillqaalsw yafrldgekp whlislpiqq lvyrqlmyiv
      661 llqsaitavt ggrlrwqklr rtgevaapve a
//
LOCUS       WP_284581841             338 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Streptomyces sp. 2P-4].
ACCESSION   WP_284581841
VERSION     WP_284581841.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426811
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..338
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=35970
     Region          53..239
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mkpltfprlt gaglaaclaa giahqgyael atrtrrhagf errrvrcdtg niityhvrrg
       61 tpggptlvce aglmntatsw llladfldps isvlvydrag ygsslrrcpe dyslnesvgd
      121 llqviadgag tdgacvlagh slggyiahra aaaapdrvdg vvlvdpnhpr elihsrkqre
      181 garaanltmk lgpwsatlga gllmdkkgmf afaagsphhr alrlegsaps twraalrewn
      241 ysyafmldgg rpldrlripv wvvaaestvr dipehhdlye eyvasgdggs iitipgsthv
      301 svtggtehtp htakaieqav adaaarrgdd gpdrreaa
//
LOCUS       WP_284581919            1124 aa            linear   BCT 25-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Streptomyces sp. 2P-4].
ACCESSION   WP_284581919
VERSION     WP_284581919.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13462669
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1124
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..1124
                     /product="non-ribosomal peptide synthetase"
                     /calculated_mol_wt=114350
     Region          67..>1086
                     /region_name="entF"
                     /note="enterobactin non-ribosomal peptide synthetase EntF;
                     PRK10252"
                     /db_xref="CDD:236668"
     Region          495..1004
                     /region_name="A_NRPS"
                     /note="The adenylation domain of nonribosomal peptide
                     synthetases (NRPS); cd05930"
                     /db_xref="CDD:341253"
     Site            order(631,634..639,641..642)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341253"
     Site            order(634..635,744..745,767..772,794,868,880,883,998)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341253"
ORIGIN      
        1 mttstphppg tsnqpeqprt paasdeagpq ntsgpseapr psagsgtpap peeartpggv
       61 yrrpvspter lylaagqprg amalrivveg dglpdpdrlr tavaraaqtc pgsrlvrsgp
      121 lwtaggppph vlhappargr fdvsdphtar lltdrsgpad qpgcevlvvp gaggarttlv
      181 fsashalmdg hgaltwvrev fralrgeaar paadpstdlg vlrrlaadqg grprrrpapl
      241 pgrrsplgpa aaagspsqtl wlrrtlpgrh paltarlaqa vadtarldtr amvpvdlrrh
      301 lphlaaatgn ltlplfldlr pgqdwaaaht rlltaltagg elaagfeagl vrrlpgpala
      361 allraaqsaa vrtdrhlasa vvshlgrldt gglsgggfta atayalpaha plvplsfava
      421 etadtteitl gvraadpslp rrapafldav ldrllaggad trtgapaapa vpsaqaapas
      481 atvvdlfraq aartpaaval dgpagpvtya eldrrsdava aelvrrgtar qdlvglvvdr
      541 tpegvaalwg ilkagaayvp ldpahpgprv rgvlascgar ltltrrhlvp glagfvpgel
      601 lavedvptpa qpadppaaag tapapgdlay vmhtsgstgr pkgvlvehrg laafvrwmtg
      661 lcrvgegtrf gfassyafdi scfplflpll aggtavlape apspavlral vaehradtla
      721 ltpshlalld gdgggrlrtl llggeeltpa avrsayaafg tgcrlingyg pteatvacla
      781 hvvddtetgp slplgtpgpd lrvdlvaedg tpigsgpqda grvgeivvhg vqvargyhrp
      841 dqapaepaga gtpfatgpdg mrsyrtgdlg rrlpgggiaf agradgqvkv aghriepaei
      901 taaleahpgv araavttrrr pgargpvlca yavpargtta tapaaadpaa paesgpapsa
      961 gapsadelra hlagilprhl ipahvltvaa lpatvsgktd fdalpdpfag taapptaepp
     1021 eppeppepag tdpggspaal harvarhwat vlgvdasalt adsdfqalgg dslalvemls
     1081 avsadlltpd qarrltedla vlvrdltlgr vcdrltavre gtta
//
LOCUS       WP_284581943             269 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Streptomyces sp. 2P-4].
ACCESSION   WP_284581943
VERSION     WP_284581943.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426811
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..269
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28916
     Region          9..>186
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mtttpspwtg tvtvddtala vtdtggpgrp vvylngcyad qshwrrviad lgstdfrhit
       61 fdargrgrsq rsadysfeac lrdidavlaa raveqpivvg wsygaalavn waarnpgrar
      121 gavcvdgalp hewlddaare kirklfrrls plfpvarrlg laarmsaaqh aeinieanel
      181 capavldpvl dsltlpvryv latggnlgge aqlmekirad ltpatlrnph iriaakapsn
      241 hskilrndfr avadtvrela gaprspqaa
//
LOCUS       WP_284581978            1063 aa            linear   BCT 25-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces sp. 2P-4].
ACCESSION   WP_284581978
VERSION     WP_284581978.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 1063)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..1063
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=113462
     Region          1..248
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          138..1061
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          730..758
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(731,734..735,738..739,741,771,774..775,778..779,
                     781..782,811,814..815,818..819,822)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          769..799
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          810..837
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mfhyrilgpl tvqragepva itapkerdll allllnadrp apaeqlidgi wggappstar
       61 ttlqnyvkrl rhalgdcrtg rdvlatepgg yvlrldhgvl dlrefdgltr gaaeasergd
      121 datasarlra alalwqgeal agsradrltq veaprlnelr mvafenrvqa dlrlgrhadv
      181 vgeirsaign hplrerlhgq lmlalyrsgr rgealtayrq ararlvqelg lepgpdltal
      241 hrrvladdpa ltderaplte paprsasrra qtaagqtppa qlpgstpafa gradalrrld
      301 amlpttgtvs tgtvrtalit gqggagktal avhwghrrrd sfpdgqlyvn lrghdagrpl
      361 rpidalagfl qafgvaaqhi pveadraaal yrslcagrrm lvvldnahsa dqvrplfpgs
      421 seclvlvtsr dslaglvare gatplplrtl epaeaqevll niigahrvha epgaadalta
      481 acaylplava itaadlavhp grslaeqaar ltgdrlgalq vpgdegtavr svldmsfatl
      541 spaaarmfsl fglvpggdlp lraaaalagv dpraagalld elvrshllee hapgrfsfhd
      601 llrayaaerv reqddesaal arlhawylgs tdnavrllqp ealrlpvesa gqglgfadaa
      661 ealdwmdaer pnavafvqha aengprklaw tladalrpym mrrayavdwl avgaaglaaa
      721 eadgsldgqa aahrslssay lnqsdydmsv chdrraldly rttgstegqs aahnslclas
      781 wyvgdlkeal rhgercvelg rstgfragga iatgnvgail hemgrlaeae eqltralvly
      841 delgfptaaa laernlgavl hesgrperar aaldraaeiq rrlgnqvdia ytffwlaltm
      901 irsgdragal dhidrgfeta tgearaesyl yvgrallsqs vgnhgvalkh fetarglarr
      961 cnartpelra llgladsslr lgrpadtarf aeaaresagr rgyglfeara llllaeasle
     1021 hgepeaaalr aeqaavllpe pghrhyraea lalaqrsreg atg
//
LOCUS       WP_284582067             378 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Escherichia coli].
ACCESSION   WP_284582067
VERSION     WP_284582067.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10530473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..378
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=42119
     Region          151..372
                     /region_name="VWA_CoxE"
                     /note="VWA domain containing CoxE-like protein; pfam05762"
                     /db_xref="CDD:399053"
     Site            order(222,224,226,281,307)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238739"
ORIGIN      
        1 mselndlltt relqrwrlil geaaettlcg lddnarqidh alewlygrdp erlqrgersg
       61 glgssnlttp ewinsihtlf pqqvierles davlrydied vvtnldvler iqpsesllra
      121 vlhtkhlmnp evlaaarriv rqvveeimar lakevrqafs gvrdrrrrsf iplarnfdfk
      181 stlranlqhw hpqygklyie sprfnsrikh qseewqlvll vdqsgsmvds vihsavmaac
      241 lwqlpgirth lvafdtsvvd ltadvadpve llmkvqlggg tniasaveyg rqlieqpaks
      301 viilvsdfye ggsssllthq vkkcvqsgik vlglaaldst atpcydrdta qalvnvgaqi
      361 aamtpgelas wlaenlqs
//
LOCUS       WP_284581649             377 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284581649
VERSION     WP_284581649.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Saurin,W. and Dassa,E.
  TITLE     Sequence relationships between integral inner membrane proteins of
            binding protein-dependent transport systems: evolution by recurrent
            gene duplications
  JOURNAL   Protein Sci 3 (2), 325-344 (1994)
   PUBMED   8003968
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004772
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..377
                     /product="ABC transporter substrate-binding protein"
                     /calculated_mol_wt=39588
     Region          74..376
                     /region_name="AfuA"
                     /note="ABC-type Fe3+ transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG1840"
                     /db_xref="CDD:441445"
ORIGIN      
        1 msvllatavl taltaacgaa pdepaaaaka gadaktatsa aafggveglv aaaekegeln
       61 vialppdwan ygeiikafea kypkikikse npdasssdei aavksrkgqd rapdvldlgi
      121 afarsgadeg lfapykveaw dkipagqkdp egrwyndygg yisigcdaqr ipvcpqtfad
      181 llkpeykgkv alngnptksg safggvyaaa lankgsfgdi qpgidffgql kksgnfipve
      241 stpatvekge tpisidwdyl nagyadqfkd kgvdwkvavp adgvyaqyys qainkdaphp
      301 aaarlwmefl ystegqnlwl kgyarpvllp amtadgtadn glvaklpkve gtpafpasae
      361 ldkakatlae kwdkals
//
LOCUS       WP_284582194             387 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Escherichia
            coli].
ACCESSION   WP_284582194
VERSION     WP_284582194.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..387
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=43892
     Region          1..383
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkrlqafkfq lrpggqqere mrrfagacrf vfnralarqn enheagnkyi pygkmaswlv
       61 ewknatetqw lkdapsqplq qslkdleray knffqnraaf prfkkrgqnd vfrypqgvkl
      121 dqensriflp klgwmryrns rqvtgvvknv tvsqscgkwy isiqtesevs tpvhpsasmv
      181 gldagvakla tlsdgtvfep vnsfqknqkk larlqrqlsr kvkfsnnwqk qkrkiqrlhs
      241 cianirrdyl hkvtttvskn hamiviedlk vsnmkksaag tvsqpgrnvr aksglnrsil
      301 dqgwyemrrq laykqlwrgg qvlavppayt sqrcaccght akenrlsqsk frcqvcgyta
      361 nadvngarni laaghavlac ggcqqtg
//
LOCUS       WP_284582205             399 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Escherichia coli].
ACCESSION   WP_284582205
VERSION     WP_284582205.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..399
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=44975
     Region          1..386
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mltdtklrni hgkpydgpee lpdagglsar isprgvisfq yryrfngkpr rmkigtygei
       61 tlkearaava ehkellnsgr dpsvakrmhl srvttratve divreymesp qarnmvnykq
      121 veamlgkhvi kpygsyivdd mdammwegvf rkvanggapv qagivlnrmk avikyairrr
      181 rvdrddisll cvkdvgkkpa qgkrvlsiqe ihrliglids skmarlnqil mkliiftgcr
      241 tseltnarre hfdldscvwt vpgalsknrn efkrglsgvs vallreamdl hsfdfvfvpv
      301 lsgrdeavdr svpktaardl mmrmggepws chdlrrtvrt nlsalgvaph vaekvlghkl
      361 agmlaiydqy dyvreqieam nkladyymkp idlqneits
//
LOCUS       WP_284581794             606 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 5 protein [Streptomyces sp. 2P-4].
ACCESSION   WP_284581794
VERSION     WP_284581794.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 2P-4
  ORGANISM  Streptomyces sp. 2P-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Henrissat,B.
  TITLE     A classification of glycosyl hydrolases based on amino acid
            sequence similarities
  JOURNAL   Biochem J 280 (Pt 2) (Pt 2), 309-316 (1991)
   PUBMED   1747104
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Schroeder,H.R., Yeager,F.M., Boguslaski,R.C. and Vogelhut,P.O.
  TITLE     Immunoassay for serum thyroxine monitored by chemiluminescence
  JOURNAL   J Immunol Methods 25 (3), 275-282 (1979)
   PUBMED   762437
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Streptomyces sp. 2P-4"
                     /db_xref="taxon:2931974"
     Protein         1..606
                     /product="glycoside hydrolase family 5 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0000272 - polysaccharide catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=64108
     Region          65..389
                     /region_name="BglC"
                     /note="Aryl-phospho-beta-D-glucosidase BglC, GH1 family
                     [Carbohydrate transport and metabolism]; COG2730"
                     /db_xref="CDD:442036"
ORIGIN      
        1 mtaaaeewtp plstrgrwiv dadgdrfrlr sgnwdgaqgs wngsgdrtdp aahhagqnsh
       61 giplgldrvp mpalladfra lglnsirlpf snemlrtsap vpdaavaanp alrgrtplqv
      121 fdavvaaltg agfavilnnh tvttrwccgl dgnerwnsgq ttarwaddwv avarryrgnp
      181 rvvgadlyne vrrdtfhdpn wglgddrdwh aaaqeaadri ltegnpdlli vveginwtgi
      241 pvdgfphgrp altpartlsh tlvrsgklvy sahfygytgp rhsgatgige tsdpryqdlg
      301 rdelaqvvhd qalfvaaesg ahftapvwis efgigadeaa arpkawfrnl agllsaadad
      361 faywplvgws taadgtpggd swallrydsa grrsgvpdag dwrtqpwagl aatagrtgpv
      421 apvpswhqlt tdhrdhsasl ltraggdwds garkaacpdg srlaglshtg grglcstsdl
      481 raaagahtvv rneahvppgg dwatgytklq cpadrfligy slrgsrvsaa lcapartalp
      541 aagpgrtvwf drgdarpaga gggewayghh kgqcgpgeya agiafttrfa arsgpaallc
      601 rplpta
//
LOCUS       WP_284582438             267 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Enterococcus faecalis].
ACCESSION   WP_284582438
VERSION     WP_284582438.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..267
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31028
     Region          187..265
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mnkkinwrrq ltqlekqtlt elknkemikq gtfykleqtf peesaytyyg lyrkeqtiqa
       61 yivgycfdge tleativapn vgpffeelvq elekqaalwg mkevflvmdd kqsvglnyfn
      121 rqgivpafse qylvfqrety sqdlakltll rpqvadlhsl arllegtplp edlqrtliyk
      181 ennqllatlc ldhfenewgi ygfvvtktqr grglgrqvlq salrmileks asatifleve
      241 tenqaalhly qtegfqvrnq ynyyqil
//
LOCUS       WP_284582466             260 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Escherichia coli].
ACCESSION   WP_284582466
VERSION     WP_284582466.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..260
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
     Region          <1..244
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 srlqqrisav mryavqsgii rynpaldmag alttvkrqhr paldlsrlpe llsrigsykg
       61 qsvtrlavml nllvfirsse lryarwseid idnamwtipa ereplpgvkf shrgskmrtp
      121 hlvplskqav ailtelqtwa gengliftga hdprkpisen tvnkalrgmg ydttqdvcgh
      181 gframacsal iesglwsrda verqmshqer ngvraayihk aehleerrlm lqwwadflda
      241 nrekfispfe yakinnplkp
//
LOCUS       WP_284582467             144 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Escherichia coli].
ACCESSION   WP_284582467
VERSION     WP_284582467.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>144
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
     Region          2..>143
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 maltdakirt akptdkaykl tdgagmfllv hpngsrywrl ryrilgkekt lalgvypevs
       61 lseartkrde arklisegvd pceqkrakkv vpdlqlsfeh iarrwhasnk qwaqshsdkv
      121 lkslethvfp fignrdittl rprt
//
LOCUS       WP_284582599             398 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Enterobacter asburiae].
ACCESSION   WP_284582599
VERSION     WP_284582599.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Enterobacter asburiae"
                     /db_xref="taxon:61645"
     Protein         1..398
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=44003
     Region          9..387
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 miknqhsslw rwicarilal aigsviviat clwlryavqn ywimgkmpaa vrqefltlsq
       61 npqanparfh sivdtwwgls ystpsiasad watvallvlv mipfivvmgl kharplalqf
      121 srlrdaakdv adgqfgrqae liedapaemv sfatdfnsmt gqlaryekel rashvamahe
      181 lrspltaaig rlqgmldgvf daspaqlgmv mkqlqhlnrl tdelhllsla dagnlvledk
      241 lfcldeliqe raawimpead ahhfritlrn prtspfrgda frlgqvvtil menalrygrd
      301 gghlevalhy asghyileft ddgpgvspqf lpemfkrfsr eeqsrarhsg gsglglsiar
      361 aiceahggei saslpetggl avrillpwhp sgnenlhs
//
LOCUS       WP_284582708             219 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Escherichia coli].
ACCESSION   WP_284582708
VERSION     WP_284582708.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10106962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..219
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=24073
     Region          17..189
                     /region_name="vWA_subfamily"
                     /note="VWA subfamily: Von Willebrand factor type A (vWA)
                     domain was originally found in the blood coagulation
                     protein von Willebrand factor (vWF). Typically, the vWA
                     domain is made up of approximately 200 amino acid residues
                     folded into a classic a/b...; cd01464"
                     /db_xref="CDD:238741"
     Site            order(27,29,31,94,131)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238741"
ORIGIN      
        1 mseqitfats dfasnpeprc pcillldvsg smngrpinel naglvtfrde lladslalkr
       61 velgivtfgp vhveqpftsa anffppilfa hgdtpmgaai tkalnmveer kreyrangis
      121 yyrpwiflit dgaptdewqa aankvfqgee dkkfaffsig vqgadmktld qisvrqplpl
      181 qglqfrelfs wlssslrsvs rstpgtevvl eapkgwtsv
//
LOCUS       WP_284582718             362 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Escherichia coli].
ACCESSION   WP_284582718
VERSION     WP_284582718.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..362
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=40565
     Region          22..137
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 merlnlsekp ahslqesaih caryanilhl vkdkvvldia cgegygsall mkagakrvvg
       61 vdiseesier akklfgkydv eyivsdanti serygedffd ivvsietieh intpdvflss
      121 ikktakenai fyitcpndyw yypnneqsnp chvrkytfqe fkelstgvlg nnvqwayggs
      181 vfgfgtvsan nrglekigss wmeisesens invlnteida vnenncsffv glwnapetnf
      241 snstfpismd aysrmteefe snvssvlred qaenkkaisi lkkdmkqltm nlrksnllls
      301 alkienvtlr kniselqqql akqiamyhdv tnaknnlele nadlislhgd latallnksn
      361 fc
//
LOCUS       WP_284582813             401 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Empedobacter falsenii].
ACCESSION   WP_284582813
VERSION     WP_284582813.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..401
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46390
     Region          81..383
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkilwkiikw fiiiicvlil tlyatgndyi frgvkltymk gektanindy kdfdnnvila
       61 gsprvwhqhl dynqfplsvn fekemkdfgt agfviikdhq ilseyyfngy aqnditnsfs
      121 maktfttmml gkaieqgyik sldqkitdfi pefkddrfgs qctigdlsam tsgydwdedy
      181 yfplnptaka yygddivkqm ldrkfvsqpg khfkyqssdt qllgiviera ienkslsqyf
      241 qdefwqpmgm emdaqwskds pkgmektycc fnattrdfak lgqlllndgn wygkqildst
      301 fvqkmvlpnk kafepnepki ygysvwmdyd yktpfyamlg hlgqrvivip sekiviartg
      361 kthndlpnnh piadgdvyrl vdeamrinqk ikendptnsl q
//
LOCUS       WP_284582924             331 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Empedobacter
            falsenii].
ACCESSION   WP_284582924
VERSION     WP_284582924.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..331
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=38206
     Region          5..256
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkiafifggs gyiayflink lieenkfdki ilfdiqkpkf fdnslpdnve yiycdvrnki
       61 yylidfnlki edswiynfaa ihrepghnrk eyfdtninga eninefaenl nirnifftss
      121 iapygkskee cseksmiyae tpygiskgla ekihqiwlak sndrrlivvr psviygphdp
      181 gniyrtiral kkgtfmlpng gdiikaygyv ygliesmlft mdqkerliiy nyaenpilnl
      241 kemiqtikke lgytkptfgi svnflvfvag iiqigfkiig kksdihpvrv kkaafptnik
      301 pnyliekgfk fnyglkeslk hwksiapedf d
//
LOCUS       WP_284582954             208 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Empedobacter falsenii].
ACCESSION   WP_284582954
VERSION     WP_284582954.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469162
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..208
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=23582
     Region          41..160
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
ORIGIN      
        1 mktifltiat lfsisafaqn kfesdlstil vewnkgnhss eanfkqlind ypnewlpkyy
       61 lslseilktf esndadynek ilsqvkiqld dllksnplnt eilnlkalyl taeivqnpmq
      121 ngavyygevl qiyqkslaln ptnprsvlgl aefninsaky sgmditqyck nvkkslalfd
      181 aekpknnepk wgknraqnll nnecktvq
//
LOCUS       WP_284583018             814 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Empedobacter falsenii].
ACCESSION   WP_284583018
VERSION     WP_284583018.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 814)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..814
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..814
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=91472
     Region          550..805
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mkkivysllf lamtigtsvk aqenvtfqlp pqeilqlaea dmppsistdr kaenaflsyr
       61 sryktinels etelrlaglr inpvtninsr etfsekitff dlktskekti aglpakgrfs
      121 nqswnksqsk favtnttdkg velwvidvkn qsatkvyedk lnanlgrpfs wvsdselivn
      181 vipaskkali dtkdaiatgp tvsvadgkea qnrtyqdllk nktdefnfeq laiselvkvn
      241 ietgakskwk daamytnist spdgqyvlvn eikkpfsylv tyssfpstdv vydingklvk
      301 evdykelqev vpkgfsstim gkrglywrad kpntlywvea ldggdankpa eyrdalyqva
      361 apftankell vkikdryrgv twgndevali rdawyntrne syytfnpsnp kqeptrffsr
      421 ntqdaynnpg sfvteineyg ynvlsinkgk lmlvgdgvsa dgilpfvddf diktqktsrl
      481 wraqksdkle viarvidpkk giileqiqsk tdypnlyvrn ifqkggkpkq vtftknpfea
      541 mnqvskelit ykradgvels gtlylppnyd ktkkeklpml mwayprefkd aatagqvtts
      601 enkftspsyg gpifwalrgy avlddaafpi igegkeepnd tfvpqlvana kaaidavdal
      661 gfidrekvav gghsygafmt anllshsnlf aagiarsgay nrtltpfgfq seqrnyweap
      721 evyntmspfm naekmktpll lihgdsdnnt gtfpmqsery fnalkglgat trlvllpkes
      781 hgyaakenvl hmlweqdqwl ekyvknkgkt sekk
//
LOCUS       WP_284583219             843 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Empedobacter falsenii].
ACCESSION   WP_284583219
VERSION     WP_284583219.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..843
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=94678
     Region          <63..154
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <356..838
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 maikntqetp ktskkqiikt ivgiiflvlg lllfvsflsy ffnglidqsq isdlldkset
       61 aenifgkfga llgetfilqg igivsffipi ffmllgikva tnwkkikpfk tlyqsiffmi
      121 wlpiffgcil pqqhmlsgvm gfevndflns figklgvvll lfvslliycv ihfrmtyqsi
      181 qqkmeerakq keldriekeq ekikkeqlel rkrkeeeeqe kinkfnqeve kqqenesiee
      241 lklvenfeke aikshtvspn esfsqeftin qpqeeeqiee spvnitelvv deieenseie
      301 pisensvtss kqeasndlel kvqkideeee featsarlvq eqgeynqrld lpnfqfppis
      361 llkkydsgnt lidqkelesn knkiietlgn ygigisqita tigptvtlye ivpqagvris
      421 kiknleddia lslaalgiri iapipgkgti gievpnsnps mvsmhsvias qkfqnsdmel
      481 piafgktitn etfvadlakm phllmagatg qgksvglnai iasllykkhp selkfvmvdp
      541 kkveltlysk ierhylaklp daeeaiitdn tkvintlnsl ciemddryel lknafvrnlk
      601 eynakfkerk lnpeaghrfl pyivlivdef adlimtagke velpiarlaq laravgihli
      661 vatqrpsvnv itgtikanfp arvafrvtsk idsrtildsp gadqligkgd mlfttgndlv
      721 rlqcafvdtp evdkitefig eqrgypdalh lpeyvgedgg snldidlsdr dvlfedaarl
      781 ivmnqqgsas llqrklklgy nragrlidql eaagivgpfe gskarqvliq ddmsleqlln
      841 nln
//
LOCUS       WP_284583229             227 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: LolA family protein [Empedobacter].
ACCESSION   WP_284583229
VERSION     WP_284583229.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter
  ORGANISM  Empedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Tajima,T., Yokota,N., Matsuyama,S. and Tokuda,H.
  TITLE     Genetic analyses of the in vivo function of LolA, a periplasmic
            chaperone involved in the outer membrane localization of
            Escherichia coli lipoproteins
  JOURNAL   FEBS Lett 439 (1-2), 51-54 (1998)
   PUBMED   9849875
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Empedobacter"
                     /db_xref="taxon:59734"
     Protein         1..227
                     /product="LolA family protein"
                     /calculated_mol_wt=26043
     Region          1..227
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mkkvlmlklt fsmlmislfs vatyaqeaeq iienhiqktg geaawnnlns iilkgeviin
       61 vgdsypmivy hqrpynkkvv fvmngkeiln egydgkigwt ysevakknva vknykpdsfd
      121 sdilkykqkg fkvkylgidk ydqnnscykv eltkntnstv ycfdknsyei vmeknkeetl
      181 yysnfktfng lsfatkvvgk pteggeyiik fndikinpai dkkhfkf
//
LOCUS       WP_284583259             448 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Empedobacter falsenii].
ACCESSION   WP_284583259
VERSION     WP_284583259.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..448
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52290
     Region          234..445
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mknnvflsmn lskkyysilf afvllilval qvyyiynsyr lvekdmnkea aeialkvmnk
       61 mnefqkaide dnlinsfkkl shekgkqfde lnvirlnidn nhqlftskvd slidfysker
      121 nyqialkmei ysvydeinhv ellpqkplvm yrsstkiihp ksinqsvwss ddisnqtdsd
      181 lgidkserhk ykiksqtnye llnlnflvlk kiiplivvsl liialiifly wksiqnlskq
      241 eekinqlhlt idsiahelnt pittmkfalh qvqhneikem inrqinrlen tvdsifvknd
      301 ennklldevi lneiiqkiql qfpainithq iifekngrll tkdfqqifqn liensikyga
      361 seilldfkfq keitlnfsdn gigipindlp fifdkyyrvd rsinqnvsgl giglylvkti
      421 ierylgtinv ennkekgvqf livlpnen
//
LOCUS       WP_284583319             295 aa            linear   BCT 25-DEC-2024
DEFINITION  rhomboid family protein [Empedobacter falsenii].
ACCESSION   WP_284583319
VERSION     WP_284583319.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Koonin,E.V., Makarova,K.S., Rogozin,I.B., Davidovic,L.,
            Letellier,M.C. and Pellegrini,L.
  TITLE     The rhomboids: a nearly ubiquitous family of intramembrane serine
            proteases that probably evolved by multiple ancient horizontal gene
            transfers
  JOURNAL   Genome Biol 4 (3), R19 (2003)
   PUBMED   12620104
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10483871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..295
                     /product="rhomboid family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33846
     Region          22..210
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
     Region          253..290
                     /region_name="DUF6576"
                     /note="Family of unknown function (DUF6576); pfam20216"
                     /db_xref="CDD:466367"
ORIGIN      
        1 mtnnilddlk lkyssgnsat kliyinvvvf ftllivdfil rtvansiint tdlfalssfd
       61 dlltkpwqif syswlhgnlf hlimnmvlly fvgqmflqqf qnrnlvtfyi fggitggiff
      121 llfqnifnys hllvgasaav yavffgmisy npkmlvrlll iltsfpllyv gyffiafdvy
      181 niianqnagg sishlggaif gylymkqfek gndflgnfii kieqlfqkkd kstfktyknt
      241 sststrtnvp kddydfnhqk vekqkkidvi ldkisrsgye slskeekdfl fkegr
//
LOCUS       WP_284583334             193 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Empedobacter falsenii].
ACCESSION   WP_284583334
VERSION     WP_284583334.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..193
                     /product="YceD family protein"
                     /calculated_mol_wt=22191
     Region          1..192
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mdklknynii ftslpfgksn ftfelsqsff dlfeieqdfe nptmiasiil dkkstmlele
       61 islkgnitvp cdltgelfqq eisnnaeliv kfgdefddtd feiwvipree yqinlaqily
      121 elamlsvptk rihpdvlnge snsemidlld qysiyelded aenveddndn dngdvddndd
      181 idprwaklkd lkp
//
LOCUS       WP_284583400             152 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Empedobacter falsenii].
ACCESSION   WP_284583400
VERSION     WP_284583400.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..152
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=17240
     Region          <17..144
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mkhiikmidq eltvfeinte gkkyyipnfg qvnagfpspa edfvndkisl derylthpes
       61 tflivvggds mypvyqkndi lvirtdlipl hnddiivsvn hddytlkrfd kvnnklvaln
      121 asykncvqiq esdeviilgv vgvlvreksn ri
//
LOCUS       WP_284583420            2030 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Empedobacter falsenii].
ACCESSION   WP_284583420
VERSION     WP_284583420.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 2030)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 2030)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2030)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 2030)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2030
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..2030
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=232975
     Region          368..2030
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mkqflfllli ltnsmlmaqs ptidqkwkei dqqmqngqfk slqpkidelk tlskkennqq
       61 sylkalfyes kikvatsdek ddvnfvfdlf kkelneksnv nnaitnsyla dlyqlyfnen
      121 rwkinsrtti enqatndvrf wteetfkkti nnyfsksiqp knelinaksq eykmilnlad
      181 dkkkaqeqld ltptlydvlv rnyinylnqn dekdkanqll sdlveinkqk nnenavlyne
      241 lillenkrds isiqdfikqk eilatkypka wyssyvyatl atdyygleed klanvkkifd
      301 iqeklaklyp nseekrvvdn lvskikaqel nvlaekyine nqntpiqlth knlnkvyvkv
      361 laynagfddk qksqilnvyn enriteaqnf lnslkvvdqy vldvksfedf qnhstivkln
      421 plnagryivl fsnhsefkin tkddidyldi mvskyainsl ndklsvvnre tgkpestisv
      481 efsnltnynk kefktlvsdk ngmiqipsgw rnfqyrvkde htiystyyyd ydrydedded
      541 fsvqiftdra iyrpgqtvyf kgiyftnkgk erqvlpkkkv tifledvngk diteielttn
      601 efgsvngnfv lpangltgdf riyaenddvd elgshsfkve eykrpkfkve ieknkgvysl
      661 ndkvkvegka iafsgatidn akvsyrvyrq eiftfwpwyr sipvgrgerd eitfgdtttd
      721 aegkfnfefv akpasekkkd evrtynyfie vnatdinget qsesssvkvg dtrmslnvai
      781 sektkaddlk vfkvevknln dekldgkghi eiyslnapke ivrrqkfttd yniyskeefk
      841 kifpnepygd emnpktwttn qkvfesdfdt kisdeikfnq asnleegyyv ikgfvfdgtq
      901 kvevdkliyv snekkanaik tllavslnks tfepkdvaki efksgskdty vyyeveanql
      961 iiekgfldls kksvveipik eeyrggiyvn yamtkfndvq tgslnlavpf tnkqlkvsae
     1021 vlrdkltpga kekwqlkieg pnkdkvsaev lasmydasld qfasnsldfn vynftnsrrn
     1081 npfnlyqfys tnpsraiyyr tnydfyargy agldlnlfdf gfnqyrmnrm mrksaapnqp
     1141 stitervegi qmepaadvsl egsvvtalgi trdkkslgya ssdsisirgi sssdnpnaly
     1201 vvdgvvydka qelnpddvqs invlkgeqat alygargang vvvittkkga nvaldnvkar
     1261 tnlnetaffy pnlktdakgn iiveftapes ltewkfmaia htpdlktgyl eqnvrtqkdl
     1321 mvvpnmprfl regdqisvss kinnlsekil ngsaklmlfd aftnqpidaq fkltnavqnf
     1381 svakgssdqv twtidvpknv qavvyrvvas agdfsdgees alpiltnrmm vtetlpiyvk
     1441 egqkksfqfd nminnkstsl dnfkltfemt tnpiwyavfs lpylreypye caeqvfsrly
     1501 gnmisekvin snpkikavfd dwnkkgelks klqlnqelkn iileetpwvk naeseeeqmk
     1561 qiavlfqlnq mqtemksafq klsdkqqsng gfvwfdggrp neyitthivs gfgnmkkmev
     1621 nfkafemdvn plikkaiqyi dnenlnrfke fkkdqksfkd vvysdglhyl yarsffledy
     1681 pmskdleemk namlknlnds kfdlslqqka maaivmnrfg mqsaakivvn sikekavesd
     1741 emgmywkenq pgwfwyqapv etqaflieaf devskdeksv eemkvwllkn rqtnqwnstk
     1801 attkavyalm nfgkswidad kgitvkignt nfdldknsqa gsgyvktswn keeikpemgk
     1861 vevaktspgv awgamywqyf edldkiksae tgiqfnkklf vktnsangpv lkeittstpi
     1921 kvgdivtvrl eisidrnmqf vhikdmrasg fepvnvlsgy kwkgefgyye strdaatnff
     1981 sdymrkgtyv feydlkanna gnfsngitsm qnmyapelsa qsegirveik
//
LOCUS       WP_284583530             432 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Empedobacter falsenii].
ACCESSION   WP_284583530
VERSION     WP_284583530.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..432
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=51286
     Region          4..429
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mknkisifwf rrdlrlednv glyhalssgv pvlpififde gilrqlddkk drrvdyihqa
       61 lqkinnqlks fgtslnvyyg dplkifqqls tefaihsifc nrdyeplaik rdtsiynyfk
      121 lfnisfkafk dqvifdkkdi lkkdsspytv ytpyakkwkq ilktedykcy npdyskflkt
      181 efktilslke igflktsilf dqpklnkeii qnyhkyrdyp alqhttqlgi alrfgtisvr
      241 kcvalaieln etwlneliwr effmqilyhf pyvvhqpfka kyneikwrnn eqefklwcdg
      301 ktgypivdag mrelnqtgfm hnrvrmitas flckhllidw rwgeayfask lndydlsann
      361 gnwqwvagsg cdaapyfrvf nptlqtekfd keylyikkwv sefetddyps pivphnfarn
      421 rvlsifndal kd
//
LOCUS       WP_284583556              92 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Empedobacter].
ACCESSION   WP_284583556
VERSION     WP_284583556.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter
  ORGANISM  Empedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Empedobacter"
                     /db_xref="taxon:59734"
     Protein         1..92
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=10534
     Region          20..77
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mdnlilekll sietllldkk kvlnpdelan ytgyskstiy kmvqgniipy skpngkhlff
       61 dkeeidewll snksksklql qneaskyans rk
//
LOCUS       WP_284583586             242 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Empedobacter falsenii].
ACCESSION   WP_284583586
VERSION     WP_284583586.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..242
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28629
     Region          25..146
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mdlqwfvkwf nspyyhilyk nrslteaedf ikkithylql pqhaklldla cgkgrhsitl
       61 nklgfdvlgi dlaeasisfa kqyenehlkf evhdmrevyh pnefdavfnl ftsfgyfeky
      121 ednfsvfeav kqqikshgif vldylnaekv vshmipyeek vidgilfkit ksiengfikk
      181 eidfedkget fhfeeyvrli yfndfkkiye tegfvldkaf gnynlddfne qtsdrlilil
      241 nk
//
LOCUS       WP_284583653             588 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Empedobacter falsenii].
ACCESSION   WP_284583653
VERSION     WP_284583653.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 588)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..588
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66778
     Region          3..588
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mkqpqrvfdl prfqekntpn itifnykekd ewkgisttdf inrvnniskg liangvqpnd
       61 kvalisenrl ewnlvdfaiq qigavvvaiy pnisdndyef ilndaeiklc ivsndllyqr
      121 llglkdrvpn leqvytfnty phtpnwielv skgisvsdet lqtsmdkvkt tdlatliyts
      181 gttgnpkgvm lshenlladv nsseysfpvq aydkalsflp achayervfq yvyikmglsi
      241 yfaqsmdtig qdlkevqphi fsavprvlek vydrimskge eltgvkrklf fwaislgeky
      301 dldesklssl ykfqlkiark lifskwkaal ggnikgvatg satlqtrllk lylaagipiy
      361 egyglteagp clsvncikrg mkigtvglpl idieiklaed geilakgkni mqgyyknpea
      421 taevlkdgwl ytgdigewvd gkflkiidrk kemfktsggk yivpqqiekl lsesifieqi
      481 mvvgegrkfp salivplyen clewakqnep silnlsreef ikhpkiqell aneinklnvn
      541 fgnwekikkf hllpyeftie ageltptlkm krkvilekyk teiediyq
//
LOCUS       WP_284583684             108 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Empedobacter falsenii].
ACCESSION   WP_284583684
VERSION     WP_284583684.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..108
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11711
     Region          2..108
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mnwillilgg lfevgftssl gkaketigse mymwygifgv clvasmflli katqtlplgt
       61 ayavwtgiga vgtvlvgifv fkepanfwri ffiftlissi vglkfvsn
//
LOCUS       WP_284583703             253 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Empedobacter falsenii].
ACCESSION   WP_284583703
VERSION     WP_284583703.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 253)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 253)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..253
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=29640
     Region          1..250
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mriaivedel lavtylknll edqtivdvss iiilrsrkqa itffkehsvd lifmdihlgd
       61 gksfeifqev elltpiifit aydeyamkvf khftidyilk pfeveelhia lqkfnsirts
      121 fdiaptlksi tvlenspsei mhrflvtngn klrsveehei ayffasgkhl fmktkdeqty
      181 iyddtikdii nkldetmffk inrkfivhid aiteiikhss qkieiylqpk peteqaviis
      241 kthinswmdw mnr
//
LOCUS       WP_284583769              83 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Empedobacter falsenii].
ACCESSION   WP_284583769
VERSION     WP_284583769.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..83
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=9515
     Region          <12..77
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mlnshlmtde nwnnfkkvfa sekadfvsyl ennfsdltes nlriiyltkl gltnieiahl
       61 lgitpdsvkk akqrlrkdmi imn
//
LOCUS       WP_284584007             328 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Empedobacter falsenii].
ACCESSION   WP_284584007
VERSION     WP_284584007.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..328
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38685
     Region          6..328
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mavnknalir yktldkcfsn pyrkfyledl iekcneilsd hygeettvsr rqifldiqfm
       61 ksdagyeapi eslkdgrkvy ykyddpdfti erkpftnder ltientielf srikgipgfd
      121 aiesiktklt evkdsqsenn iidfeenefl igiehltply nyiknkqvll vayqsfksne
      181 lqeffispyy lkqynnrwfl fgwnhkgeyi qnlaldriqs iesineqynk snidfteyfe
      241 diigvtnpld kevvqvkiql sdniipyiks kpihgsqkiv dnilnlnvkl nyelesvils
      301 ygenmkvlep ielinnlkqr inqlkdfy
//
LOCUS       WP_284584031             290 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [Empedobacter].
ACCESSION   WP_284584031
VERSION     WP_284584031.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter
  ORGANISM  Empedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Empedobacter"
                     /db_xref="taxon:59734"
     Protein         1..290
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=34843
     Region          <42..170
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          57..87
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          92..117
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdynklfndi fflilddemd enqypiwksf sfihnpiqql ikaqdllnql lhefpkdkka
       61 lflkgvvqrn lnfneesily lleakkedyy lyaanfyiae yyihklkfee aqkylkeiei
      121 vypsnkrflf lsilvslelf dfesakryln ilyqlvedkk vlellsenlq iteeivlktt
      181 nrlvlknfkl rsfnynlqlk tnlisfyknf adigvnfngi ncfimaltlk qitlyptfqy
      241 femytvqtvl dyidvdkkgv qmrlddinfd qdfvknyhey leveillked
//
LOCUS       WP_284584042             105 aa            linear   BCT 25-DEC-2024
DEFINITION  MgtC/SapB family protein [Empedobacter falsenii].
ACCESSION   WP_284584042
VERSION     WP_284584042.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10491715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..105
                     /product="MgtC/SapB family protein"
                     /calculated_mol_wt=11849
     Region          <3..35
                     /region_name="MgtC"
                     /note="MgtC family; pfam02308"
                     /db_xref="CDD:460528"
ORIGIN      
        1 mqliglfags glsiqavilt ciimlahlll rpisnqiyry sfknknhkdt eyllvikcrn
       61 dvenhlrvll mrsiennenl mmkslssddd lindsvmisa eisar
//
LOCUS       WP_284584094             212 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Empedobacter falsenii].
ACCESSION   WP_284584094
VERSION     WP_284584094.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008387
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..212
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=23240
     Region          3..195
                     /region_name="TerY"
                     /note="Uncharacterized conserved protein YegL, contains
                     vWA domain of TerY type [Function unknown]; COG4245"
                     /db_xref="CDD:443387"
ORIGIN      
        1 mnrrllayfl ldtsgsmnge piqalnngfn glinmlrmdp qamdslhisv itfdrevkni
       61 iplvdlasfq pmeiecpssg pthtgealem leklvnkeii kgspdrkgdw kpllfiftdg
      121 kpsdiqkyrn iipkikaldf gvivgcaagp kaevsflqel tfdvvkldtt dantlstffk
      181 wvsssiemgs ksqgtgeklt lppppselni iv
//
LOCUS       WP_284584137             691 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Empedobacter falsenii].
ACCESSION   WP_284584137
VERSION     WP_284584137.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 691)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 691)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 691)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 691)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..691
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78433
     Region          6..592
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mrkffvlavt lsgifafgqe eiqdsidynp ieieevliqs qrkkmfadka vytfdkeale
       61 karyakdlln tlpelnvdpi snsiqstkgg ttlllingie atdnqiravk pqdvvrveyf
      121 dipptryanr adqvvnlitr npengyvfga egvtspltgf vdgsayanft kgknnfgvey
      181 slslrdydnr entnsyayql nnnqyktteh rfdhfgytfq nailrytntd sdkytfqakl
      241 dleiltsftd vngksiflmn nvsenhttyk hgnsgytkpt vdlyysrklg kkdelslnfv
      301 gsifntdtye lskewvtnte nsvfnnemkl kaeqtsivge vahthdfksg klssgyritt
      361 ndinndlvnl dgssrykvny lqqymytefs gktkklmyrl gmgltninnq saedsqntwt
      421 itpkivlgye laknqnlrft ssytprspws dalssnvvqm vpnivrkgnp elniqktfsn
      481 nliysynsky fdlnttlfys hrkdainqly vldgnryalt yenaqnaqsl gvqvsgsikp
      541 fgtdlltlkl vltptsesvk lndgktiknd yignnfvins vyknfslmya fnipvyslsg
      601 pfldtnenks hlvlsyklnn wsfktgaywl gmpseyksks vaesivqttn htqiwnnknm
      661 filgfsydfa tgkktninrk lqnqtagaat f
//
LOCUS       WP_284584143             390 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Empedobacter falsenii].
ACCESSION   WP_284584143
VERSION     WP_284584143.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..390
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=43285
     Region          2..388
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mkkdqskiir eqaprsatre hsvplyltss fifdsaeqgr aifaeeeegm vysryanpnt
       61 tefinrvcvl ekadaglafa sgmaavfasf asyiksgdhi vssraifgst hqlitqlfpr
      121 wgvtytyver pniedwekai qpntkivfle spsnpglelf dlealaklke khphiifaid
      181 ncfatpylqq plefgfdlsi hsatkymdgq grvlggvvig kqdlinemmf firhtgpams
      241 afnawtisks letlplrmdr hcenalalae alesnpeiea vkypflpshp qyelakkqmk
      301 ggggivtfev kggkerafkf idalkmilyt snlgdsrsia thpattthak lsdaeraelg
      361 impgsirlsv gledkidiie dilqalektk
//
LOCUS       WP_284584160             459 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Empedobacter falsenii].
ACCESSION   WP_284584160
VERSION     WP_284584160.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..459
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=54026
     Region          <8..222
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          133..159
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          138..393
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          166..193
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          201..227
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(203..204,207..208,210,234,237..238,241..242,
                     244..245,268,271..272,275..276,279)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          232..262
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          267..295
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          301..329
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          335..363
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          368..398
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          403..431
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdedffnnel ierfeqmlen reykyydsed lveiiefyie vndseyakra ldfaekmhpe
       61 nieikikkie ylllinelkr sakliqelkv iaaneldyll vqarfwgmkn msrkairfye
      121 ealsidddet dficncigne flnldevqsa liafrkalkf npendysfys iiqcfeeihn
      181 peecidflkd fiddnpysev awlqlgllyn hkkmfkeain aldyviainp nsivghtnka
      241 fsfeelgdyn kaietleetl eyddspalth fkigelyekl kkpqkalkay hiaikedpql
      301 dkvwaksaal ydkmgnldea eyyiqraiel nddnseyytn styyflkqmk feealsslvk
      361 lvelkplvfn twfayvetli aigeyeqaia vlltgalknf nraeffyqls nvyylidedr
      421 lgnealrnal smditikkmm fenypilqdk indifendd
//
LOCUS       WP_284584195             516 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Empedobacter falsenii].
ACCESSION   WP_284584195
VERSION     WP_284584195.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..516
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=59015
     Region          282..516
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mkkgfykili vimsvaligl iiiqfywlnl tiqngtesfn nnvyqamnyt tekinkveld
       61 kyykkfstie sdlksskdkp qvvtnrvikd slgvtyayvt ryvveksmlp sgqyndsltk
      121 aniysqervi kidkdsassg isnlnlnfen alqdgtftle saarwdagtt pidkrvnykm
      181 ldsilknelr nrginqaipi lavlkkdste tnvksadfdr nkiefmvplf ldrkdhieyy
      241 laanfvnrkl aivaptvpvi sltfiltmii itvfslsiyy mqlqrkssei ktdfinnmth
      301 efktpiatin iasdalrnek iytdpekvky yadlikqenk rmnahvemvl rmskldrnqm
      361 dmnfqevnln gvvqksiepi rfiveerngt ifeeynaeqs fvngdpfhle nivinvldna
      421 rkyspntpdi rvktynkdns fiieisdkgm gmpqsvlkki feqfyreetg nihnvkghgl
      481 glayvkkivq lhggqvwaes aagkgstffi kiplks
//
LOCUS       WP_284584246             976 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Empedobacter
            falsenii].
ACCESSION   WP_284584246
VERSION     WP_284584246.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 976)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 976)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 976)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 976)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..976
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..976
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=108221
     Region          25..975
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrilkqslla lvlsspails aqtavkgivy dstnnavlag advsnittgv stisdeqgnf
       61 tleandgdii visnfgyedq eityagqtql qlrlgktten lkevvvigyg takkedvtgs
      121 vnqlnsedfn kgsitsaqel mtgkiagvsv tssggapgdd qkilirgnss islnreplyv
      181 vdglpladek iggsrnpldf lnpndietmt ilkdasatai ygsraangvv mittkkgkgk
      241 qfkynynstt siydpikmvd lmngdefrkl vnehgtaddi aklgntstdw qkliyktavg
      301 fdhnfsavgk ignfmpsrfs isntnqdgil rgdninrttl svnlnpslld dhlkfeinar
      361 gsyienifan rdaigaalef dptqsvysng inswqgynvy tqlidgqyfl rdltpnnpia
      421 linevndtse trrfagnaka dyklhflpdl tatvnvgydi tnangrkvtn yalpskntkw
      481 dgaysnfsne fsnklldayl tynksfglst lnavvgygyq kfgydkfsfd sekaeigqia
      541 avvdkyesvl lsyygrvnyn ydnryiltat lradasskln pddrwgyfps aavawnisne
      601 dflkgnstls dlklrvgygq vgnvngledy lfltrytqsl ssaqyqfgdk yyqvyrpekv
      661 npnlkweisn tlnigidyal frnriygsld iyqkktkdli aevyvdqftn fsnkikqnig
      721 dmenkgiefs inadiikskd idwsfgynia yndnkivnlk ndnyvggidg gtginvqvhk
      781 eghtpfsylv ykqiydangk piegayadln ddgvineddr ylhkspfadi tmgfntrfry
      841 knwdlsatar asignyvynn vasakgylak atgngqgyls nvhrdyyntg fsaitatnlt
      901 sdhyvedgsf fridnitlgy nlqqaikgmd vrlygavqnv alftnydgid pevfdgidrn
      961 fyprprtfvv glnvnf
//
LOCUS       WP_284584291             108 aa            linear   BCT 25-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Empedobacter
            falsenii].
ACCESSION   WP_284584291
VERSION     WP_284584291.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..108
                     /product="type II toxin-antitoxin system RelE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0017148 - negative regulation of
                     translation [Evidence IEA]"
                     /calculated_mol_wt=12034
     Region          2..91
                     /region_name="RelE"
                     /note="mRNA-degrading endonuclease RelE, toxin component
                     of the RelBE toxin-antitoxin system [Defense mechanisms];
                     COG2026"
                     /db_xref="CDD:441629"
ORIGIN      
        1 msysiiavpe flkqakklgk kyrsikddls slfeeleqnp tlgtnlgnnc ykvrlaiksk
       61 gkgksggarv ithilienet iyllsiydks dqdsisdeei kdllknik
//
LOCUS       WP_284584366             378 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284584366
VERSION     WP_284584366.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..378
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40614
     Region          7..361
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mvatsvsasv pqridclegi ralaavgvli thvhfqtasg pvvlerfdyf vavffalsaf
       61 llwrrpigpg flrkraarvl paylvcvavv alalpaastm swqqllanlt atqiyipdgl
      121 apglthlwsl cvefafyftl pltawvllrw qartrvlalc avgvmslgwa flpfvagfdg
      181 sdgaswaasv nrqiwppayt lwfvvgmlaa eaesagvakr pgvvrrilgm kplfwvlata
      241 clflasweai sprglthpsp lefairislg tvfaacivvp yalrptqsgl llsqpvqavg
      301 rwsyslflwh vavlsiafpl agiemfsggf viilaltlgl svavaaisyt lveeparlwl
      361 rqatapaakh aasklspa
//
LOCUS       WP_284584363             465 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284584363
VERSION     WP_284584363.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..465
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=48781
     Region          1..464
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrltvfglgy lgathaacma eaghevlgvd iaparvaqlq agrvpfyepg laelvargvd
       61 sgrlrfscdy qqaaefaqlh fiavgtpera dtpaadtsav eavvdklapl lrgehvlvgk
      121 stvpvgtaar lqeqassisp atvdvvwnpe flreghavad tlrpdrivvg tgsvesapng
      181 vsapngvvla palqklrevy rvplergtpf lvmpwasael vksaanafla tkisfinaia
      241 evcevvggdv aavaealgyd erighqylga glgfgggclp kdlrafrara delgagdala
      301 flgevelina rrrqrvvqla nelvaqssqv aepaglarpg lsgavitvlg aafkpnsddv
      361 rdspalavag elalrgarvr vcdpqavena rrvypgleyp dsladgvaga dlvilatewp
      421 eyreldpvwa aelvaepvvl darnaldlar wrgagwqvhe lgrgs
//
LOCUS       WP_284584447             535 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284584447
VERSION     WP_284584447.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..535
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=57370
     Region          35..473
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mtlrqdrpar asatmpagav detsarnsrg arkpnalval lrrlhfyagm figpflliaa
       61 isgalyavap taeklvyqdv ltvtpppgae gvtntislek qvnnaheafp dldiaqvwps
      121 sepgettrvl lidetideae lrsvfinpyt gavvgdepsy sglgelplrr wishlhesmh
      181 lgpvgelyse laaswlwffa lgglvlwasr nkkvqqlfgf gkaragketk ngdakdakda
      241 kdgkdgknkg sgrrrlvnlh gvtgtwmlig mlalsvtgit wstyaggnvn rtvealqwra
      301 dpittelsge saaeadphae haghggggga eaeaearawt peeiaeqadq vlatareegl
      361 tgslrmypge svehgwqase rwtewrttsd aisvdgetge vidrlpfsel plfskltswg
      421 iylhmgimfg lplqilllvt alaiaglvvl gyliwwkrrp tpgatagipg prtklsstqw
      481 iivavflvav ggflplfgis laamlladvl lskraghtgh tghetrraav dgara
//
LOCUS       WP_284584690             364 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284584690
VERSION     WP_284584690.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 364)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..364
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=38021
     Region          21..359
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mstqsqdtqa papvdpgyrk lvvrtrwvsl hfptrlllta lglfalavig aiaaitlgey
       61 pldlgevita lfsggdgfdt tivrewrlpi avaavafgal lgiggaifqs ltrnplgspd
      121 iigfdagayt avvitmlvig tssfwsiaaa siiggiital avyvlawrkg vqgfrliivg
      181 igisamltsl nsylitradv eegmqvgfwa agsitkvtwq gllptlvlgv iviigaails
      241 rplrhlelgd daattqgfev nrarlllivv gvattalvta aagpisfial vapqiarrlm
      301 htagvsllga aamgavlltg ahvlsliiat fyrqipvgli tvviggmyml wllireskrh
      361 ygtg
//
LOCUS       WP_284584692             340 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284584692
VERSION     WP_284584692.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..340
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34514
     Region          28..336
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mqapalfarr tlgmlailaa ivvmicfsia lganplpwge vwngllardn seaaiiiwtl
       61 riprtvvaiv tgaafgvaga liqaltrnpl adpgilgvna gagfavtlgv gffgltsisg
      121 yiwfaflgaa ittvvvyfig sgaslgasgk anpatlvlag valaavlsgi tqfltlidpd
      181 tfqairnwsl gsvaradlsd talvapflaa glvlalaiss slnsialgdd laaslgtkvv
      241 rtrvlgiiav tllaggatal tgglafvglm vphvvrwivg pdqrwiiiys alaapvlvla
      301 sdvigriiar pgeievgiit avvgapvlim lvrrrkasgl
//
LOCUS       WP_284584775             215 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284584775
VERSION     WP_284584775.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..215
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=22701
     Region          19..209
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mrtliknnah htqhpqpapr mvlasqspsr agilrsagve pviepahvde daiqaelgna
       61 spseivtala hakaqaiari ypndvviggd smllldgvlq gkphteqati arwraqagrn
      121 aqlltghcli fggetyteaa ttdiafaqas eadiaayaat gepwqcagaf tlealggwfi
      181 dridgdpssv iglslpvvrr alyhfgfgvs dfwna
//
LOCUS       WP_284584798             609 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284584798
VERSION     WP_284584798.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..609
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65530
     Region          11..609
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mqeafspaky tiepgqtllt ltidavnaqp kaeifsrpkn htwvsvsrqe fldevyavak
       61 glidagveqg drvalmsntr yewmlinyai waaggvvvpv ypssslsqvq wiiensgavl
      121 gigetqehte ilrmlqladd geprvkdsts qmraffeing gavdvlqatg kniddevvdk
      181 riaatatdhv aslvytsgtt grpkgcmlth rnwnaqilgl lsnpiggiar pgkhvltflp
      241 lahvlafsvs aaamisgatq nfwpdfatla tefqrskpnl ilgvprvfek vrngarakah
      301 dsgaiqgalf draeataiay sraldtekgp slalrsahka ldklvlskir tgmggevdyc
      361 isggsamspe lmhffrgigv pvyegyglte taaaatvdfe eqkigtvgpp lggtrvriap
      421 dgelqlagdl vfagywrnae atdeafdgqw yctgdlgeil psghvkivgr kkdlivtagg
      481 knvapggmed glrshplisq alvvgdgkpf vavlvtldee algrwksqhn idasrsvadv
      541 ahdaslraei qdainavnat vshaeaikkf yildddftee sgeltptmkv krnvvvqrys
      601 evldklysr
//
LOCUS       WP_284584871             519 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284584871
VERSION     WP_284584871.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..519
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=58992
     Region          9..512
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mpsekdtpqp almwfrddlr lhdnaalvwa akqgpviavv idedatatga ralgaaarww
       61 wqrsvhqlnk rlaahgvpll yyqgdpraii pavvqefgvs avgwsrryhk plreldaqlk
      121 rllqekgvaa ksfpghllte pwevqtqqgk qykvytpfak targvaadnv asylntgndq
      181 apsptshdel gpiglagrga dlasahplpd wdeadwthsl aqhwspgens awkvaeefls
      241 elaaaskqqa phyaadrdrl dkqatsrlsp ylrfgeisih rlwamvtean dtgriageda
      301 saflsellwr dfawhrlyhl pelhrrnvre qfnhfdwhwe ekearriast rrdprwlete
      361 keipeiatag dfrsvfsawr agktgiavvd agmrelwatg tmhnrvrmvv asfltknlgi
      421 hwrhgeawfw dtlvdadpas npfnwqwaag cgddaapyfr ifnpdtqakr fdpdyryiqh
      481 wvpeyatpiy pqpvvdlkas rrqalaayee mknfhprpe
//
LOCUS       WP_284584999             311 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284584999
VERSION     WP_284584999.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..311
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32988
     Region          18..310
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mlepqvpqvi tladaqvddp rladirqlnh prlrpdrqar leldssgdyi pasrpsvila
       61 dgalpiarmc gtdsavtpaa ifgraeklqk fatdypeqws riaqlgipvy elpavllrdv
      121 vgfelhrgll avalrpdsie lgtesaeeil apartivvle gvgdpdniga iyrsaaslga
      181 dalvfgagcg dfwdrrvirv smgqalrvps vripggfsnw hhgladlrnq gfyvaalspg
      241 aqavqlrdal vgpsgnrrek valllgaegp gltphamnaa dacvvipmaa gadslnvavt
      301 aacclyerwr g
//
LOCUS       WP_284585024             493 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284585024
VERSION     WP_284585024.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..493
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=52153
     Region          4..458
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mnflesveav ivkfndgiwa iipwlliasg vyfavrtsgv qvtklgdmfr slgekpkgkg
       61 knldpeyggi safkaftisa asrvgtgnia gvavaitigg pgavfwmwii alvggatafi
      121 eatlaqlwkt keasgnyrgg payymtrglg fkplaavfsv alaftfgfvy nafqsnaivd
      181 tmstslgleg wvfnliigiv laaissvvif ggvqrianft qvivpfmagl yvtiglvvii
      241 ininevpgmi ghiighafgv tevvgatvga afshgmrrgl fsneagqgsa pnaaatatvs
      301 hpvkqglvqt lgvyfdtllv csitafiill ggdhkyglen iegaaltqta lanevgswgi
      361 hivtfiifcl afssvlgnyy laqtnlqylt espkvlngfr vgvlvfiiig svtsipvvfa
      421 ladtfaatmv vlnliaivpl ggvalkllkn ynqqkrrgqd pvfhrdmlpg lknveawdgs
      481 dpvtrrseed alk
//
LOCUS       WP_284585097             328 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284585097
VERSION     WP_284585097.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..328
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32842
     Region          27..322
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mgaqsttrfi vafvianavl lltivlalgi gavavppsev vlrlmeadnl iwkfrvpral
       61 vgvfagagma isgcllqlgl rnplaapdtv gitaggglaa vvallgagal paqaltpval
      121 vgacigaglv ivasgkgvnn pirlaltgva vsvglgavtq lllvrtapea gaamawlkgs
      181 lyarslsdav vvgpivvtvf clsliiakhf dvlllddatm kgigavplrw rllavgcaiv
      241 sgaaavaaag vlafaglivp hlarllvgpq llrqlpmatv igsalvvgsd algrwmfspt
      301 eipvgaliai igapyfvfll mritskgt
//
LOCUS       WP_284585121             936 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284585121
VERSION     WP_284585121.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 936)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 936)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..936
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..936
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103576
     Region          2..934
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtsthfetfr sqltykldpf qvqgcraven grgvlvcapt gagktivgef avslalsrgt
       61 kcfyttpika lsnqkfhdlv aihgedavgl ltgdvsfqpd adivvmttev lrnmiyaksp
      121 aldrlthvvm deihfladqa rgavweevil nleehisiig lsatvsnaee fgrwlstvrg
      181 dtevivsehr pvpleqwmli gqkvyplfap gtpaiegptt sepagvnpel qrrvarleag
      241 daadgrddfr pgqgfrsrst agrgnsrsgn vrpqdryrpl grpevlrilq gqnmlpaiif
      301 ifsragcdga lhqclrskmv ltdedeqrii aevidtgveg iphedlevlr fsqwrkalir
      361 gfaahhagml pafrhivekl fvrglvravf atetlalgin mparsvvlek lvkfngeahv
      421 dltpgqytql tgragrrgid tlgnaivqwa pamdpqrvag lastrtypli stfepgynma
      481 inllnnlgmd dslrlleksf aqyqadgsvv eetreierav hrveklreql neaiaafapp
      541 stndqdpaql lseyvelrkr lsmeekslks rakdergdet railaklqtg dvialpskkr
      601 pvlavvntpa nqtadprpwi ttekgwsari dasgfdnppa lvgkmklpgk alknprrhnh
      661 ivvdkfared yprpkkmklr arirdterik dlrtrmkkhp ahawpamere qltqlaqkyl
      721 rrkgeldklr atvdkatetl gdmlrrivdl lteldyvdiv dgepvvsteg eklaqvhnas
      781 dlliaqclkr giwqeldpae lagvvslctf enrratggql fdgvtdamtn amentmrlwe
      841 elisdesrhg lphtrepepg fsiaihqwca gaplgyclaa aaesgaeltp gdfvrwcrqv
      901 idllqqvakt gysseikrta gqaiasinrg vvaigs
//
LOCUS       WP_284585185             366 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284585185
VERSION     WP_284585185.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..366
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40425
     Region          52..361
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 msepvpapgv ltkamkwlwk kdsplyisps tdwrfytfll rmlqhtsskh yaagtetliq
       61 lsketfstfd efvdegvevd mdfatmrtlf kdtsgmdarl delahfaenf pglsyrrmdd
      121 aelrafqpkl sedvqggies rgdahldpak ftaalykacq eagvefvasr awlrdrgfgk
      181 arvivdgsfi dpdyvvvaag awtgevvkql gqnislqtgk gygfdfpveq gwltdtlymt
      241 dakvvatpmg dhvrvagtmg fsgideslnq vraggilkgv qsffpdwpvn efdlepwqgm
      301 rpmtpdglph igalrkfpnv vvatghamqg islaprtaql vagviagetm pewmkeihpe
      361 rfsrlg
//
LOCUS       WP_284585472             538 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284585472
VERSION     WP_284585472.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..538
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=58052
     Region          1..525
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msllsvsdls ityrtehgev eavsginfav vpgemtaivg esgsgkstsa maaigllaen
       61 ativsgsitf dgqevtqlte kqwrqlrgrr iglipqdpnn slnplktiga sveeglsihn
      121 fgdkptrkrr aiellervgi ddpqrryeqy phelsggmkq rvliaaaval epeliiadep
      181 tsaldvtvqk iildlldnmc helkmgilli thdlavagdr ankivvmekg mvresgvaar
      241 vltkpqheys krlladapsl ssphlgtsrr gqetpqaqep lltvtgliqq fgdftavsdv
      301 sfsvapgtth alvgesgsgk tttgraislf srptagsial hgeeittarg krqrelrrai
      361 qmvyqnpfgs ldprlsigds iaepvrnffg asrrsaraka kevldqvsld ssmatrkpse
      421 lsggqrqrva iaraiiiepe livldeavsa ldvtvqaqil rllddlqkel gltyifishd
      481 lavvnqisds vsvlsrgkqv eygatekift qpstdytrtl idaipgsryr agdlnlgl
//
LOCUS       WP_284585977             680 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Staphylococcus warneri].
ACCESSION   WP_284585977
VERSION     WP_284585977.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus warneri
  ORGANISM  Staphylococcus warneri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 680)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 680)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 680)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 680)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 680)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Staphylococcus warneri"
                     /db_xref="taxon:1292"
     Protein         1..680
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76472
     Region          1..>426
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 meifetllif igvviissfv htfmpkvpla fiqialgmll fitpipvefn fdselfmval
       61 iapllfvegv nvsrmhlrky ikpvmmmalg lvittvigvg ffihwiwpel ptgaafaiaa
      121 ilcptdavav qaitngkvlp kgamtilege sllndaagii sfkiavgalv tgtfsimesv
      181 eqflvaslgg aivglligma lvrfrltlmr rgieninmft fiqlltpfvt ylvaelfhas
      241 giiaavvagl vhgferdria qtrtrlqmsy nhtwnilgyv lngfvfsilg flvpevvini
      301 iktephnllf lvvitvlval avylfrflwv yvlypyfyla vspfqkmisq dddgnnttek
      361 ppkrslyali mtlcgvhgti slaialtlpy yladhhafdy rndllfiasg mviislvaaq
      421 lllpfvtana pevkvgsmnf keariyileh vidylnqkst fetsyrygnv ikeyhdkltf
      481 lktvekdden skelerlqki afnvetktle qlvddgsitn silenymrya ertqvykqas
      541 lirrlivlfr gallkrrvkt tinsasslsv tdnllelvki nkivhynvvr rlgqeanndn
      601 klevgmicdg ylmridnltp nnffnspsed tltriklnal reqrrilrel iedeeitegt
      661 alklresiny demvivdsmt
//
LOCUS       WP_284586069             585 aa            linear   BCT 25-DEC-2024
DEFINITION  IucA/IucC family protein [Staphylococcus warneri].
ACCESSION   WP_284586069
VERSION     WP_284586069.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus warneri
  ORGANISM  Staphylococcus warneri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Staphylococcus warneri"
                     /db_xref="taxon:1292"
     Protein         1..585
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=67430
     Region          1..567
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mtrnewllad kniqhrmlna ivkericped akinqstdki eiqyhgrvlt ayvlrksmle
       61 ryvfdgpfty qcgderiqit slesllniln dafdieiser lyhelihsrd sfvesykqfn
      121 nrtslihqsm tfsmlpdtin fftwlqhikd ngttndlsys eslvleghpt hpltktklpl
      181 tseeirryap efekniplhi mlvssshirt tsmendeqyi vnqvipelkd klqsflkpld
      241 lemnnyraif vhpwqydhvi gerfktwise kiliptpftv eskatlsfrt mellhhpfhi
      301 klpvnvqats avrtvstvtt vdgpklsyal qdmlniypel kvsaepfgey vdvdadlarq
      361 lacivrekpv laqegstivs aslvnrnpvd ddvivdsyik winnelttes ieqfirqyts
      421 tlvrplivyi qdygialeah mqntivnlgp nyqmnflvrd lggsridlqt lkhklpdvki
      481 tnesliadsi eavigkfqha vvqnqlaeli hhfnqydmvn eerlfkivqq eieaaidank
      541 nhaqalhrvl fgptisvkal lsmrmenkvk kylntelenp ikkev
//
LOCUS       WP_284586201             647 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284586201
VERSION     WP_284586201.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 647)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..647
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=69416
     Region          22..475
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 maatgkdydr seharrkagr lhisalrisn frnfqslvvd pfprnavvvg engvgksnll
       61 talqlvldpt lprsarrlre tdvcaatlas tplsdvevrv evelqgfegl tgalsqfdgw
      121 iiskspltar vtyvwrmeha pdeaetdasd aaarnfvwri fggsdesrda nrivdelplt
      181 vvpalrdaar dlanwrtspl aaivemrpps rtvidaalaa iasatdkiaa dtallatgns
      241 lrarlddmsg nhlsveptmg vaasrgeqlv rslrlfidss rsrdvsdtst gganvvylal
      301 llerlalrte ddaqldfvlg veepeahlhp tlqrklfgfl lqaytklvlt thspniaava
      361 dlasiillrs dqstgvttar tvptadltpv eladldryld tsraellfak avvlvegiad
      421 vyvmrslaer lgfdldawgv vvasvqgtdf gpyrkllgpg gfdiphlvvt dgdqdvnvtl
      481 sglvraarli ggvegkefet kvvafreggs tidpealyaq aadagiyvgq htlevdlcpl
      541 lgtelaravs dllspdattd paqrvddlld nntpetrhsl llavnnvskg rlgqrvanei
      601 lalseahplv rlsdeelasn plrymidais aaavmvgapv vvrtkag
//
LOCUS       WP_284586356             773 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284586356
VERSION     WP_284586356.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 773)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 773)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 773)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..773
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=80365
     Region          19..757
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mptprstssp ipapstasst ielnisgmtc ascaarvekk lnkhdgvhae vnyatekati
       61 tgdtdaldad aliatvektg ygaeltpest tagtqapqda maeaeldslr rrlivsavla
      121 vpvialamvp awqfdywgwm slaltlpvvv wagwpfhrat wqnlrhgsvt mdtlislgts
      181 salvwsmval ffgsagdpgm rhgfdftvsr gdglshiyle vaagvitfil lgryfekrsk
      241 rtagsalral ldlgasevtv lrngaettin ineltvgdef vvrdgekiat dgvivsghst
      301 idtsmlsges vpveagpdda vagatinvgg gklvvqatkv gkdtqlaqma qmvedaqsgk
      361 asaqrladki sgvfvpivia vslltliawl lidgdwaaaf taavavliia cpcalglatp
      421 tallvgtgrg aqmgvlikgp evlehsrgid rvildktgtv ttgvmeladv vtaegfdrde
      481 vvhlagsleh esehpigrai araatnqrad gtlsevsdfe sirsagvrgv vegrrvavgk
      541 psladnadlg alqqpflsaq tqghtalvvl vdgtpaavlm vadqvkttsa aaiqqfhelg
      601 ietmlltgdn qavaetvaae vgiehvraev mpedkvavia dyqdrgykva mvgdgindap
      661 alaqadlgma mgtgtdvame saditlvrgd lraatdairl srrtlgtikg nlfwafaynt
      721 aaiplaalgl lnpmlagaam alssvfvvsn slrlrgftst agagvdatvr atv
//
LOCUS       WP_284586465             381 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284586465
VERSION     WP_284586465.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 381)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..381
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39871
     Region          70..376
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mmmnetqriv trgisapksl akppavdkie vankavlelg rqhrkltwqr igivsglcav
       61 aiaafvtsnf vgaidispge viagivnpss ldeqthtvlw rlrlpmavma lligvslsla
      121 gaemqtilnn plaepftlgi saaaafggas aivlhwqiva qpqlnlalva wlssvvatgi
      181 ivvaavlrgv raetmvllgi glvfffqaml aliqyrssae alqqivfwsm gsltraswtg
      241 navlagvlvi alpvlwalsw qltalrlgda raaamgvnts alrvivlvvv slvaattvaf
      301 agiigfiglv gphiarmlvg edqryfvpas maagaavmct ahalslivkp glaipigivt
      361 sllgvpffia ivmakrralw s
//
LOCUS       WP_284586536             307 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Enterococcus faecium].
ACCESSION   WP_284586536
VERSION     WP_284586536.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         <1..307
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          3..305
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 ehdalfissm kqslmyvaia allvsfilas wisarlglpl khisdfthkl trgeyadkip
       61 qetsiieins lidslndlsn qlekqhglrk rlttdishel rtplatlkgn vegmidgvwk
      121 itperlqscy deidrltrli gnieiinkie akydhlnkte fniykliesv ienfaskies
      181 knlhveiqgd ninisadkdk mnqvvinlln naikftqkeg tikfsisknk dhvllivedn
      241 gigiekdqql hifdrfymad psrsralggq giglaivksv veahkgsitv ksklglgtkf
      301 viklpfq
//
LOCUS       WP_284586550             488 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284586550
VERSION     WP_284586550.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..488
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53635
     Region          3..488
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mqhlqhdfad hfpdlcldwr aakapapqiv clneplahel gldpswlrsp egigflcgth
       61 lpegaqpvam gyaghqfgqf sprlgdgral llgevrdgag klrdihlkgs gptafsrggd
      121 gwgafgpmlr eylvseamha lgvpttrsla vistgraiar ervvpgallv rvanshirig
      181 sfqyaqltgg eelvcklaey trnrhypdaa darevfhhal daqlatvaqw mrlgfihgvl
      241 ntdnttlsge tidygpcafm defnehavfs sidhsgryry hnqphiigwn farlaeamlp
      301 tfaadpdeav gfaqetmntf qerwrkahns ercraigvey sednaklade fyeligkanp
      361 dltsahralv daavrdrhti aapgvdtars pvnvlarqlg dtaparewia rwlnhapsph
      421 alarlhpmii prnhlvenal ssatdgdlep fhqllhavth pfgknhppef lkpaprefsa
      481 tyqtfcgt
//
LOCUS       WP_284586580             232 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284586580
VERSION     WP_284586580.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..232
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=25308
     Region          1..223
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mlfdslprps eriapgvahl pgwlgvdkqa klvrevreia rtyadtpmam lrptlksggq
       61 msvyqlhlgr ywhypsyryv dkiagttvpp vpeslvalap valraaaeva eelapwvetf
      121 vpemvlvnyy ppgsgmgmhv defeesrapv islsigdeal frmghtesrt qpwddvtlcs
      181 gdlvvfggpk rfayhgvvrv naatlpdgcg laegriniti rqvsaapklq gr
//
LOCUS       WP_284586599             460 aa            linear   BCT 25-DEC-2024
DEFINITION  acid phosphatase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284586599
VERSION     WP_284586599.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130290
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..460
                     /product="acid phosphatase"
                     /EC_number="3.1.3.2"
                     /GO_function="GO:0003993 - acid phosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=50189
     Region          <137..339
                     /region_name="PAP2_acid_phosphatase"
                     /note="PAP2, bacterial acid phosphatase or class A
                     non-specific acid phosphatases. These enzymes catalyze
                     phosphomonoester hydrolysis, with optimal activity in low
                     pH conditions. They are secreted into the periplasmic
                     space, and their physiological role remains...; cd03397"
                     /db_xref="CDD:239491"
     Site            order(226,233,262..264,297,303,307)
                     /site_type="active"
                     /db_xref="CDD:239491"
ORIGIN      
        1 mfltsrrrat slltaagala vvagapslve qhggtahsma aeaslqapln antthlalpf
       61 eipqlqlpap klssehgagp eysplssiga npqhhagapv pqpfdvsylt gyvsdvssyr
      121 ygiyyevvre fkdlrsnhpe vmqknldiva eynnnaqqer vdkairdala dkdgvlftaa
      181 ealgdefgrh flaalhekrl pktefllgng yaaraggias wgraekllfn ndrpfvqape
      241 riqrhesper klydgssksf psghtnqatw ittllammlp evgtqllarg seagesrlvm
      301 gvhfpldvig grmtgqaaaa drwndpkmrd allqaraeiv aemewragkp faemiaedsh
      361 alsdqqaead ytrrmtygft pifatdepvn vptaapalle trfpelsyeq raevlrhtal
      421 psgyplddrd pdkgdwqrin larawnaqvs igaggevvvk
//
LOCUS       WP_284586601             208 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284586601
VERSION     WP_284586601.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..208
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22786
     Region          59..154
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mhtdsthsds nvpghhnsah hapsaaemed ryasnervws gdpnaallna vagmgldgas
       61 prtaldigcg egadavwlaq qgwqvtaidh aptavrraee laaengvqid aravsfqdfe
      121 ramfdlvicf fgqlsdddvp kleslvapgg wlifvhhdme sekylmparl keqltelelv
      181 ddyvfeknle rgggahhhrd lvlrarrr
//
LOCUS       WP_284586685             769 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284586685
VERSION     WP_284586685.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 769)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 769)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 769)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..769
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=85200
     Region          23..765
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 msprrttgqq stgsqrtkrv hhsnysaela aeqsyvdalf gildsdvsqa rqrladaqlt
       61 idpanadsda llrreteyhr lqekldqlnl aqiglvfgri dvdakgenpt segldrryig
      121 riglmdrddd yrsllidwra pmarpfylat tahpegvrvr rhirtadrvv kdiddellsg
      181 tapgdadrad vageaallha mnsargehme sivetiqreq daiirdstrg vlvveggpgt
      241 gktavalhrv ayllytwreq lsrtgvliig pnptflnyis qvlpelgetg vvlstigrly
      301 pglrptlhdt aetrrvkgsl qmvdvlkaav kayqhvpkhs revvlegtrv eltptmvkta
      361 rtkarrsrkp hneareifse qlqellaqgl aeiighdpld ggnllnsadi salhedisde
      421 aivdelvdef wpqlgprqvl rellsdretl haacrgngge eftsalwrse qgwsdsdaal
      481 ldelaqllgs gddeqqaaad eqewrealee aegaldilat sestdnddvf dseilsahhv
      541 idaetlarrq qardyrttae raegdrtwaf ghvvvdeaqe lsamewrmvf rrspnrwmtv
      601 vgdpaqtssp agcdswseal epfvgkryrq hqltinyrtp veiaelaesi vhkyspdttv
      661 aqairnrkga vrwlpsgtsa eevrdqlrad etaasaeddt agqnqrsyai isahnaatyk
      721 glefdhvivv epeqiiaass rgwqdlyvac tratqtlsii gtldlagwd
//
LOCUS       WP_284586785             331 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284586785
VERSION     WP_284586785.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 331)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18950610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..331
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=36354
     Region          40..163
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
     Region          177..318
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mvkksqmsea dkdnqsgfnl saryhqigkn pgaeyrkptl aagavlwrrg dngtaevavi
       61 hrpryddwsl akgkvdpges lasccvreia eetgyqvqlg sllgsvnypv qgrtkvvfyw
      121 nanitggkfq kneevnklrw lsvneahekl tydtdrrvle qaairhddav dthvlyvrha
      181 kahdrktwsg ddnlrplhkk grrqaeflvp mlsaykptal ysaeparcqs tiaplsdals
      241 lpvtteqivg dagldnlaaa tarfreiatg ggvpvivsqg gmmpeiiesl ateadfdiep
      301 refkkagtwv lalregklvg adylasplpv r
//
LOCUS       WP_284586839             417 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284586839
VERSION     WP_284586839.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..417
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=44690
     Region          9..403
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mnltelatqr lekwqqqglm rtpiefagpq tpraqlsdqp serillsssn ylglathpev
       61 idaarsalek fgtgsggsrl ttgsttwhrr ierelanfvg fedavlfatg yqanlsvlqt
      121 lahpdlhifs dslnhaslid girlattsgt kksiyphcdy taleqqlaec taryklvvsd
      181 gvfsmdgdia dlarlreict hhdawllvdd ahgigtvgkh gigstqvhnt rpdilivtas
      241 kalgaeggfv acstpvanll rnqargyvys tacsaancaa isaaleviqk pltqqhpvvr
      301 lqqraaalre itgirvfdgv dsdsvlfdsa hsgsahspii plpvgaesaa vrlaseladr
      361 gfhipairyp tvargqailr atamatlela ditqfaqtlr dlgwrpptpa kaiipgr
//
LOCUS       WP_284586922             413 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284586922
VERSION     WP_284586922.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..413
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45512
     Region          122..398
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mpsslfqraa alaltaafsl pavaavssav atpqahaqqf ssetssriaf dgssapmaew
       61 skdpavqghv lnvleffqnh tpwhqlpmwn lwgeqtpyti dkeqdfaqpr lihreaderf
      121 averlyvesp amrrvvqvqv qypkdrnaaa pmlylldgvs aprqsgwlrk gdvqgtmane
      181 hvttimpvea ggtnytdwna tdpylgrakw etfltqelpg vmeqqtgipf ngeryiggls
      241 mggsaavrla nlypqlysgt fsvsgcyssi stagrayfdl aalvmggnpe lmwgpgnape
      301 rlrndvvsdp kgiasmpvyi ysangyateh dielarpegi ptffgnitle kltnqctael
      361 ehslqekglm heriefdhaa tgihdwpyyk qqlpvawasv tqgkytypnq aen
//
LOCUS       WP_284586937             517 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284586937
VERSION     WP_284586937.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..517
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54963
     Region          15..513
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mssgfarssf ahngkarvav igagpnglta aavlaqagcr vevfesadhi ggsarthpaf
       61 gagsavdfga aahpfgvvsp vfrqlgleny glewkhpqyp mahplvdapa vilhrdlktt
      121 aaqfsdhdrr vwnhlhkplv ddvgklvnsv lpvrprypla larlglrglw parsltsrll
      181 vdeparallv gsavhairpp sqpgtaafgl lfnslgmttg wpvvsggtgq lvralarvie
      241 hyggtiktga aildlsgfvt ydavvttqtp rqllalqgld lsrlrsrslr rwkygtavyk
      301 vdylvngpvr wndprvagag tvhvggtgse mqlaesqaaa gmlperpfvm vcqqqtadpt
      361 rfsgnrrsvg agrvlsaqld agrmpedarq philwayahv phgyqekfpg evaglieaqi
      421 sryaagfsaq iierhqaspg qlqeananli ggdiaggamn laqmlrqrqy vgtltvnpev
      481 pvmqasgasl pgagvhgmag wraaqtilrr fgsielr
//
LOCUS       WP_284587041             327 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284587041
VERSION     WP_284587041.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..327
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33807
     Region          22..326
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mrktwtiagi saatllvali gsltvgsssm sfgeliglvv psqpspsalr tsiltelrip
       61 rilmaafvga ilavcgvamq avthndlaep yllgvssgas tgaviailfs twqygiifga
      121 tvgslasfal lmlllrntgg datkvvltgv ligflfqslt slvvtasgda estrsimfwl
      181 lgvlgaarwp tlfaviivgs igmlmlwals rhldalslgg dtastmgvpv valryivlic
      241 vslmtattva svgaigfvgl iiphavrmln vpkhaslipl saligavtlv iadafarsif
      301 apqelpvgvi taligvpmff lilrrkh
//
LOCUS       WP_284587052             409 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284587052
VERSION     WP_284587052.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..409
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44002
     Region          21..216
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mannrvstre rlrhldhslt srilrvrkrl ifivqaafga glafwvaqtf fgheipffap
       61 isvvvvlgis ggnrlnkale msvagvvgvg vgqllvhtlg tgdwqiaagv aislvvaafl
      121 sksllvsnqv aigailiati mpqgggterm idaaigsvig iisialipns alrdarheia
      181 kvlsvassvl hdvaegaekg dseriedalq qvrgtqsnid hmleatasgr eiaglspfrw
      241 gsrkhlrsie riltpvdnat rnvrvlarrc mvlsvdgdki tprliniide laeialelsr
      301 iyetsarvsq aheipgivnr lriigartdl svisddpvls eyailsqvrf ltvdllmvtg
      361 msqesaaavl aptsstpayp pevweiedik dnahnaadry ddsensqke
//
LOCUS       WP_284587126             436 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase
            [Corynebacterium].
ACCESSION   WP_284587126
VERSION     WP_284587126.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..436
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=48880
     Region          238..340
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mgnirkiidg svasifggwl vatllsqhpe snldrirrld drfgntiipn wkffapnpav
       61 edvhvlyrlv sedlseyspw eechtisprk msqafwfprr rfekgifdth qalvvglasl
      121 gkgdendavl rrsisdtaem lnnyirhnyt rsiskteknw ywqqlmlvrf aghdgaakpi
      181 ydlilnyqai nteqdsnisp afycddyfne yydevmktvd pnvdhaewis aavsgqlpqr
      241 ildigagtgr vlaqvasrfp naklfaiepd ekfsqsfadi danffsgtve eaftaeatmd
      301 idlafvtygs lqyisslsel teslktvrrm mtrggiiave lfaseiyhap vqpspmslkl
      361 gekphtisms slqyphgiva vttqikrqsd gktgvmkecv fpvtrqeave alhaagfssv
      421 qvnlkgaylr ctaknm
//
LOCUS       WP_284587223              97 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein
            [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284587223
VERSION     WP_284587223.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..97
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10959
     Region          3..>66
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mtyvnisals fpegaaeeie qrfaqrakgv dqaegfegfe llrpvsgedr yfvitrwdsq
       61 enyqkwsdar pegnhvedek rgmavdvlgf esiqles
//
LOCUS       WP_284587325             210 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease, partial [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284587325
VERSION     WP_284587325.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 210)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..>210
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          23..>185
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 miwsillvll livvfasgii idptpislsd vrialahnif gaeapasass tnaviwdiri
       61 prlilgaavg aglavagail qavvrnalad pyslginsga stgaalailf gvsagfgeya
      121 lqgaafigal aasavmffia rsagrltsvr llmagiavgy alsaltsfli fasdsaegsr
      181 svmfwllgpl glgavggggg gggfgppqpp
//
LOCUS       WP_284587354             232 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284587354
VERSION     WP_284587354.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..232
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=25203
     Region          1..223
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mlfdslprps eriapgvahl pgwlgvdkqa klvhevreia rtyadtpmam lrptlksggq
       61 msvyqlhlgr ywhypsyryv dkiagttvpp vpdslvalap valraaagva eelapwvetf
      121 vpemvlvnyy ppgsgmgmhv defeesrapv islsigdeal frmghtesrt qpwddvtlcs
      181 gdlvvfggpk rfayhgvvrv naatlpdgcg laegriniti rqvsaapklq gr
//
LOCUS       WP_284587545             412 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284587545
VERSION     WP_284587545.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..412
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=44277
     Region          9..398
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mnltelatqr lekwqqqglm rtpiefvgpq tpraqlkdqp serillsssn ylglathpev
       61 iaaarsalek fgtgsggsrl ttgsttwhrr ierelanfvg fedavlfatg yqanlsvlqt
      121 lahpdlhifs dslnhaslid girlattsgt kksiyphcdy taleqqlaec taryklvvsd
      181 gvfsmdgdia dlarlreict hhdawllvdd ahgigtvgrh gigstqvhnt rpdilivtas
      241 kalgaeggfv acstpvanll rnqargyvys tacsaancaa isaaleviqk pltqqhpvvr
      301 lqqraaalre itgirvfdgv dsdsvlfdsa hspiiplpvg aesaavrlas eladrgfhip
      361 airyptvarg qailratama tleladitqf aqtlrdlgwr pptpakaisp gr
//
LOCUS       WP_284587643             333 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284587643
VERSION     WP_284587643.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..333
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33847
     Region          24..326
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtrisflpat vlavavlgva iaaslffgsn nispgqvwas lsnngdtatd tlvlqqrlpr
       61 tivvvlvgaa lgvagalmqa ltrnpladpg ilginagasi avvagvafag vtginnyifl
      121 aivgallasi mvyllggagr nsapsparlt lagvaismai sslvqaiils nanafnefry
      181 waagsvegrg wpvlehiwvf ivlglvfafa sapslnalsl geemgtalgv kvwrtrvltf
      241 saitilagta taavgplmfv glavpyaarg lfghdnrail agsvvigpvf llaadvlarl
      301 vimpqevqtg llsavlggpi fiavvrmkki gav
//
LOCUS       WP_284587644             349 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284587644
VERSION     WP_284587644.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 349)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..349
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=36117
     Region          20..344
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mrhrihtsap sryvhlagir fyraslctsa vlslviiaaa ivglllgdyp mtlgqtvagl
       61 fgigddplir yfvqdqrlpr vfgalmvgaa lglagnifqr lsnnplgspd iigfstgsas
      121 galfaiiilq agpaaigvga mlggvasatl vyllsiknrk vsgtqlvlvg igvaailqal
      181 nsilivrael gpaqtaaqwl agslnattwp eigvlvaila vvvplallla rplqimlsgd
      241 dlaaglgvrv hrrrremiav gvvltalsva iagpiafval aapqlarrfd pgiamvnsgl
      301 mgavlvllsd iiaqrllapv qlpvgvvtgs lggvyliwll lrkwhtndn
//
LOCUS       WP_284587653             246 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284587653
VERSION     WP_284587653.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..246
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25829
     Region          11..243
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(29..30,32..33,36..37,74,78..79,82..83,107,111,118,
                     121..122,127,142,146..147,149..151,153..154,157..158,
                     161..162,181..182,184..186,188..190,192..193,195..196,200,
                     203..204,210,212)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(145,149,152..153,155..156,195,198..199,201..206,
                     209..211,215,217)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mkqstastaq vpvgkpmhfl hpltviiigv sawvaalsis wpllhaalia lgwlagiags
       61 rslavpatsi alsipaglsm llvhaphgeh qiaplltsdg lvtagelalr fcalmtslla
      121 amanvhipdl lkalqhvglh hsvvyvlgas lqllpqasal isevvaanrl agrkvtlttv
      181 iprmiipvit rlltrgadrg ialqgmgyda pgrrtvlypv rahrweillr lifpaaaigl
      241 vvlawi
//
LOCUS       WP_284587735             311 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284587735
VERSION     WP_284587735.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..311
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32038
     Region          1..289
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 massanpisv lciigscisl qlgsalavkl fddggtwgts avrllvaavv llaitrprvh
       61 ewnrqqwagv lglglslglm ngffyagidl vplgpavtie flgplllaaf lsrslrdgic
      121 vvlamtgmal lgldafngnp lnplgvafll gaalfwaiyi lanknagalv pgqgglavaf
      181 vvggvamlpm gadgawnlvt stdtlwfaig tgilgslvpy slelialrgl apnvfsilis
      241 lepvfaaffg wlllaqnist lklvaigvvi tasvvqtvgt ggsgadgapr sklkklqdvg
      301 rkvvprrrhs d
//
LOCUS       WP_284587768             488 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284587768
VERSION     WP_284587768.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..488
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53685
     Region          3..488
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mqhlqhdfad hfpdlcldwr aakapapqiv clneplahel gldpswlrsp egigflcgth
       61 ltegaqpvam gyaghqfgqf sprlgdgral llgemrdgag klrdihlkgs gptafsrggd
      121 gwgafgpmlr eylvseamha lgvpttrsla vistgraiar ervvpgallv rvanshirig
      181 sfqyaqltgg eelvcklaey trnrhypdaa darevfhhal daqlatvaqw mrlgfihgvl
      241 ntdnttlsge tidygpcafm defnehavfs sidhsgryry hnqphiigwn farlaeamlp
      301 tfaadpdeav gfaqqtmntf qerwrkahns ercraigvey sednaklade fyeligkanp
      361 dltsahralv daavrdrhti aapgvdtars pvnvlarqlg dtaparewia rwlnhapsph
      421 alarlhpmii prnhlvedal ssatdgdlep fhqllhavth pfgkkhppef lkpaprefsa
      481 tyqtfcgt
//
LOCUS       WP_284587795             415 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284587795
VERSION     WP_284587795.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..415
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=47177
     Region          85..409
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 markksertr rafgkvsvkg krvyaeytgp dgrihtpghs fpskidaegw lagerrlidl
       61 sawtppkqrq eekarrslae eangmtvgel vddwltratn lketakrthr kklelralcp
      121 sipgkldslk dvrvmdvdrq rvrlwveqml aiwpygedgy hacyyahkrl vtafnwakne
      181 leliesnpvs rvkmrkpipr nrdepvftsd eaktivntfp kwlqhaplil lycglrpgem
      241 lelrlkdisg ikpgatmvlk vrrnmqdvdr vegggkeili ndvpktdaal rdvhapvwva
      301 dairkhlkdm gktspddlvv srkngnqfsq gnfrdnyfnp akraagrged stvyscrrfy
      361 gtqlvrlvma gnlsleearr lmghettqql meymraeagy qqraaaalne lqtkg
//
LOCUS       WP_284587819             636 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284587819
VERSION     WP_284587819.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 636)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 636)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..636
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=68247
     Region          14..623
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mhkrlrliaa lllvfsvvla grlawvqvvw gpdlsaraed qrariyvdpa rrggvvdreg
       61 kqiaytmqar sltvspttlr kelreqaqle sderlddeqk deyvdatllk msreipkmie
      121 easedkqdlk skdlldklra dtqyevlvrn vdpdiaaeis erfhgvaadh qdirqypnga
      181 igenvvgrvs mdgtgqfgle asrdstlsgi ngrstedvst ngqvipgtlr detpavdgkd
      241 iqltldldlq tfvqqqleqa knnsraesae avvldattge vlamantdti dpngdiakql
      301 edgkhfdnrs isfpyepgsv akiitaaaai eegittadev htvpgsiqia dvtvndawph
      361 gplpyttagi fgkssnvgtl qlaeklgqdk fdeylnkfgi gattgielpn essglrpars
      421 qwsgstfanl pigqgmswtt lqmasvfqtl anggervepr iikssaedda kknadegnga
      481 ndnkvkdsnd adgagasdde pektrvvske taktvvdmfr atvqadpvgv nngtapdani
      541 egynisgktg taqkvdpntg aysnsaywit fagiapvddp rfvvaimlde pergvldggg
      601 ggasagplfh qiaswlldrd nvppsppape ltlqap
//
LOCUS       WP_284587859             763 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284587859
VERSION     WP_284587859.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 763)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 763)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 763)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 763)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 763)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..763
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..763
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=84474
     Region          32..763
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mtdnkaakrp spsvrsmsar larsltsgkv kikpvleplm sihrefhpka dadvinraye
       61 taerlhegvt rnsgdpyith plavatiaae igmdtttvva allhdtvedt dysledltrd
      121 fgtevtrlvd gvtkldklaf gsgaeaetir kmivamskdp rvlvikvsdr lhnmrtmrfl
      181 ppekqakkar etleiiapla hrlgmasvkw eledlafail ypkkydeivr miadrapqrd
      241 rvlkeitnev sstlkangie aevrgrpkhy wsvyqkmivr grefaeifdl vgirilvndv
      301 nscyaaigvv hglysalpgr fkdyiaqprf gvyqslhttv isgagkplev qirthemhhn
      361 aeygvaahwr ykelkgknsg kdaevdqmaw mrqlldwqke aadpneflds lrydlassqi
      421 faftpkgdvi tlpagstpvd faytvhtevg hrcigakvng klvalesalk pgdrveifts
      481 kdpnagpsrd wqnfvvspra ranirqwfak emrevhleag rdalaaeiqr gglpmhrlft
      541 tssmkqvatq lhypdidaly taigaghvsa qhvanqlmam fgdqedavda ladrtplsel
      601 lqskqqaahq dhnrsgilve gnpdvlakia kccqpvpgde ifgfitrggg vsvhradctn
      661 atklrdeper vlevswannv dtegafsatl qlealdrqgl lydltgifqk sslsvlsmns
      721 qssedhvatv rftftvsgsk qlgalmntlr ntegvfdvyr vta
//
LOCUS       WP_284587963             196 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284587963
VERSION     WP_284587963.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..196
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=21659
     Region          <1..157
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mdglkdkplr vrvilrlase lglraseicv lrnrdisrdg ggwavrvhgk ggrirylpvs
       61 qslaadirql qsdhdspwlf pgridghlsa ryiskigara lpgewtlhtl rhrfattayk
      121 hckdllairq alghssiqtt trytdfdptq lthiiaatel ndaddtrkkr plpssplaip
      181 kaarakpppq sssqqp
//
LOCUS       WP_284588065             554 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284588065
VERSION     WP_284588065.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 554)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..554
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=59745
     Region          29..361
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(30..31,34..35,68,71,125..126,181)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(123,126,206..212,241,266..270,301,325..329,332)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mtaavpsriq paverqqhar rgdnriavlw fpdwpvqaal leetrhgisp eslaialasn
       61 hritaccdka rghgvrrgmk lraaqalcps mvvrdtdpqr dgrlfstive elenvsasle
      121 vlrpgmvaln ltaatrfygs eqaalehfid aaahegidat agaadelpta iiaarhrvlg
      181 avvqpgdsva flyqqplsvl laepalgcqk dtvetlaglg istlgeltel pttaistrfg
      241 saglhchria saqqqrkvap gaveldlsas itpeapitrv deaafiarml adqvhqqlat
      301 qglncvriki aaetddgtti skiwrtttal tehataervr wqldgwlssg gagaivelsl
      361 tpletqiptn tgsiieadta vaeettatvv srlqsmlgfd avqqphavgg rgvadrvrfl
      421 pygqaaenir elgrrnaewi gaipsplptr lgggldhpas rvrlvdkhgn pvfvtaeall
      481 sadpagmswg kkkfqvlgws vpwpvdtgww eseifdesqr larmqlvgkn agdqhpkawl
      541 lvwqhrawri eamy
//
LOCUS       WP_284588067             324 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284588067
VERSION     WP_284588067.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..324
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33665
     Region          1..289
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 massanpisv lciigscisl qlgsalavkl fddggtwgts avrllvaavv llaitrprvh
       61 ewnrqqwagv lglglslglm ngffyagidl vplgpavtie flgplllaaf lsrsvrdgic
      121 vvlamtgmal lgldafngnp lnplgvafll gaalfwaiyi lanknagalv pgqgglavaf
      181 vvggvamlpm gaggawnlis stntlwfaig tgilgslvpy slelialrgl apnvfsilis
      241 lepafaaffg wlllaqnist lklvaigvvi aasvvqtvgp krsgedgepr aklkklqdig
      301 kkvatkrtek rlraearsrk knld
//
LOCUS       WP_284588136             417 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284588136
VERSION     WP_284588136.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..417
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=44622
     Region          9..403
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mnltelatqr lekwqqqglm rtpiefagpq tpraqlkdqp serillsssn ylglathpev
       61 iaaarsalkk fgtgsggsrl ttgsttwhrr ierelanfvg fedavlfatg yqanlsvlqt
      121 lahpdlhifs dslnhaslid girlattsgt kksiyphcdy taleqqlaec taryklvvsd
      181 gvfsmdgdia dlarlreict hhdawllvdd ahgigtvgkh gigstqvhnt rpdilivtas
      241 kalgaeggfv acstpvanll rnqargyvys tacsaancaa isaaleviqk pltqqhpvvr
      301 lqqraaalre itgirvfdgv dsdgvhsgsv hsdsahspii plpvgaesaa vrlaseladr
      361 gfhipairyp tvargqailr atamatlela ditqfaqtlr dlgwrpptpa kaispgr
//
LOCUS       WP_284588207             129 aa            linear   BCT 25-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284588207
VERSION     WP_284588207.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..129
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13471
     Region          17..129
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 mnldisltea llstasvaag afagglvrgl lsklrgrytg tassnmlacf algimlarvd
       61 lgtlvhlpyw eiafgtgfcg alstlatlar elgnltyera wirlslytvf tvlgglgavw
      121 lgwllgmav
//
LOCUS       WP_284588444             849 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284588444
VERSION     WP_284588444.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 849)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 849)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..849
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..849
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=95290
     Region          20..843
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mnlndvvpdl sevpssllee siwesflrwt kdkgislypa qeeaslaala gdnvilstpt
       61 gsgktmvata aqffclaegk rsfytapika lvsekffalc dvfgpenvgm mtgdatvngn
      121 apiiaataei vanialrdgk daridqvvmd efhfysepdr gwawqvplle lpqaqfvlms
      181 atlgdvswlr edltqrtgrt ttlvtgttrp vplafsyefi aveemidtlv dnhkapiyvv
      241 hfsqrkateq aqsltatsfl nseekqrmve eigdfrfstt fgkqlskmir rgiglhhagm
      301 lpkyrrlvek laqtgllkvi cgtdtlgvgi nvpirtvllt glakfdgrre rivksrefhq
      361 iagragragy dtegtvvvla pefeienakm rrkagddpkr lkklkkkapr dgevswsekt
      421 yerlinsepe slssqfqmsn smllnviarp gdvyahmkhl irsnhdtraq qnqsilaats
      481 lfrglrnagi vdkpanetgt dsqgrryhlt eelqrdfaln qplapfalaa vglwdpdspt
      541 ytldvistfe ailddprqll qaqqsfarge einalkaegv dytermkive einwpmpcre
      601 eldaafetyc qghpwarefd ispksvvrdm lensmtfsdl iatyglarse gvvlryltda
      661 wrtlnhsvpa eaktdelsdi ivwlgeliqq vdsslvdewa tmtdedapvs qervdrelaf
      721 gvedpsalsa npralkimvr nymfrlvqlf alereerleq lldylenypd isdalddyfe
      781 qytdldtgpe argpeyfhld asarsrlwpv qqiirdpegn ndfqfvatvd ldasddagev
      841 rlrdlrier
//
LOCUS       WP_284588466             180 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284588466
VERSION     WP_284588466.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..180
                     /product="YceD family protein"
                     /calculated_mol_wt=19087
     Region          1..180
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mtspfvfdvk alltqqqgpe qithtgpapr rigaemlaie egaevtvdav lhslgsgvma
       61 dagvsavlrg ecsrclsple rptefrisqv faaddefisg daeddedags gdeipqvshe
      121 dtidllqtvt delvvalpfn pvcedgcpdd aptpapdgvs geeteehvdp rwaglekfrd
//
LOCUS       WP_284588561             555 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284588561
VERSION     WP_284588561.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..555
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=60592
     Region          145..540
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
     Region          <434..>461
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
ORIGIN      
        1 msesepqkap epsagwgtqg erkrrsyray rthrplrlrt wlvvltvlvs afglfassfa
       61 vysvmrevfy qrvdddltqs magwaqnsel fsgnlsaspp tdyavihifp dgssrvyndr
      121 dtlpqinnlv igggprsvas vdgpqqpewr alanqqngvv tivaknlere ngllrglaml
      181 qalislvmlg flallafavi rqtlkplqiv ertasdiaeg dldlrvpkwp lntevgqlaa
      241 alnimlerlq dsvetaqske eqmrrfvgda shelrtplts lrgyvelyrs gatndvdhvf
      301 atiddesgrm kllvedllal traegsrldk rtvdvlelsl avvgtaraay pertirvenk
      361 ttdipvvsgd pdrlhqvlln litnglnhgg peasvtltlr kesqddcmrl aaeqqetgdn
      421 heaeektsgw sqedgkngka gkdgkagkdg nkgtdgesak dyvciditdd grgmskevtg
      481 liferfyred psrargaggg sglglaivks lvdqhdgeit vdsepgvgst ftvripalde
      541 psaseetfdd ygeny
//
LOCUS       WP_284588124             243 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Mediterraneibacter gnavus].
ACCESSION   WP_284588124
VERSION     WP_284588124.1
KEYWORDS    RefSeq.
SOURCE      Mediterraneibacter gnavus
  ORGANISM  Mediterraneibacter gnavus
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Mediterraneibacter.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Mediterraneibacter gnavus"
                     /db_xref="taxon:33038"
     Protein         1..243
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28915
     Region          6..233
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mrgidmirig ivddeeimrl kihqcikeil keqesveirs ydcaedflee vqkkthfdil
       61 fsdiqmlemn glelgkrlqk dmpnlyiiyi taymeyaves ykisayqyil kedmeirlpq
      121 itrkllnqiq heyaqfrvvg tngiqkkiyf rdiiyvykgk etkyvyyvtt egeykerisl
      181 nqvwellegn gflkierayl vnakhilkle gnklflsdqs qlsisryrlk evkldiakyw
      241 ggr
//
LOCUS       WP_284588576             348 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284588576
VERSION     WP_284588576.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..348
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35791
     Region          35..340
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mdrqrtqqvl rarnrnrvll fivlvfalvs gtiaslvigq ytipigelpr ilavgplgvs
       61 amdesviwqi rlprlvlgll vgaalgvgga lmqavfanpl aepsvigvta gagvgaalai
      121 vlgiswfgat tvpvfaflsg llttwlvyql arfagrirvi nlalvgiavn avagalisff
      181 ifiaptssre qvvfwqmgsl sgakwahisv vavligagia valllvgkld vlalgeraag
      241 hvgidvarlr vlalllatll tagavsyagl igfvglvvph iirtvagpsn vvllpasalg
      301 gaalivladt aarsiidfad lpigiftalv ggptffillr ammrrgav
//
LOCUS       WP_284588579             428 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284588579
VERSION     WP_284588579.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..428
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46742
     Region          157..263
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mtdrkpgakr skkhgteqnt gqstesftes vsssltrlkn slhrhlsqqw teltspsfsv
       61 pasklpepla hhatevsast ipesvvaeia eslnlrgkha hhhaatdqes enapepedgs
      121 qtaeksdynf dssrhlplga rfkprgvfed dwsarpsadk pwpvilihgt vdtkgvwqel
      181 gtelradgwc vfapdygkrg taameesavq lgayieavrt itgaeqvili ghsqggllar
      241 ywmrtsgqar yvkhlvslga pnhgttmggi lsplvtnnlt enimhsliqh wfgpvgfqqi
      301 tgseifavfn ngaddrdgdg nsddssgtnt hgsgeledgv dytciasrqd tvvqppetcf
      361 lngpadqvrn vwvqdiipra nvqhqdlpmn khvraiirtg lkkganeenl khktqntepk
      421 trrlehgv
//
LOCUS       WP_284588829             406 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284588829
VERSION     WP_284588829.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..406
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43587
     Region          1..401
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 mafilgiflf algiavtial heaghmvsar afgmrvrrfy vgfgpsvfsf tkghtrygla
       61 alplggfcdi agmtamdemt edekphamys kpawqrivvl aagpfvnivl gllilflvaa
      121 saglpdphad vratvgevtc sadqkaptqs dapaelenct gqgaggqagv qsgdiitgfn
      181 gekldnfmqf rdevqsrpge titldierng relqldveld svvrydaegq prtvgsvgla
      241 sapldvhrey svagaipasf eyswfmlqat vegiiafpsk ipavaasifg aereqdspis
      301 vvgasragge lverelwpmf wmmlatlnff lalfnmiplp pfdgghiavv lwekirnllr
      361 rlrgqepggp anyekllplt ygmaamlltv gviviiadiv npialf
//
LOCUS       WP_284588861             517 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284588861
VERSION     WP_284588861.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..517
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54997
     Region          17..513
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mssgfarssf ahngrarvav igagpnglta aavlaqagcr vevfesadhi ggsarthpaf
       61 gagsavdfga aahpfgvvsp vfrqlgleny glewkhpqyp mahplvdapa vilhrdlktt
      121 aaqfsdhdrr vwnhlhkplv ddvgklvnsv lpvrprypla larlglrgvw parsltsrll
      181 vdeaarallv gsavhairpp sqpgtaafgl lfnafgmttg wpvisggtgq lamalarvik
      241 hyggtiktga kvqdlsgfvt ydavvttqtp rqllalqgld lsrlrsrslr rwkygtavyk
      301 vdylvngpvr wndprvagag tvhvggtvse mqlaesqaaa gmlperpfvm vcqqqtadpt
      361 rfsgnrrsvg agrvlsaqld agrmpedarq philwayahv phgyqekfpg evaglieaqi
      421 sryaagfsaq iierhqaspg qlqeananli ggdiaggamn laqmlrqrqy vgtltvnpev
      481 pvvqasgasl pgagvhgmag wraaqtilrr fgsielr
//
LOCUS       WP_284588966             208 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284588966
VERSION     WP_284588966.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..208
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23086
     Region          4..134
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 madnpaihqy rvplrwsdfd ryghvmnany veiaqearla ykeayfdpag medfaafvrk
       61 ldldfrkpie pegnsvllve sqvvevgnss fvtrqeikdk hgriacvvet vsvavdmdtq
      121 mprplteeer evmrlestla kaadkaeaes gsapsasgvq ldslgdeisy ddeisygdev
      181 dygdevdygd evgygdevdy gdeigydd
//
LOCUS       WP_284589223             449 aa            linear   BCT 25-DEC-2024
DEFINITION  acid phosphatase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284589223
VERSION     WP_284589223.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130290
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..449
                     /product="acid phosphatase"
                     /EC_number="3.1.3.2"
                     /GO_function="GO:0003993 - acid phosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=48923
     Region          <126..328
                     /region_name="PAP2_acid_phosphatase"
                     /note="PAP2, bacterial acid phosphatase or class A
                     non-specific acid phosphatases. These enzymes catalyze
                     phosphomonoester hydrolysis, with optimal activity in low
                     pH conditions. They are secreted into the periplasmic
                     space, and their physiological role remains...; cd03397"
                     /db_xref="CDD:239491"
     Site            order(215,222,251..253,286,292,296)
                     /site_type="active"
                     /db_xref="CDD:239491"
ORIGIN      
        1 mklraacqar ralllvtaia itsaiavpsi gtaataptts stahlalpfe ipqlqlpapk
       61 lssehgagpe ysplssigan pqhhagapvp qpfdvsyltg yvsdvssyry giyyevvref
      121 kdlrsnhpev mqknlnivad ynnnaqsprv dkairdalad kdgvlftaae algdefgqhf
      181 laalhekrlp ktefllgngy aaraggiasw graekllfnn drpfvqaper iqrhespere
      241 lydgssksfp sghtnqatwi ttllammlpe vgtqllargs eagesrlvmg vhfpldvigg
      301 rmtgqaaaad rwndpkmrda llqaraeiva emewraakpf aemiaedsha lsdqqaeady
      361 trrmtygftp ifatdepvnv ptaapallet rfpelsyeqr aevlrhtalp sgyplddrdp
      421 akgdwqrinl arawntqvsi gaggevvvk
//
LOCUS       WP_284589305             528 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284589305
VERSION     WP_284589305.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 528)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..528
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=54979
     Region          10..247
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mspsqnslkl nytaasdrgl vrtnnedsaf agrnllvlad gmgghaagev asqllvttmq
       61 rldrdpgend mlallgtaad dantaiadtv rqrpetqgmg ttctalmfng ttfgmchvgd
      121 srgyrlrggk leqitiddty vqslvdsgsl kpedvsthpq kslilkaytg rpvdptlrmi
      181 daqpgdrlll csdglsdpvt adtieqtlke gtpeqaaskl idlalrsggp dnvtvvvadv
      241 lagddestti paapvsagal alpeaerahp ntaagraaal nrrpqvvepk aqaagahnhg
      301 tganagngsg pgnvagagtg sgawaggsag aaensahdna skrgrnwtla ivvlvllagl
      361 igggwwvyas sqdkyyiatn nsdeliierg vdyslfgkdl hepyqrvclt kddevrttdl
      421 gekpsndchp fsltdlpgsv rgsithldsg sysevtdqlq rlsdkalpvc vnraetdnng
      481 knsegknndd nsgankdtdk dtnkdaanae saddgglstp gvncrevs
//
LOCUS       WP_284589416             333 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium propinquum].
ACCESSION   WP_284589416
VERSION     WP_284589416.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..333
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33831
     Region          24..326
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtrisflpaa vlavavlgva vaaslffgsn nispgqvwas lsnngdtatd tlvlqqrlpr
       61 tivvvlvgaa lgvagalmqa ltrnpladpg ilginagasi avvagvafag vtginnyifl
      121 aivgallasi mvyvlggagr nsvpsparlt lagvaismai sslvqaiils nanafnefry
      181 waagsvegrg wpvlehiwvf illglvfafa sapslnalsl geemgtalgv kvwrtrvltf
      241 saitilagta taavgplmfv glavpyaarg lfghdnrail agsvvigpvf llaadvlarl
      301 vimpqevqtg llsavlggpi fiavvrmkki gav
//
LOCUS       WP_284589430             444 aa            linear   BCT 25-DEC-2024
DEFINITION  D-alanyl-D-alanine
            carboxypeptidase/D-alanyl-D-alanine-endopeptidase [Corynebacterium
            propinquum].
ACCESSION   WP_284589430
VERSION     WP_284589430.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Kishida,H., Unzai,S., Roper,D.I., Lloyd,A., Park,S.Y. and Tame,J.R.
  TITLE     Crystal structure of penicillin binding protein 4 (dacB) from
            Escherichia coli, both in the native form and covalently linked to
            various antibiotics
  JOURNAL   Biochemistry 45 (3), 783-792 (2006)
   PUBMED   16411754
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449638
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..444
                     /product="D-alanyl-D-alanine
                     carboxypeptidase/D-alanyl-D-alanine-endopeptidase"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45621
     Region          68..444
                     /region_name="DacB"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG2027"
                     /db_xref="CDD:441630"
ORIGIN      
        1 mkvfwwvsvv ialvavaata tvgvayhqay sdvesappye lapanlpvtp vepsladdgs
       61 ttspaagfqa paidgqlgaa vvdlttqesv yehdahrqlv passtkiata taalasmdld
      121 krlhtviehd gahvviraag dvwlddaald aaaaaighad sveidtslws gptqaegwdp
      181 gnvaegyiap mepamlyggr igatsgdvpr sttpaldvaq aladrvgash vavndnaapl
      241 pavttlespi lrerlelmik hsdnvmaeai aretavargm qpasfsdats atleilreig
      301 ldtanmqisd nsglssqnrl tahgllqclq vaahgaagae aggdtranaa gagepgnnvg
      361 dlrslldvlp vaggdgtldd ryaelsargy araktgtltd tsalvgivtg rsghtyaysl
      421 lvndapilpa raqldefvsa lreh
//
LOCUS       WP_284589448             181 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Corynebacterium propinquum].
ACCESSION   WP_284589448
VERSION     WP_284589448.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..181
                     /product="YceD family protein"
                     /calculated_mol_wt=19324
     Region          <38..181
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mtspfvfdvk alltqqqspe qtthtgpapr rigaemlaie egaevtidav lhslgsgima
       61 dadvsavlrg ecsrclsple rpmtvrisqv fsadddfitg daeddedegs gdeipqvshe
      121 dtidllqtlt delvvalpfn pvceggcpdd sltpapdgvs geedaqerid prwaglekfr
      181 d
//
LOCUS       WP_284589534             349 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium
            propinquum].
ACCESSION   WP_284589534
VERSION     WP_284589534.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..349
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36620
     Region          24..344
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkkslvtali agaavlagai mlgpqriala nqatgdeqla telaelsvpg hnqlaamtie
       61 dgvtnyagwg adneteveig svtkmltael lrheidngav klettlgeli deladpvasv
      121 tleeavnhtg glprlagvgf tanlgfsvlg tnpydgigrd dvvaaangie elenrgeeqy
      181 snlgfallgw alaenadtty eemlhdvllq plgmhntfva neplpddepa gllnngrhaq
      241 pwvtegyapa gmvrstatdm arfaeylldk glpdygwart asaqdsdndn nassnnsnnn
      301 nagwhngqtg gyscmlviap etgraafvag ntprgveqig lqlageevh
//
LOCUS       WP_284589549             389 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Corynebacterium
            propinquum].
ACCESSION   WP_284589549
VERSION     WP_284589549.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..389
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41876
     Region          4..382
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mgdssargpl agiiiadfsr vlagpfctml ladlgarvik veaprgddtr qwappvandm
       61 styfmsanrn kesimldlqd ladrdtayei iersdvlien fkpgglkkfg ldpaqttkrw
      121 prlihasing fgsdkgahla gydlliqals glmhvtgead gppqktgvai vdvctglhca
      181 vgilaaller eksqagqsle vnllsvalss lanqsggyaa tghepmrmgn dhpslcpygp
      241 faahdqplii acgndaqfrt lveelgkpql adderfitmq drnkhrealr aeiedvlqhk
      301 saqdwydell aagvmcapin svgqgidfad slglepvvai hsaegstyrt irnpvqysrt
      361 kaeyhtpppr lgadgdavrs wiaqtnpra
//
LOCUS       WP_284589566             309 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Corynebacterium propinquum].
ACCESSION   WP_284589566
VERSION     WP_284589566.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..309
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31682
     Region          1..289
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 massanpisv lciigscisl qlgsalavkl fddggtwgts avrllvaavv llaitrprvh
       61 ewnrqqwagv lglglslglm ngffyagidl vplgpavtie flgplllaaf lsrslrdgic
      121 vilamtgmal lgldafngnp lnplgvafll gaalfwaiyi lanknagalv pgqgglavaf
      181 vvggvamlpm gaggawnlvs stdtgwfaig tgilgslvpy slelialrgl apnvfsilis
      241 lepvfaaffg wlllaqnist lklvaigvvi aasvvqtvgt ggsgangapr sklkklqdvg
      301 rkvvprrrq
//
LOCUS       WP_284589665             366 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Corynebacterium propinquum].
ACCESSION   WP_284589665
VERSION     WP_284589665.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..366
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=39743
     Region          62..346
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 masikkyeta kghawrvqyr spdgrnrtkq gfrtkaaaqs wadknatlmh egqwinpteg
       61 kktiadyhda ffatkahlas sslrvmwlsw akwvepewgr mavasvrksg vqawlsahad
      121 qpvsvrrahg vlagildlav ddraiavnpa rgvslprkpe vkqvyltehq laalakecge
      181 rggivmllgt tglrwgelag lqvrdvpdvg nriklvrtvt wtggsfevgv lkgresrvvs
      241 vpasvmkwvr gvaagrggde wlfgeggvpa rrpgvkswfa ravqrlvgrg vlperitphg
      301 lrhvaaslmi ggganvlavq rqlghkdasv tlntyaslwd qdldavgamm eqrfsdvvgl
      361 swaavs
//
LOCUS       WP_284589787             645 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Corynebacterium propinquum].
ACCESSION   WP_284589787
VERSION     WP_284589787.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 645)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 645)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 645)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 645)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..645
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72308
     Region          1..485
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mrfttlrisn fqsfgltptt lnltdmtyvl gangtgktaa lealsrlfsp vttqrkiris
       61 dfhvpvgssl adlqdkeavl wievdiefpe sdsdsyhasi pphfhhmmie sadgvpkvrv
      121 rltatlaldg vveerieyvr qvnelgaptn ctemsrydrg yievhylpar rdpsehiayt
      181 atsligrtlr aadwsqertt lsglseqlnn altsngavss mgihlkkqwd glhhgkfftd
      241 ptigfgqgel egvfrhltin fspshdgasl pfnllsdgqk sllyislvla wqslsrrvlr
      301 neeasldptr lrppvhtiia leepenslsp hylgriirql hnackeedvq aliathastl
      361 lrrvepesic flrlnekret tvhrillped ndetakyvre avraypelyf srlvilgegd
      421 seqvvlpril aaagiaedda svsvvplggr hvnhfwrlln elriphvtll dldsgrrgag
      481 wgriryalnq inqirpktya ketidglpkw dspvdfpqfv dpqfpegngl vqrlerhgvf
      541 fsnpvdldll mlesfpdayc vtatppdeka ivavlgkshv nekhlpqevl slfddyhanf
      601 dlkskpdthl halskladsd llegmpkvfq rlidhvkknl selpe
//
LOCUS       WP_284589810             269 aa            linear   BCT 25-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Corynebacterium propinquum].
ACCESSION   WP_284589810
VERSION     WP_284589810.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..269
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29702
     Region          6..>133
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mgksreeilh dprittvyis satgnhyrdt laalthgkhv lvekpiclft eelaeidgaa
       61 hrhnlvvaec lsyhfhprwn rameilrgqr qkeeltlraa fciphrtksd fryrpehggi
      121 vadlgtyvvd allraglpms qlqppvgsir isrlsgqvgt asqahsharw aigdsyqnef
      181 vvagttfrmd lqrafsppin eqtvltmtse sesespvghv fapanathlc itnalrsied
      241 revgivdvds iherisilen viaegnega
//
LOCUS       WP_284590188             659 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Enterococcus faecium].
ACCESSION   WP_284590188
VERSION     WP_284590188.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..659
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=76536
     Region          8..659
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mkqkeklllr ylidhkkeyv tsqrlasell lsdrtirnyl qrikelvekn ggkiiakpgy
       61 gyqlhilqrp tfdlflsrqe ivpgyarepq gfyesedrqk yilnqllled ailfmddlae
      121 elyisrsslt kdmqeikerl ipyslkivsk hgqgtwiege ernrrhfimd tffgnhygns
      181 lkeylgqsrf fpdisfeelv iiildetrea klkvsdfiiq nltlhlalgi krlregfeik
      241 elgieqevsk rveyqvaqri vqrieviagv sfpeeeiayl tlhlmaksnh kenqndqels
      301 kelakvlkrl sqefhfslve dlqlfnglld hlspmmirls rgirienplt eeikkenpkv
      361 fdavkrhfsn mpalknytin edewaylalh lmaalekera ahklhaliic atgygsaqll
      421 knrvvsefgk nitvvsvkgy yeinettlkg idliissidl stmffkipvl hvsiflnedd
      481 vrkirkvvge sipyhssdrp ipafslqqkk qiyteqlsek ffktytyepk keeilhdllq
      541 klsineeegy iremrkqiqq renmgqiifs dtvavphpav pvgietkvav alipsgmqwd
      601 qyqeihfvfl vspsyveneg itvvtkaivr lvdqlkvqqe ilaepifenf sskfiklie
//
LOCUS       WP_284590209             262 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Enterococcus faecium].
ACCESSION   WP_284590209
VERSION     WP_284590209.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..262
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29560
     Region          4..260
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mafiqaniys nvlemevnln vilpqttkkv igtsseqett dipvlyllhg mggnhsvwer
       61 rtsieryvad yglavimpst dlgwytdtvy dmkywtfiae elpeichelf pqltrkrekt
      121 yaaglsmggy galklglaks enftavisls gavsvgnrmd dllmvrkaaf wegifgpldq
      181 iegskndpqy llkelvksgk pvprfymacg esdflyqanq emvsamqeqg lavtfeqgpg
      241 dhnwifwdqw iqralawlme ek
//
LOCUS       WP_284590313             412 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Staphylococcus aureus].
ACCESSION   WP_284590313
VERSION     WP_284590313.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     Protein         1..412
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=46927
     Region          162..400
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 menqhnskll tllliglavf iqqssviagv nvsiadfitl lilvyllffa nhllkanhfl
       61 qffiilytyr miitlcllff ddlifitvke vlastvkyaf vviyfylgmi ifklgnskkv
      121 ivtsyiissv tiglfciiag lnkspllmkl lyfdeirskg lmndpnyfam tqiitlvlay
      181 kyihnyifkv lacgillwsl tttgsktafi ilivlaiyff ikklfsrnav svvsmlviml
      241 illcftfyni nyylfqlsdl davpsldrma sifeegfasl ndsgsersvv winailviky
      301 tlgfgvglvd yvhigsqing illvahntyl qifaewgilf galfiifmly llfellrfni
      361 sgknvtaivv mltmliyflt vsfnnsryva filgiivfiv qyekmerdrn ee
//
LOCUS       WP_284590310             281 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus faecalis].
ACCESSION   WP_284590310
VERSION     WP_284590310.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10648172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..281
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32597
     Region          214..263
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mvificdnvi vymtefinsf ateynqtfmt apflktiifi ccnfaylaii ntisgrpfkn
       61 yqfvwlflig lwmlaipfsq nsalkvwlyy lsnqlfliyl gcyalyqlri dplsalakky
      121 lrfigwlsig fgvailledt fvifnidqys divfkinnrn vsediytiil siaiiyfcnr
      181 dfplsvlekd aakleenqsd epvllapfcd ayqltqrere vlsllleckt nqdianelfl
      241 sigtvkthih nifvklevnk raevfvsyql fsqqqtehla r
//
LOCUS       WP_284590336             121 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Enterococcus faecium].
ACCESSION   WP_284590336
VERSION     WP_284590336.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 121)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 121)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 121)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..121
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13349
     Region          34..107
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(35..36,38,41,44..45,48..49,52,83,102..103,105..107,
                     109..111)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(36..37,41..43,57..59,68..71,73..74,77..78,80..81,
                     87..89,94..96)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(57,60,102)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mtaevctttc ihkekvasvk nnlkdkdlst llvlgkcfsd ssrikifyal etykemcvcd
       61 laailnasia ttshhlrflk kngmaksrqy gkvvyyslan eeilsavqsf lklsenssmk
      121 a
//
LOCUS       WP_284590357             402 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Enterococcus faecalis].
ACCESSION   WP_284590357
VERSION     WP_284590357.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..402
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46943
     Region          94..365
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 maktkyagvy vdnngkyfye vdlgtdritg krlrkkgrkn qqgkkfvsaq qaykelirik
       61 neslstngya nynmtyelfm nsvyipayka dveestfyvr ektlenirdr faklelrsit
      121 irdiqqfrtw llsengagys qayaslvfgm frkslemave mqfleqnisk kvkaipkgks
      181 ivpywtktef ekviskicld dfyehlcfvl lwvyfmtgvr vsegtalwwe dvdfknkrlr
      241 vhhtmfmknk sdwtrknytk ttdgkriisl dddtlkilke wkmrqaeigi hdfifsydgk
      301 pmikstisri idryaklagi hriqakglrh shasylinef nvsvlilskr mghsspditl
      361 khyshmwsgi deliaeemtg niqfqpaltt kvhfngnqti kk
//
LOCUS       WP_284590624             385 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Enterococcus
            thailandicus].
ACCESSION   WP_284590624
VERSION     WP_284590624.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus thailandicus
  ORGANISM  Enterococcus thailandicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Enterococcus thailandicus"
                     /db_xref="taxon:417368"
     Protein         1..385
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43577
     Region          50..380
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mhnkkhqkrq arkktvllai ltiflglgvt tswyllllsd tikpvadqep atvvnltase
       61 kkaatemdql lkkskyigti yvrknnriil ektygyadke tnqpnslsld yqigsiqkam
      121 tallilkqie qkkisftkpl atfypqipgs qsitihdllt mrsglhkteq psvpltdrdi
      181 vqftvehlkw tdyqtyhyep lnftllagil mqltnksyee llsdslikpl qlqhtdfyen
      241 vknssqhaks yqmsadddyw keldenetai hnelgtgnis mntydlaaff tkvlsgqlip
      301 kkllfslwqn nqlkhpysgg vysgadyila qgninrfhsv vamtkdtkna ivmqsniqsd
      361 tkikpgavai rnqlyeiltg kklps
//
LOCUS       WP_284590660             379 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Enterococcus thailandicus].
ACCESSION   WP_284590660
VERSION     WP_284590660.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus thailandicus
  ORGANISM  Enterococcus thailandicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Enterococcus thailandicus"
                     /db_xref="taxon:417368"
     Protein         1..379
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44013
     Region          63..377
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mwveqtkdgr fkfieryvdp ytektrkkst tltsnspqaw kkaqkildkk iedalanfnk
       61 sditfknlye ewyeyykqhv krtsylkvpl mmkhvskhis ddtlvrnide tlinkiiedm
      121 ytfgelslny tkqtkttlsv mlnyavdrky iqrnpalsvk ihpkkveeek rklamdkkyl
      181 ekeeidlilk qlyskprrrl hgiiaeflyl tglrygelia lqmkdygdgm isvngtldyt
      241 fikmdnavkt tpknayshrk vqlsnrakkl ieeaiadnkl aergtelddy ifvsangtpl
      301 tlhsfnavlh kvekelklek slsshifrhs hvsllselgv plkaimervg hsdanttlsi
      361 ynhvtkkakq qvidklnsi
//
LOCUS       WP_284590676             547 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Enterococcus thailandicus].
ACCESSION   WP_284590676
VERSION     WP_284590676.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus thailandicus
  ORGANISM  Enterococcus thailandicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 547)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 547)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Enterococcus thailandicus"
                     /db_xref="taxon:417368"
     Protein         1..547
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62058
     Region          2..446
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 miekvrienf kcikgtfeld lkqginilvg nneagkstil eaihmalcgv frgktikgnl
       61 sqylfnyevv deylkdikqg iineapyili elylsegtfp mlegdrfsdk srlgrtngia
      121 lkiafdekyk eeyesllksa elvslpieyy dvewyafsrk pltsrsipik ssfidvgssk
      181 fqngsdvyis rivqnalemd ektkvaqafr kakeffskdp aianintkit gisklskkdi
      241 eltvdlgsrs twdgslitql nkipfdyigk geqaivktdl tlsnkkseas svilieepec
      301 hisharlnql lesiksnygd kqiiisthss fvanklglnn lillnqqktv rfdhlkskdf
      361 fekvagydtl rlilcdkail vegdsdelvi qraymdthng rlpiednvdv isvgtsflrf
      421 leiaenlett vrvvtdndgn vaalekkyka yigsnkkkni eicfdknett gtlkigtkdp
      481 ksfnyntlep lllksntvel fnqifetnys eedlhkymkt yktecalkif nyhsnikype
      541 yimravq
//
LOCUS       WP_284591262             585 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 35 protein [Enterococcus casseliflavus].
ACCESSION   WP_284591262
VERSION     WP_284591262.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 585)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 585)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..585
                     /product="glycoside hydrolase family 35 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=67564
     Region          9..324
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
ORIGIN      
        1 mrtfaieddf yldnkplkvi sgaihyfrvv peywqdrlek lrlmgcnive tyvpwnlhea
       61 qegvyqfdgi ldlrrfiqta qevglyvilr papyicaewe fgglpywllq dpmmklrfdy
      121 ppfmekitry fahlfpqvrd lqitqggpii mmqveneygs yandkeylrk mvaamrqhgv
      181 etplvtsdgp whdmlengsi kdlalptinc gsnikenfek lrrfhgekrp lmvmefwigw
      241 fdawgddqhh ttstqdavke lqdclalgsv niymfhggtn fgfmngsnyy erlapdvtsy
      301 dydalltewg eptakyqafk kviadyaeip efplsmkier kaygtfsvke rvslfstidt
      361 isqpiisnyp lsmeacnqat gyiyyrslig parkiadyrl intmdrahtf inqellridy
      421 dqeigqtysf dlsesenelg ilvenmgrvn ysvkmnhqhk gikdgviing afqsnweiyp
      481 lpmdnlhaid fqgkwqkgqp sfsrfecafd ecadtfielp gwgkgfvqvn ghtigrfwek
      541 gpqqrlyvpa pflkigmnei ivfesdgkiv deivfhdqad lgpea
//
LOCUS       WP_284591383             280 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Enterococcus
            casseliflavus].
ACCESSION   WP_284591383
VERSION     WP_284591383.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..280
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32200
     Region          56..170
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 myqelrkaie rpplykkmae afwddayisk qmlkahldpd fegasrkadf idesvrwisr
       61 ivppekqtql ldigcgpgiy aekfvalgyq vtgvdysrrs iayardsask qqlnitylfd
      121 nylemalpqq fdfitliycd ygalnpeerk lllnnvlahl kpggkflfdv ftiaqfltld
      181 eeqtweshes agfwrgdphl vlnqrwkypd hvlleqttil adteltnyyl wttyftkdal
      241 lrevqaagfd icevfgdvkg slyseegstm aillkkpcth
//
LOCUS       WP_284591482             400 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Enterococcus casseliflavus].
ACCESSION   WP_284591482
VERSION     WP_284591482.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..400
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46104
     Region          74..374
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msyektrktk yvgvyqdmst kkygyrvklg tdrvtgkalq ehrrgfptar eanearttal
       61 kkkqdlgals daqmtisdfl dkyyipeykn nveastwksr sgvfieikdk fgmkkprnvt
      121 tldildyknf llekhsqnya rlkfgmfskv lkhakkhgll kenlveivgg ipkkkpetqf
      181 wtkeqfekci qtfniedfye hmgfvivwly fmtgmrvnea talywednid fdnqqikiwn
      241 nldftngkvw trktkmktea grriisiddd tisvlkawkl rqkkygnfdf visytgeplg
      301 kstigriikr hahlsgipei ppkglrhsha sllinaganp lavqkrlghs diqitlgtys
      361 hlyptvdrdv adklggiiki etakdslvnw ngnqvykknr
//
LOCUS       WP_284591495             591 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 35 protein [Enterococcus casseliflavus].
ACCESSION   WP_284591495
VERSION     WP_284591495.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 591)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 591)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 591)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..591
                     /product="glycoside hydrolase family 35 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=66837
     Region          9..327
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
ORIGIN      
        1 mrtfeikedf lldgkpikli sgaihyfrmt paqwtdslyn lkalgantve tyipwnlhep
       61 regvydfegm kdicafvkqa qalglmvilr psvyicaewe fgglpawlln epmrlrstdp
      121 rfmakvrnyf qvllpklvpl qithggpvim mqveneygsy gmekaylrqt kelmeecgid
      181 vplftsdgaw eevldagtli eddvfvtgnf gsrskenaav mkefmakhgk nwpimcmeyw
      241 dgwfnrwgep iikrdgqdla nevkemlavg slnlymfhgg tnfgfyngcs argaldlpqv
      301 ssydydallt eageptdkyy qvqkaikeac pevwqanprt kqlaalgtfp iensvsllai
      361 kdqlmapqen mypltmeaas tgygyllysv qlnnyhrenk lkvveasdrl hiftdgqlqa
      421 iqyqetlgee lliqgapdke tieldvlven lgrvnygfkl ngptqakgir ggimqdihfh
      481 qgyrhypltl saeqlqaidy qagknpthps fyqttftlte vgdtfidcrg ygkgvvivng
      541 inlgrywqrg pvhslycpke flkkgsnevv vfetdgveik elvfcdqpvv e
//
LOCUS       WP_284591543             482 aa            linear   BCT 25-DEC-2024
DEFINITION  FGGY-family carbohydrate kinase [Enterococcus casseliflavus].
ACCESSION   WP_284591543
VERSION     WP_284591543.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..482
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=53773
     Region          5..474
                     /region_name="ASKHA_NBD_FGGY_GK"
                     /note="nucleotide-binding domain (NBD) of glycerol kinase
                     (GK) and similar proteins; cd07769"
                     /db_xref="CDD:466789"
ORIGIN      
        1 mdktyqlvld qstsgtklll fqegkilqry dkkhrqiypk vgwvehdple iwqnvqella
       61 qvfqeqaita dqivslsltn qretivawdr ltgnplynai vwqcnrsaai ceeltaqgwe
      121 rtinqktglr ldpyfsgtkv kwlaqelsai keksgtgela igtmdswllw nltqgtvfat
      181 easnacrtlf ynieegrwda elvklfgihl adlpaikpad tvfgnyhgip ikgiladsqa
      241 alfgegcqsl gdvkitmgtg csimmqvqqe qtlrdrrilt tvgwqtsqet afalegiirs
      301 cgdainwfse qvaplpdvae icqevltnds qediyfipal qgmgapfwdn tmtasfvgmk
      361 rtttthellk avlesiifqi kavidvmeev aerlinqvmi dggvsknral msllatlink
      421 pvivseveef saigtmlvan pimnepaiqq ttivpqaeqa virlkyekwk rfieksaafs
      481 eg
//
LOCUS       WP_284591888             326 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Enterococcus casseliflavus].
ACCESSION   WP_284591888
VERSION     WP_284591888.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..326
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34685
     Region          22..326
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mkkfswllll fsgcfiicff laitqgaadl sfetiwdaif afdyenqlhq vlrnirlprv
       61 laaflvgscf avtgaimqgi tknaladggl lgvnsgaamg laiafilfps iqpsqaalfs
      121 lfgafaatal lflltryakl gmsptglila gvalssffsa isqtlslqfd lnqelafwfi
      181 ggaanvtwqq lrfvgpiyli aivfvlrlgk alnllalgdd tvislgkhph lirasalllv
      241 vvlagmavsl vgpvsfvglm vphvvrgmvg knyqlilplt ilgggtlvma adlagrlinp
      301 pfetpfgilm aligvpflli kirreg
//
LOCUS       WP_284591903             256 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family oxidoreductase [Enterococcus casseliflavus].
ACCESSION   WP_284591903
VERSION     WP_284591903.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..256
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=27250
     Region          3..255
                     /region_name="fabG"
                     /note="3-oxoacyl-ACP reductase FabG; PRK05653"
                     /db_xref="CDD:235546"
     Site            order(13,15..18,37..39,59..61,87..89,111,137..139,154,158,
                     184..187,189..190)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:212491"
     Site            order(112,139,154,158)
                     /site_type="active"
                     /db_xref="CDD:212491"
ORIGIN      
        1 mndfknkrvi vtgaasgigk avaeqflaqg alvglidrne eelqellady daqthyravd
       61 vteaeklqea msglveelgg ldvlhvnagi ngtwtpieel tvaewdqtin tnlrstfitv
      121 kaaipfmkan ggsivitssv ngnrifsnfg ataystskag qvaftkmaal elsgynirvn
      181 aicpgaiatn idasteieee varveipvky persrplkqe tgvpeqvanl vlflsseaag
      241 nisgtevyid gaesll
//
LOCUS       WP_284591927             713 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Enterococcus casseliflavus].
ACCESSION   WP_284591927
VERSION     WP_284591927.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 713)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 713)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..713
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=81451
     Region          3..710
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mndlkaekkh ladtyqqllt rktvlnsflt egrkkdrlam qsigeeirln fnnfadrldt
       61 faaiesknre idqmnaalqs aerelaaidr lldspyfgki slqfedeeti edfyigingf
      121 vnenkegliy dwrspiaelf yakrlgpvsy qvnnqtisaa lehrrqfiie kdhlkqafdt
      181 svaiqdevll aaleannsqk mqditasiqh eqnviirdla hknllvngva gsgktsavmq
      241 riafllyhfr eemtaenvli lspnsrfidy isqvlpslge knpltltmrq fcqafpsvdl
      301 eseeayfdri qqtpneaidl lrsadfsrfl qslskqlpee lvlqfkpikr knvvlfseet
      361 idtffqetpk qaslrdriqa vkkklayawe erlqknalaa nvhdqvrslt edeqrsllgt
      421 vlkddsekti qkaairllkk kyatvskqin dltwfdtkrl ladsadyfth gqitltqttd
      481 sldytvclll irhllaekqp vpalrylfid evqdytpaqi qfllclfpmt aftlvgdqqq
      541 aiftsaitvs eiqtlfqqqa kfletyqltt syrssgaitr lfaqmlpkkt nlnisavrpe
      601 gklpqfyanl pdvalvdivk elkqpvtiit kdsrsseelk qffdkqavsf hgtvlpihla
      661 kglefkqvll ydvseenyht dqdrrilyta isrameelvv tskgtfspfl ppc
//
LOCUS       WP_284591965             473 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Enterococcus
            casseliflavus].
ACCESSION   WP_284591965
VERSION     WP_284591965.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 473)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..473
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=55149
     Region          1..471
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 maihvmwfrk dlrlgdntal tealvslqen dhllcvfhln dkqflpeaps hdyffsavah
       61 fieaakkqnl tihlltgtlt eafdqlfacy pewsqlyfnf dnrgfgrkrd lyikelvekk
      121 gitvhsfedh hlhqptevtk edgtyykkft pyykkwiqlp kpvyqkqald fekavhfdda
      181 phfkagtall akllenrktd fstivgedya hkqlqafvqk rlatyekdrd ipsikgtsrl
      241 spflsfgqis irkvwaacqg mpsstgkatf lkelawrdfy hmiyfshpeq knyeliekyr
      301 nmdwrkneee ltkwqagqtg ypiidaamrq lnqtgwmhnr lrmivasflt kdllidwrqg
      361 eayfarqlid ydvasniggw qwaastgtda vpyfrifnpi tqgkkfdkdg tfikqfvpel
      421 aqlplkfihe pylmtdeeqa dlkvvlgtdy plpivdhnea rkraldlysk iep
//
LOCUS       WP_284592333             463 aa            linear   BCT 25-DEC-2024
DEFINITION  RecQ family ATP-dependent DNA helicase [Enterococcus mundtii].
ACCESSION   WP_284592333
VERSION     WP_284592333.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Larsen,N.B. and Hickson,I.D.
  TITLE     RecQ Helicases: Conserved Guardians of Genomic Integrity
  JOURNAL   Adv Exp Med Biol 767, 161-184 (2013)
   PUBMED   23161011
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Rezazadeh,S.
  TITLE     RecQ helicases; at the crossroad of genome replication, repair, and
            recombination
  JOURNAL   Mol Biol Rep 39 (4), 4527-4543 (2012)
   PUBMED   21947842
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Bernstein,K.A., Gangloff,S. and Rothstein,R.
  TITLE     The RecQ DNA helicases in DNA repair
  JOURNAL   Annu Rev Genet 44, 393-417 (2010)
   PUBMED   21047263
REFERENCE   5  (residues 1 to 463)
  AUTHORS   Chu,W.K. and Hickson,I.D.
  TITLE     RecQ helicases: multifunctional genome caretakers
  JOURNAL   Nat Rev Cancer 9 (9), 644-654 (2009)
   PUBMED   19657341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..463
                     /product="RecQ family ATP-dependent DNA helicase"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0043138 - 3'-5' DNA helicase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=53364
     Region          2..433
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
ORIGIN      
        1 mdlldplkqy fgfssfrqgq eeiistllnq kdvlailptg ngkslcyqlt gylqegmvli
       61 vspllslmed qvgqlqkrge krvvaynsll trsekqyvla hlseykfvfv spemlqqpev
      121 lhalkqqkis lyvvdeahcv sqwgidfrpe yqslgrvake lgspttlalt atatrpvqee
      181 iehilfrakp alvkhsvnre nislfvfhtd ekdqqlrqlm aradgamiiy catkkeverl
      241 yqllhkdyav gyyhggldas qrrqlqqqfs knqlqfliat nafgmgidka diryvihydl
      301 pdslenymqe igragrdqrp ssavllyrpg degiqyffqq lskeqrhife ehlldgqtea
      361 sqfdeiqqkw lmlvnemqsp dtwllqlkkq ehvkikqlqq mlayihitsc rrerlmdyfg
      421 etlkekpkkc cdrdgaslfl setghtsptv eatdwqtill nlf
//
LOCUS       WP_284592355              71 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Enterobacter
            roggenkampii].
ACCESSION   WP_284592355
VERSION     WP_284592355.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter roggenkampii
  ORGANISM  Enterobacter roggenkampii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 71)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 71)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 71)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Enterobacter roggenkampii"
                     /db_xref="taxon:1812935"
     Protein         1..71
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=8252
     Region          9..60
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mvqnitdkhp klirlpevkr rtgfgktwiy tliragkfpk qvktglrsia fieseidewi
       61 ykiisdsrnh i
//
LOCUS       WP_284592542             426 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Enterobacter roggenkampii].
ACCESSION   WP_284592542
VERSION     WP_284592542.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter roggenkampii
  ORGANISM  Enterobacter roggenkampii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Enterobacter roggenkampii"
                     /db_xref="taxon:1812935"
     Protein         1..426
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=47762
     Region          11..395
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mkyptgvenh ggtlrlwfiy ngvrvreslg vpdtaknrki agelrtsivy avktgtfnya
       61 sqfpnspnlq rfgevskalt igelaekyls lketdvasts iktyrtiikn vllilgekti
      121 assiskeril evrkelvtgy qfpktqyvvt epgrsavtvn nymtnlfaif qfgvengyld
      181 etpfkgispl resrvvpdpl sreefvrlie acrsqqaknm wslsvytgir pgelcalgwe
      241 didlkagtmm irrnlakdkf tvpktqagtn rvihliepai ealksqleit rlgkehmidv
      301 hlreygkkek hkctfvflps vtsrtgicgd hftvdsvrqt wdtavkragi rhrksyqsrh
      361 tyacwsltag anpafiasqm ghadaqmvfq vygkwmsenn daqvallnsk lsefapsvph
      421 ttlrav
//
LOCUS       WP_284592570             380 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Enterococcus faecium].
ACCESSION   WP_284592570
VERSION     WP_284592570.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..380
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=44293
     Region          22..361
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 makfeqykkk ngekawkfqa ylginpetgk svkttrrnfk tqreaklala rlqseyednl
       61 lkkdkpktyk dvydlwmtey krtvrgstll kterifnnhv leelgdiyis eitpikiqel
      121 mdkwankydt askmmnytgl vfkyavrfgm iesnptdsir kpkrrkkttt eepfydkkql
      181 klfldalyeq pnikvqaffr llamtgmrkq eagalewrdi dfkaktvniy kavtrtangl
      241 eidttktvgs sriisidqgt ldkllewkev alppsddwli fgqtnaknph dimsldtsrk
      301 wllniqdqmd kkqkkklpri tvhgfrhtqa slliemgasl kevqfrlghe diqttmntya
      361 hvsklakeql adkfnkfidf
//
LOCUS       WP_284592689             314 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Enterococcus faecium].
ACCESSION   WP_284592689
VERSION     WP_284592689.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..314
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35238
     Region          13..287
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 meekieeskq kidqliqele kavigkrsti qlmivallag ghvlfedipg vgktllvkal
       61 akavqgtfsr vqctpdllps dilgfsvyns qskefefrsg pifttillad einrttprtq
      121 salleamaen hatidnntyp ldnhffvlat qnpieyegty plpeaqldrf lfrlqigyps
      181 fddellllld kfekvldnln evlnsyeiee iktnvanvfv spevasyalq lvsatrshaa
      241 iqlgisprgs lsfiqaakay alihgrnyvt pkdfqdlvpy vfshrlifyd rslkedekkq
      301 iihtlvaqip ipvr
//
LOCUS       WP_284593088             475 aa            linear   BCT 25-DEC-2024
DEFINITION  lipopolysaccharide biosynthesis protein [Enterococcus faecium].
ACCESSION   WP_284593088
VERSION     WP_284593088.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..475
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54568
     Region          1..383
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mkktvkdify naiyqvflii lplltipils rrigstglgi ygyvfsisqf lmtviavgmn
       61 pfrirniaks redkkalslq fwniyflqfl iglsvsflyi ayiyffdvky knlyliqlif
      121 iagltldisw ffqgieefsk vvirntvikl ssvlliilfv stkddlwiyv fitsitnflg
      181 slvfwlsihg kvgkpifnsn vfkqlwkpaf iiltpqlfmq vyttldktiv gyfvdptels
      241 yydqsqkiar iilavltsit ivmlpkiska qaegksenil vytkksfdyt iiialilfsv
      301 vfintkefvp wffgenfkpm tinmliscli ivvspiggvf anqfaiaiek dkeyaypmii
      361 gaivsiignv afvptygava ativlvvvel lvfffrvffv rkeikisyff gknvilffiv
      421 nltlttsayy flpqlfsssf ldmaiksimi fiiylpfvyf lfpdirneir kitrk
//
LOCUS       WP_284593471             581 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC1 kinase family protein [Enterococcus faecium].
ACCESSION   WP_284593471
VERSION     WP_284593471.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..581
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0004672 - protein kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=65893
     Region          1..489
                     /region_name="AarF"
                     /note="Predicted protein kinase regulating ubiquinone
                     biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport
                     and metabolism, Signal transduction mechanisms]; COG0661"
                     /db_xref="CDD:440425"
ORIGIN      
        1 maqtnprsrl aeiirvfiny nvvpnfvqqk npeqvkkafe elgptfikig qmlsvredll
       61 ssaftqtfkt lqdsvpsdtf stvkktiete lslslsdifd dfskspfasa smgqahrakl
      121 kngdsvvvki qhpniaeeir ldlqlferai plikyipets vvdlkgvlqe vkrslinemd
      181 flkesqngeq fyqknngwke irspkiydaf cskkvivmee msgknlnhlm naenktetfi
      241 tgiqnkqlkq evakllvenf mkqvfddgff hadphpgnll fhvlkkeeqt kasrkteivh
      301 ekefgsfafr aststedpva pytinyidfg mmghlsaglr qkltqavlal ytkdayriek
      361 avlrlcqqeg sfdesrfhqe ltsfleqyyd spideinlqe vfthvvtich qnnlqfdrdi
      421 tlllkafgtl egvirvldpe vslmevaspf aqhyflthld vedtlkqsgl dllegmkaap
      481 kipqqlhhll emwtsgqgkv nlelkkqdkl lsriesminr lvfgmilaal ivgssllvqa
      541 apvenaevvs llgiftyaia afviiflaid aliqmykkrk k
//
LOCUS       WP_284593561             309 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Corynebacterium propinquum].
ACCESSION   WP_284593561
VERSION     WP_284593561.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..309
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33158
     Region          3..277
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
ORIGIN      
        1 malneelvpr iplgtwgdda lmwlrenasi vfeffstvts flvegladgl kaipafllll
       61 ifafagwalr swrlaigval tfllvmgmrq weqmldtmal viiatlvavv iaipvgiwaa
      121 kndrlsavvr pildfmqtmp afvyllpavm ffsigvvpgt fstiifalap gvrmtelgir
      181 hvdaetveag rsygatdrqi lrgielplam psimaginqi imlslsmavi agmvgadglg
      241 kevvaaistl nlaqgleagl avvilavfld rltaalgnpg dypssllarw rkrkrdkhka
      301 hstlaagak
//
LOCUS       WP_284593566            1103 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Corynebacterium propinquum].
ACCESSION   WP_284593566
VERSION     WP_284593566.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1103
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..1103
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=116251
     Region          198..344
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          550..1049
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 msvkstsprn trggserkka rsnstrpasr srtsrtetkp sgsaastrag gkstrdsvtk
       61 vesthpetav fgsshraant shertgsafr avgsgigavf sktaealtkf gnigqsdeey
      121 deyaeydddv vtnrgshgkl dedlysadtp dssvkqkkpa kktessvrsn petsdtdelg
      181 devstaqkaa sgpssrsdai alvligiaiv lgasvwldia gfigrgiata thavlgagaf
      241 vipvalvvaa aalfsgkrva lenrvrvsag tglivvsmlg lihlfsgapd swaerfvagg
      301 algawtggal aagfssyvav pllilviiyg alkvtgitvk efaeylreav sgntgdteas
      361 aedsteldda yghvdkdida ivsgsprtpr rraplratpv vpparsagrg tapvnaagav
      421 apaaeqlnna ghkapsesal dngreeqtev lrntavhars eqspvstagt rrapsmsdtd
      481 eipavpdssr agsdnsstsa gsehtevlsa esrdavaqah dslqqqkkpv sqapqakash
      541 aphieqtvpe vidaepadgt elnteaviep veysipspgl lepgrapktr tetndrtiea
      601 idacfaefkv daevtgftrg ptvtryivel gpgvkvskit nlqsnlayav atgnvrilap
      661 ipgksavgie vpnsdreivr lrdvlesevi agdedptlvg lgkdiegefi sssiqkmphl
      721 lvagstgsgk safvnsmlvs lltratpddv rlilvdpkmv eltpyegiph litpiitqpk
      781 kaaaalqwlv eemeqryqdm rsarvrhikd fnhkvrtgqv qapagservm epypfivcvv
      841 deladlmmta pkeieesivr itqkaraagi hlvlatqrps vdvvtglikt nvpsrlafat
      901 ssstdsrvil dqtgaeqlig mgdglfipqg grpvrmqgaf vsddevyavv eaakaqgepd
      961 ytegvtedkq aeakkaiddd igkdmddlle avelvvtsgl gstsmlqrkl rigfakagrl
     1021 mdlmetrgiv gpsegskare vltkpeeldt tiwmikgadp aeapkevqeq eahfgeaaed
     1081 dssdgtgapq vskasynpts saf
//
LOCUS       WP_284593739             353 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium propinquum].
ACCESSION   WP_284593739
VERSION     WP_284593739.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..353
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36337
     Region          40..349
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mrknsreytr ssrslrtrri tgllalalll aaallasllf garpiafada vqalinlpsl
       61 ldepqsgsad arviadlrwp rtliglfvga algvagaliq ghtrnpladp gllgvsagaa
      121 favvlgffaf gltsalstsv vafcgavlat alvfglaslg ggqinpltli lggaaltavl
      181 hsmttaltli ddnsldrmrf wsvgalsgrd lsifwgtapf itvglivala taptlnllnl
      241 gddaasalgv ntyrarlagm vviallagaa taaagpigfi glvvphiars lcgpdyrwil
      301 pysaltgasl lllsdilgrl iarpgelqvg ivlafvgapf fmyliyrrkv val
//
LOCUS       WP_284593787             498 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium propinquum].
ACCESSION   WP_284593787
VERSION     WP_284593787.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 498)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 498)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 498)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 498)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 498)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..498
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51510
     Region          24..442
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 menraksasq tataaphprd vvtrrallvw vggvacyiva itgrtsfgva svdaierfqv
       61 dasriavfaa vqlgvyalaq iptglgidkf gpramvivga vvmglgqfil alttsyplai
      121 garvligagd asaflavmrl lpywfplrkt plftqltgai gqtgqfisav pflallgaag
      181 wtasfvtlga asiliaglag laikdlpdvd rhtmgqgskv kdaasmkdea skvdaspdtn
      241 iaslaarira lvrtpvawqg ffmhysclmf qlvflmmwgf plitlgmgls seqagavlai
      301 ntvvtvasgp lhgmfsarlg atrhwavvvf sttivltwvv ffatgtprgm aaivvvnvvv
      361 alcaasanyg fdnvregvsr etvatatgla nmggflsgma asqgigivld isadgaeysw
      421 tdfqlaalag gsvwavgiag lfcatawrtr eiqrvrsggt aapagsaaaa askgnstatq
      481 hglviheatt pepenrtd
//
LOCUS       WP_284593804             445 aa            linear   BCT 25-DEC-2024
DEFINITION  acid phosphatase [Corynebacterium propinquum].
ACCESSION   WP_284593804
VERSION     WP_284593804.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130290
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..445
                     /product="acid phosphatase"
                     /EC_number="3.1.3.2"
                     /GO_function="GO:0003993 - acid phosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=48541
     Region          <122..324
                     /region_name="PAP2_acid_phosphatase"
                     /note="PAP2, bacterial acid phosphatase or class A
                     non-specific acid phosphatases. These enzymes catalyze
                     phosphomonoester hydrolysis, with optimal activity in low
                     pH conditions. They are secreted into the periplasmic
                     space, and their physiological role remains...; cd03397"
                     /db_xref="CDD:239491"
     Site            order(211,218,247..249,282,288,292)
                     /site_type="active"
                     /db_xref="CDD:239491"
ORIGIN      
        1 mklraarqsr ralllltaia tasatavpsi gtaaptntah lalpfeipql qlpapklsse
       61 hgegtehspl ssigaspqqh agapvpqpfd vsyltgyisd vssyqygiyy evvrefkdlr
      121 snhpevmqkn ldivadynnn aqqervdkai rdaladkdgv lftaaealgd efgrhflaal
      181 qekrlpktef llgngyaara gglaswgrae kllfnndrpf vqaperikry esperalydg
      241 ssksfpsght nqatwittll ammlpevgvq llargseage srlvmgvhfp ldviggrmtg
      301 qaaaadrwnd pkmrdallqa raeivaemew ragkpfaeli agdthalsdq qavtdyterm
      361 tygfepifat depvnvpaaa palletrfpe lsyeqraevl rttalpsgyp lddrdptkgd
      421 wqrinvaraw naqvstgadg evvvk
//
LOCUS       WP_284594014             346 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Enterococcus faecium].
ACCESSION   WP_284594014
VERSION     WP_284594014.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..346
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=39498
     Region          <62..>137
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          118..344
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mkkklfsqlw iyfasivfis ilvtllcflg fifllsrhsi spaesagkpt lyplfvfagf
       61 smvvgtgisi fvgrrilhpi salgtnmslv atgdfsirmd eqqkvaevqq lykdfnvmvq
      121 elnsietlrn dfvssvshef ktplatiqgy vqllqapnls deerqiflyr viesitqlsq
      181 ltenilklnk lenqriqlek keyrldeqir evivflqpkw ekeqleldie laavnytgne
      241 eflyqvwlni mdnaikynqv ngkihiklfe tateivlevt dsgvgmneet rdrmfekfyq
      301 gdtsrqifgn glglslvkki lelhdgridy ssiegvgtta iirlsk
//
LOCUS       WP_284594030             295 aa            linear   BCT 25-DEC-2024
DEFINITION  indole-3-glycerol phosphate synthase TrpC [Corynebacterium
            propinquum].
ACCESSION   WP_284594030
VERSION     WP_284594030.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..295
                     /product="indole-3-glycerol phosphate synthase TrpC"
                     /EC_number="4.1.1.48"
                     /GO_function="GO:0004425 - indole-3-glycerol-phosphate
                     synthase activity [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30999
     Region          9..274
                     /region_name="TrpC"
                     /note="Indole-3-glycerol phosphate synthase [Amino acid
                     transport and metabolism]; COG0134"
                     /db_xref="CDD:439904"
ORIGIN      
        1 mvttaltakd ivagiladva arearlpfpd ikalsravpt prpvvpllsq pgcsviaeik
       61 rakpaarydd tfrtyatgag htdslidfga vdtladvasl aqdfesagva viacqterlr
      121 frgsledmat arvassapml crdiivdpyq ihearffgad mvplqvelle qarlealvdr
      181 ieslgmtvla evrspeqacr avsagvsvvg inarglesrt ltpdrfaaiv phlpesviri
      241 glggvlgare mwryagwgad avlvgealms apnpaatara lvaagrhpac pavrg
//
LOCUS       WP_284594090             603 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD/NAD(P)-binding protein [Enterococcus faecium].
ACCESSION   WP_284594090
VERSION     WP_284594090.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11816065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..603
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=69269
     Region          1..600
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
     Region          4..178
                     /region_name="NAD_binding_9"
                     /note="FAD-NAD(P)-binding; pfam13454"
                     /db_xref="CDD:433222"
ORIGIN      
        1 mkigiigagp rglsvaeril hnnqdrhsle lflfdpngpg grvwrlnqpp ellmnsvsqq
       61 vtlftdetls sgglvtqgpn lfqwskgpat dyieqtvtkn kqliieeinr lekdqqstrc
      121 lyglyqrwff sklqeespas iqfvyslvkk vskrkdgyll qtdqqsysid qlvlasghwe
      181 ndeteeervw vdyakknvll yqlpsnpadv dlskippken vflrglglsf fdyvglftvs
      241 rggrfenekg klvyhpsgke pivysgsrrg lpyyprgrnq kqggamawpr lltkenleqw
      301 hqsgfltget ffdylkkdve lfyykkiiee yhlpipkknf ehdflslsse eclgkhsali
      361 pyrwdwsyle tplayqnepf seasrifieg qikeaekgnc tgafastfda lkdwrdpirq
      421 aiewhvfsak eykeilwgwf thlnsfltig ppiirtkela alidagifhl ieppfdiqqk
      481 hnryvislqd keissrylie arlpqtsfsr ssnpviknlk enklvrpfsf sdntgsyhse
      541 aidvergtnr vidasgeiqs dfycygipve gvdwltaava rpytdpwnlr qadkiaqlil
      601 tdk
//
LOCUS       WP_284594182             372 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium propinquum].
ACCESSION   WP_284594182
VERSION     WP_284594182.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 372)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..372
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=38806
     Region          27..368
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 msadntpath gtphsgtvhp efthgyrrlv irnqwvslhf ptrvlvtalg llllaligav
       61 aaitlgeypl slgevfsalf srgggfdsti vrewrlpiav aavafgallg iggaifqslt
      121 rnplgspdvi gfdagaytav vitmlvvgts nfwaiagasi vggiitalvv yllawrkgvq
      181 gfrliivgig vsamltsins ylitradvee giqvgfwaag sitkvtwqgl vptmllgiiv
      241 viaaagysra lrhlelgdda attqgfavnr arlglivigv attalvtaaa gpisfialva
      301 pqiarrimrt agvsllgaaa mgailltgah ilslviatfy rqipvglitv vigglymlwl
      361 llrestrryg ts
//
LOCUS       WP_284594420             301 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Serratia nevei].
ACCESSION   WP_284594420
VERSION     WP_284594420.1
KEYWORDS    RefSeq.
SOURCE      Serratia nevei
  ORGANISM  Serratia nevei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Serratia nevei"
                     /db_xref="taxon:2703794"
     Protein         1..301
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34401
     Region          1..181
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mdfsivipiy nsarylpktl krvfnacqgf dyqvilvddc sdeddikyir qiaatnsnvm
       61 lhekkkksna avsrnlgikl aqseivffld sddyfttnyi irrmnkhedr hidiifgnya
      121 evsgdsvrdf nfhyksgssg edflflemgd irsstisirk ksdrrflfpe flnkhqdwgf
      181 lvnainlgah vahdagggvf ldvgrygrmt aklnleasdr fintflspsd rhisgfackh
      241 llaslysena qafnyyssri vrrslsgkfk mikwygdcla rlglfsvggr llrnvrqgfr
      301 r
//
LOCUS       WP_284594528             246 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284594528
VERSION     WP_284594528.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..246
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25855
     Region          17..243
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(29..30,32..33,36..37,74,78..79,82..83,107,111,118,
                     121..122,127,142,146..147,149..151,153..154,157..158,
                     161..162,181..182,184..186,188..190,192..193,195..196,200,
                     203..204,210,212)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(145,149,152..153,155..156,195,198..199,201..206,
                     209..211,215,217)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mkqstastaq vpvgksvhfl hpltviiigv sawvaalsis wpllhaaiia lgwlagiags
       61 rslavpatsi alsipaglsm llvhaphgeh qiaplltsdg lvtagelalr fcalmtalla
      121 amanvhipdl lkalqhlglh hsvvyvlgas lqllpqasal isevatanrl arrkvtlttv
      181 iphmiipvit rlltrgadrg ialqgmgyda pgrrtvlypv rahrweillr ltfpaaaigl
      241 vvlawi
//
LOCUS       WP_284594604             531 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284594604
VERSION     WP_284594604.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..531
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=57041
     Region          35..469
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mtlrqdrpaq asttmpagav detsarnkrg vrkpnalval lrrlhfyagm figpflliaa
       61 isgalyavap taeklvyqdv ltvtpppgae gvtntislek qvnnaheafp dldiaqvwps
      121 sepgettrvl lidetideae lrsvfvnpyt gavvgdepsy sglgelplrr wishlhesmh
      181 lgpvgelyse laaswlwffa lgglvlwasr nkkvqqlfgf gnartgkevk nggvkdakdi
      241 kkkgsgrrrl vnlhgvtgtw mligmlalsv tgitwsthag gnvnrtveal qwradpitte
      301 lsgesaeaad phaehaghgg gggggaevea earawtpeei aeqadqvlat areegltgsl
      361 rmypgesveh gwqaserwte wrttsdaisv dgetgevidr lpfselplfs kltswgiylh
      421 mgimfglplq illlvtalai aglvvlgymi wwkrrptpga tagipgprtk lstkqwiiva
      481 vflvavggfl plfgislaam lladvllskr aghtghtghe trraavdgar a
//
LOCUS       WP_284594630             344 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284594630
VERSION     WP_284594630.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..344
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=37796
     Region          1..325
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mrlllianpn stsqtnelfr riiplvrsid dshlitkfth yaghaedmtr glsrddydvv
       61 iaiggdgtvn evvngllgkv gdgrrkasev palaviptgs anvfvralgy pldpvhttel
      121 lvghikknlr rrirlgtwnd rwfavnagig idadvlhsid klreqgfsat plrylrisyq
      181 awrrilhapp kisahaesad gqtqhidqap lvfasntnpw tflgplpvvt nprnsfdkgl
      241 gtfgltdltg vggfvgllhl fgadekgrln kftdartlrf ddatritlec dealrfqadg
      301 eaqgklktve lssipdaiev fspeeiipvq qrgilavvrd lfri
//
LOCUS       WP_284594652             216 aa            linear   BCT 25-DEC-2024
DEFINITION  YczE/YyaS/YitT family protein [Enterococcus faecalis].
ACCESSION   WP_284594652
VERSION     WP_284594652.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..216
                     /product="YczE/YyaS/YitT family protein"
                     /calculated_mol_wt=24282
     Region          2..211
                     /region_name="YczE"
                     /note="Uncharacterized membrane protein YczE [Function
                     unknown]; COG2364"
                     /db_xref="CDD:441931"
ORIGIN      
        1 mwkkkivlsf lfylisalgi sltiqagigv ssfnafnvtf atlthlkvgt vttainfafl
       61 gtcwlldqqr kiqdyliilv aligfgfvin fflyqlfgsl vfqnylvkiv lfilgtiiag
      121 igtgqvvalg vlqfpiekfc tlisertryg fqfyrylvdi lcvslalgls igyhspifvr
      181 egtvislfll swviswsrkr gqqrilriqi kklese
//
LOCUS       WP_284594673             347 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Enterococcus faecalis].
ACCESSION   WP_284594673
VERSION     WP_284594673.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..347
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39535
     Region          9..335
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 myektkwkiq kmmkkgvfsg asfrfiegek eesncwglaq vkptkeqlts amlfdvaslt
       61 kvvgtttvil qlveegkiil dqslqtyyps fqdpnitirh llthtadlqg yipnrdqlna
      121 qelkdaynhs fhagkaigkk vvytdagtil lgfmleemfq qsmieilser vllplgmnes
      181 tflpknplnc vptelheqrg lirgathdpk afvlrehagn aglfsnvydl tkfvrmylnr
      241 gsyhnlqflk ketidlllvn qvpaadkprs lgwdfkydva tqrpllfhtg ytgtfllidv
      301 qqqsafifls nrvhpedhrn tyieerdqll atylkekssv sdemtsf
//
LOCUS       WP_284594858             181 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Corynebacterium propinquum].
ACCESSION   WP_284594858
VERSION     WP_284594858.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..181
                     /product="YceD family protein"
                     /calculated_mol_wt=19308
     Region          <38..181
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mtspfvfdvk alltqqqspe qtthtgpapr rigaemlaie egaevtidav lhslgagima
       61 dadvsavlrg ecsrclsple rpmtvrisqv fsadddfitg daeddedegs gdeipqvshe
      121 dtidllqtlt delvvalpfn pvceggcpdd sltpapdgvs geedaqerid prwaglekfr
      181 d
//
LOCUS       WP_284594919             697 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Serratia nevei].
ACCESSION   WP_284594919
VERSION     WP_284594919.1
KEYWORDS    RefSeq.
SOURCE      Serratia nevei
  ORGANISM  Serratia nevei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 697)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 697)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 697)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Serratia nevei"
                     /db_xref="taxon:2703794"
     Protein         1..697
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=78070
     Region          14..692
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mtllpkqsnn knpidlygei vddlpglicf gnrlggyfnk qwrdytgaia gehgaadwld
       61 alhpddrerl aaqwrqaiva lssfagearl rdrsgayrwf mlafnarqdg malepswylt
      121 atdihpqmlq rqqnvqalsi qqdmldasvd cikvinhdgt lrhmnrsgsl algldpgqke
      181 fgmpwlglls peirrrgrka lrsvragkna rftglsvtpq gkkqhwdnil tpvsdehgtv
      241 aeilcvsrdv tsqrvmeqrl llaseydelt dlpnrrlfkk klkqemkral hgnkslglml
      301 ldldhfklvn dtlghaagdh llrvlgkrls acmnthsfvs rlggdefavv isdveneqdi
      361 friankfllq letpithggk tlhcgmsigg aiypkdarda selmkcadta lyelkdggrg
      421 gvymfdrkmm dkararasql nyarqivrdn cirpsyqpkv sltdgsivgf eallrwhcpi
      481 ngvqlpatvs eafndyelat kiseamqlkv fadiarwraa gvavqpisln vspieflrdn
      541 yaetflqrll kfhiphhlie levtehafnk hgskyvlral qmlkemgiri alddfgtghs
      601 sfshimdypl dcikldcdfv qrmntepail aivesigilg qklsidiiae gveteqqrqt
      661 lceagfhigq gflfsravep qrvpellqaa pqpvdgr
//
LOCUS       WP_284594961             388 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Serratia nevei].
ACCESSION   WP_284594961
VERSION     WP_284594961.1
KEYWORDS    RefSeq.
SOURCE      Serratia nevei
  ORGANISM  Serratia nevei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 388)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 388)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 388)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Serratia nevei"
                     /db_xref="taxon:2703794"
     Protein         1..388
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40443
     Region          19..387
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mraffllcvs raglclgtmm fagalptirs ewqldaasag tvqtvfsltn alallvasww
       61 cdslgarrvy llfswlgaaa lmlfavfahs yagalvlmaf vgltqggayt palllamgmn
      121 gparrgyaig mmlaasslgy flsvfiagws amrwgagvaf slcaagallg alagslalvg
      181 yrepqlrtlg rqtkresyai tyatllllig yiahswellg nwawapslvs ealsgfsldp
      241 lsaglivaav ihlagmvatl ivgtvsdyfn rasvlmfmga agalgsllmg wsanwgpgwt
      301 llavsigsff ilgdsgvlsa amadnvppqq lgsvmgwrsl lgfgigsfsp lsfgvvmdtt
      361 qswctsyavl acgggiacla acllwrqh
//
LOCUS       WP_284595015             273 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium propinquum].
ACCESSION   WP_284595015
VERSION     WP_284595015.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..273
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28558
     Region          14..272
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mtldfsepft ertprvsraa klhraaarkk eqrfliegen avdaavstga atdvfvtesa
       61 aerfahivtt agfmdvyihp itdgaaklls ettttpgifa vclpvmfsag kiiksspsll
      121 tvpvetsepg nagtlirvsd algadgvvfa gntvdphsnk varasagslf htpvaretgi
      181 ndvlgqlraa nlqilataad geitleeaee sgmlekptaw llgneahgls ddvaaradhr
      241 vsipirgnae slnlataaai clyesakaqk rar
//
LOCUS       WP_284595056             579 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Serratia nevei].
ACCESSION   WP_284595056
VERSION     WP_284595056.1
KEYWORDS    RefSeq.
SOURCE      Serratia nevei
  ORGANISM  Serratia nevei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 579)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 579)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 579)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Serratia nevei"
                     /db_xref="taxon:2703794"
     Protein         1..579
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64322
     Region          1..579
                     /region_name="COG4986"
                     /note="ABC-type anion transport system, duplicated
                     permease component [Inorganic ion transport and
                     metabolism]"
                     /db_xref="CDD:444010"
ORIGIN      
        1 mnvrlnthvs arrllpngwd viafpliigl iammaiglhq tlqpivtlkt qaisldpanl
       61 peyalrttlr mlvamvaala fslvygtlaa ksrraekvlv pildilqsvp vlgyisftvt
      121 ffialfpgrv lgvelaamfa iftsqawnmt fsfyqslrtv prdlqevarg fhlspwqrfw
      181 kldapfampg liwnmmmsms ggwffivase aitvgnntft lpgigaylaq ailsqdllai
      241 gwvlltmtvv ilaydqllfr plvawadkfr mettrsasap tswllnlmrr trlihllltp
      301 lgallaktar lklslparpl rrgnsaqrqr rsrtidrcws aivilltlai awrvilyvqt
      361 gvtlndvghv mvlglitllr vavlialssl iwvplgvlig lrptlagkiq piaqflaafp
      421 anllfpvfvi tivhfrlnpd iwlsplivlg tqwyilfnvv agatalpndy reaaanfhir
      481 gwqwwrqvml pgifpyyitg aitasggawn asivaefvqw gstqvkahgl gayiaettaa
      541 gdfpkiilgi avmslfvtlf nrllwrplya yaesrfrid
//
LOCUS       WP_284595131             375 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium propinquum].
ACCESSION   WP_284595131
VERSION     WP_284595131.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 375)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..375
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39169
     Region          62..369
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtqnsnkttt apsaartats arhrlekars pqrsdvfaqr hrlrvgtfva livlligsvl
       61 lstalgqyyl slpdllrilv srssadtdia asvvwdirlp riflgflvga algvagclmq
      121 avfanplaep sivgvtsgag vgaalvivfe vnflgtftvp aaafltsliv taviyrlahn
      181 rgkvavvnli ltgiavnavc galisfmvyl apttsreqii fwqmgslngs qwkhvwvvlp
      241 ivivgfaias rlgaqldvla lgekaaghtg invavlrlva ivasavltaa avsfagligf
      301 vglivphvlr tivgpenkil lpasalagal lialadlaar tmipfadlpi giftalvggp
      361 tffillrrmm rkgsv
//
LOCUS       WP_284595378             276 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium
            propinquum].
ACCESSION   WP_284595378
VERSION     WP_284595378.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..276
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29920
     Region          13..276
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtnqepltsf dkiadwpvdn vaaalirdge lahtlgddeh vfavasvtkp vaaygfamav
       61 eegvfewdtp vgpegstvrh llahasgigk daenpdrape erriyssagf evlqeklehe
      121 tgmdfaeylk lglfeplgmn ktvlkgssgy alettaadla rfaqevlept lldpstvqam
      181 lapqfadlrg ivpgygmqkp clwglgfeih gakdphwmga elpdnavghf gmngsflwlv
      241 pdekiallal tdkdfgewak plwaeandai wkeitg
//
LOCUS       WP_284595397             253 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Corynebacterium propinquum].
ACCESSION   WP_284595397
VERSION     WP_284595397.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..253
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28458
     Region          <29..105
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mryqdgknle sfndhtndnk esednpeqga igqeqmewak qdiaqaseng anwvvldyhk
       61 pvysasyhal qdedvqvtre dfvqladelg vdvvmqghdh nltrtkslvy spdnfaygav
      121 edtkkklidg vehhvnpvgv tyvipntsgt kaydaiykkg aehvakvrpk ldwmgeevta
      181 ywnslfdiae qpddstdfae lhsnnrqsqh ehfavytvtd ntfkidfysv egdihgnger
      241 tvtlrdssgi skd
//
LOCUS       WP_284595495             337 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284595495
VERSION     WP_284595495.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..337
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35578
     Region          24..323
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkkslatali agvavlfgai algpqriala dqatgnkrla aelaelavpg hnqltaltid
       61 dgvteyagwg adseteveig svtkmmtael lrheiknkev eldttlgeli delhepvasv
      121 tleeavnhtg glprmagvnf asnlgfsvlg tnpyegvgrd difaaandie elenrgeeqy
      181 snlgfallgw alaenagtty egmlndvlfr plgmhdtyva sqplpddqpa gllnngrhaq
      241 pwvtegyapa gmvrstaadm akfaeylleq glpdygwapt vstddkdsga gwhngqtggy
      301 samlvvapet araafvagnt prgveqiglq ltgeevr
//
LOCUS       WP_284595510             767 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284595510
VERSION     WP_284595510.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 767)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 767)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 767)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..767
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..767
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=84893
     Region          23..765
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 msprrttgqq stgsqrtkrv hhsnysaela aeqsyvdalf gildsdvsqa rqrladaqlt
       61 idpanadsda llrreteyhr lqekldqlnl aqiglvfgri dvdakgenpt segldrryig
      121 riglmdrddd yrsllidwra pmarpfylat tahpegvrvr rhirtadrvv kdiddellsg
      181 tapgdadrad vageaallha mnsargehme sivetiqreq daiirdstrg vlvveggpgt
      241 gktavalhrv ayllytwreq lsrtgvliig pnptflnyis qvlpelgetg vvlstigrly
      301 pglrptlhdt aetrrvkgsl qmvdvlkaav kayqhvpkhs revvlegtrv eltptmvkta
      361 rtkarrsrkp hneareifse qlqellaqgl aeiighdpld ggnllnsadi salhedisde
      421 aivdelvdef wpqlgprqvl rellsdreal haacrgnggk efasalwrse qgwsdsdaal
      481 ldelaqllgs gddeqqaaad eqewrealee aegaldilat sestdnddvf dseilsahhv
      541 idaetlarrq qardyrttae raegdrtwaf ghvvvdeaqe lsamewrmvf rrspnrwmtv
      601 vgdpaqtgsp agcdswseal epfvgkryrq hqltinyrtp veiaelaesi vhkyspdttv
      661 aqairnrkga vrwlpsgtsp eevrdqlrad etaasaeddt adqnqrsyai isahnaatyk
      721 glefdhvivv epeeiiaass rgwqdlyvac tratqtlsii gtldlag
//
LOCUS       WP_284595512             264 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Serratia nevei].
ACCESSION   WP_284595512
VERSION     WP_284595512.1
KEYWORDS    RefSeq.
SOURCE      Serratia nevei
  ORGANISM  Serratia nevei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14398449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Serratia nevei"
                     /db_xref="taxon:2703794"
     Protein         1..264
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29221
     Region          14..108
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          169..250
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mllfhdvlpv dqpvrplard yrhgdsepdh yhncaqlihs lsgvvqvttr lgswvvppgr
       61 gvwvpakmvh slritgqvaa rtlfvdplvr adlpaqcqvv qvspllreli icameiapgy
      121 psggrdervm elildelrml pilplhlpep reasllalcr hiqatlaqpw tleqasahls
      181 vsgrtlsrrf qretglhfsd wvrrarllaa lnalatgrsv levaldlgyd spsafsamfr
      241 rllgvapsdy fsrtapttds arqr
//
LOCUS       WP_284595677             129 aa            linear   BCT 25-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284595677
VERSION     WP_284595677.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..129
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13525
     Region          17..129
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 mnldisltea llstasvaag afagglvrgl lsklrgrytg tacsnmlacf algimlarvd
       61 lgalvhlpyw eiafgtgfcg alstlatlar elgnltyera wirlilytvf tvlgglgaiw
      121 lgwllgmvv
//
LOCUS       WP_284595651             446 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284595651
VERSION     WP_284595651.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..446
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46595
     Region          17..427
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 msrtggsaph prevvtrral vvwvagvacy ivaitgrtsf gvagveaiar fdvdasriav
       61 faavqlgvya laqiptglgi drfgpramvm fgavvmglgq fllalttsyp laivarvlig
      121 agdasaflav mrllpywfpl rktplftqlt gaigqtgqfi savpflallg stgwtgafvt
      181 lgatsillag laglaikdlp dvdrraadap esgtaasgrd slrtrmrtll rtpvawqgff
      241 mhysclmfql vflmmwgfpl mtlgmglsaq qagavlaint vvtvfsgplh gifsarigaa
      301 rhwavvgfsl tivltwvvff asatprglaa ivvvnvival cassanygfd nvregvsrev
      361 vatatglanm ggflagmaas qgigvvldis saggeytwgd fqvaalaagv vwavgvigll
      421 vasawrkypg pahrilphrl ralrsh
//
LOCUS       WP_284595708             555 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284595708
VERSION     WP_284595708.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..555
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=60557
     Region          145..540
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
     Region          <434..>461
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
ORIGIN      
        1 msesepqkap eptagwgapg erkrrsyray rthrplrlrt wlvvltvlvs afglfassfa
       61 vysvmrevfy qrvdddltqs magwaqnsel fsgnlsaspp tdyavihifp dgssrvyndr
      121 dtlpqinnlv igggprsvas vdgpqqpewr alanqqngvv tivaknlere ngllrglaml
      181 qalislvmlg flallafavi rqtlkplqiv ertasdiaeg dldlrvpkwp lntevgqlaa
      241 alnimlerlq dsvetaqske eqmrrfvgda shelrtplts lrgyvelyrs gatndvdhvf
      301 atiddesgrm kllvedllal traegsrldk rtvdvlelsl avvgtaraay pertirvenk
      361 ttdipvvsgd pdrlhqvlln litnglnhgg peasvtltlr kesqddcmrv aaeqqetgdn
      421 heaeektsgw sqddakngka gkdgkagkdg nkgtdgesak dyvciditdd grgmskevtg
      481 liferfyred psrargaggg sglglaivks lvdqhdgeit vdsepgvgst ftvripalde
      541 plaseetfdd ygeny
//
LOCUS       WP_284595724             239 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284595724
VERSION     WP_284595724.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..239
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25410
     Region          76..221
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mskkvtnpnq kssagfigai aavlaivvav iayiviagqg akaekfanwe ikqvsaetsf
       61 dgntltfgaa dkaphvdlye dfscphcahl aeatdaeale einagnlavs ihpmtfldnq
      121 gdghstqava allalaehdd vnalwnlrea mfenqqdiar swgpddfada aaqmeasdea
      181 vedirsgkfl ekareagean gkdleskvgr vstprvlmdg kdlevedind wvkvavask
//
LOCUS       WP_284595782             517 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284595782
VERSION     WP_284595782.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..517
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55026
     Region          15..513
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mssgfarssf ahngkarvav igagpnglta aavlaqagcr vevfesadhi ggsarthpaf
       61 gagsavdfga aahpfgvvsp vfrqlgleny glewkhpqyp mahplvdapa vilhrdlktt
      121 aaqfsdhdrr vwnhlhkplv ddvgklvnsv lpvrprypla larlglrglw parsltsrll
      181 vdeparallv gsavhairpp sqpgtaafgl lfnslgmttg wpvvsggtgq lvralarvie
      241 hyggiiktga aildlsgfvt ydavvttqtp rqllalqgld lsrlrsrslr rwkygtavyk
      301 vdylvngpvr wndprvagag tvhvggtvse mqlaesqaaa gmlperpfvm vcqqqtadpt
      361 rfsgnrrslg agrvlsaqld agrmpedarq philwayahv phgyqekfpg evaglieaqi
      421 sryasgfsaq iierhqaspg qlqeananli ggdiaggamn laqmvrrrqy vgtltmnpev
      481 pvvqasgasl pgagvhgmag wraaqtilrr fgsiefs
//
LOCUS       WP_284595924            1001 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Serratia nevei].
ACCESSION   WP_284595924
VERSION     WP_284595924.1
KEYWORDS    RefSeq.
SOURCE      Serratia nevei
  ORGANISM  Serratia nevei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Serratia nevei"
                     /db_xref="taxon:2703794"
     Protein         1..1001
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=101134
     Region          19..>990
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 maslvyqkea aalllavlgq naspsvfdtv gnqiekgqtt aqayisslls ssagqalyas
       61 ktdveilqsi ytsvygsspt taqlqailag stlndaissa vnsllnysgf dtgtltsqsn
      121 fdaqlnnvlf pgtsaagsgp gvsdalalyy lagidpvtst vitlgtqint saqtfsqvan
      181 kfvtdraaln slsntdfink vfneayerap sssefsalna ilsgggtkgd vliniinglr
      241 gtvgsgdtaa qqfflnetqp dsagqlagla areqvasiyl avplrnvdaq glddwsnylg
      301 khgntftslt tklltsvefq kkgaqltgtd fiqhvytgvh gvaatpaqia lysgltdkaa
      361 ittaiindlr nstatdnttv aqqhafeydi gsslvyktaa sltttaaggn atgtvntnss
      421 hvlsnaetav ltnvqlnana aatvnlafad hlanltingt aasvvslstd gvnpgvavtv
      481 nngnvilnas sgsdnvvvts taniatgtaq fnlgagndsl hwagnavsgg antvantvka
      541 dggtgtdsis anfitktvvt nqnalgirts tvtsnannfs nfekidltgy igksvgtlit
      601 tpligspttt svttpthtfd fgltngtstv egttggtvtq naaatnlgaq gfvisglanv
      661 nvinaaggna aqlevkgdat sastlnftfv qnatdhfnin fdavssanvn agaislnsss
      721 sallgtaltt vnvasggtgt fnnilslagt naqvqtvnvt gdhalnltlg sgfsnvrdin
      781 astntaglnl dsshggtgdg iivqllnilp lsvittnlla pvltalglng yqmtvegssa
      841 adtlgvignt tltggagant ynikasntqs gvtikdfnsl kdsivdvnhg gltisdnasg
      901 tavanygtrs adtldallgt lvggltngvi gllggilgld snnsltakvg vasvvfsggg
      961 ntassyviid nndnhtldln dtvvyltgqn hqqlvdtlhy a
//
LOCUS       WP_284595886             475 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Serratia nevei].
ACCESSION   WP_284595886
VERSION     WP_284595886.1
KEYWORDS    RefSeq.
SOURCE      Serratia nevei
  ORGANISM  Serratia nevei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Serratia nevei"
                     /db_xref="taxon:2703794"
     Protein         1..475
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50710
     Region          2..461
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mnnrnvasrp kievrsidyv prherhgkvw hqapfwftgn fvlttmvvgf tgpalglgal
       61 ysmlaiaagv gfgtffmach anqgprmglp qmiqsraqfg lrgaivpfaa vvfvyigfnv
      121 fnvilatdai ntvlpghrlp wyalliavav llaivghdml havqrwltyv mmavfgvlti
      181 gaalslrmda avgaghfswa afliqlsaaa gyqisyavyv sdysrylpqe tpsakvifwt
      241 ylgaagsalw lmslgaflas alpapdaigs vqavgnavyp gfgtlavlia vpslvgimav
      301 ncygamltsl saidafrkvt ptlglrmtgi gvvaltvfav alaipasyla sfntfvllml
      361 yflvpwtavn lmdfyvvrgg hyaigeifnp agiygrwgrp gltayaigll amvpfmtlgf
      421 ytgpfavllg gadiaflvgl lvagsvyvvm crkldleaer rvalccegll egere
//
LOCUS       WP_284595884             460 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284595884
VERSION     WP_284595884.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..460
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48813
     Region          4..460
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mtenmkvdvl vigfgkagkt iamkraasgd rvalveqsst myggtcinig cvptkalltd
       61 aerhhakptt ddstafseai qrrgtltskm nqvnldlaeg kgvivvdgha sfisektvev
      121 tggeermeit getviintga epvvlplpga dlervidstq aqrleerpds llivgggpig
      181 mefatyfakf gtkvtvvdtv dkpfanfdrd iaehvgtimd nlgitwitga qvtefresga
      241 davttvwkdg dgneqtadta qvlvavgrkp atkdlgldka gieltergav avdkhlrtnv
      301 egvyaagdvn ggpqftyvsf ddhrvilsdr wgdgsrttdn rvvptttfid pplatvglge
      361 daareevear gntldvkaad ikdipimprp kilgkpegra kilveretdr ivgatllcvd
      421 aqelintlvl amsaeipast vgggiythps ssevfnallg
//
LOCUS       WP_284596063             333 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284596063
VERSION     WP_284596063.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..333
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37249
     Region          16..326
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mntdspeklv alvqslnlvp yfkahpersi feaakdlgls pdelvraler lhcsgistqt
       61 qdlidlsyel tkgvvihddq gmdsslrltp teagallltv evletmpglv drsavasaae
      121 klrsimddrs raiydgiaeh ssatedvqyr iaqalhtkrr vqfdywsass nststrtvdp
      181 arifirgdva yltafveqyg ehrnfrvdrm rnveilaepa rprtrklqfs sedpfgfrds
      241 ttatlavspd alwmldeydm krqdetppcp vaddqkawvk atmpigstsw ftrfalshad
      301 rvrvlgpkdl vdavheraqv giqrysmvdt nks
//
LOCUS       WP_284595999             313 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284595999
VERSION     WP_284595999.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..313
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=34025
     Region          137..295
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 msssrnafqr kpallwtlia lvvalavliv vavvrsggde ststggqdam hgpqvpsstq
       61 sgnsdsqstp mpggeyspeq arelakqvep gtdfsrpnsp dptvigpgae itsnddilnv
      121 hrrnaedpfa mgaldapvvl sefsdfecpf ctrfavetap klkekfvdtg llriewndlp
      181 vngphaetga qagraagnqd kfyefhdvly nntydnqtgg hpgydvadyv rfakeagied
      241 lekfrteien ekyrdvvrqa lhyassigmr gtpafilgdr fisgaqpyev fedevyrqla
      301 kvadgtvphp ksk
//
LOCUS       WP_284596184             517 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284596184
VERSION     WP_284596184.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..517
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55048
     Region          15..513
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mssgfarssf ahngkarvav igagpnglta aavlaqagcr vevfesadhi ggsarthpaf
       61 gagsavdfga aahpfgvvsp vfrqldleny glewkhpqyp mahplvdapa vilhrdlktt
      121 aaqfsdhdrr vwnhlhkplv ddvgklvnsv lpvrprypla larlglrglw parsltsrll
      181 vdeaarallv gsavhairpp sqpgtaafgl lfnslgmttg wpvvsggsgq lvralarvie
      241 hyggtiktga kvqdlsgfvt ydavvatqtp rqllalqgld lsrlrsrslr rwkygtavyk
      301 vdylvngpvr wndprvagag tvhvggtvse mqlaesqaaa gmlperpfvm vcqqqtadpt
      361 rfsgswrslg vgrvlsaqid agrmpedarq philwayahv phgyqekfpg evaglieaqi
      421 sryaagfsaq iierhqaspg qlqeananli ggdiaggamn laqmlrqrqy vgtltvnpev
      481 pvvqasgasl pgagvhgmag wraaqtilrr fgaielr
//
LOCUS       WP_284596187             340 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284596187
VERSION     WP_284596187.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..340
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34460
     Region          28..336
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mqapalfarr tlgmlailaa ivvmicfsia lganplpwge vwngllardn seaaiivwtl
       61 rtprtvvaia tgaafgvaga liqaltrnpl adpgilgvna gagfavtlgv gffgltsisg
      121 yiwfaflgaa ittvvvyfig sgaslgasgk anpatlvlag valaavlsgi tqfltlidpd
      181 tfqairnwsl gsvaradlsd talvapflaa glvlalaiss slnsialgdd laaslgtkvv
      241 rtrvlgiiav tllaggatal tgglafvglm vphvvrwivg pdqrwiiiys alaapvlvla
      301 sdvigriiar pgeievgiit avvgapvlim lvrrrkasgl
//
LOCUS       WP_284596193             584 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284596193
VERSION     WP_284596193.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..584
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=63150
     Region          59..391
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(60..61,64..65,98,101,155..156,211)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(153,156,236..242,271,296..300,331,355..359,362)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mtatvpsriq pqvefrsgtq qserrqqsdh sqrshqnasq strhnfgysh sagnriavlw
       61 fpdwpvqaal leetrrgisp espaialasn hritaccdka raqgvrrgmk lraaqalcps
      121 mvvrdadpqr dgrlfssive elddvsasle vlrpgmvvln ltaatrfygs eqaalerfid
      181 aaahegidat agaadelpta iiaarhrvlg avvqpgdsva flyqqplsvl laepalgcqk
      241 dtvetlaglg istlgeltel pttaistrfg saglhchria saqqqrkvap gaveldlsas
      301 itpeapitrv deaafiarml adqvhqqlat qglncvriki aaetddgtmi skiwrtttal
      361 tehataervr wqldgwlssg gagaivelsl tpletqiptn tgsiieadta vaeettatvv
      421 srlqsmlgfd avqqphavgg rgvaervrfl pygqaaenir epgrrsaewi gaipsplptr
      481 lgggldhpas rvrlvdkhgn pvfvtaeall sadpvgmswg kkkfqvlgws vpwpvdtgww
      541 eseisdesqr larmqlvgkn agdqhpkawl lvwqhrawri eamy
//
LOCUS       WP_284596354             202 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284596354
VERSION     WP_284596354.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..202
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22420
     Region          4..134
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 madnpaihqy rvplrwsdfd ryghvmnany veiaqearla ykqayfdpag medfaafvrk
       61 ldldfrkpie pegnsvllve sqvvevgnss fvtrqeikdk hgriacvvet vsvavdmdtq
      121 mprplteeer evmrlestla kaadkaeaes gsgpsargvq adslgdeisy ddeisygdev
      181 dygdevgygd evdygdeigy dd
//
LOCUS       WP_284596364             533 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284596364
VERSION     WP_284596364.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 533)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..533
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=55412
     Region          10..247
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mspsqnslkl nytaasdrgl vrtnnedsaf agrnllvlad gmgghaagev asqllvttmq
       61 rldrdpgend mlallgtaad dantaiadtv rqrpetqgmg ttctalmfng ttfgmchvgd
      121 srgyrlrggk leqitiddty vqslvdsgsl kpedvsthpq kslilkaytg rpvdptlrmi
      181 daqpgdrlll csdglsdpvt adtieqtlke gtpeqaaskl idlalrsggp dnvtvvvadv
      241 lagddestti paapvsagal alpeaerahp ntaagraaal nrrpqvvepk aqaagahnhg
      301 tganagngsg pgnvagagtg assgawaggs agaaensahd naskrgrnwt laivvlvllg
      361 gligsgwwvy assqdkyyia tndsdeliie rgvdyslfgk dlhepyqrvc ltkddevrtt
      421 dlgekpsndc hpfsltdlpg svrgsithld sgsysevtdq lqrlsdkalp vcvnraetdn
      481 ngknsegknn ddnsgnsgan kdtdkdtnkd aanaesaddg glstpgvncr evs
//
LOCUS       WP_284596455             350 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284596455
VERSION     WP_284596455.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..350
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=39347
     Region          8..78
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          181..284
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 msdlfvpeql iaarermelt raaladklgf ssrtltriek gesspshaqi qelaqalhvh
       61 tnyffddaae kinqetisfr rasrtsakkl kaaqqhgvii ekffhaiedk felpsldipn
      121 lhsfqpeaaa gqireacdig enpieniiei aeslgvrvaa lpnatkevda fcfirdsray
      181 ivinvsksae rvrfdvahel ghlalhqdes fktqdskdke qqadqfaaef lmparrvrmq
      241 nlhnasltqv idakdywgvs amamayrlkt lelisdwqhr dliirlakag yrnsepngrl
      301 ydsssllrqt ihsstrllri nsisenlslp iseiypylnk lvpvpvvkga
//
LOCUS       WP_284596466             428 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284596466
VERSION     WP_284596466.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..428
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46929
     Region          157..263
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mtdrkrgakr srkhgteqnt gqstesftes vsnsltrlkn slrrhlsqqw teltspsfsv
       61 pasklpepla hhatevsast ipesvvaeia eslnlrgkhd hhhaatdqes enapepedgp
      121 qtaeksdynf dssrhlplga rfkprgvfed dwsarpsadk pwpvilihgt vdtkgvwqel
      181 gtelradgwc vfapdygkrg taameesavq lgayieavrt itgaeqvili ghsqggllar
      241 ywmrtsgqar yvkhlvslga pnhgttmggi lsplvtnnlt enimhsliqh wfgpvgfqqi
      301 tgseifavfn ngaddrdgdg nsddssgtnt hgsgeledgv dytciasrqd tvvqppetcf
      361 lngpadqvrn vwvqdiipra nvqhqdlpmn khvraiirtg lkkganeenl khktqntepk
      421 trrlehgv
//
LOCUS       WP_284596484             399 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284596484
VERSION     WP_284596484.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..399
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43346
     Region          37..156
                     /region_name="Creatinase_N"
                     /note="Creatinase/Prolidase N-terminal domain; pfam01321"
                     /db_xref="CDD:460159"
     Region          39..398
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 msshnnstaa dsaagaaans aahstyipvt adhfrarlak aeeivaeqnl agflvspgpe
       61 fqyltgstfs sheratflvl ragkdpvavc petdvltlqq enldelgfrf eawrdgqspy
      121 eitrklleen sehktvavan amtadhvlrl daalpnhsie lgsdamsqll lakgeeeisq
      181 laaaaaaidr vheqvpallr dgvterevad klhdlilqeh hsidfiivgc genganphhs
      241 fsdrvlhtge pvvvdlggaf gdgyrsdstr tyvvdgavdk apqefrdaye ivtrafhaar
      301 eaakpgatae sidraareii teagygenfs hrlghgigls thedpfyleg nkqqvqegft
      361 fsiepgiyve gkwgmrledi vvleadgprh lnqqprelr
//
LOCUS       WP_284596765             435 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium tuberculostearicum].
ACCESSION   WP_284596765
VERSION     WP_284596765.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46179
     Region          17..383
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 msqpnprevi ttqalsiwva amavylvait grtsfgvagl daierfdvda griavftsvq
       61 lgvyalaqip tgilidkfgp rlllvvgavi mgigqvvlgf ttsygvaiaa rvligagdat
      121 aflsvmrilp ywfplhrtpm ftqvtsslgq mgqfisavpf lwllgaagwt aafvtlgavg
      181 ilvaiaaiva vadspeklgi iptekeppns qatsiparlk tvfrspvawq ayfihyigml
      241 plivfvmlwg mpmmtqgmem skaksslvlt llavflvfvg plhgkissra qhvrpwlslg
      301 fvavhvlawl lffafgterg laailvvsfi talctptany gfdivrermd rsvvatatgl
      361 gnmggftsgm lgaqlfgmvl dhssdapdys mpdftaaaaa vlavwvvgmi gviithflrr
      421 ragedgpsvt ivevs
//
LOCUS       WP_284596825             342 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Corynebacterium tuberculostearicum].
ACCESSION   WP_284596825
VERSION     WP_284596825.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..342
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=37130
     Region          16..305
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mlcvnywtki krffkeaapt lqqqrliali lllcqggitv sgsivrvtgs glgcptwpec
       61 qpgslvpmeg aapalhqaie fgnrlltfvv taaavaavia mrmarrrael kvyawlnvag
      121 ivlqaiiggi svhldlrwws valhflssml lvwlaamlys rivepddgtp rvrfpqairl
      181 laavatvals ivlitgtmvt gsgvhsgdsg vgmegrlqvd teamavtham cmyvyltltv
      241 itvfllyknr apqdakkagw vlvvciliqw avgvyqfyms iprwtvpfhi glssfvtayt
      301 allwahgvrr tdgtadlitg spsgdekyaa rqaslerera na
//
LOCUS       WP_284596978             149 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Corynebacterium
            tuberculostearicum].
ACCESSION   WP_284596978
VERSION     WP_284596978.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..149
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16237
     Region          46..>107
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mdslrgrrtv stlgvrggfd aaqakardka kakarrsdti ghlgpeavva fvdgemepkf
       61 mhrvrihlvh caecradvhq qrhasewvrh cadsakvkap qsllaklagi ateevapgpd
      121 aatpvhrpqq dfldkvemvv raikhnqrg
//
LOCUS       WP_284596985             256 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium tuberculostearicum].
ACCESSION   WP_284596985
VERSION     WP_284596985.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..256
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27888
     Region          1..244
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(17..18,20..21,24..25,62,67..68,71..72,102,106,113,
                     116..117,122,138,142..143,145..147,149..150,153..154,
                     157..158,178..179,181..183,185..187,189..190,192..193,197,
                     200..201,211,213)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(141,145,148..149,151..152,192,195..196,198..203,206,
                     211..212,216,218)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(162..169,180,183..184,187)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mpnllrganp lsriflmfiw vtplltsidw vsaaaslalt ltfaplcgvs wvrlfksgwf
       61 lfliapisgi smllygepgg keyfswwlvq vtensltlai aitlrvfava lpmvvlardi
      121 dptelgdals qilklpsrfv igavagvrmm tlfqsdwqsl gmarrarglt dvgklkhllt
      181 msfgllvial rrgdklatam eargfgrtpp gggartwarp srlhtrdgwi malgtvlafv
      241 pvvvsvltga wrffgl
//
LOCUS       WP_284597003             294 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Corynebacterium
            tuberculostearicum].
ACCESSION   WP_284597003
VERSION     WP_284597003.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..294
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30602
     Region          5..282
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(34,231,234)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(181,202,229,232..233,236)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mtihvcgegl vdlvpvapgs lndhtpalgg gpfnvaiaaa rlgadvefqs rlstdgfgqe
       61 lvgrleaegv ttthlqrgde pttlavttih edgsasynfy iegtadrlve pqlvpadiac
      121 fgtvslalep gasryaqllk dfaaqgtlva ldpnirplya taehreflae llpyvtllkl
      181 sdeeveflgd dlisqvpivv vtrggkglsv ragettltvp aahvtvsdti gagdtimaal
      241 ltqiderglg aaalaaldpa qwkdilsfav aaagitvsrk ganpprreev easl
//
LOCUS       WP_284597337             270 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Corynebacterium
            tuberculostearicum].
ACCESSION   WP_284597337
VERSION     WP_284597337.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..270
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31167
     Region          3..237
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mptvwavsdl hgavktnser idqltppdpa dwlivagdva ertdliiril rqlndryarv
       61 iwvpgnhelf srsqdryqgr ekyahlverc reigvitped pypvfhgtti vplftlydys
      121 frphgltvge aidaarakql mmtdefaiap fvdvrawcwd rlaysikrls rvhgptvlvn
      181 hwplvqeptm llrfpeialw cgtrhtrswp rrynaqsviy ghlhmpsrmn vdgvdhiets
      241 lgyprewqgr esaqawpypv lrsfveegtr
//
LOCUS       WP_284597371             847 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium tuberculostearicum].
ACCESSION   WP_284597371
VERSION     WP_284597371.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 847)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..847
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=94783
     Region          19..841
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mnlsqllpdl tevpeslvde aiwdtftswt tgrginlypa qelaslgila gdnvilatpt
       61 gsgksmvana ahfialargq rsfytapika lvsekffalc difgaenvgm mtgdatvngs
      121 apiiaataei vanialrdga eanidqvvmd efhyysepdr gwawqvplle lskaqfllms
      181 atlgdtqwle ddltrrtgra tnlvagttrp vpldfsyvfs avhetieell adkkapiyvv
      241 hfsqreaaer aqaltslsgi itkeekeaia qeiggfrftt afgkdlskll rkgigihhag
      301 mlpkyrrlve rlaqkgllkv icgtdtlgvg invpirtvlm tglakfdgqr qrilksrefh
      361 qiagragrag ydtegtvvve apeheienak errrigddpk rlkklkkksa regevswsek
      421 tfarlteaep eqltsqfrvs nsmllnvlar hgngydhmrh llrdnhdnrs kqnkdiltal
      481 dlfrglvdsg vvqkstkgld iygrpyhlvr elprdfalnq plgpfalaal slldpeaety
      541 nldvisvfea ilddprqvli aqqkqrrgee iaalkadgvd ytdrmnived itwpkpleel
      601 leqaydtfae tnawvrefel rpksvvrdml enamtfsdlv atyglarseg vilryltdaw
      661 rtlkqsipde yntpelediv iwlgelirqv dsslvdewaq magedspidq dtvdrelafg
      721 vedptaltan rraftimvrn ymfrlvqlfa lekedrlael ldyldevpdf gailddyfde
      781 yddidsgpea rgpeyfrlgd tdsrawpvrq iikdpdgdha yqfvatvdld asdeagevrl
      841 sdlrvey
//
LOCUS       WP_284597508             700 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Corynebacterium tuberculostearicum].
ACCESSION   WP_284597508
VERSION     WP_284597508.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..700
                     /product="PhoX family protein"
                     /calculated_mol_wt=76762
     Region          46..692
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 malkgrnlls slfsssrssl tctykcgnac fgecenksnn pyfadqfsrr talragslsv
       61 vtvgggaala acsnpddast easssegkgg ktseanvelt saegmkfdpv qpnekdevvi
      121 pdgyeqsvli awgdplfeda pefddknqta eaaekqfgfn ndfagliehp dddnrliyvc
      181 sheyttepqm fpnydadnpt eeqakigwag hghsivevsk vgktgelkre fgplnrrita
      241 tteftlvgpa agsdyvktsa dktgkkvkgt lnncsggitp wntmlsgeen fdqyfahakl
      301 ddkkaqesle rfgmedgesq rkwerfdkrf dvskepnepn rfgwlveinp ldpkstpvkh
      361 talgrfkhea gnihiasdgt vvcysgddsr feyiykfist kqykegdieh nltildhgtl
      421 yvakvegnsp edeidgsgvl pedgafdgkg ewiklltsdt ennkfeshvd gmsaeevavy
      481 treaadkvga tkmdrpedmq vhpdsekvyv altnnkyrga tgenakknke epmewapvke
      541 nknglvmeie ddhagekftw nlflvcgdpk eantyfggfd kekvspiscp dnlafdshgn
      601 lwistdgnal esndglyavt tegdtrgelk cfltvpagae tcgpivtder vmvnvqhpge
      661 tddatfekqt shwpeggkst prpavvvvwk kdgnigvdkk
//
LOCUS       WP_284597582             454 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Corynebacterium
            tuberculostearicum].
ACCESSION   WP_284597582
VERSION     WP_284597582.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..454
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=48434
     Region          5..242
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mtlklnffak sdrglirdnn edsgyagphl liladgmggh aagevaselm vnhleildqd
       61 pgqedttall eaaaeqanea isdhvkahpe tegmgttlst mlfngtdfgv chvgdsrgyl
      121 lrdgkleqit kddtyvqslv dkgeldpgdv sshpqkslil kaytgrpvea tlftldakpg
      181 drillcsdgl sdpvtastie talgqgsieq agsalvdlai rsggpdnvtv vigevteekp
      241 kehepfrvga lagpteepth pdssasraaq lsrkpqvipp avmadgkdeh pepnddeaee
      301 etsgrkigwk vllallivla lvigaglwak nflsnnyyva tneaqeitiq qgadysvfgk
      361 elhsthqnvc indsnsllfs sqpcegdftp lkvtdlpese rsavdhlstg dlgevqqqin
      421 dlgdkalkpc itapsqkdkk dakknkpgvt crev
//
LOCUS       WP_284597687             664 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            tuberculostearicum].
ACCESSION   WP_284597687
VERSION     WP_284597687.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..664
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=72164
     Region          1..66
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mtatltladv arltgvtrpa vnewiqrfns esnvpfpspy gehdghpyya iteiqdwlra
       61 tklgrrdtav edalfyssly rmllrnpara algllncnta lspqdfspsa avidsltaay
      121 qraadnipsd apeadiakaa eqvaeaafgp aaalarladd lsaqrqvtls srftsramqa
      181 vsealtlenp tppiiptdey slgfvtgltr eleetlvlsi gyrkdcapds lywaelacrn
      241 vefidaseei pansllvhav psppktapey fehlqdlldn ldergamfci stadmlieds
      301 laqvvrrrfl aptetgaiap lrysarlprg ifpdrgqqqg alwilkrpnr eaignpadaa
      361 vviadvpdlk rpglvsdwat mlttpdeark hafvrgrilr aadawrsrth slddsvfsst
      421 stssaadlmh tahqagldis sagledaqpk igmraesgat rleylpwkaa tnartgvlqk
      481 lsgsriaehd lapeavakle ligepeilgs tpqgarcidr lrlediaprg tltepgdvvf
      541 iknprprali deeggklvta paqalrcrtf rgrshtpleq vclpylveka ineavssela
      601 svyfpvlprk naedlstveq qlgarrrqlv eqlrsidvlr hnltisigtg avtiaesraq
      661 sppg
//
LOCUS       WP_284597757             638 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Serratia nevei].
ACCESSION   WP_284597757
VERSION     WP_284597757.1
KEYWORDS    RefSeq.
SOURCE      Serratia nevei
  ORGANISM  Serratia nevei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Serratia nevei"
                     /db_xref="taxon:2703794"
     Protein         1..638
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=72311
     Region          17..637
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mvrfpyprla ylfdalqtet lpqdelakrf avstrtvrad italneildk ygarfvhsrg
       61 agyrlqvdna alfsalqhqe rrkhatprsa qervhyllvr fltsafslkl edladewfvs
      121 rgtlqndmae vrerlahyql tietkprygm klfgaemair acltdllfql qladaenpll
      181 nneillqpqv aafagllhpl lsqyairltd egeqylifyc avalrrindg yplpdfeved
      241 gddavrqvst rlaaelrsas gkeismaeea ylrvniaarr vqdvqptein addeealvdy
      301 ilsyinahyn ynlqgdeqlr adllthiktm itrvkyqini pnpllanikq hypmaydvtl
      361 aavsswgkyt pytlseneig ylvlhigvgl erhynigyer hpqvmlvcdt gnstvrmiqa
      421 qiarkypqlv mtrivslrdy emlahidedf visnarigek nkpvvvmspf ptdyqleqlg
      481 klvlvdrtrp ymlekffdae hfmvlneplt qaelfsrvcg qleqegyiga dfypslvere
      541 aivstllgeg ialphslgll akktvvvtll apqgvawgeg evahviflla isksdyeeam
      601 aiyelfvtfv rersmsrllg sdsfdsfkav aldclsrs
//
LOCUS       WP_284597759             233 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium tuberculostearicum].
ACCESSION   WP_284597759
VERSION     WP_284597759.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..233
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25793
     Region          47..201
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 msqllpertp ewlkpalgvd psqvqelign rqasslngtn vqvpvkreaa vlmllsgesa
       61 eeasillthr spsmrshsgq iafpggrrdp adtslvdtal reaweetdlq rnsvtpleqw
      121 eqlhiratgn pvspilahwt qpgevypasp detddvflvp irelvdprnr fmvgfrkwqg
      181 pafhangyvi wgftagvlsa llqhagwsip wdnnsvmdlr dsltnsrnne kms
//
LOCUS       WP_284597911             243 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Corynebacterium
            tuberculostearicum].
ACCESSION   WP_284597911
VERSION     WP_284597911.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..243
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26999
     Region          9..147
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mtspshanqa ywdsdaanyh aehpdylssf ywcpemlhed qahllgdvsa ssvleigcgs
       61 apctqwlqtr ahfatgfdis rgmlnhagpg lpltqadals layatgsfda afsafgafpf
      121 lanldlalse vsrvlkpggr fvlsanhpmr wifpddptdl tadisyfdra yleqdrdgnl
      181 tyaefhrtia dwfqalqgeg pfliediiep ewprdltttw gqwspergei fpgtiifvcr
      241 ncr
//
LOCUS       WP_284597924             316 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Serratia nevei].
ACCESSION   WP_284597924
VERSION     WP_284597924.1
KEYWORDS    RefSeq.
SOURCE      Serratia nevei
  ORGANISM  Serratia nevei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 316)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 316)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Serratia nevei"
                     /db_xref="taxon:2703794"
     Protein         1..316
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=36263
     Region          <178..>308
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mklkrliiqy llvflvltgg fvwmyeqyfs tshnmnsagp qenyawaiak ftirlagfna
       61 kverqlrlgn sdkeelqtel dllfsssnvl llksvstryl yeeagyaktv ekinanleni
      121 dtelnkptpd ysiilkniel igqenkdlvv isdhaevrqr niiqqdyidk ansmkfpiat
      181 lyflfllmlf isyrqvksin nqlesekksf nnknaflgvl ghelrtslqa iissveviiq
      241 kkdstafdhf erlenaamkm erqmkdlaef akvdngnvei kkssfnlrkv vhdtveqsis
      301 ilnkqnvreg ankfli
//
LOCUS       WP_284598038             119 aa            linear   BCT 25-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Corynebacterium
            tuberculostearicum].
ACCESSION   WP_284598038
VERSION     WP_284598038.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..119
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13015
     Region          2..115
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 mnllcvligg figgslrygf trliparyct fvanilgsla lglaygfaql adapllhpfl
       61 alglagglst wstlakelge mikrkqwwrl ckylfwtigl givlawrgti waariyhgi
//
LOCUS       WP_284598336             129 aa            linear   BCT 25-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284598336
VERSION     WP_284598336.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..129
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13495
     Region          17..129
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 mnhdisltea llstasvaag afagglvrgl lsklrgrytg tacsnmlacf algimlarvd
       61 lgalvhlpyw eiafgtgfcg alstlatlar elgnltyera wirlslytvf tvlgglgavw
      121 lgwllgmai
//
LOCUS       WP_284598359             323 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284598359
VERSION     WP_284598359.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..323
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34285
     Region          2..319
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(40..41,45,118,122,125,143,146..148,167..168,172,187,
                     210..211,232..236,257..260,307,309)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(130,225..226,239..244,252..259,262..263)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mkaiqitrtg gpevlqiaev espipsddqv lvdvlvagvn yidtyyregi ysattpfipg
       61 fegvgrvlhd pigkiasgtm vawntafgsy aeqvcvardk lvavpndfdl staasmllqg
      121 itahylthgv yeladgdscv itggaggvgl latqfaaaag anvytvvssd ekeelsyqag
      181 athvlrygpe lanqvrelta gkgvdvvydg vgkdtfeqsl dmvrnrgtvc lfgaasgpvd
      241 pidpqilnek gsifltrpsv agwtsregef qmraqavvqa vvdgdlkfrv sdsypleeaa
      301 hahrdlqdrk ttgsivlrvq eai
//
LOCUS       WP_284598363             232 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284598363
VERSION     WP_284598363.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..232
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=25308
     Region          1..223
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mlfdslprps eriapgvahl pgwlgvdkqa klvhevreia rtyadtpmam lrptlksggq
       61 msvyqlhlgr ywhypsyryv dkiagttvpp vpeslvalap valraaaeva eelapwvetf
      121 vpemvlvnyy ppgsgmgmhv defeesrapv islsigdeal frmghtesrt qpwddvtlcs
      181 gdlvvfggpk rfayhgvvcv ndvtlpdgcg laegriniti rqvsaapklq gr
//
LOCUS       WP_284598384             380 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide)
            pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
            [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284598384
VERSION     WP_284598384.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Davies,G.J., Gloster,T.M. and Henrissat,B.
  TITLE     Recent structural insights into the expanding world of
            carbohydrate-active enzymes
  JOURNAL   Curr Opin Struct Biol 15 (6), 637-645 (2005)
   PUBMED   16263268
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   4  (residues 1 to 380)
  AUTHORS   van Heijenoort,J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit
  JOURNAL   Nat Prod Rep 18 (5), 503-519 (2001)
   PUBMED   11699883
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Ha,S., Gross,B. and Walker,S.
  TITLE     E. Coli MurG: a paradigm for a superfamily of glycosyltransferases
  JOURNAL   Curr Drug Targets Infect Disord 1 (2), 201-213 (2001)
   PUBMED   12455415
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..380
                     /product="UDP-N-acetylglucosamine--N-acetylmuramyl-
                     (pentapeptide) pyrophosphoryl-undecaprenol
                     N-acetylglucosamine transferase"
                     /EC_number="2.4.1.227"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0050511 -
                     undecaprenyldiphospho-muramoylpentapeptide
                     beta-N-acetylglucosaminyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051991 -
                     UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-
                     glutamyl-meso-2,
                     6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol
                     4-beta-N-acetylglucosaminlytransferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0030259 - lipid glycosylation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=39207
     Region          8..357
                     /region_name="MurG"
                     /note="UDP-N-acetylglucosamine:LPS N-acetylglucosamine
                     transferase [Cell wall/membrane/envelope biogenesis];
                     COG0707"
                     /db_xref="CDD:440471"
ORIGIN      
        1 masttdsalt ivlagggtag hiepalavge vlrnrygaqv lalgtsrgle sdiipargfd
       61 lelitpvpvp rrinadlfal pfkvvrsirq arkilkknra davfgtggyv sasaylaaks
      121 lgipfyvlet nalagmankm gvrlggtgfn aiagsgmpgd ivgvpvrpql aggdpsgekt
      181 arareifglv edrptilvtg gsqgaasina avagsvgrlv dagyqilhay gkknqppheh
      241 phyvslpyie dmaaalavad lvvcrsgamt vaevsasglp avyvplphgn geqglnceav
      301 vaegaarkid dakfspdtmy nevssilgds gtyqrmrtaa aasqqgdaaw rlaeriifdn
      361 svnpspftsa egtsheasst
//
LOCUS       WP_284598395             446 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284598395
VERSION     WP_284598395.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..446
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46551
     Region          17..427
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 msrtggsaph prevvtrral vvwvagvacy ivaitgrtsf gvagveaiar fdvdasriav
       61 faavqlgvya laqiptglgi drfgpramvm fgavvmglgq fllalttsyp laivarvlig
      121 agdasaflav mrllpywfpl rktplftqlt gaigqtgqfi savpflallg sagwtgafvt
      181 lgatsillag laglaikdlp dvdrraadap esgtaasgrd slrtrmrtll rtpvawqgff
      241 mhysclmfql vflmmwgfpl mtlgmglsaq qagavlaint vvtvfsgplh gifsarigaa
      301 rhwavvgfsv tivltwvvff asatprglaa ivvvnvival cassanygfd nvregvsrev
      361 vatatglanm ggflagmaas qgigvvldis saggeytwgd fqvaalaagv vwavgvigll
      421 vasawrkypg pahrilphrl ralrsh
//
LOCUS       WP_284598697             376 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284598697
VERSION     WP_284598697.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..376
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39256
     Region          63..370
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtqnsnkttt apsaartatt prhrrenpra pqqhrdvfaq rhrlrvgtfv alivllvgsa
       61 llstalgqyy lslpdllsil tsgpraetdi aasvvwdirl priflgflvg aalgvagclm
      121 qavfanplae psivgvtsga gvgaalvivf evsflgtftv paaafltsli vtaiiyrlah
      181 nrgkvavvnl iltgiavnav cgalisfmvy lapttsreqi ifwqmgslng sqwkhvwvvl
      241 pivivgfaia srlgaqldvl algekaaght ginvaalrmv aivasavlta aavsfaglig
      301 fvglivphvl rtivgpenki llpasalaga llialadvaa rtlipfadlp igiftalvgg
      361 ptffillrrm mrkgsv
//
LOCUS       WP_284598714             416 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284598714
VERSION     WP_284598714.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..416
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45404
     Region          1..411
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mkdivvigag aigmasafrl akeghnvtiv dpvapgskas shnagwvvpt msepvpapgv
       61 ltkamkwlwk kdsplyisps adwrfytfll rmlqhtsekr yaagtetliq lsketfstfd
      121 efvdegvdvg lefttmrtlf kdtsgmdarl delahfaenf pglsyrrmdd aelrdfhpkl
      181 sedvqggies rgdahldptk ftaalhkacq eagvefvasr awlrdrgsgk arvivdgafm
      241 dpdhvvvaag awtgevvkql gqrislqagk gygfdfpvgq gwltdtlymt dakvvatpmg
      301 dhvrvagtmg fseidesldh vraggilkgv qsffpdwpvn efdlepwqgm rpmtpdglph
      361 igalrkfpnv vvatghamqg islaprtaql vsgviagetm pdwmtkihpe rftrlg
//
LOCUS       WP_284598718             348 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284598718
VERSION     WP_284598718.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..348
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35857
     Region          35..340
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mdrqrtqqvl rarnrnrvll fivlvfalvs gtiaslvigq ytipigelpr ilavgplgvs
       61 amdesviwqi rlprlvlgfl vgaalgvgga lmqavfanpl aepsvigvta gagvgaalai
      121 vlgiswfgat tvpvfaflsg llttwmvyql arfagrirvi nlvlvgiavn avagalisff
      181 ifiaptssre qvvfwqmgsl sgakwahisv vavligagia valllvgkld vlalgdraag
      241 hvgidvarlr vlalllatll tagavsyagl igfvglvvph iirtvagpsn vvllpasalg
      301 gaalivladt aarsiidfad lpigiftalv ggptffillr ammrrgav
//
LOCUS       WP_284598731             155 aa            linear   BCT 25-DEC-2024
DEFINITION  Dps family protein [Enterococcus faecium].
ACCESSION   WP_284598731
VERSION     WP_284598731.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Choi,S.H., Baumler,D.J. and Kaspar,C.W.
  TITLE     Contribution of dps to acid stress tolerance and oxidative stress
            tolerance in Escherichia coli O157:H7
  JOURNAL   Appl Environ Microbiol 66 (9), 3911-3916 (2000)
   PUBMED   10966408
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 155)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 155)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   6  (residues 1 to 155)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..155
                     /product="Dps family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17738
     Region          8..147
                     /region_name="DPS"
                     /note="DPS protein, ferritin-like diiron-binding domain;
                     cd01043"
                     /db_xref="CDD:153102"
     Site            order(21..22,26,28..29,40,51,55,58..59)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:153102"
     Site            order(28,40,44,55,59)
                     /site_type="other"
                     /note="DPS ferroxidase diiron center [ion binding]"
                     /db_xref="CDD:153102"
     Site            order(123,130..131)
                     /site_type="active"
                     /note="ion pore [active]"
                     /db_xref="CDD:153102"
ORIGIN      
        1 mkfqqtkevl nqlvadlsqm svvvhqthwy mrgpgfltlh pmmdefmddl naqldevser
       61 litldgspys tlrefadntk ipdevgrwdr tiperletlv agyryladly qkgievsgee
      121 gddstqdifi efktatekri wmiqahlgka peida
//
LOCUS       WP_284598964             460 aa            linear   BCT 25-DEC-2024
DEFINITION  acid phosphatase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284598964
VERSION     WP_284598964.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130290
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..460
                     /product="acid phosphatase"
                     /EC_number="3.1.3.2"
                     /GO_function="GO:0003993 - acid phosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=50128
     Region          <137..339
                     /region_name="PAP2_acid_phosphatase"
                     /note="PAP2, bacterial acid phosphatase or class A
                     non-specific acid phosphatases. These enzymes catalyze
                     phosphomonoester hydrolysis, with optimal activity in low
                     pH conditions. They are secreted into the periplasmic
                     space, and their physiological role remains...; cd03397"
                     /db_xref="CDD:239491"
     Site            order(226,233,262..264,297,303,307)
                     /site_type="active"
                     /db_xref="CDD:239491"
ORIGIN      
        1 mfltsrrrat slltaagala vvagapslve qhggtahsma aeaslqapln antthlalpf
       61 eipqlqlpap klssehgagp eysplssiga npqhhagapv pqpfdvsylt gyvsdvssyr
      121 ygiyyevvre fkdlrsnhpe vmqknldiva eynnnaqqer vdkairdala dkdgvlftaa
      181 ealgdefgrh flaalhekrl pktefllgng yaaraggias wgraekllfn ndrpfvqape
      241 riqrhesper klydgssksf psghtnqatw ittllammlp evgtqllarg seagesrlvm
      301 gvhfpldvig grmtgqaaaa drwndpkmrd allqaraeiv aemewragkp faemiaedsh
      361 alsdqqaead ytrrmnygfa pifatdepvn vptaapalle trfpelsyeq raevlrhtal
      421 psgyplddrd pakgdwqrin larawnaqvs igaggevvvk
//
LOCUS       WP_284598970              68 aa            linear   BCT 25-DEC-2024
DEFINITION  prealbumin-like fold domain-containing protein, partial
            [Enterococcus faecium].
ACCESSION   WP_284598970
VERSION     WP_284598970.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16050634
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         <1..>68
                     /product="prealbumin-like fold domain-containing protein"
     Region          19..>68
                     /region_name="SpaA"
                     /note="Prealbumin-like fold domain; pfam17802"
                     /db_xref="CDD:465513"
ORIGIN      
        1 tkenrltpgg vvltkiddqs geilqgavfe lqnregetlq tglttgedgk laidglapga
       61 yqlvetqa
//
LOCUS       WP_284599011             418 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Winkia neuii].
ACCESSION   WP_284599011
VERSION     WP_284599011.1
KEYWORDS    RefSeq.
SOURCE      Winkia neuii
  ORGANISM  Winkia neuii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Winkia.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Winkia neuii"
                     /db_xref="taxon:33007"
     Protein         1..418
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=47482
     Region          50..418
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 makrsriata kkvtkytagg iltaqavaaa glvavdewrk rrspsgplsf palapkdlav
       61 sdnqlttymd arelyddmiy aisnaksyvf fesfiwkgdn tgqrfkdali aaarrgvdvf
      121 iiydgfgnlv vpprfkrfpk lehlhvlqfp ilkfgifkrg lramgrdhrk ivvadgkigf
      181 vggynigeiy idqwrdthlr iegpgvweld nafvdfwneh ckgsqkhlfd rgarswdnki
      241 taalntprkl lfpvrgsyin aieraskrvw itsayfipds qiqdallaae hrgvdvrilv
      301 peksnhliad waarsfyael lesgaqlwly qdvmihaktm tvdgrwstig tanidqlsmt
      361 gnyeinlqit dreqaaylek vfledltnar emsllewesr gafvrmterl vrplryil
//
LOCUS       WP_284599007             313 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Winkia neuii].
ACCESSION   WP_284599007
VERSION     WP_284599007.1
KEYWORDS    RefSeq.
SOURCE      Winkia neuii
  ORGANISM  Winkia neuii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Winkia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Winkia neuii"
                     /db_xref="taxon:33007"
     Protein         1..313
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34730
     Region          14..297
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mtdpiqipav heepvlsvlr amqlrplgtd sfeadslpqt anriyggqvl aqallaasat
       61 iedspsdprl pnsfhayfmr vgdntipvsi dvdrlrdghs fstrrvdviq rekviltmts
      121 sfqkvqpdls tqiqmpdvpe pedvpnslem frdqgnpvsk ylgktaafem rhvagslyfs
      181 erteplakga twirprgakl pswtpqsvhr allayvsdqf mlepvirsng ltwrtpgmav
      241 asldhamwfy rsvdindwhl fvqespttwg srglgitkvf nstgrlvava aqegmirsnv
      301 ptgdwvlpep plh
//
LOCUS       WP_284599079             381 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284599079
VERSION     WP_284599079.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 381)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..381
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39966
     Region          70..376
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mmmnetqrtv trgisapksp akppavdkve vtnkavlels rqhrkltwqr igivsglcav
       61 aiaafvtsnf vgaidispge vitgivnpss ldeqthtvlw rlrlpmavma lligvslsla
      121 gaemqtilnn plaepftlgi saaaafggas aivlrwqivt qpqlnlalva wlssvvatgi
      181 iviaavlrgv raetmvllgi glvfffqaml aliqyrssae alqqivfwam gsltraswtg
      241 navlagvlvi alpvlwalsw qltalrlgda raaamgvnts alrvivlvvv slvaattvaf
      301 agiigfiglv gphiarmlvg edqryfvpas maagaavmct ahalslivkp glaipigivt
      361 sllgvpffia ivmakrralw s
//
LOCUS       WP_284599158             578 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Winkia neuii].
ACCESSION   WP_284599158
VERSION     WP_284599158.1
KEYWORDS    RefSeq.
SOURCE      Winkia neuii
  ORGANISM  Winkia neuii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Winkia.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Winkia neuii"
                     /db_xref="taxon:33007"
     Protein         1..578
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=64807
     Region          6..>309
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mvatdtvvgk rykiltkigs ggmsevylai dsslnkqwav kqiknmsdat rrdmvvrslt
       61 veanmikqfd hpaiprivdl ieesgslfvv mdyvegrtla qilkddgple edqvadisiq
      121 lcdvldylhr rkppvvyrdi kpsnimvtpd gtvklidfgi akevgspess eallgdsrel
      181 gtpgfgspeq fkdaksvdtr sdiyslgati fylltgrhpk ndglvplrqv dpdltlgfer
      241 ivgkatqkdp qlryqngaem ayalahykea ddeyqrglag rwwkflgtli aagvclalal
      301 icwglgywan srdfnalmqt gdqisekdea lqyylkaadv kpadpdpyys lmdrftadnr
      361 fdgdeertyn saltehsksl qkdqqswsql afdtgklywy yyadqsllgd eanglnmnde
      421 qlvryarirn askwmhyaad dkmfknnria svyadiadfn sqivplineg sdaghykpyf
      481 gslqrlvdia seennlvvkl evanfvldal qvyprnfrad kvamndmtsl ekkvetmark
      541 vtpttdhlek qkkkatkafg ptkaaienaf vdvkgeak
//
LOCUS       WP_284599166             234 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II [Winkia neuii].
ACCESSION   WP_284599166
VERSION     WP_284599166.1
KEYWORDS    RefSeq.
SOURCE      Winkia neuii
  ORGANISM  Winkia neuii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Winkia.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Winkia neuii"
                     /db_xref="taxon:33007"
     Protein         1..234
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25043
     Region          12..232
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 menqqggkgl kilcvdnyds fvwtivgylr algatvevvr ndrvaanapa qvdidkiggr
       61 fytdqngqap qatraasvkd aiapydgilv spgpgtpsea gaspavlrdc kevgkpmlgv
      121 clgeqglaei cgakvvrapq lmhgktsmis hnragifegi esplqitryh slavdpatip
      181 televtattd dgivmgiqhr qvplwgvqfh pesvtthagh qmfanwlrqv rdhr
//
LOCUS       WP_284599258             460 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284599258
VERSION     WP_284599258.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..460
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48614
     Region          4..460
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mtenmkvdvl vigfgkagkt iamkraasgd rvalveqssa myggtcinig cvptkalltd
       61 aerhrakptt ddaaafaeai qrrgtltskm nqanldlaeg kgvivvdgha sfisektvev
      121 tggddrmeit getviintga epvvlplpga dlervidstq aqrlderpds llivgggpig
      181 mefatyfakf gtkvtvvdtv dkpfanfdrd iaehvgtimd nlgitwitga qvtefresga
      241 davttvwkdg dgneqtadta qvlvavgrkp atkdlgldka gieltergav avdkhlrtnv
      301 egvyaagdvn ggpqftyvsf ddhrvilsdr wgdgsrttdn rvvptttfid pplatvglge
      361 daareevear gntldvkaad ikdipimprp kilgnpegra kilveretdr ivgatllcvd
      421 aqelintlgl amsaeipast vgggiythps ssevfnallg
//
LOCUS       WP_284599393             378 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284599393
VERSION     WP_284599393.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..378
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40741
     Region          7..371
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mvatsvpasv pqridclegi ralaavgvli thvhfqtasg pvvlerfdyf vavffalsaf
       61 llwrrpigpg flrkraarvl paylvcvavv alalpaastm swqqllanlt atqiyipdgl
      121 apglthlwsl cvefafyftl pliawvllhw qartrvlalc vvgimslgwa flpfvagfdg
      181 sdgaswaasv nrqiwppayt lwfvvgmlaa eaesagvakr pgvvrrilgi kplfwvlata
      241 clflasweai sprglthpsp lefairislg tvfaacivvp yalrptqsgl llsqpvqavg
      301 rwsyslflwh vavlsiafpl agiemfsggf iiilvltlgl svavaainyt lveeparlwl
      361 rqatapaakh atsklspa
//
LOCUS       WP_284599397             464 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284599397
VERSION     WP_284599397.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..464
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=48724
     Region          1..463
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrltvfglgy lgathaacma eaghevlgvd iaparvaqlq agrvpfyepg laelvargvd
       61 sgrlrfscdy qqaaefaqlh fiavgtpera dtpaadtsav eavvdqlapl lrgkhvlvgk
      121 stvpvgtaar lqeraanisr atvdilwnpe flreghavad tlrpdrivvg tgaestpnga
      181 gtpngvssap alqklrevyr aplergtpfl vmpwasaelv ksaanaflat kisfinaiae
      241 vceavggdva avaealgyde righqylgag lgfgggclpk dvrafrarad ecgagdalaf
      301 lgqvelinar rrqrvvqlas elvaqpskva epagsarpgl sgaiitvlga afkpnsddvr
      361 dspalhvaae lalrgarvrv cdpqavenar rvypgleypa sladgvagad lvilatewre
      421 yreldpvwaa elvaepvlid arnaldlarw rgagwqvhal grgd
//
LOCUS       WP_284599417             351 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Curtobacterium
            citreum].
ACCESSION   WP_284599417
VERSION     WP_284599417.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 351)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..351
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38162
     Region          13..342
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mpanraprvp aeerlfslvl allstesglt kaeilanvqg yrqrftpggd naslerqfer
       61 dkddvrelgi pletietpga agnnqtlryr ipkgeydlpl dvrftpdesa llslaamawr
      121 egalsadsrr allkvrsagt ddsaaddtga ddvedprgma ayaprlrtrd aafeplrsal
      181 draaavrfdy itpgeheprq rdvaplalvq hggrwmlcah efstggtkny llsrivgpvt
      241 thhpgqhpap agageralae ldriwaerta riavqpgsda errlqrrrgt evdgggvlvv
      301 hhvdpqilae elaafgpevr vlepaalrer vaarlrglva dhtdpeetar g
//
LOCUS       WP_284599526             211 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Curtobacterium citreum].
ACCESSION   WP_284599526
VERSION     WP_284599526.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..211
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22925
     Region          8..203
                     /region_name="HAD_sEH-N_like"
                     /note="N-terminal lipase phosphatase domain of human
                     soluble epoxide hydrolase, Escherichia coli YihX/HAD4
                     alpha-D-glucose 1-phosphate phosphatase, and related
                     domains, may be inactive; cd02603"
                     /db_xref="CDD:319790"
     Site            order(13..17,114..115,146,170..171,174..175)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            141
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mslflpgrvv vfdygevisr tphgawdalv qatsvpvdel lpvyqelrhd ldrgdlsvle
       61 ywraigartg rtwsvtevhg fwaidftgwf aiepetlaiv eelhdagtrl allsnagfdf
      121 gdpyrrspmg slfetvvvsa eehvlkpdps vyrttcdrlg itpeqmvfvd nraenaagad
      181 aigavghhyt spaglraflq dlaasaegap a
//
LOCUS       WP_284599560             249 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Curtobacterium
            citreum].
ACCESSION   WP_284599560
VERSION     WP_284599560.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..249
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27578
     Region          4..230
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mpgrrwrrge lntafritas vvipvfrfsa ryhwhgskrl peggafvlap nhftnidplv
       61 vgtavwlsrr aprflakasl fkvpvfgklm sgmgqipver sgrtrlsdpl gggrsvieqg
      121 gaiivypegt ltrdpdlwpm rgktgavria lendvplipm ahwgtqgima rygkklklfp
      181 ptrvdvivgd evdlsayrgr pidqqmllea taivmqrite lleelrgeta patrwdpsan
      241 nqketgkfe
//
LOCUS       WP_284599605             464 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Curtobacterium citreum].
ACCESSION   WP_284599605
VERSION     WP_284599605.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..464
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=49685
     Region          <281..>371
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mtntwpiarg tvpereafal gaavvgvlfa gdavpntltw ygaavvwaal ggwgvsvvvr
       61 arpslartpr alwvflgwcl ltvawshwra atlasmvaqv lcvlvafaia stlswrrild
      121 avslamrwvl glsllfeavv avvvrhpiap iwtdygdrki pdafyfsrae lftggriqgl
      181 pgnanllamv allalvavav qlaegrirrd ravvwlvlgv lvlaltrsst vlvaaavvav
      241 aavvavwvrr vpsgrrapry avvavgavvl avlalvgrga ltavlgkssd ltgrgeiwta
      301 vlglvdrhpv vgsgwigyww pnipeladia hrngvvylqa hdayldvwmq tgivglvlfg
      361 lyvlstlvrs wwcatrtgyg adlrprafdp vtlfpllvvv allvqsvaes rllyqgnwvl
      421 faliaiktrn vlvgeeppsv gdgpripvaa rafrgsnata adqr
//
LOCUS       WP_284599673             314 aa            linear   BCT 25-DEC-2024
DEFINITION  TolB family protein [Curtobacterium citreum].
ACCESSION   WP_284599673
VERSION     WP_284599673.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..314
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=33516
     Region          <18..>249
                     /region_name="COG4946"
                     /note="Uncharacterized N-terminal domain of tricorn
                     protease, contains WD40 repeats [Function unknown]"
                     /db_xref="CDD:443973"
     Region          164..311
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 mtdttrgrql lpgqtsrvhv ydlatrtsrp vfasravlve apnvldertl vlngdgdlwl
       61 lrlpepgsdv vldesalvrv pmpgvteinn dhvldpsgts vvvsardgel yrvplpdggs
      121 aerltdtaav lpvvrkyylh giapdgsvla aivgertvdg vwttdvalvd pasgattflt
      181 rdeppddgca itpdgrtvlf nterftpgta qlaalrldgg dpvrltader vdwfphlspd
      241 gqhllylsyg pgvqghpadh pvelrllpgv lvrgarmavv petlvaldgg qgtvnvppws
      301 pdstwfaycd ypva
//
LOCUS       WP_284599693             449 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Curtobacterium citreum].
ACCESSION   WP_284599693
VERSION     WP_284599693.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..449
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=51207
     Region          1..447
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 msgavvwlre dlrladnpal raaidhggsv tvvvvldeet dgirpvgaas rwwlhhslaa
       61 ldgelrdrgs rlvlrkgaaa dvvpalvrda gadavywnrr ygrverdlda giksaltdag
      121 teahsfaanl lwepwtvltg qgepfkvftp fwraaqampe prhplpkprd lpapadvdgd
      181 dlddwallpt apdwagglrd awepgeagah rklerfvhda ledydqrdep amaatsdlsp
      241 hlrwgevspy qvwhrlhgel epeqrrqapa flrqlawref nwneyfhcdd iatvnvrref
      301 dafpwrdadq deidrwrhgr tgfdlvdagm relwhsgamh nrvrlaaasf lvknllvdwr
      361 igeqwfwdtl vdadpannag nwqwvagsgf daapyfrvfn pdrqlerfdp hreyvhrwvp
      421 adedrpepmv dlkasrqral daydrmrrg
//
LOCUS       WP_284599753             359 aa            linear   BCT 25-DEC-2024
DEFINITION  LolA family protein [Curtobacterium citreum].
ACCESSION   WP_284599753
VERSION     WP_284599753.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Tajima,T., Yokota,N., Matsuyama,S. and Tokuda,H.
  TITLE     Genetic analyses of the in vivo function of LolA, a periplasmic
            chaperone involved in the outer membrane localization of
            Escherichia coli lipoproteins
  JOURNAL   FEBS Lett 439 (1-2), 51-54 (1998)
   PUBMED   9849875
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..359
                     /product="LolA family protein"
                     /calculated_mol_wt=36374
     Region          <97..257
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mkksawlpav vapvvvaaav aapvianaan dpvagtdpta asvlasvaaa kdaqysgals
       61 qtsdlglpel psgsggsslq gdasdvlgll tashtarvyv dgpdkqrfql tqqlaeqdvv
      121 rngsdvwtwd skertathvv lpertaaaap tdgattpadv aqraidaitp sttvskptav
      181 rvaghdawqv tvtpkssdtl vgsvrlavdq qtglplratv laagqqdpaf evgftsldyg
      241 apaarlfdft ppsgadvttk dlsdaprhgd gkrdgsgdhr sgtaptvtgs gwdavvelpa
      301 gtvdrtklda dgsglldqlt kpvdggralq tslvsvyltd dgrvyagavp vsalvtaak
//
LOCUS       WP_284599768             590 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Curtobacterium
            citreum].
ACCESSION   WP_284599768
VERSION     WP_284599768.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..590
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=61934
     Region          1..571
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msaplleveg lrvafgdaep vvrdvsftlt pgrvlalvge sgsgksvsam svlgllppea
       61 rvtgsvrfrg delvgasaer lravrgagig vvfqepmnsf tpvlsigtqi aeavrahptd
      121 ldragvsarv dellrsaglr dprrirkayp helsggqlqr amiamalagd pvaliadept
      181 taldvtvqag ildllrtlgr erslavllit hdmgvvadva devlvmrrgd pvetgtvaev
      241 fahpaaaytr qlldavpale sdpgrearga sapsaatgav aesrperqvs gsgprdtsps
      301 aslanagdgt dttrasrpeg vvaqlrdvav ryarrgdptv sgidlelhag rtlglvgesg
      361 sgkstigral aglvpvvhgs vavegadlrt argrrlrdlr srvgivfqdp asslnprqtv
      421 gwsiaepllv hgagsaadra arvgellaav qldptwaerf phqlsggqrq rvavaralal
      481 rpalviadep tsaldvtvqa avldllarlq qefgfgmllv shdlavvrql addvvvlheg
      541 rivergttdr vlddpqqdyt rmllaaapva dpvrqaerrq awrawegaap
//
LOCUS       WP_284599788             373 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Curtobacterium citreum].
ACCESSION   WP_284599788
VERSION     WP_284599788.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 373)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..373
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=37035
     Region          25..369
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 msaaaprnaa aprsaaaprs aaapvrrgvr vgpvglawrp rvlgytvaal alavvlvvlg
       61 vavgstwiap gtvvralfgv edgpegfivt tlrlprvltg alvglvlgva galtqtvtrn
      121 plgtpdiigv tsgasvgava aivlgggsys vssvvtsggi pvaatigalv aaaavygfgw
      181 rggvqsyrlv lvgigvsatl damtsyllvr akitvataas qwlvgslsst swssvwpllv
      241 vaavavplal atsaalgigq lgdevatgvg lgvqrhrllv valavvltaa avaaagpvgf
      301 vafvvpqval rlagtnrppl llagalgavl vlgadllars afpwqvpvgi vttvvgapyl
      361 iwllvrhrke msr
//
LOCUS       WP_284599819             772 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Curtobacterium
            citreum].
ACCESSION   WP_284599819
VERSION     WP_284599819.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 772)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 772)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..772
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..772
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=78478
     Region          36..539
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mnttshtrtr raaaalatag vlvalsvpsa alaaegdati dlynvndfhg riaqslsspp
       61 rdgdaagaav lagaleqlrg sdpstsafvs sgdniggstf esfiqedqpt idvlnqmdlt
      121 vsaignheld rgqtdlrdrv igadgarnak wdyvsanild satgkpafdp yaiqeisgkr
      181 vgfigatvdl vgqglvspdg iaglemgdit tevnkvaaql tdgdegngea dvlvllvhdg
      241 aesptpvtad ggsdfaravy gvtpkvsail sahthqtyty svvpkggtvp rpviqtgsyg
      301 fnlghvqltv aadgtvtptk nenirlagst fpkdaavqat vdtavaeadr lgavelgavd
      361 rdlkravqsn gsenrggest lgnfvaevqr sqtqrqgaqi afmnpgglra diasgpvtyk
      421 eaavvqpfan tlvvldltgd qvrqaleqqw qpasasrpfl klgtssgfsy tydpladags
      481 ritsmtldga pvdadrtykv tvnsflatgg dnfaafkqaa akqdsgmvdl eaqveyfkan
      541 psvavqedqr avgvrvsdap eggfgpgdev ridlssltfs naadqagsvs vsaggqelas
      601 spidtsvvdt tdeqgratlt ftvpgvggdq ptaraaatgt alravapaat tdeplvvtlp
      661 ngqtitlavt vpieaavdpt dptdptdpgt pgtgdpsapg tgggsigggn gtgtgngvad
      721 gaqrpgtgal awtgaellpa giaagallla glvtmvlvrr nralrsatve td
//
LOCUS       WP_284599843             470 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Curtobacterium
            citreum].
ACCESSION   WP_284599843
VERSION     WP_284599843.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..470
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=49541
     Region          12..428
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mpstapppsr gwfaqlllrl hflaglfvgp fvlvaalsga vyavapsieq vvyrheltap
       61 statarplad qvaaaqryva shhpddtvve vrpapapgdt trvmfteagl lesqtravfv
      121 dpgdasvrgd lpvygtsgsl pfrtwistvh rslflgdvgr lysetaaswl givslagigl
      181 wafrlrtarr krelvvpatr lrgyrrtfsw haatgawvll galflsatgi twshfagdnv
      241 talrsalswq aptvdtalgg aaamgmtage haghhgsaaa pvgspatvtp eqfdevlava
      301 rsadvhaaev rirpaattdq awtveeikls wpvamnavav dpttmtavsq vtwddyplma
      361 qaaklginth mgalfglpnq lvllaaalgi aamvvlgyvm wwqrrtpgtr vgrapadgal
      421 arapwwgaia vvavaiglal llpvvgvtll gfllvdalvt afrsrpgatr
//
LOCUS       WP_284599846             272 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Curtobacterium
            citreum].
ACCESSION   WP_284599846
VERSION     WP_284599846.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18629437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..272
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28855
     Region          108..271
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          215..271
                     /region_name="GerE"
                     /note="Spore transcriptional regulator GerE (stand-alone
                     HTH domain) [Cell cycle control, cell division, chromosome
                     partitioning, Transcription]; COG5905"
                     /db_xref="CDD:444607"
ORIGIN      
        1 mtdtpasrsa asehartvae qadrhaltle svlavlrspr lsdtaaraea veiasaalvd
       61 lrtvtdrqrs tllepvtgaf srlradlrpl vrfgdldvqf veppatgral pgavahgara
      121 ivrtavlalv ddgvarrvri qwdcdgrnll vqlrddgagt ldvhddavrp iaervvaldg
      181 tlqvdstpgw gstlditlpl dpapgtvdlp tdtdltarer dvlrlvvtgv gnreiadglg
      241 ispntvkyhv anllrkhgar traelaalga rp
//
LOCUS       WP_284599865             355 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Curtobacterium
            citreum].
ACCESSION   WP_284599865
VERSION     WP_284599865.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..355
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=37371
     Region          5..315
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mstrravvlg gtggigsavv rdlldvsgrg gddwqvdvva rhggpaadal taagatfaag
       61 drrdtavlre llrpgadllv davgatrdda lqlrpflddv gstvfvsska vyadeqgrha
      121 nsvdrpvfgg avtelqptvp agdgdptsrd gygaakiaae qvlldhgapv tvlrpskvyg
      181 vgigrprewf vvrraldgre rilladggrg vdhttaasgi aslvrlvada pdrrilnvad
      241 etapsvleiv rtvaglvdhr fdevmldqda pafvgttpws sptpfvldtt aaralgwqpp
      301 ryaeavrpev awlletahav paggdvpwae dpfwermfdy gpedaallll slgrd
//
LOCUS       WP_284599880             403 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Curtobacterium citreum].
ACCESSION   WP_284599880
VERSION     WP_284599880.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..403
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=43399
     Region          32..392
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mttntlaper ssttrraaav grgigaartt ppppltnrap aldglrtiai lavilyhlhv
       61 pqfeggfigv tvffalsgfl ittlllgehr ktgrirlgsf wwkrllrlyp allalvavgl
      121 llwnwvgdyk gasfgpgeaa fialtytgnl frsfwdttqg vfahtwslsm eeqfylvwpp
      181 vlvllfmvra rrrwlmaglg avivgcsiaa glvyqtpngg stpdvyfspv lgvvplatgc
      241 llalllddar vrtwaagvag hvaswaglal lvgillwigd dwtqhawtfg vvlpltgvvs
      301 svliaglvsv rsplsaalaw tpvswfgrrv sysaylwhpl vialldpfai gpwgtvwlia
      361 vallvavgaa yavevpveka rkrvrearsl vaadraeras vtn
//
LOCUS       WP_284599881             392 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Curtobacterium citreum].
ACCESSION   WP_284599881
VERSION     WP_284599881.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..392
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=40261
     Region          28..>308
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mtsdptdvlv vgggpvglla avllaaegvd vrvwerrsta ptgsraigih ppslavfdrv
       61 gvagpvlaea vpvrrgvats rgrtlgtlsf dhvsdpfpfv aaldqhrtet llrerlaala
      121 phalrtgttv talaperghv avsgsgpdga pvqvrarfvv gadgarstvr dllgirttgr
      181 tyrehyvmgd fadtgdapvd tavvdvgpgg vlesfplpgg rrrsvalvtg patrpsgtdg
      241 teagrasrla tlvrertgta pdpatcsmvs afrtrrrtae rvgvgrvvlv gdaaheispi
      301 ggqgmnlgwl dvaalaplla davrsgdagp wpayaatrqa aaaraarqae anaalgrpar
      361 gallvgreal lrsvlalpsa rwlaatyamg wa
//
LOCUS       WP_284599902             752 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Curtobacterium citreum].
ACCESSION   WP_284599902
VERSION     WP_284599902.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 752)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..752
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76175
     Region          6..751
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msdgvveldi tgmtcascan rierklgklp gvtatvnyat eqaqvevagp daadtaalia
       61 aveaagygat vhaqaapesd geappadpta alrqrllvsa alavpvvlls mvpvlqfpnw
      121 qwaalalaap vavwgalpfh raawtnarhg aatmdtlvsv gvgaaflwsl yalflgdagr
      181 pgmhmafswf atdpeasdly levaaavtvf ilagrymear akqrsgealr allalgakda
      241 svlrdgpggp veqwvptasl vvgdvvvvrp geripsdgvv rdgssavdlg mltgesvpve
      301 vrpgdrvtga tvnvggrlvv evtavgadte larmgklved aqtgkaavqr ladrvsavfv
      361 pvviglavva fvgwlvaggs vtaaftaava tliiacpcal glatptallv gtgrgsqlgi
      421 liggpqaler trtvdtivld ktgtvttgem tvrdvravas aeaatvlala asvedgsehp
      481 vgravveaar vrgldvpraa dfravpgagv qalvetgdaa evvlvgtasw lvsdwavavp
      541 ddlaaavsta etaggtavvv arggaalgvv vvgdtvkpea adavrrfrel glrpvlltgd
      601 nagaaravae qvgidevhar atpaskletv rrlqadgrtv amvgdgvnda aalaaadlgi
      661 amgagtdaai aasditvvsg rltvvadavr laratlrtir gnlfwafayn vaaiplamag
      721 llnpvlagaa mafssvfvvt nslrlrrfaa rs
//
LOCUS       WP_284599973             121 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Curtobacterium citreum].
ACCESSION   WP_284599973
VERSION     WP_284599973.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 121)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 121)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 121)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..121
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13246
     Region          20..105
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mpanvdaper lpqpavsemd lptvldamsd pirlailhry lvdaaggvrs cgwvgldrpk
       61 stlthhfrvl reaglleqhq eglvrssrvr vedvqqrfpg lldlvadwqv paallldevp
      121 a
//
LOCUS       WP_284600057             340 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Curtobacterium citreum].
ACCESSION   WP_284600057
VERSION     WP_284600057.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..340
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34269
     Region          57..340
                     /region_name="COG4132"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443307"
ORIGIN      
        1 mttapaagar stgtpgpgpg tvgtapvtag paatstapaa gaglgtrttt ksaanprarr
       61 gpglawlglt pfavyvllfl avpaviavss gfftgdgaft lanlaafadp svlrafggsf
      121 glsavsavlg avigalvcwa laalrpdglv rsmidaaasv laqfggvmla fafiatigvq
      181 glvttwlvsa tgvdlnanga flytvpglvl pyvyfqvplm vltfmpaleg vktqwgeaaa
      241 tlgasratyw rrialpvlap afwgsllllf anafssfata aalisqggiv pltiraqlts
      301 etiiglqnva gvlalgmvvv mavvmgaysl lqrraarwqr
//
LOCUS       WP_284600112             279 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Curtobacterium citreum].
ACCESSION   WP_284600112
VERSION     WP_284600112.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..279
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28123
     Region          14..276
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mnalqplapt ivclaavlgl lvgsflnvvv hrvpaglsvv rpasacpacr aeirafdnvp
       61 vlswivlrga crdcgsrisa ryplveagts asfalvtggv lasgvvhaap tgptlvllvg
      121 llylmavsis lalidldthr lpdaivlpay pvlgvllats sattgdwgal lravggaaim
      181 fvlylalavv vpggmgmgdv klagvlglvl aylgwgplav gafggfalga tfaigllvtr
      241 raargsgipf gpwmlggawl giligtplwn aylgliglt
//
LOCUS       WP_284600147             327 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Curtobacterium
            citreum].
ACCESSION   WP_284600147
VERSION     WP_284600147.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..327
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35343
     Region          14..322
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtasrgmivd msgpssrmla llsllqvhre wpgdelatrl avsprtlrrd vdrlrdlgyr
       61 veavrgpagg yrlgagsdlp pllfddeqav avalalavap asgadiaeaa aralttvrqv
      121 mpehlrnrvd lvdavttpgt tradpevlva vsaavhrhev lrfgygerdt lhrvephavv
      181 arsgrwylla weperddwrt yrvdriaprm ptrlpftprp vpggdvaafv sarfrgsdrd
      241 dawpctgsvl vraedaaria pflpedavve alddgrsrit rgswswdgla gafaastvpf
      301 aveepdalra avaaltgrlq eaigdgr
//
LOCUS       WP_284600167             481 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Curtobacterium citreum].
ACCESSION   WP_284600167
VERSION     WP_284600167.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..481
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50926
     Region          1..467
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mvdavvvgag pnglaaavtl araglsvevv ernetiggga rtaeltlpgf hhdvcsavhp
       61 malqseffrl frmedrielr lpevqyghpl drgdagiayq didrtasalg ldgpafrnlm
      121 aplarsadqv adfatdallh vprhpltvlr fglraleqgs aawnvrfreq vapamvsgva
      181 ahsiqhmpsl staaaalslg syahargwpv piggsqaivd alaadllahg grietgreir
      241 slgdltpaka vlfdtsvpgm lriagkqipt pkrgalrrfr fgnaaakvdf alsdpvpwtn
      301 aelrkagtvh iggtrseiaa aehavahgrh adrpyvlgse ptvvdpgrap rgkhvfwaya
      361 hvpagsdvdp teavvrqver fapgfrdtil qsasrtavqm aeynpnyvgg diaagaasfw
      421 qlvkrpvlss dpwrmgggmy lcseaaapgp gvhgmagwha arsvlrhtfg lsehvdlape
      481 e
//
LOCUS       WP_284600186             189 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Curtobacterium citreum].
ACCESSION   WP_284600186
VERSION     WP_284600186.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..189
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20926
     Region          32..152
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mnlylrlfll tvrirlaglr pgrrpslwde grtplrvalt dldplrhvnn gkylsmldlg
       61 rydlltrsgf wheasrrgwy avvaaqtity krsltlgqrf tlvtrvlgvd dravyieqaf
      121 errgsvvara vvqarflrrt ggtvmpeelv aaaggaprdl tlpdwvhawa davrissaap
      181 tgtargasa
//
LOCUS       WP_284600261             366 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Curtobacterium citreum].
ACCESSION   WP_284600261
VERSION     WP_284600261.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..366
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37299
     Region          27..356
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mqharrpgrt vwtvlvvvla ltvvnvgvga twwsrasadp taavtvtatp tpavtptptv
       61 lpdpvgsdgi plaehpsasq gpatldlaht waprtdlpta grllhvtipa trshftarpg
      121 llwlppaalv pdppalpvvv llpgqsrgsg pedletgghl tetmdavaam haglapivvv
      181 pdqlgpdsgn pmcvdgplgn srtyleqdvp awitshlrvq tgasawtigg fsqggtcaiq
      241 lgagdpgrfg niidvsgelg ptlgspgesi argfsgnaaa yraaqpeall aahgpyrdss
      301 afftaaqlds hygpampvvs asaaaagmhv ttwvvpgvkh nwlnartaia agmawlvpri
      361 glapgp
//
LOCUS       WP_284600270             442 aa            linear   BCT 25-DEC-2024
DEFINITION  protoporphyrinogen/coproporphyrinogen oxidase [Curtobacterium
            citreum].
ACCESSION   WP_284600270
VERSION     WP_284600270.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Pawelek,P.D., Cheah,J., Coulombe,R., Macheroux,P., Ghisla,S. and
            Vrielink,A.
  TITLE     The structure of L-amino acid oxidase reveals the substrate
            trajectory into an enantiomerically conserved active site
  JOURNAL   EMBO J 19 (16), 4204-4215 (2000)
   PUBMED   10944103
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440906
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..442
                     /product="protoporphyrinogen/coproporphyrinogen oxidase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006779 - porphyrin-containing compound
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=45139
     Region          10..442
                     /region_name="HemY"
                     /note="Protoporphyrinogen oxidase HemY/PPOX [Coenzyme
                     transport and metabolism]; COG1232"
                     /db_xref="CDD:440845"
ORIGIN      
        1 mtdvvvvggg vaglvaardl akggahvvlv eagdrlggml rrhtvagldl dmgaesfatr
       61 tdavarlate lglgndvvsp dprgawlmtr dgrtapipqt gflgipgtpm aadvtavigq
      121 gggfraqmds llpspvgaka tslgalvrkr mgervlddlv vpvaggvyst hpdqldpdrv
      181 apglraalqr egslaravla lrsraaagsa vqgirgcivr lvdelladte tygvevrmrt
      241 rataverhav evvtargtre ripaqvvlss tadpmrtaap drtgielvtl vvdqpeldaa
      301 prgtgmlvhp qadgvsakal thatakwpwl aeaaggrhvl rlsyataphd datdpagvat
      361 slpvdpddav gtratrdata llgvpvtpdr vagaarvrwy gpdltaagla egvegigeas
      421 sgrglagiva aarasaervl gs
//
LOCUS       WP_284600278             240 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Curtobacterium citreum].
ACCESSION   WP_284600278
VERSION     WP_284600278.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..240
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25004
     Region          8..>63
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 msvdptahdr yaewdaayvl gslpaderle yerhlescpr ctaavaelvg lpgllgklpa
       61 dqaieiaepd grhdtgsagt lasvahrvrh rrrrrrvwva ataglavvaa vlgglavgta
      121 gergavqaga sptaagpgdr ytmtgsqgld vdlavsgeqw gtrfdwgcsy ggkqwssdgs
      181 vmydlvvvrt dgtvqtvasw saagaeargl sastdiprde iatvevrlrg esgvladvhl
//
LOCUS       WP_284600377             301 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Curtobacterium citreum].
ACCESSION   WP_284600377
VERSION     WP_284600377.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..301
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30241
     Region          4..284
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(31,235,238)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(175,206,233,236..237,240)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mssvivigea lvdvvdrpeg rsehpggspm nvavglarlg rparlvcalg dddrgaavra
       61 hveasgvrvd atavprtsta vatiaadgga sydfdldwri dpvdvhegtp lvhvgsigav
      121 lqpgaatvld avrartagtl lsldpnvrps itpdrdavla tlepllaead vvkcsdedaa
      181 wlwpdrdvda vldgllaagt tlaavtlggs gcaiasrgar rriaapavtv adtigagdsf
      241 magllaavla tgtaptdlde ddlgrlagla lacaavtvsr pgadppttde lpaevrpdat
      301 p
//
LOCUS       WP_284600401             711 aa            linear   BCT 25-DEC-2024
DEFINITION  MMPL family transporter [Curtobacterium citreum].
ACCESSION   WP_284600401
VERSION     WP_284600401.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 711)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..711
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=73570
     Region          23..706
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 mprflrivlp avvivvwlvv asvggpvfgk isgvatndqt sflpasadat kvqerssafr
       61 qasgapaivv lerdgglrdg drtaaeqlaa tlgdrsdvqg vspvipsedg daveivatlt
      121 qdaetgdava siradvedal paglsgyvtg pagftadlte afagidgill gvalaavfvi
      181 lvvvyrspll pvlvlgtatf alcasilvvy wladagivtv ngqvqgilsi lvigaatdya
      241 llytaryrea lrdhrtgwga tkaalrgafe piiasggtvi vgvlcllfsd lnsnkalgpv
      301 aaigiafsll aaltllpall mafrraafwp lrpaygsahk vltgpdargi warvgrlvar
      361 rtrtvwvvct vallamgagi vglradgvpq sdlvigssqa rdgqdvladh fpggsgspaq
      421 vigperdldr lvtairsvdg vdgvvaaakd spsgttpvgt ttkddtaarg pvadptvsdg
      481 dvlleatlta padseraeqt vrdlrtaver vspdalvggv tataldtndt girdrtviip
      541 ivlvvillil mlllrsvvap lvligsvivs fvaalgvgal vfdhvlhlpg adpsvplfsf
      601 vflvalgvdy niflmtrvre ealrhgpreg vlrglgatgg vitsagivla atfaalgvip
      661 ilflvqiafi vafgvlldti vvrsllvpav vydlgrraww psrlsrathh m
//
LOCUS       WP_284600548             386 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Curtobacterium citreum].
ACCESSION   WP_284600548
VERSION     WP_284600548.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..386
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41881
     Region          35..378
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mskpvttdam kghvgsmepm daqcftvllm ssggtssrid gldalrglai alvllrhswp
       61 qiagtggvvg vvifftlsgy litslldrdl rhfgrvrygr fyrnralrli palllllvgi
      121 tavtlvwnpl ddrsglvral vvgitytanl pfdhgsptve hlwtlateeq fyivwplvla
      181 lavrfrrert alitstiviv aalvctialt ypgvtgiysl ptswcvamlv gaaafyarvn
      241 ldcalplgap ktiwiastal tlvlvvsflp emkaspllyl vvgplvslas vplivvaasw
      301 kslpsawltp lkwlgkisya aylwnwpivl wlgpqplapa pavagvaltl laataswwlv
      361 erpaqslrri werpnarpve qerats
//
LOCUS       WP_284600537            1184 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Curtobacterium citreum].
ACCESSION   WP_284600537
VERSION     WP_284600537.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 1184)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 1184)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165397
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1184
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..1184
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=121034
     Region          192..681
                     /region_name="Peptidases_S8_subtilisin_Vpr-like"
                     /note="Peptidase S8 family domain in Vpr-like proteins;
                     cd07474"
                     /db_xref="CDD:173800"
     Site            order(201,278,364..366,396,622)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:173800"
     Site            order(201,278,622)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173800"
     Region          <425..>561
                     /region_name="myxo_dep_M36"
                     /note="myxosortase-dependent M36 family metallopeptidase;
                     NF038112"
                     /db_xref="CDD:468355"
ORIGIN      
        1 maltcgglav ggaanaapsg lssadlklaq plrdakpskt iaafvrttge galavdakak
       61 ggdltksktq stqakqrvqa iastvdavsa avkqsdakat elysteytvp gvavvadvda
      121 lrsiaersdv esiipltpkk ivdpapgdas qapsgvdpdl vkpgadgvsp knaasdvytr
      181 aldawqqtgk tgkgvniavl dtgldytqad fggpgttaay qtalastnap dpswydgsky
      241 lggydfagpt ynadtssaay dptpkpdenp idgkggdhgt hvagtaagfg ltadkktfrg
      301 dyskltnqtv qdmwvgpgta pqaglyalkv fgddggstdl tgaaldwvgk altegkdinv
      361 lnlslgsdyg apddpdnaki daltargvlp viasgnaddf tdiggspgna egaltvaasa
      421 tgqslfdgvq atapadvant yraqysqnyq gtlpvegdvv vpstnidgcq afsadeaakv
      481 kgkvvwlkwt dgalecgsgv rfnnvqaagg vgvllagtvt sfdsgiagna tipgaeltsd
      541 svaslqaaaq agtlhvrfaq elkgfqlatd qanvntlapf tsrgvhgsfd divkpdvagp
      601 gvnvisaang tgdgrmsmsg tsmatphvag ivaltfqshp swtapqvkaa vmntathdvr
      661 qgdrtatllr qgtgrvdalq avtagttvrs iendqlvtas ygvvevsgat sesrtlqiqn
      721 tdgrphtydv ayqpqvdqpg vaftlstkrv tapahgtatv kltftiadpt klrrvidptq
      781 esvqsgyqre fvaaasgvva ftptdkslnp lrlgayvapk pvsavhgkdi afsgtqttad
      841 laltgravdq gdavtgyhsv vapfvlggtd pqesfpagsa kqslqaadir syganydkas
      901 dtlafgvqta gadanpgavt nvevmidtnr dgkpdylvyd aksatvdatf attvdlatgk
      961 tvdsqplngg tagqdvntld savkvltvsa stigatapfd ysvltesaya palatsgsyv
     1021 vdetdsatyd pskpaltfaq gtttgvlfad qgslqvtrpa dvtnarilll hlgnavgdqa
     1081 dtlaaaqtap tlalrkgsav tisgdpkvgk tlraqhgswd gkkvtysyqw lrdgvavkga
     1141 tgeryslgtt dqghrfqvqv takakgyqdg satskstakv aprr
//
LOCUS       WP_284600777             151 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Curtobacterium citreum].
ACCESSION   WP_284600777
VERSION     WP_284600777.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..151
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16506
     Region          2..144
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mrwsdidayg hvnnsamlrl leearivgfw ghdpadvnge gdlpdpiidg rpgsgtmtvi
       61 aaqrleylas ipylrrpldv qmwigrigga sidvsyevws pvgvepavly trattalvmv
      121 daatnrprrl taveraaceq faeppvefsr p
//
LOCUS       WP_284600783             468 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Curtobacterium
            citreum].
ACCESSION   WP_284600783
VERSION     WP_284600783.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..468
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49259
     Region          14..353
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mekraayesv lpyvrewigy kvwqlrlpgv qvavgfegee lfaeawgyad veagrrlttt
       61 drfriashsk tftatallql adagalrldd tvgsfvpalv dagspiagat vrelmemggg
      121 vvrdgadgdh walahpfpda eqlvalvveg gakvpvgsaf nysnlgygll glvveavtgt
      181 syaehvraai teplglahtg pefdpaheda fvvgytglht artrtrvphv ttgalaaatg
      241 fhgtasdlvr yfsahvpgrg dllsdhakrl aqrkawsald tdpaargyga gfivdringr
      301 evrghsggfp gqitqsvfdp asslivsvlt ssatgpagml angivhllda aadehaagpa
      361 lpddvdtsry vgrfttfegi tdfarvgdrl laidptqpvp tespvrldvv dadtlrmaag
      421 nrfgsidelv sftrddagtv vsvrgdsgmt hrpwavpeet pevaaalv
//
LOCUS       WP_284600788             999 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-mannosidase [Curtobacterium citreum].
ACCESSION   WP_284600788
VERSION     WP_284600788.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..999
                     /product="alpha-mannosidase"
                     /calculated_mol_wt=109569
     Region          247..998
                     /region_name="MngB"
                     /note="Alpha-mannosidase [Carbohydrate transport and
                     metabolism]; COG0383"
                     /db_xref="CDD:440152"
ORIGIN      
        1 mhddiplttg rarrvlderi lpavhatsvp levawhelpg epvppaegla ldwtpyevgt
       61 pwgaawgttw frltgtvpaa yagqrveavv dlgfdknmpg fqceglvyra dgtpvksinp
      121 rnqwvlvter aeggetvelf veaasnpvll dyhpflptqe gdvqtssskr lytsrrmdla
      181 vfasevhels ldievllelq aqlpdgprrm rilqalddal drldlqhiae taadaraala
      241 dvlaapadas ahtisaigha hidsawlwpv retirkvart tstmtelidq tddflygmss
      301 aqqyawikeh rpevyarvrd avaagrflpl ggmwvesdtv mptgeslvrq fsqgqrffer
      361 efgirpkgvw lpdsfgyspa lpqlmrragf ewfftqkisw nqvnkfphht flwegidgsr
      421 vfshfpsmdt ynsrlsgeev akasrqfren rlatgsiapv gwgdggggtt remtgtaqrl
      481 adlegsakvr wehpdaffdr akseledppv wvgelylelh ratltsqhrt kqgnrrceql
      541 lleaelwatt aaartdfayp ydeldalwqq vllqqfhdil pgtsiawvhr eavakyaeta
      601 aaltaitera laalagpgdv pvvvnpapfl qagapalgat taadvpaatp vslterdggw
      661 elandlvrvv vdarglvtsa vdlstgrdai apgrvanllq lhqdfpnmwd awdvdryyrn
      721 rvedltdvtg lraavddtga arvvverafg dstvtqeivl apgsrtlefd qvtdwhetek
      781 flkvafpldv raehtvaetq fgaqkrvtht ntsweaakfe tsmhryvlve epgfgvalvn
      841 dsihgfdttr davdghvttt vrlsllrapr fpdpetdqgv qthrygivvg tdqlgataag
      901 vlmnagartv tgghgfaplv rvsgdvvlss vkladdrsgd lvvrvyepag rrgtghvavd
      961 gpfgdptdvt lleeplaaid psgfavdaye vrtvrfvra
//
LOCUS       WP_284600821             444 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Curtobacterium citreum].
ACCESSION   WP_284600821
VERSION     WP_284600821.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..444
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47400
     Region          24..435
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mnqpvplple apdtsfltsg gafvrrtvlp sgvrvltesv pgasstslgf wvgvgsrder
       61 egqfgsthfl ehllfkgter rsaldiaisf dsvggehnaa takeytcyya rvrdtdvpma
      121 vevigdmvtg svleaeafdv ergvileela maaddpadva geaffaaafd ghplgrpigg
      181 tpesiravgr aevldhyreh yapngivvta agavdhdrfr elvehvfrda phasplarrt
      241 pqpvadpavp kltvahrpte qvsmlrgsqg ldlrderrpv lsvlnavlgg gmssrlfqev
      301 rerrglayav ssfapayldn gafgvyagca pdnvagvvei idaefrrmvd dgitddelrr
      361 akgqiegalt lsledsdarm trlgrselgt geftdlgtal qrvdrvtpad vldlardllt
      421 rptitsvvga vqrdelaaai gaeg
//
LOCUS       WP_284600920             221 aa            linear   BCT 25-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Curtobacterium citreum].
ACCESSION   WP_284600920
VERSION     WP_284600920.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..221
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=23205
     Region          7..195
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 maalltipqv fallqiapdg raratvtrtq lgtaggvlad ltlrgaials kdrvviasgt
       61 ptgdqvldta lawiasespk pakwwvrqlg krtlhdgvva qlvqrgvlte eqhrtllvft
      121 ttrhperdgl praqvrqavd evlagraass pyiaavigll datdtlrsef grvdkrflrs
      181 vvqgdwvaaa vrrlladvna saamtagvia sssaattags n
//
LOCUS       WP_284600975             420 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Brachyspira pilosicoli].
ACCESSION   WP_284600975
VERSION     WP_284600975.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..420
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48211
     Region          1..408
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mvkrltlnng iriileympi letvsvgfff itgsanetek engyshfieh mlfkgtndmt
       61 skeivryieg vggvfnayts rhftsfyini iskyfdraid tlsnialnsa freedikkek
      121 kviieelkmt sdspeeimtn qffakaykgt smqfpiggni kniknisrdk ilnyfqnhfn
      181 snnlivsiag nfnvksaidk lsslelkenv lkadeelpff yksvskeksd lnqvyfalit
      241 psynakdkrk ytmnivndif ggslysrlfq sirenkalcy siysnnsafl nggtfdifgs
      301 tsldkyeetl isiyneierl lderitkeel eeakesykss msfskfsasf amnknarnel
      361 yfskylsykd lyntidkini ndinkaiedi fqnkkfflta vgpkgtkkit dkvskklkln
//
LOCUS       WP_284601086             342 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Brachyspira pilosicoli].
ACCESSION   WP_284601086
VERSION     WP_284601086.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..342
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37594
     Region          1..338
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mrvydlrtdt itkpsdemrk aiykaecgdd vymedptgnk lqdmaaeitg kekaifvssg
       61 tmgnliplli lssktrqill eeeshivhye lggvaalagv lplpvkakrg iltksiiedy
      121 fspqpyymsn vnivevensh nrhggsvypi evlkelysft ksknvhmhmd garvfnasia
      181 skasvkeias ntdsitfcls kglgapmgam lcgkkefide afkirkligg glrqiglmaa
      241 agiyalenni dsleedhika kkiasavies klgelsldev etniviaktq kksielvnkl
      301 lekgikassf gdyklrfvth rdismkevee acdiiksfkn ni
//
LOCUS       WP_284601102             441 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Curtobacterium citreum].
ACCESSION   WP_284601102
VERSION     WP_284601102.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 441)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46385
     Region          4..418
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mnsrraflvw gvavlafvla vvqrsslgvs gvdaqdrfav saavlstlav vqiavyaglq
       61 ipvgialdrv gprklvllga allvvgqavv afsptigpai agrvlvgagd amtfisvirl
      121 vpmwfsgril pqisqwtgnl gqvgqilsaf pfavllhtag wtpafsvaaa aslvglllav
      181 vfvrngpvpv rtdtiplplp hswrgafhtf ghalrrpgtq lgfwshyvtq ssgtvfsllw
      241 gvpmlrglgy tpseaatflt vivvvgfvag pvlgvlcarf plrrsnlvlg ivaalalvwt
      301 avllwpghpp twllvllvva mgvggpgsli gfdfarsfnp vgslgsangv vnvggflaaf
      361 vmmfligtll dvvsgatgrt vfawenfria ltvqyvvvgi gvgmllharr rtrremhaqd
      421 girvgplwva lvarlrkkav q
//
LOCUS       WP_284601116             407 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Curtobacterium citreum].
ACCESSION   WP_284601116
VERSION     WP_284601116.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..407
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43931
     Region          150..399
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 msrsarpaed vvqetarsag lvalgagiaa tavaaavvgg fvaavaravv tpdrkrterv
       61 pihavdpgam tvtlertadt elqgryslwf gggtghmrvg evlgttdttv trriiaidag
      121 dprsarrgrw ggwfyltpge ldvpvedvdi ptpngpapaw vvraddpdap wavlvhgrgv
      181 traetiravp vfraagysvv laswrndgva prstdgrygl gstewedvda vlrwltaqqa
      241 rsvvlmgwsm ggavvlqtlv rsrfaglvdg ivlespvvdw havlksqsrv lklprpvrkv
      301 aqrllrtpvl hhvagldhpv dlreldmvar adeltvpili lhsdddgfvp ssashdlara
      361 rpdivrlevq ttarhtklwn hdadwfdari lawltevvqp tdatsar
//
LOCUS       WP_284601166            1033 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-mannosidase [Curtobacterium citreum].
ACCESSION   WP_284601166
VERSION     WP_284601166.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..1033
                     /product="alpha-mannosidase"
                     /calculated_mol_wt=114131
     Region          247..1030
                     /region_name="MngB"
                     /note="Alpha-mannosidase [Carbohydrate transport and
                     metabolism]; COG0383"
                     /db_xref="CDD:440152"
ORIGIN      
        1 mhqnqqlvea riervlneri vpavhqartp vtlaawqvpd epvpaaeala aeyrpfavge
       61 swgrawstww fevtgavpae wagrtvellv dpgfqgdwpg nqaegllhtp dgtpvkgihp
      121 rnhhlriadr avggeqvhly lemaanpdil vnefvpttfg skrtapetpi ytfrtaelav
      181 fepevwalrf dvevlfqmvk elpeadprrh evlrdleram dvlalddivg taaaaraela
      241 galaspanps ahrlsgigha hidtawlwpi retkrktgrt fsnvlalaeq ypdfkfaass
      301 aqqyawvker yptvfagika aiargqwivv gsqwiepdgn lpggeamvrq vtqglrffad
      361 eldvethgiw lpdsfgytaa fpqiaklagl ewfltqklsw nqtntfphht fwwegidgsr
      421 ifthfppidt ynatlegeel hhavrqfrek gaattslvpf gygdggggpi remmerqrrv
      481 eslegsprve vehpddffar areeypdapv wvgelylelh rgtftshare krgnrraehl
      541 lreaelwsta aalqgapypy ecldelwqat llqqfhdilp gssirwvhee neesyrrnha
      601 eierltaral ahlgaagvva naadhdrrel vldaagapvg vvearahals pltvvtpeha
      661 vtatqgadgt vldnglvrvh vdgdglvdsi vdlvhdrelv padrsanllh lhedlpnawd
      721 awdvdahyrr svvelraaes velttdgdlr avvrvrrvfg sselvqtiav haddvrvhlg
      781 vdlewrerek llkaslplvv haqhhsaeiq fghlrrptht ntswddarfe vmahrwvhve
      841 epgygigvtn agtyghdvtr rvgahgevet evrlslvrga qspdpeqdlg hhtfaytvhp
      901 gadvaavvas gydenlplrv vpaagdtpag gtgatvtapv vssspgvrve svkladdrsg
      961 dvvvrlyeal garsdteldl rvdavsveqv dlrerpladp altarrfaws ggtvalglrp
     1021 fqvvtlrirp rga
//
LOCUS       WP_284601467             574 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Brachyspira pilosicoli].
ACCESSION   WP_284601467
VERSION     WP_284601467.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..574
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=66763
     Region          382..483
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mlneikknic iitdingiyg yghftrmnli anrladiydf tfssidngse lykrvdikti
       61 efnkigeikp yiiivdsrev eekyisylkk issviivdsv gserrladiv iemlpnldns
      121 kevnikpfia tilnnsikpi ynedspilvy lgfnkqlkdk aiqiiskitn kkfvvidfkr
      181 esefsnieyi dfskdifans ysgvityfgl tafecieski ptilfsptky hdelankcdd
      241 iffnlgffed adidesakki eafisdkekq dslienaeqi ntdesierlk tifsnikdfk
      301 dikcpfckss nierknrnle snlykcghcn tlfrkyflsp ftdysskyfv edykkqygkt
      361 yeedvdnlsr lakrriekik kikpngkvld igsamgfflk easnygyite gieiseyasn
      421 ycvntlnlnv hncslldfny kekeydiita wyvvehiynf dkifehilys lkddgifala
      481 mpngygvsgr fnknyysivp sdhafeanpk sldmffakys lkrinlenqs iyynrftdvf
      541 kifknsklse klykklaqkf nlgdtfeciy qkvk
//
LOCUS       WP_284601517             425 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Dickeya dadantii].
ACCESSION   WP_284601517
VERSION     WP_284601517.1
KEYWORDS    RefSeq.
SOURCE      Dickeya dadantii
  ORGANISM  Dickeya dadantii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Dickeya.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Dickeya dadantii"
                     /db_xref="taxon:204038"
     Protein         1..425
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=48999
     Region          2..407
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mklnarqvet akpkektykm adggglylei tprgskywrm kyrrpddkke drlafgvwpt
       61 vtladarakr deakkllvqg idpkaeqkea qaetagaytf etiarqwhas nkrwgdyhra
      121 rvmrylelyi fpyigtadir klktshllap ikavdasgkh dvaqrlqqrv taimryavqn
      181 dyidsnpasd msgaltttka rhypalpper lhefrsrlaa yrgrqmtria veltlltfvr
      241 sselrfaqwc efdfdkaywr vpaqreaikg vrysyrgmkm keehivplsr qavalleqlk
      301 aisgdnkclf pgdhdpekvm sentvnnalr amgydtqtev cghgfrtmar galgesglws
      361 ddaierqlsh sernnvraay thtseylder rlmvqwwady ldnnrdsyit pydfarvtik
      421 rndlp
//
LOCUS       WP_284600728            1087 aa            linear   BCT 25-DEC-2024
DEFINITION  UvrD/REP family DEAD/DEAH box helicase [Curtobacterium citreum].
ACCESSION   WP_284600728
VERSION     WP_284600728.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1087)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1087)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1087)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12774065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..1087
                     /product="UvrD/REP family DEAD/DEAH box helicase"
                     /EC_number="3.-.-.-"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=117260
     Region          43..855
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
     Region          <612..1074
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 mttdtsgttd tsdagalptv gatptpqhda daiadalgrp rptaqqravi esplapalvv
       61 agagsgktet masrvvwlla ngfvrpaeil gltftrkaag elsvrindri raledvglld
      121 agdafeaptv stynafanav frenallvgr dgesqvltep sawqlarrvv vaarddrlag
      181 ldrdvdtvta avvalagavs ehlvdpdrlr rfavdfgall elpgnnrgnp ykavtdavra
      241 vgaleplvel veefrrqkvd rgfvefsdqi alalaaaesa prvvedlrtr frvvlldeyq
      301 dtsvvqtrfl arlfrghpvm avgdphqsiy gfrgasaanl arfprdfgdg dtvpvtfals
      361 tswrnpvdvl aganavvgpl sdasevaver laprpgadag tvdvafpetl peeadavarw
      421 faarraadpa gsmalllrsr kdlsaftgal adhrvpfhvl gtggllqrpe ivdlvaclrv
      481 lhdpaagndl irllvgarwr vgaadvkelh glarwlfsrd hthqrldddv taafrasvav
      541 gehgsivdal dfvatapdeh galaaispag rarmralgqq laalraraag dlvdfvtlvv
      601 qemqldveva aheqgsgafl dafvdelagf vttddradlg aflgwidaaa rrddmgprse
      661 epeagtvqil tihgskglew davavprlve galparpqeg ssgwlgfgrl pyefrgdaee
      721 lprldwrgra sqkevvdaid ayreqvaarn edeerrltyv altrarhdll vsgsfwaggv
      781 rptepsrylr dlveagvvda davpdgtvye edplgtdgav qswphapfgs rgtsvvaaae
      841 rvrnanpgaa grfaadidll laerqaqrsa rhtvaiphrv pasgfkdyla qpdrvaerlr
      901 rpmperpyra trlgtlfhqw veqrvarggs letldawdge ldldpdelga adadaavtdd
      961 darrlatfqe tfsrsrwadr vpvevereih ipflghsvvc kldavyeidg raevvdwktg
     1021 kapsgaddla arqlqlalyr vayaeftgrp vdevdavfyf vaddlevrpt dlldrdgler
     1081 awraalg
//
LOCUS       WP_284601525             649 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Brachyspira
            pilosicoli].
ACCESSION   WP_284601525
VERSION     WP_284601525.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 649)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 649)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 649)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 649)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..649
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75070
     Region          63..617
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mkrfiiyfif asinmlysqt ylirelkggi wvtskveitn ntqtnneysn vskkipinvn
       61 nktitseeie rmgynnakei lenqagfvnk gnymgnevvd paggsadnik iyingvlmnt
      121 akgnadagvd lrripsnlie kieiigssiy ittktpkedi illslsygsy ntiapsilfs
      181 kniddnqift ftadsyysda nyyynftnla gkwikgnied nrqfiinssa nykyifknkn
      241 yinafanisy sssasqyqip pisytdswfn fttlassisy ngfsevldyn inlsylfdsf
      301 vdrpyfkegk fvsdykshgl ainttlkrmd elipntitly nqltpeyryd ilteeknale
      361 tnfnhnpqrh slnikyemql sfgywdnntp iftlmpsiky eyqnefftnq khnnylayna
      421 gfnlnfykgy slyfaymsdy tsptfndlyy gnfsnpnlkp etynqiltki slepitnlki
      481 esaytyttyt nkiiwyssip enadtaishi fsssigydiy fltynkikak ieysyqlayl
      541 neeklpkigl pnnvvtallg ydfvsdgkil sslsfniyyi ysspramtsn ypiyyseefh
      601 nlnisfysiw fkhlifsmhf knilnktpil saysvakpft fefevgynf
//
LOCUS       WP_284601740             329 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Brachyspira pilosicoli].
ACCESSION   WP_284601740
VERSION     WP_284601740.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..329
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36270
     Region          21..328
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mikkiiiifi llilsiitsi cigsvfispk evvsiilykl fnlgfvenin kinivfnirl
       61 phiilslfvg aslsmtgivm qsilknslas vynlgissga gfgvsliivs giyfnyyffi
      121 issilfgfit ilfilfisrk idkdissnsi ilagvvislf fssimsffay afpkysnqii
      181 fwqlgnlfvr nyfdifiiil ltiiflivli knanlldimt fgdketfllg vnpkkarilf
      241 vllsslitgv lvafvgvigf vdlisphiar rlfgakhiiv ipmsaligal ilniadifsr
      301 iiisganipi givtaiigap fflyvfikn
//
LOCUS       WP_284601780             224 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Dickeya dadantii].
ACCESSION   WP_284601780
VERSION     WP_284601780.1
KEYWORDS    RefSeq.
SOURCE      Dickeya dadantii
  ORGANISM  Dickeya dadantii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Dickeya.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Dickeya dadantii"
                     /db_xref="taxon:204038"
     Protein         1..224
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=25100
     Region          9..208
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mttspltfde pqalahlaai dahwarlidg vghirfesrp arepydalir avasqqlsnr
       61 aaaaiigklq qrfavgengf psadqlatce pevlrqcgfs arkidtvkgi aqgvqnglvp
      121 sraeaehldd etlierlctl kgigrwtvem llistlermd impvddlgik qglrylyrlp
      181 qdptrkamle mseacrpyrt laawylwrip hmpdyaeyra slrq
//
LOCUS       WP_284601958             470 aa            linear   BCT 25-DEC-2024
DEFINITION  MBOAT family O-acyltransferase [Brachyspira pilosicoli].
ACCESSION   WP_284601958
VERSION     WP_284601958.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Hofmann,K.
  TITLE     A superfamily of membrane-bound O-acyltransferases with
            implications for wnt signaling
  JOURNAL   Trends Biochem Sci 25 (3), 111-112 (2000)
   PUBMED   10694878
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004295
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..470
                     /product="MBOAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55182
     Region          1..470
                     /region_name="DltB"
                     /note="D-alanyl-lipoteichoic acid acyltransferase DltB,
                     MBOAT superfamily [Cell wall/membrane/envelope
                     biogenesis]; COG1696"
                     /db_xref="CDD:441302"
ORIGIN      
        1 mlfssmiflw lflpvvfvsy ylikieyrnv llliasiify awggvsytli mfssiiinyi
       61 fallidksie ennklkkkiy lalcivinls ilgyfkytdf aisiinsisk keliqlkniv
      121 lpigisfytf qalsyvidvy rehnkaqkni inlalyisff pqliagpivk yhdidtqite
      181 rtenleniny gikrfiygls kkvilanmfa lscdeilkqp igdigtalaw laavlytlqi
      241 yydfsgysdm aiglghmfgf kflenfnypy isksvqefwr rwhislstwf keylyiplgg
      301 nrkgkyftyl nllivffatg lwhgasfnfi lwglwhgffl iiervflgrl leknklklln
      361 hiyvilvfvl gwvlfrannl ahalelyklm fsykesfytl ryffypqtqv cfifgllfsg
      421 ifqslfpkik iaifsskvyl lesiiqfill ficimylvng tynpfiyfrf
//
LOCUS       WP_284601964             381 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal-phosphate-dependent aminotransferase family protein
            [Brachyspira pilosicoli].
ACCESSION   WP_284601964
VERSION     WP_284601964.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Koper,K., Han,S.W., Kothadia,R., Salamon,H., Yoshikuni,Y. and
            Maeda,H.A.
  TITLE     Multisubstrate specificity shaped the complex evolution of the
            aminotransferase family across the tree of life
  JOURNAL   Proc Natl Acad Sci U S A 121 (26), e2405524121 (2024)
   PUBMED   38885378
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Koper,K., Han,S.W., Pastor,D.C., Yoshikuni,Y. and Maeda,H.A.
  TITLE     Evolutionary origin and functional diversification of
            aminotransferases
  JOURNAL   J Biol Chem 298 (8), 102122 (2022)
   PUBMED   35697072
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..381
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41858
     Region          5..381
                     /region_name="PucG"
                     /note="Archaeal aspartate aminotransferase or a related
                     aminotransferase, includes purine catabolism protein PucG
                     [Amino acid transport and metabolism, Nucleotide transport
                     and metabolism]; COG0075"
                     /db_xref="CDD:439845"
ORIGIN      
        1 mrdktflmip gptpvpesal iemakhpmah rskefsnilk evyedlkyvf qtkndvflft
       61 asgtgamcaa lenivnegdk vlclvignfg arwakiaesr gaeviklevp lgevikpqml
      121 eealnknkdi kivtlthset stgaandvkt lcsiikkhga lsvvdgitsl camefktdew
      181 nidvalsgsq kgfmiapgls fltaseeafk mheqckypsf yfnwkehkks lakdttpftp
      241 avslisslht slkmikeegi envnkrhqkl slalraaikt iglklfvedd nnasyaitsi
      301 lppegitvpd irktlkddyd iivangqgsl enkifrigtl gfvcerdlim avgaleasli
      361 klgykfevgs gvkklieeln k
//
LOCUS       WP_284602065             446 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Brachyspira
            pilosicoli].
ACCESSION   WP_284602065
VERSION     WP_284602065.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..446
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=50791
     Region          1..444
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mpkilvidde knirdgikks leyegyevvt aengekgiet vykggidlvi tdlkmpektg
       61 eeflhdilef dkhipviilt ghgnietavd mmrlgaydfm tkpfnidkml liiaralenk
      121 nikktnetle krvdyhesfy gmighsskml kvyeaikqva rtkatvlieg esgtgkelva
      181 naihqisdra kqpyitvnca alsegvlese lfghekgsft gaidkkigrf eaankgtifl
      241 deigeinqvv qvkllrvlee rviervgsni pisvdirvia atnkklseei kegrfredly
      301 yrlnvikiem pplrerredi pllidnfike fsqvhnieit nvdkkvykll sslqwegnvr
      361 elrntvetmv vmskdgkide snipnwvlts stddfvidke mtleelekky inhllsknnf
      421 nkaqvakilg ieratlyrkl kdynvd
//
LOCUS       WP_284602093             326 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Brachyspira
            pilosicoli].
ACCESSION   WP_284602093
VERSION     WP_284602093.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..326
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38298
     Region          4..323
                     /region_name="PobA"
                     /note="Chlorophyllide a oxygenase/letal leaf spot protein
                     [Coenzyme transport and metabolism]; COG5749"
                     /db_xref="CDD:444459"
ORIGIN      
        1 miynmwygvl dskeikknkp lfakrlnknl vfwrdennni cciedkcchr gaslshgkvc
       61 gnniacpfhg fqfnkngkvv mipangkntq vderffvesy evrelygliw lwygdkdkin
      121 dkimfpddlk dkkfsystir dewhnhytrc ienqldvvhv afvhyntigk gnktlvngpl
      181 velnedtntl kfyvnnvidn gqkalsasem kkedfkyfly fyfpniwqny ifekmrvfaa
      241 fapvddentv vyirfyqkvv nipiiknivn figkkfsayv lkqdkdvvkt qsskesylgm
      301 keeklipgdm piiiyrshrd klkkei
//
LOCUS       WP_284602168             620 aa            linear   BCT 25-DEC-2024
DEFINITION  IucA/IucC family protein [Dickeya dadantii].
ACCESSION   WP_284602168
VERSION     WP_284602168.1
KEYWORDS    RefSeq.
SOURCE      Dickeya dadantii
  ORGANISM  Dickeya dadantii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Dickeya.
REFERENCE   1  (residues 1 to 620)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..620
                     /organism="Dickeya dadantii"
                     /db_xref="taxon:204038"
     Protein         1..620
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=70328
     Region          6..587
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mnnrnhdvls rmisekaalh gllnclikef aipegylrye wpdemkgipp gayfdgadwk
       61 gipmmiglpd qlqlfvmvdr rdtfgsqhyl sdvylrqaqg dwqcpdfepl varllaaceh
      121 iagrknpely eqilqsqrlv saivshngrq radaplqhyl qseqglwfgh pshpapkarl
      181 wpahlgqeqw apefqaraal hqfevpvdgl higangltpq qvldgfadqq paspghaiic
      241 mhpvqaqlfm qdarvqqllr dnvirdlgqs grvasptasi rtwfiddhdy fikgslnvri
      301 tncvrknawy elestvlidr lfrqlldqha dtlgglvaaa epgvvswspa aagesdshwf
      361 reqtggilre nfcrrtgaer simagtlfar gvdlqpmiqt flrthygevl ddnallywfd
      421 dyqtqllrpv lslffnhgvv mephlqnsvl vhqqgrpqqv llrdfegvkl tddlgirqip
      481 ddihprvrqs llysreqgwn rimyclfinh lsetilalsq grpqlaplmw rrvqqqlrai
      541 qaelkqpspe ldaliaghpv acktnlkvrl aaeadrqasy vrlpspwgha vqhgsesqhd
      601 errhgdvrhe evrhgevqhg
//
LOCUS       WP_284602171             258 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Dickeya dadantii].
ACCESSION   WP_284602171
VERSION     WP_284602171.1
KEYWORDS    RefSeq.
SOURCE      Dickeya dadantii
  ORGANISM  Dickeya dadantii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Dickeya.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Dickeya dadantii"
                     /db_xref="taxon:204038"
     Protein         1..258
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27509
     Region          2..239
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mlrtnqlkrk laagtpvygl iasipspvsv eliaeagfdf viidtehvli npetvenmir
       61 vaesyaltpl vrvadanpkt mlrlldggaq givlpmveqv dqvraavrac hyhpqgersl
      121 nsgrpgafgk hslaeyvala nreimlvami esaegvrqae aiagvagldm ilegaadlsq
      181 slgmpwqtaa apvqaalaev rraadahgvt ycaiprqhdd harwreqgvh afvlgdergi
      241 afralqarla atisaegk
//
LOCUS       WP_284602141             584 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Dickeya dadantii].
ACCESSION   WP_284602141
VERSION     WP_284602141.1
KEYWORDS    RefSeq.
SOURCE      Dickeya dadantii
  ORGANISM  Dickeya dadantii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Dickeya.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 584)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 584)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Dickeya dadantii"
                     /db_xref="taxon:204038"
     Protein         1..584
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64500
     Region          9..584
                     /region_name="COG4986"
                     /note="ABC-type anion transport system, duplicated
                     permease component [Inorganic ion transport and
                     metabolism]"
                     /db_xref="CDD:444010"
ORIGIN      
        1 mhhplqnimt dqamrpirrh aapsyradml fftllalvta lvvygmeqms lplsildasp
       61 vrldiallpe yalrttlrmf valgvsllft lviatlaaks rkaemviipa ldilqsvpvl
      121 gfltftvtff mglfpgrqlg vecaaifaif tsqawnmafs ffqslrtlpg dlsevsqqfg
      181 fspwrrfirl elpfatpglv wnmmmsmsgg wffvvaseai tvgnttvnlp gigswlalai
      241 aqenltaiaw avvamtvviv lydqllfrpv vawadkfrfe qtasqkrprs wvydlirrth
      301 istaianvlg wplhalaalr wprlppflrh tpgpryskit drlwlalvii gvlagvvqlv
      361 qyigaslgma dviavfsmgl atlarvvvli alasviwlpi gvwiglqpsv aerlqplaqf
      421 laafpanvlf pfaviliagf nlnpdiwlsp lmvlgtqwyi lfnviagaaa lptdlleaar
      481 iygirrwqww rqvalpgifp yyvtgaltas ggswnasivs esiswgkqhl eatglgayia
      541 nattaadfpr valgiavmsv fviafnrllw rplyqfaerr lrlg
//
LOCUS       WP_284602200             344 aa            linear   BCT 25-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Dickeya dadantii].
ACCESSION   WP_284602200
VERSION     WP_284602200.1
KEYWORDS    RefSeq.
SOURCE      Dickeya dadantii
  ORGANISM  Dickeya dadantii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Dickeya.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Dickeya dadantii"
                     /db_xref="taxon:204038"
     Protein         1..344
                     /product="isopenicillin N synthase family dioxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38287
     Region          2..321
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 msqpaslpvl dfslldgnar qradflqrln haaretgffy lthhgvdlel qqrvqrlsra
       61 ffalpdaekq rvamirsphf rgytfagaer trsepdwreq fdvgaerppl rllsgdpawr
      121 rlqgpnqwpa slpelkiall ewqqtltris lrllrafaev lglpitafda lygnkpsehi
      181 klirypgrat adshqgvgah kdsgfltlll qdqqsglqve vepdhwvdah plagsfvvni
      241 gellelatng ylratvhrvv sppasqerls vafflgaqld avvpvfplsp alaklargpa
      301 sdpnnpllre vgwnylkgrl rshpevakry ygdvvqaqqq avta
//
LOCUS       WP_284602269            1183 aa            linear   BCT 25-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Dickeya dadantii].
ACCESSION   WP_284602269
VERSION     WP_284602269.1
KEYWORDS    RefSeq.
SOURCE      Dickeya dadantii
  ORGANISM  Dickeya dadantii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Dickeya.
REFERENCE   1  (residues 1 to 1183)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 1183)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 1183)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 1183)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1183
                     /organism="Dickeya dadantii"
                     /db_xref="taxon:204038"
     Protein         1..1183
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=129027
     Region          <1..1051
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 mfintlplrl tlaqqgvlev vhgayrqlmv lleheqapls laqrcsgvap llplfgslln
       61 yrhsraaeal qawegmrmqy feerthypfa lfvddlgqdf sltaqcvsai dparlnayml
      121 tamtgllqal asdprqqils ipilpdaerr hllvgfnatq aafpqetllh qlfegqvgqt
      181 pdatavvfdg qslsyaelna ranrvahsli slgvqpderv avcaerslem vvgilailka
      241 ggayvpldpa ypsarlayml adakpvallt qralqanlgs glptllldad mgstdsdnpv
      301 vpglsarhla yviytsgstg qpkgvmveha svvnflssmt tqpglsandk llalttlsfd
      361 iaglelylpl irgaqcllvs hetskqadkl cgmierlrps viqatpstws mllqqdwipg
      421 aglkvlcgge amsstlrqql iasaaevwnl ygptettiws ltsrvlsmeg tlsigrpian
      481 triyildphg qpvpvgvrge ihiagagvar gylnrpelta arfladpfag qpgarmyrtg
      541 dlgrwlpdgt ieylgrndcq vkirgfriep geieaclvqc agvreavvia redspgdrrl
      601 vaylvaeagi lpepaglrqa laqqladyml psafvrldal pltpngkvdr kalpapddsa
      661 fvrtgyeapq geteqalaai wqsllgierv grqdhffelg ghsllvvrli aalqsqglnv
      721 pvravfehtr laelattier feqtaipenr itadsqritp amlplleltq edidrivssv
      781 pggvrqiqdi ypltplqegv lyhyllaesh dpylnsslla fatrqrleaf iaslnrviar
      841 hdilrtavrw eglpqpvqvv lrraeltatq vhlsptagda adqlfsmkpc rldlrqaplf
      901 nllmandean drwllclqyh hlcldhttla ilfdeihade rgerdqlsas ipfrnhvaqv
      961 raraaatddk affhqqlaev eeptlpgglt alvdmdeail plpdtlvgri rrqaqqegis
     1021 aaslfhlawg hvigalsgrd dvvfgtmllg rlqdgreqal glfintlplr ltladitvra
     1081 aldqthrrlt dllahehasl tlaqqcsgva asqplfsall nyrhdvtpan adaaedpwpg
     1141 iellkveert nypltlsvdd alhagfslkv qadrrlggng sdr
//
LOCUS       WP_284602479             320 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Brachyspira
            pilosicoli].
ACCESSION   WP_284602479
VERSION     WP_284602479.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10648172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..320
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38138
     Region          263..314
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mnyvfnylll ifyllsfvig fstifysivy yiiervlwlk yyiiflftfg ilifirtirl
       61 itlltlpsft snnifnmlyf filtlamalm lyfipaflyr flkikwsikt nlsylilsvf
      121 yfvlsiigil tsfniyilss mifyisifyl lvvgflnykn iedktikfiv kvlgiitili
      181 ypvliyqlii yrkdfmnins idvtlmlfyt wwnlvmlgyl lwyfismiks nnnrisdslc
      241 ekndesynni kleekievnd fnltkrekqi lsyllsgktn keislifdis lntvnnhvan
      301 iyyksgvknr velvnkfsky
//
LOCUS       WP_284602582             437 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Dickeya dadantii].
ACCESSION   WP_284602582
VERSION     WP_284602582.1
KEYWORDS    RefSeq.
SOURCE      Dickeya dadantii
  ORGANISM  Dickeya dadantii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Dickeya.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Dickeya dadantii"
                     /db_xref="taxon:204038"
     Protein         1..437
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47860
     Region          32..399
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mninalplda ningwsamlp prvakpalrq sitadwlvig agyaglafar riaenrpheq
       61 vvvldavdvd dsasarnsgf aidlphnigs staelekaan yrrllhagla qletliaryg
      121 idcdwnrhgk yhcivrpeln glleqythel qalsepyqll qgdalarklg tsyyhaaiht
      181 pncvllnpaa lvrglvdslp dnvtlyersp aleiqpgktv rvrtpygevr arqlmvatng
      241 carqlpmfsr qvvglstfat ltepltaeqq qrigqidewg mtpanaiaga tlrytrdhrf
      301 lirqhvtyvp sytvtscyta eitrrhqaif lsrfpqlaev siahtwsgmi svtrngapgw
      361 gkysdnlhaa vgcngagisk qtiagstlad latgidnpli admqalgqps yipprplldm
      421 gvrgsilker wlgrkey
//
LOCUS       WP_284602811             428 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Brachyspira pilosicoli].
ACCESSION   WP_284602811
VERSION     WP_284602811.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..428
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48863
     Region          1..421
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 menindaldy lysfmnkknl hkknnnhisn venilnilgy kqnfkiihit gtkgkgsttl
       61 slahmlsacn yktgafisph iinererisi ndewisendf isivkkiknv ieenkldesi
      121 tvfefftiig lyyffinkvd yacievgigg rfdctnivns sisiltsisy dhvdilgnti
      181 eeityqkagi iknnsivisa mqeknsieii envskeknst lytfgkdfys niikntseil
      241 efdyiekenk yhftttllge hqsenialsf kaftlleskk enikkaidsl rnfnikarlt
      301 fiernpdiiv dgahnaksls rilktiykwy dsvvilfapi sekdvggmce vlkenkdiii
      361 issakskykd snsfktyeyl rekenvyhie sfdlaveemk kiskeknipa lvigslysas
      421 dyiisqdg
//
LOCUS       WP_284603003             338 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Brachyspira pilosicoli].
ACCESSION   WP_284603003
VERSION     WP_284603003.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..338
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=38192
     Region          <92..279
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mfiedfkfvf lfviipvlif flvtsrfkvn rvlsvftknt nfkndknykr isklrifsas
       61 flilalslsi falmqpkwgi ieqkiktnny mitilldlsr smeaddvwps rlerakleie
      121 dfvkntdnls valvgfagts fvaspftqdm etfsyilnel ntksvtlqgt riadalvtak
      181 ntfnvnipgk ksiilitdge dhagyfdnil kelkdndisv ytvgvgselg atirsdigys
      241 entviskrdd ktlkliadst ggksyisdni slksifddik nnmdsvstmk nnrsykdrfq
      301 iflfastili iiasilnift qkrvlyknnk ssiikdik
//
LOCUS       WP_284603007             225 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Brachyspira pilosicoli].
ACCESSION   WP_284603007
VERSION     WP_284603007.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18798650
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..225
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=26255
     Region          <37..101
                     /region_name="TadD"
                     /note="Flp pilus assembly protein TadD, contains TPR
                     repeats [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG5010"
                     /db_xref="CDD:444034"
     Region          60..90
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          165..>224
                     /region_name="YgiM"
                     /note="Uncharacterized conserved protein YgiM, contains
                     N-terminal SH3 domain, DUF1202 family [General function
                     prediction only]; COG3103"
                     /db_xref="CDD:442337"
ORIGIN      
        1 msikkiiimf lvfgcnfifa qndleninni fknandlynq gsyieannly lnlissnvvs
       61 kdlyynlass yyeinsngya vlwyeralni spfdkeiknn inkiterkdy dsfyiiafyi
      121 slilfvffsa flfvlfikkk ninflllisc villvfsiyl yktiksdyii iirntniysg
      181 ssiksdivss vyegekfrvi kessnwyyvk giskgwinke dleki
//
LOCUS       WP_284602847             514 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Brachyspira
            pilosicoli].
ACCESSION   WP_284602847
VERSION     WP_284602847.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..514
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56610
     Region          31..496
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mkkisiillm iffallscnn ntakkstnsg eltiihmndt hgrdeeemiv nkevtppetn
       61 ymygaarras yikdvektnn nvlilhagdt itgsvystvf mgrdevdimn migvdaaaig
      121 nhfvdygldn ftaimkerkf ptlsiniknk ednsyyalpy ivtnvnglnv aiigitttds
      181 vynpkyvegl vfekeidslk sflkstplnt tnditillsh vgyegdkkia eafpktfdvi
      241 vgghshtvle eadivngtpi vqagyygryl gqidlsvnsg kiekfnykli pmdgnieqda
      301 dmlafidemk gtvdkefnvr igtlpvellh dgirsnsmai gnfacdlvld sydnldmvlm
      361 nsgglrtplk kgditlgniq neffpfdnev vlvtltgkdv iemlkisgqk rgagaflqls
      421 rgmevkynan gellsaaldg enidetkdyt valssfvflg gdgyqdsegk aigekgkniv
      481 mtgndmrdam iakikelnni pesyidnnpr vife
//
LOCUS       WP_284602945             495 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Brachyspira pilosicoli].
ACCESSION   WP_284602945
VERSION     WP_284602945.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 495)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 495)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..495
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58562
     Region          1..481
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 mlvkfsveny ksiydkveld frikpkntvd eeninnnpfv fkikddyisk lclfyghngs
       61 gktnifeail nlclsnidnh flddiykpnm iygeneeskf eiefysnils enksdyslyn
      121 yklnvknkei ddeykksiqi tkeiftengk ivfertnndl iknsitndkn itipsdetfi
      181 lflmdiytke kkefdyilky kslmssllqn digvknyllt pdltnmlfqd iynnlyelnl
      241 lnfyieliki advgiddikf eldlqnkkif eefksiitne iikdnndsdn aiknylndvi
      301 klddekekdl allisnilef tmkyvikfnd nlkeyfdknk iafsyrkkwk epfaniesdg
      361 tkiyafhmyn ivkslksgsl slhdefygvq pdliktvfll frkdmykeve qtaqlfmtth
      421 dimlmdfkyl lleqvkfvvk eknktyvysa sdiegltken lienyennkl gakyfprpyd
      481 lpikmyskvm msdkl
//
LOCUS       WP_284603040             469 aa            linear   BCT 25-DEC-2024
DEFINITION  rhamnulokinase [Brachyspira pilosicoli].
ACCESSION   WP_284603040
VERSION     WP_284603040.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167330
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..469
                     /product="rhamnulokinase"
                     /EC_number="2.7.1.5"
                     /GO_function="GO:0004370 - glycerol kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008993 - rhamnulokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006071 - glycerol metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0019301 - rhamnose catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52875
     Region          6..463
                     /region_name="ASKHA_NBD_FGGY_RhaB-like"
                     /note="nucleotide-binding domain (NBD) of rhamnulokinase
                     (RhaB) and similar proteins; cd07771"
                     /db_xref="CDD:466791"
ORIGIN      
        1 mtskiysiac dfgssggkif lskfendkmt leevhrfsls pikinnyyyt dfiymynell
       61 rgikkvvdmg iqpsslgins wgvdygyldk ngellsnpln yrdtrtidti kklekiglsa
      121 kelykitgis cmpfnsimqi yediqgrani vnnaskllft pdlfgyfltg nisaeytiss
      181 tsqlidinkk ewskeileki nfdinklpsl qepgskkgll kqeiadylgc kpfdiiavas
      241 hdtasavlsa pifddntayl ssgswsllgv elkeavltde afengftnem gynntirfle
      301 ninglwtiql lqkkyqisfn dmeqlardni kdkhridind nrfynpkdie deilnyykdt
      361 nqaniekdkk gviiasvyns laesyakyin slkkllnkdi nklcivgggt kdkliceltk
      421 ektnltvsvg pvectatgni laqfkalgvl kdtnemrklv vnsfdikqi
//
LOCUS       WP_284603014             569 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein [Brachyspira
            pilosicoli].
ACCESSION   WP_284603014
VERSION     WP_284603014.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Porat,A., Cho,S.H. and Beckwith,J.
  TITLE     The unusual transmembrane electron transporter DsbD and its
            homologues: a bacterial family of disulfide reductases
  JOURNAL   Res Microbiol 155 (8), 617-622 (2004)
   PUBMED   15380548
REFERENCE   4  (residues 1 to 569)
  AUTHORS   Kimball,R.A., Martin,L. and Saier,M.H. Jr.
  TITLE     Reversing transmembrane electron flow: the DsbD and DsbB protein
            families
  JOURNAL   J Mol Microbiol Biotechnol 5 (3), 133-149 (2003)
   PUBMED   12766342
REFERENCE   5  (residues 1 to 569)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   6  (residues 1 to 569)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   7  (residues 1 to 569)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   8  (residues 1 to 569)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   9  (residues 1 to 569)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18120940
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..569
                     /product="protein-disulfide reductase DsbD family protein"
                     /EC_number="1.8.-.-"
                     /EC_number="1.8.1.8"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=63752
     Region          30..132
                     /region_name="DsbC"
                     /note="Disulphide bond corrector protein DsbC; pfam11412"
                     /db_xref="CDD:463273"
     Region          168..542
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 mrkiyiflfi ifsltaysqs fnsllnknte aiivfslstn nnkitvkani pegyyayles
       61 kiankilffa dnkeinttyp kgekyhedii ikgeqefiln didinkinfi kttyqlcsak
      121 dnvclqpqsk viygeeidip nnnvtdekpe nassienyik gsnnifitli lifaaglasv
      181 llpctyplls itvsilgttt deknnkkssv lasllfalgv ittytllgav vsvagfafhk
      241 tilfgsigyn pivltilvll flyftfsmag fyeikapsfl qsaktnayak knqsifhkyt
      301 mgllagivat pcaapiiavi leigflnpvf atlymavyal gfasvlfvlg tfasiltkmp
      361 kagtwmvyvk yiftflmmii sfyyanilfg vlgfnkisyi lasvtilvfa llvyiiknkt
      421 amlsslekki fvsvliisia lgsiygiikq ksevsntisy tealelskqn nkpilidfsa
      481 vwcancyelk ekvfvneelk kliddnlift evdvdkykni sdeynvkwlp wiividrdkn
      541 ilytknsfss fddkmalsik edleevink
//
LOCUS       WP_284603239             491 aa            linear   BCT 25-DEC-2024
DEFINITION  MBOAT family O-acyltransferase [Brachyspira pilosicoli].
ACCESSION   WP_284603239
VERSION     WP_284603239.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Hofmann,K.
  TITLE     A superfamily of membrane-bound O-acyltransferases with
            implications for wnt signaling
  JOURNAL   Trends Biochem Sci 25 (3), 111-112 (2000)
   PUBMED   10694878
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004295
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..491
                     /product="MBOAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57932
     Region          1..491
                     /region_name="DltB"
                     /note="D-alanyl-lipoteichoic acid acyltransferase DltB,
                     MBOAT superfamily [Cell wall/membrane/envelope
                     biogenesis]; COG1696"
                     /db_xref="CDD:441302"
ORIGIN      
        1 mlfnstdfli ffpitlilyw ifpkklryic lfiasyifym fwnpkyallm atstvvtfls
       61 gilieklkyk rivvafsfii niailvffky fdfllqnini llaalniqli ekpfdivlpv
      121 gisfytfqal sytidvyrge iksekniiky alfvsffpql vagpierskh llgqiqnmdk
      181 ikrfdyqrit eglilmlfgy fqkmviadra silvdtvfnr yyiyntselv lsallfavqi
      241 ycdfasysli aigtakimgi dlmenfntpy farsikefwg rwhislstwf rdylyiplgg
      301 nrcskfrrsi nilitflvsg lwhganftfi awgaihgvcy lieditskfk nnvlsklnvk
      361 vksfsfklle viitfiivdl awiffraeti hdafyyierm ftkidlwrif dgslyklgld
      421 rfemniliis lvvlflvdli kyikketiym flknqclyfr waviffllff iiiygkygag
      481 fdpkqfiyfq f
//
LOCUS       WP_284603297             758 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Brachyspira pilosicoli].
ACCESSION   WP_284603297
VERSION     WP_284603297.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 758)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 758)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 758)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 758)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..758
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..758
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=81754
     Region          1..757
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mkmtlkiggm hcaacsrave ralkktdgie eanvniatek avfnydekkl kyddivnvvv
       61 kagyqvlgke edpavvkare ikeqkirliv saifsiplfy ismapmvsfv kfpipsflvh
      121 hinpqvfsiv aiflcvpvmi sgykfytlgf palfrgspnm dslvaigtta aftysiystv
      181 lsfmglnphg dnlyyesaav iitlvqfgky learskgktg eaikklmglq pktatiikdg
      241 eekeikisdv kvddivlvrp gekipvdgei iegyssvdes mltgesipve ksvgdkvvga
      301 sinktgsfkf kaqkvgadta laqiiklved aqgskapiah iadvvssyfv pavitialis
      361 giiwfialhn fvfsltvfvs vlviacpcal glatptaimv gtgkgaelgi lfknaealev
      421 sqkinavmfd ktgtltegkp yvtdiisddk dkllliaasa engsehplge aivreskekn
      481 ikllsienfk aisgfgiety idnkkvlmgn dklmnkenin ienynsymdk lskegktpmy
      541 vaydnkllgi iavadklkke sieainrlhk lgiktamitg dnkntansva keagidivfa
      601 evlpeeksne vkklqeqgft vamvgdgind apaltqanvg iaigsgtdva iesadivlvk
      661 sntndvvtai elskatmrdi kqnlfwafcy nvigipiaag vlhvfrepli assiggflta
      721 imgkdlllnp ifaalamsls svsvvtnalr lnffkpsk
//
LOCUS       WP_284603289             430 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Brachyspira pilosicoli].
ACCESSION   WP_284603289
VERSION     WP_284603289.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469162
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..430
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=50049
     Region          346..>424
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          352..376
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          381..414
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkrlknnkly llltlvlvaf aylytsliaq tssdrisien yndlpnsrrl vtklnikhie
       61 enkvevswvg iyhpnlmyyv yrsedpilsk tvltnakvva stkatnastt ytiydnlpky
      121 dkyyyavisy idninfytat enmdlmqfey ydpfkndmtn inneintnei itnniitndi
      181 itndiitndl ntnntyftnd mltnivssnd flsyypntnl fdtnytilpp tnyvdlyytt
      241 nridsnrgiv fstnyynytn yynltnnytn yynttkiyii nptndsltne intndfvtnd
      301 ftnqsrmven vtnelkvtsf tndknenivn veikkdntkk tpteyqryss eyqralaqfk
      361 annyagaiki lepisrkkvd salyydinll lgksyksagr kknaldtlkk iksinpnevn
      421 fwinqvlsdl
//
LOCUS       WP_284603306             328 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Brachyspira
            pilosicoli].
ACCESSION   WP_284603306
VERSION     WP_284603306.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..328
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38441
     Region          4..325
                     /region_name="PobA"
                     /note="Chlorophyllide a oxygenase/letal leaf spot protein
                     [Coenzyme transport and metabolism]; COG5749"
                     /db_xref="CDD:444459"
ORIGIN      
        1 miynmwygvl dskevkknkp lfakrlnknl vfwrdennni cciedkcchr gaslshgkvc
       61 gnniacpfhg fqfnkngkvv mipangkntq vderffvesy earelygliw lwygdkdkin
      121 dkimfpddlk dkkfsystir dewhnhytrc ienqldvvhv afvhyntigk gnktlvngpl
      181 velnedtntl kfyvnnvidn gqkalsasem kkedfkyfly fyfpniwqny ifekmrvfaa
      241 fapvddentv vyirfyqkvv nipiiknivn figkkfsayv lkqdkdvvkt qsskesylgm
      301 keeklipgdm piiayrshrd klkklnnk
//
LOCUS       WP_284603440             559 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Dickeya dadantii].
ACCESSION   WP_284603440
VERSION     WP_284603440.1
KEYWORDS    RefSeq.
SOURCE      Dickeya dadantii
  ORGANISM  Dickeya dadantii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Dickeya.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Dickeya dadantii"
                     /db_xref="taxon:204038"
     Protein         1..559
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=61321
     Region          12..545
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mdkhdailpt tattpvlavk dysldyalpd gshlpvlrdi tlhvnrgdvl glvgesgsgk
       61 ttlgwaimrw lagnaverag dihlgelnlr tlavdklhal rggklgmifq dpsaslnptl
      121 tlgeqvtevl rrhrrlnare aqeyaetllr dvdlknpalm mqryphqvsg gekqriliat
      181 afacqpdcli fdepttaldv isaaqilalf erlreetgva alyishdlal vsrvtdrvcv
      241 lekgriveqa dasalfsmpq haytrrliaa vpnpavrlld etapssqpll tlsditiqyg
      301 hhrlldkllk rqsnqtraan avsltvhege ivgivgesgs gkstlakavt glvpfsgkld
      361 frgytlfgrt qmdkdyrrrv qmifqhpdas lnprmligdi iarplrlygl pngetetqav
      421 arlleevrlp asmasryphe lsggqkqrva iarafahppe lvicdeitaa ldvsvqatvi
      481 elllelrrry gtaylfithd lnliqqiahr iavmyrgdll eilpghamas qaqhpytqal
      541 lsaiptpgdl spashsyte
//
LOCUS       WP_284603472             320 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus faecalis].
ACCESSION   WP_284603472
VERSION     WP_284603472.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..320
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=37084
     Region          96..310
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 maskeeqyaa fyqfletldc yltttnalen evaqfkenph reiagfmlas setidvpkgf
       61 irmlycleqd gnayldqqrc svsagqvmiv neatsvsyqg qgmsmiifyf kkhyfldtll
      121 nqlaeepvmy lffteiasse fenipryfvf asqpnsdvhv ysllllkqiv kmayfnnkvt
      181 kaafvllvve lgqlprealk mqdnylsnhq rvevilayie qqiahvtlae vaakfhfhpn
      241 ylsnflkdkt nktfteivla yriqlaknyl kqtdlsiqti verigyqdka ffykrfkeem
      301 gmtpkqyrqk egmadvrrsl
//
LOCUS       WP_284603709             560 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Dickeya dadantii].
ACCESSION   WP_284603709
VERSION     WP_284603709.1
KEYWORDS    RefSeq.
SOURCE      Dickeya dadantii
  ORGANISM  Dickeya dadantii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Dickeya.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Dickeya dadantii"
                     /db_xref="taxon:204038"
     Protein         1..560
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=60999
     Region          11..554
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mslplslqss tttpvleled vaiayrgddg ertvvegvsf aiqpgevval vgesgsgktt
       61 taqaviglla dngrltrgai rlngadisrw sqprldsirg rvvslvpqdp gsslnpvkti
      121 geqvdeilrl hqksdrhslr rqtlalltrv gltepelrag qyphelsggm kqrvliaiai
      181 alkpaliiad eptsaldvtv qkrildllde lrrengtail fvthdlgvaa eradrllvfq
      241 kgyiqeqgpt qqvlsapqsq yartllanip slaparrpsr aaasgqpisc esipsqpipc
      301 elivqveqlv qefppagnrk qpfravdavs fsvapgttha ivgesgsgkt ttarmilgfq
      361 rptagrilid gtditrlrge alrqfrqtiq lvyqnpfssl dpsqrlfdiv eeplrnfnry
      421 araeranrih eifervalpa sllqrrpael sggqrqrvai aralvlapkv lvldeavsal
      481 dvtvqaqilr lleelqaslg ltylfishdl avvrqiadtv svlyhgkqve sgpveqifaq
      541 paerytreli daipgqrhvs
//
LOCUS       WP_284603724             252 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Dickeya
            dadantii].
ACCESSION   WP_284603724
VERSION     WP_284603724.1
KEYWORDS    RefSeq.
SOURCE      Dickeya dadantii
  ORGANISM  Dickeya dadantii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Dickeya.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Dickeya dadantii"
                     /db_xref="taxon:204038"
     Protein         1..252
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=27808
     Region          <51..184
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mssisscrwd dltartwpyp hcvvvpraql acqtivaqar qacgvppdav lasrqlaegm
       61 lrillaplcq qeaaalrfer nphgkpflpq hptiqfnlsh thsafafafa rhspvgvdve
      121 scqghvdrkr svarrffhpd eirwldafdd arflpaftcl wsrkeayika lglglhksla
      181 sfscladgqg airvtdagqi sdcrldeawi agepsvalsy cllpaksaep dawrllilrd
      241 dapedraslq qp
//
LOCUS       WP_284603872             208 aa            linear   BCT 25-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Corynebacterium
            propinquum].
ACCESSION   WP_284603872
VERSION     WP_284603872.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Niehaus,T.D., Elbadawi-Sidhu,M., de Crecy-Lagard,V., Fiehn,O. and
            Hanson,A.D.
  TITLE     Discovery of a widespread prokaryotic 5-oxoprolinase that was
            hiding in plain sight
  JOURNAL   J Biol Chem 292 (39), 16360-16367 (2017)
   PUBMED   28830929
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Fan,C., Li,Z., Yin,H. and Xiang,S.
  TITLE     Structure and function of allophanate hydrolase
  JOURNAL   J Biol Chem 288 (29), 21422-21432 (2013)
   PUBMED   23754281
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Wang,L., Grau,R., Perego,M. and Hoch,J.A.
  TITLE     A novel histidine kinase inhibitor regulating development in
            Bacillus subtilis
  JOURNAL   Genes Dev 11 (19), 2569-2579 (1997)
   PUBMED   9334321
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005226
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..208
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=22368
     Region          4..205
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 mlipygdrgl lidfsdhddp lgqvlayqaq lerdnldavv dlipaahtll iafdrnpnei
       61 tlpeldsaas tsetgaanti evtydgadld eladdlgltp aelikahtet twtaafagfa
      121 pgflylrpdq esphaqvfad isrrsqprts ipagsvglag gfsavypqss pggwqligst
      181 eermwdldrd qpallqpgdt vrfqektc
//
LOCUS       WP_284603979             302 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Corynebacterium propinquum].
ACCESSION   WP_284603979
VERSION     WP_284603979.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..302
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31811
     Region          28..302
                     /region_name="COG4132"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443307"
ORIGIN      
        1 maadfsqqei tetnssatgp kakrvsnrgv alatllplgt vlalfflipi vgmaitsfqd
       61 gttgdftwan yeamtegnra qallnsllvs lysssialaa gtliafcisf lnskilnsit
      121 avvssvlans ggaplafsfi vlagntgyli smllaidssf slytvkglvl myqyflipmv
      181 vllllpsfqa mrtswkeant slggsawtfw rrvglpiltp tilgvwilef gaafathass
      241 avligtgtfp livlqistem sgsaasggeh iamamglstt aiaivtliaf nwlqnrsqkw
      301 lg
//
LOCUS       WP_284604100             612 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD/NAD(P)-binding protein [Enterococcus faecalis].
ACCESSION   WP_284604100
VERSION     WP_284604100.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 612)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11816065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..612
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=69150
     Region          1..586
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
     Region          4..182
                     /region_name="NAD_binding_9"
                     /note="FAD-NAD(P)-binding; pfam13454"
                     /db_xref="CDD:433222"
ORIGIN      
        1 mkiaivgagp rglsaaervi ewarkteinv qltlfdpygp ggkiwraeqp nyllmntvis
       61 qvtlftdesf sgegpivkgp tlyewtqtea aqyiqqqqpy nylellkech rlgpndhcsr
      121 afygmyqkwf ytylatrcne qtsltffkep vtavragedn yyvytqsief tadkvilalg
      181 hqenelttve qeladyakeh rlfysspkna adallalani pakqpvvlkg lglaffdyls
      241 altigrggvf srqngrlrye psgrepiiia gsgrgfpshp rgnnqkgyge tyqpvfltet
      301 ylaecrkkgq vtgaeffgyl kkeveyvyyt clieekyphl skdafqqlfi qtkgapesla
      361 hfekqdwfdw qalehpetkk tthesfrsfl leylkwdiqe aekgnlsgpl ttaldslkdl
      421 rdqirfvlde glltndesqk wlwhwftpln tflsvgpsve rteelqalve lglvtilgpe
      481 mrvemkagqf ityanlfpen rynshfliea ripkvnneks lnpltrqlla dklatlhqla
      541 ladgqivktg allivpatnq vitkdgqvat glfscgipte gihwltaaaa rpgvdpwnmr
      601 dmdriaatif ns
//
LOCUS       WP_284604122             330 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: AAA family ATPase [Bdellovibrio].
ACCESSION   WP_284604122
VERSION     WP_284604122.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..330
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36403
     Region          21..318
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 msevdimaln aaikqesqfi ekmmaeinkv vvgqkemveg immglltggh illegvpgla
       61 ktltiatvsk sisldfqriq ftpdllptdl igtmifnpks gefaprkgpi ftnivladei
      121 nrapakvqsa lleamaekqv tigdvsykle apflvlatqn pleqegtypl peaqmdrfmf
      181 kinvvypgkg eeleilnrmg tndkpvvnsv iskedllras qradqiyvdn kiknyiveii
      241 masrkpgeyg lsrianlinv ggspratisl yraakahafi rgrgyvtaed vkaiayhvmr
      301 hrliltyeae aeniktddii keilsqvevp
//
LOCUS       WP_284604159             139 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ExbD/TolR family protein [Bdellovibrio].
ACCESSION   WP_284604159
VERSION     WP_284604159.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..139
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=15065
     Region          3..139
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mgmsnggggk sratlseinv tplvdvmlvl limfmvttpl mqqgievdlp ktsssgveln
       61 eepfvlvigp dqkmtiakqk iamgdirtkl kaifehkknk qvyiqadrkv dygfvaeama
      121 evraagifni glitqpkdq
//
LOCUS       WP_284604241             262 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: substrate-binding periplasmic protein [Bdellovibrio].
ACCESSION   WP_284604241
VERSION     WP_284604241.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..262
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=30394
     Region          27..250
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mtklaliffc wslgflpqvy akncerrfri sinnqppvyf assqgakgls vellrevesr
       61 lncpfhlepv diprayedfk syrsdmyafs gpdlnwekyg nyiplykaar llivsksvyv
      121 pgkkilgylk dpkikfvdht ggrffylphe tleleeqgrl vrrpspaliy dylingkaqa
      181 sfssptfqky ysetkkfgdk ivairdpesr feigmytskk rvsaveveki kkivrqmqed
      241 gtlrkivsry vqpedlvyyq dl
//
LOCUS       WP_284604364             247 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: substrate-binding periplasmic protein [Bdellovibrio].
ACCESSION   WP_284604364
VERSION     WP_284604364.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..247
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28320
     Region          26..226
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mnvikffpll vllllfspra qaerwviatl ewppficsrc pdngaaanal retlkkvdvn
       61 vefvfsswtq tvkkgnrpdm igyfpawkee vlpefiaspv lfrsplgfie prgkplvwne
      121 ltdlrgkkig vtedygntve fnrlvknkti hveavisddt nvrkvalgkl daalmdinna
      181 ryliyvlqph lagrvsinkk ivedkelffa fnkhnvekrk klekaltlvn fqrmvddyll
      241 ryarrsd
//
LOCUS       WP_284604524            1175 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284604524
VERSION     WP_284604524.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1175
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..1175
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=124903
     Region          244..390
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <646..1119
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 msvkstsprn hrgggernka ranstrpapr trsgrtagkk lssgmpektg gdpaksreen
       61 sdsanletvv fgsaqraant shertgsafr avgsgiataf sktsgalkkf gnigqddddy
      121 eayadyddlt dgvdtdadat emgrqaagrn kkrknspagl dedlystdmt gkkaktkkgq
      181 rssgvmaqsr erkratdnhv sadgldqqsd dahaeqiegs evgtsesavp avkpeagvps
      241 srsdaialtl igvaivlgas vwldiagfig raiatathav lgagafiipv alilaasalf
      301 sgrrvavehr vrvsmgtali vismlglihl fsgapaewpe rfvaggalga wtggalaagf
      361 spyvavpllf lviiygalkv tgitvkefte ylrnvisgns nknldadpdr esvgghneyg
      421 daygrandei aaiasgaqrt prrraplrtn pvasqskrpg ftttqsstag thdvvanakk
      481 stglfprieq psqvehtevl ssngsrehqe qvsktaagle naptasdtde fpaildsptr
      541 srsartepev ekteelplap edavdqaqsg lqqkqaaenp rtvdtkyqdt arqtrvlgvk
      601 pqsgarqpea qqatqvglas qindgpreda gatqqaskla teytipsagl lepgrapktr
      661 teindrtiea idacfaefkv daqvtgftrg ptvtryivel gpgvkvskit nlqsnlayav
      721 atgsvrilap ipgksavgie vpnsdreivr lrdvlesevi agdedptlvg lgkdiegefi
      781 sssiqkmphl lvagstgsgk safvnamlvs lltratpddv rlilvdpkmv eltpyegiph
      841 litpiitqpk kaaaalqwlv eemeqryqdm rsarvrhikd fnhkvrtgev qapagserkm
      901 epypfivcvv deladlmmta pkeieesivr itqkaraagi hlvlatqrps vdvvtglikt
      961 nvpsrlafat ssstdsrvil dqtgaeslig mgdglfipqg grpvrmqgaf vsddevyavv
     1021 eaakaqgepd ytegvtedkq aeakkaiddd igkdmddlle avelvvtsgl gstsmlqrkl
     1081 rigfakagrl mdlmetrgiv gpsegskare vltkpeeldt tiwmikgadp adaprevqeq
     1141 qnqgqpdnvv edsagdtdgs ahitkatynp tsqaf
//
LOCUS       WP_284604737             208 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284604737
VERSION     WP_284604737.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..208
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22677
     Region          58..154
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mhtdsthsds nvpghhnsah hapsaaamed ryasnervws gdpnaallna vasmgldvas
       61 prtaldigcg egadavwlaq qgwqvtaidh aptavrraqe laaengvqid aravsfqdfe
      121 ramfdlvicf fgqlsdddvp kleslvapgg wlifvhhdme sekylmparl keqltelelv
      181 ddyvfeknle rgggahhhcd lvlrarrs
//
LOCUS       WP_284604698             541 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Enterococcus faecalis].
ACCESSION   WP_284604698
VERSION     WP_284604698.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 541)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..541
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=62694
     Region          7..460
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(21,23,25,29)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(60,63,100,103,145,164,168,200,242,402)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(200,242,317)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          467..>508
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; cl02706"
                     /db_xref="CDD:445893"
ORIGIN      
        1 mekhwwqevv vyqiyprsfk dsngdgigdl pgiiekldyl etlgigaiwl spvyqspndd
       61 ngydisdyea imtefgtmad mdrlieeakk rkieiimdlv vnhtsdehrw fieakksken
      121 pyrdyyvwad pasdggapnr lksafsgsaw tfdeasgqyy lhlfskkqpd lnwenqqmrq
      181 svyemmnfwi dkgiggfrld vidlvgkipg eeitangphl hrylqemnaa tfggkelltv
      241 getwgatpei akmyssperh elsmifqfeh msldqqpgke kwdlqpmeva klkqvfakwq
      301 telgndgwns lfwnnhdlpr misrwgndqe ywfessklfa illhmmkgtp yiyqgeeigm
      361 tntpitdire ardietinmy heylekgysk eeillkintk grdnarrpmq wtaeknagft
      421 tgtpwidvnp nyqtinvaaa ladknslfyt yqemirlrke hplivwgnfe lletveevis
      481 fyrtygeerw lvvtnfsdkv qpfsadvsve qvmienmptd vtaladysla pwqafvvkvs
      541 q
//
LOCUS       WP_284604746             615 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284604746
VERSION     WP_284604746.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..615
                     /product="class I SAM-dependent DNA methyltransferase"
                     /calculated_mol_wt=69825
     Region          <8..608
                     /region_name="YeeA"
                     /note="Type II restriction/modification system,
                     endonuclease and methylase domains [Defense mechanisms];
                     COG1002"
                     /db_xref="CDD:440626"
ORIGIN      
        1 mkskearrhs gehytsekni lktieplfld elraearrli nskstsvkkl refrdslann
       61 iycdpacgsg nflivayrel rkietemiva ireregsags mtfdisweqk lsidqfygfe
      121 inwwpakiae tamflvdhqa nreladaigl aperlpinit ahihhgnalq ldwaeilpet
      181 sgqtyifgnp pfigqytktk eqtadmkrvw gkdydgyldy vtgwhaqaln vlqtrhgefa
      241 yvttnsitqg qpvpalfgpi frdhwrikfa hrtfswdsea pgkaavhcvi vgfsrntsvk
      301 prlwdypdvr geavpvpvek sinaylvdgp nilvkkrskp ladippakrg sqptdggyli
      361 vesndypeva ndavaakylr pfrmgrelvr gldrwclwmd hggfepsdiq ksailkdrie
      421 kvrdfrlksk kkatqnsant pylfqenrqp sepyvgiprv vsenrnfytv qhldhnviag
      481 dkvytaedpe gllfglisss mfitwqrtvg grlksdlsfa ttltwntfpv pildsaskqr
      541 iiaagkkvle trelhpgrsl adhynplamd pallkahdvl dkevdkafga prkltnsrqr
      601 qellfmqynt fiqfn
//
LOCUS       WP_284604818             289 aa            linear   BCT 25-DEC-2024
DEFINITION  trypsin-like serine peptidase [Bdellovibrio bacteriopascens].
ACCESSION   WP_284604818
VERSION     WP_284604818.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..289
                     /product="trypsin-like serine peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=30972
     Region          99..252
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mkrnsfvaav svavaatfsv gfvnitpkvi ygednrrdvy evpradirei adstvalipt
       61 rdlstqaggl vkinssqygv dmnlcsdepf fdqptaancs gslvgddlia taghcvsnsd
      121 cskyafvfgf kmnsaksgpe tvpasevync keivareftg qqdyalvrld rpvrghrils
      181 lqktpvqpgd aiyvvghpsg lptkvadgan vraqqkgyfq tnldtyggns gsavfnaeth
      241 evvgilvrga qdftydrarq cttsnkcsnd gcrgedvtni syivdalnk
//
LOCUS       WP_284604893             335 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284604893
VERSION     WP_284604893.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..335
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=36138
     Region          17..305
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mstspetsqt ansphfspsl kwqrrlalil lfsqagitvs gsivrvtgsg lgcdtwpncq
       61 egslvpvaga qpwvhqiief gnrlltfvvv aaaiavlval ktagrrrelk aygaasilgi
      121 vlqaviggis vhmelhwwtv alhflpsmvl vwiaallysr iaeddsqspq rifaahtrqf
      181 aalaagalsi vlitgtmvtg sgphsgdada gmkgrleldt evlavvhavc myayllltll
      241 vvwqlykqka pqrakytawv lvtviiiqwg igvaqfylgv prwtvpfhia mssvvvafta
      301 alwargyarp rfqldysare tcsssglvsq rkgsn
//
LOCUS       WP_284604928             371 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: Glu/Leu/Phe/Val family dehydrogenase [Bdellovibrio].
ACCESSION   WP_284604928
VERSION     WP_284604928.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..371
                     /product="Glu/Leu/Phe/Val family dehydrogenase"
                     /EC_number="1.4.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016639 - oxidoreductase activity, acting
                     on the CH-NH2 group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39946
     Region          2..351
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mgtfeliskh gdheqvvfcn dphvglkaii aihntslgpa lggtrmwnyk neeealidvl
       61 rlskgmtyka aasglnlggg kaviigdpkt qkseglfraf gqfvnslngk yitaedvgts
      121 vqdmehiyme tpwvtgipkd fggsgdpspy tahgvlmgik asakekfgtd slkgmrvavq
      181 glgnvgsnlv nylvqegavv tvadidmnrt kavaeksgsk avspdeilfv etdilapcal
      241 gaivndqtit kfktkviagg annvlaearh gdqlkelgvl yapdyvinag glmnvfvele
      301 gysperafek tkrvydnilk vyeiakrdni gthtaadrla eerintigrl kqrhpgkssr
      361 afttlkevhn r
//
LOCUS       WP_284605008             533 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284605008
VERSION     WP_284605008.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 533)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..533
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=55422
     Region          10..247
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mspsqnslkl nytaasdrgl vrtnnedsaf agrnllvlad gmgghaagev asqllvttmq
       61 rldrdpgend mlallgtaad dantaiadtv rqrpetqgmg ttctalmfng ttfgmchvgd
      121 srgyrlrggk leqitiddty vqslvdsgsl kpedvsthpq kslilkaytg rpvdptlrmi
      181 daqpgdrlll csdglsdpvt adtieqtlke gtpeqaaskl idlalrsggp dnvtvvvadv
      241 lagddestti paapvsagal alpeaerahp ntaagraaal nrrpqvvepk aqaagahnhg
      301 tganagngsg pgnvagagtg assgawaggs agaaennahd naskrgrnwt laivvlvlla
      361 gligggwway assqdkyyia tndsdeliie rgvdyslfgk dlhepyqrvc ltkddevrtt
      421 dlgekpsndc hpfsltdlpg svrgsithld sgsysevtdq lqrlsdkalp vcvnraetdn
      481 ngknnegknn ddnsgnsgan kdtdkdtnkd aanaesaddg glstpgvncr evs
//
LOCUS       WP_284605115             171 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Bdellovibrio].
ACCESSION   WP_284605115
VERSION     WP_284605115.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 171)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..171
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19213
     Region          <63..160
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          116..>160
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mdanhgekhf lnlgkkiglc vrgqdkrvlf qnencvktcg lmmgevcaka cntlytqvee
       61 csaisegmrl fkavdveghk vdalivndge rittllypld edqekfkkqe lyfqergltk
      121 seirimqmvl qgmtnasiae klfiskatlk thlnniykkl pasmrpsqvr g
//
LOCUS       WP_284605117             332 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Bdellovibrio
            bacteriopascens].
ACCESSION   WP_284605117
VERSION     WP_284605117.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..332
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=35534
     Region          13..324
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mlkkiktpfs emmnvdfpii aapmflvsnt divveasesg gigtfpalny rpiekyeeal
       61 kiiksrtkkp vgvniivnks narqeqdlki aldhgvdlfi tslgspkkvi eeahkngakv
      121 lcdvtnleha vkvqdmgadg viavgtgagg hagpisplvl ipwlktrlqi piiaaggish
      181 gsiisaclal gasgvsvgtr fiasqeaqvd qaykdaivss tpedivmttr vsgtpaavin
      241 tpyvqklgtd lpwamkvlkd hkltkkymtp lihlmgmksl eeaavkptwk tvwsagqsvg
      301 lveeiltvqe iyqkliaeyd dsvkklsslg le
//
LOCUS       WP_284605144             109 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: RNA recognition motif domain-containing protein
            [Bdellovibrio].
ACCESSION   WP_284605144
VERSION     WP_284605144.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Muto,Y. and Yokoyama,S.
  TITLE     Structural insight into RNA recognition motifs: versatile molecular
            Lego building blocks for biological systems
  JOURNAL   Wiley Interdiscip Rev RNA 3 (2), 229-246 (2012)
   PUBMED   22278943
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Clery,A., Blatter,M. and Allain,F.H.
  TITLE     RNA recognition motifs: boring? Not quite
  JOURNAL   Curr Opin Struct Biol 18 (3), 290-298 (2008)
   PUBMED   18515081
REFERENCE   3  (residues 1 to 109)
  AUTHORS   Maris,C., Dominguez,C. and Allain,F.H.
  TITLE     The RNA recognition motif, a plastic RNA-binding platform to
            regulate post-transcriptional gene expression
  JOURNAL   FEBS J 272 (9), 2118-2131 (2005)
   PUBMED   15853797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..109
                     /product="RNA recognition motif domain-containing protein"
                     /GO_function="GO:0003729 - mRNA binding [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=11449
     Region          2..85
                     /region_name="RRM"
                     /note="RNA recognition motif (RRM) domain [Translation,
                     ribosomal structure and biogenesis]; COG0724"
                     /db_xref="CDD:440488"
ORIGIN      
        1 mgkkiyvgnl syslddqsia dafaqygnve sarivtdret grskgfafve mstdeeaqla
       61 isklngvela gramnvseak pmaprenrgg fgggnrgggr ggfgnrsrn
//
LOCUS       WP_284605174             466 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Bdellovibrio bacteriopascens].
ACCESSION   WP_284605174
VERSION     WP_284605174.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..466
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52753
     Region          52..466
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mktrfsilll glcisltaqa idptpntkpe vkeplgaikg wtaqdslkis lpvtkfvldn
       61 gltvilledh avpmvsyhtw yrvgsrdeyp gvtgaahmle hmmfkgakky dgkafdrifh
      121 engitnnaft tndytgfyen lpssklelvm dmevdrmssl sispedlkse kevvkeerrw
      181 rvdnnpmgll relmmgtmfk vlpykwpvig ymkdidnyds eklrffyntf yvpnnavlvl
      241 vgdfktskvk sliekyygkl psralperkl lteppqkvqq nailrkdvqn ssfvvafrsp
      301 eqgsqdmyal dlaanilgyg tssrlhkrlv yqkqiatsay aynyamkeag vmgvgvnmkp
      361 glgtqealdi vyneiwklrn qkvsdkelek aktqvmkdlv dslktmdgka ralavneivt
      421 gtyeslftdl ekyqavtadd ikkvadkytq qtqrsiitle pkakke
//
LOCUS       WP_284605265              95 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_284605265
VERSION     WP_284605265.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..95
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=10936
     Region          38..92
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mptveiilsn eqlenirsql heliineitk trnqadknqr ymnkkqtcny lqitnntlds
       61 wikqglpkiv isgstrfdki aidewladla knhqs
//
LOCUS       WP_284605268             145 aa            linear   BCT 25-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Bdellovibrio bacteriopascens].
ACCESSION   WP_284605268
VERSION     WP_284605268.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..145
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=15458
     Region          25..145
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 mpdgrrkspg afdfgffgwf dgcmqifwig lfglggifcr ygvdrwlapt sagfplstfl
       61 inilgcsvag viyavgergy lsqtlltglm vgfcggfttf sayalqsfdl lqkgklgmsl
      121 gylfaspalg llacyvavla trkli
//
LOCUS       WP_284605350             575 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase family protein [Bdellovibrio].
ACCESSION   WP_284605350
VERSION     WP_284605350.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..575
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=64933
     Region          137..>285
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mtfqtfsmfv gsflfvnvvq aqtlgvspnq dleskfyeem akeagvdqpk nlgffeevpd
       61 glsskdmspe cdprrfedsv vgkklstaqy yktaksyfkk cgseltknst tgilgllkfs
      121 kyqypflshp qikeflvklp ngtripgila lkqdprprpl vivkcgvfcs agptasmksy
      181 mmhlfdqspf nvlllanqtg mdyiylnktv tlggwsegye aieigkwmqe kwehrdriss
      241 vhfmgislgg naavmgaafn dkyllsngrk vynsvtaicp vislrptldk lygsqivgri
      301 fasmtrdhfr earqyitdvp dlvvdskipg srhamadyig elassslqrr giastpqsyf
      361 ksnnfwnwke evktpllvwa skddmvvnnk inayvmendd fyqnsphvgv lnltygnhca
      421 fssaygaqaa gavlrtfvln hspefvdeyn tkqqlpwtlg fkkmgaqfeh igqtwnfysq
      481 seqakvtfrl fnwrahdkcf eegpwsanps cttkkeywvp lsslkamgar vprtdaeaqa
      541 ltrefntkve frvqggplng tnkneffmtw rnnfe
//
LOCUS       WP_284605441             253 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Bdellovibrio
            bacteriopascens].
ACCESSION   WP_284605441
VERSION     WP_284605441.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..253
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27924
     Region          22..243
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mlrlflsllf fwnfssavak tivingeddw apyssatkdy knvqglapdi vraafktqgi
       61 tvitrpvpfa rclyevsegs aigcfdtvms ietqdgfifh ttplfkadmv vygrvhepqr
      121 tlsfkdlegk vvgttngyty ptefiantki ihspgpteks qleklasgrv qyailwglta
      181 pylfeerpdl aakikslgvi sttnlylsfs kkhkdgakya avlekglqai iadgtyakiv
      241 nefnsryaip tkp
//
LOCUS       WP_284605631             164 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: TlpA family protein disulfide reductase
            [Bdellovibrio].
ACCESSION   WP_284605631
VERSION     WP_284605631.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..164
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18621
     Region          41..164
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mrflfvilcg latakaafae nipnvdfrrf tavpfnkqal plsmgdlkgk vvlvdfwasw
       61 cgpckealph ynrlqkkykd qgvvfigine dddakerdaf lksqaiefaq yldknkemak
      121 dfkiqalpsl fvfdknlkpa alyrgfddkk pqalekkiqe llar
//
LOCUS       WP_284605692             232 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284605692
VERSION     WP_284605692.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..232
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=25190
     Region          1..223
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mlfdslprps eciapgvahl pgwlgvdkqa klvhevreia rtyadtpmam lrpalksggq
       61 msvyqlhlgr ywhypscryv dkiagttvpp vpeslvalap valraaaeva eelapwvetf
      121 vpemvlvnyy ppgsgmgmhv defeesrapv islsigdeal frmghtesrt qpwddvtlcs
      181 gdlvvfggpk rfayhgvvrv ndatlpdgcg laegriniti rqvsaapklq gr
//
LOCUS       WP_284605828             406 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284605828
VERSION     WP_284605828.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..406
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43493
     Region          1..401
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 mafilgiflf algiaatial heaghmvsar afgmrvrrfy vgfgpsvfsf tkghtrygla
       61 alplggfcdi agmtamdemt edekphamys kpawqrivvl aagpfvnivl gllilflvaa
      121 saglpdphad vratvgevtc sadqkaptqs dapaelenct gqgaggqagv qsgdiitgfn
      181 gekldnfmqf rdevqsrpge titldierng helqldveld pvvrydaegq prtvgsvgla
      241 sapldvhrdy svagaipasf eyswfmlqat vegiiafpsk ipavaasifg aereqdspis
      301 vvgasragge lverelwpmf wmmlatlnff lalfnmiplp pfdgghiava lwekvrnllr
      361 rlrgqepggp anyekllplt ygmaamlltv gviviiadiv npialf
//
LOCUS       WP_284606155             404 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Bdellovibrio bacteriopascens].
ACCESSION   WP_284606155
VERSION     WP_284606155.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..404
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=46728
     Region          154..397
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 miklenrffr llwqitlvlc clsvfvsksg lsiagtflll lsciiiewgv lwrerkglll
       61 ivflyplail lsffslggte safkvliswp wplfvlpayv vskrkddqki vlvtlcisll
      121 facvqsylif fkdfngvfds dvrvrsfwdi srwgvflvsa ilgllamvly fdrqrkrkyv
      181 iifqilalma evslilsntr apwisagvsv flmvlffprl fkfsmvmafl livmlsfneg
      241 mrdrlasvln iqsangrvts tdasnearly mwkvgaeffw gqpwfgtgfe nserylrtfv
      301 dskpgykeky itdqfsfrdh hssylamfvq mgaifaiifw giyfgafflm fknwhrtrdl
      361 wsgtvfllmi ahsvmfvfyt svqsfemial fpfiglipka pdir
//
LOCUS       WP_284606206             773 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284606206
VERSION     WP_284606206.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 773)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 773)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 773)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..773
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=80348
     Region          19..757
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mptprstssp ipasstasst ielnisgmtc ascaarvekk lnkhdgvhae vnyatekati
       61 tgdtdaldad aliatvektg ysaeltpest tagtqapqda maeaeldslr rrlivsavla
      121 vpvialamvp awqfdywgwv slaltlpvvv wagwpfhrat wqnlrhgsvt mdtlislgts
      181 salvwsmval ffgsagdpgm rhgfdftvsr gdglshiyle vaagvitfil lgryfekrsk
      241 rtagsalral ldlgasevtv lrdgaettin ineltvghef vvrdgekiat dgvivsghst
      301 idtsmlsges vpveagpdda vagatinvgg gklvvqatkv gkdtqlaqma qmvedaqsgk
      361 asaqrladki sgvfvpivia vslltliawl lidgdwaaaf taavavliia cpcalglatp
      421 tallvgtgrg aqmgvlikgp evlehsrgid rvildktgtv ttgvmeladv vtaegfdrde
      481 vvhlagsleh esehpigrai araatnqrad gtlsevsdfe sirsagvrgv vegrrvavgk
      541 psladnadlg alqqpflsaq tqghtalvvl vdgtpaavlm vadqvkttsa aaiqqfhelg
      601 ietmlltgdn qavaetvaae vgiehvraev mpedkvavia dyqdrgykva mvgdgindap
      661 alaqadlgma mgtgtdvame saditlvrgd lraatdairl srrtlgtikg nlfwafaynt
      721 aaiplaalgl lnpmlagaam alssvfvvsn slrlrrftst agagvdatag atv
//
LOCUS       WP_284606244             109 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: DMT family transporter [Bdellovibrio].
ACCESSION   WP_284606244
VERSION     WP_284606244.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..109
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11506
     Region          6..109
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 msnttawlvl lvagilefvw atglkysdgf tklgpsiftl vtmgisfyll slamrvlpvg
       61 vsytvwtgig avgaivigfv vfkepvslmk lvflgmivgg ilglkfves
//
LOCUS       WP_284606278             192 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: c-type cytochrome [Bdellovibrio].
ACCESSION   WP_284606278
VERSION     WP_284606278.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 192)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..192
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20769
     Region          <97..185
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mrsvinlsvg iaaaglavla lsscgprgnk pnveiiqdmm espaikaqey detsphhsgm
       61 rvppegtapv gfepyryptd iegasknlkn plsgkmdqet llvgqkyyet ncavchgfkg
      121 eggvegkstv aekmalkppa vvsdkvkgwp dghlyhvitm gqgvmgpyas hipqqyrwqv
      181 vnyirflekq ak
//
LOCUS       WP_284606296             323 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284606296
VERSION     WP_284606296.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..323
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34347
     Region          2..319
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(40..41,45,118,122,125,143,146..148,167..168,172,187,
                     210..211,232..236,257..260,307,309)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(130,225..226,239..244,252..259,262..263)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mkaiqitrtg gpevlqiaev espipsddqv lvdvlvagvn yidtyyregi ysattpfipg
       61 fegvgrvlhd pigkiasgtm vawntafgsy aeqvcvardk lvavpndfdl staasmllqg
      121 itahylthgv yeladgdncv itagaggvgl lttqfaaaag anvytvvssd ekeelsyqag
      181 athvlrygpe lanqvrelta gkgvdvvydg vgkdtfeqsl dmvrnrgtvc lfgaasgpvd
      241 pidpqilnek gsifltrpsv agwtsregef qmraqavvqa vvdgdlkfrv sdsypleeaa
      301 qahrdlqdrk ttgsivlrvq eai
//
LOCUS       WP_284606337             333 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284606337
VERSION     WP_284606337.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..333
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37334
     Region          16..326
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mntdspeklv alvqslnlvp yfkahpersi feaakdlgls pdelvraler lhcsgistqt
       61 qdlidlsyel tkgvvihddq gmdsslrltp teagallltv evletmpglv drsavasaae
      121 klrsimddrs raiydgiaeh ssatedvqyr iaqalhtkrr vqfdywsass nstrtrtvdp
      181 arifirgdia yltafveqyg ehrnfrvdrm rnveilpeta rprtrklqfs sedpfgfrds
      241 ttatlavspd alwmldeydm krqdetppcp aaddqkawvk atmpigstsw ftrfalshad
      301 rvrvlgpkdl vdavheraqv giqrysmvdt nks
//
LOCUS       WP_284606339             936 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284606339
VERSION     WP_284606339.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 936)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 936)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..936
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..936
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103490
     Region          2..934
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtsthfetfr sqltyeldpf qvqgcraven grgvlvcapt gagktivgef avslalsrgt
       61 kcfyttpika lsnqkfhdlv aihgedavgl ltgdvsfqpd adivvmttev lrnmiyaksp
      121 aldrlthvvm deihfladqa rgavweevil nleehisiig lsatvsnsee fgrwlstvrg
      181 dtevivsehr pvpleqwmli gqkvyplfap gtpaiegptt sepagvnpel qrrvarleag
      241 daadgrddfr pgqgfrsrst agtgnsrsgn vrpqdryrpl grpevlrilq gqnmlpaiif
      301 ifsragcdga lhqclrskmv ltdedeqrii gevidagveg iphedlevlr fsqwrkalir
      361 gfaahhagml pafrhivekl fvrglvravf atetlalgin mparsvvlek lvkfngeahv
      421 dltpgqytql tgragrrgid tlgnaivqwa pamdpqrvag lastrtypli stfepgynma
      481 inllnnlgmd dslrlleksf aqyqadgsvv eetreierav hrveklreql neaiaafapp
      541 stddqdpaql lseyvelrkr lsveekslks rakdergdet railaklqpg dvialpskkr
      601 pvlavvntpa nqtadprpwi ttekgwsari dvsgfdnppt lvgkmklpgk alknprrhnh
      661 ivvdkfared yprpkkmklr arirdterik dlrtqmkkhp ahswpamere qltqlaqkyl
      721 rrkgeldklr atvdkatetl gdmlrrivdl lteldyvdiv dgepvvsieg eklaqvhnas
      781 dlliaqclkr giwqeldpae lagvvslctf enrratggql fdgvtdamts amentmrlwe
      841 elisdesrhg lphtrepepg fsiaihqwca gaplgyclaa aaesgaeltp gdfvrwcrqv
      901 idllqqvakt gysseikrta gqaiasinrg vvaigs
//
LOCUS       WP_284606354             295 aa            linear   BCT 25-DEC-2024
DEFINITION  S1 family peptidase [Bdellovibrio bacteriopascens].
ACCESSION   WP_284606354
VERSION     WP_284606354.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Perona,J.J. and Craik,C.S.
  TITLE     Evolutionary divergence of substrate specificity within the
            chymotrypsin-like serine protease fold
  JOURNAL   J Biol Chem 272 (48), 29987-29990 (1997)
   PUBMED   9374470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475742
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..295
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=31194
     Region          35..295
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 myrhflkksv lllalsvlsa csgsdggkel kaepascevt gssfgivgge ilgsnnplse
       61 stvfvihkdi egktgictgt lidddkvlta ahcttpggrs qiaftnnasc tiaapkrtrr
      121 avvdeavhpd ytyfnktlln agrdlaimkf sggipegykv ralpsetyqa skddqlvmsg
      181 ygvtsetaed sgvlrfttap asrvvsnfym aivkttvtvp gtiavqqpsn gvcsgdsggp
      241 lyvhdgrdlt lvgitsmgld vtatkekdmr ichgvslftd lkphlpwikk qiesl
//
LOCUS       WP_284606384             318 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sigma-54 interaction domain-containing protein
            [Bdellovibrio].
ACCESSION   WP_284606384
VERSION     WP_284606384.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..318
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36041
     Region          <2..315
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mtegeiiars prflqvldma rrvaassanv litgesgtgk eviarmihdl sarqkktfvp
       61 incsaipepl leselfgyar gaftgatspk aglfeeadgg tlfldeigdl dlhlqakllr
      121 vlqekkvkrv genhyralni rilaathndl sedvsqkkfr edlyfrlnvv pieipplrer
      181 pedivplaey flrkfsyrhy gvqkktfsad vpsfllsqsw agnvrelens ieravvltes
      241 deitvkdida ghgkkllcle svfekifqke grllsleems hyyieyalql nkgarektar
      301 dlgidrktly rklnqryq
//
LOCUS       WP_284606397             270 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: metallophosphoesterase family protein [Bdellovibrio].
ACCESSION   WP_284606397
VERSION     WP_284606397.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..270
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31182
     Region          54..228
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mkrfwllfll iascgplqrs spfsehtnsk sdhlndrain glqrldqtpq divlvaiads
       61 hqnyddlttv vssanqqqad fvvhlgdftn qgynfeydlf inrmkklnlp fvvalgnhdt
      121 vtkgkslylr lfgdfnrmfe frgyrfiiln nnnldfkahg gvdwdwlrrn veasllpivl
      181 myhinpdntd yftdsdrqtf dsivigsrvr lmlhghhhvf atsfangilk hmvhrteeak
      241 wsritlrane isidycqkle cvrettqafp
//
LOCUS       WP_284606400             468 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sigma-54-dependent transcriptional regulator
            [Bdellovibrio].
ACCESSION   WP_284606400
VERSION     WP_284606400.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..468
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=52455
     Region          1..456
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mksrilvvdd eesireflei mlkkegyevt laedgqkakd lltkktfdmi isdlqmphvt
       61 giellkhvke typdtvfmli tafgttetav eamkmgaydy ltkpfkidev rlniqnalrs
      121 rnlevenrtl kkelvkeysf qnmvgnspam hsiydmvkrv sqtptnvlit gesgtgkevv
      181 akaihyngpl kdrpfvtvnc gaipenlmes emfghkkgsf tgavadksgl fevadggtlf
      241 ldevgelplt iqvkllraiq ervirrvgat edmkvdvrii aatnrnleem vqkggfrqdl
      301 fyrlnvinik tpglrdrred ipllanhflk kynerlnkni gaisaeamei lkkydypgnv
      361 relenliert valeggatil peslppmvnt ssgrkmassn eieigddgvd ldkvmgqiek
      421 ellikaihaa ggvkkraakl lhisfrsmry riekynlgvv gddeldde
//
LOCUS       WP_284606401             526 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: two-component system sensor histidine kinase NtrB
            [Bdellovibrio].
ACCESSION   WP_284606401
VERSION     WP_284606401.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 526)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 526)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 526)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 526)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..526
                     /product="two-component system sensor histidine kinase
                     NtrB"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009399 - nitrogen fixation [Evidence
                     IEA]"
                     /calculated_mol_wt=57959
     Region          188..526
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 mrlsfalqnn knqgllvefv rlnlfvlila isvissivqe gfinwsilgp fygvltvalg
       61 chlvwvtfwe kllekpfwlf fgfvldslfi slliyfsgis qslflflhlv nillagiacr
      121 gvgavtlalf tsiffsvaav fspemkalnf ffllalnnia ffsvaglsgy lseqlqtvgs
      181 eltktglslr saqelnevlv enipsgmvsf tesgevvkan saahtildin dltqtnwfql
      241 fpgmlkpdng ivkadvkyta agasdskilg mtvskiyspe lqshllislf ddltkirqle
      301 ysarqnekla avgglaagia heirnplagi sgsiemltqt vtneddrklm kivlreidrl
      361 nnlitefldy arpetpptdp vdlsalltev mdsmtmnnqv radveqvrey daglkilgrr
      421 dklkqaflni iinsyqamne skqpklsvka masekeihvr irdagcgmse vtkkkmfepf
      481 httkpkgtgl glavthkile ghgaqvfves evgvgtefil tfpran
//
LOCUS       WP_284606457             180 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ExbD/TolR family protein [Bdellovibrio].
ACCESSION   WP_284606457
VERSION     WP_284606457.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..180
                     /product="ExbD/TolR family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=20286
     Region          14..156
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD/TolR; pfam02472"
                     /db_xref="CDD:426791"
ORIGIN      
        1 mrrirkikvd hnsefeldla pllavmvklv pvllvssafv qmmvieselp qvvneaiqrq
       61 eqtptptnva mevdaegiri vitekgqdki etipmkngaf dleslhqkli avkkahpevf
      121 kielnpdgki pydqivkimd earqakdvnv kfpvfdtkqg knvetnymfp evvfanmmeg
//
LOCUS       WP_284606458             165 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ExbD/TolR family protein [Bdellovibrio].
ACCESSION   WP_284606458
VERSION     WP_284606458.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..165
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=18457
     Region          1..161
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 msrrrrfepn lkknstftln itsmtdmfti mlvfllqtys tsdvqiipen glrlpssasm
       61 vnpteavkls lsqeglkide tkiadvknad flpqdledkd tnfikplfae ldklaknsad
      121 kahikegril lqadkelpya tlrkvmytas magfpqlklv tmvge
//
LOCUS       WP_284606466             706 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Bdellovibrio bacteriopascens].
ACCESSION   WP_284606466
VERSION     WP_284606466.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469162
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..706
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=80170
     Region          273..>377
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
ORIGIN      
        1 mykplkilla ipllcgtala epaltvkksg rpaatglkvk sssvptfevy qkkvvkgkve
       61 vfkvknipll dlgeerilea ptlsplrlpa srdvsvaeak rrpsplplqf nvapynvtve
      121 paksltnaea fkkipdvkil npvqepvtqd plvqlakldd mqpndykllq alifleiqkn
      181 yelamglfae lmedpehrie alyhyamtak glglnsefrq ymiqvaqetk nkewqqkate
      241 alvqninvle vsdiafvdpl vikyeidvtk nddyqltrak hysekgqlgl medalvyise
      301 tsprypeall lnalfnyrqg kvedavvhld rlmkvteadk tsqirsvgal tlarmqfqks
      361 dykeafqsyl kvdksnplwl qamvesawtq ilgedyegaa gnmfslhtdf fknafapesy
      421 vvrtvgylnl cqygdgvqvl nemnkkyapw kkkledymrt rkesvnyydt vknwlknsdl
      481 kevdglprsf ivelarhpay msvqkqinny edeilrfnki altlikkere liakqneank
      541 llaeakrgik gnspsesavq nvqsaekkll syriqyhiak karisiknlr aqglarieke
      601 ktvlraqasq alqsrfgeml aslnkvldqn evlqyelysg agehiryqma ggdvntkerp
      661 elkvekeksl nwkfkgeiwe devghyrssl knvcaqqdnv aglseq
//
LOCUS       WP_284606511             251 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: substrate-binding periplasmic protein [Bdellovibrio].
ACCESSION   WP_284606511
VERSION     WP_284606511.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..251
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28450
     Region          27..243
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mkfaivfffi slsalakpip vlvggyefpp yimrknghvq gltldfiell nqkqtkyaft
       61 fvltsptrry sdmkdgrfqi ipfesstwgw sreliesski fheggevfit lkekgkdqsy
      121 fkslegktik giqgyhyefv glstapkalk nfnieltsth dgnilsvlnk raelaivske
      181 yldlylqenp dvkerllvsk dfdqiyrlgv lvkqkgspis vaevnriids vvkdgswnsl
      241 lkkkgisqrl p
//
LOCUS       WP_284606590            1819 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Bdellovibrio
            bacteriopascens].
ACCESSION   WP_284606590
VERSION     WP_284606590.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 1819)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1819)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1819)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1819)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1819
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..1819
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=203246
     Region          304..1808
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mfgflwsalv avsfaqekiq vtnvtpqgyv ssveqvrvef shpmvkfgdi kldspvksdc
       61 fkngqgrwid trnwvydfne plrggyacsl salgqkfqfn tggphvlstf pptykaidpq
      121 qyfvlmldap vkkesiekga yfvveglgdr lpaqlvdgse aakikaaaes eykydkesfk
      181 gdfvvvkstr afppggrlsl vwskqiqsvs gssspedvnf efkveepfka efscdreapg
      241 kpcvpilgmr ltftapvkis eakkiylegp dkkkifanlt eeatqetany lefkgpfakn
      301 tsyklviptd lkdeenrsla nkaqfpltvk tgedpsllkf tgtfgvieag peaalavtlr
      361 rvekslqtrf sgwtgqwtaa dfkkivsaln qiqkdptsee rlalwkntpf ekiqvqkplk
      421 asdtevvgip lkktgfyave messllgqsl lnkkapfyvr taalvtkmav hikhngneaw
      481 vwvtelknsq avsganvkiy dlngdfvaqa ttdskglayi qfknpvskwp rnensfyydg
      541 fyavaekagd fsfthtswds gieswryqlg gydegsplig havvdrtllr pgetlsakiv
      601 lrktaargle mpsasewptt livnhdsglq sfklplkwdq kkgfalvqwh ipvgaklgrw
      661 sltiekknpa lslnvgevsv esfrvpliqv rmdatkpvfv qeknvgiqis gvyfaggpas
      721 elpmkmswsv epdfflaqde dlrdfsfang vvkeglfrsg edetarhipq sgaeniklsn
      781 qgqavveikg lkygsgpqrl rtdveykdpn geiqnavrsf slwpanvvlg ikskswwata
      841 dlvefevval dlmqrplvkq kvqvdlytsr yythrkrlvg gfyayedfqe yrkigelckg
      901 etndkglfsc agkskvsgsv iavvttkdkd gresaanvtq wilrtgetqw fgsddhdrad
      961 lvpfkksyep getaefqlrt pfpqakvlvt veregvlste ivdvkgdrpi irvpikkeya
     1021 pnvvvsafai rgrlndpkpt alvdlgkpaf klgmtnikvg rkentlkvsv qtdrkkykar
     1081 ekatvtvkvq daqgkpaaqs dvaliavdeg llelrdnssw nlldammkpr ahlvqmataq
     1141 tlvvgkrhfg lkavpiggdg ggalrrelfd tllywnpsvk lnaqgeakve iklndsttsf
     1201 rivavaiqgk dqfgtgwtsi qssqdimilp glagvartgd eflagftirn aseqtqsldv
     1261 slqvhpltek fssqkmtlkp qetkevfwki kvpesvktld yvltaknaqg kavdeikksq
     1321 avlplrsati yqsqwgawpe fnklslqqpa gaergqssil vevqeglggs llglkdfwen
     1381 ysytcleqqv sravslndkk lwkkieekld vyvgsdgllq ffpantqkgn lnltayilni
     1441 aheagfafse enesrlldtl tayaegrlke dvefsradev lkkvtvfetl sryrrfnvdw
     1501 lstvefqgnq wplytlvewy qihqweksip erekkladie kilrnrfyfs akklqlreed
     1561 reampwlmrd segallrlil asmnspswkt dvprlyqgal drqkngawml tsdnawgrla
     1621 mrkineayss gkvqgtfsaq ldnekgsytw skgpsgsfel pwkeekanlv lqqegsgkpw
     1681 itvsakaaip vtqpvfagft vtktvspvtq kkkgvwsvgd iakvtlrvqa kapqswvvve
     1741 dpipvgarvt esswataier keemvrfyys wfdassevie ytirfnqagt yrmpkthvea
     1801 myspdlyadl pegvwkvee
//
LOCUS       WP_284606864             250 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase
            [Bdellovibrio].
ACCESSION   WP_284606864
VERSION     WP_284606864.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..250
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27965
     Region          54..157
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mkaqyqtfin nhevtiagne tfnnvlalng lcerdavryl qmvvhdfypq tfrmtaldlg
       61 agrgvtamtl aelgfnvvay dmyrnsiail qrialqqdln isfgmggilh leslnkkfdl
      121 indcegltnl vkpedraryl egvknslaeh gkfvmtvqvq stqytpeegf esvrldenhv
      181 lwretpecdv pgvvemngky wtaqkricpa deirrevmaa gytilsddle ilpgnnpail
      241 rlvltstlgc
//
LOCUS       WP_284606861             556 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: glycoside hydrolase family 13 protein [Bdellovibrio].
ACCESSION   WP_284606861
VERSION     WP_284606861.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 556)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..556
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=64378
     Region          9..471
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(23,25,27,31)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(62,65,102,105,146,165,169,201,258,413)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(201,258,328)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          478..552
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; cl02706"
                     /db_xref="CDD:445893"
ORIGIN      
        1 maptkkwwke svvyqvyprs fmdsngdgvg dlpgltskld ylkdlgidvi wicpmykspq
       61 ddngydisdy qdihaefgtm qdfdtllsev hkrgmkllid lvinhtsdeh pwfiesrssk
      121 dnpkrdwyiw rdgkngkepn nwesifggsa wkydekteqy fmhifsakqp dlnwenlemr
      181 qeiykmirww ldkgidgfri daishakkep gladmpnpkg leyvpsydkh mnvpgiqeyi
      241 tdlckntfvh ydimttgean gvsaehaeew vgeaqkkfnm liqfehvglw dtnpekridl
      301 lkvkevfgrw qkhlenkgwn alfvenhdvp riiskwgdaq kywresatsi asmyflmqgt
      361 pfiyqgqeig mtntvfngpe dfndvsaknh fairrkqgar daeitaelan ssrdnartpm
      421 qwtgeanagf ttgapwlkvn pnykeinvak qtsdahsvws fyknlikirr enpvfiygry
      481 qlvmkddtqv yaytrtlgds qalvisnlsd kaaqfnepgm slksknllla nydvsehqea
      541 tsfalrpyet riyrik
//
LOCUS       WP_284606971             696 aa            linear   BCT 25-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Bdellovibrio
            bacteriopascens].
ACCESSION   WP_284606971
VERSION     WP_284606971.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Shan,L., Mathews,I.I. and Khosla,C.
  TITLE     Structural and mechanistic analysis of two prolyl endopeptidases:
            role of interdomain dynamics in catalysis and specificity
  JOURNAL   Proc Natl Acad Sci U S A 102 (10), 3599-3604 (2005)
   PUBMED   15738423
REFERENCE   2  (residues 1 to 696)
  AUTHORS   Polgar,L.
  TITLE     The prolyl oligopeptidase family
  JOURNAL   Cell Mol Life Sci 59 (2), 349-362 (2002)
   PUBMED   11915948
REFERENCE   3  (residues 1 to 696)
  AUTHORS   Polgar,L.
  TITLE     A potential processing enzyme in prokaryotes: oligopeptidase B, a
            new type of serine peptidase
  JOURNAL   Proteins 28 (3), 375-379 (1997)
   PUBMED   9223183
REFERENCE   4  (residues 1 to 696)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 696)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..696
                     /product="prolyl oligopeptidase family serine peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=78998
     Region          22..695
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mrnslrrwfl llpllvgcks ktiaqdpylw leevegkkal efaqtenkkt lehfqknphf
       61 kkiekearai llaedrtpav slrkgelynf wrdqknvrgv wrktsissyk tkhpkwdill
      121 didelakken enwvwsgast lgprhdralv slsrggkdav vvrefdlntr qfvkdgfyvp
      181 eakthiswkd entvfvgtdf gagsltdsgy privkvwkrg tplskavtvq easpkdmsay
      241 syiidendkr yvfhsirkgf ysstnwyedk ngnktrlpmp edsefwgvfs dklffelksd
      301 lgsfksgsiv fmplnalsqg eaaqktlral fvptdkrfiq gmsptknhil lhvtdnvlsr
      361 iekvtftsad twttevvklg engvssvtst eeesdnylaq yvdfltpnsl ylgnasdknn
      421 hmdllkkspe rfnsvglkte rfeatskdgt kipyfvvskk dikldgknpt llygyggfqa
      481 pmqpsylnvi gkvwvekggv yvlsnlrggg efgpawhqav lkenrykvye dniaiaesli
      541 akgitspqhl gisgrsnggl ltgatfttrp dlfnaaivgv plldmlryhk llagaswmde
      601 ygdpddpkmr eailkyspyq rlnkevkype vfimtstkdd rvhpgharkm varmkeqghp
      661 vfyyentegg hagsanieqt ilwnsleysy lwerlq
//
LOCUS       WP_284606943             284 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [Bdellovibrio].
ACCESSION   WP_284606943
VERSION     WP_284606943.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 284)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..284
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=32592
     Region          13..272
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mfqnllkpkv ktalaiiwfa ftfslvawww vfflikfsps nsthrmfawe gtillaaill
       61 ggialivfsy rdqkrhqrlr fffstfshdi ktsitrlrlq aevleedlpn ynnpvmkrli
      121 qdiqrldlql enslllanle vgellqenis lnnlfsslrn eftelslele revivrgdrr
      181 allsvfknll qnsvlhgkas tvrikvrplk ghrielvvqd nglgfkgale klgseilmsq
      241 dsrsngigll ltkrllqkmk gdirfesien dgfasylele gylp
//
LOCUS       WP_284606995             227 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Bdellovibrio bacteriopascens].
ACCESSION   WP_284606995
VERSION     WP_284606995.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 227)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 227)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..227
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=25254
     Region          <6..221
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mnnyylanis heirtplgav lgfaevlsqp dltetermes leairrngel lqrliddlld
       61 ltkieaqkle feerdfsvgt llsdvrkalt lkaaerklnl iieepledvv lrgdalrikq
      121 ilfnvignal kftdsggvwv qttyqnrtlk ftvedtgigl tedevqrlfq pfnqadssma
      181 rrfggtglgl visrqlarlm ggdlvlvksv rgmgsvfeis lkikkas
//
LOCUS       WP_284607005             281 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: S1 family peptidase [Bdellovibrio].
ACCESSION   WP_284607005
VERSION     WP_284607005.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Perona,J.J. and Craik,C.S.
  TITLE     Evolutionary divergence of substrate specificity within the
            chymotrypsin-like serine protease fold
  JOURNAL   J Biol Chem 272 (48), 29987-29990 (1997)
   PUBMED   9374470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475742
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..281
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=30645
     Region          1..279
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mktkqyvssf ivlaltacgg pqnsdviftg tenaivggre ttrdnilsky vvlivdnptk
       61 knctgllisk rmiltaahcv gtkaedlsla fglnplsgny tlrkadkifa skqydknssq
      121 nrhdlglili kgtapegylp lllpdekfpl lkglaftavg ygrtsgkstp qndiqgsgvl
      181 rhvelkidsl nsdetqffvd qrsgkgicng dsggpalmry merdyvvgia savswsvpde
      241 isagkrnqyi qnkdvcaeks iymnvkkfrs widthskqll n
//
LOCUS       WP_284607089             414 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Bdellovibrio bacteriopascens].
ACCESSION   WP_284607089
VERSION     WP_284607089.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12782763
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..414
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46363
     Region          <2..393
                     /region_name="RecD"
                     /note="ATPase/5#-3# helicase helicase subunit RecD of the
                     DNA repair enzyme RecBCD (exonuclease V) [Replication,
                     recombination and repair]; COG0507"
                     /db_xref="CDD:440273"
     Region          12..183
                     /region_name="DEXSc_Pif1_like"
                     /note="DEAD-box helicase domain of Pif1; cd18037"
                     /db_xref="CDD:350795"
     Site            order(13,31..38,109,149)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350795"
ORIGIN      
        1 maaqysvels peqsealell rsgenvfltg gagsgksfli rhfmreldpk empilastga
       61 aavllggrtf hsffglgime ggpdatyara skdtkllarl rkvegviide ismipgqalm
      121 iaealaqrar esklpwggmr iisvgdfaql ppvtqtsqrd wcfmnevwrq sgfqtvmlsh
      181 nqrvsenhfl nilsdvrhgl vteqvrdfln ehikthdedh pgtrlfprki naenfnqrkl
      241 nelaeeevti dsiyfgsekh ieilmksapv pvklvlklgc rvmflqndpq krwvngtrgi
      301 vtdissdrit vkkdqgrevq vdkssfalqd segnimaqvi qfpltlayat tihksqgatl
      361 ddlwcdlssl wepghayval srlraseglh ligwnprsii vdpkvldfyk rler
//
LOCUS       WP_284607149             272 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [Bdellovibrio].
ACCESSION   WP_284607149
VERSION     WP_284607149.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..272
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30561
     Region          13..272
                     /region_name="COG4587"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443644"
ORIGIN      
        1 mktsfavfwk rnlafaklai vsnleyrlny fvdavvqptl ttgievllwf avfagaatse
       61 ingfgrefyl syalwgaffa rictswmyey rmiqeidsgs vnsllvrpms fyeyyfsqlm
      121 gykfittlvs mmipllavmi fklptkferl plafalefyy lilvhsisfv iaagafylnk
      181 vyaitgaknl alwlftgelf pldlmpepfr savialpfsa gvyvpvgylt grleiasvyq
      241 aftsvtvgiv ivnligaymw rkgvnvytgt ga
//
LOCUS       WP_284607187             692 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD/NAD(P)-binding protein [Corynebacterium propinquum].
ACCESSION   WP_284607187
VERSION     WP_284607187.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11816065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..692
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=74820
     Region          2..656
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
     Region          7..252
                     /region_name="NAD_binding_9"
                     /note="FAD-NAD(P)-binding; pfam13454"
                     /db_xref="CDD:433222"
ORIGIN      
        1 mstthialig agprgisvle rlaaylqeas gkhsrpghaq psaprvtvhi iddsqigagr
       61 vwdtdqtrtl cmntladavt lftepgssvg apvlsgptly ewirllrgdd llaaleagsl
      121 nydtaaevva akqelfrqhp prdgiaedyr eelagsveqs npsralygey lrwvyrvava
      181 qlpdsvdvve hnsrairiqq adiqradrda qagntdsasd ydaadvgtpn ydfitladgt
      241 tisahatvla tgwvlnadnd eqyqlraanq senlrwigpn npveqpveti pagkpvlvrg
      301 lgmgffdlma lctlgrggff evdptsrsgl ryrasgtepq fvvtsrrgyp flpksdygsl
      361 ppkaqmprlq dalaaaqnwe ridfsidfap aiirdafeaf yrtlarvrpd tivtsvdeii
      421 svidstpvhv lldshgvhna larhasefcd lqpyfhprae stsqvadsla rdidealkgt
      481 dspikaalwv fascrkhvgi agsqgkftpd saspslqevm algqmvgsgp plfrsqqlla
      541 lvdaglvefl gaypqleisa deftltcgsg vaarrasaat lvdawlpkpd irfpadllsq
      601 slyasgrirp fvvdgvqtgs petdtntrrt ihpdgvqdsr lhiigiptha qmpdttispm
      661 pgtdplmlqe tdhtarslha iirdlpdatp qs
//
LOCUS       WP_284607309             176 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Bdellovibrio
            bacteriopascens].
ACCESSION   WP_284607309
VERSION     WP_284607309.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..176
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=19630
     Region          <47..116
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mtlsqsvies lqkslrcpdl qvfmkpewgs hnpqhrtlir eeikfllqgr clyssishch
       61 gmglvaissf pvgvdieitd rvqdrvmarv ssqeefqaap ssaslwcake acfkalrpfq
      121 qpsvisqitv gawekidsqt etyrlsnssd faapsenrgv vlrvpehtis ffvfps
//
LOCUS       WP_284607313             259 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Corynebacterium propinquum].
ACCESSION   WP_284607313
VERSION     WP_284607313.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..259
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26972
     Region          8..243
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mpipvklprt faqqlqqesg sqvgawissg spvaaeivas agfdwllvdg ehspysletv
       61 tdllratday gatrvvrvpv gdtalikqyl dlgaqnlmvp mvdtaeqard avaamhyppr
      121 gvrgvgaala rssrwnaved ylqnasdlvs ltiqlesvta vdnaaeiaav dgvdqlfigp
      181 sdlaasmgvl gqqthpdvld avsramkacq dagkpvgvna fnleqaqayl dagasfvlvg
      241 advqllagaa rgladkfvk
//
LOCUS       WP_284607402             129 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: fluoride efflux transporter FluC [Corynebacterium].
ACCESSION   WP_284607402
VERSION     WP_284607402.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..129
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13501
     Region          11..129
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 mnldisltea llsmasvaag afaggllrgl lsklrgrytg tacsnmlacf algimlarvd
       61 lgalvhlpyw eiafgtgfcg alstlatlar elgnltyera wirlslytvf tvlgglgavw
      121 lgwllgmav
//
LOCUS       WP_284607433             259 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: MlaE family ABC transporter permease [Bdellovibrio].
ACCESSION   WP_284607433
VERSION     WP_284607433.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..259
                     /product="MlaE family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27950
     Region          4..246
                     /region_name="MlaE"
                     /note="Permease subunit MlaE of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG0767"
                     /db_xref="CDD:440530"
ORIGIN      
        1 mtfvisilde vggtllflrn ilrtlfqkkl kthevfeqiw kvtadsfftt amagffvgai
       61 mtvqfamqmk efgalgylgg latsgtfrev gplliafmls gkvgaftsae lgtmrvteqi
      121 davrclgadp mqeiivprfi giiissffll ggglimsvfg gmlmgqafag vnfeeylrhv
      181 ptivspvsvl sglvkcfffs lvlatvctfr gytttggakg vgrsvvatav ttmvcivvmd
      241 wltsflgeii lqmirgyrs
//
LOCUS       WP_284607579             254 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: substrate-binding periplasmic protein [Bdellovibrio].
ACCESSION   WP_284607579
VERSION     WP_284607579.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..254
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28582
     Region          21..245
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 myfillvlfg lassghaaet lrvsyynfpp eilktstgly gashevweka akraqvkiew
       61 vgpvpymral hlletgkvda iyrlaktper ekvfvfseva pfwgktgivv lasdrlervt
      121 tdddikgkki gwlrggtppp fleknrkniv wepatdnsiq vnmeklaqkk iwgayfifss
      181 tayfynaqnn gpeikvlpfp gsekpnrmya afsktanpai vermnkafta eldgynyekl
      241 sqkyidmaak gllk
//
LOCUS       WP_284607632             332 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: diacylglycerol/lipid kinase family protein
            [Bdellovibrio].
ACCESSION   WP_284607632
VERSION     WP_284607632.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..332
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=36449
     Region          1..330
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mrvsvlinsk agsvnaelie akvreslfrc dlrfcrpqtl temcdflhge raaktdyiii
       61 cggdgtinva lqclmkcqds shippiaiir sgtandlahe igvskridqa irnifegtak
      121 yidvieveae gakaymltng glglpakaae lankfrshlq nlancpksak aykylaqksy
      181 yavkrmgpsv yslmtaeair twnpegwgle vsipgkvnie tqspivlvnn qqtigssflp
      241 apytsnsdgt vnlllsetkn ipehalaalh irrgsvekfp afksfelkef klrsvnperk
      301 ltffgdgeil hknvqelsir cihgglpvmv rs
//
LOCUS       WP_284607668             270 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Bdellovibrio
            bacteriopascens].
ACCESSION   WP_284607668
VERSION     WP_284607668.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..270
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=30618
     Region          39..264
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mkiyaraalg llffvglgiq vpashgtknr sqcerrfsvg lnnykplayr engrlyglah
       61 dlikeleekt gcefteiemg rptaaerinn drvdmlallv ksteyekggv fvpfynshre
      121 ltvaakifak nkkiedylad enikfaymig nrtviseeee ktllkgarli gtpdpegafr
      181 llkegrvqal lfsslvtdyy irqmsidkih rvadtgrkae vgfylsarrv ssaeremfah
      241 alaeikkdgs flrifskyms eeqalrrlnn
//
LOCUS       WP_284607735             352 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sigma-54 interaction domain-containing protein
            [Bdellovibrio].
ACCESSION   WP_284607735
VERSION     WP_284607735.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..352
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39652
     Region          <35..339
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mnennsttvl pssqnanqvm wntnqtskvv enktivyqse vmgslmkmid rvapstanil
       61 vlgesgtgke liarsihers grknkpfiai ncgalretll eselfghekg sftgaynrki
      121 glaeaanggt lfldeigeld paiqakllrf iqegeiyrvg gkdpikvdir licatnreld
      181 qevvkgnfre dlfyrintiv vsapplrrrk edipalvnhf lnnsqhayln rgrsvneeam
      241 kalvrydwpg nirelqnvce rlqilseghm imlndipeni rngemekdvi eydpsmtlhd
      301 lekryilkal ahfggnktqa annlgitikt lynklheyge fekfavhtkp mk
//
LOCUS       WP_284607824             304 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Bdellovibrio bacteriopascens].
ACCESSION   WP_284607824
VERSION     WP_284607824.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..304
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33449
     Region          6..283
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mnkkfhdlih easkvvldkd veirlamtcl lagghllied lpgvgkttlv qvlgkltglk
       61 trriqftidl lpadviggqi fhpqehrfif hpgplfsqlv madelnrasp rtqsallqam
      121 eegevsvdgv thvlpkpfyv iatqnphqqt gtfplpesql drflmslelh haskttevri
      181 lqgedprhsl qkltalftee eisealgqvd kiilssavaq yiadlleksr rpgfegapls
      241 tragmslaka akawaflegr nhvrpedvqq vlvpvlghrl ggnhgikrgr ewagilqknt
      301 pvps
//
LOCUS       WP_284607962             253 aa            linear   BCT 25-DEC-2024
DEFINITION  RsmE family RNA methyltransferase [Bdellovibrio bacteriopascens].
ACCESSION   WP_284607962
VERSION     WP_284607962.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Basturea,G.N., Rudd,K.E. and Deutscher,M.P.
  TITLE     Identification and characterization of RsmE, the founding member of
            a new RNA base methyltransferase family
  JOURNAL   RNA 12 (3), 426-434 (2006)
   PUBMED   16431987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..253
                     /product="RsmE family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=28613
     Region          1..247
                     /region_name="RsmE"
                     /note="16S rRNA U1498 N3-methylase RsmE [Translation,
                     ribosomal structure and biogenesis]; COG1385"
                     /db_xref="CDD:440995"
ORIGIN      
        1 mrrywiekkd lfqnqvnftg dvfhhifdvc rqdvgskfev ltedskayfv evtqvskksa
       61 taqileersi pplkephihv alsisrfpvm daimekavem gvksiqpffs efsflrkedk
      121 lsdnkverwe kivrsatqqs grgdlmiirp aipfekvsgl inrnegkvgl fayegpstls
      181 ikeyinkvka enpqgikevw iivgseggfs hgevqefskl glhpvtlgpq vlrvetacma
      241 lvsvlkydfd lmc
//
LOCUS       WP_284608145             452 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Bdellovibrio
            bacteriopascens].
ACCESSION   WP_284608145
VERSION     WP_284608145.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..452
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=50777
     Region          8..445
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mtstrvfsll ivdddplvhq slkmclpthw kvfsapklea iqyerfyhaa fvdmhlepna
       61 ktaagpqvie klvkhnnqle vvamsgdlsr elmenclkag aqrflakplm peeillvlek
      121 iealwdlrsv dpsadrrtvr wvgtssasqk ikkriadlrg eanpvliege tgcgkevvar
      181 llheqegerp fiavnvasip enlfesemfg hvkgaftgad qnkvglteaa nggdlfldei
      241 ealplsqqak llrfletgev rrvgakettq vktrvivasn kslekmvaag efredllyrl
      301 asqrielppl rerledidel ashflqaerp rrnktfaedg lktlkkynwp gnvrelkrvc
      361 eqlsltsplp fireedvlsw lkpaatpsga psytvidfnk glntlveefe ahvirsclkq
      421 trdieqaaka lqvsrsnlyk kvkdykieed ps
//
LOCUS       WP_284608176             108 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: HesB/IscA family protein [Bdellovibrio].
ACCESSION   WP_284608176
VERSION     WP_284608176.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Lu,H.M., Li,J.D., Zhang,Y.D., Lu,X.L., Xu,C., Huang,Y. and
            Gribskov,M.
  TITLE     The Evolution History of Fe-S Cluster A-Type Assembly Protein
            Reveals Multiple Gene Duplication Events and Essential Protein
            Motifs
  JOURNAL   Genome Biol Evol 12 (3), 160-173 (2020)
   PUBMED   32108236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..108
                     /product="HesB/IscA family protein"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=11620
     Region          1..108
                     /region_name="IscA"
                     /note="Fe-S cluster assembly iron-binding protein IscA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0316"
                     /db_xref="CDD:440085"
ORIGIN      
        1 miqispeaaq klahlkkeeg kddaaflrve vkkggcsgls ykmqfendqr egdkvfesng
       61 qkvavdpqsm lyilgmtley sgglngkgfv fnnpnaskhc gcgssfnv
//
LOCUS       WP_284608269             196 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ExbD/TolR family protein [Bdellovibrio].
ACCESSION   WP_284608269
VERSION     WP_284608269.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..196
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21769
     Region          18..188
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 maifrpgerh ryhnilskrk gkrdvtalls ltamvdmftv lvifllqnyn atgeilyipk
       61 evvlpkatsv relkpahvvt isskeilldk davatfeevk asedwaiqnl kdklqealak
      121 skaeqesklq nkirdvvest rgeaeedpna wskvtiqadk gvdfltvkkv lytvteagag
      181 einfavtklp qestsn
//
LOCUS       WP_284608270             158 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Bdellovibrio bacteriopascens].
ACCESSION   WP_284608270
VERSION     WP_284608270.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..158
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=16885
     Region          7..154
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mahidsgess grkrnielnl vpfidlmsvl itfllitavw tqvsmiqigs slygkksdtq
       61 ptptpppnad vvlkvdvkei gyvltvgkqv islpmvneqf deaglvaqlq rvkqlypekv
      121 davvsvadai pyeqlikamd nclsagfsai svatggpn
//
LOCUS       WP_284608280             177 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [Bdellovibrio].
ACCESSION   WP_284608280
VERSION     WP_284608280.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..177
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20270
     Region          28..148
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mnlffrllhi llfskfrskv dvlqecatpf rvwptdldvl rhmnngvyls lqdlarvdym
       61 iragaaevie kngwypvvas etirfrrslk lfqsfelctr llswdekyly lehkfvskge
      121 vialgmirar flskkgglva pqdllkalnl qlsapsfpeh leswisadvn hskslgl
//
LOCUS       WP_284608445             527 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Bdellovibrio bacteriopascens].
ACCESSION   WP_284608445
VERSION     WP_284608445.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19960403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..527
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=58546
     Region          <46..291
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          195..>292
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
ORIGIN      
        1 mmivkslava slllgsqgaf aeddlmnile gktssaaaqf veseevaklk kavnpssaeq
       61 niffqflvek nyekalfqws tafngsafqt tetgkaleaf lnyknglklt gveallaiqn
      121 pqkidntvis lwkenlndkd pvwgmaqvtw npywtqvfgv gaemavllqk syvsediaal
      181 telikktpvd skerailqwq lvlnlgirgd sakaaqvlah lmkvknnpid qdlmtltagr
      241 llyqngflda slkyyekisk ksdywfqaqe emawaymrkg epqnalaitk tltyphfkgw
      301 vgiesyllns fsslkvcdyp svlstmksik gqfgehlial eklsvdahqp avanlmkaln
      361 egavstaklg keahqlpsva skdevltllv krhgylmkes eiaeqlfaks ltfgnlqgqf
      421 etlknqvatr aqmtqgagyq rvqdlakael edskqvmqrl rivevemiqq vdsaakflkh
      481 agvseakkgt tgskdkfamn fandkeiwfd elsnfkvdvn kgcakre
//
LOCUS       WP_284608451             165 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ExbD/TolR family protein [Bdellovibrio].
ACCESSION   WP_284608451
VERSION     WP_284608451.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..165
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=18117
     Region          25..162
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 misdgilkns vlmgtleghs iisprgaklk rniaadlllt alidafsilv ifllmnfsst
       61 geilmigknq elpkahladv lernpvikid dgklyvedkl vtantitael lelrkkyqel
      121 hpgeafpgia tiqadrrvky eflnqvilgm nqagysdikf avvlk
//
LOCUS       WP_284608414             195 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NUDIX hydrolase [Bdellovibrio].
ACCESSION   WP_284608414
VERSION     WP_284608414.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..195
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22383
     Region          23..186
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mkdeilsrle npqpldlhtk ltrhacvaii lrgpslhyle vgfiqralnp ldrwaghiaf
       61 pggkredsdk sdleaalret keevgvdlhp dellgrlddv qarkggtlld fyirpfvfyt
      121 qrefavtlda aevadffwvp lkeiqnpqrq thytverefg hvklpavqld repplwglty
      181 mmilnlferl nglkk
//
LOCUS       WP_284608452             151 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ExbD/TolR family protein [Bdellovibrio].
ACCESSION   WP_284608452
VERSION     WP_284608452.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..151
                     /product="ExbD/TolR family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=16564
     Region          5..148
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD/TolR; pfam02472"
                     /db_xref="CDD:426791"
ORIGIN      
        1 mkhskkhldf evnlipfidl lsvsicflli tavwlnvgsm nvkqavggqa qedtkksplv
       61 wirmtpagdl dlevqqsslv paslrkfrvs qldkkvnyeg lekaltnlkq vepslntgli
      121 qptaatsyee iidvmdklkk sgmtdlgvsp l
//
LOCUS       WP_284608512             514 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: leucyl aminopeptidase family protein [Bdellovibrio].
ACCESSION   WP_284608512
VERSION     WP_284608512.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Drinkwater,N., Malcolm,T.R. and McGowan,S.
  TITLE     M17 aminopeptidases diversify function by moderating their
            macromolecular assemblies and active site environment
  JOURNAL   Biochimie 166, 38-51 (2019)
   PUBMED   30654132
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Lowther,W.T. and Matthews,B.W.
  TITLE     Metalloaminopeptidases: common functional themes in disparate
            structural surroundings
  JOURNAL   Chem Rev 102 (12), 4581-4608 (2002)
   PUBMED   12475202
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415720
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..514
                     /product="leucyl aminopeptidase family protein"
                     /EC_number="3.4.11.-"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0030145 - manganese ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0019538 - protein metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56045
     Region          94..513
                     /region_name="PepB"
                     /note="Leucyl aminopeptidase [Amino acid transport and
                     metabolism]; COG0260"
                     /db_xref="CDD:440030"
ORIGIN      
        1 makksapakn snklqfkswi etfdfgkelk vkneltgfvy flgvddsnkf sslvkqhsld
       61 wqadslktnd kdfvyfvgqq gpvwilrsrk ktsvghdgli deasyaward qfgslvshfk
      121 ahhlkavvid fhgteeaqdl galvgldiav ynfrqfvdgk qlldlprvai kkslgggldk
      181 alvkeamira ravnfarhmv nlppndlnpk tfaeiamkql sfpqtlkvnv wdtkkliqen
      241 mglhvavgqg sengpcmvhm kyrptkkskl kpvafvgkgi tfdtggldik pssamrlmkk
      301 dmggaasvig lalwvaesny pgpvdfylal aentvdgkaf rpsdvitarn glrveidntd
      361 aegrlvladv ldvactakga deaeyvidva tltgaikvgl gseiaglfsn ddvlaneltt
      421 agqragdlnw rmplfekywg emsspfadfk nsgggfggai taalflqkfv rgkkwahldv
      481 yawsdkaqga llssggsgqp vqcliefltk raek
//
LOCUS       WP_284608499             485 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Bdellovibrio bacteriopascens].
ACCESSION   WP_284608499
VERSION     WP_284608499.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 485)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 485)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 485)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..485
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=54132
     Region          164..482
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mflkriykff sgfsirlrls lifvlifgat tiffnmflfq mmidtlqqdf ddalfnysvd
       61 vsegieigik gdlsfpplrl dhgkilpfpl gtaliqvrhs sgavlarvgn fgefnppykk
      121 dferiwkgee atyrtiehir nipsaeadsy rlisfpldna akpqlllqia vpmtlletqi
      181 sqrltllqig ipfvlliata gglflsaral tplnnminta keikaselsq rvpipnande
      241 ikklaltlne mldriqqafl sqerfvadas hqlltpltim rgelellkkt ekkdidqfik
      301 salqevdnls sivqemllla rvdagigaln lqdlaldelv feavsrcekl anskniklkl
      361 ninnetaddr kiirgdndll lnlmvivien aikyspngev vsltlnykde vslfivddng
      421 pgipeeqlpl iferfsrgsn vgvrvkgfgl glaiaqkiai lhnaklsaqn hsgygarfsf
      481 eikni
//
LOCUS       WP_284608524             268 aa            linear   BCT 25-DEC-2024
DEFINITION  S1 family peptidase [Bdellovibrio bacteriopascens].
ACCESSION   WP_284608524
VERSION     WP_284608524.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Perona,J.J. and Craik,C.S.
  TITLE     Evolutionary divergence of substrate specificity within the
            chymotrypsin-like serine protease fold
  JOURNAL   J Biol Chem 272 (48), 29987-29990 (1997)
   PUBMED   9374470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475742
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..268
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=28223
     Region          35..261
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mlkkwtalla ttallaacge sqnsqvdita qqngviggdk vsagtaiaqh tvglydsksg
       61 slcsgtlise slvltaahcv vsdasyikvy fspdmretpe eltrqataal pnklynpegs
      121 edindvavir fagplpagfa papllqdfsr iqkgskviva gyglnwswgi kmgsgvlrtt
      181 elkvkqslyg aseimldqsv rrgicsgdsg gpayveingq lhllgvasrg dslpipltpd
      241 cfilsvftrv daqmswiqaa stqlmsvk
//
LOCUS       WP_284608696             265 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Bdellovibrio
            bacteriopascens].
ACCESSION   WP_284608696
VERSION     WP_284608696.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..265
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29754
     Region          25..244
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 makallfifi hllasaslal pdnslrivte nwppvtyeke gqaqgmavel ahliqkemge
       61 sdpievlpwp rayhvaktrp ntllftvvrt pereqlftll gpiangeiai ytrrtadlsf
      121 sdlnyvkeny svavhrgtaf hkvledngyk kivpvnssis glkmlmagrv dmlcddvlai
      181 hriseeagyp ydaqkkvtsl qhsslyfafs kntdkdiiek wkrsfekikk ngtykalykk
      241 wfgplsspte vllvsngkka piiel
//
LOCUS       WP_284608770             100 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: RNA recognition motif domain-containing protein
            [Bdellovibrio].
ACCESSION   WP_284608770
VERSION     WP_284608770.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio
  ORGANISM  Bdellovibrio
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Muto,Y. and Yokoyama,S.
  TITLE     Structural insight into RNA recognition motifs: versatile molecular
            Lego building blocks for biological systems
  JOURNAL   Wiley Interdiscip Rev RNA 3 (2), 229-246 (2012)
   PUBMED   22278943
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Clery,A., Blatter,M. and Allain,F.H.
  TITLE     RNA recognition motifs: boring? Not quite
  JOURNAL   Curr Opin Struct Biol 18 (3), 290-298 (2008)
   PUBMED   18515081
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Maris,C., Dominguez,C. and Allain,F.H.
  TITLE     The RNA recognition motif, a plastic RNA-binding platform to
            regulate post-transcriptional gene expression
  JOURNAL   FEBS J 272 (9), 2118-2131 (2005)
   PUBMED   15853797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Bdellovibrio"
                     /db_xref="taxon:958"
     Protein         1..100
                     /product="RNA recognition motif domain-containing protein"
                     /GO_function="GO:0003729 - mRNA binding [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=10785
     Region          2..86
                     /region_name="RRM"
                     /note="RNA recognition motif (RRM) domain [Translation,
                     ribosomal structure and biogenesis]; COG0724"
                     /db_xref="CDD:440488"
ORIGIN      
        1 mgkklyvgnl sfnvdsdqlt dvfaefgsii sanvimdrdt grskgfafve mssdseaqaa
       61 lqklngmels gramniseak pqenrsggnr rgsfsprray
//
LOCUS       WP_284608772             378 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Bdellovibrio bacteriopascens].
ACCESSION   WP_284608772
VERSION     WP_284608772.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 378)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 378)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..378
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42456
     Region          <35..377
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mekslesedk ktaesfkdsi karwikavhe qsggeqrnis pvtldsmdvf ldnlmsqlgp
       61 efrdhrkafn sdmaqrygrg ragvagyllp qffkeysllr qainaelyar gkltyktrni
      121 vdqaidstvs eaatefatak qehtqealtk aeisnrdleq fagvaahdlk splatisgyl
      181 dlldeelrni pespgleyve fmskalermr nlierlleya rlttkvkafq kvdlnhvvqr
      241 tlenlqsslh etrtridvsp lpqvlgdvdl lgqvfqnlfa naikfrsekp lvitvrvdgd
      301 inpaewrfsv sdnglgfdpk qkenifglyt tlhsgknyqg agiglatcrk vvenhggkiw
      361 aesepgkgsh fyftipki
//
LOCUS       WP_284608791             734 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Bdellovibrio bacteriopascens].
ACCESSION   WP_284608791
VERSION     WP_284608791.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriopascens
  ORGANISM  Bdellovibrio bacteriopascens
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 734)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20158983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Bdellovibrio bacteriopascens"
                     /db_xref="taxon:3044166"
     Protein         1..734
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=82781
     Region          124..>400
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          295..725
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mentpvndef lppgpqefrk rrreillvlv vsflfglltw feirlfatsq qlpfvhsiff
       61 fglvnfniil lllllfmifr nvvkvfverq gkifgsslka kliaafvafs fvptvlmfii
      121 svfyinssfd kwfsakmagv lkssievtna yyfnakkkny hfahqiadsi rplrsqndvk
      181 nrieklrkdf sldaveyyps lfgkrqvvta eddnvptvpa vsleflqkgi klqaeasiih
      241 qfgdgnlvrv ivpvqegaek gavvvssflp lsliskmndi staydefrdi npleyplksi
      301 ylyilvlmtf villaatwfg fylakqlsip lvqlgratrr vaggdytple vrsgseeind
      361 liasfnsmti tlertleeld qharytdtvl rnvsagvisv delgfvttin rhaaqllkie
      421 pekfigksvr dlltleyfrt faelqktmvd hkiesiqkel rlnvqgeaip llmtlsmlkd
      481 ekgqeigkil vfddmtpivn aqraaawtev arriaheikn pltpiklsae rlqrkfgtsi
      541 tdpafsectt mivkqvdglk nlvnefsnfa rlpqarpvva nlnsvveesl glyrqahpqi
      601 rfefnkdgel pdfkfdpdqi krvlvnlvdn svsavakepq atvqvmtryd kdiktvrltv
      661 adngegipaa drsrifepyy stkeggtglg laivkriied hngfiratan eprgvkmvie
      721 mpvnevgawk psge
//
LOCUS       WP_284608852             445 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Corynebacterium accolens].
ACCESSION   WP_284608852
VERSION     WP_284608852.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..445
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=49933
     Region          1..442
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mtslmwfrdd lrlsdnqalt raaeaatdkn gskpelvavv ldepaypstr plggathwwr
       61 erslhalaqe lasrgvkllr atgdartvip riahevgadt vtwnrryhgp lrevdarvka
      121 tladaginai scpgftlvep wevtnaqgnp ykvftpfaaa arsqladeep lpvpellagr
      181 emgtsasssw pnpsadepqw aaslaqywtp geagarerla qldlahyaee rdiparnats
      241 llsphlrfge vsprevwvaa aeepdaekfh sellwrdfaw hrlyhlpdla trnvrqkfnr
      301 fdwswndprl kdwqegttgi plvdagmrel whtgymhnrv rmvvgsfltk nlgvhwrlge
      361 ewfwdtlvda daasnpfnwq wvagcgddaa pffrifnpet qaqrfdpdga yiqrwaptls
      421 appivnlkes rqaaldayae ikdad
//
LOCUS       WP_284608869             344 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium accolens].
ACCESSION   WP_284608869
VERSION     WP_284608869.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..344
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35356
     Region          13..344
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mttinsilqa qqrrrhvrvl astlvfglia faaylvllgq gpldlsprqv ldvltgggse
       61 shirvvwdlr lpvaiatviv gaalgvagsw tqtmarnpla spdilgvtgg asvlvvlgtv
      121 hsrpgfaddi pdfwwracla migallvvil lavlggigts nrivivgial slmfqaivay
      181 lmrsaqiqra aeaqtwlags tgfvrmeviv pllvalapfl aigiwcarel pllahddssa
      241 ttlgvnisrq rallliaatg icavvvsvvg pigfiallap hlarmvartp tpspvasaaa
      301 gaalltvcav iagaipvnap vgavssvigg calvvlvwna arrs
//
LOCUS       WP_284609004             341 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium accolens].
ACCESSION   WP_284609004
VERSION     WP_284609004.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..341
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34516
     Region          25..337
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msvrttrllg lgallllvlv gticsllyga rsipaedvwt alrelpaarg gqeevstnqr
       61 vvaelrlprt ilaiivgaal gvagaliqgh trnpladpgi lgvssgaals vvvsfalfgi
      121 tapwatvvva flgaiaatal vfglasagka avdpltlvlg gaalsavlsa itsafvltne
      181 nnldrmrfwt vgslagrdmn ialgilpfvv lglvlafatg pqlnilnlgd dvaaglgint
      241 taarlggmgi iallagaata aagplgfigl vvphivralt gpdykwilpy salagaalll
      301 cadvvgrlia rpgelqvgiv lafvgapffi aliyrkkvmt l
//
LOCUS       WP_284609471             938 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium accolens].
ACCESSION   WP_284609471
VERSION     WP_284609471.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..938
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103634
     Region          4..936
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtethldtfa aglpypldef qvqgceaven ghgvlvcapt gagktvvgef avslalsrgt
       61 kcfyttpika lsnqkyhdlv aehgedavgl ltgdvsinad aeivvmttev lrnmiyadsp
      121 aldrlthvvm deihfladas rgavweevil nladhvsiig lsatvsnsee fgewlstvrg
      181 dtsvivtehr pvpldqwmml grkiyplfep esggqvnsel erriqrleag dsddgradyk
      241 sgkgfrarar hkgggrsefh gkpggrsgas rpqdryrplg rpevlkvlqs qdmlpaitfi
      301 fsragcdgal yqclrsrmvl ttqeeaeeik aivdagvegi peedlqvldf rrwrealsrg
      361 faahhagmlp afrhivedlf vrglvravfa tetlalginm partvvlekl ikfngeahvd
      421 ltpgqytqlt gragrrgidt lgnavvqwap amdprfvagl astrtyplis tfapgynmai
      481 nllgmlgfed slrlleksfa qfqadgsvve etreleraeh rvrelreqld davaalappa
      541 kdgedpaevl mdyirlrrel taeekqskvd kehqrtqevv avlarlqlgd viaiagkkrp
      601 tlaavvtpan qtedprpwvt tesgwsgrid atgisnppiq lgrikipkpv rknprrntky
      661 iqdifyrekf drpkrmkskp rlrpnkrvge lrdairehpa hdwpatdreq lagvaqklar
      721 rerdleklqa kvdkatdtlg rtferivdll aemdyvefsg agsdrtpvit eegerlakih
      781 sesdllvaqc lkrgiwdeld paelagvasl ccfenrkatg gqpeaatdrm adamnatwri
      841 ytelgaderr hrlpptrepe agfalaihqw aagaplgycm aaaneagael tpgdfvrwcr
      901 qvvdllqqia ktgydgqiqr narramdaiq rgvvaiga
//
LOCUS       WP_284609472             373 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium accolens].
ACCESSION   WP_284609472
VERSION     WP_284609472.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..373
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39886
     Region          26..372
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mttqafspev ysrrlsaaqe aaaqqgidll ligtgpdfay ltgswvsshe rltvlavpqs
       61 gtpwivspnt ditdiksapv gkldvelrgw ndgdnpyela legaasinkv algqsltadh
      121 ilqfqglvsd adyvlatyal aelftrkdea eiaelrkagq aidavhakvp ellqpgrtea
      181 evahelekli leehsiidfv ivgsgpngan phhsfsdrkl aagepvvvdl ggtlpsgyhs
      241 dctrtyvvgg dlsqapqdfq dayavlydaq aaaraaakpg staeeidgva rkaiadagwg
      301 dkfvhrtghg iglstheepf imegndlale egmafsiepg iylegqwgmr ledivvltkd
      361 gyeslnvver evr
//
LOCUS       WP_284609592             234 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium accolens].
ACCESSION   WP_284609592
VERSION     WP_284609592.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..234
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24641
     Region          7..228
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(16..17,19..20,23..24,61,65..66,69..70,90,97,
                     100..101,106,121,125..126,128..130,132..133,136..137,
                     140..141,167..168,170..172,174..176,178..179,181..182,186,
                     189..190,196,198)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(124,128,131..132,134..135,181,184..185,187..192,
                     195..197,201,203)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(145..152,169,172..173,176)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mlrrssidpr tvllsvlvin avalshghlp tllisiafss ialatvkphy gliclcafal
       61 sylgywgllq lpgstffafs aaifswlsrf visisigafg lltltpstlt salrdlrlpg
      121 watippavfl rvlpiivaea kairdamvlr glqpgvkswf tqptqssaml iipllgavvr
      181 agdelaasal vrglggptrp tttadlsfkl vdataiaglg lvvasvwlpt evrl
//
LOCUS       WP_284609700             198 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Corynebacterium accolens].
ACCESSION   WP_284609700
VERSION     WP_284609700.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..198
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20238
     Region          <88..198
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mkkyvfgtvi aaiviavlvv vgvmqlrgdd tgagesaqap gagsesgaag dqdvaerpdc
       61 pagpiagvdl eclggdeagq gekadegiti anvwawwcep craelpylde vaeshpdwkv
      121 igvhadknaa ngaaflndvg vdlpsfqdpd nsfagtlglp gvvpvtvilr dgevikqaaq
      181 pftsadeiek tvkealag
//
LOCUS       WP_284609781             119 aa            linear   BCT 25-DEC-2024
DEFINITION  FluC/FEX family fluoride channel [Corynebacterium accolens].
ACCESSION   WP_284609781
VERSION     WP_284609781.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   McIlwain,B.C., Gundepudi,R., Koff,B.B. and Stockbridge,R.B.
  TITLE     The fluoride permeation pathway and anion recognition in Fluc
            family fluoride channels
  JOURNAL   Elife 10, e69482 (2021)
   PUBMED   34250906
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Li,S., Smith,K.D., Davis,J.H., Gordon,P.B., Breaker,R.R. and
            Strobel,S.A.
  TITLE     Eukaryotic resistance to fluoride toxicity mediated by a widespread
            family of fluoride export proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (47), 19018-19023 (2013)
   PUBMED   24173035
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Stockbridge,R.B., Robertson,J.L., Kolmakova-Partensky,L. and
            Miller,C.
  TITLE     A family of fluoride-specific ion channels with dual-topology
            architecture
  JOURNAL   Elife 2, e01084 (2013)
   PUBMED   23991286
  REMARK    Erratum:[Elife. 2013;2:e01700]
            Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..119
                     /product="FluC/FEX family fluoride channel"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:1903425 - fluoride transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:1903424 - fluoride transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12968
     Region          5..106
                     /region_name="CRCB"
                     /note="CrcB-like protein, Camphor Resistance (CrcB);
                     pfam02537"
                     /db_xref="CDD:460582"
ORIGIN      
        1 mnllfvligg ffggaarygf trllpspyct fvsnilgslv fglavgfaql adapfahplf
       61 alglagglst wstmakelge mvkqrhwwpl ckylfwtigi gvvlawrgvm waeliyhgi
//
LOCUS       WP_284609784             241 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium accolens].
ACCESSION   WP_284609784
VERSION     WP_284609784.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 241)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..241
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26359
     Region          71..237
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mskvsdpnak sgngfiwgvg vllviiavvi gyivwngkqa neievqdvnm smdykdnait
       61 lksdaadddt pevdlyedfs cphcadlaen tdedmkqaie dgklivhvrt lnfldgedve
      121 nedgystkav aamselaksg dvktywnlrd ymmknqqsia tkwgtediad qakelgaedd
      181 vvdsiknvdi kqgnkvakan ydklnkatgs vssprivqdg kdipdresge slndwvdiat
      241 k
//
LOCUS       WP_284609910             375 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium accolens].
ACCESSION   WP_284609910
VERSION     WP_284609910.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..375
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40160
     Region          7..368
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mnhgpgltfr flaaqvlvvv isllvaaava tmvgpslfhd hmlmtgredp slelfhaeqa
       61 yrganlitlv valptalisa llaslwlsrr lrtplqdltr aatsltagns rirvpageag
      121 pevttlahaf ntmadrleht eqvrrqmlsd lahemgtpls vltvyldglq dgvvdwnnat
      181 htimadqltr ltrlmedidd vsraqehrid ldlaeeglgd llhtaaaaag eayadkgvdl
      241 qietithtar alvdrqrfgq vmsnllsnal rhtpaggqvr isihrqgast alihvaddge
      301 gippdqlryi ferfyrgdaa rsrddggagi gltiskalie ahggtltats pgpgrgavfa
      361 lrlplsppds eeaar
//
LOCUS       WP_284609952             262 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Enterococcus faecium].
ACCESSION   WP_284609952
VERSION     WP_284609952.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..262
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28850
     Region          1..259
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mnledkvvlv tgssgglgaq icyeaakqga iviscarrma fvegvrdecr rlsgkeayaf
       61 kvdvsdpysv delyekvmee vgrvdilvnn agfgifedfl tfdlgkaydm fevnilgmmv
      121 ltqkfainma errqghiini asmagkmata kstvysatkf avlgfsnalr lelkplgvav
      181 ttvnpgpiet dffdkadpsg rylekvgqiv leptklakmi vrnmrhpkre inqpfileva
      241 skfytlfpti gdylasgifn kk
//
LOCUS       WP_284610053             294 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Corynebacterium accolens].
ACCESSION   WP_284610053
VERSION     WP_284610053.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..294
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30914
     Region          5..282
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(34,231,234)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(181,202,229,232..233,236)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mtihvcgegl vdlvpvspgr lndltpalgg gpfnvaiaaa rlgadvefqs ristdgfgqe
       61 lfrrleeegv etahvqrgee pttlavttia engtasynfy vegtadrfve pklapadiac
      121 fgtvslalep gasryaqllr dfaaqgtlva ldpnirpfya teahkkflad llthvsvlkl
      181 sdeevdflge efthqvpiva ttrggdgisv ragdtsldvp aaavevtdti gagdtimaal
      241 ltqldergld adkaaalsae ewrdilhfaa taagitvsrt ganpplrkev esal
//
LOCUS       WP_284610171             292 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Corynebacterium accolens].
ACCESSION   WP_284610171
VERSION     WP_284610171.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..292
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32080
     Region          2..274
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mtvgtisevl alegtqeadv fsgpaipsqi ertfggqvaa qalaaaqrtv dnkqvhslhg
       61 yfvgpgdtkk plelrverlr dgrsfasrqv rviqdgrlvf imlasfhrdg dtgpehqdma
      121 pqvlspdeaa rrgggapyst riilkewtdw dirlvpdegr ddaaaevtga gyrhiwfrnt
      181 gelgsdpdfh raaltymsdm tllrsaliph qgekiqlasl dhavwflrpf rvdewllyeq
      241 vsptasqgta iargklfteq gdlvalvnqe gltrfldenl gsgsahgnwh nv
//
LOCUS       WP_284610223             240 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium accolens].
ACCESSION   WP_284610223
VERSION     WP_284610223.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..240
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26135
     Region          12..204
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mttvsnsqll srpaaifwdm dgtltnsepl wgeatyylse vlgkrltpsq rmdtvgatft
       61 ttlricadna gvvlgegdve ayrhkmfdym ktlfagrlei fpgipellts lhhdgmpmmv
      121 ttntdrdvad aaiavigsey fvdticgdev ptgkpapdmy leaarrlqln paqclvfeds
      181 pagmraavaa gctviglped egvevpdgvv eisrlrdsrh lagalhtdvy ewfraiqemn
//
LOCUS       WP_284610230             373 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium accolens].
ACCESSION   WP_284610230
VERSION     WP_284610230.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..373
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39935
     Region          26..372
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mttqafspev ysrrlaaaqe aaaqqgidll ligtgpdfay ltgswvsshe rltvlavpqs
       61 gtpwivspnt ditdiksapv gkldvelrgw ndgdnpyela lkgaasikkv algqsltadh
      121 ilqfqglvpe adyvlatyal aelftrkdea eiaelrkagq aidavhakvp ellhpgrtea
      181 evarelekli leehsiidfv ivgsgpngan phhsfsdrkl aagepvvvdl ggtlpsgyhs
      241 dctrtyvvgg dlsqapqdfq dayavlydaq aaaraaakpg staeeidgva rkaiadagwg
      301 dkfvhrtghg iglstheepf imegndlale egmafsiepg iylegkwgmr ledivvltkd
      361 gyeslnvver evr
//
LOCUS       WP_284610272             218 aa            linear   BCT 25-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Corynebacterium accolens].
ACCESSION   WP_284610272
VERSION     WP_284610272.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..218
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=24492
     Region          3..200
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mlicqemfll ltkdngkkev lsnnetalra glfsdlllhe avaitaknkv hatdkkpehp
       61 vlawawdslh ehrtssvktl lqarwfspre kiaqnfqdrg qlkiedaaww qlsgdryimt
      121 dtalenevre rlaavldgtq npstkdmiil dilrevngay pllkedapem krremrnrik
      181 elkqqveydd aaasavktil qettaiiaav avstagtt
//
LOCUS       WP_284610420             158 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Corynebacterium accolens].
ACCESSION   WP_284610420
VERSION     WP_284610420.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..158
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17277
     Region          57..>114
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mnvrrvsmds lrgrrtlstl svrgeftpaq akardkakar arrsdsighl gpeavaafvd
       61 gemepkamhr vrihlvhcae cradvhhqrh asewvrhcsd dsavkapqsl laklagmate
      121 gvapgpdast pahrpeqdfl dkvetvvrai khnqrgqn
//
LOCUS       WP_284610443             610 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Corynebacterium accolens].
ACCESSION   WP_284610443
VERSION     WP_284610443.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..610
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66418
     Region          13..610
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mtlqqvhtqa eftiepgetc ltalmdtakk rphgvmftrp anyewvnvtg kefidevfev
       61 aqglialgve qgdrialisa tryewslldy aiwaagaasv pvypsssasq vrwiiedsga
      121 vlaitetreh selvenlvlq ddgepnlkgs psqlrrvlei nssaidtlkf egrsvgtdev
      181 sariaatntd dlaslvytsg ttgrpkgcil thrnwlsear alttnpigvf avpgshtltf
      241 lplahvfsra vsiavairga sqnhwsdfst isiefarsrp nvilgvprvf ekvrnsaask
      301 aadsgiksfl feqsekiaie yskaldtpdg pdrllkikhk lfdklvysti rqgvggnvry
      361 citggsamgh dllhwfrgig vpiyegyglt etaaaaavdy vdqsigtvgp plggvtlrin
      421 ddgevcikgg mvfegywndp eateeafedg wyntgdlgei dddgkltitg rkkdlivtag
      481 gknvspgpme dilrghplis qamvvgdgkp fvgalitldp dilkrwkldh nipenrsmdd
      541 iatdatlrae vqdavnkvns tvshaegikk fyilesdlte deneltptmk vkrnvvaqry
      601 asaiehiykr
//
LOCUS       WP_284610481             181 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium accolens].
ACCESSION   WP_284610481
VERSION     WP_284610481.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 181)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..181
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19610
     Region          4..156
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18879"
                     /db_xref="CDD:467590"
ORIGIN      
        1 mptpdyivkl resighdqif vpacsaiilr dvptgaalwe vpsvllvkra dnavwtpveg
       61 icepgeeitt talrevkeev gldakveavl gvgqsgpvty pngdecmfms talrlsvadg
      121 aepvisdeen teaqwfsvah lpdsvsrrhr lmiadavahl khpqgfsprm gwmkrseqpg
      181 l
//
LOCUS       WP_284610490             471 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Corynebacterium accolens].
ACCESSION   WP_284610490
VERSION     WP_284610490.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..471
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50062
     Region          3..465
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mdkqphaviv gagpngltaa arlatagwcv dvyerashpg gaavssteif pgtivdlgaa
       61 ghpfgiaspa fraldleshg lrwrhapypm ahplegaqag ilhnsleeta aglgtdaraw
      121 trlhghvvrn idahvnnalt plvrwpehpv rlaqfgapgl lpasvlaraa ftspqaralf
      181 agsavhaits ptraftsafg llfgalgmtr gwpvveggtq aladalvsll rshnariytg
      241 aditderslp radalilnlt prqilrlggl dlpartrrnl rrwrygsavy kvdfhlsepv
      301 pwadprvgqa gtvhvggsve eisgaerdig krrmpvnplv mvcqqyvadp srglvlwtya
      361 hvphgyeery prevtgliar qierfapgfr dtilatrats padlerwnpn lvggdiagga
      421 mtglqtvlrp rlsahphrla pgifmasgst apgagvhgmp gwwaagdvat p
//
LOCUS       WP_284610572             513 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium accolens].
ACCESSION   WP_284610572
VERSION     WP_284610572.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..513
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=56004
     Region          169..510
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 madsqenpaa grpaqaqsqp qraqqpqqpp kkwheqldql pqqgqgkkkr skrdyirqip
       61 qamplrtwlv vllvvisglg ltgssfavns imrnvlynnv dselrsasss wardvgndff
      121 lgdhtkrppt eyvvlnylpd gtirysgpts ttpdvegvpl ggypttvgsi enntkwrala
      181 fadsngvitv iakdmtheke ilhglamvqv siaaialaam agvgfwfirr alrplrvves
      241 taseiaagdl dkrvpewplh tevgqlaaal nimlghlqrs vvtaqekeeq mrrfvgdash
      301 elrtpltslr gytelyrsga tndvdlvfsk idkeskrmsl lvedllaltr aegtrldlrp
      361 vdllelslsv gssaraafpe revkvinnaq sipvvngdad rlhqvllnli snglrhggee
      421 atvtlqlrrd nkdilvdvid dgkgmsseda ahiferfyra dssrtrdtgg sglglaivhs
      481 lveqhggsvs vdsklghgtt ftvrlpalde pad
//
LOCUS       WP_284610663             425 aa            linear   BCT 25-DEC-2024
DEFINITION  Mur ligase family protein [Corynebacterium accolens].
ACCESSION   WP_284610663
VERSION     WP_284610663.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13558984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..425
                     /product="Mur ligase family protein"
                     /calculated_mol_wt=44747
     Region          64..>187
                     /region_name="Mur_ligase_M"
                     /note="Mur ligase middle domain; pfam08245"
                     /db_xref="CDD:462409"
     Region          312..410
                     /region_name="MurT_C"
                     /note="MurT ligase C-terminal; pfam08353"
                     /db_xref="CDD:462442"
ORIGIN      
        1 msfsvpgalk klrttaatsa aklattasra tgrgaggmig glianaidps imtnlgggrp
       61 avlvtgtngk stttrmlaaa vraehhvatn dggdnmdagi isalmagkda shlvlevdel
      121 hvphvadnln pqalvllnlt rdqldrvgei nkieralrga veahpdmlvi ancddvlmts
      181 vaydaknviw vsagagwlgd svtcprtggh vvrteddwya vkpladgref rrpqptwgid
      241 khgvitptak rplnlalpgr anrgnaaqai aaavegfgvd ldraiaaaes iddvagryst
      301 ihwkgreirl llaknpagwq ealsmvdrsa dglviatngq vadgidmswl wdvkfegfng
      361 lsvkaagerg tdlavrlvya dithelipdp mdalaacpeg rievlanyta frdlkkalsk
      421 eanna
//
LOCUS       WP_284610874             351 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium accolens].
ACCESSION   WP_284610874
VERSION     WP_284610874.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..351
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=36780
     Region          8..348
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mrpteldatr tattsvrtia aryrrretiv lfvgiaavll aavvaltypg agldrvsawq
       61 alihpdsgfg ttliyewrlp rvtaaivvga glaiagtlfq tvtrnplgsp diigfntgay
      121 tgvivvsylg fssfinvalg avigggital iivvlalrrq vsgmrlilvg igvsltlsav
      181 nrylilsadl dtamaaatwa agslngiewi fvgpaaivla liivlaftlr srcealelad
      241 dtayslglnv trtrlvlvfl salltalcta lagpisfval aaphltrflt ggqrvslpag
      301 aligatlllv cdiigqqlfh ptmlpvgvvt vtlggtylii lmlfahrtyr r
//
LOCUS       WP_284611104             402 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Corynebacterium accolens].
ACCESSION   WP_284611104
VERSION     WP_284611104.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..402
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43713
     Region          1..396
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 manllgivff algigltval heaghmftar afgmrvrryf igfgprvfsf rkghteygla
       61 afpvggfcdi agmtaqdefl teeekpyamy kkpwwqriiv laggigvnli lgfvilyfva
      121 mtaglpnpda dvrprvgevt ctadqkenqe lesctgngpa gkagvqegdi ilaldgehld
      181 sftqlrdevm qrpgetvtlt verggeekdf sieletvkrl nqqgelvdag siglsnevld
      241 ivekhsatea lpatwhftty sleatvegik qfpakvpgvv asifgherdv ngpmsvvgas
      301 rvggelvers lwasffmmla tlnfflalfn liplppfdgg hiavilyeki rdgirelmgk
      361 qplgpadytr lmpityvmaa llmglgvvii iadvvnpirl fg
//
LOCUS       WP_284611157             475 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium accolens].
ACCESSION   WP_284611157
VERSION     WP_284611157.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..475
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=50801
     Region          8..402
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mkttthgals rlhkfagviv apflivaals gffyalaptl eqwvyhdeit ataqgsprsl
       61 ddqiaaaqrq hpgaavaave asedpeettr vlftdpdaks psythavfvd pvdlritgee
      121 qqyggsralp lrtwlsnghr tlwlgepgri yaelaaswlg altivgvylw lkrrkktqkk
      181 nnkalrihar lgswllpgfl fltitgltws mvagsnigkv reelnwkeps vatsvaeaga
      241 gagaganghe ghegheghag hsggevtdnd vlegaqtals tarsegltgv lrmtppeqag
      301 dawtvregra ayklrsdava vtadgrvidr insadwplaa rltswliqlh mgtlfgiysq
      361 valaalalgl lvisiaglwm wwnkprrrlp elkitpavva gvviysiiap lfgaslllff
      421 agdwlvhrlr pqsrsrsgsq sgsqsgtgrs ngasgptarp rgesssrips tvqng
//
LOCUS       WP_284611416             359 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium accolens].
ACCESSION   WP_284611416
VERSION     WP_284611416.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..359
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36131
     Region          50..350
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msattkggqn iqtgstaesr tatpvmargk grktflvali ltslvlavas lalgsrsipp
       61 deviaalrga geqdirdivw nlrmprtfla yfagaalava gvlaqswtrn pladpgfigi
      121 tagasffval gtaigiattt gmrttlalvg agittllvla vsrrfqdplt lilvgagvsa
      181 algsgaviig lystdvldsm rrwtigstfg rgpedvtiag iglliglaca amaarpldll
      241 amgeessral ggspttarvg aalsvvvlag sataatgpia fvgfaiphiv rrvvgpsvat
      301 milpsallgg cavlaadiig rlivgnsele msivlaivga pfliwgahrg vgrawgdna
//
LOCUS       WP_284611624             671 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Enterococcus faecium].
ACCESSION   WP_284611624
VERSION     WP_284611624.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..671
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=76962
     Region          5..654
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mnykisyllk tpreisleka aeiievntse aikqltpfae yvddthirik kfraidwaek
       61 flditrfeav yteqerrdll ylmvystats vsvfhfqdfl qvskgtvlsd ikkirnelev
      121 edcqlsytrk tgfrllgsea ilrreaknrt arlmqslagr fgltyltaml sldcyakard
      181 lldntislsd lrfapnrmde layylslttn rmgkisienv kdaellasla vtdisrqvlt
      241 slgysehqns eiiffslcla sivegdvqep aldfllecss evihrmeflm aiefdsfrel
      301 lmnvfyhlvp ayfrisysfy lpnvmidqik hqyasiyemt rkallplekr igksipeeev
      361 gfftilfgge irkvdaeern rkiravivcp sgissslilk selqqlfpmi fftetnsadr
      421 lhevdetsyd iifstvpltl tdkkkslyvl hpimtdlekn qlinqvqrdw lipgfsmpsa
      481 qellsallpy ielkegvdee klyqvlnrkm nkllekkedq rpmlsellte emiqlsdqpk
      541 nwqeaitfaa qpllsenkie esyikamier veqygafihi gdhialphar pedgvnevgm
      601 sllklqqpvd llddpahpis lficlaaidn eahlralanl tkllsnkqnl qdllhastke
      661 eilaiirkgd e
//
LOCUS       WP_284611526             435 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium accolens].
ACCESSION   WP_284611526
VERSION     WP_284611526.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45965
     Region          12..421
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 msqpnprevi ttqalmiwia amavylvait grssfgvagl daierfdvda griavftsvq
       61 lgvyaiaqip tgmlidkfgp rillvvgavi mgvgqvilgf tsnygvaifa rvligagdat
      121 gflsvmrilp ywfplhrtpm ftqvtssigq mgqfisavpf lwllgtagwt aafvtlgavg
      181 ilvaiaaava vadspeklgv iplekeppns qgssigarlk avftspiawq ayfihysgml
      241 plivfvmlwg mpmmtqgmel skgkaslvlt llavflvlvg plhgrissra qnirpwvalg
      301 fvclhvltwv lffafgtggg lvaitvvsfi lalctptsny gfdiirenmd rsvvatatgl
      361 gnmggftsgm lgaqlfgmvl dhsadapnys mpdftsaala vlavwlcgma gvvithilrr
      421 rggyagpsvr ivevt
//
LOCUS       WP_284611679             329 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Enterococcus faecium].
ACCESSION   WP_284611679
VERSION     WP_284611679.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..329
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35475
     Region          24..326
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mrtmkknrll llvcfvllii ffvalsngaa tvgkadfwqa lfdfdrskqs hqiirnirlp
       61 rvagaflvgs cfalsgalmq gvtrnplads gllginagas lamalsfafw pkasdfsvfl
      121 mslagsfavt llvfgflqfs kmgmnplqli lagvaissff taisqaltqf fnlqqdlafw
      181 fvggaanitw kqlavlfply ilavlvsfsl gkaislihls ethalvlgsh pkrtrlivfc
      241 lvavlaaiav slvgpvsfig llvppvvrgm vgtdyryvlp vsflvggglv mladftarmi
      301 nppfetpfgl vialigvpfl liqvrreqr
//
LOCUS       WP_284611814             179 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium propinquum].
ACCESSION   WP_284611814
VERSION     WP_284611814.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 179)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..179
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19342
     Region          4..158
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18879"
                     /db_xref="CDD:467590"
ORIGIN      
        1 matpefitel rkhigsaplw ipatttvvir evpadapiwe vptvllvqra dsgdwtpigg
       61 icepgeqphd tavrevkeet gldivpvall gsgavgpvty pngdvcqfmd taisarlvge
      121 ydqqprvadd esvdvqwcsv ahlpqslsar hrmviadava qmknparfrp rlgfnkrng
//
LOCUS       WP_284611824             346 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Enterococcus faecium].
ACCESSION   WP_284611824
VERSION     WP_284611824.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..346
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39921
     Region          4..221
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mshpifsiii piynaedtia htievlknla feeyevilvn dgstdkteql iqsaiqgdsh
       61 fqlfttenqg pglarnegik qatgkyvlff daddepvkei ladyqqlfeq ypeadlliss
      121 ftfrtlsgee iisekdylvp eyqytdhkqf vddmyqlmnq qlmyvvwnkc ykreilmekq
      181 ilfknyssce drifnlnyye hcqqvilnpr ieyiyhfegg kgitnqykpn kfetfkefye
      241 lanvvtsdkd kpgmaslllk gttsvifsiy ensertakek reeamhilnd paiqeakkia
      301 ltdssakkvt kwlynlpapl llsavkagsf vevkmpsima llkrvy
//
LOCUS       WP_284611826             394 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Corynebacterium
            propinquum].
ACCESSION   WP_284611826
VERSION     WP_284611826.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..394
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42356
     Region          13..378
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 matdaslnkq hdpaplagvr vldcsrvlag pfcamiladl gaevikvesp wgddtrqfgp
       61 yyegestyyr lfnrskksit ldfksedgkq tlkelakhsd vvvenfrpgv lsklglsadq
      121 lmavnpgliv tsisgfgqig slakepaydl vaqamsglms itgwpegkpt rvgislgdiv
      181 pglyaaigtv salyqrvntg kgqhidlamy dslisvmesv gmralhgdtp psrigndhgl
      241 sapfstyatk dgdiviaitt nrlfdrlcea ldlqhlaedq rfataenrsd yrddlreele
      301 trlsdltmge aialfeehgv ptarvyeldd alksplaqer gvvatesdgf atlasplkls
      361 gmtgpvpasg lgqfndeies wlsepvkdeg qand
//
LOCUS       WP_284611908             239 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium propinquum].
ACCESSION   WP_284611908
VERSION     WP_284611908.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..239
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25455
     Region          76..221
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mskkvtnpnq kssagfigai vavlvivvav iayiviagqg akaekfanwe ikqvsaetsf
       61 dgntltfgaa dkaphvdlye dfscphcahl aeatdaeale einagnlavs ihpmtfldnq
      121 gdghstqava allalaehdd vnalwnlrea mfenqqdiar swspddfada aaqmeasdea
      181 vedirsgkfl ekareagean gtdleskvgr vstprvlmdg kdlevedind wvkvavgsk
//
LOCUS       WP_284611945             203 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Corynebacterium
            propinquum].
ACCESSION   WP_284611945
VERSION     WP_284611945.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..203
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21885
     Region          36..154
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mptwndltrn npshsenyaa rwkrfvaegk didgearfid alsprgaril dagcgtgrag
       61 gplidrghtv agidldpvli nhakhdfpng ewhvgdlgsa tlydqpalgh mrgsfdvvfs
      121 vgnvlgfidp vdrehaienl yaplrpggra vlafgagrgw gfgefldsct aagfaqdlll
      181 ssfniepfdt dsdfliavlr rpr
//
LOCUS       WP_284611997             505 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Corynebacterium
            propinquum].
ACCESSION   WP_284611997
VERSION     WP_284611997.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..505
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=57956
     Region          5..504
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mstpqpalmw frddlrlrdn saldwiaqqg pviavvieed pettrtrelg aaarwwwqrs
       61 vhqlknslaa hgvpllyhsg dpreiipaiv eefgvsavgw srryheplre ldaeikqmlh
      121 ergvtarsfa ghlltepwev ltqqgkqykv ytpfaktart iaevnvasyl nnvndqapsp
      181 tghdelspig lagpgtdfpa ssplpdwnep dwthtlaqhw lpgenaawki aeefldqlaa
      241 aarkqaphya adrdrldkqa tsrlspylrf geisihrlwa lvteasdtgr iagedasafl
      301 nellwrdfaw hrlyhlpelh rrnvrqqfdh fdwhwdetea qrlsttrrdp rcaeatedlp
      361 tddfrrvfsa wragqtgiav vdagmrelwe tgtmhnrvrm vvasfltknl gihwrhgeaw
      421 fwdtlvdadp asnpfnwqwa agcgddaapy frifnpdsqa krfdphyryi rhwvpefgtp
      481 mypqplvdlk esrrqalaay devkn
//
LOCUS       WP_284612081             294 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Enterococcus faecium].
ACCESSION   WP_284612081
VERSION     WP_284612081.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..294
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=31815
     Region          1..294
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mkkvllvvnp ssggeqakkf eqlaiakles vfdevvvlht kkagdaknft reaategyhs
       61 vfvmggdgtv negisgiaeq ehrpnfgffp lgtvndlara lgiplepeea inhfsiesvk
      121 pldigkindd yfmnvvaigs ipeaindvda ekktkfgkla yfmsgikqla stqsysfhve
      181 vdgkkeeies stlligltns vggfetllpn akvddgklhl vylkdsslid tlktlpdllk
      241 gvdestknla yltceqlvvs ladeeelttn vdgdegdklp vtikvlpshl qvyc
//
LOCUS       WP_284612110             228 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Enterococcus faecium].
ACCESSION   WP_284612110
VERSION     WP_284612110.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..228
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26275
     Region          1..224
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mllyfiigcc igsflcltaq riplghsiiy prshcvkccr slswyelipi lsiivqrfrc
       61 rycrcrlpfy yllaevlcgg lfawfftfss arnfstfiwv lsallfslmd lfyfmvhsht
      121 lfcswailwi fwlqagvfqw qsvlltfivg gaclrygqsy lgagdtllml swsgglslee
      181 llqilflasl fgisvfsvyf ichkkkmekl pfipflssal livlhlry
//
LOCUS       WP_284612180             348 aa            linear   BCT 25-DEC-2024
DEFINITION  GntR family transcriptional regulator [Enterococcus faecium].
ACCESSION   WP_284612180
VERSION     WP_284612180.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450768
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..348
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=39105
     Region          1..>77
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
     Region          75..346
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mnqplyqtif ndlqtailtg elpvdsqlpt ekelsrtykv sritskralt eleqlgliyr
       61 vrgkgsfvks aspeqmlasp tktrrilfll pyvadlsvgd fskglnpvmq dkqidvmmtt
      121 ldflqnktak elinefdgli yyaldteqhl dllfelslke fpvvildkki yelpfptvls
      181 dnfqggalaa sylieqghsk iaylfgtqth pqsvrqrylg ylealdkagl tfhtslddks
      241 atldellsyi tkyevtafvc endvvaiqtm nllkqhgyhi pedfsiigfd diqaaalvdp
      301 plttiaqdfe qlgklagdal vtwletkdrp sdskfpvsfi krqstkek
//
LOCUS       WP_284612298             609 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Corynebacterium propinquum].
ACCESSION   WP_284612298
VERSION     WP_284612298.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..609
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65615
     Region          11..609
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mreafspaky tiepgqtllt ltidavkaqp kaemftrpkn htwvpvsrqe fldevyavak
       61 glldagvehg drvalmantr yewmllnyai waagavvvpv ypssslsqvq wiiensgavl
      121 gigetqehse ilrmlqladd geprvkdsts qmrafyeind gavaalqaag kniaddvvdk
      181 riaattsddl aslvytsgtt grpkgcmlth rnwtaqvlgl ltnpiggiah agnhvltflp
      241 lahvlafsvs aasmisgttq nfwadfatlp tefqrskpnl ilgvprvfek vrngarakah
      301 dsgtiqgklf draeataiay sraldtedgp slalrgahkv mdklvlskir agmggevdyc
      361 isggsamspe vmhffrgigv piyegyglte taaaatvdfe nqkigtvgpp lggtrvriap
      421 dgelqlagdl vfdgywrnae atdeafdgqw yctgdlgeil psghvkivgr kkdlivtagg
      481 knvapggled glcshplisq alvvgdgkpf vavlvtldeq algrwksqhn ipaarsvdel
      541 ahdatlraei qdainavnst vshaeaikkf yildkdftee sgeltptmkv krnvvvqrys
      601 evleklysr
//
LOCUS       WP_284612295             399 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium propinquum].
ACCESSION   WP_284612295
VERSION     WP_284612295.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..399
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43329
     Region          36..398
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 msshnnstaa dvtanaaahs aanstyipvt adhfrarlak aetivaeqnl agflvspgpe
       61 fqyltgstfs sheratflvl ragkdpvavc petdvltlkq enldelgfrf eawrdgqspy
      121 eitrrlleen sehkavavan amtadhvlrl daalpnhsie lgsdamsqll lakgeeeisq
      181 laaaaaaidr vheqvpallr dgvterevad klhdlilqeh hsidfiivgc genganphhs
      241 fsdrvlhtge pvvvdlggaf gdgyrsdstr tyvvdgavdk apqefrdaye vvtrafhaar
      301 eaakpgatae sidraareii teagygenfs hrlghgigls thedpfyldg nkqqvqegft
      361 fsiepgiyva gkwgmrledi vvleadgprh lnqqprelr
//
LOCUS       WP_284612411             408 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Corynebacterium accolens].
ACCESSION   WP_284612411
VERSION     WP_284612411.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..408
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44225
     Region          27..222
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mlevmseakq rvstrqmlrv vdrsvvsrlq rirsrfvyii qatvgaalay wvassvvghp
       61 qpffapisav iilglsggdr mkravemslg givgvalgdl lfqvvgqgpf qilfivgagl
      121 vvgsfitksp lvsnqivfgs iliatifppt egpgglhrai damigsgigl itialipnsp
      181 lkearrevsk vlriassiln dvthgirdtn peiirdarda vrgtqndvnt llsaaqsgre
      241 asevspllwt srrnirsler illpvdnavr gvrvlsrral vltedgdtvs dkqlelleel
      301 seiilavgel ygrqkrdhde aieipelvqr lryvggqagm dlieedatls aytilaqtrs
      361 ivvdmlmvcg lsresavahl vptsthpafp pevwerddkp sdkqkgqd
//
LOCUS       WP_284612434             274 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Enterococcus
            faecium].
ACCESSION   WP_284612434
VERSION     WP_284612434.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..274
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30823
     Region          16..274
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mlnitirghd lsevqtiedl aektkeqgih tlqlalglsf peipsgtnei nsgmgnyvkr
       61 vlekqevtvg ilscyinmih pdltireell tkfeqslrya ssfgasmvas etgcvlpeiq
      121 yteenftdea faeavsvirr lvkagekyqm mvgiepglnh pvyslarveq liqavdsdyl
      181 giildptnli tssdyqeqvq lveeaferfg ekicavhlkd frveqekivp vnlgdgviey
      241 tkikeiimkn rpylyvvlee tkddgirygr slle
//
LOCUS       WP_284612501             473 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium accolens].
ACCESSION   WP_284612501
VERSION     WP_284612501.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..473
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51718
     Region          5..404
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msrtalrsfi qrihfyggmf vgpfiliaal tgclyalapt lekfayrdvm tveevnnpvs
       61 ledqisaaqk ehpdmpvsqv wpaesatdst rvlvadpgid eslqrtvfin padgevigdy
      121 ptysglgemp lrrwisslhe sfhlgqpgel yselaaswlw vlacgglymw wirrrpkkaa
      181 aplkkqpqrs krwkatrlhs tmgawifigl iglsatgitw sqlagenvns vvekmnwkat
      241 pvetalttds sadaahdaha gheghgahga hggdaeaage apepeviakq aervyatgra
      301 egltgplrly apedtdsgwk vserwvewry tsdevsvngs tgevidrlpf selplfskls
      361 swgiylhmgi mfglplqial falglaiaam vvlgyymwwk rrpqftpgsk rhfswattgl
      421 galfaatvgv fipllgitla aflvldiivm ntgkrkatap kkkdedaelv pvg
//
LOCUS       WP_284612521             334 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Enterococcus faecium].
ACCESSION   WP_284612521
VERSION     WP_284612521.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..334
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35882
     Region          22..329
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mkkiywtfyf llfvlvilsi gslmigtpfi yldqlfatfi gkessslali vrefrvprll
       61 isllagaclg vsgyilqgvt rneladssil ginvgagflv mlylgffshy slpflllvva
      121 flggvlaacc vylaaydrng flgmnrills giavnaglsa ltllctiqls kenygfvnaw
      181 lagsiwgasw pyvwallpwa viliplggly aqrivllsfg qeraqglgln vaksqkilll
      241 lavalasgsv avtgslsfvg llaphaaklv vrkennwtfv lsglfgsifl lsadmvarvi
      301 lpsgevptgi lialfgapyf lyalfirqkh alns
//
LOCUS       WP_284612524             603 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD/NAD(P)-binding protein [Enterococcus faecium].
ACCESSION   WP_284612524
VERSION     WP_284612524.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11816065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..603
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=69281
     Region          1..600
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
     Region          4..178
                     /region_name="NAD_binding_9"
                     /note="FAD-NAD(P)-binding; pfam13454"
                     /db_xref="CDD:433222"
ORIGIN      
        1 mkigiigagp rglsvaeril hnnqdrhsle lflfdpngpg grvwrlnqpp ellmnsvsqq
       61 vtlftdetls sgglvtqgpn lfqwskgpat dyieqtvtkn kqliieeinr lekdqqstrc
      121 lyglyqrwff sklqeefpas iqfvyslvkk vskrkdgyll qtdqqsysid qlvlasghwe
      181 ndeteeervw vdyakknvll yqlpsnpadv dlskippken vflrglglsf fdyvglftvs
      241 rggrfenekg klvyhpsgke pivysgsrrg lpyyprgrnq kqggamawpr lltkenleqw
      301 hqsgfltget ffdylkkdve lfyykkiiee yhlpipkknf ehdflslsse eclgkhpali
      361 pyrwdwsyle tplayqnepf seasrifieg qikeaekgnc tgafastfda lkdwrdpirq
      421 aiewhvfsak eykeilwgwf thlnsfltig ppiirtkela alidagifhl ieppfdiqqk
      481 hnryvislqd keissrylie arlpqtsfsr ssnpviknlk enklvrpfsf sdntgsyhse
      541 aidvergtnr vidasgeiqs dfycygipve gvdwltaava rpytgpwnlr qadkiaqlil
      601 tdk
//
LOCUS       WP_284612640             389 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Corynebacterium accolens].
ACCESSION   WP_284612640
VERSION     WP_284612640.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..389
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40936
     Region          11..388
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mneslekvas arldkwredg lwrspsvfas gqvpesslrt atgktvqdav lfsssnylgl
       61 aehpeiknav kdsvdhygag sggsrlttgt sdlhvaveaa aaqltgypds vffatgyqan
      121 lstlqalasp eltiisdarn hasiidgcrl akasgaslvv iphrdtrave nalaarstky
      181 alvvtdglfs mdgvlaplpe lsrlardyga wlmvddahsf gtvgdrglgl peffdvqpdi
      241 qlitaskalg aeggivatsk pvaqllrqqa rsfvfstspt pgtsaavlaa lkliesdpsl
      301 vsqlqdniay whntrgttpq qgpiipvhvg deaaamdasa alldrgfivp airwptvarg
      361 aailrvtlma thtraqidal cteleqlgl
//
LOCUS       WP_284612705             277 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase [Corynebacterium accolens].
ACCESSION   WP_284612705
VERSION     WP_284612705.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..277
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=30934
     Region          12..275
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 msnlfyespd vtlfhgdafs vvnslekesv dcvvtsppyw rqrdysghpd qwgqeesigl
       61 yvdhlvylfs aimpklkphg vvwlnlgdkr vdgqlcgvpw mvakdmqtdg wclrsaviwn
      121 kpngmpescl drvsqnyeqv fmfsrrvdhf fdldplrvly dgdrtpsrra rsghtnkrns
      181 atgewsgahn grnpgsvwsi ptqpfpgshe avmppelarr civsscppgg vvfdpfhgsg
      241 ttgkvavetg rryiggdine sylalslrtr lqnatlf
//
LOCUS       WP_284612865             375 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium accolens].
ACCESSION   WP_284612865
VERSION     WP_284612865.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..375
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40058
     Region          7..368
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mnhgpgltfr flaaqvlvvv isllvaaava ttvgptlfhd hmlmtgqedp slelfhaeqa
       61 yrganlitla valpsalisa llaslwlsrr lrtplqdltr aatsltagns rirvpagkag
      121 pevttlahaf ntmadrleht eqvrrqmlsd lahemgtpls vltvyldglq dgvvdwnnat
      181 htimadqltr ltrlmedidd vsraqehrid ldlaeeglgd llhtaaaaag eayadkgvdl
      241 qietithtar alvdrqrfgq vmsnllsnal rhtpaggqvr isvhrqgast alihvaddge
      301 gippdqlryi ferfyrgdaa rsrddggagi gltiskalie ahggtltats pgpgrgavfa
      361 lrlplsppds ekaar
//
LOCUS       WP_284612950             378 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Enterococcus
            hirae].
ACCESSION   WP_284612950
VERSION     WP_284612950.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..378
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=44445
     Region          1..374
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 miqakkvrlc ptkeqekqlw qssgtarwif nwtlkmqemn hrfggkfisn ndlrkhitkm
       61 kkrpkyvwln nvsnniakqa vkdacdaykk wfnsmtgksc lkaekprfks rkkskpafyn
      121 dtiklkvkpk svllekigwv ktseqlpmnr kysnprvsfd gkywyisvgi deeqpvqhlt
      181 geilgidrgi kdlaivsngr vykninktgk vrkiekrlrr lqrkvsrkye wnkegnrfvk
      241 tcniykleke irhthrklan irqnhihqtt teivktkpsk ivvetlnvkg mmknkhlakl
      301 vaqqkfyefk rqlqykcedy gielveadkf ypssklchec ghkkvdlkls drtyhceecg
      361 ytadrdynas lnlasyia
//
LOCUS       WP_284613046             368 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Enterococcus hirae].
ACCESSION   WP_284613046
VERSION     WP_284613046.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..368
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40836
     Region          25..353
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mekiaiiggg iigmtlanyv dttkysitlf dhgigqatka sagiispwls krrnktwyrl
       61 akdgaaffpk lvqdfaldpt iyarsgtlll rqkeqlaell dlaeerkkea peigeihllk
      121 adqtadllpl lkptpslfit gggrldgkay lhyltarlkr agvtvindki hlqkrnddwl
      181 ilgefgeepf drviltpgps lkplleplgy qvdlrpqkgq liaftthqlq sqkwpvamld
      241 geadlipfnd gkillgathe neqgwdltpt neaflqlteq tkaffvqpek llsqpyqlqv
      301 gtraytsdfa pffgplfdep nlivasglgs sglttgpyig yllaefintg twhgtdyqkd
      361 lhnyikkt
//
LOCUS       WP_284613160             262 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Enterococcus hirae].
ACCESSION   WP_284613160
VERSION     WP_284613160.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..262
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28604
     Region          1..259
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mnlenkvvlv tgssgglgaq icyeaakkga iviacarrsq lidevkaecq rlsgkeayaf
       61 pvdvsdpdsv drlyeqvmqt vgrvdvlvnn agfgifedfl tfdlgkaydm fevnvlgmmf
      121 ltqkfaidma errqghiini asmagkmata kstiysatkf avlgfsnalr lelrplgvav
      181 ttvnpgpvat effdkadptg sylekvsqlv lepeklakti vrtmehpkre vnrpvlleia
      241 akfytlfpti gdylasgifn kk
//
LOCUS       WP_284613282             143 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [Enterococcus].
ACCESSION   WP_284613282
VERSION     WP_284613282.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..143
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16751
     Region          13..124
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mekftgyire pfyyetdqmg iihhsnyirw meesrvalld hlgfsytkie klgviipvle
       61 vtcqykemir ygetvrilpk ieqysgtrln fsyeiygldd gklrttgssk hcflladnqk
      121 ltklervnpa ldrlfheyaq lds
//
LOCUS       WP_284613317             185 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Enterococcus hirae].
ACCESSION   WP_284613317
VERSION     WP_284613317.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..185
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=20458
     Region          1..184
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mkivlasqsp rrkellgrlv safdvhpadi detpfvqekp knyvermate kakvvkhqyd
       61 ndvlviasdt tvvfndeiig kptdekeaka ilqklsgkth evytavvltk gdqeekilaq
      121 akvtfypltt kdieaylatg dymdkagayg iqsfagafvk eiqgdyysiv gfpigavyqg
      181 lkkfm
//
LOCUS       WP_284613502             337 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Enterococcus hirae].
ACCESSION   WP_284613502
VERSION     WP_284613502.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..337
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=39567
     Region          14..335
                     /region_name="WecH"
                     /note="Surface polysaccharide O-acyltransferase WecH [Cell
                     wall/membrane/envelope biogenesis]; COG3274"
                     /db_xref="CDD:442505"
ORIGIN      
        1 mdnknqklfi aqfiaticvv vihcgtitnh pivhfflksm vcriavpfff vnnayffrin
       61 skregyskmw lrrivrlyti vfllyipfgv qllqdtvdiq wnlwsillal vvsflytgsf
      121 yhlwyfpali sslaivkymf qrfrykwvfl vcflffsvgs letyslfisn pmvisvmeky
      181 yniffttrng lffsplfisi gfvladnvhn lekhrklfiy glvaacflgg vegiitfynq
      241 gidknfmyft ipfifslygl lviskskiks fenlnsyskn iflfhmipiq ifnmrhgeit
      301 pinglfrlml gvfvpisivl fynkivkqis ifykikm
//
LOCUS       WP_284613628             389 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Enterococcus hirae].
ACCESSION   WP_284613628
VERSION     WP_284613628.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..389
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44308
     Region          58..382
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkkgkhakkr afpffsiilv llsisvlstg miigwsiytk eqarndsdsl kpkqtlsltp
       61 eekklsekin hllikhdyig siyvkknnhv ifergygyan kendqlnrpy lyyqigsiqk
      121 amtallilkq velghlslnt klakfypqip nsqkisiedl lymrsglkpt akpttplsdt
      181 evvqfavqhl nlvdyhtyry eplnftilag ilinlthqpy eklveneiik pldlkqtafy
      241 dqvknsphha vsyqmsasdd ywkpltesqt aihnelgtgn ismsvldlnt fftkvlsgkm
      301 ipqkllftlw kpsptghpyr ggvycgndyv laqgninrfh svavfkrdlk davvmesndq
      361 sdkkikltal dlrnriynli egskileen
//
LOCUS       WP_284613679             717 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Enterococcus
            hirae].
ACCESSION   WP_284613679
VERSION     WP_284613679.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 717)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 717)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 717)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..717
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=78992
     Region          51..713
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mmrefmkkll nnswmdklkk gaqepknktf rrshvpfrln flffiiftlf valiarlgyl
       61 qivngeamea kvkssstlti qtssprgmiy dstgkplvtn qanqaitftr gtkmtaedll
      121 kvatrlnqli nvpvdenlte rdkkdfwlad pkhlkeater ltakekqlds sdqykalvdk
      181 vtdseinfne eqlkiatifk rmnsayelnt vfiknsgvtd qelavvseha selpgvstgt
      241 dwtrqytaad siksilgsvt tekqglpade vdeylakgys rndrvgqsyl ekqyedvlqg
      301 tktqyevtld sngnvtnqke ifagekgsnl mlslnadfqa kvenilktny qklvdsgkat
      361 yspgayavam npqtgeilam tgfshqegsk eltenalgni tsaftpgsvv kagtltagwq
      421 tnvisgnqvl vdepiklqgs sekssvfnrs griainavka lelssntymi kvalkmlgle
      481 ytpnmglpsl neeskayeel rkafkqfglg tktgidlpne spgisrsvdf mkkfnadnga
      541 qwytpgnftd lafgqfdtyt piqlaqyast vanggkriqp rlvkgiygnd engnlgpvkk
      601 eletkvedtv dispadmsil regfhqvvhg tdvyttakpl asakmdlsak tgtaetvaeg
      661 hpdittvnsn ivaygpsdnp qiaisvvlpn lldekdhmnl viakeimdty ydmfmak
//
LOCUS       WP_284613759             605 aa            linear   BCT 25-DEC-2024
DEFINITION  polysaccharide biosynthesis protein [Enterococcus hirae].
ACCESSION   WP_284613759
VERSION     WP_284613759.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 605)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 605)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 605)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 605)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18500220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..605
                     /product="polysaccharide biosynthesis protein"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=67471
     Region          121..242
                     /region_name="FlaA1"
                     /note="NDP-sugar epimerase, includes UDP-GlcNAc-inverting
                     4,6-dehydratase FlaA1 and capsular polysaccharide
                     biosynthesis protein EpsC [Cell wall/membrane/envelope
                     biogenesis, Posttranslational modification, protein
                     turnover, chaperones]; COG1086"
                     /db_xref="CDD:440703"
     Region          285..569
                     /region_name="Polysacc_synt_2"
                     /note="Polysaccharide biosynthesis protein; pfam02719"
                     /db_xref="CDD:426938"
     Site            order(289,291..294,314..315,343..345,366..368,370,385,408,
                     424,447..450,453..454)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(315,317,321,325,341..344,347,350,368..371,374,378,
                     381,384,454..455,460)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187548"
     Site            order(370,410..412,420,448..449,455..457,460..461,
                     472..474,478,480,515,541,544)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(386,410,420,424)
                     /site_type="active"
                     /db_xref="CDD:187548"
ORIGIN      
        1 mfvltrrrki atlvvvdsll liaaniaaak fmkpfvsipm dlilisigls igfylfygsl
       61 fkvftrinry tnlreiiaif sslsasaass ililmfinrr yslrlvifay llsllliigs
      121 rliwriyvet knmryvsads akntlivgag eggrilynsf lgsktaqdih vvgfvdddpn
      181 krntylsgkk vlgalkdipe liekydiqmv tiaipslsrk klrrifelve sarvkvntmp
      241 sieelasgki svsklktidv vdllgrdevk ldiesikdqi tdkvilvtga ggsigseicr
      301 qiiqfnpakl lllghgensi ylidrelrth hqncpteivp iiadiqdrek ineimeqyhp
      361 divyhaaahk hvplmeynpk eavknnifgt knvaeaakaa rvknfvmvst dkannppnvm
      421 gstkriaemi vtglneegct kfsavrfgnv lgsrgsvipv freqiaqggp itvtdfrmtr
      481 yfmtipeasr lviqsgalak ggeifildms epvkivdlak nmirlsgyse deieiietgi
      541 rpgeklyeel lldkerndea vyekifvgni kgysiqkvmd fvknlpqdde qlakdivtfa
      601 nasnr
//
LOCUS       WP_284613813             221 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Enterococcus faecalis].
ACCESSION   WP_284613813
VERSION     WP_284613813.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..221
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=24337
     Region          <1..204
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mkqnfaiigl grfggsicqt lveagqevla idssedrvne ymniathavv anaqdemtlr
       61 slgirnfdhv vvaigediqa silvtlmvke mgvlnvlaka vneyharvld kigadmvvhp
      121 erdmgiriah klvsrnildy ielssefsla evrvtnpkfy nktlaelnfr qrfgltvvai
      181 rrsktevias pdaseivren dnllvigdta dvdlldekmn g
//
LOCUS       WP_284614081             575 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Escherichia coli].
ACCESSION   WP_284614081
VERSION     WP_284614081.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13939702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..575
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=63445
     Region          110..430
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
     Region          392..569
                     /region_name="DUF3520"
                     /note="Domain of unknown function (DUF3520); pfam12034"
                     /db_xref="CDD:432277"
ORIGIN      
        1 mrnkniimll msslilsgcg pqpenkesqq qqpstpteqq vlaaqqaaik eaeqsaaaak
       61 alaqqevqqy sgkqalqgrl qeaptfaraa kakathianp gtaryqqfdd npvkqvaqnp
      121 latfsldvdt gsyanvrrfl nqgllpppda vrveeivnyf psdwdikdkq sipaskpipf
      181 amryelapap wneqrtllkv dilakdrkse elpasnlvfl idtsgsmisd erlpliqssl
      241 kllvkelreq dniaivtyag dsrialpsis gshkaeinaa idsldaegst nggaglelay
      301 qqatkgfikg ginrillatd gdfnvgiddp ksiesmvkkq resgvtlstf gvgnsnynea
      361 mmvriadvgn gnysyidtls eaqkvlnsem rqmlitvakd vkaqiefnpa wvteyrqigy
      421 ekrqlrvehf nndnvdagdi gagkhitllf eltlngqkas idklryapdn klaksdktke
      481 lawlkirwky pqgkesqlve fplgptinap sedmrfraav aaygqklrgs eylnntswqq
      541 ikqwaqqakg edpqgyraef irlieladgv tdisq
//
LOCUS       WP_284614147            1504 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Escherichia coli].
ACCESSION   WP_284614147
VERSION     WP_284614147.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 1504)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1504)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1504)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1504)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1504
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..1504
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=166353
     Region          199..1496
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mgtglanadd slpssnyapp aggtffllad ssfssseeak vrleapgrdy rryqmeeygg
       61 vdvrlyripd pmaflrqqkn lhrivvqpqy lgdglnntlt wlwdnwygks rrvmqrtfss
      121 qsrqnvtqal pelqlgnaii kpsryvqnnq fsplkkyplv kqfryplwqa kpfepqqgvk
      181 legassnfis pqpgniyill gqqepglylv eamvggyrat tvvfvsdtva lskvsgkell
      241 vwtagkkqge akpgseilwt dglgvmtrgv tddsgtlqlq hispersyil gkdaeggvfv
      301 senffyesei yntrlyiftd rplyragdrv dvkvigrefh dplhsspivs apaklsvlda
      361 ngsllqtvnv tldarnggqg sfrlpenava ggyelrlayr nqvysssfrv anyikphfei
      421 glalakkefk tgeavsgklq llypdgepvk narvqlslra qqlsmvgndl ryagrfpvsl
      481 egsetvsdas ghvalnlpaa dkpsrylltv sasdgaayrv tttkeilier glahyslsta
      541 aqysnsgesv vfryaaless kqvpvtyewl rledrtshsg elpsggksft vnfakpgnyn
      601 ltlrdkdgli laglshavsg kgstahtgtv divadktlyq pgetakmlit fpepideall
      661 tlerdrveqq sllshpanwl tlqrlndtqy earvpvsnsf apnitfsvly trngqysfqn
      721 agikvavpql dirvktdkth yqpgelvnve ltsslkgkpv saqltvgvvd emiyalqpei
      781 apnigkffyp lgrnnvrtss slsfisydqa lssepvapga tnrserrvkm lerprreevd
      841 taawmpsltt dkqgkayftf lmpdsltrwr itargmngdg lvgqgraylr seknlymkws
      901 mptvyrvgdk paaglfifsq qdnepvalvt kfagaemrqt ltlhkganyi sltqniqqsg
      961 llsaelqqng qvqdsistkl sfvdnswpve qqknvmlggg dnalmlpeqa sniwlqsset
     1021 pqeifrnnld alvdepwggv intgsrlipl slawrsladh qsaaandirq miqdnrlrlm
     1081 qlagpgarft wwgedgngda fltawawyad wqasqaigvt qqpeywqhml dsyaeqadnm
     1141 pllhralvla waqemnlpck tllkgldeai arrgtktedf seedtrdind slildtpesp
     1201 ladavanvlt mtllkkaqlk stvmpqvqqy awdkaansnq plahtvvlln sggdatqtaa
     1261 ilsgltaeqs tieralamnw lakymatmpp vvlpapagaw akhkltggge dwrwvgqgvp
     1321 dilsfgdels pqnvqvrwre pakmaqqsni pvtverqlyr lipgeeemsf ilqpvtsnei
     1381 dsdalyldei tltseqdavl rygqvevplp pgadverttw gisvnkpnaa kqqgqlleka
     1441 rnemgelaym vpvkeltgtv tfrhllrfsq kgqfvlppar yvrsyapaqq svaagsewtg
     1501 mqvk
//
LOCUS       WP_284614365             153 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Aquabacterium humicola].
ACCESSION   WP_284614365
VERSION     WP_284614365.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..153
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16310
     Region          18..152
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 msaagrpaaa aaaagarfer plrirfghcd pagivyfpty fvmlnglved wisdglgipy
       61 asllgerrtg lptvslqtdf kaisrmgdev vlglavqrlg arsftlaldv rgadgglrvq
      121 askvivttdl ethrsieipp dlraaierfm raa
//
LOCUS       WP_284614259             312 aa            linear   BCT 25-DEC-2024
DEFINITION  N5-glutamine methyltransferase family protein [Actinotignum
            urinale].
ACCESSION   WP_284614259
VERSION     WP_284614259.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum urinale
  ORGANISM  Actinotignum urinale
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Schubert,H.L., Phillips,J.D. and Hill,C.P.
  TITLE     Structures along the catalytic pathway of PrmC/HemK, an
            N5-glutamine AdoMet-dependent methyltransferase
  JOURNAL   Biochemistry 42 (19), 5592-5599 (2003)
   PUBMED   12741815
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Actinotignum urinale"
                     /db_xref="taxon:190146"
     Protein         1..312
                     /product="N5-glutamine methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=34251
     Region          3..311
                     /region_name="HemK"
                     /note="Methylase of polypeptide chain release factors
                     [Translation, ribosomal structure and biogenesis];
                     COG2890"
                     /db_xref="CDD:442135"
ORIGIN      
        1 matwavllnd atyvlaeagv psprvdakel aeflcghkpn prsladectt adylslvgkr
       61 cgreplqhit grmyfrylel actpdvfivr petelvagaa idtarelmrq rlrstdnerg
      121 qgggvraigk eqysavlrtt eqgspsltvv dlctgsgaia lsvatevpgt rvyaaeispq
      181 afrvaernne rygnrvhiin edalhafpel egavdivvtn ppyvppgtkh spevqrdpql
      241 alwgggedgl dlprqlvcra tqllhpggml imehaetqge alrnfmnthg fcdavthedy
      301 trrprwrqar ki
//
LOCUS       WP_284614395             148 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Aquabacterium humicola].
ACCESSION   WP_284614395
VERSION     WP_284614395.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..148
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16405
     Region          12..144
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 msirpipegr etfrhharit trwmdndlyg hvnnvqyysy fdtvvnryli eagaldihag
       61 aviglvveth cnyfaplsfp meveaglrva hvgsssvrye iglfapgepl aaaighfvhv
      121 yvdrqtrrpv plpdalkqal qplrpigg
//
LOCUS       WP_284614427             345 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Aquabacterium humicola].
ACCESSION   WP_284614427
VERSION     WP_284614427.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 345)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 345)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746489
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..345
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37535
     Region          41..189
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <157..338
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          268..338
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 maaavppesr fapepsadel eavladrrfv slfetrepeh aeaflsrvyg phaltlgggg
       61 htlnmrlraf efahlhlgev rygqpavasm sqahghwvfs ylrsgsvatd vqprpyvpge
      121 aavmapdsvq qlrmsadmem rnlrvgqsem laacrsllgs dlahplrfde rvpahspqta
      181 allrvmthla atpayalaaa srlegslrda alfeillawp nnyahhleqp aalplstrra
      241 rdyihahaae lpsigdiaaa agvgvralar gfekhlgvsp qrylqqyrld rvheallapg
      301 gettvtevav qwgflqlgsf aaryrerfge spsqtlrrsp lippg
//
LOCUS       WP_284614452             248 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Aquabacterium humicola].
ACCESSION   WP_284614452
VERSION     WP_284614452.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..248
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27067
     Region          27..246
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mvskwgrwaa walvvallsp pvaaqervav dsqnapfmya dgeraaglyp allqagfdri
       61 gvpvriealp wsralaaleq aeigvggiyk nservqkydy sapifveklv lyvrrdkpra
      121 fagvpdlagl rigvirgwsy gdafdaarrg ghlqaeevas daqnfskleq krldaivave
      181 qagtaqlasg qypsvialpt plavnpthla fnksankral lqrfdralda mrrsgehdrl
      241 verallrh
//
LOCUS       WP_284614461             364 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Aquabacterium
            humicola].
ACCESSION   WP_284614461
VERSION     WP_284614461.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 364)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..364
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41226
     Region          16..361
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
ORIGIN      
        1 mttipiyrvd pdvrragtld aafyrdeaay aaaletvfar swqwigdlrd vaapgtlapr
       61 wllpgsldep illsrdargq lrclsnvcth rgnilvhect raeqircgyh srrfdlagrm
      121 tfmpefqqae cfpsdndhlv qvpfedwhgl gfasvkpaap laevfaemes rigwlplrdw
      181 rhdpsrdrsf efdahwalyv enyleglhip flhaglmqtl dfnqysyelg ryanlqlala
      241 kpgepafalp adsidagksv aayywwvfpn lmlnfypwgl slnqvqplgp grtrvvfrsy
      301 vgdasrlgtg aggdldrvem edeavvvqvq rgvrsrfyrg grysptreqg vhhfhrllae
      361 hlad
//
LOCUS       WP_284614675             198 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF3617 domain-containing protein [Aquabacterium humicola].
ACCESSION   WP_284614675
VERSION     WP_284614675.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10574053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..198
                     /product="DUF3617 domain-containing protein"
                     /calculated_mol_wt=21489
     Region          29..145
                     /region_name="DUF3617"
                     /note="Protein of unknown function (DUF3617); pfam12276"
                     /db_xref="CDD:463516"
ORIGIN      
        1 mntprciava aagllcltav qaqdhwmkrk pglwevsmqm pgpnrpamss kqciddktda
       61 emqkkamggp dqkqqcrqls skkiaggvei emecksdegt tkvvsrmtgd mqssfkvdst
      121 mtfnpprhgm stgqftmsgq hagacpadmk pgdmrmgsmv mpgpggqpgm afdmeklknm
      181 tpeerakfme qmkksmgq
//
LOCUS       WP_284614774             320 aa            linear   BCT 25-DEC-2024
DEFINITION  ribose-phosphate diphosphokinase [Aquabacterium humicola].
ACCESSION   WP_284614774
VERSION     WP_284614774.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Sinha,S.C. and Smith,J.L.
  TITLE     The PRT protein family
  JOURNAL   Curr Opin Struct Biol 11 (6), 733-739 (2001)
   PUBMED   11751055
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Becker,M.A., Smith,P.R., Taylor,W., Mustafi,R. and Switzer,R.L.
  TITLE     The genetic and functional basis of purine nucleotide
            feedback-resistant phosphoribosylpyrophosphate synthetase
            superactivity
  JOURNAL   J Clin Invest 96 (5), 2133-2141 (1995)
   PUBMED   7593598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..320
                     /product="ribose-phosphate diphosphokinase"
                     /EC_number="2.7.6.1"
                     /GO_component="GO:0002189 - ribose phosphate
                     diphosphokinase complex [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004749 - ribose phosphate
                     diphosphokinase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0006015 - 5-phosphoribose 1-diphosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009156 - ribonucleoside monophosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009165 - nucleotide biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34110
     Region          1..307
                     /region_name="PrsA"
                     /note="Phosphoribosylpyrophosphate synthetase [Nucleotide
                     transport and metabolism]; COG0462"
                     /db_xref="CDD:440230"
ORIGIN      
        1 mlvfaldphq rgfadqlalh ldtelaphee rafedgeatl rplvdpcgad ayvvlglhas
       61 pdasprdqlc rllffiaalr dhgaarvsav vpyfafarkd rrtkpfdpvt lryvaqlvea
      121 vgayqviale ahneaafqna frcptvhlhg haafaalade lhaaapvvva spdggglkra
      181 qawqedlaar lkrpvglamv dkrrsedrie gghfvagdvd gavvllvddl iatgatlqra
      241 alalraagak rvlacaahgl fvapaaerlt dpaidqvlvt dsvpgfrvpa tgalrdklrv
      301 mscvplfaaa mrashaawmr
//
LOCUS       WP_284614848             302 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Aquabacterium humicola].
ACCESSION   WP_284614848
VERSION     WP_284614848.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 302)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10440481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..302
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31730
     Region          51..262
                     /region_name="TsdA"
                     /note="Thiosulfate dehydrogenase TsdA, contains C-terminal
                     cytochrome c domain [Inorganic ion transport and
                     metabolism]; COG3258"
                     /db_xref="CDD:442489"
     Region          55..151
                     /region_name="Cytochrom_C"
                     /note="Cytochrome c; pfam00034"
                     /db_xref="CDD:459641"
ORIGIN      
        1 mkrwikitlg tvialvaaga atvgiaehrg ttlqsrtvdi arrplafsdd aatlergryl
       61 ylsrgcadch ganaggrtfv ddpksglkla gpnisprpdg vvaryrgedw eralrhgvkp
      121 dgkplmvmps qdfarwtdgd vvavasylrs vpavdggaav iqlplpvrva yglgviedaa
      181 aridhrlppa qpvpegvtvq hgqyvaqsci gchgpglsgg kitgappdwp aaanltpgeg
      241 samaryasae qfrrmmrsgk rpdgsaispv mpfealaqmn dvdldaafly lksvppraag
      301 gh
//
LOCUS       WP_284614863             389 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Aquabacterium humicola].
ACCESSION   WP_284614863
VERSION     WP_284614863.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..389
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41707
     Region          1..376
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mrvviiggga mgsavalflk rqggagvdvt vvepdpglar assalsagsi rqqfsnainv
       61 rmsqfghevi anaqawlgvd depvdlgfvp sgylflatgs tgvleanhav qrdlgvpvrl
      121 lardelasrf pwlrvedvql aslgeggegw fdgyafaral arkarsigar whrarvtgle
      181 regdrlraas lddgtrlead aivnaagpwa rsvaalagva lpvharrrtv fafscpttlp
      241 ltplvidpsg cwfrseghqf igawtpgehd ddpddlplde pdialfeerl wpalahrvpa
      301 fealrltraw agyyevhpld hnaiigphpe lanllfvngf sghglqhapa agrgiaewll
      361 eggwrsldls pfayarlaeg hafaelavi
//
LOCUS       WP_284614957             362 aa            linear   BCT 25-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Aquabacterium
            humicola].
ACCESSION   WP_284614957
VERSION     WP_284614957.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Rengstl,B., Oster,U., Stengel,A. and Nickelsen,J.
  TITLE     An intermediate membrane subfraction in cyanobacteria is involved
            in an assembly network for Photosystem II biogenesis
  JOURNAL   J Biol Chem 286 (24), 21944-21951 (2011)
   PUBMED   21531723
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Komenda,J., Nickelsen,J., Tichy,M., Prasil,O., Eichacker,L.A. and
            Nixon,P.J.
  TITLE     The cyanobacterial homologue of HCF136/YCF48 is a component of an
            early photosystem II assembly complex and is important for both the
            efficient assembly and repair of photosystem II in Synechocystis
            sp. PCC 6803
  JOURNAL   J Biol Chem 283 (33), 22390-22399 (2008)
   PUBMED   18550538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..362
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=37172
     Region          69..285
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          222..356
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
ORIGIN      
        1 miarrqllvl aalpaaghaa paaattaaat tattaaapaa aegpavlrtp alitpraaga
       61 amlavaragr rlvaagergi vrlsdddgag wsqarvpvqv sltalhfada rrgwatghlg
      121 tilrtgdgga nwtlqlhgid aarrllaaaa deparqraqr lvdegpdkaf fdldlagprg
      181 lavgayglaa etrdegaswq pvpparlpnp kglhlyaarw lgrqlfvage qglllrsddg
      241 ggsfeplasp ykgsffglla mragsliafg lrghafrstd agasweklet gvpaslgagv
      301 qradgrllll aqngdllasr ddgrhferls aarplpaaal aacddghvvv aglrglqrvk
      361 ts
//
LOCUS       WP_284614944             131 aa            linear   BCT 25-DEC-2024
DEFINITION  VOC family protein [Aquabacterium humicola].
ACCESSION   WP_284614944
VERSION     WP_284614944.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..131
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13841
     Region          <58..126
                     /region_name="PhnB"
                     /note="Zn-dependent glyoxalase, PhnB family [Energy
                     production and conversion]; COG2764"
                     /db_xref="CDD:442048"
ORIGIN      
        1 matahfilyv adqaasaafw raaldraprl dvpgmtefal dggavlglmp eagiwrllgh
       61 rlpdpgaarg tpraelyllv ddpvachara laagavelsp vqprdwghra gylldpdghv
      121 lafasdapir r
//
LOCUS       WP_284615078             338 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Aquabacterium humicola].
ACCESSION   WP_284615078
VERSION     WP_284615078.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..338
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=35053
     Region          9..319
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mndawlrrlg irlpllqagm ggiagpalaa avaeagaggi vamyrlpgpa varrvretra
       61 ltaapfgvnl ipelqtesal aaqvqaalaa darvffsiyg lppaslaatv rdagralvvm
      121 vgtpedalea errgadvvvl qgveagghll gdwplqallq asqaagcrap lvaaggiahg
      181 aawrtlqrrg aagclcgtlf vctteseahp hyqrrllaad ahdtvvsraf etgwpgrahr
      241 vlrvaaapht qappgfvgsv lidgrrhplp rhcamvptmh ttgridemam ycgtgvgals
      301 evlpaaqrie rffaearsvp yadpattvae rgcnssta
//
LOCUS       WP_284615095             794 aa            linear   BCT 25-DEC-2024
DEFINITION  efflux RND transporter permease subunit [Aquabacterium humicola].
ACCESSION   WP_284615095
VERSION     WP_284615095.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 794)
  AUTHORS   Sandhu,P. and Akhter,Y.
  TITLE     Evolution of structural fitness and multifunctional aspects of
            mycobacterial RND family transporters
  JOURNAL   Arch Microbiol 200 (1), 19-31 (2018)
   PUBMED   28951954
REFERENCE   2  (residues 1 to 794)
  AUTHORS   Hand,N.J., Klein,R., Laskewitz,A. and Pohlschroder,M.
  TITLE     Archaeal and bacterial SecD and SecF homologs exhibit striking
            structural and functional conservation
  JOURNAL   J Bacteriol 188 (4), 1251-1259 (2006)
   PUBMED   16452406
REFERENCE   3  (residues 1 to 794)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
REFERENCE   4  (residues 1 to 794)
  AUTHORS   Arkowitz,R.A. and Wickner,W.
  TITLE     SecD and SecF are required for the proton electrochemical gradient
            stimulation of preprotein translocation
  JOURNAL   EMBO J 13 (4), 954-963 (1994)
   PUBMED   8112309
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..794
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86023
     Region          8..774
                     /region_name="MMPL"
                     /note="Predicted exporter protein, RND superfamily
                     [General function prediction only]; COG1033"
                     /db_xref="CDD:440656"
ORIGIN      
        1 mnvdrfdhrs gsfverllfn hravvvvlca lvtawlgwqa sklqlnasfe ktipashlyi
       61 rnflqhqadl sglgnavria varpdgtvyd akyldtlrrl sdevfllpgi drvrmkslwt
      121 pttrwvgvte dgleggpvip dgydgsaksl qqlganiars gevgqlvard arstvifvpl
      181 laadaqgrpl dyaalsqrld tlraryeaeg vrihvtgfak ivgdlidgvr avllffalav
      241 aiatamvfwy trcvrstalv vlaslvavvw qlgllpvlgq sldpysilvp flvfaigmsh
      301 gaqkmngimq dvgrgmhrlv aarltfrrlf lagltallad avgfavllvi diqvirelal
      361 aasigvaali ftnlillpil lsyvgvspaa aarslrdeqa dangaarhpl wafldrftqr
      421 rwagiavita avlgaggfaa strlqigdld pgapelrpds rynrdvafmn taygassdvl
      481 avmvktpegq csryetlnkv dalewelrql dgveststla llnrrvlsgl negnprwyef
      541 lpnqdmlntv tagaprglyn dacglltiyv ylrdhkaatl irvvdhvaqf arvndsadtt
      601 fllaagsagi eaatnivvkd awrtmlvlvy aavvllcfit frswravlva vlplvltsfl
      661 aealmvglgm gvkvatlpvi algvgigvdy alyilsvtla qlregrslsq ayyrallftg
      721 kvvmltgvtl aigvvtwvas pikfqadmgl llafmflwnm lgalillpal ahfllvrhpr
      781 psedsatfmr slqa
//
LOCUS       WP_284615137             289 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Aquabacterium humicola].
ACCESSION   WP_284615137
VERSION     WP_284615137.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..289
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=31676
     Region          51..254
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mrawidmtgv rfapawhvap safgsalvrm alcagaallp slaaaadrpv vracghhdyp
       61 pwnwqqdahi vgvcadvarr aierlgyrvd lgfvgpwkrc qemvasgdvd vnicafrnpe
      121 reryavfsep rmaqnriavf vpadkvsslr aqpwqalags rtglvlgvsm gpdfdafler
      181 etqvsrvsvv qqalrmltlg rldivpfgwe aglieierag lagrvlpleh palvgdlwls
      241 vskrsplagr iqevgayfar peyaeelrtl laehhrralq reapgasar
//
LOCUS       WP_284615152             394 aa            linear   BCT 25-DEC-2024
DEFINITION  thiolase family protein [Aquabacterium humicola].
ACCESSION   WP_284615152
VERSION     WP_284615152.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 394)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..394
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40938
     Region          4..394
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mtsrhivlch pvrtaigtyg gslkdvpatd lgaaairetl krsglaadki etlvmgnviq
       61 aggkmnparq agiaaglpie vpalsvnrvc gsgaqgvvsa aleiwsgmid caiaggmenm
      121 drapyllpqg rwgarmgdvt mfdsmlydgl ndafsgkhsg whtedlvlkn gisredqdrw
      181 alrsqqrfaa aqaagkfeae ivavevpgrk gptlfakdeh nrpettaesl aklkpafrke
      241 gtitagnapg lnsagaamvv thaawaekqg llpmarlvsy gvgavepgff glgpvpavhq
      301 alqragwsag dvdrveinea faaialaclr eigfpedivn vdggaiahgh pigasgavla
      361 tkllhaiqrg eaqrgivtlc igggqgiala ierv
//
LOCUS       WP_284615176             156 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Aquabacterium humicola].
ACCESSION   WP_284615176
VERSION     WP_284615176.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..156
                     /product="YybH family protein"
                     /calculated_mol_wt=16751
     Region          28..143
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mrpavlgagl vaaamslgdv haqasapdla alrqqveaae rsfarsmadr dlaafgrhls
       61 ehavfygnnt vlrgraavie gwkafydgkq apfswepdqv evladgtlah stgpvrdpsg
      121 qrvsrfnsiw rqeapgvwkv vfdkgqpisd aekklp
//
LOCUS       WP_284615301             382 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Aquabacterium humicola].
ACCESSION   WP_284615301
VERSION     WP_284615301.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..382
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40703
     Region          6..345
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtspdsfdva ivgagiagas lawhlaphar vllleresqp gyhttgrsaa mfmesygppq
       61 graltrasra fytaprpgfa egpllaprga lyvgwagdea rldeveaglr atgsvierid
      121 aavalalcpv lrpegllggl weadamdidv halhqgflrg arhppsgpga tlrcdaglvq
      181 aeragghwtl tlqdgrhvta rtlvnaagaw adpvaqlaga rplglqpkrr safafaapeg
      241 ldvrrwptvd rvddswyfkp dagrllgspa nvdpvpphdv qpeeldiatg ihrieqdttl
      301 rirrpqrswa glrtfapdge lvigwdgivd gffwlagqgg vgiqtawaag alaaalwrgv
      361 plppplqaqr vepdrlsprr fg
//
LOCUS       WP_284615342             329 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Aquabacterium humicola].
ACCESSION   WP_284615342
VERSION     WP_284615342.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..329
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34318
     Region          27..327
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mhrrhlcala laalaagaal paaaqadypn rpitlvvgyp pggsvdlvar tigpelsrrl
       61 gqpvvvenvg gaggtigaqk varaaadgyt llvgsnnema igklvnpslr ydpqrdftpi
      121 gllatqpmvl vaaphtkvks lddflrvvka spgrysygss gigtglhlag emvkesgglf
      181 mvhipyrgvg pltndllggq ldfgvyvlss glphiragsv aavgvtearr aaaapeipal
      241 aehasfrkvn igiwfglfap arlpaalsar igqafqasia spdvrrklee agarppapeg
      301 kpdellaayq kielekyarv vdfakirhe
//
LOCUS       WP_284615348             335 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Aquabacterium humicola].
ACCESSION   WP_284615348
VERSION     WP_284615348.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..335
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=35281
     Region          34..333
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mtprppaspp rrlgllslaa aalaaltpla ahsqsypskp vkivvpfapg gatdilarll
       61 aekmgpkmgq tvivenkpga agivgtdqva kappdghtiv lglsnslltn qflyeklpyn
      121 verdlalvsq iavaplilvv hpsvpannan elmahigrsk gklsygsygi gayphlagah
      181 msdvanadms hvpykgeapm vqdllagniq iayasalqvk ahveagklka lavtgdnria
      241 ampnlptmve qglkdeayrl tgwlavaapa gtpkpvlqrl sdelraaceq pdvkarivam
      301 gfdvrastpe qfaavykrew pvwqrmvkts gakle
//
LOCUS       WP_284615377             480 aa            linear   BCT 25-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Aquabacterium
            humicola].
ACCESSION   WP_284615377
VERSION     WP_284615377.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..480
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=50896
     Region          10..479
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mnpassslfv irgaelidgs taprraadva vrdgriaavl ppgaaadgpv vdagglvlcp
       61 gfidthshdd glllqetvph pklmqgvatv vtgncglsla pltmaeppap ldvlgqhdap
      121 rfaafgdyla rldavspsmn vvplightnl rlqhvadlvr padpaecram rddvaaalea
      181 gafglstgvy ypparaastd emvevaaalk arpgailamh lrdeadaiap aideallvgr
      241 scgatlllsh hkvigrrnhg rtrqtlqvid aaaarqpvcl dcypyaasst mlradriada
      301 ddvlvtwsgp hpeqggrrlr tiaaewgmsl eaaarrlmpg gavyfalseg dvervlvhpl
      361 tmigsdglph dahphprlwg sfprvlghys rdrgllplet avhkmtglpa qrfglahrgr
      421 iaagcaadlv lfdparirdg atyeqpttrp eglhalwing rlvmrdgelq elhagrrlrp
//
LOCUS       WP_284615378             332 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Aquabacterium humicola].
ACCESSION   WP_284615378
VERSION     WP_284615378.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..332
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34977
     Region          41..330
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mngfdesmrh grrtwlqlaa aaaaaqalpl raaaayparp vrlivpsaag gspdavcril
       61 aeelgralgq pfvvdnkpga sgtigmvela raepdgytig ygnvgtlain rslfaklpyd
      121 pdalvgiait gtvhnalvvr lslgvktvre lielaksrpg rlmmgsagng ttghlggelf
      181 kamtgtfivh vpyrgspaai qeliggqtdl mfdnlssigp hiqagrvral avsglrrsal
      241 fpelptlnea gvtgyestaw gglvgprglp aeivgllnre vnrlimvpav rerftrlsve
      301 tmasppnlil tmakletprw levikrsgar ve
//
LOCUS       WP_284615383             884 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Aquabacterium humicola].
ACCESSION   WP_284615383
VERSION     WP_284615383.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 884)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..884
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..884
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=92612
     Region          16..869
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mtaptpaadp apfspagadp ttpaaavafg pfvldaaeqr ltrdgeplal sgrplqvlal
       61 laaragrlvd kdavldgvwg hrhvtdsvlk gavntlraal gddakapryi etvprrgyrf
      121 iaplrplpap aaasatptal pgaeagppsa qaawpgaadt agkgtgtagl igreaealql
      181 rgllaghrlv tltglggigk trlalavagd apppdgvalv rlesladgdp lastvaqala
      241 lgpgagasaa alaralaplr lrlvldnaeh vvdavaalva tlldgapllq vlvtsqvplh
      301 lagervlpla alalpddfgd aapdpagyaa arlfcervre rqpgwqpqra daagiaaicr
      361 aldgvplale laaarvpllg vagvqarldq rftlltrapr daatrhrtla aaldwtcgll
      421 daaeqralqt lalvhgrfdv eaaeslldad daldlvdalr erslivvepd gglrlfdsvr
      481 rhalqalaag nagaagfnea aahqrhlawl rtrfeaseav efctpllqwl pplaervddl
      541 raalrfglva eaadpavrdg alrllaaslm fwarsglrae glrwlelgra aapaagwtrt
      601 lldlghglfv tfaqlgapad alaalraarp alqqagetrr eylslyaerm llmrlapqde
      661 vapllarmre lqqpdwgpla rrylqmleaf awrdrgdfar yestsramaa acraaggrae
      721 vwavenaltq alalqgrlde acaliartad dvraagrqre qvqvlaiaam lhlrrdagaa
      781 tlalaheavr llradgmlww madalpwaaw hagrahdaar lqawadavak argdtrgplf
      841 srlrgalvda laghaeaapl qallqqdpgl dddaalalaf gvpg
//
LOCUS       WP_284615401             168 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Aquabacterium humicola].
ACCESSION   WP_284615401
VERSION     WP_284615401.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 168)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..168
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18380
     Region          82..159
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mpsalhvelv tasqheslve lllelhayyd agppmpreav rsylddclla pdsplrlgva
       61 adhdgrvvgl aaimltwslv ehaphrrrqc wlkelyvlss crsqgvgral mtwvarhavd
      121 ngcaridwpv nasnargiaf yeslgarpvd errsyrlagp amralags
//
LOCUS       WP_284615410             325 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Aquabacterium humicola].
ACCESSION   WP_284615410
VERSION     WP_284615410.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..325
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33412
     Region          24..323
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mtsilrratv valataglag afpalaawpd kpvtllvpfp pggstdtiar alapklqekl
       61 ggnfivdnkp gatgtigagi vkrapadgyt lfvsslgpfv iaphliknvp ydaakdfdll
      121 tvavqapnvl vvpaasphks vadvlaqlkk tpgamsfass gngssdhltv elfwqqtgts
      181 gvhvpykgga paisdllggq vdgsfqnina vishinagkl ralavtgdkr stllpqvptl
      241 seagvkgadv yswqavaapk glpadikakl haalvtalnd psvkpklveq gfeivantpe
      301 qfaafqaaef arwkkvieag kitad
//
LOCUS       WP_284615444             235 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Aquabacterium
            humicola].
ACCESSION   WP_284615444
VERSION     WP_284615444.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 235)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..235
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25878
     Region          1..>229
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msraerllcl iqllrrhrrp vsgaalsqel gislrtlyrd iaslqaqgaa idgapgfgyv
       61 lqpgfmlppl mftpdeieal vlgsrwvadr adarlggaar qamakiaavl ptearqlldg
      121 sslmvgpavd plppgepsag daglstlrla irdeqklalr yrdgqgreta rtvwpialgf
      181 fdrarvlvaw cemrqelrhf rtdritalep tghryprrrq vllrewreae gisap
//
LOCUS       WP_284615482             355 aa            linear   BCT 25-DEC-2024
DEFINITION  formylglycine-generating enzyme family protein [Aquabacterium
            humicola].
ACCESSION   WP_284615482
VERSION     WP_284615482.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..355
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=38625
     Region          99..352
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 mtvampaptd lpaptsstgh ghffwptlpa elpltlsese llglpayhvp srlstpqpal
       61 mrrllrgdea dwlerladad apiaerwlag qllalagdpr lkplappmvd vaggeftlgl
      121 apervdavma slaglgldra wiakecpayr ahiaafrigr ypvtnheyra fllatghpvl
      181 ptswelgryp leranhpvhs vdaasaeayc awlsgatgrr frlpseaewe laaggpaqre
      241 ypwgdhfdpd rcntvecgll stspvgmfpr gaarcgaqdl sgnveelvat dyapypggqf
      301 vddhlvqing ryrvarggsf arfrdlarck rrhgihrttr vyvagfrlae dpmpa
//
LOCUS       WP_284615501             527 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Aquabacterium
            humicola].
ACCESSION   WP_284615501
VERSION     WP_284615501.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..527
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=55951
     Region          52..489
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mnallhtvsr lanklvplal llaaagcasl padvvrqpss sivqhaaptp lqrtvaastp
       61 peaaalsgfr llpsgpqald arlalaqrae atldvqayli addvsgrqll galrdasrrg
      121 vrvrllvddl haapvlplla glaaqpnaev rlynplpvra gslagrvlgs lhelerinhr
      181 mhnklfiadn tlalaggrnl gdeyfmrsaq snfidmdvla sgpvvgdlag vfdgfwnser
      241 awpvlalegr gqdgaalraq ldhalagsda ppaappedvl grravsiela agrldqvfap
      301 arvladapdk arcdaadcaa gavdqaldll rhaetsvalv spyfvpgddg lallrettar
      361 gvkvqlltns lgatdeplvh agyaryrpal ldlgielrel sptlttrtta lgsfgrslar
      421 lhakvavidr rqvligslnl dprsrrlnte vgllidspal arelarlsrp dvltgayrlr
      481 lddeqriewl aqqddgglrv lrdepdssag lqlklgllsl lvgedwl
//
LOCUS       WP_284615508             264 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Aquabacterium humicola].
ACCESSION   WP_284615508
VERSION     WP_284615508.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..264
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28469
     Region          55..261
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mqdpslcslg rtgvatagll lgaavqaqta qtaqtastpp tappgaitlh yqerppysyt
       61 tadgqvqgll vaptvrafqr aqlpfhwvkt psqrqlvliq astpsmecgi gwfrnpereq
      121 lgrfslplyq drpyvaltrr naswpasrtp adllndaalp llvkdgysyg plldglitqh
      181 aanvrrtsae saqmarmvla graawmiiap eeadallael gplgaqlqls alpgvpdgqy
      241 rhlycnravp ealierlnrv lger
//
LOCUS       WP_284615550             159 aa            linear   BCT 25-DEC-2024
DEFINITION  Rieske (2Fe-2S) protein [Aquabacterium humicola].
ACCESSION   WP_284615550
VERSION     WP_284615550.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..159
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=17176
     Region          20..130
                     /region_name="NirD"
                     /note="Ferredoxin subunit of nitrite reductase or a
                     ring-hydroxylating dioxygenase [Inorganic ion transport
                     and metabolism, Secondary metabolites biosynthesis,
                     transport and catabolism]; COG2146"
                     /db_xref="CDD:441749"
ORIGIN      
        1 mpeappprgp adpgarsdaq plcagaelae rgrallfdvl lwgqparafa lryegrvvay
       61 inrcahvpve mdwqpgefld mdkrwivcsi hgasyeplgg hcvagpcgrg rllplevqea
      121 ggrvywypsr dirpvvfdep aahsgpflpq adpgpdgrp
//
LOCUS       WP_284615592             319 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Aquabacterium humicola].
ACCESSION   WP_284615592
VERSION     WP_284615592.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..319
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=35478
     Region          59..151
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mslhgqaaav vnsqpyweqr fegdweavhg reqsrffgel alamwpawla ermrgdamnv
       61 cdwgcalgdg saalaegfgv avtgidfspa avakaacryp qcrflaedwl agspdpegga
      121 npaydlvfss ntlehfdapw svferlaaha rryvvlllpf eepldgmlhe hrvrfdrstv
      181 plcphpdwvl cdaalsdlgs spfwpgqqvl lvygrcsela atgfsdlhsr rsriadadaa
      241 qrqrerddel aeicrqrdla srklaeiaqq nvalaqqnav laqqntvltq sqqqllqsrs
      301 wrwtaplrrl qarlrpgpr
//
LOCUS       WP_284615614             171 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Aquabacterium humicola].
ACCESSION   WP_284615614
VERSION     WP_284615614.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..171
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18303
     Region          28..171
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mscsparrhg lrtalalaai astggalaae prapalplrt aagepilppd dgvaprwkvl
       61 yldfwaswcg pcrqsfpwmn elherhraag laivainlda rredaqdfld rlpprfaiaf
      121 dpggasaaaf gvkampssfl vgpdrrvlha hrgfrpadra dlerriaaal a
//
LOCUS       WP_284615669             490 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Aquabacterium humicola].
ACCESSION   WP_284615669
VERSION     WP_284615669.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 490)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..490
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=54359
     Region          6..488
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mdkpnaralv wfrrdlrvdd haalhhalvs arqvwcafaf draildplpr adrrvefihd
       61 svveldaalr ekaaahgvqg gglivrhgra adelpalaar ldvqavytnh dddpaalard
      121 aavrdalaak gialhsfkdh vvferrelmt gagapysvft pyknawlral qpqhlrawpv
      181 eqhasalaar padlaglpgl ralgfeatnl hqlalptgas gaqallddfl driddyaatr
      241 dfparkgpsy lsthlrfgtv sirrladaaw qrvqggsrga evwlselvwr dfyhqvlhhh
      301 phvvghafrp aydrirwadg paadahfdaw cagrtgyplv daamrqinqt gymhnrlrmv
      361 aasflvkdlg ldwrrgeayf avhlndfdla annggwqwaa stgcdaqpyf rifnpvsqse
      421 rfdpdgrfir rylpelaglp dalihapwra rpvdlaaagl vlgrdyprpl vdhddarret
      481 larfavargg
//
LOCUS       WP_284615670             340 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Aquabacterium humicola].
ACCESSION   WP_284615670
VERSION     WP_284615670.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..340
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36599
     Region          50..319
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mamlwrrllp ialavplvgt ffcparaeap dvlpppavsa rvepivplag fttrdfdwtd
       61 evrqravpvr lylpdralnd apvplivfsh giggsrlgyt ylgrywasqg yaslhlqhvg
      121 sdrgvwqgnl lgvvgrlqaa aqereaiarv hdlrfaldql lggelaakid ttrivaaghs
      181 yganttllav garveregrp melrdprlka aivisappfy gessvqrilg gievpslhvt
      241 stddvirvpg yysaaedrla vyeatgggrk tlavfeggsh siftdrtgtg gavlnpqikr
      301 atqalslafl rsvfdgdsag laqwpqqfgp llsrytnpsr
//
LOCUS       WP_284615688             173 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Aquabacterium humicola].
ACCESSION   WP_284615688
VERSION     WP_284615688.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..173
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18778
     Region          39..169
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mttrrqlltg avagvaaagg agvawwhrqa dagpdplgpm wqmrferpeg gelvmaslrg
       61 kpllinfwat wcapclremp eidrfarefa krqgqvvgla idgptpvref lrrvkvgfti
      121 glggldgtdl vhqlgnlqgg lpftvligpd gkiaqrkmge tsfdelqsws rki
//
LOCUS       WP_284615745             512 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Aquabacterium
            humicola].
ACCESSION   WP_284615745
VERSION     WP_284615745.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..512
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=54772
     Region          7..504
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mpppaapsll vvddepdlrt lyeltlvreg ydvetagsve eawqrlaers ysvvitdmrl
       61 pdgsgldllr rleaadraek tivitaygsa enavealkag afdyltkpvd lrqfrgvvas
      121 algrapqagp lvkpaslptt aapaptavpa arptapaaiv aeaapglhps larliggssa
      181 mqqvrsmier vargmapvmv qgesgtgkel varaihgvss raaqpfiavn cgaipeqlle
      241 aeffgyrkga ftgatedreg ffqaahggtl fldeigdlpl smqskllrai qersvrplga
      301 vsempvnvri vsathkdlat evqegrfrqd lyyrlnviqv rmpplrertd dleaicgavl
      361 qriardagvs paprlsaeal ahlrayhfpg nvrelenllh ravtlaggdl ieqrdlglad
      421 geagndadwp apeapvaeta saaavpraaa epaplptdlv ayldqverdv lmralerhry
      481 nrtaagaslg lslrqmryrm arlginlsdh ge
//
LOCUS       WP_284615866             234 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Aquabacterium humicola].
ACCESSION   WP_284615866
VERSION     WP_284615866.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 234)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 234)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 234)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..234
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=25122
     Region          1..229
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mrvlivddea parrrlqqll apidgidvvg eaadgeaala laerlrpdlm lldvqmpeld
       61 glavaaslpd dgpavvfvta hdvyalqafd aqaldyllkp vaadrlarai erarrraapr
      121 atvptrqllv ptrqggvavl pcaeihwlea adnyvtlhag grehllrrtl gglladlgdd
      181 fvrvhrgaav aldqvalvrp ndkgdarivl rsgaevacsr ayrpvllerl aard
//
LOCUS       WP_284615896             268 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Aquabacterium humicola].
ACCESSION   WP_284615896
VERSION     WP_284615896.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..268
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=27712
     Region          <138..212
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
     Region          148..178
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          183..209
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mlaisfslrs mtmalgaaga lacagvavaa pkapaaapvt ggpvgpgvcg gfpkadngph
       61 dyrtvrdkrl aiveayhftp gvetltrgss sadiggdlsf tlrafpnhhr almsmvrlsd
      121 rsrseqprgs tlivecwler avrfapddav armiyanylv krnrsddalv qmdkvaevag
      181 dsafthynag lilvemkqyq raldhahkaq alglqrtelr eklqsvgqwk dapeaaapag
      241 aaasaaaasg paasapavaa paaaasap
//
LOCUS       WP_284615939             426 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Aquabacterium
            humicola].
ACCESSION   WP_284615939
VERSION     WP_284615939.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..426
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=47683
     Region          58..426
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mktlswiwia lgsclltlav vlvvinfssg ekkvsqrveh lygtddaqfr rvmgvllgpq
       61 mldgnraevl lngdaifpam laairgarrt itfetyiyws esigrefada lierarggvr
      121 vhvlldwlgs vkmesryleq mqaagieier fhephwwnlp rmnnrthrkl lvidgttgft
      181 ggvgiadkwr graqdpdhwr dthfrvegpv vaqmqavfvd nwtkatgrvl hgeayfpals
      241 prgesaaqmf ssspsggses mhlmyllavt aatrsihlss syfvpddlmt qalaaaarrg
      301 vqvriivpgp didtdivrra srarwgplle agatiaeyqp tmfhckvlvv dalmvsvgst
      361 nfdnrsfrln deanlnlida afarrqievf eqdfrqsrpv tlqawrhrpl kekalehvas
      421 wfgaql
//
LOCUS       WP_284615975             265 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Aquabacterium
            humicola].
ACCESSION   WP_284615975
VERSION     WP_284615975.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..265
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=28826
     Region          4..250
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mlqiriaskt drgarqgned dlrwgtagsg wyavvadgag ghrrgaeaaq ravtsveaal
       61 cdpmlafspa amtqvvraah avvqshqdsn dlsarmhctv valwidgqts halwshvgds
      121 rlyrirrgvt dlvtaddsvv qrmvqaglit aaqasthpqk nqllsalgid gdvqphtvvr
      181 pvelqdgdaf llctdgwwdp ldalqladtl ghsrtpqewl tlmeqrivah anpkqdnfsa
      241 vavwvgdptd vtryrpddtv prfrr
//
LOCUS       WP_284616072             272 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Aquabacterium humicola].
ACCESSION   WP_284616072
VERSION     WP_284616072.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..272
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28296
     Region          2..236
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mntfralmrs aggqpplgaw vmsaspiiae aiglagfdwg vvdmehtple mmgvthllqa
       61 lgntrmatvv rvpwnepvtv krvldagatt vmfpfvqnad earqavaatr fppegvrgmv
      121 gmsrasrfgt apnylqtanr qigvivqies aqavvqieai aavpgvdalf vgpadlsgsl
      181 glpgqtlhad vlalmadavr rakaagvpig tlafsadaat ryramafdfl avasdlnllm
      241 qgaaatlral rtqdgaarvh tlndgtqpep ga
//
LOCUS       WP_284616075             152 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Aquabacterium humicola].
ACCESSION   WP_284616075
VERSION     WP_284616075.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 152)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 152)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 152)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008128
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..152
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15884
     Region          20..149
                     /region_name="CytC556"
                     /note="Cytochrome c556 [Energy production and conversion];
                     COG3909"
                     /db_xref="CDD:443115"
ORIGIN      
        1 mkrpllalav aaaslpaaaq fqkpedaiky rqsaftvman hfgrvaamaq grvpfdakva
       61 adntaivvtm sklpyagfgd gtdkglpnra kpeiwkeqak fndlagkmqa evakldaaar
      121 sgsldavkaa vgavggscka chddyraeky sn
//
LOCUS       WP_284616176             128 aa            linear   BCT 25-DEC-2024
DEFINITION  VOC family protein [Aquabacterium humicola].
ACCESSION   WP_284616176
VERSION     WP_284616176.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..128
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14144
     Region          16..120
                     /region_name="PhnB"
                     /note="Zn-dependent glyoxalase, PhnB family [Energy
                     production and conversion]; COG2764"
                     /db_xref="CDD:442048"
ORIGIN      
        1 mndrfdhlfi epasfdatla fyrdtlgwti dfqwgsagep rgaqlngggv rlviaedhpa
       61 ddhsksggiq ghrptlhlrv ddldaryaal pdraavvvhp esthwgtrwf vvrdpdgnli
      121 ayetpqar
//
LOCUS       WP_284616189             189 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Aquabacterium humicola].
ACCESSION   WP_284616189
VERSION     WP_284616189.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 189)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 189)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007114
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..189
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18885
     Region          65..162
                     /region_name="CytC5"
                     /note="Cytochrome c5 [Energy production and conversion];
                     COG3245"
                     /db_xref="CDD:442476"
ORIGIN      
        1 msdaqhqnha ghdaphegpi ktpkqlmftv vaafvvpvvv iimltnfvaf gtksgagsdg
       61 msaeavarri rpvgsveikd vndpaamktg eqvfqaqcas chatgalnap klgdaaawap
      121 rlkagvdgll qsalkgkasm ppqgggefsd ieigravvyl anqggasfae pkapgaaasg
      181 aaaasaask
//
LOCUS       WP_284616262             399 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Aquabacterium humicola].
ACCESSION   WP_284616262
VERSION     WP_284616262.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466432
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..399
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=45675
     Region          12..390
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 mliarqtpgh laenvmhfar vlraaglpvg tdrvqlalqa lqvagfeskr dfhavlaacl
       61 ldriehrelf dqafvlfwrd pdllgrmral llpkvqvkdg mppapenrrl adalfphqpp
      121 tppedepqqq ieldaaltwn drellqkadf dtmtadewlq arrlladlpl mfeqlptrrt
      181 rpaappgrpd wrttlqamar hggelwdmrw rrartrpapl tvladisgsm srysrmllhf
      241 ahalghaear vesfvfgtrl trttrllksr dpdlaisqvv ravedwsggt rittslqefn
      301 rrwarrvlns ratvllisdg lehgdtqpla femerlrksc rrliwlnpll rferfeprag
      361 gikamlphvd rflpahnlqs laelvqvlrq mdtaprrlh
//
LOCUS       WP_284616357             267 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Aquabacterium humicola].
ACCESSION   WP_284616357
VERSION     WP_284616357.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 267)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 267)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..267
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=29923
     Region          4..267
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mtvitaliad depllrdhlq ahlgrlwpel qivgqarngr eavelfereq pqivfldvhm
       61 pgmngieaar aiarramtvf vtayeqyavq afeqgaidyl ikpfdetrlt dtigrlkerl
      121 ragavpaaav gadgdeagdr lesvldrlaa qlrhqasgkp wlqwikasvg navrlipveq
      181 iaylrsdeky tlvvweggea lirkpirelv demdpeqfvq vhrsvivnlr hvaqvtrgan
      241 etadvhlkgr tetlpvsrsy lhlfrqm
//
LOCUS       WP_284616378             398 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Aquabacterium humicola].
ACCESSION   WP_284616378
VERSION     WP_284616378.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..398
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41994
     Region          90..360
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mfpsliaarr malaalvvll vacggggggs ptpppepeep ivetvgpgqf ksatqlrvvs
       61 tgemtqaiaa agtrapvitp ryavtahrlt yltrdgqgre ilasaligvp vkpagqrspv
      121 layqhgtlfr dneapsnhav asepalimas lgyivvaady vgygvskgap hpyllsapsa
      181 savldlitaa kywrqthrvl dnkqlflagy seggyvtmaa hralqsqasp hlanlagvvp
      241 gagpysvkvt ldalldlvsd enpllgalir pgllknlgas arrqvrdell khllpddadv
      301 nfdvtfldnf laddtaeier vsnvhdwkpa lapklyhgrd drtvpypast rtvaamqaqg
      361 avgvtltdcp aipaghlecv vpywsfmlnq lalsardl
//
LOCUS       WP_284616395             319 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Aquabacterium humicola].
ACCESSION   WP_284616395
VERSION     WP_284616395.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..319
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=33592
     Region          9..310
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 malpprlqnl rlpviasplf iisvpqlvia qckagvvgsm palnarpael lddwlaeite
       61 alaahdrahp eapaapfain qivhksndrl drdlavcekh kvplvitslg arpelnqavh
      121 rwgglvlhdv inntfahkai dkgadglvav aagagghagt knpmalitei rawfdgplal
      181 sgaiatggai laaqamgadl ayigsafiat dearadeayk rmivdsssdd ivysdlftgv
      241 hgnylkpsir nagldpdalp sssphamnfg strkpwkdiw gcgqgigavr avepvamrve
      301 alareyaaar trltenvvp
//
LOCUS       WP_284616409             387 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Aquabacterium humicola].
ACCESSION   WP_284616409
VERSION     WP_284616409.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..387
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40848
     Region          4..387
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mtatassapl agvrvldltr llpgpmctlh ladlgadvik vedtgagdya apalrtlvqr
       61 nkralrvdlk qpegvavlke lacsadvlve sfrpgvmerl gvgyatlsal npklvfcsit
      121 gfgqdgphrd epghdlnyca lagvtdqigr ageppalsnv pvgdlmggsl taamgllaal
      181 fdaqrsgrgr hvdiaiadsm lahavvpmis vlkhghvqpa gtdklggala cygvyatrdg
      241 rhvalgaler kfwdrfcevl gredlkprhl gadadataal raelteifas qplahwqqrf
      301 hdtgccvtpv lrleealdhp qfrargmlve padggprqla cpvkmtgyaf avhrpapapg
      361 ehseellael gygpaqrtal rargaia
//
LOCUS       WP_284616649             271 aa            linear   BCT 25-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Aquabacterium humicola].
ACCESSION   WP_284616649
VERSION     WP_284616649.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..271
                     /product="MlaE family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28207
     Region          21..266
                     /region_name="MlaE"
                     /note="Permease subunit MlaE of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG0767"
                     /db_xref="CDD:440530"
ORIGIN      
        1 mppapaglly rtgvwfsshf agalqstqfv gelvqaagrw fagsaprhlr wrdlvwqldq
       61 sgprsvpivs lvsgligvil aymgavqlqr fgaqafiadl vtigavreva almtgvilsg
      121 rigaafaaql gsmqaneeid alralgvdpm qhlvlprvla lalvapllta yaavvamvag
      181 wavavgifdv spadylhrsl ralelrhvav glgkgtvyav lvalagcrqg lhagrsaqav
      241 gqavtasvvq aivwivvaas lltvalqrvg w
//
LOCUS       WP_284616668             478 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Aquabacterium
            humicola].
ACCESSION   WP_284616668
VERSION     WP_284616668.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..478
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51944
     Region          17..466
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 maqhalivdd dvdaadmlaa lvegerftva iahslaeark qvllhppdiv lldlqlpdgs
       61 gmalfddaql iarseivlit ghaslessiq alrlgaadyl ikpitlkhlr gvlsrvtspq
      121 klraevddlt aglaesghfg glwgrsapmr rvyqqisrva gtgvtvfitg esgtgkevva
      181 qtvhelsrrr krpflavncg aispnliese ifghekgsft gaerqhqgff erahggtlfl
      241 deitemplel qvkllrvlet gtylrvgstv tqeadvriia asnrppqqav asgklredlf
      301 yrlnvfpiel pplmqraedv pllaehflqq vieregeakr ftpaalaklq ayrwpgnvre
      361 lrnvvqrayv maeggaiddd wlptnppgve plpvpaalaa eeppplapae palpadalvl
      421 pigttlaeae rrlilatlqr hhnhkertaa algvslktly nrlkeyaaad vddpsara
//
LOCUS       WP_284616693             150 aa            linear   BCT 25-DEC-2024
DEFINITION  ferritin-like domain-containing protein [Aquabacterium humicola].
ACCESSION   WP_284616693
VERSION     WP_284616693.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10560096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..150
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16870
     Region          9..114
                     /region_name="DUF2383"
                     /note="Domain of unknown function (DUF2383); pfam09537"
                     /db_xref="CDD:430673"
ORIGIN      
        1 mdnddvvdvl ndlietskdg eygfrtsaeh artdalrtll lrradeckqa idelqaqvar
       61 yggkpqqsgs vggalhrgwv amrtkltdyd nvaileecer gedlavnryr kalqedlped
      121 lralvtrqae gvqrnheqik rlreearaah
//
LOCUS       WP_284616747             395 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Aquabacterium humicola].
ACCESSION   WP_284616747
VERSION     WP_284616747.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..395
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=42409
     Region          7..395
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mntdkhqrfa traihagqsp dpstgavmpp iyatstyrqs spgvhqgldy grshnptrwa
       61 wernvadleg gaaafafasg laasatvlel lpagshivcg ddlyggsfrl fdkvrrhsag
      121 hrfsfvdlar penltaaitp qtkllwvetp tnpllkladl ralaeiarah dliavadntf
      181 aspfnqrple lgfdivvhsa tkylnghsdv iggvaivgaa drltpirerl gflqnavgai
      241 aspfdsflal rglktlairi erhnrnaldl aqwlerqpkv srvhypgles hpqhalakaq
      301 maavgggygg mismdlktdl agakrfletv qiftlaeslg gvesliehpa imthatippe
      361 tratlgigda lvrlsvgied vedlredlaq alati
//
LOCUS       WP_284616828             203 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Aquabacterium humicola].
ACCESSION   WP_284616828
VERSION     WP_284616828.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..203
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=21556
     Region          5..203
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mpdtlylasq sprrrqlldq lgvshelllp aageeadeae aleavrpgel paayvqrvta
       61 lklkaarerl rrrglperpv laadttvalg rrilgkpada dearamlasl sgrthrvlta
      121 valwtgrrtl aalsdsrvhv aelpaaaidr yvaggepfgk agayaiqgaf agwithiags
      181 hsgimglplh etatilrqah vsf
//
LOCUS       WP_284616858             332 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Aquabacterium
            humicola].
ACCESSION   WP_284616858
VERSION     WP_284616858.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..332
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36130
     Region          1..331
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrasrlltll mllqtrgrqs apalarqmev svrtvyrdid qlsaagvpvw gepgrsggfq
       61 lregwrtqlt gltvpearai fmaglpgpaa elglgeamat aqlkllaalp sdwqadaqqv
      121 aarfhldpid wfrsavpplh lqavaeavwh aqrlamryes wngvservie plgvvlkagt
      181 wymaarsapd pardatrgre phvyrlsail slqaldqlfe rprgfdlaaw waretarfea
      241 gvysgtarlr ineagfktvq gfspviaaaa ldsaepsath egcievtlpi esvahasrql
      301 lrlgndgevl appalreala qtyrtlalry ad
//
LOCUS       WP_284616876             387 aa            linear   BCT 25-DEC-2024
DEFINITION  Kelch repeat-containing protein [Aquabacterium humicola].
ACCESSION   WP_284616876
VERSION     WP_284616876.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Shi,X., Xiang,S., Cao,J., Zhu,H., Yang,B., He,Q. and Ying,M.
  TITLE     Kelch-like proteins: Physiological functions and relationships with
            diseases
  JOURNAL   Pharmacol Res 148, 104404 (2019)
   PUBMED   31442578
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Gupta,V.A. and Beggs,A.H.
  TITLE     Kelch proteins: emerging roles in skeletal muscle development and
            diseases
  JOURNAL   Skelet Muscle 4, 11 (2014)
   PUBMED   24959344
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Adams,J., Kelso,R. and Cooley,L.
  TITLE     The kelch repeat superfamily of proteins: propellers of cell
            function
  JOURNAL   Trends Cell Biol 10 (1), 17-24 (2000)
   PUBMED   10603472
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..387
                     /product="Kelch repeat-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=39428
     Region          54..100
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          104..145
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          107..382
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          153..201
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
ORIGIN      
        1 mqrrtllplf plaalaalta cgggggdasa pspapaplpp pngslrrldt saaraehasv
       61 vmpdgevlai ggsaagessp sqqvigfrra serfvergel ltgrflhtat avsahqvlva
      121 ggqrsvsntp laelfdlrsg rsaptpqapd gprhdhsata lgdgrvllig grrsfgtppr
      181 ddaelfdlat grftplpgrl lqgrhghgvv aldaqrllvf ggrtsggapa lpevldlatm
      241 rfdaaplswi epaprsgmva lrsagghall iggvggddap lpglvsvqpa ttplrseafa
      301 lrqprarlaa aalvdgrvli tggmvdmgtq gsastelfdp ttgrsaagpt masarwahsa
      361 erlpdgsvli fggydgagya tsvelfs
//
LOCUS       WP_284616983             323 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Aquabacterium humicola].
ACCESSION   WP_284616983
VERSION     WP_284616983.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..323
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=34171
     Region          9..318
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mplppvlanl plpiigsplf ivsnpklvie qckagivgsm palnarpasq vdewlaeite
       61 tlaawdrdhp eqkaapfain qivhktnerl ehdmaacary kvpivitslg artdindavh
      121 swggvvlhdi innkfakkai ekgadgliav aagagghagt rspfalvqei rqwfdgplal
      181 sgsiatggav laaqamgadf ayigsafiat eearasegyk qmivesssdd ivysslftgv
      241 hgnylrgsiv nagldpdklp esdpskmsfg ggtdgeisak kawkdiwgcg qgigavnqvv
      301 parelvarlk reydearrrl sla
//
LOCUS       WP_284617138             252 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Aquabacterium humicola].
ACCESSION   WP_284617138
VERSION     WP_284617138.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..252
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27017
     Region          44..145
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mdqnqaaptv appsigllgi eplralcefv gsrflnaqal ppgdghpvvm fpglasdrha
       61 liplrdcces lgyvvydwaq gfntgpppay epwldglaah vgsiarrhgr rasvlgwslg
      121 giyarevakr vpqatrhvit lgspfagtgr ennvawvyrl lagekpivde alaarlrsnp
      181 pvpttsvysr sdgvvawqac lldetegeae nievdgshig lgwnaevlri vadrlsqpeg
      241 ewqrwgaeac da
//
LOCUS       WP_284617144             400 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Aquabacterium humicola].
ACCESSION   WP_284617144
VERSION     WP_284617144.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 400)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 400)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 400)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..400
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=43339
     Region          <49..398
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mniptpaaaa dvdmatapas asdstilvvd dlpgnlelva ghleqsgyrv vvaqggdeal
       61 erallvrpal vlldvmmpgi dgfetcrrlk ardelrdvpv ifmsaraeis dklsgfatga
      121 vdyvtkpvds aellarvdth lamaalrrql aaqnvllqre iasreeaqaa lqrsnaeleq
      181 layvashdmq eplrmiasyl qlierryadr ldadghefig yavdgakrmq alindmlays
      241 rvgtkgrapa pvesatimki vrehlrlaie eagaeielge lprvhgdgaq lvqllqnlvs
      301 nalkfrgpap prirvecstd aqgwcfsvrd ngigiapeha erifamfqrl harsaypgtg
      361 iglalckriv erhggrlwve padgggsvfr ftlprmatap
//
LOCUS       WP_284617155             236 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Aquabacterium humicola].
ACCESSION   WP_284617155
VERSION     WP_284617155.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..236
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24534
     Region          10..107
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          130..210
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mplrplsclm allaatlpai aqpardarvp dtaaqralac tachrltdvp tregyipria
       61 gkpagylheq lqafrdgrrr ndamarllen qseasmrala ahfadqhapy pppaaapaga
      121 aaqrgaawvr qgdaargvpa cvrchgealt giapmvpglv glpagyltaq lgawrsgvrq
      181 grapdcmaqi arrlpadavs eiaqwlaaqp vpvpatpaas appapwppmd cgilak
//
LOCUS       WP_284617154             408 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Aquabacterium humicola].
ACCESSION   WP_284617154
VERSION     WP_284617154.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..408
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42678
     Region          74..292
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
     Region          216..394
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 msralralla allasllaac gggrsaddpt qatppaatpq qiahgaylat lgncagchtm
       61 pggaayaggr glatpfgmvy agnltpdaat glgrwsaedf wralhhgrsr dgrrllpafp
      121 ytaftqvrre dsdalfaylr slppvnrtnt ahalrfpydt paaiavwqwl fftpgtpppa
      181 aadadpvarg aylvnglghc aachaprnvl gassaapagg dilgqpwyap slhpsagrra
      241 sadelvqllr sgrnaldsat gpmaavifrs tqhwkdadlq avaayltrlq pqpaddppep
      301 aspaqllrgg elygrhcadc hgqrgegrag aypplagnat vqqpgarnlv qlmrhgsfap
      361 ataanpqpys mphagldtrd maavasyvrq swgnrasavd eidvlklq
//
LOCUS       WP_284617284             249 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Aquabacterium humicola].
ACCESSION   WP_284617284
VERSION     WP_284617284.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..249
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27737
     Region          48..237
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mirrrvlval valgaglghg aataqplvig thaqedtvqg rlvrnihrea frrigvevrv
       61 dvfplqrltm lsrsgeidgd varvhgygaa hpdlvrveep myalqfglfa vkeglqvrql
      121 qelagqpwrv vylrgvalcr dgleatlkpa qiqalndedq gldmlladra dlycasdavl
      181 edrlsrpryr dapkfrlqvp lgpplplyay lhrrhaelap rlaaalrqmk aeglidryrq
      241 esllhqtar
//
LOCUS       WP_284617244             436 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Aquabacterium humicola].
ACCESSION   WP_284617244
VERSION     WP_284617244.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 436)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 436)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 436)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..436
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=47150
     Region          110..432
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrsiesrikw rlllgslgls avlgltawww vgrqvrdlld yqleqvartl vdhdfaragm
       61 asqedpamhl avvawddtgr llyrsspele lrfdappgfs rmdsgsqpda vtlrvftlrs
      121 ggrviqvaqp lslrqelare agleilapal aglaalslli vvtvrrslap lrdlgeeltr
      181 rdaqslapie lpqapgelqg alttlnalle rlqasltlhr qfiadaahel rtplaavrvq
      241 adnvahaada qqreaamtql rggierlqrl veqllelari esssmqrrtr velvqlardc
      301 lvdlaaqaav rrmelaldsr gehwidadpr airslldnlv gnalkhapag tgivvtisgg
      361 pggvalsvrd hgpgidpglr ermlerfhrg egaapgsglg laiaaeaarr hgarlelrap
      421 engpglearv lfaagr
//
LOCUS       WP_284617306             760 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Aquabacterium humicola].
ACCESSION   WP_284617306
VERSION     WP_284617306.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 760)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 760)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 760)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 760)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 760)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..760
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..760
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=83823
     Region          26..760
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mgirsfaael llpaalqpkh rapaietapk peaasfaals dklgylskge ikqireaykf
       61 adeahlgqfr asgepyithp iavagmvadw rldaqavmaa lmhdamedcg vtkvelierf
      121 gaptaelvdg ltkldklqfp treegqaesf rkmllamard vrvilvklad rlhnmrtmaa
      181 mqpakrkria retldifapi ahrlglnqiy relqelsfah lfpwrhgald kavkrsrgyr
      241 rdivdrvhkd vekafaaskm kvlvsgrekt vysiyrkmre khtsfaqvnd ifgfrivvqt
      301 lpdcylalgv lhqlykpvpg rfkdyiaipk pngyqslhtt lvsplgtave fqirteqmha
      361 vaesgiaahw lykndrragg sgdahplgam wlqslldiqd etrdaaefle hvkidlvpea
      421 vyvftpmski malprgatav dfayaihsdv gdhcvaakvn gepvalrtel ksgdvveivt
      481 apgarpnpaw lnfvrtgrar skirhflktm eqeesrslge kllqqalrae glglpstdpt
      541 dteanalwhq ltrwsgnrgr gelltdiglg rkiativakr laqlmaergt rpdavtltlg
      601 ryaaddaaps qggvaidgse gasvqlatcc rpipgdaivg ylgrgegllv htadchngkr
      661 lkerdperwm avewaeqpvr afetmiavqv rngkgalaqv aasvsaaead ithidmdner
      721 dadiaelrls lavrdrhhla dvlrtlkrsp pvvrasrvkp
//
LOCUS       WP_284617309             305 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Aquabacterium
            humicola].
ACCESSION   WP_284617309
VERSION     WP_284617309.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 305)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..305
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=33142
     Region          3..248
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mrfsvyqvsr kggreknedr mgycytrssg lfaladgmgg hpegevasql alqtmaalyq
       61 rdakpglkdp lrflhdaila ghhqllryat dkalldtprt tivacvlqgn aaywahcgds
      121 rlylvrgdkl iartrdhsyt elqdtmaqvv piaqrfnrnv lftclgspgk pvvdtagpll
      181 mqpgdkvllc sdglwgsvtd aviteqlslr pisdavpela eqalrnagak sdnvtilave
      241 weaaedhest vavstqnlgd evfastiqas lgageappde lddaeiersi reineairrs
      301 sqkkh
//
LOCUS       WP_284617333             244 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF1223 domain-containing protein [Aquabacterium humicola].
ACCESSION   WP_284617333
VERSION     WP_284617333.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 244)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..244
                     /product="DUF1223 domain-containing protein"
                     /calculated_mol_wt=26031
     Region          11..242
                     /region_name="COG5429"
                     /note="Uncharacterized conserved protein, DUF1223 domain
                     [Function unknown]"
                     /db_xref="CDD:444181"
ORIGIN      
        1 mdarspwcaa tlalglatst gvvadagrce arsapqqarl velytsegcn scppadrwls
       61 tlkgrddvla aafhvdywdh lgwkdrfgaa ahterqaqrv aagasrfayt pqvlvdgrdw
      121 rrwpqlppag gpapvaiqlr redtrvivdv apltgapgti aawwvlledg hasavkagen
      181 rgvalqhdhv vraygqrasw asaaparfei taprhgeggr pvrllvvvsd arsglplqav
      241 qlgc
//
LOCUS       WP_284617396             495 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat-containing sulfotransferase family protein
            [Aquabacterium humicola].
ACCESSION   WP_284617396
VERSION     WP_284617396.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11929146
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..495
                     /product="tetratricopeptide repeat-containing
                     sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=54637
     Region          3..>187
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Site            order(15..16,18,42,45..46,49..50,52..53,77,80..81,84..85,
                     89)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          40..69
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          76..105
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          255..437
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mdlppelrrl qavaetllqq grvlqaieaf eqllrhearl pdawynlafl qhrarrfdea
       61 lasygqalvn gvagaeevhl nravilsdhl arhdeaeqal haalalqpry lpalinlgnl
      121 reqrgertaa leayeaalai epghalalsr lphlkppqra ddpligrlrr aiaqagpaeq
      181 adlgfalgka lddaqaydda faayaaanaa sraagggvry daaahercid sliaafpdar
      241 prgmpappav gprlifvcgm frsgstlver ilarhpdvta ggeidllpgl mrerfgpmpq
      301 vvspldeatl qrwrthyler iatmfpgarc vtdkrpdnfl yiglirrlfp davivhtrrh
      361 pldnclsihf lhlshtmpha ldlldtahwy rqyerlmahw qrlhgdtmhd vdydalvadp
      421 qpvvaallea cglawsercm sfhegdgvva tpsgwqvrrp lytassgrwr hyarhldglq
      481 aalgmppgke ppvta
//
LOCUS       WP_284617410             181 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Aquabacterium humicola].
ACCESSION   WP_284617410
VERSION     WP_284617410.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..181
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=19221
     Region          1..112
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mhdslppspw ierwahllrp gataldlacg sgrhvrflaa rglgvtavdr daaalvalrg
       61 vaevivadle gapwplsgrr fdvvlvtnyl wrplwpqlla slapggllly etfaagnetv
      121 grpsradfll qpgellqaca glrivgyedg fldapprfvq rvaalapdpa apsplrvplp
      181 s
//
LOCUS       WP_284617554             497 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Aquabacterium humicola].
ACCESSION   WP_284617554
VERSION     WP_284617554.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 497)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..497
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53048
     Region          40..164
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 maddqdglra ladridelsr qrlafareqa rseppdeasp vlwvhlihgt wanpekagsr
       61 ptwfepggsl esalrahgha ddwqrvrfad vppwsgrnsf aarsvavkdl adyfegvlfc
      121 prttfdrhvv vahshggtva aealrhlgpl aaefsglltl gtpfverfrk veapesvsfd
      181 sltgiyahav afffaftlal cflfegwpgl aaasavvalm pwgfariprl rlvaevlnaa
      241 ipwaalavhv aafdlwgpsg slgnliisav vslalavvla pklmvlrsvh flgssdglre
      301 dehpaplkte llairapgde ashaiaaasa avwisdqlse vgfktlgrip raayavlgva
      361 livtagglfv fpdraawkla aalawslpvv gpmgllmlal lgksmatlli alacgpealq
      421 apgvmkvfae plprssdgla atatlrmvfp saadlealrf kgslrhaiyd ypsvqkyvaa
      481 wilhhatrpg ptaphrq
//
LOCUS       WP_284617627             352 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Aquabacterium
            humicola].
ACCESSION   WP_284617627
VERSION     WP_284617627.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..352
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38751
     Region          40..339
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrhlrrivca alvlglaagg lvaasdavyp aaqwtevdpa akgwsaeklq qadelarqlr
       61 saaylvvheg vivhrfgdie rpldvasvrk sllslligmq tgrggidldk slgelgiddk
      121 agltadekra tvrqlmqars gvylpaanet pdmarqrper gshapgtfwy ynnwdfnvlg
      181 tvyqratgrt vfegleaela qplgfqdlqp akhfrfnrid asehpaymmw lsardlarig
      241 llvsrqgrwg prqivapewi aestravttf ppggaygymw wtrpafgnvw aegsrgqfll
      301 inaardlvvv hrvgwglfdg pgvdaeqfta lyrrilaaap wrrdtpaapk ap
//
LOCUS       WP_284617685             811 aa            linear   BCT 25-DEC-2024
DEFINITION  efflux RND transporter permease subunit [Aquabacterium humicola].
ACCESSION   WP_284617685
VERSION     WP_284617685.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 811)
  AUTHORS   Sandhu,P. and Akhter,Y.
  TITLE     Evolution of structural fitness and multifunctional aspects of
            mycobacterial RND family transporters
  JOURNAL   Arch Microbiol 200 (1), 19-31 (2018)
   PUBMED   28951954
REFERENCE   2  (residues 1 to 811)
  AUTHORS   Hand,N.J., Klein,R., Laskewitz,A. and Pohlschroder,M.
  TITLE     Archaeal and bacterial SecD and SecF homologs exhibit striking
            structural and functional conservation
  JOURNAL   J Bacteriol 188 (4), 1251-1259 (2006)
   PUBMED   16452406
REFERENCE   3  (residues 1 to 811)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
REFERENCE   4  (residues 1 to 811)
  AUTHORS   Arkowitz,R.A. and Wickner,W.
  TITLE     SecD and SecF are required for the proton electrochemical gradient
            stimulation of preprotein translocation
  JOURNAL   EMBO J 13 (4), 954-963 (1994)
   PUBMED   8112309
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..811
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86619
     Region          22..793
                     /region_name="MMPL"
                     /note="Predicted exporter protein, RND superfamily
                     [General function prediction only]; COG1033"
                     /db_xref="CDD:440656"
ORIGIN      
        1 mhaptasdtl aapptladfg prsgsllerg vfnhrrlvlg lcamltivlt liaamrltln
       61 asfdkmiprs hpyiqnfleh rddlrglgns lrivvaareg diyqpkyvet lkrihdevfl
      121 tpgvdrawvk slwapgvrwt evteegfrgg pvmpdnydgs aaaterlrgn iaranlvgsl
      181 vgkdfrssml vvplldqdpg tgqridyral sraieairtk aegegqvsvh vvgfaklvgd
      241 lieglkqval yfglaalvaa liiqaytrcl rstalvlacs lvavawqlgl vaalgfeldp
      301 ysilvpflvf aigvshgaqk mngimqdigr gahrlvaarl tfrrlflagl talladavgf
      361 gvlmlidipv irelalaasl gvavlivtnl illpvllsyv gvsakaaera lraesgangg
      421 aflqrvwrgl erfteprfaw aaiaaaiglt afgvitsqrl aigdldpgap elradsrynr
      481 dnqfinasya lssdtfaviv ktpkegclqy atlietdrla walqqvagvq ttvaltnavr
      541 qitagsnegs pkwltiarnq dvlnygaqqa svnnpdlfnt ecsvmpviay ladhraetld
      601 rvvaasadfa aahstperqf llaagsagie aatnivvrqa wtqmllwvya avivlafitf
      661 rswravviav vplvvtsvlc ealmvalgig vkvatlpvva lgvgigvdya lyllsvqltq
      721 qrqgvplrea yaqalkftgk vvalvgitla agvltwalsp ikfqadmgil lafmflwnmv
      781 gavvlipals avlmpqakpg rqagaiaaaa t
//
LOCUS       WP_284617701             845 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Aquabacterium humicola].
ACCESSION   WP_284617701
VERSION     WP_284617701.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 845)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..845
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..845
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=90599
     Region          13..845
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mtpaptfrfh rfelrpasre lcadgvpqrl gerafdllla laeaggavvs rdalferawp
       61 grvviddnlk vqvmalrkll gpeavvtvpg rgyrlgwpll dspdaappav ppaapdpsrl
      121 fgreaelarl rsalaagrll tvtgpggigk trlaaaaada ergrwpdgva wvelaaltep
      181 dampaavaha lrlpagprpv daagiaralr plqlllvldn cehllpaaaa llsaiaaaap
      241 qvallatsqv rldiageavl aldglalspa daapdaaqrs psealfaarv rtvapqield
      301 spadvslarq ichrldglpl alelaaarvp alglagvlqr ldhqlqlltr gpahapprqq
      361 tlratlawsh elldevqrvv frrlgifadr ftlddaqava adqsidewav ldavddlvar
      421 sllrpldpvg gagerryrll vharayaleq leaaaehdav mrrladhlvr sfvaaeqgfl
      481 haalgpwvda lwprlhdlra alqwaarqpa eadrllalas aagpfwaaan ldreaapwle
      541 rvrplgeapg ladeplaryc kavafrlvnp tapvaesvaa aergaelfer lgdhasayrl
      601 lglvaqhgrr idpqrdwqpl fqrlralerp ewsatmrltr lraegvaqar agdwagyrer
      661 fqleaallae agdalrawga syhvalaela lkrpaaaiav lepmvaqvra agllrelwtr
      721 pvllalarie agqgaeaapa vreavtllrv agahawcadh fawwaldcge palgarlagw
      781 adatvrrngq prhaharaah eqaslrlavk lppaarealr aegeafddel allrvlqlad
      841 alitr
//
LOCUS       WP_284617765             370 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Aquabacterium
            humicola].
ACCESSION   WP_284617765
VERSION     WP_284617765.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..370
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39533
     Region          81..365
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mndalahaie laqahetpwp rdpfaapapg qqpwgvhhdd pppynrlfgp vhargpqsgv
       61 llqhgrelaa wgeperadlt fsvaktylal iagiadargl lvldqpvhqa lpgigfddna
      121 hnravtwrql ltqtsewegt cfglpdtvdr wrqvaqdprp aggpkggarp lqapgtywey
      181 ndvrinqlsl allhllrepl palfleallr plgggegfaw rgydaswaev pglgrvasvp
      241 ggahwgggvs isardqarig qhlldvlagr tggrtdgrtv gpvrrewiaa maepcpvapf
      301 ygrlvwlnrg grafpgasdd ammmlgaggh tvwvdpalda vvvlrwldpa wsgavtaaig
      361 aalrgeaatr
//
LOCUS       WP_284617784             109 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Aquabacterium humicola].
ACCESSION   WP_284617784
VERSION     WP_284617784.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 109)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 109)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 109)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 109)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..109
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11691
     Region          <16..91
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdeqavvral aalaqplrlq vfralivaga egltpgtmae aldvpqnsls fhlkelshag
       61 lvtqerasrh iiyraafeqm nallrylten ccqgaacvpe rglnrssca
//
LOCUS       WP_284617786             167 aa            linear   BCT 25-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Aquabacterium humicola].
ACCESSION   WP_284617786
VERSION     WP_284617786.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..167
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=16620
     Region          30..163
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mktitsvpll tlallattlq aqaqtalvrt eknmslelan qiaaqgvaac ganghavava
       61 vvdragtlra lqradnagph tveaslqkaf tsasaknttl ammdtaqknp gaanlvhlpg
      121 flllgggvpv kagsevigav giggapgghl deqcavaald kvkdllk
//
LOCUS       WP_284617835             411 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Aquabacterium humicola].
ACCESSION   WP_284617835
VERSION     WP_284617835.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..411
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=45732
     Region          130..406
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mnpswllpsl rraaarppla arlllpmlar lrgglldltl pdgrrecfgs gdgpvarlvv
       61 hdwrvfgrvl aagdigfada fiagewqsse patllrllla nrgvldaaih grgpakllhg
      121 lralaqrntr rgsernihah ydignafyre wldetmsyss awfdgdltrs ladaqrlkmr
      181 ralaecgiap ggrlleigcg wgalaelaar etgaevtgit lsrqqlawgr eriadaglaq
      241 rcrlqyadyr dlpalaegrp fdavisiemf eavgaaywrs yfdvlrrslk pggraciqti
      301 tmhealydry vrstdfiqqt ifpggrlpsa svfraeaera gfevertlhf gadyaetlrr
      361 wrerflarsa vlpalgldqr fertwhyyla tceaafavgd tdvvqftlrr a
//
LOCUS       WP_284617839             257 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Aquabacterium
            humicola].
ACCESSION   WP_284617839
VERSION     WP_284617839.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 257)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 257)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..257
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27376
     Region          9..254
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mamnppieqw tgrvawlvga ssgigratae rlhaagatvv lsarnaaalq afaarhpgsi
       61 aapldvtdaa avarvadell qrhgrldlvv ycaahyramg vddfdladal qhlqvnyaga
      121 lhllnavlpa lraagsghls lvasvagyrg lpqalaygpt kaalqhladt lyldlrprgi
      181 gvsvinpgfv dtpltarngf rmpalltpee aarhivdgwr rghfeihfpa rftlwlklln
      241 hfghagyfra vrwatgs
//
LOCUS       WP_284617885             407 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Aquabacterium humicola].
ACCESSION   WP_284617885
VERSION     WP_284617885.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..407
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=42561
     Region          23..391
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 miplelaall drsglqplrl rgrtllpilq ggmgvgvsah rlagsvaaqg avgtlssvdl
       61 rrhhpdlmer trglgvgpea kqaidaanle alerevtaar alsqgrglla mnvmravsey
      121 aayvkrslaa gidaivvgag lpldlpdlaa dhpetalvpi lsdargvqll vrkwerrkra
      181 pdaivlehpr lagghlgaar vedvndprfd fersvpetla vlraaglent pviaaggigs
      241 vddirrlqgl gaagvqlgta favttegdad pafkqvlaea tpadivefts vaglparava
      301 tpwlkaylka epklqavaqv karctkafdc laqcglrdgk vgwgqfcidq qlaaalkgdv
      361 rrglffrgag alpfgtqirs vrelierllg gelptvpaal eatpaaa
//
LOCUS       WP_284617914             643 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Aquabacterium humicola].
ACCESSION   WP_284617914
VERSION     WP_284617914.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..643
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=69357
     Region          32..608
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mntlhspval acaallatlp latraqelpt ptvvvtatrh amlaldapaa lsvvtrrdle
       61 araaddlfda lrgepgitlq grtiggrkvl glrgldskht lflidgrrvg asdgivghsd
      121 fqydwipved ierievvrgp lsvlygseam ggvvnvitrp agdrwrtgar vdggvasgqr
      181 ggdsqraslr idgplaerls lvagaadsrr salasiedpr iseleghrks dvwmglgwrp
      241 tgtqridldl rageetrvad arersgrkry hetvnalers laslgwsgdf dddrqsaklr
      301 ayesrldven rrsagvainp pqrltervle gqwriargsh avatgfearn elladpglpg
      361 geslaehrsl flqdewalrs tlnatlgvrh drhslygnst spraylvwrg gpqwtlkggv
      421 ssgfkapnlk qivpgarpeg pnsflgnpgl kpersrggev vlayaegarq aqltlfqqrv
      481 tdlidvrlvs pgsvpgtgty tyenisrarl rgleaslvqp lgagftaqla asklsaedgq
      541 gralerrpsy sasarldwqr qawraglrie rsgpqwlpat sgpaqrapal tlsgayaart
      601 laeglelsvg vdnlgnlrpv eksalythae aprtwrmais gqw
//
LOCUS       WP_284617964             521 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Aquabacterium humicola].
ACCESSION   WP_284617964
VERSION     WP_284617964.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 521)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 521)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 521)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..521
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=56325
     Region          8..502
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          267..505
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mtpptppral rssvsrlllp llawigawta mlaldgyvdl anlamvlvlg aavaslwlpi
       61 waslamsaas vtafnwlfvp prytfsvdlr qdalllaaml vvcwivagvm arqrvladaa
      121 rqharrteql rslaqalrdt ddptrradil attlaqllgk aplmlllkda lpssddddaa
      181 livgsptahq rsglwhctrr aqpfgpgtgr yaelpewylp lrgrarafga vaielddpva
      241 addemraqaq alcdqmgavl eqvqtqrvad aarqaaqtqg vrnallaais hdyrtplati
      301 lgsasslleq gdrlapeqrq klaraivdec gqlkrltdnt lqlarldapg vqlrtdwesa
      361 eeivgavlrr vrthdharrv karlepglpl lrcdallltq llenlvdnal kysdgaiell
      421 vrgqadgvtf avrdrgpgvp paererifev fqrgppnasd aarrgagvgl avcraiarah
      481 ggeltlrprg hggasfecrl paleappprp gngqveeeer s
//
LOCUS       WP_284617987             153 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Aquabacterium humicola].
ACCESSION   WP_284617987
VERSION     WP_284617987.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..153
                     /product="YybH family protein"
                     /calculated_mol_wt=16195
     Region          36..150
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mtdrrhalia aaslpafaaa gcatpratas pdellaqvra aetafadtma rrdlagfgsf
       61 laddavfvng gkplrgkaai vvhwtrfyap gpapfswkpe laevsgegrl gytegpvmdp
      121 sgkvfakfft twqlggdgrw rvifdngytv cka
//
LOCUS       WP_284618003             166 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Aquabacterium humicola].
ACCESSION   WP_284618003
VERSION     WP_284618003.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..166
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18619
     Region          8..36
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(9,12..13,16..17,19,43,46..47,50..51,53..54,77,
                     80..81,84..85,88)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          41..71
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <43..>134
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Region          76..104
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mntpdasieq rlalietlfe ksdfsavlqi cndiielddg hfeahserar anqrlgrlgd
       61 amsdlqvlid lrpdsptayl rraalnmelg hdalavmdls rvvelgdgyy lstahfyrai
      121 ayhnigdkea srrdatllpn dfrffvktkd hgtrqlsrqe vldlas
//
LOCUS       WP_284618004             183 aa            linear   BCT 25-DEC-2024
DEFINITION  SRPBCC family protein [Aquabacterium humicola].
ACCESSION   WP_284618004
VERSION     WP_284618004.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..183
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=19884
     Region          27..168
                     /region_name="SRPBCC_CalC_Aha1-like"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of Micromonospora echinospora CalC, human Aha1, and
                     related proteins; cd07814"
                     /db_xref="CDD:176856"
     Site            order(27,29,31,40..42,44..45,50,58,66,68,70,72,83,85..86,
                     88,91,97,99..100,116..117,119,121,132,134,136,138,
                     147..155,157..159,162)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mkktaliaal laalgpaapa gaaeraveke vvvpaalpav weawttsrgi tsfmaphavv
       61 eprvggafhi hfapdappgq rgaddmrfma lqpmkmlsfd wnappslpqa raqrtfvilr
      121 fepvtptstr vrlhhtgwgd ggewdeayry fdrawgavlg klvqrfeqgp vdwgrpvklp
      181 vaq
//
LOCUS       WP_284618092             310 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Aquabacterium humicola].
ACCESSION   WP_284618092
VERSION     WP_284618092.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..310
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32806
     Region          1..300
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(34,247,250)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(187,218,245,248..249,252)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mfivcgealf dvfstgdtat glafdgrigg spfnvamgla rlrqpvgflg gigtgfager
       61 lmralldegi dtrcaarlda pttlslvgld argvpsyafy ghgaadralr pehldavppe
      121 arafhfgsya mvvdpvastq rllverehpr slisydpnir anvepdlavw rstllwmlpr
      181 thllkisded lallhpgrtp eafaaealaa gtalvvvtrg adgalgftar etvavpgvpv
      241 alvdtvgagd tfqaalltwl aerdrldaaa laslrrdeld galrfaaqaa aitcsrrgad
      301 lprraelpdr
//
LOCUS       WP_284618241             476 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Aquabacterium humicola].
ACCESSION   WP_284618241
VERSION     WP_284618241.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..476
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=51355
     Region          25..>207
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mntldarala alcdketgta prgprravvl gaslagllaa rvlhehvdev lllerhalpm
       61 dlgpretmph thhthallar grqvieqlfp gigdewmaag grlgdvgsda lfyagrrrfa
      121 qapadaqaic lgrsaiegvl rwrvralpri tlvsgveatg llgaadrsav tglhwrlrde
      181 pagdrrtlra dlvvdasgrg srlpkwlvel ghdapreeqv hcqiryatay lqrepqhapg
      241 leavicaatp dhprpsvlls qeggrwvvtq ggygedappl dregfirraq eaapselaav
      301 vrdaqflcep fgyrfphsqr rryersslpa gvlaigdsic sfnpvfgqgm svaacealal
      361 qqalqagaai drglarryfr aaarsidiaw qtavgadlai psvqgerplp vrlinayvak
      421 vfdaaqtdpd vavafervsh lleapptlmr pamlarvlsa rwrrpadatr pavaaa
//
LOCUS       WP_284618288             108 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Aquabacterium humicola].
ACCESSION   WP_284618288
VERSION     WP_284618288.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..108
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11966
     Region          3..81
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mndddidrll ralsdatrrr lldrlrdqpg ltlgeliegf tqsrqalskh lalleavdlv
       61 vpvwrgrekl hylnpvplqt lparwvttsa rehsaalaal hkalegas
//
LOCUS       WP_284618282            1949 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Aquabacterium humicola].
ACCESSION   WP_284618282
VERSION     WP_284618282.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 1949)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1949)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1949)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1949)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1949
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..1949
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=211242
     Region          226..1938
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mrlgiaafsr iagnivaalm aaavtapaea aritgvtpqg evaqvrqlvv rfddavspag
       61 dmlrqapltl qcsggalper sarwnterew vldfhaplpp gvrcttqrnp awqprsgtle
      121 grtdfnfstg gpaiersdpw dgsttiaedq hfllrltgpa tpasiaanaw cevdgigeri
      181 glnivngaar davlkarrvr aadaartllv hcarplspqa klrivwgagi asaadpavqt
      241 rapqrlrfev qprftaefsc ereraqapcm plaaaivrfs apipralaeq lrltpsdskh
      301 gaartpklpd nesqtsevrf paplpeqasl qltlprelkd iadrplanad rfpltvatgp
      361 mpplakfaas pfgivehgpd amlpitlrhv qgeiraggav rikkiderew lkwmgqlaaa
      421 qnnefksret allarqpdvr kldlpqlqgg dprpfevvgi plaepgyhvv eiesqvlger
      481 llatrapmfv rtgvlvtnlg vhfkrghens lvwvttldra qpvadaevll hdcvgkrlwe
      541 grtdaqgral vpqalpdpne erctwqpgyy vtaskvmkta qgqpqrdsaf vfsnwnrgie
      601 pwrfnqvsgl ygdergaeql rvhtifdrll lragetvsmk hlvrqettag lrdadraslp
      661 ttlkivhvgs gdevtqplqf daagraalss waipptarlg lydvilksar rvwsggrfrv
      721 eefrlplida klmpprgdvi apaetvlslq lnhlsgggva raparasall rdrdvsfpgy
      781 enfsfqpprp errdpsadde pasgdaaklv vdkqalatda ngaaavtlkg lpkitrpsel
      841 qaevtfndpn gevqtvssrv plwpaarvvg vrtgswaaai gkvkfqaial dlrgkpiant
      901 klgviarvtq weasrkrlvg gfyaydqrsl qkplgevcsg ksdergmllc easidaagev
      961 elvarsidea griaeaattv witrqgelwf eqdnddridv ladkphyapg etarlqvrmp
     1021 yrqatalvsi eregivdsrv vqlqgddpvi elvipnrdak sgtagastas wapnvyasvl
     1081 vlrgrvrhvp wysffnwgwr spgewwrafr yegreyqapt amvdlakpsh kfgvanlkig
     1141 laahqldvkv tpersqyavr qtvktrvqvt qagqpaagad mafaavdesl lallendswk
     1201 vlesmfppra wavetstaqg eiigrrhygr kaipaggggg rnptrelfdt lllwrgsvtl
     1261 dargeatidv plndsltsfr lvalassgad rfgtghatvr vtqdlqllpg lppvaregdr
     1321 fdavytlrnt tarelkvdaa laasvqrddg agglqrtplt fapqavtlpa ggaaevkwpi
     1381 elptgaislv yeataqekvd rggvrdavkt tqlvrpalpv rtwgatlqql dgpvtlpvap
     1441 padaipvdpa kpdgpraggl viglqptlag alpgirrffe qypfscleqq ssralalqda
     1501 aawtrlvnal pgyldadgla lyyppragda prgsdrltay liaaaheakq tipdaprerm
     1561 lqalvnfveg rlerkpwvpa ssagidldvr klaaiealsr hgraraaqlq sitiepnrwp
     1621 taavidwlri lqridgvper aqrlteaqtv lrsrityags mlkfsteagd fwwwlmdsgd
     1681 anaaklilal vddpawkdel prlvlgalgr qqrgawlttt anlwgvlale rfaarfesaa
     1741 vggrsvatlg sasvshdwsa qknggrmslp wpaaaasgat lqvtqqgggk pwltvqalaa
     1801 vplkapvaag yrltrtvsav erkadgawsr gdvlrvrvei daqadmtwva lndpvptgat
     1861 llgsglgrds aiatggerre gsawltyeer aqdafratwe fmprgkhvie ytlrlnsagr
     1921 fglppsrvea myapesfgev pnavlevkp
//
LOCUS       WP_284618406             874 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Aquabacterium humicola].
ACCESSION   WP_284618406
VERSION     WP_284618406.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..874
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..874
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=94174
     Region          <2..874
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mqdraapgap alierempla rfadwlrala apgaggrcll lhgeagvgkt svlqaaraaa
       61 ppgldwligw cepllsptpl gplldmvdgl ppglaslvqr ghrvqdvmpe llawlrqrra
      121 plvlavddaq wadhasldll rflgrridal plglvlsyrd delppehplh vviaglppaa
      181 tlrlplapls argvelaahr agrapnglhr ltqgnpfyvg ellrergggq lpasvrdtvl
      241 araqrlspla rrlldaasvs pvpveravlh gidpalidai decaasgllv dhddsivfrh
      301 elarraiesa ladgrrrtlh rqllqllpea patrrvhhad gaglddevlq lapqaaedaa
      361 raaahrqaaa lytmalersa qappalragl ltdqaeqcel igeldraqaa reqaialqre
      421 agdavatalg qarlarlrwl rgdlaggkrl ageaiaalep lqrprelgra vavmaqmhll
      481 dpsraaedwg rralalaeaa rddetlahal ntvgseelvr adrddawakl erslrmsler
      541 gwseqaaray mnliahalvh rrmaraaqlc dealaycear dfelyvarih vrrafarlet
      601 gdwaradqel aallsrtdll pmdraqcehh rarlalrrgq paapavrtyw idalagrrgp
      661 dpapwyapla paaaeaawll gqrdgllriv haawapslat gepwrcgqla vwlrrldale
      721 alpafdvapp caaelagrld daaaawlrlg naweaglall ggtvaqlera lalfdelgaa
      781 paaalarrrl relgstarrg lgkatradpl gltpreralv elvaqglsdr aiaarwhrsp
      841 rtvehhvasl laklglarrg dvaafvatsa arkp
//
LOCUS       WP_284618418             432 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Aquabacterium humicola].
ACCESSION   WP_284618418
VERSION     WP_284618418.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..432
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=45376
     Region          <98..296
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
ORIGIN      
        1 mfanrfsarp hraalvssll callvsaapv gaqtaapasa asapagptvr aevanplnaa
       61 qtmiranqgk ealakvaeae gvpnltpyeq htinhtkava alaagdpals lslfekvlas
      121 sfmpekdrlp itesavrlai qsknhakaie hlksykqqgg ndgallraha qllaetndfa
      181 gaiaeakaqi aaetaagrkp petlyrvlgy sqqkandtag yvqtleqlvq qyptpdywad
      241 llsrivrkpg fsddrlrldv yrlqrslgvk legeeiadma qramliglpa eakalldegy
      301 gagllgkgkd aaaqaklrdq ankaaaqdak alaeneaaaq kakdgtalvn lgmavagtga
      361 wdkaatlieq giakgglrra deaalhlgyv qwragrsdda lrsfggvkga degtndlarl
      421 wayhvraaak ks
//
LOCUS       WP_284618592             857 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Aquabacterium humicola].
ACCESSION   WP_284618592
VERSION     WP_284618592.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 857)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..857
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..857
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=91619
     Region          7..855
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 msnmsnpppl pavlrfgrfe lrsleqrlla dgelvplggr afdlllalaq ragqlvtrne
       61 lieqvwpgrv veennlsvqv nalrkalgae wlvtvpgrgy rfvapaqpvp raaapppepp
      121 rgprtrlpaa qplligrsed laalgtlidq hrlvtvvgag gmgktrlaqa llqlranaya
      181 qsvcwvelgp vataealpaa vaaalelplp pgdalaqlsq amrglqmlva ldnaehlldd
      241 varlaqalld aapglrlvvt sqaplrlsse rvlrlgpmav pqgvlparea qafgavalfc
      301 eraaaadhrf vladadvpav ialcqrldgl alaielaaar apllglarll daltdrlall
      361 kssrsrlapa rqqslraale wsvglltpiq qrlfrrlgvv agsagldlvq qlgadapdgt
      421 asdpwavvda ldeliqrslv dvqvadgdgt pryrllespr alalerlaea geeqavrerh
      481 aralldafer aewtmlagaq dvagwrrdge plfvdmlqal awaekaadhr lslglatsll
      541 grvpdprhve trdavrices qlasgeiadd llacrawsvv slvtfrgpqr sqeattrala
      601 rarrlgasdd erfmrydvlc eaarvraagq dfeqaqalle eadaladpaw apvrlrnaqr
      661 araflalaqk qpelalhhmr qtlalslaag dpslatrlni adfeltagqa aaavetgral
      721 vqalagrrat gllqlarlnl aaahlaleqt gearellqaa wdasrsvgrd wphlaqyldl
      781 mallcalqgr heaaaqwlga adaryeavsg grtaneqwav grtlgllhda lpapvrdalr
      841 aqgrslsdae laqlgks
//
LOCUS       WP_284618619             420 aa            linear   BCT 25-DEC-2024
DEFINITION  lanthionine synthetase C family protein [Aquabacterium humicola].
ACCESSION   WP_284618619
VERSION     WP_284618619.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Zhang,Q., Yu,Y., Velasquez,J.E. and van der Donk,W.A.
  TITLE     Evolution of lanthipeptide synthetases
  JOURNAL   Proc Natl Acad Sci U S A 109 (45), 18361-18366 (2012)
   PUBMED   23071302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10141013
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..420
                     /product="lanthionine synthetase C family protein"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0031179 - peptide modification [Evidence
                     IEA]"
                     /calculated_mol_wt=46165
     Region          62..400
                     /region_name="euk_LANCL"
                     /note="Eukaryotic Lanthionine synthetase C-like protein;
                     cd04794"
                     /db_xref="CDD:271202"
ORIGIN      
        1 mlhdparhep lrtmawdear vratiarivd etvaaftpdg lwpvhprdve sgedpdapvt
       61 nlyygaagvi waldwlraag aakspsfapy ldplrqrnra avaampgdnt gswlmgdlpf
      121 emmawghapt gplravradt iaaliernid hparelmwgs pgsllaaamm hgasgdarwa
      181 alfrriaqrl reqlqwsqrh achywtqdly grqsryidav hgfvataral llgrhllpea
      241 dwlqwqacie ttvahtavrd dgratwpcqi deppgtpqkw lmqychgapg fvicladlpg
      301 haldalltaa geatwaagpl akgsnlchgt agngyaflvl lartreprwr erarafamha
      361 iaqfedetar vgrlrhslwt gdvglaiflw dclreraqfp tldvffaapv tgmsaasaka
//
LOCUS       WP_284618747             639 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Aquabacterium humicola].
ACCESSION   WP_284618747
VERSION     WP_284618747.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..639
                     /product="PhoX family protein"
                     /calculated_mol_wt=69190
     Region          23..633
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 makdfdtmed snrssnpsih evsdpsrrrv lhgglavlss allanlsgca tarsegavae
       61 aagprlgfks vsasledair vpegythqvl vpwgdpvgva gampafkpda gnsgaeqelq
      121 mgmhhdgvhy ypldgarrgl lvmnheyvdy gllypdgdkt whadkvrkaq aahgvsvsei
      181 aqradgswqa vrpsrharri taatpmavqg paaghpmmkt aadpqgrrvl gtlnncasgk
      241 tpwgtyltge enwayyfald adpvdahhrr wglrkgrgar whehderfda akhpnepnrf
      301 gwiveidpfd ptstpvkrta lgraahegat valtkdgrav vysgedarfe ylyrfvsker
      361 mkpggaaana glldegvlyv arfdadgrgr wlplqhgqgp ltaangfadq gevvikarqa
      421 sdalgatkld rpewvaldqq trevycsltn ntnrggdryp gvdaanprah ntmghilrwk
      481 eagdfdgetf ewshfvlagd paneraeakg nvrgdifgcp dglwvdqrgl lwictdmsss
      541 vrgqgefarl gnnmllaadp rsgeirrflt gpagceitgs tmtpdgrtlf invqhpgetp
      601 seqsdpanpm rfsrwpdgsg rprsatvair kldggvigt
//
LOCUS       WP_284618667             328 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Aquabacterium humicola].
ACCESSION   WP_284618667
VERSION     WP_284618667.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..328
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=34560
     Region          72..321
                     /region_name="2-desacetyl-2-
                     hydroxyethyl_bacteriochlorophyllide_"
                     /note="2-desacetyl-2-hydroxyethyl bacteriochlorophyllide
                     and other MDR family members; cd08255"
                     /db_xref="CDD:176217"
     Site            order(72,131,135,155..160,179..180,184,211..212,214,
                     234..235,261..263)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176217"
ORIGIN      
        1 mkapaparac wlaepgrael rdeplatpgd gdvlvralhs gisrgtetlv frgevpaseh
       61 rrmrapfqqg efpgpvkygy asvgvveagp aallgrvvfc lhphqtryvv padavhplpn
      121 gvpparavla anletavnal wdaaprigdr iavvgggtlg alvawlaarm pgcavqlvdv
      181 qparralaer lglgfalpde awgdadlvvh asgrgeglat alrlagfeat vlelswygtr
      241 pvavplgeaf harrlrlqss qvghvaaaqr grwdfrrrla lalslltdpa ldallgepap
      301 fdalpavlar laagdepdvl cqridypp
//
LOCUS       WP_284618779             338 aa            linear   BCT 25-DEC-2024
DEFINITION  GGDEF domain-containing protein [Aquabacterium humicola].
ACCESSION   WP_284618779
VERSION     WP_284618779.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 338)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 338)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..338
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36650
     Region          43..332
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mnalselaag pdqppsgval dgalarlles haalqgwfvs vkdaadgryl qvnaalaeff
       61 grpadqvvgr sdaellepal atlvrsadqt alasatgtla gehrfdwrge rrdwsvlrlv
      121 vpsgerrllc alwqdqspqr qreaqlkaai eqleqqqkan valrrelgdh glrdqatgls
      181 tsahfddqmr reldlssreh refalvymel dppsdkvraf gdralerihe amgrllrgnt
      241 ramdascrid errfavllsg vglatahsrm eglrrqcatq ivaldgqelg ftvsvgvasy
      301 phtaqaqegv vaaceaalaq arqrggnava lasirfgd
//
LOCUS       WP_284618785             327 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Aquabacterium humicola].
ACCESSION   WP_284618785
VERSION     WP_284618785.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..327
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32305
     Region          29..311
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtplrtalll ggltvlllla glaagsdgwa lpdaaqselv lwqiraprtv gawlvgallg
       61 lggalaqglf rnplaepfll gaapgatlav vlvlaasafa gsvlspvtag qlarvglvga
      121 afggalvgvt ltltlargav qpttlllagi vvgfllgals dlvtlaapea lrgkqafllg
      181 stgylgwpac vllagglvlt laaawpaara ldaltlgdet aaslgigvgr mrlmlvatma
      241 latavavaqa gmvgfvglaa phlarrsvaa rhallvpasa alggllllaa dlaartlvap
      301 qelpvgvlta vlgggylmll lrqrrra
//
LOCUS       WP_284618872             217 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-L-isoaspartate O-methyltransferase family protein
            [Aquabacterium humicola].
ACCESSION   WP_284618872
VERSION     WP_284618872.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Edwin,R.K., Challa,N., Sharma,R., Satyamoorthy,K., Parsa,K. and
            Misra,P.
  TITLE     PIMT/TGS1: An evolving metabolic molecular switch with conserved
            methyl transferase activity
  JOURNAL   Drug Discov Today 27 (8), 2386-2393 (2022)
   PUBMED   35462043
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Furuchi,T., Sakurako,K., Katane,M., Sekine,M. and Homma,H.
  TITLE     The role of protein L-isoaspartyl/D-aspartyl O-methyltransferase
            (PIMT) in intracellular signal transduction
  JOURNAL   Chem Biodivers 7 (6), 1337-1348 (2010)
   PUBMED   20564550
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Kagan,R.M., McFadden,H.J., McFadden,P.N., O'Connor,C. and Clarke,S.
  TITLE     Molecular phylogenetics of a protein repair methyltransferase
  JOURNAL   Comp Biochem Physiol B Biochem Mol Biol 117 (3), 379-385 (1997)
   PUBMED   9253175
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..217
                     /product="protein-L-isoaspartate O-methyltransferase
                     family protein"
                     /EC_number="2.1.1.77"
                     /GO_function="GO:0004719 - protein-L-isoaspartate
                     (D-aspartate) O-methyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0030091 - protein repair [Evidence IEA]"
                     /GO_process="GO:0036211 - protein modification process
                     [Evidence IEA]"
                     /calculated_mol_wt=23586
     Region          12..209
                     /region_name="Pcm"
                     /note="Protein-L-isoaspartate O-methyltransferase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2518"
                     /db_xref="CDD:442008"
ORIGIN      
        1 mnveqarfnm ieqqirpwdv ldasvlqlla tlkreefvpa ayralafvda evplpegqcm
       61 lapkiearll qeahvqrher vlevgagsgf maallghraq svvsleirpa lvqlaqdnlr
      121 raaisnvsvr qadgaqglaa eapfdvivls gsvallpqvl ldqlriggrl iaivgsepvm
      181 qavrvtrvsd atfqtvelfd tvaqrlqgfd aptrftf
//
LOCUS       WP_284618844             759 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Aquabacterium humicola].
ACCESSION   WP_284618844
VERSION     WP_284618844.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 759)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 759)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 759)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 759)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..759
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=82637
     Region          48..758
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mktravatae adaapivrls daeldagfga agpaddhgaa allrarafse plltgqrldt
       61 gedalghadg vaailqaiga apsmraaayl vyagdflqrp eemvakafge syaslvahtr
      121 klvqiqraar eaqveaeqra lqtervrkml lafsrdlrvv llrlasrlqt lrwyastkqt
      181 cpkplaeetq qvfaplasrl giwqikwele dlafrvlrpd dyrqlarqla esrierersv
      241 egvrrqmlqe laavgiaaev qgrpkhlysi wkkmqgkqla lgqvfdvral rvivadvhac
      301 yaalsrvher yravageydd yiarpkpngy qslhtvvlgd dgrpvevqir tqamhehaeh
      361 gvaahwayke agtkgyagvs aagdfeerva earkavlrql lawerdfvdq aaggagpsgg
      421 agpsgpsfed riyvftpqat vielpagatp idfaysvhtd lghrcrgarv dgamlplntp
      481 langqtvevi aakeggpsld wlnselgylk shrsrakvra wfnaqalsgt vargrelvek
      541 llqregrtal klddlaaqlg fkgadalfev vgkdeyslrh ienllkpaep papqeeiipl
      601 krargteggv lvvgvesllt qlarccrpap pdaiagyvtr gkgvaihran csnfrhmaeq
      661 qpdrvipvtw getpagreaa ypvdvvveaa drpgllrdis evftkdklnv igvhtqtvkd
      721 vtggtafmtf taevadahrl asvlrvvaqi pgvrrarrr
//
LOCUS       WP_284618927             348 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Aquabacterium humicola].
ACCESSION   WP_284618927
VERSION     WP_284618927.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..348
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38133
     Region          43..327
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mqrrpllafa glcaiapttr aataapwife ldapdaravf lagdmtawda gkralqread
       61 grwrlriale pgqwvykfvv dgrwiadpan pqrdsdglgg qhsfiwvgdg dwqvpagapr
      121 grvetlrlps rawrgerlvh vylppglaqp ptqptpllll lhgagmdadq wlrtgqvdrf
      181 mdsllargrl arpfgivmps sdavpydgrs erhlmqellp qvqkrygfaq srekvavagm
      241 smggrgaval ahrhprhfgl ayglagwypp ellaalplrp vppieldlvc gtgdelitgn
      301 ralaarlkaa grtfvydeip gahdwhtfsg qsarllmrvg effarggr
//
LOCUS       WP_284618951            1045 aa            linear   BCT 25-DEC-2024
DEFINITION  CHAT domain-containing tetratricopeptide repeat protein
            [Aquabacterium humicola].
ACCESSION   WP_284618951
VERSION     WP_284618951.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Classification of the caspase-hemoglobinase fold: detection of new
            families and implications for the origin of the eukaryotic separins
  JOURNAL   Proteins 46 (4), 355-367 (2002)
   PUBMED   11835511
REFERENCE   4  (residues 1 to 1045)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19591600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..1045
                     /product="CHAT domain-containing tetratricopeptide repeat
                     protein"
                     /GO_function="GO:0004197 - cysteine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=111146
     Region          123..>344
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          328..1035
                     /region_name="COG4995"
                     /note="Uncharacterized conserved protein, contains CHAT
                     domain [Function unknown]"
                     /db_xref="CDD:444019"
     Region          731..1039
                     /region_name="CHAT"
                     /note="CHAT domain; pfam12770"
                     /db_xref="CDD:432771"
ORIGIN      
        1 mnlrraaall latfaglaaa qppcdgvapp dpaalaaead alrrnqppla laracarhra
       61 aastatgiel aqalaanery daaaallgal aasaapgslt asevalaqgt lesdqgayar
      121 aaphferala qlraldqhgr lpalaavgls qalrtlreap daldraaall deaerelkda
      181 glarsrdmgd llnqrtmhay arqdlpaaig hasaevalir eldgadapda fdalaslgam
      241 lsqlnrgdea etalnegrrl malhpavspa aqlgvlnnls alqqdrgrya dalavaeeav
      301 afaqqrfpkh pamhlvamnn ratclmhlsr laeaelrfee arallranpg lpalrrlrll
      361 dnlaelytrl ndadaaqgvi deglgvagrd asfgywhgrl lrlqatlasa rgrwaevdal
      421 harsapliaa vvgeqhafve vstvhrciaq vrgrlageac dtlrrrastl dtavplhrfr
      481 vhhalalqad aagrageare hhlralaaaq sagtahplwi aydalaehlr rsgaralaih
      541 fgktaveqie amrrdfsrta rdserqfvad khavyrrlad wlaedgride aldvlrllka
      601 eefldfvrga gdapapggpa ltpreagwra aspaaagdsa aaeaerlqsw qallgsepan
      661 grapraatap vatrapagtl vawlfagdth lnlvldgprg rtlqrrpqdp aalardvgrl
      721 laqigrredv lplaqslhar vaapiaqaad varvqrlvlh ldgalrylpf aalhdgrryl
      781 geryaieqri aaadrtagda panggadapl aepppreayv rafgvsrala glpalqavpr
      841 elcsivdgev igldaadgpc ergllpgagw lneaftterl ravadggtaa relaparrel
      901 lhlgthfvlr pghigrswll tgdaqklsle rfaafdwrgq alitlsacet glggaqgadg
      961 revdglaall arrgagavia slwrvedest galmtalyra lrsdadpara lqqaqvqvrr
     1021 radrawrhpf fwaafmvsrp erlqp
//
LOCUS       WP_284619171             411 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Aquabacterium
            humicola].
ACCESSION   WP_284619171
VERSION     WP_284619171.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..411
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44334
     Region          90..389
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mklkkvlvgl laivavaata gwfslhkdar avvatmptnr dllfwsqpqr daafraldrl
       61 pllakvrdip agstplplpp gpplklpldv daymagqrsa allvlhdgrl rleryglgfd
      121 asgrwtsfsv aksmtstlvg aalrdghirs mddkvsdyip amkgsaydav sirqlltmts
      181 gvqwnedyad pksdvalfnk hepepgvdal vsylrrlpra appgerwlys tgetnlvgil
      241 vsqatkrpla dylsekvwkp agmeqqatwi lnktgqeisg ccvqaaardf vrygqfilng
      301 arvngqaivp dgwlaeatse rtgigqpgrg ygyqwwtyad gtfaargifg qglfidpkrk
      361 lviasnanwa ggardrtasa aredfyravq ravdeetggg vatgaaasaa k
//
LOCUS       WP_284619268             401 aa            linear   BCT 25-DEC-2024
DEFINITION  maltoporin [Aquabacterium humicola].
ACCESSION   WP_284619268
VERSION     WP_284619268.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..401
                     /product="maltoporin"
                     /calculated_mol_wt=42715
     Region          35..400
                     /region_name="LamB"
                     /note="Maltoporin (phage lambda and maltose receptor)
                     [Carbohydrate transport and metabolism]; COG4580"
                     /db_xref="CDD:443637"
ORIGIN      
        1 mhapipspsa tprrarlasa aalallaaag saqavdytgy fragpgltse dtsracygln
       61 ggsagmkyrl gnecdfygef qlsqgfqkdg idyratlmvn qytpqtqnag dkglnieqmw
      121 aeargfdiap natfwigker grrgdvhivd tffiemlgvg agfknqpvga gklgvafykt
      181 dsdyprpgnr vnveylglpv npdgtlnfff hatkgdfkgg ksgagftvrh dqaklfgtgl
      241 snslwlqfaq gsaglngnwg dltagskaks wrivetfngq sgalggqaml llasekngag
      301 lktdsasvgg rvsyaltknf kllaeaglsq ykpeggqtar ltkftfaptl svgpdfwtrp
      361 efrlyvttak wnkaagnvtg qaafngetsg tsygaqveww f
//
LOCUS       WP_284619173             497 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Aquabacterium humicola].
ACCESSION   WP_284619173
VERSION     WP_284619173.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..497
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53601
     Region          1..497
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mtepalrplf hfdnsyardl pglavpwqpr rvdapsllwf nralaeelql daealagerg
       61 aaifggnevp egatpiaqay aghqfggfsp slgdgralll gevldrhgrr rdiafkgsgp
      121 tpfsrggdgr aavgpvlrev iigealqalg ipttralaav atgepvfreg tlpgavltrv
      181 aashlrvgtf qffaargdid klrlladhai arhdpqlagd pdrymgllra vaerqaalia
      241 rwmhvgfihg vmntdnmtis gesidfgpca fmeahdpdav fssidthgry ayanqpliar
      301 wnlarlaeal lplvdaddpq ravagatdvi dsfpalydrh wltgaraklg largddgdqa
      361 laddwlallq sqavdhtlaw ryladaadgd gpklqalfed arplhewlar wraraqaess
      421 mpaqraaamr rasplyiarn hhvedalraa sadgnlqplh allavlaqpf derpgleaya
      481 mpappevtah yrtfcgt
//
LOCUS       WP_284619319             494 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Aquabacterium humicola].
ACCESSION   WP_284619319
VERSION     WP_284619319.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 494)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..494
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=52127
     Region          11..482
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mtteaaetgr lqpllerlga gldayltfeh pdalhggarw rarldaplpq qgigadavvd
       61 ellhevvpfg saiprpgfsg fittgattva tlaataasva spqrygltsf nflealslrw
      121 ladafglgam qgvyssggst anllalgaar qqaferlgcd paadglqlhr pvavyastet
      181 hhtvqraagv lglgrravra iacdaggrmr vdalraaiea drragvlpma vvanagttnt
      241 gaidplssig elakaqglwf hvdgayglpg lldervatlf kglaladsvi vdphkwlgaa
      301 vgigatfvhd rgllqraftq epahylegsv epaatepgtq hsmddfgtpy fdygvelsap
      361 argvvvwall reigiaglre rvrrhndmat avaqmarahp nlellleptl siccfryvap
      421 gvddldalnq rlhrrlmren rnmpsttrig grlalrpcfv gartgmaqar elvadvlrig
      481 dalvregala aaaa
//
LOCUS       WP_284619322             975 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Aquabacterium humicola].
ACCESSION   WP_284619322
VERSION     WP_284619322.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 975)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..975
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..975
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=105379
     Region          80..974
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          690..718
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          730..758
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(731,734..735,738..739,741,771,774..775,778..779,
                     781..782,811,814..815,818..819,822)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          769..799
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          810..838
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mlalpferrt qlavllalrr qwvprtevaa llwpelsdkq ayanlrktlf rlpslpwaqa
       61 vavepaalrf dvptdvgefe aalndgrtad alaayggdll dgfddgqsdg wtrwlgferd
      121 rlraawrhaa latldggtld tsaalalstr llesdpldea alqhrlaala asgqagaara
      181 ayrqfverlq aelgiepgaa lralhdglga gaaapprppa vmappladdg fvgrsgelar
      241 iaellsrdec rllclvgpgg vgktrlarra mqllgpqqdd galfialddv etaaqlglrl
      301 aqeagvatgp ragqaldrai eawrerqlll vldnfeqlsg etatlsrllr dcprlkllvt
      361 trvrlqlade wslpleglpc pdpedrdrve afdavrlfvk aaqrvepgfs aaadaaaivd
      421 icrqvdglpl alelaaawvr mlscaeiaqe lhqgtellra adarlperha sletvfeqsw
      481 qrlsaserev larlsvfhgg fsvetarava gaslpvlgal adkslltkdr qrmrlhplvq
      541 qlaalklqal dassathdrh arhfhgwllq lepaaargrr ealkaidddf enarrawlhs
      601 iarqdaaall rvlpawrhyf ehrarfedgl alwraaadse laaadallra rvlaqaalme
      661 mrlaryadaq vtagtaidaa eapadrdary qalavqagca hyagrsadar eiylraldla
      721 rarenvsdia stldnlalce krlghydeal gltlealaeh rrhgddarla vclnnlgsly
      781 tfldedaaar ehlleaqalc erhglvstra falanlgdla lkagdiddar sfgeqglega
      841 daaglrslva wfkvhlarva vrqaalddar twladaaala lslgaqaikp lvlnalaell
      901 daqgqpraar rvlgfaaaep tlsapdrdel maaftrhrpp dtpdppwpgw sltelmqriv
      961 aeaplahapl iaals
//
LOCUS       WP_284619334             329 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Aquabacterium humicola].
ACCESSION   WP_284619334
VERSION     WP_284619334.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..329
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34820
     Region          29..327
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mneltwrrra llqaaaagaa gafaptlraq aawptkpirf vvpfapggss eivarssaae
       61 lakllgqsvy vdnkpgaagn vamqevarad dqhtlilghi gtlavnpyif dklpydpnkd
      121 fkpvsllakv pslylvhpdl paknlkefva lvkskpgrln ygsagngsag hlameylkma
      181 gelfmvhvpy rgtgpqltdl lagrldaasv gapavlqfik tgklrciatg tpqripqlpd
      241 vptvaeqgfp gfemtqwygm lapsslpqpa idklaaacak amkeptaler lnadaaiavg
      301 gtpaefakfi gveqqrwkav iarakikpd
//
LOCUS       WP_284619374             326 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Aquabacterium humicola].
ACCESSION   WP_284619374
VERSION     WP_284619374.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..326
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33673
     Region          6..323
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 msldpslsrr ralqglaaag agawlpmaga qdkvvkfilp natgsgvdai traaqpalak
       61 algmqvivdn qpgaggivgl qalarsapdg mtlsvvsnnv vifpsvyktl pfnmpadftp
      121 iaicgftpvv lvvnpkvaas nakeftallk akpgelnfgs ggngtilhla semyldavga
      181 karhipykgv gpmvtdligg qiefatvalp svqqhlktga lkaigvatsq ripaapeipt
      241 fveqgvpsyv veawfavigp kglpaaevkr vhdavvsafa qpevkdamak qgnvinvsat
      301 dyaqnffrse ltkyaalvkk agvelq
//
LOCUS       WP_284619411             226 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Aquabacterium humicola].
ACCESSION   WP_284619411
VERSION     WP_284619411.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..226
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=25122
     Region          <53..>111
                     /region_name="PRK11447"
                     /note="cellulose synthase subunit BcsC; Provisional"
                     /db_xref="CDD:183140"
     Region          119..220
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
ORIGIN      
        1 mrnkplemrr tsrqsvplwr klpsllrrrg apeaaeapat vaapeafwdr lnallddcry
       61 geaiaalkda lrssphdpel ndqlhalyte vgdtvsvlah gpqwvaaqal dgrgraalaa
      121 lktlqkidar felqdadall plakaavqhg eqalavqllq gfdkrfpehp dlpgvyflga
      181 qlmseygrrh eqatkllkrl lkrysghala gemrtylell qrvqvr
//
LOCUS       WP_284619413             274 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Aquabacterium
            humicola].
ACCESSION   WP_284619413
VERSION     WP_284619413.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..274
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29807
     Region          32..258
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mpydrdtlfa tpliswqqvr llapqpqwsd gyrpagarll llqqdrlece ltpevsghga
       61 ggrrflcdgt salwltpsrp yrmrqpgagv rghllclhgd epshagrrav slqqhlalrr
      121 wqralhdgli eplaleeall allqdvlaqr vddagaapra vertrellaa dpargdtlae
      181 iaravhaspy hlarqfrrht gstvhghrtr lritlalqrl aqgasdltql aldlgfashs
      241 hfsaafrrat gttpsalrti staragagaa dsar
//
LOCUS       WP_284619428             237 aa            linear   BCT 25-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Aquabacterium
            humicola].
ACCESSION   WP_284619428
VERSION     WP_284619428.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     BTLCP proteins: a novel family of bacterial transglutaminase-like
            cysteine proteinases
  JOURNAL   Trends Biochem Sci 29 (8), 392-395 (2004)
   PUBMED   15288868
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..237
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=26460
     Region          <11..137
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mnapaatvla ptplldfhhp aiealvaarg wrslpvaeri gavyefvrne ipfgyndgde
       61 lpasrvladr lgqcntkgtl lmallravgi gcrfhgftih kalqkgavtg lfyrlappri
      121 ihswvevwlh erwielegfi ldeaylrslq rrfpqamafc gygaatrdls spgvawcgrs
      181 tyiqkegiad dfgvfdspda fyarhgsnls gfkrllyrhv vrhamnrnva riragrw
//
LOCUS       WP_284619445             750 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein [Aquabacterium
            humicola].
ACCESSION   WP_284619445
VERSION     WP_284619445.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 750)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 750)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 750)
  AUTHORS   Porat,A., Cho,S.H. and Beckwith,J.
  TITLE     The unusual transmembrane electron transporter DsbD and its
            homologues: a bacterial family of disulfide reductases
  JOURNAL   Res Microbiol 155 (8), 617-622 (2004)
   PUBMED   15380548
REFERENCE   4  (residues 1 to 750)
  AUTHORS   Kimball,R.A., Martin,L. and Saier,M.H. Jr.
  TITLE     Reversing transmembrane electron flow: the DsbD and DsbB protein
            families
  JOURNAL   J Mol Microbiol Biotechnol 5 (3), 133-149 (2003)
   PUBMED   12766342
REFERENCE   5  (residues 1 to 750)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   6  (residues 1 to 750)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   7  (residues 1 to 750)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   8  (residues 1 to 750)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   9  (residues 1 to 750)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12109673
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..750
                     /product="protein-disulfide reductase DsbD family protein"
                     /EC_number="1.8.-.-"
                     /EC_number="1.8.1.8"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=78054
     Region          52..161
                     /region_name="DsbC"
                     /note="Disulphide bond corrector protein DsbC; pfam11412"
                     /db_xref="CDD:463273"
     Region          339..723
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 mqidllwrra aallgaagva vvcapalaap gavvrtdqvr aelvahapeg vapgkplqlg
       61 lliehqphwh tywrnpgdsg lpttlawqlp aglvageiqw prphrlpvgp lvnygfegrl
      121 llpvpvqvtq apaganltid lradwlvcke vcipesgefr lqlpvqaata vhgalfeaah
      181 kaqpkmlaat gsqaridgat laldigglpa awrgqpvdyf agdagvieha arieqrwqge
      241 rlllrvplsa qrsaspavld avlarpgsdd avqlglkvag awpapgaatp aaeatapasp
      301 avppadtarv pspataseag gtslglawll afagglllnl mpcvfpvlsl kvlgftrdag
      361 hrgqllaggl aysagviasf vvlaalllml raagaglgwg fqlqspgfvt glavlftmlg
      421 lnlsglfefg kfapnsactm harkpladha ltgvlatlia spctapfmga algvaltqpt
      481 gialalfatl gagmatpyll ltavprltaw lprpgpwmah frsamafpmy gtvvwllwvl
      541 gqqvgvdgaa allavlvlla fvawvfkasr ggarrwawrg gaaallllvs swaapwllra
      601 daslqasavp asasasawqp wsaealrear dagrpvfvdf taawcvtcqf nkrvvlaqre
      661 vmadferrnv llmradwtrr daritaalse lgrsgvpvya lygpgeatpr llsemlsvae
      721 vrdaiaawpa apagplapka tgtpvasaap
//
LOCUS       WP_284619474             574 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Aquabacterium humicola].
ACCESSION   WP_284619474
VERSION     WP_284619474.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 574)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 574)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..574
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=62831
     Region          5..573
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mprgdaalrq tlaqqqaile glqvgvgffv drqpvwvnpq wealfqrsgd evrrlgtavy
       61 fqapedwsaf ggraypalar gevvteelql rradgtlfwc rvrgsavdra dplrgvvwif
      121 edvtdrrlaa damqryqahl ehlahtdplt glpnrqylha tldldaaaaa agghalallf
      181 idldrfkivn dtlghalgdq llcavaqrlr gcldaggsgg hciarlggde ftvlcrlegr
      241 aavetvarrl iaalaepfvv dgyeltvtas igicrcphdg aqpaellmra dtamyraker
      301 grnnfqfyep gmgrqaervh llerelrhal krhqlelhyq pkvelasgra ssvealirwq
      361 hptlgavspa efipiaeevg aivpigewal reacsqlarw ralgcdcsva vnlssrqfrq
      421 pdlagaimrt ideagvpcel veleitegvl medtdgtiaa lkllagrgir iavddfgmgy
      481 sslsylrrfp vhvlkidrcf vadigrpggd atiartiiam ahalnlqvva egvetaaqad
      541 flrqhgceta qghffgmplp arettalllr qarr
//
LOCUS       WP_284619634             651 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Aquabacterium humicola].
ACCESSION   WP_284619634
VERSION     WP_284619634.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 651)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 651)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..651
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=71089
     Region          9..642
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mlkipspsrr vwprfimlva avaaavvllm lllrqastql lqrdaehval awaelasasi
       61 edlegifrge pptpaahrdl lrhrkvqevf rfklfdrdgr vvlvsddldr papvvkdnti
      121 ghgnakvrdl vlngkhviel kqgqdasrpa lyseayvpvm rggrvigvve vyvdqaeraq
      181 riqaafglva agvfallgal ttvfcgwwyr rlkaeraaee rarylsrhdv lsgllnrssf
      241 nealdeaawr hagggpgfsv lcvdldhfke vndtqghaag ddmlrqvgdr lralvrqgdr
      301 varlasdefa lllsgatape svtmlaervi aalaepfqid rhsvssgcsi gaavfgvdas
      361 tpdevlhkad lalqrakqag rgafhfydat ldrrlddrrq lvrdlreaig spqmalhyqa
      421 lyaadgrtvt gyeallrwrh pvrgpiapvd fiplaedsgl iaplgrwvle tacaaaagwp
      481 apltvavnls aaqfsqgdlv dvvraaleas gleaarleve iteslllght eevtgtlral
      541 dalgvkiamd dfgtgyssls ylwrfpfhkv kidrsftlhl addpkvrliv rsivslarsl
      601 glrvnaegve neaqlkllqe qgcdelqgfl larplpleal thpetadver g
//
LOCUS       WP_284619658             690 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Aquabacterium humicola].
ACCESSION   WP_284619658
VERSION     WP_284619658.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 690)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 690)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..690
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=76490
     Region          3..678
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mnllsawaqt idalgdaawl vdgasahvla anaaavellg lplerllgcn aahliatped
       61 lafwdevrag hdqwlqsdtv lvhasgrlvk vsrrvrlldp aqrcflvtvq drteaqrrcd
      121 ereslvaelr atlestgdgi lvtdlagrit afnrrfaqlw gvpeelltqr ndeavydwmr
      181 rsvrepeayq rrlaviqeat lmqaheriel lsgrvlervt qpqschgrpn grvwafrdrt
      241 eletasqrin tlsttdgltg lfnrrqlget laesmrqahr asgtlallil dldrfkqind
      301 slgheigdrv lldtaerlks clrqgdfvar iggdqfalvv qrvdhrgaea aaqrvleais
      361 rpcsvdglqf tmtcsvgval fptdgedgde lvrhaetamq rakqggragf rfhqphhdad
      421 lrqrmrldha mrqalasnrf rlkyqpqldl rsgavigaea lirwrdpelg evspgefipv
      481 aedtgfivai gdwvlqqavr qaarwrnegl vmpvsvnvsa lqfqqadfid rvaavlsdne
      541 lpgsllelel tesilvhdad ealarlsqls qlgvrlaidd fgtgysslsy lkrfpierlk
      601 idrsfiegip qndsdagivr aivqmsaalg mkviaegvet epqrnflvev gcdqfqgfly
      661 apaldalsfd ervrgrprgg akpqlslvar
//
LOCUS       WP_284619679             108 aa            linear   BCT 25-DEC-2024
DEFINITION  (2Fe-2S) ferredoxin domain-containing protein [Aquabacterium
            humicola].
ACCESSION   WP_284619679
VERSION     WP_284619679.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790154
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..108
                     /product="(2Fe-2S) ferredoxin domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=11838
     Region          1..105
                     /region_name="COG3411"
                     /note="2Fe-2S ferredoxin [Energy production and
                     conversion]"
                     /db_xref="CDD:442637"
ORIGIN      
        1 msyyqhhvff clnkrdngea ccadhdaqsa fdhckkrvka eglagpggvr inkagcldrc
       61 aggpvavvyp eavwytyvdq hdideivesh lkkgqvverl vlppnvgr
//
LOCUS       WP_284619717             353 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein [Aquabacterium humicola].
ACCESSION   WP_284619717
VERSION     WP_284619717.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..353
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39630
     Region          6..353
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 msnglipati ltgflgsgkt tllkrvltea hgqkiavien efgeenidnd ilvmdsneqv
       61 iqmsngcvcc tiredlrstl sdlaekrrkg eldfervvie ttgladpgpv aqtffmddei
      121 aesylldsvl tlvdakhadq qldtrqearr qigfadqifi sktdlvdeda vhalthrikh
      181 mnprapqqkv hfgevplsqv fdlrgfnlna kleidpeflt aaddhdhdhh ghdhdhdhdh
      241 ehgehcdhph hhahdddvks mvfrsdrafn aakledflgs ivqvygpkll rykgvlwmkg
      301 adrkvifqgv hqlmgsdlgp kwlpsekkqs kmvfigidlp rdilqqgleg clv
//
LOCUS       WP_284619756             270 aa            linear   BCT 25-DEC-2024
DEFINITION  triose-phosphate isomerase [Aquabacterium humicola].
ACCESSION   WP_284619756
VERSION     WP_284619756.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10085182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..270
                     /product="triose-phosphate isomerase"
                     /EC_number="5.3.1.1"
                     /GO_function="GO:0004807 - triose-phosphate isomerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0031625 - ubiquitin protein ligase
                     binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27921
     Region          3..245
                     /region_name="TIM"
                     /note="Triosephosphate isomerase (TIM) is a glycolytic
                     enzyme that catalyzes the interconversion of
                     dihydroxyacetone phosphate and
                     D-glyceraldehyde-3-phosphate. The reaction is very
                     efficient and requires neither cofactors nor metal ions.
                     TIM, usually...; cd00311"
                     /db_xref="CDD:238190"
     Site            order(8,10,91,162,171,210,229,231..232)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238190"
     Site            order(8,11,40..42,44,47,60,78,81..82,93..94)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238190"
     Site            order(10,91,162)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238190"
ORIGIN      
        1 marlvignwk mngtpallra faaaalrepp rceaalcvph pllaaartaf gttalrwgaq
       61 dcsaeldgaf tgevsarlla dldtryvilg hperrlghge tdgqiaakaq ralavgltpv
      121 vcigetaeer dgeqtsavlr rqllqlarll grrlaavvla yappwaasrh gcgdcvapgl
      181 ledtfaaiae llafhaglsa asvrviyggs vdarnagall slpgiggvlv gaaslrpadf
      241 ieickaaarc gdppvraasl wpviatsare
//
LOCUS       WP_284619777             271 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Aquabacterium humicola].
ACCESSION   WP_284619777
VERSION     WP_284619777.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..271
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=28554
     Region          38..261
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mrslplddrr sggafsvlhr plpseaaepe sarapsvdil slvahelrng llplrlaaaq
       61 idaarvdakr ltrlrftieq qvdhlsglig dlldvsrarn gklrlacrpl dvatilarcv
      121 adcrprmaah aqhlevrvpa gplplsgdpe rlvqvfdnll dnackytppg grivlcaalm
      181 pdgvevsvcd dgigiaaeal grvfepfvqv dtavgfngag lgiglsvvre lvqahggqvi
      241 arsagpglgs cftitlpfag pprtvaqees r
//
LOCUS       WP_284619845             330 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Aquabacterium humicola].
ACCESSION   WP_284619845
VERSION     WP_284619845.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..330
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34541
     Region          26..328
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mtarssarrh llcaaaaasl aalpmgsala qawpvkpvti vvpfpagggt dafarplfam
       61 msknagkqfi idnkggaggt vgaslasraa pdgytffmga vhhaiapsmy pkldyqletd
      121 fvpvgliasv pqvivvhpqr lpvndlkgll ehlrknpgkv nygsagngts hhlagelfkl
      181 qtktfvthip yrgagpalqd liagqvdmmf dglgssashi kggrikaiav asdkrapgfp
      241 dlptaaeggv ptyqvatwyg lwapkntpke avdamiaemk kalnsdelka twaglganpp
      301 nswgpdfgkf vssevkrwhe vvkssgakld
//
LOCUS       WP_284619854             530 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Aquabacterium humicola].
ACCESSION   WP_284619854
VERSION     WP_284619854.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..530
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57558
     Region          4..>113
                     /region_name="PLN02487"
                     /note="zeta-carotene desaturase"
                     /db_xref="CDD:215268"
     Region          66..530
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 msrsaafrfl arcaataawc drtgqpeaea vaqrreasrq rrrllqgaag gaalmtlgap
       61 faraqsapad vaivgagfag lyaatvlask gigaqlyeag trsggrvwsl rnhfpgqvve
      121 rgaelidtth stvrglanaf gltleshekq pgeeffffmg rqwseaevva eyrafsaamn
      181 ddlkrlsggp tadshnayda eldrlplsdy ldsrgagpll rrvmdtayti efgreihrqs
      241 slallffaqa nkrshftpfg nfsderfhiv egndaiatgl eralpravay ghqllrvgrl
      301 adgrlklafa qgnktvervh aaailalpap mmrlvefeag vglaahsrsa iagldygtns
      361 kmmigfrarp wlerqhcngg sysdlpnhqn twetspetal vgqrgvitdy sggergarld
      421 parlqteata flgdleriwp gcgafvrrda qgraiahlen wsrnplfrga ytnnqpgyft
      481 tlegqcakpg apglwfageh tdsfysyqgf megallsgar aadqvwralr
//
LOCUS       WP_284619898             333 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Aquabacterium
            humicola].
ACCESSION   WP_284619898
VERSION     WP_284619898.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..333
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35393
     Region          20..319
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtpparllrl lallqaqpnw tgpalaqrld itertlrrdi dklrglgyav eassgvaggy
       61 rlapgtklpp laieedeala ivlglaslgg gtlasvadag qralakidqv lpaplrqrla
      121 rvrralvvrg phaaaagaqv gaeriaalad acaerrtlqv ryadhaqhas erriepqqlv
      181 fgdgrwylva wdlgrddwrt frvdrlevla tgavfaarrp paedmgryva qgvasaahrf
      241 aavvrfdaaa eqlapslewv pavvealpgg gtrvhvgsqs ldalavwlac tglaftvesp
      301 palvkhlatl ssrlaeaaar ssrlrtasvr kar
//
LOCUS       WP_284619939             276 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Aquabacterium humicola].
ACCESSION   WP_284619939
VERSION     WP_284619939.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..276
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30837
     Region          52..153
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 malnrrrkpa gppppgvdll qppgalllml earapwewaa miaaapwlrq lprgdghpvl
       61 vfpglgatdi ttaplrtfle drgyvpypwk qgfnfgprng vlealreqlr hvaerhqcrv
      121 sllgwslggv yarelakefp erarcvitlg spfaghprat nawrfyemvs gqsvehndel
      181 isqlrvppsv pttsiysktd gvvawqcsin pdephtenie vhashigmgm nplalyaiad
      241 rlaqdparwe rfdlrgarrw fyktthqspm qaasrf
//
LOCUS       WP_284620014            1108 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Aquabacterium humicola].
ACCESSION   WP_284620014
VERSION     WP_284620014.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1108
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..1108
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=117550
     Region          3..1108
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mndrasaaaq vavrldllgp prlvpaglpa ielnrldaal lallvfeggv drtraaallw
       61 pdadarragl slrqrifrln rgagtevvtg arrlvlaaai ahdlgllita agtddagppr
      121 gellggldyt dsgeladwva aarerwrgar realsgqaer leaagrlala lqyaerlleh
      181 ephsehahrr lmrlhylrgd rtaalvayea crralqqqmg eppgaetral aerivgsglp
      241 gpaspaappl allrpprlvg rdatwrrldd aaalgrpall sgepgigktr llvdrlqaag
      301 pgllvdarpg drrvphavlv rllqaladhq gpppdegvrg elaalqpggv grsasapspa
      361 rlqaalarel vraaagglrl fglddlhyad dasleillpl tldvsgprwl lavrsaerpa
      421 llqrwqdesd pgsgpivlal eplsaeavhe llcslalpgl etdawaqalq artgghpmll
      481 letlraawsa daalpprpgp lpqphslarl ieqrlqplep garrllqlaa ladvdfsvpl
      541 aahvlqvhal dlaapwrele aagllsgdgf ahdlvreaal rsvpeaiarp lhgqiaayia
      601 atdaparvae hlrragrpad aaaqwrraaa galaagrrre eaellqaaaq dfraagldea
      661 afaaecdrig alvqcaggde lraalqalqa rpvdepgrar calaaaeaqi vfgefepvva
      721 ampaaivqla adpeaavlgt rrlavallnl graadaaral esclsrlqal ddpraryefl
      781 gefgtvlerc nrrregfehl qrgialaida rdvgtaatmy anlgvnrvyw gdptaaiaat
      841 eqglalrqqh dglaglasgm dmtlgamcrd agrlgeaier lershaafva dgnalwtant
      901 ashlallwlq lgqwaraarv lqghgeglpa fiaarleaar alldegqgrs alpgldrala
      961 rlaaadrvdv rlgiqlerlr llppaealvl seqvacearq aelmghahga evltvdalrr
     1021 agrtaeaaer tsalaaaasp lvpsgfyrpt lwlallralr aggradeaar fgeraradlm
     1081 rlraslppaf hdshdhrqpv nrallter
//
LOCUS       WP_284620007             695 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Aquabacterium humicola].
ACCESSION   WP_284620007
VERSION     WP_284620007.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 695)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 695)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..695
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75072
     Region          11..644
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mklpptlivh aalvamtlpa ahaiteddel aqaygdqati slatgarqpl rrapavatvi
       61 taedlramgv teldqvleav pglhvnvaps mgnrlyvirg vfslqtpqvl vlqngipitv
      121 lltssrgnls glaavenvar ieiirgpgsa lygadafsgv iniithgagd dpgtrlaari
      181 gsfdsadawl rhagrsggle walfakvart dgfdatiesd aqsrndrlfg traslapgpv
      241 naqgdtvdag ielahgawrw rtlykrrddl gtyaglgsal dpvgrgrsdr lisdlawsap
      301 adaggwgfsa glshmlyaqr ypvparifpp garlptgvfp ngmigspefd drstrlwvha
      361 ayggiaghal rlgaghddlh mamardtnnf rytatgipip sdpvrlsdlp fiyphrrrvd
      421 hvfvqdewrl hpdwtltagl rhdrysdagg ttnprlalvw daavdwtvkl lygrafraps
      481 fseqyatnnp iasgnpsvqp ettrtieavs twaatpalql nlslysyrlr dilravpnpp
      541 pvpgttyanv grqqgkglea elvwdatrll rvtghlslvr atdaatgldv gnvprrdafv
      601 ridwrlasgw rmdamlnhva drrrapgdsr ppvrdyttld lalttersgr gwfagatlrn
      661 vfdedvrepn lapglipndl pqagrsftlq agytf
//
LOCUS       WP_284620065             135 aa            linear   BCT 25-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Aquabacterium humicola].
ACCESSION   WP_284620065
VERSION     WP_284620065.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..135
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=13925
     Region          3..134
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mktkpqltld dvraiaqaae aearshqwav siaivddggh llwlqrldga apisaqiapa
       61 kartaaigrr eskvyedmin qgrvsflsap tlegmleggv pilaegqcvg avgvsgvksn
      121 edaqiaragi talgl
//
LOCUS       WP_284620089             139 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Aquabacterium humicola].
ACCESSION   WP_284620089
VERSION     WP_284620089.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..139
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15588
     Region          12..139
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mrfdipeqkk ltfemvipir wgdmdamghv nntiyfryle slriewfrsi dclpdpggvg
       61 pviinafcsf irqleypgev larhyagamg rstidtyatl ertdrpgevy asggatvvwt
      121 dfkaqksvpl pdsiralla
//
LOCUS       WP_284620182             682 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Aquabacterium humicola].
ACCESSION   WP_284620182
VERSION     WP_284620182.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 682)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 682)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 682)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 682)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 682)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..682
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75268
     Region          146..645
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mktlgrqall pdpdgetlpw sdsitplrng aavssssawr lgavglslva amaaafaawq
       61 llpllasgla gglqqgliag afsaallagl avvlwraqri asrtlrqsvn elrrgqwesa
      121 vaglrepkra vpsafgdlae qvegvlsese rrwrarvems tdwyweidqr fklsnlsada
      181 piakpagral gdllgrrhde lkcfeppamg wpafheller hekfrdleia vtglgtrehg
      241 wiaisgrprf radgqfagye gvardissnk eafrrlqase qryavmagls adwywitdaq
      301 hrfpqpsadm qrrfgnlvqr nvgktrweay pdalsaeawe lhraeldarq pfralefpvq
      361 rddgrtiwls lagaprfddn geflgyhgvg rditlrkvte qmlqrhnrel qlavtsrtre
      421 lelanrdlda farhlahelr tpighvqnls ellrqrlgpr lqpaegemld lqaraaqeml
      481 atleallela rsssaaierq avdlsalare viaqlpvler eapidwqvqa glsvwaspqq
      541 lrivlqnlfg naakftrria qpriafgger daegqlllrv edngagfepa qasrlfqpfq
      601 rlhrddefhg tgigltivqr ivqrhggtia asgapgqgav feftlgqrea arpdlppadp
      661 slepparasa vrasecpaps ar
//
LOCUS       WP_284620258             223 aa            linear   BCT 25-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Aquabacterium
            humicola].
ACCESSION   WP_284620258
VERSION     WP_284620258.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     BTLCP proteins: a novel family of bacterial transglutaminase-like
            cysteine proteinases
  JOURNAL   Trends Biochem Sci 29 (8), 392-395 (2004)
   PUBMED   15288868
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..223
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=25252
     Region          <2..137
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mrpsdlapta lidsdhpgvi afaerhgtga ddtaravsly yavrdgfryd pyrvdlsveg
       61 mrasavltlg hgwcvtkaal laaacraigi parlgyadvr nhlstermre tmqtdlflwh
      121 gytdieldga wrkatpafnl slcerfgllp lefdgredsi yhpfdrhgnr hmeyvhqrgs
      181 fddmpldqiv ddfrrvyprw mtqtdtmqra dflaevdreq pas
//
LOCUS       WP_284620347             221 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Aquabacterium humicola].
ACCESSION   WP_284620347
VERSION     WP_284620347.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..221
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24374
     Region          1..221
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mvaltlfdld htlldgdsdv lwceflmdrg vldrddfgar naamdrdyra gtvsaqdfca
       61 fyvstlagrs ldawqplrrv fldevvapri kpaaralvqr haeagellvm ttatnrfite
      121 ltaahlglph liatecerlg dgfsgrpagt lnmregkvar lqawlaerqi rldecrstly
      181 sdsindlplm savkhavavd pdprlqaeat argwpvislm h
//
LOCUS       WP_284620367             429 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Aquabacterium humicola].
ACCESSION   WP_284620367
VERSION     WP_284620367.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..429
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46851
     Region          3..415
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mlavrpepht sicqlpngvr viaialpwld svslsvfvra gsqhenaran gishvvehma
       61 fkgtetrdcq rinldaerlg gevnahtdkd htafhihgla ehavpflhml adivrhsnfp
      121 eaelererqv ilqefaeded dplstayklf drncfgrhpl aqpvigtqan irrftrdell
      181 ayvgqhytga nvvvavagri dpetlqheae kafgtmragp vnavappdwr gglrerrqag
      241 ssqshvvlgf plpslaaddp agelaaavfg egmsspllde lrerrglvyh ascsadvlpa
      301 agqfvveasm apehldpfld avgtllldha eridaialer arnqlavrsl rtqerpfrrl
      361 eeavqqlcvq grvrsraeql erlqalgtae vgsafrrlla eppalaivgk lkpgagerfv
      421 qrlatarga
//
LOCUS       WP_284620448             744 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Aquabacterium humicola].
ACCESSION   WP_284620448
VERSION     WP_284620448.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..744
                     /product="PhoX family protein"
                     /calculated_mol_wt=78246
     Region          21..738
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mssasqqtrp hddedhntsg npsfqsvlda rlsrrgllrg svgtaatamf gslafagcss
       61 dddapapapa papapaekll gftavaksla dsvvvpagyt asvlyalgdp ltadtpafrn
      121 dgtdeafdkr agdhhdgmew fglsatgtps ttsvarglla mnheattdet fasffvhang
      181 gtstlprpaa evdkemalhg lsvvevaktg sqwayvqnsa fnarlhqqte ieiagpargd
      241 allvtkysht gtvtrgtlnn cgtgrtpwgt lltgeenwsg yftrptgdda argndrsvta
      301 lkrygraega gsrhawetgg sedrftrwin aktgtstdgs ddyrnemngm gyiveldpyd
      361 rtkkatkrta lgrfaheaaa fgklvagqpl avymgddsrg eycyrytsta lwdaadagaa
      421 nrmatgdkyl dagklyvakf nadgtgqwie lsitnpavag yttyrfanqa dvlvnarlaa
      481 davgatkmdr pewsavhptt gevyytltnn snrraepsgs sqfapdaanp raytdqrgss
      541 tqqgnvnghi vrlkesggpa gttftwdvyl fgaeagagst vnlsalsaeq dfsspdgiaf
      601 tpstglcwiq tddgaytdvt ncmmlaavpg qvgdggkkti qharasggpl nvdtyvgkap
      661 tadtlkrflv gpvgceitgi tetpdgkalf vniqhpgest akaniadpak ytsqwpsnag
      721 ygagkrprsa tivitkndgg rvgt
//
LOCUS       WP_284620482             300 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Aquabacterium
            humicola].
ACCESSION   WP_284620482
VERSION     WP_284620482.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..300
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33016
     Region          14..283
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mshrrsieha iagfgmdtit lagpleakld amrgagfgqv mlkandlvgh pqgwqaavaa
       61 vkasglrgtg fqvlrdfegl sghlhqykvd iaktmlqmcs algcdvllac sststhastd
      121 ldhlardlrk lamlalphgi riayeglswg rtvnefttaw dvvqradcpn lglgfdsfha
      181 laagtsleai davdpakifl vqlsdfmwqe trtfeermat artfrvfpge gvhsaqlvem
      241 vrrldargya gdysfevfnd dyvqmplpmv aerarrsalw laedvlrrat prpnqlrlrr
//
LOCUS       WP_284620493             240 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Aquabacterium
            humicola].
ACCESSION   WP_284620493
VERSION     WP_284620493.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium humicola
  ORGANISM  Aquabacterium humicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Aquabacterium humicola"
                     /db_xref="taxon:3237377"
     Protein         1..240
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26211
     Region          72..237
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mptlndyqav aeartkdell aallavahkl dfgllntllv verpqqaavt vplantpdgf
       61 eeasrepsas krdpvlqklk rlsipivwdq styadedavd lwdaqapfgy rtgvavalhl
      121 pgarhfllgv drehalpknq mkltrllgdi qllavhaqda avrllaplaq ptvavsltrr
      181 etevlhwtml skdtsaiaqi lglspntvkf haenamakln cesrhaavlr aleygllert
//
LOCUS       WP_284620915             721 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidase U32 family protein [Brachyspira pilosicoli].
ACCESSION   WP_284620915
VERSION     WP_284620915.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..721
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=81207
     Region          5..293
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
     Region          443..505
                     /region_name="DUF3656"
                     /note="Collagenase; pfam12392"
                     /db_xref="CDD:463557"
ORIGIN      
        1 mnnknkkiel lapvgdergl kaavnagada vyfgtksfna rvgaaenfde kaleenikfa
       61 klrnvnvyit vntlvyndei dkvlpliktv sdlgadaiiv qdlgiidivr nnlniamhas
      121 tqmscnnlds vkllksigid rvvlaremsl enikyirdnt dieletfvhg alcvsfsgqc
      181 aysylhggrs anrgacaqpc rmeytggktd yplstkdlmt idiipnlles gitsfkiegr
      241 akrseyvavt tsiyrhaidl alenkdipiq kyreslmkif nrggfsqgyy ynskdifeny
      301 kpshdgeyig evvaykknki hikaekelnv ydglsfgdsg qvgmqisdly kdnirvkrak
      361 gnlsfsavik nvnvgdevyr ttdklqmdea dkiiesdnfk hlldlnciig fndiddnkki
      421 klvvkskydg rlnnieyisd ytlqeaktka ttkedifnsl sktggtvfef eninieekfk
      481 npfipvkiln earrciiekl envlmqskki dynkdfekni nypntnikvl ianseekinl
      541 ysdihydkki lfpnvydeni iklfenkkid giilphvtfd kdieviksiv ektnnmivic
      601 nnlghiealk gkailwagig lnainnytvd flyklgvnvv isaieagknl khtlsikegl
      661 ipamnfafcp ksmsvgcskc keediidhkg nivifdcvki ynktsfilen iknktgeiyi
      721 k
//
LOCUS       WP_284621006             355 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Brachyspira pilosicoli].
ACCESSION   WP_284621006
VERSION     WP_284621006.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..355
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=40579
     Region          8..334
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mavndaiqrl rdyihsnnid avilnrrssf awfsqcessm nfytdfglgy iyvdkndvfy
       61 ytsnneapri ereifkgvip vksyswvdgp aknvaelisg kkvngdfgfn gvkedftnik
      121 klryslfddq iaiarelgkt sasilektmk nikpglteyq ieaeiryafg kenielpvll
      181 iasddnlnvy rhplatskia nerfmavlcp rykgvvials rilyfrkrte qekkrdetic
      241 kinnllmnet nigtdsktlw dfmvktykee gveteyfnhh qggaigfesr ewilrptlqe
      301 tiyknqmiay nptligtkae etllmlegak eiltigndfp tlthsgmtst lplek
//
LOCUS       WP_284620939             342 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Brachyspira
            pilosicoli].
ACCESSION   WP_284620939
VERSION     WP_284620939.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..342
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=39298
     Region          29..333
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mnkilqedln fileklknni dinrlkntni fitggtglfg klfletflff ndtldtniri
       61 tvltrnydkf isnypqfinn nikfingdir nfnidcdnid yiihaaasvd pilekenpde
      121 mfsiivggtk yllekikpyn ikrilftssg avygkqpsnl kyisedfkcd pnsiygrgky
      181 isenilldsn idsiivrcya lvgpylnlki hyaignfild clekrdiiir gdgtpirsyl
      241 ytsdliiwli tallnsdsne iynigsmket sildlaqlvt kqfdyktdik vlskkevgia
      301 psiylpdnnk iisklnvken ytlenmirrt iywnygemne nn
//
LOCUS       WP_284621030             367 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Brachyspira pilosicoli].
ACCESSION   WP_284621030
VERSION     WP_284621030.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 367)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 367)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 367)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 367)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10543770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..367
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41377
     Region          82..221
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
ORIGIN      
        1 mpnnnnnqhq kplmeelyke eleilksrdk nlkpknwkls pqavrdfilg kkfedgtiik
       61 kkfygddalv eraiitlagn rglmlvgepg taktmlsell saaisgnsti tiqgtagtne
      121 dnikyswnya llfakgpvde alipspiytg msngfitrfe eitrcpieiq dslisilsdk
      181 imnipeqnrv lfantgfnii atantrdkgi nemssalkrr fnfetvepik dikleseiit
      241 nqceslfela nidmnidydv vnvlattfne lrngisedna klqelnsims taeavsvyyq
      301 salhsyyyad gninmstvve nligsvvken kddvsklqhy fnnavkikaq klgrrwqeyy
      361 esrniir
//
LOCUS       WP_284621117             283 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Brachyspira pilosicoli].
ACCESSION   WP_284621117
VERSION     WP_284621117.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..283
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31430
     Region          7..280
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mvstltakni nealelklkh naiifaggtd lmvehlrgsn liakferpvl finevnelkg
       61 ikedenniii galttfdeii ksplipqvlk dsalgiagpp irniatiggn icnaspsads
      121 lpslyamdsv lilkskdsqr evkikdfitg vskttikdde ilthivipkk nyeysfykki
      181 gtrkanalsk laicalvcke nnkyrfrisf ctlgitvtrd esieekfavs disewknkik
      241 diqeayssim kprdsarsta lyrkkcalnl iecfleealk nic
//
LOCUS       WP_284621242             468 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Brachyspira pilosicoli].
ACCESSION   WP_284621242
VERSION     WP_284621242.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..468
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=53798
     Region          40..304
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          68..96
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          101..131
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(141..142,145..146,148,172,175..176,179..180,
                     182..183,206,209..210,213..214,217)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          141..165
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          170..200
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          205..229
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          239..267
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          277..304
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtiyiivfiv vfsillfias kilpklysky vqsdmdrvnn yiasekynla ikklrdilsk
       61 nkshnksykv ykiigdcyyk mgeypfaive yrhaidtgdn spetvislgr slnaigrkee
      121 slaqflsllk lggeykvnvs ieigkiyydn gqyntafqff enalendstn kealkykayc
      181 yvsagnynea ivimngiink ypndpalnyn lgraykgkld cknaikhyki sskdreyaik
      241 slyeialcyi elnniefaik ylemaiaydg idrelnlail yqlsecysrm enlnkaieyl
      301 eniiiidpny kdankklney kesrysdnik nffkldendf adlalkivss mnlipyslkt
      361 tdkkyviifa kdgksvhstk kivffrmsys pifneeliql ydyavnsniv nsvlvtcama
      421 tpdairyaam sridivgikr lenlvekstf tsvpvgitrt eekldwii
//
LOCUS       WP_284621359             321 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase [Brachyspira pilosicoli].
ACCESSION   WP_284621359
VERSION     WP_284621359.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..321
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=37358
     Region          47..298
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mdakvksvkn ktidfdintk egkaylnkci idndalkeyk kkdiinktin gdtfdvlkki
       61 eknitdlmiv dppyniskny hgykfkdrdn lsydkythlw vesiipilke natiyvccdw
      121 ksslvignvl ekyfkiqnri twqrekgrga knnwkngmed iwfatlsnky tfnidkvkir
      181 rkviapykie gkpkdwiete ngnfrdtcps nfwddisipy wsmpentahp tqkpekliak
      241 lilassnend fvfdpflgsg ttsvvakklg rnysgieqnp aycawaekri esalqnkeiq
      301 gytdnifwer ntmqlqnklk k
//
LOCUS       WP_284621282             469 aa            linear   BCT 25-DEC-2024
DEFINITION  rhamnulokinase [Brachyspira pilosicoli].
ACCESSION   WP_284621282
VERSION     WP_284621282.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167330
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..469
                     /product="rhamnulokinase"
                     /EC_number="2.7.1.5"
                     /GO_function="GO:0004370 - glycerol kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008993 - rhamnulokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006071 - glycerol metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0019301 - rhamnose catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52850
     Region          6..463
                     /region_name="ASKHA_NBD_FGGY_RhaB-like"
                     /note="nucleotide-binding domain (NBD) of rhamnulokinase
                     (RhaB) and similar proteins; cd07771"
                     /db_xref="CDD:466791"
ORIGIN      
        1 mtskiysiac dfgssggkif lskfendkmt leevhrfsls pikinnyyyt dfiymynell
       61 kgikkvvdmg iqpsslgins wgvdygyldk ngellsnpvn yrdtrtidti kklekiglsa
      121 kelykitgis cmpfnsimqi yediqgrani vnnaskllft pdlfgyfltg nisaeytiss
      181 tsqlidinkk ewskeileki nfdinklpsl qepgskkgll kqeiadylgc kpfdiiavas
      241 hdtasavlsa pifddntayl ssgswsllgv elkeavltde sfengftnem gynntirfle
      301 ninglwtiql lqkkyqisfn dmeqlardni kdehridind nrfynpkdie deilnyykdt
      361 nqaniekdkk gviiasvyns laesyakyin slkkllnkdi nklcivgggt kdkliceltk
      421 ektnltvsvg pvectatgni laqfkalgvl kdtnemrklv vnsfdikqi
//
LOCUS       WP_284621422             251 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Brachyspira pilosicoli].
ACCESSION   WP_284621422
VERSION     WP_284621422.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..251
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29417
     Region          16..139
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 msevkknyyg slctemyeil hkkapedeln fylsyaekgk kileplcgsg rflipfierg
       61 fditgidmsn emlkklklkf pnaktihtdi meydpkekfd yifissgsvs lftdidickq
      121 iliriknwlc ktgkfvfavd tiknrciddn dyniaasvkt kenfeivlks knyyeeqtqt
      181 qfspsiyemy nnieliqsef mdfqthlyky gemekylkev gftqvktfss fekeiavnde
      241 cdmflfecsf l
//
LOCUS       WP_284621596             721 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidase U32 family protein [Brachyspira pilosicoli].
ACCESSION   WP_284621596
VERSION     WP_284621596.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..721
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=81222
     Region          5..293
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
     Region          443..505
                     /region_name="DUF3656"
                     /note="Collagenase; pfam12392"
                     /db_xref="CDD:463557"
ORIGIN      
        1 mnnknkkiel lapvgdergl kaavnagada vyfgtksfna rvgaaenfde kaleenikfa
       61 klrnvnvyit vntlvyndei dkvlpliktv sdlgadaiiv qdlgiidivr nnlniamhas
      121 tqmscnnlds vkllksigid rvvlaremsl enikyirdnt dieletfvhg alcvsfsgqc
      181 aysylhggrs anrgacaqpc rmeytggktd yplstkdlmt idiipnlles gitsfkiegr
      241 akrseyvavt tsiyrhaidl alenkdvptq kyreslmkif nrggfsqgyy ynskdifeny
      301 npshdgeyig evvaykknki hikaekelnv ydglsfgdsg qvgmqisdly kdnirvkrak
      361 gnlsfsavik nvnvgdevyr ttdklqmdea dkiiesdnfk hlldlnciig fndiddnkki
      421 klvvhskydk rlnnieyisd ytlqeaktka ttkedifnsl sktggtvfef eninieekfk
      481 npfipvkiln earrciiekl envlmqskki dynkdfekni nypntnikvl ianseekinl
      541 ysdihydkki lfpnvydeni iklfenkkid giilphvtfd kdieviksiv ektnnmivic
      601 nnlghiealk gkailwagig lnainnytvd flyklgvdvv isaieagknl khtlsikegl
      661 ipamnfafcp ksmsvgcskc keediidhkg nivifdcvki hnktsfilen iknktgeiyi
      721 k
//
LOCUS       WP_284621764             574 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Brachyspira pilosicoli].
ACCESSION   WP_284621764
VERSION     WP_284621764.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..574
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=66731
     Region          382..483
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mlneikknic iitdingiyg yghftrmnli anrladiydf tfssidngse lykrvdikti
       61 efnkigeikp yivivdarev eekyisylkk issviivdsv gserrladiv iemlpnldns
      121 kevnikpfia tilnnsikpi ynedspilvy lgfnkqlkdk aiqiiskitn kkfvvidfkr
      181 esefsnieyi dfskdifans ysgvityfgl tafecieski ptilfsptky hdelankcdd
      241 iffnlgffed adidesakki eafisdkekq yslienaeqi ntdesierlk tifsnikdfk
      301 dikcpfckss nierknrnle snlykcghcn tlfrkyflsp ftdysskyfv edykkqygkt
      361 yeedvdnlsr lakrriekik kikpngkvld igsamgfflk easnygyite gieiseyasn
      421 ycvntlnlnv hncslldfny kekeydiita wyvvehiynf dkifenilys lkddgifala
      481 mpngygvsgr fnknyysivp sdhafeanpk sldmffakys lkrislenqs iyynrftdvf
      541 kifknsklse klykklaqkf nlgdtfeciy qkvk
//
LOCUS       WP_284621765             198 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Brachyspira
            pilosicoli].
ACCESSION   WP_284621765
VERSION     WP_284621765.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..198
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=23186
     Region          <31..125
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 miylkyvfnn eyngniesls kemankhynk dsliikrnnn gkpyfenedn iffngshskd
       61 licvgmsdsl igldaefike rkffdiagey fsfkerkflk sskkleidff tlwtlkeayi
      121 kkfgkvifdi kdsieidlde rviynadnlf fatfilddsy iislcsdmkn kdviittddf
      181 nlnmlfsypv lpqiyisi
//
LOCUS       WP_284622006             396 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Brachyspira pilosicoli].
ACCESSION   WP_284622006
VERSION     WP_284622006.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 396)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..396
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42338
     Region          2..>392
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mllslalifl cgmilgkifs llklpsllgl iitgivlgpy clnlldnsil sisadlrela
       61 liiiltragl nldiedlkkv grpailmcfv pasfeiigmi liapklfdis lldaalmgsv
      121 vaavspavlv pkmlklidek ygtnksipql lmagasvddi fvivlftsft slvkggnisy
      181 ldfvkiptsi ifglllgiii gfilskfftk fhirdsakvv iilsisfilv sietsisnlf
      241 ggvigisgll avmsigaylk kskeelskrl slkysklwva aeiilfvlvg aavninyafn
      301 agvlgiilif avlifrmlgv lvsliktkln kkerifsmia ycpkatvqaa igsiplslgl
      361 asgeiilvia vlailitapl gafaieasyk kllehe
//
LOCUS       WP_284622024             569 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein [Brachyspira
            pilosicoli].
ACCESSION   WP_284622024
VERSION     WP_284622024.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Porat,A., Cho,S.H. and Beckwith,J.
  TITLE     The unusual transmembrane electron transporter DsbD and its
            homologues: a bacterial family of disulfide reductases
  JOURNAL   Res Microbiol 155 (8), 617-622 (2004)
   PUBMED   15380548
REFERENCE   4  (residues 1 to 569)
  AUTHORS   Kimball,R.A., Martin,L. and Saier,M.H. Jr.
  TITLE     Reversing transmembrane electron flow: the DsbD and DsbB protein
            families
  JOURNAL   J Mol Microbiol Biotechnol 5 (3), 133-149 (2003)
   PUBMED   12766342
REFERENCE   5  (residues 1 to 569)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   6  (residues 1 to 569)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   7  (residues 1 to 569)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   8  (residues 1 to 569)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   9  (residues 1 to 569)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18120940
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..569
                     /product="protein-disulfide reductase DsbD family protein"
                     /EC_number="1.8.-.-"
                     /EC_number="1.8.1.8"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=63779
     Region          30..132
                     /region_name="DsbC"
                     /note="Disulphide bond corrector protein DsbC; pfam11412"
                     /db_xref="CDD:463273"
     Region          168..542
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 mrkiyiflfi ifsltaysqs fnsllnknte aiivfslstn dnkitvkani pegyyayles
       61 kiankilffa dnkeinttyp kgekyhedii ikgeqefiln didinkinfi kttyqlcsak
      121 dnvclqpqsk viygeeidip nnnitdekpe nassienyik gsnnifitli lifaaglasv
      181 llpctyplls itvsilgttt deknnkkssv lasllfalgv ittytllgav vsvagfafhk
      241 tilfgsigyn pivltilvll flyftfsmag fyeikapsfl qsaktnayak knqsifhkyi
      301 mgllagivat pcaapiiavi leigflnpvf atlymavyal gfasvlfvlg tfasiltkmp
      361 kagtwmvyvk yiftflmmii sfyyanilfg vlgfnkisyi lasvtilifa llvyiiknkt
      421 amlsslekki fvsvliisia lgsvygiikq ksevsntisy tealelskqn nkpilidfsa
      481 vwcancyelk ekvfvneelk kliddnlift evdvdkykni sdeynvkwlp wiividrdkn
      541 ilytknsfss fddkmalsik edleevink
//
LOCUS       WP_284622719             344 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium accolens].
ACCESSION   WP_284622719
VERSION     WP_284622719.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..344
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35237
     Region          15..344
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mttinsilqa qqrgrhvrvl astlvfglia laaylvllgq gplelsprqv ldvltgggse
       61 shirvvwdlr lpvaiatviv gaalgvagsw tqtmarnpla spdilgvtgg asvlvvlgtv
      121 hsrpgfaddi pdfwwracla migallvvil lavlggigts nrivivgial slmfqaivay
      181 lmrsaqiqra aeaqtwlags tgfvrmeviv pllvalapfi aigiwcarel pllahddssa
      241 ttlgvnisrq rallliaatg icavvvsvvg pigfiallap hlarmvartp tpspvasaaa
      301 gaalltvcav iagaipvnap vgavssvigg calvvlvwna arrs
//
LOCUS       WP_284622720             359 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium accolens].
ACCESSION   WP_284622720
VERSION     WP_284622720.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..359
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36013
     Region          50..350
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msattkdgqt iqtgstaqnp tatpvmargk grttflvali laslvlavas lalgsrsipp
       61 deviaalrga geqdirdivw nlrmprtfla yfagaalava gvlaqswtrn pladpgfigi
      121 tagasffval gtaigiattt gmrttlalvg agittllvla vsrrfqdplt lilvgagvsa
      181 algsgaviig lystdvldsm rrwtigstfg rgpedvaiag iglliglaca amaarpldll
      241 amgeesslal ggspttarvg aalsvvvlag sataatgpia fvgfaiphiv rrvvgpsvat
      301 mllpsallgg cavlaadiig rlivgnsele msivlaivga pfliwgahrg vgrawgdna
//
LOCUS       WP_284622759             471 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Corynebacterium accolens].
ACCESSION   WP_284622759
VERSION     WP_284622759.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..471
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49981
     Region          3..465
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mdkqphaviv gagpngltaa arlatagwrv dvyerashpg gaaassteif pgtvvdlgaa
       61 ghpfgiaspa fraldleshg lrwcharypm ahplegaqag ilhnsleeta aglgtdaraw
      121 trlhghvvrn idehvnnalt plvrwpehpv rlaqfgapgv lpasalaraa ftspqaralf
      181 agsavhaits ptraftsafg llfgalgmtr gwpvveggtq aladalvsll hshnarihtg
      241 aditdvrslp radalilnlt prqtlrlggl dlpartrrsl rrwrygsavy kvdfhlsepv
      301 pwadprvgqa gtvhvggsve eisgaerdig krrmpvnplv mvcqqyvadp srglvlwtya
      361 hvphgyeery prevtgliar qierfapgfr dtilatrats padlerwnpn lvggdiagga
      421 mtglqtvlrp rlsahphrla pgifmasgst apgagvhgmp gwwaagdvat p
//
LOCUS       WP_284622785             847 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium accolens].
ACCESSION   WP_284622785
VERSION     WP_284622785.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 847)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..847
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=94832
     Region          19..841
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mnlsqqlpdl tevpeslide aiwdtfnswt tskginlypa qeeaslgila gdnvilatpt
       61 gsgksmvana ahfialargq rsfytapika lvsekffalc eifgaenvgm mtgdatvngn
      121 apiiaataei vanialrdga eanidqvvmd efhyysdpdr gwawqvplle lpkaqfllms
      181 atlgdtdwlq edltrrtgre tnlvagstrp vpldfsyvfs avhetieell adnkapiyvv
      241 hfsqreaaer aqaltslsgi inkeekedia eeiggfrftt afgkdlskll rkgigihhag
      301 mlpkyrrlve rlaqrgllkv icgtdtlgvg invpirtvlm tglakfdgqr qrilksrefh
      361 qiagragrag ydtegtvvve apeheienak arrrigddpk rlkklkkksa regevswsek
      421 tfarlteaep eqltsqfrvs nsmllnvlar hgdgyahmhh llrdnhdprs kqnkdiltal
      481 dlfrglldsg vvqkstkgld iygrpyhlvr elprdfalnq plgpfalaal slldpeaesy
      541 hldvisvfea ilddprqvlq aqqkkrrgee iaalkadgvd ytdrmnived itwpkpleel
      601 leqaydtfae tnawvkefel rpksvvrdmv enamtfsdlv atyglarseg vilryltdaw
      661 rtlkqsipde yttpqiedii iwlgelirqv dsslvdewaq magedspidq dtldrelafg
      721 vedptaltan rrafgimvrn ymfrlaqlfa leeedrlaev ldyldevpdf gavlddyfde
      781 yddidtgpea rgpeyfrlee sssrswpvrq iikdpagdra yqfvatvdld asdeagevrl
      841 selrvey
//
LOCUS       WP_284622826             182 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Corynebacterium accolens].
ACCESSION   WP_284622826
VERSION     WP_284622826.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..182
                     /product="YceD family protein"
                     /calculated_mol_wt=19173
     Region          1..182
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mtsplkfdvg ellnaqgada mpeqrtqtgp aperigvemi aipkgedltv aailtplgsg
       61 vlvdadisgv ltgecarclk elhpqldlhv tqvfaadesf vsgddadsdd agsgdeipei
      121 eddeldllqa videaglnlp fapvcedgcd iqtpegvttg iseeeeeeek vdprwaglek
      181 fl
//
LOCUS       WP_284622833             256 aa            linear   BCT 25-DEC-2024
DEFINITION  inositol monophosphatase family protein [Corynebacterium accolens].
ACCESSION   WP_284622833
VERSION     WP_284622833.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..256
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=26739
     Region          5..252
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mmdprelvaf aeaavdqvep ifrsgigapp ahfksrgdfa tevdlaiekq lrdilqqmtg
       61 ipvygeesgg sihdtvwvvd pidgtanysa gnpmagilva lvhegqpvaa isdfpllgrr
      121 lvasdgsplr saggpsggfg ggeefpefdd arghvgcfsn lptaafhelr esglrpritg
      181 svgldnafva qgvfdgavnf sphpwdnaag allikaaggi itdpegnpwt vqsrgmvsgt
      241 pqvhetilei lshhtn
//
LOCUS       WP_284622888             938 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium accolens].
ACCESSION   WP_284622888
VERSION     WP_284622888.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..938
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103536
     Region          4..936
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtethldtfa aglpypldef qvqgceaven gqgvlvcapt gagktvvgef avslalsrgt
       61 kcfyttpika lsnqkyhdlv aehgddavgl ltgdvsinad aeivvmttev lrnmiyadsp
      121 aldrlthvvm deihfladas rgavweevil nladhvsiig lsatvsnsee fgewlatvrg
      181 dtsvivtehr pvpldqwmml grkiyplfep esggqvnsel erriqrleag dsddgradyk
      241 sgkgfrarar hkgggrsefh gkaggrsgss rpqdryrplg rpevlkvlqs qdmlpaitfi
      301 fsragcdgal yqclrsrmvl ttqeeaeeik aivdagvegi peedlqvldf rrwrealsrg
      361 faahhagmlp afrhivedlf vrglvravfa tetlalginm partvvlekl ikfngeahvd
      421 ltpgqytqlt gragrrgidt lgnavvqwap amdprfvagl astrtyplis tfapgynmai
      481 nllgmlgfed slrlleksfa qfqadgsvve etreleraeh rvrelreqld davdalappa
      541 kdgedpaevl mdyirlrrel taeekqskvd kehqrtqevi avlarlqlgd viaiagkkrp
      601 tlaavvtpan qtedprpwvt tesgwsgrid atgisnppiq lgrikipkpv rknprrntky
      661 iqdvfrrekf drpkrmkskp rlrpnkrvge lrdairehpa hkwpatdgeq lagvaqklar
      721 rerdleklqa kvdkatdtlg rtferivdll aemdyvefsg agsdrtpvit eegerlakih
      781 sesdllvaqc lkrgiwdeld paelagvasl ccfenrkatg gqpeaatdrm adamnatwri
      841 ytelgaderr hrlpptrepe agfalaihqw aagaplgycm aaaneagael tpgdfvrwcr
      901 qvvdllqqia ktgydgqiqr narramdaiq rgvvaiga
//
LOCUS       WP_284622912             322 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Corynebacterium accolens].
ACCESSION   WP_284622912
VERSION     WP_284622912.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..322
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34413
     Region          2..319
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(40..41,45,118,122,125,143,146..148,167..168,172,187,
                     210..211,232..236,257..260,307,309)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(130,225..226,239..244,252..259,262..263)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mhaiqitetg gpevlryaev paptpsedev lvdvtvagvn yidtyyregi ynaqtpfilg
       61 fegtgrvvhd pkgeiaegsl vawhhafgsy aeqvcvprng lvavpddfpt eiaasmllqg
      121 mtahflshgv yelgegatcl itagaggvgq lltqmasslg atvytvvstd ekeeisykcg
      181 adhvfrysdg lgeqvrrfng grgvdvvydg vgqatffesl eavrprgtva lfgaasgpve
      241 pidpqllnkh gsifltrpsl gawtaqegef qmraqavvqa vmdgdlkfnv sasypleeae
      301 qahrdlqsrs ttgsivlrvr qd
//
LOCUS       WP_284623118             172 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Corynebacterium accolens].
ACCESSION   WP_284623118
VERSION     WP_284623118.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..172
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18497
     Region          27..117
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 meeryrataq vwsgspnatl vdhvsdlpag taldigcgeg adaqwlherg wqvlgidfap
       61 tavartkarg vpaevatfde fshapfdlvt vhygsvrata gevalleklv apggtllyvh
      121 hdmeseeiar pewlaenlte ltvqtlrrsp rhvtsgagah htsdvvlvak rr
//
LOCUS       WP_284623273             389 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Corynebacterium accolens].
ACCESSION   WP_284623273
VERSION     WP_284623273.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..389
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40885
     Region          11..388
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mneslekvas arldkwredg lwrspsvfes gqvpesslrt aagktvqdav ffsssnylgl
       61 aehpeiksav kdsvdhygag sggsrlttgt selhvaveaa aarltgypds vffatgyqan
      121 lstlqalasp eltiisdarn hasiidgcrl akasgaslvv tahrdtrave dalatratky
      181 alvitdglfs mdgvlaplpe lsrlardyga wlmvddahsf gavgdrglgl peyfgvqpdi
      241 qlitaskalg aegglvatsk pvaqllrqqa rsfvfstspt patsaavlaa lkliesdpsl
      301 vnqlqgniay whnargttpq qgpiipvhvg deaaamdasa alldrgfivp airwptvarg
      361 aailrvtlma thtraqidal cteleqlgl
//
LOCUS       WP_284623539             471 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Corynebacterium accolens].
ACCESSION   WP_284623539
VERSION     WP_284623539.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..471
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50126
     Region          3..465
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mdkqphaviv gagpngltaa arlatagwrv dvyerashpg gaaassteif pgtivdlgaa
       61 ghpfgiaspa frslnleshg lrwrharylm ahplegapag ilhnsleeta aglgtdaraw
      121 trlhghvvrn idahltnalt plvhwpehpv rlaqfgvpgl lpasalaraa ftspqaralf
      181 agsavhaits ptraftsafg llfdalgmtr gwpvveggtq aladalvsll rshnariytg
      241 aditdvrslp radalilnlt prqilrlggl dlpartrrnl rrwrygsavy kvdfhlsepv
      301 pwadprvgqa gtvhvggsve eiggaerdig krrmpvnplv mvcqqyvadp srglvlwtya
      361 hvphgyeery prevtgliar qierfapgfr dtilatrats padlerwnpn lvggdiagga
      421 mtglqtvlrp rlsahphrla pgifmasgst apgagvhgmp gwwaagdvat p
//
LOCUS       WP_284623668             194 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Escherichia coli].
ACCESSION   WP_284623668
VERSION     WP_284623668.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..194
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=22375
     Region          <105..189
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtvfsfikev lsphirllys pqelgfndag livlnhfgyd nniyysvtlt rkeitsfqnt
       61 senthyfays ktikktidri fkitgekiti gnitpsingk vsvtlilsll emklidfiad
      121 dntdvrvrlt vlnmlnnntt tirelaasvy lqedylkrif rrytgtglyq fynwikllka
      181 iskiqnndki kklq
//
LOCUS       WP_284623749             275 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium accolens].
ACCESSION   WP_284623749
VERSION     WP_284623749.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 275)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19108954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..275
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30829
     Region          26..232
                     /region_name="NUDIX_AcylCoAdiphos_Nudt19"
                     /note="Nucleoside diphosphate-linked moiety X)) motif 19;
                     cd18870"
                     /db_xref="CDD:467582"
ORIGIN      
        1 mnnhihdrld aidasdttgf nggrmaatvl llrdgpdgle vwvqervstm rnypghavfp
       61 gggvdprdfp prswdsgdlw agksvvamar rmgvtkykah alvfaaarel feesgtlfai
      121 rddgtisnar ryhrerrlle shtisftefl snngmrvdad mllpwarwvg qsknhwfdtf
      181 ffvgllpsgq epdgdthead dagwfspqli legwraglvr lvvptwaqmq rlckystvqe
      241 vlddasssdl rpvigdprdd pqyaeyfatt pteri
//
LOCUS       WP_284623854             181 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium accolens].
ACCESSION   WP_284623854
VERSION     WP_284623854.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 181)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..181
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19665
     Region          4..156
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18879"
                     /db_xref="CDD:467590"
ORIGIN      
        1 mptpdyivkl resighdqif vpacsaiilr dvptgaalwe vpsvllvkra dnavwtpveg
       61 icepgeeitt talrevkeev gldakveall gvgqsgpvty pngdecmfms talrlsvadg
      121 aepvisdeen teaqwfsvah lpdsvsrrhr lmiadavahl khpqgfshrm gwmkrseqpg
      181 l
//
LOCUS       WP_284623911             164 aa            linear   BCT 25-DEC-2024
DEFINITION  LGFP repeat-containing protein [Corynebacterium accolens].
ACCESSION   WP_284623911
VERSION     WP_284623911.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..164
                     /product="LGFP repeat-containing protein"
                     /calculated_mol_wt=17832
     Region          <7..164
                     /region_name="Psp3"
                     /note="LGFP repeat-containing protein, may be involved in
                     cell wall binding [Cell wall/membrane/envelope
                     biogenesis]; COG5479"
                     /db_xref="CDD:444230"
ORIGIN      
        1 mkfakkltat iavcasvtfa gagvssakvf hghwiggrie eayhrlggwq tfgdattder
       61 vaknngrfqv fakdasiywh agvdngiahq vggrirnkwg dlgwegaalg ypitdelktp
      121 dgkgrfnhfq ggsiywspet dahqvwggir dkwaqqgwet gelg
//
LOCUS       WP_284623983             359 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium accolens].
ACCESSION   WP_284623983
VERSION     WP_284623983.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..359
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38630
     Region          63..358
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mkrlnsvlaa aavctglaya pvagaaeltp qqvagdaaqs tispleptpe iegkswykky
       61 kddarvekle atspamngrk iplavvraqh enrptvylln gaggaeqdmd wlklsdavdf
      121 yhskdvnvvv pqagafsyyt dwisepnssf lqgpqkwetf ltkelpgaie khinadnhra
      181 iagmsmsats slllaqhnqg fydavgsfag caataypier qgveltvgrg ggsvdqmwgp
      241 lgsptnrynd ammnaeklhg telyvssgsg laseedtfsy iqskgynplq aaqgsatlqv
      301 eggaieagvn ycthnfkakl dqagvpatfn frntgthswp hwnqdlkdsw pvfergfns
//
LOCUS       WP_284623992             196 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Corynebacterium accolens].
ACCESSION   WP_284623992
VERSION     WP_284623992.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..196
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20143
     Region          <86..196
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mkkyvfgtvi aaiviavlvv vgvmqlrgdd tgagesaqap gmesgtagdq dvaerpdcpa
       61 gpiagvdlec lggddagegd kadegitian vwawwcepcr aelpyldeva eshpdwkvig
      121 vhadknagng aaflndvgvd lpsfqdpdns fagtlglpgv vpvtvilrdg evikqaaqpf
      181 tsadeiektv kealag
//
LOCUS       WP_284624006              97 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein
            [Corynebacterium accolens].
ACCESSION   WP_284624006
VERSION     WP_284624006.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..97
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10869
     Region          3..>66
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 msyvnitals fpegagpeie qrfaqrakgv dkaegfesfe llrpvagedr yfvvtrwdsq
       61 enyqkwadar pagnhledek rgmsvdvlgf esiqles
//
LOCUS       WP_284624048             268 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Corynebacterium accolens].
ACCESSION   WP_284624048
VERSION     WP_284624048.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..268
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30449
     Region          3..237
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mptlwavadl hgavsdnfar iaelappdpa dwlivagdva erselivril rdlaarydtv
       61 iwapgnhelf srsqdqykgr ekydhlvaac raigvitped pypvfngiti vplftlydys
      121 frppgtsvee avqqarakkl vmtdevaiap fvdvrawcwd rlaysikrls rvqgptilin
      181 hwplvqeptm vlrfpeialw sgsrhtrswp rrykaeaviy ghlhmpskmn vdgvdhievs
      241 lgyprewrnq phriawpypv tstfgevn
//
LOCUS       WP_284624133             373 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium accolens].
ACCESSION   WP_284624133
VERSION     WP_284624133.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..373
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39972
     Region          26..372
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mttqafspev ysrrlsaaqe aaaqqgidll ligtgpdfay ltgswvsshe rltvlavpqs
       61 gtpwivspnt ditdiksapv gkldvelrgw ndgdnpyela lkgaasikkv algqsltadh
      121 ilqfqglvpe adyvlatyal aelftrkdea eiaelrkagq aidavhakvp ellqpgrtea
      181 evarelekli leehsiidfv ivgsgpngan phhsfsdrkl aagepvvvdl ggtlpsgyhs
      241 dctrtyvvgg dlsqapqdfq dayavlydaq aaaraaakpg staeeidgva rkaiadagwg
      301 dkfvhrtghg iglstheepf imegndltle egmafsiepg iylegqwgmr ledivvltkd
      361 gyeslnvver evr
//
LOCUS       WP_284624134             938 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium accolens].
ACCESSION   WP_284624134
VERSION     WP_284624134.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..938
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103740
     Region          4..936
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtethldtfa aglpypldef qvqgceaven gqgvlvcapt gagktvvgef avslalsrgt
       61 kcfyttpika lsnqkyhdlv aehgedavgl ltgdvsinsd aeivvmttev lrnmiyadsp
      121 aldrlthvvm deihfladas rgavweevil nladhvsiig lsatvsnsee fgewlvtvrg
      181 dtsvivtehr pvpldqwmml grkiyplfep esggqvnsel erriqrleag dsddgradyk
      241 sgkgfrarar hkgggrsefh gkaggrsgss rpqdryrplg rpevlkvlqs qdmlpaitfi
      301 fsragcdgal yqclrsrmvl ttqeeaeeik aivdagvegi peedlqvldf wrwrealsrg
      361 faahhagmlp afrhivedlf vrglvravfa tetlalginm partvvlekl ikfngeahvd
      421 ltpgqytqlt gragrrgidt lgnavvqwap amdprfvagl astrtyplis tfapgynmai
      481 nllgmlgfed slrlleksfa qfqadgsvve etreleraeh rvrelreqld davdalappa
      541 kdgedpsevl mdyirlrrel taeekqskvd kdhqrtqevv avlarlqlgd viaiagkkrp
      601 tlaavvtpan qtedprpwvt tesgwsgrid atgisnppiq lgrikipkpv rknprrntky
      661 iqdvfrrekf drpkrmkskp rlrpnkrvge lrdairehpa hewpatdreq lagvaqklar
      721 rerdleklqa kvdkatdtlg rtferivdll aemdyvefsg agsdrtpvit eegerlakih
      781 sesdllvaqc lkrgiwdeld paelagvasl ccfenrkatg gqpeaatdrm adamnatwri
      841 ytelsaderr hrlpptrepe agfalaihqw sagaplgycm aaaneagael tpgdfvrwcr
      901 qvvdllqqia ktgydgqiqr narraidaiq rgvvaiga
//
LOCUS       WP_284624175             368 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium accolens].
ACCESSION   WP_284624175
VERSION     WP_284624175.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..368
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39162
     Region          13..366
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 maladtrfsd rrrklaaela gqridavlvt hlihvrylsg fsgsngalll rkdlsalmat
       61 dgryttqiaq evpdleaveg ravgkvllqq fdkdetpvrv gfeadymsvs eledlkdsap
      121 egvtlvpvsg iiedirltkd pvelekleei aalanqaled ilaagelrag rterevaadl
      181 efrmrilgse rvsfdtivas gpnsamphhg addrviedgd lvtidfgahl rgfnsdctrt
      241 yvvgtandfa keiydlvlra qqagveaava gtslsdvdaa crnviadagy gdyfvhstgh
      301 gvgldvheap faattgkgel apgmtltiep gvyvpgkggv riedtliitd gapkiitaas
      361 kdftelpa
//
LOCUS       WP_284624306             329 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium
            accolens].
ACCESSION   WP_284624306
VERSION     WP_284624306.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..329
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34978
     Region          21..329
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrrlalsigt aiafasvlll agprrltlal tdtgdaalas tlrehakpgf hhltaftlrd
       61 giatfagvgs nehteveigs vtkmftgelt hqlveegtlr ldstvgefld vdnapvadit
      121 ikelldhtsg lpptadgnff gflwsavagt npyegestqd ivdaaaaael snrgeesysn
      181 lgyallghvi etaadtpyer llkqrifepa gltetylmtp gavpadaprg rtatgqqaqp
      241 wemdgsapag airstasdma kfaewfmahg dpaygwqknd ngtgfwhngg tygystmlii
      301 dpktkraafa nndsltgtee lghtlfael
//
LOCUS       WP_284624336             172 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Corynebacterium accolens].
ACCESSION   WP_284624336
VERSION     WP_284624336.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..172
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18512
     Region          17..117
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 meeryrataq vwsgspnatl vdyvsdlpag taldigcgeg advqwlherg wqvlgidfap
       61 tavartkarg vpaevatfde fshapfdlvt vhygsvrata gevalleklv gpggtllyvh
      121 hdmeseeiam pewlaenlte ltvqtlrrsp rhvtsgagah htsdvvlvak rr
//
LOCUS       WP_284624392             277 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase [Corynebacterium accolens].
ACCESSION   WP_284624392
VERSION     WP_284624392.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..277
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=30809
     Region          12..275
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 msnlfyespd vtlfhgdafs vvnslekesv dcvvtsppyw rqrdysghpd qwgqeesigl
       61 yvdhlvylfs aimpklkphg vvwlnlgdkr vdgqlcgvpw mvakdmqtdg wclrsaviwn
      121 kpngmpescs drvsqnyeqv fmfsrrvdhf fdldplrvly dgdrtpsrra rsghtnkgns
      181 atgewsgahn grnpgsvwsi ptqpfpgshe avmppelarr civsscppgg vvfdpfhgsg
      241 ttgkvavetg rryiggdine sylalslrtr lqnatlf
//
LOCUS       WP_284624757             264 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium
            accolens].
ACCESSION   WP_284624757
VERSION     WP_284624757.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..264
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28638
     Region          9..264
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mselellcqw pvdnvaaall krgdvldeig dvsrefpvas vtklvsayai mlaveegave
       61 leqpagpega tlehllahas gvkfdsreqq kpvgerriys sagyewaaei vekatgiefa
      121 eylregvcep lgmsstrleg saghglvstv qdlaafsaev qdpqllhpnt vadmrrvhfg
      181 glrgivpgyg sfkdctwglg feirgekdhw mgalpadaig hfgmsgtylw lagdyamval
      241 tdrefgdwak plwnetnski wqal
//
LOCUS       WP_284624537             471 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Corynebacterium accolens].
ACCESSION   WP_284624537
VERSION     WP_284624537.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..471
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49760
     Region          3..465
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mdkqphaviv gagpngltaa arlatagwrv dvyerashpg gaaassteif pgtivdlgaa
       61 ghpfgiaspa fraldleshg lrwrharypm ahpledapag ilhnsleeta aglgtdaraw
      121 trlhghvvrn idahvnnalt plvrwpehpv rlaqfgapgv lpasalaraa fsspqaralf
      181 agsavhaits ptraftsafg lifgalgmtr gwpvveggtq aladalvsll rshnalihtg
      241 aditdvrslp radalilnlt prqilrlggl dlpartrrsl rrwrygsavy kvdfhlsepv
      301 pwadprvgqa gtvhvggsve eiggaerdig kprmpvnslv mvcqqyvadp srglvlwtya
      361 hvphgyeery pgevagliar qierfapgfr dtvlathtts padlerwnpn lvggdiagga
      421 mtglqtvlrp rlsahphrla pgifmasgst apgagvhgmp gwwaagdvat p
//
LOCUS       WP_284624799             478 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium accolens].
ACCESSION   WP_284624799
VERSION     WP_284624799.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..478
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51088
     Region          8..407
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mkttthgals rlhkfagviv apflivaals gffyalaptl eqwvyhdeit ataqgsprsl
       61 ddqiaaaqrq hpgaavaave asedpeettr vlftdpdaks psythavfvd pvdlritgee
      121 qqyggsralp lrtwlsnghr tlwlgepgri yaelaaswlg altiagvylw lkrrkktqkk
      181 nnkalrvhar lgswllpgfl fltitgltws mvagsnigkv reelnwkeps vatsvaeaga
      241 gtgagegsga hagheghggh eghaghsgge vtdndvlega qtalstarse gltgvlrmtp
      301 peqagdawtv regraayklr sdavavtadg rvidrinsad wplaarltsw liqlhmgtlf
      361 giysqvalaa lalgllvisi aglwmwwnkp rrrlpelkit pavvagvviy siiaplfgas
      421 lllffagdwl vrrlrpqsrs rsrsgsqsgt grsngdsgpt arprgesssr ipstvqng
//
LOCUS       WP_284624881             268 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium accolens].
ACCESSION   WP_284624881
VERSION     WP_284624881.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..268
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28809
     Region          3..262
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mhisdprdpr lddirnlnks dksgeglvia egplvaarlm esrfpmrclv gfpqkleaff
       61 aeygepecpv yevsretlae vagfdmhrgl vaaadrapep evgeildnsr tiavlegvgd
      121 henigaifrh aagmnvdavl lgsgaadply rrsvrvsmgh vlrvpfahle ggfttwqrsl
      181 qaladasftl isltpnpqav hlaeamrgqd kvamlvgaeg pgltehamka tdiraripma
      241 pgtdslnvat aaaisfyerq rslsdlnv
//
LOCUS       WP_284624926             524 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Corynebacterium accolens].
ACCESSION   WP_284624926
VERSION     WP_284624926.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..524
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55554
     Region          128..515
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mttphthest aqsegaedpg aprnewrrqf iglfiglala ilvffifpsn aidtvqqstg
       61 vdeeadytls airtvaavti lmgvwwmtea iplaatalip lvifplasvg tikevgapya
      121 satiflfmgg flialslqrw nlhrrlalyv vkligtsprr lilgfmlatg flsmwvsnta
      181 tavvmlpigt svlaltaetv ggwdkqkkfa talmlgiays asigslgtli gtppnaflna
      241 ymadtwdvtl gfgrwmavgv plaltfllia wvllitifkp emteipggre lindeikalg
      301 pwtrpqimtg iifvlaalaw vslpivlgdf dnyddaivgi aagillfilp adserrirll
      361 dwktanempw dvlllfgggl slssafnssg lslwigemak glsslpivli vaavaalvlf
      421 lteitsntat aatfipimgg vavgvgltte gdinvlllti pvalaatcaf mlpvatppna
      481 iaygsgyvki gemikggvgl nvigiflitl tvfllavpif gltv
//
LOCUS       WP_284625419             927 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Escherichia coli].
ACCESSION   WP_284625419
VERSION     WP_284625419.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 927)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..927
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..927
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=104137
     Region          22..443
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          512..927
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mrnlcflltl vatlllpgrl iaaalpqdek litgqldngl rymiyphaqp kdqvnlwlqi
       61 htgslqeedn ergvahfveh mmfngtktwp gnkvietfes mglrfgrdvn aytsydetvy
      121 qvslpttqkq nlqqvmaifs ewsnaatfek levdaergvi teewrahqda kwrtsqarrp
      181 fllantrnld repiglmdtv atvtpaqlrq fyqrwyqpnn mtfivvgdid skealalikd
      241 nlsklpanka aenrvwptka enhlrfniin dkenrvngia lyyrlpmvqv ndeqsfieqa
      301 ewsmlvqlfn qrlqeriqsg elktisggta rsvkiapdyq slffrvnard dnmqdaanal
      361 maelatidqh gfsaeelddv kstrltwlkn avdqqaerdl rmltsrlass slnntpflsp
      421 eetyqlskrl wqqitvqsla ekwqqlrknq dafweqmvnn elaakkalsp aailalekey
      481 ankklaayif pgrnlsltvd adpqaeissk etlaenltsl tlsngarvil aksageeqkl
      541 qitavsnkgd lsfpaqqksl ialankavsg sgvgelssss lkrwsaensv tmsskvsgmn
      601 tllsvsartn npepgfqlin qrithstind niwaslqnaq iqalktldqr paekfaqqmy
      661 etryaddrtk llqenqivqf taadalaadr qlfsspadit fvivgnvsed klvalitryl
      721 gsikhsdspl aagkpltrat dnasvtvkeq nepvaqvsqw krydsrtpvn latrmaldaf
      781 nvalakdlrv nireqasgay svssrlsvdp qakdishlla ftcqperhde llmlanevmv
      841 krlakgiseq elneyqqnvq rsldiqqrsv qqlantivns liqyddpaaw teqeqllkqm
      901 tvenvntavk qylshpvnty tgvllpk
//
LOCUS       WP_284625615             117 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Acinetobacter
            baumannii].
ACCESSION   WP_284625615
VERSION     WP_284625615.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 117)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..117
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13095
     Region          11..112
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mantenkcev tvngktypch ismamdlvgg kwkgvilyyl kdgpkrfnei nqlmptitem
       61 tlspqlkqle qsglisrtvy gekapikvvy emtelgqsfk pvleslslwa htmiqqs
//
LOCUS       WP_284625637             516 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Acinetobacter baumannii].
ACCESSION   WP_284625637
VERSION     WP_284625637.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..516
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=57446
     Region          16..456
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mvtkprtntr trktqevahi ydtfivgagi sglaaaikln eagltnfkii ekasrvggtw
       61 rentypgcgc dvpsalysys fapsakwshl farqpeilsy ledvsrefdi esliefntel
      121 lkaewdnvkn vwkletssgl yiaktvlfat gpiteaqipr legldtftge mfhsakwnhd
      181 ydltgkriav igtgasaiqf vpqiqpkake lfvfqrtapw vlpkpdtdlg elsksiiaky
      241 pkiqatwrqt vagalnvinf glrnpkalkp vnfaakqllk lqikdpvlrk nvtpnfdigc
      301 krilfannyy palqasnttl iphglvkveg ntviaanger hevdviiwgt gfevshppig
      361 krvhnekgec laelwkdssp eaylgtnien vpnaflmlgp nvlvydsfig laeaqlqyiv
      421 dgllqmkakg iaklsvksei ikkhnelvqk hlqttvfnsg gcksyyldan grnfaawpws
      481 lkklrqrlhh lnleeydviy eadlvkvkpk veevag
//
LOCUS       WP_284625704             371 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Acinetobacter baumannii].
ACCESSION   WP_284625704
VERSION     WP_284625704.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..371
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41715
     Region          1..364
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mhiaiigagi sglmsalelv eqgctisifd qqqagqaasw agggilspmy pwryvhavnq
       61 laqfgkasyq awnqklypit gidfeihdtg mlifdeedfd vglsyaeqhq epmqrceylq
      121 rdaleqvnph isdqfqeaiy fpelsnirnp rvlqslisyl kqhpnveffe ntpvkkliqq
      181 gdaiqalqte dgrkhtadhf vitsgawshy wnsqlqleip vepvqgqmll fktpahwlpt
      241 mcmnrvmyli prmdghivcg ssmahrgfdt stdettqqni leaclemvpe ladfpivhrw
      301 aglrpsspng vpyigkmpem dnlwanfghf rnglcmgags aqllrqlmlg qptlvdakay
      361 sperlqnkil a
//
LOCUS       WP_284625911             243 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Kingella
            negevensis].
ACCESSION   WP_284625911
VERSION     WP_284625911.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..243
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26848
     Region          32..237
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mlyiknliyw tiltlsmpim ficvifalpf dkgvnkvgla wvkmllwvlk nivglnyvvr
       61 gaenipstps iicakhqsgw etlalqeifp lqiyvakkel fnipffgwgl klaktigidr
      121 kagakatqml leqgmarkne gfwiaifpeg trmpagergr yklggarmak lfemdlvpva
      181 hnsgeywarn aflkypgtie vvigkpiahg sgdeaalmaa cedwietqqv eisgkgpcak
      241 kaa
//
LOCUS       WP_284625927             254 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Kingella
            negevensis].
ACCESSION   WP_284625927
VERSION     WP_284625927.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..254
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=29465
     Region          4..>230
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mlilkafkfe lipngeqirk lkqfcgcsrf vfnralayqn eqyeadksfk fsyakianll
       61 pewkrelvwl kdchsqvlqq alkdleasfk nffakrsdfp kfkrkgekds frfpqgckle
      121 qhnnriylpk mgwvryrnsr aisgslknvt vsqkcgkwyv siqteweiet pkpnggeigi
      181 dmgivrfatl sngeyfepin afknlkgkla klqkrfknkt kfsknwqklk akiakklaek
      241 fgscaiafki svvs
//
LOCUS       WP_284626097             734 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Kingella negevensis].
ACCESSION   WP_284626097
VERSION     WP_284626097.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 734)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 734)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 734)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..734
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=81125
     Region          67..734
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mklkhlslli ctlgasiata apveqqdlqt ltvtskrvra lskntggdlr dtanlgllgk
       61 tnsfqapitv vnydakvinn teartlvdvi akkdvstwqf ggetntltgl yfrgfqldar
      121 qfsvnglagm ygtqgtasvh vgsaqlikga stavtgmdpe gavsgamnie tkkasnkgnr
      181 disaawfsds raqiaadvgq rfgeskewgl rvngkmrhgd tpregydedn kefaingdyy
      241 gerlrlslds iyakrktngg rgriqdiqna qgrlfnaldg knnlapswqa qttrsttnma
      301 tfeydvaena mitggvgynd aryygnfasp taetsgltyk sgearltdqr fktlsmnlaa
      361 rgdfntgsis hswnaafdri nrkrltytgv nktksvsinp aldlsaqlnr lnsnlgtawq
      421 nnpttdtkiv vnslalsdtl gfknneyrlt lggryqmvkq ddhkeklsad asrfspmvma
      481 awvpnssltv ygnymedlep vsprsdedgn stmtdprvsr qfeigvrknw gsfvttlnaf
      541 qitrpgywyg kanskdktkt ddfkalgnav yagkaqgker nrglefniys slfnntvrps
      601 fglmylqshl kdypnykdnl ingvqvanpr ivakanvewd tpfvkgltln agvqhygksy
      661 qdtqktyafp sytlvdigak ysmnlrnkqr vsvsgavenl fnknywqvqr gqydrsfavl
      721 gmprtfwvka dwsf
//
LOCUS       WP_284626169              77 aa            linear   BCT 25-DEC-2024
DEFINITION  transcriptional regulator [Acinetobacter baumannii].
ACCESSION   WP_284626169
VERSION     WP_284626169.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008341
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..77
                     /product="transcriptional regulator"
                     /calculated_mol_wt=8522
     Region          11..68
                     /region_name="YdaS"
                     /note="DNA-binding transcriptional regulator YdaS,
                     prophage-encoded, Cro superfamily [Transcription];
                     COG4197"
                     /db_xref="CDD:443351"
ORIGIN      
        1 msqdlvtiyv klvkffggqt ktakallvtq psvnawingk sqmsekialr aervtkgrfk
       61 ahklcpslke fekqlvs
//
LOCUS       WP_284626555             703 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Acinetobacter baumannii].
ACCESSION   WP_284626555
VERSION     WP_284626555.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 703)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 703)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..703
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=78276
     Region          56..703
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mkrsvlfiss vgvmtshvya leadqqavtn lptisvkadk eislkqevgq assatkglmq
       61 lkdvpqivnv vpkqvlreqt vtsmqgalqn vaglsfsvgd gqrdqvmirg fsaitdnyvd
      121 girddalyfr dmsnveriev lkgpasvlyg rgsagglvnk inkkpidqsl revsligstt
      181 gqrraevdvn ekvaenvkvr ltgavedsdg yrdqaflkrq avapsvqwdi tdktklllqa
      241 dylhdnrlad qgfptdpitg kpvktnpktf ygalngkevg dvdteissqt isldhefndn
      301 fkyhgavrhy nysldrqysv vshqdpdknk lpadqiqlsq nkrirnedgi yvqqelsalf
      361 ntgflkhntl igaeyskqhk deilwqgakt ttdlynpkle ywvpintgtt tarnnnsntf
      421 enygvylqdl mtvtdqlkvl vglrydnlsq drddktstnl dlnrtdntys prigvvyqpv
      481 nnlslytsyn rsfqpladsf vfyqnsddlr ptktenyeig akwdvndqln vtlalfemsq
      541 tniqnqdpan pnqallageq ktkgvelslt gqltdqlsvl agysymdgki eksaigftgn
      601 hsaltpndta nlwlkyqind hwyaavggrg essrfsapdn knvlpgyavv naalgyqser
      661 ydvnlnlnnl fdrdyfvsgh sgandsnmmg dplnaqvalr yrf
//
LOCUS       WP_284626955             449 aa            linear   BCT 25-DEC-2024
DEFINITION  cytochrome b [Kingella negevensis].
ACCESSION   WP_284626955
VERSION     WP_284626955.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Tolkatchev,D., Yu,L. and Yu,C.A.
  TITLE     Potential induced redox reactions in mitochondrial and bacterial
            cytochrome b-c1 complexes
  JOURNAL   J Biol Chem 271 (21), 12356-12363 (1996)
   PUBMED   8647838
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Howell,N.
  TITLE     Evolutionary conservation of protein regions in the protonmotive
            cytochrome b and their possible roles in redox catalysis
  JOURNAL   J Mol Evol 29 (2), 157-169 (1989)
   PUBMED   2509716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..449
                     /product="cytochrome b"
                     /GO_function="GO:0008121 - ubiquinol-cytochrome-c
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=50049
     Region          5..417
                     /region_name="QcrB/PetB"
                     /note="Cytochrome b subunit of the bc complex [Energy
                     production and conversion]; COG1290"
                     /db_xref="CDD:440901"
ORIGIN      
        1 manqtnnkak alldwvdtrf pltklwndhv gqyyapknfn fwyffgslal lvlviqivsg
       61 ifltmnfkpd gttnaqnlpv afaaveyimr dvsggwiiry mhstgasfff itvylhmfrg
      121 liygsykkpr elvwvfgsli flalmaeafm gyllpwgqms fwgaqviinl fsaipvigpd
      181 lstwirgdfn vsdatlnrff alhviavplv llglvvahli alhevgsnnp dgveikklkd
      241 engipldgip fhpyytvkdi lgvvvflivf csvmffkpdg ggyfleapnf dsanplvtpa
      301 hiapvwyftp fyailraips flgtqvwgvi gmgaavvlia llpwldrgev ksvryrgpif
      361 ktalvlfiis figlgilgam vatdtstlva rilsivyfaf flgmpfytki dknlpvperv
      421 tmstpkqkim ffvyvaitvi gsylfatii
//
LOCUS       WP_284627057             207 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Kingella negevensis].
ACCESSION   WP_284627057
VERSION     WP_284627057.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..207
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22318
     Region          7..100
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mnvtqnvvli hglytspvim rvlgkrlseq gfvphyfaya ttkqnlhqha lalanwlrek
       61 qlvpchfvah slgglllqhl advapelfqa rvvtlgsphr gsltakwvhg fqaallggaw
      121 qdaldgslpe kplpvlcgni agcaengvgk lvlklpqpnd gtvaleetrl pesvpllvhc
      181 ghtdllfnkd vaqqtgyflq ngcfqaa
//
LOCUS       WP_284627360             600 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Kingella negevensis].
ACCESSION   WP_284627360
VERSION     WP_284627360.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19961245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..600
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=68506
     Region          <199..578
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          293..324
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          331..356
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          450..476
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(452..453,456..457,459,483,486..487,490..491,
                     493..494,520,523..524,527..528,531)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          454..585
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          481..514
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          519..547
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          552..578
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkplfhqria plaaaillaf sgsvyaands gpvdskqkie qeertrkeea akrtdhiftl
       61 lfgeialten rlseslgsyv nvynrsqspe vaerimeist qvraynvaet iyqkwrasep
      121 npspalrrwg wvraisnnql dvamadmkqv faeansdeqr skllailaey alqspnkaeg
      181 issqviqlar eysdlpesal veviyngnkg aqvmsalkrl atldkdispt tmrilfheln
      241 knpdllttff kktdssklap iwrelevenl iasgqydaae qkiqkllnee tksanvyfqa
      301 arlhmyqgad idivakyyqq ayehgndddk araainmsvq yasmsdwrna edwaqriths
      361 hylfdkwsll tmiadkqqnw qktyeyskea fkhptysdsi fsildlqgay lrsmsqvlpq
      421 kkllaelnah manleksqqs vlktellmia lefranlysl msqpekgiad lrkllaldpd
      481 namfknnlgy vlleskpsky mnealpliqa aydaepnnvm yndslgwayy kkgqaqmalp
      541 ylefaydnle naevashlge vywalkqpek akeiwqkawi qspkdkylln tlkrfkvqfk
//
LOCUS       WP_284627526             466 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Kingella negevensis].
ACCESSION   WP_284627526
VERSION     WP_284627526.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..466
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52983
     Region          94..439
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mctvffvsfg lwavqtrmse thsrqmrnme stlllntlit lqaqgedgvr rlfqrwedlp
       61 askniivisg rgkhnilnrk iseeeinqay nyslqnrnst lafvyydpfg eeyllfvrhf
      121 dqpkvermpt lmipglpiap iwhefivvgv ifvigltlay liannvakpi silengmnrl
      181 asgelttrvs hqlddrkdel aslgiqfdrm aaqlqqlvek erhllhhvsh emrsplarlq
      241 allglmqarp ekqneyiakl eseltrmdnl vgelltlsrl etanmameke plpivpfmeq
      301 lvedsqavae qrghhitldt gslkeearlq anesylyraf dnvirnamny spegstikiq
      361 mhedrknlhv eitdngpgvk pdqlphifta fyradssank pgtglglait khiaeqhcgk
      421 lfaenvqpng lkmhfvfpkt tvpkhskkne eqteeyqpdh sgslke
//
LOCUS       WP_284627413             105 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Kingella negevensis].
ACCESSION   WP_284627413
VERSION     WP_284627413.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 105)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 105)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 105)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..105
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11998
     Region          16..89
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(23..25,39..41,50..53,55..56,59..60,62..63,69..71,
                     76..78)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(39,42,85)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mvheqtiakl recipafvml gdenrlkims llyqhgelsv neltehlhls rpavshhlkl
       61 lldaylvtvr qegtaryysa nfdcavrlld ellvlmkmqq lqtpk
//
LOCUS       WP_284627652             216 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Pseudoglutamicibacter
            albus].
ACCESSION   WP_284627652
VERSION     WP_284627652.1
KEYWORDS    RefSeq.
SOURCE      Pseudoglutamicibacter albus
  ORGANISM  Pseudoglutamicibacter albus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Pseudoglutamicibacter.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Pseudoglutamicibacter albus"
                     /db_xref="taxon:98671"
     Protein         1..216
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22768
     Region          71..208
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mdhtgmnasi tpnprygrra vlgfmlataa agltacstes snlanqnkeg sgkgyvagdg
       61 svseyapedr gepveftget fsgtkidaas yaagdvlvln fwyaacspcr veapalkava
      121 defkdkgvtf lgvnvrdeka aaeafektfk ipyesvrdle ggvllalsqy vppqavpttl
      181 vldpnrrvsa rvlgvveest lraliktaqe tpadtk
//
LOCUS       WP_284627719             626 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Pseudoglutamicibacter
            albus].
ACCESSION   WP_284627719
VERSION     WP_284627719.1
KEYWORDS    RefSeq.
SOURCE      Pseudoglutamicibacter albus
  ORGANISM  Pseudoglutamicibacter albus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Pseudoglutamicibacter.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 626)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Pseudoglutamicibacter albus"
                     /db_xref="taxon:98671"
     Protein         1..626
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=67231
     Region          10..328
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
     Region          357..>568
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msksnikpvs paakavglmr vltstriglt aamlrdripd yqglsdaafe raferdksrl
       61 rslgieltve kleadalgev ryridlpahr lpelhlsdqe rlvtalaaaa vggsgwgsha
      121 rrasvrlggv sasspgvgag araelssppd aaealilaal ceypvsfdyr aangehterr
      181 ilpwgvgqqa grwyvfggdi erggermfrl driqgsvaqa nvrkaemvhe iygrpdkflm
      241 rdelarlthr dllqevwval aegagaelka rgrsmvkdrg vevvavngvy sdvvrecaav
      301 gaavvgpgdv aqdiadtali eaalaahdsa gedqssprlr lsaggrpstd qvladvisla
      361 sviqsegaqd idelatrfav prseierwla tlelgahive dvstdqasfg lrldgntvel
      421 sadealtypl nvslqeatal llgcellmsv pglepsvhda adavvekltq araqlndfsa
      481 ivaiesgqlr getlrlaeml gqaiaeqrta hmryasfeat ternidpltl vrfddklyvr
      541 awchlrgger tfnverivnl evtdkqatht lsdehpatst gfasgggfvg ggrgteallg
      601 fgrdsqwmvs sfrpsvtrrt dtevia
//
LOCUS       WP_284627743             516 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Pseudoglutamicibacter albus].
ACCESSION   WP_284627743
VERSION     WP_284627743.1
KEYWORDS    RefSeq.
SOURCE      Pseudoglutamicibacter albus
  ORGANISM  Pseudoglutamicibacter albus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Pseudoglutamicibacter.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Pseudoglutamicibacter albus"
                     /db_xref="taxon:98671"
     Protein         1..516
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=53875
     Region          4..414
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
     Region          <402..454
                     /region_name="PHA03264"
                     /note="envelope glycoprotein D; Provisional"
                     /db_xref="CDD:223029"
ORIGIN      
        1 mwgallaavv tagsilvpva psvaagnass wfdkelgyak lrdqgldgag vtiaiaetgv
       61 dlkspdlqga diefvpmpde clpireasks aidldggtye esvahgtqva tmivgqggdg
      121 riqgvapkak llvmeqpfal tpgssgwpsg cdemvvlggg rmmeaeklga dimsmsqlgp
      181 tqptsyqnay wqmrgkalit gagndgkvta esaglpgvvs vtaskpagaa tnwaaagkgl
      241 tvaapgeklt lreadgklvs ngagtsfssp ivagtlalgr qkwpdatyhq lihsltetas
      301 nggrqsselg fgvidpvafi dndpmqypde pitypgmand dpqwdvvrql cdgfaddstm
      361 aypehykvda gldpeavvwl pqvakdegwl gmapnagvwg ngsdtpsdve paddvavppv
      421 tpatpaqpvt paqpagfptf vvigiaagvi vvlaliivma rrknrtahag psqqyppqqy
      481 ppqefapnqq qyygdpnqqq wqepggqqwr qptnhq
//
LOCUS       WP_284627778             430 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Bacteroides ovatus].
ACCESSION   WP_284627778
VERSION     WP_284627778.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..430
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48712
     Region          31..430
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mrikgffyil vflllalgsv llflssqlnt iffyigegli lfiliyltff yrkivkplnt
       61 igsgmellre qdfssrlspv gqyeadrvvn ifnrmmeqlk nerlrlreqn nfldllikas
      121 pmgviitsld edlselnpma lkmlgvrled vqgkkmkeid splavelanl pkgekvtarl
      181 ndsniyrcth ssfidrgfqh pfylvetltd evmkaekkay ekvirmiahe vnnttagits
      241 tldtveqals seegmedicd vmrvctdrcf smsrfitrfa dvvkipeptl ssvnlndlvf
      301 tckrfmegmc ndrritlrme ideslkdvml daalfeqvlv niiknaaesi atdgeiivrt
      361 lapatvevid nglgiskete aklfspffst kpngqgigli firevlmrhg ctfslrtyad
      421 gltrfritfp
//
LOCUS       WP_284627983            1043 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_284627983
VERSION     WP_284627983.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=115389
     Region          38..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksnqkgnhl yaykdtirrl flltlfsfli vesyaqnkti sgtvtdftge pvigasvlvn
       61 gttngtitdl ngkfslsnvp tkgtitityi gykkqevsva gntnfkitlq edtetldevv
      121 vvgygvqkks dvtgamarvg ekelkampvr nalegmqgkt agvditssqr pgevgninir
      181 gqrsinaeqg plyvvdgmvi qnggieninp sdieaidilk dasataiygs rgangvilvt
      241 tkkgkegkvt lnysgtvtfe tlhdvtemms aaewldyarl akynagsyas atptyeadka
      301 afgsvtaswk niekawvngv ydpslvgsyd washgkqtgi thehtlnasg gsdkfqgyas
      361 fgyldqkgtq pgqayerytl ktsfdvtpan wfkmgssina systqdygys fsksvtgsgd
      421 fysalrsmip wtvpydenge yvrypsgdvn iinpireldy ntnqrrtfra saslysqidf
      481 gkiwkplegl syrlqfgpef qfytlgvana adgingdgnn gaqykneqkr awtldnliyy
      541 nkalgqhnlg itlmqsasay hyemgdmrat nvassdelwy nigsagtlns fgtgltetqm
      601 asymirlnyg ykdkylltas mrwdgasqla eghkwasfps aaiawrmdqe gflkdiswln
      661 qlklrigmgv tgnaaikaya tkgaitglyy nwgqnesslg yvpsdpsqke pakmanptlg
      721 werttqynvg vdygffnnrl tgsidayktk tddlllkmsi psltgyvsty anvgktsgyg
      781 idlqvnaipi qtkdfswstt ltwsmdrnri delsngrted vnnkwfvgee igvyydwvyd
      841 giwkteeaee aakygrkpgq ikvkdlnndd tidanddkki vghtrprwtg gwsntfsykn
      901 felsffilsr wgftvpqgav tldgrymqrk idywvagtne nakyyspgsn gegadafnsa
      961 mnyqdgsyik vrnislgynf tpqqlknlgi nnlklyvqam npfniykacd fldtdlvnyd
     1021 nntktfgspt tlksfvigvn igf
//
LOCUS       WP_284628049            1876 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Bacteroides ovatus].
ACCESSION   WP_284628049
VERSION     WP_284628049.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1876)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1876)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1876)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1876)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1876
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..1876
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=208801
     Region          520..1876
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mgqtkttrsi satglfllim mtvglysctr tqkdiipsad yapyvnaytg gvisqnstir
       61 ielthdqpmv dlnnelksnp fsfspslkgk aywvsnntie fvpeegalkp gtlyegtfrl
      121 gdfievdkkl kefnfsfrvq ernftlqles lpitatqpne inmkgeirfs dvvkkeevek
      181 mltasdgkks ypvevtatdn htrylfsirq ipreaddypl titangnpag idrkqteevl
      241 ipakdcfrfm saeridqpen gieivfsapl sttqdlkgli eipeisssif qisenrvfiy
      301 feantqnklt lnihegvkds qgkalgtsht isfsevslkp qvemsttaai lpdsksliip
      361 fravnlyavd lsvirifenn vlmfmqtnsl asanelrrsg rlvykktlwl akdaskdihh
      421 wgdysidlag lihqepgaiy rvilsfrqey saypcgggen qdmkfadsst sdgltkvsgs
      481 vlseedeaiw ntpeayyyyn ggtmdwsvyr wterdnpchp syymdsdraa acnvfasnlg
      541 mivkrnslnk lwiavsnild tkpigkaqvt aynfqlqpig kgetngegfv eitpngvpfi
      601 ivaesdkqka yvrvvdgeeq svsrfdvggk diqkglkgfi ygergvwrpg dtlhisfile
      661 drekripdkh pvaleiynpr gqfytkmist qgmngfytfd vptqatdptg lwnayikvgg
      721 ttfhkglrie tikpnrlkin lalpkvlqat dknfyaplts twltgatask lkakvemsls
      781 kvntqfknyg qyifnnpatd fttiktdifd gtldaegkan vtlkvptate apgmlnatft
      841 trvfepggda siytqtipfs pftsyvginl nqpkgkyiet dkdhvfdivt vntqgqlvns
      901 snleykiyri gwswwwensg esfgtyinns sitpvasgnl qtrggkasfk fridypswgr
      961 ylvyvkdkes ghatggtvyv dwpewrgrss ktdpsgikml afslnkdsye igetataiip
     1021 aaaggralvs iengstvlrq ewievsnggd tkytfkitpe mtpnvylhis llqphaqtvn
     1081 dlpirmygvv pvfvtnsqtv lqpqiqmpev lrpetnfnvt vsektgkpmt ytlaivddgl
     1141 ldltnfktpd pwndfysrea lgirtwdmyd nvlgasagsy sslfstggda tlkpadakan
     1201 rfkpvvkfig pfylgkgksq thtlklpmyv gsvramvvag qegaygnaek tafvrtplmm
     1261 lstlprvlsi qeeitvpvni famenqvknv tislqtsggg vqivganqqs lkfsqpgdql
     1321 vfftlktgsk tgkatihlta ngggqqtket ieievrnpnp vvtlrnsqwv eagqskelsy
     1381 nlssssannq iklevsrips vdisrrfdfl ynyqhhcteq ltskalpllf vgqfktidki
     1441 eaekiktnvq eairqiygrq lpnggfvywp gnavadewis syagmfltla qekgyavhsn
     1501 vlnkwkrfqr aaaqnwrmpq dasgwqqwqs elqqafrlyt lalagapeyg amnrmkeqag
     1561 lsiqakwrla atyvltgkmk paeelvynae ttvspyssmn qiygssdrde amiletlilm
     1621 nrerdalqqa kvvsknlsqe ewfstqstaf almamgrlae klsgtldfvw twndkqqpav
     1681 ksakavfeke iattpksgmi avknqgkgal svdlitrtql lndtlpaisd nlrmdiryan
     1741 lngtpisvnd iiqgtdfmai tsisnisgts dytnlalthi ipsgweiyne rmvapetesg
     1801 aadgsgksvs kynyldirdd rvltyfnlrr getkvftvrl qatyagnfil pavqceamyd
     1861 vnvqarnkag rttvsr
//
LOCUS       WP_284628088             349 aa            linear   BCT 25-DEC-2024
DEFINITION  sialidase family protein [Bacteroides ovatus].
ACCESSION   WP_284628088
VERSION     WP_284628088.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 349)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468221
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..349
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38093
     Region          2..321
                     /region_name="NanH"
                     /note="Neuraminidase (sialidase) NanH, contains C-terminal
                     autotransporter domain [Carbohydrate transport and
                     metabolism, Cell wall/membrane/envelope biogenesis];
                     COG4409"
                     /db_xref="CDD:443531"
ORIGIN      
        1 mfsagddnvn syripsllta kdgsllvfce arreswkdks rtdivvkrst dngrtwsamq
       61 dltqgttgay mdptplldsa tgriflfttf wpaddhtgtk nrailltsdd ngctwaapvd
      121 vtgtlmpkgs riygfgpgag lqmvgekyrg rlilparvse vtgekahdva iysdnhgktw
      181 kmggngdndd efqiaespag vlvynarvpk armvsfsvdg getwskavke lalpgvskgc
      241 qasvlgkgkt lyfsgiqgip etseyderak ltlyksedgg rkwdngllly dkaagyscms
      301 flpdgrmaii fetadtqsft rkslpntkpl krpddwmkld lilvpvinl
//
LOCUS       WP_284628094             432 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Bacteroides ovatus].
ACCESSION   WP_284628094
VERSION     WP_284628094.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..432
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=48805
     Region          171..410
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mtnkvtafhl llaaqfalia asmfvnikig lfsmvlillf tticliqlgn dertnwkpgq
       61 nimtyffivw llfyileiln pnnvmaawni nltpyaltpl icafvvpivi rtkkdielll
      121 iiwsifvlif tlkgywqknh gfsskdlyfl hvvggarthi iwsgiryfsc fsdaanygvh
      181 aamstvtfai asffvdsrwk riyflfiafc giygmgisgt rsamgvlmgg mlmitviakn
      241 wkallggifi sisifaffyy tnigsgnqyi hkmrssfhpt edasylvrve nrmrmkelma
      301 kkpigygvgl stgnfepkeq mpyppdswlv gvwvetgivg lilylgihgi lfawcswllm
      361 fkvrnkslrg lvaawlcmda gyfiaayvnd vmqypnpltv yigfalcfaa phidkrisee
      421 ekekglvatq kn
//
LOCUS       WP_284628438             291 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium accolens].
ACCESSION   WP_284628438
VERSION     WP_284628438.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..291
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28734
     Region          11..286
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mgssvaeiag ilatiriprt vlaivvgaal glagtlvqgl trnpladpgl lgvnagaalf
       61 vaagiflfgl tsmqshlfla flgaglaall vfglsaggig rgdtlglvla gsalsavlaa
      121 atsaivyidp naldtlrfwq agsvtgrgfd iitpalvpla igavlalalg ptlnilnlga
      181 eaaqalgtnv aranilglva itllagaata aagpigfigl vvphvargit gpdykwvtpy
      241 salagaclll gadivgrlim rpgelqagiv iallggpafi wlvrhrtvvs l
//
LOCUS       WP_284628557             359 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium accolens].
ACCESSION   WP_284628557
VERSION     WP_284628557.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..359
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36026
     Region          50..350
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msattkdgqt iqtgstaqnp tatpvmargk grktflvali lvslavavas lalgsrsipp
       61 deviaalrga geqdirdivw nlrmprtfla yfagaalava gvlaqswtrn pladpgfigi
      121 tagasffval gtaigiattt gmrttlalvg agittllvla vsrrfqdplt lilvgagvsa
      181 algsgaviig lystdvldsm rrwtigstfg rgpedvaiag iglliglaca amaarpldll
      241 amgeesslal ggspttarvg aalsvvvlag sataatgpia fvgfaiphiv rrvvgpsvat
      301 milpsallgg cavlaadiig rlivgnsele msivlaivga pfliwgahrg vgrawgdna
//
LOCUS       WP_284628559             344 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium accolens].
ACCESSION   WP_284628559
VERSION     WP_284628559.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..344
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35299
     Region          13..344
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mttissilqa qqrrrhvrvl astlvfglia laaylvllgq gplelsprqv ldvltgggse
       61 shirvvwdlr lpvaiatviv gaalgvagsw tqtmarnpla spdilgvtgg asvlvvlgtv
      121 hsrpgfaddi pdfwwracla mcgallvvil lavlggigts nrivivgial slmfqavvay
      181 lmrsaqiqra aeaqtwlags tgfvrmeviv pllvalapfi aigiwcarel pllahddssa
      241 ttlgvnitrq rallliaatg icavvvsvvg pigfiallap hlarmvartp tpspvasaaa
      301 gaalltvcav iagaipvnap vgavssvigg calvvlvwna arrs
//
LOCUS       WP_284628636             335 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Globicatella sanguinis].
ACCESSION   WP_284628636
VERSION     WP_284628636.1
KEYWORDS    RefSeq.
SOURCE      Globicatella sanguinis
  ORGANISM  Globicatella sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Globicatella.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Globicatella sanguinis"
                     /db_xref="taxon:13076"
     Protein         1..335
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=38445
     Region          24..319
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mpigmygeee mtayeyfklt paklelakqs favviiflgi glaywqmkrk istihlnhll
       61 eyltyiargn yqlripdmqv delseivrsv nslvdstvha meeerriekt kdelianvgh
      121 dlrtpltsii gylglienkr yhseeqlley thiaykkams mqvmvndlfd yaasrlvsye
      181 vtpeevhlnf ffeqlaaefe leaaekniei einvmpknli vhfdpekmar vfnnllsnal
      241 kyghgatkik mnanqidddd qiimdvvnng ellkleelek vfqrsyradt srnsaipgtg
      301 lglgiarniv elhngiiyam iennemifri emsrl
//
LOCUS       WP_284628787             292 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Corynebacterium accolens].
ACCESSION   WP_284628787
VERSION     WP_284628787.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..292
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32092
     Region          2..274
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mtvgtisevl alegtqeadv fsgpaipsqi ertfggqvaa qalaaaqrtv dnkqvhslhg
       61 yfvgpgdtkk plelrverlr dgrsfasrqv rviqdgrlvf imlasfhrdg dtgpehqdva
      121 pqvlspdeta rrgggapyst riilkewtdw dirlvpdegr ddaaaevtga gyrhiwfrnt
      181 gelgsdpdfh raaltymsdm tlirsaliph qgekiqlasl dhavwflrpf rvdewllyeq
      241 vsptasqgta iargklfteq gelvalvnqe gltrfldenl gsgsahgnwh nv
//
LOCUS       WP_284628834             230 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium accolens].
ACCESSION   WP_284628834
VERSION     WP_284628834.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..230
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24572
     Region          1..227
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(13..14,16..17,20..21,58,62..63,66..67,91,95,102,
                     105..106,111,126,130..131,133..135,137..138,141..142,
                     145..146,165..166,168..170,172..174,176..177,179..180,184,
                     187..188,194,196)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(129,133,136..137,139..140,179,182..183,185..190,
                     193..195,199,201)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(150..157,167,170..171,174)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 myrlhpstvl tiaacgwlli lalnsplasa vvagamlayg vwatrslaiv lasaalcvpv
       61 alsmlvihap ygdnqliplv tsdglliaat lalrffalmv cfivamsvlr isdiakwlqv
      121 sraghkiayi vgaslqslpq gaqawrtvrd anqlagikvt wrntisrvvi pvisrlliqg
      181 terghalaav gfdeegtrtl lrpvpdsnls rvlryivplg tigvmvfvwi
//
LOCUS       WP_284628902             341 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium accolens].
ACCESSION   WP_284628902
VERSION     WP_284628902.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..341
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34437
     Region          25..337
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msvrttrllg lgvllllvlv gticsllyga rsipaedvwa alrdlpaasg pqdevptnqr
       61 vvaelrlprt ilaiivgaal gvagaliqgh trnpladpgi lgvssgaals vvvsfalfgi
      121 tapwatavva flgaiaatal vfglasagka avdpltlvlg gaalsavlsa itsafvltne
      181 nnldrmrfwt vgslagrdmn ialgilpfiv vglilafatg pqlnilnlgd dvaaglgint
      241 aaarlagmgi iallagaata aagplgfigl vvphivralt gpdykwilpy salagaalll
      301 cadvvgrlia rpgelqvgiv lafvgapffi aliyrkkvmt l
//
LOCUS       WP_284629136             223 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Globicatella sanguinis].
ACCESSION   WP_284629136
VERSION     WP_284629136.1
KEYWORDS    RefSeq.
SOURCE      Globicatella sanguinis
  ORGANISM  Globicatella sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Globicatella.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 223)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Globicatella sanguinis"
                     /db_xref="taxon:13076"
     Protein         1..223
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=24413
     Region          <8..181
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mkptiigvlg lgvfgrtiak qlgrfgrevi vvdkdqhnid lvaddvttat igdftdydll
       61 edigiancda vvvatgtnle savlavmhck rlgvphiivk ahsavfeqal kelgatkiis
      121 perdsgkrla sqllrthige vlslddntsi vefsvpdkwv gksilalelr knydmnvigy
      181 rpykgakmts tlniqtpien gmifvaitds hrfeehdyld rin
//
LOCUS       WP_284629312             381 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium accolens].
ACCESSION   WP_284629312
VERSION     WP_284629312.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..381
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41725
     Region          11..356
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mrtqasvkrl pqhlpeldgl ravaalgiiv thvsfqtgtg wgfagrfdff vavffalsaf
       61 llwrrrglht vrgyahsria rlapayyacv vsvllllpdv hsitptqila nltstqiyvv
      121 dglapglthl wslcvefffy lvlpllvwai gglpqrwrmg viagaavlsw gwgfipfvad
      181 ygedqvnsqi wppayaswfa vgmlaaevee rgigkrtari lqvrwawvvl aglvlwvasr
      241 dwfgpaglvh pepaefarri iagavfagcv vvpvalvprg tswlnsplmq algawsysif
      301 lwhvavlava fpltgvalfs gkpldfwvil avtvvgtvvv saasytlier pgrdllmgrv
      361 rgrgqgrrrr kgrpaprhis t
//
LOCUS       WP_284629321             440 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium
            accolens].
ACCESSION   WP_284629321
VERSION     WP_284629321.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..440
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=47214
     Region          1..438
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrmtvigtgy lgathaacma elghevlgvd vdedkiavlq sgkvpffepg lpevlernid
       61 agrlgfstdy deaaqfanvh flgvgtpqrr gsyaadmtyv kavitdlvpk lrgehvifgk
      121 stvpvgtaae lqeladslap egtrveiawn peflregyav hdtitpdriv igtresesra
      181 eelareiyaq plaqdtpfiv adlqtaelvk vsanaflatk isfinavsei ceiagadvva
      241 ladaigidkr igrkflgagl gfgggclpkd irafmarage lgadqaltfl revdainmrr
      301 rdrmvdlske afngsllghr vtvlgcafkp nsddvrdspa lsvagslsla gaavtiydpe
      361 gmdnakkvfp tldyaadtes alreaelvil atewqqfkel dpneagelvd nkhiidgrnv
      421 ldvaawsnag wkiqalgrtl
//
LOCUS       WP_284629508             530 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Corynebacterium accolens].
ACCESSION   WP_284629508
VERSION     WP_284629508.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 530)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..530
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57159
     Region          1..503
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mevllvligl mlltvfvvai gdrvglpwpa lltiitacav fvpglpqfdi ptelilpifl
       61 ppllwalarr tswgvirgqw vtilslsvll vvattlavga tayaflpgis iaaailigaa
      121 iappdpvavd avaepagipr riittlqteg lfndaasiva fhlalaavtq ggdisfgsgv
      181 lsflyssvva laigwligrl talfithvhd vvarnaltwv vpfatflvae eleasgviav
      241 viaavelnsr adiqaedrls gqsfwetmel lftgvafgli gltvntaiae vgsdlwhsvm
      301 vgvilslvaf vvrfvwmffy yrlnvsrgrp hvaplrmqev llmtwsgmrg lvtlalvlsi
      361 ptgvfafhhe lavialtvll vtmvlpglll pwlmrqldlt easqaandkm raavvsrara
      421 asidalsqfr peddatgeae tvdpeisanv iqwfedrlgd genpaennde rkqraeearr
      481 valearrtal naaqsellal rkdkafnpai vdeileeidr mvigtkhrei
//
LOCUS       WP_284629661            1014 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-mannosidase [Globicatella sanguinis].
ACCESSION   WP_284629661
VERSION     WP_284629661.1
KEYWORDS    RefSeq.
SOURCE      Globicatella sanguinis
  ORGANISM  Globicatella sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Globicatella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Globicatella sanguinis"
                     /db_xref="taxon:13076"
     Protein         1..1014
                     /product="alpha-mannosidase"
                     /calculated_mol_wt=119446
     Region          220..1013
                     /region_name="MngB"
                     /note="Alpha-mannosidase [Carbohydrate transport and
                     metabolism]; COG0383"
                     /db_xref="CDD:440152"
ORIGIN      
        1 mfefeyirkq yyklanfikk eeypihnvrl vkgdlnedyv lgtyfgqkns yytllseiki
       61 pqldvgetfw ieaysslkew dnstnpqlkl ylneelvqgl dvnhrhtvvp ekfwgqkvsl
      121 rleifsgree kqfpmyikay kidqatynty wdfrvaveaw qaieedsykl iyqetllkct
      181 klldfrqvys ddyyqrleti qsilqlnlyq kfkelssvdv yaighthidl awlwtfqqai
      241 ekgersfsti lkfmedypnf tfiqsqpqly qdikeqypel yqliqtqike grwipegamw
      301 vesdtnlisg esmvrqflyg kqyfknelgi eskicwlpdv fgysptlpqi maktntpyfm
      361 ttklswnqmn qipndsftwk gldgsevlvh fiptvsvgys ptpfyttyng mldpltlkks
      421 wdryinkdkn nfimnaygyg dggggptiem letakrleng lpgipkvkns naldffenle
      481 kssekqnfnt wvgelyfeyh rgtytsigki krqnrfaefy lqnieklytl yklenypksa
      541 lenlwkivlk hqfhdvlpgs siqevydead stfeklfasf eqlynnlfps peekndliif
      601 npngisqngy iqlkestgsl llngqkeles qqlttherly ylpnlkplst vkvgleetks
      661 eeadsrfkyn dktrqletpy ycvefdkdyq iislydkevq rmvnvdrgll nelvvyedip
      721 mdydawdidi yypykrwtir hlnsvkvken gslifsllia rhyqhstiqq emifhaysrr
      781 idfktevdwq enqqllraef nvdihtyest hdiqfgnikr pvhrntswdi akfetcahkw
      841 idlseedygc almsdckygy nteyqklgis likspidpyp kadigyhqfs yslyphlgdw
      901 knsdvvaesy qlnnplvvlp vaknqqiqsp piefdndaii idtlkqsedg kgiivrlfdf
      961 kgrrsklnak vissftkvye cnlleeiete lridsnnhfm cevkpyeikt ikli
//
LOCUS       WP_284629704             454 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Corynebacterium
            accolens].
ACCESSION   WP_284629704
VERSION     WP_284629704.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..454
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=48428
     Region          5..241
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mtlklnffak sdrglirgnn edsgyagshl liladgmggh aagevasqlm vnhleildqd
       61 pgkedteall aaaaddanea isehvtahpe tegmgttlst mlfngttfgv chvgdsrayl
      121 lrdgkleqit kddtyvqslv dkgelaaedv sshpqkslil kaytgravep tlftfeakag
      181 drillcsdgl sdpvtastie talgqgsieq agstlvdlai rsggpdnvtv viaevteekp
      241 athepfrvga lagsveepth pdssasraak ltrkpqvipp avmadednaa kdsdeeeaed
      301 epsrrkigwr llialiiila lvigaglwvk nflsnnyyae tndaqeitil kgadysvfgk
      361 dlssthqyvc indknsllfs aqkckgdftp lkvsdlpese rgavnhisag dlskvqdqin
      421 dlgekalkpc itapsqkdnk dtkenkpgvt crev
//
LOCUS       WP_284629908             230 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium accolens].
ACCESSION   WP_284629908
VERSION     WP_284629908.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..230
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24556
     Region          1..227
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(13..14,16..17,20..21,58,62..63,66..67,91,95,102,
                     105..106,111,126,130..131,133..135,137..138,141..142,
                     145..146,165..166,168..170,172..174,176..177,179..180,184,
                     187..188,194,196)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(129,133,136..137,139..140,179,182..183,185..190,
                     193..195,199,201)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(150..157,167,170..171,174)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 myrlhpstvl tiaacgwlli lalnsplasa vvagamlayg vwatrslaiv lasaalcvpv
       61 alsmlvihap ygdnqliplv tsdglliaak lalrffalmv cfivamsvlr isdiakwlqv
      121 sraghkiayi vgaslqslpq gaqawrtvrd anqlagikvt wrntisrvvi pvisrlliqg
      181 terghalaav gfdeegtrtl lrpvpdsavs rvlryiipig tigvmvfvwi
//
LOCUS       WP_284630073             311 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Globicatella
            sanguinis].
ACCESSION   WP_284630073
VERSION     WP_284630073.1
KEYWORDS    RefSeq.
SOURCE      Globicatella sanguinis
  ORGANISM  Globicatella sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Globicatella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Globicatella sanguinis"
                     /db_xref="taxon:13076"
     Protein         1..311
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34906
     Region          1..293
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mnhlyiiani qagsgngadv lnqaqdylrk frapfitltt eykghsielt qqilakaeqr
       61 tidtiivvgg dgtlhevvat lkkakqtipi iylaagtgnd fkrtwspnas vestlqkylf
      121 hrqittvtif esynhltknt divlnslgfg ldgkviyevn ttpqdaffhq flngkfsylv
      181 nvfkavrkld hfdvhltvdn qtiefencql islmnspylg ggiqlsndik adekiinvva
      241 iknvkpinli klmwqilvsk ttpaaehyfy tkgekvtiqi eepilsqvdg ellnkdqahl
      301 tltlteypfy l
//
LOCUS       WP_284630163             457 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Globicatella
            sanguinis].
ACCESSION   WP_284630163
VERSION     WP_284630163.1
KEYWORDS    RefSeq.
SOURCE      Globicatella sanguinis
  ORGANISM  Globicatella sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Globicatella.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Globicatella sanguinis"
                     /db_xref="taxon:13076"
     Protein         1..457
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49839
     Region          1..445
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mvvdlfqmid dfiwgpplli llvgtgiylt fvlrgiqfnq lfhslrlifk netdsdgdis
       61 sfaalcttla gtvgtgnivg vataiaiggp galfwmwfaa lfgmatkyse gllavkfrvk
      121 deqqhvsggp myyilngmgq kyrplatmfa fsgilvalfg igtftqvnai tealhnqfal
      181 snlltgfila llvmlivfdg itiiskvasf ivpfmallyi aaclfiiian wqllddslll
      241 viqsaftkta atggfvgstm kaaiqngiar gvfsnesglg sspiasaaak snsaveqglv
      301 smtgtfidti iictltgivl iitgawqtef rgasmtqyaf nayfseygtf iltislslfa
      361 fttilgwnyy gercfeflfg lkyiryyhlf fvsmvfigsf lnldlvwiia divnglmaip
      421 nlislialsp iiinetrayv kakqynnvtr lepikyy
//
LOCUS       WP_284630169             236 aa            linear   BCT 25-DEC-2024
DEFINITION  tRNA (adenine(22)-N(1))-methyltransferase [Globicatella sanguinis].
ACCESSION   WP_284630169
VERSION     WP_284630169.1
KEYWORDS    RefSeq.
SOURCE      Globicatella sanguinis
  ORGANISM  Globicatella sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Globicatella.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Hori,H.
  TITLE     Methylated nucleosides in tRNA and tRNA methyltransferases
  JOURNAL   Front Genet 5, 144 (2014)
   PUBMED   24904644
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Roovers,M., Kaminska,K.H., Tkaczuk,K.L., Gigot,D., Droogmans,L. and
            Bujnicki,J.M.
  TITLE     The YqfN protein of Bacillus subtilis is the tRNA: m1A22
            methyltransferase (TrmK)
  JOURNAL   Nucleic Acids Res 36 (10), 3252-3262 (2008)
   PUBMED   18420655
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Globicatella sanguinis"
                     /db_xref="taxon:13076"
     Protein         1..236
                     /product="tRNA (adenine(22)-N(1))-methyltransferase"
                     /EC_number="2.1.1.217"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0160105 - tRNA
                     (adenine(22)-N1)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26671
     Region          5..236
                     /region_name="TrmK"
                     /note="tRNA A22 N1-methylase [Translation, ribosomal
                     structure and biogenesis]; COG2384"
                     /db_xref="CDD:441950"
ORIGIN      
        1 mnseklsprl akvceflvhy qkdairladi gsdhaylpch lalnkqlefa iagevvegpf
       61 qsakaevatr gltkvidvrk gdglavitea dqinaiticg mggslirnil denkaiiren
      121 tvlvlqpnma syqlrkwlnq ngfvflnetv vedhhreyei mvvkknhyhk qiltvnelqf
      181 gkynledpta afyqkwqkel sllettyqsi vkkagadhpk vqlmqeeinq ikevln
//
LOCUS       WP_284630317             550 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Globicatella sanguinis].
ACCESSION   WP_284630317
VERSION     WP_284630317.1
KEYWORDS    RefSeq.
SOURCE      Globicatella sanguinis
  ORGANISM  Globicatella sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Globicatella.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 550)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 550)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 550)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Globicatella sanguinis"
                     /db_xref="taxon:13076"
     Protein         1..550
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=60208
     Region          1..526
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mnkinksiqs fligalgifi fimplltlfa lafeteggfs lqnfnaifss srsglaiknt
       61 livggastvl afllgglyaf mvaytnvkyk klleiliilp ylipgyivtl awtslfsgng
      121 vinrllmqlg lpkvsmyslg giifvlgvsn aalvylnlvd vlrkipqeqe qasqvagyal
      181 ketlmkinlk svrgpilsav vlsflsaidn faipitlgtp ggisvlstyi yekaigfgpt
      241 sfneasalai vlssislsav liqksltlre kplesqmasy hhrvalkpvq rrliqfvliv
      301 llmilniipl ifmflsslhk gyvrsifdvs hmslanyqfi lttpgmysgf ltslwltlss
      361 lvvclligvw vmymksryql ksvffvetga sltysvpgiv lalsmifywg kvpnvygtml
      421 ilwiayvtry alllirgsqt afmtvgpele eaaivsgsss iekwfkiilp mirqqllsss
      481 flmiigalte ltlssllsaa nsktigltif alqtggdnai aqaysvlltl liltilmmrs
      541 rweskegenk
//
LOCUS       WP_284630266             550 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Globicatella
            sanguinis].
ACCESSION   WP_284630266
VERSION     WP_284630266.1
KEYWORDS    RefSeq.
SOURCE      Globicatella sanguinis
  ORGANISM  Globicatella sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Globicatella.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Globicatella sanguinis"
                     /db_xref="taxon:13076"
     Protein         1..550
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=61550
     Region          1..547
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mcvlfitriv qltvlksvng vdlvsyteia nerssitqar rgtifdskdq piamdttsys
       61 lfailrnade evivkdydlt akvlsenidl trdqvltllr npdanqiefg eagrnlskev
      121 kekieeanlp gvyfasettr qyindffash ligyatplma genddyedae ilkgqlgiel
      181 sydeqlsgak dyreqweasn nlnylsgddl yltldsrlqn qledllntai ttyqpkemga
      241 ylvevktgkl iaaaqrpsfn lntregidke wrnflteday epgstikilt msvaydhnly
      301 qpdekyhsgt ieifdtkind hnlygwgdit feeglarssn tamvtlierl geekwidela
      361 kfgfgkstns glineidgtf sfdnpvsrym ssfgqafstt piqllqafts vanhgtmvkv
      421 qyiegigekn nqykvqelgq piskeaadhv lglmvdtvek dygtakpfks divkvaaktg
      481 taeianedgt gyltgpndyt dsvvaffpan dpkymmylym kqptdkkgli gsqilaqtfh
      541 pfiesiyinq
//
LOCUS       WP_284630355             509 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Corynebacterium accolens].
ACCESSION   WP_284630355
VERSION     WP_284630355.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..509
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53381
     Region          137..505
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 maqaqastas ssshsspqes teptkkekfh ldavwfalaf lalaavllip ipgldwpakv
       61 algmlafavi mwvteavsyp vsallivgli slllglgpdp dsdgiygtsn alkvamagfs
      121 ssavalvaaa lilagamqat glhkrialyv lkiagektsh ivigaiaiai ilaffvpsat
      181 aragavvpil lgmvaafgls yesklgallv itaaqavsiw nvgiktaaaq nlvavgfied
      241 qmgqsvswgq wfiwaapwsi lmsvalyfim ravikpeter ieggkeliak qledlgptsp
      301 eekrligfsl lllffwateg llhpissavi tavavalmll pkigvftwpe aqksvswgtl
      361 ivfaigislg sflldtgaat wlsektfglm gldslpilat ialvslfnil ihlgfasats
      421 lasalipvfi alastldvpn ggigfvviqq fvicfgfllp vsapqnmlay gtgafstkqf
      481 lrsgipltiv gyllilllsa tywswlglv
//
LOCUS       WP_284630392             395 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Globicatella sanguinis].
ACCESSION   WP_284630392
VERSION     WP_284630392.1
KEYWORDS    RefSeq.
SOURCE      Globicatella sanguinis
  ORGANISM  Globicatella sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Globicatella.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 395)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 395)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Globicatella sanguinis"
                     /db_xref="taxon:13076"
     Protein         1..395
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45792
     Region          51..350
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 mkvikidiln hplfeekvev nflldarvtt dekhellnlf nnyylnytyt ftglnasgkt
       61 qllntisfal nllqaqpiny risflptdni lnlelgqtit fviyfyenln qkptlnrlet
      121 tvsrkrdeld gqikyiieee yltvkkttgv rtkkdifnfe kgsylkkher nnedvylgls
      181 qdvsmmnvfy kkndyqslyf kdmvkftnfn ffsgygsipe eiikfldpsi ekinfiskqd
      241 sneigveihf knqdrivkln svtdihtvls sgtvkgmslf memlvvlekg gvlivdelen
      301 hfnreiaatl ikffldrkvn tngailiytt hyaelldmld rndaifivkk qvkinvekls
      361 aslkrndvar sdqfikgvle ntapdyeakm kciwq
//
LOCUS       WP_284630431             617 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Globicatella sanguinis].
ACCESSION   WP_284630431
VERSION     WP_284630431.1
KEYWORDS    RefSeq.
SOURCE      Globicatella sanguinis
  ORGANISM  Globicatella sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Globicatella.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Globicatella sanguinis"
                     /db_xref="taxon:13076"
     Protein         1..617
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=72521
     Region          18..608
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 msiidrwykl lnylllndtv sindlenylq nsqqtiknsi nqlnsemsqi ahiteknnyf
       61 rieilnysef erimggsikl qtdfnssdkr qayiikrlle eekyiitldl seelgvsrgt
      121 fsndlktikk ltndygvqii svpnkgikle geelnlrlfg iyhcidffef kninqehidm
      181 ilglqnkysf rkqdahfllk vlelticrir nnqhltkpip kyvnyiknsq lyneiilyie
      241 teftitlney ekdfitfplc ingnsinisi sqlmendyll esfqlimgti knyfmieide
      301 dnffndlskh laflnnrlif nyqiedifhg eiekkypfsy rlakdtlkvl ktyfnshisd
      361 veanfltfyy eldsktkdee kvkkeiaiic ntgkatagmi rrqiekvvgq nikivqfses
      421 nyenedlsky faiittiplk nipqeiptir ltnifkddyl alewgklkvd rnnlgdktlv
      481 flnrysssty eevitkmvse lreeklidyd fkerlfnrka pvlnnngiif phelnytskk
      541 iiikigvlen tvildnesve lillvaipnn iqnddndlld lydfifgigq npqlkeriir
      601 mdsveefnry fskgmmk
//
LOCUS       WP_284630459             402 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Globicatella sanguinis].
ACCESSION   WP_284630459
VERSION     WP_284630459.1
KEYWORDS    RefSeq.
SOURCE      Globicatella sanguinis
  ORGANISM  Globicatella sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Globicatella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Globicatella sanguinis"
                     /db_xref="taxon:13076"
     Protein         1..402
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45346
     Region          26..382
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mdlykgkrfw ptltkeasfs kqkgthkvdv liigggmsgl lsayslarag kkvflvekds
       61 iangssslnt gliqymsdvv mvdideeknk mvsndfylrs qkaldyieei vnelddptis
      121 frrnnslyvs ndeekilkik revarqneln fetefldqqr lkkeygidal ggllskndve
      181 lnpmafvsam atsatqnfdl liseqtqvne hnfsfeenkl ivddlsvqyd klviatgydv
      241 fpsfskylpk idlvtsfvvv tepisnqkvt dtmfwessss ylyfrkspdn rliiggedee
      301 nitlsenkak inseklikqv qsyqtnsikl kseyfyeaif gessdglpyi gphpenhdif
      361 iihgvggngt vysamgaiei vdfskgkfde kmsylwpset nn
//
LOCUS       WP_284630572             729 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium accolens].
ACCESSION   WP_284630572
VERSION     WP_284630572.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 729)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 729)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..729
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76269
     Region          2..723
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mshvdlgvsg mtctscssrv erklnkvdgv easvnfates asiefdpets tpadlikvve
       61 gagysafdms gsddgdqdgd aegtpvddar aaeqesllrr tiisavlsap imvvsmvpal
      121 qfqnwqwaca mlatvvfifg gapfhsatwt nlkhgsftmd tlismgtsaa ylwslyalff
      181 gnagepgmtm smswssssae mdhiyfesvg mvitflllgr wfevkakgqs sealrtllsm
      241 gakeasvlrd gketripisq lqvgdvfvvr pgekiatdge vvsgnsavda smitgesvpe
      301 evgvgdtvtg atinasgkle vkatqvgedt vlsqmatlvt naqaskapvq rlvdriaqvf
      361 vpvvigisvl tllvhlifgg vapafiaavs vliiacpcal glatptailv gtgrgaqlgl
      421 likgpeiles tkqvdtivmd ktgtvtagem svtavhgdvl eyaaaverns ehpiaqaiar
      481 erdvepgadf ststagveat adgvrvgvgk prgdlgqyae afreaeaaga tpvavyldde
      541 laglievrdt vkptsaeavq qmkqlgltph lltgdnegaa krvaeevgit evtagvipee
      601 kvdvikklqs eghnvamvgd gvndaaalaq adlglamgag tdvaieasdi tlmngdlrsa
      661 adairlsrrt lqiikgnlfw afayniilip vaafgllnpl fagiamalss vfvvsnslrl
      721 rkfssqryd
//
LOCUS       WP_284621134             648 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Brachyspira
            pilosicoli].
ACCESSION   WP_284621134
VERSION     WP_284621134.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..648
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=74774
     Region          58..616
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mkrfiiyflf asinllysqt ylirelkggi wvtskaeitn qtnnttasns sykspinvni
       61 ktitseeier mgynnakevl enqagfvnkg nymgnevvdp aggsadniki yingvlmnta
      121 kgnadagvdl rripsnliek ieiigssiyi ttktpkedii llslsygsyn tiapsilfsk
      181 niddnqiftf tadsyysdan yyynftnlag kwikgniedn rqfiinssan ykyifknkny
      241 inafanisys ssasqyqipp isytdswfnf ttlassisyn gfsevldyni nlsylfdsfv
      301 drpyfkegkf vsdykshgla inttlkrmde lipntitlyn eltpeyrydi lteeknalet
      361 nfnhnpqrhs lnikydmqls fgywdnntpi ftlmpsikye yqnefftnqk hnnylaynag
      421 fnlnfykgys lyfaymsdyt sptfndlyyg nfsnpnlkpe tynqiltkis lepitnlkie
      481 ssytyttytn kiiwyssipe nadtaishif sssigydiyf ltynkikaki eysyqlayln
      541 eeklpkiglp nnvvtallgy dfvsdgkils slsfniyyiy sspramtsny piyyseefhn
      601 lnisfysiwf khlifsmhfk nilnktpils aysvakpftf efevgynf
//
LOCUS       WP_284630605              97 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein
            [Corynebacterium accolens].
ACCESSION   WP_284630605
VERSION     WP_284630605.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..97
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10883
     Region          3..>66
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 msyvnitals fpegagpeie rrfaqrakgv dkaegfesfe llrpvagedr yfvvtrwdsq
       61 enyqkwadar pagnhvedek rgmsvdvlgf esiqles
//
LOCUS       WP_284630771             218 aa            linear   BCT 25-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Corynebacterium accolens].
ACCESSION   WP_284630771
VERSION     WP_284630771.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..218
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=24391
     Region          3..200
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mlicqemfll ltedngkkev lsnnetalra glfsdlllhe avaitaknkv hatdkkpehp
       61 vlawawdslh ehrtgsvktl lqarwfspre kiaedfqdrg qleiedsaww qlggdryimt
      121 dtaledevre rlaavldgtq npsakdvlil dilrevngay pllkedapem krremrnrik
      181 elkqqveydd aaasavktil qettaiiaav avstagtt
//
LOCUS       WP_284630889             236 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Globicatella sanguinis].
ACCESSION   WP_284630889
VERSION     WP_284630889.1
KEYWORDS    RefSeq.
SOURCE      Globicatella sanguinis
  ORGANISM  Globicatella sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Globicatella.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 236)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Globicatella sanguinis"
                     /db_xref="taxon:13076"
     Protein         1..236
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=27256
     Region          1..222
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mriaivddhk efrerlvryi ednaanleip vditcfadgi elvdrfqssf diiyldveme
       61 fmdgmstakk iretdsevli vfitnhaqva iqgysveasd fllkplnkft feehfkkiik
      121 kvkkqddsiv vrvsgtvkrv dqhsilyces qghyidfvtl ngrftlidsm knieekldpv
      181 rffrcnnsyi infehvehid ksagtahlge hkiqisrark kecvekftqy lggqvl
//
LOCUS       WP_284630900             372 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Globicatella
            sanguinis].
ACCESSION   WP_284630900
VERSION     WP_284630900.1
KEYWORDS    RefSeq.
SOURCE      Globicatella sanguinis
  ORGANISM  Globicatella sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Globicatella.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Globicatella sanguinis"
                     /db_xref="taxon:13076"
     Protein         1..372
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41682
     Region          5..368
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mmneriflss phmsdegyeq eyikeafdtn wiaplgpnvn gfeeeliemt ngghalalss
       61 gtaaihlalk tlnvgqddiv fcqsltfsas anpiiyqnat pvfidsapgt wnmdpealee
      121 aftkykpkav ivvhlyglpa eikkiraicd kyntplieda aeslgstvdg kwtgtfgdlg
      181 ifsfngnkii ttsgggmlvs qdkakidkar fwstqsrepf rhyehkeigy nyrlsnvlag
      241 igrgqlkvla ervekkrsif hayqeglkdi deitfiqekd gehanywlsg iiinsekvtp
      301 nmlidalene niesrpvwkp mhlqpffeky dfigkgvaee lfnkgiclps dskmteeqvq
      361 atikvirslw rm
//
LOCUS       WP_284630953             256 aa            linear   BCT 25-DEC-2024
DEFINITION  inositol monophosphatase family protein [Corynebacterium accolens].
ACCESSION   WP_284630953
VERSION     WP_284630953.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..256
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=26641
     Region          5..252
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mmdprelvaf aeaavdqvep ifrsgigapp ahfksrgdfa tevdlaiekq lrdilqqmtg
       61 ipvygeesgg sihdtvwvvd pidgtanysa gnpmagilva lvhegqpvaa isdfpllgrr
      121 lvasdgsplr saggpsggfg ggeespefdd arghvgcfsn lptaafhelr esglrpritg
      181 svgldnafva qgvfdgavnf sphpwdnaag allikaaggi vtdpegnpwt vqsrgmvsgt
      241 sqvhetilei lshhsn
//
LOCUS       WP_284631055             351 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium accolens].
ACCESSION   WP_284631055
VERSION     WP_284631055.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..351
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36778
     Region          40..346
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mvsgevaalt qqhkkltwqr isivaglcli aavafvvsnf vgaidispge virgivnpss
       61 lddqthtvlw klrlpmavma lligvslsla gaemqtilnn plaepftlgi saaaafggas
      121 sivlkwqllt qpqfnlalva wlsaavatai ivvaaiirga kaetmvllgi glvfffqaml
      181 aliqyqssae alqqivfwsm gsltranwva ngvlagvllv alpilwalsw rlmalrlgda
      241 raaamginta rlrvvvlivv slvaattvaf agiigfiglv gphiarmlvg edqryfvpas
      301 maagaavmca ahaaslmikp glaipigivt sllgvpffia ivmtrrralw t
//
LOCUS       WP_284631069             534 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Corynebacterium
            accolens].
ACCESSION   WP_284631069
VERSION     WP_284631069.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..534
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=57864
     Region          1..521
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msllsvkdls ityrtdkgdf qaasginlev nagemtaivg esgsgkstsa maaigllpen
       61 asivsgsisf dghdvtqysq kqwrelrgrr ialipqdpnn slnplktiga aveegmavhs
      121 qgtkhsrrqr avellervdi ddperrygqy phelsggmkq raliaaaval epeliiadep
      181 tsaldvtvqk iildllddmr deltmgilfi thdlavagdr ansivvmekg hvresgvaan
      241 vltapqheys krlladapsl stptltrrta tegatpllev eglskrfgdf navrdisftv
      301 argtthalvg esgsgktttg raislfsrpt egtirlsgee ltgvrgkrlr elrqkiqlvy
      361 qnpfssldpr lsigetiaep vrnfkrasrr dankkaqkfl dlvaldsama grkpkelsgg
      421 qrqrvaiara mivepelvvl deavsaldvt vqaqilrlld elqkeldlty ifishdlavv
      481 nqisdtvsvl shgqqvesgr taevfahpet aytreliaai pgsryragdl nlgl
//
LOCUS       WP_284631134             241 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium accolens].
ACCESSION   WP_284631134
VERSION     WP_284631134.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..241
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25260
     Region          14..235
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(23..24,26..27,30..31,68,72..73,76..77,97,104,
                     107..108,113,128,132..133,135..137,139..140,143..144,
                     147..148,174..175,177..179,181..183,185..186,188..189,193,
                     196..197,203,205)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(131,135,138..139,141..142,188,191..192,194..199,
                     202..204,208,210)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(152..159,176,179..180,183)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mslqkqgvlr rasidprtvl lsvlvinava lshghlptll isiafssial atvkphygli
       61 clcafalsyl gywgllqlpg stffafsaai fswlsrfvis isigafgllt ltpstltsal
      121 rdlplpgwat ippavflrvl piivaeakai rdamvlrglq pgakswftqp tqssamliip
      181 llgavvragd elaasalvrg lggptrpttt adlsfklvda taiaglglvv asvwlptevh
      241 l
//
LOCUS       WP_284631227             630 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium accolens].
ACCESSION   WP_284631227
VERSION     WP_284631227.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 630)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..630
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64787
     Region          32..624
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mssacgcehe tgteideldr pwwkdpelll pifsgvalit glaldwsdle tpatvlywvg
       61 lllgaytfap gairnlvtkr klgigllmti savgavilgf vgeaaalafl ysiaealedk
      121 amdraqgglr allklvpqta tvlrdgtaae vaakdlevge lmlvrpgeri atdgiirsgr
      181 ssldtsaitg esipeevapg devpagains agvlevetta agtdnslttl vdlveqaqae
      241 kgdrariadr iaqplvpgvm ilavlvgvig sllgdpetwi tralvvlvaa spcalaisvp
      301 ltvvaaigaa sqfgvviksg aaferlggir hlavdktgtl trnqpevtgv vpadgfdrpq
      361 vlsfaaaveq qsthplaaai aaagpeapta sdiseeaghg iggtvegrrv lvgsprwida
      421 gplkadverm esegqtcvlv tvddalagai gvrdelrpev peavqalhan dvevsmltgd
      481 nsrtaralag iagiddvrae lrpedkasiv aefssktpta migdgindap alagatvgia
      541 mgatgsdaai esadvaftgh dlrlipkalq harrgsriin qnivlslaii ivlmplaisg
      601 vlglaavvlv hevaevivil nglraaqakr
//
LOCUS       WP_284631243             212 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Corynebacterium accolens].
ACCESSION   WP_284631243
VERSION     WP_284631243.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..212
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23151
     Region          <1..84
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mgnilrqdgw avfapdyghr atqtipessq qlgayidtvl avtgaekvil vghsqgglla
       61 rywmrmdgga ekvvhlmsis apnhgtthgg iasrlirtqr qeavirsiid gwfgpagmdq
      121 vvgsevlrdv nrdgdlesgv sytciatrsd avvvppetcf ldpegapega vrniyiqdfd
      181 rhavvmhedm pmdrrvhaiv rtllrmveht pr
//
LOCUS       WP_284631276             226 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Photobacterium damselae].
ACCESSION   WP_284631276
VERSION     WP_284631276.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..226
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24768
     Region          1..202
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mqaicfdfdg tlvdsevfha anwslymash dvelsadvfm hkyagvtwpn iakiliekfq
       61 lniepqqivd dmealteeqi rakgipakeg aetllkqltg kvplavvtga priyvegila
      121 qkgwlewfdv iftgddvehn kpapdiyqla cqhfelptes viavedsttg atsaltaglk
      181 tifvntinlp isgqvarhfs dlieaqptic amlsldcdkn nkqhva
//
LOCUS       WP_284631492             473 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium accolens].
ACCESSION   WP_284631492
VERSION     WP_284631492.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..473
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51782
     Region          5..404
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msrttlrsfi qrihfyggmf vgpfiliaal tgclyalapt lekfayrdvm tveevnnpvs
       61 ledqisaaqk ehpdmpvsqv wpaesatdst rvlvadpgid eslqrtvfin padgevigdy
      121 ptysglgemp lrrwisslhe sfhlgqpgel yselaaswlw vlacgglymw wirrrpkkaa
      181 aplkkqpqrs krwkatrlhs tmgawifigl iglsatgitw sqlagenvns vvekmnwkat
      241 pvetalttds saeaahdaha gheghgahga hggdaetage apepeviaeq aervyatgra
      301 egltgplrly apedtdsgwk vserwvewry tsdevsvngs tgevidrlpf selplfskls
      361 swgiylhmgi mfglplqial falglaiaam vvlgyymwwk rrpqfapgsk rhfswattgl
      421 galfaatvgv fmpllgitla aflvldiivm ntgkrkatap kkkdedaelv pvg
//
LOCUS       WP_284631546             342 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Corynebacterium accolens].
ACCESSION   WP_284631546
VERSION     WP_284631546.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..342
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=37133
     Region          25..308
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mhlvnywtrt krffkeavpt veqqrliali lifcqggitv sgsivrvtgs glgcptwpqc
       61 qpgslvpveg aapaihqiie fgnrlltfvd saaagaavia mymacrrpel riyawlnvag
      121 ivlqaviggi svhldlrwws valhflpsmv lvwlacmlya rikepddgta qprfpqairi
      181 iaviatials ivlitgtmvt gsgvhsgdsg vgmegrldvd tesmaiaham cmyvylifta
      241 itvfllykhr apqetkkagw vlivciliqw avgvlqfylg vprwtvpfhi gmsavvtgft
      301 allwahgrhr vggtpdlisg spagddkyav rqqslneera av
//
LOCUS       WP_284631443             595 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Corynebacterium accolens].
ACCESSION   WP_284631443
VERSION     WP_284631443.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 595)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..595
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62439
     Region          3..472
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          529..594
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(552,561..563,570)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            562
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mqiktvlian rgeiavriar vardlgiksv aiyseadaga lhtqvadeay alpgntaadt
       61 ymntpalldi avragadaih pgygflsena dfartvtdag miwigpspes iellgdkiaa
      121 rrvaeevgap lapgtsdpid dwqearafae ehglpiaika ayggggrglk vvdsmdeieg
      181 afnsagream eafgraecyv ekflthprhv eaqvladthg nvrvlgtrdc stqrrfqkli
      241 eeapapalsd aqrtgiiega rsicshvgyt gagtveyivs edgtisflev ntrvqvehpv
      301 tevvtgtdii aeqfriaage plsisedpas tghafefrin aedilngfap cpgtivsfep
      361 ptgpgirvds avrsgsiipp yydsliakli vwgptreval arsrqalref dvsgvrtvlp
      421 fhrdmmdepa ligtpssaea dagasdigvf tdwldhnyrp saanqvdkve aiytkrrtva
      481 veidgklvni gvpmdflaga gagagagaag dsgatapsta gaqssddnav tspfeanlva
      541 wnvsdgdsvs egdsiatvea mkmesaikap rggtikilae egdrldsatv iatid
//
LOCUS       WP_284631784             752 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium accolens].
ACCESSION   WP_284631784
VERSION     WP_284631784.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..752
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=82460
     Region          29..752
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mnsapknspa thspadatss sraenagisa ieaeqnyvdg lfdrlddeva aanarlnevq
       61 aevdpatpda dalvrretey hglqakldrl nvaqmglvfg rididapgdn pteegldrry
      121 igrmgldare enyrtllldw rapmarpfyl attaqpegvh trrqirmsgr tvtdvndeal
      181 ngpgvreeet gvasesalyf amqrartghm tsivetiqre qdeiirdntr gvmvveggpg
      241 tgktavalhr vayllythre qlsstgvliv gpntnfldyi srvlpelget gvvlstiggl
      301 fpgitpthte glvgreikgs aamaeilsaa vkdyqqvpse prditvdglt ltitpsmvkr
      361 artrarrsrk phnqareafi ehfvedlaqe matkvgtdpl ggenllsrad vdqfhddlai
      421 desvvgcidd fwpeldpsev laallssrer iasaargyde etqaalyrpd gytwtdsdaa
      481 lldelavlig lpnpeekkaa kdakwreqia daedaldils ssestdnddd mfeaeilsah
      541 dvidaetlaq rqevrdtrtt aqraredhtw afghiivdea qeltpmewrm lfrrcpsrwm
      601 tlvgdtsqtg spagvddwge alepfiaqrf rhhlltvnyr tpepitelan rllasidpda
      661 tpaiairdge pvrrladadf tpgvtteddg rltavidatn aeavkglefd hvivlnprei
      721 vdaspqglqn lyvcitratq tltlvgdtsg vl
//
LOCUS       WP_284631754             530 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Corynebacterium accolens].
ACCESSION   WP_284631754
VERSION     WP_284631754.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 530)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..530
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57145
     Region          1..503
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mevllvligl mlltvfvvai gdrvglpwpa lltiitacav fvpglpqfdi ptelilpifl
       61 ppllwalarr tswgvirgqw vtilslsvll vvattlavga tayaflpgis iaaailigaa
      121 iappdpvavd avaepagipr riittlqteg lfndaasiva fhlalaavtq ggdisfgsgv
      181 lsflyssvva laigwligrl talfithvhd vvarnaltwv vpfatflvae eleasgviav
      241 viaavelnsr adiqaedrls gqsfwetmel lftgvafgli gltvntaiae vgsdlwhsvm
      301 vgvilslvaf vvrfvwmffy yrlnvsrgrp hvaplrmqev llmtwsgmrg lvtlalvlsi
      361 ptgvfafhhe lavialtvll vtmvlpglll pwlmrqldlt easqaandkm raavvsrara
      421 asidalsqfr peddatgeae tvdpeisanv iqwfedrlgd genpaennde rkqraeearr
      481 valearrtal naaqsellal rkdkafnpai vdeileeidr mvigtnhrei
//
LOCUS       WP_284631845             257 aa            linear   BCT 25-DEC-2024
DEFINITION  nuclease-related domain-containing protein [Photobacterium
            damselae].
ACCESSION   WP_284631845
VERSION     WP_284631845.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Grynberg,M. and Godzik,A.
  TITLE     NERD: a DNA processing-related domain present in the anthrax
            virulence plasmid, pXO1
  JOURNAL   Trends Biochem Sci 29 (3), 106-110 (2004)
   PUBMED   15055202
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10551559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..257
                     /product="nuclease-related domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29539
     Region          33..144
                     /region_name="NERD"
                     /note="Nuclease-related domain; pfam08378"
                     /db_xref="CDD:462454"
     Region          <204..251
                     /region_name="YrdD"
                     /note="DNA topoisomerase I, ssDNA-binding Zn-finger and
                     Zn-ribbon domains [Replication, recombination and repair];
                     COG0551"
                     /db_xref="CDD:440317"
ORIGIN      
        1 mnifevfinv leqvwyllpl llivsvfksr wlkgifgeyl vnrllsklpe sdytlikdvt
       61 lptsngttqv dhivvskygi fvvetknmkg wifgsarqkl wtqkiyrhss kfqnplhqny
      121 khikaletll gcsadylhsv ivfigdstfk temppnvtya rgsiryiqqf nkvvfsdkdy
      181 arltdsinqi klkrgvitdl khrnhvkeiv askvssnqcp rcgsemvlre tkrgenigkq
      241 fwgcstfpkc ravkqln
//
LOCUS       WP_284632295             502 aa            linear   BCT 25-DEC-2024
DEFINITION  SPOR domain-containing protein [Photobacterium damselae].
ACCESSION   WP_284632295
VERSION     WP_284632295.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..502
                     /product="SPOR domain-containing protein"
                     /calculated_mol_wt=55632
     Region          45..500
                     /region_name="DamX"
                     /note="Cell division protein DamX, binds to the septal
                     ring, contains C-terminal SPOR domain [Cell cycle control,
                     cell division, chromosome partitioning]; COG3266"
                     /db_xref="CDD:442497"
ORIGIN      
        1 mighdattrl dldsqiqfls rlqfvtqfss hliqisgpfg agktellhcy lehfspeqhq
       61 vllsaepdms ltsvrtqllq qlvptkpfne qdsllqsish mlssdrlhcl lvvdnahyls
      121 ipilaelwel vchanqqadw qlnvllftep dviaqplakm thgqsemple leiaplpane
      181 vlqliehcye qdlqkrrelk lryqhsfafp gqldedtqpp geevsmtash qlsprtglli
      241 glllalvval lwlwpeskps edlaidssas qvvegtelig sgeptedtaa lppdvtqegl
      301 tvgrtdsdkr vvvpaqvvda mmgdqalglv gaqthfsdae inaldpanvh pssvtspqat
      361 ttplsesepi sesvkpepeq paksldkslk qhdtpqpish nnqhsdkqil qqvnsrhyal
      421 qlaavhswqq akqfvakygv tesahiyqte rqgkawfivv igdyssatqa kraknqlshe
      481 vqalkpwpks yaqiqkemnr vk
//
LOCUS       WP_284632410             948 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Photobacterium damselae].
ACCESSION   WP_284632410
VERSION     WP_284632410.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 948)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..948
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=105119
     Region          37..465
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          505..931
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mqkwilplal lsvtnttwaa kqsdvplpkg vsfieqvkpe pgkavipfrk yelsngltvi
       61 lhqdksdplv hvdmtyhvgs areevgksgf ahffehmmfq gskhvgdqeh frliteaggt
      121 lngstnrdrt nyyetvpanq lekvlwlesd rmgflldavs qkkfeiqrst vkneraerye
      181 nrpyglvyer mgealfprdh pyswqtigyv adldrvdvnd lkafflrwyg pnnatltigg
      241 didiaqtldw vekyfgsipr gpevnnapkq pvtlkadryi tledkvqqpm lmmgwptsyr
      301 gakdeasldm laqiigdgtn sllyqklvkt gqvvdagafn dcaelactmy vyaigpsgek
      361 gnlksirgkv meivnslekq gvkqqavdei kgvaessaif glqsvsgkva qlaayqtfyg
      421 dpnhlgveld nirkvspssi eaaynqyiyq hpnvtlsvvp qgkldlvaak tnftpeprki
      481 pehqkinddq ltlrmakdnf drsvmpqpsk pveammpsly dvtlangiki lgtqydetpt
      541 velqlvvpag rryeaegkag laqltaammn eattkasaeh iaseldklgs svsfdaglyg
      601 ttitlsslak nlkptlaile qrlfhpafaq adfdrlkkla leglvyehqh pewlagqatr
      661 dvmfkgtvfs qapegtkasi esitladvkd fyqryytpng admvvvgdik pqtlqqdlas
      721 lgqwkgqaap tyhtpklpsi ekpaiwmvdk pgapqtiirl vrqglpydat gelyktqlan
      781 fnlagnfnsr inlnlredkg ytygaggylt ggkelglatf yaqvradasl aatkeflael
      841 kkmsqggltd kemkfmrlav gqqdalkyet pakkaqllgq mltyslpkdf veqrnkiaat
      901 iskseldkla kkwfnpqdyq iivvgdvakl kpqfatlglp ihvikpqq
//
LOCUS       WP_284632516             752 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidase U32 family protein [Photobacterium damselae].
ACCESSION   WP_284632516
VERSION     WP_284632516.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002788
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..752
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=84581
     Region          3..295
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
ORIGIN      
        1 mqnkfellap ggdldsikaa iaagadaiyc gldsfnarnr atnltfdvls giirlahknh
       61 ckifltlniv vldseipavi rllnklvntk vdgvilqdlg lfsiikehfp tldvhastqi
      121 nthndgqilf lkqlqasrvn lsrelninei khlaqfghqh dvlmevfvhg sycigfsglc
      181 yissvkngns gnrgrcsqpc rdqyqttaag kdfplnlkdn safsnmaela dagvyslkve
      241 grikkshyvy tvvdqwrqqi drylnqqpll tdtkslytvf nrdfsnsylq gdinknmfid
      301 nprdnavthf tkvyqcttpe tvngvkqkly ddkteiiqtv eqvtanmdvs slpltivltg
      361 qegeplsisv ttpnhhfvlc sdsvlrasnk qtlthdmlek rfqslanege feivefntkg
      421 lnealsvpfa elaqlkdqmg yrlngnvaiv apieppkprn manhrkptgi apklavlise
      481 pkdvtlgrgd evalyyampe glsmeletlv alfeqnphli pwfpailige nyqaavefie
      541 rvkpqqlvtn nngiayvayq heidwiagpy lnitnsfslq ciadefkakg afisneinrk
      601 qinpmvcpen felyysiyhp lmmlmsrqcl fhqtvgckkk rfdnkclrkc dksasilslk
      661 easfvldkqr gthnalysqq nymnlsavtd fpdkftrfmi dlrdiktetq vnldkptlvn
      721 lfsryiqgdm taqeqlesgi igtihhqykk gl
//
LOCUS       WP_284632879             510 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Photobacterium damselae].
ACCESSION   WP_284632879
VERSION     WP_284632879.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..510
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=56594
     Region          3..367
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mniaiigagp agiisarnai kaghsvvlfe knahiggiwn pwsggayrna cmqnsrytfh
       61 ytdfppgnid efpcvaqvfa ylsavtgeda lrastrlnte vvalrkdskh wvirstsagn
      121 dreeifdrvi iatgelwqpr qptlpgaehf sgtlitskdy qepevfkgkn iliigggvsg
      181 adiasdlvpf arsvslsvkk mglylprqfr mgpndmmhsy lgrcllsrls yadfvgyldt
      241 tmpdymqtyr asgllpdman nnavhvneki ipnvaaglik lkpqakrftg egeiefvdat
      301 qekydviitc tgyempdysf ipgfdraqly ehffwtedps lavinppvdt agfgaafpyf
      361 diisqwvinv fsgesplpek eamrkwcaeh maslhvkrfy dswletirig llaglfpdpa
      421 rdfsrywnii ssvvkpayla sppetpepgm mdslfdfraa ririlsglgn dalgyllkkg
      481 ditdaehqaa letdprqsls vhlpysqtyl
//
LOCUS       WP_284632881             338 aa            linear   BCT 25-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Photobacterium damselae].
ACCESSION   WP_284632881
VERSION     WP_284632881.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..338
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37373
     Region          11..257
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 miigivgcgg iarahvsalc lnplvtglam ydvnadnvrl lseistvpvi ccqdlkqlag
       61 vsegfvictp nhlhvsvaee vlrykqlpfv cekplstdln laqylqeiap qgsivsfnyr
      121 ynrvidtmmr lrnerdlgel hffsaefnkn saltrhhltw rdsarqskss galgdlschl
      181 ldlfcfiges pvvvngirtv kgtrvgaksd grvevddngy vmgssekgay frihaskset
      241 gqdlglhmql vfekgeirys thhenslllv lfnetdaetv gfdglkclpd pprelpfwsd
      301 sfihlhddwc alikyghtap kladlssglh iqeiieaf
//
LOCUS       WP_284632983             345 aa            linear   BCT 25-DEC-2024
DEFINITION  HlyD family secretion protein [Photobacterium damselae].
ACCESSION   WP_284632983
VERSION     WP_284632983.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446287
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..345
                     /product="HlyD family secretion protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39881
     Region          27..295
                     /region_name="EmrA"
                     /note="Multidrug resistance efflux pump EmrA [Defense
                     mechanisms]; COG1566"
                     /db_xref="CDD:441174"
ORIGIN      
        1 mkikfnldke rnpeiedgmk vmygpdkrnk ykirwyfili lvisplfima yylfrtqilv
       61 ispgiitsyp ltinseqpai vegiflesgd dvnkeqilik lknytlnkei dfikkeihkl
      121 snlkitnndn ihrnaiknte isaykvyeiq kkydqykqkg hisdidyati vnlknaidsq
      181 lsdqqiiynd dkfnkdqirv agpvaqqyrn lmqqlviket qkeslyfksp fngrvldihv
      241 rngqriqtgt plvtisqnvt pqvvaflepk hleysaintk akvifpdgkk ftatvfkpve
      301 vvnklpqelq npfegqsgyl kltlafdnai dkirwvegve vevkf
//
LOCUS       WP_284633100             259 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Photobacterium damselae].
ACCESSION   WP_284633100
VERSION     WP_284633100.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426811
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..259
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29167
     Region          8..256
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mlgkkkrkal flvhgldnnl hiwedlatrl sehhyvvaid lrgngksswa spntytlddm
       61 cndineviqh lginsvilag hslggkialk ysvvhpykvd rlllldcspq ldtklkqald
      121 gyfssrtqvf sspkeyedel kaihiladet lvkefaksnl syrngtyyrn sdpkfnisml
      181 ddsgplmsgr vweyfpnisc pvlivraqms silteksand myqklqfsti vniknathsl
      241 mldqpsilhs vvddfvisf
//
LOCUS       WP_284633052             835 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-mannosidase [Photobacterium damselae].
ACCESSION   WP_284633052
VERSION     WP_284633052.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 835)
  AUTHORS   Nascimento,A.S., Muniz,J.R., Aparicio,R., Golubev,A.M. and
            Polikarpov,I.
  TITLE     Insights into the structure and function of fungal
            beta-mannosidases from glycoside hydrolase family 2 based on
            multiple crystal structures of the Trichoderma harzianum enzyme
  JOURNAL   FEBS J 281 (18), 4165-4178 (2014)
   PUBMED   24975648
REFERENCE   4  (residues 1 to 835)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 835)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14312040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..835
                     /product="beta-mannosidase"
                     /EC_number="3.2.1.25"
                     /GO_function="GO:0004567 - beta-mannosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005537 - D-mannose binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=96449
     Region          23..>644
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          754..830
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; pfam17753"
                     /db_xref="CDD:465483"
ORIGIN      
        1 matllldgqw qltspqhshi aipctlpgdv hsallaaeli vdpyfaenes lvqwvgesdw
       61 lltrefevsq emldhhaidl tlsfvdtvad iqinqhsvlh csnqfqtyhq evkstlklgi
      121 nhisillkrs dieakvraek lpfpipwaeg nnqiphmntl rktqchagwd wgicllvsgv
      181 yqsitlepln ntrlvnvrtt qnwlssehcq lelaityqal aafeqqqlti dfnqqvhtia
      241 lpidnqdidk nhtlyytidv hqpkrwwpag ygeqplyple itlneqsiik qigfrqleld
      301 tslddigskm qfvvngqtit akganwipld ampsqqtper yrqllqnavd anmnmirvwg
      361 ggtyeqdcfy qicdelgllv wqdlmfacal ypstdefiqe veqeviqqid rladhpclal
      421 wcgdneviga inwypesrqh rekyvvnydr lnrvlaqiva khdssrrfwa sspcngeldf
      481 gdawhddncg dmhfwdvwhs gksldayyqv kprfcsefgy qswpslptvk tfadydewnv
      541 tsptfeshqk nkrgnsiite mftryfrfps nfanmlylsq vqqalaikta seywrahknh
      601 crgilywqln dcwpvsswss ieytgrwkql hyhakrffap qlvtfiqqdn glltlsaind
      661 ehkavnyqgq vlqlswqgdi lqtwpingel tsdssdiiwq hfintsnine kdhfyhhvei
      721 tieccsesnn gqistiendy fptvfkqakl qpgkihaqvi edelgiiiel dceepclfvh
      781 levddhlsrf sdssftllps tcsgykkqir yigllnkhci ekqlkiyhls qsyls
//
LOCUS       WP_284633233             373 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Photobacterium damselae].
ACCESSION   WP_284633233
VERSION     WP_284633233.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..373
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=42146
     Region          3..348
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 makltqewid qhkpkarltk ladsqcrgly flsrpsgnhs ylldfscqgv ryhitlgksk
       61 tlslaqardr alqerakrdp slalrtppkk avpfesfgre flqsqarhwk pstvtwyssl
      121 fslnllpafs glmvdqitad kvkvwygtqt hhgalsllsn mmkraeaigi ipagsnpcqg
      181 lrkpdsrlsg yaftsqelvq lwhkldhgav snptierlir lliftgcrss eirtlkhgdy
      241 ragklylpds ktgtktiyls sfarylletq qkdstnewvf segdgcvskd rlarawkvlr
      301 qsmnlphvrl hdlrhtyatr alengehlln vskllgheqp ettlryahla kapmyhasec
      361 vsqtiaremq lcg
//
LOCUS       WP_284633328             442 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Photobacterium damselae].
ACCESSION   WP_284633328
VERSION     WP_284633328.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..442
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=49427
     Region          79..425
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mdykdmdidd impigmignk lrsqkinsid vigsaylnkq nklitqqqwg ydsalmkgsq
       61 aradilfsdn edikenvsvw sinhylglnr seemmeaaie tiktygtgsg tsamsgghse
      121 lhkelqqkfs siwnkeesll yptgftanlg aisglmkgts rdnlilldee chasiidgck
      181 lsgarflrfs hndindlkyk lykyqhsfsn imvvvesiys msgdsaplve itklkqehnf
      241 ifyvdeshsf gfygdegegl cyelnilndv dvlmttlsks casiggvist shkycamlkw
      301 sssylyqaai pahdvavilk aldiikspkl rnelkektay lrsrlrtasf digsgnssii
      361 pvyisddall kqmenalikn giytvaiqyp ivkahtsrfr fivnvshtyq didnlvdvlv
      421 kirnqfgdst ynpittqlsy sl
//
LOCUS       WP_284633272             371 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Photobacterium damselae].
ACCESSION   WP_284633272
VERSION     WP_284633272.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..371
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=42528
     Region          3..348
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 makltqewid kyqpksnpvk csdpqcrglf lifrpsgyhs ylldftsqgv rynltlgntq
       61 tlslakarel ayqerakrdp klnlhaqpqk pilfdefgqs flihqarlwk prtitwydsl
      121 fqrnllpafq gltldkittd nvkvwygtqs hhgalallsn imkkaealgy ipagsnpckg
      181 lrqprqrltg yaltsqelaq lwraldngti hnptltrlir llvltgcrcg elrnvkqcdy
      241 rmdklylpds ktstktiyls sfarywlqeq qqestneyif sdelggikrg rltqawktlr
      301 qsiglphirm hdlrhtyatr alengehlln vgkllghelp ettlryahla sapmyhasec
      361 vsqtiaremr p
//
LOCUS       WP_284633340             487 aa            linear   BCT 25-DEC-2024
DEFINITION  TraB/VirB10 family protein [Photobacterium damselae].
ACCESSION   WP_284633340
VERSION     WP_284633340.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20365647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..487
                     /product="TraB/VirB10 family protein"
                     /calculated_mol_wt=53183
     Region          65..>120
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          204..407
                     /region_name="TraB"
                     /note="TraB is a homolog of VirB10 which forms part of
                     core complex in Type IV secretion system (T4SS); cd16430"
                     /db_xref="CDD:319756"
     Site            order(206..207,209..210,214..215,217..220,231,233..234,
                     239..241,243,254,256,258,260,266,269,271,273,276,278,280,
                     285,289..293,299,302..304,314,316,319,322,324,327,
                     372..381,387,389,391..393,395,399,402..406)
                     /site_type="other"
                     /note="putative oligomer interface [polypeptide binding]"
                     /db_xref="CDD:319756"
ORIGIN      
        1 mddtpsalee dnvstrnknw tlfgilllfl glcglvfwli nkpketfipp ppefepvite
       61 dftdkdaksa lqaqqrtiia leksvselkk erqrlseqva tglerlekri ndsgeeterl
      121 innnldafrd nantdssnpv tppldpfgsl dqyphtppta prgyiddhsl kdipttarrg
      181 iqtfsyrwpk pasetsyrrt sdnyvptgsf vtavligaad anagvnaqgd tapivfrtih
      241 egilpngkrs rikdcfvtas vygeissnrg iarlnrmsci fddngeedil dipvrgtafs
      301 farngmrgtp vmrngkiiqm agisglftgl gdtaknasss titgpsgvvs tvdpskalln
      361 mggsalenig skladyyikl aeqyhpiiel npgsvvnlvf legfpldplm rdgyeqrlsa
      421 qevpqsvgdm asqlmtnmmn plaaqpalpv nplkqqlpaq lqqkanqfda ttqsppqpvy
      481 spikesr
//
LOCUS       WP_284632812             572 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 36 protein [Photobacterium damselae].
ACCESSION   WP_284632812
VERSION     WP_284632812.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Rigden,D.J.
  TITLE     Iterative database searches demonstrate that glycoside hydrolase
            families 27, 31, 36 and 66 share a common evolutionary origin with
            family 13
  JOURNAL   FEBS Lett 523 (1-3), 17-22 (2002)
   PUBMED   12123797
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 572)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10201328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..572
                     /product="glycoside hydrolase family 36 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016052 - carbohydrate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=64388
     Region          126..>233
                     /region_name="AmyAc_family"
                     /note="Alpha amylase catalytic domain family; cl38930"
                     /db_xref="CDD:476817"
     Region          190..476
                     /region_name="GH36"
                     /note="glycosyl hydrolase family 36 (GH36); cd14791"
                     /db_xref="CDD:269892"
     Site            order(196,229,266,341,345,384,399,402)
                     /site_type="active"
                     /db_xref="CDD:269892"
ORIGIN      
        1 msctlnsipf qptanidvsi cheqlnvvyl taesthslsa ttligrfsfp yqgtesiigd
       61 gfqmlaqtgg tieqpqaigr cpdnnseyri yphdapnryy nylvieqegq ftlfgftsch
      121 cfagyfeihd qsiyafidge hcvfkpdtan gitleqivtv vgsnlqdvyq sftkainrnh
      181 pkrndtqrsp vgwcswyayy aevsasdieq nircmtgenk niewvllddg yqaymgdwlt
      241 pserfsdgiq tviakikqqg kqpgiwlapf iaepsseifk qhpnwfvchk egellkaetv
      301 tyggwrctpw yildtshpev qahltsvvkt mreewgvelf kldanywgtl kgaryqkdct
      361 gvaayrlgme aiakgagsaw llgcnapmwp slglvdamrv sddvernphr fsqiaqetfy
      421 rswqhlalwh idpdcvtlid lasqktshns ylfhrdvvla sgglllsgdp lahwtpfaqq
      481 sfhrlverqc qtpnsaefnd lslaqaelil dkqqtlyigf nyndanartv tfdaqgnkdw
      541 fdfwtgecva tsvssyqvql spglnscsvv ar
//
LOCUS       WP_284633456             500 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Photobacterium
            damselae].
ACCESSION   WP_284633456
VERSION     WP_284633456.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..500
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=56913
     Region          <166..500
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mkqwltytae miecrkcsel itffqnvsve qlavaqcwvf ypsddgrfli sdngseqwev
       61 ddfdhpfsha lhhakpilld skklhfwrqs sdfehfsqqv sddesllvvp lpfqshrvka
      121 vvglignkqi innilndenw lkfsqvfisq willrelask hrqelqlnes itqlksnktn
      181 kgrrdlshhl igsspvmesl reqiaiaaqs sltvliqget gsgkelvaka ihtlsdrkdk
      241 afvavncaai penlleself gyekgaftga isarkgliaq adggtlflde mgemplalqa
      301 kllrvletle yrplgsnkel rsqfrlvaat hvnlrknvnq gsfrqdlfyr lyqypldvps
      361 lsnrlndide laevfieqyn qrenrhvlgf dtqtlallkt feypgnvrql rslveyacvh
      421 tdsnqfineq alpktdmsse klvsslpfee iddlklalee yerkiicdrl tffagdraka
      481 aeslglpkrt lahkcqklei
//
LOCUS       WP_284633510            1558 aa            linear   BCT 25-DEC-2024
DEFINITION  NACHT domain-containing protein [Photobacterium damselae].
ACCESSION   WP_284633510
VERSION     WP_284633510.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 1558)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 1558)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1558
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..1558
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=177758
     Region          265..1010
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 maleaggyae klgnryesnw vayqllrllq ekityvivep igddevgvdl vignnddsye
       61 hhqckassgn seywhlsklh ssnilknasf qigrgatefh lvsplssrii sdlcesalns
      121 nampfdfley qvkqsqerek cfnslceylg msveleedir kvmlflqrfk iirydlnkhn
      181 qseledkasf lfsgrstklv qflkyypvey nklrnkitan qllndlkkag fvargipede
      241 rvlsvvdnls kefdesiqpf licnqlikrr eldsitdsle enpvtlirae agvgksslll
      301 elhnylrksg aisvpvrldr rnpednlday gralgfpysp pfslsalskh nkvviildql
      361 dairwtgahs nialhicqel irqtialrke gadisivlas rdfelnedia lsswldsise
      421 slhevtlstl deekvdelvs pfetysqlss vkkeilkipl wlgiyltiad rtqtaprfdn
      481 klelvknfwd drlsqisahh lsveeaekli dklvgimmkq gclsvslnsl pvgsrwalev
      541 lisigvltkq dqrvsfrhqa lydyqvgskl yragsessek llsvlggfdn qtldkrehlr
      601 yalnmlldas qknycssiea vlfsdkvrfh lkflalnslk dlkvikapar klinklvhap
      661 alnkkfists cfknpeiiey liengfledw lsssdeklvd asvgllssis eikpdlvvat
      721 lrpyvdvsds wnqkiynslc wkieddsddm felrkdllqk ncpasyidwr slskrhpqrv
      781 lslievvleh yrevickpry seevrahekl tqrdnwspte ledilgvsdv ipeavisrll
      841 kkvndiaesq pnresvflwl hkdeasdydh dsrltsglfs liekageklg sdpnmlhelv
      901 rpylstanpv tvhlvarlll nlsqnesdnv idwllahpdl hlscgntyre piwilpgkli
      961 gkfsescsle rftalekcis slqsyrslde vrrklearkw gvypsywgqa qhfllpkldp
     1021 trvanstrql idmlarkfes ysyldfcskf estggrvtsp lpfgnklsdk swtrliltpe
     1081 eqfkgkrrkq laaelvaess idqfsqtleg avcnepirfa nlalllprdi naqyvsaffr
     1141 glangskeka hadykegwap csdilldrvi ahfphseseh alvrlldcqs lasdakafhl
     1201 lfhlarhakd pelnrlnvwn pdkgrsaeda sakslmdnsi ncvrgqayia iariffnnel
     1261 lanqnrdvva haivdehpav kmsalellkp ylnydspfah tkfielctkd irvsggygan
     1321 hffnqgfese hvneyielvl rmldsqyvdi rkeaarqiya rwffnelfed elalvltgdk
     1381 elrsgcanvl sqflredkyh drmskiessy rmlvndddkd ilqkvgsciq ydnywakhns
     1441 tvlfsefvks kavkhciydl frklesfpgm lvdmsdslle lvqnivevdk ndesfkhrqm
     1501 hiressllsv lqrlydeate dedddaistc ldiwdellns eiytamsavk vldnglls
//
LOCUS       WP_284633652             486 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Photobacterium
            damselae].
ACCESSION   WP_284633652
VERSION     WP_284633652.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..486
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=53879
     Region          6..476
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mnqtcvlvve dddglreali dtlvlagynw leansaeqal lmlkeqsvdi vvsdvqmsgm
       61 nglsllrsik ltypklpvil mtafanieda viamregavd ymskpfapev llnlvgryap
      121 ikndlgraiv adekskrlln laekvaktda nvmvlgpsgs gkevmsryih ehslrcdgpf
      181 iaincaaipe nmleatlfgy ekgaftgavq acpgkfeqaq ggtilldeis emdlslqakl
      241 lrvlqereve rlgsrksikl nvrvlatsnr dlrqyveqgq fredlyyrln vfpitcppla
      301 erlgdiapla qffaerhcik qglpvphvse caikklccyn wpgnvreldn viqralilce
      361 ekithdhill egvdwldadc lqqaicqqqq vselsesela sdqaaksvep epedtkkped
      421 nskkmivsca dglgnelreq efsiifdtlm acdgkrkdva erlgisprtl ryklakmrsa
      481 gieipv
//
LOCUS       WP_284633773             808 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-mannosidase [Photobacterium damselae].
ACCESSION   WP_284633773
VERSION     WP_284633773.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 808)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 808)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 808)
  AUTHORS   Nascimento,A.S., Muniz,J.R., Aparicio,R., Golubev,A.M. and
            Polikarpov,I.
  TITLE     Insights into the structure and function of fungal
            beta-mannosidases from glycoside hydrolase family 2 based on
            multiple crystal structures of the Trichoderma harzianum enzyme
  JOURNAL   FEBS J 281 (18), 4165-4178 (2014)
   PUBMED   24975648
REFERENCE   4  (residues 1 to 808)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 808)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14312040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..808
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..808
                     /product="beta-mannosidase"
                     /EC_number="3.2.1.25"
                     /GO_function="GO:0004567 - beta-mannosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005537 - D-mannose binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=93340
     Region          23..695
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          732..806
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; pfam17753"
                     /db_xref="CDD:465483"
ORIGIN      
        1 mtislngqwi ltcvqraaiq ditvelpgdv hsalleagei pdphwatned kvqwirecdw
       61 lvsrsfqlte eqltcqamdl vlhdlesive irvnghtvad fnnmfirhkv eilpclkvgl
      121 nhiemvlrhq dptqvaldkl afnmpideqg aaqidlnalr qssclsssfw gvnipvigvf
      181 ddielqplqq irvshistkq nwqesgcela vtlhyeavts rglaiaevtf ddqtfhltld
      241 rdaeqasvlf ridnprlwwp agygqprlyd lrvevdgqli eqkiglrkle vvtepneqgh
      301 nfsvkvndel ikvrgtnwlp ldalpgrmta eryqkllada aeanmnmvrv wgggryekei
      361 fyrqcdalgl lvwqdvmfsd afmlptpdvm tevkeellwq arrlknhsci alwggdnpiv
      421 dgiyqqlpnr qerdkylsny drlmrnirqv leqedpkrlf wvsasyydds ehcrpwqdld
      481 sgdchywdiw hqgldyvhsr khipnfcsef gfqswpslpt vrtiapekhw nisspsmeqh
      541 qrngkgnati vdmftrnyrf pdgfanmlyl sqvqqaivtk taveawrlqe kntgmllwql
      601 ndfspqsscs sveyngrwkp lhyhakrffa pltatfmadn dgvklyllnd srrgevlkge
      661 vvwqswegei lfrdpinqyl epgkclsvwe wltedlagre eegffhvhlr qganiientw
      721 fpkrlkhcel aepdlryeva eidnqlyvmi tsskpaffvh leyqgaghfs dssftlvpeh
      781 qrqikytgpa tleeltaglt vyhlrnsy
//
LOCUS       WP_284634001             391 aa            linear   BCT 25-DEC-2024
DEFINITION  YcjF family protein [Photobacterium damselae].
ACCESSION   WP_284634001
VERSION     WP_284634001.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..391
                     /product="YcjF family protein"
                     /calculated_mol_wt=42444
     Region          41..388
                     /region_name="COG3597"
                     /note="Uncharacterized conserved protein, DUF697 family
                     [Function unknown]"
                     /db_xref="CDD:442816"
ORIGIN      
        1 mndykdflgd syneesgefd hqkaknkaln ekercniiic gasgvgkstl inaifgedvv
       61 kagtgkpvtq hlekvsipek giclwdtkgi eaenyqgtme slnkefskai dqanndsdip
      121 higwvcikas sdrvedrdlt ligilaerni paivvftrvt gkaerefvek akliidkkys
      181 dflrgayvsv nsvpyeided ivvkakgles lievtearfp egkksaknaf lkaqrlkmee
      241 rlmamqegar klvhvaalsa gtagaspipg sdapiiaaiq samiykinte feldadnskm
      301 tsiltgimgv tafaqigktl vsnalkfipg agsliggsis aataisitea vghayiavle
      361 yfydmdtgyv vfpensdril svfkevfsyk k
//
LOCUS       WP_284634020             948 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Photobacterium damselae].
ACCESSION   WP_284634020
VERSION     WP_284634020.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 948)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..948
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=105219
     Region          43..465
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          505..931
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mqkwilplal lsvtnttwaa kqsdiplpkg vsfieqvkpe hgkavipfrk yelsngltvi
       61 lhqdksdplv hvdmtyhvgs areevgksgf ahffehmmfq gskhvgdqeh frliteaggt
      121 lngstnrdrt nyyetvpanq lekvlwlesd rmgflldavs qkkfeiqrst vkneraerye
      181 nrpyglvyer mgealfprdh pyswqtigyv adldrvdvnd lkafflrwyg pnnatltigg
      241 didieqtldw vekyfgsipr gpevnnapkq pvtlkadryi tledkvqqpm lmmgwptsyr
      301 gakdeasldm laqiigdgtn sllyqklvkt gqvvdagafn dcaelactmy vyaigpsgek
      361 gnlksirgkv meivnslekq gvkqqavdei kgvaessaif glqsvsgkva qlaayqtfyg
      421 dpnhlgveld nirkvspssi eaaynqyiyq hpnvtlsvvp qgkldlvaak tnftpeprki
      481 pehqkinddq ltlrtakdnf drsvmpqpsk pveammpsly nvtlangiki lgtqydetpt
      541 velqlvvpag rryeaegkag laqltaammn eattkasaeh iaseldklgs svsfdaglyg
      601 ttitlsslak nlkptlaile qrlfhpafaq adfdrlkkla leglvyehqr pewlagqatr
      661 dvmfkgtvfs qapegtkasi esitladvkd fyqryytpng admvvvgdik pqtlqqdlas
      721 lgqwkgqaap tyhtpklpsi ekpaiwmvdk pgapqtiirl vrqglpydat gelyktqlan
      781 fnlagnfnsr inlnlredkg ytygaggylt ggkelglatf yaqvradasl aatkeflael
      841 kkmsqggltd kemkfmrlav gqqdalkyet pakkaqllgq mltyslpkdf veqrnkiaat
      901 iskseldkla kkwfnpqdyq iivvgdvakl kpqfatlglp ihvikpqq
//
LOCUS       WP_284634258             350 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Escherichia coli].
ACCESSION   WP_284634258
VERSION     WP_284634258.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>350
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
     Region          2..349
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 maltdakira akptdkaykl tdgagmfllv hpngsrywrl ryrilgkekt lalgvypevs
       61 lseartkrde arklisegvd pceqkrakkv vpdlqlsfeh iarrwhasnk qwaqshsdkv
      121 lkslethvfp fignrdittl stpdllipvr aaevkqiyei asrlqqrisa vmryavqsgi
      181 irynpaldma galttvkrqh rpaldlsrlp ellsridgyk gqpvtrlavm lnllvfirss
      241 elryarwsei didnamwtip aereplpgvk fsyrgskmrt phlvplsqqa vailaelqtw
      301 agengliftg ahdprkpise ntvnkalrvm gydttkevcg hgframacsa
//
LOCUS       WP_284634034             395 aa            linear   BCT 25-DEC-2024
DEFINITION  GspE/PulE family protein, partial [Escherichia coli].
ACCESSION   WP_284634034
VERSION     WP_284634034.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..395
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
     Region          <60..383
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 lqtvdedqpa lgyslcatai lsmadvtets ffpqreqdar lspqlmrkig ifgaryshrp
       61 tgdgliavmr lipddgdkvp tfkqlgfipe qirllnvmlr rpegkivlsg ptgsgksttl
      121 rsacrvyldd nqgrhlltie dplegqilga tqtpiicdks deeavklaws raissamrld
      181 pdaimegemr dlvsmmstty aaqtghivlt tlhtnsalgi permitmgmn adlicdaqll
      241 igmisqrlvp tlcpscripw ekrvpelsed draylerhcn kdslcstdni wfrnphgcsd
      301 cnhdviingr krgeigkglt grtviaevie pdnrlfqilk trgkvaarky wlenmhgisr
      361 vehllrrine glvdpleadr iipldederl sidda
//
LOCUS       WP_284634317             665 aa            linear   BCT 25-DEC-2024
DEFINITION  BCCT family transporter [Citrobacter portucalensis].
ACCESSION   WP_284634317
VERSION     WP_284634317.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..665
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73604
     Region          4..510
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 msendtiqkk sksqinkavf ftsallifll vafaavfpdv adknfkllqq qiftnaswfy
       61 ilavalills vsflglsryg diklgpdhaq pdfsyhswfa mlfsagmgig lmffgvaepv
      121 mhylsppvgt petvaaakea mrltffhwgl hawaiyaiva lilaffsyrh glpltlrsal
      181 ypiigeriyg pvghavdifa vigtvfgvat slgygvlqvn aglnhlfgvp inetvqvili
      241 vvitglatis vvsgldkgir ilselnlgla vlllalvlcl gptvlllksf ventggylse
      301 lvsktfnlya yepkssnwlg gwtllywgww lswspfvgmf iarvsrgrti refvtgvlfv
      361 pagftlmwmt vfgnsaiyli mhqgaadlan tvqqdvalal fnflehfpfs svlsfiamam
      421 vivffvtsad sgamvvdtla sggvvntpvw qrifwaslig ivaialliag glsalqtvti
      481 asalpfsvil lisiygllka lrrdltkres lsmatiapta arnpipwqrr lrniaylpkr
      541 slvkrfmgdv iqpamtlvqe elnkqgtish isdtdderir levdlgneln fiyevrlrgy
      601 nspafamaam dndeqqaeqh ryyraevylk eggqnydvmg wnqeqlindi ldqyekhlhf
      661 lhlvr
//
LOCUS       WP_284634870             834 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-mannosidase [Photobacterium damselae].
ACCESSION   WP_284634870
VERSION     WP_284634870.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 834)
  AUTHORS   Nascimento,A.S., Muniz,J.R., Aparicio,R., Golubev,A.M. and
            Polikarpov,I.
  TITLE     Insights into the structure and function of fungal
            beta-mannosidases from glycoside hydrolase family 2 based on
            multiple crystal structures of the Trichoderma harzianum enzyme
  JOURNAL   FEBS J 281 (18), 4165-4178 (2014)
   PUBMED   24975648
REFERENCE   4  (residues 1 to 834)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 834)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14312040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..834
                     /product="beta-mannosidase"
                     /EC_number="3.2.1.25"
                     /GO_function="GO:0004567 - beta-mannosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005537 - D-mannose binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=96416
     Region          23..>644
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          753..829
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; pfam17753"
                     /db_xref="CDD:465483"
ORIGIN      
        1 matllldgqw qltspqhshi aipctlpgdv hsallaaeli vdpyfaenes lvqwvgesdw
       61 lltrefevsq emldhhaidl tlsfvdtvad iqinqhsvlh csnqfqtyhq evksalklgi
      121 nhisillkrs dieakvraek lpfpipwaeg nnqiphmntl rktqchagwd wgicllvsgv
      181 yqsitlepln ntrlvnvrtt qnwlssehcq lelaityqal aafeqqqlti dfnqqvhtia
      241 lpidnqdidk nhtlyytidv hqpkrwwpag ygkqplyple itlneqsitk qigfrqleld
      301 aslddigskm qfvvngqtit akganwipld ampsqqtper yrqllqnavd anmnmirvwg
      361 ggsyeqdcfy qicdelgllv wqdlmfscal ypstvefiqe veqeviqqid rladhpclal
      421 wcgdneviga inwypesrqh rekyvvnydr lnrvlaqiva khdpsrrfwa sspcngeldf
      481 gdawhddncg dmhfwdvwhs gksldayyqv kprfcsefgy qswpslptvk tfadydewnv
      541 tsptfeshqk nkrgnsiite mftryfrfps nfanmlylsq vqqalaikta seywrahknh
      601 crgilywqln dcwpvsswss ieytgrwkql hyhakrffap qlvtfikqdn glltlnavnd
      661 ehkavnyqgq vlqlswqgdi lqtwpingel tsdssdiiwq hfmntsnine keyfyhveit
      721 iecysgsnnr qtskiendyf ptvfkqaklq pgkihtqvie delgiiield ceepclfvhl
      781 evddhlsrfs dssftllpst csgykkqiry igllnkdcie kqlkiyhlsq syls
//
LOCUS       WP_284634871             457 aa            linear   BCT 25-DEC-2024
DEFINITION  M17 family metallopeptidase [Photobacterium damselae].
ACCESSION   WP_284634871
VERSION     WP_284634871.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Lowther,W.T. and Matthews,B.W.
  TITLE     Metalloaminopeptidases: common functional themes in disparate
            structural surroundings
  JOURNAL   Chem Rev 102 (12), 4581-4608 (2002)
   PUBMED   12475202
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087321
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..457
                     /product="M17 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=49788
     Region          40..448
                     /region_name="Peptidase_M17"
                     /note="Cytosol aminopeptidase family, N-terminal and
                     catalytic domains. Family M17 contains zinc- and
                     manganese-dependent exopeptidases (EC 3.4.11.1), including
                     leucine aminopeptidase. They catalyze removal of amino
                     acids from the N-terminus of a protein and...; cd00433"
                     /db_xref="CDD:238247"
     Site            order(50,147,149..151,194,196,224,230,235,238,241..242,
                     274,276..279,281,283..287,293,295,299,336..340,343,
                     369..370,372,377,379..380,385,387,397..398,400,435)
                     /site_type="other"
                     /note="interface (dimer of trimers) [polypeptide binding]"
                     /db_xref="CDD:238247"
     Site            order(220,225,232,243,302,304,306,331)
                     /site_type="active"
                     /note="Substrate-binding/catalytic site [active]"
                     /db_xref="CDD:238247"
     Site            order(220,225,243,302,304)
                     /site_type="other"
                     /note="Zn-binding sites [ion binding]"
                     /db_xref="CDD:238247"
ORIGIN      
        1 mlilhlhhhe ittnrtssll idlgeqenie idfqaedydg tvsksaysia diqdlgcllg
       61 qqlsksrqlt lyitplclqh ieaeywikwl sfglalanyr yqhqptatls tsitqyqlet
      121 sntrwqqafn egkvlalsql tarelinkpg nvlypesfvs aveqlalsgv tlsvldditm
      181 qeqgfgglmg vsqgsnkapr lltleytpan psctialvgk gvtfdsggis lkqpsymstm
      241 ktdmagaaav vgaiqaisal qlpvhviglc glvenmpssq alkpgdvvtm lsgksveiit
      301 tdaegrmvla dvlhyaqqqy qpdylidiat ltgaagialg kayaavmgnd eelikqaqhs
      361 glqcferlwp lpidpwyqdi lasdyadyrh ggetpdgspc vaatflaqfi qpqqkwihid
      421 caamtfqpqr klyskastgf gtllltqlce hiaknni
//
LOCUS       WP_284634955             491 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Photobacterium damselae].
ACCESSION   WP_284634955
VERSION     WP_284634955.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..491
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=55907
     Region          1..491
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mkrldqlvfn ntfrqlpdvf gqavtpigld naflvsanpd vaallelnpe elqtpsfvri
       61 fsgnqqlmqf epiamkytgh qfgqynpdlg dgrglllgev vtdrgqkwdl hlkgsgktpy
      121 srmgdgravl rssireylas aamsglgipt thalaiigse tpvyreqqey gatlirvaes
      181 hirfghfeyl fftrqypalk rlmdyvidhh yldlkqqenp yqalfdrice ttaemiaawq
      241 avgfahgvmn tdnmsilglt fdygpyafld dyipnficnh sdysgryafn qqpgiglwnl
      301 talgyafsaf vdknhiesal ehyqvhlqer ysqriksklg ltlnddgdsa lgnqlftila
      361 eqeadytlff rtlssipyev laeampkfed ivddpmalap wlttykkrik qeltqqtdlk
      421 rleqmkqanp kfilrnylaq qaiehaergh yekieallhv lrdpfsehlq fehlaqqppy
      481 wgkhlpiscs s
//
LOCUS       WP_284634980             276 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Acinetobacter
            baumannii].
ACCESSION   WP_284634980
VERSION     WP_284634980.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 276)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..276
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29914
     Region          12..269
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 milfgkkdqp srnayavvtg agsgigrsfa velakrggsv vcadinleaa eetvelieql
       61 gqkafavqcd vgqaeqvqtl adqaeqlldh pvtliinnag vglggkfdem sledwkwcmh
      121 vnlwgvihgc hafvpkfkkl gygaiinvas aasytaapem svynvtkagv lalsetlsae
      181 lrkfnikvnv lcptlvptni ikngripgry skladhalmn yamttsdava tltlnrldrg
      241 qlyttpqida klfwlmkrts ptlyakflgl syqlfk
//
LOCUS       WP_284635169             425 aa            linear   BCT 25-DEC-2024
DEFINITION  protoporphyrinogen/coproporphyrinogen oxidase [Brachyspira
            pilosicoli].
ACCESSION   WP_284635169
VERSION     WP_284635169.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Pawelek,P.D., Cheah,J., Coulombe,R., Macheroux,P., Ghisla,S. and
            Vrielink,A.
  TITLE     The structure of L-amino acid oxidase reveals the substrate
            trajectory into an enantiomerically conserved active site
  JOURNAL   EMBO J 19 (16), 4204-4215 (2000)
   PUBMED   10944103
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440906
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..425
                     /product="protoporphyrinogen/coproporphyrinogen oxidase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006779 - porphyrin-containing compound
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=50170
     Region          1..421
                     /region_name="HemY"
                     /note="Protoporphyrinogen oxidase HemY/PPOX [Coenzyme
                     transport and metabolism]; COG1232"
                     /db_xref="CDD:440845"
ORIGIN      
        1 mnkviilgsg lagiasaykl kqnniefeif ekeneygglc rrlkigkfif drfphfsftk
       61 nkeirelfdt ssneyyship nianyykslw lgnptqnnly pldkeqkiei iegfknrpni
      121 enpknyrewl dasfgyyfak efsdkytrky wttepenmsv dwvgyrvmks nldeieygaw
      181 nkeskskyya semrypkhgg fqsffdswtp keniklnhnl irwnvkkkel lfdngyktny
      241 dkiistlplt yianiiedip dnvkeaaskl yytsgytvsi glkgkvnvpy lwfyiydegi
      301 lfprvyiatl kspynapegy sslqteipcs kfkqinlsnn eivehtinkl vemrifdykq
      361 vefaqldyhq yanilftldt etnkkivldw lkendiltag rygkweyfwt dqainsgfei
      421 vndnf
//
LOCUS       WP_284635245             241 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Brachyspira pilosicoli].
ACCESSION   WP_284635245
VERSION     WP_284635245.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..241
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27776
     Region          4..233
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(14..15,17..18,21..22,60,64..65,68..69,83,87,94,
                     97..98,103,118,130..131,133..135,137..138,141..142,
                     145..146,171..172,174..176,178..180,182..183,185..186,190,
                     193..194,200,202)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(129,133,136..137,139..140,185,188..189,191..196,
                     199..201,205,207)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(150..157,173,176..177,180)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mnnrfdprti flstifftvs limmkninqi iffiiviiih ilfvginvgn ilkiflasiw
       61 lllsiifiny fligrdvyyi lnttsrlffi iilaavmlss mtvidigfai ekifyplkyl
      121 kipienisii ialslkfipl ikdeavrifk aqkargldyd iisiydkiln vtsifipivv
      181 laiqssikta iameirgynd sskktrlyes slrlkdyvyi lfsiacffln lllrkleini
      241 f
//
LOCUS       WP_284635380             402 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Brachyspira
            pilosicoli].
ACCESSION   WP_284635380
VERSION     WP_284635380.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..402
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45037
     Region          5..399
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mnkiipfspp ditdneieav vnvlksgwit sgvvnkelee elckyinvkr vkllssatma
       61 melalkifgv tegdevivpa ytyastanva ihlgakvvfi daadndfnid leklekaits
      121 ktkaviavdv ggkpcdydgi ikilekkkdl ftaletnkyq kqlnralfll daahsigafy
      181 kgnrvgsqad fssfsfhavk nvttaeggal sfndigdina deiykevsvw alngqnksal
      241 dktklgswry dievagykcn msdihaaigl sqlkrydeml knrknivniy nsvldaskkv
      301 ilpvfkddea essyhlyllr ikdyeeadrd lliekmaelg ivlnvhylpl pfhkvykdya
      361 dndyinafnl yknevtlply stlkeedaly iaknifryle sn
//
LOCUS       WP_284635410             169 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Escherichia coli].
ACCESSION   WP_284635410
VERSION     WP_284635410.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..169
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
     Region          <1..157
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 eidftnrvwt ipatrepiig vrysgrgakm rmphivplse qsiailkqik ditgnnelif
       61 pgdhnpykpm centvnkalr vmgydtkkdi cghgframac salmesglwa kdaverqmsh
      121 qerntvrmay ihkaehlear kammqwwsdy ldicrkayvs pymmvqenr
//
LOCUS       WP_284635431             295 aa            linear   BCT 25-DEC-2024
DEFINITION  SPL family radical SAM protein [Brachyspira pilosicoli].
ACCESSION   WP_284635431
VERSION     WP_284635431.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Berteau,O. and Benjdia,A.
  TITLE     DNA Repair by the Radical SAM Enzyme Spore Photoproduct Lyase: From
            Biochemistry to Structural Investigations
  JOURNAL   Photochem Photobiol 93 (1), 67-77 (2017)
   PUBMED   28027411
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Frey,P.A., Hegeman,A.D. and Ruzicka,F.J.
  TITLE     The Radical SAM Superfamily
  JOURNAL   Crit Rev Biochem Mol Biol 43 (1), 63-88 (2008)
   PUBMED   18307109
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Sofia,H.J., Chen,G., Hetzler,B.G., Reyes-Spindola,J.F. and
            Miller,N.E.
  TITLE     Radical SAM, a novel protein superfamily linking unresolved steps
            in familiar biosynthetic pathways with radical mechanisms:
            functional characterization using new analysis and information
            visualization methods
  JOURNAL   Nucleic Acids Res 29 (5), 1097-1106 (2001)
   PUBMED   11222759
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18546879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..295
                     /product="SPL family radical SAM protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=34886
     Region          5..275
                     /region_name="SplB"
                     /note="DNA repair photolyase [Replication, recombination
                     and repair]; COG1533"
                     /db_xref="CDD:441142"
ORIGIN      
        1 mikyreinck salnkinnky gfcydlniyr gcihkcyycf avyshkyins rdffgeifvk
       61 kniaemleke lssrnwkrdi inlgsvtdny qdaekdyklm rdilklliry ktpmcistks
      121 dlilrdfdli delsnivpvr iavtittlne klssliepnv isplkrleil kefkktkatv
      181 aihtmpvmpf itedelenif ktakecdidy caadalklcg ecrkiflnfv renfpnhykk
      241 ylyiygsngi lkddykekmy kkikaleeky nisyksreel hkekiniqee emllf
//
LOCUS       WP_284635526             293 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Brachyspira pilosicoli].
ACCESSION   WP_284635526
VERSION     WP_284635526.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..293
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=34290
     Region          31..274
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 menninenin vqpqeqnsnn dsnsaslpnn efkvslssid yegplsilfd mlkrsekniy
       61 evsileiidq fieylkeqaa lnldstgefl vvasdfhlyk skmllphdmd ddkftdrlkf
      121 eiveqmlefq rykmvseeld rlqeysdsif erkdtervkf fqnnssnedn emawkdvtly
      181 dlvyaftkvq fvpetdlavl sgmsnfhidn aidmirikla eedvfpfivl fkdgvtkrql
      241 vtfflamlel vkekeillkq dikfgdiyvf krkdnnnnnn nnnnepnqdl nne
//
LOCUS       WP_284635603             349 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Brachyspira pilosicoli].
ACCESSION   WP_284635603
VERSION     WP_284635603.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..349
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=40077
     Region          7..>185
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          20..44
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          51..78
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          117..147
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          152..178
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdnieneike iiketnenil naintfiekn nldyakkial qlinkepnyk egylvlsdif
       61 ydeedyksvi hildkalehl pkdkdilesk iealistyky eearetieel islgnvnasv
      121 ygqygvllsi emkykeaiek fkmaisldke dvlsminmsi vyaaiyeydn aieilekafs
      181 iskdsniqdk idnikrqken sifnfskftv inakpdkfnl ivpenfnasv ennvlkiend
      241 ektisillsy dnskydekei aqilnnfkae nknlysiisp lyvakrkenn difgsiifnc
      301 ktknnnlfna maivvkeees ivltiistla tsnnliflak eiinslyik
//
LOCUS       WP_284635680             251 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Brachyspira pilosicoli].
ACCESSION   WP_284635680
VERSION     WP_284635680.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..251
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29391
     Region          16..139
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 msevkknyyg slctemyeil hkkapedeln fylsyaekgk kileplcgsg rflipfierg
       61 fditgidmsn emlqklklkf pnaktihtdi meydpkekfd yifissgsvs lftdidickq
      121 iltriknwlc ktgkfvfavd tiknrciddn dyniavsvkt kenfeivlks knyyeektqt
      181 qfspsiyemy nnaeliqsef mdfqthlyky gemeqylkev gftqvktfss fekeiavnde
      241 cdmflfecsf l
//
LOCUS       WP_284635722             425 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Brachyspira pilosicoli].
ACCESSION   WP_284635722
VERSION     WP_284635722.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469162
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..425
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=49507
     Region          341..>419
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          347..371
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          376..409
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkrlknnkly llltlvlvaf aylytsliaq tssdrisien yndlpnsrrl vtklnikhie
       61 enkvevswvg iyhpnlmyyv yrsedpilsk tvltnakvva stkatnastt ytiydnlpky
      121 dkyyyavisy idninfytat enmdlmqfey ydpfkndmtn inneintnei itnniitndi
      181 itndlntnnt yftndmltni vssndflsyy pntnlfdtny tilpptnyvd lyyttnrids
      241 nrgivfstny ynytnyynlt nnytnyyntt kiyiinptnd sltneintnd fvtndftnqs
      301 rmvenvtnel kvtsftndkn enivnveikk dntkktptey qrysseyqra laqfkannya
      361 aaikilepis rkkvdsalyy dinlllgksy ksagrkknal dtlkkiksin pnevnfwinq
      421 vlsdl
//
LOCUS       WP_284635729             758 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Brachyspira pilosicoli].
ACCESSION   WP_284635729
VERSION     WP_284635729.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 758)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 758)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 758)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 758)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..758
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..758
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=81769
     Region          1..757
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mkmtlkiggm hcaacsrave ralkktdgie eanvniatek avfnydekkl kyddivnvvv
       61 kagyqvlgke edpavvkare ikeqkirliv saifsiplfy ismapmvsfv kfpipsflvh
      121 hinpqvfsiv aiflcvpvmi sgykfytlgf palfrgspnm dslvaigtta afsysiystv
      181 lsfmglnphg dnlyyesaav iitlvqfgky learskgktg eaikklmglq pktatiiqng
      241 eekeikisdv kvddivlvrp gekipvdgei iegyssvdes mltgesipve ksvgdkvvga
      301 sinktgsfkf kaqkvgadta laqiiklved aqgskapiah iadvvssyfv pavitialis
      361 giiwfitlhn fvfsltvfvs vlviacpcal glatptaimv gtgkgaelgi lfknaealev
      421 sqkinavmfd ktgtltegkp yvtdiisddk dkllliaasa engsehplge aivreskekn
      481 ikllsienfk aisgfgiety idnkkvlmgn dklmnkenin ienynsymdk lskegktpmy
      541 vaydnkllgi iavadklkke sieainrlhk lgiktamitg dnkntansva keagidivfa
      601 evlpeeksne vkklqeqgft vamvgdgind apaltqanvg iaigsgtdva iesadivlvk
      661 sntndvvtai elskatmrdi kqnlfwafcy nvigipiaag vlhvfrepli assiggflta
      721 imgkdlllnp ifaalamsls svsvvtnalr lnffkpsk
//
LOCUS       WP_284635734             279 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Brachyspira pilosicoli].
ACCESSION   WP_284635734
VERSION     WP_284635734.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira pilosicoli
  ORGANISM  Brachyspira pilosicoli
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Brachyspira pilosicoli"
                     /db_xref="taxon:52584"
     Protein         1..279
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=32336
     Region          39..240
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          65..93
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          99..127
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(100,103..104,107..108,110,134,137..138,141..142,
                     144..145,168,171..172,175..176,179)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          132..162
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          167..194
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 milgfkvlek mkikivilfl llfslsftyd asninnayrl yraknykkaa elleeeiktt
       61 pilkieyyem lanaymyikd ynnmlrvard giivnrfshk lyfqkgyaly klgktneaie
      121 pvrhslilnp ddaymnnflg llylytedyk laeasflkan iystnnivym inlaatyerd
      181 knyvsalkiy edvynidkty rnvaesinrv knylgytned ikvvntveta hnedtevnli
      241 npientnqtv itnniytnni intnstvntn dtnssttnq
//
LOCUS       WP_284635811             300 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Escherichia coli].
ACCESSION   WP_284635811
VERSION     WP_284635811.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..300
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34453
     Region          10..293
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mgkhdklgyr lgliltrlnn geslavrels eefnvcekti rrdltqrlsy lnlirqngry
       61 rlsdgvlgqr snadlrhftr ilgieglfpr wddrllsill gntknnpfli kqrpyencgs
      121 fmsilnvlsd ailsqkkvnf nykdrefrav epyrlvndng lwylaaahds tlksfvissv
      181 kdvcmsnisf riipeineki ektdgiwyse dlikvlisvs ahvapwfthr hllpgqeiih
      241 tsrsgdllvi srvthtdqim plmkywipdv eviqpssirq qlaedmqsal krytqpsnap
//
LOCUS       WP_284635863             445 aa            linear   BCT 25-DEC-2024
DEFINITION  maltoporin [Klebsiella pneumoniae].
ACCESSION   WP_284635863
VERSION     WP_284635863.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..445
                     /product="maltoporin"
                     /calculated_mol_wt=49327
     Region          1..445
                     /region_name="LamB"
                     /note="Maltoporin (phage lambda and maltose receptor)
                     [Carbohydrate transport and metabolism]; COG4580"
                     /db_xref="CDD:443637"
ORIGIN      
        1 miklkhsipl allslagass pacadpkydf alhgyirsgi lansdgnrad svglmpdgkw
       61 rlgneedtki eliptvtlta dsgvvakvqa nlthqskcts dwncqdddgh dvqfregfae
      121 lsnldfapem tfwagkryss sntsshqfdw eyiqyngtgg gfdnmdlgfa rfdagvyafs
      181 ptdetkaypv dkgdqgypdd yslnlwlkki agtgfdleli ghhmnrnenh ptsaekgygv
      241 tgiynfdgfy gltggysrla lqygkglaag dslgkngwgw anlentqswr vvldsvasmg
      301 dleistfafw qkdknyrwwt edengwgrsm wvagirpyhq itrnfamqye lgyeylddkn
      361 ykgvngkgkg gltkvtvapt ltfdsgfwar pqlrffvtya kwdkgvsdal dgnynwdtnt
      421 itaggyshsg stdtvnfgvq aevwf
//
LOCUS       WP_284635919             497 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Citrobacter portucalensis].
ACCESSION   WP_284635919
VERSION     WP_284635919.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..497
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55298
     Region          21..457
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mqgtkirlla ggllmmatag yvqadalqpd pawqqgtlan glqwqvlatp qrpsdrievr
       61 llvntgslte saqqsgfsha iprialtqsg gldasqarsl wqqgfdpkrp mppvivsyds
      121 tlynlslpns rndllkesls ylanisgkls itsetvnhal nsedmvatwp sdtkegwwry
      181 rlkgstllgh dpadplktpv daskiqsfyq kwytpdamtl iivgnvdars vaeqinktfg
      241 elkgkretpa paptlsplra eavsimtdav rqdrlsimwd tpwqpiresa allrywradl
      301 arealfwhiq qeltknnakd iglgfdcrvl flraqcainv espndklnan lgtvarelak
      361 vrdkglpeee fnalvaqknl elqklfatyg rtdtdilisq rlrslqnqvv diapeqyqrl
      421 rqsflnslsv emlnqdlrqq lsqdmalill qpkgepefnm kdlqatwdsi mapvtaaats
      481 vetdeshpev tdippvq
//
LOCUS       WP_284636098             218 aa            linear   BCT 25-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Corynebacterium accolens].
ACCESSION   WP_284636098
VERSION     WP_284636098.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..218
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=24392
     Region          3..200
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mlicqemfll ltkdngkkev lsnnetalra glfsdlllhe avaitaknkv hatdkkpehp
       61 vlawawdslh ehrtgsvktl lqarwfspre kiaqdfqdrg qleiedsaww qlggdryimt
      121 dtaledevre rlaavldgtq spstkdviil dilrevngay pllkedapem krremrnrik
      181 elkqqveydd aaasavktil qettaiiaav avstagtt
//
LOCUS       WP_284636250             256 aa            linear   BCT 25-DEC-2024
DEFINITION  inositol monophosphatase family protein [Corynebacterium accolens].
ACCESSION   WP_284636250
VERSION     WP_284636250.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..256
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=26646
     Region          5..252
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mmdprelvaf aeaavdqvep ifrsgigapp ahfksrgdfa tevdlaiekq lrdilqqmtg
       61 ipvygeesgg siqdtvwvvd pidgtanysa gnpmagilva lvhegqtvaa isdfpllgrr
      121 lvasdgsplr saggpsggfg ggeespefdd arghvgcfsn lptaafhelr esglrpritg
      181 svgldnafva qgvfdgavnf sphpwdnaag allikaaggi vtdpegnpwt vqsrgmvsgt
      241 pqvhetilei lshhsn
//
LOCUS       WP_284636452             240 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium accolens].
ACCESSION   WP_284636452
VERSION     WP_284636452.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..240
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26190
     Region          12..204
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mttvsnsqll prpaaifwdm dgtltnsepl wgeatyylse vlgkrltpsq rmdtvgatft
       61 ttlricadna gvilgegdve ayrhkmfdym ktlfagrlei fpgipellts lhhdgmpmmv
      121 ttntdrdvad aaiavigsey fvdticgdev ptgkpapdmy leaarrlqld ptqclvfeds
      181 pagmraavaa gctviglped egvevpdgvv eisrlrdsrh lagalhtdvy ewfraiqemn
//
LOCUS       WP_284636548             524 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Corynebacterium accolens].
ACCESSION   WP_284636548
VERSION     WP_284636548.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..524
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55522
     Region          128..515
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mttphthest aqsegaedpg aprnewrrqf iglfiglala ilvffifpsn aidtvqqstg
       61 vdeeadytls airtvaavti lmgvwwmtea iplaatalip lvifplasvg tikevgapya
      121 satiflfmgg flialslqrw nlhrrlalyv vkligtsprr lilgfmlatg flsmwvsnta
      181 tavvmlpigt svlaltaetv ggwdkqkkfa talmlgiays asigslgtli gtppnaflna
      241 ymadtwdvtl gfgrwmavgv plaltfllia wvllitifkp emteipggre lindeikalg
      301 pwtrpqimtg iifilaalaw vslpivlgdf dnyddaivgi aagillfilp adserrirll
      361 dwktanempw dvlllfgggl slssafnssg lslwigemak glsalpivli vaavaalvlf
      421 lteitsntat aatfipimgg vavgvgltge gdinvlllti pvalaatcaf mlpvatppna
      481 iaygsgyvki gemikggvgl niigiflitl tvfllavpif gltv
//
LOCUS       WP_284636776             381 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium accolens].
ACCESSION   WP_284636776
VERSION     WP_284636776.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..381
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41784
     Region          11..356
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mrtqasvkrl pqhlpeldgl ravaalgiiv thvsfqtgtg wgfagrfdff vavffalsaf
       61 llwrrrglht vrgyahsria rlapayyacv vsvvlllpda hsitptqila nltstqiyvv
      121 dglapglthl wslcvefffy lvlpllvwai gglpqrwrma viagaavlsw gwgfipfvad
      181 ysedqvnsqi wppayaswfa vgmlaaevee rgigkrtari lqvrwawvvl aglvlwvasr
      241 dwfgpaglvh pepaefarri iagaifaacv vvpvalvprg tswltsplmq algawsysif
      301 lwhvavlava fpltgvalfs gkpldfwvil avtvigtivi saasytlier pgrdllmgrv
      361 rgrgqgrrrr kgrpaprhis t
//
LOCUS       WP_284636884             119 aa            linear   BCT 25-DEC-2024
DEFINITION  FluC/FEX family fluoride channel [Corynebacterium accolens].
ACCESSION   WP_284636884
VERSION     WP_284636884.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   McIlwain,B.C., Gundepudi,R., Koff,B.B. and Stockbridge,R.B.
  TITLE     The fluoride permeation pathway and anion recognition in Fluc
            family fluoride channels
  JOURNAL   Elife 10, e69482 (2021)
   PUBMED   34250906
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Li,S., Smith,K.D., Davis,J.H., Gordon,P.B., Breaker,R.R. and
            Strobel,S.A.
  TITLE     Eukaryotic resistance to fluoride toxicity mediated by a widespread
            family of fluoride export proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (47), 19018-19023 (2013)
   PUBMED   24173035
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Stockbridge,R.B., Robertson,J.L., Kolmakova-Partensky,L. and
            Miller,C.
  TITLE     A family of fluoride-specific ion channels with dual-topology
            architecture
  JOURNAL   Elife 2, e01084 (2013)
   PUBMED   23991286
  REMARK    Erratum:[Elife. 2013;2:e01700]
            Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..119
                     /product="FluC/FEX family fluoride channel"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:1903425 - fluoride transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:1903424 - fluoride transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12931
     Region          5..106
                     /region_name="CRCB"
                     /note="CrcB-like protein, Camphor Resistance (CrcB);
                     pfam02537"
                     /db_xref="CDD:460582"
ORIGIN      
        1 mnllfvligg ffggaarygf trllpspyct fasnilgslv fglavgfaql adapfahplf
       61 alglagglst wstmakelge mvkqrqwwpl ckylfwtigi gvvlawrgvm waeliyhgi
//
LOCUS       WP_284637502             165 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium accolens].
ACCESSION   WP_284637502
VERSION     WP_284637502.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 165)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..165
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17816
     Region          86..161
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdslesrlhd learvarleg kssippqaps eestywlvda lapstqlpdg svifggnial
       61 gkrtyayqwq rpttaitdee wsenlerlaa lahpvrgeil rrllaapata aelvdedivs
      121 stgtayhhls altsagwttk tsgeysirpa rvipllaiit asedh
//
LOCUS       WP_284637602             359 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium accolens].
ACCESSION   WP_284637602
VERSION     WP_284637602.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..359
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38632
     Region          63..358
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mkrlnsvlaa aavctglaya pmagaaeltp qqvagdaaqs tispleptpe iegkswykky
       61 kddarvekle atspamngrk iplavvraqh enrptvylln gaggaeqdmd wlklsdavdf
      121 yhskdvnvvv pqagafsyyt dwisepnsgf lkgpqkwetf ltkelpgaie khinadnhra
      181 iagmsmsats slllaqhnqg fydavgsfag caataypier qgveltvgrg ggsvdqmwgp
      241 lgsptnrynd ammnaeklhg telyvssgsg laseedtfsy iqskgynplq aaqgsatlqv
      301 eggaieagvn ycthnfkakl dqagvpatfn frntgthswp hwnqdlkdsw pvfergfns
//
LOCUS       WP_284637678             137 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Corynebacterium accolens].
ACCESSION   WP_284637678
VERSION     WP_284637678.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..137
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15172
     Region          4..133
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mmatdnahth qvptrwgdfd myghmmnany ievaqearla fakeniyakg ihfmalvrhl
       61 dvdymrpipf egnahvivet tvshigsssf ttsqqvktaa gevaatvncv qvvidkkkht
      121 prpltdeekd ilqmsas
//
LOCUS       WP_284637874             451 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Paenibacillus silviterrae].
ACCESSION   WP_284637874
VERSION     WP_284637874.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..451
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50360
     Region          1..443
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 msqfesarea vdwvtrfipt vgikpglkrm erimellehp errlkfihva gtngkgsvca
       61 ylteilktcg yhvgtftspy iekyneriri ngenisdedl latinkikpa idavaatelg
      121 qpsmfeistv iaieyfarea cpdyvvwetg lggrldstni vtpvisvitn ighdhmdvlg
      181 dsleqiaaek agiiksgvpv vsaveqpevi rvieetakak kstlyllgre fhfetlsske
      241 ndqrfrfqgt frnvpelsis mngahqlkna svalmtievl rqyyalived edlqkamkea
      301 fwpgrlelvs reprtlidga hnpegaevla galkdtfsyt klhfmmgmlg nknhtgyfrh
      361 ilpivdtlil tepdwhkkaq aaelaglart llaeigrtdv evivepdwkt alellkrrta
      421 qddlavvsgt lyligdvrsw inhqtdsekg w
//
LOCUS       WP_284637913             410 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Paenibacillus silviterrae].
ACCESSION   WP_284637913
VERSION     WP_284637913.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..410
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43843
     Region          9..403
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mdvknfkkag hfpslmsafl yfdvsfmiwv lcgalslyit rdfgltdaqk atmvaiptlg
       61 gsifripmgi ladrigskka gmigmsltil pllwgwlggv slnqvyafgf llgiagasfa
      121 vslslasrwy ppqyqglamg iagagnsgta latffgpqla naygwnnvfg maiiplllvm
      181 iayalmakda pnqpapkslk dylsvlkvpd twwfsifyai tfggfvgfss yfniffydvy
      241 gdkvmegglt kvqvgylvti tviagsffrp iggyiadkig gmrfmlllys iiticaygis
      301 lmpssfvvml iitsimmacl gmgngsifqi vpqrfskeig vvtgivgaag glggfllpnn
      361 vlgplkqatg shvtgflvva sivlivtlvf yavtrswrka watadsgvnf
//
LOCUS       WP_284638120             272 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Paenibacillus
            silviterrae].
ACCESSION   WP_284638120
VERSION     WP_284638120.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 272)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..272
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30135
     Region          1..246
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mknlnvlitg asggighela ktfaennnnl iliarniskl keirsellkq nisitiiqkd
       61 ltepgaaydi yeemsrrkir ihvlvncagv gvygdslect iqqksqmlki nidtltnlth
      121 lfakdmvddk fgrilnigsi ssvmptpfms lyaatkayvl sfsealnsel irkgdiavtt
      181 lcpgftktnf iteanlghme tllnrialsp svvakqgyna lkkkksvkvv grlntlmlim
      241 irilprnwvq slafhllrdh sklksnpqqn pd
//
LOCUS       WP_284638472             731 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium accolens].
ACCESSION   WP_284638472
VERSION     WP_284638472.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 731)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 731)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..731
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76622
     Region          2..725
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mshvdlgvsg mtctscssrv erklnkvdgv easvnfates asiefdpets tpadlikvve
       61 gagysafdms gsddgdqded adaegtpvdd araaeqhnll rrtiisavls apimvvsmvp
      121 alqfqnwqwa camlativfi fggapfhsat wtnlkhgsft mdtlismgts aaylwslyal
      181 ffgnagepgm tmsmswssss aemdhiyfes vgmvitflll grwfevkakg qssealrtll
      241 smgakeasvl rdgkekripi sqlqvgdvfv vrpgekiatd gevvsgnsav dasmitgesv
      301 peevgvgdtv tgatinasgk levkatqvge dtvlsqmatl vtnaqaskap vqrlvdriaq
      361 vfvpvvigis vltllvhlif ggvapafiaa vsvliiacpc alglatptai lvgtgrgaql
      421 gllikgpeil estkqvdtiv mdktgtvtag emsvtavhgd vldyaaaver nsehpiaqai
      481 arerdvepgt dfststagve atvdgvrvgv gkprgslgqy egafreaeaa gatpvavyld
      541 delaglievr dtvkptsaea veqmkelglt phlltgdneg aakrvaeevg itevtagvip
      601 eekvdvikkl qseghnvamv gdgvndaaal aqadlglamg agtdvaieas ditlmngdlr
      661 saadairlsr rtlqiikgnl fwafayniil ipvaafglln plfagiamal ssvfvvsnsl
      721 rlrkfstqry d
//
LOCUS       WP_284638536             270 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Paenibacillus].
ACCESSION   WP_284638536
VERSION     WP_284638536.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..270
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31246
     Region          14..269
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          182..265
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 meitridlpe ngillyeskh gdghevaehr haihqilyvl dgngyitmeg krseltpdnf
       61 vlivprsdhs ivsvrrltll vlafeeaalg eevqrgllmk qlrqsmvlyi npmmatdirq
      121 llrkmmfeqg nhdalcswal rvylqevlll lsrsqqqgak adsnhyraer irkyiddnyf
      181 kpitngdlss kmnmsarhvn gifkecygit pfqymtevri raaqkllset dkdivticfe
      241 vgyenvptfy rsfrnvvklp pnkfrqqhke
//
LOCUS       WP_284638626             286 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus
            silviterrae].
ACCESSION   WP_284638626
VERSION     WP_284638626.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..286
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32747
     Region          27..286
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          196..279
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqdygmeyae llfyspteqe rlrglwplra grnlakptyr vgprvmetys lhfvmdgavr
       61 llyeeqqiel eegdffcvfp gikyeymqps dsrqplkmcw ltvdgelvpe llqetglsee
      121 kpyarrmmtr elerelvgal aaftqanepg gyarlmsaly gvfsalqagk greaagrkdd
      181 wlersirfme ahfceritve daaseagihr syfstkftek lgiapakylq klrmekaasl
      241 lldsewpvte iaqavgypei ysftrffthy yglppsryrk eggnap
//
LOCUS       WP_284638652             178 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: deoxycytidylate deaminase [Paenibacillus].
ACCESSION   WP_284638652
VERSION     WP_284638652.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Maley,F. and Maley,G.F.
  TITLE     A tale of two enzymes, deoxycytidylate deaminase and thymidylate
            synthase
  JOURNAL   Prog Nucleic Acid Res Mol Biol 39, 49-80 (1990)
   PUBMED   2247612
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788416
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..178
                     /product="deoxycytidylate deaminase"
                     /EC_number="3.5.4.12"
                     /GO_function="GO:0004132 - dCMP deaminase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006220 - pyrimidine nucleotide metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0009972 - cytidine deamination [Evidence
                     IEA]"
                     /calculated_mol_wt=20167
     Region          12..169
                     /region_name="ComEB"
                     /note="Deoxycytidylate deaminase [Nucleotide transport and
                     metabolism]; COG2131"
                     /db_xref="CDD:441734"
ORIGIN      
        1 maeqqekstt prkdwdtyfm dmaymastrs qcsrrhvgav lvqgkkllga ayngapmgvq
       61 dcseagcmlv eeyelvkeeg qeqvikkqrc irtihaeqnl llftdrkdre gsvvyvtdqp
      121 cwtcanmlan sgiieivfhr pypkdsdkvr llmeqkgvrf raleeyeppa gamsevqh
//
LOCUS       WP_284638637             319 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Paenibacillus silviterrae].
ACCESSION   WP_284638637
VERSION     WP_284638637.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..319
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35518
     Region          13..300
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 metmlkedvq alrriqtnle scilgktdei mllltamigg ghvlledvpg tgktvlikal
       61 aksisgqfrr iqcnpdllpt ditgvsiyhp kdevfmfrpg pimtnillad einrattktq
      121 salleameer hisvdgethe lpkpflmlat qnpidfegty mlpeaqldrf mmkfslgypd
      181 eatetrmivs qsivhpldel eavaevdqil alqkqvkqvh leeavagylv sivratrehp
      241 siylgaspra tmalvqaska yallqerdyv ipddikflap yvlghriilq aearmegatv
      301 gtvlqsvfqq vrvpvrwek
//
LOCUS       WP_284638656             299 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Paenibacillus silviterrae].
ACCESSION   WP_284638656
VERSION     WP_284638656.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..299
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32151
     Region          2..293
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mstkwkasiy vlfgaasygi lssivklgya agfsasevtg sqvmfgaaml wilcyttgsf
       61 rkvtkssilk llaggsftgm tgvfyyyslq mldasiavll lfqftwmgll ldwllqgkrp
      121 grnqgwavll ilggtllatg fsyeslaqld tlglilglls aasytffiyf sgrletelpa
      181 lqrsawmitg asifvaviyp pqflwngslq qglwlwglll svfgmvlptf lyakgapkld
      241 tglssvlgai elpvvilcsa lllgeasgpl qwigiatill giavseikps esrqsrksr
//
LOCUS       WP_284638819             267 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Paenibacillus silviterrae].
ACCESSION   WP_284638819
VERSION     WP_284638819.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..267
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30105
     Region          9..254
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mayiqtqlys evlgtemdvs iivpqekqpy agdgrlkvlw llhggsgdht awqrmssier
       61 iameyglavi mpgafqscyt dmvhggryft ylseelprii rhmlprlspa rednyisgys
      121 nggygclrvg larpdlfgai gafsagdksd iefvndgsqr akdrimlfge gdfkgtendl
      181 khlgreglki gksvarvyhg cgsldpwldl nlllrdffls legnpykyhy heaeghghtw
      241 qfweqelvrf leylgldkte gqylmgm
//
LOCUS       WP_284639015             752 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium accolens].
ACCESSION   WP_284639015
VERSION     WP_284639015.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..752
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=82154
     Region          29..745
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mnsapknspa tqspadatss sradnagisa ieaeqnyvdg lfdrlddeva aanarlnevq
       61 aevdpatpda dalvrretey hglqakldrl nvaqmglvfg rididapgdn pteegldrry
      121 igrmgldare enyrtllldw rapmarpfyl attaqpegvh trrqirmtgr tvtdvndeal
      181 dgpgvreeea gvasesalyf amqrartghm ssivetiqre qdeiirdntr gvmvveggpg
      241 tgktavalhr vayllythre qlsstgvliv gpntnfldyi srvlpelget gvvlstiggl
      301 fpgitpthte glvgreikgs aamaeilsaa vkdyqqvpse pqditvdglt ltitpsmvkr
      361 artrarrsrk phnqaceafi ehfvedlaqe matkvgtdpl ggenllsrad vdqfhddlav
      421 desvvgcidd fwpeldpsev laallssrer iasaargyde etqaalyrpd gyawtdsdaa
      481 lldelavlig lpnpeekkaa kdaewreqia daedaldils ssestdnddd mfeaeilsah
      541 dvidaetlaq rqevrdtrtt aqraredhtw afghiivdea qeltpmewrm lfrrcpsrwm
      601 tlvgdtsqtg spagvddwge alepfiaqrf rhhlltvnyr tpepitelan gllasidpda
      661 tpaiairdge pvrrladatf tpgvtteddg rltavidatn aeavkglefd hvivlnprei
      721 vdaspqglqn lyvcitratq tltlvgntag vl
//
LOCUS       WP_284639044             332 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium accolens].
ACCESSION   WP_284639044
VERSION     WP_284639044.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 332)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18950610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..332
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=37209
     Region          40..163
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
     Region          176..319
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mpsakkmhet dkdkksekfi sgrhqeipvv pakefprttl aagavvwrgd panpeialih
       61 rphyddwslp kgkvdpgesl pttaareiee etgfhvrlgk ligkvtypvq grtkvvyywa
      121 afylsgtytp ndetdelrwv pidqaqqlls ydvdndvvsk aqkrlqlapt trllyvrhah
      181 ahdrkkwegd dnlrpldkkg rrqaemlvpm laayhptaiy sarphrcqqt aapladelgk
      241 diainkdfgd eaweknpaaa kkafrrvved ggvpviisqg qtipgiiedl apqflkkpqe
      301 elkfkkasvw vlsfnngelt gadylpsplp vr
//
LOCUS       WP_284639107             441 aa            linear   BCT 25-DEC-2024
DEFINITION  nitrate/nitrite transporter [Corynebacterium accolens].
ACCESSION   WP_284639107
VERSION     WP_284639107.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Yan,H., Huang,W., Yan,C., Gong,X., Jiang,S., Zhao,Y., Wang,J. and
            Shi,Y.
  TITLE     Structure and mechanism of a nitrate transporter
  JOURNAL   Cell Rep 3 (3), 716-723 (2013)
   PUBMED   23523348
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   7  (residues 1 to 441)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..441
                     /product="nitrate/nitrite transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48281
     Region          31..429
                     /region_name="MFS_NRT2_like"
                     /note="Plant Nitrate transporter NRT2 family and Bacterial
                     Nitrate/Nitrite transporters of the Major Facilitator
                     Superfamily; cd17341"
                     /db_xref="CDD:340899"
     Site            order(41..42,45..46,49,82,137..138,140..142,145,164,
                     167..168,171,254,257..258,261..263,266,303,307,362..363,
                     367,371,387,390..391,394..395,398)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340899"
ORIGIN      
        1 mtaldtsgkv iqgwdpedsd hwdskiawrt lwistfvlii gfatwylvsa iapqlnqigf
       61 dlsrsqlywl taipglacgi frlifmflpp ilgtrklvfs ssllfvipml gwffavqdss
      121 tpywwlmtla flsgigggvf sgfmpstgyf fpkrlsgtal giqagignfg isfiqlvapw
      181 lmgftllgvg fvapqrtddg eifvhnpaif lvpwaivgaf lawtllkdvp vkanfrqqmd
      241 ifgnkntwil tvvyfmtfga fsgfaaqtal linqifgegs efagtydnlp agasyaflgp
      301 ligalvralw gplcdkfgga iwtfigclgm tiftvvatff ltpdepdevw wflgtmliff
      361 fftglgnagt fkqmpmilpk rqaggvigwt gaigafgpfv agvllsmmsa ptffwgcavy
      421 faittvlvwi yyarpnapfp g
//
LOCUS       WP_284639352             343 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Paenibacillus silviterrae].
ACCESSION   WP_284639352
VERSION     WP_284639352.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..343
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=37717
     Region          24..341
                     /region_name="Tdh"
                     /note="Threonine dehydrogenase or related Zn-dependent
                     dehydrogenase [Amino acid transport and metabolism,
                     General function prediction only]; COG1063"
                     /db_xref="CDD:440683"
ORIGIN      
        1 mvrkmsvppm elvdydgpgt qmcavmdaig eisvkralip epkegevrvk vkwvgicgsd
       61 vevfrgarep efityptrlg hevagiidkv gpnvigvkeg dhvalryvwg afaeyvccsp
      121 fsvkvlpkdl pliegsliev lpgilhaael gdispnknvl itgqgvsglv mtqvislfsp
      181 rnlvvtdlfd eklalarkyg athtykiphe hantmdivgk dfpdgfdvvi pcllegagmv
      241 daihaaaqng rivmygcigt chkpvdffkv hkkrldilst epkrdidnrr yfeeglrlvl
      301 dglvnteemi thivplaevn rafqlrnehk gdtihvmidc esk
//
LOCUS       WP_284639385             264 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium
            accolens].
ACCESSION   WP_284639385
VERSION     WP_284639385.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..264
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28727
     Region          5..264
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mselellrqw pvdnvaaall krgdvldeig dvsrefpvas vtkpvsayai mlaveegave
       61 leqtagpega tlehllahas gvkfdsreqq kpvgerrfys sagyewaaei veeatgiefa
      121 eylregvcep lgmsstrleg sagyglvstv qdlvafaaev qdpqllhpst vadmrrvhfg
      181 glrgivpgyg sfkdctwglg feirgekdhw mgalpadatg hfgmsgtylw lagdyamval
      241 tdrefgdwak plwnetntki wqal
//
LOCUS       WP_284639412             357 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Corynebacterium accolens].
ACCESSION   WP_284639412
VERSION     WP_284639412.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..357
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=37221
     Region          15..356
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mpesslrtaa gktvqdavlf sssnylglae hpeiksavke svdnygagsg gsrlttgtse
       61 lhvaveaaaa qltgypdsvf fatgyqanls tlqalaspel tiisdarnha siidgcrlak
      121 asgatlvvta hrdtraveda latrttkyal vvtdglfsmd gvlaplpels rvareygawl
      181 mvddahsfgt vgdrglglpe ffgiqpdiqi itaskalgae gglvatskpv aqllrqqars
      241 fvfstsptpa tsaavlaafk liesdpglvs qlqdniaywh ntrgttpqqg piipvhvgde
      301 aaamdasaal lnqgfvvpai rwptvargaa ilrvtlmath traqidalct eldqlgl
//
LOCUS       WP_284639413             293 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284639413
VERSION     WP_284639413.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..293
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33359
     Region          6..285
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mkrqnirigh taitwdnkev eqaasaigsc gywgsetfgw vleewerssr sllevferad
       61 lqltslychl divdaskree giqqvmdwvr lyqkfngpvi viggtmlqrs gftisehlln
      121 mkttinelak riadegllcc fhphtgtpve tedeihrvmn avdsrvvhfa pdlgqiskgg
      181 sdpfefikey yelirmvhik dyiggpverd aegreidktg flgytplgmg vvdikgiley
      241 leerkyshya mveldgnqws atrkgnpmmp qleaiqtskr yleqlgydnf rtv
//
LOCUS       WP_284639416             322 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284639416
VERSION     WP_284639416.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..322
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35586
     Region          24..311
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mldtketadq lqmernvsak irsmkigvqg sfypapeemp keditewqmr rlaamgctvh
       61 qigfghlpdd rgklleikal adslgmelel ttagafgvsg syadaeeksr flnaidaaal
      121 lqvpvvrtgy grlnvktsrf nksmsvhehl dslvpslrea griaadagia lavenhcdft
      181 gremvylfdk anmpnvgaal dtangftvfc dpqedmeala pyaftthmkd mvvvdmpvrg
      241 yipmiaqgcr lgeghvdiss aidllarhsp raeglhllie pgwmvwdpnr drldqeyeyf
      301 ehgiryiqgl ieekiqdaeg il
//
LOCUS       WP_284639547             563 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Paenibacillus silviterrae].
ACCESSION   WP_284639547
VERSION     WP_284639547.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 563)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..563
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=66304
     Region          7..474
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(21,23,25,29)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(60,63,100,103,144,163,167,199,255,416)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(199,255,331)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          484..559
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; pfam16657"
                     /db_xref="CDD:435493"
ORIGIN      
        1 mdpkwwhksv vyqiypksfy danndgtgdi qgitdkldyl qelgidiiwi cpvnrspmad
       61 ngydisdyye iapefgtneq feqlireadr rgikmmmdlv inhtsdehpw fmesrsskdn
      121 pkrdwyiwre pkqgrepnnw asyfsgsawe fdsltgeyyl hlyskqqpdl nwenqqmree
      181 iyqvirywae kgvkgfrfdv isklskhqdf pdvpdveegs yalgrryyld gprihefmke
      241 ihqvyepydi vtvgetsgvt ienarlytep srkeldmvfq fdhmavdagp ypagkwevsp
      301 frflefkeim srwqkglhgi gwnslywsnh dqpravsrfg nhekyrvksg kmlatclhlm
      361 qgtpyiyqge eigmtnvkfe sigdyndiel lnmykenlqk ghtheelmqk iwakgrdnar
      421 tpmqwddgeh agfsqsspwl kvnpnykhin vktaiadpds lfyyykrlie lrkdseysdv
      481 ivygsydllf ashprlyiyk rshmdktlvv icnffhetet idvkeelhyk eikyvigngd
      541 vtipgedgsl slspyecmvy eid
//
LOCUS       WP_284639563             272 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus
            silviterrae].
ACCESSION   WP_284639563
VERSION     WP_284639563.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..272
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31324
     Region          28..272
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          185..268
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mrqfivpvit nrsllpvyly svggmenqip ihrqhgytef iwlhtiqgkg rllldaaeyv
       61 lepnmgmliy pgvahkyhal eepwethwia fhgfgvrpll qkllmtkskv yrlqnaqlle
      121 rhihdiftaa cskhhdigln ttgklynfll dlpscivder tpantaaysl lnqvqeymeq
      181 hydsnislse magaagishq ylcrifkqtm qmtpiayltk lrlqkakell hekdvtitqa
      241 grsvgfwdts yfcavfkqhe gitpldykrn yr
//
LOCUS       WP_284639586             322 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Corynebacterium accolens].
ACCESSION   WP_284639586
VERSION     WP_284639586.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..322
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34443
     Region          2..319
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(40..41,45,118,122,125,143,146..148,167..168,172,187,
                     210..211,232..236,257..260,307,309)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(130,225..226,239..244,252..259,262..263)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mhaiqitetg gpevlryaev paptpsedev lvdvtvagvn yidtyyregi ynaqtpfilg
       61 fegtgrvvhd pkgeiaegsl vawhhafgsy aeqvcvprng lvavpddfpt eiaasmllqg
      121 mtahflshgv yelgegatcl itagaggvgq lltqmasslg atvytvvstd ekeeisykcg
      181 adhvfrysdg lgeqvrrfng grgvdvvydg vgqatffesl eavrprgtva lfgaasgpve
      241 pidpqllnkh gsifltrpsl gawtaqegef qmraqavvqt vmdgdlkfnv sasypleeae
      301 qahrdlqsrs ttgsivlrvr qd
//
LOCUS       WP_284639633             328 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            accolens].
ACCESSION   WP_284639633
VERSION     WP_284639633.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..328
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35148
     Region          13..324
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mvasrstpsr qdaaverltn lsfalqgaan sggspdrsaa wirshvagys dksdeaftka
       61 lardiatlqr agvpivhtgg edgasyrldq snyqlppvef speeamvlgi aggvgtsggl
      121 sdfslsgwtk iaasgasrnl egapvytavn ditrlapevi tfvlaavrnk vritfayrph
      181 paaetvrrtm dpwgvvnhqs riyivgfdvd raaprvfral rlsdikrshq paehieptvd
      241 idklvkealq rgekvdatlh ipegqaqele sagertaegt vvltgvqkdw lvrtaagyap
      301 evkvldppev rtdiinllrt aanhngae
//
LOCUS       WP_284639635             938 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium accolens].
ACCESSION   WP_284639635
VERSION     WP_284639635.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..938
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103635
     Region          4..936
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtethldtfa aglpypldef qvqgceaven gqgvlvcapt gagktvvgef avslalsrgt
       61 kcfyttpika lsnqkyhdlv aehgddavgl ltgdvsinad aeivvmttev lrnmiyadsp
      121 aldrlthvvm deihfladas rgavweevil nladhvsiig lsatvsnsee fgewlatvrg
      181 dtsvivtehr pvpldqwmml grkiyplfep esggqvnsel erriqrleag dsddgradyk
      241 sgkgfrarar hkgggrsefh gkaggrsgss rpqdryrplg rpevlkvlqs qdmlpaitfi
      301 fsragcdgal yqclrsrmvl ttqeeaeeik aivdagvegi peedlqvldf rrwrealsrg
      361 faahhagmlp afrhivedlf vrglvravfa tetlalginm partvvlekl ikfngeahvd
      421 ltpgqytqlt gragrrgidt lgnavvqwap amdprfvagl astrtyplis tfapgynmai
      481 nllgmlgfed slrlleksfa qfqadgsvve etreleraeh rvrelreqld davdalappa
      541 kdgedpaevl mdyirlrrel taeekqskvd kehqrtqevi avlarlqlgd viaiagkkrp
      601 tlaavvtpan qtedprpwvt tesgwsgrid atgisnppiq lgrikipkpv rknprrntky
      661 iqdvfrrekf drpkrmkskp rlrpnkrvge lrdairehpa hkwpatdreq lagvaqklar
      721 rerdleklqa kvdkatdtlg rtferivdll aemdyvefsg agsdrtpvit eegerlakih
      781 sesdllvaqc lkrgiwdeld paelagvasl ccfenrkatg gqpeaatdrm adamnatwri
      841 ytelgaderr hrlpptrepe agfalaihqw aagaplgycm aaaneagael tpgdfvrwcr
      901 qvvdllqqia ktgydgqiqr narramdaiq rgvvaiga
//
LOCUS       WP_284639674             377 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium accolens].
ACCESSION   WP_284639674
VERSION     WP_284639674.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..377
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41250
     Region          11..356
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mrtqasvkrl pqhlpeldgl ravaalgiiv thvsfqtgtg wgfagrfdff vavffalsaf
       61 llwrrrglht vrgyahsria rlapayyacv vsvvlllpda hsitptqila nltstqiyva
      121 dglapglthl wslcvefffy lvlpllvwai gglpqrwrmg viagaavvsw gwgfipfvad
      181 ygedqvnsqi wppayaswfa vgmlaaevee rgigkrtarl lqvrwawvvl aavvlwvasr
      241 dwfgpaglvh pepaefarri iagaifaacv vvpvalvprg tswltsplmq algawsysif
      301 lwhvavlava fpltgvalfs gksldfwvil avtvigtvvv saasytlier pgrdllmgrg
      361 rsrrrrkgrp aprhist
//
LOCUS       WP_284639741             716 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Paenibacillus silviterrae].
ACCESSION   WP_284639741
VERSION     WP_284639741.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 716)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..716
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=81442
     Region          3..708
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 meadtrttfd qeyerltqti qemeqqlayl enipvytghd ateqvlesir enkrynlkha
       61 kpepyfgrld fqeegkpept plyigkfgve kadspelmvv dwrapvaslf ysftggleka
      121 gyespegvie glvylkrnlv irkqllqrvv dtfdragdam avtdefllyr lgenkdnrlr
      181 divstiqaeq dqiiragknh slviqgvags gkttvalhrl afllyqyrdq vkaenmiifa
      241 pnrmfldyis gvlpelgvgh irqttftdwa lellehevkl adpgqrlrhw ldsgtnrppm
      301 ddtapgrfkg svhfmawlde vlaayelrav ptadfepweg vrltaatire wyyteykhep
      361 lmkrrdrvla rvkrwlemgl dklrgshlak eykkkssakl reygkswtdy tpvtfykelf
      421 ngkvgfltse ltaripeair eetaanlkkk qvqpedlapl myirqrfhgi gsdqrfdhtv
      481 ideaqdfspf qisllsrhtk ngsfsilgdl sqgihayqgi hdwqeflslf paeqaayftl
      541 nrsyrstmei iyfanevlrn gmaeppalav pvfrsgepva mvqadgkgll lqlkskveah
      601 rrasetgtla vlarsearcr elhkqleklg iatnlilpgq qqyeggvsvl pvymskglef
      661 dsvllvdvdt enypaepvda kllyvgctra lheltlyyag epspliaaie gdfvrr
//
LOCUS       WP_284639782             329 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus
            silviterrae].
ACCESSION   WP_284639782
VERSION     WP_284639782.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..329
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38062
     Region          1..322
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mskskrliel miavnkrrkf tvrelaeefa vssrtimrdl qaleelglpl yaeygpnggy
       61 rllnehllpp ivfseqeava iffayqslqh ygslpfdeea vtalnkfyyy lpddtkrtid
      121 kmkqrvifws pkrkapsphl rllldaslqm rpvrvlydsr egaksrtiqp igvysqngyw
      181 ycpaycfhre kyllfrvdrv lqaeqmeega etvdvsgypl qmwflpqgqp vsavyasdpe
      241 rmpliaeltt egvsrfqweg ifhdelqvnd dgtgilrlhi reddfgyytq yflsmgadav
      301 irepqelreq lrqaavklfe ayhaskpsc
//
LOCUS       WP_284639851             108 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Paenibacillus
            silviterrae].
ACCESSION   WP_284639851
VERSION     WP_284639851.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..108
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12490
     Region          6..108
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 maeqphhhqm cpkfeaafei lgkrwtglii rallegprrf kdisemipgm sdrmlaerfk
       61 eleacglisr hvypetpvri eyeltekgka lqpvmeavqq wgeswvqr
//
LOCUS       WP_284639920             495 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Paenibacillus silviterrae].
ACCESSION   WP_284639920
VERSION     WP_284639920.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..495
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55360
     Region          20..491
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mmvkresrki aivgggiggl taalllsyrg hkvtvlekgs rlggrmayes vkgfridqgp
       61 tivllpgmir galqaagvdp nlfefqqvdp lyrihfedgr tltkwtdkrr maleiermfp
      121 geggsflnym evmqerfnlg ykqflskdfv rkrdfwtpgn vrslvklkay ssvrqdvarf
      181 fhasrlreay sfqtlyiggn peatpalysl ipfsehahgi wyvkggyagm igklaqllee
      241 rgvevrlnta veqvlvrdge cygirakgvs wafdqvvlng dfpmtrallg gqrgkgwgma
      301 kayepssgcf lmylglnrvy esasvhqfff tdrfaemlkd vfvskivpeh pclytfhpsl
      361 idsslappgk gvlyvlvpvp sgdggawetm reafadrile elerrgfpgl rqavewrkvr
      421 tpheakqegl yqggsfglap tlrqsgvfrp qvqpygikrl favgasihpg ggvpiimqga
      481 rllaefmerq reimh
//
LOCUS       WP_284639932             503 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Paenibacillus silviterrae].
ACCESSION   WP_284639932
VERSION     WP_284639932.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..503
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55206
     Region          14..498
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 msatgkgvii gggigglvts illasrgfni tlleknetlg gklqqvklga yafdfgpstl
       61 tmpwifekvf eaagepldpe lhflkldvns rnhfedgsvi dlstdpdrmq eqlstfsadd
      121 rkgfqrylqe vkriytiaee qffsrsfagw qdyvspklgv allsvhpfta mdafhrrffr
      181 dprllammnr yatyvgsspg qtpatlsmia ylelirgvyy lkggnyklie vlerlarkag
      241 vtirkgavte riehkrgtvl gvqaagmrfe adfvvsnvdv httqkllydq pqqsraslss
      301 sgflcllglk kpmtglhhhn lffpkdygse fadmfdagcw psspalyvcn ssysepergg
      361 lngagsnlyv ltnvpalakt pssplkqlsv qeirayrafi lnrladclkl dtieplieee
      421 aiytpqsiad qtgafagaly gnashgwgpt ffrpsladrk vqglyyvggt thpgggtpmv
      481 tlsgiqaael isarhrkktr tal
//
LOCUS       WP_284639995             226 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Paenibacillus silviterrae].
ACCESSION   WP_284639995
VERSION     WP_284639995.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..226
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26010
     Region          6..218
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 maerhclllh gftggpyevl plaehleglg yvchvptlpg hgeefsvigk ipfhhwldsa
       61 aelterltre ygeidlvgfs mggllsmyla nrypvrrlvl lsaaaiyvsp vrlardmayr
      121 irikdweqlg rvkrtpfkaa vqfmklvrlv kqqelrrvtv ptlivqgkqd hivhprsahy
      181 iyrrirgere lylleqskhm ictdpeaqql fhkveqflvh aqqegr
//
LOCUS       WP_284640022             557 aa            linear   BCT 25-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Paenibacillus silviterrae].
ACCESSION   WP_284640022
VERSION     WP_284640022.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..557
                     /product="long-chain-fatty-acid--CoA ligase"
                     /EC_number="6.2.1.3"
                     /GO_function="GO:0004467 - long-chain fatty acid-CoA
                     ligase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=62508
     Region          25..546
                     /region_name="FC-FACS_FadD_like"
                     /note="Prokaryotic long-chain fatty acid CoA synthetases
                     similar to Escherichia coli FadD; cd05936"
                     /db_xref="CDD:341259"
     Site            order(210,213..218,220..221)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(213,330..331,352..357,436,448,451,462,542)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(213,255..256,303,305..306,309,330..331,352..357,436,
                     448,451,459..462,523)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(255,305..306,309,330,459..461,517,523)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mstkpwlrhy pvevpatypy pkhnlasfli qtsslypght alhflgknit yrqllnaayr
       61 fanaltrlgl rqgdrvaiml pncpqaviay fgtllmggiv vmtnplympr eleyqlndsg
      121 akllvtldil fsrvmkavpa tgvqytvvts ikdylpfpkn ilypikakkd glkrkvlyse
      181 qvlsfmkllh qadttptlav vnaeqdlali qytggttgva kgvmlthynl iantiqsrlw
      241 ayrsqvayer ylaalpffhv fgltvllnqs vylagtllli prfeptqvle aihqeqptif
      301 pgaptmyisl lqhpkikqfd lssidfcisg aaslpyevqe sfekatggkl iegyglteas
      361 pvthanniwe krkvgsigip fpdtecrvvd ietgkelpvg eigeltvrgp qimkgywkrp
      421 eetakvlkdg wlytgdmarm deegffyild rrkdliiagg yniyprevee vlyehpdvve
      481 avvagvadpy rgetvkayiv lkkgseadga elqawckdrl aaykvpklfe freslpktiv
      541 gkilrrklle eeteqqe
//
LOCUS       WP_284640169             514 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Corynebacterium
            accolens].
ACCESSION   WP_284640169
VERSION     WP_284640169.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..514
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=54793
     Region          1..472
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 manfldalns iiwspalvfl clgagvyftv vtrglqvrcl pdmlrqiskg eksddgvssf
       61 qslmvslsgr vgvgniagvs taiafggpga vfwmwavall gsstsfiect laqiykekdq
      121 dtgeyrggpa yyiekaykht kaapfmmvyg ilfaiamila tsyflpgiqa navaaaadta
      181 wgvnstwaav vlagilaiii iggvkrianf atlvvpfmav iyigisivvm linysqipev
      241 fglifksafn leagfsgmlg vaimwgvkrg iysneagqgt gpqsaaaaev shpakqgfvq
      301 sfavyidtlf vcsatafmii stdmytvfrg esedgevvyq gslpddvavg pgfvqsglds
      361 vfagwgptfi avsiaffaft tvlayyymse vnltyfnrwv ksrpirrglv walriliivs
      421 vivgatttpg sawalgdigv gttawlniia ilflqvpalk vlkdyekqkk agkdpefdpe
      481 avgvknadfw vdrknaraaa qaaskqaage naes
//
LOCUS       WP_284640201             208 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Paenibacillus silviterrae].
ACCESSION   WP_284640201
VERSION     WP_284640201.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..208
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23588
     Region          1..>81
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mkcediqelf aeywdlnerd lkrqavdehi khcvqcaeef emwresedli ksvtetmgte
       61 rqapiisesv mkriyqdesw rvpvgdklyh fsykmrrnvt avvafcltlf iftfvfsaag
      121 gfssdtvasq qssvfgrlge pvviagssgd smnvhsmpta vaslkgfnep fmykvgpiqt
      181 vkdymmflsl lgltctllim nwlsrtrs
//
LOCUS       WP_284640225             473 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium accolens].
ACCESSION   WP_284640225
VERSION     WP_284640225.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..473
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51699
     Region          5..404
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msrttlrsfi qrihfyggmf vgpfiliaal tgclyalapt lekfayrdvm tveevnnpvs
       61 ledqisaaqk ehpdmpvsqv wpaesatdst rvlvadpgid eslqrtvfin padgevigdy
      121 ptysglgemp lrrwisslhe sfhlgqpgel yselaaswlw vlacgglymw wirrrpkkaa
      181 aplkkqpqrs krwkatrlhs tmgawifigl iglsatgitw sqlagenvns vvekmnwkat
      241 pvetalttds sadaahdaha gheghgahga hggdaeaage apepeviaeq aervyatgra
      301 egltgplrly apedtdsgwk vserwgewry tsdevsvngs tgevidrlpf selplfskls
      361 swgiylhmgi mfglplqial falglaiaam vvlgyymwwk rrpqfapgsk rhfswattgl
      421 galfaatvgv fmpllgitla aflvldiilm ntgkrkgtat kkkdedaelv pvg
//
LOCUS       WP_284640226             260 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: CheR family methyltransferase [Paenibacillus].
ACCESSION   WP_284640226
VERSION     WP_284640226.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..260
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30404
     Region          1..259
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 medqdfllfi kkvkdytsid laqykeaqmk rrlttlrmkk gynsfaaffd amtkdkelfy
       61 efldrmtinv sefwrnpnrw evleqrflpe mlrksrklkc wsaacstgee pytlamilse
      121 lnalqdslvl atdidegale kakkavyadr svrdvpagyl kkyyrqenlt yhiadslkks
      181 irfqkqnllt dtfdtqfdli vcrnvmiyft eeakhllyqk fanalkpggl lfvgsteqif
      241 spgqygmepa dtffyrkisq
//
LOCUS       WP_284640287             414 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: Glu/Leu/Phe/Val family dehydrogenase [Paenibacillus].
ACCESSION   WP_284640287
VERSION     WP_284640287.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..414
                     /product="Glu/Leu/Phe/Val family dehydrogenase"
                     /EC_number="1.4.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016639 - oxidoreductase activity, acting
                     on the CH-NH2 group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45902
     Region          5..413
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mtenlnvlhs tqliieqalt klgytqamid llkepmrvlt vripirmddd tvrvftgyra
       61 qhndavgptk ggvrfhpdvn edevkalsiw mslkcgivdl pygggkggii cdprqmsfre
      121 lerlsrgyvr aisqivgpsk dipapdvmtn sqimawmmde ysrirefdap gfitgkpivl
      181 ggshgretat akgvtimidq alkkkgiplk darvviqgfg nagsylakfm qdagakvcgi
      241 sdvygalydp ngldieylld rrdsfgtvtk lfkntitnqe lleqecdilv paaienqits
      301 enadrikapi iveaangptt leatrmlter gillvpdvla saggvvvsyf ewvqnnqgyy
      361 wteaevhtrl qemmekgfen vynvhmtrnv dmrlaaymvg vrkmaeaarf rgwv
//
LOCUS       WP_284640333             261 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Paenibacillus silviterrae].
ACCESSION   WP_284640333
VERSION     WP_284640333.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..261
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=30061
     Region          1..249
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 mkvtvkletf egpldlllhl idkaevdiyd ipikditdqy msyldamqel elevtseflv
       61 maatllsiks kmllpkppvi eleyddymmd ddydpraelv aklieyrkyk aiadhlrdke
      121 tersliytre pedltpfvpa tienpvkglh vgdlvrafhk amrrmqsrnt iakirkdeis
      181 vkdrmvevld vltrtggkvv fsklidekat kdtivvtfla llelmkvkki vcyqhrlfdd
      241 iviqaredga tdgfwtaein y
//
LOCUS       WP_284640417             179 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium accolens].
ACCESSION   WP_284640417
VERSION     WP_284640417.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..179
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=19030
     Region          <57..173
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(69,73,76..77,79..80,126,129..130,132..137,140..142,
                     146,148)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(90..97,114,117..118,121)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mrfciilsrv lgpitaswly ifrffggnfs wlsrfvisis igafglltlt pstltsalrd
       61 lrlpgwatip pavflrvlpi ivaeakaird amvlrglqpg vkswftqptq ssamliipll
      121 gavvragdel aasalvrglg gptrptttad lsfklvdata iaglglvvas vwlptevrl
//
LOCUS       WP_284640513             357 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Paenibacillus silviterrae].
ACCESSION   WP_284640513
VERSION     WP_284640513.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..357
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39445
     Region          8..357
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mqqqerirrl revmqqqglq allvtgdinr ryisgftgsa gyvlitdrra illtdfrymt
       61 qapqqaigle viehapkame tvrelltqek vtalgfeqnd lsygafrsis evlsgielip
      121 tdnlveklrm vkdageieim qeaadladrt fshilgflkp gavekdiale iemfvrrhga
      181 astsfetiva sgersalphg kasdrvlgnn efvkldygay ykgycsditr tvvvgkasdq
      241 hreiyrivle aqlealdkir pgmtgreada iardvikrhg ygdkfghgtg hglgmevhea
      301 prlsmmgdiv lepgmavtve pgiyipgfgg vrieddiiit etgiriltks tkellei
//
LOCUS       WP_284640462             107 aa            linear   BCT 25-DEC-2024
DEFINITION  thioredoxin family protein [Paenibacillus silviterrae].
ACCESSION   WP_284640462
VERSION     WP_284640462.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 107)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..107
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11409
     Region          2..106
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 mslkqandsn fteltgsgit lvdfgaawcp pckvllpile elehelseas glsvlsldve
       61 espvtssafg vmsmptvilf kdgqpmdklv glrskeayvn mvqkhla
//
LOCUS       WP_284640634             315 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284640634
VERSION     WP_284640634.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..315
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36051
     Region          23..283
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mftdkgeysf stcwnikkht tgrgmieeik elgfrrveln ynvteellqt iepmiergei
       61 gisgvhntfp hdpdpdygtd svllgfedet kreraiellc rsidyaaryg aeavvvhpge
      121 vpfegnidsr lkklyhdagk eseayrslwt emlqrreals pkyartiges lervsdyiak
      181 kgykvavgie trsrcyqmpt pqeakaiidk lkgapvylwy dfghammmdr mglydsvkda
      241 relkpyiygi hihetvglsd hycpyvhsgt evfddfldiv rdaplkvyel kaickpieie
      301 qshtllqrki aalpr
//
LOCUS       WP_284640650             630 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium accolens].
ACCESSION   WP_284640650
VERSION     WP_284640650.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 630)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..630
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64869
     Region          32..624
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mssacgcehe pateideldr pwwkdpelll pifsgvalit glaldwsdle tpatvlywvg
       61 lllgaytfap gairnlvmkr klgigllmti savgavilgf vgeaaalafl ysiaealedk
      121 amdraqgglr allklvpqta tvlrdgtaae vvakdlevge lmlvrpgeri atdgiirsgr
      181 ssldtsaitg esipeevapg devpagains agvlevetta agtdnslttl vdlveqaqae
      241 kgdrariadr iaqplvpgvm ilavlvgvig sllgdpetwi tralvvlvaa spcalaisvp
      301 ltvvaaigaa sqfgviiksg aaferlggir hlavdktgtl trnqpevtgv vpadgfdrpq
      361 vlsfaaaveq qsthplaaai aaagpeapta sdiseeaghg iggtvegrrv lvgsprwida
      421 gplkadverm esegqtcvlv tvddalagai gvrdelrpev peavqalhan dvevsmltgd
      481 nsrtaralag iagiddvrae lrpedkasiv aefssktpta migdgindap alagatvgia
      541 mgatgsdaai esadvaftgh dlrlipkalq harrgsriin qnivlslaii ivlmplaisg
      601 vlglaavvlv hevaevivil nglraaqakr
//
LOCUS       WP_284640715             392 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Corynebacterium accolens].
ACCESSION   WP_284640715
VERSION     WP_284640715.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..392
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42416
     Region          125..387
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mkiiarllsv plalvaflal wlavapftph ipywgagali gpqyigpvii fslillvlaa
       61 lgrlgsrsfy vpgafaaval iagialfgtq ihaakeqgtd vdiraalswa gvestdegpd
      121 htvaydsfhg edldmdiytp ndggthpvmm yvhgggwdqm nkhsqafnmr qmaqrgylvl
      181 sidytlsswd qptwkvaagh vgcamnwvna haadydgdpg rfftygesag gqlvlnatad
      241 aaahpnhlps adcpgtpavp ravyadspal dvrhiydsdd pyaaqgsrdt vqkylggtpe
      301 eypdradfvt sathlttdmp pikivrsdnd rlvppesydd frriaqekni dlseyvrpha
      361 dhasalsahg vwnqhllqam pqffaehdpq gs
//
LOCUS       WP_284640835             189 aa            linear   BCT 25-DEC-2024
DEFINITION  HIT family protein [Corynebacterium accolens].
ACCESSION   WP_284640835
VERSION     WP_284640835.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..189
                     /product="HIT family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21059
     Region          45..170
                     /region_name="FHIT"
                     /note="FHIT (fragile histidine family): FHIT proteins,
                     related to the HIT family carry a motif HxHxH/Qxx (x, is a
                     hydrophobic amino acid), On the basis of sequence,
                     substrate specificity, structure, evolution and mechanism,
                     HIT proteins are classified into...; cd01275"
                     /db_xref="CDD:238606"
     Site            order(69,71..72,79,81,127,134,136,141,143)
                     /site_type="active"
                     /note="nucleotide binding site/active site [active]"
                     /db_xref="CDD:238606"
     Site            order(139,141,143..145)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238606"
     Site            141
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238606"
ORIGIN      
        1 mpganpqkgq seetfvdtga gepdrlerlw apyrmayiaq rsedpfveap kssdedglii
       61 argetvyall nlfpynaghl mvvpyrkese lenlteeesh elmafaqkav rvlkrvsrpe
      121 ainvgfnlgr asggsvgdhl hlhvvprwpg dsnfmtvldg tkvlpqllqd trrvlaegwr
      181 dmeeedsra
//
LOCUS       WP_284640960             250 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Paenibacillus silviterrae].
ACCESSION   WP_284640960
VERSION     WP_284640960.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..250
                     /product="metallophosphoesterase family protein"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27575
     Region          3..227
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mvkiaiiadi hgnlpaleav aadirrhrik rviclgdlvg kgpqpaeavd rirelceltv
       61 qgnwdlgine pqdkeaglwq qdrlgkerle ylrtlpfcad lwlsgkrvrl fhasaksvyh
      121 rvlkkadkte rlalfnntea tgsfagedgv tpdvvgyadi hvsfhrtfks kdkqglmlfn
      181 tgsvgapydg iaqasyvild glsdcrepgp favsmvrvpy dvskaiaiae qvglpnlerf
      241 ryeqqtameg
//
LOCUS       WP_284641027             260 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284641027
VERSION     WP_284641027.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..260
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28888
     Region          1..252
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mklgwcsgst nahkirqagy dfielplaal qledpdayha qvqeilslsl ptaafniffp
       61 rtikivgpea epnrikdyva raaqavnlak arivvlgsga srhipegwek ehaeaqflet
      121 lsvidaefkg cgatlviepl nrkesnlins iseavrmaql inspviqala dvyhmmeene
      181 pleeirrhae wiahihvadt grkppgegsf dftslshmlq qmnyqgmvsv ectasaehfd
      241 silqdchsfl rkemqlketk
//
LOCUS       WP_284641081             321 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus
            silviterrae].
ACCESSION   WP_284641081
VERSION     WP_284641081.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..321
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36044
     Region          1..320
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 makadhmlai lmllrtrrkm taqqlaeele ihirtvyryi dalcmsgvpi vsetgrdggy
       61 fipdhvkldp lyfdaaeqka llhaakfire sgypqeeale raigkikryt syaqaerlgq
      121 leaglevihs pangkisgel rlleqaieaq csldieydag yentstsrtl dpygivhwkd
      181 kwyavgycrl rgavrcfrvd rirsmtlagn tfdkpstfsa rnalleslqg htgdseeglv
      241 tvrvqggpqa lndlcghwmf ghsliereke lavfkvdeay lythapyyll sfggsirvle
      301 peplraclad iatklveyyk s
//
LOCUS       WP_284641093             219 aa            linear   BCT 25-DEC-2024
DEFINITION  formylglycine-generating enzyme family protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284641093
VERSION     WP_284641093.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..219
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=24998
     Region          6..218
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 mleipmvpip agevelrddr ikrnwttrvd sfllgqvpvt rglydaiipr aveahyepqs
       61 pvvdvswhda vafcnllsrq aglqecysvs edgervdwnr eacgyrlpte aewqyackag
      121 tggyrygele tiawylenae grvhhvgqkq pnawglydml gnvwewcwdv ydpkvygsyr
      181 ifrggswaee argcgatcrr rshptfridd lgfrlarsc
//
LOCUS       WP_284641299             259 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Paenibacillus
            silviterrae].
ACCESSION   WP_284641299
VERSION     WP_284641299.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..259
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28799
     Region          37..136
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mnrmessnew naghydehig yvsrlgrgvv ellkpapger ildlgcgtgd lahlirqsga
       61 yvlgmdqsea mivearakfp eqdwiqgdge tfrlpgvpaf davfsnaalh wmkrpelvaa
      121 svhkalrteg rfvaefggkg nveqlvkail qstapfgvdg aarhpwyfps vgeytgllee
      181 hgfevgyael fdrptplsgg eqglwhwlka fagmffeglt eeqqeeayqs cermlkpvlw
      241 ngdtwvadyr rirvvavkk
//
LOCUS       WP_284641408             389 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Corynebacterium accolens].
ACCESSION   WP_284641408
VERSION     WP_284641408.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..389
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40924
     Region          11..388
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mnesleqvas arrekwredg lwrspsvfvs gqvpesslrt aagktvqdav lfsssnylgl
       61 aehpeiksav kesvdnygag sggsrlttgt selhvaveaa aarptgypds vffatgyqan
      121 lstlqalasp eltiisdarn hasiidgcrl akasgaclvv tahrdtrave dalatrttky
      181 alvvtdglfs mdgvlaplpe lsrvareyga wlmvddahsf gtvgdrglgl peyfgvqpdi
      241 qiitaskalg aegglvatsk pvaqllrqqa rsfvfstspt patsaavlaa fkliesdpsl
      301 vsqlqdniay whntrgttpq qgpiipvhvg deaaamdasa alldqgfvvp airwptvarg
      361 aailrvtlma thtraqidal caeldqlgl
//
LOCUS       WP_284641388             344 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Paenibacillus silviterrae].
ACCESSION   WP_284641388
VERSION     WP_284641388.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..344
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36665
     Region          23..340
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mkrrlllwgg cglalllism taalalgsvk vpfvqvwkim lyhmpwvggs ivpdwtvase
       61 qiiwkvrlpr vvlgslvgaa lalagasfqg vlrnpladpy tlgvstgasv gasflilfgl
      121 hyalfgqwtv pvvafvtgsl sllavlslak tngkmqietv vlagvvmhaf lgafvslmvs
      181 msktvineiv fwlmgslalr gwayslvllp ylavgavlll sfgramnlfs lgerqaahlg
      241 vnvertktmv liaatlitaa avsvsgvvaf vglivphllr mligpdyrll lplsmlggav
      301 yvlwadllar tllspteipl gvvtaflgap ffayllkrrk kklq
//
LOCUS       WP_284641738             373 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium accolens].
ACCESSION   WP_284641738
VERSION     WP_284641738.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..373
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=40012
     Region          27..372
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mttqafspev ysrrlsaaqe aaaqqsidll ligtgpdfay ltgswvsshe rltvlavpqs
       61 gtpwivspnt ditdiksapv gkldvelrgw ndgdnpyela lkgaasikkv algqsltadh
      121 ilqfqalvpd adyvlatyal aelftrkdea eiaelrkagq aidavhaqvp ellqpgrtea
      181 evahelekli lqehsiidfv ivgsgpngan phhsfsdrkl aagepvvvdl ggtlpsgyhs
      241 dctrtyvvgs dlsqapqdfq dayavlydaq aaaraaakpg staeeidgva rktiadagwg
      301 dkfvhrtghg iglstheepf imegndlale egmafsiepg iylegqwgmr ledivvltkd
      361 gyeslnvver evr
//
LOCUS       WP_284641750             458 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284641750
VERSION     WP_284641750.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..458
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=49390
     Region          1..444
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mniavvgtgy vglttavtla ylghrvtavd vnaekidrlr agqlpiyepg lkelldasge
       61 rltfttsyae alleadvvfv avgtpsqedg spdltylnas leemlvylrh ketttllvtk
      121 stvpvgtgdr meerirregl dgkvtvasnp eflrqgqava dtlyperivv ggnetawqim
      181 revysaivaq sfsmpalvqk parravisyi evgrrsaels kyaanaflam kisfineian
      241 vcervgadve qvadiigkdt rigssflrag igyggscfpk dtnalhymag tngydfklls
      301 avievnnaqk lhlvhkaker lgtlygkkla vlgltfkpgt ddlrespsla iiealagega
      361 rvfvhdpial ekaaglvpeg vqlaaqvgda lagaeaalli tewaeyvnld paylrsvmlr
      421 pllldgrnaw nvdkrtlley dgigtltasp arlqqpvr
//
LOCUS       WP_284641834             397 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Paenibacillus silviterrae].
ACCESSION   WP_284641834
VERSION     WP_284641834.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..397
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42279
     Region          5..391
                     /region_name="FucP"
                     /note="Fucose permease [Carbohydrate transport and
                     metabolism]; COG0738"
                     /db_xref="CDD:440501"
ORIGIN      
        1 mktflwcgyg sylliglahv ivgsllpeml syyavdyssg gqlialqfag flvgvlsgpw
       61 wsarlgkrga lllsltclta aelvfallpp wtivmtvapl agfgfgmvet vigalviqyl
      121 eeqrktkvmt rlevffgvga lvmplisslm ialgmwrgaf imlasssaal llmwlflplg
      181 smsslmsrte ggnggteavs pqpskgapal ylgvfllifl vyvgtemsia nflpsmfiet
      241 lhvkpeigal satcfwgama igrlfaanvv ervgtpryll wsiagatlll gafamntglw
      301 gsfalvllig lmlsgmfail liyangffpg reeritslli asggvggall plltgwsmdr
      361 ftveqtllvp vmfsalllll igwasrfpka savgknv
//
LOCUS       WP_284641997             329 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium
            accolens].
ACCESSION   WP_284641997
VERSION     WP_284641997.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..329
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34818
     Region          35..329
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrrlalsigt aisiasvlll agprhltlal tdtgdaalas tlrehaepgf hhltaftlrd
       61 gnatfagigs nehteveigs vtkmftgelt hqlveegtlr ldstvgefld vdnapiadvt
      121 ikelldhtsg lprsadgdff aslwsavagt npyegestqd ivdaaaaael snrgeesysn
      181 lgyallghvi etaadtpyeg llkqrifepa gltetylmtp gavpadaprg rtatgrqaqp
      241 wemdgsapag airstasdma kfaewfmahg dpaygwqknd dgtgfwhngg tygystmlii
      301 dpktkraafa nndslagtee lgqalfael
//
LOCUS       WP_284642020             324 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus silviterrae].
ACCESSION   WP_284642020
VERSION     WP_284642020.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 324)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..324
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36668
     Region          7..324
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mskvqpamkp qtraqqikag tpgwwkqfrk nrfllmltlp mvlfifvfky vpmfgaivaf
       61 krfqfnkgiw gsewigfsnf kflldspdlw rivrntlayn safitlnlag allialllye
      121 mssrkllkay qtvmffphfl swvvvaymay aflnprsgmm nqllewmgya pldyynlagp
      181 wvyilpiaql wkeigmgaii yyaalmgidp tyyeaakidg askfqmmfhv slpfvypiit
      241 iltilavgqi leadfglfyq lpmnsttvya ttdvidtyif raltvngdig msaatgliks
      301 cvgfvlvigt nalvrkinsd nalf
//
LOCUS       WP_284642106             500 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Corynebacterium
            accolens].
ACCESSION   WP_284642106
VERSION     WP_284642106.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..500
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=53066
     Region          1..455
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 meflenvvtt fndavwtwil pwlligagll fgartavvqi rkvpdmlrav verpqsdded
       61 egagsggisa fkaftisaas rvgtgnvagv avaisvggpg avfwmwiial lggatafves
      121 tlaqlwkvrn gdtyrggpay ymkrglgwgp lgvlfsiaiv ftfglvynsf qtnaiaeava
      181 fsfgreddat fgsiigiiia iaagliifgg vkrianitqv vvpfmalayl liggfvvitn
      241 fdkvpgmlgd iighalgfke iagagigaam mkgiqrglfs neagegsapn aaatatvshp
      301 vkqglvqtlg vyfdtivvct itaflillgp evaygeeaeg vsltqaalsa evghwgihfv
      361 sfilfflafs silgnyylae anleylttnk tvlntfrlvv lffvwfgavg slplvfalad
      421 tgaatmviln iiaivplsgv aiqllknfne qrskgvdpvf hrdmlpdvpg vecwdgsdpv
      481 trrsdadrki lrdrgeadry
//
LOCUS       WP_284642247             729 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium accolens].
ACCESSION   WP_284642247
VERSION     WP_284642247.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 729)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 729)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..729
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76340
     Region          2..723
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mshvdlgvsg mtctscssrv erklnkvdgv easvnfates asiefdpets tpadlikvve
       61 gagysafdms gsddgdqdgd aegtpvddar aaeqqsllrr tiisavlsap imvvsmvpal
      121 qfqnwqwaca mlatvvfifg gapfhsatwt nlkhgsftmd tlismgtsaa ylwslyalff
      181 gnagepgmtm smswssssae mdhiyfesvg mvitflllgr wfevkakgqs sealrtllsm
      241 gakeasvlrd geekripisq lqvgdvfvvr pgekiatdge vvsgnsavda smitgesvpe
      301 evgvgdtvtg atinasgkle vkatqvgedt vlsqmatlvt naqaskapvq rlvdriaqvf
      361 vpvvigisvl tllvhlifgg vapafiaavs vliiacpcal glatptailv gtgrgaqlgl
      421 likgpeiles tkqvdtivmd ktgtvtagem svtavhgdvl eyaaaverns ehpiaqaiar
      481 erdvepgadf ststagveat vdgvrvgvgk prgdlgqyae afreaeaaga tpvavyldde
      541 laglievrdt vkptsaeave qmkelgltph lltgdnegaa krvaeevgit evtagvipee
      601 kvdvikklqs eghnvamvgd gvndaaalaq adlglamgag tdvaieasdi tlmngdlrsa
      661 adairlsrrt lqiikgnlfw afayniilip vaafgllnpl fagiamalss vfvvsnslrl
      721 rkfstqryd
//
LOCUS       WP_284642290             409 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Paenibacillus
            silviterrae].
ACCESSION   WP_284642290
VERSION     WP_284642290.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..409
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45397
     Region          16..403
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 meqlaflggp kvkttpfgtg rrfgleeatq llealeqntl fyhfggkvkq flndfnvmyg
       61 vkysvatssg taalhvamga agvsvgdevi tspitdqgtl igilyqnaip vfadldphty
      121 nmtpasiear itprtkaivv vhlagnpcdm dpimdiarkh glkviedcaq ayltkykgrl
      181 vgtigdygcf stndfkhist gdggmvtvns adetdyqvth afadknyrrf gtglqrdthy
      241 vapnyrmtel qgavgiaqlk klewicsqrr rfgdritagl ekvnglaphy vaegnectyw
      301 fymfrlreee ltctreefcq altaegipnr agyipdvcym qplfqqrqay lgshfpfdqs
      361 dvsydrglcp eaerilqtav qiplsefyte qdveeiiaal rkvagsyar
//
LOCUS       WP_284642328             125 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium accolens].
ACCESSION   WP_284642328
VERSION     WP_284642328.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 125)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..125
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=13347
     Region          2..124
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 mievaaivfr nsfghmlgvr kasstkfqlp ggkleegesp vqaaareaee eigvrvrlpe
       61 ltelgtftap aanepgqtvr ghiftyprpv iahaaaeiae tawidpadpq celadllrse
      121 vfpal
//
LOCUS       WP_284642345             490 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Paenibacillus silviterrae].
ACCESSION   WP_284642345
VERSION     WP_284642345.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..490
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=54788
     Region          7..489
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 misisdydlv etiyegtrtl isrgrhqatg rhvivkrlrs dhplpeddar lrreydiars
       61 vnlagvvrpl amvpdgrsya lfledfgges lhhllarrrl elsealqlsv klaaileslh
      121 rsgvihkdvk psniivdssc etvkitdfgi aslldtetse plsprelegt lthmspeqtg
      181 rmnrvidrrt dfysfgvtmy elltgqlpft ttepmelihs hiakaplppa qmdssipqsv
      241 sdivmkclak naedryqsay gllcdlehcy egllssslsd efaigtndrk dsfyipqrly
      301 greqelerlh avyerlsfse sicvlvsgys gigkssfile mmkranedeg qfilgkfdsl
      361 rrhvpysafl qafrllirrl asesgeelet kanalrstlg ehapvlaevl pelewilgpq
      421 prveplpase akqrfhtair lfltcfsahg tppvprrsav grprlapada lsdrggqagi
      481 vphhrrlsrq
//
LOCUS       WP_284642423             445 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284642423
VERSION     WP_284642423.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 445)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..445
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47635
     Region          51..433
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(163,165,286,288,323..325,366)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mkntrkrwfg tgaavlltas lvagcgggag gatqgasdak apaakpfegk tlnlvtanhp
       61 wgdaikpllp efeaatgmkv tvqglfedql tqkltvqfts gsatpdvfmy rplqegklfy
      121 kngwvqplde yvkkdaaydf ndfsksavgs atvdgklagi piiteqeily yrkdllkqag
      181 ievpktldel vaaakklhdp skemygfvar gqrsplvtqv ssflyseggd ftkgdqasin
      241 tpeaikaftt ygtllkdygp pgvlnmswpq aigifaqgkv afytdansiy qnatdkeksk
      301 iadqvgfavf pagkagskpy nitswglamn akaankdaaw efikwatske ivlktqqkgn
      361 pgprasvwek pegvtgfpae lvpiikesak ggvdhdrpvv isvgeardav geivqkiitg
      421 egnvqetadk anktlqaiid kdktk
//
LOCUS       WP_284642447             314 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus
            silviterrae].
ACCESSION   WP_284642447
VERSION     WP_284642447.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..314
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36232
     Region          1..311
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mklqrllgit mlllsrkrig aqeladrfev slrtiyrdie aindagvpva sfagldggye
       61 imdefrierq ivtlddllsi vtalkgmqtt lqdqqldhll dkinalfaks eqhrieeage
      121 qliigmspwt rvdtdkdkla elrlaaknrn vvwltylspe geaeeravep iglawkgsaw
      181 ylyaycrlrk dfrtfklsri rklrvdmevf prrkerlvdl dakwgrwkmg pyitmvlrfh
      241 prvrvrveec fgpeqmtvee dgsllvrsel pidswlygll lsygpdvrvl epeflaeeis
      301 gqarriaely gqfp
//
LOCUS       WP_284642466             318 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus silviterrae].
ACCESSION   WP_284642466
VERSION     WP_284642466.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 318)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..318
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36599
     Region          4..317
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mrtetaiaaq vpeskiyrkq rarrmlrnrw lyimllpgvl yflifkylpm ygvliafkny
       61 qpflgfwdsq wvgmkhfnrf fgdplfwqll kntfilaiyn ivfffplpii malmlnelrm
      121 eflkrtiqtv vyvphfmswv vivsivylff ttegglvnea ieslggekin fllsadwfrt
      181 fitaeviwke tgwgtiifla alagvdpqly eaarmdganr fqqllhitip airstivill
      241 ilrlgnfldt gfeqiwlmln amnrevgevf dtyvystgis egqysystav glfksivglv
      301 lvaasnyiak kmgeegiv
//
LOCUS       WP_284642521              87 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Paenibacillus
            silviterrae].
ACCESSION   WP_284642521
VERSION     WP_284642521.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 87)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 87)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..87
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10292
     Region          2..86
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mgkrwtglii rallsghkrf tdiskmieqm sdrmlserfk eletegivvr rvydetpvri
       61 eyeltekgra lepmmkecek waeewis
//
LOCUS       WP_284642546             348 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein [Paenibacillus silviterrae].
ACCESSION   WP_284642546
VERSION     WP_284642546.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..348
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39132
     Region          1..348
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mikvpviils gflgsgkttl llrllqeagd rqlksvvlmn elgqtdvdgg lirsglpnas
       61 leklldgcic cskksevaac vrrlidqqpd vlfieltgva npeevadalt epyllnrvel
      121 rhivtvldse wvleynslfn tdhalkhtlr rqmeaadtil vnktdlvaps qlikiekaik
      181 kqndkaiihf tqhsqaestd lfsslqpldh gtpivrksfk viggpirkke tlaghrhdhl
      241 hhkrndhegt vttpsfsriq titlsvpehv pitvkqveqf iqrwgdlllr akgyvtvsdk
      301 klknrlvqfa gkriywdisd yhgpsylvli gielnrqrie qewnhllg
//
LOCUS       WP_284642544             118 aa            linear   BCT 25-DEC-2024
DEFINITION  (2Fe-2S) ferredoxin domain-containing protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284642544
VERSION     WP_284642544.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790154
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..118
                     /product="(2Fe-2S) ferredoxin domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=13313
     Region          8..99
                     /region_name="COG3411"
                     /note="2Fe-2S ferredoxin [Energy production and
                     conversion]"
                     /db_xref="CDD:442637"
ORIGIN      
        1 mttwnlqqtr chllicnggs cmkrgaeevt qaireeitkl dadnvihttr trcngrcada
       61 cvviaypdgv wyrditretg rqlvrkymeg qlleeqivys ferefiasgr siqgiakg
//
LOCUS       WP_284642667             256 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium accolens].
ACCESSION   WP_284642667
VERSION     WP_284642667.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..256
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27832
     Region          1..244
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(17..18,20..21,24..25,63,67..68,71..72,102,106,113,
                     116..117,122,138,142..143,145..147,149..150,153..154,
                     157..158,178..179,181..183,185..187,189..190,192..193,197,
                     200..201,211,213)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(141,145,148..149,151..152,192,195..196,198..203,206,
                     211..212,216,218)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(162..169,180,183..184,187)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mpnllrnvnp ltriflmfvw gtpllasidw vsaalslslt lilaplcgvs wvrlwkagwf
       61 lfliaplsgi smllygapgg eeyfswwlit vtensltlai aitlrvlava lptvvlardi
      121 dptelgdals qilrlpsrfv igavagvrmm tllksdwqsl gmarrarglt degrfkhllt
      181 msfgllvial rrggklatam eargfgrtpp gggertware srlhardgwv macglalacv
      241 pvvtsvltga wrffgl
//
LOCUS       WP_284642659             752 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium accolens].
ACCESSION   WP_284642659
VERSION     WP_284642659.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..752
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=82147
     Region          29..752
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mnsapknspa thspadatss sraenagisa ieaeqnyvdg lfdrlddeva aanarlnevq
       61 aevdpatpda dalvrretey hglqakldrl nvaqmglvfg rididapgdn pteegldrry
      121 igrmgldare enyrtllldw rapmarpfyl attaqpegvh trrqirmtgr tvtdvndeal
      181 dgpgvreeea gvasesalyf amqrartghm ssivetiqre qdeiirdntr gvmvveggpg
      241 tgktavalhr vayllythre qlsstgvliv gpntnfldyi srvlpelget gvvlstiggl
      301 fpgttpthte glvgreikgs eamaeilsaa vkdyqevpsa pqditvdglt ltitpsmvkr
      361 artrarrsrk phnqareafi ehfvedlaqe matkvgtdpl ggenllsrad vdqfhddlav
      421 desvvgcidd fwpeldpsev laallssreh iasaargyde etqaalyrad gyawtdsdaa
      481 lldelavlig lpnpeekkaa kdaewreqia daedaldils ssestdnddd mfeaeilsah
      541 dvidaetlaq rqevrdtrtt aqraredhtw afghiivdea qeltpmewrm lfrrcpsrwm
      601 tlvgdtsqtg spagvddwge alepfiaqrf rhhlltvnyr tpepitelan gllasidpda
      661 tpaiairdge pvrrladagf tpgvtteddg rltavidatn aeavkglefd hvivlnprei
      721 vdaspqglqn lyvcitratq tltlvgdtsg vl
//
LOCUS       WP_284642734             927 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Escherichia coli].
ACCESSION   WP_284642734
VERSION     WP_284642734.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 927)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..927
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..927
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=104078
     Region          22..443
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          512..927
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mrnlcflltl vatlllpgrl iaaalpqdek litgqlgngl rymiyphahp kdqvnlwlqi
       61 htgslqeedn ergvahfveh mmfngtktwp gnkvietfes mglrfgrdvn aytsydetvy
      121 qvslpttqkq nlqqvmaifs ewsnaatfek levdaergvi teewrahqda kwrtsqarrp
      181 fllantrnld repiglmdtv atvtpaqlrq fyqrwyqpnn mtfivvgdid skealalikd
      241 nlsklpanka aenrvwptka enhlrfniin dkenrvngia lyyrlpmvqv ndeqsfieqa
      301 ewsmlvqlfn qrlqeriqsg elktisggta rsvkiapdyq slffrvnard dnmqdaanal
      361 maelatidqh gfsaeelddv kstrltwlkn avdqqaerdl rmltsrlass slnntpflsp
      421 eetyqlskrl wqqitvqsla ekwqqlrknq dafweqmvnn elaakkalsp aailalekey
      481 ankklaayif pgrnlsltvd adpqaeissk etlaenltsl tlsngarvil aksageeqkl
      541 qitavsnkgd lsfpaqqksl ialankavsg sgvgelssss lkrwsaensv tmsskvsgmn
      601 tllsvsartn npepgfqlin qrithstind niwaslqnaq iqalktldqr paekfaqqmy
      661 etryaddrtk llqenqivqf taadalaadr qlfsspadit faivgnvsed klvalitryl
      721 gsikhsdspl aagkpltrat dnasvtvkeq nepvaqfsqw krydsrtpvn latrmaldaf
      781 nvalakdlrv nireqasgay svssrlsvdp qakdishlla ftcqperhde lltlanevmv
      841 krlakgiseq elneyqqnvq rsldiqqrsv qqlantivns liqyddpaaw teqeqllkqm
      901 tvenvntavk qylshpvnty tgvllpk
//
LOCUS       WP_284642789             109 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FtsB family cell division protein [Paenibacillus].
ACCESSION   WP_284642789
VERSION     WP_284642789.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..109
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=12574
     Region          19..109
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 mqatsksiqa dmqskgsgrr krilliglac ffswagitlw nqhgkigers mkvsaldqkl
       61 sevqkvnsdl nrdiqrlndr eyleqiiqrd mnyvkenqil fhqvkpqkk
//
LOCUS       WP_284642891             392 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Paenibacillus
            silviterrae].
ACCESSION   WP_284642891
VERSION     WP_284642891.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616068
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..392
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=44398
     Region          156..293
                     /region_name="Methyltransf_32"
                     /note="Methyltransferase domain; pfam13679"
                     /db_xref="CDD:379330"
     Site            order(186..192,215..216,241..243)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
ORIGIN      
        1 mehdlqellq eiikerkliq atvsqprrsd psgctkvtvk pvqlkgdlyy qfssfcgpkv
       61 fhdnlepaaa qeklsvllge qyrqallqsa dadyqvlisk kgkvgilkkp ptkeapktlt
      121 hnrkkqylle egvpvpflve lgimnaegkv laakydkfrq inrfvemiad vvphlakdrt
      181 lnivdfgcgk syltfalyhy lkelqgldir vigldlkedv iahccalaek fdyrglrflv
      241 gdiakydeld rvdmvvtlha cdtatdaale kavrwgadvi lsvpccqhel frqvrsdvls
      301 pllqhgilke rfsslatdam rarlldmmgy rtqllefidm ehtpknilir avkgkrppqa
      361 eleklrqgye afrdflgadp yleralqqel ka
//
LOCUS       WP_284642968             448 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284642968
VERSION     WP_284642968.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..448
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49229
     Region          6..443
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mtgpydtdvi iigaglaglt aameikrrga acivleardr vggrmystva dgvvidygaq
       61 wvssaqprim sllqqfhipt tptytdgktf yellgrrkaa rsgihplplp slfdfyrmqk
      121 rleqlsghid ncapwsskqa ssldartvqs wletsmftry gkalfrviae eglcgdlsef
      181 slldlawsls csgsfkglfs aeefwmlggs qtlpqqmaat lgdsvklner vrtiawqada
      241 vtvftdqekw vgrkvilamp paftarihye palpflrdqf tqrvgqgaal kfilvynkpf
      301 wrnngwngka yldrgpvttt ldstapgqpr gvlsaiatgt narslgllkp qerhakvlqs
      361 varafgteal qpaavhewdw lsdpwarggy sahlapgvlt qfgpallqpi gplhwagtet
      421 atewrmymeg avqsglraae evllsfre
//
LOCUS       WP_284642977             153 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Paenibacillus silviterrae].
ACCESSION   WP_284642977
VERSION     WP_284642977.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..153
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=17234
     Region          5..>112
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mnrissarye qldslrglaa ltvvihhlfl vplaltpffq llfhfkspvk llisghaavl
       61 lffvlsgfvl slplhrhqsv dylpfllkrl friylpylvs iliamgaasl fysgsidgls
      121 swfqsswkqp lnpasfmehm vhlpislpsr pfq
//
LOCUS       WP_284643116             182 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Corynebacterium accolens].
ACCESSION   WP_284643116
VERSION     WP_284643116.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..182
                     /product="YceD family protein"
                     /calculated_mol_wt=19120
     Region          1..182
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mtsplkfdvg ellnaqgada mpeqrtqtgp aperigvemi aipkgedltv aatltplgsg
       61 vlvdadisgv ltgecarclk elhpqldlhv tqvfaadesf vsgdeadsfd agsgdeipev
      121 kddeldllqa videaglnlp fapvcedgcd iqtpegvttg isgeeeeeek vdprwaglek
      181 fl
//
LOCUS       WP_284642991             317 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus
            silviterrae].
ACCESSION   WP_284642991
VERSION     WP_284642991.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..317
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36422
     Region          1..313
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mlsmlwilrt grkltatqia dsleisvrtv yryidalcas gvpvvaesgh dggirilesf
       61 ketplffnsv evkalldafk faqgagypyt eelesalkkv englheeqrh dlscrtngld
      121 vispsrlpsv vpllrdleqa akdgltvrit yrkanaeqdd erevdpygla ydrnewyvva
      181 fchrsqavrt frvdrvarle pteawfekpe rfsasvyfsd qskrereadg pltviriege
      241 pdtlnavsrh whmrhylter tdrevrflld vptmnkylpm ylmtfgtair ireplelkrq
      301 iqelaygiak hydedsd
//
LOCUS       WP_284643149             451 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Corynebacterium accolens].
ACCESSION   WP_284643149
VERSION     WP_284643149.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..451
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49076
     Region          1..451
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mhlhhdyakh lpdlvsathg eeqpdpqlvv lneelavqlg ldtdwlrsae gldfllgrdg
       61 ghamaysgfq fgsfnpqmgd gramllgeve kdgklwdlha kgtgltpysr lgadgrgtls
      121 smlreylvse amhalgvptt rslavistgr piqrghvqpa gvlvrvaash irvgtfhyaa
      181 qsghlqalad yaiarhypga dyreffqgvm drqiatvssw mrlgfihgvm ntdnttisge
      241 tidygpcafm esyspdtvfs sidqqeryaf gnqpailgwn larlaeslvp lfdadinagv
      301 dfaqetingf qekfatqrrs dlatsldtst evasaylaam qlsrpditla hraladaarg
      361 htlpaqelft dtdflddyla thpapdavda amprviprnm aveaalraae tgdmqpftel
      421 lhavthpwqp hpsyeqpdpn glagfltycg t
//
LOCUS       WP_284643233             409 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Paenibacillus
            silviterrae].
ACCESSION   WP_284643233
VERSION     WP_284643233.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..409
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45487
     Region          4..401
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mmrkvpviip hftqeekdav saviesgwva qgpkvtefek aiaahegvrh giattsctta
       61 lhlamvalgv qagmdviaps ftfvatvnsi kmtgaepvlv dvcedtynin sanvrqlihn
      121 qyflidgklq nklngnilwg ivvvhqfglc admeafnnia nefgisiled sacavgakig
      181 nthqgsfgnv sclsfhprks ittgeggmvl tnndeiaerm rilrshgasv sadqrhngkg
      241 fllpefnevg ynyrmndmqa alglvqvkkl dwlleernrr allynqlvak sasfliapra
      301 pqnyyhtyqs yvcmldrekl emdtieaage frnalltrle eqgvstrqgt havhllgyyr
      361 eayqykpedf pvsyacdkls itlplyvqms dedqyhvidm isrmkeell
//
LOCUS       WP_284643256             230 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium accolens].
ACCESSION   WP_284643256
VERSION     WP_284643256.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..230
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24614
     Region          1..227
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(13..14,16..17,20..21,58,62..63,66..67,91,95,102,
                     105..106,111,126,130..131,133..135,137..138,141..142,
                     145..146,169..170,172..174,176..178,180..181,183..184,188,
                     194,196)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(129,133,136..137,139..140,183,186..187,189..190,
                     193..195,199,201)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(150..157,171,174..175,178)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 myrlhpstvl tiaacgwlli lalnsplasa vvagamlayg vwatrslaiv lasaalcvpv
       61 alsmlvihap ygdnqlipli tsdglliaat lalrffalmv cfivamsvlr isdiakwlqv
      121 sraghkiayi vgaslqslpq gaqawrtvrd anqlagikvt wrntisrvvi pvisrlliqg
      181 terghvlaav gfdeegtrtl lrpvpdsnls rvlryivplg tigvmvfvwi
//
LOCUS       WP_284643271             317 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            accolens].
ACCESSION   WP_284643271
VERSION     WP_284643271.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..317
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35443
     Region          9..316
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 madgshklqa lvrslnlipy fqnhpdktpm eaaadlgmdp gelkdavdrl fcsgtgrnte
       61 elidlsfsyr dgvtiyndqg lgqalrltpt eagallltle sleampglld araiksaaek
      121 lrsimdertl siydtlstvd pqefdiqatl nrglnekrri rmrywsassn keterlvdpa
      181 rifivdaepy laaweeekqg hrtfridrik haelteetah prlkeldfda aapfnlgtad
      241 svelvireef twlaeyydmr lgkrlengti aatmqvgsvd wvvrfalgqa drlrviapqs
      301 ivnliaergn aalkgyt
//
LOCUS       WP_284643285             368 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Paenibacillus
            silviterrae].
ACCESSION   WP_284643285
VERSION     WP_284643285.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..368
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40884
     Region          14..366
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 miripifdss aevasiheev lasvkdvlfs gqfilgpnvk afekeaaeyl gvkyafgvns
       61 gtdalviglr aagigngdqv ittpftffat seaiqqvgad pifvdidpit lninikelqk
      121 vitprtkaii pvhlfghacd meeiqaiaat hdlkiiedva qgfggeykgr klgsmgdvgc
      181 fsffptknlg tygdgglvtt ndaeiarlig mlrahgsekk yhnemfgyns rldelhaail
      241 rvklpkidew nqkrreiaae yrrelceiqd ivlpeekenv khvyhqftir vknghreplk
      301 qfladkgigs mvyypvplhr lpvyqeehws fvlsekaaee vlslpmwplm savtqsevis
      361 avkayfgy
//
LOCUS       WP_284643308             473 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium accolens].
ACCESSION   WP_284643308
VERSION     WP_284643308.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..473
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51698
     Region          5..404
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msrttlrsfi qrihfyggmf vgpfiliaal tgclyalapt lekfayrdvm tveevnnpvs
       61 ledqisaaqk ehpdmpvsqv wpaesatdst rvlvadpgid eslqrtvfin padgevigdy
      121 ptysglgemp lrrwisslhe sfhlgqpgel yselaaswlw vlacgglymw wirrrpkkaa
      181 aplkkqpqrs krwkatrlhs tmgawifigl iglsatgitw sqlaggnvds vvekmnwkat
      241 pvetalttds sadaahdaha gheghgahga hggdaeaage apepeviaeq aervyatgra
      301 egltgplrly apedtdsgwk vserwvewry tsdevsvngs tgevidrlpf selplfskls
      361 swgiylhmgi mfglplqial falglaiatm vvlgyymwwk rrpqfapgsk rhfswtttgl
      421 galfaatvga fmpllgitla aflvldiivm ntgkrkatap kkkdedaelv pvg
//
LOCUS       WP_284643437             267 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Paenibacillus silviterrae].
ACCESSION   WP_284643437
VERSION     WP_284643437.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..267
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29637
     Region          4..247
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 meriykttep fmlegsgkra dthllmihgf tgspsefrrl gyylndlgyt vhgvllpghg
       61 ttpeemirtg wkdwsghvtk vydamkeqga kqivalghsm ggllalrlsm erqldavvsl
      121 aapiflmskk tifavllqyv ikyiekkptv aahiieeact ysktpvpcvv dlrkllkmvk
      181 sglnkvkapi fvgqgeldgl vhpksagyiy qhvsspvrqv ayypltshai lldeereqvy
      241 edvyrflahv enngtngtsa dgcidir
//
LOCUS       WP_284643350            1105 aa            linear   BCT 25-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284643350
VERSION     WP_284643350.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Pereira,J. and Lupas,A.N.
  TITLE     The VCBS superfamily forms a third supercluster of beta-propellers
            that includes tachylectin and integrins
  JOURNAL   Bioinformatics 36 (24), 5618-5622 (2021)
   PUBMED   33416871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..1105
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=121830
     Region          455..539
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          528..593
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          582..646
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          635..706
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mkrirhrkas rvlvliglll lasvlallli aekklsvrml yltsetsfdt aaygqlqqsl
       61 vanlelerra wdqeltekrl qtyhsiyldp slherlteaq qkllegyvak gghlflentf
      121 aadfpaeflg aqaivdvkap degpltaarl naqqsgtaag tegkelrpda gifftfpepa
      181 vnlrslqell isaadhlvkh dtenswkhfs wgkgmipsta qplmtlkgtd ialyslnrfg
      241 kgtvflsgtl lpnryfptgy dlaggmdpkl gfdryaavkn takgpvqgal yfdrsqlpve
      301 pffhftfaae salfrseyaa fvakelygys vkkvlgpygr pamahqnhfe aweairdgeg
      361 irwaemlrey qqipsfslvr safrwgqwve gvavhlntgt qaapafages psshyssglr
      421 lmttdgplrl apyptyrslg drielpyray paladlngdg radlivgsgd gslqaymnag
      481 tsaaayegqp lpagiqappf vfgapeplrq tdgtplavgs yasvaaydln adgrpdliig
      541 sadgtllaay geaggryskp aplraggqpi raagpvaaav gdvtgdgipd lvvgdgggqv
      601 tlykgqrsts galawlagtp lvrvpapfaa psvrdmdgdg radlvvgnle gdlrvylqta
      661 qgdfreagtl qgasmnqlgs halvgghnsv plwydvnadg kddlivgqle fglampidhp
      721 qfplkeqlne firytkehyl elyphifvhn ytsneqekqe ialhreafek lgipwrmtgt
      781 nqhtwrishp drlqtlrner eadiwfnfgf rspyapndpr lgfeydvslp flmtdseglp
      841 elqqpmllht papvlrtrqk qpmystedlf etytaldlpi dyfehveyqt iahpenllef
      901 vryldklrdt hdynfmteqq marsflntlt tkvevyrswg tvladrikka lhlptspsfl
      961 irqdtsrvpd qaaeykgtlg lvvdpggfym grtaatnaev hdtkagklyl gaaagastlv
     1021 sfeqqaeqas dmhlirvnvp yklnaqknrw tlelnapgmq qvklyssapl qfegpdgmtv
     1081 eqdkqqntyt ithfgdrtti tmtmp
//
LOCUS       WP_284643441             729 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium accolens].
ACCESSION   WP_284643441
VERSION     WP_284643441.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 729)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 729)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..729
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76394
     Region          2..723
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mshvdlgvsg mtctscssrv erklnkvdgv easvnfates asiefdpets tpadlikvve
       61 gagysafdms gsddgdqded aegtpvddar aaeqqsllrr tiisavlsap imvvsmvpal
      121 qfqnwqwaca mlativfifg gapfhsatwt nlkhgsftmd tlismgtsaa ylwslyalff
      181 gnagepgmtm smswssssae mdhiyfesvg mvitflllgr wfevkakgqs sealrtllsm
      241 gakeasvlrd gkekripisq lqvgdifvvr pgekiatdge vvsgnsavda smitgesvpe
      301 evgvgdtvtg atinasgkle vkatqvgedt vlsqmatlvt naqaskapvq rlvdriaqvf
      361 vpvvigisvl tllvhlifgg vapafiaavs vliiacpcal glatptailv gtgrgaqlgl
      421 likgpeiles tkqvdtivmd ktgtvtagem svtavhgdvl dyaaaverns ehpiaqaiar
      481 erdvepgtdf ststagveat vdgvrvgvgk prgdlgpyae afreaeaaga tpvavyldde
      541 laglievrdt vkptsaeavq qmkqlgltph lltgdnegaa krvaeevgit evtagvvpee
      601 kvdvikklqs eghnvamvgd gvndaaalaq adlglamgag tdvaieasdi tlmngdlrsa
      661 adairlsrrt lqiikgnlfw afayniilip vaafgllnpl fagiamalss vfvvsnslrl
      721 rkfssqryd
//
LOCUS       WP_284643494             375 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium accolens].
ACCESSION   WP_284643494
VERSION     WP_284643494.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..375
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=39982
     Region          7..368
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mnhgpgltfr flaaqvlvvv isllvaaava tmvgptlfhd hmlmtgqedp slelfhaeqa
       61 yrganlitla valptalisa llaslwlsrr lrtplqdltr aatsltagns rirvpagkag
      121 pevttlahaf ntmadrleht eqvrrqmlsd lahemgtpls vltvyldglq dgvvdwnnat
      181 htimadqltr ltrlmedidd vsraqehrid ldlveeglgd llhtaaaaag eayadkgvdl
      241 qvetitdtar vlvdrqrfgq vmsnllsnal rhtpaggqvr isvhrqgasa alihvaddge
      301 gippdqlghi ferfyrgdaa rsrddagagi gltiskalie ahggtltats pgpgrgavfa
      361 lrlplsppds eeaar
//
LOCUS       WP_284643499             316 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus
            silviterrae].
ACCESSION   WP_284643499
VERSION     WP_284643499.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..316
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36954
     Region          1..313
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mhkaqrliql imlvnerkrf tvqeladecg vsrrtmlrdl melselgvpl ysevgvgggy
       61 rvlrekvlpp isfteheata lffacqslkn ykvlpfenev gtalqkffhy lssdlkrkie
      121 rmqqrlvfwv pphelevrfl eelleaaldq rvvtivyeaa srrermiqpl glytmnglwy
      181 cqaycflagd yrvfrvdrvk hfseeadqsl rldtseerle swimrmeesd avelevelta
      241 egvrrcqsdl wlygtierre dgsgtirtrm sasyipwavh yflgfgmean vrrpqavrde
      301 irsklrslqe qydlea
//
LOCUS       WP_284643673             275 aa            linear   BCT 25-DEC-2024
DEFINITION  SPL family radical SAM protein [Paenibacillus silviterrae].
ACCESSION   WP_284643673
VERSION     WP_284643673.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Berteau,O. and Benjdia,A.
  TITLE     DNA Repair by the Radical SAM Enzyme Spore Photoproduct Lyase: From
            Biochemistry to Structural Investigations
  JOURNAL   Photochem Photobiol 93 (1), 67-77 (2017)
   PUBMED   28027411
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Frey,P.A., Hegeman,A.D. and Ruzicka,F.J.
  TITLE     The Radical SAM Superfamily
  JOURNAL   Crit Rev Biochem Mol Biol 43 (1), 63-88 (2008)
   PUBMED   18307109
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Sofia,H.J., Chen,G., Hetzler,B.G., Reyes-Spindola,J.F. and
            Miller,N.E.
  TITLE     Radical SAM, a novel protein superfamily linking unresolved steps
            in familiar biosynthetic pathways with radical mechanisms:
            functional characterization using new analysis and information
            visualization methods
  JOURNAL   Nucleic Acids Res 29 (5), 1097-1106 (2001)
   PUBMED   11222759
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18546879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..275
                     /product="SPL family radical SAM protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30415
     Region          9..>210
                     /region_name="SplB"
                     /note="DNA repair photolyase [Replication, recombination
                     and repair]; COG1533"
                     /db_xref="CDD:441142"
ORIGIN      
        1 mkpfiafttp srllnpasgy lagythtlnp ytgcafacsy cyvrempvak frpapwgtwv
       61 dvkegaaakl hkelvrerkk ggpitiflss atdpyqpiey rtkltrslle tmlevrpdfv
      121 lvqtrsplav rdidvlrqlg sgvrvsmtie tdlegvrkaf spaappipar lralrqlcda
      181 gipaqaavsp llpssdafad rladtgvqri clddyfmgdg slgkrtarlg lqpiyqslna
      241 adwydpsayl rvmeqlkhrf akdqvrisqa gfmpf
//
LOCUS       WP_284643677             165 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Paenibacillus silviterrae].
ACCESSION   WP_284643677
VERSION     WP_284643677.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 165)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..165
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18455
     Region          3..153
                     /region_name="NUDIX_MutT_Nudt1"
                     /note="MutT homolog-1 and similar proteins; cd18886"
                     /db_xref="CDD:467596"
ORIGIN      
        1 mlkynlcflk kgnqvlmlnr akapllgiwn gvggklepge tpeesmrrei reetgleape
       61 tlrftgtvtw dvdgsytggm yvyvaevpen tlrqtpldte egilawkpid wvcdaenrgv
      121 avhvkfflps mleggepmey rcafrgerll gveprplhlq tseka
//
LOCUS       WP_284643723             324 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus silviterrae].
ACCESSION   WP_284643723
VERSION     WP_284643723.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 324)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..324
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36510
     Region          10..324
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mqhiepasgs anvsakssit ggfrrtvakd fvrnkyiymm vvpvviyyii mhympmygav
       61 iafkqfniak giwnspwvgf khfqeffesy yfwrvvrntl linfyglifg fpapiilall
      121 lneiraalfk rviqtatylp hfislivicg miidfvgreg lindiivwlg gerssllsea
      181 gnfrtiyias gvwqeigwgs iiylaalsgi npelyeaskv dgagrwrqlf hitipgitpi
      241 ilillilkig hmmdvgfeki illynpttfe tadvissyvy rkglsgsyey ssssaiglfq
      301 slinfsllit anwltkrmng sglw
//
LOCUS       WP_284643748             256 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium accolens].
ACCESSION   WP_284643748
VERSION     WP_284643748.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..256
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27870
     Region          1..244
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(17..18,20..21,24..25,63,67..68,71..72,102,106,113,
                     116..117,122,138,142..143,145..147,149..150,153..154,
                     157..158,178..179,181..183,185..187,189..190,192..193,197,
                     200..201,211,213)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(141,145,148..149,151..152,192,195..196,198..203,206,
                     211..212,216,218)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(162..169,180,183..184,187)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mpnllrnvnp ltriflmfvw vtpllasidw vsaalslslt lilaplcgvs wvrlwkagwf
       61 lfliaplsgi smllygapgg eeyfswwlit vtensvtlai aitlrvlava lptvvlardi
      121 dptelgdals qilrlpsrfv igavagvrmm tllksdwqsl gmarrarglt degrfkhllt
      181 msfgllvial rrggklatam eargfgrtpp gggertware prlhardgwv macglalacv
      241 pvvtsvltga wrffgl
//
LOCUS       WP_284643794             796 aa            linear   BCT 25-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284643794
VERSION     WP_284643794.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     BTLCP proteins: a novel family of bacterial transglutaminase-like
            cysteine proteinases
  JOURNAL   Trends Biochem Sci 29 (8), 392-395 (2004)
   PUBMED   15288868
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..796
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=89090
     Region          410..576
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mlspehsspr ryratwagna tlsfllfsll lewlyplrql srvtevymig pfivafalll
       61 lvdsmrppgw vgwpvkvlll vsvtaylhgg aqalqpvwwe mwaadlaqdg ieavqgrwga
      121 weastrtmlf lagwaffisi vqtfvlerhy lfwfvlltlg ylgflqwmfe ldlwyavirt
      181 vgiglllqgw iqsgiwrrws deptyqrens egrkvtgvra plllalvcvi lgslggmlhp
      241 aemrpmdmsk syraweqwvt gkygspegga sqartgygtd dtllgqpltl ddkqaftavt
      301 prltywrges ksyytghgwt epegarvqnl ngaamanped pihrskellt qeirfhdprl
      361 grqlftggei isvdamstae grliaedwvw lggesgkytv psmvdpmmsy rvtvltppda
      421 agvlpssepl spemkskylq lpdglpervr slagtitssg gtqlektqav vrylqenyky
      481 aldasripkr dedlvdrflf eqkagycdhf ssamvvllra sgvparwvkg fapgdvsnie
      541 qrdgnpqytv evrnkdahsw vevyfpsygw vpfeptpgfs ggaltgdgtq altavaaatt
      601 kvsstasana satvaangse gtmvqrlapl vrqaavlaae aadramfyia slgkrdlvyv
      661 magtvllpvm gmllllafsw rhwrktvaag avqlqgdmgp qlffvslrhr alllygerlw
      721 kriertygrs sntqtlreya amhagqeess rqawlhfirq levlryereg ircsqvnrrs
      781 lyeawrqlkr ykaskn
//
LOCUS       WP_284643790             330 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Paenibacillus silviterrae].
ACCESSION   WP_284643790
VERSION     WP_284643790.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..330
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35876
     Region          21..310
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mqkpsslpss spsvapqqvl driryqvekv ivgkrevldq lliallcggh vlledvpgvg
       61 ktmivralar tidcdfkrvq ctpdllpsdv tgvsvynqrs aefefrpgpl mahmvladel
      121 nrtsprtqsa lleameekrv tvdgttyplp epfflmatqn padfegtysl peaqldrfll
      181 klrlgyptas eeadmlgrms ereplsavra vvlreeflal qreaqqahvd eaiklyival
      241 tsatrqhaev algasprasi almraaqaka fllgrtyvip ddvkslavav lahrlvlaps
      301 ailagrtaee vmasvaastv vpirriaagr
//
LOCUS       WP_284643813             205 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Corynebacterium accolens].
ACCESSION   WP_284643813
VERSION     WP_284643813.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..205
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22002
     Region          125..>184
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mkiiarllsv plalvaflal wlavapftph ipywgagali gpqyigpvil fslillvlaa
       61 igrlgsrsfy vpgafaaval iagislfgtq ihaakeqgtd vdiraalswa gvestdegpd
      121 htvaydsfhg edldmdiytp ndggthpvmm yvhgggwdqm nkhsqafnmr qmaqrgylvl
      181 sidytlsswd qptwkvaava sfsvv
//
LOCUS       WP_284643821             511 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium accolens].
ACCESSION   WP_284643821
VERSION     WP_284643821.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..511
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55859
     Region          167..508
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 madsqenpaa grpaqsqsqr tqqpqqppkk wheqldqlpq qgqgkkkrsk rdyikqipqa
       61 mplrtwlvvl lvvisglglt gssfavnsim rnvlynnvds elrsassswa rdvgndfflg
      121 dhtkrpptey vvlnylpdgt irysgptstt pdvegvplgg ypttvgsien ntkwralafa
      181 dsngvitvia kdmthekeil hglamvqvsi aaialaamag vgfwfirral rplrvvesta
      241 seiaagdldk rvpewplhte vgqlaaalni mlghlqrsvv taqekeeqmr rfvgdashel
      301 rtpltslrgy telyrsgatn dvdlvfskid keskrmsllv edllaltrae gtrldlrpvd
      361 llelslsvgs saraafpere vkvvnnaqsi pvvngdadrl hqvllnlisn glrhggeeat
      421 vtlqlrrdnk dilvdviddg kgmssedaah iferfyrads srtrdtggsg lglaivhslv
      481 eqhggsisvd sklgqgttft vrlpaleepe d
//
LOCUS       WP_284643831             375 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Paenibacillus
            silviterrae].
ACCESSION   WP_284643831
VERSION     WP_284643831.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..375
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41916
     Region          5..368
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mekkniplld ltaqyeqiee qilsvtknvl ksgnyimgpe vknfedevak ycnvkhaigl
       61 angtdalllt ldalgishgd evittpftff ataevisqvg atpifvdidp dtyninvkni
      121 ekaitpktka ilpvhifgqp vdmdeimeia nkhslyvied saqamgsvyk gkkigsigta
      181 gtfsffptkn lggygdggmv itnddelark lrilrvhgsn pkyyhsmigy nsrldtlqaa
      241 mlsiklpyld hwnqarreka kiydealvgl plrtpyiked retiyhlyii htdyrdelmk
      301 ylsekgissg vyypvplhrq nvylnlgyel gtlinaenss sgtmalplyp eltiedqryi
      361 istikdffsn vkkgn
//
LOCUS       WP_284643853             367 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Paenibacillus silviterrae].
ACCESSION   WP_284643853
VERSION     WP_284643853.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..367
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41836
     Region          12..352
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mayffersky dasmktikgf nglraisvll viashggwfq alsitnpvir gilsadvgvq
       61 iffvlsgfli trlllkehke ygninirnff irrilrifpl yflalsvvpi mesqgkiavk
      121 gcvyehayff lynftpqgce lnayshfwsl aveehfyliw pliflfnkrv afflvtlfai
      181 vasifglslw pdllsaynsg rwtypaaapi afgciaaylv tserfchwvs trlfriillv
      241 fsvatfianv fgeprfifyl gitclvlyvy fsqdshvikv lefqplayig qisfglyvwq
      301 gilagngsyr eypdyplplg egialtflla plsyhffekp ilrlkkyfes srgtslpnel
      361 grnkpla
//
LOCUS       WP_284644055             389 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Corynebacterium accolens].
ACCESSION   WP_284644055
VERSION     WP_284644055.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..389
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40852
     Region          11..388
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mneslekvas arldrwredg lwrspsvfgs gqvpesslrt atgktvqdav lfsssnylgl
       61 aehpeiknav kdsvdhygag sggsrlttgt sdlhvaveaa aaqltgypds vffatgyqan
      121 lstlqalasp eltiisdarn hasiidgcrl akasgaslvv tahrdtrave dalatrttky
      181 alvitdglfs mdgvlaplpe lsrlardyga wlmvddahsf gavgdrglgl peyfgvqpdi
      241 qlitaskalg aegglvatsk pvaqllrqqa rsfvfstspt patsaavlaa lkliesdpsl
      301 vnqlqgniay whnargttpq qgpiipvhvg deaaamdasa alldrgfivp airwptvarg
      361 aailrvtlma thtraqidal cteleqlgl
//
LOCUS       WP_284644048             276 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Paenibacillus silviterrae].
ACCESSION   WP_284644048
VERSION     WP_284644048.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..276
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32505
     Region          4..273
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mnvtlsmeqf hrlrdyiyqk tgiyfpdskl yfverrliqr mealglsdin yyysmlrfen
       61 ngtelqafie vltvnetyff refsqlkcfa eevlpelvrr ekgnlvfwsa gcstgeeayt
      121 laiilhemlg penlarcrii atdidnkvla farkgcyaer strhiptpyv rkyfeqsgte
      181 lkvnqqlrnl vefqqlnlme stmmrqlqev dvifcrnvli yfddqsrrqv aldfylsikp
      241 ggyvflghse smsritsifq lrkfqhsiiy qkpvar
//
LOCUS       WP_284644099             566 aa            linear   BCT 25-DEC-2024
DEFINITION  two-component system sensor histidine kinase NtrB [Paenibacillus
            silviterrae].
ACCESSION   WP_284644099
VERSION     WP_284644099.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 566)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 566)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 566)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..566
                     /product="two-component system sensor histidine kinase
                     NtrB"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009399 - nitrogen fixation [Evidence
                     IEA]"
                     /calculated_mol_wt=63618
     Region          225..563
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 madgwgmvtm lglkdtmlqv llalfpalll gigysqrdge rkpesglgfs mnqrlvllcg
       61 iscilcilfs fpmesfymfd mrivpyavgv lyggyvsgll ltllyfglra vmfggglafv
      121 vfialhsili pafflykkkf qaadvrgkmr iavglqglgw lmtsaglayr kwqaptelsa
      181 efylflicfc vlqlvsvavv vhlvenlrer qrlqhelrem svkhrseafk lqqlidatpv
      241 niiaideqqs vtlindtmms ffphlnkkhl lgtpysyise vfgrnheqsl miqalqgeyi
      301 rsqiqtyqer tfvtsafpik ledgriagav mvslettell rlrkeitnme qlslvgqmaa
      361 sitheirnpm avirgfvqlm qekkmvsneh ylqvmleeld rangiiddfl slaqnrvvpm
      421 eyadlhaiir qleplvlaea nlrghtlvld fgsetsrlll nakeikqlll nllrnameam
      481 eekgvltiat reldnevelr isdtgkgipe evqrklfepf fttkpggtgl glavclsive
      541 rhhgkitvns iegkgsvfti rfpkqk
//
LOCUS       WP_284644138             393 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Paenibacillus silviterrae].
ACCESSION   WP_284644138
VERSION     WP_284644138.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..393
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42167
     Region          6..>393
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mfthwlilla iavgiaylad kikqpyptll vvgglllgli pipaldelkq yvvsdevfrt
       61 aviliflsal igdaalklpf hevkenkspi lllallgtll tfvlisglsy svlgltlqqs
      121 lifgalmaat dpvsvlsifk smglnkklsi ivegesland gvavvlfkia ivttvlslts
      181 alqgsfefvk vicggiaiga aagwlvsrit sridnylvei glsiilfyga felseafhls
      241 gvisvvfagl llgtygrnig msdlthekmd sfwetiafia naliflmvgl evaniefgdk
      301 wgtilmsiai vlaariiavy aslvfdrevp ktwkpiiawg glkgslsial mlsvtpdfeg
      361 relllamtfa nvifsllvqg ttiqrlvayl kvs
//
LOCUS       WP_284644372             268 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Paenibacillus silviterrae].
ACCESSION   WP_284644372
VERSION     WP_284644372.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..268
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28838
     Region          3..268
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 meisslqnpr vkqwtglldk kgrdkeghfl ieglhlvqea lrsdiqpytv vysaererps
       61 eelrallmla aeqriecvgv seavlakctd tqtpqpvfav mpklpwkpeh vlkasasggl
      121 vvvidgvqdp gnlgtiirsa davgasgvll gkgtvdlynp ktvrstmgsl fhlpiaqgvl
      181 tewlpqaadt gvgivttslq gavscydydf rgptwivign egqgvseevr altgqhvlip
      241 mqgraeslna amaatvilfe amrqrqsr
//
LOCUS       WP_284644443             222 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein, partial [Corynebacterium
            accolens].
ACCESSION   WP_284644443
VERSION     WP_284644443.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         <1..222
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          <34..217
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 ppdlkhrtey raestngytt trdltvaagh vgcamnwvna haadydgdpg rfftygesag
       61 gqlvlnatad aaahpnhlps adcpgtpavp ravyadspal dvrhiydsdd pyaaqgsrdt
      121 vqkylggtpe eypdradfvt sathlttdmp pikivrsdnd rlvppesydd frriaqekni
      181 dlseyvrpha dhasalsahg vwnqhllqam pqffaehdpq gs
//
LOCUS       WP_284644531             254 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284644531
VERSION     WP_284644531.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..254
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28525
     Region          1..251
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mniavqlftl kkfvqtpedi aaslkrvkei gynavqvsav gpiddqalkg iadqngltic
       61 athipytqlt enleaviekh rvwdcsyvgl gsippqyrds legyltfaqq aneigkrlad
      121 aglsfiyhnh nfeftklngr lgmdilleet dprfvgfeld mywvqaggad paewirkvkg
      181 rmkvahfkdm miypereqrf aevgegnmny aaiveacrst gvewaaveqd ncydkdpfec
      241 latsyrnlrq lgls
//
LOCUS       WP_284644596             322 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Paenibacillus silviterrae].
ACCESSION   WP_284644596
VERSION     WP_284644596.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..322
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35497
     Region          11..300
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 memqnltami erlrqsvgsv ivgkehtvdl lltallaggh vlledvpgtg ktllakalaq
       61 avggtfkriq ftpdllpsdv sgihyynqkl gefqfrpgpv ftnilladei nratprtqss
      121 llecmeerqi tidgethqle kpflviatqn pvdnqgtfpl peaqldrflm rvsmgypsfe
      181 egvgilrrfq eanplqtlqa avtldevrla qaqasrvhia eellgyivrl aetsrkhpdv
      241 vlgisprgtq sllkavqaya lvrgrdyvep ddikamalpv lthrillqga mrvregrsed
      301 vlkrllneve vpsegpalsr gr
//
LOCUS       WP_284644639             679 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284644639
VERSION     WP_284644639.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 679)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 679)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 679)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..679
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=75539
     Region          39..666
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mksslglddp qkheankrrq ytlrinvfff vtfflfsvli vrlamlqfve gqelraqead
       61 qtkaqtkipp irgnildrng apiaittstq slyfrmesgq akddvvalak qlatifatyg
      121 sptqkqlspe diikamdvgy dlekkkthdp sysftprrik sdltkdeiay iserrdelkw
      181 ieiteesirs ydsintiavq lvgymrpfnt arssqghafy rdpektkeyl dtedvgfdgi
      241 erqyqeelrg kngsktypvn asqkiigkmt itppqkgnnl fltinkdvql taeqaimdql
      301 aymksaeara lkfpaigkna vagyavamev dtgkvvamas mpdydpnvwn ggippaeykr
      361 iepyinngti ttaypdypen erknhpssiv yvgstikpls vliglneglf tpstvyndtg
      421 vftygrngna rlqnsdgksf gpitattair vssntfmsam ignklyekyg kqapqlwsdy
      481 lakfglgvst gsglpreyeg lsefltntke teqsrmvfas wgqnekyttl qlaqyattla
      541 nrgkrlqpll vdkietydge lvkkfdepvv ldesqfsklh wdtvlngmes fvtgfddfpy
      601 klarktgtst qnvggqhvdn avfiafapad kpklavavvv peggfgswga apiarkifda
      661 ydqyygldgv pkngkgkte
//
LOCUS       WP_284644746             283 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus silviterrae].
ACCESSION   WP_284644746
VERSION     WP_284644746.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 283)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..283
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31875
     Region          25..283
                     /region_name="COG4587"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443644"
ORIGIN      
        1 msmntnpraa ayssirrall pkwlkyqavg rislsnqlay vadffvrsif ltvimyifmq
       61 lwtttyqgeg tptiagytiq qiiwyilfae altmafpsls trieeevksg dvgykltrpl
      121 hyigyhyaay laevyirlgv nllmgcligt alvgfpsfgl gwagfllmsf gavtvhftls
      181 mtlalcafwv eetrglefvy hkllftiggm lmplelfpet lqticrwlpf qtimyfpskt
      241 avryedvnll pmlltqaawi vilgivvlsv yrlgvrklnv ngg
//
LOCUS       WP_284644818             731 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Paenibacillus silviterrae].
ACCESSION   WP_284644818
VERSION     WP_284644818.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 731)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 731)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 731)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..731
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=83438
     Region          1..730
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mgieqlleka styikdsdli rireayefad qahygqvrks gepyilhpla vaeilvnmqm
       61 dtisiiaall hdvvedttvs lesvqdrfgp acakivdglt klekikfksk eehqnenyrk
      121 mfvamaqdir vilikladrl hnmrtlkhqs eeaqrriade tleifcpiah rlgisaikwe
      181 medialryln pqqyyrivnl mqkkrtereq yindvimnvk dklhemgieg disgrpkhiy
      241 siykkmtvrn kqfneiydll alriivdnir dcyatlgiih tlwkpmpgrf kdyiampkpn
      301 myqslhttvi gpkgeplevq irtfdmhrts eygvaahway kegtatsgad afgdnlnfir
      361 eiielqneaq dasefveslk mdffsdlvfv ftpkgeviel pagsvpldfa yrihtevgnr
      421 tigakvngri vpldhklktg diieiltskh sygpsqdwik iaqsshaksk irqwfkkekr
      481 eenvlkgkel ierevkrlgf epsvimkdde lmevakkfnf neiedmmsav gfggitaaqi
      541 vtrltekark eaeeaqqqal qltneikevk apnperrgrp tngvrvkgvd nllvrfarcc
      601 npvpgdrivg yitrgrgvsv hrldctnipa pdmgeegnrv ievewaddie anynveieit
      661 ghdrrgllne vlqavseskt visavsgrsd knkmamihmt ilirnidhlh svvekikrvk
      721 dvysvtrimq s
//
LOCUS       WP_284644843             416 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Paenibacillus silviterrae].
ACCESSION   WP_284644843
VERSION     WP_284644843.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..416
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44330
     Region          1..>70
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
     Region          <152..331
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mcqevielmq ryldqdldet eyrrmllhvq gcaacselfe rlvnlsqele slpkvtppvs
       61 lvdsimprlq lidagevsga vetaepakrr hipawrqrmr ewvslpvagg vvaaglvlgf
      121 fvfsqqqlss ndqkaevlls isagsadkaa stsnsakpev ngaapqasta apmargaapa
      181 aandmksdap qskqvptmqd eapkdkapaa ppqsekinps naapaptpsp kqeepeaaad
      241 akatetapgd smalkkqvvp pdgsqepvqs paataapepe rtlmgkmgsp gtesapegsm
      301 gnfrqtpgeq ygiaalppma sfahpsvqdq sgmkestsag neytaslnae ghvvirdnaq
      361 qkavftssyq wkpeqvtlig wspelvftye vkvseqtket ytirvkelke eklktp
//
LOCUS       WP_284644886             825 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-mannosidase [Paenibacillus silviterrae].
ACCESSION   WP_284644886
VERSION     WP_284644886.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Nascimento,A.S., Muniz,J.R., Aparicio,R., Golubev,A.M. and
            Polikarpov,I.
  TITLE     Insights into the structure and function of fungal
            beta-mannosidases from glycoside hydrolase family 2 based on
            multiple crystal structures of the Trichoderma harzianum enzyme
  JOURNAL   FEBS J 281 (18), 4165-4178 (2014)
   PUBMED   24975648
REFERENCE   4  (residues 1 to 825)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 825)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14312054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..825
                     /product="beta-mannosidase"
                     /EC_number="3.2.1.25"
                     /GO_function="GO:0004567 - beta-mannosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005537 - D-mannose binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=94634
     Region          18..>643
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          648..735
                     /region_name="Mannosidase_ig"
                     /note="Mannosidase Ig/CBM-like domain; pfam17786"
                     /db_xref="CDD:465505"
     Region          741..>800
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; pfam17753"
                     /db_xref="CDD:465483"
ORIGIN      
        1 mrqtidlnga wsmrpvgdee wipakvpgsv asdllragri edpyyrdrqy evfdiflkdy
       61 eyerefelea aqleaarlel vcegldtiae lrlngkelah twnmhrtyrl dlkglavagr
      121 nklqvtfrsp vnyvvnmqke rylwaanddy vvqgyphlrk ahhmfgwdwg pkvpdsgiwr
      181 niyieahqvg riedvyvvqk haedgtvtld vrvqterftg telqldavll apdstvaass
      241 eltvgetpdr illsvsepel wwpnglgkqp lyelklqlis egaavheqsy klglrtltvr
      301 qepdawgesf efevngisif tmganyiped niherlsrkr teqlirdcvk anfncirvwg
      361 ggfypdddff elcdqygliv wqdhlfacae yemteaftae ikaevadnvr rirhhaclgl
      421 wcgnnemewa wmswgfpkre klrtdyikqf eilipevtka hdpetfywka spssgggfdd
      481 pnasdrgdvh ywevwhggkp fteyrkhyfr fcsefgfqsf pshktvaaft epgdrniftp
      541 vmeshqknag gngkilfgis enflypkdfs sllfvsqllq aeamrygveh wrrnrgrcmg
      601 svywqlndcw pvaswssidy ygrwkalhya akrfyaplll saeetgaqvk lvvtndtlne
      661 eagtvvwklr eaggriveeg slnvlsgams aqpvadldfs esvqgredel yleyalhqgg
      721 qevsegwvlf vrpkhfrlsp epklicdiee aedrfiltlh aeslalfvel dfaqldarls
      781 dnffhvsagr pkrielmksd lsspasadql rrelllrsla dsyvc
//
LOCUS       WP_284644892             707 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus silviterrae].
ACCESSION   WP_284644892
VERSION     WP_284644892.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 707)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 707)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 707)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 707)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..707
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=78850
     Region          52..>190
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          170..692
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          444..691
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mkfaacllig lligcstlts awatspeyna asnkqdlqqw hpredgsvsl ngpwelywnr
       61 lfepgdfteg apgnaltvti paqwksyenn gqalsnegya tyrmqfvvss evagqplgly
      121 fnnvatayrf wingeggdgn gtvgtdakhm vprsypkvyf fqprpgdnei iiqvsnfaqr
      181 tggiwesiel gdaediaalq rnrvmlwtfg tgclllmtvf saflflfrrq ergalwfgli
      241 claicirssl lgesfiyvlf pglswewgvk leylseivti islaafvnkq ypqdavprif
      301 lpfavalagf gafvlatpak vytqlmvpyv ivllfpvfly vmyvyiraaf rrrigsqanm
      361 lgflvffltv ihevlyytgy lsngglvsfg llfflltqll nlsllftrav tqsemlsmel
      421 nqviasqeet irqrtsslqa lnlqleqgnl elcrieqars kllaevhhdl stpitaikgy
      481 skaistevia aeeapayagr iyersllleq lidnvvelsq lksgetpfql devpllpflr
      541 qlcqryaadt mvrgitltwe ehdltlpmer ellaaldrfr fervfanlis navkytpndg
      601 hirvwiefri pegsdhghvt ihvkdsgigi pegelehifk rryripgirq sttgsglgla
      661 icteiiarhq geigvrshpg qgsdffislp aklgdssant gkntegg
//
LOCUS       WP_284644937             311 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus silviterrae].
ACCESSION   WP_284644937
VERSION     WP_284644937.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 311)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 311)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 311)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..311
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35400
     Region          2..311
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mnrrlnhakg rsriwfdlkr drylyllalp glifflifky vpmwgviiaf qnyspyvgvl
       61 ksewvgfehf akffsnpefm llfrntmain lmsltlffpl pillslllne vrseaykriv
      121 qsivymphfl swviiagltf llfakgeglv nklleaggfe rmdfltnpdg fwfmltvqsi
      181 wkeagwgtii flaaiagvdp qlyeaarmdg agrirqmwhv tlpairnvvi illilrlghm
      241 mdvgfeqvfl myngavseva evfdtyvyrv giqqgqfsfs taaglfksiv glvlvvgank
      301 lakkmgeegv y
//
LOCUS       WP_284645137             579 aa            linear   BCT 25-DEC-2024
DEFINITION  Rieske (2Fe-2S) protein [Paenibacillus silviterrae].
ACCESSION   WP_284645137
VERSION     WP_284645137.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..579
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=64138
     Region          4..98
                     /region_name="NirD"
                     /note="Ferredoxin subunit of nitrite reductase or a
                     ring-hydroxylating dioxygenase [Inorganic ion transport
                     and metabolism, Secondary metabolites biosynthesis,
                     transport and catabolism]; COG2146"
                     /db_xref="CDD:441749"
ORIGIN      
        1 mngwiqagtv eelreqgpkl vkggivvfhh edevhaldnr cphlgfplhm gslckgiltc
       61 hwhharfdvc gggtldpwad dvpvhdttvr dgviwvnpns rnsnqvqlyk drllsgleqn
      121 iglviakaiv glmeagvpet eiveigiefg vkqrrqgwgs glttltaman vlpkldkqgr
      181 ilalfqgmlh tardssgngt rflldplpht nvseerltew yrdcievrdt rgaervllta
      241 vqagademrl fsmmsmaatd hfyingghtl dfhnkafesl kyvgdeqrhy vlaslvpmfg
      301 sasrseelhs wqspvnlvqp lkeafeelsg kgvssgiegs giddekllqv llgddplrtv
      361 rvlkeallgg aspvrisqia alaaaervvr fhtqndfgdw nsvlhtftha havheglirs
      421 tdpwlvrgif htaatiyldr flnipaaprp avigaaevaq eptelleild kqqqvapaaa
      481 wvirylhsgg kpeplfnvlg hallredtef hsfqmyeaav teydrwases gpfaekaret
      541 lilavtryla ahaptsretp htakiawrlh rgeklfeee
//
LOCUS       WP_284645185             319 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus silviterrae].
ACCESSION   WP_284645185
VERSION     WP_284645185.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 319)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..319
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35969
     Region          8..319
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 msaeightka ssvrtgwkar nrtfvkiaqn yqlyllffpt llyfvifqyg pmyglqiafk
       61 nfspskgiwn spwvglqhfe rffdsaqfii tlkntllisl yelvlfpipv llallmnqll
      121 sqkykrvvqt ivyaphfism vvlvgmlylf lnprnglinq glvalgldtv hfmadavwfk
      181 sifvwsnvwq nagwgtiiyl aaltsinpel heaaimdgas klqrilhidi pgimptvmil
      241 lilnmgsfmt vgfekaylmq npmnaqasei iqtyvyktgl vgaqfgysaa iglfnnvtnf
      301 iiliamnsla krlkqaslw
//
LOCUS       WP_284645203             439 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284645203
VERSION     WP_284645203.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 439)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..439
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48382
     Region          43..430
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(148,150,282,284,321..323,366)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mkkstlsils imlaataavg cakteepkqd aeapaaandh vqltwwvdtr gdvqqayeem
       61 kqgfekanpn vkinivktpd drinerisia antnempdiq qgsffwplsy akkgllvpld
      121 divdkqdfee ktlknvsvdn kiyiypnstv aigflvnkdl fkeknaldll pknmepwtfd
      181 qflkaakavt dpgkqvygyg lyagdtggdq athsllwgfg aktwndennk ailnspegvk
      241 gvefltrlid egvvppgapg lkasalmndm fvqgklgmaf gnignlptln kaftegtakk
      301 fevdivpfps vdgkssntvl fgygtwmwnt kdetkmkwak efikyansqe nmakmakaes
      361 vliarkslak tyaegtlqyk ttqlfkyagn iglsvpgype trsafypelq aaftkkktaq
      421 qalddwtkka neiianssk
//
LOCUS       WP_284645262             477 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus silviterrae].
ACCESSION   WP_284645262
VERSION     WP_284645262.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..477
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=53759
     Region          90..476
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mqltkrfftm naltvllsig ltalaavifi aaytkvfgge gyvdgwkrvy evrtglselk
       61 reamslefdq llnksyqhel fervkalggs aillknrevl qstrnfsdid ierslmltgg
      121 tpnqdtleld gkvylfaras yqlrsgdegi llmlapvqln tdfymllgif tvcfflivfl
      181 llnfwvsyrf srgiirpvsr lrdaavkise gdlsggiaee gegevrelsr tlelmriklk
      241 esvylqqkyd dnrkflvssi shdlktpvts ikgyiegimd gvagtpekma ayletarska
      301 ilvntmiddl llyskldlnq lpyhfektdl vsyfedcvad yryeyekagi rlelvnqleg
      361 tvcalvdrer lkrviqnild natkysdkdd grvtiflret rtsaiieikd ngkgipqeel
      421 phifdrfyrv dssrksadgs glglaiakql veghegklwa rsavgegtsm iislkkl
//
LOCUS       WP_284645230             427 aa            linear   BCT 25-DEC-2024
DEFINITION  Gfo/Idh/MocA family oxidoreductase [Paenibacillus silviterrae].
ACCESSION   WP_284645230
VERSION     WP_284645230.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..427
                     /product="Gfo/Idh/MocA family oxidoreductase"
                     /calculated_mol_wt=47284
     Region          1..326
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
     Region          <279..410
                     /region_name="GFO_IDH_MocA_C"
                     /note="Oxidoreductase family, C-terminal alpha/beta
                     domain; cl21649"
                     /db_xref="CDD:451345"
ORIGIN      
        1 mkkvtavlig agdrgayaya pyalhyphel afvavaepne qrrqafaeah glsseqtfes
       61 wqellqspsv adiaiictqd rmhleptlga leqgyhvlle kpmspdprqc vemelaakkh
      121 nrllsichvl rytpfwqtvk riiregkigd iasvqlnenv ghlhmahsfv rgnwnnsdvs
      181 spmilaksch dmdilayvld kpclrvssfg slmhfkeeca pegapercld gcpaeascsy
      241 yapryylgeg sgwarkitgd tskegilhal rttpygrcvy rsdnnvvdhq vvtmefegga
      301 tamfsmcgft hdntrivqim gtkgeirgnm eenqitvydf vtkeqsvirl hdskvghngg
      361 dvgiirdfln qvrgetkges ltsasvsvrs hlmafaaees rlkggapvdi tlfherlteg
      421 lhsgkee
//
LOCUS       WP_284645315             341 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Paenibacillus silviterrae].
ACCESSION   WP_284645315
VERSION     WP_284645315.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..341
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35919
     Region          35..338
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msivtihkhe hsglkhfviw ltiscilgti gfaasiklgs spirwedlwy gligaqetke
       61 qlivrtlrlp ralvavmvgs slavagvimq avtrnplasp qifgvnsgaa lvvvasivfi
      121 psltpsqlvi saflgaalgg wlvytmasgg gkftpvklal agmtvsmlls avteglivlh
      181 dqktqnilfw magavdgsdw ndvllmlpww ligilgalll sgswnvlnmg ddvaqglglh
      241 iryvrsaagi lvillagasv svagpigfvg lvvphivral vgtehrfvip lsallgasll
      301 lyadigsrfi sypfeapvgi vtaavgapff lylvrkgrrs e
//
LOCUS       WP_284645512             286 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284645512
VERSION     WP_284645512.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..286
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31544
     Region          1..282
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mklgvstysl yqalrsgemd vldvidyvae iggqhveivp lgftlldnds lieaikeraa
       61 akgleisnya iganfadksg teleqeierv mrevdvaakl gvklmrhdva saqdisfrhf
      121 seqlpmlaea crriadyaad kgittsvenh grfiqaserv qalilatgrt nfkttldvgn
      181 flcadedpvi avannisyas mvhvkdfyir pedstlnegw frsvngrylr gaivgqgdin
      241 mrkvletikg sgydgyvsle fegiepcklg vrlglnyiqt vwrelp
//
LOCUS       WP_284645513             285 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284645513
VERSION     WP_284645513.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..285
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30749
     Region          4..283
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mnnkigvivd sfrvgvregl qkakavgadg vqiyavsgef apealstear qewksyiasl
       61 gleisalvgd lgghgfqdan anpvkieksk rildlavelg tqvvtthigi vpddenspvy
      121 aamhkacael sdyaasmnay faietgpeta rhlkkfldgi sskgmavnfd panmvmvtgd
      181 dpvqgvhtlr dyivhthakd girlrevdpr diygavdhek ladmatdgda frevplgegs
      241 vdwprylqal kdigyggylt ierevgtnpe adiskavqfl ktfra
//
LOCUS       WP_284645542              75 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Paenibacillus].
ACCESSION   WP_284645542
VERSION     WP_284645542.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 75)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 75)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 75)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..75
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8050
     Region          2..70
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 maiiinidvm lakrkmsvte lservgitma nlsilkngka kairlstlea ickalecqpg
       61 dvleyksded ttiig
//
LOCUS       WP_284645572             322 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus silviterrae].
ACCESSION   WP_284645572
VERSION     WP_284645572.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 322)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 322)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 322)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..322
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36081
     Region          7..322
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mrteqlsiqa rtkrqsvglr klwnavrlnr fyylliipgm lyfvifdyip mfgviiafkd
       61 ispfegvgav ltgewvgfkh fvkfwnsyyf wnvmrntlli sgykllfgfp asillallln
      121 elknavfkri vqtisylphf istvvvaglv mmvlstdsgm inaavaalgg epihflgape
      181 yfrsilvish vwqsigwgsi lylaamtgid pglyeaakmd gasrfrqmwh itlpgithii
      241 vimlifsigg llnagfekvl llyspsvyev adiidtyvyr egltslqysf atavglfkni
      301 lamililgan yiakklnqtg iw
//
LOCUS       WP_284645617             332 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus silviterrae].
ACCESSION   WP_284645617
VERSION     WP_284645617.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 332)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..332
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37212
     Region          3..332
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 msmvhetgsr salarprwis rwladcltra kkqrllllll lpgvlyfiif nyiplygvli
       61 afknfkmqeg qsflsaliss pwagnlgldh fkqfvqgphf gklmantfll glysivfgfp
      121 apilfallln elrhkyyksf vqtisylpyf lsvvavvgmm kmvlspgdgi vnvvlqklgf
      181 epvyfmsmpe wfrtlfigsg iwtglgmgav iylaalskvd sdqyesavid gatrlqqiwh
      241 itlpaikpvv iimlilnlsg vlqvgaekii lmyspltydt advlstyvyr rglvelnfsf
      301 gaavdlfnav invlflvtan hlarrftees lw
//
LOCUS       WP_284645644             266 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284645644
VERSION     WP_284645644.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..266
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28476
     Region          2..260
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mirlginsvl fkeydfataa khiqlcgydg ielaaikgmc ehlelerwre qapqikaite
       61 elglallsme vasldeqrlq lafeaarelg vpivnvgpgg ksnvdedlsa sidklarmae
      121 lageygvtlc vkahvgqsvy ntpttlrame sigssafgid mdpshiyrag enpeealaqv
      181 vsrvrhihir dckgrqagpg pieaqacgrg dinlidyckv lvesgydgpv nlevigangh
      241 slaqlsvvaa esrgylhavl kslgar
//
LOCUS       WP_284645689             337 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus silviterrae].
ACCESSION   WP_284645689
VERSION     WP_284645689.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..337
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=37117
     Region          16..335
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mkmrlklfft fwafgivifl lsnqrmtrlt vgndgietti tvlllgvsai agvsyllait
       61 lclrleilag qtknavrqhp glpsglersq deiamltytv nllkeqlteg esirnqlvad
      121 iahelrtpla ilrghletil egaeefdrah liplldetkr msrliqdmqd lnlaeagkla
      181 ldrtwslfrs tleeivsile iaaeaksitl hldgggdgel ymdasrikqv finlignavr
      241 ytpeggridv hysyqhgqvi vtvsdngpgi ppeslpyifk rfyrvensrn rmsggtgigl
      301 aiakefievh ggtihvesep gvgtsftvtl pvfppnp
//
LOCUS       WP_284645718             307 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Paenibacillus silviterrae].
ACCESSION   WP_284645718
VERSION     WP_284645718.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 307)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 307)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..307
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34944
     Region          10..98
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mrtleltlqe alevckalsh ehrmeivril seeplnvnei aermslpfst aavnikkled
       61 agiisteivp grgtqkvnsk kydriiinlt ererqeehel lmelpigefv nceveptcgl
      121 lseegilltq ddprsfyeld rkraqllwir sgfieyqfpn rlpygakvee ldlslelcse
      181 apyhkldwps ditcwingve igtwtspgdf ggergfltps wwgtnntqyg mlktwktnte
      241 gsyidglpss tisildlrlh dkpyisvrlg vkkdatnvgg mnifgrkfgn yeqdllmkvk
      301 ytpgrnr
//
LOCUS       WP_284645801             307 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus silviterrae].
ACCESSION   WP_284645801
VERSION     WP_284645801.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 307)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 307)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 307)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..307
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35226
     Region          3..307
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mlptrglsat wrhirrdrql lllflpcilf fiifrygply gmiiafkdyn vyqgildsew
       61 vglrhferff dspdfwllfk ntfllgvftl vwafpfpilf avllnevrhm afkktvqtfs
      121 ylpaflsvvi vssmiidfls pthglinqvl klmgfdgiyf laapewfrtv yvsteiwqhm
      181 gyeaiiylaa iagidptlye aakvdgatrt qmmryitlps imptvlimfi ikagamfrig
      241 yekvlllynp mtyevadvfs tyvyrkglle tnysyasavg mfealialvm llisnliskk
      301 aggkglw
//
LOCUS       WP_284645833             287 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284645833
VERSION     WP_284645833.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..287
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32364
     Region          6..280
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtkgiigvqm mmlkgkveel gvyetlrrva elgyrcvevs qipmttenvt elrrasqdfs
       61 ieiaalsaal epmmpgmkge tltndfdkiv adckalncsf lrigmlpfhy igsrektmef
      121 iakadeaaar laeegislyy hnhhiefqky ngeylldmik nhtshigfel dvhwiqrgge
      181 npvevikrya grvallhikd yrvgkmdtsa lengdfgkfm qaftnviefa eigegslhmk
      241 dileaglvsg vhyflveqdd vygrdpfdcl rtsaenlkam gygdwfh
//
LOCUS       WP_284645966             315 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus
            silviterrae].
ACCESSION   WP_284645966
VERSION     WP_284645966.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 315)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..315
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35978
     Region          1..314
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtkskrlmel mmtvnrkrrf kvqeladefg vskrtilrdl qelselgvpl ysevgphggy
       61 qvvrervlpp iaftegeaaa mffavhalrh ysslpfeaes asalskfylh mpgdvrdrid
      121 smkhrvdfit ptrrgdapcl ailldaaihk kvlmihyesk vegetsrriq pgsiyahngf
      181 wyckaycflr qglrvfrcdr iseaaedtsg iepldlddvh lerretyepr epvrlraels
      241 sigvqrceae lwlapllqvr edgggsidan vsrsdvpfyt effislgnev dlkepkelve
      301 sirrrlseql trysp
//
LOCUS       WP_284645994             320 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus silviterrae].
ACCESSION   WP_284645994
VERSION     WP_284645994.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 320)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..320
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36321
     Region          1..320
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mstvikeqag rpsaedknsf kyrairdlav nkyvylmlap vvlyyfvfyy tpmyglqiaf
       61 kdfspglgmw espwvgfkhf qdffnsyyfw rllrntllls lyellfafpa sillalllne
      121 lrsavfkrav qtvtymphfi sivviagmmv dflardglin nvlawfgiep iaflresgwf
      181 rtifissgiw qsvgwgsiiy lsamsgidps lyeaakvdga nrwkqtmhit lpgiaptvii
      241 llilqignfm tvgtdkilll ynsstyetad vigtfvyrkg ilesdfsysa avglfnsiin
      301 fillvlanti srrtsetklw
//
LOCUS       WP_284646027             122 aa            linear   BCT 25-DEC-2024
DEFINITION  VOC family protein [Paenibacillus silviterrae].
ACCESSION   WP_284646027
VERSION     WP_284646027.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..122
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13512
     Region          3..120
                     /region_name="PhnB"
                     /note="Zn-dependent glyoxalase, PhnB family [Energy
                     production and conversion]; COG2764"
                     /db_xref="CDD:442048"
ORIGIN      
        1 mianpfivve nckdeikyyq svfggeiail rrqgeqvlna dlhvegatlk fadtqaakpa
       61 lkgdyvrvfl rietesafrs iygqfavggi vntevyeapf ngllaivtdr ngvcwvlsyy
      121 rt
//
LOCUS       WP_284646013             131 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Paenibacillus
            silviterrae].
ACCESSION   WP_284646013
VERSION     WP_284646013.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..131
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15028
     Region          11..106
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mlkpektfnt avevtleiig gkwkpvilfh ltfgkkrnge flrllpaitq kvltqqlrel
       61 eddgiikrtv yneippkvey eltefgwslk dilhlmcrwg dlyveraygg rakvlfgikk
      121 lmkndpekag p
//
LOCUS       WP_284646037             288 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus
            silviterrae].
ACCESSION   WP_284646037
VERSION     WP_284646037.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..288
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33712
     Region          39..287
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          201..283
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mayqahfptn kalkreriyi rhqvsewqds wplhthdgye iyfflhgnah liigneiyml
       61 qpgdmflfsg dvlhrpnpak dtpyirsyin ftadyvqema gadmaekllg lflqpnglli
      121 rwdehgvnem dshyaslfhe rekeaignef miqsllvqll lkiyrkskem yalltappqs
      181 qketnvrril vylnqhykna islealskem hlnkyymchs fkeitglsin nyitrkride
      241 akkllrlsde pvgfmseqlg fsnpvhfsrm fkqyagvapq tyrkmhqt
//
LOCUS       WP_284646038             436 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284646038
VERSION     WP_284646038.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 436)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..436
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47531
     Region          49..427
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(156,158,283,285,314..316,356)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mmksaksaml lslaavltfg tvacsnggst qsggkdagta gsaakkevtl dylwftdgie
       61 gevmkaitad yqkqnphvki nlievpfkdl gtklktmisg gkppalarmt dtgqfanqal
      121 dltpyvgsad sftsqfidsi kpyyvvdnki iaapmdvtan giiynktlfd kagvkvptsk
      181 dniwswdefa aslkqvmdkg gaksglvwdf tphrwstmly qfggsmisad gkkaainspe
      241 gvqaleyfvk lhkdgiipqs vwlgsenpnn lfrsgtvavh wagnwmlsny kdintfewgv
      301 tympkqkirs svpggkyvma fkgtgveket aefikylssk evnarynkds lfisprkdsa
      361 kldyafgkem fevfadelan ttplaandws rqdivpkfst dlrnniveai sgkvtakdal
      421 dktaklidka igeqak
//
LOCUS       WP_284646075             218 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284646075
VERSION     WP_284646075.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..218
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=24236
     Region          <14..201
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 msvvfqlrpe eprvqalcra drrfaelaqq igtikisakr dafaylaqsl isqqlsvkaa
       61 dticrrvreq cgdftvdhml svseealraa gvsgpkiryi kglaelirlq eldldslhgc
      121 sneevlallt kvkgvgrwta emflifylgr edvlslgdag lrraarwlye eetpsgpell
      181 elkgekwkpy rsiaslylwe ainvglvdag plpttdlc
//
LOCUS       WP_284646097             280 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284646097
VERSION     WP_284646097.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..280
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31381
     Region          10..274
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 msdagallcs lctisfrhal isfdqilqya drhgfdgvel wgvharqlye qrqqerlslg
       61 rlhvsmisdy ldigshadmp atitrcceml nvaewagakh irtfagrkps klvhtkelec
      121 ivgqlrilgd lclaqgvdll vethpgtlad dtqsslqlmk mvdheavgln ldflhlweag
      181 dqpvdsyrql epwvghfhfk nvasrsychv fepqevysps gkregmaalg dgavnyreil
      241 rhvgrsgkfa slewfgaspf trlstdlqwl rhqlnqaiak
//
LOCUS       WP_284646166             324 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus silviterrae].
ACCESSION   WP_284646166
VERSION     WP_284646166.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 324)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..324
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36706
     Region          4..324
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mevsaskgkt wsaivgkken yftrlkknas shwqlyllml lpiiyllifk yvpmygalia
       61 fknyiptkgv wgsewvgmkh fdrffhsyef vrimkntill smyslfagfp fpiilalsln
      121 yvnarffkkt vqmityaphf istvvmvgii lqmmdprvgl iqtimkyfgl ptinfmgipe
      181 wfshvfvwsg iwqnvgfsci iylaalaavd pslheaavmd gankirrmwh vdlpgimpva
      241 villimntgh vldigfekvl lmqnplnmsa sevidtfvyk vglastainy syssaiglfk
      301 svinlillvl vnrlarklgq tslw
//
LOCUS       WP_284646268             412 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Paenibacillus silviterrae].
ACCESSION   WP_284646268
VERSION     WP_284646268.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..412
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46205
     Region          100..405
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mkqidafdrp fdsfdtladr igealrcpvt ienanhqlia ysshkvpadp artatiisrr
       61 vpeqvvsslw kngilrmlmd sdqpvrvpai sdvglgdrvv vairhhnevl gyiwaledee
      121 rldeqglmtl rqaarasrdl mlqlqlqrsk eeagkqnlfw qlltgnrmta deikrkaael
      181 gidlprayqv lvlqfgseiv lneyrqiqym ltaaagmsvk lqvrdarhli vlagtasgqp
      241 dnkasgafvr sfirqwserm ggaavdgagg lfyddytlve rsyrealqvl slkrdfpqal
      301 sdavsygalg fyrflplmdq agnaameepg vihkllkydr ehgscllqtl rvyleqdshv
      361 kdtadalhih tntltyrlkr iaevggidln smdqkvdvyl qlklmtmtrs vc
//
LOCUS       WP_284646474             293 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus silviterrae].
ACCESSION   WP_284646474
VERSION     WP_284646474.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 293)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 293)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 293)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..293
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33073
     Region          5..293
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 msmlwplyim avpgilflit fkyiplvgtv iafkdysvfk gmldspwvgl rhfqsliqhp
       61 dfirifgntl mlgflkialv fpvpvllalm inevrksalr kgiqtalyip hflswviiag
      121 ivfdffslsg lfnvvigwfg ydpvlvmqes dyfrmvyiit aiwrdagwgt vvymaaissi
      181 dpqlyesami dgaskfkqll hitlplllpt vlvlflleig nfmelgfdhv fnlltpmtys
      241 vgdildtyvf rtgiqqaqys fatavglfqs vigfvlvyif nrlsrkvsdg glw
//
LOCUS       WP_284646437             752 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284646437
VERSION     WP_284646437.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..752
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=86842
     Region          <607..752
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mpgwkgfkgn tpslfaklms sflvvivlla afnftsflyl kskihseiik ynelnlnstv
       61 vryenhfrlm remiiglsrd dkwmanlnll rnvkqfngyd rmesviadik llianpfmsm
      121 dnillhfrnd gyvlekegts eaerlftryy aspaysadfw krqfedpamf kllpaaefve
      181 tsahveknkg rllpaiikfm plkdmyfivm lqpdkmfqsy hyatdtdfti lgedgtaiys
      241 srpesslttt eafqgaeghf srdqhyyfyk kgqdtgltyv svvpiqtisn qliklnlifl
      301 tllvitials vvtslfftfr lnspvqmimd amqkrgsslp lqgqvrefdl isekvssilk
      361 tndqmtedld kkksllryya ytnklrsihm nlaeltdmva adtpfvlvmy qvtfkesfae
      421 ldtelekaly fvreyiassl lqvfkdpltf qmekdtvlsl ifnpeeaeid qtleqlrqvf
      481 aldrdllfvt vsvspvysts tellsaynia ssmlqqrtln dltqiirtpk apastvhftv
      541 leeeefhtrf msgseesvme wirkqlqaly kkeatvvefk qlakeithll nksamklnlh
      601 qeqsdtalpl leplnsfysl eqyeqwfqqq lspmlskvle ktaekdpmts fvidyldhhl
      661 dqditldima dklnitpgyl styfkektgt nfsdylnglr mqrakeqlhn ldlkihevaa
      721 rvgyqnvnsf irmfkrysgm tpgeyrkkyg as
//
LOCUS       WP_284646511             289 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paenibacillus
            silviterrae].
ACCESSION   WP_284646511
VERSION     WP_284646511.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..289
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33159
     Region          6..289
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 maieagvnvs svqddlckdy frtlerlael gyknveligy nkskytrfmd dipidqlkek
       61 ltqydltvis aqelgrsdrp idvhdwdavc syyeqinchs iviptvwmqn rddavriage
      121 mnrvgqrlka ngfafyyhnh ahefqrdgee tlydiliqnt dpdyvrfeld lgwvlragiq
      181 pteileklgs rceivhlkdi ninprfpvni fealkqdgmk afdsfkiyqs ytspedyadl
      241 gsgaydlasl ftfikemght ryaiveniga ssdkfnslas dldivrqyi
//
LOCUS       WP_284646630             356 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus silviterrae].
ACCESSION   WP_284646630
VERSION     WP_284646630.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..356
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=39329
     Region          <63..356
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrkptirtyf vlsllllllm pwlffvaahl ittqslniga erpnsytvqw aaalagllla
       61 flivgvrmrt lllvplermg qaarriaagd wdiqlpqsai reiaevrdgf evmvnglqss
      121 hrkqaeleee rrfviaaaah dlrtplfalr gyldgleqgi artpdqvaky vavckeksaq
      181 ldrlvedlft ftrmeyletg isentddfav ivqksvdslg pqaqqkhisi avfssaddcv
      241 iradshlver aisnlldnav rytpaygria vqcrregeqv aftihdsgpg fapeelkrif
      301 eplyrgeqsr nrstggaglg ltisqrilrq yggeltacnh pdggailsgw ipaank
//
LOCUS       WP_284646664             323 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus silviterrae].
ACCESSION   WP_284646664
VERSION     WP_284646664.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 323)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 323)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..323
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36255
     Region          10..323
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 maqstgnplt atkrikasgd pkvwqtirtd vkrnwaiyam alpviayyii fhygpmyglq
       61 iafkdfapak gilgspwigf khfesffngi yfwrllkntl linlyellfg fpaaivlall
      121 lneirnalfk rlvqtisylp hfisivvvag mmvdflsrdg lvnqllapfg ieaidflkeq
      181 dwfrflfvss giwqgigwgs iiylaaiati dptlyeaarm dganrwkqtl hitipgimpt
      241 ivilfilnmg smltvgsekv lllynpltye tadvistyvy rkgvleasys ftaavgffns
      301 vvsfiliiaa nsiskrvsen klw
//
LOCUS       WP_284646671             112 aa            linear   BCT 25-DEC-2024
DEFINITION  SRPBCC family protein [Paenibacillus silviterrae].
ACCESSION   WP_284646671
VERSION     WP_284646671.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..112
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=12303
     Region          <4..81
                     /region_name="SRPBCC_CalC_Aha1-like"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of Micromonospora echinospora CalC, human Aha1, and
                     related proteins; cd07814"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mtledggtvl eavayekfvf qwtpgesttt isftltslgg gtlvtvlesg ytrseqdlka
       61 fgdcavgwge amtllkyyld hgitygavpr hhlektmtee ylkrtdnfta kh
//
LOCUS       WP_284646900             300 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_284646900
VERSION     WP_284646900.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..300
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          <1..290
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 fkkrgqndaf rypqgvkldq ensriflpkl gwmryrnsrq vtgvvknvtv sqscgkwyis
       61 iqtesevstp ahpsasmvgl dagvaklatl sdgtvfepvn sfqknqktpa rlqrqlsrkv
      121 kfsnnwqkqk rkiqrlhsci anirrdylhk vtttvsknha miviedlkvs nmsksaagtv
      181 sqpgrnvrak sglnrsildq gwyemrrqla ykqlwrggqv lavppaytsq rcaycghtak
      241 enrlsqskfr cqvcgytana dvngarnila aghavlacge mvqsgrplkq eptemiqata
//
LOCUS       WP_284646753             297 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus silviterrae].
ACCESSION   WP_284646753
VERSION     WP_284646753.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus silviterrae
  ORGANISM  Paenibacillus silviterrae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 297)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 297)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 297)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Paenibacillus silviterrae"
                     /db_xref="taxon:3242194"
     Protein         1..297
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33639
     Region          3..297
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mmriwhnyel ylfliptivy filfhyvpmy gvqiafknfi avkgingspw vgldhfqrff
       61 esyqfitvlk ntlgislyel lvafpapivl alllnqttne rfkklvqtvt yaphfisvvv
      121 vvgmlylfls pkhglvnlml lglgidpiyf masaawfkti fifsgiwqnl gwatiiylaa
      181 lsgvnpdlhe aavvdgatkl qrirhidlps imptimilli lnigsfmsvg fekvylmqnq
      241 lnvdsseiiq tyvykaglln aqfsysaaig ffnsvvnfil llsvnrlaqr mkqaslw
//
LOCUS       WP_284646902             217 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_284646902
VERSION     WP_284646902.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..217
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          <1..196
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 vaklatlsdg tvfepvnsfq knqktlarlq rqlsrrvkfs nnwqkqkrki qrlhsriani
       61 rrdylhkvtt tvsknhamiv iedlkvsnms ksaagtvsqp grnvraksgl nrsildqgwy
      121 emrrqleykq lwrggqvlav ppaytsqrca ccghtakenr lsqskfrcqv cgytanadvn
      181 garnilaagh avlacgemvq sgrslkqept emiqata
//
LOCUS       WP_284646959             423 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Listeria
            monocytogenes].
ACCESSION   WP_284646959
VERSION     WP_284646959.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..423
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=49420
     Region          1..71
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          <211..>269
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
ORIGIN      
        1 mnliglrikn irkekqltlk dvaqgiisvp ylaniengik iasletlihi akrlevpeqi
       61 lliseeesnk ellkemdaif ellvfsntve mesrlnsiae nvdllhespa velsfyclqt
      121 ayyyktwefs kaeeieakyl nntkkraees fprqllsyyy ygqavkhsha tcdyqlavey
      181 wekcvdltes kgfqvvfhvc icinyicqsi yepalahikq alelikdeeq erivailyfy
      241 gyiyfqigfm aeaknrfeqa veyfekypes kkiyyfvvql kmaeienieg nealfnekia
      301 slyeelmaye ttntsfntnd ylvitelmvi faekgfvdea aslmglmnkv dervkelnff
      361 ieytetllly hqneqvsyee kmikllkkid dsndpilidr vkkhaskhfa kstkykmayd
      421 ils
//
LOCUS       WP_284646965             907 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Listeria monocytogenes].
ACCESSION   WP_284646965
VERSION     WP_284646965.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 907)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 907)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 907)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 907)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 907)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 907)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 907)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18767243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..907
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..907
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=105586
     Region          1..907
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          1..196
                     /region_name="AAA_27"
                     /note="AAA domain; pfam13514"
                     /db_xref="CDD:433272"
ORIGIN      
        1 mritsidiig ygkwsdahfn nianfqvfyg eneagkstim afihsilfgf ptkqqsiprm
       61 epknggpygg rltledtplg kviierlkgk atgdvriyyg dgqtageekl peiigeidrn
      121 tyeaifsfdi hglqnihqwk kkeferylla tgttgsdall kgaealqkkl dslykpsgrn
      181 plinqqlkkv keaqqafqna kkqnaqyeql inekeqaivr qtelqkektt mrveldtlat
      241 ladlwplyqe wkalsnkase tteatfppdg virlehlhlr ekewqnqliq leerqknlis
      301 nnnyehsaff aeneaevtyl ietyaafger eiqlknlkqe ikfqqvdtkq plriwssele
      361 qtmihlkeke qshkeqqhdi qlklkftnds eeklqkkidq ieaemwdnkt fqqakekmqd
      421 spktsktktm vslgifavvf vlmivfqaiw svalvfvsal ivgyafittg kssptnneqi
      481 lafleqkkir qewqqllnem dmvasqiael raaenklsen iyqhtmeirh ffsdlginse
      541 pssnwlyels iykknsekrq lameliskle plvekqeayr trlenlklpi eytdteekit
      601 flrqgllyyr nhltenakla ekleqvtmql dlvkqdlllv kkekadller anvsneedfr
      661 maamrvkeeq kwrerlvlie aqlepekrea lnryenqati kekelqlees lrqieleqeq
      721 ihaslaaqnh aidkleeggt favlmqefys eksklqqisa ewtetklalq mlqntmqqlq
      781 egklpktlkl aseyfnhlts gnyrkvylqd nrlqveskds ipffpeelsq atkeqlylai
      841 rfalidvihk dfplpiiidd gfvhfdssrm gqmmqllqkr ksenqvifft chqetrkyfs
      901 sedirvl
//
LOCUS       WP_284647263             422 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Escherichia coli].
ACCESSION   WP_284647263
VERSION     WP_284647263.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..422
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=48276
     Region          2..402
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mklnarqvet akpkdksykm adggglylev sakgskywrm kyrrpsdkke drlafgvwpt
       61 vtlaqarakr deakkllvqg idpkaeqkea qaensgaytf etiarewhas nkrwsedhrs
      121 rvlrylelyi fphigssdir llktshllap ikkvdasgkh dvaqrlqqrv taimryavqn
      181 dyinsnpasd magalsttka rhypalpssr fpeflarlaa yrgrvmtria velslltfvr
      241 ssemrfarwd efdfekalwr ipakreeikg vrysyrgmkm keehivplsl qavalleqlk
      301 qisgdkellf pgdhdatkvm sentvnsalr tmgydtktev cghgfrtmar galgesglws
      361 ddaierqlsh sernnvraay ihtsehlder rlmvqwwady ldinkcerit pfdfakkgna
      421 is
//
LOCUS       WP_284647313             311 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Aeromonas veronii].
ACCESSION   WP_284647313
VERSION     WP_284647313.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas veronii (Aeromonas ichthiosmia)
  ORGANISM  Aeromonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Aeromonas veronii"
                     /db_xref="taxon:654"
     Protein         1..311
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34752
     Region          239..>284
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mknskmdkki aelkalamna dvagwkglsl arpcadsgag ddnwhvvndn dtmsthcfdf
       61 nhstsvnses vsrfiaavtp qlvielieal aaekcradaa saevaelyeq rrqfwielka
      121 adcraktgel alkrimekse nnsynwgech faltkcaeft fertekleev etvekfnrlv
      181 dscainlrsf lpnliygqlt ehlsenpvkr ekvleramlk airlhavdaa psaakrkvfi
      241 trklltklig crydtidrmv akgelpkpir lgangrhrfi aseiipalmk hdidlerlam
      301 ahgvdlnnpd a
//
LOCUS       WP_284647341            1120 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-glutamate dehydrogenase [Legionella pneumophila].
ACCESSION   WP_284647341
VERSION     WP_284647341.1
KEYWORDS    RefSeq.
SOURCE      Legionella pneumophila
  ORGANISM  Legionella pneumophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 1120)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1120
                     /organism="Legionella pneumophila"
                     /db_xref="taxon:446"
     Protein         1..1120
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127559
     Region          <5..1117
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 mmtnswkdkl qkqltqqfgs pkgkqlidky tetmsmsyce qhtpeeaiqd ilqieklskd
       61 nplvidfyek thlqyplhik lyryetpipl sdilpmlenm glrtyterpy kiktrdgqlf
      121 wisdfnvtys qtdsfnitqv nnifaealin inlgicendg fnklvlsagl swqeitilra
      181 yakylhqigi rysqsyiekt iemhaaiard lihffylkfg lkrksaiqkd msaleqkiqi
      241 nidaisslde drimryfwsl mkatlrtnyf qknhaglpkd ylsfklksse ipdlppgqpl
      301 yeifvystrf egihlrstkv arggirwsdr pedfrteilg lmkaqkvkna vivpsgakgg
      361 fvlkkplhaa sreqiqqevi scyksfingl ldltdnlind ktippqnvic yddpdpylvv
      421 aadkgtatfs diansiakeh gfwlgdafas ggsagydhkk mgitargawe svkrhfreld
      481 iniqqqdftv vgigdmsgdv fgngmlyskh irllaafdhr hifldpnpdp lksyeerlrl
      541 fnlptsswed ynlqliskgg gvykrssksi pispqvkksl aieanaltpn elirallkap
      601 vdllfnggig tyvkattesh advgdktnef cringaelhc kvvgeggnlg ftqlgrvefa
      661 lkgglintda idnsagvncs dhevnikill dkeirekklt ekkrnqllsr mtdevadlvl
      721 qdnynqalil sisaahsshy sglyqdymke lekwvnldrs veflpddkkl lerkttgagl
      781 trpelavlma htkihianel lkshlpddsy fttfletgfp islrkpyaka lpkhplsrei
      841 iatqlsnklv nnmgitfmyr mlmetgmsia diacaytisa cifqtdvlqn lidsfqdkis
      901 lstqyellhh irqllnlatr wflhnnrlag giekniknyg esvkkleqli pklmggvtke
      961 yleklisqfv sigiekdmaq kiaitralyt slniievatq nkfdlsltae tyfkvgsqfn
     1021 lvwfrdqian dsreghwntm arlslrdeld nlqrrltiai lttntkerts eklinywleq
     1081 nhpiqkrwek llemllgsen idytiffial relssliqvl
//
LOCUS       WP_284647516             456 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Photobacterium damselae].
ACCESSION   WP_284647516
VERSION     WP_284647516.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..456
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48792
     Region          96..456
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mttlalsikn wlinrnslif iadvilfvvl lntlpfeknv viglsilafv avlwlteaih
       61 vsitailvpl lavgfgifqt pqalsnfanp iiflflggfa laaalhqqel dkaiadkvlv
      121 iakgrmsvav fmlfgvtavl smwisntata ammlplvlgv lnkvdakqer ntyvfvllgi
      181 aycasiggia tvvgsppnai aaaevglsft gwmafglpvt lvllpmavai lyfmlkpnln
      241 hmfeldhkpv ewnhgkcmtl aifaltvflw ifskpinaml ggfskfdtlv altaivllgv
      301 srvvrwkdie kstdwgvlll fgggiclsni lkatgtsvfl ahslseflaq aglfftilvv
      361 atfvvfltef asntasaall vpvfatiaea lgvspvvlsa liavaascaf mlpvatppna
      421 ivfgsghikq semmkvgiyl nlaciialtf fawffw
//
LOCUS       WP_284647532             381 aa            linear   BCT 25-DEC-2024
DEFINITION  RHS repeat domain-containing protein [Photobacterium damselae].
ACCESSION   WP_284647532
VERSION     WP_284647532.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..381
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43596
     Region          <6..240
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mlfqgdahfe ydefgrlite rcgknqtlvt hyeydcqhrl iratmpdgsq acyvydafgr
       61 risktvtdkl gqssttefvw qgdkllaeqt dgqnyqtyly qpdsfkplal lkgegkacei
      121 yhyhldhlgt ptdltdeqgn ivwqaqyrsy gdvvaqhvek ivnpirfqgq yydsetglhy
      181 nrhryyspkt grfttvdpig lagglnnyqy vpnpvnwvdp lglsnkkgnv cssfnnsgvn
      241 srnwlnqevk tydghlwspl dpdmreppiv qygpytdeqr daflkgkqsk tfiaphhrhq
      301 lsiiehngvi delngpghps gnnhtkling lnrhpgpsyf nqiqggsalr areirmhlre
      361 kgkrlikden snlwidpmfe e
//
LOCUS       WP_284647671             337 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Photobacterium damselae].
ACCESSION   WP_284647671
VERSION     WP_284647671.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..337
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=36722
     Region          1..333
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mddlktalsl sqqaryqqvf dvmptgvlll datgrihdan peahrlldep ligerwidii
       61 krafapqddd ghevslhngr kvklaisass egqlifitdm tetrllqsrl selqrlsslg
      121 kmvaslahqv rtplssamly ashlgseqla patrqrfqgk lvdrlhdlek qvsdmllfak
      181 ggdnkvvtrf slesllncle amieqpvihh qidfsidcdd esccllgnen alasaisnlv
      241 inaiqnagdg aqiaiqcqlq qgnvlisvvd ngpgipvelq hkilepfytt rsqgtglgla
      301 vvqmvvhahn gqlnvvsepe qgacftlqlp ladtdte
//
LOCUS       WP_284647892             503 aa            linear   BCT 25-DEC-2024
DEFINITION  SPOR domain-containing protein [Photobacterium damselae].
ACCESSION   WP_284647892
VERSION     WP_284647892.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..503
                     /product="SPOR domain-containing protein"
                     /calculated_mol_wt=55726
     Region          45..501
                     /region_name="DamX"
                     /note="Cell division protein DamX, binds to the septal
                     ring, contains C-terminal SPOR domain [Cell cycle control,
                     cell division, chromosome partitioning]; COG3266"
                     /db_xref="CDD:442497"
ORIGIN      
        1 mighdattrl dldsqiqfls rlqfvtqfss hliqisgpfg agktellhyy lehfspeqhq
       61 vllsaepdms ltsvrtqllq qlvptkpfne qdsllqsvsh mlsrdrlrcl lvvddahhls
      121 ipilaelwel vchanqqadw qlnvllftep dviaqplakm tygqsevple leiaplpane
      181 vsqliehcye qdlqkrrelk lryqhsfafp gqldddtqpp geevsmttsh klspqsglli
      241 glllalvval lwlwpeskps edlaidssas qvvegtelid sgeptedtaa lppdvtqegl
      301 tvgrtdsdkr vvvpaqvvda mmgnqalglv gaqtqfsdae inaldpanvh pspatspkat
      361 ttplseskpv sesvkpkpeq ppvesldkpl kqldapqpis hdnqhsdkqi lqqvnsrhya
      421 lqlaavhswq qakqfaakyg vtdsahiykt erqgkawfiv vtgdyssatq akraknqlsh
      481 evqalkpwpk syaqiqkemn rvk
//
LOCUS       WP_284647935             292 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Photobacterium damselae].
ACCESSION   WP_284647935
VERSION     WP_284647935.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..292
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=32398
     Region          8..287
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 maifsyypwl fpvfatifgl lvgsflnvvi yrlpimmerq wrnecieafp dlikadakln
       61 tdtfnlsvpr srcphcghli savenipvis wlvlkgkcks chapisrryp mielltaalc
      121 gtvailfppt wwavavifft falialtfid idkmllpdqi tlpllwagif lallgispvs
      181 lqdsvigaia gylclwsvfw vfklltkkdg mgygdfklla algawlgwqm lpivvllssl
      241 agaicgiill kvqksdhqtp fsfgpylaia gwisllwghs iitwyvsnil gm
//
LOCUS       WP_284648009             631 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidase U32 family protein [Photobacterium damselae].
ACCESSION   WP_284648009
VERSION     WP_284648009.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..631
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=70656
     Region          17..315
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
     Region          458..516
                     /region_name="DUF3656"
                     /note="Collagenase; pfam12392"
                     /db_xref="CDD:463557"
ORIGIN      
        1 mtsaselsta plnnisnrie llapaknadf gieaikhgad avyiggpafg araaagnsie
       61 diqrlcefah ryhaqvfval ntilsdsela qaeqliwdiy hagadalivq dmgilqlnlp
      121 plalhastqi dnrdkekvef leqvgftqvv larelslpqi hdiathtnmq ieffihgalc
      181 vsysgqcyis haftnrsanr gscsqmcrlp cnlktrqgev laenqhllsl kdnnqtanle
      241 alidagvrsf kiegrlkdls yvknvtahyr reldaimarr pelyssshgr vetnfnadpd
      301 ksfnrgktdy fvqdrnagis dfrtpkylgq kagkvrlvgk dfieldsdle fnngdgiayf
      361 sqnylkvqqs ddklqgirvn radgnrlyfa qmpkdlkvgm vvyrnfdkaf edllakdssr
      421 rrigvsmila dshrglmltl tddygfsaqv efecektpan daektlanir kqlnklgntd
      481 feardiqvkt sqmwftpasv lnglrrdgia aleqarfdgy qrpapgkynp dvefpkrhls
      541 ylgnvantsa kafyqqhgvi evedayelnk vyedvplmit khclrfsfnq cpkqvegika
      601 epmilemgge tlklvfdclk cemkvvghnk q
//
LOCUS       WP_284648186             319 aa            linear   BCT 25-DEC-2024
DEFINITION  HlyD family secretion protein [Photobacterium damselae].
ACCESSION   WP_284648186
VERSION     WP_284648186.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446287
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..319
                     /product="HlyD family secretion protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34573
     Region          5..315
                     /region_name="EmrA"
                     /note="Multidrug resistance efflux pump EmrA [Defense
                     mechanisms]; COG1566"
                     /db_xref="CDD:441174"
ORIGIN      
        1 myknlafils isalasiagc ndstshqalg tlerdsvrlt atsneiirqm piqegqkvka
       61 gdllvqlddq mqkaalekar aeqgkakayl qrllngerpe diataqahla ksqanlqdak
      121 qnfqrvaklv krkvmtqadl dnaqaqlsaa iadvtanqet ldklvqgtri ediaqaeqal
      181 kasqaevalq qqklsdltvv atrdgildsl pyhvgsrvpl ngvvaivean sapyaqvyip
      241 epyrvqlkag dkltvhvdgl dtpfqgtlrw iatestftpy yalnaedrar lvylakidlp
      301 adavdlpsgv paqvdmphe
//
LOCUS       WP_284648212             141 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Photobacterium damselae].
ACCESSION   WP_284648212
VERSION     WP_284648212.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..141
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=15491
     Region          17..140
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mittgnsrwq ddelspdltp lldiifivmv fllltasvki kslnvdlpqt etqilqttsa
       61 dpitinllas ephwaldgnq qksweafstt lldevkasps kpvvigaekt asveqmlkll
      121 aflqkndika tqllmeednk a
//
LOCUS       WP_284648244             500 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Photobacterium
            damselae].
ACCESSION   WP_284648244
VERSION     WP_284648244.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..500
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=56890
     Region          <165..500
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mkqwltytae miecrkcsel itffqnvsve qlavaqclvf ypsddgrfli sdngseqwev
       61 ddfdhpfsha lhhakpilld pqkrpfwmqh sdfshfskqi sdaesllivp lpfqsqkika
      121 vvgligekqi isgiindehw lkfshvfisq willhelank qrqevklnes isqlknhrtn
      181 kgwvdlsrhl igssavmesl reqiaiaaqs sltvlvqget gsgkelvaka ihtlsdrkdk
      241 pfvavncaai penlleself gyekgaftga isarkgliaq adggtlflde mgemplalqa
      301 kllrvletle yrplgsnkeq rsqfrlvaat hvnlrknvnq gsfrqdlyyr lyqyplevps
      361 lsnrlndide ltevfieqyn qrekrhilgf dtqtlallkt feypgnvrql rslveyacvh
      421 tdsnqfineq alpktdmsse klvsslpfee iddlklalee yerkiicdrl tffagdraka
      481 aeslglpkrt lahkcqklei
//
LOCUS       WP_284648411             329 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein [Photobacterium damselae].
ACCESSION   WP_284648411
VERSION     WP_284648411.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..329
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36540
     Region          1..322
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mkriptniit gflgagktta ilsllarkpe nekwavline fgnvgvdgam meqqgaiike
       61 vpggcmccva glpmsvgina llaqkpdrll leptglghpk evinkltsdt yknyidlrat
      121 itlvdprhfs esiytenenf qdqlaladiv vankidqcdd ydlflfeetl akaeppkall
      181 ahvengkldp awldverlqr eashshhhhh nddntelapl pefelapgqq firkenqgqg
      241 yhscgwffaa eqlfdfsklf sllsninaer vkavvntdkg cyafnvvnri vtvnelsleg
      301 fesrlevidk eilpwdelen ilcsivtaa
//
LOCUS       WP_284648455             948 aa            linear   BCT 25-DEC-2024
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Photobacterium damselae].
ACCESSION   WP_284648455
VERSION     WP_284648455.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 948)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..948
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=105263
     Region          58..947
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msvelsrrsf ikqgvmagic iytvpalarf nlnldgsssl ispelesswk snfkvnfrtd
       61 avakvtgekv ygrdlragdi dewpnqqywa yyirvdradh iyegidinfl pqnakpttvi
      121 taetlikdnv qlppfygvnm lvaegqtpdy lgqaaallif dsfltfnrak smiqfndnvi
      181 kygkktplva nsldpwgtwr itrvegnskg tlpdlysplk nglnfpnyvd hkpfwpqana
      241 ngssleqqms vaktiesamy epnnfildrr yqtqiidpmf mepecfngwy dkqtqtmhti
      301 ptsqspadfy ryatlmlsqg plagkvknlv vhspyigggf ggkdhsilpy ygllaamycd
      361 kpvrmandrf qqfqsglkrh pfdmhnrlsi nkktgkfqgi issmsldggg renfssvvae
      421 vgasalqsiy yfprnditav anvsdnpdag smrgfgtlqt maamemmvne aaqllnidpi
      481 dlrlrnaikv gqantqgavp tstehykeil kqvqnheiwt qkeqrrkefe aknpnkkfgt
      541 gfaictkdyg agneapstyi emdrtgnlvl gvavveigtg aqtsqaavie pyfgrpadtv
      601 nlaevegwvp lqlietesaf tmsqsyqdkm qqnprwtpsv elassasnsa yfqskatena
      661 akivfeyglw paakaiwskl yysgseysdi dfgpmedavw vdgklsaqgm vplelsmlaq
      721 yahqhglvts amvhsfnrwa wvesdftieg ntqryeldav aikygsgasa dkqklmsseg
      781 whlldrsnvr ypatalnnam vvyyapcatv vdlavelgtg kveivrthtw ldagkvivke
      841 lvegqieggl vmgighalhe ylpsgnegpg dgswnlnryh vplapdvgvw nmehtlmppf
      901 nnsdqrkgia evvmipivpa itealyqitn trfyhlpvta qdikeala
//
LOCUS       WP_284648493             339 aa            linear   BCT 25-DEC-2024
DEFINITION  formylglycine-generating enzyme family protein [Photobacterium
            damselae].
ACCESSION   WP_284648493
VERSION     WP_284648493.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..339
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=38554
     Region          68..331
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 mkvnsillii isanlvacnd srntvsseii skqeiaridt ninklypdad sklkqhilnv
       61 aveslesmvf ikggtfmmgd fkapcsplni krmdwtpeas cntalsmtrt ganyqhkvtl
      121 snyslsdhet tyyetdafnr senkpvanqd srydkefpiq deqlknrpss tkswqeakdy
      181 clwlgkltny pidlpteaqw eyaarnrghn hyfatnngyv qeigsnyvdk dgaiqeytkd
      241 qgnygsfgdi krwppnplgl ydmagnshew vndwyskdyy kvspelnpqg pktgtekvtr
      301 gwgdsmpltt trshekpids myysrrgfrc avqsptsiy
//
LOCUS       WP_284648579             349 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Photobacterium damselae].
ACCESSION   WP_284648579
VERSION     WP_284648579.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 349)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..349
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37695
     Region          37..345
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mttitdalkv hqarnrnkkv alaaffvmsi vflitdilig sqgltlhqvl salfhptsss
       61 iasriivwdi rmpmslmapl vgaalalaga qmqttlhnpl adpytfgisa aasfgaslii
      121 tnviaipwip sqyqvafmaf imclgttfli agistikris iegvmlfgva vmfaydsllt
      181 mmqyiasetq lqtlvfwhmg sldrgswgki itlaivlpiv iflmmkdswk lstlkigner
      241 aetmginvrr lriktlvlvs vitalsvsfv gavgfvglva phiarmilge dqrfflpasc
      301 ligavllela siaskaimpg iilpltvvms fvgipffifl iikkggkfs
//
LOCUS       WP_284648654             724 aa            linear   BCT 25-DEC-2024
DEFINITION  GumC family protein [Photobacterium damselae].
ACCESSION   WP_284648654
VERSION     WP_284648654.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 724)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..724
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=80641
     Region          13..707
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 maislvengt klessvdlsq yfvelkkhwl kllsvtvvvt glsipfiysm tseyvstatv
       61 llkakednvs pienvetyds tqaeyyptqy dliqsrvvla eavkllklnd npdfngesdl
      121 ikkddglask lldfiglsse vnqdqfvpkl tddmklenai dvvqknltvs gvrltqlvkv
      181 syqspspqla keiangvvea ykiytinqkr nktvdaeqwn niqisylkne idkkkhamdv
      241 ylkdhgllty ngidgfeteq msivanrlad avqkramaqa dyelvkhiss tnlssvanls
      301 qisnhpqlqd lkialiqarr klselqkryg pkysqvieak aeitaiqqqt dvllqglkag
      361 iydnyqaavr neneykklls iqkndftnit akrdkyndlk adldktqely qelykrtqeq
      421 kisakyeead vvlydpavlp vkpikpnkpl fvimvmiltl visvvftivk aalnnkvltl
      481 sdverklgls kigevpllig vnsvsiskai yahdtaveml lgmknilqlk hkktkvlgit
      541 ssisgegstl iasmlasifa idkkvllldl nyrksglsdq llsthsdgfa ewvysdskga
      601 vpyivkqdng veflnrgnvk gsplqflmqs etqlsfqqla qhydmvivdl paisegqdal
      661 vvadfidsll vtvaanqadv seikenlerl aivnsniiga vlnkvsdenv vteevirfls
      721 dser
//
LOCUS       WP_284648656             318 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Photobacterium damselae].
ACCESSION   WP_284648656
VERSION     WP_284648656.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..318
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35435
     Region          5..306
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 miinnfqkln qhlrsqvigq pelveqllia lladghilve gppglaktra vkvlsdcieg
       61 qfhriqftpd llpadltgtd ifrpetgefs fqagpifnsl iladeinrap akvqaamlea
      121 maekqitagr ktyplpklfl vmatqnpieq egtyplpeaq ldrfllqlmv dypnadsele
      181 ilrlnrgeal gnkvaeavti sqeeifeark qvltiymaed veqyiirivm atrqpekysd
      241 tlaswlqmgv spratlaldr carahawlqg rdfvtpedvq tmaspvlrhr lllsyeaqae
      301 giasdrvieh lleqvasv
//
LOCUS       WP_284648758             249 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Photobacterium damselae].
ACCESSION   WP_284648758
VERSION     WP_284648758.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426811
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..249
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27013
     Region          28..242
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mikniivasv laiisnsvia kddtvnnvil vhgayadgsg wkpvfenlrk egynvyiaql
       61 petslkedva svnrlvdyin ddvilvghsy ggvviteagn npdvkglvyi savvpdanen
      121 ikdlrvkyka pandviklgd gfqilnpety hndfaadlpk dvaefmaysq vpvavpyalg
      181 akvskaawkd kpswylvakd drkinpdllr fmakragsnt ieasgshaif rsqpkvvsdl
      241 iitasenvq
//
LOCUS       WP_284648765             705 aa            linear   BCT 25-DEC-2024
DEFINITION  tRNA(Met) cytidine acetyltransferase TmcA [Photobacterium
            damselae].
ACCESSION   WP_284648765
VERSION     WP_284648765.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..705
                     /product="tRNA(Met) cytidine acetyltransferase TmcA"
                     /calculated_mol_wt=79419
     Region          9..694
                     /region_name="TmcA"
                     /note="tRNA(Met) C34 N-acetyltransferase TmcA
                     [Translation, ribosomal structure and biogenesis];
                     COG1444"
                     /db_xref="CDD:441053"
ORIGIN      
        1 mhiqfshylt qlipflqqtn srrlvviqgs yewaqpylkl ctsyyqeplw vgelssdlyq
       61 grhisykkak tvlgqetdcv ifdgnsdlsy eaigavvgti kggglailfl peeweeanla
      121 yqrllnyidi ntvlflsesr alfpklpevd dsivhtassv leygaitldq qkgieaiikv
      181 mtghrkrplv ltadrgrgks aalglaaaql lsqrkikivv tapslkaaqn ifyhaadrlg
      241 lechlgrels wqqsmlvyva pdellqqhvd cdllfvdeaa aiptsileri lnrysrivfs
      301 stihgyegtg rgfaikfkqi lankmpqfrs illhqpvrwa endplekwcf dalmlnaema
      361 dvtqlpshhs eiiyslvsid vlakdeerfr qfvgllinah yqtspndiql llthqdvlcf
      421 iasyqgriig ccivlkeggf dnilaeevrl gqrrikghll pqsiaahigl daaltqgcgr
      481 iqriaihpnc qqqglglkll etvtsqaktl dldylgtsfg assdltqfwi kanyqfirlg
      541 ltkdassgvh salavypltt ksetwlesaq tlfaanlmyq rvevfsqlep slllllwrsl
      601 kqenqvsfls ldlmnmqlsa flrggmgydl vvasleqlmm wylsqpsfls eqdesffcrk
      661 vfqkrswsel vidyelvgqk qaeqklrsiv qeiflkwste hanis
//
LOCUS       WP_284648772             256 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Photobacterium damselae].
ACCESSION   WP_284648772
VERSION     WP_284648772.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..256
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29501
     Region          <58..154
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 manlkhqyvn lvdlyqktaq gkyttaehyk dipihamkgl heyavsivtq yqnldqqtai
       61 dlgagagals qrladfgyqv tsldlvpdnf rlstqsfsfl pvdlnlpfcq ciqerydlvt
      121 aveiiehlen praffrecqa llqdngilll ttpnitsays vteslikdnf tyfddgqyln
      181 gghispishw qiikmaeenq leiihhstfg khhihfrewp rfwllyhinr llrpalkhrn
      241 gcinvylmkk kqeivk
//
LOCUS       WP_284648456             176 aa            linear   BCT 25-DEC-2024
DEFINITION  (2Fe-2S)-binding protein [Photobacterium damselae].
ACCESSION   WP_284648456
VERSION     WP_284648456.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..176
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=19384
     Region          1..161
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mitvnmtinn kvigpvdvde svkmidflhe ylgltgtkfg cgigvchact iivdeadgss
       61 htertcingv gnfngkklrt veghakrntl gqittlspvq qtfvdhfsfq cgwctsgfvn
      121 estvlieklq kspikredve svieetlkdh vcrcsgyrky yvglrdlvls qkglvr
//
LOCUS       WP_284648819             443 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Photobacterium damselae].
ACCESSION   WP_284648819
VERSION     WP_284648819.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..443
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=51158
     Region          91..431
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrrlyiesfi glivlfglsl ycyeviiyrw ntdydyvled yeaealhdlv dniyhnegsk
       61 aaylaiekya tktrqtltvh nkeelpddvk tfffttapqs ytyhdedril wfrltlssdf
      121 yslkpnfdtp lrraidfddn mvwvffiggf alysilfiwy lsrrvrllek ttlafahgef
      181 sarartesrf rvgtlnqsfn ymadkisnll isnkaltnai ahelrtpifr iqwqaellad
      241 sikdkaikqk iesivedtee mesmvnelly yakveqpdte lhcqnivlnq yladmlqiwe
      301 ktvhnkitlk mpfkqnieis ldtqlfkhvl nnlisnasry sendtlvtls qdhefifitv
      361 eddgpgisse hwpylfdpfy sadparnkaq sgfglglaia kqivarhkgq itvgdsallg
      421 gakftvvlpi acqckqmldi ipk
//
LOCUS       WP_284648880             318 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Photobacterium damselae].
ACCESSION   WP_284648880
VERSION     WP_284648880.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434433
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..318
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=35929
     Region          33..244
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          112..142
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          147..172
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          215..244
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
ORIGIN      
        1 mkkniiallf mfcipswaes lplpesmsve dayqlgdllv dqykikqgqp ylkyaadkgn
       61 aeaalaysrs fktnimvqsp keheyavkaa klgnedamlt lslsrnifgd reafrsalln
      121 klkekaaqgd adamrklsil yfgtskevdw kkkaaehgna taqhelaryy evgkgwffip
      181 gkrekevkrl ykasaeqgnl rgmegyasii ydegnkkeal diwtkmantg dafsiiflaa
      241 qylhslpgit ypekdevlgs ayskiyldsm gtdkennlye iykenyleam shlseaqkeq
      301 vndfakeflk thtvrvlr
//
LOCUS       WP_284648899             489 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Photobacterium
            damselae].
ACCESSION   WP_284648899
VERSION     WP_284648899.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..489
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=54880
     Region          12..480
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mtdfssswta vsvlvvddep gmrtilqkal skkfaqvdva gsveeaeeir krchfdlliv
       61 dinlpgrsgi dwheafdptt krsdvifmtg yadlemaika lragasdfil kpfnleqmmq
      121 svsrcierrl merqnfalqr dversypvei igdaastqrm kkmiaqvaps laavlveges
      181 gtgkelvara lhqlskrsgp fvplncgaia pdlleselfg hvsgaftgak kareglfrva
      241 nngtlfldei gemplsmqss llraleqkai rpvgaereis vdvrivaatn rnlkeeveag
      301 rfrrdlyyrl nvltielpal reriedipal ahhfthqlak dlgmqsiswt hedivamqay
      361 dwpgnirelr nlmercillg kppadywrel nddfpvshvv dsklnkatss dsvtnvsder
      421 pcrchengqe qycyptdwtl kevekahilq vvdsndgnks aaarqlgvar ktlerkfkew
      481 sdeveelkv
//
LOCUS       WP_284648965             410 aa            linear   BCT 25-DEC-2024
DEFINITION  NRAMP family divalent metal transporter [Photobacterium damselae].
ACCESSION   WP_284648965
VERSION     WP_284648965.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..410
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=43057
     Region          28..407
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 mttstttaip ssesqtaswq skaimsvafl mattsvgpgf ltqtavftnl ykidmafpvl
       61 isafitfgiv mniwrivgvs glriqdiank vapglgyvvg illalgavaf nfgnvsgsal
      121 ginvltgvdt twgalftggl gcllfvlhna skrmdqmary lglfmiilia yvamtslppm
      181 gqtliaavap sdmsnlllpt ltivggavgg yytgaqrlvd iglqgqnnvd nikkaawagi
      241 siavvirvll flaifgviat gavldkanpa adafrhgagd vgyfifglvl fvasitsvvg
      301 nsymaislik tlfpvvarne klwcigfiii tslgtvmmnm pilllmlagl vnsiilpivl
      361 gsvlaatrrk divgdykhpi lltaigaliv vvmafasytn ilnfmtkflg
//
LOCUS       WP_284648345             486 aa            linear   BCT 25-DEC-2024
DEFINITION  peptide MFS transporter [Photobacterium damselae].
ACCESSION   WP_284648345
VERSION     WP_284648345.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..486
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52828
     Region          2..443
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mrlasqpkgl fhliaiqmwe ffsyygmrsl lilfltqkll mtdhhayaly gaytslvyvt
       61 piiggyladr yfgnywsvvi gallmvagha vlsipsvgni smyialslii cgygffktns
      121 scllgelytk kheksresgf sisyvggnvg salapifcgy aamkwgwhvg falagigmli
      181 gliifstgrr nfthvkkcnk daltqksagv phwliiivll altafglvfv lkdllagyil
      241 avicavsfyq ivalyrrssp sdrsklnsil yfmifgtvfw afdqqggssi slfiernint
      301 difgfhipta ffqsvnpvav ivgggavawl wkvlasksis vrtltklnmg lllltagftl
      361 itissklamn tghttflwlf iglfligvae lfidpvalaa itrlnpqgat stlagiymlm
      421 ggsvanyiaa niaeftasnt pvnadatdli asaaqyhhvf qsilfvtvav lvlgllvdfk
      481 nrhkav
//
LOCUS       WP_284648926             220 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Photobacterium damselae].
ACCESSION   WP_284648926
VERSION     WP_284648926.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..220
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24047
     Region          1..202
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mqaicfdfdg tlvdsevfha anwslymash dvelsadvfm hkyagvtwpn iakiliekfq
       61 lniepqqivd dmealteeqi rakgipakeg aetllkqltg kvplavvtga priyvegila
      121 qkgwlewfdv iftgddvehn kpapdiyqla cqhfelptes viavedsttg atsalaaglk
      181 tifvntinlp isgqaarhfs dlieaqptic amlsldcdkk
//
LOCUS       WP_284648972             658 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Photobacterium damselae].
ACCESSION   WP_284648972
VERSION     WP_284648972.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 658)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 658)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 658)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..658
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=74851
     Region          106..642
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mnqeytlfnn lqcpvwifdi dnkkiiwane kslplweaks lseltnrdls fdmsaaveat
       61 lvdykatfar gktiktwwsf tphevlkkyl cifsgiplsd grigmlvevl anettlrrdl
      121 afsecsnlal lfnqsgqlvs tnaafshqfg ecvndlasfi gdiaqarqll enaqqnrivd
      181 qkllcwtgqr hlwfhiegkw leeqqqlllq ltnisperek lrqakynseh dfltglmnrr
      241 gissaikish htkqpysllf ldldgfkmin dtyghavgdr llravsirlr qviqhrglla
      301 rfggdeflih verrnittpc afakevital nkpfhikevg elsigctvgt tnypedaqdi
      361 dtlvtqadma mhraklrgrn cchhfspdma dalyrkmilr hhltlalnan afelyyqpiv
      421 dlkkaklkgf ealirwnddd lgqispaefi plaeetgqiv plgqwilkta crqlaewkkk
      481 ydhsfimsvn lsraqlqtgl vqsvkaclda yqidpkqlal eltestmlqd ysdakqclte
      541 laelgielyl ddfgtgyssl sqlqdlpist vkldrsfvqg ehkgsqaiie atqaicekld
      601 lkvvaegvet eqqldylrqc nfdycqgyyl ghpmppqtie erqfslchdl dinnptih
//
LOCUS       WP_284649032             257 aa            linear   BCT 25-DEC-2024
DEFINITION  nuclease-related domain-containing protein [Photobacterium
            damselae].
ACCESSION   WP_284649032
VERSION     WP_284649032.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Grynberg,M. and Godzik,A.
  TITLE     NERD: a DNA processing-related domain present in the anthrax
            virulence plasmid, pXO1
  JOURNAL   Trends Biochem Sci 29 (3), 106-110 (2004)
   PUBMED   15055202
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10551559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..257
                     /product="nuclease-related domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29539
     Region          33..144
                     /region_name="NERD"
                     /note="Nuclease-related domain; pfam08378"
                     /db_xref="CDD:462454"
     Region          <204..251
                     /region_name="YrdD"
                     /note="DNA topoisomerase I, ssDNA-binding Zn-finger and
                     Zn-ribbon domains [Replication, recombination and repair];
                     COG0551"
                     /db_xref="CDD:440317"
ORIGIN      
        1 mnifevfini leqvwyllpl llivsvfksr wlkgifgeyl vnrllsklpe sdytlikdvt
       61 lptsdgttqv dhivvskygi fvvetknmkg wifgsarqkl wtqkiyrhss kfqnplhqny
      121 khikaletll gcsadylhsv ivfigdstfk temppnvtya rgsiryiqqf nnvvfsdkdy
      181 arltdsinqi klkrgvitdl khrnhvkeiv askvssnqcp rcgsemvlre tkrgenigkq
      241 fwgcstfpkc ravkqln
//
LOCUS       WP_284649283             449 aa            linear   BCT 25-DEC-2024
DEFINITION  lipopolysaccharide biosynthesis protein [Photobacterium damselae].
ACCESSION   WP_284649283
VERSION     WP_284649283.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..449
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49693
     Region          1..386
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 msyasailiy sfgliiskli gllmqpfvts qlgienyarl dilivtssia siivtfglid
       61 gicrfahden yrqddclsta mglvfwgggv ftsiallngh viqqvlpgsp plwaiyltfi
      121 nlylnalaai pltklrmqhr pikfaiaqav faitqaigii vlipyfqvtg ifiaavvsql
      181 lqliilyrdl pslrlvyssi firygssiml sgvlgficlg aerwaiayyl glefltpyai
      241 amqwaiaasl llepfslwwf pkrfnllkne klladitilg cqicvlicai vtmfgplflh
      301 fwlsanfsqs anligliaim imlkgistll nigcyyqasg qriiqinlva tglsiinifm
      361 ilptfgllgi iwgsiviqai kvfafyywsq kelplpypls rlfialmlla gifassalil
      421 iqalllilli gliitpfflt risywsnta
//
LOCUS       WP_284649225             800 aa            linear   BCT 25-DEC-2024
DEFINITION  M9 family metallopeptidase [Photobacterium damselae].
ACCESSION   WP_284649225
VERSION     WP_284649225.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 800)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 800)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10280819
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..800
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..800
                     /product="M9 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=90330
     Region          25..202
                     /region_name="Peptidase_M9_N"
                     /note="Peptidase family M9 N-terminal; pfam08453"
                     /db_xref="CDD:430004"
     Region          267..548
                     /region_name="Peptidase_M9"
                     /note="Collagenase; pfam01752"
                     /db_xref="CDD:426409"
     Region          589..663
                     /region_name="PPC"
                     /note="Bacterial pre-peptidase C-terminal domain;
                     pfam04151"
                     /db_xref="CDD:427748"
ORIGIN      
        1 mthilkysai afflsssasv aatncdiaql ahvpdkasvi ehadnvcmqt wfhpdkasin
       61 svfseeqmvl ianalntkia ayqgdeasat eiyylseyvr aayyvnyyns tviapyshal
      121 nlrfttainr flqspyalta sqhnmnalgs ltslvdsvrv lpenlptlmt llptlnkdna
      181 enstyvealn nifralngss sdkgvqdyls hhlevldqlh qfiisndwal kthaavvvsn
      241 aarelsrllk iqdpaiknki ltiqedllar yplggendsi wvgiaemvgy yapdkqqqlg
      301 lsdaklrleq hilpmtfrce gpatvraqkm tqeqaievca alnqkeqdfh slitsasnpv
      361 nddlndhvev ivfdsnydyt vysnflfgnt tnnggqyleg npsdlhniar fvayrntsad
      421 gysvwnlehe yvhyldgryn qygdfnynlq hgfvvwwleg faeymhygns ytdaialgqe
      481 rtyslsevla ttyshdtnri yrwgylavrf lfdnapdqve qllqlsrqgh ytqwaalvqk
      541 lglqyneefa twlttlkapt tpttpshsnk svitltaetp velsgakyse qlfaitvpkh
      601 vteffvslsg gdygdaelya sfnqvahyyn yqitdarsgn nerirfatde qgfvkpgvyy
      661 fsvagrsaye hvvlntemkt aestqtayqa ddlspitlqa dthtnitvnk erymvyfvpk
      721 ghhnvrvwvt pkdqkqdnqg nvdlyfgkkt wpvleqydlv sqrsdsyeyl etkvdgghfv
      781 flmlnaknph ntmdvyvtsn
//
LOCUS       WP_284648827             519 aa            linear   BCT 25-DEC-2024
DEFINITION  GspE/PulE family protein [Photobacterium damselae].
ACCESSION   WP_284648827
VERSION     WP_284648827.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..519
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=57621
     Region          29..494
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mnhtvlrdpt itrlclddgh tcvteqgeil canphsakld diieavqsls fmagqspiit
       61 svsqdyietl levlthsths pqdkekesll glhlvalcqa avdkgasdih ievyrkttry
      121 lirvdgkrei larfadgqsa lhqdrskgid lssyvfstlg nqdvnerepa ndsfdvnltw
      181 dkkpktfefr aalmpldrgi kltlrcltpr dkplelsdmd lpssytdqli ravnqrggai
      241 vitgpmgsgk ssliyalldt vdstarcihs ledpvefeqa gicktavepn tetklgsgiy
      301 kdyayyakeq lrhdidvapf gelrdhaaak efcrkaetgg laittlhtns vlgipqtfie
      361 qmgispaiva apdlmrlfvh qklvrklcph calsyqeaie spqtkakaql lstllpdhyq
      421 hcrvkspqgc sacggkgekg rlvvmelvvl ddsdrqyifa qdylawkqsl ksrgwpdird
      481 htlsrikrgq vdiesaseqi ndlmpikade vyknmmeel
//
LOCUS       WP_284649288             372 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal-phosphate-dependent aminotransferase family protein
            [Photobacterium damselae].
ACCESSION   WP_284649288
VERSION     WP_284649288.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Koper,K., Han,S.W., Kothadia,R., Salamon,H., Yoshikuni,Y. and
            Maeda,H.A.
  TITLE     Multisubstrate specificity shaped the complex evolution of the
            aminotransferase family across the tree of life
  JOURNAL   Proc Natl Acad Sci U S A 121 (26), e2405524121 (2024)
   PUBMED   38885378
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Koper,K., Han,S.W., Pastor,D.C., Yoshikuni,Y. and Maeda,H.A.
  TITLE     Evolutionary origin and functional diversification of
            aminotransferases
  JOURNAL   J Biol Chem 298 (8), 102122 (2022)
   PUBMED   35697072
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..372
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40511
     Region          11..372
                     /region_name="PucG"
                     /note="Archaeal aspartate aminotransferase or a related
                     aminotransferase, includes purine catabolism protein PucG
                     [Amino acid transport and metabolism, Nucleotide transport
                     and metabolism]; COG0075"
                     /db_xref="CDD:439845"
ORIGIN      
        1 maitsfqppr rvlmgpgpsd iypqvlqals rptighldpl fitmmdelka llqyafqtqn
       61 pftiavsapg sagmeacfvn lvepgdkvvv crngvfgqrm venvercggv avtvdntwge
      121 pvspelleqt lnqhpdakiv afvhaetstg alsdaktlae iarrfdclti vdavtslggv
      181 pllvdewqld avysgsqkcl scvpglaplt fsakalekia srqhkvqswf ldqslvlgyw
      241 nggakrsyhh tapvnslyal heallllqqe glehawqrhq emhqelkagl melgiefvvd
      301 eayrlpqlna vyipqgvdda vvrktllery nleigaglgd lagkawrigl mgygaraenv
      361 alcvkalaqt lr
//
LOCUS       WP_284649313             421 aa            linear   BCT 25-DEC-2024
DEFINITION  cytochrome b [Photobacterium damselae].
ACCESSION   WP_284649313
VERSION     WP_284649313.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Tolkatchev,D., Yu,L. and Yu,C.A.
  TITLE     Potential induced redox reactions in mitochondrial and bacterial
            cytochrome b-c1 complexes
  JOURNAL   J Biol Chem 271 (21), 12356-12363 (1996)
   PUBMED   8647838
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Howell,N.
  TITLE     Evolutionary conservation of protein regions in the protonmotive
            cytochrome b and their possible roles in redox catalysis
  JOURNAL   J Mol Evol 29 (2), 157-169 (1989)
   PUBMED   2509716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..421
                     /product="cytochrome b"
                     /GO_function="GO:0008121 - ubiquinol-cytochrome-c
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=48049
     Region          1..415
                     /region_name="QcrB/PetB"
                     /note="Cytochrome b subunit of the bc complex [Energy
                     production and conversion]; COG1290"
                     /db_xref="CDD:440901"
ORIGIN      
        1 msgfstwlek rlpvmnaykk hlseypmpkn fnfwylfgsl amlvlvnqli tgiwltmnyv
       61 psgegafasv eyimrdvdyg wllrymhstg asaffvviyl hmyrgliygs yqqprellwl
      121 fgmliflvlm aeafmgyllp wgqmsywgaq viislfgaip vigddltlwi rgdyvisgat
      181 lnrffalhvi alpivllllv vlhvlalhev gsnnpdgiet klpkgskgeg yspqfkfhky
      241 ytkkydiids ipfhpygtvk dligvavfaf lfsyviffnp emggyflepp nfeaanplkt
      301 pehiapvwyf tpfyailrav pdkllgvvam glsiimlfll pwldrckvrs fryrsklhla
      361 niaqftvsfv algilgalpa tptytllaqi fsfayfmffv llffysknea tkplpervny
      421 k
//
LOCUS       WP_284649442             283 aa            linear   BCT 25-DEC-2024
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Photobacterium
            damselae].
ACCESSION   WP_284649442
VERSION     WP_284649442.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..283
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=31027
     Region          181..276
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mfvfpstpel ivwlllavsi vtaissskpw wslplgmtli salwvgvltp igafvviigl
       61 aiayitqkfs rgywhiaghi fvlgwaialt ihalpgfhnl lvldkvitsp dsvpftlyfn
      121 ldkpmivfgl llllpnmvgd kpivwqltak qwlgigvglv vlplvamgvg ivkpdftips
      181 wigwfifnnl lftcvaeevl frgyvqtqla rklpivwaii fasllfgiah iaggvmlvii
      241 aalagglygl syywskkltl aiavhfgfnl ihllfftypl lka
//
LOCUS       WP_284649330             541 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Photobacterium damselae].
ACCESSION   WP_284649330
VERSION     WP_284649330.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 541)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 541)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 541)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..541
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=60210
     Region          25..541
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mkekflfwqt sswslslllv lpilaiffta lgqsdqvfsh llntvmptyl antfwvvvgt
       61 vvlallfgvp sawimamckv psektlqwal vlplampgyi vgyiytdwfd yagpiqiflr
      121 dlfgwqtaae ywfpnfrsig gacfvlalvl ypyiyllvra afmeqsvsll qsarllrcnp
      181 wqsfcrvslp lvrpaiavgv slvametlgd fgtvsyfavn tlttavydtw lgysnlhaaa
      241 kisalmlvvi filisaerfs rrkqklfqqq lngsdsvryt ltgwkkwlav iwcwglvtva
      301 filpmlqlad yawiyfgqsw teafrqysin sfvvsivaav ialfiallvn fshrllpskf
      361 ntvpirlasm gyavpgtvla igvmipltga dhfindvaks lewgrpglil sgsmfamifa
      421 fvvrfsavai gsiesslakv spsldmaskt mgvasfkmlr rvhfplvrrg cliavilvfi
      481 esmkelnaal llspfnfetl atyvfnyasd ehlelaalpa illilvglvp lilvnrsleq
      541 k
//
LOCUS       WP_284649572             821 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Photobacterium damselae].
ACCESSION   WP_284649572
VERSION     WP_284649572.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 821)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 821)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 821)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18109159
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..821
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=91353
     Region          132..373
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
     Region          575..819
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mlspvikalw ghykrhpfqi mlvwlgltlg iallvgvmgv nqqaresyrq gellfsnpyp
       61 yrirtaqlgl kvpqgfyiql rraglkscap ldsyrivteq grdfelvgld pvamfsaftr
      121 seknmatlra dmldlmkppy piiageqlas ymgvksgdmi tldsgkkigp veivpdeltg
      181 gprlvadiar lrdiqpssgf tsivcgemsh eqlvrltqil ppgltlqrnq sarlesltna
      241 fhlnlfamgm lsfvvglfif yqamslsftq rqplvgrltq lgvtglqlaa alsielilwi
      301 ilgliggnll glvlaqqlmp svaatlsdly ganvnlavsw hwqwgvasli iagcgsilac
      361 gwpmvrlikt ppvrlvthma lvrfsgrefa wqsiislifi lvaigiyqlp hgqfagfvli
      421 aliltasgll mpyllwksfq ilgvifpsvk mrwfftdaas slsyrgvaam afmlalasni
      481 gmetmvgsfr htthtwleqr laadiyirps mnmaprmyrw ledqpevndv wwrwqketpt
      541 dagtlqvmsi gqsegemtal svkdiepnyw qslhsqravm vseslalknn whigdmvdlp
      601 tpmndnwriv giyydygnpy gqllisynkw hrywphsgqv glaihlnpga ndeallaklg
      661 erfrlqperi rnnsdlmtqa mrvfdqtfvv tstlgsltlf iavcglffat lagevsrqrq
      721 fallrcmgmt glelavlggg qllliglfta lmalplglil aqllidvvlk ysfgwtmpih
      781 yfptqylftl gsalvvllia ggwpvwrlvk rsailslrea f
//
LOCUS       WP_284649600             387 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Photobacterium damselae].
ACCESSION   WP_284649600
VERSION     WP_284649600.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..387
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=44629
     Region          11..384
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 msltdrqlnl iskqdtydgk aeisdgeglv vritpqakiy fhyrcrfnkk slririgkyp
       61 vtslkearrm hklmmelres grnpniaitg elefitlddc vaywlkhyvp qlkegtqaly
      121 rsfannylig afpernveti parewmqwld aisldkpkta nslftklrsc lnfckskfii
      181 ektdldrikr qhvgkapevg trvptfsels miwlaiersr asssnkalhq ltmlwgnrls
      241 elrlarrshf dmeagiwtvp kelsktntpi rrpiptkara ilervmatyd dvlfpggdld
      301 kpitisaanr yirrirdglp iedwrthdfr rslstgasel gvmphvvekm lghelggvls
      361 vynkhdwlke qlegyelyae kldsylk
//
LOCUS       WP_284649685             642 aa            linear   BCT 25-DEC-2024
DEFINITION  McrB family protein [Photobacterium damselae].
ACCESSION   WP_284649685
VERSION     WP_284649685.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..642
                     /product="McrB family protein"
                     /calculated_mol_wt=73819
     Region          137..587
                     /region_name="McrB"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrBC, GTP-binding regulatory subunit McrB [Defense
                     mechanisms]; COG1401"
                     /db_xref="CDD:441011"
ORIGIN      
        1 maiycgnnns tylienanef kekcliqgks lftehsvwns stnqelidyf venldegdgd
       61 ffekletqla daspeakvlv semlwlmflc psntgpkskr nsiervfsws gyevntksrq
      121 rflsdkaltg igsagtaynt lrwrelvyvi rlveallkls dlerkellkd verlpqwles
      181 ipengtrqfr hmflyllfpd aherifgntd rksilttlad isstqynrmh tkdadaklla
      241 lrqlfeaeyg tqeldyyvep lrskwkepks lstnevndtv peysvksndk pqplntilyg
      301 ppgtgktyns inkaleivdp efyhqhnddr vaikkrfdel lnsnrigfvt fhqsfsyedf
      361 veglkatten nqvnyeiedg ifkrlcesar akstvkeeqd haegivskrm spsnqassdk
      421 rvliideinr gnisnifgel itliepskra gakealsvkl pyskemfsvp dnlhiigtmn
      481 tadkslaqid ialrrrfqfe emmtnyella eiplidgidi eqmvrvinkr iellydreht
      541 ighsfflslk dnpsiehlae ifelqilpll eeyffenwer vamvlgdhlk tdeglrfvve
      601 qfdaneiaql mgddwdqegi qpyvrndhaf kaaaayigiy nv
//
LOCUS       WP_284648830             163 aa            linear   BCT 25-DEC-2024
DEFINITION  type II secretion system protein [Photobacterium damselae].
ACCESSION   WP_284648830
VERSION     WP_284648830.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..163
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=18039
     Region          1..>47
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mkknqqgftl telvltfvvv gvilattvpl llsklsmqqq qneidqaisl tlerlqdqvs
       61 krieecsish ivtvnelglp tqtlhtlprl hvsigtngki isnvslsfel aseafaqqiq
      121 hgttlthvwi trhgkqlsit qpvsyldsql krmnydattg cfk
//
LOCUS       WP_284649721             724 aa            linear   BCT 25-DEC-2024
DEFINITION  GumC family protein [Photobacterium damselae].
ACCESSION   WP_284649721
VERSION     WP_284649721.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 724)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..724
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=80615
     Region          13..707
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 maislvengt klessvdlsq yfvelkkhwl kllsvtvvvt glsipfiysm tseyvstatv
       61 llkakednvs pienvetyds tqaeyyptqy dliqsrvvla eavkllklnd npdfngesdl
      121 ikkddglgsk lldfiglsse vnqdqfvpkl tddmklenai dvvqknltvs gvrltqlvkv
      181 syqspspqla keiangvvea ykiytinqkr nktvdaeqwn niqisylkne idkkkhamdv
      241 ylkdhgllty ngidgfeteq msivanrlad avqkramaqa dyelvkhiss tnlssvanls
      301 qisnhpqlqd lkialiqarr klselqkryg pkysqvieak aeitaiqqqt dvllqglkag
      361 iydnyqaavr neneykklls iqkndftnit akrdkyndlk adldktqely qelykrtqeq
      421 kisakyeead vvlydpavlp vkpikpnkpl fvimvmiltl visvvftivk aalnnkvltl
      481 sdverklgls kigevpllig vnsvsiskai yahdtaveml lgmkntlqlk hkktkvlgit
      541 ssisgegstl iasmlasifa idkkvllldl nyrksglsdq llsthsdgfa ewvysdskga
      601 vpyivkqdng veflnrgnvk gsplqflmqs etqlsfqqla qhydmvivdl paisegqdal
      661 vvadfidsll vtvaanqadv seikenlerl aivnsniiga vlnkvsdenv vteevirfls
      721 dser
//
LOCUS       WP_284649738             418 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Photobacterium damselae].
ACCESSION   WP_284649738
VERSION     WP_284649738.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 418)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 418)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..418
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=47394
     Region          123..416
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mkiksakqlt ftyfsivafa iiaihfsife stiedlemfn aqnrldmale svqqnlpqde
       61 lehnnpytsf yfgkanipsd ihlpenlpfn kavevykpsq deleteyfvm rskvtyqgke
      121 qevyifnidp iferseeqmm dsqsyqmllt lglllvslfa vlrisvrlts plsslskqlq
      181 nrahndftpi qlpssgqtre lvqlveslnd yqqqitdlle rerafnrfas helrtplmvi
      241 kggltllghs qqpefverqr nrmlpavdem qeyvqtllsl trdeqltetp wqiredlihs
      301 lvssyqqlld gktvkidvva ngeptvnapl pavkillgnl iknaftyteq grititlsas
      361 nvvisdtgvg idpdaengqk gyglgllivk dicrkynwsv elsnnrangc datvdfin
//
LOCUS       WP_284649751             430 aa            linear   BCT 25-DEC-2024
DEFINITION  lipopolysaccharide biosynthesis protein [Photobacterium damselae].
ACCESSION   WP_284649751
VERSION     WP_284649751.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..430
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49324
     Region          15..414
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 meqqstcape pvdsltklqk afitgiwatl asisvsflfk vwlaqwvaks dlalfnsvvd
       61 iislslilmt gfrssmvvsf sqtnndrdii nifrfslivm vlitwgivip yikhelhinv
      121 syfemvgvii gmgmkvyftn liamyrlyhi snkvtwiepi snvliflvcy yglhftalas
      181 lfysmmlssl ivahymywqr rkeiatkpis nvqlnsdmin ymkksftasl eagasilmiy
      241 iavlltithf sidelgdfqv vvrpiftymt mlfvfpiyrf vlpelsvcvr qgkhdeikai
      301 rrwvfklafi vsavffalml fwgneivmfi fppqykgavl vlfhfsmffv fmmlnayqla
      361 yikahgkftl slmirisgiv tlvaayyils eftanvvsii valclgyvmm filstieekk
      421 ilrgyqqqdi
//
LOCUS       WP_284649767             106 aa            linear   BCT 25-DEC-2024
DEFINITION  putative quinol monooxygenase [Photobacterium damselae].
ACCESSION   WP_284649767
VERSION     WP_284649767.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..106
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12309
     Region          5..99
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 msnnlifyve fdvkpecvek flqgatqvle amskestfvs tqfhrhtenp nkfslyevwn
       61 epsmdefvkn qlqgksyrde yesylpella tprkfsvles igswak
//
LOCUS       WP_284649793             348 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Photobacterium damselae].
ACCESSION   WP_284649793
VERSION     WP_284649793.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..348
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36578
     Region          34..344
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mkllsrikpv eirgdlrlsi kltaavmtll aisslllgry aisfhdlvaa lqtalghpdl
       61 esnhyevika vvfharlprv italmvgagl aiagsafqav frnplvspgl lgvlngcafg
      121 aalglvlqag lygvpllacl fgclavaigv liakriggds illlilggii snalfaglls
      181 lvkymadpen qlpgiiywll gslssvslpl levtlpimvi amalllvlgr vldamslgdd
      241 ealslgipvs tmrygvifla tiisaitvci agvvgwvgll iphltrliwg ashrfvlpls
      301 allgaiflli addlarmlts seiplgvvte llgavifffl ltrtwqar
//
LOCUS       WP_284649809              65 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Photobacterium damselae].
ACCESSION   WP_284649809
VERSION     WP_284649809.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 65)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 65)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..65
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=7043
     Region          <11..62
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mkrfgvegtf ellsgliqha kehtswqali ggvasdnqas ahllvklgfv lqakeqdvmf
       61 fklvc
//
LOCUS       WP_284649839             256 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Photobacterium damselae].
ACCESSION   WP_284649839
VERSION     WP_284649839.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..256
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29305
     Region          55..154
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 manlkqqdvs lvalyqktaq gkyttadyyk dipihamkgl heyvvslaiq yqhsshlqai
       61 dlgagagals lrlidqsyqv tavdlvtdnf rlspkqaali qvnlnsqfsy ciqrtfdlvs
      121 aveiiehlen praffrecqa llqdngilll ttpnitsafs vteslikdnf tyfddgqyln
      181 gghispishw qvikmaeenq leiihhstfg khhihfrewp rfwllyhinr ilrpnlkhrn
      241 gcinvylmkk kqeivn
//
LOCUS       WP_284649916            1087 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Photobacterium damselae].
ACCESSION   WP_284649916
VERSION     WP_284649916.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..1087
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=110785
     Region          <61..942
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mnthlkpisk wvaaglitvg agtlssqala ataagtdikn latvtyedss gnsyqatsne
       61 avvtvaqiys atieqdintt gspgqtvylp hvltntgngs dtytltfaqn lpgtdtrgad
      121 tidattiklf ndennngqpd ageaeftsgd tvtlnageqm nlivaaavpt tavpgdtlgv
      181 tleaeanngt gsavdgsvtd igdnndsadd tnaslitvtn davinmtksa thlenigtes
      241 slgidldgdg atdralslir ytvtvsntgn tdakdvvifd gipdgtvfvt gstgaaydat
      301 ssglltvngd tpiayaanlv deashgvdld qdstndtaes qidggldlng ngvttdttvp
      361 gvyavddqla snttvsmtfy vayspetmqg dteignvays csdlngdgdy vdagecndpd
      421 pttagpdpsn pttttttttt gvgiidtgte tgtsgggdsd gtdnntqtvd saaagsdvff
      481 ynkiinngnt vdsfdlttvn tsfpagttfe ywnadgsaql vdtngnvtpd tgpvnpstct
      541 daattidgit vncnetlfrv vaklpsdaad sttpfdavtt atsyndatqs dtkterldni
      601 tgptvdiant pitaidpavd vdpvdtgdgf tsadvatvfn deplgstvta piyianeggs
      661 sdsfllgaeg syngasweta lpagwtvvfk hngidtnadg tvdiaatgav itstptipag
      721 avlwvtaeit ipsdptqala dsdqasaida ntdgdldyii sltvqstasg aidrkveafd
      781 vatsasidit ptslsnqiep ggsvtyehtl gntgnttetv dlssgnnttg fnntisidtd
      841 gdgtpdtevg nlcdapvtsp itvqqadgst advevtcdat dgsdtvpslt lepgetipme
      901 vtvfaptdat sgtnnittit avsttdptvt aegqdnsevi tgqvrlykya dldtdcdgaa
      961 dtdknylkqh tttvepgqci vwkliavneg tsdalntvit dqlteftqfe sggslvscrn
     1021 ttdagtvval adatyplqsd dlgplclpdg ttgadvtgav sgntvtftvg tlvpgdkavg
     1081 hfvvkvd
//
LOCUS       WP_284649929             315 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Photobacterium damselae].
ACCESSION   WP_284649929
VERSION     WP_284649929.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..315
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33958
     Region          7..311
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mmimvfslml gqyplslsql yhgflhpffn ddlanhilws irlprivial cvggclafsg
       61 ailqgvfhnp lvdphiigvs sgaafggtla illgfptalm mgstfvfgll alviiyvlan
      121 llgkndrlml illgivlsgi faalvnlvqy ladteeklps ivfwllgsfa tanwhkvill
      181 lvplllaggv lyqlrwrini lslgdsdars lgvsvtrlrq wvlllcavli aaqvavsgsi
      241 gwiglvvphl artivgadhr rllpmsfwig agimvivddi artisqaeip lgiitallga
      301 plfifllake krgqq
//
LOCUS       WP_284649935             465 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Photobacterium damselae].
ACCESSION   WP_284649935
VERSION     WP_284649935.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..465
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49384
     Region          6..465
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mtmhnstdnq fdvdssidel giglippshq tkkpselffv wcaanigilg vvygaiivsf
       61 glsffqsvla aivgvasfsl vgissiagki grtttltlsr ssfgkkgnia ptafcwlnlm
      121 gweavniitg tltlvalfva vgfeentflt tfslilfggl tvavsilgqd tvltmqkwit
      181 rtfgamtfiv avylmftanw htilalpsgd wltgflpavs iiaagtgisw aiagadysrd
      241 qsphssqgsi fqsvvggaal plimlmltgi lltsqipdla snenpisaig kllpnwmaip
      301 ylaaavagii tiavlslysa slnllsmgvk lkqrtaitld aiivltiavy vlfisgdflg
      361 pfisflvfcg iflaswaaif vtdfyhshvk qgyteqelyg dtgvnkptla cwligslsgl
      421 mvsktgfidg pfaigvfads slglfisfav amilyrivli skkvr
//
LOCUS       WP_284649954             324 aa            linear   BCT 25-DEC-2024
DEFINITION  HlyD family secretion protein [Photobacterium damselae].
ACCESSION   WP_284649954
VERSION     WP_284649954.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446287
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..324
                     /product="HlyD family secretion protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35891
     Region          20..324
                     /region_name="EmrA"
                     /note="Multidrug resistance efflux pump EmrA [Defense
                     mechanisms]; COG1566"
                     /db_xref="CDD:441174"
ORIGIN      
        1 mskvktlavv vpvaalvswl gytfwqayqp vpermqgqie aqqynisski pgridkvlvh
       61 kgdevkpgql iftlltpeid akliqakagk saagalaeea ekgarrqqva aaqdqwrkas
      121 aaadlmekty rridnlykdg vvaqqkrdev ytqwqaakyt esaayqmyqm akegarvetk
      181 kaaqekvkma egavaevqay addakatswh ngevsqillh dgelapqgfp vvtimdmsda
      241 wavfnvredk lkdyqkgael tvkipalgeq eyrfkvthia vmgdfatwra tdtakgfdmr
      301 tfevearpme pidglragms vive
//
LOCUS       WP_284650041             175 aa            linear   BCT 25-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Photobacterium damselae].
ACCESSION   WP_284650041
VERSION     WP_284650041.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..175
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18987
     Region          1..163
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mkilafgatn srnsinqqfa ryaaslvpna evevldlndy elpifsfere eqlgqpelaq
       61 kfykklgead aiiisfaehn gsyavayknt fdwvsrinqk vfqekpmlll atspgpggaa
      121 svlgsavgsa pyfagdvras vslpsfydnf dvatgkvina eidtklkeav eelvk
//
LOCUS       WP_284650154             445 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Photobacterium damselae].
ACCESSION   WP_284650154
VERSION     WP_284650154.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..445
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=51388
     Region          91..430
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrrlyiesfi glivlfglsl ycyeviiyrw ntdydyvled yeaealhdlv dniyhnegsk
       61 aaylaiekya tktrqtltvh nkdelpddvk tfffttapqs ytyhdddril wfrltlssdf
      121 yslkpnfdtp lrraidfddn mvwvffmggf alysilfiwy lsrrvrllek ttlafahgef
      181 aarartesrf rvgtlnqsfn ymadkisnll isnkaltnai ahelrtpifr iqwqaellad
      241 svkdkeiqqk iesivedtee mesmvnelly yakveqpdte lhcqdivfnq ylndmlqnwe
      301 ktaqskitlk tpfkqnivss idtqlfkhvl nnlvsnasry srkhilvtls qerdsvfitv
      361 eddgpgipne hwpylfdpfy sadparnkaq sgfglglaia kqivarhkgq itigdsallg
      421 gakftvilpi tcqcdpildr pnisk
//
LOCUS       WP_284650171             373 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Photobacterium damselae].
ACCESSION   WP_284650171
VERSION     WP_284650171.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..373
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=42658
     Region          5..350
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 makvtlttaw iqklktpskl ikyrdlkcdg lylfarptgn hsfvlvfqnq nknyqislgn
       61 iqtlslakar elayqerakr dpklnlhaqp qkpilfdefg qsflthqarl wkprtitwyd
      121 clfqrnllpa fqgltldkit takvkvwygt qshhgalall snimkkaeaq gyipagsnpc
      181 kglrqprqrl tgyaltsqel aqlwraldng tihhptltrl irllvltgcr cgelrnvkqc
      241 dyrmgklylp dsktgtktiy lssfarywlq eqqqestney ifsdelggik rgrltqawkt
      301 lrqsiglphi rmhdlrhtya tralengehl lnvskllghe lpettlryah lasapmyhas
      361 ecvsqtiare mra
//
LOCUS       WP_284650471             235 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Ligilactobacillus
            salivarius].
ACCESSION   WP_284650471
VERSION     WP_284650471.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus salivarius
  ORGANISM  Ligilactobacillus salivarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Ligilactobacillus salivarius"
                     /db_xref="taxon:1624"
     Protein         1..235
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27675
     Region          1..70
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(5,9,46)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(8,45)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(15..16,39,42,46..47)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mnrikelrtk kqltlkefss nfnkftkdnr dniksisyat vsrwekgine pklemwqala
       61 kyfnvpvsyl qglgmsesef keklfntivh npkfakniag yfsgvnqdiv lnasneiten
      121 nyqelkdsfv lsfditpfkd kynffssidy sisddefqnm ildklnndni svfdfsymfp
      181 elykrlidif dkmtlddeyf ilkkvgknil fdelkkhyqe rvekeskens isdes
//
LOCUS       WP_284650758             484 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Ligilactobacillus
            salivarius].
ACCESSION   WP_284650758
VERSION     WP_284650758.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus salivarius
  ORGANISM  Ligilactobacillus salivarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Ligilactobacillus salivarius"
                     /db_xref="taxon:1624"
     Protein         1..484
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=56434
     Region          10..439
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
     Region          412..449
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275375"
ORIGIN      
        1 meekvlesrr iriyptkdqq ayltfnmfan ikmwnallae vykpvselde vqalprnkqs
       61 kevykrierm sweeqrdlfk glrglstkai ydadetvfes gwtlkdadts mysytlrtlk
      121 tamsnhlknp rhfgiprfkt tmdvenqgsy tsgahvceis edgkylrvgk lkrfklglie
      181 manhypsdgr lykvtikhes sdtwyvsfvf eqaehtvkrp rtglaagidl nvtgnshivl
      241 qdgtryqlpy dkirkleqki ekenvkrsrk yeqwkkevai ieednkkali pkhvptlaer
      301 snyqknkkki aklhlriknl kkdyikktcs klaneydviv medlavsdme knkyrarait
      361 rsnfreirdt ltymmdwadk kivfidrwsp tskrchtcgy ikhnlklkdr nwtcpvcnsh
      421 hdqdinaakn ildegldlld kmndsckkcg hertvittde kwtcakcgak nkttpkkees
      481 sdva
//
LOCUS       WP_284650796             392 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Flavobacterium terrisoli].
ACCESSION   WP_284650796
VERSION     WP_284650796.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..392
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43397
     Region          3..387
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mklpkslqak leqrqannal rqlpvakdwv dfasndyigf ahseiifsqt hqylldhnik
       61 sngatgsrli sgnhdlysvt eafiaqfhqs esalifnsgy danvgffsav pqrndvilyd
      121 elchasirdg iqmsnaksyk fqhndleele klitkftihh shsseceqak qftiyivtes
      181 vfsmdgdspn leelvalaek qnaylvidea halgvfgeqg egvvqnaglq nkvfarimtf
      241 gkglgchgaa ilgsaelksy lvnfarsfiy ttglsphsva tillayqhla aekealqalk
      301 nnilffnqek lrlglkpmfv ysksaiqcai ipgnatvkni aaqlqdkgfd vkpilsptvp
      361 egqerlrfcl hsynseaeis nvlellstfv fk
//
LOCUS       WP_284650945             637 aa            linear   BCT 25-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Flavobacterium
            terrisoli].
ACCESSION   WP_284650945
VERSION     WP_284650945.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     BTLCP proteins: a novel family of bacterial transglutaminase-like
            cysteine proteinases
  JOURNAL   Trends Biochem Sci 29 (8), 392-395 (2004)
   PUBMED   15288868
REFERENCE   2  (residues 1 to 637)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..637
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=74264
     Region          <277..393
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mktiqlllvf lcffvnvava qkgidptped itkakqlrek ytkddiaile ssdfisfdln
       61 kkdgkvivkh takqnlmnin hradihkyef ydsessiqaf gmkyrndkpa mfrvtdefyk
      121 dkdlfyndak vkyisvdfpt qgynykyeme kkyedvkyft slyfndeypv lkkkisfdip
      181 nwlevelref nfegnkitkt stqegnvthi tytfddvpai ykeeetpgrs yiyphilvla
      241 ksftkdgakt plfgdyndly kwyhslvlmm kddtsvlkdk vteltanakt deekikniyy
      301 wvqdniryia fedgiagfkp desnnvftkr ygdckgmanl ikqmlkvagf darltwigtk
      361 hiaydyktps lavdnhmict lfhkgkkiyl dgtekfnslg dyaeriqnke vmiedgdkci
      421 iekvpggtad ankeifkatl nienetmvgs cnksfwgesk tqflniynsf etnkkkerld
      481 gflsrqnksi lvkdlktsdf kdrdipltld yniavsnkis sfddeiyvdl dfmneyksfe
      541 lkdrkvdyem dyktnfnsli tlkipegykv tkmpsnlvvk eanfdinisf entgkeivyk
      601 ktflfkngci kanemekwnd fnkklvenyn qqitlsk
//
LOCUS       WP_284651064             145 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Flavobacterium terrisoli].
ACCESSION   WP_284651064
VERSION     WP_284651064.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..145
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16789
     Region          3..128
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mgtftkeisi rwsdldpnyh vrhsayydfg aqhrieileq lgltlkvmqe qhfgpvlfre
       61 ecvfrreirl nsrvfintki gkikadasrw tivhelknen delfatlsvd gawidtqlrk
      121 ianptpqvav dvmnsfpktn dfiql
//
LOCUS       WP_284651194             470 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Flavobacterium terrisoli].
ACCESSION   WP_284651194
VERSION     WP_284651194.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..470
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=53455
     Region          167..470
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 miililiasi lmasisiiqf kneakdyhqe rldrkefaik ehinyvlstt typltpenlp
       61 lifkdkihel sdihnleini yslqgklvks skssfsvdkv appipnyilk lvqssvdkry
      121 vdiksidgvk nrssysqikd dkfkplgiln ipyveddgfy etelrefllr lsqvysfmlv
      181 iafalayfls syitkslkti sdkinetsln qknekiviea nskeinslin aynqmvdkle
      241 esasmlaqse reqawremak qvaheiknpl tpmrltvqsf qrkfdpndpe lkqklndysk
      301 tliqqidtms svasafsnfa smpaqqnetl nvvevvefsl difnedfvrf esssdeiitv
      361 mdrtqlirii tnlvknaiqa ipdeqeekdi lvsvnemedk viisvkdngi gidaentehi
      421 fepkfttkts gmglglgiik niienykgti tfetepekgs tfivslpivk
//
LOCUS       WP_284651128            1372 aa            linear   BCT 25-DEC-2024
DEFINITION  NACHT domain-containing protein [Flavobacterium terrisoli].
ACCESSION   WP_284651128
VERSION     WP_284651128.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1372)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 1372)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1372
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..1372
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=161723
     Region          222..>568
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mtsqgkgksf eilteeffls lfeqlkiqvn nnwiqkagyq ygfdvgfeva ilkddifkrg
       61 ifiecknyek sileqsqlht kllqfdrsdy ekrnsififl spkidlskct qdsnpkqled
      121 yfnrksdfkt liltpnnnik dilslekeif tkvygddlfi epdeesknki feyfnillfs
      181 kgeipnfsev sqreiylkea sivdndvlyi kralkrnkfs ffqddkslle likdeniill
      241 lgepgsgktt elinlskyfe knisdlgvtp ifinlsnkdr fedisdlmpv dwkannrivi
      301 lldgfdefef ksvlseqikr llenkeisfk iviscrtyay neelsqlepa kfyldgftta
      361 qsmkllngkf glpvevydki ekdkfkdile dpfmlnllgi yytshniipd svfeiyenik
      421 ggmpadeiem ykifalilel tkntsiekae lrslfglgyn klinlkfiqk sfdkrsfkfi
      481 hknyqeyfaa lalselsydr iidfivikgt nkthqslfnt itflinivei dkynllvewl
      541 kandrellfk adknrienir veifreyfet ecidktfwit nnktltvkei adfgdcvenf
      601 dylnrivnnd knhyrviisa lellsfftvp ldrrddfkqe llcllksesi sdaikahvvs
      661 cindqmfcde dieylhkife ifkaetskqi niellsllkd ykpiddffwy ikdeflrdkr
      721 ilprvekddv mrgnswklek liirlksssn fiffakfyfd ettnsytdnr faediiekcl
      781 ffeseesdfl vrllssfedk ekyylretll kalilkssin sqiesfkyli enftfnnvgy
      841 flasittekt inividkfkd gsldsdnldf frnvianhgn rklagefnsi mieneftfkh
      901 dfllerefee qkmefenkpq dnfdklfnkp qllseiqvif geygnsvkpe rmreidmawy
      961 eknghgnrid iaysllsrlv ykekreityd dvveilneef iiikeikski egsdkikvke
     1021 eqkeflcqwc levskdidfn kimkriddsr fsllkdyerl ktvlffmiel dinlpqqfml
     1081 dsieffdvdk snvednnldi lkgriknidv fnqrivenll nkqlvffsln khiqyaldns
     1141 lvetfskire cflidgliyn sdsqlsqyik ltsdtdllve lcidvkshvc wssikilmdl
     1201 gihkelciek aieylelemd dekryyysna lailfesnsl ealkyleyfl nidsvpslke
     1261 ssfanydiie dynileelfn kiyledrnki gfsgvsnflk iyisnlartt egyekiiakl
     1321 neiknkivni etdnglfyin lliddcrdny inskskalnf ddaltkieei ls
//
LOCUS       WP_284651358             202 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Flavobacterium terrisoli].
ACCESSION   WP_284651358
VERSION     WP_284651358.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 202)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..202
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23669
     Region          2..180
                     /region_name="HAD_sEH-N_like"
                     /note="N-terminal lipase phosphatase domain of human
                     soluble epoxide hydrolase, Escherichia coli YihX/HAD4
                     alpha-D-glucose 1-phosphate phosphatase, and related
                     domains, may be inactive; cd02603"
                     /db_xref="CDD:319790"
     Site            order(8..12,102..103,141,165..166,169..170)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            136
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mintiifdfg dvfinlekek sieefkklgl agpneellah ndlfekgqit dvqfvesfhk
       61 fipnasieei tkawnsvigd fplyrleflq llsnkyrlfl ltntdsihin rfehkvgmsf
      121 ysdfyrcfek vyysyemgmr kpqpeiftai mnkhdlspkr tlfvddkken tdaaeklglh
      181 vwnlqvgked vinlfdqkhl pf
//
LOCUS       WP_284651372             371 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Flavobacterium terrisoli].
ACCESSION   WP_284651372
VERSION     WP_284651372.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..371
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=43892
     Region          5..370
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mignqnqnri fgldvmraaa ilmvmfghci wvfpltygvf hqlmllsgfl gvevffilsg
       61 fligkilyel ylkqdfsmns vvfflkrrwf rtlpnyllil ivniliafvi gndisyswky
      121 fffaqniftp mtpfftesws lsveefayiv lplflflvgs vvkpqqkskf flfsvlilil
      181 lffcnkifyq ntttnttlnq wnmslkavvi yrldsifigv lcswiylnfk eswrkyryif
      241 fvigiflflf qfvaigyfgl fietypafwn ilylplvsvv vacflpffse wkkektvikk
      301 pivfisiisy smyllhygvv lqllkhnidy naqnpielyg flsayvfitl flsyllyrfy
      361 ekplmdlrdk n
//
LOCUS       WP_284651441             399 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Flavobacterium
            terrisoli].
ACCESSION   WP_284651441
VERSION     WP_284651441.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..399
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=46582
     Region          184..398
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mlfqfgfyss lllisfsqgi iysvlllaka iktenkpnyw lslfiflcsl yiapwmlgfa
       61 gwydnqpyrd ilfytpfqhl fligpviffy tqsllnanfs ldkkkilhfi pgiayllyia
      121 ilwvydkfiv heyyfyqngl dkdfdywyqk tglvsmivyf vlsiryynny skliyqvvsf
      181 adsvlfrwik tylcafliml llpvvfdiia ifqpeiesyt gtwwfflffs iimyyiaitg
      241 ysnpivtkip feisvfpnqp allvqsnkse eviidieqet flkqespets iwknkiatli
      301 aeeklyqnpe ltltdlakkl etnasiiskt inqsfglnfn dfinqyrina vkkafdageh
      361 kkstllgiaf dcgfnskatf nrafkkntgl spkefiekp
//
LOCUS       WP_284651456             420 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Flavobacterium
            terrisoli].
ACCESSION   WP_284651456
VERSION     WP_284651456.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..420
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=47283
     Region          <8..420
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mesvqnikqr feiigndpkl nraiekaiqv aptdisvlvv gesgvgkesi priihslshr
       61 khgkyiavnc gaipegtids elfghekgaf tgannaregy fevadggtif ldevgelplt
      121 tqvrllrvle ngefikvgss qvqktnvriv aatnvnmfda iekgkfredl yyrlstvdip
      181 lpplrdrkdd ihllfrkfaa dfahkykmpp iklsddavqf lqkyrwsgni rqlrnvaeql
      241 svletnrdis latlqsylpi egstlpsvig grksdsdfan erdilykvlf dmksdlndlk
      301 kltlelmkng tkvqdinpsl iqkvygsaak eseisfeeep rvnvippqnq shqeefdded
      361 dsdylmaeti eeeetlslea kelelikkal drnkgkrkaa adelgisert lyrkikqfdl
//
LOCUS       WP_284651553             364 aa            linear   BCT 25-DEC-2024
DEFINITION  fatty acid desaturase family protein [Flavobacterium terrisoli].
ACCESSION   WP_284651553
VERSION     WP_284651553.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..364
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42398
     Region          4..364
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mnnttpifsk tdslkffrtl nsrvnsyfke nnldrtgnwk lhlktivmfs ifltpyfill
       61 amhmpiwayl llnvvigvgm agvgmnvmhd gnhgaysnks wvnkimggsi yilagnvynw
      121 qvqhnvlhht ytnilghded leagrimrft keakwyrfhk fqhyysvfly glltfnwait
      181 tdflqmkryl krnlsygefk kpvirwttli itkiiyfsiw lvlpmvlgvs wwkvvlgflv
      241 mhytagvils vvfqlahvve etenpipddn geientwaih qlfttanfap knwlvnyytg
      301 glnhqvehhl fpnishihyg kiaeivkqta kecelpyyef kttraaiash fkhlrelgrq
      361 pqla
//
LOCUS       WP_284651583             376 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Flavobacterium
            terrisoli].
ACCESSION   WP_284651583
VERSION     WP_284651583.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..376
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41438
     Region          13..375
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mrkiqmvdlk sqyekikdtv nasiqevldt ttyingplvh efqknleqyl dvkhvipcan
       61 gtdalqiamm gldlkpgdev itadftfaat veviallqlt pvlvdvdvvn mnisidaikk
      121 aitpktkaiv pvhlfgraan meaimaiaaa hnlyviedna qaiganckfs ngtkkkagti
      181 ghvsstsffp sknlgcygdg gaiftnddal ahkirgivnh gmyvryhhdv vgvnsrldsi
      241 qagvlnaklp fldaygkarq daarkysaaf eghkniiapt icdncdchvf hqytlriida
      301 drnalmehll akgipcaiyy piplhsqkay ldprykeedf pvtnqlvkev islpmhteld
      361 deqikfitds vleflk
//
LOCUS       WP_284651631             160 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Flavobacterium terrisoli].
ACCESSION   WP_284651631
VERSION     WP_284651631.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..160
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17951
     Region          27..160
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mliknqvkyf itlfiiftfs tkaqikvgds ipsitlksnt nsevitssfk gkyvlvdfwa
       61 swcapcrlgn kklvklhnev spdkieiigi sididvnkwl kaiekdkikf tqlidpkgfd
      121 anaalvfgvd elpskylfnp egvliaknpt eeeimklike
//
LOCUS       WP_284651678             248 aa            linear   BCT 25-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Flavobacterium terrisoli].
ACCESSION   WP_284651678
VERSION     WP_284651678.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..248
                     /product="MlaE family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27395
     Region          1..247
                     /region_name="MlaE"
                     /note="Permease subunit MlaE of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG0767"
                     /db_xref="CDD:440530"
ORIGIN      
        1 mmlvrylsqi gkyflmlkev fnkptkwsam rqlifkeidd liidslgivc fisffvggvv
       61 siqtalnltn plipkyligf atrqsvilef aptfisiima gkmgsfitss igtmrvteqi
      121 dalevmgvns lnylvfpkii alllypfvig iamflgvfgg wiacvyggfa ssnefvtgiq
      181 qefipfhiay afiktfvfam ilatipsfhg yymkggalev gkastvsfvw tsvtiilany
      241 iltqlllt
//
LOCUS       WP_284651721             319 aa            linear   BCT 25-DEC-2024
DEFINITION  YbgA family protein [Klebsiella pneumoniae].
ACCESSION   WP_284651721
VERSION     WP_284651721.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007153
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..319
                     /product="YbgA family protein"
                     /calculated_mol_wt=36123
     Region          69..315
                     /region_name="YbgA"
                     /note="Uncharacterized conserved protein YbgA, DUF1722
                     family [Function unknown]; COG3272"
                     /db_xref="CDD:442503"
ORIGIN      
        1 mntqpvigis gcltgsavrf dgghkrmgfv mdelaqwvaf kpvcpemaig lpvprpalrl
       61 vqtpvgeirm gfshaphedv tekmadfasa hlatlgelsg fivcakspsc gmervrlyde
      121 kgnrgrkegv glftgalmar ypwlpveedg rlhdpllren fvervfalhe lnalrarglt
      181 rhgllafhsr yklqllahhq agyreigpfv aslhewedle affevyrekl mailkqpasr
      241 knhtnvlmhi qgyfrdqlns rqrgelrevi lnyragllpi lapltllkhy laeypdrylq
      301 aqnyfdpypq dlalrltvn
//
LOCUS       WP_284651711             232 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Flavobacterium terrisoli].
ACCESSION   WP_284651711
VERSION     WP_284651711.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..232
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=26633
     Region          <21..230
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(21..22,25..26,28,52,55..56,59..60,62..63,86,89..90,
                     93..94)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          21..45
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          50..80
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          128..163
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          166..194
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mklifqiivl fplmifsqtd fekaeklflq knyvlakpil mdfikenpnh vkgleylgei
       61 egankswtka mayflrlqkl kpteanyyyk yggclgmkak esgklkalgm ideikvsfek
      121 aiqlkpnhve arwalielyi qlpgivggse kkaqeysgql lkispvdgyl skgriaeyfe
      181 rykeaeknyk laievggski tyqklanlyk ykmnqpekak lvletyqekn ks
//
LOCUS       WP_284651777             252 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Flavobacterium terrisoli].
ACCESSION   WP_284651777
VERSION     WP_284651777.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 252)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 252)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..252
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28475
     Region          1..248
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mitailvddd snlrngmksl lsryapeiqi igeadsvesg talllesqpq vlfldihlgd
       61 gsgfdlleev skkgkinsqi ifitaheqya ikafrfsald fllkpvdpee lgkvigklkq
      121 vidkndsvah idlllenikk kvdnfkrial snsdgihlfe vsdiircese dnytkfyikn
      181 nkpilisktl keyedllteh gferihqshl inlaylksyi kkdggyvima dnsnlpisqr
      241 kkdrlqellk tm
//
LOCUS       WP_284651782             789 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Flavobacterium terrisoli].
ACCESSION   WP_284651782
VERSION     WP_284651782.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..789
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..789
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=81488
     Region          <23..668
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mkknyifftt lallliafks saqtdntfsg tgaganstgn fntgfgvdal kdnashsnna
       61 fgaralsvti ggfnsafgne slrnnttgtl nsafgtrslf snvsgqsnia fghrameanv
      121 sgsgntaigy gamlkaignn nvalgvntpr nlvsgnnnvf igaetgknli ngsnnlflgn
      181 valepaltsa klagtntdgt iiladglgnq rffvskfgna glglgnnvip anrldvnggv
      241 vigknyvpsa gtttatttla ptngllvegk vgignrlpnn kveithgvng nsglrftnlt
      301 sqytppvaqt stkfltvnan gdvvlqrmag ltntnvmssn anlmttnvns vtasapivns
      361 isniinssnq litsvngvas apvnlpqsld nsvtnelqtl sqvgntitls ngggsvtilp
      421 iedtdtdqqs lgltgnvlsi sngnsvtlpt vtpqtltqsg ntitlsnggg svvippyidt
      481 ntdqqslfls gqvlsisngn svtlpaqtls qsgntislsn gggsvvippy vdtntdeqvl
      541 sitgnvlsis ngnsvvlpnh gpqsitqnga ivtlsngggs itlqssivta gtnvnvlgng
      601 tagtpyvvsa tdtslyadng aidatttisg nrvvnmnnsn iwfntansss nakiylgsta
      661 sypnttgnyk lfveggilte kvkvalrssa nwadyvfakd yklmplkeve kfvtankhlp
      721 gidsaevlak ngldvaemqs kqmekieelt lyiidqdkki eaqdkaiekn nkeieelkal
      781 vqalmaktk
//
LOCUS       WP_284651811             316 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Flavobacterium terrisoli].
ACCESSION   WP_284651811
VERSION     WP_284651811.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..316
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37161
     Region          1..191
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mfsvvisyyk kikyiercld svmnqsfqnf evilvddgsn dnvkelldqk ypkvklitkk
       61 negvsiarnt giaaasfdyi alldadddwh fqylefmnav irehpdakii gthysvnrdd
      121 ipkgsttlry rklehyfkia ivntlftsss svirksffes nqgfnpalrs gqdvdvwfrt
      181 vlsgggvyfi dntlmfycqe dtqgvtklkl nqtielkdif lgnipknyyp lydtidneef
      241 kvfiskyiyf nlyryyyser fhdlaveilk skkhsyflld lvykiplfvg yklirkpkfs
      301 lllrnymkfv frrilk
//
LOCUS       WP_284651820             379 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Flavobacterium
            terrisoli].
ACCESSION   WP_284651820
VERSION     WP_284651820.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..379
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41560
     Region          5..378
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 msnskiwlss phmggneqkf vqeafdtnwv aplgpnvtgf eqdlekylee eihvgalssg
       61 taalhlalil lgiksgdevi cqsmtfsasa npivylgatp ifidsepetw nicpvsleka
      121 iqdriaagkk pkaivgvhly gmsfkvdeit aiadkyeipl vedsaealgs tykgrkcgtf
      181 gdisilsfng nkiittsggg aivtktleqk nkavflstqa rdnaphyqhs eigynyrmsn
      241 icagigrgqm eildkhiglr ramhdfyvnl fenipgvtvf sepnsdyfsn hwltcisida
      301 nktngitsek lrlalekeei ecrplwkpmh lqpvfsdcly fggnvaenlf anglclpsgs
      361 nltendrnri tnaveavfr
//
LOCUS       WP_284651851             244 aa            linear   BCT 25-DEC-2024
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Flavobacterium
            terrisoli].
ACCESSION   WP_284651851
VERSION     WP_284651851.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439579
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..244
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27331
     Region          5..240
                     /region_name="PssA"
                     /note="Phosphatidylserine synthase [Lipid transport and
                     metabolism]; COG1183"
                     /db_xref="CDD:440796"
ORIGIN      
        1 mnikrlipnl ftmlnlfcgc vavvlvagne fdwafyfvcl giffdffdgf farkfgvsgp
       61 lgvqldslad mvtsgvvpgf vmyqllmdrk nlyvsnldwf dislpylgfi itlgacyrla
      121 kfnidtrqsd sfigvptpan alfitslplv anyfhteidm gfsyncwfll lltalsayvm
      181 nakiplfslk iknfsvakyk lqifflaisv lmlvflqila vpliillyvl lsvinnivnk
      241 kass
//
LOCUS       WP_284651869             136 aa            linear   BCT 25-DEC-2024
DEFINITION  6-pyruvoyl trahydropterin synthase family protein [Flavobacterium
            terrisoli].
ACCESSION   WP_284651869
VERSION     WP_284651869.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Phillips,G., Grochowski,L.L., Bonnett,S., Xu,H., Bailly,M.,
            Blaby-Haas,C., El Yacoubi,B., Iwata-Reuyl,D., White,R.H. and de
            Crecy-Lagard,V.
  TITLE     Functional promiscuity of the COG0720 family
  JOURNAL   ACS Chem Biol 7 (1), 197-209 (2012)
   PUBMED   21999246
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Colloc'h,N., Poupon,A. and Mornon,J.P.
  TITLE     Sequence and structural features of the T-fold, an original
            tunnelling building unit
  JOURNAL   Proteins 39 (2), 142-154 (2000)
   PUBMED   10737935
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..136
                     /product="6-pyruvoyl trahydropterin synthase family
                     protein"
                     /EC_number="4.1.2.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15570
     Region          2..136
                     /region_name="QueD"
                     /note="6-pyruvoyl-tetrahydropterin synthase [Coenzyme
                     transport and metabolism]; COG0720"
                     /db_xref="CDD:440484"
ORIGIN      
        1 mrvtvsrkah fnsahrlyrk dwsmekneav fgkcnnpnfh ghnyeltvsv tgeidpetgy
       61 vidtkvladl ikehieyafd hknlnldvpe fadlnptaen iavviwnklr phisgnkdle
      121 vvlyetprnf vtykge
//
LOCUS       WP_284651897             726 aa            linear   BCT 25-DEC-2024
DEFINITION  B12-binding domain-containing radical SAM protein [Flavobacterium
            terrisoli].
ACCESSION   WP_284651897
VERSION     WP_284651897.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   2  (residues 1 to 726)
  AUTHORS   Banerjee,R. and Ragsdale,S.W.
  TITLE     The many faces of vitamin B12: catalysis by cobalamin-dependent
            enzymes
  JOURNAL   Annu Rev Biochem 72, 209-247 (2003)
   PUBMED   14527323
REFERENCE   3  (residues 1 to 726)
  AUTHORS   Ludwig,M.L. and Matthews,R.G.
  TITLE     Structure-based perspectives on B12-dependent enzymes
  JOURNAL   Annu Rev Biochem 66, 269-313 (1997)
   PUBMED   9242908
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..726
                     /product="B12-binding domain-containing radical SAM
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0031419 - cobalamin binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=83372
     Region          196..549
                     /region_name="YgiQ"
                     /note="Radical SAM superfamily enzyme YgiQ, UPF0313 family
                     [General function prediction only]; COG1032"
                     /db_xref="CDD:440655"
ORIGIN      
        1 mkdillitpp ftqlntpypa taylkgflnt knisgfqmdl gievilemfs kegllnlfgt
       61 npkpetsnse rilclqqdyi ntidavisfl qgknqtlarq icsgnflpea srfdqlddme
      121 wafgsmgmqd kakhlatlyl edlsdfivec vdenfgfsry aerlgrsans fdemyvhlqn
      181 dltyidkitl kilkqrliea qpklvcisvp fpgnlysafr caqfikkyfp aikvsmgggf
      241 pntelrdlkd qrvfeffdfi tlddgelpve llhnyvtlsa vegifkrtfl lennevvykn
      301 nstqsdykqs evgtpdysdl fldkyisvie ianpmhslws dgrwnkltma hgcywgkctf
      361 cdisldyikl yepisakilv drmeemmaqt gengfhfvde aappalmrev aleilrrkia
      421 vtwwtnirfe ksfsrdlcfl lkasgciavs gglevasdrl lelikkgvtv eqvaqvtrnf
      481 tengimvhay lmygyptqtv qetvdslemv rqlfeagvlq sgfwhqfamt ahspvgmfpe
      541 efgvipeqnn itfanndiqf kdktginhdk fsfglkkslf nymhgicfdy elqdwfdfki
      601 prttiasdfi leclekedhl evkptakvfw lggkpqteaf akskkghawe mmklvffdkk
      661 dtfeislekd kaewflkaid llqisnqktl tfaqlkadfe mqfedfelfw fskplktlke
      721 fgllll
//
LOCUS       WP_284651929             251 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Flavobacterium terrisoli].
ACCESSION   WP_284651929
VERSION     WP_284651929.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 251)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..251
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=29381
     Region          1..249
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mniiiiedek paarllqrkv eklglqvntl lhsveesihw fnsnthpdli fldiqlsdgl
       61 sfeifenidi ksavifttay deyalrafkl nsidyllkpi deddletavn kfktrnmaap
      121 nlsldfemik kmlvnpidrv ykkrftikmg qqlkminiee vecfysenkg tyihtldnrd
      181 yllditleql eteldpadfy rvsrkfiipm ktikeiqlhs nsrlkvilpt ykddevivar
      241 ervndfkewl g
//
LOCUS       WP_284651946             314 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Flavobacterium
            terrisoli].
ACCESSION   WP_284651946
VERSION     WP_284651946.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..314
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=34901
     Region          2..310
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrilvtgaag fiashlcekl hdlghevvgl dnfndyyspa lkrlnasdlk akgiavfeid
       61 lnddltsvfe rpydyiyhla aqpgisaetp lsdyvtnnif atqnlldavq kynpklksfv
      121 niatssvygl vanvdenvpa kpisfygstk laaeqlvlgl qrlgklnacs irlysvygpr
      181 erpeklytkl ienlyadkpf plfegsvkhe rsftfvgdiv dglsaiigke divngeiinl
      241 gtdevhttqe ginlveqimn ktliidhkpa rkgdqertsa vidkarkllg yepkvtfkkg
      301 leqqvqwyld kfts
//
LOCUS       WP_284651959             334 aa            linear   BCT 25-DEC-2024
DEFINITION  DHH family phosphoesterase [Flavobacterium terrisoli].
ACCESSION   WP_284651959
VERSION     WP_284651959.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..334
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=37742
     Region          8..329
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mkkedifaiq qllatpkria iiphrspdgd amgstlalyh fllkmnhqpi vispnefpnf
       61 lawlpssetv lvyendkekc skiiqeseiv ftldfnalhr tgemeqvlsk vtapmimidh
      121 hqkpdtfaty tysdtvfgst cemiynfisf lgkkdlidtt iasciytgia tdsgsfrfps
      181 ttgtthriva elidlgidns eihnqlfdnn synrlqllgr alqnmkvfpe yktsyitlsq
      241 keldefhyek gdtegvvnyg ltikgihfaa ifiehrdeni ikisfrsqgn fdvnqfardh
      301 fnggghinaa ggksyesmke tikkfenlis kiti
//
LOCUS       WP_284651968             972 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Flavobacterium terrisoli].
ACCESSION   WP_284651968
VERSION     WP_284651968.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 972)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..972
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..972
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=110336
     Region          33..496
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          561..951
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mkktiiascl llavttiqaq tfstekkqds qgysyetvkn dktglrvytl knglkvflaq
       61 ntdepriqty ipvktgsnnd psdntglahy lehmvfkgts kigtqnweve kkliaqisdl
      121 yeqhkaetdp ekkkaiykqi devsqeasky svaneydkli sslgakgtna htnlyetvyk
      181 nnipanelek wmmvekerfs elvlrlfhte leavyeefnr sqdndgrlvn felmsalfpd
      241 tpygqqttig ksehlknpsm vaihnyfnqy yvpnnmavil vgdldfdkti kmvdkyfgtf
      301 qykelpmkkk vvekpmtaiv srevksptae rvslawrtsg tgtkeallad mtseilsnag
      361 dvglidlnin qkqlalsaqg fsttfdeygy fglnlstkeg qtleqgrdll lsqiellkkg
      421 efdewmiqai innrrldvmk ayesadglat siyrnytqgi sweknlsein elakitkadi
      481 vkfaneffkd nyviiykrkg vndklvrvsn pkitpiqlnr daqsefyknf akltstdlap
      541 vfvdfksaiq tkkvkntnis fiknntntis nlyyvfnmgs dhdkklqlaa gmldywgtnk
      601 lspedvkkef ykigisysvn ftndmtyisl tglennlpkg ialledllkn vkadqevynt
      661 qvesvlnsra nakkrkesil nalvnyakyg kdsrfrdiis ekelremnvn kladlvkgmt
      721 syehqiffyg tdlnpivtal eknhnlaank pipapklype petnnkvyfa nydmvqtemt
      781 rvakggkynp sfsgtvnvfn syfgsglssi vfqeiresks laysaranym iandknlndy
      841 mqvaigtqan klpeavdain alladmpkid kqfnnakess lkqiassrii ktniffnqln
      901 vkklgfdydi rkdayksieg ltlnatneff nkevkpkkyn taiigkkesl dfealkklgq
      961 ieevtleeif ny
//
LOCUS       WP_284652093             341 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Flavobacterium terrisoli].
ACCESSION   WP_284652093
VERSION     WP_284652093.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..341
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37521
     Region          1..339
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 meinlisdtv tkpspemlka mfnakvgddv fkqdptvnaf ekmvadlfgk eaalffpsgt
       61 manqtaikln tnpgdqiicd kwshihlyea ggasansgvn fnlldgnrgm itaeqvkagi
      121 ndpefyhapl skmvgientt nkgggacydl eelkkikqvc tdnnlkyhld garlwnaive
      181 kkqhpkqfge lfdtisvcfs kglgapigsv lisdaetmhk alrirkifgg nlrqsgylaa
      241 agiyalqnni nrladdhrra kelgqalqql swvekvepae tnilifevnk alnekaviek
      301 lkskgiliss mgqgklrmvt hldykqvlhe yvlealgkie f
//
LOCUS       WP_284652119             418 aa            linear   BCT 25-DEC-2024
DEFINITION  MDR family MFS transporter [Flavobacterium terrisoli].
ACCESSION   WP_284652119
VERSION     WP_284652119.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023665
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..418
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47281
     Region          20..398
                     /region_name="MFS_MdtH_MDR_like"
                     /note="Multidrug resistance protein MdtH and similar
                     multidrug resistance (MDR) transporters of the Major
                     Facilitator Superfamily; cd17329"
                     /db_xref="CDD:340887"
     Site            order(30..31,34,37,70,120..121,123..125,128,148,151..152,
                     155,228,231..232,235..237,240,268,272,323..324,328,332,
                     348,351..352,355..356,359)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mlktafqryi nnfkgfsrei wiltiitfin ragtmvlpfl skylkedlgf hydeigtimv
       61 cfgvgsmlgs wlggklsdki gfyrimifsl ltsglmffvi qfvtsfvglc vsmflimtva
      121 dmyrpamfvs igayakpenr traltlvrla inlgfaagpa mggliimnig yrglfwadgi
      181 tcivailifw ikvkekkksa frdkehpgev lthsvfkdkp fwiflftclv sgvlffqvft
      241 tiplyhreqf hltelqtgll ltmngvlvfl cemaivsyve rkkiskvkvv sfgcllmavs
      301 lflmlvntwa gilvimmlfm tfaemfafpf snsvalsrap kghegrymai ytmsyslahi
      361 lsakigmgii ayysleygfq fgyqmnwlfm gilglmgafs giwvyrliqk enksismv
//
LOCUS       WP_284652128             428 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Flavobacterium terrisoli].
ACCESSION   WP_284652128
VERSION     WP_284652128.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..428
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=50501
     Region          1..426
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mnifwfrrdl rlednvgffh alksgdevlp ififdenils qlpkddarvt fihqqlskiq
       61 nqlksvgksl avfygdpfev fnkiltenqi ttvytnhdye pyarkrdlel yhlfseydie
      121 fktskdqvif eksevvkedg tpyvvytpys nkwkehfnkl klvnynsedy lekitvhsyp
      181 fltlsaigfk pseikvppyd isndlidnye atrnfpaidk tshlgiylrf gvvsirqmvi
      241 kaaesknetf lkeliwreff mqilwhfpht ihksfrpkyd eiqwrndetl fqkwcdgqtg
      301 ypfvdagmre lnttghmhnr vrmivasflc khllidwrwg etyfasklld yeqasnvgnw
      361 qwaagsgvda apyfrifnpt eqikkfdkdl ayikkwipel ntsdypepiv dhatardncl
      421 kiykkale
//
LOCUS       WP_284652305             214 aa            linear   BCT 25-DEC-2024
DEFINITION  endonuclease III domain-containing protein [Flavobacterium
            terrisoli].
ACCESSION   WP_284652305
VERSION     WP_284652305.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Kuo,C.F., McRee,D.E., Fisher,C.L., O'Handley,S.F., Cunningham,R.P.
            and Tainer,J.A.
  TITLE     Atomic structure of the DNA repair [4Fe-4S] enzyme endonuclease III
  JOURNAL   Science 258 (5081), 434-440 (1992)
   PUBMED   1411536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..214
                     /product="endonuclease III domain-containing protein"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=23861
     Region          19..210
                     /region_name="Nth"
                     /note="Endonuclease III [Replication, recombination and
                     repair]; COG0177"
                     /db_xref="CDD:439947"
ORIGIN      
        1 mslfetnsdw aqklqpiidl yknkkhpldy enlyqlmvmv ilsaqdsdan inkvapalfk
       61 eypnlealst asmdtlipfv tkvrnfntka swlieiaqtl kkdsniptsl pelvalkgvg
      121 rksanvimre mkvpaegiia dlhvirvapr igvipeakdg nkvekllmet lpkeiwgevg
      181 maisflgret crptnpkcpq cpiqndcqyp lkti
//
LOCUS       WP_284652334             398 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Flavobacterium terrisoli].
ACCESSION   WP_284652334
VERSION     WP_284652334.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 398)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..398
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=45284
     Region          1..392
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mieaklplne arrlrileey hildtenend fdeitklase icdspisqit lidtnrqwfk
       61 sshglasket prslsfcaha ihgdemfvve darkdirfhd splvtsdpni vfyagvplid
      121 kegyalgtlc vidnktkkln pfqekalktl shqvlklmel kkanyklnak nnllkesyse
      181 lerfshvvsh diksplnnil gltdllredh cqvtnteanl yidlikesse klkeyidatl
      241 raykngtlas dekeffhlns ilkesiklln pknefeinlp enleifnyks yfeqifmnli
      301 snaikyndkp kvivdikvtp gndfytikvk dngigietdk ldlifemfyt lektdrfnnm
      361 gtgiglstvk tlaqrtggei svtstvgvgt efvlkfkp
//
LOCUS       WP_284652367             187 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Flavobacterium
            terrisoli].
ACCESSION   WP_284652367
VERSION     WP_284652367.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..187
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=21947
     Region          <94..174
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkihikymvs lrckmavkee ldklklkhtt idlgevnlkk nihaedresl rkallkkgle
       61 liddkkslli ertknvivel vhysekypkv nfsdylskel dynythlsnl fsevtgttiv
      121 nyiilnkier vkelllydel slteisylme yssvshlsnq fkkvtgltps yfkqikqykk
      181 riqleel
//
LOCUS       WP_284652392             212 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Flavobacterium terrisoli].
ACCESSION   WP_284652392
VERSION     WP_284652392.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..212
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23827
     Region          47..204
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mhfeeflkyt pkiqnvelpa tnahakmapa nrldlikaid fskvtpkqaa vmmlfypkns
       61 qahlalilrt syngvhssqi afpggkvedi dldlketalr etheeigvhp ehikvirpft
      121 evyippsnfm vypylgyses elefvlqdde vaglvefpfa dfmddsivvn mtmvtsyags
      181 ikvpgfqvke hfvwgatamm lselketlkm vl
//
LOCUS       WP_284652408             419 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Klebsiella pneumoniae].
ACCESSION   WP_284652408
VERSION     WP_284652408.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..419
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=47102
     Region          14..385
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mskesyptgv enhgkslriw fifkgkrvre nlgvpdtakn rkvagelrts vcfairmgtf
       61 dyaaqfpnsp nlktfgickk ditvkflsek wlelkrmeic anainryesv vrsmlpriga
      121 kklvscvtre ellyirkdml sgekglsvvt vnyymstiag mfqfaadngy vsenpfngik
      181 plkrariepd pltrdefvrf idackhqqtk nlwsiavytg lrhgelvsla wedidlkagt
      241 mtirrnytkl gdftlpktea gtdrvvhlik paidalrnqa emtrlgrqyq ievalreygr
      301 tvihdctfvf npqlvkksgs vgylykadsv gdswdaalkr sglrhrkayq srhtyacwsl
      361 saganpsfia sqmghasaqm vfnvygawma dsssdqiaml nqklsdfaps mphgmvigi
//
LOCUS       WP_284652440             261 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Flavobacterium terrisoli].
ACCESSION   WP_284652440
VERSION     WP_284652440.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..261
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=28220
     Site            order(146..147,150..151,153,178,181..182,185..186,
                     188..189,215,218..219,222..223,226)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          146..170
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          150..251
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Region          176..206
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          214..242
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 matfnkrgyk apkekaekld nnfiedvnvd ekdsatakaf dtldqsasra edfiaknqkv
       61 ilgflgaivl avvgyfaydk fiaepnqqdg aeqlfvaqqn fqkavdgdvk adslfnlvln
      121 gsegkygvvk iaeeysgtaa gnlanyyagi aylntgkyae avsslekfss kdimlstlaq
      181 gaigdayaqq nkqkealefy lkaadasqnd ftrprylmka gktalalgnk adalkyftei
      241 kesfdgtpea qnidgligla q
//
LOCUS       WP_284652460             174 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Flavobacterium terrisoli].
ACCESSION   WP_284652460
VERSION     WP_284652460.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..174
                     /product="YybH family protein"
                     /calculated_mol_wt=19402
     Region          31..158
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mknkmlkgiv lsmvsllffa ckpkteevvv dkeqikneiq sienkmaelf ndrnvnasey
       61 yaddatsfsq nkpplvgkaa ieksikddla nfpegyqiaf vvneifpsdn anqvveigny
      121 rvsdaggnal ytgnyiavfe krdgkyvcir dmsasdrprl eskkelaaet ekke
//
LOCUS       WP_284652461             169 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Flavobacterium terrisoli].
ACCESSION   WP_284652461
VERSION     WP_284652461.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..169
                     /product="YybH family protein"
                     /calculated_mol_wt=18130
     Region          37..164
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mknkilkgit lgiivalaia cnpkkeeapa aepvavdkeq iktelqamet afadamnagk
       61 pesivyyadd aksfeqnekp lvgkaaidak lakevsegpk gtkvtftane vfpssdgnlv
      121 velgsykvad ttnttkysgn ymalfekrdg kyvcvrdmga sdmpkeekk
//
LOCUS       WP_284652618             424 aa            linear   BCT 25-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Flavobacterium
            terrisoli].
ACCESSION   WP_284652618
VERSION     WP_284652618.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..424
                     /product="metal-dependent hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45558
     Region          22..>84
                     /region_name="NagA"
                     /note="N-acetylglucosamine-6-phosphate deacetylase
                     [Carbohydrate transport and metabolism]; COG1820"
                     /db_xref="CDD:441425"
     Region          66..410
                     /region_name="Met_dep_hydrolase_A"
                     /note="Metallo-dependent hydrolases, subgroup A is part of
                     the superfamily of metallo-dependent hydrolases, a large
                     group of proteins that show conservation in their
                     3-dimensional fold (TIM barrel) and in details of their
                     active site. The vast majority of the...; cd01299"
                     /db_xref="CDD:238624"
     Site            order(82,84,248,268,341)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mkklflfvsl fitsvlfaqe tyihcgklid tkigkvftnk tiivsgktik rledgfvnpk
       61 dsstkvvdlk nntvmpgwid mhvhlegets psayleeftl ndadvaynae gfakttlmag
      121 fttvrdlggt gvnvslrnai nsgkvigpri ftvekaigst gghadptsgy rkdlmgnpgp
      181 kegvvnsidd akqavrqryk ngadwikitv tggvlsmaks gsnpqfteee iaaivstakd
      241 ygmkvaahah gdegmqravr agvktiehgt emseatmdlm iknnaylvpt itagkavaen
      301 aekenyypav vvpkaraigp kiqgtfakay krgvpiafgt dasvfehgln akefmymaea
      361 gmpimkaiqa atvtnamlld mdkkigviep gfladiiate ldptqdvnav mkvvfvmkdg
      421 viyk
//
LOCUS       WP_284652692             116 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Flavobacterium
            terrisoli].
ACCESSION   WP_284652692
VERSION     WP_284652692.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..116
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12886
     Region          10..116
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 miketstnne nrktisavcp vsfaldkvgg rwkplilwnl kdgrlrysel kkaippitek
       61 mliqhlkqle sdslvlrtvv evmpphveys lthsgaellp altaladwgv rnsskp
//
LOCUS       WP_284652888             211 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Flavobacterium terrisoli].
ACCESSION   WP_284652888
VERSION     WP_284652888.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..211
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23362
     Region          7..>87
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 makvkmhkks tsidmtamcd vafllltffi ltatakmpep lpvdtpsstv qtklpetglv
       61 titvgksdgk eqvffgmkdr airegaldym srtykvsftd kekqefklme efgvpmsdlk
      121 gllaktgser skkgtqsgip cdsigdnnql kdwimaarta nienggekel qfaikgdake
      181 eypqikrvmd ilqdqkinsf nlvtglrgkd y
//
LOCUS       WP_284652892             553 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Flavobacterium terrisoli].
ACCESSION   WP_284652892
VERSION     WP_284652892.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..553
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=60805
     Region          11..294
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          122..151
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(158,161..162,165..166,168,192,195..196,199..200,
                     202..203,226,229..230,233..234,237)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          158..185
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          190..220
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mnkfkifsla lvattiakaq dlepakkaid aeqfekaksl lksviqtkps ngkaafllgn
       61 iylkqniads asiyfqkgla asdgarlnni glaqldldan nkaaaqakfd mvikelkkkd
      121 teeyvyiara ymnadkpdya saitvltkaa aanpadaqvq lalgdayyge kkqneayvay
      181 rnayqadssl irakmqlgvl lkgakaytea vkayneviai npnygpvyre laethylwgn
      241 nvpstytdni qkalgfyeky msltdysins rmrhadflil akdykaleae atqmkaldgv
      301 nprilrylgy sayengnada aldalqkyts npankiiprd ylylgqakik kgtaadgksv
      361 dptllasame dikkavtmep laanelnelg kklydqklfa aaaavfevav tnptsknyll
      421 dnfylgnaly ydntrkdvvk vdpvalqkad vafgnvitas pttqdaylfr artnkllesd
      481 qvmadnyqly idtvtakgea eitknkakfi eaynnmashy antdkakake llaktlaldp
      541 enayaleamk llk
//
LOCUS       WP_284652934             408 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Klebsiella
            pneumoniae].
ACCESSION   WP_284652934
VERSION     WP_284652934.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..408
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=45562
     Region          4..397
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mliqkaykyr lnptdaqaqr lrqmcgcarf vwnyalaetq rileagqklp safelnkmlt
       61 gwkklpdlaf lsdaytdnlq qklkdlhgaw ercfdkklaa kapvfkhksh gndsvrfvnf
      121 dkycqlqhrr vklpsglgwv tfrqsravvg kiknatvsqh aggwyisfqv emvveqpthp
      181 stsavgldag icklvtlsdg tvfepvnsfk qnqsrlarlq rqlarkvkfs anwkkqkaki
      241 srlhahitni rrdylhkvtt tisknhamiv iedlkvsnma ksaagtadep grnvtaksgl
      301 nraildqgwy emrrqleykq rwrggevlav npaytsqkca ccghtskenr qsqatfvcva
      361 cgyeanadvn gacnilaagh avlacggtvq svrpmkqepg tersvvth
//
LOCUS       WP_284652899             233 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Flavobacterium terrisoli].
ACCESSION   WP_284652899
VERSION     WP_284652899.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..233
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25804
     Region          51..153
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mkdlfgkail dfqthnaped lvtetnisea demsveylfr syndmpkiek kalqlakgki
       61 ldvgcgagsh slylqekgfd vtaidispna ikacqlrgvk naraqnlldi engtfdtiil
      121 lmngtgifgt laetskylqk lksllnpdgq ilidssdiiy mfdededgay lipadgyyge
      181 ltfsvsykgq tedtfpwlyl dyntlqnaah anglecelvl egkhydylaq ltl
//
LOCUS       WP_284652961             116 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy-metal-associated domain-containing protein [Flavobacterium
            terrisoli].
ACCESSION   WP_284652961
VERSION     WP_284652961.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086127
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..116
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13061
     Region          42..96
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
ORIGIN      
        1 mrnallilff tlftcslsaq eakknqkavi kttlycnhck vcetcgknfq tnllkikgvk
       61 myehddkemt itvyynaqkt dlqtikvais kmgydadevk advaayeqld gcckke
//
LOCUS       WP_284652972             191 aa            linear   BCT 25-DEC-2024
DEFINITION  YdeI/OmpD-associated family protein [Flavobacterium terrisoli].
ACCESSION   WP_284652972
VERSION     WP_284652972.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Pilonieta,M.C., Erickson,K.D., Ernst,R.K. and Detweiler,C.S.
  TITLE     A protein important for antimicrobial peptide resistance,
            YdeI/OmdA, is in the periplasm and interacts with OmpD/NmpC
  JOURNAL   J Bacteriol 191 (23), 7243-7252 (2009)
   PUBMED   19767429
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..191
                     /product="YdeI/OmpD-associated family protein"
                     /calculated_mol_wt=22991
     Region          1..186
                     /region_name="YdeI"
                     /note="Uncharacterized conserved protein YdeI,
                     YjbR/CyaY-like superfamily, DUF1801 family [Function
                     unknown]; COG4430"
                     /db_xref="CDD:443542"
ORIGIN      
        1 meekehlyfk naqewrewlh dnhnsstgvy lifyrvdsdk esmrweeavq vaicygwids
       61 tvkrldderr rqmftprkdk svwsklnkty iekliaenlm hesglrkiei akqngswesl
      121 dhvenhimpe dltlafeqnk tafenynkfs psyrksylyw lnqakreetr ksriaeivkl
      181 ceqniktrgn f
//
LOCUS       WP_284652995             344 aa            linear   BCT 25-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Flavobacterium
            terrisoli].
ACCESSION   WP_284652995
VERSION     WP_284652995.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Rengstl,B., Oster,U., Stengel,A. and Nickelsen,J.
  TITLE     An intermediate membrane subfraction in cyanobacteria is involved
            in an assembly network for Photosystem II biogenesis
  JOURNAL   J Biol Chem 286 (24), 21944-21951 (2011)
   PUBMED   21531723
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Komenda,J., Nickelsen,J., Tichy,M., Prasil,O., Eichacker,L.A. and
            Nixon,P.J.
  TITLE     The cyanobacterial homologue of HCF136/YCF48 is a component of an
            early photosystem II assembly complex and is important for both the
            efficient assembly and repair of photosystem II in Synechocystis
            sp. PCC 6803
  JOURNAL   J Biol Chem 283 (33), 22390-22399 (2008)
   PUBMED   18550538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..344
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=37890
     Region          187..338
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
ORIGIN      
        1 mkkpflffvi fflglvaqsn sqsfqsikid tvfndeisir altifgdkvy fagnkkkvgy
       61 isisdkqkte ivnnslsdec rslavngenv fvlsinnpar lykfsksled ltlvyqeshe
      121 kvfydsmqfw nekegiaigd ptndclsiii trdggniwrk tdcdnlpeia dgeaafaasn
      181 tnivlkgnhv wivsggkrar vfhspnkgkt wevfetpivq geamtgifsa dfydekigfi
      241 vggnyekpal nsqnkaittd ggktwnliad nsgfgyascv qfvpksngkg ivsvgasglq
      301 ysadggntwk qlstdatlyt irfldedtaf aagrnkivki efkk
//
LOCUS       WP_284653113             475 aa            linear   BCT 25-DEC-2024
DEFINITION  MBOAT family O-acyltransferase [Flavobacterium terrisoli].
ACCESSION   WP_284653113
VERSION     WP_284653113.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Hofmann,K.
  TITLE     A superfamily of membrane-bound O-acyltransferases with
            implications for wnt signaling
  JOURNAL   Trends Biochem Sci 25 (3), 111-112 (2000)
   PUBMED   10694878
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004295
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..475
                     /product="MBOAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54218
     Region          1..475
                     /region_name="DltB"
                     /note="D-alanyl-lipoteichoic acid acyltransferase DltB,
                     MBOAT superfamily [Cell wall/membrane/envelope
                     biogenesis]; COG1696"
                     /db_xref="CDD:441302"
ORIGIN      
        1 mifnsytfva ffililflhn lplswktkkv nlllasyify aawnppfill lwlstvidfy
       61 vgralytqen phkkklllvv slignlgmlc ffkygtffle nfvslthllg fdfnpakpni
      121 ilpagisfyt fttlcytidm ykkeskpvks lldfslfvtf fphlvagpiv rppqlvpqfe
      181 sprvasrkqm mdglllltlg lfmkvvlads mlavtadnvf nstdvlpsld awigvlafsg
      241 qifldfagys tcaigvalcl gfvlpqnfny pyaaigfsdf wrrwhitlss wlrdylyipl
      301 ggskngkakm yfalmmtmll gglwhganwt fvvwgglhgl ylwvekffkd rrgvqndasi
      361 ssntlpnffy alltfmlvni twvffradtf gkswgmlqsm fgmadgkpll ttlailkvai
      421 iiplivlchw flrntkildv aykmswiwls ifwsamllml iwaqesgssf iyfqf
//
LOCUS       WP_284653121             111 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Flavobacterium terrisoli].
ACCESSION   WP_284653121
VERSION     WP_284653121.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 111)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 111)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 111)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..111
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12758
     Region          4..83
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mrrdvfqaia dptrrtilsl laaqtltlna vaenfdisrp aiskhikiln ecglieitdk
       61 greryceakl dklsevsvwi eqykqfwetk lddletylek lqkdnnndsi s
//
LOCUS       WP_284653203             252 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Flavobacterium terrisoli].
ACCESSION   WP_284653203
VERSION     WP_284653203.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..252
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29347
     Region          <96..170
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 malledlerq strvykywqt lpsvmliigy fvlidleklp hglflkqspy enifegiclg
       61 isilgliiri iiigytpsft eknskgtaiq yhynlgaysi vrhpllladl iiwigmiait
      121 gdfwfiisfg llyilyleri ilakekrlks kfgfkysrwa egvpafipni wlyrkangvf
      181 gwrkifrsem lrfsrilfvf ftfeilgkls eekkkvayai lvlsiicavi nfiikrksii
      241 tylrrllikl ln
//
LOCUS       WP_284653239             250 aa            linear   BCT 25-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Flavobacterium terrisoli].
ACCESSION   WP_284653239
VERSION     WP_284653239.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 250)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..250
                     /product="MlaE family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27520
     Region          1..239
                     /region_name="MlaE"
                     /note="Permease subunit MlaE of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG0767"
                     /db_xref="CDD:440530"
ORIGIN      
        1 mkdflieige isyfikrffr elpmrpfefn ellrqcflig nrslplvivt afiigmvftl
       61 qsrptleefg avswmssmvs isivreigpi italicagri ssgisaelgs mkvseqidam
      121 evsgtnpfry lvvtrivatt lmipllvilg datsiyasfl vehfkgnvsl llyfnevfea
      181 lkfsdivpav iktfffgfti gligcykgya ckkgtagvgi aanasvvfts mllflidfva
      241 vfvadiiyqt
//
LOCUS       WP_284653275            1355 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Flavobacterium terrisoli].
ACCESSION   WP_284653275
VERSION     WP_284653275.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1355
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..1355
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=143207
     Region          <202..1120
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mgyanenldd atiatnnfqn sgllqfstga qtngatmsgv mefgfpamna lfpatsgayg
       61 lsieginaas ytslslqysy ykmsavahat fsvdywngsa wvnlantsaa lftegvstge
      121 gwysaialal pagaqinnlk irfvktgtna iridnvvlsg iqttttatew klagnfptds
      181 dflgtlnnkd lvfrrngafa grlgsasgnt tfgfnslnnn gssgayntiv gsknlslntt
      241 gssnavvgae nlnhntsgyg nvaigreiln enttgahnig mgngdvlaln ktgngnialg
      301 qetmemnvsg sgnialgiea lsvsqtgnmn vaigagtlig nvsghnnvav glfagdgvng
      361 dnniflgsnt tavgmaptss nklnignwiy gdngsigigv aqptaslhtd stlrfqnlgt
      421 ntsnvnvltt dssgnvttrs ltnwgsssss lnwalngnal ttsngtefmg stnnydvifk
      481 rnnweagrin etntslglfs llqnsgyyns afgmramelk gggdsntafg hgagmnltng
      541 synifigaga qpnisntgsn qlnignwifg nngnigigvd hptaslhtds tlkfenlaan
      601 tnqtkvltvg ddgnvtfrql idwtgsssan niynsdgtll kerfvyfgkv npfnlhfidd
      661 ifnnelvlss qnfvdqkdsf ssikmtannf yqdpnligwg msnitqpgsa ialtqglnsk
      721 atwlqssrrr pegrfgrate pleseefetf nllinplhgn vgvgvmdpta qlhtintvrf
      781 enlanpsekp vnilgtdsag nvyewdpgif sggsttdtdd wqlngnagtd pnfnfigttd
      841 ardfvartnn verfrftnsa sgrivvnsef gsnwsknfyi gggnnsvntt aspygplaan
      901 taigygtlvn nttgilntal gsnallanqt ggynvaigvn alfsnktgsy nvalgqnals
      961 lagttsgqln sgntglgyqs lekvttgqnn vgigymsgfn ltsgsnnili ngeapsfinn
     1021 ptvttasdel niggwitgkg grlgigvspn fplatlhtng tlrfqglgss ttntnilttn
     1081 gsgdvairdi ssiltsngan iyntsdnlqs nrivasngnt lrfnfgtias lsanevsmnp
     1141 gvgastasls vasnrnntsn yvgtghfriq ragltntflt tgynqdgqgq hyfwtqssyn
     1201 slaasyminp dggkvaigtl nvnmdagcpd cdqyrlfvaq girtekvrvd ialvrgwsdy
     1261 vfdtgyklmp lkeleeyina nkhlpnipta eevkdkgidl aemdakllek ieeltlhtie
     1321 inkknealek nnktqqaliq slierlekle nkakq
//
LOCUS       WP_284653316             167 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Flavobacterium terrisoli].
ACCESSION   WP_284653316
VERSION     WP_284653316.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..167
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19329
     Region          1..133
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mmtitptsvy tirfsdcdlf ghlnnaryid yflnaredhl kehynlnlae yyqkniswvv
       61 ggheiaylrp avynevvsiq stlleanpey llvetqmkne sqshlkaimr tkfvpidikt
      121 grkaphessf lewaktienm avgqyntlqe rindllkeks lskelvk
//
LOCUS       WP_284653473             130 aa            linear   BCT 25-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Flavobacterium terrisoli].
ACCESSION   WP_284653473
VERSION     WP_284653473.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..130
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=13533
     Region          1..127
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 meitqkqafk sldqaiskan eigvnanitv ldtaghikaf vrmddaylgs idiamgkakt
       61 amlfrmnsea vgeflnpenk tygmvntngg lvgfkggvpv ksgdeivayi gvsggspdqd
      121 feiatagsev
//
LOCUS       WP_284653486             873 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Flavobacterium terrisoli].
ACCESSION   WP_284653486
VERSION     WP_284653486.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 873)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..873
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..873
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=99594
     Region          605..860
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mpvtriknsf ilfflvvscs vmgqvtnqkn lteadyhlws tmemqavsak gdwvsyhlay
       61 esgndtlfvr nknatkthsf pkgydgkfak dswfacmipe nvlevvnlkt glkrqmrgat
      121 qyafssdglt litltdshql sierldgsat etidnvtgff lnpsstgmvy tiakekasly
      181 ycpfdgkreh fqklvtdgea tfenivwqrk gqafafvkky kdtldsrngk nlhlyqlkqn
      241 niysfdantv asidkgsnie ppiwtrftis ddgqrvffyl testpntaek pivqqwngnd
      301 awtypqvqls grwdlqakca vwypktgevr qltsndqpkl llsgdqqyai tynpmgqkpq
      361 ftmlsktdwy ctnlntgkrt lflknyicdm eeisasyggk yivyrnaehw wvyelatgkh
      421 vnisvniphl iydeaydyag akpafgiagw ttnddtviiy deydlwsvnl knlqakrltk
      481 grekqivfri anqsgqpdrf mnfdgftfpe lamekgvylk asgkltkesg yyywdgkekp
      541 lvfsdksits laftnesktl yymeqdynsp psimamgken gqtnlvvmsn thqknyhwgk
      601 silisyrnsk nknlqaalyy panydplkky pmvvyiyerl sdqvhryvnp sllngagfni
      661 snlttqgyfv lqpdlsfelg nvgmsaadcv vsatnvvidi glvqpdkial tghsfagyqv
      721 syiatqtknf fativagagv sdligsylsi gwnsgrpeiw ryedqqwrmg kslyedmday
      781 lrnspvihaq nitsplliwt geldrqvhyy qtigfynalr rlekkvimlv ypesghalsk
      841 rnsnidfthr yeewlasylk dipapqwikk gme
//
LOCUS       WP_284653626             246 aa            linear   BCT 25-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Flavobacterium terrisoli].
ACCESSION   WP_284653626
VERSION     WP_284653626.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Bagautdinov,B. and Kunishima,N.
  TITLE     Crystal structures of shikimate dehydrogenase AroE from Thermus
            thermophilus HB8 and its cofactor and substrate complexes: insights
            into the enzymatic mechanism
  JOURNAL   J Mol Biol 373 (2), 424-438 (2007)
   PUBMED   17825835
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..246
                     /product="shikimate dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27823
     Region          4..245
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 msrrqyglig knisysfskk yftekfalgn lvdcsyenfd lqsieefptl iadnpdlkgl
       61 nitipykeav ipylgklskt aaqigavnvi rftkkgklkg ynsdyygfmk slepllqphh
      121 kkalilgtgg aakavafald qlgilytyvs reekegmidy drinvttfdh yhiiinctpl
      181 gtspdtkafp pisydfftek hiafdliynp eetqflkkak kkgaitkngy emlvlqaeka
      241 wkiwnk
//
LOCUS       WP_284653597             419 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Flavobacterium terrisoli].
ACCESSION   WP_284653597
VERSION     WP_284653597.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..419
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49240
     Region          1..>162
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mssflkkyry hlfiilvglc cletlnfllq lgkqtlvypd cdnylesaqk myhkftghyy
       61 rpmvmafitg ipylfgssda gifqwslfvn ifcwlgtsil lfeiakhfvk ekiafwfail
      121 pffllgniiw nfhiltenif vffimlafyl lfqyyktqqf wflslaltll lssmlikpga
      181 kffaiimtlf ffreifrnyk dksmvfiygs llmiviqvvg mrvqygdfti syidgvtyhn
      241 yicskaecfk ngkeysqmnn praeylfglp fteqkrvase diknqittnf pnfvkayfdd
      301 vkenaisgng ciedlknhan rshfafwksl vfditkwqnr lftllavlls ayfllkyykk
      361 eklyffiaff ivyiivlsgv scgqgdrfhl vtfpfailll akfltdrnwi kpsseplqk
//
LOCUS       WP_284653689             187 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Flavobacterium terrisoli].
ACCESSION   WP_284653689
VERSION     WP_284653689.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 187)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 187)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..187
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20456
     Region          <83..184
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mksllkiafv lgsvvslssc kddlkpnyqy mpnmyesvay etnaesdafn sptglhgkvg
       61 qlpaegsikr gfipyeypnt pealvavkaa nlkspldpaq vdmkkgeelf niycaichgt
      121 agdgkgklvk qekflgvpsy kdreinegsi fhvetyglns mgshanqlsq eerwqvaayv
      181 mqlkskl
//
LOCUS       WP_284653703             487 aa            linear   BCT 25-DEC-2024
DEFINITION  B12-binding domain-containing radical SAM protein [Flavobacterium
            terrisoli].
ACCESSION   WP_284653703
VERSION     WP_284653703.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Banerjee,R. and Ragsdale,S.W.
  TITLE     The many faces of vitamin B12: catalysis by cobalamin-dependent
            enzymes
  JOURNAL   Annu Rev Biochem 72, 209-247 (2003)
   PUBMED   14527323
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Ludwig,M.L. and Matthews,R.G.
  TITLE     Structure-based perspectives on B12-dependent enzymes
  JOURNAL   Annu Rev Biochem 66, 269-313 (1997)
   PUBMED   9242908
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..487
                     /product="B12-binding domain-containing radical SAM
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0031419 - cobalamin binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=56215
     Region          21..426
                     /region_name="YgiQ"
                     /note="Radical SAM superfamily enzyme YgiQ, UPF0313 family
                     [General function prediction only]; COG1032"
                     /db_xref="CDD:440655"
ORIGIN      
        1 msnilfshsy yykldpkqwk nktpfpplgt lyaasllrkn gytvslfdtn lldspnties
       61 ilksskpnyl vvyddgfnyl tkmcltnmre acfemirlgk iyhctvivcs sdstdhyady
      121 lkmgadyilq gegeisllel inaletqntf edikgivfrk dnktrvnpkr evlqnldelp
      181 lpawdlvdme syrniwkqsg qpftlniatt rgcpykcnwc akpiygnryn ahspeyivke
      241 iaflkenfgv trfwmcddif glkpnwvqef naklkdqnlk isyyiqsrvd lllkedtidc
      301 laesgleevw vgaesasqki ldamdkgttv eqiyqatqil kdkkirvaff lqfgyldenq
      361 ediqktiamv kelmpdnigi svsyplpgtk fydkvkddlk lksnwtdsdd femmfhgtyk
      421 snyyrklqrf vhkefrkqqg fqnlkqlfak pssisaahlk siaklgyyip safldtlslk
      481 klqqngs
//
LOCUS       WP_284653729             141 aa            linear   BCT 25-DEC-2024
DEFINITION  Rieske (2Fe-2S) protein [Flavobacterium terrisoli].
ACCESSION   WP_284653729
VERSION     WP_284653729.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..141
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=15218
     Region          <63..139
                     /region_name="NirD"
                     /note="Ferredoxin subunit of nitrite reductase or a
                     ring-hydroxylating dioxygenase [Inorganic ion transport
                     and metabolism, Secondary metabolites biosynthesis,
                     transport and catabolism]; COG2146"
                     /db_xref="CDD:441749"
ORIGIN      
        1 mkkiiillll lplaygcdgg sinnrnpnip nytvylqinm slpgysnlqf psnhivdygp
       61 msgarglvvf ntgsgfvafd lacpnqpfes cpspmtisgi eatcdcddtv ynlfsgqspg
      121 qqypmkqyrv evngntlvvt n
//
LOCUS       WP_284653737             209 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Flavobacterium
            terrisoli].
ACCESSION   WP_284653737
VERSION     WP_284653737.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..209
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=23970
     Region          10..153
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mpllkikaln ettqllvwki tetfdelfrs valkdvslar legmkaeshq kgflsvrrll
       61 meagytdfdl yydefgkphl qdgkhisish sndfsvivls nvnigadlei lkdktvkiap
      121 rfmdvshlkn lseedllkka tvvwgikesv fkikneigis fkdhifendf tladkkctve
      181 lrfndktehf nilfdfiedy vfvcafnsv
//
LOCUS       WP_284653779             159 aa            linear   BCT 25-DEC-2024
DEFINITION  peroxiredoxin family protein [Flavobacterium terrisoli].
ACCESSION   WP_284653779
VERSION     WP_284653779.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Schroder,E. and Ponting,C.P.
  TITLE     Evidence that peroxiredoxins are novel members of the thioredoxin
            fold superfamily
  JOURNAL   Protein Sci 7 (11), 2465-2468 (1998)
   PUBMED   9828014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003123
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..159
                     /product="peroxiredoxin family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18017
     Region          22..158
                     /region_name="Bcp"
                     /note="Peroxiredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG1225"
                     /db_xref="CDD:440838"
ORIGIN      
        1 mtkfiicafl iglnlnaqtn lpdvtlanle gkkvsltkdy sekdklyvfs fwatwctpci
       61 neldeindvq newkkdvnfe vvaisiddsr tqkrvkplts gkewnfaill dsnqdlkral
      121 sivnvpytiv vknnkivhvq ngyvpgneve lleklkslk
//
LOCUS       WP_284653970             332 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284653970
VERSION     WP_284653970.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..332
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38093
     Region          1..313
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mkrsdrlaai vmalqtgtet aqsladkfev skrtilrdmq alseigvpfy assgpvggyr
       61 lmdgyklppl qfspleamtv lcalqgmtql adtpfnaerw saldkikqal peqvrseiep
      121 vmdklilsmp krnyrvpmln rlmdhaaegi wirahyrsan qarwlrlrpl rivtahgfwy
      181 ceafsldhee ertfrvdrfq eieriedaae leaarlkrsr ikktrdared eipirarlty
      241 rgallaeqde higdqvlqig eeewavefac prsewawavr ffyglgpege vlapaalrre
      301 ireraarmce ryaadepage ldvrqisked el
//
LOCUS       WP_284653994             327 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus thiaminolyticus].
ACCESSION   WP_284653994
VERSION     WP_284653994.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 327)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..327
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37161
     Region          13..327
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mptpkqaaar prsrakrspd aradrsflqr virdaklnky vylmllpvva yyaifhygpm
       61 ygiqiafkdy spalgfldsp wvglkyfeef fnshffwriv rntlllslye lifsfpapii
      121 lalmlnelrh qlfkravqti tyiphfisiv vivgmmvdfl ardglinnil swfgveavay
      181 lrepgwfrtl yissgiwqgv gwgtiiylaa isnidpslye aakvdgaskw rqvvhitipg
      241 impvviilli lqmgsimsvs tdkillmyns styetadvig tyvyrkglle anysystaig
      301 lfnsvinfal lilantfsrr tsdsklw
//
LOCUS       WP_284654053             486 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus thiaminolyticus].
ACCESSION   WP_284654053
VERSION     WP_284654053.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..486
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55201
     Region          116..473
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrrsgwrhan glfvkifvll limlvvsygl fgfitglffk gdlmkrqrld drmqldrigh
       61 flteakqngw ndemvmagle ltvprhvrsl yiihqatgnv rykledetgp yrldeariqe
      121 vlagiadgry fgeetfgrgk tvlvgqtlrv dgegdfvllt asnlfqrdvr iwneplwigi
      181 gimlscgalf afmlsnhlsr rvkkleaasr siakgqfqie ipvhsrdelg rlaraleqma
      241 qdlgsldrmr kefvanvshd mrspltsmng yleaildgti ppermakyir ivqeqnkrli
      301 rlvndlldia kieagqfqis pvtfnmtekv rqvlarmdpq lskhevvfdq adadrdlwvh
      361 adpdrieqvv vnllqnaiey srpgtritvr iskadakhav vgisdqgigm eaedigriwe
      421 rfyktdkart rkngagigls ivkaildqhr mpievysipq qgttflftlp lteldpeqtk
      481 grerse
//
LOCUS       WP_284654188             201 aa            linear   BCT 25-DEC-2024
DEFINITION  SRPBCC family protein [Paenibacillus thiaminolyticus].
ACCESSION   WP_284654188
VERSION     WP_284654188.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..201
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=22895
     Region          81..199
                     /region_name="SRPBCC_CalC_Aha1-like"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of Micromonospora echinospora CalC, human Aha1, and
                     related proteins; cd07814"
                     /db_xref="CDD:176856"
     Site            order(81,83,92..94,96..97,102,112,118,120,127..128,130,
                     133,139,141..142,155..156,158,159,169,171,173,175,
                     184..187,188,190..192,195)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mvgslcreai lantgqawee wiqqldrgvd pvwsherivr hiageydvpp ewsdmlally
       61 gqklgrvpvg qtasagvqig vrrtmpiske kvwtfllsse glscwlgslp slplevrhey
      121 vteegtrgqi rsvipeqklr ltwqpqgwdr pstlqlyvls kspdkttvsv hqeklddiym
      181 revmrrhwea aldriqsrli g
//
LOCUS       WP_284654262             475 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus thiaminolyticus].
ACCESSION   WP_284654262
VERSION     WP_284654262.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..475
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52635
     Region          132..465
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mlkpgirrsv vmhyfivvfl tmlileaifl iavrsyyyds isshmsshls vttsfyqqgn
       61 agvntqdrsw lpvllkqynm kkaevqilsp qgevlisssy frvdkpvata dfisaqsgtv
      121 gkwigkqpgt geavmsiasp iyakgdivyi vrlvtsldlv narinsivll svviaiavli
      181 vvliisigla nsivkpinei tsasaqmakg rfdvrikeey qyeigelart lnfmaheivr
      241 snqlkndfvs sishelrtpl tgikgwsetl lsgqfeeees klgmnvilke tdrliglvee
      301 lldfsklqen klqfnwspvy lsgiledtvl qvkmkaeqkq ihievrsrga eqpisgdanr
      361 lkqvflnlid navkfspnes vitvhstwde nnvvvrivdq gigiseehla kvmdkfyqvn
      421 pshggtglgl aityelvkah hgdmtieskp dvgttvivtl pihqpaasep eeekq
//
LOCUS       WP_284654266             303 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284654266
VERSION     WP_284654266.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 303)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..303
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35741
     Region          213..301
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtyhvridys svyeligsfm lfvhrkwirn vengmewars ieqqlppqwn aysekirkhs
       61 lsdfdmlyal alernhndip syleqleqlt paewdrvgle nglrlgsfql ercldlyvpa
      121 lrfwyehyir hslpewepil lhdaeekrrl ldkikpqdli elatngvvip ehesldevil
      181 apmwhyrpin nnctfrsril ilypvdkpep dlmvpshnlr rmtealadek rlrilrlvgq
      241 kpytfeeiqe yiplstgalk hhlavlrsag yirtywngkv qrislrpegl adlsafleay
      301 ihs
//
LOCUS       WP_284654322             325 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein [Paenibacillus thiaminolyticus].
ACCESSION   WP_284654322
VERSION     WP_284654322.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..325
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36380
     Region          10..322
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mtnaisdkah kipvvilagf lgsgkttllq qwlqwsldag mkpavvmnev gevnldgqll
       61 pedvamtell ngciccsmrg dfslklyelv qserpdiiyv ectgiaqpme lvdsiteisl
      121 ysdvvlnhiv tladashlna mldegekpnr klmnllqeqv raaqlillnk adrvneaqle
      181 avqrelrawn aeadmlvter aaidrsrwqd airtgdapve qeakpgcaps hhahdkvtvw
      241 traipravds erferwllgq psnvyrakgi vtftdttkry mfqyayrate fvpimpqgev
      301 edvivmigeq mdvaelersl rdicq
//
LOCUS       WP_284654550             554 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus thiaminolyticus].
ACCESSION   WP_284654550
VERSION     WP_284654550.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 554)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 554)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 554)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 554)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 554)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..554
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=61085
     Region          1..550
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 maankkrlfs vwnlssilil avfllfilfp lvlvlkksif dpytgeltls yfskfferkf
       61 ywitlvnsfk vtlvttalsv aiglpiayvm rkvkirgsky lqiliiisyl sppfigayaw
      121 iqllgrngvi tqfindlfhv qlngiygfpg ivlvmtlqsf pliyiyisga lqnldnslne
      181 aaeslgyssv qrvfkiivpl imptvlasal lvfmrviadf gtpmligegf rtmpvliytq
      241 fmsevggddg faaalcvlii llticlfmvq rilaryysys msalkpmvpe qskgmkniia
      301 hgavyftvll ailpqcvvif tsflatrggq vftsgfslns yrdilfnkdt svifntylig
      361 iaailiivvc gimisyltvr krnaltstld tismfpfiip gsvlgisflf afsqspllls
      421 gtmfimimaf airrmpytir sstaiisqis psieeaaisl gasetkaftr vivpmmmpgv
      481 iagaimswit viselsasii lytsktqtlt vsvytevirg nygnasayst iltltsilsl
      541 ilffkltgkk disv
//
LOCUS       WP_284654590             420 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus thiaminolyticus].
ACCESSION   WP_284654590
VERSION     WP_284654590.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 420)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 420)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 420)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..420
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=47414
     Region          13..413
                     /region_name="KinB"
                     /note="Sporulation sensor histidine kinase B [Cell cycle
                     control, cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG5806"
                     /db_xref="CDD:444508"
ORIGIN      
        1 midsilsqef kgllyimsac lmfllitpqf mfanyrrkml figillvlty fyiryekihp
       61 fvygihltpi sltlaalfeg flpgivtwla fnvitvlllg envlatavgs tlllvmglff
      121 hyrhmlqsty wqicllavtl tttyllgyll cftqwehltg idagvavvgt ylsamyvsyi
      181 yhhvknqekm reelfraeky qvvgqlaasi sheirnpltt sqgflqlmkk enltpeqfen
      241 yhrhavagie qanaiitdyl nyakpvvela qplhvqkevd dvvamiaplc alsevkvntq
      301 hltkcpryvs geskklqqcl lnimknaves mpsggeltvt twsdnegvhi hikdtgvgms
      361 esqikrigmp fyttkekgtg lglmvviglm kamngkvsyy srpeegttcv lqfkqvrlfr
//
LOCUS       WP_284654661             171 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Paenibacillus thiaminolyticus].
ACCESSION   WP_284654661
VERSION     WP_284654661.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 171)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..171
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19052
     Region          58..136
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mnihlqpita gnwgecialk vgsgqegfia snlysiaeaq fldgfqckgi yldehmigfa
       61 mygidpddgk ywiyrfmvda sfqgqgygkr alqlvldeig arpdrtehcl lgydpnneaa
      121 rrlyasagfv etgiapwgem makyefpglt rwtrrdqari akkpnseeag r
//
LOCUS       WP_284654846             294 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284654846
VERSION     WP_284654846.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..294
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33763
     Region          29..279
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          188..272
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdsihfpilt deerllplvv ttvgswtnql etirphgypd yqwlqcttgr gmfqwegggp
       61 aveigpgqgv llypdvphvy rpleepwgiy wlgyhgalaq eltsmvhvhh saamtvgdpe
      121 qtlalirrai swldrasggh gprlsaltye lmmawsecgr hdrglyrksg vqplapllew
      181 ihehyqedvs lqqmadrlqv spqyvctlfr rtfglrplqy vnrlrirksk elliscpdma
      241 vahvgkeagf rhasyfiqrf kqqehmtpvq frqmygrlpy kpdeqermll pdsm
//
LOCUS       WP_284654870             211 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284654870
VERSION     WP_284654870.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..211
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24362
     Region          9..210
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mkqsdskmst rqqmlmllkt ngamsaaqla ielnmtemgv rrhlytleee glletemvrq
       61 pmgrplrtyr lstqgdeqfp kqyhqlvldl lkemevwped egigklfesr kqsllakytp
      121 qmgqsslder vealgtiqdh ngymveteqe edgswllhey ncpiaqvaqh ykqpcacela
      181 lfrelldadv trteciaeqg qrctyrirkr i
//
LOCUS       WP_284654929             503 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfatase family protein [Paenibacillus thiaminolyticus].
ACCESSION   WP_284654929
VERSION     WP_284654929.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Sardiello,M., Annunziata,I., Roma,G. and Ballabio,A.
  TITLE     Sulfatases and sulfatase modifying factors: an exclusive and
            promiscuous relationship
  JOURNAL   Hum Mol Genet 14 (21), 3203-3217 (2005)
   PUBMED   16174644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..503
                     /product="sulfatase family protein"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=55487
     Region          24..459
                     /region_name="ARS_like"
                     /note="uncharacterized arylsulfatase subfamily; cd16143"
                     /db_xref="CDD:293762"
     Site            order(32..33,72..73,127,129,247,299..300)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293762"
     Site            order(32..33,73,127,129,247,300)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293762"
ORIGIN      
        1 msmngnanmn rsknqmdank sthpnviyil addlgygdis clnpdsriat phldrlgreg
       61 liytdahsss avctpsrysi ltgrynwrse lkegvlwgys psileegrmt vaslfkqagy
      121 rtacygkwhl gldwhrtgpa aedvdfsqpi rrgpvdagfd efygisasld mppyvyiend
      181 avvqlpdrlt rnddkkgfwr egpvapdfrh eevlprltgk vlerieqfss aadgspffiy
      241 yplpaphtpi vpapefvgrs gtnlygdfvl mvddvvgaim rkleecgiad ntvvlftsdn
      301 gcspsadyae laryghnpsy vfrghkadiy egghrvpllv rwpariaaga vsgepvclvd
      361 fmataadvtg qtlpddaged svshlplwlg tngteplrea ivhhsidgsf sirkgewkle
      421 lcpgsggwsd papgqeppgs psfqlyrlsd digerqnvid rfpdivqelt alltryikeg
      481 rstpgapqpn kgmprwsqlh wme
//
LOCUS       WP_284654944             578 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus thiaminolyticus].
ACCESSION   WP_284654944
VERSION     WP_284654944.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 578)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 578)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 578)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 578)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 578)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 578)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..578
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=64073
     Region          30..573
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mipkrnikpr kpgiapfrpi sitqspyfvy vlvaplflvl layvvyplfq tfmqsiqaed
       61 qlslhnyarf fslehtsnle alwtsiyisv lsvitcaivg vamafllery efpgrkilav
      121 lvlvpmalpp lvgvlsftfl ygesgiipra lkellqleqv pfalkgiwgv lvvhtftmyt
      181 yfymtassai rnldpsleea aaslgagrly iwrrvilpml tpalvassll vfmiamasyt
      241 aplifgiert mtmqiylsrt ngnldmaaaq stilsvvsiv fllvmrwyqg lrnyqnmskg
      301 vsvhrtevks pagkyvamll siagvivlll pilvlvlisf sadgrwttqi lppeytvehy
      361 vklftdsktw rpiansfqms fvatignvif gvaaayamvr lsfrgktlld vlimlpwalp
      421 gtvvavnlia afseptafsf nqvligsfwi lplayfvrhl plvfrstsat lvqmdasvee
      481 aarnlgasww ysfrrvvfpm alsgilagtl lafvqgigef vssillftak stplsveifq
      541 rmysfefgta caygvlqisl iiivlfisrk itgdstam
//
LOCUS       WP_284654969             302 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Paenibacillus thiaminolyticus].
ACCESSION   WP_284654969
VERSION     WP_284654969.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..302
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31924
     Region          8..286
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mklfryallv figacsygtl ssimklgige gytvpqiigs qyffgwllla saallfsrrr
       61 vsgkqvlvll acglsvscts isygiaveql pasiavvflf qftwigvlle allnrnwpdr
      121 akllsvlill vgtvlaggla dhglsgltak gaifglisav sfafyimvng rvatdmpiln
      181 kslslttgaa aslflvfppt fladgalasg lwkyglvmgl lgvlvpgvff glgvpkigpg
      241 lgtilgaael paavimsvtv lqeqvswlqw agialifagi clpqfafvrq erhrralart
      301 rl
//
LOCUS       WP_284655005             461 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus thiaminolyticus].
ACCESSION   WP_284655005
VERSION     WP_284655005.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..461
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=49831
     Region          81..461
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mgirqrlvgs ylavilitvs ilevfliasv dyyyhysvrr ilvnqaeisa affqqyfsgq
       61 dvaeqserll rgfsqnttaq vqiidasgql lqdnvnvqai gsridypdvr qardgemgiw
      121 rgtsassges llavsyplvt dgktvgvvry vasltstvat irwiaavcia agllvvaiva
      181 lvsvflsrti tgsiqelkla adrmaegdls aragkrykde lgaladtlnt masrlqrsdq
      241 lknefissvs heirtpltsi kgwavtlksa gddskdllee gldviesesd rltelvdell
      301 dfsklangki tlsrgpvqlp ellrhvgtql aprasrlgle levrggdavp vidgdanrlk
      361 qvlinlldna mkftppggni tmradalkec vivtvedtga gipeedignv lqkfykgnns
      421 eagsglglsi cheivklhgg hlrvesepgr gtkvqvflpr r
//
LOCUS       WP_284655080             372 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284655080
VERSION     WP_284655080.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..372
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41555
     Region          6..368
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mkkyypiaap ilngnekkyv adcldstwis sngsylgmfe qqfaafcqtk haitcsngtt
       61 alhlaliahg vepgdevivp tltfaatana vaycgatpvf vdsepetwnm dpkavvrkit
      121 prtkgiiavh lyghpvhmdp imqaarehgl fviedaaeai gaeykgrrag slghtaafsl
      181 fgnkiittge ggiittdddd iaenirlfkg qgmdkfrkyw htvigynyrm tniqaaigca
      241 qvenidwhiq qrirvamhyy dclqyderis lpvqkvwskn vywmmsvvln gcseakrdrv
      301 merlkedgie trpffypmhi lppyrhlqph tefpvanria aqginlpshg ilteedihwi
      361 ggklqsaldk es
//
LOCUS       WP_284655224             439 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284655224
VERSION     WP_284655224.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 439)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..439
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47772
     Region          57..423
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(172,174,294,296,326..328,365)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mtkrssllml afvlalsmll tacgsggags sespgketgt pgtdlpegqq eqtlsgtitv
       61 wvhpyvseek kndmkavfdg viseynskyp dvkvkleeip wknreqkilt alaagngpdv
      121 fyqlpdqipq fasknvlepl gpymddnqmd dftpgalaag tyqdtlyalp ilqeaqlmfy
      181 nadiikeige dpsalpqtwe efnvwaekav akgyyardfn ggsaccnatl ypilwqqggd
      241 vitgsgeivi nneagirtfq mikdmydkgw ipkdsisnqd qsaeflsgkm lavwgsgftq
      301 tvlkeekfny aagpplkgae qasfgtvgmf avpknsknkq aavefikvlt nteaqkkfnk
      361 lanyiptrks assiyegdkd meifltvtdy trpgvmspva rtimpkiqae laamleggks
      421 pqeaadaaak aiqddmnks
//
LOCUS       WP_284655307             324 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus thiaminolyticus].
ACCESSION   WP_284655307
VERSION     WP_284655307.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 324)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..324
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36960
     Region          1..324
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 msqeasavka gwsrrhrsgt gersrlwkrv rrhyqlylll lpciaffiif syipmaglvl
       61 afkeyqfnkg ifgspwigft yfkmffqdpq slqlirntli isamkvflam pfpivlalmf
      121 nevknsrlrn lfqgiaylph ffswvivigm lqrilapdtg lvnqiiswfg gdgstfflme
      181 ekafyptmfw syiwkdvgws siiyfaaivg ispslyeaak mdgankwhqi whitlpgirp
      241 tiivlfilsl gnilsagfdq iyllktpgnm nvseildtyi iymglesgqf gfgtaigmmq
      301 gvvglilvlt vnrvakkwfq sslw
//
LOCUS       WP_284655340             383 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284655340
VERSION     WP_284655340.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..383
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43583
     Region          71..355
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mktdtqagac qpqydlakld tllhedhiar nfrsmdhilp khdilapadk frfsenlqhq
       61 ddvrysyngq astvreymek vkatawliik ddaiiteryy ngytrestat smsvaksfvs
      121 almgiafdeg amrdvhdpvt rylpelagsg ydgatikdvl qmssgvrfne dyadpdaeiy
      181 tfmndvfges ampiseyvrk ltrmqppghy qyksvdtqvl cmllerttgk kvsvyleekl
      241 wqplgmeyda ywntdlhgnd iafaflnaal rdyakfgrlv lhqgawngrq iisekwmkes
      301 vipdradlqp gqaeecfgyq yqwwtphgsd gsevmargiy gqhiyinrrh havivksgvd
      361 ptvfnvhdge avtayrtile hlg
//
LOCUS       WP_284655376              74 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284655376
VERSION     WP_284655376.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 74)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..74
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8376
     Region          1..69
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mivnklselm grkrlkvadv vrmtglarnt vadlyygrss qanfetlnrl ctalecnled
       61 ileyvpddeq epre
//
LOCUS       WP_284655505             221 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Paenibacillus thiaminolyticus].
ACCESSION   WP_284655505
VERSION     WP_284655505.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..221
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=25825
     Region          <55..203
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          68..94
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          100..128
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(101,104..105,108..109,111,137,140..141,144..145,
                     147..148,170,173..174,177..178,181)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          135..164
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          169..197
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mskflafgml fwllgnpiaa iivlllilyv ldrrfvglsp sllkplkrrs rigklkqqlg
       61 tnphdvsakm elarllierr ayrearqwle plqetmdhsa efwddlgtcw lhtgeperge
      121 aairkaleln prvkygqphl rlaslyaatd knraiealqa yqevhsssce syyrlgqlye
      181 qldrkeeare awkqavaiyr slprykkree rkwmlksmlk r
//
LOCUS       WP_284655550             227 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Paenibacillus thiaminolyticus].
ACCESSION   WP_284655550
VERSION     WP_284655550.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..227
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25058
     Region          3..208
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 msikaialdf dglivdteta sydsfcelvr sfdldmplev wkewaggiqt wqlacdylde
       61 qlgkpvdrea lhrrhremyt alieeldvmp gvkqlledar riglrvglas sasaawaveh
      121 ikrcglidyf dvlqtrddaa kvkpdpeiyr kaveklgvqp eetiafedsl vgtlaakaag
      181 lsciavpnrv tglfsfehvd lqlasladms leeiictleq srsaaqg
//
LOCUS       WP_284655561             303 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus thiaminolyticus].
ACCESSION   WP_284655561
VERSION     WP_284655561.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 303)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 303)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 303)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..303
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34146
     Region          3..303
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mtqsqlwkri wkhkvfylfl lpgiiwfilf syiplfgiqv afrdytfsgg itgspwaglk
       61 yfeqffdyyq snaiirntim isllklligf smpillavll nevhntrfkk vvqtlsylpy
      121 fvswivvvtl lqrlltpygg pvnglldlfg igpiqflynk twfyqiiiss diwknigwns
      181 iiymaaiagi dqqlyeaakm dgagrfrqiw hitlpgirnv avilfilscg simnagyeql
      241 lllngpatas igsvldvhvi taglregrls yaaavglfqs liglililiv nqiarkksdv
      301 slf
//
LOCUS       WP_284655656             411 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284655656
VERSION     WP_284655656.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..411
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46252
     Region          18..411
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mtkqgwkkkw ialiaggall ltlvpptvge aseldkvnkq lqdlqrqmqe aeqkqqeada
       61 qkaqaeklik kttkdlnyvv geiekktkem ldltleidqt eanleeaaqe ledikhriae
      121 reklldsrvq lmytngavsy idvlfsatsf sdfvdrldsm qtiasrdkei ltehkrdkel
      181 avvkkqeiet elkrvkllya kldeakknlq lkekekkvmi asyekeaedn hgiseeqerl
      241 lmefakqrae lirkknelna qrqqrktgqt srkvytysgg klglplqady yisspfgyrt
      301 dpitgaksaf hsgidmatpg gtpiyaaedg avivaewygg ygncviidhg nglwtlyghi
      361 rpggikvqkg divkrgdkia evgqtgratg nhlhfevrln geqvnpdtyl k
//
LOCUS       WP_284655671             473 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus thiaminolyticus].
ACCESSION   WP_284655671
VERSION     WP_284655671.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 473)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 473)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 473)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 473)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..473
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52163
     Region          2..468
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mnsiiaasct tvmsvilafc layiidrshi kgkeiwrtlf vlpmlvpsia hgfglinlfg
       61 dngfltqafg inihlygmkg ivfgsviyal piaflmfsdi lryvdsgvyd acrtlgipka
      121 nvffditlgl mkkqflivss tiftmvftdy gvalaiggkv stlpvllyre viglldfskg
      181 gfiailllip aiitftlgrk tnnveldqvn gpeytaitnk trdilytiic aitafivlmp
      241 visytvmglv eqypknmtft wkhlqaviyg gagktiynsl vislstalig tsiayliayv
      301 sirlpnkfma raiyslsvvp lvipgivlgl gyiqffsftp iygtafiiil vnivhffstp
      361 yllaynsqik ipkeleqaas tmgikpmkyi rdilvpttgg tiiemfsfff insmvtisav
      421 aflsntknmt ialminqyea qmlfeeasvv vllilcinla fklivsqlkk hlf
//
LOCUS       WP_284655743             363 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Paenibacillus thiaminolyticus].
ACCESSION   WP_284655743
VERSION     WP_284655743.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..363
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39673
     Region          6..361
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mneswnrlrt amdqeghdal litdpkhvyy ltgfacdphe rflglviqrd aeptlivpal
       61 dadkaasass vknivthtdt dnpydvlkpc lpaglkqlaf eknhisvarf ealaaaldak
      121 ryadagpilq elrvikspee verlleairv ieavllegvs rvrpgiteld vvaeleylmk
      181 kkgaerpsfd tmvlageraa lphgvpgnrv iregelllfd lgvyvngyas ditrtfavge
      241 vneesrriyd tvlaaneaai aavkpgvtfg sldrtarqti edrgygpyft hrlghglgld
      301 vheypsvhgr nedvlkpgmv ftiepgvyvp nvagvriedd vivtedgvrv ltsypkeltv
      361 igg
//
LOCUS       WP_284655759             453 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus thiaminolyticus].
ACCESSION   WP_284655759
VERSION     WP_284655759.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..453
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=51021
     Region          140..452
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mmrtlyvrvv ltflfaviag iivaftasgf fferemreiv frdltqlgnd mvrlyqqvpe
       61 aefrdyldsl asfewtqvhv fdskgdptvq hvlagrppes ieaqvvkdvl sgrpyhstep
      121 estepvigis flkegepyal flrmkyrddn lisrlilftl avvlaagslc flvaaryvvr
      181 pikkmteatk rmakgdfstk lsfrrkdeig vlaasfnhma qelgqmeqmr qdfvssvshe
      241 iqspltsiyg fskalrnrvi seadqdryle immtecerls rlsdnllqla sldsehhpfa
      301 priyrldgql rqvivaaepq radkalrled rledvtiead edlmslvwtn lignaikftp
      361 engritvsla rqdgralvti adtgigmaee drarvferff kadkarkrna ggsglglaiv
      421 kkivilhhgt irldsepgqg ttvsvmlpir rns
//
LOCUS       WP_284655802             331 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Paenibacillus thiaminolyticus].
ACCESSION   WP_284655802
VERSION     WP_284655802.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..331
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=38386
     Region          59..254
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          116..146
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          151..179
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          184..213
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          218..246
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtqnahqepa qdptdtepcp paaqeqtpaa deansdcgre eydqhtiryl qqaiqrinql
       61 yqrqeyqeal reamqlqley pehptimsla avvhkpvdpd kaldwageal rrdiyqpdaw
      121 rvrmgiyydr gewvafetaa rqliamapdd ptphlllaqh qmrkgaleqa vlslercidi
      181 epaglayaty syvlaqldrt veskeaerqa lameeehayt lmqlawaadq rgekshslrl
      241 mekavrldpe dsqvreeyme tlqkanlafr lvwlpaqwfq klnpwilfvi wvlfaylkpv
      301 llvafvllhv sthwisrwyv nwkvygrpwa s
//
LOCUS       WP_284655880             319 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Paenibacillus thiaminolyticus].
ACCESSION   WP_284655880
VERSION     WP_284655880.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..319
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35085
     Region          10..300
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mdlsrihsla qaikrnvqqv ivgkddtldr ifvalftggh vlledvpgtg ktllaksvak
       61 sidgtfkriq ftpdllptdl sgmnvynqkr gefefrpgpv ftnllladei nratprtqss
      121 llecmeerqv sidgvtmqle epfivlatqn pldnfgtfpl peaqldrfml klklgyptfe
      181 eglrilsrfr tedpiqelap vatredikaa rsgytqvhvd daileyvlgi vertrshpdi
      241 algasprasq allravqaya virgrdyvsp ddvkamaapv lahrlllhha agsrddqaes
      301 vlaqivsqvp vpaearaae
//
LOCUS       WP_284655885             303 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Paenibacillus thiaminolyticus].
ACCESSION   WP_284655885
VERSION     WP_284655885.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..303
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=33368
     Region          18..>303
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mnamtngltl pgyevdkiis epvngvtlrs yfemqpvscn eflelgigmc rmiealhqqq
       61 vlhlnlkpdt ilvqmvtkri yvtgfgyalf lqqgerqpmk rpllegnpiy lspeqtgrmn
      121 rdlgpysdly slgvtwyell agelpveadn alawshahma rrpvplterr pelppelaei
      181 vmrllekdpe arypdarmlr valeeclegr rnsraselpe gtlrdqaapa rqlsvtalyp
      241 vdpgpgrilp hpalgqagda plfgltgqva gddsggypqt ldlaavvqss hsfaegwegw
      301 gla
//
LOCUS       WP_284655906             364 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284655906
VERSION     WP_284655906.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..364
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=38735
     Region          12..356
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mtkvntelck tlniaypivq agmaggpttp dlvasvseag algtlgaaym epediraalr
       61 lirqrtakpf avnlfaadmt ddasriaevn dvlrgirsel elgepapelh tpdrfeqqmq
      121 vlieeqvpvi stafgilpar fmedvkrrgi kvttmvtmvr eaveaerags dvivaqgsda
      181 gghrgtfdig lhpnganigt fslvpqiadq vrvpvvaagg vmdgrglvaa lalgascvql
      241 gtrfltaaes gahraykqal ldsteestvi trvfsgrpar gisnafirrf desgveplpf
      301 ptqnsatnei rkaaavrnea dymslwagqa trlltdgdpa srivmeimee aqqllselpa
      361 lnqa
//
LOCUS       WP_284655926             336 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284655926
VERSION     WP_284655926.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..336
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34788
     Region          29..332
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mmketkrslp ltykwlagll vfaatflvam rfgaadttlr dvwlaltsra tdehialiqe
       61 irlpreiaaa avgaalavag aimqgmtrnp ladpgllglt aganaalaia iallpgagyl
      121 tmaaacflga aagagmvfgi galrrggfsp lrmvlagaav sallyaiaeg valyfkiskd
      181 vsmwtaggli gmswvqlqav gpfialgivi alllarqlti lslneevavg lgqktnrika
      241 llfvvivlla gasvalvgnl tfiglmiphi vravvgtdyr yvlpmsammg asfmlladtl
      301 grtihapyet pvaaivaivg lpfflfivhk ggkafs
//
LOCUS       WP_284655935             296 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Paenibacillus thiaminolyticus].
ACCESSION   WP_284655935
VERSION     WP_284655935.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 296)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..296
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=34192
     Region          70..290
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 melrdrnglt erefldqyra gdyerpsvat dmviftvtdt aeenyrklpe kelrilliqr
       61 gghpylgqwa lpggfvrpve tteqaaqrel reetgvdnvy leqlytfsep grdprtwvms
      121 csymalidss qvrveagdda dnaawfqvsy rllreskell edgylktrqy eltlvngddk
      181 ltavverkit stdkayatdy aivsneglaf dhakiiacai erlrgkveyt dialhlmpkl
      241 ftltelqqvy evildrellk aafrrkvahl veetdhften aghrpsrlyr rsweri
//
LOCUS       WP_284655962             502 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Paenibacillus thiaminolyticus].
ACCESSION   WP_284655962
VERSION     WP_284655962.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..502
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=57958
     Region          8..>295
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mvkvsqqrlk klyvvqlknl nnleidfsss pltaivging sgkstvlhal accfkpvder
       61 nfynykfsyf ftptpdsiwq gslltithdy rydknfiene qttfskntdr wapkydrrpp
      121 rnvvyigirs cvpkieeeyq nsfirytttp fsddisqlik ekagvimnrd yssynlhtst
      181 rtnylgvelg dirysslsms ageqrifkil tevynapkys lilideidll lhsfalkrmi
      241 kvlyeraivk nlqiiftths pnilseqeli nirhlyntpe ktlcfsdtkp dtiyrmtgeq
      301 ekpleifled dlaqtivdhv aeslnlskyv nttrygaain cfsvaaglal snrltdnclf
      361 vldgdeyntd fkkeerinav itgntehshk mrrevlsqit qfnlpegfsp eryihfllke
      421 lrnkyvqnqi idcaieirkv dnthkyvddi lerigfanra vglskvvelv snhekwsdfv
      481 spikewlkdi ahkvvevpik vs
//
LOCUS       WP_284656045             255 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Paenibacillus thiaminolyticus].
ACCESSION   WP_284656045
VERSION     WP_284656045.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..255
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27813
     Region          1..251
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(26..27,29..30,33..34,71,75..76,79..80,110,114,121,
                     124..125,130,145,149..150,152..154,156..157,160..161,
                     164..165,189..190,192..194,196..198,200..201,203..204,208,
                     211..212,218,220)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(148,152,155..156,158..159,203,206..207,209..214,
                     217..219,223,225)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(169..176,191,194..195,198)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mksmslyvek dsaihrvdpi tklayiatai aipiivpslh aawvcmlisf gllaaggvfr
       61 rglavmgfvg fvlvtvviiq gffhvgnetv lftagtwpfy kegllfalgi sfralnivga
      121 flilvlttkp sdlvealvrk glsprigyvl nsvfqiipqm matvgtitda qrsrgveteg
      181 rlmtrikafl pligpvvlss lldtkertla lqargfnvpg rktflneekr yrhsgilrla
      241 mlvivaaall wrifa
//
LOCUS       WP_284656423             858 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-mannosidase [Paenibacillus thiaminolyticus].
ACCESSION   WP_284656423
VERSION     WP_284656423.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 858)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 858)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 858)
  AUTHORS   Nascimento,A.S., Muniz,J.R., Aparicio,R., Golubev,A.M. and
            Polikarpov,I.
  TITLE     Insights into the structure and function of fungal
            beta-mannosidases from glycoside hydrolase family 2 based on
            multiple crystal structures of the Trichoderma harzianum enzyme
  JOURNAL   FEBS J 281 (18), 4165-4178 (2014)
   PUBMED   24975648
REFERENCE   4  (residues 1 to 858)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 858)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14312054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..858
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..858
                     /product="beta-mannosidase"
                     /EC_number="3.2.1.25"
                     /GO_function="GO:0004567 - beta-mannosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005537 - D-mannose binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=99324
     Region          6..>679
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          685..770
                     /region_name="Mannosidase_ig"
                     /note="Mannosidase Ig/CBM-like domain; pfam17786"
                     /db_xref="CDD:465505"
     Region          775..848
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; pfam17753"
                     /db_xref="CDD:465483"
ORIGIN      
        1 mrlnenwklr dfnvgeerdl evaspeyvdy fwmtakvpgd vhttliekgi iedpfyghnd
       61 qtcrwveekv wwyrttfhwd gqredmdrme lvfegldtfa tvylngvelg stdnmfishs
      121 fdvtrelnkg knvlavkldp vhlhvkskmq yywsgfskkr iwtrknqshy gwdwgprlvc
      181 agiwkdvhlv krsrayvdnv fahtvevkdg eamievavea rvfdrrgact aevalldaeg
      241 rqvagqtfvl drglgfmpdg aicahglsgs arlrvpnprl wwthdlgepy lyrldvtlrn
      301 ggdavderqq rfgirtldlm lhdeegqhaf tfvlngvklf akganwipid sfiaavpder
      361 ysryirlaqe anmnmlrvwg ggiyerdify eecdrlgllv wqdfmfacal ypdynrnfmd
      421 nvrreieqvv krlrsrtcla lwcgnnendw lyealhssge iphpfygeki yhelmpalle
      481 tldptrrfwp sspyggndhn sreigdthnw qvwhgniepr vfgepqlqdy sveglsfkkf
      541 kgdttkfase fgmhassnry tlqrnipesq fywgsdemmy rnkdihhpkg illmegytga
      601 ptnmeeyiny smltqaeglk ygiehyrrrk pdtsgalfwq lndcwpgtsw svidyyglpk
      661 aayhyarkfy apvlltadhd agralhlwai ndrlepyedq vrlavyrmdg mklyereyev
      721 clepngkrel dalseaeltn gadpaevvcl issgsglted nyvylrdyke mhfepaqlqi
      781 svdeeagvir ietdraarmv kieldeawia asdnffdllp grakeirvsq aegkripwet
      841 lrvtalnspe avngddgr
//
LOCUS       WP_284656451             452 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284656451
VERSION     WP_284656451.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..452
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48932
     Region          9..452
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mntqessvfl paaerngtpk elffiwfasn igilgvvyga mivgfqlsfl qsllaaaaga
       61 lsfalvgyls lagrdtgatt fvlsraafgf kgnyiptfmg wlnlvgwlav nvvtgtltll
      121 alfnvfgiss nqfltvisll ifaaliivss vfgqdalvki qtfftyvfgg ltllvllili
      181 pktnwpelmn msngdwltgf lpavsiiiag tgiswsiaaa dyscyqkptq ssrsvftrvt
      241 fgafiplfvi msvgvlmsts vpdlaasanp ievisqalpr wmtilyfvta lgglipqcii
      301 slksarvnle tlnirvkdst sviihaiimi lipiytlfvs enfmgnfqtf lgllgigmaa
      361 waatflidyv kirkaagydq rlladpdynq anyrgifswl agvivgfmft nspffdgpfa
      421 rgifqdnslg vllaftvsal iyfillsans rk
//
LOCUS       WP_284656454             485 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus thiaminolyticus].
ACCESSION   WP_284656454
VERSION     WP_284656454.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..485
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55789
     Region          111..484
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mkikhwlmlc flvvmllpvl agyvfyqsih tyderqelke yiemtgrlae iepllqdvsl
       61 yrvqpderfa alqreasdsl kitlyrvdgv tvfssmadsl tpklyrvrpe vlyehlyemr
      121 kshraytlkk pvfdqeklag fyeitmvrdq wleafqhrtl ivaggwvlff lllyaaaifa
      181 lhrklirpmq glmrqmaafa ngeaapnpvh rakdemgeli grfhemraqi ecarehlsae
      241 qrereymvaa lshdlktplt slrayaealq qegelseeek sdyyavlfdk iahmrrmldn
      301 ltmytalkss ekleervevd gdelfemlfs gydglcaqrr irlavdsavs gpyymnaqqm
      361 irlvdnlmsn airytdsgrs iwlgaysasq plpdwifpti mdevqawrge rlillvqnqg
      421 aaipaeqler lftpfyqpds srtkahagss glglsiakmi vekhdgdiri wseasfgtlv
      481 acrfr
//
LOCUS       WP_284656539             384 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Paenibacillus thiaminolyticus].
ACCESSION   WP_284656539
VERSION     WP_284656539.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..384
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41586
     Region          26..315
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 memgghqnrt aeqdvwlasf aergwpafld rmgqvvagkr evirlaglam lsgghilmed
       61 vpgvgktlla ralartaggs frriqmtpdm mpaditgsmi wepasgglry segalfgnvv
      121 ladelnrapa rtqsalleam eegtvtvdgt tralpqpffv iatqnplafe gtyripeaem
      181 drfamrlslg ypgaeqeagm llhqqeespl arvkplwtpe ewqllvrrir qvhldatlcr
      241 ymadiahatr ahpavklgis pratlslmrm aqahawtegr tyalpedvka vahpvlghrl
      301 hlqreallag tteadvvadv lrttpvpvfp ealagggraa akssrreerr ipaagaapmv
      361 qvplagdgsa qpaagrfrfg gwfr
//
LOCUS       WP_284656633             551 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus thiaminolyticus].
ACCESSION   WP_284656633
VERSION     WP_284656633.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 551)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..551
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=60383
     Region          1..547
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mkgthkrfdv wtnisflifl fyvlflalpl ftmliksvyn gttgefsfay fvkffskpyy
       61 lnalfnsikv tvcvtalaai iatplayima tvkikgnsti rililissms apfigayswi
      121 lllgrngvit rfvsntfgit mpdiygftgi lvvltlqmvp lifmyvsgal knvdqslmea
      181 aesmgykgfs kmrkvllpli tptllaggll vfmraladfg tpmligegyk tvpvlifnef
      241 isevggddgf aaaisvivvl fataiflmqk yishrnsftm salhpieakk kkgigniaah
      301 aviylytfia llpqlyviyt sfqksngrif vdgyslqsyr dafnnigsvi tntfflaiis
      361 lvviillail iayvtvrrkn altntldift mfpyivpgsi lgiallitfn nkplilsgta
      421 limiisfvir rlpytirssa ailhqisdgi eeaaislgas kmktffkitl pmmlagvvsg
      481 ailswitiit elstsiilyt gktktvtvai ytevirgnyg vaaalstilt iitvvsllif
      541 lrlsgqkels l
//
LOCUS       WP_284656670            2402 aa            linear   BCT 25-DEC-2024
DEFINITION  amino acid adenylation domain-containing protein [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284656670
VERSION     WP_284656670.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 2402)
  AUTHORS   Konz,D. and Marahiel,M.A.
  TITLE     How do peptide synthetases generate structural diversity?
  JOURNAL   Chem Biol 6 (2), R39-R48 (1999)
   PUBMED   10021423
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01733.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2402
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..2402
                     /product="amino acid adenylation domain-containing
                     protein"
                     /calculated_mol_wt=262316
     Region          7..>2115
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
     Region          2141..2367
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mhdlddgrwp lsgaqsgiwf aqqldpdnpi fntgeyidir gpvdpdrfet avrqavmeae
       61 alhvrfgedq dgpwqtlvps sdwtmhridv sseedphaaa ealmkhdlaq pvdlrrgplf
      121 tealfklapd rfywyqrihh ividgygfsl ltrraaqiyt alahdlplse gafgswrsvl
      181 eedaayrase rlerdrqfwl arfadhpeaa slgeraqrta rsflrqstel pssvmddwqa
      241 aasgmgtswp davlaaaaly vhrlagtddv ilgvpmmcrl gsaalrvpgm vmnllplraa
      301 vrpdmsvsel vgqisgnmre irrhqdyrhq dlrrdlklvg dnrrlfgpli nimpfieeln
      361 fagyrgsirn laagpvddlt ihvscgssgs gpridfdanp avydagelsa hlrrflhvld
      421 klaasdpgqp igrldlllpe erlqvadawn dtahglaqws vpalfeeqaa stpdavaaif
      481 edtalryadl nacanrlahl liahgagpdr ivalalprsl emviailavh kagaaylpid
      541 pdyppariay mlndaapmcl vtvqeadssl sgsglmpril ldepetrdrl erqaehnpnd
      601 adrlcrlspl hpsyviytsg stgrpkgvll tfeglanlll cmrerfaldg rdrllsvtti
      661 sfdisvmevl lplttgasid iapkdtildp qalarkikdt gatimqatpt lwqalaashp
      721 gsfdgltvit ggealpiglk lalqdldcev nnqygptett iystaallgp ertgkpsigg
      781 piwntrlyvl dgalqpvppg vagelyiaga glargylgrp eltaerfvad pfgppgtrmy
      841 rtgdlvtwla dgsidylgra dhqiklrgfr ietgeiedll vrhadvaqaa vivredrpge
      901 rrlaayvvpa spsgidpdav rryaagqlpd ymvpaaivml dampltpnkk idrkalpmpd
      961 sgqaaagrgp rtpqeemlca lfaealglpr vgidddffal gghsllagrv ilrireslga
     1021 dlsigslfee ptvaglvrrl ddsrearpai rranreddip lsfaqrrlwf lyrlegpapt
     1081 yniplaarls geldiralea algdvadrhe tlrtvfpdda sgasrqlile agearprlil
     1141 tktseaelpe rlkeavryrf rladepslra elfelgpnky vlllllhhia gdgwslsplt
     1201 rdlsaayaar srgehlawpp lpvqyadyai wqerllgsgg dadslmarql efwtrtltgl
     1261 peeldlpady prpaaashqg gtirfhinke lhgqlldlar agkaslfmvl qaalavlltr
     1321 lgagtdipig spitgrndda ldglvglfin tlvlrtdtsg dpsfrellar vrevnlnaya
     1381 hqdvpferlv eavnpvrsrs rhplfqimlv lqntpapald lpgvaaslql esadtakfdl
     1441 tvelqerrda nggpdgldgm veysadlfkr stadalaary vrvlesagaa pdkpmgqldi
     1501 lmpeerrril tewsapeaaa lppvtipelf eaqairspea aavvhegram syeelnlran
     1561 rlahllmaeg vgperlvala lprsiemvvg vlavlkagaa ylpldpdypa eriaymledg
     1621 aplcmvtnaq vssrlpeagg lprivldepa vqerlreqss anpsaqercg llsplspayi
     1681 iytsgstgkp kgvviphqnv vrlfastrhw frfgaedvwt lfhsyafdfs vweiwgallh
     1741 ggrlvvvpha vsrspdeflr llaqegvtvl nqtpsafyql mqadreqpel gqtlslryvi
     1801 fggealelgr ledwyrrhpd haprlinmyg itettvhvsy neldrdsaap gansliggpi
     1861 pdlrvyvldg alqpappgta gemyvagagl argywgrpgl taerfvadpf gppgsrmyrt
     1921 gdvakwladg tldyvgradh qvkirgfrie pgeieavlar hpevaqaavv vredrpgdkr
     1981 laayvvfaag aslgpselrr haasllpdym vpsaiigida lpltpngkld rqalpapela
     2041 lesgggnprt pqeevlcdlf aevlgvrrvg iedsffelgg hsllavrlis rirealgrel
     2101 gigslfeapt vagiaerldm dgghsalqvl lplrtygaql plfcvhpagg lswcyaglmk
     2161 hlgmdypiyg lqargiaqae elpktleemt sdyieavrsi qphgpyrllg wslggnvaha
     2221 mavqlqeege evsflamlda ypshylpirg epdeeealta llalggydkd tiggvpltva
     2281 naieilrsds salatldeat ilnlkktyen svrllgaytp rrfegdllff rstiipdwfd
     2341 piepemwipy iggrldrhdi acrhkdlcqp gplaeigatl laklnsvnge aarrdgreli
     2401 he
//
LOCUS       WP_284651447             347 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Flavobacterium terrisoli].
ACCESSION   WP_284651447
VERSION     WP_284651447.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrisoli
  ORGANISM  Flavobacterium terrisoli
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Flavobacterium terrisoli"
                     /db_xref="taxon:3242195"
     Protein         1..347
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39200
     Region          3..334
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mldyiivgsg lagiafaetl lqnnksfvvf dnhsqkstmi agglynpvil krfsqvwkan
       61 eqlelaevfy krieaklntq vdfkmpiyrk ffsveeqnnw faasdkpnls pflsteivhk
      121 kysaidspfg ygevlhtgyv dtavllnqyq aylkelglls edsfayaeln vlethleyqd
      181 lkvkhivfae gfgmhanpff kylpldgtkg elfiikapdl dldvivntsv filplgnnlf
      241 kvgatynwdd ktdlptaegk qelvdrikei ltcdfeiieh fagvrptvkd rrpllgthhl
      301 hknlhilngl gtrgvmlapa maldlydhie ngkpldktid ikrcpif
//
LOCUS       WP_284656743             291 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284656743
VERSION     WP_284656743.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..291
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34063
     Region          2..287
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mslrtiqrdl rdleelgvpl yaefgpkggy rllkekllpp ltfteneava mffayqslhd
       61 yvsvpfgeea vsalskfysv lppnakrtid rlkdciqfwv prrereapfl qqlleaaver
      121 qvmtirydsa qgenerdivp lglyahngyw ycpaycfrrq ayrlfradyi rslepresle
      181 remrrqmkkl mtfeqwflpp vrqhtvplrv eltrlgvrkc eadpwldkai trhedgtgti
      241 dtrigegele yyaerifglg tdalvkeppe lvdfivarle qlrsryrtek a
//
LOCUS       WP_284656780             354 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus thiaminolyticus].
ACCESSION   WP_284656780
VERSION     WP_284656780.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 354)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 354)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 354)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..354
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38246
     Region          91..354
                     /region_name="COG4587"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443644"
ORIGIN      
        1 mdmrrpgmrw kdsgeqrwqd gsgtndqand dpndqtddrp deqpndrtge qagdqpmekp
       61 gskqgrgglp argtgtagcs rasrfrlaag kygaafkigl qasmeyrlqf liglvslvfp
      121 igiqsliwta vyrssadgvl ygydysqmil ytllsgivtk lvmtqlehti aediksggln
      181 aylvrpisyf gyrlsayags rvisdtvllg lvaavlliav rygqdplppv rlalfaaall
      241 laaavqflls yaicalafrl aeisyffvit glivqivsgg ivplevfget vngwfsllpf
      301 kytiyfpvnv ltgripases lggiaiqcgw ivilagtahi awriglkryv glgg
//
LOCUS       WP_284656801             263 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Paenibacillus thiaminolyticus].
ACCESSION   WP_284656801
VERSION     WP_284656801.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..263
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30089
     Region          9..251
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(70,74..75,78..79,109,113,120,123..124,129,145,
                     149..150,152..154,156..157,160..161,164..165,189..190,
                     192..194,196..198,200..201,203..204,208,211..212,218,220)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(148,152,155..156,158..159,203,206..207,209..214,
                     217..219,223,225)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(169..176,191,194..195,198)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mnlltpqtet wlhrvnpayk lfvfvllllv tllnrqfdfa lnqliaytal lflfsghsrk
       61 kvllitlpfl flfissastm ilfgkgehiw wswglirise esfyrglmlg cktltfgmlg
      121 lafalttkpi hlfyalmqqf rlpakyaysf iasirmlpav wddirtrsda ltvrgaryak
      181 gikgmyerlr nyalpllaqs irraqrvava meakrfqmgk artyyyatry tradigftlv
      241 mlglmgaayy mavrlplvgw glg
//
LOCUS       WP_284656853             401 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Paenibacillus thiaminolyticus].
ACCESSION   WP_284656853
VERSION     WP_284656853.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..401
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=44079
     Region          14..398
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mkgvlkreie griarlqaam qertmdgcli tqnvglyyft gsmqagylfv pkqdepvyfv
       61 krslerarhe agvaveplgs frsfgtllqe rfpavfasgr pviateydvl pvqvferlrs
      121 vmpetawtdg samlrglrmv kspweidrir taahaahhal eqaaayvrpg mmelqliahi
      181 ehvfrmqghv gfirmrgynq eiitgmvasg eagaeptyfd gpaggrgltp aspqgssrkv
      241 idenepilvd igccidgyvi dqtrtlvigk ldedleraye sseailraae aslkpgavce
      301 tlyadalkla eqyglsdhfm gfgsdqvsfl ghgigmemde wpvlargftm plepgmviai
      361 epkftfpgrg vvgientyli tddgfekltt ppesvwriaa p
//
LOCUS       WP_284656870             365 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Paenibacillus thiaminolyticus].
ACCESSION   WP_284656870
VERSION     WP_284656870.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..365
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40091
     Region          4..359
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mkatqaqqyv evliigagqa glalgaelir rqprlsllli erhsrigdnw rerydslvlf
       61 tprkyselpg lplpgdpegf perdeiadyl eryaqhgklp vrlestveqv taaadgssgp
      121 psflvalrgq eqplrcrklv vacgpfrnpy ipewaaslgs giaqlhssqy qrpsqlpdgp
      181 alvvgggnsg aqiafelsqs rmtvlsargp vrhlplrlln rstfewmdrl tllhapaggk
      241 ragwlrrkgd pifgyelrda vragrirlfp eavgsgedga avlfkdhasf rpaaivwatg
      301 frpdyrwlhv pgtvdarghl iyhshrtpaa dlyvigmpwq qarssallcg agrdarllav
      361 ellrd
//
LOCUS       WP_284656892             698 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284656892
VERSION     WP_284656892.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 698)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 698)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 698)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 698)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..698
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=78044
     Region          15..671
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mnhphhdpek revinrrnfs hrlnlfffvt favfsvlivr lailqfvegp slkekeaqlg
       61 yketpipplr gsiydasgeq vayststqsl yfnieknygd pkkaeltdvq kknreeakll
      121 aqrladvfme ygdpedkplt adaiyndlmd lsarvnftyt priiktgltq kevayflehk
      181 pefpgidive dsvrhydpma vqtvgylkkf kgvrdnpgyy ndiynnratt psekkyldye
      241 dvgfdgielm yqeelrglng vkkfpvnvan riigpmeltk pqrgddihlt ihrhvqkate
      301 daimqtleri rnssnrsera pyartgyava mevdtgniia masmpdydpn vwrngsitpe
      361 dyeqyqyylm ngtirdvpap yeddkermkh pgsvvylgst mkplsvligl qeklfslget
      421 yydggyaqfg rvgyetkvwn sgnvgygrig asralevssn afmvdmigkr lysmptvngr
      481 nglsvwdeym dafglgvptg sglpreqaga kdylleaern naqsalvyas fgqqgkyttl
      541 qlaqfaatla nrgtrikpql vskitdgngq vvktfgreel nktkiddayw kvvedgmlkv
      601 nvhgfdgfpy sfyrktgtsq mdvsggrvdn avfiayapad kpklavavvv peggfgsyga
      661 apiaramfda ydevygltgt pkkkpdeqad tsagqgte
//
LOCUS       WP_284657054              71 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284657054
VERSION     WP_284657054.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 71)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 71)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 71)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..71
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7751
     Region          2..70
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 maiiinidvm lakrkmsvte lservgitma nlsilkngka kavrfstlek icevldcqpg
       61 dileyvqedp s
//
LOCUS       WP_284656967             258 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284656967
VERSION     WP_284656967.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..258
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27924
     Region          1..255
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mdwtgkivli tgassgigal taqavaakga vpvltgrsrn kleaavlgit aehavytmdv
       61 tsdddvervv tdvlkrfgri dillnnagyg efervtdmsv arfagmmdvn ymgvvrctka
      121 vlphmlarrd ghivniasma gkigspksag ysatkhavlg ftnalrmela gtgvavsavn
      181 pgpvdtpffe ladpsgqyan nvrwfmmppe kvvrhllrim etrrqevdlp wlgalgmrfy
      241 sffprisnri aarllnkk
//
LOCUS       WP_284657132             496 aa            linear   BCT 25-DEC-2024
DEFINITION  FGGY-family carbohydrate kinase [Paenibacillus thiaminolyticus].
ACCESSION   WP_284657132
VERSION     WP_284657132.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..496
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=53509
     Region          4..433
                     /region_name="ASKHA_NBD_FGGY_FK"
                     /note="nucleotide-binding domain (NBD) of L-fuculokinase
                     (FK) and similar proteins; cd07773"
                     /db_xref="CDD:466793"
ORIGIN      
        1 mwmvgidlgt tnrkvglyed ngrlvaktsr ptltedsgeg yvvyqpeamw ndvaemirel
       61 tdvhadkpvs yigitsmaes gllvnrrtge vqspllpwfe tcsapqaeri rkegtplelf
      121 qrtglhlsfk hglakllwlq drdpamlqda vwlsvsgyva yrlagamafd pslatrtfay
      181 dmrqnswdep wirgfgldpa ifpdvlpsga tlgtvhpdla drlglsggtk vaigghdhvc
      241 aamavgaiep gdvyvsmgta etlvgtmamq plgqaefetg lsygchvvpg cgfwmggnas
      301 sggavewirr lladealaye qiqemtagin dgpgevmffp ylsgsgaphp nsktraafig
      361 lekshgkael lravlegtay qlemirqsae rtsahpirrm navgggtqlp awlqmkadia
      421 nstllvppie eatmlgaaca aalggghfgs aaevrqalqs rgvkayepda erheryrqay
      481 eglyvpmaah lrslnr
//
LOCUS       WP_284657205             397 aa            linear   BCT 25-DEC-2024
DEFINITION  purple acid phosphatase family protein [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284657205
VERSION     WP_284657205.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Klabunde,T., Strater,N., Frohlich,R., Witzel,H. and Krebs,B.
  TITLE     Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on
            crystal structures
  JOURNAL   J Mol Biol 259 (4), 737-748 (1996)
   PUBMED   8683579
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11244734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..397
                     /product="purple acid phosphatase family protein"
                     /EC_number="3.1.3.2"
                     /GO_function="GO:0003993 - acid phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=43568
     Region          26..126
                     /region_name="Pur_ac_phosph_N"
                     /note="Purple acid Phosphatase, N-terminal domain;
                     pfam16656"
                     /db_xref="CDD:465220"
     Region          169..343
                     /region_name="MPP_superfamily"
                     /note="metallophosphatase superfamily, metallophosphatase
                     domain; cl13995"
                     /db_xref="CDD:472684"
ORIGIN      
        1 magillvsgm agigwdnlqr gtaakpvslg ttikgdprts raftwhtast glqgkvqvke
       61 gmeadtwdgd nvltftaesa siiseegkae svhkaeaigl kpgttyvyrv gngedggwsd
      121 pavfvteaae pdtflfinvt dsqgvteadf tfwgrtldqt fatfpdarfi vhngdlteel
      181 dnekgwesff gqaakwlvsv plmpvtgnhd eiegnaerft shfnvpdnga dgsiqgtsys
      241 fdygyahivv lntesnikrq tdwlredlan ndkpwviaam hrpayggntn kkvqdlvkvf
      301 dqfgvdlvlq ghnheysrsh pvrngqiape gkgtvyvvty aagpkfnalk ktkfyhavhf
      361 qnnkqmfagi tvsehslsyq aydldgilqd efvlnre
//
LOCUS       WP_284657232             256 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase [Paenibacillus thiaminolyticus].
ACCESSION   WP_284657232
VERSION     WP_284657232.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..256
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=28738
     Region          15..251
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 meitygdiiq lgrhrlmcgd stitgdidkl mqglkadmcf tdppyaafgs stgmfngivd
       61 trmiepflrs tlggiktivk dfghvyvtcd yrtyhawrkc adeiyfplkn livwvksrgg
      121 glgsnytnch efvmffhrep evnklamtdk ksggrlvrgk gnvwfynkvi rklseklhna
      181 ekplpmvvea iqnssepgdl vvdlfggsgt tlsaceqter tcymmeiepe hcltiikrwe
      241 qetgkkakvl kesgka
//
LOCUS       WP_284657466             927 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Escherichia coli].
ACCESSION   WP_284657466
VERSION     WP_284657466.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 927)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..927
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..927
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=104088
     Region          22..443
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          512..927
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mrnlcflltl vatlllpgrl iaaalpqdek litgqldngl rymiyphahp kdqvnlwlqi
       61 htgslqeedn ergvahfveh mmfngtktwp gnkvietfes mglrfgrdvn aytsydetvy
      121 qvslpttqkq nlqqvmaifs ewsnaatfek levdaergvi teewrahqda kwrtsqarrp
      181 fllantrnld repiglmdtv atvtpaqlrq fyqrwyqpnn mtfivvgdid skealalikd
      241 nlsklpanka aenrvwptka enhlrfniin dkenrvngia lyyrlpmvqv ndeqsfieqa
      301 ewsmlvqlfn qrlqeriqsg elktisggta rsvkiapdyq slffrvnard dnmqdaanal
      361 maelatidqh gfsaeelddv kstrltwlkn avdqqaerdl rmltsrlass slnntpflsp
      421 eetyqlskrl wqqitvqsla ekwqqlrknq dafweqmvnn evaakkalsp aailalekey
      481 ankklaayif pgrnlsltvd adpqaeissk etlaenltsl tlsngarvil aksageeqkl
      541 qiiavsnkgd lsfpaqqksl ialankavsg sgvgelssss lkrwsaensv tmsskvsgmn
      601 tllsvsartn npepgfqlin qrithstind niwaslqnaq iqalktldqr paekfaqqmy
      661 esryaddrtk llqenqiaqf taadalaadr qlfsspadit fvivgnvaed klmalitryl
      721 gsikhsdspl aagkpltrat dnasvtvkeq nepvaqvsqw krydsrtpvn latrmaldaf
      781 nvalakdlrv nireqasgay svssrlsvdp qakdishlla ftcqperhde lltlanevmv
      841 krlakgiseq elneyqqnvq rsldiqqrsv qqlantivns liqyddpaaw teqeqllkqm
      901 tvenvntavk qylshpvnty tgvllpk
//
LOCUS       WP_284657489              74 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284657489
VERSION     WP_284657489.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 74)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..74
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8741
     Region          4..71
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mgrirsnlka ladsrgigir qiardidyry etvrqmynde skqfprdlld klctyfdcdi
       61 nelllfeeek dphe
//
LOCUS       WP_284657504             276 aa            linear   BCT 25-DEC-2024
DEFINITION  RCC1 domain-containing protein [Paenibacillus thiaminolyticus].
ACCESSION   WP_284657504
VERSION     WP_284657504.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Hadjebi,O., Casas-Terradellas,E., Garcia-Gonzalo,F.R. and Rosa,J.L.
  TITLE     The RCC1 superfamily: from genes, to function, to disease
  JOURNAL   Biochim Biophys Acta 1783 (8), 1467-1479 (2008)
   PUBMED   18442486
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Renault,L., Nassar,N., Vetter,I., Becker,J., Klebe,C., Roth,M. and
            Wittinghofer,A.
  TITLE     The 1.7 A crystal structure of the regulator of chromosome
            condensation (RCC1) reveals a seven-bladed propeller
  JOURNAL   Nature 392 (6671), 97-101 (1998)
   PUBMED   9510255
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..276
                     /product="RCC1 domain-containing protein"
                     /GO_function="GO:0003682 - chromatin binding [Evidence
                     IEA]"
                     /GO_function="GO:0005085 - guanyl-nucleotide exchange
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=30394
     Region          17..238
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
ORIGIN      
        1 mfggisvpkv melpfdgtri kdiasgynfv ialledgtvw irgegskskq feqvpglngi
       61 asidttayya yglgadgklw qwsgysptyg vydppqartd vqdivqvtgg yivkedgtvw
      121 nlgfgseepl tqvqgltdve riavgnidqt gyalrkdgtv wgwgnrkldk mdlpalqtdy
      181 krffeavpie glehvkavaa gyhhflalke dgtvwawgqn esgqlgngst ansgervqey
      241 vrtradfver qaisylyqpl agwrrgshld rqgdld
//
LOCUS       WP_284657656             476 aa            linear   BCT 25-DEC-2024
DEFINITION  leucyl aminopeptidase family protein [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284657656
VERSION     WP_284657656.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Drinkwater,N., Malcolm,T.R. and McGowan,S.
  TITLE     M17 aminopeptidases diversify function by moderating their
            macromolecular assemblies and active site environment
  JOURNAL   Biochimie 166, 38-51 (2019)
   PUBMED   30654132
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Lowther,W.T. and Matthews,B.W.
  TITLE     Metalloaminopeptidases: common functional themes in disparate
            structural surroundings
  JOURNAL   Chem Rev 102 (12), 4581-4608 (2002)
   PUBMED   12475202
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415720
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..476
                     /product="leucyl aminopeptidase family protein"
                     /EC_number="3.4.11.-"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0030145 - manganese ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0019538 - protein metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50680
     Region          37..474
                     /region_name="PepB"
                     /note="Leucyl aminopeptidase [Amino acid transport and
                     metabolism]; COG0260"
                     /db_xref="CDD:440030"
ORIGIN      
        1 mkftigstea aqviiypifl etaatpfqsl plhqhmgerg avtwyydkqd eqhlllaglg
       61 slqsfepehl reaagnaara aeqhklctaa vcldgcagig dmreavavwv egwllgtyaf
      121 dkykskqavr yvetvrfdle pqagleeaia tgearaagia fardignepa nhmrpktlae
      181 rveawfadsg vqvacyegee laarqmcgli gvgqgsphpp vliemryctd psmelialvg
      241 kgitfdtggi slkrdhdisd mridmggaaa vigaieiirr sgmranvaai ipaaenmpdg
      301 sallpgdvlt ypngvsvqvg ntdsegrlvl adaliyahai gakeavdmat ltyscqgalg
      361 skyagiwgde ptvsalrslg rltgekvwel plaeeyagyl asdyadlcni srvgeagait
      421 aalflrnfvh ssmrwahidm aamkeaasta gyvaagatgy garllaefva ersrls
//
LOCUS       WP_284657754             318 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284657754
VERSION     WP_284657754.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..318
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34795
     Region          16..294
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mnahcseiev tidsaypvag tlsvpraavq papaillisg tgesdrngng gglnmniykd
       61 ladalgkmgl vtlrydkrgt hasggnfydt gfwdlvedst acvrflqsrp eidpnrivil
      121 ghsegaiiap vvqanqpvqg lmliagafdn lvhdtmprqs aqalqemesa egikgllfrl
      181 fnvpgrtrkq saafmemals saaptlqfkg akfcakwfqe haalnlaeyv kkvscpllai
      241 tgandiqtpp ehakmfaeaa kgeaewhivp qmnhilrkyd kphtmlglvk eykktiadpi
      301 daeflklleq wmrkykfi
//
LOCUS       WP_284657765             328 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus thiaminolyticus].
ACCESSION   WP_284657765
VERSION     WP_284657765.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 328)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..328
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=38137
     Region          65..326
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mklfwrehlp lagftcvqll lvllvfwydg ydrpltamya mflglcvfal ylgyryathr
       61 lmykrltdpp asltstiqla daaplsravd dtidhqyryy qqqlkvwerk qqehlafmnq
      121 wvhqmktpls vielitqdae dpklasisee adqmkrglem vlymarldtf ehdfhvekkp
      181 lrdivhdvvh enkryfirsy vypdiqiape ltvetdvkwl rfvlqqivtn aikysagsrs
      241 kvtamayteg ravvlevkdr gagipkqdvk rvfqpfftge ngrkykestg mglylakeii
      301 dklhheiele seegqgttvr iifpfart
//
LOCUS       WP_284657815             322 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus thiaminolyticus].
ACCESSION   WP_284657815
VERSION     WP_284657815.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 322)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 322)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 322)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..322
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36385
     Region          11..322
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 maasppalpp dkkarerrkl ekrslikkdl krnkyiylla lpviayyaif hygpmygllm
       61 afkdysiadg iwgskwigfd hfknffnsyy fgrllrntil invyellfaf papiilalll
      121 neirgrifkr tvqtisylph fisivvvvgm mfdfmardgl inqllgflgi dsipfmsepg
      181 wfrtlfvgsg iwqglgwgsi iylaaiatid ptlyeaakid gagrfkqvlh itipgmmpti
      241 vimfilnmgs mmsvgsekvl lmyspltyet advistfvyr rgvldsdygf ttavglfnsv
      301 vsfillvvsn tiskrvsehk lw
//
LOCUS       WP_284657877             865 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus thiaminolyticus].
ACCESSION   WP_284657877
VERSION     WP_284657877.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 865)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 865)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 865)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 865)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..865
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..865
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=96859
     Region          19..>162
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          128..417
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
     Region          621..863
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnivnrltvr hmkhnkkrtl vtiigvvisv amvtavatla fsyldvmkrq tiadggewhv
       61 lykdvnreql eaiqnddatk tvvlirdrgy aplaggqnpi kpylfikeyn aqglaefpie
      121 lskgrlprtd kevviseaia tnakvnceig dqlalqvger ftegtdkpln qwkalrvend
      181 kvtetlqnvt treytivgii krpaweptwa pgytaisyvd enllgandqv naavvlqkvn
      241 rslfahaenl aknnniesvq ynhellhyyg vakseaaqnt lfslsaiima vimigsvsli
      301 ynafaisvse rsrhlgmlas vgatkrqkrn svffegviig lisiptgmic glvgigmtlw
      361 finsmlqgal gitekltvtv tplslliaca vsmltifist yfpaikaski saidairqat
      421 dvklagkavr tpmfirrlfg ieaeiglknl krnkrrynai vfslaisivl flvvsfftas
      481 lkeslvlsqd gvnydlqvsy gnekriddrl lqsiaslddv eeysvihely geaeleeavi
      541 adqlkeivke dqsrlrdgky pyfirinaln dsnlkayaka vgadykqltd pthvaaivid
      601 tihykdmese kyveakaiyk kvgqsidvis tvfdresvkd ilvnkvkiaa ltdqypmgmv
      661 teglgrlnii vserimeqfm ydnekdesht ylylkssdpi kteqkiedmk eanlvvhnly
      721 qyrkqneqki llmsvfsygf ialislisia nifntistsi slrkrefaml ksvgispkgf
      781 nkmmnyesif ygikslcygl pssfvvmyli yramtnkfny gfvfpwmsvi yviaavfviv
      841 csamlyssak vkkeniidai kqesi
//
LOCUS       WP_284657878             433 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284657878
VERSION     WP_284657878.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..433
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48211
     Region          99..423
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mgilflviaa vfeaalavyc iwtksnqnkv rgmmrigala lfvmftlasv iewsfrwvgi
       61 gllllvwavl gvrtlirske erqqyrcgri vrnavvmlvl vviavtpalv fpqyalpqvt
      121 geyevasvsy tymdknrmeq ftgtgenrvv nvgfwypdna dgtyplvvfs hgayginesn
      181 astytelash gyvvcsidhp yhsfytasad gtvtlvnsey mqevnnankg vytveetygl
      241 iqkwmklrtd dmnfvidtil ekaktgsenv yqlvnpekig vfghsmggaa svslgrered
      301 igavvnidap lfselvynre tgdfaasrqp yttpllnmys dsvwvqlnrn styaankaid
      361 ehgtevytvy vqgakhmslt dlalfspmla nmlqggraei dsyyaidtmn riileffdcy
      421 lkgkgrftsa gty
//
LOCUS       WP_284657902             112 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Paenibacillus thiaminolyticus].
ACCESSION   WP_284657902
VERSION     WP_284657902.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..112
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12270
     Region          4..105
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mnkywmyvil tcllemvwvf gfstadaawh willvgviiv dfyflskace glptgtvyai
       61 fagvgsigtv lmdyflfggn msplkllfig llvagviglk ladnkveerg hq
//
LOCUS       WP_284657935             483 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284657935
VERSION     WP_284657935.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..483
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=56282
     Region          10..>442
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mktsnrlval yqylvehdgw ittqqlaaml ccsvstirnd leilksflpd twfiesrrgk
       61 gvhinrpsnq pivpfkqlln etdrvqnlig ylihnesgct ltelsqklfy svstiskiik
      121 ilkhelkkyh lklgtkpvki hgnefhlrqf yfdyylnknc tawiqqdtln sictlmksie
      181 qkgrfkfsdt ayiqlpivls iwqsrllkkq yiskfvyptl fyessdsfrw iipmieehlk
      241 klyirvsshe lqygaalilg vpriegrmag stqtlhemae qchrdpvnkl iqsieekarl
      301 pfsddpilfq qlydyykyas irwitgihsn anqntikikd sefslfksvh eamhhyfnyv
      361 esfreddvad itmffvaskl gyhmkqkekt illyvseigv mryvklklle nicgrikmvt
      421 tnhahemqyl astknidiiv ttnqqsytll pnnipiihid pipssydmni iqdalkrvsd
      481 hgn
//
LOCUS       WP_284657970             658 aa            linear   BCT 25-DEC-2024
DEFINITION  elongation factor G [Paenibacillus thiaminolyticus].
ACCESSION   WP_284657970
VERSION     WP_284657970.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Margus,T., Remm,M. and Tenson,T.
  TITLE     Phylogenetic distribution of translational GTPases in bacteria
  JOURNAL   BMC Genomics 8, 15 (2007)
   PUBMED   17214893
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 658)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..658
                     /product="elongation factor G"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=72422
     Region          1..627
                     /region_name="PRK13351"
                     /note="elongation factor G-like protein; cl46912"
                     /db_xref="CDD:481252"
ORIGIN      
        1 mktinigiva hvdagktslt erllyetkvi relggvdsgn tqtdsleler rrgitikasv
       61 vsfvvneaki nlidtpghad fiaeverafg vldgavlvls avegiqaqtk llmavlekla
      121 ipvilfvnki drsgaqpeav ckairerlsr caiplygtvq agtkqanivk kqcgkenpdf
      181 yeqyielaad hdeqllasyv yggeisgsri eetmtrlire arvypilags amtgiginel
      241 leaiawfipa pqpcadapls gvvfkiersp sgekiayirv fngsfgvrqt iqvnrkqadg
      301 qieaasykvk riqlfdrgrt adaacagage fckvwglkev rigdvigtws erireihvaa
      361 pqmesrieav pksrdhalyq almnmaeedp lihiwrdehh retyirlfge vqkeviettl
      421 keayqldvrf aetrivciek prgtgtavef mgaernpfya tvgfridpge pgsgvtyhle
      481 velgslplaf haaiedtvya tlrqglygwe vtdnavtlth tgyaspvtva gdfrklaplv
      541 lmealsragt dvyepiheye ltvpagsiss amhrlaglqa vmkepvmsag tclltgtipv
      601 ktteafkrsl haitegegvf iarpcgfirm esgypvrkrs dynplnrkdy llhvlray
//
LOCUS       WP_284657973             281 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284657973
VERSION     WP_284657973.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..281
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=30840
     Region          42..125
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          151..>212
                     /region_name="DUF2141"
                     /note="Uncharacterized protein conserved in bacteria
                     (DUF2141); cl01930"
                     /db_xref="CDD:470398"
ORIGIN      
        1 mnakreltpq egqamriqmm kdehiaaaeq ailymkshle dditseqlaa hvgyspyhft
       61 rifksvtgis prhylsalrm esgksallqa psllvkvlls igfrsagsfn trfkqqvgvp
      121 prafrigsga ltaymnqfqn relslpvpgk eaaaqitcri eapasfrgli fvglfprpip
      181 dqrpiagtal aggkrtcafa dvppgtyhal aagipwslrp kdyfvlerai rgkypsaiev
      241 neqtelgiai qlrdplpydp pivislpqll feknkesnta k
//
LOCUS       WP_284658012             478 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Paenibacillus thiaminolyticus].
ACCESSION   WP_284658012
VERSION     WP_284658012.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Erzberger,J.P. and Berger,J.M.
  TITLE     Evolutionary relationships and structural mechanisms of AAA+
            proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 35, 93-114 (2006)
   PUBMED   16689629
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..478
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51443
     Region          <4..>64
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          <195..444
                     /region_name="RPT1"
                     /note="ATP-dependent 26S proteasome regulatory subunit
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1222"
                     /db_xref="CDD:440835"
ORIGIN      
        1 mdrlsfllrm aqqhpndaea iywlaaeyaa rgqwvdaigq ysaalavcad dalrsallag
       61 lseatarlqs gggsaeqhaa agnagreaga gssesgaesr tgvgssesgi esrtgvgsse
      121 sgiesptgvg ssapdseead deddeeieve dvadeeweta qaghaavfar sgiglqvldg
      181 gksaaaspad ashkvtfadv aglqelkkti qlriispfqn qglfsrfrkk agggvllygp
      241 pgcgktfmak atagecraaf fpihiadild kyigvseqnl rdlfdnarah kpsilffdei
      301 dtvgfnrsks sssmrgmidt flsemegvdt stdqllviga tnmpwdvdda lkrpgrfdrl
      361 vfvappdeea rehmfrlkle gryienidtv rlanrteffs gadiehlces aaervlgeil
      421 esgqerpirm sdfealleta rpstlewlgk aknyvkyanq tgayndvedy lrtygrri
//
LOCUS       WP_284657994             243 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Paenibacillus thiaminolyticus].
ACCESSION   WP_284657994
VERSION     WP_284657994.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..243
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=27898
     Region          4..240
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mmppirtlvv dderhsrdel iyllkqhsti eivgvadsge qavlramqlq pdvifldvam
       61 pilsgieaak aianmkdvpr lvfvtanrqf gaeafrleaf dyllkpldke hladtvrrle
      121 kwtcpphapp pprigsklav eveqeiiyin pkdiifithk ngvtrivtit reyhmktslk
      181 elesrmrhhs fmrihkshiv nlhfakrlip wfngayqlel fgadefvsvs rnyvkafrra
      241 lel
//
LOCUS       WP_284658051             404 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Paenibacillus
            thiaminolyticus].
ACCESSION   WP_284658051
VERSION     WP_284658051.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 404)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..404
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45778
     Region          6..395
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(106,108,247,249,279..281,322)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 miprsainyl ipdfeskhpn ikvkvekapy eqfdsklqan iaaknapdvt shfgyggfae
       61 yynkylladl taimkednfn padygiteel mdiykvqdkt ygipfsnyvt illynkdlfd
      121 kagvpyppse yedpswtfdk mvelaeklti rdddiekaqy gvdfnwgeld mrqayfgakv
      181 ysddtwtngg kpsethfdsq eaiaaykkwi gliwdkqvsp spawsksvag qfgdpflsgk
      241 igmsvggswn lasqdqynfk vgvaavpfgg nekersvlyv dplfvlkdsk hpkeayefik
      301 ymiskdvqek sielsggtpp ineqakekyy nnfegvdlqv iknvydgank ygvesfnhlv
      361 anysqinelf inefaaaqnn tksveevmpe iqkkldklle rvnr
//
LOCUS       WP_284658119             414 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Paenibacillus thiaminolyticus].
ACCESSION   WP_284658119
VERSION     WP_284658119.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..414
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=44346
     Region          14..411
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mrpkaaagta erwdwmrael dalegagrvr klepaawleh gwieragkrl lhlasnhylg
       61 fepwlddagw arlaaecrrl gepavrigsg asrlitghdp qhdalerela sfkdteaalv
      121 fssgymanag vipalvgrng vvfsdrlnha sitdgiilsr aqhiryphrd mdrletalkq
      181 wrsggpdvls rqgrmlivtd avfsmdgtva pladlvalke rygamlmvde ahsggvygpg
      241 grglchalgl htkvdiimgt fgkafgavga yiaaedivvr ylvnrartli yntglpplma
      301 afirqrlrdv caadsarael mrkaalfrar lqaggldtgp gdshivpvlc gtdqhavals
      361 aalaeagvag vairpptvpe gtarirfapt pahrdadllq aadavvrlaa earp
//
LOCUS       WP_284658166             341 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD-IIIC family phosphatase [Paenibacillus thiaminolyticus].
ACCESSION   WP_284658166
VERSION     WP_284658166.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..341
                     /product="HAD-IIIC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39183
     Region          1..339
                     /region_name="FkbH"
                     /note="Predicted enzyme involved in methoxymalonyl-ACP
                     biosynthesis [Lipid transport and metabolism]; COG3882"
                     /db_xref="CDD:443090"
ORIGIN      
        1 mikcivwdld dtlwegtlre deaaikllpe masvldtldr rgilhsiasr ngweqvkdkl
       61 eqlgiahyfl spqchfdska asigriaqel nigldamafi dndpferfev nfyvpevrty
      121 dagqyrelpg ypefqagqlt eeaanrrqym qarhmreear kahtgsreqf lkecgmklri
      181 rlareedypr vvelsrrtnq mnslleridf pfvesycard nhylyvarle drfgahglig
      241 tcfasaaadg idinlfcisc riegrgiasa flytvleqle qqqpqaatar crlvskqrnl
      301 parlllemlg fkktttedeq svymlqlplp rkafdwleig e
//
LOCUS       WP_284658153             368 aa            linear   BCT 25-DEC-2024
DEFINITION  MDR/zinc-dependent alcohol dehydrogenase-like family protein
            [Paenibacillus thiaminolyticus].
ACCESSION   WP_284658153
VERSION     WP_284658153.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus thiaminolyticus
  ORGANISM  Paenibacillus thiaminolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Gonzalez-Duarte,R. and Albalat,R.
  TITLE     Merging protein, gene and genomic data: the evolution of the
            MDR-ADH family
  JOURNAL   Heredity (Edinb) 95 (3), 184-197 (2005)
   PUBMED   16121213
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Paenibacillus thiaminolyticus"
                     /db_xref="taxon:49283"
     Protein         1..368
                     /product="MDR/zinc-dependent alcohol dehydrogenase-like
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=39976
     Region          19..366
                     /region_name="Zn_ADH2"
                     /note="Alcohol dehydrogenases of the MDR family; cd08256"
                     /db_xref="CDD:176218"
     Site            order(55..57,60,174,178,198..203,222..223,227,250,
                     266..267,269,289..290,314..316)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176218"
     Site            order(55,86..87,174)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176218"
     Site            order(116,119,122,130)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176218"
ORIGIN      
        1 mtnewvqtle gkaiipktmr aivayapgdy rleevpvpei gegeillkve gcgicagdlk
       61 afegapsfwg detqpayika pmipghefig hvaalgpgve gfaignrvis eqivpcwkcr
      121 fcnrgqywmc ekhdlygfqn nvnggmaeym klpkeainyk vpanlpleka iliepfacsy
      181 havqraqiql gdivvlagag tlglgmigai kqsgpgkliv ldlfeerlrl akqfgadlvl
      241 npskddvayi vkeltggygc diyieatgaq ksveqglali rklgrfvefs vftdpvtvdw
      301 siisdrkeld vlgshlgpyc yepvikgias gdlptegivt hqlpldqfkh gfqlvksgsq
      361 slkvvlip
//
LOCUS       WP_284658231             115 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_284658231
VERSION     WP_284658231.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>115
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          1..>115
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkrlqafkfq lrpggqqere mrrfagacrf vfnralarqn enheagnkyi pygkmaswlv
       61 ewknatetqw lkdapsqplq qslkdleray knffqnraaf prfkkrgqnd afryp
//
LOCUS       WP_284658397             407 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Klebsiella pasteurii].
ACCESSION   WP_284658397
VERSION     WP_284658397.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pasteurii
  ORGANISM  Klebsiella pasteurii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Klebsiella pasteurii"
                     /db_xref="taxon:2587529"
     Protein         1..407
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=46774
     Region          129..401
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mtdpvfalep diprnvriar wllfrllsgi regsltvreg aqtfhfgdpt aalraevrvl
       61 sanvywrllt ggslaaaeaw mdgewesqql tpllqmlarn gqvlgrlerg frllgkpver
      121 lrhwtrrnsr aqakaniaah ydlgndfyah flddellyss alftddgqdl tqaqrakmar
      181 lcerlalmpg dhlleigtgw gamaeyaarh ygcrvttttl sqeqfqwana riaraglqdr
      241 vevllcdyrd ltgqydklls vemieavgqr ylpaffrtcq arlrpggrma lqaitiqdqr
      301 yrgysknvdf iqryifpggf lpsitamnel mtrhtdfvmr dlfdmgpdya rtlahwrqrf
      361 ihawqdiekl gfddrfrrmw lyyfgyceag fnartisvvq ltaerts
//
LOCUS       WP_284658409             551 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Klebsiella pasteurii].
ACCESSION   WP_284658409
VERSION     WP_284658409.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pasteurii
  ORGANISM  Klebsiella pasteurii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Klebsiella pasteurii"
                     /db_xref="taxon:2587529"
     Protein         1..551
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=63012
     Region          261..535
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mgnrldnrap kfttkrgntf yinfrlpdgt ffrrslgtds lravevtmsr lspyiplvqn
       61 gslsveqfkm hidgfreatq rdfdtylldw lrmgveeaqr mpglgrfqrk idsenaispa
      121 atvteakgrt dlhlnrvysg ddstarmmla alhqkkvafs eknldqayev agqidmhqam
      181 lhqayeafys gdivryralf esmqsqladt eklkkpvikq avatveapea dntpllsdaw
      241 rlfvaekgkt waitiarenn rfyevlmhvl gdvpvgsitk qhirqtlavi eslprrnlkp
      301 ysdmsldeci dfdvpeddli ssanvkkhlk iyssffkvll kdekdmleks ptegikyevt
      361 enkgghyskp emkrlierln tftdwrrdyf ltliytgarr geiaairken irkdeetgrf
      421 yifieggkte haqrqiplsk qieglllari kplksdglvf gdlptyehia flwrslmeec
      481 nipkynefgq krvihalrht fiseaiartg naalvqfvvg hsrtqslgit arythrpaln
      541 qlltvvdcvs w
//
LOCUS       WP_284658475             148 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Klebsiella
            pasteurii].
ACCESSION   WP_284658475
VERSION     WP_284658475.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pasteurii
  ORGANISM  Klebsiella pasteurii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Klebsiella pasteurii"
                     /db_xref="taxon:2587529"
     Protein         1..148
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16639
     Region          4..109
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mparekitnq tcpvarsldi igdrwslliv rdafdglrrf sdfqrslgma rnilsdrlhk
       61 lvnsgilttq sasdgtayqe yvltakgerl fpvvvalrqw geqhlfapde phsvlidkrt
      121 lrpvpmmspa tedglvltfy etevqkik
//
LOCUS       WP_284658631             398 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase
            [Enterobacteriaceae].
ACCESSION   WP_284658631
VERSION     WP_284658631.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..398
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=45156
     Region          2..389
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mklnarqvda akprekaykl adgaglylev vpsgsrywrm kyrfngkekr mafgvypavs
       61 laqaralrde akkklaegid psfakkeekl vrdvqlnntf qavalewhgt kvsrwsegya
      121 sdiieafnkd ifpyigqqpv neikplvlln vlrrmesrga tekakkvrqr csevfryaiv
      181 tgraeynpaa dltsamsghe skhypfltve elpdffkals gytgsplvvl aarlliltgv
      241 rtgelrgafw sefdlekavw eipaermkmk rphliplstq aleivqqlkv msgqyplvfp
      301 grndprktms easinqvfkr igytgkvtgh gfrhtmstil heegfntawi etqlahvdkn
      361 airgtynhal ylegrremmq wyadyidnig kfnliias
//
LOCUS       WP_284658781             297 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Klebsiella pasteurii].
ACCESSION   WP_284658781
VERSION     WP_284658781.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pasteurii
  ORGANISM  Klebsiella pasteurii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Klebsiella pasteurii"
                     /db_xref="taxon:2587529"
     Protein         1..297
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34034
     Region          <100..286
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          200..281
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mngkiqishv knettynipl vleenvissg isllslwhtl adesyrvswp rdkkkplian
       61 swvaiytlkg cgkiylkdht eitlngncvi flkpieiksy hcaglvweqy wmefipttlm
      121 pipvlqigti yhadifnkel nevalliadr dplknnlava yltkiiyqwi cliaengnkd
      181 rqlqklenli aalhanpqkr wsvadmadam qcsepwlrrl flrytgktpk eyylnaqlel
      241 aqsllkqegn tvgkvaemln ffdsfhfska fkrrfgyaps avlkmndrhp mdagqqd
//
LOCUS       WP_284658839             186 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Klebsiella pasteurii].
ACCESSION   WP_284658839
VERSION     WP_284658839.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pasteurii
  ORGANISM  Klebsiella pasteurii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 186)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Klebsiella pasteurii"
                     /db_xref="taxon:2587529"
     Protein         1..186
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20687
     Region          18..165
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mstpshltaq plvwghgprt fevflestcp fsvrafnkld dlldevgadn vtikirlqsq
       61 pwhlfsgviv rcilaastlp hgreqahkvl kavadhreef eftdhcsgpn mdvtpqqiie
      121 rieryshvsl aaafarpelq neikwhskya rqngihvspt fmvnglvqpd lgsgddvsvw
      181 aarila
//
LOCUS       WP_284658890             457 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Klebsiella
            pasteurii].
ACCESSION   WP_284658890
VERSION     WP_284658890.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pasteurii
  ORGANISM  Klebsiella pasteurii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Klebsiella pasteurii"
                     /db_xref="taxon:2587529"
     Protein         1..457
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=50137
     Region          8..393
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mttctsraaw lnllrrlhfy iglcigpfif vaaltgtlyv aspqleswly qdalrgtlsg
       61 ekqplsaqit vateaiqgnl rlhavrpgil agdttrvmfi dpslgesetr aifvdpvtlr
      121 vkgdlpvygt sgilplrqwi dyahrslllg svgrlysela aswmwvaalg gialwsmtrp
      181 rrrinnkmqn srrlhvslgw allvgmlifs atgltwsqwa ggnvdkmraa fgwltpqvnt
      241 qlqsavpavh dphaehhmgs rmmgeaaasp lrveefdkvl laaraaglda gkleirppsg
      301 sgrawtvnei drswptqvda vaiegstmri vdrthfsdfp lmakltrwgv dfhmgilfgl
      361 vnqllliafg talcvmivvg yrlwwirrpa raafnpantl iqawfglawp arlltavial
      421 llgvalplmg gslalclavd ylrwraatam leakpve
//
LOCUS       WP_284659074             307 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Klebsiella
            pasteurii].
ACCESSION   WP_284659074
VERSION     WP_284659074.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pasteurii
  ORGANISM  Klebsiella pasteurii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Klebsiella pasteurii"
                     /db_xref="taxon:2587529"
     Protein         1..307
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33995
     Region          24..305
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtihianapc swgvddpknp ylppwskvle eaatagyksi elgpwsylpt radelsaalt
       61 kqglslvagt ifddlvseen fanivelthn lcrnlsqvpa aektpgnpfq ppylviidfg
      121 npqrakyagr gelaprlspa dwqrmidhii tiselawqey gvrpvihpha ggciefadei
      181 dllatqiphk vaglcldtgh lyysgmdpii wldrhfdrld ylhfkdvdpk vfasvisrgi
      241 dffsacaegv mcplgsgaid ypavrafldk rgyqgwitie qerdprnveg slqavteslr
      301 ylrsvgf
//
LOCUS       WP_284659438             723 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Providencia stuartii].
ACCESSION   WP_284659438
VERSION     WP_284659438.1
KEYWORDS    RefSeq.
SOURCE      Providencia stuartii
  ORGANISM  Providencia stuartii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Providencia.
REFERENCE   1  (residues 1 to 723)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 723)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 723)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 723)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..723
                     /organism="Providencia stuartii"
                     /db_xref="taxon:588"
     Protein         1..723
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=79468
     Region          74..723
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mknklltipf kdiakhkity hslfcvvisf fypntlfaks dnklskdsii vsakgnnnlq
       61 pnlfssrsmq agllgdndim dipfnitnyn saylesqqaq qisdilshdt siqissskgg
      121 lldslyirgf pitegnigef alngiygvsp nfqlladyae rvdilkgpas llygmspegg
      181 vggvinvvtk rasaqpitrl taqylsdsql ggkldvgrly dlgnnqyfgi rvngsytngn
      241 tavdhqdrql gvgaialdys serfrasldl itqnqnmnat nrpfflgeng vvppapsgkt
      301 nlaspwtwwk snddsallhm eydvlsntsl fmdiggartr idrvneqtyt vlndqgdist
      361 yimnfqsktq rysvgtgiks efmtgntshq lalqwnryfd rynvgtnagt pyntnlyhpt
      421 yidkqipdyp eitkrsentl sgvslvdtig ffndsfmvip giryqniksd sftlgalstt
      481 ydesaitplv gllfkptdni slyanyvegl skgstapvna knsgemmkpf rskqyelgvk
      541 yehpvaittl slfqiskpsg sldpnsliys andeqrnrgi elsvsgkpfd slrltggvty
      601 iqaeltktas gqnkgnepig vspwvanfga eydipsvsgl singninyht rqyvnkenth
      661 sipswttvdi gsayktkisn tpvtlrlnit nilnerywsg vasystfaqg sprtvlgsis
      721 vdf
//
LOCUS       WP_284659278             200 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Klebsiella pneumoniae].
ACCESSION   WP_284659278
VERSION     WP_284659278.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18527488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..200
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21113
     Region          16..96
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          91..191
                     /region_name="COG3837"
                     /note="Uncharacterized conserved protein, cupin
                     superfamily [Function unknown]"
                     /db_xref="CDD:443048"
ORIGIN      
        1 mnvkvnittd sgsdvdhvsr avatrlkayr kakkmsldel srrasiskgm lvemekeaan
       61 psiailckla aalgvsvadi vnvasepalh iipaeqiptl wqgplggsar llagtagpnm
      121 ielwrwemqp geaftspghp attfellhve tgaltltlge tcrtvaages avarteiehg
      181 yrnegtaplv ftmtvaelps
//
LOCUS       WP_284659439             107 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_284659439
VERSION     WP_284659439.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..107
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          <1..97
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 nrsvldqgwy emrrqleykq lwrggqvlav ppaytsqrca ccghtakenr lsqskfrcqi
       61 cgytanadvn garnilaagh avlacgemvq sgrplkqept emiqata
//
LOCUS       WP_284659632             321 aa            linear   BCT 25-DEC-2024
DEFINITION  ParB/RepB/Spo0J family partition protein [Providencia stuartii].
ACCESSION   WP_284659632
VERSION     WP_284659632.1
KEYWORDS    RefSeq.
SOURCE      Providencia stuartii
  ORGANISM  Providencia stuartii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Providencia.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Providencia stuartii"
                     /db_xref="taxon:588"
     Protein         1..321
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35850
     Region          80..>205
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 msksqgeptn gcyqltprsq rrnrpeelkk gdgftispql lleeegfntr gafcenyyer
       61 pdikagirvl adaykrgdyv ppiivkvidg kvyvreghrr rraillaiee gadiqfvqvv
      121 ehkgdeaeqs lliatsndgl plspleravi yarlanwgws dqmiaqrvgr saehvriara
      181 llemplelkr miqegsvaat yaqelynehg tnaveilkka qeeqangndg kkapkkltkk
      241 svekgprlgk kvveamhrgv ssitsrldni kpnddgetft ltlsredvda fqelkaklae
      301 lepktdesne dqqeldlagn q
//
LOCUS       WP_284659842             551 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Klebsiella pneumoniae].
ACCESSION   WP_284659842
VERSION     WP_284659842.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 551)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..551
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58171
     Region          4..548
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mkqtflsgat laalvmlval plvfillqai fphfsagslg dafggipall adpqlpamlg
       61 gtlwiaagva lvsvmiglpl gilrgmfslp lprlwdllfl ipfltppyis alswmlalqs
      121 qgylqqltgw qlndllfsrs givlvmtfni fpvvyfavsr sllasgtrla vvarvhgasa
      181 wrafwhvtlp mlspalaagm llaftlaiee fgvpaalgsr agvvmltvgi ekkladwpvd
      241 lpgaallsll lmavalfaww lqrrlvgeke vtsvtgkpge nygallgwmt lpavlamaav
      301 gglavgvpav smmltsvmgt lsggvsvenv tlrhfaalfd qqgdalsalg tslslalgsa
      361 livgalglla awlvmvqkik grgmvdalsl mpaalpgvvv gvglillwnq pfwprspynt
      421 lwmlllsycc lllpwpvryv gsalrqlgpn lepaarvhga splqalrliv lplvfpalla
      481 amlmvfavas relvtsllls pagtqtvavf iwrqfeqgsv gqgmamaslt lltglvlmlt
      541 alalmqrrtc g
//
LOCUS       WP_284659844             369 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Escherichia coli].
ACCESSION   WP_284659844
VERSION     WP_284659844.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469162
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..369
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=41941
     Region          <194..290
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
ORIGIN      
        1 mnepanrtvn nlrksgdlqg awefgfqalq aapqdtylkg alfwvcyefl khqlenlnkr
       61 asssnnyrpt dfefeqienl lqtivnldia tggleykmll vqfkkslewf ptlihlvlrh
      121 qtvlfddeak tpfqaekgev pslmlstarq vasawlrare ywhldlnqvm afinqtreqa
      181 sdtkhmmwld ydqakclvva gqydqareli lpilrkkqke swawgalaat yskqdqrlam
      241 kffargivsa hdvtfslrll qgiiplllan qqqaeasmcl ktaiaayqah gwklkqeleq
      301 lsmqawydsg vdekqlspfl nsishdalny lhgpmekvva ivenihksgk gfqvfvnkst
      361 slisshggs
//
LOCUS       WP_284659884             188 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase, partial [Escherichia coli].
ACCESSION   WP_284659884
VERSION     WP_284659884.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 188)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 188)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 188)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 188)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 188)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..188
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          <12..163
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 yefktaaiit tsrninkeat iknvsklltq krkdeiignl kridnrindi aiiatdqnke
       61 ifldiglsel neismlgegv sralsfissi lvqkdsiili deiengihys vikdminali
      121 eaaktnnnqi fttthshdvi cainelyeks kdisyirlgr dkesqkptam qfnmddfsfs
      181 vengwevr
//
LOCUS       WP_284660119             138 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein, partial [Escherichia coli].
ACCESSION   WP_284660119
VERSION     WP_284660119.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..138
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
     Region          <1..128
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 kqitlvpvis wvqagawkev gysevdlsta etypcpvpcg emtyilrvig dsmideyrpg
       61 dmifvdpevp achgddvial mhdtgettfk rliedgtqry lkalnpnwpe pyikingncs
      121 iigtvifsgk prrykika
//
LOCUS       WP_284660315             797 aa            linear   BCT 25-DEC-2024
DEFINITION  M9 family metallopeptidase [Photobacterium damselae].
ACCESSION   WP_284660315
VERSION     WP_284660315.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10280819
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..797
                     /product="M9 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=89967
     Region          25..202
                     /region_name="Peptidase_M9_N"
                     /note="Peptidase family M9 N-terminal; pfam08453"
                     /db_xref="CDD:430004"
     Region          267..548
                     /region_name="Peptidase_M9"
                     /note="Collagenase; pfam01752"
                     /db_xref="CDD:426409"
     Region          586..660
                     /region_name="PPC"
                     /note="Bacterial pre-peptidase C-terminal domain;
                     pfam04151"
                     /db_xref="CDD:427748"
ORIGIN      
        1 mthilkysvi afilsssasv aatncdiaql ahvpdkasvi ehadnvcmqt wfhpdkasin
       61 svfseeqmvl ianalntkia ayqgdeasat eiyylseyvr aayyvnyyns tviapyshal
      121 nlrfttainr flqspyalta sqhnmnalgs ltslvdsvrv lpenlptlmt llptlnkdna
      181 enstyvealn nvfralngss sdkgvqdyls hhlevldqlh qfiisndwal kthaavvvsn
      241 aarelsrllk iqdpaiknki ltiqedllar yplggendsi wvgiaemvgy yapdkqqqlg
      301 lsdaklrleq hilpmtfrce gpatvraqkm tqeqaievca alnqkeqdfh slitsasnpv
      361 nddlndhvev ivfdsnydyt vysnylfgnt tnnggqyleg npsdlhniar fvayrntsad
      421 gysvwnlehe yvhyldgryn qygdfnynlq hgfvvwwleg faeymhygns ytdaialgqe
      481 rtyslsevla ttyshdtnri yrwgylavrf lfdnapdqve qllqlsrqgh ytqwaalvqk
      541 lglqyneefa twlttlkapt tpshsnksvi tltaetpvel sgakyseqlf aitvpkhvte
      601 fsvslsggdy gdaelyasfn qvahyynyqi tdarsgnner irfatdeqgf vkpgvyyfsv
      661 agrsayehvv lntemktaes tqtayqaddl spitlqadth tnitvnkery mvyfvpkghh
      721 nvrvwvtpkd qkqdnqgnvd lyfgkktwpv leqydlvsqr sdsyeyletk vdgghfvflm
      781 lnaknphntm dvyvtsn
//
LOCUS       WP_284660266             637 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Photobacterium damselae].
ACCESSION   WP_284660266
VERSION     WP_284660266.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 637)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..637
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=72090
     Region          66..537
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 msdkmnvdal flgpksenqv ffkemmdyai sehmhwrsdf hpedaplvtp vaqhqpdfrd
       61 tlyrtegilq dlsarlktks vpwfsprylg hmnadtlmis nlayvmtmly npnncaheas
      121 pvttelelda ghdlcrmfgy dvnkswahit sggtvanyeg vwvarnlktm plaiaaydks
      181 kdlvegmseh qllnmkskdi ldltdelkkr gifeevralt argvgvdagk lgkflvprsk
      241 hyswmkamdv lgigqehiip ldvdgnyrtd vqkmreitfk lmeegtpilg mvsvvgttee
      301 gsidavhevv klrqeceeky gssfyihvda ayggyvrsmf ldennefmey nalieryrhd
      361 eiipegvvwp krdvynafsa msevdsitvd phkvgfiqya agavamkdkr ivdlisyhaa
      421 yvfeeagddn dedkqvvlgs simegskaga taaavwaahr lvplnisgyg hvigrgivta
      481 dwfakklats epfivagrkf evrplmhpdf hmvdftfkei dnnsleahnk lnqriyelcs
      541 yatgrtytkd fltsstslse eeygqtpriy aesrgfsede wntvgsvyil rsavmthflr
      601 deirfnnywn nlrdvfvsil seiideenke klahhaa
//
LOCUS       WP_284660537             752 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidase U32 family protein [Photobacterium damselae].
ACCESSION   WP_284660537
VERSION     WP_284660537.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002788
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..752
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=84590
     Region          3..295
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
ORIGIN      
        1 mqnkfellap ggdldsikaa iaagadaiyc gldsfnarnr atnltfdvls giirlahknh
       61 ckifltlniv vldseipavi rllnklvntk vdgvilqdlg lfsiikehfp tldvhastqi
      121 nthndgqilf lkqlqasrvn lsrelninei khlaqfghqh dvlmevfvhg sycigfsglc
      181 yissvkngns gnrgrcsqpc rdqyqttavg kdfplnlkdn safsnmaela dagvyslkve
      241 grikkshyvy tvvdqwrqqi drylnqqpll tdtkslytvf nrdfsnsylq gdinknmfid
      301 nprdnavthf tkvyqcttpe tvngvkqkly ddkteiiqtv eqvtanmdvs slpltivltg
      361 qegeplsisv ttpnhhfvlc sdsvlrasnk qtlthdmlek rfqslanege feivefntkg
      421 lnealsvpfa elaqlkdqmg yrlngnvaiv apieppkprn manhrkptgi apklavlise
      481 pkdvtlghgd evalyyampe glsmeletlv alfeqnphli pwfpailige nyqaavefie
      541 rvkpqqlvtn nngiayvayq heidwiagpy lnitnsfslq ciadefkakg afisneinrk
      601 qinpmvcpen felyysiyhp lmmlmsrqcl fhqtvgckkk rfdnkclrkc dksasilslk
      661 easfvldkqr gthnalysqq nymnlsavtd fpdkftrfmi dlrdiktetq vnldkptlvn
      721 lfsryiqgdm taqeqlesgi igtihhqykk gl
//
LOCUS       WP_284660604             295 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfurtransferase [Photobacterium damselae].
ACCESSION   WP_284660604
VERSION     WP_284660604.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..295
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=33929
     Region          50..294
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mlsryslltf ilffimtmlv lytqkilane tfvitplelq tklssqpnsl liydvrsveq
       61 ynmehipqai sfpfmstyek knngyyvkdk khiesllrdh gitndkmivl yddgslfhas
      121 rlywvlalyg vknikiingg ltlwkqqyst skiktdisns eyipilnssi yanqviakia
      181 shnqdiysll dsrsyeeyig etsvtdkrgh ipnalfinlk dffvelpngv nwlknieylk
      241 dnlshiprtk kiitycnkgt asglsflilk yagynvahyd gswidwslsd lpvek
//
LOCUS       WP_284660742             834 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-mannosidase [Photobacterium damselae].
ACCESSION   WP_284660742
VERSION     WP_284660742.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 834)
  AUTHORS   Nascimento,A.S., Muniz,J.R., Aparicio,R., Golubev,A.M. and
            Polikarpov,I.
  TITLE     Insights into the structure and function of fungal
            beta-mannosidases from glycoside hydrolase family 2 based on
            multiple crystal structures of the Trichoderma harzianum enzyme
  JOURNAL   FEBS J 281 (18), 4165-4178 (2014)
   PUBMED   24975648
REFERENCE   4  (residues 1 to 834)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 834)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14312040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..834
                     /product="beta-mannosidase"
                     /EC_number="3.2.1.25"
                     /GO_function="GO:0004567 - beta-mannosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005537 - D-mannose binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=96262
     Region          26..>644
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          753..829
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; pfam17753"
                     /db_xref="CDD:465483"
ORIGIN      
        1 matllldgqw qltspqhshi aipcilpgdv hsallaaeli vdpyfaenes lvqwvgesdw
       61 lltrefevsq emldhhaidl tlsfvdtvad iqinqhsvlh csnqfqtyhq evkstlklgi
      121 nhisillkrs dieakaraet lpfpipwaeg nnqiphmntl rktqchagwd wgicllvsgv
      181 yqsiilepln ntrlvnvrtt qnwlssehcq lelaityqal aafeqqqlti dfnqqvhtia
      241 laidnqdidk nhtlyytidv hqpkrwwpag ygeqplyple itlneqsitk qigfrqleld
      301 tslddigskm qfvvngqtit akganwipld ampsqqtper yrqllqnavd anmnmirvwg
      361 ggtyeqdcfy qicdelgllv wqdlmfacal ypstvefiqe veqeviqqid rladhpclal
      421 wcgdneviga inwypesrqh rekyvvnydr lnrvlalive khdpsrrfwa sspcngeldf
      481 gdawhddncg dmhfwdvwhs gksldayyqv kprfcsefgy qswpslptvk tfadydewnv
      541 tsptfeshqk nkrgnsiite mftryfrfps nfanmlylsq vqqalaikta seywrahknh
      601 crgilywqln dcwpvsswss ieytgrwkql hyhakrffap qlvtfiqqdn glltlsavnd
      661 ehkavnyqgq vlqlswqgdi lqtwpingel tsdssdiiwq hfmntsnine kdhfyhvein
      721 ieccsesnng qtstiendyf ptvfkqaklq pgkihaqvik delgiiield ceepclfvhl
      781 evddhlsrfs dssftllpst csgykkqiry igllnkdcie kqlkiyhlsq syls
//
LOCUS       WP_284660762             446 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Photobacterium
            damselae].
ACCESSION   WP_284660762
VERSION     WP_284660762.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..446
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51267
     Region          29..435
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mtvnhqanvk kvnkkvvils ssndswvlll ernnydvvrc kdireldail edetncicia
       61 dltncvfsla cittkamnnq hvrwitilnk eqldvdvvrs figkfcsdyf lspivdgqfm
      121 pfikhqmgmt kitnnknpkd lliklllsge skkvkrlkdl vrrvsssdvn ifitgengtk
      181 kqslarylwh ssgrkygrff tidcdlllts stqrdifyhy fsnsaknten fknetvylkn
      241 lqslpqdfql klleffnldl ksrlrletqn dikiissssi qpdallneyq fnkelfykln
      301 ifhldvpslr ersedirkfa qyfldihlnk intmavkfse didnlllsyp wpnnlielen
      361 qvkqavisse gpvitsdafl lpstkcakrs lksikdeaek dillsalhlh hgqvmsaakd
      421 lgisratmyr llskhqilpd gdrira
//
LOCUS       WP_284660923             339 aa            linear   BCT 25-DEC-2024
DEFINITION  formylglycine-generating enzyme family protein [Photobacterium
            damselae].
ACCESSION   WP_284660923
VERSION     WP_284660923.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..339
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=38486
     Region          68..331
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 mkvnsillii isanlvacnd sgntvsreii skqeiaridt ninklypdad sklkqhilnv
       61 aveslesmvf ikggtfmmgd fkapcspldl krmdwtpeas cntalsmtrt ganyqhkvtl
      121 snyslsdhet tyyetdafnr senkpvanqd srydkefpiq deqlknrpss tkswqeakdy
      181 clwlgkltny pidlpteaqw eyaarnrgkn iyfatnngya qeigsryvnn dgsiheytke
      241 qgnygyfgdi krwppnplgl ydmagnsrew vndwysknyy kvspelnpqg petgtekvvr
      301 gwggsmpltt srshekptds kyisrrgfrc avqsptsiy
//
LOCUS       WP_284661042             799 aa            linear   BCT 25-DEC-2024
DEFINITION  McrB family protein [Photobacterium damselae].
ACCESSION   WP_284661042
VERSION     WP_284661042.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..799
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..799
                     /product="McrB family protein"
                     /calculated_mol_wt=92403
     Region          <332..723
                     /region_name="McrB"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrBC, GTP-binding regulatory subunit McrB [Defense
                     mechanisms]; COG1401"
                     /db_xref="CDD:441011"
ORIGIN      
        1 mnsqkdrask hqqlwndflq rwpresleql tleeyvsvnd qdtftywlet ktrelgsiqg
       61 ntsakfgiyk rngegkeqng ighgevytwr trygnnesev fnyvkkvliq isqaaydgnl
      121 aeidsidfap likwkiafly qnqsnpvlin tfskpmlevl tnsnsktsfp smyqkliaek
      181 geqnllefga ecwdkaaqks keihqksild kfshidvfnr gveqwspetv tafcdliqda
      241 ydnkldvftt amdtgamiri grkelgvpra eevfatfept lqkinyelry qhrdgyecst
      301 vanelylrtr kskklaefsq qypitrkpyw pesyfgdsda dityddyeva epgkdymmtk
      361 lsplnqilyg ppgtgktfht mesavkaaep dfiwtdrnql kaeyerlvse krirfvtfhq
      421 sygyeefveg lsaktegdqv syyekdgifk tianeanryr vsktiksdkd fdslwscfvs
      481 elsesengvr vdtvrtfftv tdvdnntvrf ekdkgnsihs lsvktlkavf dgereikggl
      541 npyysaliky lqryvqsied vhterkkfvl iideinrgni skifgelitl iepskrkgae
      601 ealevtlpys gdifsvpdnl hiigtmntad rslammdtal rrrfdfvemm pkpelfknrk
      661 irnidltkll ttlnnrievl ydrehtlgha flfpvyneqd edkafellka afknkiipll
      721 eeyffddwnk irlvlgdnqk etalcfvtkq edsyeslfgt nhglnlyedt kvtfqlasfd
      781 ghdsvwdqpe ayiaiytkg
//
LOCUS       WP_284661108             609 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Photobacterium damselae].
ACCESSION   WP_284661108
VERSION     WP_284661108.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   3  (residues 1 to 609)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   4  (residues 1 to 609)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
REFERENCE   5  (residues 1 to 609)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18512141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..609
                     /product="vWA domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=68322
     Region          <54..278
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
     Region          332..>439
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          391..421
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 madftfihpm wliaivplll llpwlkgksq sssliaphia aklglsqpqh ktwplyllgl
       61 awilaviala gpswektklp ayslsgarvl vmdmsksmya tdiapnrltq arfkaldmlp
      121 gwkegstglv tyagdgytis pltddsstla nlipslspki mpipgsnaas gikqaidllk
      181 qagdtngdii litdgmteke sqeslaelkn thyrvsilav gteqgapiem pdgrlltqng
      241 qtviakvdpn tlsaitsktg gllqfsqadn qgvnnivkft akprnqleqg kqkeleerln
      301 ngfwlllpli llallgfrrg ivlaalmvfm pldyahaspw knqdqqgydn yqqgqytdav
      361 kdfsspawkg iaqykagqfh qaiktleplk dttsrynlgn ayaqsgqyek aintyeevlk
      421 keptntdakk nleivkkale kqqqnqqnqq nqqnqqnkqd qskkqdkqqs qnqqnqqnqq
      481 ekdqqqqqqq qqqqqqqqqq qqqqqqqqqq qqqqqqqqqq qqqqqqqqqq aeaktdeske
      541 kkgnnkekel avtpsqegkk pgeatvtqsn pilkkleqip ddtseliraq milqarqraq
      601 qqqetensw
//
LOCUS       WP_284661113             407 aa            linear   BCT 25-DEC-2024
DEFINITION  HlyD family secretion protein [Photobacterium damselae].
ACCESSION   WP_284661113
VERSION     WP_284661113.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446287
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..407
                     /product="HlyD family secretion protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45240
     Region          70..378
                     /region_name="EmrA"
                     /note="Multidrug resistance efflux pump EmrA [Defense
                     mechanisms]; COG1566"
                     /db_xref="CDD:441174"
ORIGIN      
        1 mleglavwal fiyllrlvgm pwnkftksfa ylggggwlvf vwfglitfap mdlsggslvq
       61 sphiqlrpas sqikghvkai hvepnqtvek gqliyeldde pyrialtkae tkldsahvdl
      121 kmaiedvana ktqyrsavkd iditknqlva atedlrfkqa tlnryvkqnq vvkhtvtesm
      181 ldeqrtavkv gkaqvttlds qvekaviase qakvrleqaq lavtsrevav kseqenvaqa
      241 qwnlehtqvy apadgyltnf imregqyvgv apriqmytde kyvlmrvnhq airnvkagqm
      301 aefasavypg kvfaaevegi ieatgeaqgs llarddnvrq ttganiankh hfvrlkliet
      361 egydipvgsv glawvsaekp igflgfldvi rgiiirmksq ifyvwsm
//
LOCUS       WP_284661172             106 aa            linear   BCT 25-DEC-2024
DEFINITION  putative quinol monooxygenase [Photobacterium damselae].
ACCESSION   WP_284661172
VERSION     WP_284661172.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..106
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12374
     Region          5..99
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 msnnlifyve fdvkpecver fihgatqvle tmskegtfvs tqfhrhtenp nkfslyevwn
       61 epsmdefvkn qlrgksyrde yesylpella tprkfsvles igswak
//
LOCUS       WP_284661184             445 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Photobacterium damselae].
ACCESSION   WP_284661184
VERSION     WP_284661184.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..445
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=51492
     Region          91..430
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrrlyiesfi glivlfglsl ycyeviiyrw ntdydyvled yeaealhdlv dniyhnegsk
       61 aaylaiekya tktrqtltvh nkeelpddvk tfffttapqs ytyhdedril wfrltlssdf
      121 yslkpnfdtp lrraidfddn mvwvffmggf alysilfiwy lsrrvrllek ttlafahgef
      181 sarartesrf rvgtlnqsfn ymadkisnll isnkaltnai ahelrtpifr iqwqaellad
      241 svkdkeiqqk iesivedtee mesmvnelly yakveqpdte lhcqdivfnq ylndmlqnwe
      301 ktaqskitlk tpfkqnivss idtqlfkhvl nnlvsnasry srkhilvtls qerdsvfitv
      361 eddgpgipne hwpylfdpfy sadparnkaq sgfglglaia kqivarhkgq itigdsallg
      421 gakftvilpi tyqcdpildr pnisk
//
LOCUS       WP_284661286             176 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Photobacterium
            damselae].
ACCESSION   WP_284661286
VERSION     WP_284661286.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..176
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19740
     Region          18..72
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(19,23,48)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(22,47)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(29..30,41,44,48..49)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mdiedknanf stlsliilke irldrgihqg viadrigksp sawtkiengq ssltfdvlig
       61 acsalqihps hvtalidkli plfapykfyf qvgtlsyeed dllrlaseyf nskgydelrt
      121 rpyerfnien lgspfgftst ptivryccep efkewidnga egavpsspif sspyly
//
LOCUS       WP_284661374             130 aa            linear   BCT 25-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Myxococcus sp. SDU36].
ACCESSION   WP_284661374
VERSION     WP_284661374.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 130)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 130)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 130)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..130
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14412
     Region          <29..111
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mnakqreelk alllalhsel tektpsriep nrtddarigg dedeqplnem mqaiasnrnr
       61 nmdgvlarvl kalgklredp dgygeceecg deipfgrlra mpyaefcvtc qgnkdgpkgr
      121 atrskltdyt
//
LOCUS       WP_284661435             474 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Myxococcus sp.
            SDU36].
ACCESSION   WP_284661435
VERSION     WP_284661435.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 474)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..474
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=52086
     Region          5..464
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mplfrtilva ddepsirhil tlvltghgye vravadgeda lkelnardyd vllcdvrmpk
       61 kdglsvlrea laahpaltav vmsaygsqeq alqavaagaf dyvqkpfkpd eivfvlrkae
      121 ererllrenr rlkqaslpst peghilgesp alhallrqva rlapvdttvl isgesgtgke
      181 liarelhvrs prapmsfval ncgaipsgli eselfghakg aftdartakr glfaeadggt
      241 lfldevgelp lsaqvkllrv lqegeirpvg enrvekvnvr vvaatlrdls rlvakgefre
      301 dlyyrlnvvn lrvpplrerr edvpllartf iarfnrelnr eppvaglsse aeallmayaw
      361 pgnvrelena meravllade alilpanlpe rlwaapppgq qgatpqvgpv lqdggdlslk
      421 raireleesy iraalrktkg nrtraaelld ishrallyki keygidpdae aerg
//
LOCUS       WP_284661585             365 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Myxococcus sp. SDU36].
ACCESSION   WP_284661585
VERSION     WP_284661585.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..365
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40910
     Region          28..324
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mkpsrrhfra nlrylralvr rfrttlmlsa vlflggpllf hwrfrgpdgd ridfgealhh
       61 tyfllygqps lpyvddwlve llnlvippsg ialvadgvvr faylffarhk ndkewievvs
      121 etmkghvvvc gagrvgyrvv tqlremgkdv vvvekredaa fvsalrderv plliddtrsp
      181 lclprtnvkd asaivcatdd dlanlniald arklnpnirv virlfdddls gkvretfkae
      241 alsssslaap amalaamdpr ivhsfhlakh lmvvslfear lglpsltise vrdrfgcltl
      301 slqrngeeql hprgdevirs gdvlslqasy peyrrlraft heaepplwsq heavavvtps
      361 srkvg
//
LOCUS       WP_284661530             451 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Myxococcus sp.
            SDU36].
ACCESSION   WP_284661530
VERSION     WP_284661530.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..451
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=48970
     Region          1..445
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 msrilviede piirtelrrl lvraghdvse agsvheassd yaldsfdlvl sdlrlpgapg
       61 tdiialcpgv pvlimtsyat vksavdamkl gavdyiakpf dhdellmqve rvlreglltr
      121 qnaalkrevd qthpvsgmvg ssaamrevfe rvrkvapspa tvlvlgesgt gkelvaralh
      181 aqspradgpl vavncaaipe glleselfgh ekgaftgaqa ahpglveaah ggtlfldeig
      241 elpapaqarl lrmlqdgevr rvgatrprkv dvrivaathr dlprrvqegs frqdlyfrlr
      301 vveirlpplr ertedvpala rhllekasrk vgrptaslap eamdaltshp wpgnvrelen
      361 aleravilad gpvvtaglla lelpeaadsf gasateetsg aapdsmeeyf rrfvmehqeh
      421 mgetelakrl gisrkalwek rqklgiprtr a
//
LOCUS       WP_284661699             726 aa            linear   BCT 25-DEC-2024
DEFINITION  Kelch repeat-containing protein [Myxococcus sp. SDU36].
ACCESSION   WP_284661699
VERSION     WP_284661699.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Shi,X., Xiang,S., Cao,J., Zhu,H., Yang,B., He,Q. and Ying,M.
  TITLE     Kelch-like proteins: Physiological functions and relationships with
            diseases
  JOURNAL   Pharmacol Res 148, 104404 (2019)
   PUBMED   31442578
REFERENCE   2  (residues 1 to 726)
  AUTHORS   Gupta,V.A. and Beggs,A.H.
  TITLE     Kelch proteins: emerging roles in skeletal muscle development and
            diseases
  JOURNAL   Skelet Muscle 4, 11 (2014)
   PUBMED   24959344
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 726)
  AUTHORS   Adams,J., Kelso,R. and Cooley,L.
  TITLE     The kelch repeat superfamily of proteins: propellers of cell
            function
  JOURNAL   Trends Cell Biol 10 (1), 17-24 (2000)
   PUBMED   10603472
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19803719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..726
                     /product="Kelch repeat-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=73945
     Region          <35..132
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          56..96
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          100..145
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          101..375
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          148..193
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          197..244
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          247..293
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          297..344
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          336..624
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          346..393
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          444..489
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          493..540
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          544..589
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          592..638
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          640..688
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
ORIGIN      
        1 mfepvgfgrk aallmtlvfa gcshedfada lnapgtqdae lasvswvgtp smstqrldht
       61 atvlpngrvl vtggqsstsa eqydvatarw lsagnmtvir rrhtatllpn gkvlvvggdv
      121 aaantgtael ydvatgtwst tgsldslrsg htatlllngq vlvmggedgn gtalmtarly
      181 dadtgtwsat hsmrvprmgh aatlladgkv lvsggrsssw gtvlrtaely dpatgtwsst
      241 aamssprtgh astallngkv lvsgglvddi aatrsaelyh vetgvwgpag nlmpverahh
      301 tatvlhsgev fitggsdgse pylqsaalyd pvnalwtsta smatsrlght aallgtgevl
      361 vaggspdgvl rtasaerylp stlpwraana mlsaryhhsl tvlssgevla aggtangsta
      421 ltgaerysea tghwlqtgal ltarylhtat llrdgkvlva ggqstsssyl ssaelydaat
      481 gtwtatgvla aprarhtatl lpdgkvlvag grrsssfsgm lataelydga tgtwtatgvm
      541 srqrqyhtat slpsgkvlvv ggntqngdts saeiydvstg qwtltgslsg pryghtaval
      601 psgkvlvtgg wgargalata elydpatgtw tsltsmqhsr ygpmstllps grvlvlggdg
      661 ggtvgllasa evydpasgqw hgagtlptal tsagvvtlvg svrvlvsggl spsgslsaag
      721 lyspap
//
LOCUS       WP_284661701             267 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Myxococcus sp. SDU36].
ACCESSION   WP_284661701
VERSION     WP_284661701.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..267
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29621
     Region          6..267
                     /region_name="COG4587"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443644"
ORIGIN      
        1 msarttlraf ptllrvgfae avayraemli wvlsttmplv nmvlwmavsr eapvgrfgea
       61 dfisyflatf avrqlatswa awlinwevkq gtlamrllrp isplwayave siaafpmrlm
      121 vavpvillsv alvgqkavpq hawqwgcfvl aviggwavaf lanvaigalc fflessqkvl
      181 evwlvlffvc sgymypvell pptlrtvidw lpfryqigvp vemltadygw eeslrllaaq
      241 wawvavlgal aavawkqgvr rfaafgg
//
LOCUS       WP_284661714             250 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Myxococcus sp.
            SDU36].
ACCESSION   WP_284661714
VERSION     WP_284661714.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..250
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27294
     Region          2..229
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mlrilfflms klpegarqqv vralmdgvwd tlanekvlgr enipdqpclf lcnhlsnadg
       61 ftldrafrpr kvvflagvkl kstvmtrlaa etmetiaikp nspdieamrr aldtlkagks
      121 vlifpegars rtgtltqakk glsliakrag vpvvpvalqg teklmpinds dmggerlfna
      181 dvfvrfgppf rvealeveva gaedprqalv dammrrvael lppeyrgfya eapaqpapap
      241 dwerpsapas
//
LOCUS       WP_284661775             262 aa            linear   BCT 25-DEC-2024
DEFINITION  indole-3-glycerol phosphate synthase TrpC [Myxococcus sp. SDU36].
ACCESSION   WP_284661775
VERSION     WP_284661775.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..262
                     /product="indole-3-glycerol phosphate synthase TrpC"
                     /EC_number="4.1.1.48"
                     /GO_function="GO:0004425 - indole-3-glycerol-phosphate
                     synthase activity [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27208
     Region          7..255
                     /region_name="TrpC"
                     /note="Indole-3-glycerol phosphate synthase [Amino acid
                     transport and metabolism]; COG0134"
                     /db_xref="CDD:439904"
ORIGIN      
        1 msqagtldri markrqelaa rppmaprarp tprdfaqglv thrsgrplsv iaevkrksps
       61 ggdfphadvv avarayeaag asaisvltdg pdfgggledl vavraavslp vlrkdflvaa
      121 reveesalwg adavlliada ledgelremv atakavgvaa lveahteaha eralaagarl
      181 vginnrdlat lktdtgtalr vmpklrsrar vlvaesglks ladleaarea gadavlvges
      241 llrapdpgha lrrllgveda ap
//
LOCUS       WP_284661782             187 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II [Myxococcus sp. SDU36].
ACCESSION   WP_284661782
VERSION     WP_284661782.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..187
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=19392
     Region          2..184
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 milvidnyds ftfnlvqlly tlgaevkvvr nddldaqgva asgashlvis pgpctpheag
       61 vsvaaiaqsr vpvlgvclgh qsigaafggk vvrapepvhg kaahiqhggt glfaglsagf
      121 aaaryhsliv eapslpaele atawsqdgli malrhrerpv vgvqfhpesv ltpdgpalvr
      181 nflegrl
//
LOCUS       WP_284661849             229 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Myxococcus sp. SDU36].
ACCESSION   WP_284661849
VERSION     WP_284661849.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 229)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..229
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25744
     Region          1..>221
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrradrlfei lqvlrrargp mtasaiaeql etsqrtvyrd laalmarrvp irgeagvgyv
       61 lergfdlppl mltpseieav vlgaqwvaan adktlsaaag dvlakvaaiv pkhlrelvdd
      121 pvvgtppakq rhpdgtvdls rlrewsrkql klhihyadae gtaskrtvwp ilvgyvtgvr
      181 vliawcelrr dfrifrterl lsvefldapy perrsalrrr weaqlshtk
//
LOCUS       WP_284661854             358 aa            linear   BCT 25-DEC-2024
DEFINITION  lipase family alpha/beta hydrolase [Myxococcus sp. SDU36].
ACCESSION   WP_284661854
VERSION     WP_284661854.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18498059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..358
                     /product="lipase family alpha/beta hydrolase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37592
     Region          108..214
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
     Region          <169..311
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mvqvtrpssl tpstrtratp eapvpakaaq ginavvegds ftasppaamq rsnalaqana
       61 lrlpipwpgk geadkigwiq kayppakdst aeftklnqav ragkdvlpae akdcvylavg
      121 gllseaapkq lyfdrnldal eaqglqvgrv pvdtdmgven naaivrqavl daakdgkqvv
      181 lighskggld saaalamype lqehvralvt lqspyggspm aqdlldnplv rygvggaiea
      241 lggsiqaged ltydsrkafl arhpmppgip tvcmasttsn ptsplfaaeg ymqqrygvks
      301 dglvlpqdaf ipgsksvtls gldhldatgt tlnpfkpyqp edltlslvam alnmpker
//
LOCUS       WP_284661855             585 aa            linear   BCT 25-DEC-2024
DEFINITION  RCC1 domain-containing protein [Myxococcus sp. SDU36].
ACCESSION   WP_284661855
VERSION     WP_284661855.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Hadjebi,O., Casas-Terradellas,E., Garcia-Gonzalo,F.R. and Rosa,J.L.
  TITLE     The RCC1 superfamily: from genes, to function, to disease
  JOURNAL   Biochim Biophys Acta 1783 (8), 1467-1479 (2008)
   PUBMED   18442486
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Renault,L., Nassar,N., Vetter,I., Becker,J., Klebe,C., Roth,M. and
            Wittinghofer,A.
  TITLE     The 1.7 A crystal structure of the regulator of chromosome
            condensation (RCC1) reveals a seven-bladed propeller
  JOURNAL   Nature 392 (6671), 97-101 (1998)
   PUBMED   9510255
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..585
                     /product="RCC1 domain-containing protein"
                     /GO_function="GO:0003682 - chromatin binding [Evidence
                     IEA]"
                     /GO_function="GO:0005085 - guanyl-nucleotide exchange
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=60278
     Region          324..581
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
ORIGIN      
        1 msvrrmtsms hpahpepgat pplaatlalt aaivatlllp svghasstgh vtvlcgspap
       61 lpwgytgssp tpqcegvcys gwtdgvcndp adpgsrvvvy gcagktsgsg yscdgdtngg
      121 vllatftage avsissflgn tdyctfqldv lrphaqdpig lrdfivwerd eceppeppcy
      181 cpngtdhqgn pvtshtcgep vcgadfqwys cqpggwsseg gacgdpgsdc sctgtdflgh
      241 tvtvdscgeq vcgadfqyya cgttgwtaqg vscgappeec sctgtnaqgh pvtidmcgep
      301 vclddfqsyt ceesgwvsqg sscsggtsws avsaggyhtc glradgniqc wgdnwwnqap
      361 afvqgpftqv sagfdfncgl radgniqcwg snvygqapsf fsgpftslsa gtthgcavts
      421 vgtiacwgmm ngtaptglft qvsaggyhsc alrtngtlac wgdngsgqat ppsgtfvels
      481 anyttscgrr sngtvecwgq digqlddpsw pftqvaagya thcgvktdsq vacwgngsmy
      541 pemlavpqgs ftqvatgyqh tcalstsgal scwgdndvgq ldvpn
//
LOCUS       WP_284660159             257 aa            linear   BCT 25-DEC-2024
DEFINITION  nuclease-related domain-containing protein [Photobacterium
            damselae].
ACCESSION   WP_284660159
VERSION     WP_284660159.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Grynberg,M. and Godzik,A.
  TITLE     NERD: a DNA processing-related domain present in the anthrax
            virulence plasmid, pXO1
  JOURNAL   Trends Biochem Sci 29 (3), 106-110 (2004)
   PUBMED   15055202
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10551559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..257
                     /product="nuclease-related domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29568
     Region          33..144
                     /region_name="NERD"
                     /note="Nuclease-related domain; pfam08378"
                     /db_xref="CDD:462454"
     Region          <204..251
                     /region_name="YrdD"
                     /note="DNA topoisomerase I, ssDNA-binding Zn-finger and
                     Zn-ribbon domains [Replication, recombination and repair];
                     COG0551"
                     /db_xref="CDD:440317"
ORIGIN      
        1 mnifdvfini leqvwyllpl llivsvfksr wlkgifgeyl vnrllsklpe sdytlikdvt
       61 lptsdgttqv dhivvskygi fvvetknmkg wifgsarqkl wtqkiyrhss kfqnplhqny
      121 khikvletll gcsadylhsv ivfigdstfk temppnvtya rgsiryiqqf nkvvfsdkdy
      181 arltdsinqi klkrgvitdl khrnhvkeiv askvssnqcp rcgsemvlre tkrgenigkq
      241 fwgcstfpkc ravkqln
//
LOCUS       WP_284661903             124 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Myxococcus sp. SDU36].
ACCESSION   WP_284661903
VERSION     WP_284661903.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 124)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 124)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..124
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13774
     Region          7..92
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mvtpmvqqrs eqldavfhal sdptrremlr slssgprsig elaapfsmsf agaskhvktl
       61 eraglvnrsv egrthrcsla paplagaadw lrfyerfwnd rldalerelr kperggarkg
      121 arke
//
LOCUS       WP_284660040             252 aa            linear   BCT 25-DEC-2024
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Photobacterium
            damselae].
ACCESSION   WP_284660040
VERSION     WP_284660040.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..252
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28394
     Region          3..249
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mdiqlsidng iaqltldrpq tynaltlnmy qklgrhfiel tnnpevkiii ltsssdffcs
       61 gndmfdfqti ghcseqeiqk hrldiesfmf nfincskpii aavtgpaigi gttllqycdy
      121 vvasshsyfq tpftalglcp efgasvvlek ligarkaram llfsekmtas easelrfina
      181 isakpikhsy eiagqlqhls inaithskrm lkniqyhnle etikqendli fqliqqpdaq
      241 ariekfieks rr
//
LOCUS       WP_284661972             117 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Myxococcus sp. SDU36].
ACCESSION   WP_284661972
VERSION     WP_284661972.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 117)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 117)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 117)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 117)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..117
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13479
     Region          1..83
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mietftalad pnrfriveyl lggarsvgai gealhlnqpq vskhlrvlke arlvdveara
       61 qqrlyglrpe plrelnawle ryrdiwderl gqldslleel ktqdletaqr hprkkkg
//
LOCUS       WP_284662039             377 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Myxococcus sp.
            SDU36].
ACCESSION   WP_284662039
VERSION     WP_284662039.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..377
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=41121
     Region          26..358
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mraeaspptl tapgvrlpid evreerltll dggaeayprm leaiasaqvm vhlevytfer
       61 egigarflda lvaaahrgva vkvvvdgwgs igasryltqt lkaagakvrv ynpltslctg
      121 rawrnhrkil lvddsvaflg ginigdayaa kgdvlgwadl alelrgdicr qlgarlhaga
      181 salesgavkl flsgvagghr lrkrylqaid gakhevvlah ayflpdkgli rslkrasrrg
      241 vtvrlllpgr sdvvfaraat mrlyrdflra gvsihewtds tlhakaalvd grkllvgsfn
      301 ldplslvnle tlvevedpgv aaqaqrwldk hllgsrrvyl edcarsglqq wlldivgltv
      361 ariaerfasf mgwrrkr
//
LOCUS       WP_284662047             242 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Myxococcus sp. SDU36].
ACCESSION   WP_284662047
VERSION     WP_284662047.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..242
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25280
     Region          1..219
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mnridksili tgasrglgla lmngfarrga rvvgvarhaa emeaaaaalr kegleahala
       61 cdvgdkeaiy plvgaatalv gpldvlvhna stlgptplpl lldtacedlq rvlevnvvgp
      121 frltkavagn mavrgkglvl hltsdaavsa yprwgaygvs kaalehlgrv waaelegtgv
      181 rfvsvdpgem dtrmyrdavp dgdysqlsrp eavaarlvew valrseslps garleaakle
      241 aa
//
LOCUS       WP_284662053             731 aa            linear   BCT 25-DEC-2024
DEFINITION  trypsin-like serine peptidase [Myxococcus sp. SDU36].
ACCESSION   WP_284662053
VERSION     WP_284662053.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..731
                     /product="trypsin-like serine peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=79409
     Region          205..400
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mriklrglll agmllaggga maeesavceg rtsqpplqrd aqgrvkvged vvvtfksrqp
       61 tarpdgvraq aelawtdrvs spgatyiaph fsqfalapgd yvivrapdgs reyrydgfgk
      121 gegdapvrgg fwsghisgdv aivelwsvgg qaksgytidr fargfanlaa lgedldseal
      181 cgpddsrnar cyqtsdprqy kharavarll ingsgactgw lvgnqghvmt nehciantsd
      241 alntdfefma eggactsacn swfgcpgtvv atsstliavn aprdyalvrl ptnptatygy
      301 lqlrnttavv deriyipqhp aawgkhiarn sthasdasgf aeifalnrpa cspggpldig
      361 yyadtqggss gspviansdh rvvalhhcan cpnrgvpits iishlgallp qcalrsatcp
      421 dpydvwmrdt wsdtglepdp atagqdmwas pyiwirrnpd galpanhhah qnpelgatny
      481 ayvklhggpr pgasgrlkly yanastglsw ptdwtqfgdv pvngftpdth vvqapwsglp
      541 geghyclvar wesafdpmsf tettdiganv rqnnniiwrn vnivdlesgs eeihfivrnv
      601 hqrvralrla vrvpeadrdr pfpvhggrvv vrlpeelfqr wleaggkaeg lkmvregefe
      661 vvspeggvfh nlplgfreeh qvrmrfernd aatpepyhle vvqfdqdsqe reslggigyd
      721 iyahgepkpk e
//
LOCUS       WP_284662124             607 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Myxococcus sp. SDU36].
ACCESSION   WP_284662124
VERSION     WP_284662124.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 607)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 607)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 607)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 607)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..607
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=66569
     Region          121..602
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          386..602
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mlrrllptli alllgfagla wglgslqrif aterddaqas ldsrrealeq yaraslaqsl
       61 rdrleaarpa leaaaldpla patglylrer gaqllprlal hdtgedtpak gryaglragt
      121 eradeaedpw aerlalirev dralargdrr astvalmall qhrsqyvlas trdvpgllvv
      181 leslaergdp vpqlmhalvr dgladgrsgr ldglqrllll rrarftkedf dflrerival
      241 stkagvpvad fearaaelas eplplpralp gpalvragwy leprggnhvr gvavdsgall
      301 qsltremrer glleadgqvr lladaevlpl aalplsvdtp ewaraqgala rryrlktgmv
      361 aacavlalgi aalafvaqhr klrfvelksd fvatvshelr tplasirlla etlewrlaeg
      421 tdardypari vreadglgfl venllsfnri dkgrwvpkle pvrldelvgl lrrdweswsk
      481 vpveldadvg erslradgql lrlllsnlar nacayntrsp vrlriealad grvrfsdngv
      541 gipqaqwera feefvrlpgq ghdapgsglg lalcrrimrv hggtlrvaas spegttfelr
      601 fphpvtt
//
LOCUS       WP_284662142             425 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Myxococcus sp.
            SDU36].
ACCESSION   WP_284662142
VERSION     WP_284662142.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..425
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=47286
     Region          49..421
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mdemqeleal ipkpgalgfs dgaererhem kgpftlppgp eafsfalyqs tgvglipghs
       61 lellensavf ermlediraa rssvhvlvyi wrpcalsdrv vealverara gvacrvvvdp
      121 vgseeirgdr dfdekvekvl teagvevhyy rllagkvlgr llgrshqklv ivdgrigytg
      181 gfgiwkvweg dglkpdewrd thvrvegpev rrmqlsfsrh wqesggglip psafpedled
      241 sgpcaagfid sagklgltda ermiriviga areriwiana yfsppnaile qleekcrqgv
      301 eirvlgpgpn hdvpimrasq rstyerllaa gvriweyqps mmhsktllvd dwlavvgstn
      361 mdslslnklk egslvihdas fvrklarcwa tdlrhskeit lenggrtnpw rrlarratql
      421 vgqdr
//
LOCUS       WP_284662193             332 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Myxococcus sp. SDU36].
ACCESSION   WP_284662193
VERSION     WP_284662193.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..332
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35385
     Region          44..317
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 maaellspae aqgaaevaar lkdelntvml dqesvveqvv vavlarghvl leglpglgkt
       61 elckalarll slpfrriqft pdllpgditg tyvlegdgrr dfvfregplf aslvladein
      121 rsspktqsal leamqersvt vlgqtrplpd pffvlatqnp ielegtyplp eaqldrflfr
      181 iqvppvgakt lrallttrvr gappelspvl daeglgrlfa aadrvhlpgp vadfigrlve
      241 asdprqasap davrrfvryg aspraalala aagralallr grpnvgfddv vaaassalnh
      301 rlvlayeasl ekvsaadvvr allqaipevp ra
//
LOCUS       WP_284662201             144 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Myxococcus sp. SDU36].
ACCESSION   WP_284662201
VERSION     WP_284662201.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..144
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=15241
     Region          1..134
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 maggaqdndd eitginvtpl vdvvlvllii fmvtanfivr etvevdlpra anggetvqgl
       61 vnvvldkegk lffdgaelte qdlekrvqea vakdkdtrai isadqsipyg rvmrlidvvk
      121 gqgiakfaln iekdvapaaa paap
//
LOCUS       WP_284662214             941 aa            linear   BCT 25-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Myxococcus sp. SDU36].
ACCESSION   WP_284662214
VERSION     WP_284662214.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 941)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 941)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 941)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 941)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..941
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..941
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=100027
     Region          25..920
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mrdppaaper pdapaparpp agtkppwhal ppdqvlssle staegltdee arqrlsrhgp
       61 nvlertqgdg plkllwrqvn spfiwvlias avlavimgkv tdglvvaavv vlntligfvq
      121 eyragkaies lsrmvpenat viragrklrv paaqgvpgdv melapgdkvp admrlltarn
      181 ltveeaaltg esvpaqkava pvpedvelgd rtsllfggtl vtsgsatavv vatgqatelg
      241 ristllheat dlqtpltqal aviaryitlg ilvisaalla vglvrgyavs eavvvaiala
      301 vaaipeglpa ivtialaigv qrmaarravi rklpavetlg sttvictdkt gtltrnemtv
      361 qalwtthgry alsgvgyspk grltregqpv eapppdvrel llagalcnds alqhrdgqwd
      421 mtgdpteaal lvaaekagvr vddarrahpr vdaipfesen qfmatlhddg kggrrmllkg
      481 apevvlrrcv leegfssstv lteveglarq gmrvlavasr evpvshaalr medvegglrl
      541 lglegmidpp reeamaavra cheagitvkm itgdhpataa aigaqlgllk pdeegipgar
      601 laatedtale evalrsnvfa rvapehklrl vralqrrqhv vamtgdgvnd apalkqanig
      661 vamgvtgtav akdaadivlt ddnfasivaa veegrrvydn likslafvlp tnlglalill
      721 fgvsffpiqe vegrlvplma mlptqllwin lvatvslalp lafearepdv mrraprapga
      781 pvlsrfvlmr tglvallmaa gaiglflwef rrdiprtgqa halaeaqtma vntvisfqif
      841 ylfmcrslmg pvrkvglfsn ravfvgmgll vllqvafmyl pfmqrvfgta plgwedvgls
      901 ilvgavvlpv vglekwlrqr kedtdassgr gaprlrerap a
//
LOCUS       WP_284662530             268 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Myxococcus sp. SDU36].
ACCESSION   WP_284662530
VERSION     WP_284662530.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..268
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28591
     Region          1..252
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mdprktapfe lgrgedacll lhgftgspwd vrplgealaa rglrvvaprl pghgttpqal
       61 ldvtwrdwla aaehalhalr ghrsvfvagl smgallalgl aarhpeavra ltlvapavrf
      121 rgprmflvrq lartpvlewt hswvektgtd isdpealaqa pvlpafpvar lrdvctlqal
      181 airdtarvrc ptlvavaeqd hvvdpeggrw larrltaaps vrvlslrqgf hviprdaagp
      241 llaaevgdfl aqqrsasgwe saapaaga
//
LOCUS       WP_284662573             480 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Myxococcus sp. SDU36].
ACCESSION   WP_284662573
VERSION     WP_284662573.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 480)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..480
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=51947
     Region          16..478
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mtdfrariaa aydadafrre shrlmdtlsd ylarttraeg pvlpwaapav nvdrfaaafp
       61 eaptgdfadl itrvlsssnh lhhpryvghq vtapvplaal cdavssllnn gmavyemgpv
      121 stamernvlr wmaarlglpe ttdgvltsgg slgnltalla arqaragyda wnggahagpp
      181 ltvltaqtth yslaraarim gfgeggvtpv pvdehfrlrp ealdaalesa tragrkpiav
      241 vasagstatg afdplepvad fcerhglwfh vdgahgasav lspahrhlvr gidradsvvw
      301 dahkgllmpa lvtavlfrdg arsfesfsqe asyifhgdse rpwsdialrt lectkemmal
      361 kvyaclavlg tqlfsdavte syeqtrrfae rlsaasdfev avppecnilc frhtpahvpa
      421 eqwdtlqtkl rerlvtrgdf ylvqtklprg vylrvtlinp lttdadldal mdalraaalr
//
LOCUS       WP_284662584             333 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase family protein [Myxococcus sp.
            SDU36].
ACCESSION   WP_284662584
VERSION     WP_284662584.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..333
                     /product="zinc-dependent alcohol dehydrogenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=34895
     Region          1..332
                     /region_name="MDR7"
                     /note="Medium chain dehydrogenases/reductase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cd08276"
                     /db_xref="CDD:176237"
     Site            order(39..41,44,141,145,166..171,189..190,194,209,
                     234..235,237,256..257,281..283)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176237"
ORIGIN      
        1 mkrwqakqag rahlelaeve ipspgagevl irvsavslny reklmldggg yltahqpftp
       61 asdmagvvva agagvhrfke garvianfqt dwvdgpvprg tvrslggnap gvlaeyvimp
      121 epwlvaspgt lddvqastlp cagltawtsl velgglrpgh tvvtqgtggv slfavqlaaa
      181 mgaevivlsg dedklarvka lgaahgihrr htpewhtavl dltrgagadh ilelvggenl
      241 grsvkalasd grvsligvfe gfesrfpvqp lflssgviqg ifvghrrgle nlvravdrla
      301 lkpvvdavyp lealptaleh ldrgpfgklv ita
//
LOCUS       WP_284662759             148 aa            linear   BCT 25-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Myxococcus sp. SDU36].
ACCESSION   WP_284662759
VERSION     WP_284662759.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Schwartz,C.J., Giel,J.L., Patschkowski,T., Luther,C., Ruzicka,F.J.,
            Beinert,H. and Kiley,P.J.
  TITLE     IscR, an Fe-S cluster-containing transcription factor, represses
            expression of Escherichia coli genes encoding Fe-S cluster assembly
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 98 (26), 14895-14900 (2001)
   PUBMED   11742080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..148
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=16075
     Region          2..136
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mhltlhadys lrvllylatr tgrpvstqem adaygiskhh lvrvvqtlag qgvvdaragr
       61 sggvvlarap adirvgsvlr aaepdfhlve cfdrernacp ispacglkgv ldeareafla
      121 vldrytledl lrrsrpnlqd yflpaaap
//
LOCUS       WP_284662836             324 aa            linear   BCT 25-DEC-2024
DEFINITION  fatty acid desaturase family protein [Myxococcus sp. SDU36].
ACCESSION   WP_284662836
VERSION     WP_284662836.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..324
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36714
     Region          12..258
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 magmlryaad rrtmlwclam pvvalsmyva pgwipylcpl acylalsagv iahnhnhcpt
       61 frnrklneam gmwlslfygy ptfvwipthn lnhhkfvnka gdatitwrys kkhnflvafl
      121 fpfvstywqq eptkafidka rernrplyrq iltqyavwgg thvallglam alhgvaggar
      181 iwafaflvpa lfslwtimff nyiqhvhtdp wseydhsrsf tgrlinfflf nnglhtvhhe
      241 tpglhwsllp eahakieagi spalkpvsff gwcfrsyvva pflprfgtaq vgrapyeppe
      301 gvaldvrfgd dlqavdsgvn varv
//
LOCUS       WP_284663075             415 aa            linear   BCT 25-DEC-2024
DEFINITION  trypsin-like serine peptidase [Myxococcus sp. SDU36].
ACCESSION   WP_284663075
VERSION     WP_284663075.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..415
                     /product="trypsin-like serine peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=44227
     Region          188..375
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mlrgirrsmf calglmaaac ggeasrsqve ppvqvvpeaw lgeaagaelp hlealgdvrm
       61 lkdvnaealy reasarqpag dtraaaetpa rpstersfig idvknnkayr lrtdaaslgr
      121 vaeelarrgl ngasrgtldd aarlepvnsd ealtsgtvsg qtwssgvdtr irmgltngya
      181 tnswpyrtig hlsagcsgal vgrrvvvtaa hcvvsaysgw npifntftar rdgatapwgv
      241 qdaiwywvpe gyingscnsv ascnrhdvai mvladnfpng hpgwmghwna ptdtlktwst
      301 ymrgypgcsh vaapasctar tlygdvnlck tgnayspdad gwhqeieigc dgspgqsgsp
      361 iysydapvsg pvvvgqynqy ycdaaacagn afpnrmghlt pswnnsisyf kslyp
//
LOCUS       WP_284663108             515 aa            linear   BCT 25-DEC-2024
DEFINITION  RAD55 family ATPase [Myxococcus sp. SDU36].
ACCESSION   WP_284663108
VERSION     WP_284663108.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..515
                     /product="RAD55 family ATPase"
                     /calculated_mol_wt=55136
     Region          14..230
                     /region_name="RAD55"
                     /note="RecA-superfamily ATPase, KaiC/GvpD/RAD55 family
                     [Signal transduction mechanisms]; COG0467"
                     /db_xref="CDD:440235"
     Region          249..467
                     /region_name="RAD55"
                     /note="RecA-superfamily ATPase, KaiC/GvpD/RAD55 family
                     [Signal transduction mechanisms]; COG0467"
                     /db_xref="CDD:440235"
ORIGIN      
        1 mtdtaerpde pdarvssgvp gldtllrggf frggtyiiag apgtgktilg nqfcfatvaq
       61 ggravyltvl sesharmmqh lrsmnffhpe avgralnyes gsaalkaegl aglgklifra
      121 vrehgatalv vdglvameer sedplrlref lhglcvhnal agcttllltg qhggpadpry
      181 tmvdgvvalv qervgvksvr lvevtkfrgg pqvpgqhgfh ishdglsihp rveavytrlp
      241 artlatdarv tfgvpsldem lsgglvrdss tlvagppgsg ktqlglhflm egarrqepgl
      301 ylgfvetpsr lvnkaermgl algghvdagr vhlvsrmaae sqpdalaeel fgwvkqhgiq
      361 rlvldglgsf cqeltdpert prflaalmye llnlgvtpll lqqtralaap eadarlnvea
      421 lvdnvlvlrl valrsrnyhv lsvlkaresd hdaaqrlfsm tsrgievaad sesaealfng
      481 qtpsqaappr kpkrkagskp vvrrgkpsrr ggrga
//
LOCUS       WP_284663320             414 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Myxococcus sp. SDU36].
ACCESSION   WP_284663320
VERSION     WP_284663320.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..414
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=45696
     Region          15..392
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mslnsgrvda ptahaprlqg hlpvldgvrg lavllvvffh tthlsdqsva grvtwwlaga
       61 gwtgvdlffv lsgflitgil weakgqpyff rnfymrrflr ifplyylala vsflvlpsla
      121 grlglderit tdgavwylly lsnfyqlwvd tthpilgvvw slaieeqfyi vwpfliaavs
      181 yrgairlclg tiamailvrv gltlygasie styvvtfcrv dslamgglla malrhpeglg
      241 lkafpwmrwa awasvpvvla lvvlpvgptf elvkrtagyt aiavlyavcv ykavavskgh
      301 vlhrflttrl lltfgkysya iylihsplda ilrrtvlktp lktvagsdmp mqlvfyvvaa
      361 glslglalvs wnlfekhmlk lkdhfpygqr papapvplpe gaqaerteap arva
//
LOCUS       WP_284663336             318 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Myxococcus sp. SDU36].
ACCESSION   WP_284663336
VERSION     WP_284663336.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..318
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=35171
     Region          75..294
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(75..76,79..80,82,106,109..110,113..114,116,140,
                     143..144,147..148,151)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          75..99
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          104..134
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          139..167
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          206..234
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(207,210..211,214..215,217,241,244..245,248..249,
                     251..252,275,278..279,282..283,286)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          239..269
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mqgaegarhr tlsrgtrsll ivctvvtlih liplfiprnm peqqlsiara mssvsqrvpf
       61 lrplkddaka tpaelreaat lllegapdda halareaerr spqevetqll laricdverm
      121 srcvstalsr aetlaprdsr pdllraelqe kdgdvvgaae ameraydkap ddplvglryv
      181 hllsaakrgd ealavlqkle grlpharllv eqgrvhsqeg qdteavklfr aavaedpkls
      241 mgffelglaw hrlgkvdtae ealrqadrld radpkalaal caiqlkerrv ddarltrmdl
      301 errfsgqpel irkscsip
//
LOCUS       WP_284663358             402 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Myxococcus sp. SDU36].
ACCESSION   WP_284663358
VERSION     WP_284663358.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..402
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=44554
     Region          1..391
                     /region_name="CoxE2"
                     /note="Uncharacterized CoxE-like protein, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3825"
                     /db_xref="CDD:443037"
ORIGIN      
        1 mflpffyelr rrglkvgaqe alalagalra glhdshldgf yhvarallvh setqldafdq
       61 aflahfqgve tasleltqel lnwleearer pdlnpeelal leqldpeeir rlfeerlkeq
      121 kerhdggnrw vgtggtspfg nngfgregir vgggagnrqg ralmqagarr yagyrddvvl
      181 dtrqmavalr klrafardga pdeldvdesi aatarnagel evvtrpprrp ntrvvlamdv
      241 ggsmdpyaal vsrlfsvasq athfkelrty yfhncvygkl yatpqltggi tvpelvaqvg
      301 rhhklvlvgd asmapyelsi rtdaqghykt dglegltwlm qlaqhfernv wlnpepmgtw
      361 rtgtisviar vfpmfaltve glgeavthlt rgrtvrgaaa rr
//
LOCUS       WP_284663389             445 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Myxococcus sp. SDU36].
ACCESSION   WP_284663389
VERSION     WP_284663389.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..445
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=48359
     Region          46..>439
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mmtpdtttee lpgdprrprv mftvagtvfe fvrklemrst gellmlarrr yrnglsgpvv
       61 vkrlrnpatf verrrlveev dltfrlnhpa iakvmllkly rgaphvvmeh vegrsldtvl
      121 nlaamrrrpl saafaahvta evaealnhah gltdewgrpl hivhrdvspr nirvgvhgev
      181 klthftvaas slpgrevtsr elvkgdiaya spealrrrkv darsdlfslg lvllelltgr
      241 hplmvddlap vlepeplelh aqgptwmpvk evavrmaqvg peqverlaag vteplraill
      301 ralrqdpser fqtgaemaea lrawleaqgg aqgrraiaqe veqaaveatv rrnqaelleg
      361 glqpegltve eaalagepss etplgeaags airlsqvael tlearitqtv epaaessddg
      421 dappaplaps ttdpeatask kpgtp
//
LOCUS       WP_284663533             146 aa            linear   BCT 25-DEC-2024
DEFINITION  SRPBCC family protein [Myxococcus sp. SDU36].
ACCESSION   WP_284663533
VERSION     WP_284663533.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..146
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=16630
     Region          5..137
                     /region_name="SRPBCC_CalC_Aha1-like"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of Micromonospora echinospora CalC, human Aha1, and
                     related proteins; cd07814"
                     /db_xref="CDD:176856"
     Site            order(6,8,10,19..21,23..24,29,43,45,47,49,62,64..65,67,70,
                     76,78..79,90..91,93,95,105,107,109,111,116..124,126..128,
                     131)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mttktirrel kftqppaavw ralatreala dwmypndfep rvghrftfrv ppdarakfdg
       61 ltvhcevlqc appseleftw vvgegwldtr vryrleadge gtrvlfehsg fkedqafhga
      121 efgwklmhgk laktlekesn npalka
//
LOCUS       WP_284663593             567 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Myxococcus sp. SDU36].
ACCESSION   WP_284663593
VERSION     WP_284663593.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..567
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=61511
     Region          12..507
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mpaegfpidf yrgerigkye vvtqlsvggm aelflgftsg pggfrkyvvi krvlpdardn
       61 aqfermflde aritaafnhp niaqvfdlgr eddglylame fiagqnlnqi tgaclrrheq
      121 lplgftlsva rdvcmalhya htytapsgap spvihrdvaq knimvtydgv vklldfgiak
      181 akdslertnv gtvkgttgym speqvrgetl dgrsdlfavg vmlhelitga rlfagqnerd
      241 emmkileepv pwpshvaphv peevskvvmr alersrekrf atgrdmarai eaaagkllld
      301 ahdraalmkd lfaermsatr vmlesadgtt ngvmlesakr alrgddgpyl perkdlptps
      361 ngvagmprkp srkvqaavap rkpaaagprq ppesktsnvl wglvllgilv gggyaawhls
      421 kvlnetveee dasalrtlpr hdpnlpiypv pgydaptpda gtpeapakav gaavggedve
      481 esrpkeaasp rpakgrgklt llvlpeaevf rgkkrvgrtp mfnvampvge hdltlvgpdg
      541 kkrmlsvpit agettqfrlk laeiper
//
LOCUS       WP_284663680             491 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Myxococcus sp. SDU36].
ACCESSION   WP_284663680
VERSION     WP_284663680.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..491
                     /product="ATP-binding protein"
                     /calculated_mol_wt=55832
     Region          6..330
                     /region_name="COG1672"
                     /note="Predicted ATPase, archaeal AAA+ ATPase superfamily
                     [General function prediction only]"
                     /db_xref="CDD:441278"
     Region          <365..418
                     /region_name="DUF4143"
                     /note="Domain of unknown function (DUF4143); cl24018"
                     /db_xref="CDD:474127"
ORIGIN      
        1 mkswgfygrh qelgrlreil arkrwfflkv sgrrrigkts lvqqalqpsq rekvlyiqip
       61 dsdpagvvst ardfmqmfgi sdglpsnlrs latrigslae agwivaldef qyfnrkvlfe
      121 ftsqlqaevd rlaaradqvp gglivlgslh temaalleer naplynritd dldlghldia
      181 sllemltaha daspmrllfl wnlfegvpkf yrdcfeqgvi agerrellrq mffssssplr
      241 teadnwflke lrgrydlvlk fiathpgcsn adivahvrsv epdsekqvgg ylkilderyr
      301 mverlqpifa ktttrsgrfy irdnflrawl aalsvpvasv sfrpleslvt qvderlvdae
      361 ghglerlaat lyeersrlel gdfaltqrvk gwwdrndtel dlvalndder ilrlgtckrs
      421 peklvkdlgr fdghiqrfls veqryrswkv ervaisplls gdhrqaiqna gyipqdladl
      481 tkglssasan s
//
LOCUS       WP_284663748             184 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Myxococcus sp. SDU36].
ACCESSION   WP_284663748
VERSION     WP_284663748.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 184)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..184
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20071
     Region          <58..140
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mrhlvaniat ytiaallilg salfawmrsa qlvlsdeyat laryeptpeh qfewrevgeh
       61 ayasncrnch ggegqgwdqy pglqdtarlf aapggreylv elhlhgltsp rwgapmpsmg
      121 hlpdvelaav lnhvlthfgn tpppgtrlyv padiaalrgp krspwevnel rpggaeeasg
      181 rtvn
//
LOCUS       WP_284663878             478 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Myxococcus sp. SDU36].
ACCESSION   WP_284663878
VERSION     WP_284663878.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455327
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..478
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=51028
     Region          35..280
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
ORIGIN      
        1 mnrslllvaa tgvlavgall lgtppappap pppivtdtsh tvkrpedppa trtlplvtsq
       61 pedgalrmag klsgayvqtg pseafawlel karpaetgqr vpvslalvld rsgsmngqkl
      121 adarraatel vqrltpedrl afidygtdvr vqpsrrmtee araelltlis glqddgstni
      181 sgaldaaana lrphlreyrv sraillsdgq pttgivsepg lldqvhqlrr dgitvsalgv
      241 grdyqetlmr gmaeqgggfs gfiddsarla evfsreldqa tstvarlvel rldvppevrh
      301 vevmgmasfr egnvlkvply dmasaqtvrv maklslhtpr tagalallna rvhyvdvard
      361 lpaetalrlt aevtsdldlv rayldkevrv hatralgtqq mvaaaeemkr gnkakarsll
      421 dnarsifgts aaslsgelad vsrsqaalag assaeeaqae srnllkksik nfgqnnty
//
LOCUS       WP_284663881             574 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Myxococcus sp. SDU36].
ACCESSION   WP_284663881
VERSION     WP_284663881.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 574)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 574)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 574)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 574)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..574
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=62505
     Region          54..555
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          316..557
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 masgsaplsm mhldseeada llkegvlrll leqagealvl vdvtgrvlaf nmeagrqfrm
       61 srperaeqgw lpgcvwtrae dasmsvevpp laraltgewv aearwrvrrq dgthvllras
      121 avplehdegl tagallrace vassagldav gsarllaeag allgaafdde aaprllrllv
      181 paladaavly lglpgepprp vtalhaeper hglleellrr yplppervlp lfgagqserl
      241 rvteahmeaa ardaeharll rglglrcylg vplvarervi gtlalfrade irdfsteelr
      301 laeevarrta lsvdnaqllq eareavrlrd eflgiashel ktpltplhlk vqllqkqvdg
      361 maahnqpvsa ervsetlevv qrqvrkltsl vdnlldvsri tagrlrleve emdlasvaae
      421 ilyrfapsas qlqcelelha pvpvmgrwdr lrleqvvtnl lsnalkygag hpvrvaveae
      481 glsarltvrd ggigisaedl priferfera vsdrhygglg lglyitrqiv eafggtvrat
      541 sepgqgsvfv lelprgdipe ewlmahgape psss
//
LOCUS       WP_284663919             328 aa            linear   BCT 25-DEC-2024
DEFINITION  formylglycine-generating enzyme family protein [Myxococcus sp.
            SDU36].
ACCESSION   WP_284663919
VERSION     WP_284663919.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..328
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=36208
     Region          85..327
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 mfaqsvtsps ecrssfarkp sqrsmcvect ggggtwekss sagswgcalp kgvdrigqfr
       61 rsksvkrdeg pkkpssvgah fakyvavpag tfqigsdged vdrksneyva qvkltrgfsm
      121 katevtqgew ffitgkpndf ydaecgydca avgmnffqal eylnalskre klepcyeidg
      181 dkaswpkgld ckgyrlptea eweyaargks terrygelee vawydknsdn klkpvaqkka
      241 nayglfdmlg naaewvwdis eytafdkege vvdpiiggtt lgdygvertv rggsaldrpy
      301 dsraafrsqa ypkasldrig frpvrtlp
//
LOCUS       WP_284664029             774 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein [Myxococcus sp.
            SDU36].
ACCESSION   WP_284664029
VERSION     WP_284664029.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 774)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 774)
  AUTHORS   Porat,A., Cho,S.H. and Beckwith,J.
  TITLE     The unusual transmembrane electron transporter DsbD and its
            homologues: a bacterial family of disulfide reductases
  JOURNAL   Res Microbiol 155 (8), 617-622 (2004)
   PUBMED   15380548
REFERENCE   4  (residues 1 to 774)
  AUTHORS   Kimball,R.A., Martin,L. and Saier,M.H. Jr.
  TITLE     Reversing transmembrane electron flow: the DsbD and DsbB protein
            families
  JOURNAL   J Mol Microbiol Biotechnol 5 (3), 133-149 (2003)
   PUBMED   12766342
REFERENCE   5  (residues 1 to 774)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   6  (residues 1 to 774)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   7  (residues 1 to 774)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   8  (residues 1 to 774)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   9  (residues 1 to 774)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12109673
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..774
                     /product="protein-disulfide reductase DsbD family protein"
                     /EC_number="1.8.-.-"
                     /EC_number="1.8.1.8"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=78995
     Region          58..162
                     /region_name="DsbC"
                     /note="Disulphide bond corrector protein DsbC; pfam11412"
                     /db_xref="CDD:463273"
     Region          349..753
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 mthrqskrlg cvggiglllv aavawadlpa savassapde gdpriegall vdatqvkpgd
       61 tfrvgvrfrl dpgwhvywkn pgdsgletev awdtpgvtvg plqwpfpqtf rtpdgfitth
      121 gydgeailva daravegaat gtvtvsaave alvcevhcip aelmltrsip lgpqtvrdae
      181 taavldaela kvprpaqdsg haatlaldap qltagqdftg tltltapgga avpavegdff
      241 vadripgvar vglasdgpgr fklkgkaepd aqasapgltg vlrlgtaatg yqylevtapl
      301 apmvaaggaa gtpaavkpps vkdsiaavkp vgaaiapppa aessmglgla lvfaffggal
      361 lnlmpcvfpv lalkaygftr mvqqeqgrvg ahaaayaggi igsmlllagg vlavraggas
      421 vgwgfqfqep lfvagvcavl vafalnlfgv fnvgldgtal agkvdqshgl mhsagegvla
      481 vvlatpcsap llgtavgfaf aagpltvlav ftalglglal pfcvlvlvpg lakklprpga
      541 wmerfkqvlg fallattvwl vwvmgglagv dgmarllafl vavglvtwly gqgqaqdgvr
      601 klatvavaag vlvasglltl rfededpvaa prlgsavaqa rpwssdavna alaagqpvfi
      661 dftadwcltc kfnertvlat devrdaftkh qvaffiadwt rrdasittkl aehgragvpm
      721 ylvlspgapd tpevlpellt pgvvadavkr aaecapsklg sganvlcaag fpnh
//
LOCUS       WP_284664341             219 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase [Myxococcus sp. SDU36].
ACCESSION   WP_284664341
VERSION     WP_284664341.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..219
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=23316
     Region          72..206
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mdldalrreq hkrrlswmpw lyfvlkprhr gwaeawqrev qallreletv diaegcfiap
       61 earifaepgr tvsigpgcgi aaevflhgpv tlgprvsina rasldggaag irigegtria
      121 tgatlyafdh giapdrpvre qpvtsrglvi gadvwvgana gitdgvtvgd havvamgavv
      181 trdvpewaiv agvparvvgd rrqrprsgap ggwepedga
//
LOCUS       WP_284664279             557 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Myxococcus sp. SDU36].
ACCESSION   WP_284664279
VERSION     WP_284664279.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..557
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=59249
     Region          5..494
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mavpfgkyel lrkiasggmg qvflarehgt gferlvvlkl ilphlaedde flamfldeag
       61 lvarlthpnl itildlteie grhclameyv qgddvrrldk tsraqgkplp vglilriiad
      121 aaagldyahq ardaqgkplr lvhrdvspqn ilvgfdggvk vidfgvakaa tssqntatgv
      181 lkgkypymsp eqasglaida rsdlfalgvv mwelltgkrl fkgesdmmtl rlvkdcqvpr
      241 psqlnprlpp gldevvlkal apspdqrypd cgafrlaled ytlnlrlpss sahlsaflre
      301 lyadriahet dpakldqlae dadldsrsns slsgvpgvlg pagrssasra mrgsphggpg
      361 trsrhaaaat aapplqektr gtaplarppp epprripwlp vataglglli agvgivffrs
      421 padatpvrpp vevavphqpe iapdvppppr idveparhvn lpviteppga rvsvngearg
      481 etplrlelea gaapvsvtla lngyepvtrq vsatdeelrl elrraeggkp vtvtpaagtk
      541 rpphsgqggg lgiktgr
//
LOCUS       WP_284664483             521 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Myxococcus sp. SDU36].
ACCESSION   WP_284664483
VERSION     WP_284664483.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 521)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 521)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 521)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..521
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54282
     Region          2..518
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mrrrapvglw vagvamaala lvpavylgvr aveadadawg lllrdrtwgl lgrtlglaaa
       61 vtgcaallsl plawltartd lpgrrlwtvl lcvplavptf vsgyvllaaf gvggaleepl
      121 trwglpvppv ygfpgallal tvstypyffl alragmqsqd pawlegarsl gltparaflr
      181 itvpllrpsf asgallvgly vlsdfgaval lqydafsrai yvqyegaydr syaallglal
      241 vsvtvgvlal elwlrgrasy hrsakgaara sslvllgrwr vpalllcgav vavgvglpvg
      301 vlvywgargl svdsgpmmgp awnsvsasml gavaavvgal plaflavryp srltvalerv
      361 syagyalppi vlalslvflg vqavpflygt lvmlvlayvv rflpqavgvv rasllqlnph
      421 lpeaaaslgq ppsgvlrrvt apllrpglla gaalvfltam kelpatllla pigfetlatr
      481 vwgataegrf aeaalpalvl mavstlgvgl lvsqegrssp g
//
LOCUS       WP_284664506             468 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Myxococcus sp. SDU36].
ACCESSION   WP_284664506
VERSION     WP_284664506.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..468
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52000
     Region          31..456
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mfrqsllwas clallsgpva caqtqarpva ksavaaapkl gagiesrtlk nglkvivwpn
       61 hdipsvvlyn wfrvgsrney pgitglshff ehmmfngakk ygpgefdrvm eanggannaf
      121 tsedvtvymd wfprsaldvi fdleadrlqh laidpkvtes ergvvyserr saidndnmga
      181 lmeqvqataf vahpyqfpvi gwpsdieswr iedlqryykt yyapnnatlv ftgavtpaei
      241 falaekylgp ipsqpapepv rtkepeqqge rrivvkkqaq apliqlayhg isgkdadvea
      301 ltlllgilan gessrlhrrl veeeraalrv nthfspgfdp slvwvyadlp pgadvarveg
      361 llteelarvv kdgvsdaelk karnitlsqf wrsletnngr gralgaaetf rgdyrqlfda
      421 peryervtrd dvrevaarif nsqrrtvgwl vpadaqvatp dsrkeasr
//
LOCUS       WP_284664548             550 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Myxococcus sp.
            SDU36].
ACCESSION   WP_284664548
VERSION     WP_284664548.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..550
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=58971
     Region          3..404
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mkanfrqsms wlhtwaglvl gwllfavflt gtiayfrqev tlwmqpelhg svpspraael
       61 glaklaevap dasswtvnlp adrnetlrvs wrkaasrgga erdagrgggr gdglildast
      121 gevlkprate ggnflyrfhf elhamprawa rtlvgiatlv mfiaiisgii thrrffmdff
      181 tfrpskgqrs wldahnvtav lalpfhvmit ysglllvaan llpwssqvif gdnpraamaa
      241 sraaeqkeae alkaelaklg ggtsvpipkl maeaerewgq pvsritvsep gkpgsivell
      301 ptrndslile sgsgglggvk lafvaktger lsppaprags fvgglqaslg slhrarfasv
      361 glrwvfflag vcgtlmiatg lvlwsvkrae krkgapgtlg hrlvdhlnvg avaglsvava
      421 ayfwanrllp vdlasrgdre iqvffavwal tflqplarpl rrawleqlga agllfvaipv
      481 lnalttdshl gvtipagkwl iagfdivafv tglamlhaar kvwrrrqpva pvasrpspsa
      541 ppaaavaves
//
LOCUS       WP_284664590             481 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Myxococcus sp. SDU36].
ACCESSION   WP_284664590
VERSION     WP_284664590.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..481
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53023
     Region          3..481
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 matleqlrfd ntyarlpagf garvhpspfp daklvsvnpa alalldltpe earrpefvaa
       61 lggekplpgm epfamvyagh qfgvyvprlg dgralllgev rnaagekwdl hlkgggptpf
      121 srggdgravl rstireylcg eamqglgipt trglgilgsq apvyreavet gamlvrmaps
      181 hvrfgtfeff hyteqrehva sladhviaeh fphlagqegr yarfytevve rtarliaqwq
      241 avgfahgvmn tdnmsilglt ldygpfgfld dfepgficnh sddrgryafd qqprigmwnl
      301 aclgealltl isedearaal atyqpafnah fmdrmraklg lreardedre lvsdlfarma
      361 eapvdytrff ralgsdarpv rdmfpapegf dawagryrar laaegsvdpe rharmarvnp
      421 kyvlrnwvaq eaisraeagd fslvdrllgv lsdpfaehpd aesyaaappa wgrhlevscs
      481 s
//
LOCUS       WP_284664620             516 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Myxococcus sp. SDU36].
ACCESSION   WP_284664620
VERSION     WP_284664620.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..516
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57521
     Region          28..492
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 msastqgrri vvvgagvggl aaaarlahqg fdvqvfektq gpggrcnrlq vegftwdlgp
       61 tivlmpevfe etfravgrri edyltllkcd pnyrvhfrdg sdvtftselc amgrelerve
      121 pgsyarylaf laqgrvqyrt sldhlvgrny eglrdylspr vlarifqvra hrrmygdvsr
      181 ffqderlraa mtfqtmylgv spyaspavyg llpftelgvg iwfpkgglya ipqalerlar
      241 eegvrfryga pveriltdgg rtqgvrlegg evveadavlc nadlpyaydk lldpkattlk
      301 rkeklrytss gymlylgmkr rypellhhnv vfgrdykgsf ddiferfrvp edpsfyvnap
      361 trtdaslape gkdalyvlvp vphqhpdldw kvegpkvrak ffarmaelgf pslesdieve
      421 rvftpddwag tfnlargsaf glsqnftqig pfrpanqdar vknlffvgas tqpgtglptv
      481 lisarlvter lmtwaqaqgv tlsprtaaap vegvaa
//
LOCUS       WP_284664646             260 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Myxococcus sp. SDU36].
ACCESSION   WP_284664646
VERSION     WP_284664646.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..260
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27547
     Region          1..253
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 msrkvalitg asaglgeqfa hlfakdghdv ilvarsaprl ealaakleqa hgvkahvfpa
       61 dlgrpespeq lfeavrakgl aveflvnnag fgscgpfleq dlareaemve vnctallkls
      121 hlfarpmrer gsgrilnvas taafqpgpfm atyfatkafv vslsealahe lkgtgvtvtc
      181 hcpgathtef tqragngqtr lfqrpgvaka qdvaahayam mlrgrvlsih gllnwvgalg
      241 vrfsprvavr alaaslnqqg
//
LOCUS       WP_284664742             109 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Myxococcus sp. SDU36].
ACCESSION   WP_284664742
VERSION     WP_284664742.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 109)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 109)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 109)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 109)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..109
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11662
     Region          <5..102
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mmkrlvlvls lggatsahad avadvwkakc tvchggdgka rtkmgqkesi gdmsrpdwqr
       61 artdadlrev iangdpsnrk mkpfkdkltp aqidalvgyi rtmkapaap
//
LOCUS       WP_284664770             417 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Myxococcus sp. SDU36].
ACCESSION   WP_284664770
VERSION     WP_284664770.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..417
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=45242
     Region          23..>417
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 msnvddprpt egavlfragd tayeflqslg tgrngervml alartpagiq gkvvlkcvvl
       61 perkfseqyp cararleeev rlarflqhpn iarvhglfem ryglcavmec veglsldall
      121 siaqargryf seafvlyvfa evaaalahah srtddagapl sivnrdvnps rirlrprgav
      181 altdfgvafs rlagriatsl prprgealya ppeaflgarv dargdlfslg ltmlefatgr
      241 hlydpgdlri peaelrltte ehrrvldasi lametglpsf medalwcama yrpgdlaras
      301 agvsqplrai lhkllrrrps drfesaaele aalrarlsel apfgpadavk evqqalldag
      361 aaleefdlle deggfvpagw rehpdpvetr pggrcedevt tapgagarra vkappta
//
LOCUS       WP_284664797             343 aa            linear   BCT 25-DEC-2024
DEFINITION  Leu/Phe/Val dehydrogenase [Myxococcus sp. SDU36].
ACCESSION   WP_284664797
VERSION     WP_284664797.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Brunhuber,N.M. and Blanchard,J.S.
  TITLE     The biochemistry and enzymology of amino acid dehydrogenases
  JOURNAL   Crit Rev Biochem Mol Biol 29 (6), 415-467 (1994)
   PUBMED   7705101
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10500541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..343
                     /product="Leu/Phe/Val dehydrogenase"
                     /EC_number="1.4.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36746
     Region          25..133
                     /region_name="ELFV_dehydrog_N"
                     /note="Glu/Leu/Phe/Val dehydrogenase, dimerization domain;
                     pfam02812"
                     /db_xref="CDD:460706"
     Region          144..342
                     /region_name="NAD_bind_Leu_Phe_Val_DH"
                     /note="NAD(P) binding domain of leucine dehydrogenase,
                     phenylalanine dehydrogenase, and valine dehydrogenase;
                     cd01075"
                     /db_xref="CDD:133444"
     Site            order(178,180..182,201..202,206,235..236,257,259)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133444"
     Site            289
                     /site_type="active"
                     /note="Phe binding site [active]"
                     /db_xref="CDD:133444"
ORIGIN      
        1 msyftqlleg gyeavhllsd sktglraivg mhntrlgpgl ggtralstyt seeeavadal
       61 rlargmtyka alaglphggg kavimlprgs fdrerifesf graveslggr yittedsgts
      121 pddmehvrrh tkyvvglker sgdpspvtay gvarameata khvfgspdlk glrvtvlgvg
      181 hvgmylvkel hqrgarvwvs dlnpasvqha vtqygatavd adalhrmead iyapcalgga
      241 indttlplln vkavcgaann qlltsrhgeq larrgilyvp dyaanaggli nvaqewagyd
      301 rdkaysrash ifdtidtvlt rakesglrpe qvadrmveer lag
//
LOCUS       WP_284664839             469 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Myxococcus sp.
            SDU36].
ACCESSION   WP_284664839
VERSION     WP_284664839.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..469
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=50534
     Region          6..467
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mneslkgtvl lvdddpavak vlgalltqag ltthaardgq ealallaskp vdvvvsdvrm
       61 pgmdglqvla evsrgwpdvp villtahgtv plaveamkag aadfvlkpfd reeilftvrk
      121 allraqgeea rqqarptggf igrsrpmadv qavlakaaag tatvllrges gtgkelaaka
      181 vhdgsprreg pfvklhcaal pdtlleself gyekgaftga atrkpgrvel ahggtlflde
      241 vgdispavqv kllrviqere lerlggtqtv kvdvrfvaat hqpleervke grfredlfyr
      301 lnvvpvwlpa lrerpddiep lalhflevha ktngrppftl tpdglaalra qpwpgnvrql
      361 qnflerlvvl sdtqvlggqe vlnelarqpg lspaptstlp vsaaspssel qaaptadsar
      421 tlesqrkeme rqamtdalrr agdnrtlaar llgisrrtly nkleeygll
//
LOCUS       WP_284664991             340 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Myxococcus sp. SDU36].
ACCESSION   WP_284664991
VERSION     WP_284664991.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..340
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37841
     Region          18..332
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mdrterildl vallldarep iswaelrehf pgdyggsdda aerkferdka elvelgfplt
       61 yaqgdderrd gylvdrdayy lpeadlskee lavlyaagsa alasgafpgr ddlahalrki
      121 gffagqslpt prvrmelgsv hegqekevsa rleqlwdaca arkwvdltya spkqagttqr
      181 rvdpfglalr rgawtlvgyc hlrkdlrtfh vhrirelkvn tarprtpdfq vpadfsleah
      241 vayfpwqhrf heqvevvlhl sgtlasraas llpgatlepa eagavrarlp vtfvdglmrf
      301 clalgpdcrv egperaqarl remasrivac hddsldkvsa
//
LOCUS       WP_284663931             345 aa            linear   BCT 25-DEC-2024
DEFINITION  synaptic vesicle VAT-1 family membrane protein [Myxococcus sp.
            SDU36].
ACCESSION   WP_284663931
VERSION     WP_284663931.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Kim,S.Y., Mori,T., Chek,M.F., Furuya,S., Matsumoto,K., Yajima,T.,
            Ogura,T. and Hakoshima,T.
  TITLE     Structural insights into vesicle amine transport-1 (VAT-1) as a
            member of the NADPH-dependent quinone oxidoreductase family
  JOURNAL   Sci Rep 11 (1), 2120 (2021)
   PUBMED   33483563
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Watanabe,Y., Tamura,Y., Kakuta,C., Watanabe,S. and Endo,T.
  TITLE     Structural basis for interorganelle phospholipid transport mediated
            by VAT-1
  JOURNAL   J Biol Chem 295 (10), 3257-3268 (2020)
   PUBMED   32005660
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   6  (residues 1 to 345)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   7  (residues 1 to 345)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..345
                     /product="synaptic vesicle VAT-1 family membrane protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36804
     Region          4..345
                     /region_name="MDR3"
                     /note="Medium chain dehydrogenases/reductase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cd08275"
                     /db_xref="CDD:176236"
     Site            order(42..44,47,127,131,152..155,157..158,179..180,181,
                     196,219..220,222,241..242,284..286)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176236"
ORIGIN      
        1 mrarkvvirk aggygqlhle evnqdspgvg evrvateaig vnyadcvirm glyasakeyv
       61 gwpitpgfef agrveavgeg vedlapgarv fgvtrfggya thvtvprhqv falparlsme
      121 qaagfptvfl tayyalfela hprpgahvlv hsaaggvgga llqlgriagc rmvgvvggth
      181 kvetalaqga avvidksrea lwaaaeraap rgydvvldan gpstlrdsyk hlaspgklvi
      241 ygfhsmlprt ggrpnyakla wdwlrtprfd pltltndnts vlafnlsylf eqravleesm
      301 arllgwleeg klvpppvksf pldavadahr alesggtvgk lvlvp
//
LOCUS       WP_284665168             224 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Myxococcus sp.
            SDU36].
ACCESSION   WP_284665168
VERSION     WP_284665168.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..224
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=25010
     Region          <21..213
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mprpppdvir ypsyytpsvr ralsradptl galmkqvgpf rlqvrplhsp fgalaesivy
       61 qqlhgkaaat ifgrvcervg sgrkftpqal lavpdtslre aglsanklaa lqdlarktld
      121 gtvpplakvr rmddaelieh ftqvrgigqw tvemllmfql erpdvlpvdd ygvrkgfmka
      181 yglpempkpk alfafgerwr pwrsvaswym wrsaelpdtp pveg
//
LOCUS       WP_284665233             478 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Myxococcus sp. SDU36].
ACCESSION   WP_284665233
VERSION     WP_284665233.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..478
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53278
     Region          38..463
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mrkvfgaval aaftgcattq etqkpepppa aetakveapa eqpklqvpvd yykldnglkv
       61 vlsrdssapk avvavyynig friepkdrtg fahlfehmmf qgstnlgkme firliqkngg
      121 vlngstrfdf tnyfevipsn tlepilwaea drmrgldvte enlknqqgvv mnevkvnvln
      181 qpyggfpwld mpqvansnwy nahnfygdlk dleaasledv raffktyyap snaalvivgd
      241 fepeqvkgwi qkyfgplptv aqpskpdise prqtkekrhd kqdklaqrpa lavgyhmpdv
      301 gtpeyyamal vdevllrgnd salyqqlvqk kgltgevsgg vnqlgnhwny ngpmqwtayl
      361 fhdadtttet llaefdgvva rlqeqpidaa tlerarvkar srlygqlegf lgfgradlla
      421 sfalffddpa rinrleselm kvtpeliqkt akeylrrenr tvltvtpaaa taaqtkap
//
LOCUS       WP_284665292             416 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Myxococcus sp. SDU36].
ACCESSION   WP_284665292
VERSION     WP_284665292.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 416)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007442
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..416
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46024
     Region          <45..>96
                     /region_name="decahem_SO1788"
                     /note="decaheme c-type cytochrome, OmcA/MtrC family;
                     TIGR03507"
                     /db_xref="CDD:274617"
     Region          179..273
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
ORIGIN      
        1 mdlrslplsy lagvailvat agggfvlvrd advlalrlpt kvlaptkrap etprdavehf
       61 qcnrchvvpg iepasaplse ncvtchqait agrldpwyke aevqrwkehl thlmrtpdlr
      121 slgqrvkrsw liawlqaphm vrplygatmp rmkidpkdae riadflavte eeseepprgd
      181 aaagralyek nacaschylg daplaalryg apefrapsar rrapdlryvr srmslaqlrr
      241 wlraphsilp dtemptfpft prevedlaaf lrepaaevaa gpgppykprl lerevrypev
      301 arkltrhlcy hchsdsrrgg dqgpgntggf gydgvsldla tragilrgik rdgrfrglpd
      361 rmedgtprlv aslvarhael dghahpsvtg mplgfpplpd edidllftwi eqgape
//
LOCUS       WP_284665372             283 aa            linear   BCT 25-DEC-2024
DEFINITION  exonuclease/endonuclease/phosphatase family protein [Myxococcus sp.
            SDU36].
ACCESSION   WP_284665372
VERSION     WP_284665372.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10178909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..283
                     /product="exonuclease/endonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006308 - DNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=31377
     Region          32..282
                     /region_name="DNase1"
                     /note="Deoxyribonuclease 1; cd10282"
                     /db_xref="CDD:197337"
     Site            order(37..38,40,44,69,71..73,105..106,108,136,159,162,193,
                     195,200,232,236..237,274..275)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197337"
     Site            order(37,69,108,159,193,195,237,274..275)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197337"
     Site            order(37,69,274)
                     /site_type="other"
                     /note="putative Mg binding site IVb [ion binding]"
                     /db_xref="CDD:197337"
     Site            order(39,159,193,195,275)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197337"
     Site            39
                     /site_type="other"
                     /note="actin binding site [polypeptide binding]"
                     /db_xref="CDD:197337"
     Site            order(40,44,71..73,105..106,108,136,159,162,193,195,200,
                     236,275)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:197337"
     Site            order(129,137)
                     /site_type="other"
                     /note="Ca binding site II [ion binding]"
                     /db_xref="CDD:197337"
     Site            order(193,237,275)
                     /site_type="other"
                     /note="putative Mg binding site IVa [ion binding]"
                     /db_xref="CDD:197337"
     Site            order(197,223)
                     /site_type="metal-binding"
                     /note="metal binding site III [ion binding]"
                     /db_xref="CDD:197337"
     Site            order(226,228)
                     /site_type="other"
                     /note="Ca binding site I [ion binding]"
                     /db_xref="CDD:197337"
ORIGIN      
        1 mpslktfshn fvatllilga mtwardasaa lkvaswniqi lgsnkiknpd vvkviidtik
       61 qydlilvqei kdttdatams llnqvnaatg naygilvsnr lgrtsareqy ayfykksalk
      121 vvdsyhyada ddlfarepfv vrfsttqatv knffvvplha epsaavaeig slvkvyddaa
      181 krwnikngil mgdwkagcsy fakkywgtnp lrsdarftwl igddnnstvg ksdcaydrav
      241 vagdklrana akgrtayvdt kfnltlefmr lvsdhypief ein
//
LOCUS       WP_284665537             538 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Myxococcus sp. SDU36].
ACCESSION   WP_284665537
VERSION     WP_284665537.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..538
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58415
     Region          66..479
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mktrallslt allglagcat tpqapppdek apppaapaqa aapepapppa rpeavpatpl
       61 rqpepmelvv laqpdspivs frlvfhtgsv ddpkgkeglt altarlmaeg gtqkltssql
      121 lealypmaae ldvfvdkeft tfsgrvhkdf larfqdlftd vllaprldaa elerlranai
      181 sdvenglrsa ndealgkaal dalifeghpy ahftggtvqg lkaltlddvk ahaqrvftqd
      241 rlviglaggv dealaqtlrs rlsalpakga prvalpavpt tagrtviiqk ptlstavsmg
      301 avstirrgdp dffpvafams nlgehrqsig vlftelrekr glnygdyaya ehfiespgtt
      361 ynrtniartq qdlslwlrpv vptqgvfatr gavffldqmv eegipqerfe lmrgflqgyt
      421 rlweqtdqrr lgyaidgrfy gtpdfleqyr qamskmtpks vqealrrrvr pealnfafvt
      481 edaeglaqal rsgapspity aspkpetlla qdqaisaskl plrpeaiqvi paqqfmek
//
LOCUS       WP_284665466             495 aa            linear   BCT 25-DEC-2024
DEFINITION  TolB family protein [Myxococcus sp. SDU36].
ACCESSION   WP_284665466
VERSION     WP_284665466.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..495
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=51293
     Region          136..300
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          294..460
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 mtmrvvfsal cgallvlstg cgdecvdafd crsdngpppe gqewtcrsgn celrdvqppp
       61 eedagteeda gteedagtee dagteedagt dagtgggvvv igtgakgeac tssadcaagl
      121 rcegaaeamt cqslhvafta mddtdamaav vtrfdepept rlsdaavdsr yprwnpagnr
      181 iafvqgatet gtstgnlage lvardvpfve veptvlangt tgstegflyl ewepgdslly
      241 vrragdsisg isrvpaeggt veeataagtf pdwrngdtfa fststvglst atvggaptpl
      301 aiagataeqp hynrvndqll flrpddtrpv glnaalyivp vggaavqtia efsttavegg
      361 svdsyianpa wapdgswvay vrayffnptt gepvlcgagt spcagdpgni vflrrinpad
      421 gtpegdevsf aegatlpsfs pdahyvayvq ggqlyvqqid paagakvgdp iihpvgdytl
      481 qtsrgddhrp rwqpr
//
LOCUS       WP_284665580             713 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Myxococcus sp. SDU36].
ACCESSION   WP_284665580
VERSION     WP_284665580.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 713)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..713
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=74087
     Region          72..558
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mrlaaripll stlltsllls acgsespeps hpvtggaltq laatpapler petrrrfapg
       61 qaivklkdsa karasatvps vrgyqtalie plpggaslvs lvreqplara svaeeeastl
      121 aaiealrqdp dveyahenly felfatptdp lyslqwnypa mnlpqawntv tgnvtiavld
      181 tgrldhpdll grwttgydfg dgdadpyatg tyhhgihvag ilaarpnngv ggagicwgcq
      241 lmplkvsasn ggilmtgvna airhaadnga rvinmsfgag ynpnapstlh pcsnypdmqs
      301 avnyalskgv vlvaaagnhg aanyqtanvt pascngviav gastqsggva nwsnkgsrvd
      361 viapgglasa slygqgigcl pdstmdpyvs gtdqivsawa tgkpssaltp gdycyrylsg
      421 tsmsaphvag laalmlsqkp sltpaqvtar ikqtatpvsg caghcgtgrv naaaaiythl
      481 psrptqglww nparsgnaid lqhvaadqly vtwftytsag tpiwyisslh aepgewrgdl
      541 vrtswngasa ttsvvgtarl ilsggqwhfy wmlggftgse piqpfvfasg apamnltgvw
      601 ynplqsgwgv tfasqgtlhv anvtvyqgsn pvwlqgvvns sgtslsfpms yitgynlcpg
      661 csgtpsvnst pagtftihga agipsavpss lsvsfpggtw nrpsfslqrl tgp
//
LOCUS       WP_284665836             470 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Myxococcus sp.
            SDU36].
ACCESSION   WP_284665836
VERSION     WP_284665836.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 470)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..470
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=50845
     Region          2..449
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mtsptvlvvd ddranldsvv rifqregmat laaangteal ellrrpevaa mvtdlmmpnm
       61 dgqellraar airpdvevvl mtaygtveta vaamkdgayd fitkplkrha lvkaiqkale
      121 kralvaenqs lkaklaemna aggrsmvgqs paframldti rqaapstatv lllgesgtgk
      181 elaarsvhef sqrargpfva vncgalpeni leaelfgver gaftgavarr egrferahgg
      241 tlfldevgem plpaqvkllr alaegeierl ggtqtvrvdv rlvaatnkdl qkevaegrfr
      301 edlyyrlnvv eirvpalasr redipllada flrrfaakng kvlrgfsqea lgvlenyawp
      361 gnvrelehav eravvlarge vleasdlpea vrkgplgsag qlvipigtpm eeierrvihe
      421 tlrhtrgdkt laarllgiaa rtiyrklere qstgdgsgaa ppgpdtdtdd
//
LOCUS       WP_284665864             325 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Myxococcus sp. SDU36].
ACCESSION   WP_284665864
VERSION     WP_284665864.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..325
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35587
     Region          1..321
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mradrlvslt lllqtrpkmt agelarelqv sertihrdld alsgagvpvy atrgaaggvs
       61 lmegwrtqlt gftrtelhal aavaapgald dlgltsalrs glvklaaslp alqqpaleya
      121 rqrlhvdass wfpereavph latlrdavwq drrvsltyrd fegkpsrkvv dpyalvikad
      181 rwylvartge eeprvyrgsr vegarmrpet fvrparfdlp afwkawcsrf aekratyevt
      241 lrltpealea lrrirpaadg arldaaplaa dgrktvvvdf ereaialgql cdvstgfevl
      301 apdalrtrfl alatgildah ggaap
//
LOCUS       WP_284665877             376 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Myxococcus sp. SDU36].
ACCESSION   WP_284665877
VERSION     WP_284665877.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..376
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=38656
     Region          17..340
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 mhyalvllal gglltlhelg hlvaarllgv rvprfvfgfg pplvsfrlwg tqyvvaavpl
       61 gatahlqgmn phradadeaa gfaargpllr iliilagpla nyalalgvlf alytsgthvv
      121 vpltvgtvqp gseaaraqll pgdrivkvae qplrswsefv ekvgaapgvp leldverggd
      181 arsvvvrprr dergtgrigv sqqyvykahs agealshsft htgkvaaegv allnrmmrhg
      241 lesadaaspg alvrqesada masgtdallr tlvaasvvla lltllpvpgl dggrvvlllv
      301 eaasgrripp rvetvaqtvg flgiavavvl mataeirral parlgledsp aqdagtgagt
      361 nappdagatg tadagp
//
LOCUS       WP_284665940             198 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Myxococcus sp. SDU36].
ACCESSION   WP_284665940
VERSION     WP_284665940.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..198
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=20898
     Region          10..194
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mhmnadqtll vlasasprrr ellsqldlrf tvsaadidet phageaaeay vgrlarekar
       61 vvasrhpgaw vlaadttval gaellgkprd aeeaqamltr lsgrthdvyt gvalagrhee
      121 mlvvrtrvtf ralsagemsw yahsgepldk agayaiqgrg gflvasvegs tsnvvglplg
      181 etvallerag valpwsts
//
LOCUS       WP_284666006             121 aa            linear   BCT 25-DEC-2024
DEFINITION  (2Fe-2S) ferredoxin domain-containing protein [Myxococcus sp.
            SDU36].
ACCESSION   WP_284666006
VERSION     WP_284666006.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790154
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..121
                     /product="(2Fe-2S) ferredoxin domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=13129
     Region          1..110
                     /region_name="COG3411"
                     /note="2Fe-2S ferredoxin [Energy production and
                     conversion]"
                     /db_xref="CDD:442637"
ORIGIN      
        1 mkryrvsvck gssckaggad avhaeardtl saqglvprce lyrggcygfc hmgpnvvvre
       61 dtggkrdpls pedyqlmgwp gevyysamta ekmrrvvaeh iakdspvkel fgqpdsddge
      121 q
//
LOCUS       WP_284666007             254 aa            linear   BCT 25-DEC-2024
DEFINITION  NuoI/complex I 23 kDa subunit family protein [Myxococcus sp.
            SDU36].
ACCESSION   WP_284666007
VERSION     WP_284666007.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Yu,H., Schut,G.J., Haja,D.K., Adams,M.W.W. and Li,H.
  TITLE     Evolution of complex I-like respiratory complexes
  JOURNAL   J Biol Chem 296, 100740 (2021)
   PUBMED   33957129
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..254
                     /product="NuoI/complex I 23 kDa subunit family protein"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=28431
     Region          21..192
                     /region_name="PRK05888"
                     /note="NADH-quinone oxidoreductase subunit NuoI"
                     /db_xref="CDD:235637"
ORIGIN      
        1 maykvskdpr tdirertyvp nllrglgita khffrnlfgt rdtntqvvdr tgaslmttva
       61 ypeekpiype gyrglhrlvp redgkprcva cymcaticpa qciyieagey edeasdsedr
      121 viekyptqfv idelrcivcg lcvdacpkda irmdtythtp peytrqnfvy dipkllkgpp
      181 vshpsdpwnk regseephhv hkeahtrige glvelklphg ahdghgkalp agahaghqtv
      241 vtqqgpiqvt kfik
//
LOCUS       WP_284666008             477 aa            linear   BCT 25-DEC-2024
DEFINITION  complex I subunit 1/NuoH family protein [Myxococcus sp. SDU36].
ACCESSION   WP_284666008
VERSION     WP_284666008.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Friedrich,T. and Scheide,D.
  TITLE     The respiratory complex I of bacteria, archaea and eukarya and its
            module common with membrane-bound multisubunit hydrogenases
  JOURNAL   FEBS Lett 479 (1-2), 1-5 (2000)
   PUBMED   10940377
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..477
                     /product="complex I subunit 1/NuoH family protein"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=51256
     Region          47..412
                     /region_name="NuoH"
                     /note="NADH:ubiquinone oxidoreductase subunit 1 (chain H)
                     [Energy production and conversion]; COG1005"
                     /db_xref="CDD:440629"
ORIGIN      
        1 msrvltilva mftivflmag gmasaylvgg lveehwftga srltnvlflv lifvmviatl
       61 ltmaerkwsa fiqdrmgpnr arialpglkn rslgglphil tdvlkmltke dlipatanrf
      121 mfnlgpilaf aptfalfavv pagpsvqvfg rnvdmvvatp dfgvlyvlai aslavygtal
      181 agwasnnkfa llggvratsq misyevalgl slvglfltfs svqfpaiigd igsaltggtg
      241 qaqylwrtdg afdlglpawg ifiqplgfll ffaasfaetk rapfdlpege seiigyfvey
      301 sgmkfglfmi sefvevvvla gvttalffgg yhlpfgnewl anlpvmqehg wllgtilgtv
      361 fwlkvlfliw vqllirwtfp rfrydqiqsl gwkillpigl anvfvtgalv lwdpslrala
      421 ilglaeigll vvlttttkvp eggdahggah ghdhghgghg ahdvpahahg aapasth
//
LOCUS       WP_284666085             289 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Myxococcus sp. SDU36].
ACCESSION   WP_284666085
VERSION     WP_284666085.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..289
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30899
     Region          83..283
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mdwfevktss rearrltarn atpalavvlv vwilmvgwpr fdpefpgpfp ytgtpltaaa
       61 rselasggwt vtgpdappwn laltrppaag etrwlvyfgg ntpgylaeak sillsldqgr
      121 glglaafapp gfdgspgeps pealrdsatn amrwlvsthp taaqgihlvg fsmgsmaalt
      181 aantlheret parglvlfap flrmkvrpsg fmgrvfgrhe ydnrpllrth rqrptlvlhg
      241 gadsalpllq gervsralaa plkvypdigh adllkhppal aaarqglgl
//
LOCUS       WP_284666186             113 aa            linear   BCT 25-DEC-2024
DEFINITION  (2Fe-2S) ferredoxin domain-containing protein [Myxococcus sp.
            SDU36].
ACCESSION   WP_284666186
VERSION     WP_284666186.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790154
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..113
                     /product="(2Fe-2S) ferredoxin domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=12342
     Region          3..104
                     /region_name="COG3411"
                     /note="2Fe-2S ferredoxin [Energy production and
                     conversion]"
                     /db_xref="CDD:442637"
ORIGIN      
        1 mappyqrhvf vctnrrpdgn pkgccatkga eevraafkee ldkrglkgrm ranaagcldm
       61 csfgvavvvy pegtwyggvk vedvkdiveq hllegrpver llmpfsrkap ppa
//
LOCUS       WP_284666259             453 aa            linear   BCT 25-DEC-2024
DEFINITION  J domain-containing protein [Myxococcus sp. SDU36].
ACCESSION   WP_284666259
VERSION     WP_284666259.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   4  (residues 1 to 453)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
REFERENCE   5  (residues 1 to 453)
  AUTHORS   Hahn,Y., Lee,J., Seong,C., Yoon,J. and Chung,J.H.
  TITLE     Structural analysis of phylogenetically conserved J domain protein
            gene
  JOURNAL   Biochim Biophys Acta 1447 (2-3), 325-333 (1999)
   PUBMED   10542335
REFERENCE   6  (residues 1 to 453)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   7  (residues 1 to 453)
  AUTHORS   Cheetham,M.E. and Caplan,A.J.
  TITLE     Structure, function and evolution of DnaJ: conservation and
            adaptation of chaperone function
  JOURNAL   Cell Stress Chaperones 3 (1), 28-36 (1998)
   PUBMED   9585179
REFERENCE   8  (residues 1 to 453)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20412694
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..453
                     /product="J domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=49145
     Region          118..185
                     /region_name="DnaJ"
                     /note="DnaJ domain; pfam00226"
                     /db_xref="CDD:395170"
     Site            order(146..148,163,166..167,170..171)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
     Region          266..>446
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Site            order(345..346,348,372,375..376,379..380,382..383,407,
                     410..411,414..415,418)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          370..401
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          406..434
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msapntiigl galtdhlatv pqldaarlql taeegavlql vgrveridqv larsklgepr
       61 tiavllalra kgaivparvv prgapapvvd aamaeavdle perkkeiiel ersldamdhf
      121 avlglkpgap aaevkqayyn asrrfhpdry fgknlgsfra rmerifrrlt dahnvlmqpd
      181 kreaylranp alaqaeraaa ppppaapppp apaqqlltpe pppvhqvspp ppaprppvas
      241 srpssippps rplapppedg asdarraerq arlarhpyla rtgrlaefma rgkaaiange
      301 werayhdfhq vqtmdpknre aalllvkarr ghdsqratie vargremeqh gdtqgamaay
      361 rlacslddqn aeaawrcarl shllgqdaae srglaqravd ldparvehhl tlgkvlldag
      421 skklakrafe daaklapdna eakaalkklr wtf
//
LOCUS       WP_284666405             253 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Myxococcus sp. SDU36].
ACCESSION   WP_284666405
VERSION     WP_284666405.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..253
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27389
     Region          <21..141
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 msppepfply hpadvrrafs sddatrrfak vaqlepgsrv lvlgcgpdgs aalllarelg
       61 ctvvaadtdd tvlnpvrerv raqglaeqie vrrvaldalg lsdgefngil iqgrvlyplk
      121 atlanmrgll akrgrlgftf parvgrfapk atldfwerrv sgalllprel lqvaegagye
      181 pesaeslhda eldahyrdie aflssipgaq paalreelal hresngkasv syafvvvrrk
      241 eqgekppasr drg
//
LOCUS       WP_284666424             553 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Myxococcus sp.
            SDU36].
ACCESSION   WP_284666424
VERSION     WP_284666424.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 553)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..553
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=59875
     Region          6..391
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
     Region          506..541
                     /region_name="HTH_8"
                     /note="Bacterial regulatory protein, Fis family; cl22895"
                     /db_xref="CDD:451442"
ORIGIN      
        1 mdriavlvvd deesvrtfls ellgsagyqv rcaangsqal emlsggsfda vlldvvmpem
       61 sglevlrryq smgggapviv lsalsgadda vramkmgasd ylakpfgnde lqdalaralg
      121 traperqvva pvlpargvmp aaepaqeqrv listspamrr aralveriad tdvpvlllge
      181 sgtgkeviar eiharsqrrn rpfikvncaa lpgellesel fghergaftg ataekpgkfe
      241 ladqgtifld eigemairlq akllqvlqde effrvggkks vrvdsrvvva tnrdlekeia
      301 lgnfredlfy rlnvvairlp alrerredvv pltdhflkky grgyisgvse lptevlhafa
      361 dydwpgnvre lenmvrrlcv lkdptlvlde lragvrapas apslptsyag ddggpfgrah
      421 degfrtpppa vqvlempsrg aafglasvap lappshapml mesanavvaa pryvnpfdvp
      481 qpppppapag epslkdigkr aamlaereai lamlqrtawn krraatklri sykallykik
      541 ecgiidprss ael
//
LOCUS       WP_284666459             164 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein [Myxococcus sp.
            SDU36].
ACCESSION   WP_284666459
VERSION     WP_284666459.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..164
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17223
     Region          100..149
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mpyvdteyvl tvgrtehcgr taadgslshe vpglaagell vklsgppapp prrsappaap
       61 kgvpppyppt itdedfpdaa paaasepvtl rwalqlqslp gfesdalraa qerlhnlgya
      121 idgergspga stksavrafq rrhglpetgq ladisrelir lhda
//
LOCUS       WP_284666585             606 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Myxococcus sp. SDU36].
ACCESSION   WP_284666585
VERSION     WP_284666585.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..606
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66906
     Region          2..603
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 msaalpmtla gqlwlqaeqr phavairekq rglwrelsfr dyldrvgwva ralwelgvra
       61 gdsvailsdn rpewlfmdlg aqvlgarsvg iyqtnpaadv ayilndarcg vvlcedqeqy
      121 dkvaavaaqt psvrhvivie trglrgveda rlqpwsglle rgrvllavtp awlreqlaqr
      181 tpdeaamviy tsgttgapkg alvssrnmlq gselfverlg lgpgdsvvsy lplchvaekl
      241 fslllplvvg gqvhfgesle tvqqdlaevs ptvflgvpri wekmhatvqv kmkdaswlkr
      301 tlfttftrlg gqlrerrrdg qrrwwdslvw fvgdllvfrp lqarlglrrc rlplsgaapv
      361 spellawfdg igvpiregyg qtesagtshl nlpdatrlgt vgrtapgvec rvaedgevli
      421 rganvflgyl nrpdataevr gedgwlhtgd lgevdadgyl ritgrkrevl itsggknlsp
      481 eriqsalkns pyikeavaig drrpfvsalv qvdpetvadw alrrglafts ytdltqrpev
      541 relidaevar aneglarveq vrafrllpre ltqdagevta slkvrrkavl elhaslveam
      601 yartre
//
LOCUS       WP_284666589             292 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Myxococcus sp. SDU36].
ACCESSION   WP_284666589
VERSION     WP_284666589.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..292
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30824
     Region          53..>171
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mkqtelafrl glllaltwts aagaqslssf satyrgggts lcgatynlrg qepaasgkyp
       61 vfiytvgtte nydhssalaa veemasrgyv aatveydnat fgscstmsar srcifdssrs
      121 tsavgtlcsr skadcskgiv vagfsqgsim ailaknhdsr vqaayglgag vdysiynlss
      181 cvangnralp snrlrvvnge gdaflgptes gvrsqnrdlt gyscplatsc lqgngsgwyi
      241 vrdsqvgdls adhcymrtgs cigllldstw rlgtqpwslr tnldwltqft tp
//
LOCUS       WP_284666594             330 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Myxococcus sp.
            SDU36].
ACCESSION   WP_284666594
VERSION     WP_284666594.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..330
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=36394
     Region          9..327
                     /region_name="PobA"
                     /note="Chlorophyllide a oxygenase/letal leaf spot protein
                     [Coenzyme transport and metabolism]; COG5749"
                     /db_xref="CDD:444459"
ORIGIN      
        1 mneatgskha eqwaahwyav arspalgagr plgiqrlgrr lvlwrdaage ahcadaacph
       61 rgadlglgrv rqgalecpyh gfrydgggac lampcegrda kpsrglalrl hpvreahgfi
      121 wawlggrape alpalpwlad apepdsssaa veevwnarft rvmegmmdlh hfpfahrryv
      181 ppgytrldpy evhvdagair tvgwlrketr ppgtgfrfdi dvgypgvlhl rfsprldaav
      241 vctpvdaeht wiaarfhqry vrlpglrwla arlaiafefr fiqpddyrmv rsslprsgal
      301 thgtlvradr aiaawhdlhr aalgdtpgas
//
LOCUS       WP_284666606             452 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Myxococcus sp. SDU36].
ACCESSION   WP_284666606
VERSION     WP_284666606.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..452
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48343
     Region          223..450
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mrlvrrlwlw gavvpmvavv aalgvavqvf rvvlertlde allsqaaaes vslfdapdgr
       61 phlhvepspl agevrafvpa trlygpdgtl lsvfppespt vhervlpedg ptsrletqrl
      121 gtglrlrvlt vqvrspegvp hvlqlvaslg tvdqavgtft tvatvlalll ggvligiqgw
      181 qarglarrlh giadqvarsr dggmvapvpv deprdeirev rlaltesavr vraareaqer
      241 liaraahelr tplalmrtgl dlalrrerga eelrtvleen rrevdrlasv agallelsaa
      301 ggaldlqpgd lrglldeaaa gvraeadrrg vslrvvgpae angrmdamav rravdnllan
      361 alryaprgse vrlelahrda qwevavqdag qgipeahred vftpfhrler daggvglgls
      421 lvrevarghg gdarvvespg pgarvlltlp gr
//
LOCUS       WP_284666702             474 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Myxococcus sp.
            SDU36].
ACCESSION   WP_284666702
VERSION     WP_284666702.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 474)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..474
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51347
     Region          1..459
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 makvlvidde anlrkvlaam lrrdgfdvtv aengeqglae fhkngadivv tdlvmpkvgg
       61 mevlgtiraa npdvpviiit ahgtvdsavd aikagafdyi tkpfdqaels svvakaaktn
      121 esarrsvrpd vkaraaiigd sstiqevyki idkvadtpst vlitgesgtg keliatalhg
      181 assrrdkpfi kincaaipat lleselfgye rgaftgavts kpgrfelade gtlfldeige
      241 ipvemqvkll ralqegefer vggikttrvd vrlvaatnrd lqaeieagrf rkdlyyrlav
      301 vpislpalre rrtdvpmlar hfvekynrrl nkkiegiadd amallqgyaw pgnirelenl
      361 iervllfadg plitardlpe pvrqgtsvqa ganlasavas idvptgevgl kdivrmkaae
      421 lerdlivkkl eetggnvtra arllqisrks lqtkmkefgl rdttpdgled gsde
//
LOCUS       WP_284666741             846 aa            linear   BCT 25-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Myxococcus sp. SDU36].
ACCESSION   WP_284666741
VERSION     WP_284666741.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 846)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 846)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 846)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 846)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..846
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..846
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=90203
     Region          16..800
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mripvpirrl paplddargl dtdevserra rygrndvlar phrswlhvlr etagdpmlwf
       61 lvgtsglyfv lgarteglvl llaivpllgm daflhrrtra staglqsrla aratvlragn
      121 eqvvpadelv vgdlarvqag ehfpadglvl rgeglqaees sltgealpvr krplsrlppg
      181 depavegshw glagtrlltg tawvrvvftg retlygsivr satqgahart plqqavahlv
      241 avlmgvaavm cavlafvrwr qgfgwmdall savtlavaal peefpvaftf flgagvyrla
      301 rrqalvrrsv svenigrvtc icsdktgtlt egrlrvarvl papgvqadal lwtaalasre
      361 egrdpldaal leeaararpg varpstqatf pfteerrret avvddgerrl laavkgaper
      421 vvdlctleag armdwarrvs alaaegrkvi acasqpldsa swrggepdrg fhflglvafe
      481 dpvrpgvrea vreceeaglr tvmvtgdhpa talavarklg lggarprvlt gealearlne
      541 ggavpevdvv aravpaqkya lvaalqrrge vvaatgdgvn dvpalqaadv giamgergtr
      601 sarevasivl ldddfgtlvr aiaegrqlfr nlqacflyll lihiplvvta alvplagypl
      661 lylpvhivwl eliihptaml afqaaarpgr lapvrrrgaa rffsagdwrl lalvgglmtv
      721 glvwsydrsl gagsdvahgr aaavasltla savfaavltg lrtrtarwvc alttgvslsl
      781 iqvpalahll mlrpldvddw arvaagvava slplvlarwr vaakahapra gtaapplhrq
      841 vrrgaa
//
LOCUS       WP_284666823             104 aa            linear   BCT 25-DEC-2024
DEFINITION  FmdB family zinc ribbon protein [Myxococcus sp. SDU36].
ACCESSION   WP_284666823
VERSION     WP_284666823.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..104
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10210
     Region          1..68
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 mpiyeyscqs cgkmidvlqk isdpapatcs acgaegsmtk vvsrssfvlk gggwysdlys
       61 stkkdgggst ssssasssss sassppasst papapaptas gdkk
//
LOCUS       WP_284666826             171 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Myxococcus sp. SDU36].
ACCESSION   WP_284666826
VERSION     WP_284666826.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..171
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18025
     Region          34..169
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 msrallrgal valvalagcr gtrpvdagha flnalalpsv gptphdvral dgkvvlvsff
       61 atwcfpclae mptlealqkd ygsrgfqvva vgmdlegekv lapfadhyal rypvlianqa
      121 midghsafga iqglpttvll drrgravagw hgveshadma kavekllaqp e
//
LOCUS       WP_284666850             271 aa            linear   BCT 25-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Myxococcus sp. SDU36].
ACCESSION   WP_284666850
VERSION     WP_284666850.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..271
                     /product="MlaE family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28520
     Region          23..271
                     /region_name="MlaE"
                     /note="Permease subunit MlaE of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG0767"
                     /db_xref="CDD:440530"
ORIGIN      
        1 mttqtpsepa repgpftqav trfgqglidi vstlggivtl gldvfrwsvr rpfrlvnlfa
       61 qldfvgvgsi fivsltgtft gmvfalqtst afqlfdaesl vgptvaltlt relaavfsal
      121 mvtmragsam ctelgtmrvt eqvdaletma vnpvqyllvp rvlaglfmvp altmlfntmg
      181 mggayvvavg glgispgtfl srtqqwlape difqgllkga vfglavslic cfkgfnasgg
      241 akgvgqatte amvasalsif ildfilgvlf f
//
LOCUS       WP_284666872             333 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Myxococcus sp.
            SDU36].
ACCESSION   WP_284666872
VERSION     WP_284666872.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..333
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=34940
     Region          2..329
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrflltggtg figqrlarri vergdtltlm vrassrrgpl eglgarfvva dlttgaglae
       61 avrdvdcvlh lagvtksrap egylegnakg trrlveamaa lphpprlvyc sslaaagpst
      121 pgrprreedp papvslygrs klggeeavra ladrvpsviv rppivygpgd veflpsllpm
      181 aklglalksg fgpkryslih vddlctalla aaqrgatvtk edaargvyav sdgvehswed
      241 vcaamagalg kgrpavlsvp qtvsymvglg seavarlrgt vpilnrdkvr emrcpawtcs
      301 terasqelgf lptiplaqgl agtlaayrea ggr
//
LOCUS       WP_284666986             368 aa            linear   BCT 25-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Myxococcus sp. SDU36].
ACCESSION   WP_284666986
VERSION     WP_284666986.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..368
                     /product="isopenicillin N synthase family dioxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39990
     Region          4..348
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 maetsslnip tvdladlasd dsarveraaa aireafgvfg lvylknhgvd tqalnrfyda
       61 faafiarpae ekkpygradi wyqrgwtppn tevavagngq pdfkecyfva pypndaqsal
      121 efpelypenv wpqdappyfe dgimtlgrsl heaglkllrg samalglpet lftdlcdrga
      181 hvtralqylp lthaqvntdi vwgeehtdfn lltllpggrf ldpegspapg pdnksglylr
      241 tratpdapng lqvrgtapag civaqvgqql eiltggtfla tphvitapgv pgwqrqsaah
      301 fmhvhtntvl fplekfrgee avrnyappvl agtydiktlv diglapasal dklgyrhydr
      361 lnrqraga
//
LOCUS       WP_284667042             264 aa            linear   BCT 25-DEC-2024
DEFINITION  trypsin-like serine peptidase [Myxococcus sp. SDU36].
ACCESSION   WP_284667042
VERSION     WP_284667042.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..264
                     /product="trypsin-like serine peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=27396
     Region          65..254
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mfpksvralf lvgalsacgt eapldvpnad gqeplqsqes nvivgtvnwv sattlsgtqr
       61 trsravgyls ipavgsrcta wlvsrdviit nnhcvasssq asgvrasfny edgvsstarv
      121 wyncgtmirt wagddmtalr ctatngqlpg dvygwltvas anaatnssiy vvhqncdyyt
      181 ssgctptkks spgvvlnany sttdlsynad tlggssgspv lsssshqvvg lhhyglggns
      241 qgrgtansgv katrvkarla eigl
//
LOCUS       WP_284667043             285 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Myxococcus sp. SDU36].
ACCESSION   WP_284667043
VERSION     WP_284667043.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..285
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30973
     Region          6..257
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mrplpidqgt vliigaargi grelarllar rvrtlvlvdr eaqaleplre elllhyptlg
       61 vlvesydvcd prqvdallas leaqfvrvdv lvnnaaegdq alyaqegwar veamlranvw
      121 vpallthrll kpmlergrgg ilnigsgaaq lilpgsatfa atqrfldgft ealrlevegq
      181 gvtvtrvapg plweagmegt eslapffhls lercareala gfergealvy pglghrwvmr
      241 llpmlprglk rslgrmalrg lrrealllpg qapktlplsg epspa
//
LOCUS       WP_284667018             400 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Myxococcus sp.
            SDU36].
ACCESSION   WP_284667018
VERSION     WP_284667018.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..400
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=43375
     Region          2..383
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mrtfrnilfw ihlivgvatg lviaimsftg vviafekqli ewaerevrtv qlpapgarrl
       61 pveelvervr asgsegqpsg vtvypeptsa vlvsigrgav syvnpytgev lgngatglrg
      121 ffqwnvglhr wlaaggdnra vgkaitgasn avflflaisg lylwwprkwt lramrpslwf
      181 rrglkgkard wnwhnvigfw slpvlivlta sgmvisykwa sslvftvtgn tppatkgppg
      241 satvkvpape eetprqpldv liaeaqrtsp twssatlrlg ggagggkegv davtvtlrea
      301 dawplfsskq vsvnpfsgev akqetyadys sgrklrtwlr flhtgealgl wgqlvaaias
      361 lggvflvytg falswrrffp rrrtnsepge daaaqsepav
//
LOCUS       WP_284667142             281 aa            linear   BCT 25-DEC-2024
DEFINITION  tRNA pseudouridine synthase A [Myxococcus sp. SDU36].
ACCESSION   WP_284667142
VERSION     WP_284667142.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Hur,S. and Stroud,R.M.
  TITLE     How U38, 39, and 40 of many tRNAs become the targets for
            pseudouridylation by TruA
  JOURNAL   Mol Cell 26 (2), 189-203 (2007)
   PUBMED   17466622
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Foster,P.G., Huang,L., Santi,D.V. and Stroud,R.M.
  TITLE     The structural basis for tRNA recognition and pseudouridine
            formation by pseudouridine synthase I
  JOURNAL   Nat Struct Biol 7 (1), 23-27 (2000)
   PUBMED   10625422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414743
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..281
                     /product="tRNA pseudouridine synthase A"
                     /EC_number="5.4.99.12"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=30515
     Region          11..257
                     /region_name="TruA"
                     /note="tRNA U38,U39,U40 pseudouridine synthase TruA
                     [Translation, ribosomal structure and biogenesis];
                     COG0101"
                     /db_xref="CDD:439871"
ORIGIN      
        1 mlpstskrip valwiwyrgg ifrgfqrqpe gptvqsalee alrsvgvpat lmpsgrtdrg
       61 vharmqvvsv rleagdsaes lekrlpprlp pglglcgvrr ptsfhaqwsa cgkeyryrfq
      121 lggavtpewa pyaldvsaep lfqaaavtpe rlgallraae gtrdfiafhe kssprkprtl
      181 esatlhalgg glyearlrgd gfaryqiryl vgsalkvaag llpeeawlaa letgramegf
      241 kapahglvlw evryppgvdp fsagerlhpp glpleppfhl g
//
LOCUS       WP_284667335             702 aa            linear   BCT 25-DEC-2024
DEFINITION  two-component system sensor histidine kinase NtrB [Myxococcus sp.
            SDU36].
ACCESSION   WP_284667335
VERSION     WP_284667335.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 702)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 702)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 702)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 702)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..702
                     /product="two-component system sensor histidine kinase
                     NtrB"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009399 - nitrogen fixation [Evidence
                     IEA]"
                     /calculated_mol_wt=76145
     Region          339..698
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 mryalvpill lcvalttvgv gvftllernr eaqwhqfave rqaqldeatr gvaetledva
       61 edlrfagelm sqpgtlaehr remralleav gqykvliayn asgkewlrml drrlgkqvar
      121 apvlaqmaea grrallrppg dvtlsppmed ggfdslrvma talpvdaqgr pegavavlvd
      181 ttsfftplri vtsdpdarll llgtygqpts asdptladwf rrletegsrv pgfmalaarm
      241 regergalpl raeeaerlgl ghseaiavft pirvrggshw aaatlvstat lrshqqaliw
      301 rlmaaallva lflvtfavyv vlaqrraaal resrqhadql ahlqdktqki ldhipsgvla
      361 ltvdgrisav nqvlrermpp daigapleta fpqapapvvs rirslvaaav sesrahgilg
      421 etlvlfgeeg rfnlhavple arhpevhtll vvedlsnvra letqllraek latvgvlaag
      481 iaheigtplg vvrgraeyvl gklgkehpqg pgiaviieqi drvsrtlrql ldfsrlqpta
      541 vrpvplssll hdvqellrme verrgvrfev tvpqtlppla adpdqlqqvl vnlalnacha
      601 cgeggqvtlt aavpeaepwg lvaltlrddg cgiprehlnq vfdpffttkk rgqgtglglt
      661 mvahvvrnhg grleleseeg rgtcvtvlwp iakpsaeern vg
//
LOCUS       WP_284667391             532 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Myxococcus sp.
            SDU36].
ACCESSION   WP_284667391
VERSION     WP_284667391.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..532
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57308
     Region          36..503
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 msrlvsalga llvlasgcas srppvadsap tsqrqqltvl yvadlhaqlr shpelfwrdg
       61 kerievaggf arvaaaiqqi raerggdvlv ldagdtiqgs gaaalsegga lieplnalgl
      121 dgavpgnwev vygpavlgqr arelkhpffa anlrdaasge rlfppylvkt vggvkvavvg
      181 ftdpdvprrq ppgysqglry dgpevlpalv revreregaq vvllmthvgl akavglaarv
      241 pgvdahlssd thertyapie qagswvvepg afgsflgrmd lwledgkvvd rrwelielta
      301 srfpedpeva rlvdaalapy eealstpvgh tgvtlaryav venpldnvla dairaaggtq
      361 iglsngfrfg tpllpgpvre adlwsffpit nklktgkvsg rqlrafweqe lenvfakdpe
      421 krfggwlprp sgmtlrfrsd apkgrrllal evagepvvde rlytvtacer egdspdmlcr
      481 ipgvqeprvl evdaheavrr flagkprlra slegravgvd lpavlrtqqi hp
//
LOCUS       WP_284667468            1386 aa            linear   BCT 25-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Myxococcus sp. SDU36].
ACCESSION   WP_284667468
VERSION     WP_284667468.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 1386)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 1386)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 1386)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 1386)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1386
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..1386
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=152852
     Region          36..1376
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 msellkklag lspekreavl rklrqqnvva apmeeartpg iprasreqpl plsfpqrrlw
       61 fldqfepgtp aynipefvrl tgplhvpsle ralnevirrh evlrttfvak dgepqqrilp
      121 eltltlgvld lsylpgpqre plceelalql agtsfdlaag pllharlvrm geedhvlllv
      181 vhhivsdgws tgifvqelta lyaafsqdkp splpelplqy adfaawqqqw mqgdvlasql
      241 dywrrqlegs dsalklptdr prprvrtyag gkrsfqvdpa vaqqlktlgt qekaslymvl
      301 laalqtllhr ytreprisvg tyianrnrte vepligffln tlvmrtgleg nptfrellrr
      361 vvdvtlgayg hqdipfekll eelapsrdts hspffqvmlv lqntptppae lgalrmesfs
      421 vsgeafaqfd ltlwfseeag glqgiweynr dlfdastver mvahfqtlla giatnpaqrl
      481 velpvlpake rqrilrdwnq arldvppgtc lhhlieahaa rtpdatavtd serrltyaql
      541 nakanqlahh lrsvgvgper itgvfldrsv dmvvavlavl kaggayvpld psyppertal
      601 mladsrpavl vtrqglasll saalppvvdi dtdagaiaar ptttpeggas pehlayvvyt
      661 sgstgrpkgv mishrsfana ylawerdyrl pelrahlqma sfsfdvfsgd laralgsgkt
      721 lvlcprewll epeklyglmq reqvdsgefv pavarllmgh lqehklrldf mhllivgsdt
      781 wdmreyhqlr glcgpdtrlv ssyglseati dstyfeqpep tpseqivpig rpfansrmyl
      841 ldsamqpvpi gipgelfvgg dglargywgq ahltaerfvp spfsatpgar lyrtgdlary
      901 tedgtlafig rndtqvkirg hrieldeika kllehsavqa vellvhedag nkqlvayltl
      961 tapdvataed lrqhlkkhlp pymvpaafvi laafpltpng kvdrkalpap esvrrdaqdg
     1021 fvaprdevet rlaaiweell avrpigvhdn ffdqgghsll avrlmvrire qfgralplsv
     1081 lfqnpaleql akalheeaap apwsplvtlq pgasrpalfc vpgaggnavy lrelaqalgp
     1141 tlpvhafqar gldgraephr sveemaacyv ealkqvqpqg pyhllghsfg swvafemaqq
     1201 lrkqgesiaf lgilnttvpv neappseapp fddadwmasv astagrlygv dlgisaetlr
     1261 plsaearreh ltrrlvqagl lpdgadsqqv qgfievykaa yaidyvprdt lpvpvalfra
     1321 qerheedgiv pesftddpsw gwghhasaav tpvtvpgdhm tmlaaphvqv laehvrqglf
     1381 ragglr
//
LOCUS       WP_284667524             309 aa            linear   BCT 25-DEC-2024
DEFINITION  LysM peptidoglycan-binding domain-containing M23 family
            metallopeptidase [Myxococcus sp. SDU36].
ACCESSION   WP_284667524
VERSION     WP_284667524.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11517909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..309
                     /product="LysM peptidoglycan-binding domain-containing M23
                     family metallopeptidase"
                     /calculated_mol_wt=32536
     Region          76..120
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
     Region          125..305
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mapcvssrar galrvfllav llsgcagtra ssvagpdtgt dtgtgtgtgv pdaaerttpl
       61 pfnlrgvhae pelvavrhvv aagetmyris rtygltveel gsangikapw tlavgqelti
      121 pgvergapvr alaeadpepv rtstsaegrr svpavgrree ppsrrrtlsr pasatgpprv
      181 atqgqldwpl rgvlygrfgk kgkephdgid laapagtpvk taqagtvlya geqrgygniv
      241 ivehtnklit lyahnrdlrv rtgqkvrreq viatvgesgr tsgphlhfev rmdgkpvdpl
      301 dylgpmpss
//
LOCUS       WP_284667480             541 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Myxococcus sp. SDU36].
ACCESSION   WP_284667480
VERSION     WP_284667480.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 541)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 541)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 541)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..541
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=59340
     Region          49..530
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          306..533
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mpssdsadiq lehltpssfl hhqegrllre lgasagperh egrdapspla lprilahlqt
       61 vvrniqggaq pcvpvelrrh leqrvalpdf slrdavrevt vlrrciirgw lktgvraprs
      121 egvtildeal dqlslavldc wteaqqrtlk aldrvsalia qsrhlpella gvarllaetg
      181 sharwvtlwl kdgaalvqra awgldlpega arvrlpkeld magadagpht tapsswqdlg
      241 sllltrqgpe egpsvllpil hegqllglar vghawdeels qdersclasm leraapsiih
      301 lqlkdqleve rddflnvlvh dlktplsavs vaarlarnqa qaldghpleg llekiqsqvt
      361 risrllndll dlrmlsagrf rvlgecldlr plvrelasew qsaspshtiv vempegalve
      421 adpvrvtqvl nnllsnavky spegahirvs awvrpeevit wvedegigie psalsgvfer
      481 ytrtqggkvq akghgiglfi aselvrlqgg rmwlestvek gstfyfslpr wrpgptpppr
      541 a
//
LOCUS       WP_284667623             905 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Myxococcus
            sp. SDU36].
ACCESSION   WP_284667623
VERSION     WP_284667623.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 905)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 905)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 905)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 905)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..905
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..905
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=97630
     Region          268..873
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mrandlarrg lwgslkmmal vfsretafpr tqvlapspsp drtyrtsgvh appldvrtmh
       61 stvfgeprqg aakavagrra lraglplsim lcvlslvvps sataqevaqa eapakvkrrk
      121 rvvkparpaa rtakkpkkav pppvedaedp adepeipvlg ggpsteeppp palapaapla
      181 patpltaepl pmppppvstd fippdaptnp ppatarpepa snvpitapfa epamnrplpp
      241 psglagldgd plggadalee svnrvlseav vttagkrnqr isdvpltvsw ipadelegtg
      301 qftlceaiqy fpgmecrrgs mrkaavsarg lgsnylsnrl lllqdgrplt dpwtgqfyad
      361 ettpltnlkq vevirgpgss lygsnafsgv iniiqrqpsd liekgkdvga earvlagqdq
      421 twrlhgtvag rggpveallg yygfgsdgpq lfndprvgrv dtnqdslvhq vngkvrigpl
      481 aldadftdae igrpggthis tvgncgrchy tpndsesvqn fnasaqvdqq vtdnlrlfgq
      541 aygffkrrdv lmenafggdp tralgkrrrl ggearalwtv gdlnvtfggd lkadavnvpn
      601 vlpelsmddt rqtilggfvd aeyrlfdrlv fgagarydry qipenvwqnr tdqisprasv
      661 vfhavpellt lrtnygrafr aptlaelain qqmyaatlvg nsnlraetld tieasvdfwp
      721 fdrrvrltgt gfynlaknfi nqqlvfgsvs qfqnlgdarv agfeleaaaq ipsinssfdi
      781 ayqflnaksl pyddgpqspl dyapahriya rgrtnigkva fvelyallvg srydpgfevd
      841 ettglptirv qlpsyvtasa rvgfnvydgi svsflgsnlf naqyeeshgf pappqsffse
      901 vkvry
//
LOCUS       WP_284667646             704 aa            linear   BCT 25-DEC-2024
DEFINITION  two-component system sensor histidine kinase NtrB [Myxococcus sp.
            SDU36].
ACCESSION   WP_284667646
VERSION     WP_284667646.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 704)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 704)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 704)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 704)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 704)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 704)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..704
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..704
                     /product="two-component system sensor histidine kinase
                     NtrB"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009399 - nitrogen fixation [Evidence
                     IEA]"
                     /calculated_mol_wt=75887
     Region          338..700
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 mrlpvlpvll lclmlsgiia gvlhfmqrdr qalvdqmare rqaqlleavr gvsaalegae
       61 edlrfagell aqpgtaeehr remralleav gqykailvfg mdgqerlrlv drrsaaamth
      121 qftaedlalt vaqarghppg hvvsspplpr aqsgwlrafa talpedaqds gavvvvlvda
      181 eplfaplkll asdsetrllv lgahgtptal thpdladgyr rldtgghqtp glaalvqalr
      241 agesgtriie reeaarlglg dsevvvtfsp vrfkngaawp vatlastrvl rtherglvlr
      301 lslaavlvsa fliafgvyvv larsraealr esqrhaqrla hlhdktqkil dniptgvlal
      361 sstrhisaan ralslrmpad avgrpltaaf pqaqapviqr ledlvhaats dgrvrslhge
      421 plclfeepgq ynvhavplep ntpevhalvv iedvsslral egqllraekl atvgvlaagi
      481 aheigtplgi vrgraeyvqe klgrehpqaa glgtiveqid rvsrtlrqll dfsrlqpada
      541 qavpleplvh svrellwmea errrlklevt vaspmpavaa dpdqfqqvli nlvlnaydac
      601 daggrvrlsa nmdtgdapga wgmvrvdved ngcgiaprhv hqvfdpfftt kkrgqgtglg
      661 ltmvahivrn hggrieldsa aergtrvtvr wpaaapagee rhvv
//
LOCUS       WP_284667647             457 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Myxococcus sp.
            SDU36].
ACCESSION   WP_284667647
VERSION     WP_284667647.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..457
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=50283
     Region          3..448
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mssrarvlvv ddhvemgqml kepltddgyt vdiatggada iaqlrarvyd avlcdlrmqd
       61 vdgfdvldaa ckldpdlpvv mmtafggves aveamkrgaf hyftkpfrld evrlsleral
      121 eqrrlrtehr tlkqqaadra glgalvgsst amrdlytlie rvawssapvl vrgesgsgke
      181 lvaralhfeg trragpfvav nctalphtll eselfghvkg aftgattarr glfveadggt
      241 lfldeigdma pelqarllrv ledgevravg adgsrtvdvr vvaathqdle trvkegrfra
      301 dvfyrlnvvt lrlpplrerr edipallehf lqqakarnpr smvqrfspet laalgalpwd
      361 gnvrelenlv qrlvvlgste vvdlpqlrph lpadtsqenh plaaaqrtiv plrqleteyi
      421 awavarcggn ktkaaellgi dvstihrrer aegnpqr
//
LOCUS       WP_284667678             446 aa            linear   BCT 25-DEC-2024
DEFINITION  ParB/RepB/Spo0J family partition protein [Myxococcus sp. SDU36].
ACCESSION   WP_284667678
VERSION     WP_284667678.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19943518
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..446
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46436
     Region          <4..243
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Region          250..>423
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mstephdsga sseqgehpre gaspesggeh raegappaeg seqraegtpp aegtppaegs
       61 eqrvegtpse qgepqnagsa qeqggappvd gtpssheasp atgdtqgega rphdasseap
      121 gsadasgsea skdptgsreg glqaegttsh gpgephakda shaqgehqav sesqgqdgse
      181 sggrsdanae araeqapsdg esratpglde rpqgafwtgd adgdkasdsg eesqedvlpe
      241 peqrlsgrvt tvllpleklq desafklrpe gdvsglatdi arlgqlfpvd vrpagedryq
      301 lvcgfrrvaa lrflkrdavq arihlrlsde dalvmslaea ihatpvgpev leakrdelea
      361 qgrlsaavrd mlekalated tlapegveee idadelaqev aqrlgainqd lslladvfaa
      421 ldesrkaell mqlrysselv tylegl
//
LOCUS       WP_284667779             290 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Myxococcus sp. SDU36].
ACCESSION   WP_284667779
VERSION     WP_284667779.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..290
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=33759
     Region          9..283
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 marfddgrpe msaeefrllr dhvyshcgil vhedmkfvme rrlwprlell glpdygayhr
       61 ylrydanrha eleaaveslt thetyffrep tqlkaftdel lpvveqrnar lrrlrvwsag
      121 cssgeeaytl amllkdsrrf ddwdvevlgt disrrvlama rraeygpsal ratspeller
      181 hfvslgnhrv rvrdevrawv sfghhnllde vgsqlvprmd vvfcrnvliy fdlaarrkfl
      241 sivrdrlvpg ghlllghsen llnlgsdfef vhlrgdlvyr rpeldegarr
//
LOCUS       WP_284667799             454 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Myxococcus sp. SDU36].
ACCESSION   WP_284667799
VERSION     WP_284667799.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..454
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48522
     Region          97..448
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mplratllpl llpavvvatl valldgpkev vaaalvalag slmslgvsrg tlqrqldlla
       61 rhtrdradgg pptstpvvpe rldevagleg aidslhaqls arntvlnqda rtltavldgm
      121 aegiwvtdee gtvvrhndal ramldstsnp ltgqrplali rnealhdavm racresassh
      181 leltldglfp rtlsirvtpl akdlpgsaav fhdvtelrrl ekvrkdfvan vshelrtpit
      241 avrgyaetlq ggalndpvma pkmveiihrq serlselved llelsrlesr evslklahvp
      301 ladaaaraad tvrpkaeskg qvvslhvpqg llavgdtrav eqvllnlldn avkytpaggr
      361 vevygaceqg rcvvrvkdtg vgiepkhlsr iferfyrvdk grsrdmggtg lglsivkhll
      421 qamdgevkve sqpnegstft iflplaassg aatg
//
LOCUS       WP_284667801             164 aa            linear   BCT 25-DEC-2024
DEFINITION  SixA phosphatase family protein [Myxococcus sp. SDU36].
ACCESSION   WP_284667801
VERSION     WP_284667801.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..164
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=17779
     Region          8..149
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mssrelpllf irhavaedsh vlgdearalt pegraafrhh arklarltpl rgiitsplvr
       61 avqtaellae afgvsgvevh pallpqrgah krivdlgrer gagwalvghn psleraaira
      121 lehelpdklr kgaalalhpl knggftlaww amqgkpvkrp gdlr
//
LOCUS       WP_284667806             447 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Myxococcus sp.
            SDU36].
ACCESSION   WP_284667806
VERSION     WP_284667806.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..447
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=48914
     Region          5..446
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mstylllvdd drtfaslaas vlrhegfrvt lahslhdara amsreapdlv vldrrlpdgd
       61 gidflpelra qlpdtpvlmv tahgdiasav eaiqagardy lskpvelddl vlrarraaad
      121 lqlqerlrqa eselggrrrl srphspkmla alqmleriak aprspvlllg etgvgkevia
      181 rhlhalqggq gsfvhvncaa lpatmvesel fghergaftd artarrglve vaaggvlfld
      241 evgelplqlq aklltfldkg afrrlggtae lsssarvvta tnrdltkeva egrfredlyf
      301 rlsvfrvdip plrerredll plaqslvael caelgrrpvg fssaararle gypfpgnvre
      361 lrnvleralv leagpelela slepqgasgp pavdpdafvv pgaprplqdv erlyvrhvla
      421 rlegrrmeaa rvlglsyptf lrrleee
//
LOCUS       WP_284667844             753 aa            linear   BCT 25-DEC-2024
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Myxococcus sp. SDU36].
ACCESSION   WP_284667844
VERSION     WP_284667844.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..753
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=80250
     Region          23..>215
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          190..748
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mtklltlisr rsfleglnls vgglalgvfs gglamaasea stakgapgln pnvfvhvapd
       61 gavtivcars emgqgirssl pvlvadelga dmarvtvaqa dgdkvygdqn tdgsssvrgv
      121 yddirrmgat arvmlvaaaa rrwkvkpeac eardhavflr ggtrslgfge lvadaarlpi
      181 pkekdvklrp krelrmagrp mplldgpayv tgtavfgadi slpgmliavv arppvvggkv
      241 vrfdatrala vpgvkkvfel papkppytfq lwggvavlae ntwaamrgre alditwddgp
      301 nasydsttyr eqltasirep gavarnvgdi daalasaarv vqseyhvphq shvpmeppva
      361 larvengmce vwaptqhpqa argvaaatae lpeekvqvhv tflgggfgrk skadfiaevv
      421 wlakeagvpv rvqwtreddv rhdyyhsvsa qqltagldas gkviawrhrt afppiastfg
      481 qatrpspsdl qqgvldlals vpnvraetce apphvrigwl rsvynifhaf svnafvdela
      541 hlrgtdprdm llevlgpprq aslqelgita lrnygasved hpvdagrlrg viervtamsg
      601 wdarkakgra lglaahrsfl syvavvasvv kddqgrirvd eawvsvdagt ilnpervrsq
      661 megsvifgms ialhgavtmk ggvpeqsnfh dlklvrigea prkihvdivp selpsggige
      721 pgvppvapai inaifaltgt rirelpvsrt lav
//
LOCUS       WP_284667860             404 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Myxococcus sp. SDU36].
ACCESSION   WP_284667860
VERSION     WP_284667860.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..404
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=43356
     Region          92..>357
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mrqvasfvvl vasprtreng mskaiefklp pgailfsadg vgyefredlg athhgmslfv
       61 arlraasgap rgkvllkavp apsekeggrv rrarakldeq vrlaaslshp ailkvhglhk
      121 vegywyvsae hpsgnslnel ltlvvecrrw fsplfvmfvg sqvaaaleya htakdasgrp
      181 lnivhraidv ahifvdwdgs vrlgdfglal sdlpgrvass vrgpggdyfy sspemllggr
      241 vdarsdlfml gvvllelatg knllfcpdil tpevmgslsa kkrrrvsqai eratlagass
      301 mvedaiwraa tltdadvdam teglpqglrv tlnrllrvsp reryqsagel aadlvawigg
      361 tftkadaaae lraraaqaee aldamgltpp rgrgnrkpdd vtta
//
LOCUS       WP_284668048             502 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Myxococcus sp. SDU36].
ACCESSION   WP_284668048
VERSION     WP_284668048.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..502
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53253
     Region          13..>237
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mcsdrflkai sstaqhpwap wlligagawl lrvagffhrg galgypvdyd egvyfsaaal
       61 lthgvlpyrd yffvhppgiv vllgplaalg grvdaatafs vvrgfipllg alsavlcgri
      121 vqsrwgtrag vvaalvyaly peaaatergp flepalnlac lgtawgllrp adtgralrrd
      181 vcagvllata caikltagvw vvavawalgg agdlrrarrv igvaaftgll wvgpflavaa
      241 gpmvegllrf qlqrppdgel epvrrlltil geghwgvsvl sllglagala rarrsdavae
      301 rlfslawllt vavflasksy wgqynaslap atavlaglga sllldwaerr srrlevamva
      361 avgllalssl paalrsanqr drglltigna irasvpakat lcafepawai aagrlpglpw
      421 gspllvdpyg lmlhdasdgs arftsataaf edertqrtvl pllercdalv llgrgewqls
      481 aaserwvgeh ftregdvwkr rp
//
LOCUS       WP_284668049             756 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Myxococcus sp. SDU36].
ACCESSION   WP_284668049
VERSION     WP_284668049.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 756)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..756
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=83988
     Region          68..552
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mahksqpdys sraldelkqa lrerlktnql ahrellwdst hgreapiedg rdveawflgp
       61 raenadvfeq lvlealrdha fwrrnfhpmd ppaitqsikr dpgylraldt lhtefnnlla
      121 elkksapffs mryqghmtwd qtlpgmagyf aamlynqnnv aleasplttv levrvgedlc
      181 rmvgytqkgd irpwshltsg gttanieamw aarnlkfypl slreaiqres alaaakslqv
      241 tlpsgtrarl ldldawqaln ldvdevlgip triqeefsip vetltarvgn ymlqdlglve
      301 ftrrylgdip apvfmvpgsk hyslpkaaai lgigadhmfs ipldeegrmd vsalevrldq
      361 ckadqqpvia vtavmgttee glvdplasvl alrkqkyhpq gmsfcvhada awggyfasll
      421 rappstdksr agppapvlpl sryvtqqfea lpeadtitvd phktgylpyp agalcyrnqs
      481 mrslvafeap yintagsqed ltvgkygieg skpgaaaagv ylshavvppd qrgygkilgr
      541 alyncklfha rllmmnsaas dyvvvpgprf klseplkrky ggekqaletl rhqitgvpqe
      601 klltasgeee lellretgad lniltyafnf tsgqglnpsl eeantfnrki yerlgvkadg
      661 rdiygyrllv sttdfieedy gkkffddykt rllgsgatsg rgeegritvl rsvimdpwit
      721 edlqrrpfld tiieelraav edalnemrgt askrsr
//
LOCUS       WP_284668292             595 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Myxococcus sp.
            SDU36].
ACCESSION   WP_284668292
VERSION     WP_284668292.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 595)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..595
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=61942
     Region          30..569
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mrsfrliala wvcgaslaca garpraappe piritlvgin dfhgqvephr tplkdgqvve
       61 eggaatlaay varlradnpg gvvlldagdm fqgtlpsnlt egavvidvyn hlgvdaaaig
      121 nhefdygpvg pgsmarrpgd dalgalkari aqarfpllsa nlrdaatgap pawtgndgts
      181 llevkgvkvg liglstedtp kvtnpanvts lrflplapaa leasrslrar gaevvvavah
      241 aggkcadlsn prdtsscdlg daeilsmler lppgtldavv aghthqtmgh ffaqvpiiet
      301 tglarslgvv elfvdpasrr vlpertriqa aiplcakvda trgtcdgrrl rdapqvrlep
      361 asfmaepvvp daqvapllap alalareaqh rqvglmaatp lvrgyteega lgnlvadvlr
      421 asanadvglm npggvranlp agpltfgqvf ealpfdntva visltgpels rllslaygnd
      481 lgsifavsgl evtlercpgh erfsgvalag gqplvsddrt lyrvalpdfl arggdglepl
      541 lrtvpperie mapvngldlr ealiaygkar ggtldapalg rvhykgvakc qpvar
//
LOCUS       WP_284668170             291 aa            linear   BCT 25-DEC-2024
DEFINITION  formylglycine-generating enzyme family protein [Myxococcus sp.
            SDU36].
ACCESSION   WP_284668170
VERSION     WP_284668170.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..291
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=31407
     Region          30..277
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 mtfisdrscv vllllmggcg takrvpaqvs arvepvaear avwlpagrfe mgspegeagr
       61 dadegprtkv alerfqmdvt pvtvrafaar agqvrakeph arwwtdaetp aawlgrcnlg
      121 sartehpmnc vdwraarayc elvggtlpte aeweyaarat apaaywwgaa fdgarvvssv
      181 acasrgcqgg tapvvhaglr cngwglcdma gnvwqwtata yreqlgeatp tepsgvpenp
      241 vlrggswlnh vpslfrsahr glayprnglt gvgfrcvhrr ppkvmsrrth e
//
LOCUS       WP_284668350             808 aa            linear   BCT 25-DEC-2024
DEFINITION  glycogen debranching protein [Myxococcus sp. SDU36].
ACCESSION   WP_284668350
VERSION     WP_284668350.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 808)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 808)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 808)
  AUTHORS   Dauvillee,D., Kinderf,I.S., Li,Z., Kosar-Hashemi,B., Samuel,M.S.,
            Rampling,L., Ball,S. and Morell,M.K.
  TITLE     Role of the Escherichia coli glgX gene in glycogen metabolism
  JOURNAL   J Bacteriol 187 (4), 1465-1473 (2005)
   PUBMED   15687211
REFERENCE   4  (residues 1 to 808)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
REFERENCE   5  (residues 1 to 808)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445913
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..808
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..808
                     /product="glycogen debranching protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004133 - glycogen debranching enzyme
                     activity [Evidence IEA]"
                     /GO_function="GO:0019156 - isoamylase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0005980 - glycogen catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=92178
     Region          48..807
                     /region_name="PulA"
                     /note="Pullulanase/glycogen debranching enzyme
                     [Carbohydrate transport and metabolism]; COG1523"
                     /db_xref="CDD:441132"
ORIGIN      
        1 msrlvgavls talfaagcse sdyvrlyhge arapsysvdd ieslrqigpt yvdkgvnfal
       61 ysenatrlel llfedpesnr partyemtry gdvwsvyveg vgagqhygfr awgpnweydp
      121 rwfpgsihgf kadadvygnr fnpnklltdp yskalhrdhd wgkgstasgp artevtyaas
      181 aksvlvkdgd yawgeveqqw ranrqdehwq ghgwqdlivy evhakgftad pasgvrfpgt
      241 yrgfgekaay laelgitave llpihekpld ggywgyqtin ffapevsyaa fkephqvine
      301 fkwmveqlhk hgievlvdvv ynhtgegglw rekletddvm pgeplesldp aetaglysfr
      361 gidnqayyal npdrrtywnn tgvgnqmrpn hrptrkliid slrfyveelh vdgfrfdlap
      421 ilgerdgdyn rwddprntvl qdviddpvlq kyntriiaep wsaggwycmp lgefpnsktq
      481 pgngwyewng rfrdwwrafi nqdgwklnsn egslcgrpgt vdggflmygs qewferngrr
      541 pyhsmnfitv hdgftmydlf ayeekqnrcg plnpvccdnp nspfcdkvsg eehnrsrnwg
      601 pigderaesm rrqmirnafm smmishgtpm ilggdewmrt qlgnnnayst lsdnafnwyq
      661 wgaylarder hrmfefvkaa irlrkehaya fapkdygtga plawksaqnt eaawdskqlm
      721 ihyhdasygp ellvlinmep raveftlpeg rkwtrlidtq ayfdspaylt tagldsrstg
      781 nawldvpspv ngptygmper tivvlrae
//
LOCUS       WP_284668343             222 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Myxococcus sp. SDU36].
ACCESSION   WP_284668343
VERSION     WP_284668343.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..222
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23888
     Region          40..145
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 msalleqall rydglpvaer fhvharafsa pllamaartp ggtvadigcg hgllsallal
       61 edsgrivhgv dpdsrkvawa rralagqpnv rieegtveet largasgrfd aavvcdvlyl
      121 lpeskwpgfl stvrgllkpg grlllkeveg dgswkhrkal tqewvmvsll grtkasggma
      181 lkpreeltry lrdagfevre vvdlgqgytt phvlyvaens vp
//
LOCUS       WP_284668375            1652 aa            linear   BCT 25-DEC-2024
DEFINITION  OTU domain-containing protein [Myxococcus sp. SDU36].
ACCESSION   WP_284668375
VERSION     WP_284668375.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 1652)
  AUTHORS   Du,J., Fu,L., Sui,Y. and Zhang,L.
  TITLE     The function and regulation of OTU deubiquitinases
  JOURNAL   Front Med 14 (5), 542-563 (2020)
   PUBMED   31884527
REFERENCE   2  (residues 1 to 1652)
  AUTHORS   Mevissen,T.E., Hospenthal,M.K., Geurink,P.P., Elliott,P.R.,
            Akutsu,M., Arnaudo,N., Ekkebus,R., Kulathu,Y., Wauer,T., El
            Oualid,F., Freund,S.M., Ovaa,H. and Komander,D.
  TITLE     OTU deubiquitinases reveal mechanisms of linkage specificity and
            enable ubiquitin chain restriction analysis
  JOURNAL   Cell 154 (1), 169-184 (2013)
   PUBMED   23827681
REFERENCE   3  (residues 1 to 1652)
  AUTHORS   Balakirev,M.Y., Tcherniuk,S.O., Jaquinod,M. and Chroboczek,J.
  TITLE     Otubains: a new family of cysteine proteases in the ubiquitin
            pathway
  JOURNAL   EMBO Rep 4 (5), 517-522 (2003)
   PUBMED   12704427
REFERENCE   4  (residues 1 to 1652)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A novel superfamily of predicted cysteine proteases from
            eukaryotes, viruses and Chlamydia pneumoniae
  JOURNAL   Trends Biochem Sci 25 (2), 50-52 (2000)
   PUBMED   10664582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17784946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1652
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..1652
                     /product="OTU domain-containing protein"
                     /GO_function="GO:0004843 - cysteine-type deubiquitinase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=182096
     Region          1023..1193
                     /region_name="OTU_232R-like"
                     /note="OTU (ovarian tumor) domain of Invertebrate
                     iridescent virus putative ubiquitin thioesterase 232R and
                     similar proteins; cd22758"
                     /db_xref="CDD:438595"
     Site            order(1039,1122,1125,1132..1135,1165,1167,1184,1188..1190)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:438595"
ORIGIN      
        1 mqcpncapgt mrdlsvtppr clecgavlvp apsstqssfg smetdveeed fefeeyatye
       61 dllasqeeve rlesgdyddv lddfldddep yrlssdemre etlraslatd dltppeppps
      121 ntmsddvaee rcvplgaett vsdkpvvpps fplrmllwni adlgggpsgt lpvreqwtid
      181 alahvirtan adivtilelk kkggirlvep kpptemkqnt grgssgkklp vlmqlatafv
      241 eptgyqikka sgtevgqiaa reaallndla khfselvrrt lwprdeegsd seawdpsdie
      301 wsktskelgt dtldiiegrl eaawgacepd lvkrfgrppa ktakdaddee deeedeeppe
      361 alvatsidvf gkqqaklday cllcvrllve egyydwlqpy asryssqekd akkggpeaae
      421 lrkrdelakl gvallrehcg ilfhrylavi agmkankvpa rrelvlensl hrsndahlqr
      481 vyekklaqyq erkngvkdap tshaglsefi ririalndqc kargeevyas wpaevpdqpv
      541 kglytqdeay gvlwrkskld vdeaaisyls ayvakrsqgg espsmdvdtv kslyskrepi
      601 ripvrlaqvq sapevsvvaw hppapgnhnk nargtdfraf lqyckderqe kvlgvvlsdl
      661 nidtarpkae lakdgtpyie tcverlsfhq ffqtllgpea dashlyamap qrstiakskf
      721 gswavdseka fgdgslktlr sfvnskvkpe qfaplktskg relrpvlsaa edvlahiesf
      781 itppqqryga sgfdkilvys rrtdgwlleq ssvyvipfpm vladeqekgl ffihgnllpk
      841 hlqpfwrliq ledaklpeke rifdnlrapg vkltgsedvr weavmaaakk lsdhmplvsd
      901 lrlvysgeea lvveevevat etvstelgal ealcaayqks haaddeatea lsaildaaer
      961 vpasdharsn alvaeamqwr etfaalrsag fdpeeywdrr pelksekgkd kgggngisld
     1021 thlasihqgr vpnagggdcl fralsqlffg teehhrevrq avvnhledll agqsldgggl
     1081 vgpataatfr qdmgllldwh rvawphepay rrvagvdpwr qylramsrdr awgdhvalaa
     1141 ashlfqvrfe mfartgatsy wtdlvdfvpr teghaarpll rlanlgnahy eavgptdapl
     1201 paasafpael ealsarrrrd egqappsgsm kvespqsata ptktatsdps tvgpvckwth
     1261 thyfksdtpa hhphalflfg endvakknky fqkstqavir mnpnalgirt cwvagvgmqd
     1321 tdlaknqvai dqdcdeavql lqsgkyttlv vpwnhaldsv digtgvaalp tnapktwahl
     1381 tkridalitw agkhlgtvlv vpqvnalvpt gvrqqpsdlh lqevsdvmhr aatmgedsst
     1441 svlgqpnvvs lrtllfsgat spetgllsdk dyeknkamld edlavltqkv esgqyrrlvl
     1501 erdeegdivl gtalgkldeh aprtldylre rlealcrrca evhvededsm qgieasqsld
     1561 flsaddggtp sggvkrkkps ladedddatq emdpaeriap sshkkrkfmg spadaeedee
     1621 vhlfdddvpp pppiveegde anpkkrkkgp te
//
LOCUS       WP_284668432             308 aa            linear   BCT 25-DEC-2024
DEFINITION  lipase family alpha/beta hydrolase [Myxococcus sp. SDU36].
ACCESSION   WP_284668432
VERSION     WP_284668432.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18498059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..308
                     /product="lipase family alpha/beta hydrolase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32636
     Region          28..135
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
     Region          32..278
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mrnavrtlvl avaalglwaq palantqtkt rypivlahgm agfdslfgvy dyfygigsdl
       61 raggatvyvt svpqfntteq rgeallaqvk divarsgkgk vnlighshgg mdvryvaavr
      121 pdlvasvttv gsphkgadla dylrgnlrgg sftesvlayf annlgtvlgl lsgktnpqda
      181 igalaalsks gtaafnqkyp agipssscgq gaatgtqgqr yyswsgtdpf tnlfdvsdyp
      241 mklssffyse andglvgrcs shfgtvlrdn ydmnhldevn qvlgltafft npktvfrnha
      301 nrlkglgl
//
LOCUS       WP_284668443              59 aa            linear   BCT 25-DEC-2024
DEFINITION  cbb3-type cytochrome oxidase subunit 3 [Myxococcus sp. SDU36].
ACCESSION   WP_284668443
VERSION     WP_284668443.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008800
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..59
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..59
                     /product="cbb3-type cytochrome oxidase subunit 3"
                     /calculated_mol_wt=6494
     Region          9..52
                     /region_name="CcoQ"
                     /note="Cbb3-type cytochrome oxidase, subunit 3 [Energy
                     production and conversion]; COG4736"
                     /db_xref="CDD:443770"
ORIGIN      
        1 mykqfyqgms ltelplfalv lfiavflgvv awvfvarrsg dfdalarmpl seqgeaghe
//
LOCUS       WP_284668449             218 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Myxococcus sp. SDU36].
ACCESSION   WP_284668449
VERSION     WP_284668449.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..218
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=23234
     Region          <2..203
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mkriivvglg nfgsvlavrl heqghdviai dprpavvdal gsrvskamvg datqrqvlee
       61 vgargadaai vstgedlsas ilallalrdt giediyvkvr sddhariada lgatesifpe
      121 resalglasr itsgrllqyv qlgpefglqe mpvpeewygk slralalpqr yrvhvvavhd
      181 vlqdrmlpvp dpdrlltpsd allvagepsa leavaalr
//
LOCUS       WP_284668559             284 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Myxococcus sp. SDU36].
ACCESSION   WP_284668559
VERSION     WP_284668559.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..284
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32158
     Region          27..148
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mekrtdwyeh pqyyeaifgt dtvrevdflq tlserfgtgg klwlepacga grlveeassr
       61 glrvvgydis eamlaharkr ltpaqrrrvk lgpsrmesfa dpslegqvdv ahclvstfry
      121 ldseaaarqh lqgtrrllkp ggiyvlgfhl tdyararpeh erwvgqvged rvvcntnegl
      181 peqrarrspm rnrlrvtgpd kdwlietqwh frtysnaqaa klfrdagmrv lagytfdydi
      241 dapvergslr ldrvfvlqpd pgaasarkap ttastprkpr kvsr
//
LOCUS       WP_284668668             138 aa            linear   BCT 25-DEC-2024
DEFINITION  RCC1 domain-containing protein [Myxococcus sp. SDU36].
ACCESSION   WP_284668668
VERSION     WP_284668668.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Hadjebi,O., Casas-Terradellas,E., Garcia-Gonzalo,F.R. and Rosa,J.L.
  TITLE     The RCC1 superfamily: from genes, to function, to disease
  JOURNAL   Biochim Biophys Acta 1783 (8), 1467-1479 (2008)
   PUBMED   18442486
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Renault,L., Nassar,N., Vetter,I., Becker,J., Klebe,C., Roth,M. and
            Wittinghofer,A.
  TITLE     The 1.7 A crystal structure of the regulator of chromosome
            condensation (RCC1) reveals a seven-bladed propeller
  JOURNAL   Nature 392 (6671), 97-101 (1998)
   PUBMED   9510255
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..138
                     /product="RCC1 domain-containing protein"
                     /GO_function="GO:0003682 - chromatin binding [Evidence
                     IEA]"
                     /GO_function="GO:0005085 - guanyl-nucleotide exchange
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=13839
     Region          5..>135
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
ORIGIN      
        1 msvavavgpg frhslvlmeg gavrafgnnq ngqlgdgste swdypmvvag ltdvvkvtgg
       61 smhsaalkrd gtvwvwgrnd ygnlgtgvad gashplptpv pgmtdvvdia ngrdhilaan
      121 adgtvsaggl dasgqpwg
//
LOCUS       WP_284668695             498 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Myxococcus sp. SDU36].
ACCESSION   WP_284668695
VERSION     WP_284668695.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus sp. SDU36
  ORGANISM  Myxococcus sp. SDU36
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Myxococcus sp. SDU36"
                     /db_xref="taxon:2831967"
     Protein         1..498
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=53916
     Region          4..410
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mlsgfpyfvt dyvegetlhe wrwrtepsaa rlltvftevv rqvsalhqrg vchrdlksdn
       61 ilirtedekp lvfdygvarl pgmttltvgv pptspyllpp ecvtflgket wkqgahfdpg
      121 vpgdlyalgm llfealtdgy afhpklpydl lmvaiatrvp aaphmlnpkv prvlsditlr
      181 llekrpeary psaeallqal wdaakerkqp ewqtslalpp peeeapespt paahlhaaee
      241 ssavecvera aaadelaqvk aetpgapmle gtdgvsveap vlprwrsvlw slcsllvlsl
      301 alwlglstla ttldkgsphv ptatpesplt alrsgpsrfl tatlcavagl acsaaqvrpe
      361 paecpeeare amsrvlavdt tkglkavidi nqpgdqsqlg tyrngavvgr iagyswadps
      421 lpdgtllygr lwtglvdeyg rpaamaryse aklpdgrtfp vcivvgnpdg rvrtqpgsnp
      481 dtavlprelp vsaverwp
//
LOCUS       WP_284668813             325 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Photobacterium damselae].
ACCESSION   WP_284668813
VERSION     WP_284668813.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434433
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..325
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=36514
     Region          <129..251
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          155..179
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          189..219
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
ORIGIN      
        1 mekikigyww llclcllfvs qtqaqatypa pntmsveday qlgdllvdqy kikqgqpylk
       61 yaadkgnaka alaysrslst nvmvlgpqeh eyavkaaklg nedamltlsl srnifgdrea
      121 frsvllnklr ekaaqgdada mrklsllflg tsdeldwlkk aaehgdanaq yelgrtyevg
      181 dgwffipgkr ekevkrlyka saeqgnfrgm egyasillre gkkekaleiw tkmantgdag
      241 siiflaagyl natpritype kdevlgaays kiyldsmgtd kkqslyeiyk edyleamshl
      301 seaqkeqvne fakeflktht vrvlr
//
LOCUS       WP_284668822             500 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Photobacterium
            damselae].
ACCESSION   WP_284668822
VERSION     WP_284668822.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..500
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=56955
     Region          <166..500
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mkqwltytae miecrkcsel itffqnvsve qlavaqcwvf ypsddgrfli sdngseqwev
       61 ddfdhpfsha lhhakpilld skklhfwrqn sdfehfsqqv sddesllvvp lpfqshrvka
      121 vvglignkqi innilndenw lkfsqvfisq willrelask hrqelqlnes itqlksnktn
      181 kgrrdlshhl igsspvmesl reqiaiaaqs sltvliqget gsgkelvaka ihtlsdrkdk
      241 afvavncaai penlleself gyekgaftga isarkgliaq adggtlflde mgemplalqa
      301 kllrvletle yrplgsnkeq rsqfrlvaat hvnlrknvnq gsfrqdlfyr lyqypldvps
      361 lsnrlndide laevfieqyn qrenrhvlgf dtqtlallkt feypgnvrql rslveyacvh
      421 tdsnqfineq alpktdmsse klvsslpfee iddlklalee yerkiicdrl tffagdraka
      481 aeslglpkrt lahkcqklei
//
LOCUS       WP_284668905             342 aa            linear   BCT 25-DEC-2024
DEFINITION  formylglycine-generating enzyme family protein [Photobacterium
            damselae].
ACCESSION   WP_284668905
VERSION     WP_284668905.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..342
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=38629
     Region          68..334
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 mkvnsillii isanlvacnd sgntvsseii skqeiaridt ninklypdad sklkqhilnv
       61 aveslesmvf ikggtfmmgd fkapcspldi krmdwipeas cntalsmtrt ganhqhkvtl
      121 snyslsdhet lalsfdvfrq annlpflsea fsqlkrtred kkfmtllknt pmptkswqea
      181 kdyclwlgkl tnypidlpte aqweyaarnr gqnvyfatnn gyvqeigsyy vnkdgsiqey
      241 tkvqgnygsf gdikrwppnp lglydmagns rewvndwysk dyykvspeln pqgpetgtek
      301 vvrgwggsmp ltttrshekp tdsryisrrg frcavqspts iy
//
LOCUS       WP_284669084             438 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 dependent transcriptional regulator [Photobacterium
            damselae].
ACCESSION   WP_284669084
VERSION     WP_284669084.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18347682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..438
                     /product="sigma-54 dependent transcriptional regulator"
                     /calculated_mol_wt=49511
     Region          2..122
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <105..431
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mrtsfrfesd vshlfvfgsi esscltaleq sewqchfchd mrmaesvlle lgpciglvdl
       61 sqsyfslhsf asllnrhkqv rwialidekq lnneavcqfi vnfcfdyfsl pipipqlltt
      121 ighqcgmlal eryvwpelrq lgqiglqgds avmrklqnqv trtalsdlpv fiqgeigtgk
      181 eivaqaihrg sirakypfir vncrellagw nietadgvkn clmaaqggvl flddivhlsl
      241 ehqaqllqil elgyyqnsdq erlfidirmm asttvshqel lvsgklmtel yyrlnivsit
      301 vpplrergdd ivslahllll qysrqyngva qcfsddalna lrqypwpgnv relvsklkrv
      361 alladhqcvg sellelpgtq edthslkqar adsdraavik vlennhnqit asarelgisr
      421 atmyrllkky dlhpnknk
//
LOCUS       WP_284669085             237 aa            linear   BCT 25-DEC-2024
DEFINITION  tRNA1(Val) (adenine(37)-N6)-methyltransferase [Photobacterium
            damselae].
ACCESSION   WP_284669085
VERSION     WP_284669085.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..237
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25568
     Region          4..233
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 mssgftlkqf hvnhggcgmp vstdgillga wakldqtqpi ldigtgsgll almaaqrtcd
       61 asitaieldp taalvakdnf ghspwsarls cieanlihwf ptiskqtfgs ivcnppyfnf
      121 gqqaqqgqra qarhtdtlsh sallqalkhl ladngqasli lptyegeqli kaatgyglsc
      181 crlcrvqsta kkpifrllma ftasenrnce ettlcihdgn gysaefitlt qsfylnm
//
LOCUS       WP_284669102             808 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-mannosidase [Photobacterium damselae].
ACCESSION   WP_284669102
VERSION     WP_284669102.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 808)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 808)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 808)
  AUTHORS   Nascimento,A.S., Muniz,J.R., Aparicio,R., Golubev,A.M. and
            Polikarpov,I.
  TITLE     Insights into the structure and function of fungal
            beta-mannosidases from glycoside hydrolase family 2 based on
            multiple crystal structures of the Trichoderma harzianum enzyme
  JOURNAL   FEBS J 281 (18), 4165-4178 (2014)
   PUBMED   24975648
REFERENCE   4  (residues 1 to 808)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 808)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14312040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..808
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..808
                     /product="beta-mannosidase"
                     /EC_number="3.2.1.25"
                     /GO_function="GO:0004567 - beta-mannosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005537 - D-mannose binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=93358
     Region          23..695
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          732..806
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; pfam17753"
                     /db_xref="CDD:465483"
ORIGIN      
        1 mtislngqwi ltcvqraaiq ditvelpgdv hsalleagei pdphwatned kvqwirecdw
       61 lvsrsfqlte dqltcqamdl vlhdlesive irvnghtvad fnnmfirhkv eilpclkvgl
      121 nhiemvlrhq dptqvaldkl afnmpideqg taqidlnalr qssclsssfw gvnipvigvf
      181 ddielqplqq irvshistkq nwqesgcela vtlhyeavts rglaiaevtf ddqtfhltld
      241 rdaeqasvlf ridnprlwwp agygqprlyd lrvevdgqli eqkiglrkle vvtepneqgh
      301 nfsvkvndel ikvrgtnwlp ldalpgrmts eryqkllada aeanmnmvrv wgggryekei
      361 fyrqcdalgl lvwqdvmfsd afmlptpdvm tevkeellwq arrlknhsci alwggdnpiv
      421 dgiyqqlpnr qerdkylsny drlmrnirqv leqedpkrlf wvsasyydds ehcrpwqdld
      481 sgdchywdiw hqgldyvhsr khipnfcsef gfqswpslpt vrtiapekhw nisspsmeqh
      541 qrngkgnati vdmftrnyrf pdgfanmlyl sqvqqaivtk taveawrlqe kntgmllwql
      601 ndfspqsscs sveyngrwkp lhyhakrffa pltatfmadn dgvklyllnd srrgevlkge
      661 vvwqswegei lfrdpinqyl epgkclsvwe wltedlagre eegffhvhlr qganiientw
      721 fpkrlkhcel adpdlryeva eidnqlyvmi tsskpaffvh leyqgaghfs dssftlvpeh
      781 qrqikytgpa tleeltaglt vyhlrnsy
//
LOCUS       WP_284669347             631 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidase U32 family protein [Photobacterium damselae].
ACCESSION   WP_284669347
VERSION     WP_284669347.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..631
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=70610
     Region          17..315
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
     Region          458..516
                     /region_name="DUF3656"
                     /note="Collagenase; pfam12392"
                     /db_xref="CDD:463557"
ORIGIN      
        1 mtsaselstt plghisnrie llapaknadf gieaikhgad avyiggpafg araaagnsie
       61 diqrlcefah ryhaqvfval ntilsdsela qaeqliwdiy hagadalivq dmgilqlnlp
      121 plalhastqi dnrdkekvef leqvgftqvv larelslpqi hdiaahtnmq ieffihgalc
      181 vsysgqcyis haftnrsanr gscsqmcrlp cnlktrqgev laenqhllsl kdnnqtanle
      241 alidagvrsf kiegrlkdls yvknvtahyr reldaimarr pelyssshgr vetnfnadpd
      301 ksfnrgktdy fvqdrnagis dfrtpkylgq kagkvrlvgk dfieldsdle fnngdgiayf
      361 sqnylkvqqs ddklqgirvn radgnrlyfa qmpkdlkvgm vvyrnfdkaf edllakdssr
      421 rrigvsmila dshrglmltl tddygfsaqv efecektpan daektlanir kqlnklgntd
      481 feardiqvkt sqmwftpasv lnglrrdgia aleqarfegy qrpaagkynp dvefpkrhls
      541 ylgnvantsa kafyqqhgvi evedayelnk vyedvplmit khclrfsfnq cpkqvegika
      601 epmilemgge tlklvfdclk cemkvvghnk q
//
LOCUS       WP_284669530             468 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Photobacterium
            damselae].
ACCESSION   WP_284669530
VERSION     WP_284669530.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..468
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49621
     Region          6..456
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mnplhdtifs flkafdnlvw gppllillvg tgmyltfrlg fiqirylpla lryvfggkkd
       61 kdaqgegdvs sfaalctals atigtgnivg vataiklggp galfwmwlaa lfgmatkyae
      121 cllavkyreq dangqmlggp myyldkgvgs kwlaklfalf aigvacfgig tfpqanaive
      181 aaqisfsvpk eitvviltvl vamvtlggiq sissvaskvv plmagfyiia clivlgtnis
      241 hlpeavslvi esaftghaat ggflgagiml aiqsgiargv fsnesglgsa piaaaaaqte
      301 ssvrqglvsm tgtffdtiii ctmtgltlvv tgawqtdlag atmtthafsm glnsdyygpl
      361 mvsiglmffa fttilgwnyy gercvaylfg vkailpyklf flvliaagaf mkldmiwiia
      421 divnglmaip nliglvclrh viiaesqtff aqlkaereqe kqqaaqam
//
LOCUS       WP_284669590             410 aa            linear   BCT 25-DEC-2024
DEFINITION  mechanosensitive ion channel family protein [Photobacterium
            damselae].
ACCESSION   WP_284669590
VERSION     WP_284669590.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..410
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46206
     Region          89..394
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mskqirqava egmsklgini qphdnfstiv ililctvvaf gtyvivrwgv lkilnamikr
       61 tkskwgtilv hhqvleklcl iipavvmnll iplvldqyvl lsdlidrvlg iwlifalirs
      121 syafldasnd ifnmnhlskn lpvksfvqlf kltiffigff vgisiladrs pvyflsglgv
      181 atglvllmfk dtilgfvagi qlaanqmiqv gdwiqmdkyg angsvdevsl ttikvknfdn
      241 tvtnipayal vqdsfinwrq mqesggrrik rsilinidti rflteddeqk latipfvgqy
      301 ikekkdelnr sgnpylvnsl tnitvfrayl eaflqqnthl rkdmtflvre leptaqglpi
      361 qiyvfandtr wayyegiqad ifdhvfavlp qfglaayqsp aasdireiki
//
LOCUS       WP_284669704             724 aa            linear   BCT 25-DEC-2024
DEFINITION  GumC family protein [Photobacterium damselae].
ACCESSION   WP_284669704
VERSION     WP_284669704.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 724)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..724
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=80647
     Region          13..707
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 maislvengt klessvdlsq yfvelkkhwl kllsvtvvvt glsipfiysm tseyvstatv
       61 llkakednvs pienvetyds tqaeyyptqy dliqsrvvla eavkllklnd npdfngesdl
      121 ikkddglgsk lldfiglsse vnqdqfvpkl tddmklenai dvvqknltvs gvrltqlvkv
      181 syqspspqla keiangvvea ykiytinqkr nktvdaeqwn niqisylkne idkkkhamdv
      241 ylkdhgllty ngidgfeteq msivanrlad avqkramaqa dyelvkhiss tnlssvanls
      301 qisnhpqlqd lkialiqarr klselqkryg pkysqvieak aeitaiqqqt dvllqglkag
      361 iydnyqaavr neneykklls iqkndftnit akrdkyndlk adldktqely qelykrtqeq
      421 kisakyeead vvlydpavlp vkpikpnkpl fvimvmiltl visvvftivk aalnnkvltl
      481 sdverklgls kigevpllig vnsvsiskai yahdtaveml lgmkntlqlk hkktkvlgit
      541 ssisgegstl iasmlasifa idkkvllldl nyrkfglsdq llsthsdgfa ewvysdskga
      601 vpyivkqdng veflnrgnvk gsplqflmqs etqlsfqqla qhydmvivdl paisegqdal
      661 vvadfidsll vtvaanqadv seikenleql aivnsniiga vlnkvsdenv vteevirfls
      721 dser
//
LOCUS       WP_284669706             318 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Photobacterium damselae].
ACCESSION   WP_284669706
VERSION     WP_284669706.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..318
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35428
     Region          7..306
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 miinkfqtlk lhlqsqvigq pelveqllia lladghilve gppglaktra vkvlsdcieg
       61 kfhriqftpd llpadltgtd ifrpetgefs fqagpifnsl iladeinrap akvqaamlea
      121 maekqitagr ktyplpelfl vmatqnpieq egtyplpeaq ldrfllqlmv dypnadsele
      181 ilrlnrgeal gnkvaeavti sqeeifeark qvltihmaed veqyiirivm atrqpekysd
      241 tlaswlqmgv spratlaldr carahawlqg rdfvtpedvq tmafpvlrhr lllsyeaqae
      301 giasdrvieh lleqvasv
//
LOCUS       WP_284669472             509 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional NUDIX hydrolase/phosphatase PAP2 family protein
            [Photobacterium damselae].
ACCESSION   WP_284669472
VERSION     WP_284669472.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   5  (residues 1 to 509)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
REFERENCE   6  (residues 1 to 509)
  AUTHORS   Stukey,J. and Carman,G.M.
  TITLE     Identification of a novel phosphatase sequence motif
  JOURNAL   Protein Sci 6 (2), 469-472 (1997)
   PUBMED   9041652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10120923
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..509
                     /product="bifunctional NUDIX hydrolase/phosphatase PAP2
                     family protein"
                     /EC_number="3.1.3.-"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=56796
     Region          41..120
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cd02883"
                     /db_xref="CDD:467528"
     Region          193..374
                     /region_name="PAP2_like"
                     /note="PAP2_like proteins, a super-family of histidine
                     phosphatases and vanadium haloperoxidases, includes type 2
                     phosphatidic acid phosphatase or lipid phosphate
                     phosphatase (LPP), Glucose-6-phosphatase,
                     Phosphatidylglycerophosphatase B and bacterial acid...;
                     cl00474"
                     /db_xref="CDD:469784"
     Site            order(268,275,295..297,347,353,357)
                     /site_type="active"
                     /db_xref="CDD:238813"
ORIGIN      
        1 mhniigqril llffilvslt fgsigsawas sttsevpegi vgavcvirhd nkvvmisevi
       61 teklalpggy idsgynapqt aiqealeetg lhvhvdkflq yrgraaiyac vandpipvte
      121 fktksgftav aswssahfgk evkqvylinp fkvdgknyry pddiallkkw lqqtpnsavt
      181 yyhnlsqevn plhrwelsqm ltfqhwvdgl pswqqtlfss wmtvtnlpge ygfiftvlfg
      241 cliafgpvsf lrlstvmlsv tmvasiiklt iasprpfyii palqkvaasg ygfpsghtlm
      301 alvlwsfigi qvyryikvhn psaqltrwrv giistvvlfs lsqavarvwy gvhfisdtva
      361 slvigsvmia gftlwinldk hnltrcmtnk wfwlnvtvaf gliagttqap dhiylfscvl
      421 aiflindyvp rqyqrlnlry llglitclli gcsvilysgy mlinlsnvsl ivlairsiti
      481 vvlitwilgc sswfyrqtcp plahaqqan
//
LOCUS       WP_284669655             572 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 36 protein [Photobacterium damselae].
ACCESSION   WP_284669655
VERSION     WP_284669655.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Rigden,D.J.
  TITLE     Iterative database searches demonstrate that glycoside hydrolase
            families 27, 31, 36 and 66 share a common evolutionary origin with
            family 13
  JOURNAL   FEBS Lett 523 (1-3), 17-22 (2002)
   PUBMED   12123797
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 572)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10201328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..572
                     /product="glycoside hydrolase family 36 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016052 - carbohydrate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=64429
     Region          126..>233
                     /region_name="AmyAc_family"
                     /note="Alpha amylase catalytic domain family; cl38930"
                     /db_xref="CDD:476817"
     Region          190..476
                     /region_name="GH36"
                     /note="glycosyl hydrolase family 36 (GH36); cd14791"
                     /db_xref="CDD:269892"
     Site            order(196,229,266,341,345,384,399,402)
                     /site_type="active"
                     /db_xref="CDD:269892"
ORIGIN      
        1 msctlnsipf qpaanidvsa cceqlnvvyl taestyslsa ttligrftfp yqgtesiigd
       61 gfqmlaqtgg tieqpqaigr cpdnnseyri yphdapnryy nylvieqegq ftlfgftsch
      121 rfagyfeihd qsiyafidge hcvfkpdtan gitleqivtv vgsnlqdvyq sftkainynh
      181 pkrndtqrsp vgwcswyayy agvsasdieq nircmtgenk niewvllddg yqaymgdwlt
      241 pserfsdgiq tviakikqqg kqpgiwlapf iaepsseifk qhpnwfvchk egellkaetv
      301 tyggwrctpw yildtshpev qahltsvvkt mreewgvelf kldanywgtl kgaryqkdct
      361 gvaayrlgme aiakgagsaw llgcnapmwp slglvdamrv sddvernphr fsqiaqetfy
      421 rswqhlalwh idpdcvtlid lesqktshns ylfhrdvvla sgglllsgdp lahwtpfaqq
      481 sfhrlverqc qtpnsaefnd lslaqaeltl dkqqtlyigf nyndanartv tfdaqenkdw
      541 fdfwtgecva mgvssyqvql spglnscsvv ar
//
LOCUS       WP_284669865             596 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Photobacterium damselae].
ACCESSION   WP_284669865
VERSION     WP_284669865.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 596)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 596)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 596)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..596
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=65374
     Region          20..493
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mheemigltl aglgvlglgc qwlawrlklp ailflliagi vigpvtgifq pndmfgdllf
       61 plislsvaii lfegsltlnf keirevnktv qsivsigavv twlitstath ylldlswsms
      121 flfgsmtvvt gptvivpllr tvrpqaklan ilrwegilid pigalfvvlv yefmvsssev
      181 hslevfalil avglifgala gwfiavvlrr hllpeylqpf avlavvlgvf agsnaiesea
      241 gllavtvmgm wlanakevni qhilhfkenl tillisglfl llaaridltd fkalgfsaaa
      301 lfiviqfvar pasiflstlr sglqckeklf lawvaprgiv aaaisslfai klsqagikea
      361 ellvpltfmv iigtvvlqsi sarpmakllk vaepsprgfl ivgandvart igielkkydc
      421 rvvmtdsnwd yirnarmagl dtyygnpvss hadeylnlig vgkvlamtpd khlnvvacmh
      481 fmndfgersv yslygnrsns nfnekhyaaq erhgltlfnq dvsykklasf inqgaevrht
      541 kiseafsled yyeqyktaqi iplfavdpkl nihvfsstiq pdvkagwtmi slikea
//
LOCUS       WP_284669914             446 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Photobacterium
            damselae].
ACCESSION   WP_284669914
VERSION     WP_284669914.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..446
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51324
     Region          29..435
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mtvnhqanvk kvnkkvvils ssndswvlll ernnydvvrc kdireldail edeincicia
       61 dltncvfsla cittkamnnq hvrwitilnk eqldvdvvrs figkfcsdyf lspivdgqfm
      121 pfikhqmgmt kitnnknpkd lliklllsge skkvkrlkdl vrrvsssdvn ifitgengtk
      181 kqslarylwh ssgrkygrff tidcdlllts stqrdifyhy fsnsaknten fknetvylkn
      241 lqslpqdfql klleffnldl ksrlrletqn dikiissssi qpdtllneyq fnkelfykln
      301 ifhldvpslr ersedirkfa qyfldihlnk intmavkfse didklllsyp wpnnlielen
      361 qvkqavisse gpvitsdafl lpstkcakrs lksikdeaek dillsalhlh hgqvmsaakd
      421 lgisratmyr llskhqilpd gdrira
//
LOCUS       WP_284669942             467 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 1 protein [Photobacterium damselae].
ACCESSION   WP_284669942
VERSION     WP_284669942.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Strazzulli,A., Perugino,G., Mazzone,M., Rossi,M., Withers,S.G. and
            Moracci,M.
  TITLE     Probing the role of an invariant active site His in family GH1
            beta-glycosidases
  JOURNAL   J Enzyme Inhib Med Chem 34 (1), 973-980 (2019)
   PUBMED   31072150
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Ketudat Cairns,J.R. and Esen,A.
  TITLE     beta-Glucosidases
  JOURNAL   Cell Mol Life Sci 67 (20), 3389-3405 (2010)
   PUBMED   20490603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006560
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..467
                     /product="glycoside hydrolase family 1 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53317
     Region          4..459
                     /region_name="BglB"
                     /note="Beta-glucosidase/6-phospho-beta-glucosidase/beta-
                     galactosidase [Carbohydrate transport and metabolism];
                     COG2723"
                     /db_xref="CDD:442035"
ORIGIN      
        1 mttqtlgfpp hflwggaiaa nqvegaynqd gkglstsdml pkgilsphqp rsertsgikd
       61 iaidfyhryp edislfkemg fttlrlsiaw trifpngdel epnelglayy drifdelakh
      121 hiqpfvtlsh yempmylteq yggwadrrli dfferyartv feryknkvkl wltfneinms
      181 lhapftgvgl aedsteqqiy qaihhqllan akavnlchqi ipnakignml lgamnypltc
      241 tpddviaamh ennkwlffgd vqvrgrypgy mlryfrendi qleieegdle llanasvdfv
      301 sfsyyasgca sadpkqketg nivasvpnpy leksewgwli dpkglrylln flwdryqkpl
      361 fivenglgah dqmtsdgeil ddyriqylnd hlvqareava dgvdlmgftc wgpidlvans
      421 taemskrygf iyvdrhndgs gsltrtrkks fywyqkviat hgqsltv
//
LOCUS       WP_284670010             948 aa            linear   BCT 25-DEC-2024
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Photobacterium damselae].
ACCESSION   WP_284670010
VERSION     WP_284670010.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 948)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..948
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=105340
     Region          58..947
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msvelsrrsf ikqgvmagic iytvpalarf nlnldgsscl ispelesswk snfkvnfrtd
       61 avakvtgekv ygrdlragdi dewpnqqywa yyirvdradh iyegidinfl pqnakpttvi
      121 taetlikdnv qlppfygvnm lvaegqtpdy lgqaaallif dsfltfnrak smiqfndnvi
      181 kygkktplva nsldpwgtwr itrvegnskg tlpdlysplk nglnfpnyvd hkpfwpqana
      241 ngssleqqms vaktiesamy epdnfilerr yqtqiidpmf mepecfngwy dkqtqtmhti
      301 ptsqspadfy ryatlmlsqg plagkvknlv vhspyigggf ggkdhsilpy ygllaamycd
      361 kpvrmandrf qqfqsglkrh pfdmhnrlsi nkktgkfqgi issmsldggg renfssvvae
      421 vgasalqsiy yfprnditav anvsdnpdag smrgfgtlqt maamemmvne vaqllnidpi
      481 dlrlrnaiki gqantqgavp tstehykeil kqvqnheiwt qkeqrrkefe aknpnkkfgt
      541 gfaictkdyg agneapstyi emdrtgnlvl gvavveigtg aqtsqaavie pyfgrpadtv
      601 nlaevegwap lqlietesaf tmsqsyqdkm qqnprwtpsv elassasnsa yfqskatena
      661 akivfeyglw paakaiwskl yysgseysdi dfgpmedavw vdgklsaqgm mplelsmlaq
      721 yahqhglvts amvhsfnrwa wvesdftieg ntqryeldav aikygsgasa dkqklmsseg
      781 whlldrsnvr ypatalnnam vvyyapcatv vdlavelgtg kveivrthtw ldagkvivke
      841 lvegqieggl vmgighalhe ylpsgnegpg dgswnlnryh vplapdvgvw nmehtlmppf
      901 nnsdqrkgia evvmipivpa itealyqitn trfyhlpvta qdikeala
//
LOCUS       WP_284670043             284 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfurtransferase [Photobacterium damselae].
ACCESSION   WP_284670043
VERSION     WP_284670043.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..284
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31407
     Region          17..283
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mvkrhpngss lvtvewlkqh itdqnlvvld aswfmpntgr ngeqewlqqr ipgarffdfd
       61 qkiaapntvf phmlptveqf aqevgklgin nhshvvvyds qgifssprvw wmfkvmghdg
      121 vsildgglpa wieagyelet dapqpvveqk fnvqyqnnwv idadnlyakl nnsnvsvida
      181 rpadrfyalv aepragvrsg hmpnakslpf pellncgrml paselsarfs alvasdqqli
      241 fscgsgvtac ilalaadlag yenltvydgs wsewgaveky pvvn
//
LOCUS       WP_284670089             445 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Photobacterium damselae].
ACCESSION   WP_284670089
VERSION     WP_284670089.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..445
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=51370
     Region          91..430
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrrlyiesfi glivlfglsl ycyeviiyrw ntdydyvled yeaealhdlv dniyhnegsk
       61 aaylaiekya tktrqtltvh nkdelpddvk tfffttapqs ytyhdddril wfrltlssdf
      121 yslkpnfdtp lrraidfddn mvwvffmggf alysilfiwy lsrrvrllek ttlafahgef
      181 aarartesrf rvgtlnqsfn ymadkisnll isnkaltnai ahelrtpifr iqwqaellad
      241 svkdkeiqqk iesivedtee mesmvnelly yakveqpdte lhcqdivfnq ylndilqnwe
      301 ktaqskitlk tpfkqnivss idtqlfkhvl nnlvsnasry srkhilvtls qerdsvfitv
      361 eddgpgipne hwpylfdpfy sadparnkaq sgfglglaia kqivarhkgq itigdsallg
      421 gakftvilpi tcqcdpildr pnisk
//
LOCUS       WP_284670272             352 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Pseudomonas sp. HR1].
ACCESSION   WP_284670272
VERSION     WP_284670272.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..352
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36740
     Region          42..345
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mseaanashg naiaeqrare rrrwracgvf llltlaglvl diatgpslls plevlksltg
       61 lgerqpmtda ivrdlrlpva lmalavgaal gaggaqmqtl lnnpmaspyt lgmaaaagcg
      121 aalslalgsf glgaligmpl gafafamlaa lflfalaslk rtgsdtiilg giallflfqs
      181 llslvqflss pelsqqilfw lfgslgratw ttlaivagvt llccllllrd awklaalrlg
      241 earaeslgvn irrlrlkvli lvavmtatat sfvgvigfvg lvaphiarwq vgedqrfllp
      301 lsaicgalml sfasvlsksi lpgalfpvgi vtaivgvpfl lwlifaprrs sp
//
LOCUS       WP_284670205             559 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Pseudomonas sp. HR1].
ACCESSION   WP_284670205
VERSION     WP_284670205.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..559
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60901
     Region          9..301
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mlpssstasp raaqlerall lgclaaylla glfgrglwka depysfgmvw nflttpdwlv
       61 prvgtapfme kpplmywtga ltarlatpwl sapdgarlav lgwmlvtlaa lawlterllp
      121 grrreavlal lgmlgvvqhs hlliadvpql agatlglagl aaqlhdnrhp wrrgllfgsg
      181 lgiafmskgl lvpgvlgltg llcalcwprr lvepegrhwl laaslaalpw llvwpallwh
      241 rspelfhtwl wtnnigrffg learnsdtdg lassladlla lsfptglill gatlwqlyrr
      301 ggsplkrlgr hpglatvvly aivclavllk savfrslyll plfpalalla arlqpppala
      361 algrtlglaf wtpiivlltl ggfglalgwp lpwpalvrdh lplaerlpvg llawtlaala
      421 llgwglalgl hrrlapgslw fvgltvswsl anslwlpwvd lgnsyarpft elqrvlprtd
      481 cvasyglges ersmlhvygg yppleltalr qapcqvlvvq dewheavavp pgwqllwqga
      541 rpgnlkerfr afmvsprvp
//
LOCUS       WP_284670407             243 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Pseudomonas sp.
            HR1].
ACCESSION   WP_284670407
VERSION     WP_284670407.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..243
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=26132
     Region          8..243
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 matalsiart hpgkerahne dallerpsdg lwavadgmgg hqdgarasrl aierlaetpl
       61 sggldqrleq vrrvlhdinr rltqdltvla egperligtt vvalvvsgge aaciwagdsr
      121 aylwrgdrly qltrdhrlle rlidveglsp rqaarhpgar altqalgare alaldivrfg
      181 lqpsdrllls sdglhdalee ralgaalslp spalalerll dgvlkgpard nltaivihlr
      241 eaa
//
LOCUS       WP_284670520             215 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pseudomonas sp. HR1].
ACCESSION   WP_284670520
VERSION     WP_284670520.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..215
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23083
     Region          84..>127
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(85,89,114)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(88,113)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(95..96,107,110,114..115)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 msytstgyms ipatsnreff ksvtratvaa iglvlgtgsv apstnyndrh gnyrpvnpts
       61 nlgsrpiakl spevadlitv eqhlkkikth iglsiselsg flgvtrqaiy kwqaglstpd
      121 tenimkvrel srladglaea kvsrpsdlvk akafngssil dlmkrdedys eslaalikey
      181 rvldasytas kisvlkgagn sdwkssisvp sanev
//
LOCUS       WP_284670586             266 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Pseudomonas sp. HR1].
ACCESSION   WP_284670586
VERSION     WP_284670586.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 266)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..266
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28216
     Region          1..231
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtrspqgtal itgassgiga hyaeqlaqrg ydlilvardr qrldalaqrl tdatrqsvqv
       61 lpadladpaa laevertlre dasltllvnn agmgthtpll qsdpaqmlrm ialnvtaltq
      121 ltyaavpafv argrgaiinv ssivslapel lngvyggska yvtaftqslq relagtgvra
      181 qavlpgatat dfwargglpl ahldpeivms padlvaaalt dferevaisi pslhdlsrwe
      241 tyeasrlama dqlssrqlap ryhtah
//
LOCUS       WP_284670587             489 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Pseudomonas sp.
            HR1].
ACCESSION   WP_284670587
VERSION     WP_284670587.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..489
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=53777
     Region          <177..482
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mlplfialgq hedpaqlalg lvegiqrlar ldlvqyyrld athtqlvcla qsldstaama
       61 gnalpleqes llhyclsqnr slhlreldpl lhtttflpgd gwrslgclpl tgpsgsvegl
      121 lvqasrcrre lethaevltp lgcfalaqsq lleraqtqpl gavterptsp avgdgfgmlg
      181 dsgamrqvhr ligkilhspi tvlltgetgt gkelvaraih ergsrrtqpf vvqncaalpe
      241 hlleselfgy rkgaftgaer draglfdaan ggtlfldeig dmpltlqakl lrvlqegevr
      301 plgsaethrv dvrivaathr qlvrlveqgt fredlyyrlt hfpiqlpplr ergedlplla
      361 rhfadqacac lqrsrcrwss aaldllagya fpgnvrelkg lveravllcd gnellpehfa
      421 irsadltgna gsltlrerld qlergllvdc lrknrgnqtq taqelglprr tllyrlqrls
      481 irsadlqls
//
LOCUS       WP_284670596             525 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Pseudomonas sp. HR1].
ACCESSION   WP_284670596
VERSION     WP_284670596.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..525
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58115
     Region          7..512
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mslirpdrrr vlqglgatll lpalgqrtwa apagrpgipd gvqagdvtgg qaliwsrtdr
       61 parllvewdt qesfrslrka agpvttaaqd ytaridlsgl padqhifyrv rfedvdsgal
      121 sepvighlrs apsqrgdirf vwggdtvgqg fginpdiggm riynamrerr pdfflhsgdt
      181 iyadgpvpaq ltveegriwr nltteakskv aetldefrgn yrynlmdahl krfnaevpqv
      241 wqwddhettn nwspsktldd ryrvkdinvl sgrarqafle yapmrgvsad gagriyrria
      301 ygplldvfvl dmrsyragnd snlgseeggq gafmgqeqld wlkkelqask atwkviaadm
      361 piglqvpdgk daqgqarwea iangdpgapk greletadll rfiarqgirn tvwltadvhy
      421 caahhyhpdr aafqdfepfw efvagplnag sfgpnpldat fgpevvfqka ppqantspls
      481 nfqffgevei dgktaelqvt lrdqdglpqf tqklqplnsn ttpva
//
LOCUS       WP_284669749             486 aa            linear   BCT 25-DEC-2024
DEFINITION  peptide MFS transporter [Photobacterium damselae].
ACCESSION   WP_284669749
VERSION     WP_284669749.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..486
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52875
     Region          2..443
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mrlasqpkgl fhliaiqmwe ffsyygmrsl lilfltqkll mtdhhayaly gaytslvyvt
       61 piiggyladr yfgnywsvvi gallmvagha vlsipsvgni smyialslii cgygffktns
      121 scllgelytk eheksresgf sisyiggnvg salapifcgy aamkwgwhvg falagigmlv
      181 gliifstgrr nfthvkkcnk daliqksagv phwliiivll altafglvfv lkdllagyil
      241 avicavsfyq ivalyrrssp sdrsklnsil yfmifgtvfw afdqqggssi slfiernint
      301 difgfhipta ffqsvnpvav ivgggavawf wkvlasksis vrtltklnmg lllltagftl
      361 itissklamn tghttflwlf iglfligvae lfidpvalaa itrlnpqgat stlagiymlm
      421 ggsvanyiaa niaeftasnt pvnadatdli asaaqyhhvf qsilfvtvav lvlgllvdfk
      481 nrhkav
//
LOCUS       WP_284670941             405 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudomonas sp. HR1].
ACCESSION   WP_284670941
VERSION     WP_284670941.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..405
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43558
     Region          9..372
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mlqgsvdsdv ciigagytgl stalfllehg fsvtvleaar vgfgasgrng gqivnsysrd
       61 idtierqlpa kqaqllgema feggriirer iarygiqcdl kdggvfaalt gkqlghleaq
      121 qklweryght qlqlldkagi grvvgtdryl gglldmsggh ihplnlalge aaavaslggk
      181 iyeqsaatri drganpvvht aqgqvkarfv vvagnaylgg lvpelaaksm pcgtqvltte
      241 plseelarsl lpqdycvedc nylldyfrls adrrliyggg vvygardpad ieaiirpkml
      301 qtfpqlkgvk idftwtgnfl ltlsrlpqvg rlgdniyysq gcsghgvtyt hlagkvlaea
      361 lrgqaerfda faglphypfp ggqllrvpft algatyyqlr drlgi
//
LOCUS       WP_284670928             231 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Pseudomonas sp. HR1].
ACCESSION   WP_284670928
VERSION     WP_284670928.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 231)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..231
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25003
     Region          58..217
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mkkpailatp wglygvlaam lactstvias qghgtqesvq tsskppifvy gntsarftli
       61 eygdlecpyc kdafpqlkql iarhdqlnwq wqhlplpmhg eaaqyearlv tcagwyggnp
      121 vfwqaieavy qhsrsngagl avpidqlglq pavslqhlqg cvqdnaavrq aiatqtsaaa
      181 kqridatptf elkdnssgrv irlpslldda gmlsamdwla tqegadaqqr q
//
LOCUS       WP_284671058             517 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Pseudomonas sp. HR1].
ACCESSION   WP_284671058
VERSION     WP_284671058.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..517
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=57566
     Region          4..516
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mnpsrrqalg llglglsapw fagcsarepq ldpftlgvas gdpaadgfvi wtrlapdpla
       61 edglgglhap vevrwevald pglrqvvqsg tvqaqpraaf svsitlvgll pgrpywyrft
      121 alghqsrigr altlpppasa pqrlklvaas cshyekgffs ayrhmadeqp dlalflgdyi
      181 yesnvplllp airrhglpea rdlasyrrrh alyrtdpdlq ylhadvtsll twddhevqnd
      241 ysgpwsadpr vslaafaarr qaayqafreh aplrawrtqg salrlydrwr fgdlaeihll
      301 dgrqyrsepa cattrtrggh lvapdcpglr dttrsmlgra qedwlldgfr hngtqwnlia
      361 qdlllaplrq rlpdgdparw tdgwdgypat rerllaamaa srlanpvtlg gdihsfwvtd
      421 lhrdpeders pvvasefvgt sitsdgpdyr rfqallpenp qvrffdsrer gylaleltre
      481 rlqvdlrtis drtrpdarrg trasfvveag rpgavpv
//
LOCUS       WP_284671063             328 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Pseudomonas sp. HR1].
ACCESSION   WP_284671063
VERSION     WP_284671063.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..328
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35179
     Region          1..325
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mnrfgyakpn avpdairqhg pqthfiaggt nlldlmkenv erpeqlidvn glplrevett
       61 aegglrigal vknaevayhp evqrryplla kailagaspq lrnmastggn llqrtrcyyf
      121 ydvgtpcnkr epgsgcgare gqnrihailg hseqciathp sdmcvalaal earvevsgps
      181 gervidfadf hrlpgdtper dtnlaadeli tavtlpadsl aansaylkir drasyafalv
      241 svaaaleldg erikqvrval ggvahkpwrl peaeqavvgq madkaafghl adrllqgaqg
      301 fahnafkiel arraivralt eaaggtlq
//
LOCUS       WP_284670998             445 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Pseudomonas sp. HR1].
ACCESSION   WP_284670998
VERSION     WP_284670998.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..445
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=47453
     Region          1..435
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mptlliiddd aglrdalaet aadqgyrvlq adggeaglql ltqeavdavl ldlrmpgldg
       61 levlariral peppavtvlt afasagntie amrlgafdhl tkpigrdeli rvlagmtaqr
      121 gpasappaav eghtlvggsd alrqvqktig rlvdseatvl vtgetgtgke lvaraihehg
      181 krrgapfvav ncaaippdll eselfghvrg afsgatanrl gafreaqggt lfldeigdmp
      241 lpmqakilra lqerevtpvg gapvrldvrl vaathrdlaq rvasgdfred lfyrlhvvpi
      301 hlpalrerra dilplaehfl apsgrvladd aaalllrhpw pgnvrelrna iqraatlaqg
      361 erivatdlaf lqsetpdeva idaswpeetl aeatarlerl lieralqrsg gnraeaarrl
      421 gihrqllytk lsrlglgvga ddspa
//
LOCUS       WP_284671071             344 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Pseudomonas sp. HR1].
ACCESSION   WP_284671071
VERSION     WP_284671071.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..344
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=38688
     Region          2..336
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mlvslqalra laawlvvfhh fmqvffdfha dslgghllst rgqvgvdiff vlsgfvihls
       61 tagrplrrst flwhriariv paywlytavt alilylasdv mpiygvaare lllslffips
      121 enpagfghyp ilpvgwtlnf emlfyllfal sfgvaerwri gmvsllvilv slvlaresfv
      181 ssfyrnpiif efllgvslaa lyrrgalrgp kplalvaala altclvafpa dhpwrlltwg
      241 vpsavlvgac vilepwfags rlckalgdws ysvylvhviv lwlgdywlhq qwgfspyqtl
      301 avclpvilll awasyewier rlsrtlrqlg erlagrrpqw vagq
//
LOCUS       WP_284671084             408 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Pseudomonas sp. HR1].
ACCESSION   WP_284671084
VERSION     WP_284671084.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..408
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43659
     Region          55..279
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
     Region          204..390
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mrslalplla gmlllskaap vradeatlar geyltrlgnc qgchtrpdga pfaggvafdt
       61 pfgrlyssni tpdrehglgd wtadefrral hdglgrdgeq lypafpytaf trlsdediag
      121 ifaylqiqrp vpyappangl rfpfdqrali rgwkwlnftp gplpvtadaq vaqgaylaea
      181 vghcqechtp rtwsqgldsg rayagatqqg wtawnltadp rglggwsdak lasylreghq
      241 rgeavaagpm aevvsggtrh lndadlgali aylrtlpaqp gavparaevq ppgetgplta
      301 aeaesaallq sacaschapd dqgpagpypr sfsnysavrd pagtnlvrvl ldgldrqgrt
      361 ehafmpayre llsdqqladl atyigrrfgg haadirpedv aaarereh
//
LOCUS       WP_284671091             717 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pseudomonas sp. HR1].
ACCESSION   WP_284671091
VERSION     WP_284671091.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 717)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 717)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 717)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..717
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=79507
     Region          54..710
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mtdaphsaas prevapasrl rlkprslfak fflafilvda lgtllftlhs yrqardassq
       61 sidyrlmsaa lalpeilged ylaqlqdpak adperyqrtl vtldryarka glaslyafvk
      121 egsdfrfimd saneeeirvg yfgdyrqlyd qappelgavf adhqprfaey qdnfgsfrsl
      181 flaipgqdgq avvigadmfm egiaaaeqsa lldslligai ifamgalvsr ilagalnryl
      241 arlgqateri adgdyqlglk egrdpvgrlg ramnqmgaal aarerrisql afrdmltrlp
      301 nqvrlvleir qrieraaagr favllldvan frninellgq eggdkilrhl arrlrvaape
      361 engvarigad tfvlllpwfd dasaeaalls lrnlvekpfv sgnqrvslri tfgiacypeh
      421 ggsaeallan aetalqdarr rqlpfafhdp dqerqrqlgi amldaldlav dhdqlrlylq
      481 pkialpdgrv egaevlirwq hpelgllkpd afvgiaeqsr kicditlwvl ercmrlqrer
      541 qlgalklnvn lslldlehpa fiarigrlld etgamaagfc leitesrams npvqvldclr
      601 qlkamgfels lddfgaghss laclssfpid elkidrqfie hcqlpgdqev irllvqlgql
      661 rglrvvaegv etrqalevlt dlgcdqiqgq lvagalsldd fqrwyaeqeq glwalra
//
LOCUS       WP_284671114             388 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudomonas sp. HR1].
ACCESSION   WP_284671114
VERSION     WP_284671114.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..388
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41637
     Region          2..361
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mivigaglhg lstawhlaqr gvrvivlead yagrhasgvn aggvrtlgrh laeiplalas
       61 ralwhhlpal lgtdasfvar gqlklaetda elqecrdrva hlqahgfthe vlinreevfe
      121 llptvaphvv ggiwvaddgy atpyqvvtav rhaaerlgvv lheqtpalsi tqrgtcwqve
      181 trqgrfdadq lvvtagawag rlaaevgepv ptypqglmlm vthrvapfcr qvlgatgral
      241 sfkqfdngtv viggkligal dfdarhgevd iarlvtsaqt vtdlfphlrh lginrawsgi
      301 eafteddlpv issssrasgl tysfgycgsg fqmslgtgqr vaqlvlgess pidlaafaid
      361 rfhrdfstpr qpkepicnpl pvskptsa
//
LOCUS       WP_284671140             818 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pseudomonas sp. HR1].
ACCESSION   WP_284671140
VERSION     WP_284671140.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 818)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 818)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 818)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 818)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..818
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..818
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=89852
     Region          134..797
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 msslssssal rtlrvvwpfv iilscqalva ivslqllstv rayvsaeslw skslgnamla
       61 lgayldegrp efyhaylasi svndldraar qeldsagdra eaarllrlag nspddidgli
      121 alfqmarhve pfegviarwq itdpymdefq alartgfeli klrgpgpali plkrqlldlh
      181 drmmpetvaf serlgvasrq lvaalfianv lvgallvlla iwrmhslvqq rwrseqalqa
      241 ekehiqvila slgdavlaln aqgrllyhnp aaerllawpg laagtpvthl fdiqtedqpa
      301 stqplaerlr sqdwlagnep lahqlvridg trvpvaltvt plprgesgtg vvlvmhdqtr
      361 eraflhdlaw qashdaltgl lnrrefetrl erllaredla casllfidld qfkivndtsg
      421 hfhgdrllrq lcellaqqlg eedclarlgg defgvllesr tpaqveavae rlrccvgslq
      481 feaagqgfrv glsigvvhlg gqalapeeal rladlacyaa kdkgrnriqv fapgdveldq
      541 rhgemawvqr lhralaedrf rlylqpilgl gqetvadrhv evlmrleege rliapgafip
      601 aaeryglmpd ldrwviaaal arfaelpdgl ldtlainlsg hslgeaglad fvrqqlqrwq
      661 iaparicfei tetsavanld aarlfmdelr glgvrfsldd fgagmssfty lkhlpvdylk
      721 idgsfvrhll edavdsamve ainqlghltg kktiaefaen pavvaaltal gvdyaqgygi
      781 arpqpftedt cqallrqvwh etsgtrvvvl eaaeeggq
//
LOCUS       WP_284671156             469 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Pseudomonas sp. HR1].
ACCESSION   WP_284671156
VERSION     WP_284671156.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..469
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=53302
     Region          5..331
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(7..8,11..12,44,47,101..102,154)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(99,102,175..181,210,236..241,270,296..300,302)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mrwacilfpq laldavlrrh pqperplvll sgppqrrllq avnpaaralg lrpgltltaa
       61 qaltrdfeqh eydpalieta eallaawgyg fssqvsrhyp rallleiqss lpllgpwprl
      121 errlrqelqg lgfrhrlala pnpvaarmlt nvadgliaap ddlprlldrl pveragfapq
      181 qaqalvrmgi rrleqlkalp raalarrfap ellqqldllg gsrslalefy rppdrfvarv
      241 elnfeveshq allfplrrlt adlavwlasr drgvqrfllw lehrqgpatt ltigllaper
      301 daallfefar grleqlqvva pvlalrlese elplfvperh glfderpaqa vgwevlrerl
      361 rarlgeeavl glgiqadhrp eralvwrhqr rletalpglr pgwllseprp ldgqprrvla
      421 gperiesgww dggdqrrdyy rievadgrqa wafrrygeea pwwiqgwfa
//
LOCUS       WP_284671158             258 aa            linear   BCT 25-DEC-2024
DEFINITION  DODA-type extradiol aromatic ring-opening family dioxygenase
            [Pseudomonas sp. HR1].
ACCESSION   WP_284671158
VERSION     WP_284671158.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Vaillancourt,F.H., Bolin,J.T. and Eltis,L.D.
  TITLE     The ins and outs of ring-cleaving dioxygenases
  JOURNAL   Crit Rev Biochem Mol Biol 41 (4), 241-267 (2006)
   PUBMED   16849108
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Siegbahn,P.E. and Haeffner,F.
  TITLE     Mechanism for catechol ring-cleavage by non-heme iron extradiol
            dioxygenases
  JOURNAL   J Am Chem Soc 126 (29), 8919-8932 (2004)
   PUBMED   15264822
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..258
                     /product="DODA-type extradiol aromatic ring-opening family
                     dioxygenase"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016701 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27995
     Region          4..255
                     /region_name="45_DOPA_Dioxygenase"
                     /note="The Class III extradiol dioxygenase, 4,5-DOPA
                     Dioxygenase, catalyzes the incorporation of both atoms of
                     molecular oxygen into 4,5-dihydroxy-phenylalanine;
                     cd07363"
                     /db_xref="CDD:153375"
     Site            order(10..12,45,109,165,219,247..248)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:153375"
     Site            order(10,45,219)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:153375"
ORIGIN      
        1 mslptlfvsh gspmealdag aagaawralg rslptpaaiv vvsahfdtri pvfgnatwpa
       61 tvhdfygfpe alyqldypap gaptlaeqla qglreqgwea etgeqgldhg awvplrylyp
      121 daqipvvpls msaargpdyh falgralarv lpadtlligs gslthnlgdf rrggaespgy
      181 vrdfqhwiqs rlrerdlnal ldyrrqapqa rqahptdehl lplfvalgaa dpegtfsvhh
      241 dgiahrilam dlygfsrh
//
LOCUS       WP_284671163             478 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Pseudomonas sp.
            HR1].
ACCESSION   WP_284671163
VERSION     WP_284671163.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..478
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51798
     Region          19..474
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 msrtppglpg ledyadirqr airslfeiie qtsngtvivd rearivwinq ryaqhfglpd
       61 aaaaigqpve qiiphsllre varngqpill dmletrngpl vvmrlpihtd egeligaigf
      121 alfdqlqqla plvtrylriq eelattrrsl qhartakygf ghfvgsgpvs levkrrarra
      181 aaseaavlll getgtgkell ahaihgaspr agrpfvsina aaipesllea effgtapgaf
      241 tgaerrarpg klqiaqggtl fldeigdmpl alqakllrvl qekeyeplgs nevlacdvrm
      301 iaatsrdlet avaegrfrad lyyrlnvlpi ripplrerld dlallaeail dglpqvggqs
      361 tpdltadgla llqrqpwpgn vrelrnvler avllgddsql daaalaealg vsaelpakpv
      421 tsatgetyae arqrfdrelf qatlaacggk vdeaarrlgl grstlykklv alglmsri
//
LOCUS       WP_284671217             397 aa            linear   BCT 25-DEC-2024
DEFINITION  cytochrome b [Pseudomonas sp. HR1].
ACCESSION   WP_284671217
VERSION     WP_284671217.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Tolkatchev,D., Yu,L. and Yu,C.A.
  TITLE     Potential induced redox reactions in mitochondrial and bacterial
            cytochrome b-c1 complexes
  JOURNAL   J Biol Chem 271 (21), 12356-12363 (1996)
   PUBMED   8647838
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Howell,N.
  TITLE     Evolutionary conservation of protein regions in the protonmotive
            cytochrome b and their possible roles in redox catalysis
  JOURNAL   J Mol Evol 29 (2), 157-169 (1989)
   PUBMED   2509716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..397
                     /product="cytochrome b"
                     /GO_function="GO:0008121 - ubiquinol-cytochrome-c
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=43458
     Region          7..390
                     /region_name="QcrB/PetB"
                     /note="Cytochrome b subunit of the bc complex [Energy
                     production and conversion]; COG1290"
                     /db_xref="CDD:440901"
ORIGIN      
        1 mrdrepgwle rrlpigafwr rhlsdyrvpr nlnvfylfgs lllfilalqv ltglwllfgy
       61 eptvkgafas vqlfmrevpf gwlirylhav gasalfvcly lhmlrgllyg syraprelvw
      121 sfgvllyvll laqaffgyll pwgqlsywga qvslsaveav pligptladl lrggivlsda
      181 slrrfqalhv vglpllilal vslhvvalrq tgsnnpegde rdvsgaagvp fhpyltlkdl
      241 cglavfllvf lavvllapdl gglvlepanq qpadplvtpa hiappwylap fyallravps
      301 kagglglaal aiallfvlpw ldrspvrsvr hkawparlgl ylaclafval gvlgvvaltd
      361 grlllarlaa gvyfigllgm pwysrlgrpr tpaesrs
//
LOCUS       WP_284671488             613 aa            linear   BCT 25-DEC-2024
DEFINITION  IucA/IucC family protein [Pseudomonas sp. HR1].
ACCESSION   WP_284671488
VERSION     WP_284671488.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..613
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=69155
     Region          17..607
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mtaqlslaaq pwpspadaal yrqveqrvva qllqtliyee vlkaevqpla eglaayrlag
       61 taadgtpvqy lgyapaaasf glirldpqrl vrqdaqgsra ptlhetlael lgeqsdsplw
      121 prfvqeleqt llkdlqsrrq dyrparpahe ldvdalerhf mdahgyhpcy ksrigfslae
      181 nrrygpefge siqlvwlala rerasvghsr rldfpafiaa efgverwtal aaewreqgra
      241 lddyqlipvh pwqweqhlaa lfqpelvsge llylgssrdq yaaqqsirtl anrsaperpy
      301 vklamcltnt sstrilarht vlngplitdw lqrliatdat ardldfvvlg evagvaydsr
      361 alpvsragqv ygtlgavwre sihaylrade qavpfngltq venrygqgap wpfvtawier
      421 hgldawlqql lkvtvtplmh mlhaegigme shgqnivlih rdgwplrial kdfhdgvrya
      481 erhlarpelr ptleplpash arinrnsfil tedvaavrdf tcdafffial gelavflrqh
      541 falaeaafwq atatvildyq rahpqhrery elfdvfaptf eveeltkrrl lgdgerrfka
      601 vanplhpyrs aac
//
LOCUS       WP_284671419             314 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD-dependent epimerase/dehydratase family protein
            [Pseudomonas].
ACCESSION   WP_284671419
VERSION     WP_284671419.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..314
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=34395
     Region          2..302
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrilitgase plgaglacdl ldrgqlvrvh grpgatldal vergadyhpa lldqpaqvva
       61 lcddidaiah ctdvagvpsa adldhgqvli eaalqqqvaq fvyvssarvy erggealked
      121 qvpakpasre aqrrlqlerl alaagefgpq vtvlrpaqvl gladrdwarw llerakarql
      181 grsgnglnrw dftsagnlrk alvtlllrqp aatqgkvfnl sdgqplvcwd ainfllrrfe
      241 lppvverkaf dprrlyarlr tpghesrwpd lldspftldi raaqeafgyl peasswnale
      301 eyrprapqar sgpv
//
LOCUS       WP_284671471             385 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pseudomonas sp. HR1].
ACCESSION   WP_284671471
VERSION     WP_284671471.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..385
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41465
     Region          7..374
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mnqtanradv ivvgagimgs asafflrrrg lsvlllerdq vgrfasgtnf gnvrrqgryl
       61 tqvalsnrsr glwgrlpeli gddlefipgg hlrvvydpcr iamlheyara petaaldlqv
      121 legaalhekf pylgpevvag syaphdghan prlaapafar aavregvnlq egmeitqvtk
      181 pdgdflvqaa dgrryqaprl litagawgsr lssqfgepvp iethgpqmgv teplpyafke
      241 avgvssplvs etiyfrqipr gnvifggcfr srpdldtrla raephgllnq ltqlrrlapa
      301 larvnvirtw sgvegyiadd lpimgpssqv dglyyafgfc gagfqlgpgv gdtmaeliat
      361 grtetplaaf digrfaqprs eslag
//
LOCUS       WP_284671561             391 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Pseudomonas sp. HR1].
ACCESSION   WP_284671561
VERSION     WP_284671561.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..391
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=44368
     Region          1..389
                     /region_name="CoxE2"
                     /note="Uncharacterized CoxE-like protein, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3825"
                     /db_xref="CDD:443037"
ORIGIN      
        1 mfldfftrlr aagipvslge lldlhaalda glavadpeaf yllaravlvk derffdrfdq
       61 vyagelarse rapdaqalpa dwlrlelqrr lseedrqrlq alggldelle tlrqrlaeqr
      121 erhaggnkwv gtggtspfgs ggynpfgvrv geagtrqgra akvweqrdfr nlddrapldr
      181 rnlqlalrrl rrfarqgaaa efdleetiaa taregglldv ryrperhnat kvlllldvgg
      241 smdlhvqlcs elfsacrlef rhleyyyfhn cvyervwrdn arrheeglat gellrrygad
      301 yrlvivgdas mgpyelthpg gsvehwneep galwiqrlcq hfpraawlnp yprdgwdfst
      361 sigllrelmg qrmfpltgeg lgeairslth p
//
LOCUS       WP_284671617             316 aa            linear   BCT 25-DEC-2024
DEFINITION  amidohydrolase family protein [Pseudomonas sp. HR1].
ACCESSION   WP_284671617
VERSION     WP_284671617.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..316
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35609
     Region          8..300
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 maelydgpiv dahhhfwepr rnfhpwlsgt etipfrygdy naikgdylpe hyladaaghe
       61 vvqtvyvete wdprdplget ryvhdlarrh gaphavvaqa wldaadaael laaqaaferv
      121 rsvrhkpggp arpeevgsqr tlmsderwrq gyaelqrhgl hfdlqtpwwn ldeacrlard
      181 fpatqlilnh tglpsdrsae gltawraala rlaewpnval kisglglagq pwraednawi
      241 vheaiavfga eramfasnfp vdrlcgsydt iiggfkhlva dlpitaqrql fhdtaqrlyr
      301 pvadvfrldt ylrtsa
//
LOCUS       WP_284671619             132 aa            linear   BCT 25-DEC-2024
DEFINITION  tautomerase family protein [Pseudomonas sp. HR1].
ACCESSION   WP_284671619
VERSION     WP_284671619.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..132
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=14246
     Region          2..59
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mphivlhlsg erdvalgqra aavindlvae hlgkrpelma ttvhyiaaad wflggeslat
       61 lggsafhldi sitdetntkg ekarflhevq aamakprpdv helcyvhlid araaaygfgg
      121 rsqewrhqqa gv
//
LOCUS       WP_284671649             542 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Pseudomonas sp. HR1].
ACCESSION   WP_284671649
VERSION     WP_284671649.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HR1
  ORGANISM  Pseudomonas sp. HR1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Pseudomonas sp. HR1"
                     /db_xref="taxon:1463361"
     Protein         1..542
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59739
     Region          6..368
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mssipsparl rleslalcll avplftlglw eqpfigfdgr falfaqemfr hgasafptsy
       61 gqpypdypat stllidvfaq lfgevnrlat vmptalasaa ivgllyrlla ersrawglla
      121 vlvllltngf lakarsicld qfvtlaalgc fyllwsadqr glsrrrglvf lcmaagfavr
      181 gplgliepcg vvcvywlvqg dwrrsfgygl vgavvlalcc allfglawrt ggplfvedvl
      241 rmqvsgrldd tdgagypwwy flqlglyrya pafplallal ptlrhhwrqr qaqadsrlll
      301 qlagfaaliv valsiptfkk pyyilpaipa caalgawvll qgqgalawvr rlflpllvif
      361 plvlgvlvkl rqprlqaagw wpeldlrfll gafailalfa lvaawrerga frlgmplaaa
      421 alaqwllvvl aldpmqalry dtrafvtrle slrqgepgql vffglgqdtk afrylmnldy
      481 dvplptfidi gqagqlaqvt rpayvlldad sqaalagtpl asrqpvlegr fndnrwqayy
      541 lp
//
LOCUS       WP_284671774             399 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Morganella morganii].
ACCESSION   WP_284671774
VERSION     WP_284671774.1
KEYWORDS    RefSeq.
SOURCE      Morganella morganii (Proteus morganii)
  ORGANISM  Morganella morganii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Morganella.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Morganella morganii"
                     /db_xref="taxon:582"
     Protein         1..399
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=46079
     Region          6..395
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 magenklsdk klksmlgrsr daqvmvsdgk gmsarvsktg cvsfvyqfrl pgasknttwl
       61 tlgrypdlsl ssarkkrdec rawlaegkdp rlelsvdtre nkpvtvkdvi diwfdkyvkl
      121 krknpepiyq rinkhllski gmhplknite dtwisvfdkv setspvvaki mfqevrqain
      181 ftnakrytky ftlnnfstnn igefgnrksr flskdeirdi wflshqeinn lhiqprlcrl
      241 iiislvfgcr iseainsswd ewdfndwvwt vpernskngh kiirpvpyri rgwllalksa
      301 ssghksilgf dllqtrassm ghtlwsnlsh qekwtlhdlr rtfatytcel gvdhyvieql
      361 lghtlpgvmg iynrsqqldk klaalnlwve yldsllmki
//
LOCUS       WP_284671979             332 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Pantoea agglomerans].
ACCESSION   WP_284671979
VERSION     WP_284671979.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..332
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35223
     Region          24..328
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mikdnalrgl vlmlifllva mvlaanlgam slsvralwqa plsdliwqiw ldirlprvll
       61 avvmgmalav sgavmqgvfr npladpgllg issgaglava laiiiplalp aplalwlpmi
      121 aafigsllvt llifsfsrla rgnlsrlllv giainalcga avgvlsllsn dqqlrqlslw
      181 gmgslsqaqw pallicllli lpallllqtr arhlnllqsg eedahymgvd vkrtqhqlli
      241 lsallvgtav svsgvigfvg lvvphvmrfc lggdhrwllp gsalagaill lladtlaril
      301 vvpaempvgl ltsliggpwf lwlilrqqrg le
//
LOCUS       WP_284672033             165 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Pantoea agglomerans].
ACCESSION   WP_284672033
VERSION     WP_284672033.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..165
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18042
     Region          76..137
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 meycftlrfs lpegrapvde lletlaaagc ddaliglgmp grialeftre sdsatdvlkq
       61 aeedvlraip gatlveaapd fvgltdvaei igmtrqnmrk lmlshrppfp lpvhdgktai
      121 whladvlewl sqrgnytlpa atrelaqvtr qrnlngslqr yglqa
//
LOCUS       WP_284672044             389 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Pantoea agglomerans].
ACCESSION   WP_284672044
VERSION     WP_284672044.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..389
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=44754
     Region          2..381
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 malsdtklrs ingkayngpa eltdgdglsv ritpsgtitf qhryrwngkp vrltvgryps
       61 tslkdariav gemrglytkg inpktyfags tgeltlkecl dnwwekyvkd lkhntqvlyk
      121 svvyntmyne fedvpvanip vsawvqffdk qeklnkkkar vlllqlrsvi hwcisrqlip
      181 sceitklsvk nigkkpdvgd rvltyselak vwlalenski vtsnrllhqm lllwgarlse
      241 lrlanaaefn ttdwiwttps ehskmgniir rpifeqmkpm verllnngnk ilfpgqeldk
      301 aidrsssnly mrklresidi pewrthdfrr slvtnlsseg imphvtekml ghelggvmav
      361 ynkhdwledq rkayelyadk ifwhvkqlg
//
LOCUS       WP_284672235             473 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Pantoea agglomerans].
ACCESSION   WP_284672235
VERSION     WP_284672235.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..473
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=51315
     Region          175..395
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mdanryalet ipsppafpga aspvmsdetl hrrlaaiier mqqqqiaqli iyadkehgsn
       61 feylagfipr feeallvvtq qgeltyimgn enlklvpfar npgrclhaav fslpnqpmrg
      121 eqpldqllte agivagertg lvgwklftgr qqgmfdlpqf iyaaaaqaag gdaqlvnatg
      181 lfispdngar cvngadevaf yeaganlast amlaaldsva pgvtekalga rlnaegqpnt
      241 vvtiaatgdr faqarlypsd kriatgdkls lttgykgglt srsayvvsda selqcnvsdw
      301 lirlaipyyh amvswleqlr igitggelys lietvlpkaq ygwhlnpghl vadeewlssp
      361 iypdsavtlk sgmllqidii psvpgyggcs iedtvglada alrhelacrf pdlwqrmtqr
      421 kayltdvlri elaeevills ntvgylrpfl ldkrralvrq qglnrpdaag nnl
//
LOCUS       WP_284672419             411 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal-phosphate-dependent aminotransferase family protein
            [Pantoea agglomerans].
ACCESSION   WP_284672419
VERSION     WP_284672419.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Koper,K., Han,S.W., Kothadia,R., Salamon,H., Yoshikuni,Y. and
            Maeda,H.A.
  TITLE     Multisubstrate specificity shaped the complex evolution of the
            aminotransferase family across the tree of life
  JOURNAL   Proc Natl Acad Sci U S A 121 (26), e2405524121 (2024)
   PUBMED   38885378
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Koper,K., Han,S.W., Pastor,D.C., Yoshikuni,Y. and Maeda,H.A.
  TITLE     Evolutionary origin and functional diversification of
            aminotransferases
  JOURNAL   J Biol Chem 298 (8), 102122 (2022)
   PUBMED   35697072
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..411
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=45270
     Region          14..409
                     /region_name="PucG"
                     /note="Archaeal aspartate aminotransferase or a related
                     aminotransferase, includes purine catabolism protein PucG
                     [Amino acid transport and metabolism, Nucleotide transport
                     and metabolism]; COG0075"
                     /db_xref="CDD:439845"
ORIGIN      
        1 mdinhypqln ppqrllmgpg pinadprvlr amssqllgqy dpamthymne vmalyrgvfr
       61 tenrwtllid gtsragiesi llssirpgdk vlvpvfgrfg hllceiarrc raevhtievp
      121 wgevftpdqi edaikkvrpr llltvqgdts ttmlqpleql gaickqygvl fytdatasla
      181 gnaletdawg ldavsagmqk clggpsgtsp itlsaemeav irkrkcveqg irteahqdge
      241 eemiysnyfd lgmimdywgp erlnhhteat salfgarecg rlilqegldn giarhklhge
      301 allkgiqgme letfgdlkhk mnnvlgvmip sgvngdqvrk lmledfgiei gtsfgplhgk
      361 vwrigtmgyn arkdcvmqtl saletvltyv gyrtpqgaaa qaawdhygsh a
//
LOCUS       WP_284672614             368 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Pantoea agglomerans].
ACCESSION   WP_284672614
VERSION     WP_284672614.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..368
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=41995
     Region          <39..340
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mtpdltqipa rsahvgrhvl iwleqvkkas lseldnfgde gtveqvmkvw vklsllisrr
       61 rpeiaissll khvlpnigsq plktlnrlrl nrlyniliad skkeearrvf altkqflawa
      121 emqgyldhsp iasmkkrdva gratpprsrq ltdaeiwvfw hgldnwalse qarwalrlcl
      181 vsarrpdeiv qaqkaefdlq lglwmqgtrn ksqrehvlpi splmrqciea llraadpasp
      241 wlvpaprdpq qplskgalnq alrrmirapr glgleaftpr dlrrtarskl saldtpndva
      301 rkimnhaleg idrvydthdy lsqmrsamsi fsdaveqiie yesyhllrhr ydgetltldd
      361 lslmamsr
//
LOCUS       WP_284672684             147 aa            linear   BCT 25-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Pantoea agglomerans].
ACCESSION   WP_284672684
VERSION     WP_284672684.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Schwartz,C.J., Giel,J.L., Patschkowski,T., Luther,C., Ruzicka,F.J.,
            Beinert,H. and Kiley,P.J.
  TITLE     IscR, an Fe-S cluster-containing transcription factor, represses
            expression of Escherichia coli genes encoding Fe-S cluster assembly
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 98 (26), 14895-14900 (2001)
   PUBMED   11742080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..147
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=16057
     Region          2..138
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mkrdsrlssa lhallhmaeh dgpvtsqnla rclrtnpvvv rrtmgylrea givtsdrgha
       61 ggwriaadlg svtlrqlhet lgepttfaig srnetpecli eqsvnaaleg tlaeaealll
      121 rrfseitiad laadfarrye avrhkkd
//
LOCUS       WP_284672742             352 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Pantoea agglomerans].
ACCESSION   WP_284672742
VERSION     WP_284672742.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..352
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=37272
     Region          9..350
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mnnilcqtln lrypiiqapm agvstpelaa avsnagalgs vsvgastpdq aegmitrals
       61 ltdgplnvnv fchapvernh elerawisrf sevferyead ipaelieiyq sfhnneemma
      121 llldmapavv sfhfglpsea flqrlksrgi vtlasatcvr ealaieaagi dyivaqgiea
      181 gghrgifsie geddqlstft lvqaikkvtr lpvisaggim dgagigamlr lgatgvqmgt
      241 afilcpessa nttyrvalks ekaastvmts aisgrparci tndfchltrq fsqdcippyp
      301 ltyylgkala vaaaakgahg fgaqwagqga slarelpage lirtlvtewq ng
//
LOCUS       WP_284672968             288 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Moraxella haemolytica].
ACCESSION   WP_284672968
VERSION     WP_284672968.1
KEYWORDS    RefSeq.
SOURCE      Moraxella haemolytica
  ORGANISM  Moraxella haemolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Moraxella haemolytica"
                     /db_xref="taxon:2904119"
     Protein         1..288
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=33035
     Region          2..>278
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 maltdtkikk lvptqksidt kvpdkysdmn glqlwvrytg vkswviayry qgkqanqsig
       61 qypqislaqa reelaelkrl laqgidpkeh akqakavqvd tcfdvfaqkw lehhetrtkp
      121 htfkrdksay hnhiypiign kdiyalrlpd imavhdrlav vgktstahrv igwitaiydy
      181 aiekglaenl ynpiprnigk slcehktkhy prikitelpq lladidssns elltkygfyv
      241 mcytfvrtke lrgmrwqeld fennlwhipa drmknglpph ctacptsg
//
LOCUS       WP_284673359             372 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Moraxella haemolytica].
ACCESSION   WP_284673359
VERSION     WP_284673359.1
KEYWORDS    RefSeq.
SOURCE      Moraxella haemolytica
  ORGANISM  Moraxella haemolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Moraxella haemolytica"
                     /db_xref="taxon:2904119"
     Protein         1..372
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=42071
     Region          1..370
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mltdnkikgl kptekrysls ageglsidvm ptgrkswvle ytalgkrkrk klgeypatsl
       61 kkarelanqi kgnagltpit vselihewie lyskqwtsek ykytviyrlt yitndfkdma
      121 vadvsramvs kavsqmvaqg tyetakrslr llsqvfnyai aheyaqnnpc tlvdniipth
      181 tvqnmatlsa demagfwhti rktptiglap valslanyla vrpselckat wdefdldkgv
      241 wiipayrmkt rlehavplas qplkilkely ssrlddgfvf khhsnpakpm piesvlavik
      301 ragfggrmtt hgfrslfstv andsglwrad vierqlahtk kdvrhvynra eywdervglm
      361 swwadivadw qa
//
LOCUS       WP_284673370             231 aa            linear   BCT 25-DEC-2024
DEFINITION  XRE family transcriptional regulator [Moraxella haemolytica].
ACCESSION   WP_284673370
VERSION     WP_284673370.1
KEYWORDS    RefSeq.
SOURCE      Moraxella haemolytica
  ORGANISM  Moraxella haemolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Moraxella haemolytica"
                     /db_xref="taxon:2904119"
     Protein         1..231
                     /product="XRE family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=25792
     Region          1..72
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          100..227
                     /region_name="COG2932"
                     /note="Phage repressor protein C, contains Cro/C1-type HTH
                     and peptisase s24 domains [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442176"
ORIGIN      
        1 melkdrlkaa rkaakltqae vaekvadltq saysqlesgk tkstnaifel anilqvnpkw
       61 latgegemkt pqhhvdelva smpngithde vepwreqlwv nfydvsfccg dgggypefep
      121 lkktlpfdqs ffkyrnlnsk yfkmiyakgd smahyiqegd avgidvsdie pregevyalf
      181 wdgdllikri ykegggvlrl ssdnpaypak ivnetngesl viigrvvyrs g
//
LOCUS       WP_284673488             380 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Moraxella haemolytica].
ACCESSION   WP_284673488
VERSION     WP_284673488.1
KEYWORDS    RefSeq.
SOURCE      Moraxella haemolytica
  ORGANISM  Moraxella haemolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Moraxella haemolytica"
                     /db_xref="taxon:2904119"
     Protein         1..380
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42836
     Region          8..376
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mnhkftpyhq liaslhakds irsfrpqtal inlssndylg lindqalkde flhtyqhctd
       61 frfgssssrl ltgnfnaheq leatlskayk revlifnsgy hmnigimpal cdqqtlilad
      121 kwvhasmidg irlakergtk syryrhqdfc qlnalldkhh ahyrhiiimt esvfsmdgdv
      181 tdltalaalk qaypnvslyv deahgvgafg ryglgvaeqm gvmneidflv gtfgkafasi
      241 ggflvcdevi kqvlintmrp vifstnlppi nalwsdfifq kssslhkkrq elldnakyfi
      301 qrlkelgyqc psdshiipii igdnnqtval adkfrshgfy vlpirpptvp vgtsrlrvcl
      361 taditrrqid dflhvlgsfq
//
LOCUS       WP_284673516             264 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: prepilin peptidase [Moraxella].
ACCESSION   WP_284673516
VERSION     WP_284673516.1
KEYWORDS    RefSeq.
SOURCE      Moraxella
  ORGANISM  Moraxella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Moraxella"
                     /db_xref="taxon:475"
     Protein         1..264
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28931
     Region          <89..262
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mdnikallst llahqptlai lvgviglvmg rfiniiahrt pmtmmnqwwh evmafiqhdd
       61 riddttkarl dslhlhshra dspthsnhli taitallsmm iahhfgantq mllalvfvwy
      121 lvalscidwq vrllpdrlla plgmigllan taalfttpvl siwglvvgfv vfwgvnvlcr
      181 wfihqdglgl gdakllgvlg awlgvsaipi ivliasllgv mvgvmgrvfg grhdstlafg
      241 pylaigglia mlfgeqfwaw ylmv
//
LOCUS       WP_284673790             349 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: Bug family tripartite tricarboxylate transporter
            substrate binding protein [Moraxella].
ACCESSION   WP_284673790
VERSION     WP_284673790.1
KEYWORDS    RefSeq.
SOURCE      Moraxella
  ORGANISM  Moraxella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Moraxella"
                     /db_xref="taxon:475"
     Protein         1..349
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=37161
     Region          1..341
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mklfkhgait lsilalaacg gdkketaqat daaagtevvt qapkrpecia pakpgggfdl
       61 tcklaqsglq dlelidkpmr vtympggvga vaynkivand rkngdaivaf stgsilnlsq
      121 gkfgqftekd vrwlaavgtd ygmvavnads pyknladlvd alkkdsksvt fgaggsvggq
      181 dwmqtallak aaginpdamg yvamegggea vtavlgnhiq vvsaglaevm phvkagklrv
      241 lavfaperle gegfkdipta keqgfdiqwp virgyymape asdasynwwk gqfdkmladp
      301 kfaelrtnre lfpfamtgde ltqyiydetq klhalsnefn lvktaeqak
//
LOCUS       WP_284673944             201 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Moraxella haemolytica].
ACCESSION   WP_284673944
VERSION     WP_284673944.1
KEYWORDS    RefSeq.
SOURCE      Moraxella haemolytica
  ORGANISM  Moraxella haemolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Moraxella haemolytica"
                     /db_xref="taxon:2904119"
     Protein         1..201
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=21992
     Region          1..190
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mrvilastsp rrqellrvag vdfdimnapi descydnera tdyamrmvha kadraielmg
       61 ddealiitad tigvledgqv ltkptdkdda famwaklsga theiwtavcv sgiqggrlta
      121 rqsmicrtqv hfvklsnqmm vrywqtgepa dkagayaiqg gamawvkein gsytnvvglp
      181 laqtlelmtq vvdmmktdca n
//
LOCUS       WP_284674048             500 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alanine/glycine:cation symporter family protein
            [Moraxella].
ACCESSION   WP_284674048
VERSION     WP_284674048.1
KEYWORDS    RefSeq.
SOURCE      Moraxella
  ORGANISM  Moraxella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Moraxella"
                     /db_xref="taxon:475"
     Protein         1..500
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=53613
     Region          16..477
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mydnpfscta qptfveglhc vvnafsaplw dvllwlliia glfftvmsgf aqfrlfgrsv
       61 ktmlgsrtgh derqgisafq afatglasrv gvgniagval aigiggagav fwmwlialig
      121 mcsalaessl aqlfkikdea tgrfrggpay yieqglgqkw lglvfalali vcfgfvyqsi
      181 qsntitlsiq savgctaqdd acqsdwqiyk hiigavlvil aapiifggik rvskiaeviv
      241 pvmatiyllv sayvilmnig dlpgvitlif skafafeaag ggllgsmvsm ammqgikrgl
      301 ysneagqgsa pnaaaaasvk hpveqgtiqm lgvfvdtliv csctafvill atmpenaadl
      361 sgvqltqaal eshvgswgqy flvvilfmfa fstiignyay aesnmqflkn npavltlfrl
      421 lvlgfvyfga vtkvavvwdm gdltmgimaf inliaillls ryvfllvkdy tkqikagvae
      481 pefkldnype lkakiksdiw
//
LOCUS       WP_284674415             428 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC1 kinase family protein [Moraxella haemolytica].
ACCESSION   WP_284674415
VERSION     WP_284674415.1
KEYWORDS    RefSeq.
SOURCE      Moraxella haemolytica
  ORGANISM  Moraxella haemolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Moraxella haemolytica"
                     /db_xref="taxon:2904119"
     Protein         1..428
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0004672 - protein kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=47394
     Region          50..418
                     /region_name="AarF"
                     /note="Predicted protein kinase regulating ubiquinone
                     biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport
                     and metabolism, Signal transduction mechanisms]; COG0661"
                     /db_xref="CDD:440425"
ORIGIN      
        1 mpiktsplai ikqsastgln vlgriqktas vaglsalrva kgekmdanll kdafeqmgvt
       61 yiklgqfias tpsifpreyv lafqdcldqt tpvplteila ilreelgttc dldeifeyid
      121 pnplasasia qvhravltdg rqvalkvqkp kvgtiihtdl tvlhggfwvi ekmmpvmrta
      181 niapildeir krmlmeidfi aesrhierfl aflsrtgnak vtaptvhhhl strrvltmdl
      241 lvgkslvdet lglakdttka qkvmsdvldt wflslmttge fhadlhagnl mmlddgriaf
      301 ldfglvgqie pksleacftl vqnlqasdyh gmaqamaqig mthqkvdvtk lgedlhrmlg
      361 kvgqdnqpea lntmmlemad igkkhgihfp qdfalllkql lyfdrfmvtl apemelfege
      421 rlkvisan
//
LOCUS       WP_284676270             305 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: EamA family transporter [Bacillus amyloliquefaciens
            group].
ACCESSION   WP_284676270
VERSION     WP_284676270.1
KEYWORDS    RefSeq.
SOURCE      Bacillus amyloliquefaciens group
  ORGANISM  Bacillus amyloliquefaciens group
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Bacillus amyloliquefaciens group"
                     /db_xref="taxon:1938374"
     Protein         1..305
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33386
     Region          13..290
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 msilekhaal sysrttgiwl vltgailwgv sgtvaqylfq hrhfntewlt svrllvsgal
       61 llgiayrkek griwavwkdr rdriplllfg ifgmlgvqyt yfaaiehgna atatvlqylg
      121 paiitcflai rakripsgke lfavllavag tfilvthgnv gslsisglav fwgissafal
      181 afytlqphrl lkkwgsaivv gwgmliggaa lslirppwtf egewsfpaya aivfiiifgt
      241 liafycyles lkylsasets llacaeplsa afltviwlhv pfgisewlgt llilttiall
      301 sikkk
//
LOCUS       WP_284676321             253 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Escherichia coli].
ACCESSION   WP_284676321
VERSION     WP_284676321.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..253
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28722
     Region          6..250
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 miehipqwmm llfvffyasv itsflclavd rlphqlkwre epdenltiys ppshcneckt
       61 kirwwglipi igyllckgkc lncnvkipiv yplselccsl tcviifwkiq dfqtslilcs
      121 iflclfflsf idireqwlpa cvtiplfwsg lvfsyfaepe skilgactgf fimylsmkiv
      181 shmkkddvva ggdialscaa gawlgvdeim ifllissvif llysipyrfk gtvfvpmgpa
      241 lsagfficll rvi
//
LOCUS       WP_284676424              73 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein, partial [Enterococcus faecium].
ACCESSION   WP_284676424
VERSION     WP_284676424.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 73)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 73)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         <1..73
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
     Region          <1..70
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 ldgdnvivrk qetaqngdiv iamtaedeat ckrfykeknf frlqpendll epiildqvsi
       61 lgrvvglyrs hiy
//
LOCUS       WP_284676535             180 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase [Vibrio sinus].
ACCESSION   WP_284676535
VERSION     WP_284676535.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sinus
  ORGANISM  Vibrio sinus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Vibrio sinus"
                     /db_xref="taxon:2946865"
     Protein         1..180
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=19657
     Region          42..179
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mvdkmsemyr kvckvlyflv anrlphsgsf gggvskrmrq flikrfvtfc genvnpepna
       61 ifsrnlsigr nsgigpnsrv ygdisigedv mmgpdvvilt khyetkdvtr smmfqgfkee
      121 rpvvikddvw igtraiimpg vtigrgsivg agavvtkdvp eysivggvpa kvigdrrtea
//
LOCUS       WP_284676553             287 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Vibrio sinus].
ACCESSION   WP_284676553
VERSION     WP_284676553.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sinus
  ORGANISM  Vibrio sinus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Vibrio sinus"
                     /db_xref="taxon:2946865"
     Protein         1..287
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=33702
     Region          21..287
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mgrvlaqeqe misdsnveef eltakdfkyi qwfmhksvgi flgdrkramv ygrvsrqlrr
       61 lklrrfseyk eliendener mlfinslttn ktdffreyhh fefiekvlkq ewreggeshl
      121 riwsagcstg qepyslissl yvsgilesce disllasdld ttvlqtaktg vysdesveti
      181 pdmylrkcfv rgkkqqqgki kikkglqqfi efkqinllde wpmdvkfnli scrnvmiyfd
      241 rptqehlirr fhqylkpngi lflghsesvg scadifhhlg htiyvkq
//
LOCUS       WP_284676642             423 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Vibrio sinus].
ACCESSION   WP_284676642
VERSION     WP_284676642.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sinus
  ORGANISM  Vibrio sinus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Vibrio sinus"
                     /db_xref="taxon:2946865"
     Protein         1..423
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=48399
     Region          31..414
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
ORIGIN      
        1 mtqndllnit yanldlarse mtkilvdrqp gyslprplyt dpylfridve eifqkewlfv
       61 gmtseipskg dyftveiaqn pvlivrdadg svnafhntcr hrgsriclea rgkvanlvcp
      121 yhqwtyntkg nllyagtemg egfnlsehrl hdvhcktagg fificlgdtp pdsdfdefls
      181 tldeymapyd vektklaaes tmhekanwkl viennrecyh cagshpelln tllewddttd
      241 prasaeflay ckrmaaewea eaiphahknf gqrnrlvrmp lkegtqvmti dgsqgcskll
      301 griknrqlgs lrilhlpnsw nhmqsdhfiv frvlpisaqe slvttkwfvh kdavegvdyd
      361 pdrlrqvwda tndqdrilge enqrginsls yqpgpyskty eyavldflnw ysdrvldnln
      421 tss
//
LOCUS       WP_284677917             286 aa            linear   BCT 25-DEC-2024
DEFINITION  TRM11 family SAM-dependent methyltransferase [Frankia sp.
            AgKG'84/4].
ACCESSION   WP_284677917
VERSION     WP_284677917.1
KEYWORDS    RefSeq.
SOURCE      Frankia sp. AgKG'84/4
  ORGANISM  Frankia sp. AgKG'84/4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Frankia.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Kozbial,P.Z. and Mushegian,A.R.
  TITLE     Natural history of S-adenosylmethionine-binding proteins
  JOURNAL   BMC Struct Biol 5, 19 (2005)
   PUBMED   16225687
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437146
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Frankia sp. AgKG'84/4"
                     /db_xref="taxon:573490"
     Protein         1..286
                     /product="TRM11 family SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30345
     Region          35..>201
                     /region_name="Trm11"
                     /note="tRNA G10 N-methylase Trm11 [Translation, ribosomal
                     structure and biogenesis]; COG1041"
                     /db_xref="CDD:440663"
ORIGIN      
        1 msstsprray slipagqqhp rvqrtgrytp tstqhparml palaahliaa ysnpgdvvld
       61 pmcgigttlv eaahlgrrsl gvdlesrwis ltranlrlaa qqgaagtgrc frgdarhleq
      121 lippayhgri gllltsppyg qathgsitla pgqgvhktdy rysdspanla ngdldglldg
      181 laavfrsahr llspggilal avrpfrhhgt lvdlpgalvd ladetglhlh artaallaai
      241 hpdgaltsra tffaqhnirv argaghplhl iahedilllr tptrpd
//
LOCUS       WP_284678168             254 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Frankia sp. AgKG'84/4].
ACCESSION   WP_284678168
VERSION     WP_284678168.1
KEYWORDS    RefSeq.
SOURCE      Frankia sp. AgKG'84/4
  ORGANISM  Frankia sp. AgKG'84/4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Frankia.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Frankia sp. AgKG'84/4"
                     /db_xref="taxon:573490"
     Protein         1..254
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26027
     Region          11..88
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 magrqaevpl lrrlvgealr rrrlaqgrtl rnvadaarvs mpylseverg lkeassevla
       61 aicralhvrl adlldevrle larvepqpaa plravaaaha iagepgdahv ivstvtarat
      121 ptarigftas vgpvasedra apvagstapf isltsavgsv dvggragmwv rlsgptdaia
      181 pidatgvspn lgssahfagt lgtgrivvpa garadshpaa rrtavrrasr pasrrgpsap
      241 rchararldt saaa
//
LOCUS       WP_284678677             776 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein, partial [Frankia sp. AgKG'84/4].
ACCESSION   WP_284678677
VERSION     WP_284678677.1
KEYWORDS    RefSeq.
SOURCE      Frankia sp. AgKG'84/4
  ORGANISM  Frankia sp. AgKG'84/4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Frankia.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 776)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Frankia sp. AgKG'84/4"
                     /db_xref="taxon:573490"
     Protein         <1..776
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
     Region          29..772
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 gdaapviprl ghespplprr vrgrlsrlst hratpssald pvlrgllanh pradisqvqr
       61 afevadaaha gqirfsghpy ithpiavasi ladlgmdtat lsaallhdtl eettltpeai
      121 retfgdqial ivdavsklnr vkvgeaaqae tirrmvvama rdpralvvkl sdrlhnmrtl
      181 rflpehkqer karetlevya plahrlgmns lkweledlsf aalypkryde ivrlvadrap
      241 srdvylaevi gqvqaglrdt riravvsgrp khyysiyqkm vvrgrsfddi ydlvgirilv
      301 dsvrdcyatl gnvhanwkpi pgrfkdyiam pkfnmyqslh ttvigpegkp velqirtham
      361 hnraeygiaa hwkykedgva arssessrsg rrknpepdlt twlrqvldwq resadpgefl
      421 dslrfaaesd evfvftpkgd viplpvgsts vdfayavhtd vghhcvgtri ngriatldtt
      481 ldngdtvevf tsrahsagps qdwlmfvrss rarakirqwh arerredaiv agrdalgram
      541 rrhglplsrl msgdallgla kdmrhadvaa lyaavgenhl saesvvsrll vslggpegae
      601 edvgetelpi rtlrrstgep gvlvtgspdv wtklarcctp mpgdeiagfv trgkgvsvhr
      661 tdcsnlgglr ggphdrlvav ewapssgsmf laviqveaqd rtkllsdvtr vlsdrhvnil
      721 sasvatsrda strepvaisr ftfemgdakh lghilsavrs ldgvydcfrv tsgvqv
//
LOCUS       WP_284678805             288 aa            linear   BCT 25-DEC-2024
DEFINITION  LysR family transcriptional regulator [Frankia sp. AgKG'84/4].
ACCESSION   WP_284678805
VERSION     WP_284678805.1
KEYWORDS    RefSeq.
SOURCE      Frankia sp. AgKG'84/4
  ORGANISM  Frankia sp. AgKG'84/4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Frankia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Frankia sp. AgKG'84/4"
                     /db_xref="taxon:573490"
     Protein         1..288
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29864
     Region          9..280
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mvrpvpstld italrslvai adsggfrraa avlcvsqsav sqhvrrlekt igrplvapdg
       61 ratrftpdge llltaarrll dlhdgalvql gvgaparpst itvgatehaa dhllplwmaa
      121 ltagypeari qfrldrgari tealedgavd vavligaahs pacrpagalr lawyaaagwt
      181 ppppdrplpl vaindpctir rqalstlarv grtawiagea ghlagvlqat ragvgvalla
      241 dvgpvppglv rrddlpaadp eplhvragrg apprladlir davtvala
//
LOCUS       WP_284678830             258 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Frankia sp. AgKG'84/4].
ACCESSION   WP_284678830
VERSION     WP_284678830.1
KEYWORDS    RefSeq.
SOURCE      Frankia sp. AgKG'84/4
  ORGANISM  Frankia sp. AgKG'84/4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Frankia.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Frankia sp. AgKG'84/4"
                     /db_xref="taxon:573490"
     Protein         1..258
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=26336
     Region          32..248
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mttvstpalv aaacaaglvg afptsncrst teladwldei eatvaanliv hrsntrlded
       61 ldtlvrrgvr lvitsvgtpv pvigplhrag vrvfadvasl khaekaaaag adglvllaag
      121 agghtgwanp fafaravrrf hdgplvlagg isdgtalwsa itlgydlgym gtrfiataes
      181 gatdawrrav vdatldditl gtapngvtvs llpgaagsag htaagvhait taaevidttr
      241 rewndarart rrllaata
//
LOCUS       WP_284678911             319 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-binding oxidoreductase, partial [Frankia sp. AgKG'84/4].
ACCESSION   WP_284678911
VERSION     WP_284678911.1
KEYWORDS    RefSeq.
SOURCE      Frankia sp. AgKG'84/4
  ORGANISM  Frankia sp. AgKG'84/4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Frankia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Frankia sp. AgKG'84/4"
                     /db_xref="taxon:573490"
     Protein         1..>319
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
     Region          27..>319
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mpaghvapeg vgpegvgpdg vgpdgaadpa vveafavalp vgrwstdpav vdahrldrsg
       61 wipsgrplgv afardvadvr atlrvatarr vpvtvrgagt glaggaaagq ggivldvagm
      121 nrirelsaed svavvepgvi tadldaaaqa vglsyppdpa saaistiggn iatnagglrc
      181 akygvtresv lgldvvladg emlrtgrrtv kgvagydlts lfvgsegtlg vvvaatvrlr
      241 plardpvtla affdtldaav davtalgaag vvpavaelld artvravdaa tgsdlaaqga
      301 vfllvqtdgp gaaaeadla
//
LOCUS       WP_284679075             258 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Aceticella autotrophica].
ACCESSION   WP_284679075
VERSION     WP_284679075.1
KEYWORDS    RefSeq.
SOURCE      Aceticella autotrophica
  ORGANISM  Aceticella autotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Aceticella.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Aceticella autotrophica"
                     /db_xref="taxon:2755338"
     Protein         1..258
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30324
     Region          4..256
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mltyedfvlk icqltgidls lykekqmkrr inslilnsny knyddyykal ttnknlynef
       61 inyitinvte ffrnldqwiv leneilpyli kknlkiwsaa cstgeepytl amilskhinl
      121 edvniiatdi denalakaqk giytdkslek vpaeyikkff tkvnntsyii setlrkniif
      181 kkhnlltdky penvnlvicr nvliyfndka kndtykkiyd clsndgiffv ggteqiilpy
      241 rynfepiktf fykkisnn
//
LOCUS       WP_284679098             261 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Aceticella
            autotrophica].
ACCESSION   WP_284679098
VERSION     WP_284679098.1
KEYWORDS    RefSeq.
SOURCE      Aceticella autotrophica
  ORGANISM  Aceticella autotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Aceticella.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10648172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Aceticella autotrophica"
                     /db_xref="taxon:2755338"
     Protein         1..261
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29764
     Region          13..>192
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
     Region          <140..258
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 meelqiynem lssykrcmei gikssipcpa itlkeedlqi rlnkniglin vfhncvdnil
       61 nqtkgeyifl ltdydgylln ircnkktrcc idksgfrigt sfkeeavgtn aismamklrr
      121 lvylepqhhy cdilkkwyci aapiiidemi igyldvstie hgmvnemtiv lelladkian
      181 eyktnikeqe lnngninltd nqieillmla kgykelaisi eigikpvtvk yhkrkiiekl
      241 cvtsiqeava kavklnlidi e
//
LOCUS       WP_284679194             355 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Aceticella autotrophica].
ACCESSION   WP_284679194
VERSION     WP_284679194.1
KEYWORDS    RefSeq.
SOURCE      Aceticella autotrophica
  ORGANISM  Aceticella autotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Aceticella.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Aceticella autotrophica"
                     /db_xref="taxon:2755338"
     Protein         1..355
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=40223
     Region          8..354
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mncrlnilks llkereidaf lilkpvnvty itgftgddsv aiisrdvsaf itdsryveqa
       61 qdevsgleil qykytmndai kefvdkfnik rlgfeedfit yaqysslhkk lcidlipqkn
      121 liedmrkikd dseienikka qyitdetfky flsyikigme ekyiavemey ymkklgaeek
      181 sfdfivasgk rsslphgkas nkkieygdfv ifdfgckvng ycsdmtrtiv mgkasdkqke
      241 iynivleaqm nainnlksgi kecegdnlar kiindkgygk yfghslghgv gleiheaplm
      301 gtlgqnilqp nmvvtvepgi yiydfggvri edmvllkegg vidltnspkh lievn
//
LOCUS       WP_284679329             159 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Aceticella autotrophica].
ACCESSION   WP_284679329
VERSION     WP_284679329.1
KEYWORDS    RefSeq.
SOURCE      Aceticella autotrophica
  ORGANISM  Aceticella autotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Aceticella.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Aceticella autotrophica"
                     /db_xref="taxon:2755338"
     Protein         1..159
                     /product="YceD family protein"
                     /calculated_mol_wt=18357
     Region          1..157
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mkidlskikg hkcrnididy eenldmiean nntykldgpi hvsgnitsnl edvflklfik
       61 gklivqcdrc lenfiykfdi sleeslssfd knyfednlqd klnlskaike simlslpmkf
      121 vcseeckgly yhcennqshe scncqhidpr lealkklsh
//
LOCUS       WP_284679551             334 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Aceticella autotrophica].
ACCESSION   WP_284679551
VERSION     WP_284679551.1
KEYWORDS    RefSeq.
SOURCE      Aceticella autotrophica
  ORGANISM  Aceticella autotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Aceticella.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Aceticella autotrophica"
                     /db_xref="taxon:2755338"
     Protein         1..334
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=36528
     Region          13..314
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 meslkklaia fqallvvivi giigfmylek fnflqaawlt ittiftlgyg niipktvagl
       61 yfnifliiig vglaaytlse fvgvivegkl qdvlgrremy kkiiqlndhv iicgagrige
      121 nvierlkkek vpflvidkde kivqklsddg vlviqgdate dsvleqagir kakglitala
      181 tdadnvfvtl takginpdll vvaraiqkes qgkliragad kvisptmigg mrmaaavikp
      241 fiaefidtil yenemplaie eikvnfpsei igrelknsgi kektgclima ikrgkeilhn
      301 pnsneiileg dlliaigste qlekleklvl ltri
//
LOCUS       WP_284679598             298 aa            linear   BCT 25-DEC-2024
DEFINITION  TolB family protein [Aceticella autotrophica].
ACCESSION   WP_284679598
VERSION     WP_284679598.1
KEYWORDS    RefSeq.
SOURCE      Aceticella autotrophica
  ORGANISM  Aceticella autotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Aceticella.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Aceticella autotrophica"
                     /db_xref="taxon:2755338"
     Protein         1..298
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=33432
     Region          51..196
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 mikkfliifl iflfvfiinf htyeaktyvn stdvvygnis kvfylagfpg diklkdfttg
       61 kvatlikgdg gnfdvsrdgr rivyassktg awqiyiadvn rdklsnirml sdgisrsedp
      121 rlswdgskvv ykrngdivvc aldgsiirei tntsdteewa pnfapdgria ftrgigdkcq
      181 ivvwddgreq tvapgwypaf gedgslyfvg rfndneddiy rilpnstyke llplnapgvs
      241 dadphwvlgt nkymtfnser gnderryegy iadittnris kiasdvlpvl npiviikn
//
LOCUS       WP_284679727             147 aa            linear   BCT 25-DEC-2024
DEFINITION  deoxycytidylate deaminase [Aceticella autotrophica].
ACCESSION   WP_284679727
VERSION     WP_284679727.1
KEYWORDS    RefSeq.
SOURCE      Aceticella autotrophica
  ORGANISM  Aceticella autotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Aceticella.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Maley,F. and Maley,G.F.
  TITLE     A tale of two enzymes, deoxycytidylate deaminase and thymidylate
            synthase
  JOURNAL   Prog Nucleic Acid Res Mol Biol 39, 49-80 (1990)
   PUBMED   2247612
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788416
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Aceticella autotrophica"
                     /db_xref="taxon:2755338"
     Protein         1..147
                     /product="deoxycytidylate deaminase"
                     /EC_number="3.5.4.12"
                     /GO_function="GO:0004132 - dCMP deaminase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006220 - pyrimidine nucleotide metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0009972 - cytidine deamination [Evidence
                     IEA]"
                     /calculated_mol_wt=16338
     Region          1..147
                     /region_name="ComEB"
                     /note="Deoxycytidylate deaminase [Nucleotide transport and
                     metabolism]; COG2131"
                     /db_xref="CDD:441734"
ORIGIN      
        1 mrpswdeyfm qivdivkmrs tclrkhvgav ivkdmhiist gyngapsglk hceetgcmre
       61 klkipsgerh elcrgihaeq naiiqaalng vstkdatiyv nvcpcslcak mlinagikri
      121 vyqegypdel smefikeagl divkier
//
LOCUS       WP_284679754             363 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal-phosphate-dependent aminotransferase family protein
            [Aceticella autotrophica].
ACCESSION   WP_284679754
VERSION     WP_284679754.1
KEYWORDS    RefSeq.
SOURCE      Aceticella autotrophica
  ORGANISM  Aceticella autotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Aceticella.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Koper,K., Han,S.W., Kothadia,R., Salamon,H., Yoshikuni,Y. and
            Maeda,H.A.
  TITLE     Multisubstrate specificity shaped the complex evolution of the
            aminotransferase family across the tree of life
  JOURNAL   Proc Natl Acad Sci U S A 121 (26), e2405524121 (2024)
   PUBMED   38885378
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Koper,K., Han,S.W., Pastor,D.C., Yoshikuni,Y. and Maeda,H.A.
  TITLE     Evolutionary origin and functional diversification of
            aminotransferases
  JOURNAL   J Biol Chem 298 (8), 102122 (2022)
   PUBMED   35697072
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Aceticella autotrophica"
                     /db_xref="taxon:2755338"
     Protein         1..363
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40136
     Region          4..361
                     /region_name="PucG"
                     /note="Archaeal aspartate aminotransferase or a related
                     aminotransferase, includes purine catabolism protein PucG
                     [Amino acid transport and metabolism, Nucleotide transport
                     and metabolism]; COG0075"
                     /db_xref="CDD:439845"
ORIGIN      
        1 mnkkilmtpg ptmvpeevle ingrqpmhhr tqefyelfsg lnlnlkkifk tkmevmtlta
       61 sgtgameasv anlfskgdkv lfatighfge rfydiakiyg ldaelldfgw gnavdlnvle
      121 dklkdgdyka lfitqnetst gvtndikaaa etagkysipv ivdavsslgg iplemdkwgv
      181 dvvitcsqkc fmsppglsfi slserawgma ekstlpkyyf dlkkarkgvm kekpdtpytp
      241 avstimaakr atdmllslgl dnvykrqedf gkkvrdyikd iglqlfpeec iasnlisaik
      301 vpedisasdi inyilekhni litggqgrlk gkiirighmg yvteemlekt lnalkeavlk
      361 lkk
//
LOCUS       WP_284680169             471 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Aceticella autotrophica].
ACCESSION   WP_284680169
VERSION     WP_284680169.1
KEYWORDS    RefSeq.
SOURCE      Aceticella autotrophica
  ORGANISM  Aceticella autotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Aceticella.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Aceticella autotrophica"
                     /db_xref="taxon:2755338"
     Protein         1..471
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=53654
     Region          107..471
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 maknrlfkkl fitniliili tmiilsgffy lmfqnyyfae kekimieegq qlnmiisgft
       61 vgdvdvdkln qelsvvdrli natiwivsrd gliysqsshl eknwvgitls kdeienilkg
      121 htiikrgyfg grfsqpvltv glplkisgsi kgaifmhapi lemnktlmni ffimiismvi
      181 aifiggilis faskkisepl kemssaalkm akgdfstkiq vagddeitdl aisfnkmsre
      241 leqmedvrke fvanvshelr splttiqgyi dgiidgtipq dslikylkiv qeetrrmsrl
      301 isgllditkm esgkfplyit dfdineliri tiikmesrin ekrvhvkvdf dydknivqgd
      361 kdkieqvltn lfdnaikfse vngyihvyte rkgsklyiti hnmgeiipee diehiwdkly
      421 kvdksrsgnt gaglglyivk niinkhdeei waeskenegt titftmklkn d
//
LOCUS       WP_284680451             295 aa            linear   BCT 25-DEC-2024
DEFINITION  damage-control phosphatase ARMT1 family protein [Aceticella
            autotrophica].
ACCESSION   WP_284680451
VERSION     WP_284680451.1
KEYWORDS    RefSeq.
SOURCE      Aceticella autotrophica
  ORGANISM  Aceticella autotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Aceticella.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Huang,L., Khusnutdinova,A., Nocek,B., Brown,G., Xu,X., Cui,H.,
            Petit,P., Flick,R., Zallot,R., Balmant,K., Ziemak,M.J.,
            Shanklin,J., de Crecy-Lagard,V., Fiehn,O., Gregory,J.F. 3rd,
            Joachimiak,A., Savchenko,A., Yakunin,A.F. and Hanson,A.D.
  TITLE     A family of metal-dependent phosphatases implicated in metabolite
            damage-control
  JOURNAL   Nat Chem Biol 12 (8), 621-627 (2016)
   PUBMED   27322068
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Perry,J.J., Ballard,G.D., Albert,A.E., Dobrolecki,L.E., Malkas,L.H.
            and Hoelz,D.J.
  TITLE     Human C6orf211 encodes Armt1, a protein carboxyl methyltransferase
            that targets PCNA and is linked to the DNA damage response
  JOURNAL   Cell Rep 10 (8), 1288-1296 (2015)
   PUBMED   25732820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003977
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Aceticella autotrophica"
                     /db_xref="taxon:2755338"
     Protein         1..295
                     /product="damage-control phosphatase ARMT1 family protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33900
     Region          2..284
                     /region_name="DUF89"
                     /note="House-cleaning carbohydrate phosphatase, DUF89
                     family [Defense mechanisms]; COG1578"
                     /db_xref="CDD:441186"
ORIGIN      
        1 mninldciyc iikksdslft lfekderkkl rfmkevflvi gksnerdtsp ylsavimrll
       61 kselnlgdiy fdiknkynkl llsmeedilk hiynsedkml talkyamign fidfgamdkv
      121 disqlerlie napnqtidmk kyeefinqlk nakrlaylad nageivldki fikilkefyp
      181 aidiivivrg kpiyndatia daeeiglcdl vnvigngtdi pgtqlnelnt esreiinnad
      241 liiakgqgnf etlfpcgkni yyiflckcdl flrrfniekf kgvfanekdi kvmmk
//
LOCUS       WP_284680477             359 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Aceticella autotrophica].
ACCESSION   WP_284680477
VERSION     WP_284680477.1
KEYWORDS    RefSeq.
SOURCE      Aceticella autotrophica
  ORGANISM  Aceticella autotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Aceticella.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Aceticella autotrophica"
                     /db_xref="taxon:2755338"
     Protein         1..359
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=41079
     Region          38..156
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mnlgnaeenr lfvinnekry fataddinpn dknsslpyii naisensvvl dvgcsygylg
       61 ewltknkncq vygidideea leyvkergyy kdvfhldldy pentkdefer faklqdifdf
      121 aicadvlehl knptnaldfi ssklklggqv lisipniahm diilnllesk fnysefgild
      181 nthlrfftkk sfaewinsan efyknkgfkf dakylggtty iseflvdvkn nhaelynkil
      241 ginneleilq hifvltkvns fantyglnki intanypnaf sviassissl eneltskete
      301 inilnneias kdqsiqelns kvvsleneli svllsrswry trpirkllhk lnlnkkqrg
//
LOCUS       WP_284680680             361 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Aceticella
            autotrophica].
ACCESSION   WP_284680680
VERSION     WP_284680680.1
KEYWORDS    RefSeq.
SOURCE      Aceticella autotrophica
  ORGANISM  Aceticella autotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Aceticella.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Aceticella autotrophica"
                     /db_xref="taxon:2755338"
     Protein         1..361
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=42510
     Region          1..360
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkisqhfrie ptkeqesklf htlylcrkfy nysleqriks yqetgkglsy kkqqnmlpqy
       61 keenleykav qsqilqdvlr rlygaykkff akeagyphfk dkyhyysitl pqctakrnfk
      121 kegyvyipyi gdlkmivhrd fdpntvktin ikyhagkwya nlsieipegk tenitkyvgl
      181 dkgvkvigat sdgkifenpk wiqnaerrlk rlqrqlskkk kgsknrekqk krlqklhekv
      241 anqrkdylhk isyrltekyd aifvedlqvk nmtknhklak sianvgwgml dtfleykslk
      301 kgklfkkinp ayttqkcsrc gkivekdlsv rihkcecgle idrdinaain ilheglrqla
      361 v
//
LOCUS       WP_284680610             256 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Aceticella autotrophica].
ACCESSION   WP_284680610
VERSION     WP_284680610.1
KEYWORDS    RefSeq.
SOURCE      Aceticella autotrophica
  ORGANISM  Aceticella autotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Aceticella.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Aceticella autotrophica"
                     /db_xref="taxon:2755338"
     Protein         1..256
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29170
     Region          3..256
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 miitsdknel ikkikklnnk kdryesglff vegrnnvnev lkskfsiryi iisenynnni
       61 dfdlnriikv pdnlfkkisd tvtpqnimai vripryelnt iidknnvyii adevqnpgnl
      121 gtiirtadaf kvravftinn svdiynpkvi rsamgsifhi pvvniddide lmnrlkksci
      181 kiystdlkad qyifdfkisn nvafifgnea kgvnpmlngy idgkfkipmt gnaeslnvsi
      241 tasiclyesq rqrlik
//
LOCUS       WP_284680739              85 aa            linear   BCT 25-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Aceticella
            autotrophica].
ACCESSION   WP_284680739
VERSION     WP_284680739.1
KEYWORDS    RefSeq.
SOURCE      Aceticella autotrophica
  ORGANISM  Aceticella autotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Aceticella.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Aceticella autotrophica"
                     /db_xref="taxon:2755338"
     Protein         1..85
                     /product="type II toxin-antitoxin system RelE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0017148 - negative regulation of
                     translation [Evidence IEA]"
                     /calculated_mol_wt=9930
     Region          4..84
                     /region_name="RelE"
                     /note="mRNA-degrading endonuclease RelE, toxin component
                     of the RelBE toxin-antitoxin system [Defense mechanisms];
                     COG2026"
                     /db_xref="CDD:441629"
ORIGIN      
        1 mkktyniels kkaskfilnq sknqqkrllk aiyklpegii nplkgyepmq kirvgdyrii
       61 feinekqsli riytignrgd vykki
//
LOCUS       WP_284680830             269 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Aceticella
            autotrophica].
ACCESSION   WP_284680830
VERSION     WP_284680830.1
KEYWORDS    RefSeq.
SOURCE      Aceticella autotrophica
  ORGANISM  Aceticella autotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Aceticella.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Aceticella autotrophica"
                     /db_xref="taxon:2755338"
     Protein         1..269
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31276
     Region          1..263
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mdvgistasf ypeylteeti pfigemgint ievflesyse ygldyckrmk dtldkyniip
       61 ysvhalgsqf epqlfaater qrndakklye kvlkaanilg akvyvfhgpp inknklpvld
      121 fekigkitse lsdmagqydi rfswenvfwc wfsfpefakn lvqasnsknl yftfdikqam
      181 ksrkdpmdfl kamgnkitnv hlcdfddrgk lylpgegsfd fkvlkynldi igykgpvime
      241 vyrfnynhyk emlnsikflk nifekemdm
//
LOCUS       WP_284680834             238 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Aceticella
            autotrophica].
ACCESSION   WP_284680834
VERSION     WP_284680834.1
KEYWORDS    RefSeq.
SOURCE      Aceticella autotrophica
  ORGANISM  Aceticella autotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Aceticella.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Aceticella autotrophica"
                     /db_xref="taxon:2755338"
     Protein         1..238
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=28277
     Region          <41..172
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mikiygiklr dkikkeffdn yiiyvskekr erirrfrrld davrslmgdi ivriaicqet
       61 glknedlify knkygkpclk nncnvqfnis hsgdwiiaai hdlpigvdiq kiqpvnmdia
      121 krfftldeyk eimrkdneer lsyfyelwvl kesyikavgk gmniplnsfc fqiqenkiif
      181 ksknevkkhc fklynldkny kmavcaaind fpdhieikdl drlheelllm grnregyn
//
LOCUS       WP_284680917             370 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Aceticella autotrophica].
ACCESSION   WP_284680917
VERSION     WP_284680917.1
KEYWORDS    RefSeq.
SOURCE      Aceticella autotrophica
  ORGANISM  Aceticella autotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Aceticella.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Aceticella autotrophica"
                     /db_xref="taxon:2755338"
     Protein         1..370
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39111
     Region          48..367
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mnltknsdfi erytdaeklk giyakhtgkk isivfiilll lalavlysva vgaasisisd
       61 vikvltnkif hlkytysnsl aetivmqlrl prillavltg iglagagavm qgilhnplvs
      121 pytlgmsgaa slgaaigivl gksilgnyfg vagtyliafn afvfgfltif iiiglarmkg
      181 sspetlvlag valgyifsag vsalkyfsnn dalkdlvvwl mggmwgaswk avglltpvvl
      241 icmvillgya wdmnalsage dvatnlgvnv kklqfvclti atlaasatva ftgvigfigl
      301 vaphisrlfv gsdnrflipc sclmgalill fadtvgriii apvelpvgii tglvggpyfl
      361 ymllrkkkfy
//
LOCUS       WP_284680936             264 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Aceticella autotrophica].
ACCESSION   WP_284680936
VERSION     WP_284680936.1
KEYWORDS    RefSeq.
SOURCE      Aceticella autotrophica
  ORGANISM  Aceticella autotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Aceticella.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10106895
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Aceticella autotrophica"
                     /db_xref="taxon:2755338"
     Protein         1..264
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=29337
     Region          81..261
                     /region_name="vWA_Magnesium_chelatase"
                     /note="Magnesium chelatase: Mg-chelatase catalyses the
                     insertion of Mg into protoporphyrin IX (Proto). In
                     chlorophyll biosynthesis, insertion of Mg2+ into
                     protoporphyrin IX is catalysed by magnesium chelatase in
                     an ATP-dependent reaction. Magnesium chelatase is...;
                     cd01451"
                     /db_xref="CDD:238728"
     Site            order(88,90,92,156,188)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238728"
ORIGIN      
        1 mlskdknlrr kgsgrrsltr innrsgryvr sriqretndi afdatlraaa pyqlnrdkeg
       61 laisikdkdi rekvrekkig nfivfildas gsmnanqrik etkgaivsll ldayqkrdev
      121 amvvfkgdaa evvlpptssv elayklteel ptggktplad glnkglevik naryknpdiy
      181 pvvvlisdgr anvsigskkp ieevreiasl vkkeeiksiv idvekdnfit fglakeiadl
      241 mdakyykidn lkaetiidav kesl
//
LOCUS       WP_284680975             150 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Aceticella
            autotrophica].
ACCESSION   WP_284680975
VERSION     WP_284680975.1
KEYWORDS    RefSeq.
SOURCE      Aceticella autotrophica
  ORGANISM  Aceticella autotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Aceticella.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Aceticella autotrophica"
                     /db_xref="taxon:2755338"
     Protein         1..150
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17258
     Region          <25..143
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mklrrlvyle pqhhyydilk kwyciaapii idekiigyld vstieygmad emtivlella
       61 dkianeyktn ikeqelnngn ikltdnqiki lqmlakgyke ltisielgik pvtvkyhkrk
      121 iieklcvkti qeavakavkl nlidnlidid
//
LOCUS       WP_284681010             705 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Aceticella autotrophica].
ACCESSION   WP_284681010
VERSION     WP_284681010.1
KEYWORDS    RefSeq.
SOURCE      Aceticella autotrophica
  ORGANISM  Aceticella autotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Aceticella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Aceticella autotrophica"
                     /db_xref="taxon:2755338"
     Protein         1..705
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=78104
     Region          10..150
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <243..702
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 mkskrediyk neiigiifcv iailsilsly tkstgilgyn isillkglfg igayvvslli
       61 lvfaflflfk ksdflktkkv islliiflcf isidhlyyfn nvisirdyia eaykngikni
      121 gggmiasiil yvllkligii gtllflsasl iicsiiitdi sfvnsikmll aliknkinnk
      181 kiivddfekt iaevtitken qdcndleenn ieivqpilee kvksnnqkpd mvpanknngn
      241 ynfppltllk dgnqrqkinn niiienvkkl eqtllnfgie akviqvtrgp aitrfelqpn
      301 pgikvsrivs ltddislsla apsvrieapi pgksaiglev pndkisivtl kevidtnkfk
      361 nhksdlsial gkdiagnviv tdlakmphll iagatgsgks vcintliisl lykalpdkvk
      421 milidpkvve lniyngiphl ltpvvtdpkk aagvlnwavq emtnrykmfa dinvrdiegy
      481 nrinkenhms kiviiidels dlmmvspsev eeyicrlaqm araagiylvi atqrpsvdvi
      541 tgvikanips risfavtsqi dsrtildmag aekllgkgdm lfypigeakp lrvqgafisd
      601 kevedvvnfl klqaqpeyte invetkfeti ksigedelik daiavildtg qasismlqrr
      661 lrigyaraar iidqmeekgi isgydgskpr qilltedeik kiind
//
LOCUS       WP_284681150              66 aa            linear   BCT 25-DEC-2024
DEFINITION  cbb3-type cytochrome oxidase subunit 3 [Pseudomonas hormoni].
ACCESSION   WP_284681150
VERSION     WP_284681150.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas hormoni
  ORGANISM  Pseudomonas hormoni
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008800
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Pseudomonas hormoni"
                     /db_xref="taxon:3093767"
     Protein         1..66
                     /product="cbb3-type cytochrome oxidase subunit 3"
                     /calculated_mol_wt=7117
     Region          1..50
                     /region_name="CcoQ"
                     /note="Cbb3-type cytochrome oxidase, subunit 3 [Energy
                     production and conversion]; COG4736"
                     /db_xref="CDD:443770"
ORIGIN      
        1 masemssgmi rglgtvvvfv afvgltlwvf nskrnpefae arllpfadep laddatqepe
       61 trstrs
//
LOCUS       WP_284681304             148 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Sphaerisporangium fuscum].
ACCESSION   WP_284681304
VERSION     WP_284681304.1
KEYWORDS    RefSeq.
SOURCE      Sphaerisporangium fuscum
  ORGANISM  Sphaerisporangium fuscum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Sphaerisporangium.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Sphaerisporangium fuscum"
                     /db_xref="taxon:2835868"
     Protein         1..148
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15977
     Region          5..145
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtgnttppag daaaiadelq mvvgalvrrm ravspgrevt lsqvsilkrl dregahtvad
       61 larldkithq svtvsvaglv erglvhrvpd rsdrrrkllv itdegrrlla errdaghenl
      121 teaiaarlta aeqarlsgal vllrrlld
//
LOCUS       WP_284681496             104 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Sphaerisporangium
            fuscum].
ACCESSION   WP_284681496
VERSION     WP_284681496.1
KEYWORDS    RefSeq.
SOURCE      Sphaerisporangium fuscum
  ORGANISM  Sphaerisporangium fuscum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Sphaerisporangium.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10648172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Sphaerisporangium fuscum"
                     /db_xref="taxon:2835868"
     Protein         1..104
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11006
     Region          35..87
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mvlasnacpr ggilkvapyt rrirtasfph pgtrvaldar egalvallla ghtdasaarr
       61 lqisprtvtn vlralmdrlg vnnrfqlgva igqqipltar rnas
//
LOCUS       WP_284681666             384 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-protein kinase family protein [Adonisia turfae].
ACCESSION   WP_284681666
VERSION     WP_284681666.1
KEYWORDS    RefSeq.
SOURCE      Adonisia turfae
  ORGANISM  Adonisia turfae
            Bacteria; Bacillati; Cyanobacteriota; Adonisia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Adonisia turfae"
                     /db_xref="taxon:2950184"
     Protein         1..384
                     /product="tyrosine-protein kinase family protein"
                     /calculated_mol_wt=43112
     Region          <4..194
                     /region_name="Mrp"
                     /note="Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG0489"
                     /db_xref="CDD:440255"
ORIGIN      
        1 mgsivtfysf kggvgrtmal aniavllaqm gkkvlmidwd leapglpnyf sgfeikgnns
       61 glldlllksr dsnsieelsw qeyvsriklg sncylymiss gssdenyngk vltfdwelff
      121 ekfnggelie slrddwrkaf dfvlidsrtg itdsggicti qvpdalavif tanyqslhgv
      181 kdivsraqka rqsldfdrmp llilpipsrf dsrtefkesq kwikifekel tpfyadwlsk
      241 gntpievier tklpyvaffs fgeklpvlve gtsdpeslgr ayltnavlil elfqdpntde
      301 israapsdkl dnlaeiskkl stslnsinsn kghnhdqeqp pdfavvsapk yicpegdytw
      361 yrfdisdpip tcpthhcsle reda
//
LOCUS       WP_284682049             136 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Chondrinema litorale].
ACCESSION   WP_284682049
VERSION     WP_284682049.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..136
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15873
     Region          1..133
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mysseykvri ryadtdqmgf vyygnypify eigrveamrs lgfsykkled ngimmpvles
       61 rskyilpaky delitiktti tslpkvkihf nyeifnetnk lihigettla firkdsmrpc
      121 rvpseiidll npfyna
//
LOCUS       WP_284682370             447 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Chondrinema litorale].
ACCESSION   WP_284682370
VERSION     WP_284682370.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..447
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=51176
     Region          32..60
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(33,36..37,40..41,43,67,70..71,74..75,77..78,101,
                     104..105,108..109,112)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          35..313
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          65..95
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          100..128
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          139..165
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          170..204
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          210..244
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(211,214..215,218..219,221,251,254..255,258..259,
                     261..262,285,288..289,292..293,296)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          213..>422
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          249..279
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          284..313
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mksylfllml llcqvihlya qeehqatkad aieefykkge mmrkarqydk alleydyala
       61 isdtisrvhy akgltyyaqk nmvkaievie rtveldkknt qaynllvkmy sqaensdkvi
      121 eslerlaeae envkekqitl lkvagyyikk kqfekakeyt dkslaldktd letlyysaqv
      181 nnalgnyeda kksmesatst issedpkvya kfyyelgyay hylknyekke qaflkadfgp
      241 fkaliakltp dyfynlgscy sqiydlskad emlkealkid eehpstnqll aeiaikaeth
      301 pqkaidyykk aiegeedskk avklyetvie lllsskkyee sikvadecls kalnarnill
      361 mksmalhktd ktadglvile klildanitp lemvkynfaa gvmfrtqndf dkakeafaks
      421 ikgpfgtvaq yeyelmhidt adnqaae
//
LOCUS       WP_284682375             426 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Chondrinema litorale].
ACCESSION   WP_284682375
VERSION     WP_284682375.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..426
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48457
     Region          25..425
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mldrssppdf vpvkdisltq adsrvldngi rlhaisagsq pvinlqiifn agkwyekvpg
       61 ssillsklml egtkkfsaee innyfeshgi fweigggtdh ltidiyllsk ylhkiseiit
      121 dilsnallpe sefatvkkrl thqlkinqek tsyraaslfr tnifgeshpy gyaltpeiln
      181 gvnyqdvisf yesqvknrnf emlasgdlse evleqlisdf agltltdpli tdktvkdhpg
      241 msldsyanly eerdnnvqts irigrqinkr kdldtiklei lnrvlggyfg srlmknlree
      301 kgytygvhsn mvflkhggyf fintdvikek kddalseiyk eirtlyteai sedelalvkn
      361 hmvgsfiksi nspfslaehf ktmyfhkldt nyfnhyvsei nkvsseelle takkylqiel
      421 leitvg
//
LOCUS       WP_284682452             629 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284682452
VERSION     WP_284682452.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..629
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=70610
     Region          30..380
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mqnwsnfskl lfsffainvl flsytsalka qdhipqsvpa lidsiehime rkkiaglmlt
       61 lvendsiifc gglgysnlst eqkvdkntlf rvgsitkslv slaviklire dkftlnsnlk
      121 evapevpftn eweetdpiki vhllehttgf ddmhfskmyn ltgedisiee rlkndetsli
      181 srwrpgtrhs ysnpgytilg ylvekyagks feayvtdeil kpigmehanl lsfpkdkasy
      241 aqgydydkgd fkevpfyain svpagalnas atdmaeflkf flnnglvdst qffsaeeine
      301 mekvhstlaa knglengygl gnytsgygqk qlfqghnggi dgfissyayn relgigyavs
      361 nntsngmgdv iklvksfllr nsannsisst nidasslkef egyyqfknpr nhildlvtem
      421 fngvdvsied gkvfyksfmq dkkllapvgn ylfkteesnf antvfmltps gkqaielngl
      481 yfekgsfayi lwlrviifgn llialvsait flswlilfsk kelgfknfmv rtmpflallc
      541 fvimlyclqs mltgnivela tmngaglsfl issvllpils vvalisiflh kekmsrflqv
      601 wlivssvfvc clsyilydyg figlkiwey
//
LOCUS       WP_284682502             306 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Chondrinema
            litorale].
ACCESSION   WP_284682502
VERSION     WP_284682502.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..306
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34649
     Region          2..300
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mlklgfvsai laeksfeevv sfasehrfsc lemmcwpkgk aerryagvth idtneldadg
       61 iakiksvlde kkifisglgy ypnpldpdae kaayyrehiv evikaaakld ipvvntfigr
      121 dpsknlddnf kefakhfpai vkvaeennvk laiencpmff tndewpggkn maispvvwrk
      181 mfeiipspmf glnydpshlv wmqmdeikpi yefkdrlhhi hlkdvkvyrd klnevgilan
      241 pleyhspkip glgdvkwgsf faaltdvayk gpvcievedk ayegseedik sailtarnyl
      301 sqflvl
//
LOCUS       WP_284682482             301 aa            linear   BCT 25-DEC-2024
DEFINITION  rhomboid family protein [Chondrinema litorale].
ACCESSION   WP_284682482
VERSION     WP_284682482.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Koonin,E.V., Makarova,K.S., Rogozin,I.B., Davidovic,L.,
            Letellier,M.C. and Pellegrini,L.
  TITLE     The rhomboids: a nearly ubiquitous family of intramembrane serine
            proteases that probably evolved by multiple ancient horizontal gene
            transfers
  JOURNAL   Genome Biol 4 (3), R19 (2003)
   PUBMED   12620104
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10483871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..301
                     /product="rhomboid family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33937
     Region          <65..212
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
     Region          <266..299
                     /region_name="DUF6576"
                     /note="Family of unknown function (DUF6576); pfam20216"
                     /db_xref="CDD:466367"
ORIGIN      
        1 mnsfiedfky awnkpnngvv kliiinvivw vivnllyfls smldnpgmfs ffynniklqp
       61 tfgtfifkpw tiityffthq dffhilynmi fmywfgkliq eylgsqklva lyiwggiagg
      121 fayllvyyil glqssgmvga sagvyaiivg aatfkpehrf hllfigpvql kylaavavll
      181 sffqlpqtnt ggnvahlgga ligfifikql qrgddwskpv tsvlqffani ftpksgfkvt
      241 ygkkskvtvs kggyktnnks kdempeqavv daildkises gyeklskeek qilfkasqkk
      301 k
//
LOCUS       WP_284682509             187 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II [Chondrinema litorale].
ACCESSION   WP_284682509
VERSION     WP_284682509.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..187
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=20965
     Region          3..186
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 mkllildnyd sftynlvhlv kelgytpvvk rndkidlekv neydkillsp gpgipveagi
       61 mmdliktyap tksimgvclg hqaigesfga klknldlvyh givtdtnila kevtfnglpe
      121 tfktcryhsw vvdtkdlpdt levtatnseg vimalqhkky dvrgvqfhpe sfltehgdkm
      181 llnwlkn
//
LOCUS       WP_284682593             125 aa            linear   BCT 25-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Chondrinema litorale].
ACCESSION   WP_284682593
VERSION     WP_284682593.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 125)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 125)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 125)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 125)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..125
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14254
     Region          24..121
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mateqirysk eelkefeell kekiektkte lkhlkdsitr sasgydsnhy gvktledgad
       61 alekeqlnql aartlkylkq lenalirikn gtygicidtg kliskerlra vphtqhsiea
      121 klnrq
//
LOCUS       WP_284682699             408 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Chondrinema litorale].
ACCESSION   WP_284682699
VERSION     WP_284682699.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..408
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43981
     Region          6..349
                     /region_name="FucP"
                     /note="Fucose permease [Carbohydrate transport and
                     metabolism]; COG0738"
                     /db_xref="CDD:440501"
ORIGIN      
        1 memkinrsrl flgsctaliv tamtfairag ileklgvefe lsdtelgyit smaflgfpia
       61 miiggplynt lgpkkigyia ffshiiglgl tmlsqgfwgl fvstffvgfa ngmveaafnp
      121 liadmfpekk ttmlnrfhvw fpggivigsl vsqvmsdmsw qsqigvmlip tliygiiffg
      181 qkfpshvsdi stssatnlka mmsplyifmi lcmfltatse lgttqwverl lgnagaepll
      241 vlalvtglma vgrffagpiv hklnptglll assviafigi yllsiaegnm tyvaaivfai
      301 gvcyfwptmi gfiaeyipks gafgmsimgg agmfatsvfq piigswldsn reqakalgld
      361 gqaaelfagq etlsnitilp ailivafagl ffyirmkkkk evaatqta
//
LOCUS       WP_284682753             427 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Chondrinema litorale].
ACCESSION   WP_284682753
VERSION     WP_284682753.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..427
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48541
     Region          1..427
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mfsqtyfitv afvaglvvyq vsaminllen tnrevidfls siryddfsqs yqlsgrggtf
       61 dqlnnefnnv iqnfknirne keaeyqylkn iihhigigil sfdkkgdvqi intaakrlfk
      121 inrlrniskl qvfspelveh lhqlrtgska lvrvrdngei vqlaiyaiel ylkgeefklv
      181 tvqniqsele ekemeawqnl irvltheimn svtpisslan tvhgeieyik staeqevsqe
      241 dledigmaid tikrrseali rfvsdfrnlt hmpepnfnhv kvaemfrhiq ilmnneckly
      301 kinfttklep eslivtadqe lieqvlinmv knavqalgem geeenankti mlsayqnsnn
      361 rpvisindng pgidkdaidr ifipffttkk sgsgiglsls rqimrkhkgt itansnpgeg
      421 ttfnlvf
//
LOCUS       WP_284682970             469 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Chondrinema
            litorale].
ACCESSION   WP_284682970
VERSION     WP_284682970.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..469
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=52370
     Region          21..468
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mdcsnlkqcf esdmqdtegi ilvvdndsdv lftasliled dfaevhtvqk seaafsflgk
       61 ndvdvvlldm nftkgatsgk qglslleqik eiypevqvim ctafgdidla vssmqkgacd
      121 fvmkpwepvk lisrinkala nkqklevaqi eevsetetqs rlvflstamq eimklvekva
      181 atessvlilg engtgkglla keihrlsqrt hkpfvqidlg slpaslfeae lfghakgayt
      241 dagemkkgmi emadggtlfl deignlppml qaklltvvqs krivrigeme ersidfrlis
      301 atnmpleemm eqsrdgmpaf rrdlffrint veivlpplre rvedipllts hilqklenky
      361 akkelklsqe asislkkhsw pgnireleqv leravilsds evieaealkl rgihqssntn
      421 tleslnleem ekqaivklid khkgnmtkva kelgvgrttl yrrlqkygl
//
LOCUS       WP_284682988             805 aa            linear   BCT 25-DEC-2024
DEFINITION  GumC family protein [Chondrinema litorale].
ACCESSION   WP_284682988
VERSION     WP_284682988.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 805)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 805)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 805)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..805
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..805
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=90693
     Region          220..805
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 menqdtvfid ikaianrvls kwyyfvgsli vafllafvhn ktaqriyqfk ssliigqnqn
       61 gpksandili amgaeqknit nlkdemgrlt sftmvrktfe alnlkaayyk gedkgkneqf
      121 gagefpfkvv idsldpqplg vpifvklfpd styevevdae nvpiydysln evvrvepelk
      181 ikeriharek fthenlsfmi ipddkylagi peervhfifn sydrladtyi krlevkerdr
      241 dsyildlevt gsnpkkeiai lnklmevfkt tdllekmklg entleyintq lydarfnltq
      301 seqgltnfqt ssdivnadla tttlsaemqr lkqqqnelav tlklyerlkg ylesdlelte
      361 siaasaynln dggvqamlte iirlnsektq qepivgpehp sikrinlqin sarealkqqv
      421 rtaiqstvik kqeidrqlas nqaqfnkipl qqrriqelqr ssefdkttyq nllqkkteae
      481 illtnttsdv kildsarmmg sqpvspkttv syllaliigl aipyvlitlk dylddsvksk
      541 ddlitstkip ylgmilrgek snalvfegks rsgvaesfrs lrvnlehmrp slngvnghgn
      601 naagvngkvn gfksiqtigl tssvsgegkt fcsvnlasaf aqsgkktiii cgdlrkpkfs
      661 eyfdinnktg lsgyligdft indiiqptki enlyvidagy apnnpnptii ldsarmeqlm
      721 dklkqefdqi iidtppigfv aeyfilkkyv dssiyvvrsn ytnkkllgei ndlynnkkvd
      781 nisvvlndvk lsqalygygd krngy
//
LOCUS       WP_284683008             392 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Chondrinema litorale].
ACCESSION   WP_284683008
VERSION     WP_284683008.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..392
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=43117
     Region          6..389
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mpeysnfetk airhqaersh nrehsvpiya tssfvfedae earamfaeei pgniysrysn
       61 pnndefiekl cllehtedgi atasgmaamf csiaafvgqg dhivasrslf gsthqiltsl
      121 mpkwgvshty vsidnleewe naiqpntklm fletpsnpaq dladlealgk laakhniils
      181 vdncfatpyi qnpadfgahi ithsatkfid gqgrvlggav lgttdlikev rflarhsgps
      241 mspfhgwils ksletmavrm drhcdnamel atelekiddv awvkyphlas hpqyelakkq
      301 mkkggglvtf elkggvergr kfldalqmvs lsanlgdsrs iathpastth sklleeerla
      361 vgisnglirv saglehiedi kkdifraiev sa
//
LOCUS       WP_284683056             231 aa            linear   BCT 25-DEC-2024
DEFINITION  KdsC family phosphatase [Chondrinema litorale].
ACCESSION   WP_284683056
VERSION     WP_284683056.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..231
                     /product="KdsC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=26037
     Region          76..224
                     /region_name="KdsC"
                     /note="3-deoxy-D-manno-octulosonate 8-phosphate
                     phosphatase KdsC and related HAD superfamily phosphatases
                     [Cell wall/membrane/envelope biogenesis, General function
                     prediction only]; COG1778"
                     /db_xref="CDD:441384"
ORIGIN      
        1 mqndslfkhn lifflkkeed kipeaekild kkfsessykk lnlyldqaik lanlldvpid
       61 qliskdyqll eafntkeikl fivdidgvmt dggmyyseqg defkkfntkd glairaitke
      121 dfpvgiissg fnkkliqrra dllgikwlsv gtkpkievlk ewcdalhisy eniayigddl
      181 ndlevmqtvg lsacpadatg kikgtarvil skkggegcvr efienylshl f
//
LOCUS       WP_284683090             335 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Chondrinema litorale].
ACCESSION   WP_284683090
VERSION     WP_284683090.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..335
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36793
     Region          1..335
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 miadlrsdtf trptpemlqf mmqapigddv ygedpsvael erkmaemfgm ddaifcpsgt
       61 mtnqigikll tqpmeeiicd knshiqiyeg ggiaynslis sklidgdrgm itaeqveaai
      121 npddlhqpis kivalentmn kgggaiydme eirkiaavce khalhlhldg arlfnalvvt
      181 ndspkeygrl fktisvclsk glgapigsvl lfngiprika vrlrkvmggg mrqagliasa
      241 gtyaldhhve rlnddhrrak qlanalkeaa fvedmypvet nivifkvkns aemvktlaek
      301 gvkcitfspv hvrmvthldf tddmlehtlq aihsi
//
LOCUS       WP_284683105             468 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Chondrinema
            litorale].
ACCESSION   WP_284683105
VERSION     WP_284683105.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..468
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=52327
     Region          1..465
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mpkilivddd psfglmlkkf lekkgfeane vltgksclek maeesfdlal ldfrlpdmdg
       61 ldllkairqk niqipiilmt syanirtavk aiqmgafeyl vkpinpdetl llikqalnqp
      121 ketkkseape tdkgsaeksk pvskggikfi egisnestev ikyidlvapt slsviilges
      181 gtgkeyvsrm ihqkskradk pfiaidcgal seelagself ghlkgsftga vtdktgqfqa
      241 anggtlflde ignlsyevqv kllraiqegm vrkigsnkde avdvriiaat neelsdaakr
      301 gdfredlyhr lnefkievsp lrkrkediqv fadhflaqsn neldkkikgf tpevkkyfqe
      361 yswpgnlref knivrravll stgdyigqes lpeeitnpiv edsfdegtpq ssssvstnnl
      421 kemieknere tivrtleqvk ynkskaaril nidrktlynk lkqygida
//
LOCUS       WP_284683108             145 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Chondrinema litorale].
ACCESSION   WP_284683108
VERSION     WP_284683108.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..145
                     /product="YybH family protein"
                     /calculated_mol_wt=16740
     Region          22..144
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mklyfyrifc tlllslsffy vsaqdkdida vknilqrqik dwnsgdvekf mvgywesekl
       61 kfvgsngvty gyeatleryk tnypnqkimg kldfdiiste klapkvilvv gkfhltrevg
      121 daegyftltw kkidgkwvii vdhtg
//
LOCUS       WP_284683131             213 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Chondrinema litorale].
ACCESSION   WP_284683131
VERSION     WP_284683131.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 213)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 213)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..213
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23136
     Region          <119..210
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mftgllhthk lvvvlflliy iiktvlllig ktenlemftk kvkvpemiis flflvtgavm
       61 lfqlpeiktl liikiigvfa siplavigfk kknkllavls lillfgaygl aevnkrrvai
      121 apvsadvvtd eadasydplv hgkaifetnc vachgpagdl navgaknlqt selsdeevst
      181 virngknamp pygkvlnete vdalveyvks mrk
//
LOCUS       WP_284683229             349 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Chondrinema litorale].
ACCESSION   WP_284683229
VERSION     WP_284683229.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..349
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39522
     Region          73..327
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mknkiwllip vvilllaiif fmgnrpnvsn lnpkisdike ivpneldkqi tdkeatitgl
       61 kdkneskifw knpetkektp ysivylhgfs asygegnpvh rktaqyfgcn lyvprlykhg
      121 ideknalldf nseayiesak eaikvgkqig ekvivmgtsa ggmlaiylaa knpdlieali
      181 lysplvdfyd ddihllnlpw glqigqmvtg sdivnittkn emqkqfwttq yrleavvnlv
      241 slneaimkpa ifneikcpvf lgyyykdeen qdkvvsvpam lemfdelgtp enlkqkvafe
      301 dakehvicse ivsgnwqrvm dsthyflaft lnlnpadele edvlelled
//
LOCUS       WP_284683267             189 aa            linear   BCT 25-DEC-2024
DEFINITION  YdeI/OmpD-associated family protein [Chondrinema litorale].
ACCESSION   WP_284683267
VERSION     WP_284683267.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Pilonieta,M.C., Erickson,K.D., Ernst,R.K. and Detweiler,C.S.
  TITLE     A protein important for antimicrobial peptide resistance,
            YdeI/OmdA, is in the periplasm and interacts with OmpD/NmpC
  JOURNAL   J Bacteriol 191 (23), 7243-7252 (2009)
   PUBMED   19767429
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..189
                     /product="YdeI/OmpD-associated family protein"
                     /calculated_mol_wt=22656
     Region          2..185
                     /region_name="YdeI"
                     /note="Uncharacterized conserved protein YdeI,
                     YjbR/CyaY-like superfamily, DUF1801 family [Function
                     unknown]; COG4430"
                     /db_xref="CDD:443542"
ORIGIN      
        1 mevlffptpa dlkkwfvenh dqlvevwvgy ykksvkkdsi tweesveeai cygwidgirk
       61 tideesykir ftprkknsiw slknintvek likekrmqep glaayklrke sksgiyafeq
      121 ektafskefe sqfkqnnkaw kyfneeapyy kkiaihwvms akqektrikr letliedsen
      181 hlriksqrr
//
LOCUS       WP_284683321             237 aa            linear   BCT 25-DEC-2024
DEFINITION  RsmE family RNA methyltransferase [Chondrinema litorale].
ACCESSION   WP_284683321
VERSION     WP_284683321.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Basturea,G.N., Rudd,K.E. and Deutscher,M.P.
  TITLE     Identification and characterization of RsmE, the founding member of
            a new RNA base methyltransferase family
  JOURNAL   RNA 12 (3), 426-434 (2006)
   PUBMED   16431987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..237
                     /product="RsmE family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=26949
     Region          1..234
                     /region_name="RsmE"
                     /note="16S rRNA U1498 N3-methylase RsmE [Translation,
                     ribosomal structure and biogenesis]; COG1385"
                     /db_xref="CDD:440995"
ORIGIN      
        1 mhafyhpdtn ktdieiklse aeslhcskvl rlkagdeihi fngkggifng kiakqekkqt
       61 ivaiqsqisd ikqrefkihl aiaptkntdr iewfvekaie igidkitfil sryserkhlr
      121 ldrihkiavs amkqsynpfy peitelqrfe dflqsdieek ekylayeeta tnqslikeak
      181 pnssyciivg peggfnseel qnadnagfkk vslgpnrlrt etagvvacni lnmihlr
//
LOCUS       WP_284683242            1867 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Chondrinema litorale].
ACCESSION   WP_284683242
VERSION     WP_284683242.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 1867)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1867)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1867)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1867)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1867
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..1867
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=207450
     Region          321..1862
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mkpfasisil alsvtrkvfi tafilavvig gflyfsstlk agrsvkttvd aayasyvsay
       61 tagviskksp iriqlasqfa dsarvgesvt ssyftfdpei tgdaswidsr tiefipakel
      121 qsgtkyvlnf elgkvvdvqd gmenlsyefs tisqnfdlql eglapddnde psmqklsgsi
      181 ytadiasnee veklltasln dktldiswvh peeglthyft vsgierkdsk rtlelewnge
      241 pmgvsykgte nvdipalgdf klmntevvhn peqyvrlrfs dpiqanqdld gliqitglnn
      301 lrfqiqanei lvyptvrqtg akevrvspgi knsqgyplkd dlsfslafeq mkpevrfvgn
      361 gtilpnskgl ilpfeavgln evdvrvirvy edniaqflqv nsleertemk rvgrpillkn
      421 iklnnsgnad msnwsrysld lsdmiqtepg aiyqvnisft kdyaayvcqe efdlgegase
      481 snketslqel eeeydkntwd yyddyyyygy ydwehrddpc hpayygarrs vnknvlasdl
      541 gviakrgnng emlaavtdlr tteplsnvev avynyqhqll ddnltdsegl arldpkkkpf
      601 llvatlgnqk gylkiddgss lslsnfnvrg qeiqkglkgf iygergvwrp gdtlflnfil
      661 edkdrllpen hpvvfqlqnp mgqvvkkevr sqgvdgfynf itttdadapt gnwtakvmvg
      721 gttfskniki etvkpnrlki nldfgtdklt asngkitadl evkwlhgapa pnlkaefeld
      781 ltkgktafed yqnynfddeg kqfygesqqv fsgrldengk atistsidve daapgvlqan
      841 frgkvfeegg nfsvdrivip yypfssfvgm klpdskswsk lfydksnsvd iatvdangep
      901 vdrqgvivsv yrlnwswwwn qssedvanyv srqnktpvat grvntsggka tfnfdlnewg
      961 ryyikvcdpv sghctgeihy tswggdsnem psgatmltfa sdkekyqvge kvtlnipgsk
     1021 nsralisien grkvvqtfwl qteegdnpfs fevteamapn vyvnisliqp haqtindlpi
     1081 rlygvipvmv ddpethlspe lkmpdvlepe stfevqvses egkpmtytla vveeglldlt
     1141 rfktpdpwsn fyarealgvk twdlyddvmg afggslgrll algggdgvda kenakanrfk
     1201 pvvkylgpfq ldagdanvhk ikmpryigsv ktmvvaakgg aygntekvtp vkkslmvlgt
     1261 lprvlgpeek vklpvnvfvs dpsissvtvn ieasdllslp taskqvqidk sgeqivffdm
     1321 dvkattgign ikitasangv tsvdeveidv rnpnppvtnv iegmiqpgkt wdasygaigv
     1381 agtnssmlev srippinlek rlsylirypy gcieqtvssg fpqllvnnlm eitperskki
     1441 esnikatiar lnsfqtndgg maywpgqres sdwgsvyayh fiieaekkgy qvpsflksnl
     1501 krylkksare wryskaywnd dlmqayrlya lalsndaetg amnrlrelke lttqgawrla
     1561 aayyltgkns agkelvkglt tdvksykels ytygsdtrdk amiletlclm ndkakgfdll
     1621 kdiaahlsad twlstqttay sliavakfag mdnasqssgm kftlnlpegs pveastdlsm
     1681 iqkklnvkag gvynlslknt sntvlftrii tegvpargdq saaesslkls vryldlneke
     1741 mdptslaqgt dfmveakvtn pglrgnyeel vlnqifpsgw eilnsrmdgs ldsdkvsepe
     1801 yqdirddrvy tffdlkaset ktfrirlnas yageyympti sceamydhsi narkpgkvvk
     1861 vegvenq
//
LOCUS       WP_284683406             742 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Chondrinema litorale].
ACCESSION   WP_284683406
VERSION     WP_284683406.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 742)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 742)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 742)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..742
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=85684
     Region          12..738
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 meidevkeke qilslyrrll rkakpflkdd dakqikkafr faedahkemr rksgepyiyh
       61 pievalitve emglgttaii aallhdvved tgyeisdiee rfgtkiakiv dgltkistka
      121 tkgksiqaen fqrllvtise dvrvvlikia drlhnmrtle smpdhkqmki kseteyiyap
      181 lahrlglyti kseledlclk fsdtvayndi vkkieetkaa ryrftkrfik pieislkkqg
      241 fnfkiktrik siysiykkmr kqniefeqvf dlfairiivt tkpaeeksac wkiysavtdf
      301 ytpnvnrlrd wistpksngy eslhttvmsn tgqwvevqir termddiaek gyaahwkykq
      361 qkltskqkne rgidlwlqev remlettkse gvdfvqdfrs nlfikevfaf tpkgdmkiyp
      421 kgatildfaf dihsevgakc maakangklv pfnyelqngd qieiltsnky kanegwlsfv
      481 ktskarskik eylredkkqf akegkeivrr klkhlkldys eetlrnlceh fnqkteself
      541 ykigkglieh neikgfvnkk pvekpitqli sesdellnsd erdvkkikde eivvgdlssl
      601 dyslatccsp ipgddifgfv tvskgikvhr kscpnavtmm anfgyriira rwmsdkpdke
      661 kefdvsinle gmdrvglvne vtsvisnqmq vniksitigt rnnifngkld lfvhnkdefe
      721 kllkklekie gvvkvtriee tv
//
LOCUS       WP_284683425             378 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284683425
VERSION     WP_284683425.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..378
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42748
     Region          21..370
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mvssikqlti tilifftltv qaqpveklny lfenfqsknn fsgnvyvsvn gkalynkstg
       61 ianhefsisv dedtrfdias iskqftaali lkywedglid ldapiseylp yyrsdigkfv
      121 tvsqllthqs gipnytslpg vwidslrnhy sfkyliqhfc sgnlefepgs kfsynnsgyv
      181 llagiieeis grsfeneiqe kilnklglen tgissreqii snkaygydvl fdewqnanyt
      241 ympnlngags mystvkdltk wtlalhngkv lskkayelmf qpyavdndwi ppyknaygyg
      301 igmlntrkii peeldgwnmy fhsghisgfs sflayypedq kivvllsntd girtvnmndl
      361 tismieaiee fsevssgk
//
LOCUS       WP_284683455             541 aa            linear   BCT 25-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Chondrinema
            litorale].
ACCESSION   WP_284683455
VERSION     WP_284683455.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..541
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=59785
     Region          19..538
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mryiyfftla lfvfsctpyd tiitngkvyd gtgggmqtvd igikndrikt vgviekkkae
       61 niidaegkvv spgfinnlsw aaypleldgr smsdikqgvt leifgegssp gpynsekvkh
      121 trfslgqnmd ylvekgistn iasfigattl rlhqigsddr pptpeelkkm qelvkegmee
      181 galgigssli yppaffaste elialskiag eyngtyishm rsegdklkea veelitiake
      241 anidaeiyhl kaagernwdk ldevleliek aqesglnita nmynytgast gldaclppwt
      301 qdggkekwla rlndpetkke iiaemqqsen ewenflqlag dpknilllgf dkdslsylng
      361 knlgevakar gispaetvid livanngdis tayflmseen vkkqlklpyi tfcsdarsia
      421 segdnlkymt hprtygnfar llgkyvreek vlrmeeaiyk lsglsaeklk ivergklleg
      481 yfadvvifdp ekiidtatft ephqyaegve yvfvngtlvl engkhtgatp gkfvkgpgfk
      541 k
//
LOCUS       WP_284683549             486 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Chondrinema litorale].
ACCESSION   WP_284683549
VERSION     WP_284683549.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..486
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52373
     Region          5..482
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mnietsktkp ankaqgvney erervpdskl kgigsfvgmy agehaagtef vigplfvahg
       61 vsavelvigl lignllavls walicapiav knritlyyql ekicgsklvn fynianglmf
      121 cflagsmiav sataigipfn mkmpglndfy pnsiswilav ffvgaiitvv amrgyemvak
      181 vaniaapwmi lvflsagiav lpelgvssig efwsvakeki wvgatasdvs kfnfwhvtff
      241 awfanmamhi gmadmsvlry akkwqygfss atgvyighym awiaagilys vvliqivpeg
      301 ytlaeylpqv tsgdlppvap gplafnaagl agaicvviag wttanptiyr aglafqsifp
      361 kqnrmqvtmi agavatigai fpalvmklld fvalyglvlm pmgavifidh yfmkkfnlhs
      421 nyaelagikf napagiawiv tlcicvglni fggveifflg lpgwfiaail yivsskiaqk
      481 kqlvin
//
LOCUS       WP_284683569             194 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Chondrinema litorale].
ACCESSION   WP_284683569
VERSION     WP_284683569.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..194
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21748
     Region          61..190
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 meikvkrsyi etaifllvif iiyitgwqte iagllqrgvm ltglhnasvk tveqpkksql
       61 nfsitsldge evnvsalkgk tlfinfwatw cppciaempe ienlwkdvss eeiafllist
      121 ddemqkvkdf idrkefefpv yklnssvpke lssssipatf ivapdgsivy khsgianynt
      181 dsfkdflaki qkgi
//
LOCUS       WP_284683614             588 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Chondrinema litorale].
ACCESSION   WP_284683614
VERSION     WP_284683614.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 588)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 588)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..588
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=68205
     Region          42..501
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(56,58,60,64)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(95,98,135,138,178,199,203,235,289,443)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(235,289,357)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          508..581
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; pfam16657"
                     /db_xref="CDD:435493"
ORIGIN      
        1 mktlfylfla smvifscsdk saentkeeta stkldkkpgw wkegviyqiy prsfkdtdgd
       61 gigdlkgiiq kldyikslgv dmvwlnpiys spnadngydi sdyrnimdef gtmedfdiml
      121 kgmhdrgikf vmdvvvnhss dqhewfkqsr ssrdnpyrdy yhwwpaergk pnyryslfda
      181 kgeawkydsl tnayylhyfs qqqpdlnwen pkvrqevydv mkfwadkgvd gfrldafqyv
      241 akdttfpalp egyekeviky ygmgpnlhdy lremnedvls kyevfavseg agstfedahs
      301 lvdadrkelq mvyhfegmdv gnsldrykla efkkvyskwd safsekgwls iflanhdvar
      361 mvskfgndsp eyraasskml ntfilsmrgt pycyygdelg mtnidfekie qyqdiaaqns
      421 fikaksegad meafmetlnf lsrdngrtpm qwdatenagf tagtpwlpvn nnyqeinvta
      481 qdkdpnscln yfrkmvafrk nnpilvygdy elelpddeqi faytrtqddk kllillnfst
      541 eqattniser fnlkqepvin nypsvsmedt slvlepyqal ifeveksl
//
LOCUS       WP_284683665             446 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC1 kinase family protein [Chondrinema litorale].
ACCESSION   WP_284683665
VERSION     WP_284683665.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..446
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0004672 - protein kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=51097
     Region          14..434
                     /region_name="AarF"
                     /note="Predicted protein kinase regulating ubiquinone
                     biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport
                     and metabolism, Signal transduction mechanisms]; COG0661"
                     /db_xref="CDD:440425"
ORIGIN      
        1 makeneeves qksipaskvq raarfmktgv kvgrnyikhy arnavnpgtg kdllhednar
       61 diydslselk gsalkiaqmm smdknllpaa ysekfqmaqy sapplsyplv vrtfrkdvgk
      121 tpeeifdtft rnavnaasig qvhqatmgdk kfavkvqypg vaesvtsdlk mvkpfavnil
      181 glndsdvnhy mdevrnmlla etdyelelrr sreisaatsh iphlrfpsyy peyssrhilt
      241 mdwldgmhld aflktnpsqe ictqigqamw sfydyqihhm ksvhadphpg nfilndegel
      301 giidfgavke ipdefynkyf vllgkdited derlmkifkg lnfiyeddsq kdqeeiftil
      361 ktmvellgrp frrdtfnfgd dsyfreiyef geasakakvl keskkprgar dglylnrtyf
      421 glysilnqlk anidtksywq ensfqi
//
LOCUS       WP_284683724             325 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Chondrinema litorale].
ACCESSION   WP_284683724
VERSION     WP_284683724.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..325
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35942
     Region          14..314
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtekdvhqli gkihalkaei qkviigqedi idqllicfma gghallegvp glaktlmirt
       61 lseavhlnfk riqftpdlmp aditgtevle editsgkkff kfnhgpifan iiladeinrt
      121 ppktqaalle amqeyevtyg gktyslekpf filatqnpve qsgtfplpea qldrflfyiq
      181 lgypeeqdef tilssttgsk ktkvesvitg eeiaavqqlv revpvndtli srvnrivrat
      241 rpqttsvdmv kswvqwgagp ragqammlta kaaalldgrf avtpndiekv aypvlrhrml
      301 mnfkaeasgk ntdeitsail qeika
//
LOCUS       WP_284683739             449 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Chondrinema litorale].
ACCESSION   WP_284683739
VERSION     WP_284683739.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..449
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=51687
     Region          40..449
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mflksyrvni lfrilllils itlflycffi ihkhlrafyv fvlislqffe ffyftdkvnr
       61 dlsnfmlavt nndfsshfgg irgnsfekly nsfnqisnrm qelnneremh flqlqtlidh
      121 idigilsfdk tgeilllnpf mkekilnskl vrprninelk nninnrasif dmkpgerkll
      181 kiefqnqlml vsfqasafkl kdkyftlisa hdikselvgq eldswqklir iltheimnsv
      241 apitslsstl leivkhqihs dtviptfhhn nlinglsaie drgngllnft eayknltrlp
      301 qpifknvdcy sliksvialy qpvlyengin lnlervektl sltadpnlle qvfinllnna
      361 adalqgtenp eikvsifene nkricftvad nacgmdtetm eqifipfytt kergsgigls
      421 fcrqvmylhr geilvssatg kgtkftlif
//
LOCUS       WP_284683746             232 aa            linear   BCT 25-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Chondrinema litorale].
ACCESSION   WP_284683746
VERSION     WP_284683746.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10105453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..232
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26018
     Region          4..211
                     /region_name="SIRT5_Af1_CobB"
                     /note="Eukaryotic, archaeal and prokaryotic group (class3)
                     which includes human sirtuin SIRT5, Archaeoglobus fulgidus
                     Sir2-Af1, and E. coli CobB; and are members of the SIR2
                     family of proteins, silent information regulator 2 (Sir2)
                     enzymes which catalyze NAD...; cd01412"
                     /db_xref="CDD:238703"
     Site            order(13,15..16,23..24,71,88..89,91,106,172,177,198..199)
                     /site_type="other"
                     /note="NAD+ binding site [chemical binding]"
                     /db_xref="CDD:238703"
     Site            order(90,106,146,148..152,176..178)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238703"
ORIGIN      
        1 mkkkklivls gagisaesgi atfrasnglw eghdvnkvat ydgwlkdkel vlnfynerrk
       61 kaleaepneg hkilanfqky fdttiitqnv dnlheragsk nvihlhgelf ksrstvdenl
      121 vynidgweik lgdkcekgsq lrphivwfge mvpmmdlavq kaieadifiv vgtsllvypa
      181 aglidyvhde vpkyivdpel ppisrrpnlh lfpdigsvgl kkvseeiiqh ya
//
LOCUS       WP_284683806             242 aa            linear   BCT 25-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Chondrinema litorale].
ACCESSION   WP_284683806
VERSION     WP_284683806.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 242)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..242
                     /product="MlaE family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26182
     Region          1..241
                     /region_name="MlaE"
                     /note="Permease subunit MlaE of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG0767"
                     /db_xref="CDD:440530"
ORIGIN      
        1 mkslgkymmf lgrlvsnrep frvyrklffe eciligidsl tivvlvsvfi gavmclqtaf
       61 nlvspiipky vislvvrdmt llevaptfta ivfagkvgsn iastigtmki teqvdalevm
      121 ginsasylvl pkimagmfmy pilvilagfl ailggyiagv lggvitpdey iygirsdfmq
      181 fsvtfsivka fvfsflivsi saykgyftdg galevgrast kavtnsciav liadfflaqf
      241 lv
//
LOCUS       WP_284684007             422 aa            linear   BCT 25-DEC-2024
DEFINITION  peroxiredoxin family protein [Chondrinema litorale].
ACCESSION   WP_284684007
VERSION     WP_284684007.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Schroder,E. and Ponting,C.P.
  TITLE     Evidence that peroxiredoxins are novel members of the thioredoxin
            fold superfamily
  JOURNAL   Protein Sci 7 (11), 2465-2468 (1998)
   PUBMED   9828014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003123
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..422
                     /product="peroxiredoxin family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47327
     Region          265..422
                     /region_name="Bcp"
                     /note="Peroxiredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG1225"
                     /db_xref="CDD:440838"
ORIGIN      
        1 mklrllntil lgllflnacn npqreeqtaq gitdlpdatw raemqpndst iipftlktsh
       61 deagklsiav ingdevlple eyrfegdsii ipmlsfdtdl rlkveedkli gmyekywyev
      121 pyeipvtifk dddrrfivnk peplgnvtgt wdvdflndsd tpekavgife qkginvtgtf
      181 ltptgdyryl agvmdgkslk lscfdgshaf lftaelgadn kltngtfysg shwyqpwvav
      241 qddnaklpda gslthlkegy dkltfrfpnl dstlvsiede kykdkvvivq imgswcpncm
      301 detnfltsly ekyqgqglei iglayerkpd fayakakvek mkdkfgvdye vliagtsdkk
      361 aaaetlpmld hilsfptaiv idregnvsyi htgfsgpgtg kyytqfvdef tsiidglikk
      421 da
//
LOCUS       WP_284684016             306 aa            linear   BCT 25-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Chondrinema litorale].
ACCESSION   WP_284684016
VERSION     WP_284684016.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Kutner,J., Shabalin,I.G., Matelska,D., Handing,K.B.,
            Gasiorowska,O., Sroka,P., Gorna,M.W., Ginalski,K., Wozniak,K. and
            Minor,W.
  TITLE     Structural, Biochemical, and Evolutionary Characterizations of
            Glyoxylate/Hydroxypyruvate Reductases Show Their Division into Two
            Distinct Subfamilies
  JOURNAL   Biochemistry 57 (6), 963-977 (2018)
   PUBMED   29309127
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10187381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..306
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=34438
     Region          1..304
                     /region_name="GDH_like_2"
                     /note="Putative glycerate dehydrogenase and related
                     proteins of the D-specific 2-hydroxy dehydrogenase family;
                     cd12164"
                     /db_xref="CDD:240641"
     Site            order(47,66..68,91,221,269)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:240641"
     Site            order(67..68,85,91,95,137..141,159..162,164,191..193,
                     197..198,219..221,245..246,269,271..272,304)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240641"
     Site            order(94,96..98,100..101,104..105,108,110,113..114,
                     116..117,121..122,124,127,130,152,243,247,250..252,254,
                     258..259,261,264,266..268,270..271,275)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240641"
ORIGIN      
        1 msivviapep hlaevksklc lllpevsvft ineventddi dfavlwkktp ehlkdfpklk
       61 lvcslgagvd himsyalpnn lkiarigdag lsgkmskyvq aaiyhwehrf leyakyqsqn
      121 lwkpmiprki ntvgimglgv igtrvakdlv sngykvkgys rslksiefvy tfagennles
      181 flenldclvc llpltdqtkh ivnlpvfqql nkgaffinva rgavlnendl lealelgfis
      241 eafldvfeke plptehpfws htkisitphv asltdldrac kqlaenyfrl krgdellfev
      301 drvkgy
//
LOCUS       WP_284684186             521 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Chondrinema litorale].
ACCESSION   WP_284684186
VERSION     WP_284684186.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 521)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 521)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 521)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..521
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=60025
     Region          83..517
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mnsikyfffk lfdvsdfpar wfcgkwsdfh gwlyifsnll iwasyfaipa illyfsikrk
       61 dvpfkgifll fvffillcgl shlidavifw mpvyrlnavi lfctgivsti tvislfkvlp
      121 safelktpqe lsrileqrta elkqanlele sskdllkkli dnnpdaiskl dknykhlfvn
      181 ksitkhldvs peiiegktyd dlaypnklkr fleknidkai esgnilqkki ksldltenei
      241 slnvvfvpla naergevevl tiarditkee iakkelafki kelnkttktl rdhnkqmedf
      301 syivshnlrs pinniislle lyeleresnn vklndnskei fdhlkkvtln lnitiqelte
      361 iiniklhkfe ntkvlyfsdl lfnlkeslks eiesnrlevi eefeadsief vkaymesilq
      421 nlltnaikyr dtekksyvkf ssrnkenkvv ltcednglgi dmakfgndif slsktfhnhp
      481 dargvglfmt knqieafggs isvtsepsvg ttftltfmrs k
//
LOCUS       WP_284684205             258 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284684205
VERSION     WP_284684205.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..258
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29938
     Region          <149..255
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mesnskyhql pildglelld akshildfpf hthetfnial ilistfntkl sdkflkapvg
       61 tlsitnpkev hatpcdkdlg nsfftyyvsp eaiktfnngv evffedkiiy dqqlfgefya
      121 lsknithtnf ekrlsqvlkv lvekytspmr fnfqtrnlfq efinettfek fslsktahqf
      181 giskfkflrl fknetgltpn hyillkriek skkmlkegkp vfdvaidcnf ydkshfyknf
      241 krftgvnpse yqnaalls
//
LOCUS       WP_284684243             562 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284684243
VERSION     WP_284684243.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..562
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=63953
     Region          30..362
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkslkfqyll lffslftfsf svfsrqlskd sqdrltklle sfdqknapgf vlkvvrdgdv
       61 lfeknaglan letkeknnde tvfrvaslsk qftaacmlll eekglinldd pislyfpsfp
      121 dyadeitirh lihhtsglrd ffkladlsgy neddfnseea vlnmivrqkk lnfapgedml
      181 ynnsgyflla rivkdvsgks igdfandelf kplgmsstqf fnqetykvkn raygyslgds
      241 dkyeldesnl mitgdgglft tvndmvkwld nfyvnklpit dfdnrmyakg klndgtelny
      301 afglehadim gidciehsga yvgfksavln ipqkklaivc lgnlsnlqpe qicrkvaeii
      361 leegfkkpev tqerkplpfe rrainipekt fevysgkyel gngqilqfyt ennryyvdii
      421 gqtvielfpe simsffvket dlsfsfitdk egnailails innkrllakr vntttgmnnk
      481 emvdyvgayy neeldvvykl mmldkklfiq ignkpfeeig mikqdkmilg egmaefhrdg
      541 kgkvasflle agsvkdllfv kr
//
LOCUS       WP_284684213             229 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Chondrinema litorale].
ACCESSION   WP_284684213
VERSION     WP_284684213.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 229)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 229)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 229)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..229
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=26268
     Region          1..225
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mrcivvdded varmvikdfv erteglelva didnaidayn llkkekidlv fldiempqmt
       61 gielvesleh kpqfvlvtgr ndyavkayel titdylikpv eykrflqavq kvennfskdv
      121 ldtqgkediy vkadskivri klndikfvea lsdyviihtg qkkfivhstm kgiasrlpds
      181 efsrvhrsfi vninqietie dmsniimpnk iipigasykt sffkklnfl
//
LOCUS       WP_284684340             998 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chondrinema
            litorale].
ACCESSION   WP_284684340
VERSION     WP_284684340.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 998)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..998
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=110787
     Region          25..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miklipylqt illvfslsvg faqdrtitgs iksasdespl pgvniivkgt tvgtisdfdg
       61 nfrltvpqgg svllftyigf ktqeveigsk snftislaed veelseivvl gydtrdkdsf
      121 sgsavqvste vlqaplttvd qalqgnvagl nlrassgtpg aaqdirirgi sslnagndpl
      181 yvidgvpvvs gdlsasssts sfnalasinp adiesitvlk daastamyga rgtngvivit
      241 tkkgksgkat ysanfeygiv kqatdgipll nasqfmevnq eayanalavd siqasavpdw
      301 dalwdgetdt dwkdiitndh anyqnynism tsgtekgnmy aslgyynsds yviasslkri
      361 sgklsvsrql sdkinlsstf tgsnttqkgy legsgyyssp iyqsynllpi espynedgsy
      421 ntdltkmnnp laqaewdrdq lsmtrllnnt slsvdilqnl nftsklgvdf ayneeqhyds
      481 ryegdgetan aqeseyttrn lnyvwqnmls ynfdvnsdnk lsfklihegq knkkyllygy
      541 gydyavdgly tltnaattea sskkedwaqe svtflvnygf kdflfldgti rtegsskfan
      601 dyrwgtfgsl gaslvfsnlm dldwlnlakl rvsfgktgns didlnqyqst lsydkaynga
      661 sgtyisqmgn tdltweksnv fdigidfeiv nrvsgtieyf nretydmlld vplsfttgfd
      721 eqtfnvgrmv ndgievslnv dviqtknlsw slggnlsyir nevksltdda gqllesgtdq
      781 rleegkeayt wympkwagvd setgsplwyv ndeseetttd ynsaeyvyhg grmpnlyggi
      841 ntnlnykgiy fsanlfysfg nqiydsysky lytdgnygig rnnyamvyyd rwqqsgdtak
      901 npklfygrdd nsysqssrfl ydgsylrlrn vtigynipdk itnhikvsnv niylrgsnlw
      961 tytydddlef dpevdsdgyf dpttpplkty tmglkfnf
//
LOCUS       WP_284684362             520 aa            linear   BCT 25-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Chondrinema
            litorale].
ACCESSION   WP_284684362
VERSION     WP_284684362.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..520
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=56807
     Region          22..514
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mykitlllll alltqcnskk tqvdlvlsgg nvydgiaeda tvkdiviqgd siiaitsdwq
       61 ekyscgnvin lqgytvspgf idphthafdd lssttnnanl nflkqgvttv itgndgggpv
      121 kvaetfakwq dqgiginagl lvghgtvrkl amglrdekpt eealntmkmf vkqameegal
      181 glssglyysp gsfaqteevi elakvasayn giydthmrde ssyniglkaa veeaveiavk
      241 gniplqishi kclgtdvwnt ssdlinyids crnagvnita nqypynasgt nvisaifprw
      301 sqaggpdafl qrihdpaqrp kiykeiteni rkrggassll itrykdaslv khnlqevadi
      361 wqltpeeaaf riaengnarl asfnmieedi tnfmkqdwvv tgsdgstghp rkfgtfprkm
      421 qkyimdekvm smgefinkss aktakifgit drgklakgyk adiivfkpee vaekatfqep
      481 elyaegiqyl iingkiaike geytgilage tikkqvalvn
//
LOCUS       WP_284684439             467 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Chondrinema
            litorale].
ACCESSION   WP_284684439
VERSION     WP_284684439.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..467
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=52936
     Region          7..465
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mgkkvnkagk ilivddnedv lkaaklylkr hflqvdvekd penipdllnn esydvilldm
       61 nftkdvssgh egfywldkil eidpsavvvl itayggveta vraikegatd fvlkpwenek
      121 llatlssaik lresrmelnq lkdkhkqlnt dinskfqdii gqsssmikif etielvaktd
      181 anvlilgeng tgkeliaral hrqsaradei fmsvdlgavs eplfeselfg hvkgaftdar
      241 eeragrfeta sggtifldei gnlslplqak lltvlqsrtv trvgsnkpka idirlicatn
      301 mhlyemvkdn rfrqdllyri ntieinlppl reriedipll aehflsfyvk kygkhvrsis
      361 pslikrmqky hwpgnirelq hameravims qgpvldadqf ffsgttlqkq qdkgseelnl
      421 enydlekvek ilirkvlqkh ngniskaane lgltrsslyr rlekyel
//
LOCUS       WP_284684508             291 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284684508
VERSION     WP_284684508.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..291
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33692
     Region          53..280
                     /region_name="PRK09978"
                     /note="DNA-binding transcriptional regulator GadX;
                     Provisional"
                     /db_xref="CDD:137624"
     Region          <199..287
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mivipqklfn dtqvsiilrd gnicvlqkel pvsvkqregy vashaisfvq sgeqiinfyn
       61 geevrikake lviiprgvyy isdlissgeq fksllfyfdd diihqflssl nhseyqrkat
      121 sqhllinnsp nlntfctsli siyknssyqq salaaikile llhllhqnnk dliaflfqlt
      181 lpqkrniksf mqknfdkplk iedyayltgr sestfrrdfk safeitpqkw lkvkriekal
      241 silknkeisv telafevgye nisyfikefk ketgetpkqy ilskhknhlq l
//
LOCUS       WP_284684571             222 aa            linear   BCT 25-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Chondrinema litorale].
ACCESSION   WP_284684571
VERSION     WP_284684571.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..222
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=25203
     Region          15..193
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mnltlaeell lialddrrgk litssdfsid yclagallfd ltfenkvilk dkvlvvvsee
       61 kpqdsilrqa fdvitksstp enlqywlnel cekipglrya lmehlvakdv lykvekkllk
      121 ifsnprylpk qgesehlvrt rireiilhnk pfdlksvmli glvnaadlve eifpalndlk
      181 vardwikqip rsqkihgtis etleeiqsav nasinvpiiv rt
//
LOCUS       WP_284684774             264 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Chondrinema
            litorale].
ACCESSION   WP_284684774
VERSION     WP_284684774.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..264
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29862
     Region          29..255
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mklhkipkik kgnlkvkiik kdpfgnilif kriligvlat ftygrinivn klkvegteyl
       61 sdlpsknvlf isnhqtyyad vialyhifcs vkwkfrntig iplymliprv ntyyvaaeet
      121 mkesglipki fsyagavtvr rswrakgqnv srgadrsape kikkaldhgw vvnfpqgtts
      181 pyapirkgta niikhynpiv vpividgfrr afdkkglffk krgstlqvkf kkplqfseda
      241 tieeitsaia esieqskekk srat
//
LOCUS       WP_284684867             328 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Chondrinema litorale].
ACCESSION   WP_284684867
VERSION     WP_284684867.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..328
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=37756
     Region          <231..320
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          276..306
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mreaavvtfs fkyvnrlgvp dsfiprsgrv trdgliledg riffrdihrv erhhksivvv
       61 lkpgatisre isnhifkgft tfliniggfa rqvqsiinrr vsmarlndrk memdeeevst
      121 rfvkadcpnc daaidlidvv rshyiyceyc gaifdhygyl vpggdsyrvc petgyyervr
      181 dywqhtfyvt rhefafksrk lfcsdtyvhm vfekvfvknl tllfgaflag yekikslsgr
      241 dpnyielvda nlaahkgdme kalfeyaklv trnkyhpglh mnlglihlkn gnerkalvef
      301 krsldncsny tpvieilrkf sgpsssde
//
LOCUS       WP_284684983             147 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Chondrinema litorale].
ACCESSION   WP_284684983
VERSION     WP_284684983.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..147
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=16400
     Region          <13..147
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mlniidpeev vlllpeinqk qvvplygcyv qagfpspadd flekkidlne fliqnksstf
       61 lvrvsgesms gvgiyegnil ivdrsvtpkh nqivvgslng eftvkrlike gkriilqpen
      121 pdykpieitk esnlkiwgvv tfaiqnf
//
LOCUS       WP_284685002             473 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Chondrinema litorale].
ACCESSION   WP_284685002
VERSION     WP_284685002.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 473)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..473
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=52499
     Region          11..464
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mnarlnndlk dtesllnaal qvglkylael dqvptsikvs eeanmpelsa egkgglailq
       61 efkerfsemm vasagprywg fvtggttpaa imgdmlatiy dqntqtlkgh gdvsgkvefe
      121 tvqllldlfn lpkdylggfv tgatmsnftc lgvarqwlgk elamdvakng mqstfkvlsa
      181 vphssaiksl amlgmgsanv qlvktiaptr ecvdlealea eikalngqpf ilissggtvn
      241 tvdfddfkgi sklkekynfw whvdaafggf aaispsyshl ldgwenadsi cidchkwlnv
      301 pyesafffvk ekhkflqvet fqnsnapylg dplenfnfln flpensrrfk alpawftlka
      361 ygkdgyqeit ernirqakql gsfinessaf ellapvrlnt vcftlrgemn eakiqafldt
      421 lndsgkvfmt ptffnkrkgi raalvnwrtt endvlivqqe mqkafdqisk msf
//
LOCUS       WP_284685019             196 aa            linear   BCT 25-DEC-2024
DEFINITION  HD domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284685019
VERSION     WP_284685019.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..196
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22548
     Region          9..156
                     /region_name="YfbR"
                     /note="5'-deoxynucleotidase YfbR and related HD
                     superfamily hydrolases [Nucleotide transport and
                     metabolism, General function prediction only]; COG1896"
                     /db_xref="CDD:441500"
ORIGIN      
        1 msenrllqqi efikeidklk yikrrtklin sdrhendaeh swhlavmali laehgntkvd
       61 llkvikmlli hdiveidagd tflydtqknh snteeeliaa krifgmlpee qakeyiaiwe
      121 efeagesdea kyaksmdrfe pvlqnasnng gtwaeynvpy skvhsklspi qkgseaiwqy
      181 teetlnesve kgilkk
//
LOCUS       WP_284685045             127 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Chondrinema
            litorale].
ACCESSION   WP_284685045
VERSION     WP_284685045.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..127
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14658
     Region          22..115
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mceqkdfpke rnfatcqvvl mpvrdalevl sgkwkilili sllnetkrfk qisrdlqtit
       61 dkilskelkq leenklikrt vkdtfpptve ynitehgkti ekvigelaew gkshrqvvmg
      121 kvnsyed
//
LOCUS       WP_284685266             323 aa            linear   BCT 25-DEC-2024
DEFINITION  MraY family glycosyltransferase [Chondrinema litorale].
ACCESSION   WP_284685266
VERSION     WP_284685266.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Anderson,M.S., Eveland,S.S. and Price,N.P.
  TITLE     Conserved cytoplasmic motifs that distinguish sub-groups of the
            polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase
            family
  JOURNAL   FEMS Microbiol Lett 191 (2), 169-175 (2000)
   PUBMED   11024259
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Lehrman,M.A.
  TITLE     A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P
            transferases
  JOURNAL   Glycobiology 4 (6), 768-771 (1994)
   PUBMED   7734839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10160628
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..323
                     /product="MraY family glycosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=37334
     Region          26..265
                     /region_name="GT_WbpL_WbcO_like"
                     /note="The members of this subfamily catalyze the
                     formation of a phosphodiester bond between a
                     membrane-associated undecaprenyl-phosphate (Und-P)
                     molecule and N-acetylhexosamine 1-phosphate, which is
                     usually donated by a soluble UDP-N-acetylhexosamine
                     precursor; cd06854"
                     /db_xref="CDD:133464"
     Site            80..81
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133464"
     Site            188..191
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133464"
     Site            order(235,246..249)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:133464"
ORIGIN      
        1 miffflfasl fliqkiyfvt adkynivdkp nersshdylt irgggiifpi aiyigaivfq
       61 vtipfflfgl flisvisfwd disslpsryr ilvhfisial lmfsvgvfel sywvilpifi
      121 vatgiinafn fmdgingitg gyslitlltl lyidqeiinf inerlilvii fsviiflffn
      181 frkrarcfag digsvsiafi iiyllltlil ksnnliyill lsvygidsif tiverllnke
      241 nifkphrkhl yqllanemqi shlkvssiyi ifqalinavl viflhvkeyn fwlltflnla
      301 lqsilylfvk nkikyiiknr hvi
//
LOCUS       WP_284685172             274 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Chondrinema litorale].
ACCESSION   WP_284685172
VERSION     WP_284685172.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..274
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32350
     Region          1..274
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mydieiadlr klielvkeky dydfknyams sfkrrikriv elykfdsvda lverlthnps
       61 ffdefvsevt vnvtemfrdp dfwtilrdei ipnilsnhnk lsiwhagcss geevfsmqil
      121 leemgvrdks htiatdidsa iinrakdatv skknidlnss nyeryqgkyt ldkyftedke
      181 kyyfnkqlls nvsfrkhdlv kgqvfskfdl ilcrnvmiyf nqtlqndvly llheslfkyg
      241 flcigskesl iwcdiankfi vinneekiyk kvke
//
LOCUS       WP_284685265             678 aa            linear   BCT 25-DEC-2024
DEFINITION  polysaccharide biosynthesis protein [Chondrinema litorale].
ACCESSION   WP_284685265
VERSION     WP_284685265.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 678)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 678)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 678)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 678)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18500220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..678
                     /product="polysaccharide biosynthesis protein"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=77394
     Region          157..273
                     /region_name="FlaA1"
                     /note="NDP-sugar epimerase, includes UDP-GlcNAc-inverting
                     4,6-dehydratase FlaA1 and capsular polysaccharide
                     biosynthesis protein EpsC [Cell wall/membrane/envelope
                     biogenesis, Posttranslational modification, protein
                     turnover, chaperones]; COG1086"
                     /db_xref="CDD:440703"
     Region          317..603
                     /region_name="Polysacc_synt_2"
                     /note="Polysaccharide biosynthesis protein; pfam02719"
                     /db_xref="CDD:426938"
     Site            order(321,323..326,346..347,373..375,396..398,400,415,438,
                     454,480..483,486..487)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(347,349,353,357,371..374,377,380,398..401,404,408,
                     411,414,487..488,493)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187548"
     Site            order(400,440..442,450,481..482,488..490,493..494,
                     505..507,511,513,548,575,578)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(416,440,450,454)
                     /site_type="active"
                     /db_xref="CDD:187548"
ORIGIN      
        1 msttnsngtv lkamsqkspa ainfylrlkk mlvnaygtri iilgvdvvvs vmafvlanll
       61 rfnfvitdip ldkalptisa lilirtitfk yfktyssvir ftsehdlltl lksvtlgsfv
      121 fflftfqfnf fdeifffrks ivmidylicl fllinyrval rvihiqmnre rqvhenvvvf
      181 gagscgdmtr ktidhdkdth lkvlaffddd lslhrktmgg iriyhtdhyf eevvskfkik
      241 kaiiaihkis ikrkeelvel clkhnitpli vppvenwlns klkvssfrki nieellhrap
      301 ialdyknias qvenktilvt gaagsigsei arqlmnfhpd klilldqaet plvnlqlemq
      361 ekfdysvtip ivadvrdqkk mrdvfskfkp divyhaaayk hvpmmevnpe eavkvnvfgv
      421 qivanlavry gasrfvmvst dkavnptnim gttkrmaemy cqslndysrn lktrfittrf
      481 gnvlgsngsv vprfknqiea ggpitvtdpn itryfmtipe acqlvleaga mgkggeiflf
      541 dmgepvkivd larkmirlyg leenkhisie ftglrpgekl yeellnqaen tikthhdkit
      601 iakvrkelfe kvykdlkkiq kallenddml lvaymkqivp efksncskys eldntenllk
      661 vvrkgkkelr ighrayln
//
LOCUS       WP_284685348             369 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284685348
VERSION     WP_284685348.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469209
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..369
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=42340
     Region          1..368
                     /region_name="COG4867"
                     /note="Uncharacterized conserved protein, contains von
                     Willebrand factor type A (vWFA) domain [Function unknown]"
                     /db_xref="CDD:443895"
ORIGIN      
        1 mkgfrftkfv pqkdaeksef enllniftql ltitsgdvse alswltnldk qynltnpqyg
       61 igdfiedlkn kgyikedenn kgtfkitakn eqnirrsale eifgklkkan kgdhnttysg
      121 nngeelsadf reyqfgdtld qismtdsirn aqvnhgtsnf fltendlevv ekeyksqtst
      181 vlmidishsm ilygedritp akkvamalse littkykkdt ldiivfgnds wqiqikdlpy
      241 lqvgpyhtnt vaglelamdl lrrrkntnkq ifmitdgkpt cikegiryyk nsfgldnkil
      301 nktlnlaaqc rklkipittf miasdpylke fvreftkvnn gnayysslkg lgnlifedyr
      361 rnrrknfkq
//
LOCUS       WP_284685364             490 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Chondrinema litorale].
ACCESSION   WP_284685364
VERSION     WP_284685364.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..490
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55773
     Region          1..490
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mkkniiviga gfaglsaais ladkgfsvki leknsvtggr aryfkeqgft fdmgpswywm
       61 pdvfesffnr fgkktsdyye lvrldpsyrv ffgkddfldi paemqainql feslepgsst
      121 qlqeflkqaa ykyevginnl vykpgqsvme fmdvkllsdv ikmdifqsfs khvrkffknd
      181 klirliefpi lflgatpent palyslmnya dialgtwypk ggmhkiieam valakekgve
      241 iitgeevkvf didqkditkv itentefead vvvagadyhh idkqvlpadf snytesywdk
      301 rvmapsslif yvglnkklnk lihhnlffdr dlgphaveiy enpkwptepl fyvsvtsktd
      361 etvaeegmen vfilmpvapd ledneeirek yfniivdrie nitgekfreh iiytrsyahk
      421 dfkkdyhafk gnayglantl mqtailkpgl knkklnnlyy tgqltvpgpg vppslisgiv
      481 vadevekqfs
//
LOCUS       WP_284685384             312 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Chondrinema
            litorale].
ACCESSION   WP_284685384
VERSION     WP_284685384.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..312
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34925
     Region          56..297
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mkskinrkef lqysgkaiaa gylsswmlss caapvgnaen agrmkkslkf gmieedlsvl
       61 dkfkllkdlg fdgveldspn elsekeilda rdktgleipg vvnsvhwkap lsdpdpsvrk
      121 kcvdsmetal qdckkyggtt vllvpgvvge nvsydeayar sqeeikkilp iaeetgvkia
      181 ienvwnnfll spleaaryid efesdmigwy fdvgnivryg wpeqwirilg kriikvdike
      241 ysrklaneeg vwegfkaell egdcnwqnvm talnevgyag wgsaeipggd rkrlekisql
      301 mdeiysyyps pv
//
LOCUS       WP_284685765            1143 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Chondrinema litorale].
ACCESSION   WP_284685765
VERSION     WP_284685765.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 1143)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1143
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..1143
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=129932
     Region          574..810
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 myrlllavfl ffltfisnsy advwvseifs dgmvlqqgke itiwgtaapr ekvavtlrgr
       61 saitradrng ewevkippls pggpyimnil gknlitinev migdvwlvtg epfenfnkee
      121 istkeatqdk pvhffnitpq ialtpsenik stgkwhslqs idqtefqlfh afadslyqqn
      181 nvpvaiiysq ykdaslaawi npdtlrqyke yqdtlsimek qflgierfls erkvdnfvkt
      241 ypsvvyntmv npiapytlng ifwhqnqsdi qyafytqklq qdlvnsfrar wnnrklpfii
      301 lntnissssn dsteniykse fleiqnhlft kplvsvinkl vdssensisa iltvcnslse
      361 nntsiskspk pnsfsiegek milhfsgdks lffdnkygyg kgfsiagrdq kfysarafvr
      421 ndslievysd nvkqpiavry sfnsflkdan lktsnglnal pfktdnwpgv tdtssfrtkw
      481 ldagkvdtid mvnkyqqtla nqyppkakpf penlaewesq kpyyyeklvn slgfsknewe
      541 nrnaiqslyk gqniefedyt irhvlyqsqp sfwvsanlyv pkniefprpa ilylnghsgn
      601 gkatenyqls mislvkkgyv vmsidetgag erkytsqhtp qffltghsdg gwqiwdasra
      661 ldfllsqknl vdkdrvgvtg rsgggfqsfy laavdkrvka vapvmyvssf egmidsnkih
      721 tidnylptir kymeqfhvlg lmapnpvfig sgqqdffpin atkttvdkak eiyqfynesk
      781 ypelnvvdig hkdtivhrea vyaffnkvfn vdnnssepqi qinsdsllnv gipsyssatt
      841 lslankelin ssrkhnayis lperryklle ildldnlnnr sleigyhsis tdktgnrtne
      901 kfliqtdysi ylnaelsyld neakhsvvii nnpeislkds likagfavfs fsprkgents
      961 hntssnkidy eyltfsnsiv lgesmlgqka ydfiravdfl qtksdvidis ninlvnldtt
     1021 lnskieilaa aaldnriqkv avnnalisil psttewanwn yttytpnlag fgniqdiisl
     1081 iaprkiklyt pkntngnnlt nyqlinetsr sryeyrkqna tknldvsnqe ysnellldfl
     1141 rnd
//
LOCUS       WP_284685792             978 aa            linear   BCT 25-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Chondrinema
            litorale].
ACCESSION   WP_284685792
VERSION     WP_284685792.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 978)
  AUTHORS   Rengstl,B., Oster,U., Stengel,A. and Nickelsen,J.
  TITLE     An intermediate membrane subfraction in cyanobacteria is involved
            in an assembly network for Photosystem II biogenesis
  JOURNAL   J Biol Chem 286 (24), 21944-21951 (2011)
   PUBMED   21531723
REFERENCE   2  (residues 1 to 978)
  AUTHORS   Komenda,J., Nickelsen,J., Tichy,M., Prasil,O., Eichacker,L.A. and
            Nixon,P.J.
  TITLE     The cyanobacterial homologue of HCF136/YCF48 is a component of an
            early photosystem II assembly complex and is important for both the
            efficient assembly and repair of photosystem II in Synechocystis
            sp. PCC 6803
  JOURNAL   J Biol Chem 283 (33), 22390-22399 (2008)
   PUBMED   18550538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..978
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..978
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=109339
     Region          78..264
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          391..>508
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          644..784
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
ORIGIN      
        1 mklkttsnfl llitcssllf fnqvfaqpaf tsskkrmdgm qqrkkllens liknvnfksi
       61 gptvmsgrvv dldvnpedps hfyigfasgg lwkttsngmd mqplfqhqes itvgdiavnw
      121 kngetiwlgs gennssrssy agtgiykstd kgetwehlgl egthhigrvi lhpsnpdvvw
      181 vaalgnlyss nkdrgiykte dggkswkkil findntgfid lvidpsnpev lyaasweker
      241 kawdfvgsgd gsdiykttdg gknwkkintg kngfpddkgv grigldisvs nsqiiyavld
      301 nqnrrsksed vsekaivtte llssidneaf inlsdkeind yldknnfprq ynateikeav
      361 kqgelkpval vdylgdants lfetpvigte iyrsddggnn wkkmnddyid gvyysygyyf
      421 gqirvsptnp dkiytfgvpv iksedagktw kninggnvha dhhalwlnpn kdghlvlgnd
      481 ggvnisyddg nswikcnnvp lgqfyavnyd lakpynvygg lqdngvwygs hnanistswe
      541 meganpfkel mggdgmqvei dtrnnnivya gfqfgyyfri nkatgerkmi qpkhelgekp
      601 lrfnwqspih lskhnqdily fgsnkfhrsl nqgddfetls gdltnggkng nvpygtltdi
      661 nesplkfgll yvgtddglvh vskdggynwt kitadlpenm wvsrvtasaf sesrvylsln
      721 gyrwdnfdam vyvsedygkt wtaigkdlpa esvnvikedp knenilyvgt dhglyisldr
      781 gksfmmages lpnvpvhdlv ihpkeneliv gthgrsiyia dvsliqklte dilskslysf
      841 eldevrysdr wgnsigaswy gfneptlqip fyvntsgtvs invisekgtv lkteemevqk
      901 glnyfhydms isesavaqfs kelteidgnl dknengkvyl kqgtytielk lsgstvkemf
      961 tvkpvnkrpe rkplektp
//
LOCUS       WP_284685819             609 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF885 domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284685819
VERSION     WP_284685819.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..609
                     /product="DUF885 domain-containing protein"
                     /calculated_mol_wt=71062
     Region          1..542
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
ORIGIN      
        1 mkrnikiiiv valvsivswv inliwykpfs idlffermfv efglrnpell tdshvlenyg
       61 fynhnrelnn isleyrqesf tkmtrafeml rsykrtkldk hqllsydild fylekiifkq
      121 qfaqheipln hingihaqip lhliesqfis dlkdaenyls riskirekiy qsiqnimiks
      181 eddkpprfvf dyivqqidcf lvtdieknli yqdfknklek anlinenart ellyelklei
      241 gdnvypafhe lklkmevere hvsedagiwr yvdgdtyyyt lltesltidt smfdmeiwam
      301 geverlhgkv adiiefeeke vtdnsvteml nlfsdkylte ntgikhpsdt lnkmlnslfe
      361 qngvshlqnt invkenlpff nnyqisqyyp asldnyrkas llvsdkllkh lpaymlkgli
      421 isevfpghhf qkelitnses lpnirkqief nafaegwkyy vlenaeslql tsnkleklgc
      481 lqwqllfasa avvdlkihqn tfsreeaisf mlevtglpkq iiiavvdkti vmpakapafl
      541 vgfqayqqln dflldktgnk kdrflqscni indkgavpar mfsevkkels lvftkaddki
      601 vaekelvee
//
LOCUS       WP_284685871             895 aa            linear   BCT 25-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Chondrinema litorale].
ACCESSION   WP_284685871
VERSION     WP_284685871.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 895)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 895)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 895)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 895)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..895
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..895
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=98160
     Region          1..895
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 meklknayql esdevisslk tdpdqglssn eaesrlnefg rnklkeekkk slfqilidql
       61 nnpviyllla avtlsfvfgd iaeaiaiivv ivlntvigfw melqamqsmd alqkmdklvv
      121 niirdgqakq ldaeelvpgd lleveagdli padcriiyna qlkvdesplt gesipvdktt
      181 dkiegdtgig drkntlykgt avtngngkai vvntgmetel gnisqmvsda gneevplnkk
      241 leklskhliw atlglaavff vvgwlsgedp yelvqtsiaw tiaaipeglp ivasialarg
      301 mlklakqnvi vkklsavetl gettviftdk tgtltlnqls vnavmspekd ydvtngkngy
      361 sddenvkkml siavlcnnan iensnghngs dnghdgdgee kekadgvgdp ieiaslqytk
      421 nadesryqel ikaekiledp fdsdkmmmgt ahvvndgkvm vsakgatekl irecnkilaq
      481 gkeealseeq kqewidknne lsedglrila faykdmdnkp ssedellhdl tfagligyid
      541 ppresvkdai dtchkagiev imltgdhpgt akniatqvhl vdkddtnvvh geelsdktde
      601 htiveskvfs rvdpsqklai ieayqkeghi vgmtgdgvnd apalkkadig iamgdkgtqv
      661 aqevadmvlk ddsfesivta ikqgrvifsn irkfiiyqls yhlseiivia svsfslfflp
      721 llplqllfln lisdvfpala lgigqgnphv mnnkpnskqe piitkekwis ivvyavilal
      781 cvggayffsy fnwdageeis nnvafftlaf sqllhvlnmr dadenifvnq vtknkfiwma
      841 lafcftcmga ayfipqlaei lsiqeleaky wgliatmsim pvviiqllka vtkkl
//
LOCUS       WP_284685895             316 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Chondrinema litorale].
ACCESSION   WP_284685895
VERSION     WP_284685895.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..316
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36581
     Region          42..304
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mstrrkfiqk lglaagatgv lahdtfassk tdiqtkkakr vlriahitdv hllaqpksen
       61 avitmfseik nmkdqpdfii ntgdtimdan nqlpetveer wkawhkvseh nafetfhcig
      121 nhdvwylpke kkeqykdder lgknwvlnel kmnnryysfs rngwhficld sinygengvh
      181 ldeeqlnwlk nelenidsnt pvcvyshipi lsitsftyyl nrkpapevqf prgdmhsdyn
      241 elkalfykhk nvklalsghn hyiddvaylg ttymcngavs gnwwsgdlde fppayaiidl
      301 yedgtaqrem vyynwe
//
LOCUS       WP_284685897             232 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Chondrinema litorale].
ACCESSION   WP_284685897
VERSION     WP_284685897.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..232
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26098
     Region          58..155
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mkliednqlr lshvvannkm nrqrqltgvn syakeigini feflsnriet geetvlwldi
       61 ccgegkalie caqllketdy ekqviiigld lvsmfeaypr kdlsnlklle caielwetdr
      121 qfdlitcvhg lhyvgdklgv ikkiaallkp tgklvghidl nnlknnlgkp idkcikdswk
      181 smgwvynsks hllkidgrsd wkhvgvyqga ddtagpnytg qeavnsyykl dg
//
LOCUS       WP_284685952             104 aa            linear   BCT 25-DEC-2024
DEFINITION  thioredoxin family protein [Chondrinema litorale].
ACCESSION   WP_284685952
VERSION     WP_284685952.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..104
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11604
     Region          1..101
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 mfqeltddtl nevvksnetv lvqfsagwcg ncrimkpkfk kmareneaat fvivdaekfp
       61 nsrklasvdn lptfaafkng efvkqvqtnk veslkelvde vtsn
//
LOCUS       WP_284685974             781 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-glucosidase [Chondrinema litorale].
ACCESSION   WP_284685974
VERSION     WP_284685974.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 781)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 781)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 781)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 781)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 781)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13307224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..781
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..781
                     /product="beta-glucosidase"
                     /EC_number="3.2.1.21"
                     /GO_function="GO:0008422 - beta-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0030245 - cellulose catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=85364
     Region          1..749
                     /region_name="PRK15098"
                     /note="beta-glucosidase BglX"
                     /db_xref="CDD:185053"
     Region          39..>384
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mkrhiiagaf valtsmqgsf aqkapkfgka piekvieamt ieekvsilig pgmpgyaglv
       61 plegepdvrv lgaaggvngi erlgipeivv adgpaglriq pkrnndenty yatafpvgta
      121 lastwnteli eqvgkamgee vkeygvdill apalnihrnp lngrnfeyys edplvageia
      181 aayingiqsn gvgtsikhfa annqetnrlt inehvseram relylrgfei aikkskpwtv
      241 msaynkingt yassnkdllt tvlrdewgye gfvmtdwfgg ypgfqsimkd csdvvaqiea
      301 gndllmpgmd iqrekliaam kagkiseeav ntsvkkilei vlksptynkv kftnkpdlka
      361 haeitrqsat egmvllknes nilpytekst piavfgitsy nfiaggtgsg dvneaytvsl
      421 ieglnnagyk idqelekayv pfvkaevake mkrreenggl lavpqrlkem aldndliakk
      481 akasevavit igrnsgened rhinedfyla qdeitlinqv skafhaenkk vivilniggv
      541 ietaswkdkv daillawqpg qeggnsvadv fsgtanpsgk ltmtfpvdyn hhpsatnwlg
      601 tpisnpeevy ykegiyvgyr yfntfdvkps yefgygssyt tfeyadlkvn tsnvdkqvev
      661 svkvtntgkt agkeivqlyl sapaklvdkp eselkafakt ktleagesqt ltftltskdl
      721 asfideksaw iaedgsytvk igassldikl teiftvsedi vaekvnntfd ldkdfkdlts
      781 k
//
LOCUS       WP_284686039            1142 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chondrinema
            litorale].
ACCESSION   WP_284686039
VERSION     WP_284686039.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 1142)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1142)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1142)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1142)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1142
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..1142
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=124866
     Region          141..1141
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkilrqvl lmskygflgi clqalfcsll laketnaqkv smeeiyitan lkdatikdaf
       61 dlislktpfk fayeltnadl kekvdlqrln snyhketlan llrdisktsn lkfkrinnni
      121 fvsakeafad pieeiislns fqvkgvvtss ddgeplpgvs ilikgtqtgt ttnlngeytl
      181 dvnegdillf sfigyqtqea tigskttlni alefdqeqle evivigygtv kksdltgsvs
      241 alksedlnpg anasvdqmmq graagvqisq sssepgggls irirgsssin agneplyvid
      301 gfpidnssnl sgsglssdpn nvgaaqaigs nlspknplns lnpndiesie ilkdasatai
      361 ygsrgangvv littkkgsnd kltvsyntyf gtqsvakqid vmdaeqymnf indisadrgn
      421 sevfstsdis tigsgttwqd eiyrsapisd nnvslsggvg nskiyasidy fnqkgilknt
      481 gikkyigrln ldsklgentn igfnintshi adqngidgvn tnesagpiyt sllydptepi
      541 fnadgsyavs enltinnpms lidgvksksq tdrtlanfyv sykiidglia klnlgsdisn
      601 vkrdvfvstl tnrgealggy advtssrrss ilgeytmnys keinenhrfd vlggvtyqkf
      661 yfsvfnanin gfptddietn nlslgdtntd nlysnkednt lfsylgriny tlfdkflltg
      721 siradgssrf gdnnkygyfp sfafgykmse eafvpdffee lkfraswgqt gnqeisnyas
      781 qltfgtgsfv vfdgqiqgst nplrianpdl kwetttqfnv gldasmlsgr invtldyfsk
      841 sttdllfnla lpqssgyssi ltnvgevsnk gveilinstn istkdfswnt slnftsikne
      901 vvdlgridqi ttgylqvvgg nsaiikegsp lasyygyeit giqqegdeip gypkfkdqng
      961 ddqittadqt ivgdpfpdft yginnqfeyk nwglsfffqg meggdlfnvm aaesmypand
     1021 rrnrmtmmmd rwtptntdaa wpsatnpnsy pagsagkvns ltimdasyfr lknvqisynv
     1081 ptqnisflst lrlyatgqnl ftitdypgyd peanafgrnn vkvdyasypl artfmvglna
     1141 tf
//
LOCUS       WP_284686087             106 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Chondrinema litorale].
ACCESSION   WP_284686087
VERSION     WP_284686087.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..106
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12379
     Region          4..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mrrdvfqaia dptrraiigl ialqamtpna iadnfntsrq avskhlrils ecelvsqeqq
       61 greiyyqlev eklkeidqwl aqyrkiwetr fnqlddilst mkknkk
//
LOCUS       WP_284686110             783 aa            linear   BCT 25-DEC-2024
DEFINITION  GAF domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284686110
VERSION     WP_284686110.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   2  (residues 1 to 783)
  AUTHORS   Ho,Y.S., Burden,L.M. and Hurley,J.H.
  TITLE     Structure of the GAF domain, a ubiquitous signaling motif and a new
            class of cyclic GMP receptor
  JOURNAL   EMBO J 19 (20), 5288-5299 (2000)
   PUBMED   11032796
  REMARK    Erratum:[EMBO J 2001 Mar 15;20(6):1483]
REFERENCE   3  (residues 1 to 783)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005630
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..783
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=90697
     Region          <306..>405
                     /region_name="GAF"
                     /note="GAF domain [Signal transduction mechanisms];
                     COG2203"
                     /db_xref="CDD:441805"
ORIGIN      
        1 miyngqeief paimqlsfvk lienlenqae ssndieaaha knilqvvgky palkdgitne
       61 edfdkynegi qllgkllfpe vlstneikil appfyfkpli tskrfdsiik asgkpfsftf
      121 knisknefyl fccnfilgky ygypvngsgs qmfeilneqq glirtfkmli nadmcefipt
      181 dkavditded feelinnfed ielwkkkfpp nswilrgini vnlmdmtteq aigaitsnli
      241 vkthdsfeki qwgirkifnn aalsigvlll egdqlvtfkk egmysilldk gnmlncstel
      301 cnysygklie nkqpliitnv dkfhntmqsg lsnrlmasdi ksymviplvh ddeflgyiei
      361 gskntydlhq gslkslekvl pmlamaqkrf kteaqnliea iiqqecttih pavkwrfeee
      421 akqfmfkryn geqpvfkdii fnnlyplyaq mdikgsssrr nkavstdlck qlgevkkils
      481 siskqtdmti fdelicrtdt yikelhlela agsehkilnf lksdiypvfe yfekidsklk
      541 eqieeyrsfl dpslqtvyee rkkydssvny inqrlasfid nkqteaqkaf phyferyktd
      601 gieyniyigq sitknkefdd iylrnlrlwq livmcemele fkkiqkeldt tieiaslvlv
      661 yntpisvhfr mdekkfdveg aynaryeiik krvdkahikd tneritspgk ivivysqeqd
      721 akeyltylhy lsqkgyvkee iedlaledlq gvhglralra evvynnpitv delitemqrg
      781 nin
//
LOCUS       WP_284686128             542 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Chondrinema
            litorale].
ACCESSION   WP_284686128
VERSION     WP_284686128.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..542
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=60532
     Region          3..394
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mskrdynvff nthtvsgivi siglyviffa gafalfmeni dhwetnepke tadaiidydg
       61 liaevaskgy dmhgrtflin ghgeninins rplrdstlvs ssldilpdsv akgpikleln
      121 annyaaskan kekkqkaelg nflfdlhyfn qipvvgiils glvslfflfa iisgiiihwd
      181 kifsnfftfr lkgsvknlwt dahtalgvig lpyqlmyalt gtvfgltill ffpyaqvlyg
      241 gsqqamlaev fpapatqsye lhgysessva inplveqtva qlsqesskhi svsiknfhdk
      301 nahlivgiin dqkssffntv esiylladgk lirekkaddl ppyavgmvef lhkihfgqyg
      361 gnfvkliyfl lalltclvii sgvmvwlkar ntkkylakqk fntnvgaiyl gvclglypai
      421 allfilsktf pvemenrfii iswlflafwv lysvysyrik nyflinrnal ilsgtfgiai
      481 pifngfhsgl wlwkslslgy pdtffvdliw llsgaitllv avklrspqpe kvrkkvavaa
      541 vn
//
LOCUS       WP_284686136             173 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Chondrinema litorale].
ACCESSION   WP_284686136
VERSION     WP_284686136.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 173)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 173)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 173)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 173)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..173
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=19966
     Region          <29..167
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 msfswsnyww iinrtfvlgs ipfsffilid ykrrdvinke lalnmlnekt etkqtpkigi
       61 hsivtdlkne iftfedrdfs yavaegnytd fyfsgkgeln svtyrislss fekqinssnl
      121 qrchrsylvn ldkvinisgn aqglkltldd ntseipvsrk yismikasll kkf
//
LOCUS       WP_284686226             292 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284686226
VERSION     WP_284686226.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..292
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33515
     Region          53..292
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 menkntrsvs efntelklkg fnifqiekdg natkvysrkd fykiclttgk siihyadrsf
       61 eandtilffg nphipyswet vsstyvgytc lfsedflaps drseslqqsp lfkiggtpil
      121 kitveqrefl nsifrkmiee qqsdysykdd lirnyihlii healklqpse nfdqhknass
      181 rltsvflell erqfpiespe aplklrtaqd yasnlsvhvn ylnravkevt gksttthite
      241 riaseaksll qhtnwniaei afalgfeypt yfnnffkkit getpksirtq aa
//
LOCUS       WP_284686225             379 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284686225
VERSION     WP_284686225.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..379
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=43708
     Region          164..379
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mepnkavaim egmvsrtlks iyflwpfsii ssivliiicy fasiedleif pktqdynydy
       61 ytdlenggss qvinhivsds lltldfklee gfespyagmi itasnkkyid aekyneiqln
      121 isgknidrvg vafytpplsy vkynsqdetl hhsylnisss pktysipftd fehpewwedr
      181 hhipegleea psfnniihln intaftpsid kvkaieirsi tftrnnqvlf lkliaayiit
      241 itlffcillw lnarkkddst iaisykpiei seevngeekc iefinqnfqn selsldlvak
      301 etgiaqrrit nyingkynct fksyinkiri seakrllnes klnigeiayk vgfnnqshfn
      361 rvfksemein pteyrinhh
//
LOCUS       WP_284686303             349 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Chondrinema litorale].
ACCESSION   WP_284686303
VERSION     WP_284686303.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..349
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38997
     Region          95..334
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mkllkltfki lsvlllsaal ilgsiiassi slskelqfes veetkerfgn fkegeiikke
       61 kvgfikhlvl staglfikry kalekvniys iayksdgliv tgimltpkka gnfpciiynr
      121 ggnrdagrls fnqlnkfmap yaaegyvvia snyrgnsgse gkeefggadv sdilnlipal
      181 sqvekadtsr vgvlghsrgg mmtykalqnk evfkaaavia gsanlyktis lrpdmekyvy
      241 aeiipafyen rdelikdrsv vywpeklsat pllilhgtgd krvsydvade lsnkldslnf
      301 pykfitftgd nhvldknrfe aqsqimdwfn kylrdlkpys esekrvtyp
//
LOCUS       WP_284686102             231 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Chondrinema litorale].
ACCESSION   WP_284686102
VERSION     WP_284686102.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 231)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 231)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 231)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..231
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=26641
     Region          3..225
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mnpyktivid deplaidvit hylkrfsnfe vvgtftdsve afnylkrnqq vdvvftdiam
       61 peisgielvk ltaeptkfim ttsysehave sfnlevidyl lkpisferfa kalnryerls
      121 kstidegssf fvkdgddfik illddidyiq glkdyakivt gnnyclvlkt lksvevdlsa
      181 ynfmrihksy ivplnkirqy ngkcvlinnv eipvgsryrd dlkkyfqsnr f
//
LOCUS       WP_284686329             391 aa            linear   BCT 25-DEC-2024
DEFINITION  ParB/RepB/Spo0J family partition protein [Chondrinema litorale].
ACCESSION   WP_284686329
VERSION     WP_284686329.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..391
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45136
     Region          53..275
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mddisgkwmk manktaskte tlskisekqs esrknyvkls slvteekyer yirkhtkeey
       61 ealskaiaqd gkirdpltvk lvegeldrer tfividghhr lraakellee grlefekvpi
      121 tiekfandqe ifvwmlrhql grrnltpfer aeigfritsf letlaqdkkk hkkvdnklls
      181 kwikapetdk idyaevvsdl tgvprttiir akklhnqadd elkgliragd isiskayqql
      241 vdvekqlkke aqirqraedf qqalfsikei enflkpklil navgknakss vrinllertn
      301 esllfalied dqieyvrvfy nlpkqstsaa fanrniyilh ensklktskk dalltinpeg
      361 viameqkste iyelepmqel emlrkavsss r
//
LOCUS       WP_284686339             413 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Chondrinema
            litorale].
ACCESSION   WP_284686339
VERSION     WP_284686339.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..413
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=46865
     Region          15..382
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 meseikkknw ashqrnwygk whvwlgliag siifivsitg tilvyrdeid malnpeifei
       61 dkgkehlsfq kivsqlktdh pgwepififk sesgpnypyr lilgddkekq iyvnpfngev
      121 tgarihdshf iglvteihrt llipvvgryi vgisalilvi ltisglrlwi pkqwkhlksr
      181 htikrkaslk rqnydlhqvl gfyfapmvtl ialtgvvitf lnilapimfl lsfeppksle
      241 qimssksvye egyktipids vvaiaetaip dcevvglglp mkkdtakvft aytespyvte
      301 tgnnnfmyid qysgkinfnt nsdlpntgkm ylnwvtpvhy gtfggnvtrv lafiatlipp
      361 ilfitgiviw lprwkgkkkr kansdyskgn vqrrmnaipk pvisnrkken ves
//
LOCUS       WP_284686442             244 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Chondrinema litorale].
ACCESSION   WP_284686442
VERSION     WP_284686442.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 244)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 244)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 244)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..244
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28207
     Region          1..233
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mitclivdde qgainilkey iertpflkli etttnpmevl qlvnnhqidl ifmdiqmphl
       61 tgidlikmlg gkckviftta ysefaiegfe yealdyllkp ipfqrfltaa qkalnkdifn
      121 mpdwqpeene ddyifvkten kgkmvkvnfk dityveglkn yvsiytsdge rvvtllnikd
      181 lkarlpekkf mrvhrsyiva ldqikavdgn qillynmkay lplgdtyrqp ffevlkekim
      241 ggkk
//
LOCUS       WP_284686466             232 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Chondrinema litorale].
ACCESSION   WP_284686466
VERSION     WP_284686466.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 232)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19271407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..232
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26867
     Region          13..>73
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cl00447"
                     /db_xref="CDD:469772"
     Region          46..218
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mdskkycyey prpsvttdcv ifgfdgvdln illiergiep ykgkwafpgg fvqmdesaee
       61 gakrelseet gikdvfieql ytfsdvnrdp rgrvisiaff alvktsdyql lagddaikaq
      121 wfkikdipal afdhdlilri aqnrikgkir yqpigfelld kkftmpqlql lyesildvkf
      181 drrnfsnkmm ktglltqlne kmenvphrap rylmfdkkky nelqssgfnf ei
//
LOCUS       WP_284686467             290 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284686467
VERSION     WP_284686467.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..290
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34429
     Region          <201..283
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mfdsykhfle tpgyhkiige dylivefkcp ikeelfdaws echsviyvln gqkkwitpsn
       61 eflvkedqsi fvrkgafknq qyfeesfcvl mffmkddfik rcmdsdieke mtalqrvdhp
      121 efiyrinvee slrvlyhsff sylkqpqeip qkiielkfre mlmnicldpg nreiknvlyt
      181 lasnsgytie qvmeeqyiyn lkveeyarlc gksassfkry fkkvydttpa kwlqtkrlnl
      241 arelllstdf tvqeicydcg fesdshfirs fkaeygvtpn awrvsktqtv
//
LOCUS       WP_284686529             186 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284686529
VERSION     WP_284686529.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..186
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=21676
     Region          <94..180
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mmlyikymvs lrckmmvkae leklglhyvv ldlgvveile niskhqydkl kinllksgle
       61 llddkksilv ekikniviem vhysdelpkg nysdfisekl nydytylant fsevkgitiq
      121 qfiilhkiek vkelllynel tlseisyrln yssvahlsnq fkkitgltps ffkamkkkrr
      181 nnlddl
//
LOCUS       WP_284686534             320 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284686534
VERSION     WP_284686534.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..320
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=37511
     Region          80..320
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 miaillyalp sgrkkqnlpl cffllltalh sltdltidsp lfgsakihlv vgpfiflyap
       61 llyfhycrlf dveikkvesh faifgiflvy hllwgfshti ffavfsmqyl yysiwigrlv
      121 kirqkekpik riwilfitys fglvwlfais anvfsqlnye plaswtelia yisavilfcg
      181 fiyftmsqps lfmqvrvavs nqiryeestd rrvkkqmltl telltkekif sdpelnreil
      241 aqklgmdvqq lskeinqhfk mnlselinqy riseakillq nqelnikeiy yktgfqsrsa
      301 fnnafkkqte ktpseyrktl
//
LOCUS       WP_284686651             191 aa            linear   BCT 25-DEC-2024
DEFINITION  chorismate--pyruvate lyase family protein [Chondrinema litorale].
ACCESSION   WP_284686651
VERSION     WP_284686651.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Meganathan,R.
  TITLE     Ubiquinone biosynthesis in microorganisms
  JOURNAL   FEMS Microbiol Lett 203 (2), 131-139 (2001)
   PUBMED   11583838
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Siebert,M., Severin,K. and Heide,L.
  TITLE     Formation of 4-hydroxybenzoate in Escherichia coli:
            characterization of the ubiC gene and its encoded enzyme chorismate
            pyruvate-lyase
  JOURNAL   Microbiology (Reading) 140 (Pt 4), 897-904 (1994)
   PUBMED   8012607
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Nichols,B.P. and Green,J.M.
  TITLE     Cloning and sequencing of Escherichia coli ubiC and purification of
            chorismate lyase
  JOURNAL   J Bacteriol 174 (16), 5309-5316 (1992)
   PUBMED   1644758
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..191
                     /product="chorismate--pyruvate lyase family protein"
                     /EC_number="4.1.3.40"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0008813 - chorismate lyase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006744 - ubiquinone biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22038
     Region          21..175
                     /region_name="UbiC"
                     /note="4-hydroxybenzoate synthetase (chorismate-pyruvate
                     lyase) [Coenzyme transport and metabolism]; COG3161"
                     /db_xref="CDD:442395"
ORIGIN      
        1 mnwrylqine lnnipykeln wltrpyilsk aiknvsvsfk vhllsqgngn lipddllnsa
       61 nnssnngfir qvflcgndip wvyarvaipn etlinhsnff ndldtrpige tflynnpkvs
      121 rslfqvksft radeiyqlal ctdgkkikpe klwgrrsify leespftite vfleeiplyt
      181 pitdslrpsd f
//
LOCUS       WP_284686698             291 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Chondrinema
            litorale].
ACCESSION   WP_284686698
VERSION     WP_284686698.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..291
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33348
     Region          33..288
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mktktqrnfl illlfsalyf isfqgfsqsk fggatlytvr aemdkapeet lqeianigyk
       61 yieatgykdg kfygmepkef kkflkklklt pvsthmgaat ldnadefiad akaagfkyfv
      121 ipvppmghfk fdpetrtmym sddiefvtnf lttvgkkckd agmellyhnh dfefkedkng
      181 ivpiehflkn tdpeivnfqm dlywvtkaga dpveyfekfp grfkmwhvkd mdeegkfapv
      241 gtgtidfaki rekkelsgmi yyiveqdqtf elapleaiki shgnlkkfgf k
//
LOCUS       WP_284686793             417 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Chondrinema litorale].
ACCESSION   WP_284686793
VERSION     WP_284686793.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..417
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45294
     Region          1..>407
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mgiftivsil tvlsaifafi ntrflklpft iglmimaial tfavlalgav npviledska
       61 liqsidfeti lldvmlsfll fagalhtkld vlrsykapia lfstlgvlls tflvggmmyf
      121 ltnslghqvd fiycllfgal isptdpiavl gilkeakapk kleikivges lfndgvgvvv
      181 flvifnmask gidaisftdv vllfaeevgg givlglilgw vgfqlmriid hyetevmitl
      241 alvmggysla sflhfsgpla ivvaglfign wspqaawsdt tqnyvdkfwe lvdvflnail
      301 fvligfelli itidteyilf gllaipvslv arylalagpi avfdkkldfi pktnmimtwg
      361 girggisial alslepqmqr dffltityti vvfsiigqgl tlgrlvksvl nknniev
//
LOCUS       WP_284686865             556 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284686865
VERSION     WP_284686865.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..556
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=63451
     Region          25..358
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrllksklsl lllgmlhlyi ctrsfaqqtp eailkkadsl lnnfnydapg tavfavkdge
       61 viinkaygla nlehkvpitp ntafdlasvs kwftafvvsl liekgdikpe ddirkyipkl
      121 pdygdtvtis hllhhtsglk nfitllpiag wsfddritfd qvlnlvytqk elefkpgsqy
      181 kysntgylvl aelvqkvtgv sfrewtikni feplementq fvdnysviip nrassyydns
      241 sgmefqvspn nyavpgpssl ystandlikw lkfidhhpdt lntvferift pgklndgtei
      301 shgysvlirn frntkrishq gywfsftsll vylpeyhlsi gvlnnyaign ykvaheiasy
      361 yipaiqkknp iaqedtveav lpealedyvg tykinsanyv aimqkgnelw mqqtsdypll
      421 mtaigndkfi vkdnrdqlmt fhrnelnqvt hitvngkecp lmeknhydpd nlqeytgdyr
      481 gediktiysi vyeddtlklg hirmgklslq niwdddfqil ggnrwfastl efirddcgei
      541 tgfnlsehsf lkvnkd
//
LOCUS       WP_284686916             349 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Chondrinema litorale].
ACCESSION   WP_284686916
VERSION     WP_284686916.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..349
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41192
     Region          11..348
                     /region_name="WecH"
                     /note="Surface polysaccharide O-acyltransferase WecH [Cell
                     wall/membrane/envelope biogenesis]; COG3274"
                     /db_xref="CDD:442505"
ORIGIN      
        1 mnnntiapsl skkkilldih yfrafailci igihvhsqvk wndneilgni ikvllenstf
       61 yfvfisgflf qhlskkfefk dflekkfkyv lqpylifsip iivgriilnr hapfaleyds
      121 nfenlsifeq fffyvitgsh lrpfwfipll vffyvcapll nkidkkpqly wflpivllfs
      181 fyfergnlyq lprnflhfvp iyilgmfasr nkktiyaflk khrkslvfat ivsfyyafie
      241 menhsfylqk listflifsf fhsfskhink kiakiidfva vysfglffih difevllkhi
      301 nlhlfkfhdi isgfsglvil yitiivasit ilyllksiig kgsrkfigv
//
LOCUS       WP_284686939             277 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284686939
VERSION     WP_284686939.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..277
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32133
     Region          <175..251
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mraiakdtks rilkeqfipd hvfiyiakgg isffdgnkty ilnagdgcia rknqlakfil
       61 lesedefepi ifcfeeaflr tfqqkhktqs ssfktndafi eirktdlmdn filslkpyyk
      121 gimeldeafq dlkyeellii llkqdpdlaa vffdfgipek inleafmnkn fkfnvsikrf
      181 afltgrslss fkrdfkaifn dspshwlvkr rlqeayllie qknekpsdiy ldlgfesish
      241 fsvafkkclg chhqslllkn esvkshipyr qnslsls
//
LOCUS       WP_284687112             173 aa            linear   BCT 25-DEC-2024
DEFINITION  peroxiredoxin family protein [Chondrinema litorale].
ACCESSION   WP_284687112
VERSION     WP_284687112.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 173)
  AUTHORS   Schroder,E. and Ponting,C.P.
  TITLE     Evidence that peroxiredoxins are novel members of the thioredoxin
            fold superfamily
  JOURNAL   Protein Sci 7 (11), 2465-2468 (1998)
   PUBMED   9828014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003123
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..173
                     /product="peroxiredoxin family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19545
     Region          27..164
                     /region_name="Bcp"
                     /note="Peroxiredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG1225"
                     /db_xref="CDD:440838"
ORIGIN      
        1 mkfylilafs fltlavsaqe lkvgdtapdi imkdvngqei klsslrgkvv lidfwaawck
       61 pcrmenrnlv kvyeeykdee fdngqgftif svsldnkeap wkkaiandnl vwehhvsdlq
      121 gwdnaaaqly qvrsipqsyl idgsgkiiki nprggalers lkkvtkssgf wsw
//
LOCUS       WP_284687199            1156 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chondrinema
            litorale].
ACCESSION   WP_284687199
VERSION     WP_284687199.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 1156)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1156)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1156)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1156)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1156
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..1156
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=129265
     Region          141..1155
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkllrqfl kmsgfalggf iiqclcftvl faadtnaqkv sigeiyvkmd ggkkeiksvf
       61 nelerktafy fnfdektidd lqkvqmassv kslkavltdi asqsnlsfkr iddniyvikn
      121 kksntlpekd elvqevlqmr itgkvtssed geplpgvsii vkgtnvgttt dvdgnyslna
      181 nsgttlqfsy igfasqevai dnqsivdvll apdleqleev vvvgystqkk ttltgavsvv
      241 knddivrtkn enilnsltgk lpgvrivqks sapgaydtri dirgmgnplf vvdgivrdqd
      301 yfarmsaeei esvsvlkdgs aaiyglraan gvvlvttkrg viqdgkvdvs fnssmsmqef
      361 lyvpesvgai dymtlsnern wqdfgknylv rtnplftddh fepyyngtkq synwfdqvfn
      421 rtspqynhnv svnggsekfr yyftlgynkq igayksgdyy sdrinmrtni esqitkrlna
      481 kvslgaimlk tsqpngtgwt tykltwltrp daafyandnp eypngdsqyl neganmivqt
      541 dddyvgynls kdrryngtlt lsydipgidg lsakgvydya tnlpdftsyk raynlfrynp
      601 dddtyssivr ntpsditrtv nmsystnmql glhydnsfgn hnvssfviye dryntwdsys
      661 ayrellvdse ylfagedknq rategeiadr asksllgqln ynfmgkylld lrfrydgssr
      721 fpegsrfgff psisagwrls eesfiknnlp vlsnlkirgs ygemgddssa gnyppttgys
      781 ldgnnygwfy ggtltggvta ssipnpnltw ytiksydlgl dfgffnnklt gvidiyrrdr
      841 sgllatsaav ipgtvgaslp qenlnsdrnf gyeislqytn eirdfnyyvs gqlsatksmr
      901 tdwletpagn sydkwrnrss gryndiwwgn esqsmissye diqnyglpla qstlpgdwvl
      961 ndwngdgvin gnddhpiasy glpvfnygvs lgasgkgfdl aldfqgaygv yvqyaevlte
     1021 alpfggqntl twfldrwrpv dpnadyfnpn tewisgyypv tghdgrrtgt ngiqnasyir
     1081 lktaelgytl pekwmskinv snfriyvsgy nlltftglen vdperpgasg gsstsnidfy
     1141 nypvnrtytv gaslkf
//
LOCUS       WP_284687273             233 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Chondrinema litorale].
ACCESSION   WP_284687273
VERSION     WP_284687273.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 233)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 233)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 233)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..233
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=26589
     Region          3..226
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mrinciivdd epasrevlek fisdcptltl lqscknafea sdainqfdlq lifldinmpk
       61 lsgikfyksl vnppfviftt aypefavegf evdaidyllk pfpferfyka vnkasetiis
      121 ksseskpqef ilwkadkkih rvlldeinyl eaigdyvkvq fadksimvhn tfqkllaqlp
      181 dnkfvrvhks faialhklet idgnriilkg ksipigqtyr tdfmeliknq gls
//
LOCUS       WP_284687283            1042 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chondrinema
            litorale].
ACCESSION   WP_284687283
VERSION     WP_284687283.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=113644
     Region          28..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkngllhlli aclsmlclsq qafsqddvvt gtiisaedge pvigasiqik gttsgtitdi
       61 dgkyklsrvp sngvlivsyi gfesqeieva grnqidisls tdiqqleeiv vigygqqkks
      121 vvtgaitsik aadletlpin nvgqalqgrt sgitiasnng qpgsgatirv rgitsfggsg
      181 ndplwvvdgv vvdnggigyl nqsdiesiev lkdaasqaiy garaaagvvl vttkkgksgk
      241 lnvnysgyyg tssparrlnl tnateyatlr nessiaaggg vvysdpqalg egtdwqdqif
      301 nndarrqnhe lsisggnevs tfhmsfgyle qdgivateis qykrvnvrln sthkltkwlt
      361 vgenvgyahn ksiglgntnn efggplssai nldpitpaiv tdanlansal ylnnpvmrdd
      421 fgrpygispy vgqeitnpla ymqtrlgnys wgdniignvf aelkpieglt lrttlggkla
      481 fwgdesftpi fylnsstqnt qtsysrgtnr rydynlenti sysrkfgdhd ltllvgqgay
      541 rdnntynvnl qvfgipvdnf ddaslnykvp ptsenadgye npahtvsslf srvtynfkek
      601 ylltallrrd gssrfgnnnk ygvfpsaslg wvtsaedfwp qnnvvtflki rggygvvgnd
      661 nigdfaylst ispgrnytig tsgeytigys pdapsnpdlk weetsqtnig feaslfdnld
      721 vtfdwykkvt tgllmnprip gyigaisnpa anvgdmentg lelelsyrks igkldltvsg
      781 nvshlsnkvt ylgegieyre ddqqtfqast ypitrvalgh alhsfygfkt qgifqneqdi
      841 qnhlnsegql iqpnaapgdf iwadlnddge itqedrtfig spipdwtygl tikanyknfd
      901 ltifgqgvag neifqglrrl diansnyqad algrwtgegt sndfprlidg dpnnnfsnps
      961 dfylqkgdyf rlkniqlgyt lpstlvskig lqktrvyvms enlftltnyt gydpeiggnv
     1021 msidrgiypq arsfmvglnf sl
//
LOCUS       WP_284687383             179 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Chondrinema litorale].
ACCESSION   WP_284687383
VERSION     WP_284687383.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..179
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20819
     Region          90..174
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 minqivvrki dvteveklke vgiltftesf ahlntesdmk qyldksfnna qilselenpe
       61 sdfyfaeing evvgylklny gkaqteqklq nsleieriyi lakfqgnrig qlffdkalev
      121 anarkaeylw lgvwehnega lrfykrngle pfdkhvfwlg edkqydilmk mplkaeqis
//
LOCUS       WP_284687437             334 aa            linear   BCT 25-DEC-2024
DEFINITION  fatty acid desaturase family protein [Chondrinema litorale].
ACCESSION   WP_284687437
VERSION     WP_284687437.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..334
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38906
     Region          38..301
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mtinnnvsep nrlrtgkeli laskeyanei perswyctls tllflilafa gtyinfhwtl
       61 tlgfsllsal livrffvifh dyqhgailrk sklakiimti fgvfvmspas iwkrthdhhh
      121 hhnsklsnng vgsypllcke kylkltqser yiylakrhpl tiffgyftlf ifdfnikpif
      181 ksfsnhwdsl vallfhftva wliysyagmh glifswilpf fiahgfgayl fyaqhnfpea
      241 sfeqnmdwsy snaalnstsy lvmgttmnwf tgnigyhhvh hinhripfyr lkeamkgmpe
      301 lqnpktttlh prdiinclkl kvwdsekkqm vtsv
//
LOCUS       WP_284687495             150 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Chondrinema litorale].
ACCESSION   WP_284687495
VERSION     WP_284687495.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..150
                     /product="YybH family protein"
                     /calculated_mol_wt=17186
     Region          20..144
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mkifklitvl lvllflfnva naqeadikan geemlqalnd gnaekymkyk hpsfsqylpl
       61 slelasrpdt kviqtqfdeg rdfdftltdh evkvygncav vtamqegtih fedgridtgk
      121 wkhtslwvke nnewlqvhmh vskvqdeqpe
//
LOCUS       WP_284687503             371 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284687503
VERSION     WP_284687503.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..371
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=43295
     Region          <248..366
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mevpiiyigf aqalftilif llkrpfkiad gllcvlllav tcmfllniiq yqlhiqndtw
       61 ifslsisfvy paslylysky ltkeieqfkl sdllhftsti llvlaliiyg fggksdflsn
      121 lvqynkqlwl rdilgycylf flwfygilal knvkqfrski keiysyksas inliwlhvlv
      181 isflivynii vvisilnnyk ivtqyidltr dvsllvyvym vsiwgyqqkp liketeetat
      241 gkyqksglkd eqanehlkkl idfmeeteaw kdneltvakl alqtkipkhh itqvlneelq
      301 knfftfvney rvehakemis saqyqsftfv giayecgfns ktafnnffkk htemtpseyk
      361 ksvsqklekg m
//
LOCUS       WP_284687504             254 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Chondrinema litorale].
ACCESSION   WP_284687504
VERSION     WP_284687504.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..254
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28984
     Region          1..250
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mkiviiedek ltandlasti keydeqieip ailssvkeai ryfeqekepd lifsdielgd
       61 glsfevfkst glqvpvifct aydeyalsaf nangidyllk pftlstvgaa ldkyfritqq
      121 kqspitpqfn kviqllenre teppstilvh ykekilpikl qdiaafylen qivhlitfdk
      181 kiyfpsksle elekltskyf frtnrqslvn reaivdvsnr lgrklwvnlk vplndsvtvs
      241 kekastfldw lsgs
//
LOCUS       WP_284687606             359 aa            linear   BCT 25-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Chondrinema
            litorale].
ACCESSION   WP_284687606
VERSION     WP_284687606.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Rengstl,B., Oster,U., Stengel,A. and Nickelsen,J.
  TITLE     An intermediate membrane subfraction in cyanobacteria is involved
            in an assembly network for Photosystem II biogenesis
  JOURNAL   J Biol Chem 286 (24), 21944-21951 (2011)
   PUBMED   21531723
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Komenda,J., Nickelsen,J., Tichy,M., Prasil,O., Eichacker,L.A. and
            Nixon,P.J.
  TITLE     The cyanobacterial homologue of HCF136/YCF48 is a component of an
            early photosystem II assembly complex and is important for both the
            efficient assembly and repair of photosystem II in Synechocystis
            sp. PCC 6803
  JOURNAL   J Biol Chem 283 (33), 22390-22399 (2008)
   PUBMED   18550538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..359
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=40630
     Region          42..239
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          162..339
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
ORIGIN      
        1 mkllagtskg lviyerksgs welldiqftg fpvsmlfvde rngywwvgvs hrhwgqklhy
       61 stnegkswet vptpsykdye yrpgkkvplk kiwvmqgage dkpgclwlgt epgglfysdd
      121 ngknfelveg lwnhpsrmnd mewfgagkdy pfihsivvnp qnsdhvyigv scagvfetkd
      181 agknwipknn glraaylpnp kaevghdphl llmnqdnpqv iwqqnhcgif ktddagenwf
      241 dvsgkdqfpy ygfglaiged ektawvipae sdekripkdl elavyktvda gkswqaqlng
      301 lpkppvfeiv lrhsfvrkdk tlafgtnngn lylsdnkgen wfnlsnhlts vnfllltkk
//
LOCUS       WP_284687545             247 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Chondrinema litorale].
ACCESSION   WP_284687545
VERSION     WP_284687545.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..247
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=27992
     Region          133..161
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(134,137..138,141..142,144,168,171..172,175..176,
                     178..179,202,205..206,209..210,213)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          141..247
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Region          166..196
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          201..226
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 meepskerli qdylngtlti ekkaliekel eedaefaaev kefetletgl hsigvdafke
       61 dmlqwekeyq qkqkptgkii kfwpgylava atillllvag lflyntesdn nalyashfva
      121 yedmiisrge aspesllitg meaynneefa taseklngyl vkntenkgva lylgiaqmqi
      181 gkyteaassf nmaqqdlkfk qqaqwyeall yikseqldka ksllqqiskd tqhykseeav
      241 eileeln
//
LOCUS       WP_284687714             241 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Chondrinema litorale].
ACCESSION   WP_284687714
VERSION     WP_284687714.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 241)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..241
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27985
     Region          7..>237
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 maedkprlar ltaiitqlqs krlltareis ekhkisirtv yrdirtleqs gipivteegk
       61 gyslmagykl ppvmftedea halitaeqli lknkdqslae qyqnavtkvk svlrfnqqtk
      121 aelisqrlqv rnneanekts nyliklqsti annlivkiny lslenqqner liepfalytt
      181 qdnwiliafc lkrndfrafr ldriqnlqit nqhfephkit lqeyldqcre kykptpdipl
      241 t
//
LOCUS       WP_284687583            1020 aa            linear   BCT 25-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Chondrinema
            litorale].
ACCESSION   WP_284687583
VERSION     WP_284687583.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 1020)
  AUTHORS   Rengstl,B., Oster,U., Stengel,A. and Nickelsen,J.
  TITLE     An intermediate membrane subfraction in cyanobacteria is involved
            in an assembly network for Photosystem II biogenesis
  JOURNAL   J Biol Chem 286 (24), 21944-21951 (2011)
   PUBMED   21531723
REFERENCE   2  (residues 1 to 1020)
  AUTHORS   Komenda,J., Nickelsen,J., Tichy,M., Prasil,O., Eichacker,L.A. and
            Nixon,P.J.
  TITLE     The cyanobacterial homologue of HCF136/YCF48 is a component of an
            early photosystem II assembly complex and is important for both the
            efficient assembly and repair of photosystem II in Synechocystis
            sp. PCC 6803
  JOURNAL   J Biol Chem 283 (33), 22390-22399 (2008)
   PUBMED   18550538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1020
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..1020
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=112748
     Region          65..251
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          231..388
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          513..702
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          <913..>1016
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
ORIGIN      
        1 mkrhgttire tlkllfagfl inllgtasif aqsvttdqlk gldfrnvgpn rggrattatg
       61 viqepgtfyv gstggglwkt idygnswhnv sdgyfttpsl gavsvapsnp eivyagtgsd
      121 glrsnvitgk giyksndagd swefiglekt ghigavevdp knpdrvfvaa igngfvpnee
      181 rgvyrtldgg kswdkvfyls dtvgssdlef apdnsqiiya gmwhgqrkpw tiisggtegg
      241 iyksadggdt wkklenglpt gligkidlav saaapevlya lveapegvgg lyysedrges
      301 ftlvstekgl ldrpfyycnv dvnpqnpktv fvsatrffhs edggknwtni rtphgdnhgv
      361 wihpndttlw vqvndgganv trdasenwst qfnqptaely qvevddqfpy wlyagqqdny
      421 ttiavpslpp fgvqagsnsy iintggcetg pavpkpgnpd ivyanckgrf gvfnkktgqe
      481 mqyyvgasnm yghnpkdlkf rfqrvspvhv sphnpdvvyh asqylhktvd egktweiisp
      541 dltaftpetq visgspitrd itgeefysti yavkesiike geiwvgandg pvhvtkdggk
      601 nwdnvtpkdl lpggrvqtve psphkegkay faiyryllgd fkpyiykted ygkswelltt
      661 gsngipsdyp arviredtev egllyagtdy glfisfddgk nwlpfennlp ltpvtdikih
      721 qgdlvmstmg rgfwilddiq ilrdlkngvd kntpqlfvtn eayrlryrdt dsesvpyfpe
      781 pgltidyylp sntdvaieiy ddannlvqsf enkvaaakek gernmsteft pfgagltlse
      841 tagahrvvwd mrhvgpwstn krrsgnggpm vtpgkytvkl iadgkevsks teikidprva
      901 eggvttadle aqeeltlkvr elltnvrkle ntvnmkvegy keakrvkkke kqtieeiesq
      961 lttvsgryet pmlsdqtsyl ynmleradqk pgkdaydrye elkkeyealk eqglnylgsk
//
LOCUS       WP_284687760             689 aa            linear   BCT 25-DEC-2024
DEFINITION  GumC family protein [Chondrinema litorale].
ACCESSION   WP_284687760
VERSION     WP_284687760.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 689)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 689)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 689)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..689
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..689
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=78878
     Region          9..>553
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mllekvlvif kkfwkfkiwl igipvlsgal vffltrnqer kyiskatlqv smptsgdvsl
       61 igrefkqyea slfffdliev insrkttemv rleilkkyme geyqffsfdd npelredsvk
      121 iynrakelgk eynllnlsds ldigitllle nnrlsikemq gqlnasrvgk snyvdikyec
      181 enpykaayit gcyiniitqq ykvlsqkkie dnrerlevlv dnakkeldsk isqlenfkie
      241 nniinlpeht kaivnqvvnm evklahlket ydahdkaaei vkknlqnags fnfndisnkt
      301 iaslkdslrn vsesllffeg deiekqelet kvehlkneit aqiitmldkv pydpsqarqe
      361 lmsrligyei dkemessmle svenelekln lyaakfaple sslstytsei hiaqeaylil
      421 lnklnlvrti eqgsgdvkit ifsppilpre pesskrafai vgaciasfil iaagivafvl
      481 ldkrvystsy ftelttilpf isindksdni heikrlrkki sdlpnelrti liiglsekdi
      541 dnsfleslmq slatfpgnql mlnatgsekt iegydssnlp ekieqiqepe dsknyvinid
      601 nktspfekhh pefwqeytqk slisrkciii aappallssd weewlstaha filvrmggqg
      661 mtekdkdiir siytheksfq atvfiekeq
//
LOCUS       WP_284687797             226 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Chondrinema litorale].
ACCESSION   WP_284687797
VERSION     WP_284687797.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13031027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..226
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0030488 - tRNA methylation [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25764
     Region          18..184
                     /region_name="SpoU-like_TrmH"
                     /note="SAM-dependent tRNA methylase related to TrmH;
                     cd18092"
                     /db_xref="CDD:349965"
     Site            order(115,117,137..140,143,157..158,160,166..167,169,172)
                     /site_type="other"
                     /note="SAM binding site [chemical binding]"
                     /db_xref="CDD:349965"
ORIGIN      
        1 mnrkdiiiek lkkhigekra rrineviqqr tnlirvvied inyernagav lrtcdcfgiq
       61 nasiiekyyh ewvthliakg aekwvdidrf dtpktnntla cieklkqdgy lvvactphnp
      121 ditlpdfeit kktallfgce edgltndaln nadlklsvpi ygfaesfnvs vsaalilqdl
      181 vtkmrksnmq wqlseeerkd leivwlvram grpgqlilkk iqaevl
//
LOCUS       WP_284687887             525 aa            linear   BCT 25-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284687887
VERSION     WP_284687887.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Pereira,J. and Lupas,A.N.
  TITLE     The VCBS superfamily forms a third supercluster of beta-propellers
            that includes tachylectin and integrins
  JOURNAL   Bioinformatics 36 (24), 5618-5622 (2021)
   PUBMED   33416871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..525
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=59460
     Region          250..311
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          300..363
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          352..421
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mtikifplag lisiilwksf ssftyvqnse tnrdkgqely lrycaichlr pdpkslskei
       61 wrnnvlpama trmgivypgi dplgglskee qevinknhii psqpllsfde wqqlvdyive
      121 napesipvde erltrnlplk nfvahdikle dekpslitsl kynnetktlw fgdyynsvyt
      181 wqypkgiine vktnsptvdf sfdhdktyft eigslyptel stgsfvkyen gnsstllssl
      241 hrpvnsvved ldddgepefi vcnygnrigs lslftkddsd gysekvlfgm pgaincqvkd
      301 idgdgkkdii amfaqgdesv yifyqkdnlk fknkrilrfp phygttdmvl tdynqdgftd
      361 iitvhgdnad ysnilkpyhg irihlnngkg sfnesffypi ygvtkvlaed fdkdgdidlv
      421 ataffpdfne lvdesflyle nidseefkfk synlnrnipi kslalikadv dgdgdmdvva
      481 ghfadtpsrs vpksvddkfh sanygltvfi nqlhkrgess gfpgy
//
LOCUS       WP_284687896             625 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Chondrinema litorale].
ACCESSION   WP_284687896
VERSION     WP_284687896.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 625)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..625
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=71954
     Region          <234..>371
                     /region_name="PRK13560"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:106506"
     Region          <306..603
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mkfntallfl ftsvglilsf rdkptfktln kfvalfilli sgitlteyif kyqsvidnff
       61 vtdrysttyp grmspstafc fflislcfwg ihkkkqkiis aiiqclhlvn ilslisilsf
      121 lllipvksrm fffnsmalht svlffvlsft lllkfnnkgv iglltgehsg nklfrrllpf
      181 iiflpivqny illellsnkl isydfgvvis talflvlciv yistiafgln ksdekktsle
      241 ksltatnqel mqfkyaldqs siiaftdekg iinyvndkfc eiskfkreei lgkthsiins
      301 gyhskdffrd lwktikagkv wigevknkak dgtyywvhts iipfrdensk iyrylairqd
      361 itqrkaieem lasqyvkkle qknkeleqfa yiashdlqep lrtittfgel lhkkyhnqlg
      421 tdankylnfi testgrmrdl vkalldyari ggdkemeevd clsiiksiqq dmipyigetn
      481 ttliinelpk iiafkteirl lfqnlisnai kfrkqdvspv ihissrkvgh ywefaiedng
      541 igidekfnqr ifeifqrlhk rsqyegtgig lthchkivel hggsiwiksk vgegstffft
      601 lpifnekvlh splapdniks sfket
//
LOCUS       WP_284687968             118 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284687968
VERSION     WP_284687968.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..118
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=13367
     Region          <30..117
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 melsttqksh npsllsdfhk fksllnenfi alrqvgeyas lmnistyrln tvctsavrkp
       61 amaiikervl ieaknmvaht smnvseiayn lnfsdtsnfi kffksqtslt pieyreki
//
LOCUS       WP_284687972             362 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Chondrinema litorale].
ACCESSION   WP_284687972
VERSION     WP_284687972.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..362
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40745
     Region          226..344
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mktsiltsll illslaahss piltiefddi ksgniflinv qkeladtlsi kngkvtyeak
       61 iaaptffyli vdgynntrpl elvlssqlte mnfesykvvg entvdeaypn npifisdpnn
      121 niaffeflss wksfyntiqa lsennseeql ekrkntyhtf lsdnkqiiek nsdkyvsani
      181 idfllsnnll qfetlqtyyd llstkvkesy lgfkigeksg kagyfqpgkp apeitlvdmq
      241 gkkynlqslk gksvllhfws sscapcikea pdllklqqgn tenlvvinfs ldtddskwkk
      301 gieragieem invcdlqayn svtaksfdvt fipvyylida ngnislkgtl rqitekiken
      361 mp
//
LOCUS       WP_284687977             311 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Chondrinema litorale].
ACCESSION   WP_284687977
VERSION     WP_284687977.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..311
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35896
     Region          31..264
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mqsqlhiydd gevvnmpdfy esnllndpsl ykagkelkda vniamllgkp llvtgepgtg
       61 ktqlahsvay kfgmdsplif ntrststatd lfyvydaikh lqyaqnqhne vlnddeierk
      121 fihyqalgka iqsgkrqvvl idevdkaprd lsndilnvle dmeftvpevh klyktekakr
      181 pviiftsnse knlpdaflrr ciyihlkfps ednlleivss kienhfyskq elqdyviphf
      241 mvirdtlkkk kpstseflhw vtvlenirfs arnltvfknl sndekqklym tycvlaknee
      301 dvniirefie i
//
LOCUS       WP_284688115             482 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Chondrinema litorale].
ACCESSION   WP_284688115
VERSION     WP_284688115.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 482)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003416
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..482
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54780
     Region          98..261
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
     Region          296..442
                     /region_name="DUF3526"
                     /note="Domain of unknown function (DUF3526); pfam12040"
                     /db_xref="CDD:432281"
ORIGIN      
        1 mqykilllia shfwkdtfks kaiypimvii ylllffaaqs gwqnnrtqne mrakyqqkar
       61 esweanpdkh phrmahfgtf afrlqhplsm ldfgiesftg tavfleahkq ntvnfseasf
      121 stgllrfgel smamilqtil plcifflgfa tvvterengt lkitftqgas wkeillgksl
      181 glmavvqlff ipvllvtlff lllsdahlna dilirfiavf sayfiffail cfitigisat
      241 sqksknalvk llgiwlifvv lmpktsqalg syfhpspski kfkseiedel vrkgdshnpd
      301 dpyfmslkds ilheynvesv tdlpfnyggf vmsigeknss eiynkhfsql ldiyrsqnlv
      361 srfgaiinpy iaiknismal tgtnfvsytd fqmqaesyry nlaqemnelq meyispnkth
      421 gsegkthvig qehweefpdf eyiflsigsv lksevlsils llgwilltvg fiinltktak
      481 vl
//
LOCUS       WP_284688119             121 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Chondrinema
            litorale].
ACCESSION   WP_284688119
VERSION     WP_284688119.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..121
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13574
     Region          17..118
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mrkeqssnfi neqflfqvce lnsavsvisg rwksqivysi sqgnnrfhll lqelpniset
       61 vlarqlkele thailvkqei pdsvpvgvny vltnkgkdlv pileslcdwg ktyaegkeis
      121 i
//
LOCUS       WP_284688126             273 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Chondrinema litorale].
ACCESSION   WP_284688126
VERSION     WP_284688126.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..273
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31950
     Region          1..273
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mfrlshtdfq klsefintys gikmphtkkt llesrlqrrv kelnissfee ycnivfssnq
       61 ksteviklid rvctnktsff reighfeylq khilpemvdn nkkhmkiwsa gcssgeepys
      121 iaiainefrk nnefidyqil gsdlsttilk qaknaiyhes kiedlsieik kryflkgkge
      181 ykgvvrvkpe iskkvmyqri nfmdneypia etfdlafcrn vliyfdrntq ekvikkickk
      241 ikiggyfflg hsestmgmql plkqlsptiy qri
//
LOCUS       WP_284688152             954 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chondrinema
            litorale].
ACCESSION   WP_284688152
VERSION     WP_284688152.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 954)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 954)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 954)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 954)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..954
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..954
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=107321
     Region          51..949
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfyiniikd rvsniylava licfchitya qsvedttqte laetqidsdk vpvaygmqss
       61 kqliaaisyl dgekmaktlt ptlsnslygr lpgltvlqqs gepgydsplm lirgmgtynn
      121 nnylvfvdgf easfdqlsve eiesiavlkd aaalslygmr gangvilvtt krgfdgktki
      181 afnarygwqq ptelpdflgs ydyarlynea atndginapy seadleayrt gsdpflhpdv
      241 nwydqllrks spisdynttf tggnetmkyf vllgymhnqg lyantdperk tnsnadfsry
      301 nfrtnidvni spkitgsldf ggrvedrsfp dyngpqlwqn marypanayp vknpdgtwgg
      361 nsvypdnpva svletgysst hdrnimatir laekldfite gltfrqvvsd nnwhrgvynk
      421 tkdyayyelt vgqtddgrds liylqrgndt dfsvgegsnn dspsyndqyn rfnfqlgldy
      481 nrqwgastvs amllyhqdly eisgnnvpya qqrlmgrvny dykskyfael gfsysgsesf
      541 pegnrfgffp slsaawvise edfldaswvd ylklrasagl tgndliignr faytqdyyys
      601 ggyyfgpnls ysssmiegtt anpnitweks mkynvgidgt lfydkldfsv dlfyerrtdv
      661 lsdgdatvpa ylgvdaayen vgivnnrgfe vdlkysdhig dfnyfvgast fyaknkivem
      721 nevvrpedym yrtgspigsm yglqavgfyq tadfdengdl negipvstfs pvqpgdirye
      781 dlnndgfine kdetiigksn ipaltyslql gasykgfyme lffhgiserd vyvngpyfwa
      841 findnniatn aldrwtpdnp idatyprltt qpnannyrss tfwkrsgrvl rlrnaeigyn
      901 lpekwigkig lsnakifasg vnlftwdeve nvdpealggy pvlksmsigt hief
//
LOCUS       WP_284688171             606 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Chondrinema litorale].
ACCESSION   WP_284688171
VERSION     WP_284688171.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..606
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=69423
     Region          <307..429
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mkkiyliffi pliycinact kseqkptkpq qiafladvhl tnifghlsds eykgienpat
       61 geyviartma sqlhstrifn enyfafiaal dditergikl vafpgdytdd gqavhvrglr
      121 eilkkyeeqy nmqfmittgn hdpvrpfhhe agksdflgeg gknqpifska nmyqinpdtd
      181 fpvvetadia emgykgilde lgsfgftpne nylywstpfs dynvddysfe karkaaelsn
      241 rtyevapgft vpdvtylvep vediwllaid gniyvpkdes gdendpdsyk spslgfnnls
      301 dnkdyliswi skvfeqaetr gktviafshy pmvdfnddas pilklllgen kwqlarvpee
      361 riakvfadag iqihvaghmh indtgirtss egnilvniqt pslaayqpgy kiltvhsdnk
      421 ievetvkids vprfkelfal yeieydflks lgednlwdrs ilevdsyhdf mlwhlkelvr
      481 lrflndwpep iksfiteknl reiagiidve lpneadqffg ydllidfyki rnadllalnd
      541 iseeqlelyq qlikayktve skdelttqlk effeildhfl ngkpadhfmi dlrqgtvkey
      601 lettne
//
LOCUS       WP_284688173             286 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Chondrinema litorale].
ACCESSION   WP_284688173
VERSION     WP_284688173.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..286
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31093
     Region          6..279
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mnwsyqipph lyfvasaifh ylgpsfavll ftrvsvdgva wlrilsaaii faiwrrpwnt
       61 fmhvnikvry liialgvtfa lmnysfyyai dklplgtvaa iefigpvlla ltgtktfrnl
      121 falaltttgv wfltdarieg elegffwafv naicfivyii lahrlssida qtksvdrlga
      181 svifaavmit plgiegalpa ftntvailag igvgisssvi pyvldqlams klsratyslf
      241 vallpatavi igiivlkqip tsveiaavta iisgvlisqd kkqdnk
//
LOCUS       WP_284688233             318 aa            linear   BCT 25-DEC-2024
DEFINITION  TolB family protein [Chondrinema litorale].
ACCESSION   WP_284688233
VERSION     WP_284688233.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..318
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=35817
     Region          <55..>118
                     /region_name="COG4946"
                     /note="Uncharacterized N-terminal domain of tricorn
                     protease, contains WD40 repeats [Function unknown]"
                     /db_xref="CDD:443973"
     Region          95..235
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 mrisftisll llfiqigiaq risskpffgl ndkndsvqml lpdivssiaw etngnfspdg
       61 tifmystgfm wsgnsiifmt lkngkwsdpe iapfsgeyad idpifspdga rvyftsrrpv
      121 nkndpdkgdt nlwyvdvled nfgepkqvsp ainndknqay nsvtkngtiy fhsrdsistd
      181 iyravlkdnn ymvvkldsti ntinneaepy ispnedymif asnrpdgfgg idlyisfnnn
      241 gewttptnlg nkinsmnddf apclssgllk ftsgrmilpw ssfnkknfks lkakmnsadn
      301 qtsniwytnf dlskyenq
//
LOCUS       WP_284688235             227 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Chondrinema litorale].
ACCESSION   WP_284688235
VERSION     WP_284688235.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..227
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26324
     Region          90..227
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mykitllfia llflnisilf aqdkkqiyyd ekgnkisfme fvsiemsgry tsysdsssky
       61 kvewkwians eqqknefisk arvenivads igqtfpgisf ydinnqlynk dslngkivfi
      121 nywfvgctpc eaerpelnrl yekyknkddi vflsfsnsde ktvrkflksh ainypvaifs
      181 rtlddklgis efpvniildk slkyklymkg iskgtsllie etledll
//
LOCUS       WP_284688270             516 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284688270
VERSION     WP_284688270.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..516
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=58457
     Region          36..361
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 migkylrfvg lclllflakp gfcflenqsd slykedlktl nkkianvlkd hhglcagial
       61 isknhpdmil evgncesnge rpasentifr iasvskmiva lailklqeed klsledqlin
      121 fipevefenp weethpiqvv hllehtsgwd eihlvemmyd etppipmkka lefhphtrks
      181 rwvpgsrmay snvnyavaay ivekvsgmsy eeyvrkaifk plmmshstff ndklykewga
      241 vtynwameki pyknelyrsp gglnssardm aqilkmllnr gkidsldflq eesiirmetp
      301 kssigaqagl elgyglgnwk ssykgftsqg hdgamnggla qliyfpeygi ghvillnann
      361 gwvmqqital irgfemnllp ddqsisqkyn glleieegyy lainprsqnr fyqdifisie
      421 kieiqnnvvk rswigsgqtt syypvsptqc ilsnsnktgl vlaedplagk vlysenfvlk
      481 pistfqvytq millglwitl mpagllcfwh lplqfs
//
LOCUS       WP_284688356             284 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Chondrinema litorale].
ACCESSION   WP_284688356
VERSION     WP_284688356.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..284
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32124
     Region          48..268
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mnknnsrrnf vkksaalaas vptilaptgv faakpetkqn ddgkmdvirf avasdghfge
       61 kgtaykmyyr nivawlnaea enegldfcvf ngdiihddpk llkeanayfk elkipyyatq
      121 gnhdkvsedl wkevfnipfn ysfekgnsgf ilcttsnekg eylcadadfv keklelyksk
      181 ksvfvflhis hkkwvdngid ckeitdmles yenvacifhg hdhdhheamy sggktylfdg
      241 hfggswgqey kgyrivevrg gtevytyqcn plargiqnnn kvnl
//
LOCUS       WP_284688423             229 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Chondrinema litorale].
ACCESSION   WP_284688423
VERSION     WP_284688423.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 229)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 229)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 229)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..229
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=26384
     Region          1..226
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 minaiaidde plpleiiesf cddldfidlk ntftqsnkal aylesnlvdl ifldiqmpav
       61 sgidfykslk kdipviftta hkeyaiegfd lnaidfllkp ysydrfmvav nkakelfdlr
      121 nkdenenssy livkaeysti kiffnsiqfi esigdylkiy vddnnaivtr malknvldsl
      181 pnnfvrihrs fvvplervev yrnkkvfiag qeipvgttyq kefkklfkd
//
LOCUS       WP_284688446             136 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Chondrinema litorale].
ACCESSION   WP_284688446
VERSION     WP_284688446.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 136)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 136)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..136
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15255
     Region          <30..118
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mkdkkliyfa pfvvmvvval vlifstkskn rgevlyenrc anchmeqgvg lqslipplan
       61 vdylnkyrdk lacivkkgmd gkvivngvey eqqmpaneef tdtdianvln yvltnwgnee
      121 kplslqevqk qlegcp
//
LOCUS       WP_284688459             313 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Chondrinema litorale].
ACCESSION   WP_284688459
VERSION     WP_284688459.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..313
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=35036
     Region          1..294
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mkkvlfvinp iaggekkdif lskleafade neldyqiykt tgkddeqhvh kiivedkpei
       61 avaiggdgtl lmvarcilht naklgiipfg sangmatelq iptdkeealk lilegkevli
      121 dtllidgkht clhigdvgfn akvikrfeed ktrgllsyak nffrewkfsq rmkciltten
      181 gvrkikchmi afanarkygt gavlnpigkl ddgffelcil ktisfkvlll liltfftgal
      241 yktrfakiiq ckeariklkr nrkmlvqvdg eiigeqnsvk ieivpkslri ivpavssssf
      301 ldylvakiey ekg
//
LOCUS       WP_284688463             320 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Chondrinema
            litorale].
ACCESSION   WP_284688463
VERSION     WP_284688463.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..320
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36133
     Region          45..291
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mkmeftrref iqkssmlsaa lpfvplfsqa nqnaqkqhpd neleihifsk hlqflnynem
       61 aeaaaemgfa glditvrpkg hvlpenakkd lpkavkaikd aglkattitt aissadepyt
      121 kdiletasdl ginyyrsnwl hyseeisipk amqsfqtqik klselnkktg iigayqnhsg
      181 ryvgaaiwev wellkdsnph smgcqydirh atveggkswq tglrliapki ktivlkdfkw
      241 mqtdkgweav nvpigegmvn fteyfsllkk yniqvpvslh meydlggaeh ggkdihipke
      301 eifmkmkkdl nsiqtlwksv
//
LOCUS       WP_284688470             271 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Chondrinema
            litorale].
ACCESSION   WP_284688470
VERSION     WP_284688470.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..271
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30301
     Region          4..253
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 menlcihtit tkpwnleeav vkfseagvkg isvwedstlk lgaeksgrli rehgleivsy
       61 vrggffpsin vakreqaikk nkkmmedaaa lgapslvlvc gaepmqslen srmqiqagie
      121 allplaekln vklsieplhp myadtrsain tlkqandiae ainspyvgva vdvyhlwwdd
      181 nleneikrcg engnlfafhi cdwsvptvdm lndrglmgeg ciplsnikkw vvdagfsgyh
      241 eveifsnkfw qmdqdiflkk iieaykdyqi q
//
LOCUS       WP_284688506             299 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284688506
VERSION     WP_284688506.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..299
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34728
     Region          <194..297
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mekaqtieef yrsklnwlpd nlkkemghfn vfrleefsgh nakaipysrk dyykislivs
       61 kskinyadks fnvdevallf anplvpykwe yleenpkgff cifteeffsq fgnikeypvf
      121 qpggtpifsl daeqkerisa iytkmleeis seyaykydvl rtlvfdiihs aikmkpaask
      181 lykgsnaatr isslftelle rqfpiesneq rikihtpaef aeqlavhvnh lnralkevtg
      241 kttsqliadr iaqearillk htnwniseis wclgfeelsh fikffkknsa qtpktfret
//
LOCUS       WP_284688619             254 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Chondrinema litorale].
ACCESSION   WP_284688619
VERSION     WP_284688619.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..254
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=29581
     Region          1..249
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mnvlivedek ktaellkeli edqpdylvvn icdsvestva ylkkhqqkld lifldiqlad
       61 sesfeifdsv evttpvifct afdeyvmqaf ksngvdyilk pfkesdilqa lgkieklrns
      121 ltkgtlppeq ykqfgnekke fqksfivryr evmfpisvdd iafillenei vhifnfkgek
      181 faifkkldei enavdnkqff rinrqmivnr naikeivpyf nrkvivqlki nipkkaivsr
      241 lkvtpfiswi ekpe
//
LOCUS       WP_284688675            1010 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chondrinema
            litorale].
ACCESSION   WP_284688675
VERSION     WP_284688675.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 1010)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1010)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1010)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1010)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..1010
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=109167
     Region          31..1008
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkaftkall vasmlliivs srllaqdeqi ikgniidesk dplpgvsvii kgttkgtvtd
       61 fdgnysinan sgdilifsyi gytsqeitvd sktdidilmk vnveqltevv vvgygsvkks
      121 dvtgavssvk skeltafpvl saeqalqgra tgvvvqsnng gepgapisik irgntsilas
      181 sdplivvdgf vgatmpqqnd iqsievlkda sataiygsrg sngvimvttk kgqsgelsfe
      241 lnstysaqnt anrldllnad efaafqqsfn psyvqgsadt dwqdllyrtg atqnhqfsfs
      301 ggrnninfya sanyfnqkgv iinsdfdrls flsnvdaqvs dklklginly grrdtkngvp
      361 tqstgetang ggddvislmf rfmpdlpiqd enginttstv gdnidnpyav ateainetkv
      421 dnnranlyan ydilenltfk stfgfstqnt tlgvfrpstl vitagggtgg fatidnsrnt
      481 tilsenylty tkvferssls llagysyqks ttesfsagaa gftsnsfsyr nlaggslvyl
      541 psssfsetei qsqftrvnfe lhdkylltat vrrdgasnfs enekyaifps aaigwkisne
      601 nflkdndkis nlklrvsygv tgnqaigaye slarfntift singgivnav vpdqaansnl
      661 kwessyqanf gldlglfddr vslalnyyni dtkdllmndq sqaeylgfqt lasvrnvgei
      721 nnkgvevsls tvnisnkdfr wttdfnwstn knkvvslvgd tdllldaspg yfsvasthil
      781 regesvgvfw gydyqgvyqg gsipegtatl aafsdpgdpl ftdvdgsgsi dtddykiigd
      841 ptpdftfgin nsfsyknfdl nifiqgtqgg dvfnltnvql fngdgnatke ilnawtpent
      901 dtdipraigs rgreissrfv edgsyvrlkn iglaytlpss mvekigcdnv rlsvsaqnli
      961 titnysgldp evsyfgsgge ntgssnttng fdfgnyptik svtfslnlmf
//
LOCUS       WP_284688709             299 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284688709
VERSION     WP_284688709.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..299
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34574
     Region          66..296
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msehkifdsi ksyndfnnhs tlhplvsvld fskaklrhgy kmsfgiyaii lkkvdcgdiv
       61 ygkntydyqe dtlvfigpkq vldvshksdm yqpvgraltf hpdlilgtpl aqrfdeygff
      121 synlnealhl ssdeqstlvd llfkidhelk rpidkhtkkl issniglfld ycerfydrqf
      181 itrqhvntsi lakfednlns yfnsekpysl glpsvgyfae elhlssnyfg dlvkketgks
      241 aqeyiqtkli diaknkifds qksvkeiafe lgfkypqhfn rvfkqkvgit pkefrqlnn
//
LOCUS       WP_284688740             483 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Chondrinema litorale].
ACCESSION   WP_284688740
VERSION     WP_284688740.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..483
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55929
     Region          349..479
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mktsditkll lillmpimvm gckdgqtrde gkivltfenp skkkilltyi ddwsipykmt
       61 vqdktkqiki atlrpyldis lqdksglisy flfkngdsiy idlsskdpla kilnrqvpvy
      121 etnfekwkqn elfgekepak erffdywslv nggfglitgd emakelqpvk sealnelvle
      181 nnfidslvtk erldsytasy fnaknkmldm llnlhginsi dctkkamviq afkeahiglp
      241 tqmgntvayt fwddflktfy dnclnksavg rkslrefias tnefpltmrd llvfkhteqi
      301 lqtlsvakgi etlqelnnns mqkawvehfs kkynldqgfd tewlvysnng esitfnelly
      361 khhgkllyid iwaswcqpcl iqmpyfeklk reysvkgvdf iyisidedpk nwkwaeekyl
      421 sfdkgnsyrv dssgyellkt efnlntvprd llfgrngdll hmdapqpssl eiqhtlneid
      481 sdy
//
LOCUS       WP_284688795            1173 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chondrinema
            litorale].
ACCESSION   WP_284688795
VERSION     WP_284688795.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 1173)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1173)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1173)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1173)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1173
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..1173
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=132128
     Region          136..1172
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrfnairvik mlskfifygi tlqvmlfstl iasdsmaqkk nvkevfikvg snyqslnaff
       61 dsietqsdyk faysknivan ikdvsittgt rsvydvllev srnkrlkftq vnnsisveki
      121 kklreepeve ivtdiidisg kitddndepl pgvnilvkgt tigtisdvdg myklqveens
      181 tlvfssvgfi sqeipvsnns vidvqlvsdt kaleelvvig ygtekkvnlt gaisavetee
      241 ltnistsnls ntlagrapgv nitnasglag asssirirgs fgeplyvidg iirdkdafda
      301 ltaneianls vlkdaatasi ygsqaangvi lvttikgsnq apvfnyqtsf sfsnptqell
      361 sdkttatdel iyqnrvaefq gtappngeee fayfadknyn vndfiwqtpk sqrhllsvng
      421 gnekvtyyvm ssyrtedgsy knleydkfnl rsnvsvklsn ritmdlnlsg vqensdrfyw
      481 pftddddysv sdlyrctfnw pktypfylee dgtpadyvtd ypvqtpmgsw qawsvidqvi
      541 gdryiktrer elngimslnf dlgdfvpgls tkvmgnyiag dymrkkylsf qenyvftsad
      601 pdgnrfipsa pdpertnift fsqnqeflsy emqtrwsyqf dwfvnyeqrf gksnvtamvi
      661 leqrerglyg sfsraedplt nfdqdfvyst daerrygsgw egngalssvi grlnynfdek
      721 yiaefsfryd gnslfpedkr wgffpsvsaa wrineesfmd nasswldnlk irgsygttgs
      781 sldingyain pfsfrniyet sgsyifgdnl ytaispgstp nvnltwatst tynvgldigv
      841 lnnqlsgsie vfkrkeedil gsrivtlpdt ygqslapeny aarswrgief salwqdrvfn
      901 eelkysvygn igyskdqwdv ldqsaayeeg gnqawrsaig kpvnriigyk slgivrtqeq
      961 ldalleaglk qfgrdpylgg lyfedirgen ysegpdgiid gndiqvlsen nsprinygfg
     1021 fnliwknftl dahfqgvgny driisnqega gmrqhggsvr pyypiwaddv wtpentdaky
     1081 prpvghnwye sgtgtssywi tngayvrlkn lnigyslpet vvsalrlksa qvffnsnnlf
     1141 visemtefhd peqdyydsyp imksftfgld ikf
//
LOCUS       WP_284688833             417 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Chondrinema litorale].
ACCESSION   WP_284688833
VERSION     WP_284688833.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..417
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=45341
     Region          <159..>392
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mdklkslfsi ysfimllvcf stlmsceelf kgneedvlpe sdgkswyvvl medgfaplnd
       61 siplesnkdm qtrydqhqtl ireeirnyvk sniqidaide nlddvyssfq igfsiyltev
      121 ealelydldg vdtffvdedf yielpltdff ipisfqevdw gvelvgsgng vgktawvmdt
      181 gvdqdhpdln vstylsrsmf rvgtssdkdd rnghgthvag iiaakdnlig tkgvaagatv
      241 agvkvldhcd ngcsrgnyrk liaaldyirg calpgdvlnm sigreirtrr rrriftnavq
      301 rlgnagifvv saagnssdda skrypaavng tnvytvsamd nsqnwapfsc fgdvvdycep
      361 gvailstdkd ggytiksgts maaphlagil llnngvvnti gtvsgdpdgn pdpigvl
//
LOCUS       WP_284688976             529 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Chondrinema litorale].
ACCESSION   WP_284688976
VERSION     WP_284688976.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..529
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59445
     Region          1..362
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mkktavylai lalvafsani wgtdiymyde vknaqcarem yhsgnylvpy fngelrvdkp
       61 plhyffmila yqifgfgafg arifsalfgv ctvlgtyffs kkylgetaal fagvalvcsi
      121 qvatqfhmat pdpylitlvs lalfsyyrgy eekkfkwylg ayvllafatl akgpvalllp
      181 giivllflfl egelnvknil slkpvlaigl illiaapwfl avhfvtdgew tigffikhnl
      241 qrysdpmegh gapffmslvy vitgllplsv llpqslifaf kerkqnsfvq lclvtvtvfv
      301 gffafsgtil psypapclpf aaaligyfiq qkkeafqikr ldiqisywmi flialalpia
      361 ayfglkaesy laetayvgty livfpigaia vlflfykski qqslialait ffigtavihf
      421 vaypkidkin pvavcfphid kqvpvvaykq mnpafvipvg apvnqfehis elktfmkdek
      481 rfylisrkky fdeleavsgl klvvsqhelf erpeatlyef nqlhveagr
//
LOCUS       WP_284689039             468 aa            linear   BCT 25-DEC-2024
DEFINITION  MBL fold metallo-hydrolase [Chondrinema litorale].
ACCESSION   WP_284689039
VERSION     WP_284689039.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..468
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51516
     Region          2..183
                     /region_name="POD-like_MBL-fold"
                     /note="ETHE1 (PDO type I), persulfide dioxygenase A (PDOA,
                     PDO type II) and related proteins; MBL-fold
                     metallo-hydrolase domain; cd07724"
                     /db_xref="CDD:293810"
     Site            order(54,58,110,133,136,140..142,183)
                     /site_type="active"
                     /db_xref="CDD:293810"
     Region          257..356
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
     Region          357..454
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mkieqiytgc laqgayyies egeaaiidpl retapyieka ernnakikyi fethfhadfv
       61 sghvdlakkt gativygpga ktnydihegt dgetfeigkv kikilhtpgh tpesttylli
      121 deagknhaif sgdtlfigdv grpdlaiksd vtqedlagll fdslrnkimp lenevivypa
      181 hgagsacgkn msketydtlg hqkevnyalq emskdefvtk vldgltkppq yfaknakmnk
      241 egydsfddvm kkgavplsse tfeeianseg alildtrpaq vfnkgfipns ifigidgsfa
      301 swvgtlitdi kqpilivsde greeevvmrl srvgydnslg fleggieawk nagkeidsit
      361 sisaeelakr kidnadlnim dvrkpteyqs ehvvgadnqp ldyvnehmqe idkdktyylh
      421 caggyrsmim asilkargye nlidviggfk aisetsidkt ayvcpstl
//
LOCUS       WP_284689102             392 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Chondrinema
            litorale].
ACCESSION   WP_284689102
VERSION     WP_284689102.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..392
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=44346
     Region          11..374
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mntrqsnstw kkvrkffndv hlwlgiasgl ilfvvcltgt iytfsseiqe mlnaevyevk
       61 neaglprkte eeiitaveae lgakvssiei padaerslgl nvkkegkrrg ttylvdpyta
      121 eikgttkgag seffmvmfrl hrwllldmnv grpivgwatv ifviilltgm viwfpqkvky
      181 wrqglkiksn agwkrinhdl hnalgfyafi lmlvmaltgl qwsfewyrtg lydilgvdrs
      241 rgrgpkeeka vnlpeqevkl sladyikkad eslpyegdyr lnlpqenqas vsvskyktgf
      301 fapnggdelk lnkytaeves lekfsdkpln ekiarsikal hvgnvygtfs kilyfiacli
      361 atslpvtgti iwinklkkks krkksktlsy sn
//
LOCUS       WP_284689118             317 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Chondrinema
            litorale].
ACCESSION   WP_284689118
VERSION     WP_284689118.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..317
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35001
     Region          34..282
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mnrrnfikst tlaaatinlp ftgftqdtsl krkfklclsp gnigvsldqk galqaaidyg
       61 yeaivsfpne iqnwsddeva sfkkemksnk iawgsggipv efrkdeqtfk dglsklakaa
      121 ealqkvgask mntwimpthp tlsysenmkq hasrlgecak iladydvklg leyvgpktlm
      181 ardrypfiht laecltlien tkqpnvgiql dtfhwycged tvadllslkp sqiitvdlnd
      241 arsdlsrdaq ldgtrelaga tgviditafl kalmeigydg tvrsepfnkk lndmddkkam
      301 eldmqslqav lkncgvk
//
LOCUS       WP_284689149             548 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284689149
VERSION     WP_284689149.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455327
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..548
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=62726
     Region          <375..543
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
ORIGIN      
        1 mkttslitil pdkpyrffll ifflclmhyl atpvaakqde gqasiaaaln qqikvinkcv
       61 rstwknqrsy srynedlnkn vhkegenilq gavpyfaitk ylklpvsdye kakiaakeip
      121 teyrekvill fdslwqlqeq qviigrqfse ltnfnprktd tttvnqayky laeldkintd
      181 yrnlslqfea lalqihkryc ssgqnswvkg atamkividt arnylemari gkfskqnqld
      241 tlqlglmlte lqknrsintq niketgsydg nsapnrydkf iekirkmmge yygyiplety
      301 spkpyeyivn efnwavesyn nfarvsamen mgeapafllq svielglykf qypllkqqne
      361 kaeqkismeg faynhtvlll dvsgsmnqpe klpllkeais qlsevmrked rlsvviysdn
      421 arvilenvsf tdkqslytls kltssgrtna qkgiklayql aekefieqgn nrvilasdgd
      481 ftvfeetikd vneatekgih lsvfsfgwqv enetqlkhla eagqgnyihv tkknsfeall
      541 selqaisk
//
LOCUS       WP_284689169             295 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Chondrinema litorale].
ACCESSION   WP_284689169
VERSION     WP_284689169.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 295)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 295)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 295)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..295
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=33892
     Region          <157..287
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 msitqihnte qlanklklks nlqlliesvl lgslanllin yffnpikpdf ilqeyitaff
       61 lsfpivlcnq iihlhldkay dwkqqptqrf ffhlmylavv lllsinlfgn lymaisakgy
      121 fslyellsin llaftvaill tsfkwakdfy nnwinadknl kytqkqleal sntnqhktlk
      181 velqkgtqqy fveaqeilwa ktedgivwva lkngnhfink ntlsqlmqil pepqfflvsr
      241 nvivskevis nispstygkv sltlkdsirg enhltvsrpk aasfrkwfns nsacn
//
LOCUS       WP_284689288             669 aa            linear   BCT 25-DEC-2024
DEFINITION  GumC family protein [Chondrinema litorale].
ACCESSION   WP_284689288
VERSION     WP_284689288.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 669)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..669
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=76569
     Region          1..>483
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mgiplllgtl vffltrnqer kyisfarlqv siptsgdvsl igrefkqyet slfffdliem
       61 insrktsemv rmemlikyme gdyklftfdk npdlrkdsid ifkraqqlrk qyqlldlsds
      121 ldhhisllle nnrlsmkemq aqlaayrvsk snyvdikyec enpykaamit gsystivteq
      181 ykvlsqkkie nnrerlenlv snarkeldsk ikqfenfkie nnvinlpeht kaivnqvvnm
      241 evklaelqet hqahtkaaei vkknltnags infndtsnkt iaslkdslra iseelllfeg
      301 nqeekkalea qveylkneit aqiismldki pydpsqarqe lmsrliayei eiemeasvme
      361 svenemkkln ayaaqfaple snlstfisei hiaqetylil lnklnlvkti eqgagdvnlt
      421 ifspavlpqe pesskrgfai vgaaiasfil iaagiaafal ldkrvysagy ftdltnilpf
      481 itinddfdni heirrirkki vdlpnelrti lilglskadi esnfiehlmq slavfpgeql
      541 flnatgqekk iegyevlslp esveqiyayq eekhylvnid ndsspfekqa pefwqaftqk
      601 sllhrktiii aappalihsd weewlstvha fillrmggqs mtekdkemir aiyshkksfq
      661 atvfiekeq
//
LOCUS       WP_284689439             153 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Chondrinema litorale].
ACCESSION   WP_284689439
VERSION     WP_284689439.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..153
                     /product="YybH family protein"
                     /calculated_mol_wt=17340
     Region          25..152
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mktilqlfci tclcifatis citpksdlpk eivqehldnm ingyveedid qiiagfteda
       61 qmledggpiv ngkseiiqst kallenieft kgsaeiieiq admnmayevs yfrltqfvnd
      121 stsvdlkwkh laiwqkqndg ewkisrliyn eve
//
LOCUS       WP_284689416             280 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Chondrinema
            litorale].
ACCESSION   WP_284689416
VERSION     WP_284689416.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..280
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=32218
     Region          3..280
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mmkilvtgss grlgkeivkl lrqnnyevlg tdlvksettd eildirnlds vlqitksida
       61 iihtaaihgk hyelnypree fiaaningtf nllkacvqng isklvytstt siygeamvdn
      121 skavwvtekl tpiprdiydi tkltaellck dyfekeqiet tvlrvsrflp eidnlkaihr
      181 lyrgldeedg amahmlalqk hfdsfeifni snhsafketd vdmlyqnpke vilkyypqae
      241 tfferenwqf pqkidrvyvi ekaikllgyk pahnfetflk
//
LOCUS       WP_284689480             341 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Chondrinema
            litorale].
ACCESSION   WP_284689480
VERSION     WP_284689480.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..341
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=38640
     Region          3..335
                     /region_name="HisC"
                     /note="Histidinol-phosphate/aromatic aminotransferase or
                     cobyric acid decarboxylase [Amino acid transport and
                     metabolism]; COG0079"
                     /db_xref="CDD:439849"
ORIGIN      
        1 mlyghgddlh afekaqitan fstnvwpdgp hplllsklsd sikqldaype pagkpfveql
       61 safynvsaeh flatngtada iyliaqvfrk rtatifvptf aeyedaaklh qiecsfcnwn
      121 eiekipklst dlaficypnn ptgqivatei leafikknpe tlfiideaye gflkhsqsll
      181 gkidqfknll llrsltklft lpglrlgyis ghpsiikkis eykppwsvns lavqagvfif
      241 qdyekylpdv ralleetqwf lnevnqidgl kvlptvtnff lvkslfaeak qlkvylaekg
      301 mlirdaanfr alspnyfrla tlqreknqql inelklwnpn s
//
LOCUS       WP_284689643            1035 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chondrinema
            litorale].
ACCESSION   WP_284689643
VERSION     WP_284689643.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=112008
     Region          28..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mndcysksia aaillffsai smaiaqdkri tgkivaasdg lgipgasilv kgtttgtstd
       61 vngnfdlilp pnaemlvisy igyvskelsi gnqtnfdisl dedvqqleev mvvgygtqer
      121 akvigaissv kseeitsvpv ispdqalqgr aagvtvvnng apgqgatvri rgvgtpndns
      181 plyvidgmps gdlnqinpnd iesmevlkda saaaiygsra angvilittk kgtrgktrvs
      241 idsyagvqkv wktldllnte qyidyaseiq tnaglsvpsr ftdtqwssll nnntdwqdqi
      301 fqtgviqsyn anvsgggens mynisggyfd qegtmlntgf erysiranse fnvgkkfkvg
      361 qtlsiayset qsepynggrs qiehtiksap ylpvyysdyv aitgleqsnl ggfkgpdqvd
      421 dndaenpvsv amlndqhtda tkilgtvyge leiieglkyk lllgidmtya dyytfrpayd
      481 ngdfhnvdfa aitqnrrnyi splitnslty drtfadkhnl nvlgviekqt svstntntss
      541 qnsisnvieq lttealsats grsewalisy lgrvnydydg kyllsasvrr dgsarfgpen
      601 kwgtfpsvsv gwrisqepfl qsvdfitdlk lrgswgqagn qnignygyqa tinsnyaysf
      661 qdgvlasast vtelanpalk wettemlnig ldmsvldgkv smaleyfdne tqdvlvqvpl
      721 aaslglsgsp yvnagtvsnk gfevtlgyrd aegefqwsvd anlshvknev vslgggnpin
      781 sfnfegdnit qtiegqpiay ffgwqtdgif qsddevaaha tqdnaapgdi rfkdlagapd
      841 engnltapdg vidandkvnl gnpfpdftyg lnatanykgf dftlfiqgvs gndiyntniy
      901 dlegmtrvfn agtsvlnrwt gagtsntipr gvtgdpnrna rasnryvedg sflrmrnial
      961 gytlpsslle nigsgfisnv rvyvssqnlf titnysgydp eiggfrgent tlqlgvdrgn
     1021 ypqprtflgg vqisf
//
LOCUS       WP_284689791             864 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Chondrinema litorale].
ACCESSION   WP_284689791
VERSION     WP_284689791.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 864)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 864)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..864
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..864
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=101503
     Region          <385..>496
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
ORIGIN      
        1 mensdvfdir keakdlrgqs kinkllegag iannifrnge gdewtkkala wvlidlvkef
       61 islgnisnae qyynkllqid fyesddiisn qiqflkpkid vqykeikqae elskankhse
      121 afslmkqlia sgklkpmhhe sygwiiyryi kseintldsv svrtylrdym nlkndrpsml
      181 hsmilnfgln yskehsdfnl lnffnlwgpe nlryedktns ehegnnipsl isricrelid
      241 kdysfdvaef idkvklessd wgftsyetid llrepffwkt ynyqknkqwd elwksfdfyv
      301 enysiapase whskilslae rnmteanawr ffnffkgwhp slltshdwkd vekddktyks
      361 igvkalkkaf ehlktnqetd lnwliqayee ginkcpenew lkrelailyq kngdidksit
      421 iykklalely dkpyywnefs slvknnedlh lsmlckaali eqnddflgdv rlalavvfer
      481 ksliqeagie lnlykenrqk nqwkigadfd eltskinlve gsntekykel kgmseefafn
      541 dlpwislvyi dsfkdkkgrt rwvfsdgkei eisplkkfln lsninlgdvl nfklkesvke
      601 iegperswlp skkikqfkpl iyritelekw stfeneyaiv dyinqdknvi haitfsnqei
      661 ffksnskdfk kndlisgkri qkkdgdafrt elvniqkesn nqpiyeiepk iavvdgvnhs
      721 kslfhfvvns kidgivrfne telrpnegdf ievrllskkd rkkgivrfkv itvnetekvn
      781 dtllkdsige ielkyktsyg treyfelnea dqeflvpdfa fmgdfyipqf llkkheiksn
      841 cfgkikvind gskwkvidle ildr
//
LOCUS       WP_284689808             260 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Chondrinema litorale].
ACCESSION   WP_284689808
VERSION     WP_284689808.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..260
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29295
     Region          24..136
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mtynriisev sfskavdikr lgfiikaies ytkgdrkvld vgcgnglitm elgkigyqvk
       61 gvdisnktid kaiannnltn vtfevadvev lsiqdvkydv iicsevlehl kepgkmliil
      121 krllkengil ivtvpngkgp relfitkpmq wlktntpqiw vivdkvkhhl gydgkteqsd
      181 addlthihff tkkklnklss dkgysilkfg kanflgdvfp fsfimkkslk lqyfdcnlad
      241 ilphyftcgf ntvwkknnac
//
LOCUS       WP_284689885             292 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfotransferase family protein [Chondrinema litorale].
ACCESSION   WP_284689885
VERSION     WP_284689885.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..292
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=34054
     Region          14..241
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mdnyqtnsva tepvfivgmp rtgskiykni inyhsdinis peifyltpnw irkdfiqltq
       61 sligetssdn sldklaslmf enkffgtywr dikgekkdml kllkgtngsf keifiailey
      121 daqinnkvkl gakfpvhitk ahelqqwfpk akfihinrhp laiynsqkrk hiknktnfts
      181 kiltltkvfl vtiityrssy kfnrankgnk nyelfeyekl tsnpedqirr lcdflainyk
      241 pemlqppvkd ssyqinsqpi gihqessarw kkevnyieki vfklltkstf sn
//
LOCUS       WP_284689889             436 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Chondrinema litorale].
ACCESSION   WP_284689889
VERSION     WP_284689889.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..436
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=48306
     Region          1..435
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mkisifglgy vgavscacfa keghqiigvd vnehkvdlin kgkspivekd ldefiaegnk
       61 ksllkattdv dyainnseis iicvgtpsqi ngnidlsyiy kvcvqigeal ktkneyhtiv
      121 irstvvpgtv kqcidiiedn sgkkhiesfg lgsnpeflre gtaiydfwnp pytiigiese
      181 ksknmlkely ksinaplytl kpeesemiky annnfhavki tfaneignic kelgvdghvv
      241 mdivakdkkl nlsnyymkpg fafggsclpk dvrglnyrak ildvktplln slidsneiqi
      301 qrglqliynt gkrkigilgf afkagtddlr espmitliet ligkgfnvsl ydanvllskl
      361 mgknkdfiig riphisrllk agaeqvveea evivlgnkse efkeilphip kdktiidlvr
      421 ieknkqtgen yvgicw
//
LOCUS       WP_284689910            1010 aa            linear   BCT 25-DEC-2024
DEFINITION  CHAT domain-containing protein [Chondrinema litorale].
ACCESSION   WP_284689910
VERSION     WP_284689910.1
KEYWORDS    RefSeq.
SOURCE      Chondrinema litorale
  ORGANISM  Chondrinema litorale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Chondrinema.
REFERENCE   1  (residues 1 to 1010)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 1010)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 1010)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 1010)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Classification of the caspase-hemoglobinase fold: detection of new
            families and implications for the origin of the eukaryotic separins
  JOURNAL   Proteins 46 (4), 355-367 (2002)
   PUBMED   11835511
REFERENCE   5  (residues 1 to 1010)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18641671
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="Chondrinema litorale"
                     /db_xref="taxon:2994555"
     Protein         1..1010
                     /product="CHAT domain-containing protein"
                     /GO_function="GO:0004197 - cysteine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=116874
     Region          33..62
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          35..308
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          71..105
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(73..74,77..78,80,112,115..116,119..120,122..123,154,
                     157..158,161..162,165)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          110..140
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          153..182
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          180..967
                     /region_name="COG4995"
                     /note="Uncharacterized conserved protein, contains CHAT
                     domain [Function unknown]"
                     /db_xref="CDD:444019"
     Region          196..224
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(197,200..201,204..205,207,238,241..242,245..246,
                     248..249,280,283..284,287..288,291)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          236..266
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          279..307
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          320..351
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          364..391
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkffylfiif iiynttssak havdndsidq inlskgeili ndyqfdkaid fyhsiiqqsy
       61 lkkdwenyfl aknqlgycyr rirnydkayt vlnstidsck lllgeqnkit algyfylgqy
      121 ydflnnskea inyytkalni rlelhtephk dvalsyynlg nvynhvvfny keaevyykka
      181 lsieleisnk etiqtariyn klgsvnrqkr dydnailyts raleihksan sndndisnil
      241 inlgniylqk ndfknaikvy llaielkvkl fgdksdrlii vynnlgtafq kqedysnalk
      301 yynkaldlvd nfedsnsiwh snlylnigls igygsinyss akyylnkslk ircdrygnkh
      361 pevakihywi gkihqhfken dkaleyfqna lvasiedfnd tliqinpnke ivpndllivd
      421 ilkekanilk lkanfsdslh hlllasecyt iareiilsnr fsyihdgskl flfeeygnif
      481 eeaidcyyql feqtkdenyl nllfsfmetn kagllvesiy stennqlent qpllkrrkhl
      541 invqekikne ilqrnssdke lnqelfrisi qleqlsdsln klhpqyhill spawdnvqlv
      601 qnklqnsssq lieyffgekh iymlgisssn ykimriinsk ktnqhladyy kvltksnees
      661 sqleeekiff kssfniykel vhpvllnhdk innliivpdg ilellpfesl vtlldnenin
      721 yknapyllye ystrylysss llnshlkkgt nndrnnmlaf sysdtknigs sysslsnird
      781 sdlnelpgtg ielqqianyf egdffmgdea tkqnflekan nyniihlalh gyggknskyd
      841 srlffnpeke ndslsgvlft hellglglna nlvvlsaces gigkqfkreg vfsvgrgfiq
      901 agcptvlnsl wnindfysak iiinfykkiy dgkpidkalq sskidfltdv deiganpyhw
      961 agftvvgqnh tiesnlwnky litllivlni ivisvtlfik kiknktllka
//
LOCUS       WP_284690116             115 aa            linear   BCT 25-DEC-2024
DEFINITION  cytochrome-c peroxidase, partial [Campylobacter jejuni].
ACCESSION   WP_284690116
VERSION     WP_284690116.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter jejuni
  ORGANISM  Campylobacter jejuni
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10504354
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Campylobacter jejuni"
                     /db_xref="taxon:197"
     Protein         1..>115
                     /product="cytochrome-c peroxidase"
     Region          58..>115
                     /region_name="CCP_MauG"
                     /note="Di-haem cytochrome c peroxidase; pfam03150"
                     /db_xref="CDD:427168"
ORIGIN      
        1 mkvksllias lvafsslnaa slideaknsg lvalpkdqkg vdeilkqngv kaseftleka
       61 elgkklyfep rlsksgiisc ntchnvglgg tdgistaigh kwtanphhln sptvy
//
LOCUS       WP_284690370             186 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Bacillus subtilis].
ACCESSION   WP_284690370
VERSION     WP_284690370.1
KEYWORDS    RefSeq.
SOURCE      Bacillus subtilis
  ORGANISM  Bacillus subtilis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 186)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Bacillus subtilis"
                     /db_xref="taxon:1423"
     Protein         1..186
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19748
     Region          1..>184
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mnpqnprymg hmdsiptlis clgdfisssl nnnmlslems pvfskveaql lktiarmfgy
       61 ddksggvmts ggslanlhal tvarnhqlnm kktgifglsg qpvifvsdvs htslhkaami
      121 lglgtssiip vksnnlarmd ihdleikihr akseghipfa vvatagttvt gsidpilpia
      181 ritkgl
//
LOCUS       WP_284690362             198 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Paraconexibacter
            algicola].
ACCESSION   WP_284690362
VERSION     WP_284690362.1
KEYWORDS    RefSeq.
SOURCE      Paraconexibacter algicola
  ORGANISM  Paraconexibacter algicola
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia;
            Solirubrobacterales; Paraconexibacteraceae; Paraconexibacter.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14302692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Paraconexibacter algicola"
                     /db_xref="taxon:2133960"
     Protein         1..198
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20948
     Region          9..89
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          98..192
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(101,116,118,132,135,141,175,177,189)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mtaapeeler qahvgprvra lreamslslr dlaersgvsa pmlsqverge tsptlqvaak
       61 iaagldlrls qllrldesgs vtvvkagegr rggtaegghr fevltaplpg qraelsrhel
      121 kpgartgreg dppmhepgsr etalvehgtv vlvvdterhe lsagdcvtfd adlphhfenp
      181 gpddaallav lsaglrrs
//
LOCUS       WP_284690555             109 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Propioniciclava flava].
ACCESSION   WP_284690555
VERSION     WP_284690555.1
KEYWORDS    RefSeq.
SOURCE      Propioniciclava flava
  ORGANISM  Propioniciclava flava
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propioniciclava.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 109)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 109)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 109)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 109)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Propioniciclava flava"
                     /db_xref="taxon:2072026"
     Protein         1..109
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11788
     Region          9..85
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(13..14,16,19,22..23,26..27,30,61,81..82,84..86,
                     88..90)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(14..15,19..21,35..37,46..49,51..52,55..56,58..59,
                     65..67,72..74)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(35,38,81)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 msrecvdlav evlriladvt rvrlvlalhe aselsvsala eavekkpsav sqhlarmrma
       61 rivstrqqgt svlyrltdeh alavvleaik qaehavsqgq ipphhhgad
//
LOCUS       WP_284690749            1596 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Acinetobacter
            pittii].
ACCESSION   WP_284690749
VERSION     WP_284690749.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter pittii
  ORGANISM  Acinetobacter pittii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1596
                     /organism="Acinetobacter pittii"
                     /db_xref="taxon:48296"
     Protein         <1..1596
                     /product="beta strand repeat-containing protein"
     Region          4..1592
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 vvnvngtnyt vtaadlangf itaaipvtge gpvtihaeav daqgnldvad advtvtvdtl
       61 padligaiti pedlngdgil nadelgtdgt fnaqvalgpd aidgtvvnvn gtnytvtaad
      121 langfitaai pvtgegpvii haeavdaqgn ldvadadvtv tvdtlpadli gaitipedld
      181 gnlilnadel gtdgtfnaqv algpdaidgt vvnvngtnyt vtaadlangf itatlaataa
      241 dpvtgqivih aeavdaqgnv dvadadvtvt ldvtppditt tvlaidpvta dnildateag
      301 gsvtltgtlt niptdavttg vvvtvngvdy tatvdavagt wtvdvagsgl aadsdltvda
      361 tatftdlagn astlqdtqty tlassiiafd ntdtavlapq pllvqdgasl gsetylalvs
      421 lagldlqlgs eaidftvgag qegnatftys allgadvlsd yslvlqkldp itgdwtsvyg
      481 ggeadildlt llggtpsvvi dgleegqyra fmtyngllgi gllgtltgtm dvydttqvgg
      541 yytevadgnv itdintsget dvvtamtvvt avngqpvtal dtvinglygt lvidpdgtyt
      601 ytptasaagv gqtdvfvytl tdpvtgdtaq anlniqlssv kavdnvvtae inpepllvad
      661 dvalgsasyl vavslagldl qllgndaief tvdpnregta tftfdaiita dllsnyaivv
      721 qkfdeatgqw vsiggtnpea slidltligg tptavlegld agqyrafigy eglvgvglgg
      781 tltgtmdvyn pyivagysve pisgnvikda sltgevdaas ssavisqvng vavdpvagat
      841 ivgaygtlvi dqdgnytytp tvdganlgqv dqftytlldp vtgntseatl yvrldsdsvd
      901 mtwndadpsq pavitsplpv damdnvasae idmvypvtte vldnaisynw llgvggivig
      961 skegtatftv dpgnltdaii avnfgsvatv vdglhvvltr vnpdgtrtvv adssdtgvid
     1021 llgifgsevq fkidnlsagt yelfmesntl ltalgsvtad itlnhgditq ppvlvvdpvt
     1081 gnvladdnsa vygtnyvpdy itttsvvtav taengntttv vagtpatvvg vygtltinad
     1141 gtysyqatad manvgkvdsf tytvtdpvtg rtdtatlhvq vgspdvdvtw ntadpsadat
     1201 lptpsvtadt ddatismepv vdpvvdvasg nvtignlagf pplpvlsstv tssqftiaan
     1261 tvsdvhvqln ytaslslsal pttgytiqql vggtwvntay sgsatalagv lgapaysadv
     1321 phlsegtyrv vfslsslisl gtvtldsvvt ttathldqyt pdgqtdwitg nvltndvveg
     1381 tqlyvmnstt gtyelaagqg vntgegtlyl yndgsyfykp ldsaanatvd vidyklvsvi
     1441 dgseyastlt inlsqelnsl avstaandtf algngsdtli yntltaasvt natggnttag
     1501 gvdvwtdfhv gntatddqad kidlsnllig sqtnltigqy vsvsydagtq tatisvdrdg
     1561 gllvegtyte tpllqltnlt gpvtlndlin ngqiif
//
LOCUS       WP_284690818              95 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Bacillus subtilis].
ACCESSION   WP_284690818
VERSION     WP_284690818.1
KEYWORDS    RefSeq.
SOURCE      Bacillus subtilis
  ORGANISM  Bacillus subtilis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Bacillus subtilis"
                     /db_xref="taxon:1423"
     Protein         1..95
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10560
     Region          <42..92
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mpalpnhpnq atncihiagt ttnntpkatl qnrslftsvl fisvsflyvw vnneqlteed
       61 kvksinveal drickvlnck ledviefved dpkds
//
LOCUS       WP_284690836            1167 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Acinetobacter
            pittii].
ACCESSION   WP_284690836
VERSION     WP_284690836.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter pittii
  ORGANISM  Acinetobacter pittii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1167
                     /organism="Acinetobacter pittii"
                     /db_xref="taxon:48296"
     Protein         <1..1167
                     /product="beta strand repeat-containing protein"
     Region          3..>1165
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 ldtidaindn vtfdpgpfvs tiwdapiiaq dinvldtsii gdtsmnvefs vprnsadigt
       61 ghegdvviqv sqdnliavas gfsvlveyfd gtnwvqytta tttnggliad alglgvlgiv
      121 ddgktiavhl tgvpegqyrv vvqndssaig dllddltlae lgdqgillga dnqdavldav
      181 etalngqvlt lgtlvrnvle pllnaanaag etlavtdiva aivqiplvgs llggvdtvld
      241 fiadalvdnl ltvleftnvt ingsetyytt pelagnvfad ngsgaddrgn snaalvtkvd
      301 gvdiptdgtd avikglygtl yinkdgvyry vlngsvdsng qvddftytls dgiqsdtavl
      361 tisvadviap kapivsslde ttvtgfvgaa eadsiinvyg gidsdgdgip dtllgittan
      421 pdgsytvtln paialgdtvv vtsrdaagni stptiaslhn ivalddpnet nyelsttadr
      481 pdisggiftl anagvlgdli dldlsatsap gvtvgtneqi tltltasgst gldisavgnl
      541 idailggnig gsldliiake tstgsyevyn tvanaytlnn svltftasgs qsislddagv
      601 ykfilapnss tssalsnlls lnllgnlvls sndvvatinn tdlitgnvls ndttapigld
      661 lsvvsikett vgvdenvisg tpkviegmyg tltidstgay syqmtanata lgkveaftyt
      721 vqdndghskq atiyirldss lvtldwtdki gleeadklvt qltadnkasa gtvttlfdqv
      781 lngsgdslns iqvtgsngal ptsppatgst aipddsgrft lgagqtayis ftsilpsnvt
      841 qnfglggnqt saynvviele rdgavldtql atwtstisgt kyyykvtntg tssadydlni
      901 aygdgsglfn wtnttgktfg inniqlditg ttytastvsg dlisndtlys svfkigvaag
      961 sttpstyldv nstpivgtyg tltvnldgty syqangeiad lgkddvftyk ietldgtvnt
     1021 qtltikvdad nvligtpnag tagndiavsq stnevftlgd gadlliynvl ngssptggng
     1081 tdqwldfnms egdkidvssl lsgatattin nylsvtisgn qvtllvdrdg sgsasspttl
     1141 ltltneehat npitslvdll nnnsiiy
//
LOCUS       WP_284691146              73 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lactobacillus
            crispatus].
ACCESSION   WP_284691146
VERSION     WP_284691146.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 73)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..73
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8359
     Region          1..73
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mtmqaklfgr rlmrarknrq ftqlqlaeri gtsattvsry englsfpskr rlseiahflg
       61 vkvdwlltgf ked
//
LOCUS       WP_284691226              84 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase, partial [Lactobacillus crispatus].
ACCESSION   WP_284691226
VERSION     WP_284691226.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         <1..84
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
     Region          <6..70
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 vlagviepas akpvqidanv migdnavvie gvhvgegavi aagavvthdv pahtmvagvp
       61 akiikkvdek tsskteledn lrkl
//
LOCUS       WP_284691254             107 aa            linear   BCT 25-DEC-2024
DEFINITION  tRNA (adenosine(37)-N6)-dimethylallyltransferase, partial
            [Lactobacillus crispatus].
ACCESSION   WP_284691254
VERSION     WP_284691254.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Seif,E. and Hallberg,B.M.
  TITLE     RNA-protein mutually induced fit: structure of Escherichia coli
            isopentenyl-tRNA transferase in complex with tRNA(Phe)
  JOURNAL   J Biol Chem 284 (11), 6600-6604 (2009)
   PUBMED   19158097
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Moore,J.A. and Poulter,C.D.
  TITLE     Escherichia coli dimethylallyl diphosphate:tRNA
            dimethylallyltransferase: a binding mechanism for recombinant
            enzyme
  JOURNAL   Biochemistry 36 (3), 604-614 (1997)
   PUBMED   9012675
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..>107
                     /product="tRNA
                     (adenosine(37)-N6)-dimethylallyltransferase"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006400 - tRNA modification [Evidence
                     IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
     Region          1..>107
                     /region_name="MiaA"
                     /note="tRNA A37 N6-isopentenylltransferase MiaA
                     [Translation, ribosomal structure and biogenesis];
                     COG0324"
                     /db_xref="CDD:440093"
ORIGIN      
        1 mkkvlaivgp taigktnlai dlakrlngei isgdsmqvyq evavgtakat aeeqaqvkhy
       61 lvdtqsvfde ysvkdfvdqa tkaieeisqk gklpiiaggt gfyvnal
//
LOCUS       WP_284692014             391 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Clostridium zeae].
ACCESSION   WP_284692014
VERSION     WP_284692014.1
KEYWORDS    RefSeq.
SOURCE      Clostridium zeae
  ORGANISM  Clostridium zeae
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Clostridium zeae"
                     /db_xref="taxon:2759022"
     Protein         1..391
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=44958
     Region          112..371
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mvadklfykt llknmfsdpf qvkfwdgnte dygvgkakfk iifnepipkk dllsdpstaf
       61 gegymtkkid iegsiqdvie slynnkesfl kngekyesli kkfkssikas kenikfhydi
      121 gndfyklwld dsmtyscgyf rdqtdtlnea qknkvnhilk klnlkeglsl ldigcgwgel
      181 iisaaknygv kamgitlsse qfegvkerik regledlvdv klidyreikg itfdrvvsvg
      241 mlehvgkenl keyfqvvnrl lndrgisvvh sitgvndggt ntwidkyifp ggyvpaikei
      301 iteiaeqdfe lidveslrrh ygrtlenwar nfekalseie kdkeevfirm wrlylnscaa
      361 sfncgninih qalfakglnn dlpwtreymy k
//
LOCUS       WP_284692061             149 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Pinirhizobacter soli].
ACCESSION   WP_284692061
VERSION     WP_284692061.1
KEYWORDS    RefSeq.
SOURCE      Pinirhizobacter soli
  ORGANISM  Pinirhizobacter soli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Pinirhizobacter.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 149)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 149)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Pinirhizobacter soli"
                     /db_xref="taxon:2786953"
     Protein         1..149
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=15902
     Region          <29..130
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtevfqgvtr yarfpnaqpw hqgtaapdas fqpvpymavy aatkafvlsl sealryelas
       61 egvqvmascp gpaatsffeg tktgmkgkdf dtaesvvert liafakgkav typgrlsvrv
      121 atvlprffpr ktmvrlsgaa trgmglvda
//
LOCUS       WP_284692229             382 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Desulfobaculum
            bizertense].
ACCESSION   WP_284692229
VERSION     WP_284692229.1
KEYWORDS    RefSeq.
SOURCE      Desulfobaculum bizertense
  ORGANISM  Desulfobaculum bizertense
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Desulfobaculum.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Desulfobaculum bizertense"
                     /db_xref="taxon:376490"
     Protein         1..382
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41562
     Region          5..380
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mkmpfidlks qfksiesdir kridavlehg qyimgpevhe lneklaefag vkhaiscssg
       61 tdalllglma knigpgdavf ttpftfvata evvaltgatp vfvdidpvtf nidveelrkv
      121 iadvengthp lckdselkar aiipvdlfgi paeydainai aeehglfvle dgaqsfgaty
      181 hgkrtgslsh vgatsffpak plggygdgga vftdddetak lmqsvmihgm gedryqnvrl
      241 gingrldslq aavllpklei fpdelvkrqq vadayserls qipgvtppsl pehctsawaq
      301 ysvlsekrda iqsalreadi ptatyypipl hlqkmfadln ykqgdmpvse rcaaqifslp
      361 mhpylkeeqi ddvcqviaka ak
//
LOCUS       WP_284692517             126 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: pyrroline-5-carboxylate reductase family protein,
            partial [unclassified Actinomyces].
ACCESSION   WP_284692517
VERSION     WP_284692517.1
KEYWORDS    RefSeq.
SOURCE      unclassified Actinomyces
  ORGANISM  unclassified Actinomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="unclassified Actinomyces"
                     /db_xref="taxon:2609248"
     Protein         <1..126
                     /product="pyrroline-5-carboxylate reductase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004735 - pyrroline-5-carboxylate
                     reductase activity [Evidence IEA]"
                     /GO_process="GO:0055129 - L-proline biosynthetic process
                     [Evidence IEA]"
     Region          <1..126
                     /region_name="ProC"
                     /note="Pyrroline-5-carboxylate reductase [Amino acid
                     transport and metabolism]; COG0345"
                     /db_xref="CDD:440114"
ORIGIN      
        1 lmgavgrttr iaerdfpafv glagsspafv ltfiealara gvlagvpkaq avdivaqavl
       61 gsaltvqaea asragggrtp adlvdavcsp ggttvaglva meragfssav iegfratvar
      121 drelga
//
LOCUS       WP_284692622             571 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paraburkholderia terrae].
ACCESSION   WP_284692622
VERSION     WP_284692622.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia terrae
  ORGANISM  Paraburkholderia terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 571)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 571)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 571)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 571)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Paraburkholderia terrae"
                     /db_xref="taxon:311230"
     Protein         1..571
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=63812
     Region          73..558
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mvadrrepgp acdarrkcga nasakpppgs ageylqqirp hgqahssrpg patrlrqsir
       61 kqnhleiele pcrqlgslth elfrqvveaa psamvmadrd grmvlvnaqa eklfgyvrde
      121 llgysvdrlv perfrsahpg yrrtfhddpk srpmgggrdl falrkdgsef pveiglnpvt
      181 tdegvfvlaa ivditerkrl eerfrqvvea apnamvmvdr aglivlvnaq teklfgytre
      241 elfsktietl vpqrfraghh tyramyfddm kprlmgtgrd lygrrkdgse fpveiglnpv
      301 ttseevfvla aivditerkr aelellkkte elarsnqdle qfayvashdl qeplravagp
      361 lqllqrrylg qldaradefi thavdgatrm qkliddllay srvgrsgavh qltqcedvld
      421 qalkslsvgl qeagaqinrg elptvlaipt lltllfqnli gnalkfrrsd rpvqidvdaw
      481 rqsddwvisv kdngigidpq yferiflifq rlhgraeypg tgiglalckr iveqhggriw
      541 vesapgngtt ffftlsaatd dsgrsqpnpr e
//
LOCUS       WP_284693361             194 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Escherichia coli].
ACCESSION   WP_284693361
VERSION     WP_284693361.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..194
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=22002
     Region          <2..169
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mrflevagqa dirtrfmlal aydcglrree lctvatgdid psqrlltvra ehtknrfgrv
       61 vpyspvtgel ytawlterrm lsssrgplfl srsprnraep isnwtwskvv rglaikadlp
      121 listhtfrhl cltelarvgw diheiaafag hrriqstlly ihlsardlss rfnytvaslh
      181 tcrltvlqqq dpsp
//
LOCUS       WP_284693408             298 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Pseudoalteromonas sp. SCSIO 43101].
ACCESSION   WP_284693408
VERSION     WP_284693408.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. SCSIO 43101
  ORGANISM  Pseudoalteromonas sp. SCSIO 43101
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Pseudoalteromonas sp. SCSIO 43101"
                     /db_xref="taxon:2822847"
     Protein         1..298
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33184
     Region          16..296
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 menfflditt amqtqqwfyf ltvglvslci gsflnvviyr lplmmkrewq tecrillade
       61 lnskqqteqa pfnlikpnst cpkckapika wqnipvlswl flkgrcanck tvisvrypiv
      121 emltavlsli vaavfgptkl allyivitwv lvaltfidid hmllpdqltl plvwlaliaa
      181 tiditiaptd aiigaavgyl slwsvywlfk latgkegmgy gdfkllavfg allgwqdilt
      241 ivllssvvga iigiaqifiq gkdkttpipf gpylaiagwv tllwgqqiqs yyfnylgy
//
LOCUS       WP_284693571             611 aa            linear   BCT 25-DEC-2024
DEFINITION  polysaccharide biosynthesis protein [Anoxybacillus kestanbolensis].
ACCESSION   WP_284693571
VERSION     WP_284693571.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus kestanbolensis
  ORGANISM  Anoxybacillus kestanbolensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 611)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 611)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 611)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 611)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18500220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Anoxybacillus kestanbolensis"
                     /db_xref="taxon:227476"
     Protein         1..611
                     /product="polysaccharide biosynthesis protein"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=69118
     Region          119..236
                     /region_name="FlaA1"
                     /note="NDP-sugar epimerase, includes UDP-GlcNAc-inverting
                     4,6-dehydratase FlaA1 and capsular polysaccharide
                     biosynthesis protein EpsC [Cell wall/membrane/envelope
                     biogenesis, Posttranslational modification, protein
                     turnover, chaperones]; COG1086"
                     /db_xref="CDD:440703"
     Region          279..563
                     /region_name="Polysacc_synt_2"
                     /note="Polysaccharide biosynthesis protein; pfam02719"
                     /db_xref="CDD:426938"
     Site            order(283,285..288,308..309,336..338,359..361,363,378,401,
                     417,440..443,446..447)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(309,311,315,319,334..337,340,343,361..364,367,371,
                     374,377,447..448,453)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187548"
     Site            order(363,403..405,413,441..442,448..450,453..454,
                     465..467,471,473,508,534,537)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(379,403,413,417)
                     /site_type="active"
                     /db_xref="CDD:187548"
ORIGIN      
        1 mayrtrltll mlldsaivls aiyislftlh phieifkyps lllsavtllf shhifafhyr
       61 lyhkvweyas igeliaiakt vtfsiiitaf vqwaiyedmy vralmitwmi hmlllggsrf
      121 vwriyrdrym nqkkgkkrtl iigagaagtm varqlltsre pdlcpiafid ddrtkqklhi
      181 lgipvlgttn diayvvkaqr idhiiiaips lkkselnrif secaktdakt qtvpklediv
      241 tgkvsvnqfr dvqvedllgr dpieldtesi seyikgkvil vtgaggsigs elcrqvcqfh
      301 pkkiillghg ensiyqidme lrnqykhdie iipvigdiqd rermfevmeq hrphvvyhaa
      361 ahkhvplmey npkeavknni fgtknvaeaa dtfgvetfvl vstdkavnpt nvmgatkrfa
      421 emliqqldkq sntkfvavrf gnvlgsrgsv iplfkkqiqa ggpvtvthpd mtryfmtipe
      481 asqlviqaga lakggeifvl dmgepvkivd laknliklsg ytveeigief tgirpgeklf
      541 eellnenevh peqvfpkifv gkataveeei lknfldqfpv mdcehmcewl lniannrlhr
      601 vydmkqkvvn r
//
LOCUS       WP_284693962             403 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Paraclostridium ghonii].
ACCESSION   WP_284693962
VERSION     WP_284693962.1
KEYWORDS    RefSeq.
SOURCE      Paraclostridium ghonii (Paeniclostridium ghonii)
  ORGANISM  Paraclostridium ghonii
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Paraclostridium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Paraclostridium ghonii"
                     /db_xref="taxon:29358"
     Protein         1..403
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46076
     Region          44..400
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mqeyvkgkpi ftninntnkq yeyltkdiet dvlvvgggvt gaicayylak ndvgtvliek
       61 griahlstsv ttsllqyeld dnlselreal vltdaikayk lglkaldeie mfineygnec
      121 dyikrdtlly tsktsekkai yeefkqrken gfdvkyldek enpypfdlka giisknggae
      181 idpykfthql levsekygls vyenteaksi nymndgveve tcygykikak kiivatgynt
      241 slftkrnfst kyntfniatk qlktingwkn nilirdncdp ynylrttvdn riiiggedvd
      301 fkyindeals kekyeileqr lkamfsnidd idieykycgc fastkdnlgf igpdtnhknl
      361 wyclgygang ilfailggim lnklynnevd edmrlfkvdr fdn
//
LOCUS       WP_284694401             472 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Rhodoplanes serenus].
ACCESSION   WP_284694401
VERSION     WP_284694401.1
KEYWORDS    RefSeq.
SOURCE      Rhodoplanes serenus
  ORGANISM  Rhodoplanes serenus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Rhodoplanes.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Rhodoplanes serenus"
                     /db_xref="taxon:200615"
     Protein         1..472
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50794
     Region          45..460
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mirsavmsla faaalallpa aaataasppa apaapaspgd saggalrpse ftlpnglqvv
       61 vvpdrrspvv thmvyykvgs adeppgksgi ahflehlmfk gteknpsgrf skmlatiggq
      121 enafttsdyt gyfqrvprey lgevmafead rmtglvltda nvlperdvvl eeynmrvans
      181 pdarmgeqva aalylnhpyg rpvigwrgei ekldradala fyrtfygpnn avlvvtgdvd
      241 paevrrlaea tygklpargd ltvrkrpqep ppaavrqvtl ddprvaqpsl nrsylvpsya
      301 takrgdaeal dvlaqilgsg pnsrlyqrlv vekriatgag awyqgsalda trlgvyarpt
      361 pevalpelek atdavideii tggvaadele raktrmiada vyaqdnqasm arwygtalat
      421 gstvqdvlsw pervravtae qvrdaarvwl dkrrsatgyl ikspptgeek rs
//
LOCUS       WP_284694726             538 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Geomonas sp. Red32].
ACCESSION   WP_284694726
VERSION     WP_284694726.1
KEYWORDS    RefSeq.
SOURCE      Geomonas sp. Red32
  ORGANISM  Geomonas sp. Red32
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Geobacterales; Geobacteraceae; Geomonas.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Geomonas sp. Red32"
                     /db_xref="taxon:2912856"
     Protein         1..538
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=58981
     Region          8..284
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
     Region          357..>489
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          425..455
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          460..488
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtrpaagetl klfasfvsrt lgllfgperf eelerrvapl aqeagfpace pyllwlltar
       61 ptppgelekl agvltigety flrdpksfrl feerllpelv aarrregrlr ltiwsagcss
      121 geepytiail ltrlipdlpa weirlvasdl nehalarara giytpwsfrn appwlseyft
      181 rlpdgrfels prvrsmvrfc rlnlaepssf rkgtgidqad lifcrnvmly fspsqalrtq
      241 aglhdllreg gwlfvaptev dhrnlggfrc lhvagsfvle ksgplapfpg keapllpppg
      301 ptertrrlrl psrpepgqas spappkrelg appappqvpp aaaapapapp gpspegegea
      361 ryrealdlyr egryleaaer crpipregep garalalsar alanlghcee aaelcrqaid
      421 cdrlsaanhy llslileqqg ddaaaaralr nalfidhdhl maylalgnlk rrggepeesr
      481 rcfanalrll errlphevlp eaegltagrl aeivrgllge rgagrekgss parggaeg
//
LOCUS       WP_284694748              76 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Geomonas sp. Red32].
ACCESSION   WP_284694748
VERSION     WP_284694748.1
KEYWORDS    RefSeq.
SOURCE      Geomonas sp. Red32
  ORGANISM  Geomonas sp. Red32
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Geobacterales; Geobacteraceae; Geomonas.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Geomonas sp. Red32"
                     /db_xref="taxon:2912856"
     Protein         1..76
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=8237
     Region          12..76
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mesippfptg vrylrlkqii gdkkagsppi ipisksswwa gvaagrfpkp vklgprttvw
       61 rsedilalfe hakeaa
//
LOCUS       WP_284695364             104 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein, partial [Escherichia coli].
ACCESSION   WP_284695364
VERSION     WP_284695364.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>104
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
     Region          <1..104
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 qyeyplfssv qagpfsevgs ytasdgkawv atttkaseka fwlevkghsm tapqgvrpsf
       61 pegmlilvdp aepvesgdfc vasangdsea tfkkyekdag vsyl
//
LOCUS       WP_284696448             106 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Escherichia coli].
ACCESSION   WP_284696448
VERSION     WP_284696448.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>106
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
     Region          <8..>105
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 ldnprsnkkg rtvrtvdnyi allcsllrfa yqsgfistkp fegvkklqrn rikpdpiskt
       61 efnalmesek gqsqnlwkfa vysglrhgel aalawedvdf ekgivn
//
LOCUS       WP_284696466              44 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family transcriptional regulator, partial [Escherichia coli].
ACCESSION   WP_284696466
VERSION     WP_284696466.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 44)
  AUTHORS   Nazaret,F., Alloing,G., Mandon,K. and Frendo,P.
  TITLE     MarR Family Transcriptional Regulators and Their Roles in
            Plant-Interacting Bacteria
  JOURNAL   Microorganisms 11 (8), 1936 (2023)
   PUBMED   37630496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 44)
  AUTHORS   Will,W.R. and Fang,F.C.
  TITLE     The evolution of MarR family transcription factors as
            counter-silencers in regulatory networks
  JOURNAL   Curr Opin Microbiol 55, 1-8 (2020)
   PUBMED   32044654
REFERENCE   3  (residues 1 to 44)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   4  (residues 1 to 44)
  AUTHORS   Grove,A.
  TITLE     Regulation of Metabolic Pathways by MarR Family Transcription
            Factors
  JOURNAL   Comput Struct Biotechnol J 15, 366-371 (2017)
   PUBMED   28694934
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 44)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (residues 1 to 44)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   7  (residues 1 to 44)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   8  (residues 1 to 44)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10581578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..44
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>44
                     /product="MarR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          13..>44
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
ORIGIN      
        1 mrhqrgages yqtgtgvtqm tildyiaanp gcsggeiaaa lntp
//
LOCUS       WP_284696618             126 aa            linear   BCT 25-DEC-2024
DEFINITION  RHS repeat domain-containing protein, partial [Escherichia coli].
ACCESSION   WP_284696618
VERSION     WP_284696618.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..126
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
     Region          <1..85
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
     Region          <1..41
                     /region_name="RHS_core"
                     /note="RHS element core protein; NF041261"
                     /db_xref="CDD:469161"
ORIGIN      
        1 ryydplqgrc itqdpigleg gwnqyvyasi hptysidplg lidkpapvfn relnsdayyl
       61 avnncysyal nrygnpgsri fgggglqpge lsgkefsklt cssifeaskn dgakdrerss
      121 evhfly
//
LOCUS       WP_284697569             258 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Thermoanaerobacterium sp. RBIITD].
ACCESSION   WP_284697569
VERSION     WP_284697569.1
KEYWORDS    RefSeq.
SOURCE      Thermoanaerobacterium sp. RBIITD
  ORGANISM  Thermoanaerobacterium sp. RBIITD
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Thermoanaerobacterium.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Thermoanaerobacterium sp. RBIITD"
                     /db_xref="taxon:1550240"
     Protein         1..258
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30847
     Region          4..254
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mtnydefiik iykltgidls lykekqmkrr idsliasnnc knydeffykl tidkrlynef
       61 lkyitinvte ffrnieqwni lkleilpkli kknmriwsaa cstgeepysl amilsefidl
      121 sqvfilatdi desvlekakk giynkksvek ipkeyfykyf skhgentyii seelrkninf
      181 kkhdllidky penfdliicr nvliyfndka kddiykkinl slsdegvffv gsteqiifpy
      241 kynfepvktf fykklknk
//
LOCUS       WP_284698122              43 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl-CoA carboxylase biotin carboxyl carrier protein, partial
            [Shigella dysenteriae].
ACCESSION   WP_284698122
VERSION     WP_284698122.1
KEYWORDS    RefSeq.
SOURCE      Shigella dysenteriae
  ORGANISM  Shigella dysenteriae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
REFERENCE   1  (residues 1 to 43)
  AUTHORS   Li,S.J. and Cronan,J.E. Jr.
  TITLE     The gene encoding the biotin carboxylase subunit of Escherichia
            coli acetyl-CoA carboxylase
  JOURNAL   J Biol Chem 267 (2), 855-863 (1992)
   PUBMED   1370469
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423502
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..43
                     /organism="Shigella dysenteriae"
                     /db_xref="taxon:622"
     Protein         <1..43
                     /product="acetyl-CoA carboxylase biotin carboxyl carrier
                     protein"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
     Region          <1..43
                     /region_name="AccB"
                     /note="Biotin carboxyl carrier protein [Lipid transport
                     and metabolism]; COG0511"
                     /db_xref="CDD:440277"
ORIGIN      
        1 tlciveamkm mnqieadksg tvkailvesg qpvefdeplv vie
//
LOCUS       WP_284699717             104 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Planococcus beigongshangi].
ACCESSION   WP_284699717
VERSION     WP_284699717.1
KEYWORDS    RefSeq.
SOURCE      Planococcus beigongshangi
  ORGANISM  Planococcus beigongshangi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Planococcus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Planococcus beigongshangi"
                     /db_xref="taxon:2782536"
     Protein         1..104
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11297
     Region          2..104
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mawislviag lfemagvami nkwhhdrkwl smammlagfa fsfiflsiam etlpmgtaya
       61 vwtgigasgg aiigmlfyne dkdwkrilfi amvlgsavgl kmvs
//
LOCUS       WP_284699725             108 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Planococcus beigongshangi].
ACCESSION   WP_284699725
VERSION     WP_284699725.1
KEYWORDS    RefSeq.
SOURCE      Planococcus beigongshangi
  ORGANISM  Planococcus beigongshangi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Planococcus.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Planococcus beigongshangi"
                     /db_xref="taxon:2782536"
     Protein         1..108
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12285
     Region          23..98
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(27..28,30,33,36..37,40..41,44,74,93..94,96..98,
                     100..102)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(28..29,33..35,48..50,59..62,64..65,68..69,71..72,
                     78..80,85..87)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(48,51,93)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mmkqdetfta sehpldeetl fivsqtfkal sdptririln llcvaehsvn elaekldlgq
       61 stvshqlrfl kqlrlvkfrr agttlyyskd dehvinllnq aiehaahp
//
LOCUS       WP_284700308             355 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: M24 family metallopeptidase [Planococcus].
ACCESSION   WP_284700308
VERSION     WP_284700308.1
KEYWORDS    RefSeq.
SOURCE      Planococcus
  ORGANISM  Planococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Planococcus"
                     /db_xref="taxon:1372"
     Protein         1..355
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=38744
     Region          7..355
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mntlklqklr aemkqrdvea llvtspfnlr yiteftgtag laivtaeqav fitdfryteq
       61 ageqvkefdv iqaeknlmde tvksvkslgi rtlafeqdym tystvvqyks kidadlepvs
      121 nliekirmik tpdevailka aakiaddafe hicgfirpgl televsnele ffmrkqgats
      181 ssfdtivasg lrsalphgva tdkviekgdm itldygalyn gyisditrtv avgepsaqmk
      241 eiydivlkaq elgvekigpg msgieadaia rdyikskgyg eafghstghg iglevhegpg
      301 lsfrsetvle pgmavtvepg iylpgvggvr ieddilvtes gnerltnstk elril
//
LOCUS       WP_284700538             294 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Serratia symbiotica].
ACCESSION   WP_284700538
VERSION     WP_284700538.1
KEYWORDS    RefSeq.
SOURCE      Serratia symbiotica
  ORGANISM  Serratia symbiotica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Serratia symbiotica"
                     /db_xref="taxon:138074"
     Protein         1..294
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=34096
     Region          2..275
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 msgmvipysl kseyggvrff ivsrffrfyp aywfsiliav itsmlfyqvq peikvvllnt
       61 tmlqsvfgil nlfgvywtli iellfyglcv fififgllkn rtsnfiiavs flilavaisw
      121 lrwyldrkip vtvplamslm ffgslwreat vkkdiysrni ciwwticfal slpaicflas
      181 sksygfgenp iaylmtyacs vaffivmtsk wkltfrpfif lgaisysmyl lhqfahelfs
      241 rkfnisgdfs flkislylla vlslsylsyr fiekpnlifs ikikgklhfa rktl
//
LOCUS       WP_284700549             294 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Serratia symbiotica].
ACCESSION   WP_284700549
VERSION     WP_284700549.1
KEYWORDS    RefSeq.
SOURCE      Serratia symbiotica
  ORGANISM  Serratia symbiotica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Serratia symbiotica"
                     /db_xref="taxon:138074"
     Protein         1..294
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=34130
     Region          5..275
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 msrmvmpysl kseygavrff ivsrffrlyp aywfsvliav itsmlfyqvq peikvvllnt
       61 tmlqsvfgip nlfgvywali iellsyglcv fififgllkn rtsnfiitvs flilavaisw
      121 lrwyldrkip vaiplalslm ffgslwrevt vkkdiysrnl ciwwticfal slpaicflas
      181 sksygfgenp iaylmtyacs vaffivmtsk wkltfrpfif igtisysmyl lhqfvlelfs
      241 rkfnisgnfs flkislylla vlslsylsyr fiekpnlifs ikikgklhfa rktl
//
LOCUS       WP_284702819             411 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Peribacillus simplex].
ACCESSION   WP_284702819
VERSION     WP_284702819.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..411
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45542
     Region          1..400
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mkrkaleglk vlemgqliag psagrlfaef gaevikvenp ksgdpirnwr ivengtslww
       61 yvqarnkksi tldlrqhegq evirglakei diiienfrpg tlekwgigye elkkinprli
      121 mvrvsgygqd gpykdkpgfg aigeamgglr yltgypdrpp trvgisigds isslyaviga
      181 mlavfhrdig gsnqgqcvdv alyesifslm esmlpeydrt gvirertgst lpgitpsnty
      241 eckdgkyvvi gangdgifkr lmvviglpey adddrfknnn trsehaelld ksierwtksl
      301 dlteilnild eagvpagaiy siedivndph yqaremiqev vingigklki pgivpklset
      361 pgdiewagpe lgqhnkeili eklqlskeyl evleekgiig nlerygtkvk n
//
LOCUS       WP_284702855             471 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Peribacillus simplex].
ACCESSION   WP_284702855
VERSION     WP_284702855.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus simplex
  ORGANISM  Peribacillus simplex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Peribacillus simplex"
                     /db_xref="taxon:1478"
     Protein         1..471
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=50419
     Region          134..355
                     /region_name="Peptidases_S8_Subtilisin_subset"
                     /note="Peptidase S8 family domain in Subtilisin proteins;
                     cd07477"
                     /db_xref="CDD:173803"
     Site            order(141,171,214,233,262,323)
                     /site_type="active"
                     /db_xref="CDD:173803"
     Site            order(141,171,323)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:173803"
     Region          <391..>470
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
ORIGIN      
        1 mknnkkknrk mnlvnvmavs alllsipvst asakaidtvn vvggkeklii nfkddvneke
       61 ksqikregki krnlelinav smeidsekve qlkknpnvks iepdiklnia qsigygqegv
      121 napeswssgl tgkgtkvavi dsgvsthpdl ivsggqsfvd ytnsyaddng hgthvsgiis
      181 aenndigvvg vapdsdifal kamdqygsgy lsdiieaidw svannmdvin mslgttqass
      241 alksavnkay qngilvvaaa gnesssvnyp akyssviavs atdennklay fsnygqevev
      301 sapgtnilst sslgdyenms gtsmatpfva gqlsllkeld ptytavqlre elhknvldlg
      361 tagkdkfygy gliqapvksv npeesevvst pvtpsnfkat kvtnryvtln wdsidnatyy
      421 qvtrdnvvvy kgsnltftdt svsryktyly kivagnesgt gdsasitvkt r
//
LOCUS       WP_284702921              84 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-binding oxidoreductase, partial [Escherichia coli].
ACCESSION   WP_284702921
VERSION     WP_284702921.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>84
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
     Region          <1..84
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 qviretrehc aqapffvamv ghvgdgnfhl smqldrddpa efalasaind rmvalalklg
       61 gtctgehgvg igkmkfmrae hgda
//
LOCUS       WP_284703285             246 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Streptococcus
            pneumoniae].
ACCESSION   WP_284703285
VERSION     WP_284703285.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus pneumoniae
  ORGANISM  Streptococcus pneumoniae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Streptococcus pneumoniae"
                     /db_xref="taxon:1313"
     Protein         1..246
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28201
     Region          2..143
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 matyetfaav ydavmddsly dkwtnfslrh lpktkekkkl lelacgtgiq svrfsqagfd
       61 vtgldlsadm lkiaekrats akqkiafieg nmlnlskagk ydfvtcysds icymqdevev
      121 gdvfkdvyna lneegvfifd vhstyqtdev fpgysyhena edfamlwdty edeaphsivh
      181 eltffikgvd gsfsrhdevh eertyeilty dilleqagfk sfklyadfed keptetstrw
      241 ffvaqk
//
LOCUS       WP_284703468              40 aa            linear   BCT 25-DEC-2024
DEFINITION  single-stranded DNA-binding protein [Coprococcus intestinalis].
ACCESSION   WP_284703468
VERSION     WP_284703468.1
KEYWORDS    RefSeq.
SOURCE      Coprococcus intestinalis
  ORGANISM  Coprococcus intestinalis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Coprococcus.
REFERENCE   1  (residues 1 to 40)
  AUTHORS   Bianco,P.R.
  TITLE     The tale of SSB
  JOURNAL   Prog Biophys Mol Biol 127, 111-118 (2017)
   PUBMED   27838363
REFERENCE   2  (residues 1 to 40)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 40)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..40
                     /organism="Coprococcus intestinalis"
                     /db_xref="taxon:2949662"
     Protein         1..40
                     /product="single-stranded DNA-binding protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=4314
     Region          1..>38
                     /region_name="Ssb"
                     /note="Single-stranded DNA-binding protein [Replication,
                     recombination and repair]; COG0629"
                     /db_xref="CDD:440394"
ORIGIN      
        1 mntivlmgrl ardpetklas tqkgqtkvsr fplvvkrncg
//
LOCUS       WP_284703658             400 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Clostridium swellfunianum].
ACCESSION   WP_284703658
VERSION     WP_284703658.1
KEYWORDS    RefSeq.
SOURCE      Clostridium swellfunianum
  ORGANISM  Clostridium swellfunianum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Clostridium swellfunianum"
                     /db_xref="taxon:1367462"
     Protein         1..400
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43288
     Region          3..377
                     /region_name="FucP"
                     /note="Fucose permease [Carbohydrate transport and
                     metabolism]; COG0738"
                     /db_xref="CDD:440501"
ORIGIN      
        1 miltvlliii yiafislglp dsllgsawps myqsmgvpis yagivsmiia ggtivsslfs
       61 dkvirkfgtg lvtsisvfmt agallgfsls gefyhlclfa iplglgagsv daalnnfval
      121 kykakhmswl hcfwgigamt gpiimsyyle rgaifqsgyr tvaiiqftlv iillvtlplw
      181 kkvssfnsst snkdesggke qeqkvlskre llklpgakqa liaffcycai eatiglwgss
      241 yvvmshgisa etaakwaslf yfgitfgrfl sgfitiklsn rqmiylgevl igtgiimmmv
      301 pfgqvtllmg fvmtgigcap iypsllhetp vnfgaqysqs imgvqmacay vgstfmpplf
      361 gvlasrigya lmpfyaasif limfimiivl nrsvddekns
//
LOCUS       WP_284704753             748 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Nocardioides bruguierae].
ACCESSION   WP_284704753
VERSION     WP_284704753.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides bruguierae
  ORGANISM  Nocardioides bruguierae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 748)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 748)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 748)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 748)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..748
                     /organism="Nocardioides bruguierae"
                     /db_xref="taxon:2945102"
     Protein         1..748
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76187
     Region          26..748
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msattptpaq asspgapgag eeapgqdvdl aitgmtcasc ahrierkltk legvtasvny
       61 atetahvtap vgydlqrlld tvsaagygas vpepdaeped gdpvlagyar rlvvsavltv
      121 plvvlsmvmp lqfpgwtwva lvlaapvvtw gawpfhraav lgarhgattm dtlvslgvta
      181 stvwsvavlv sgpdsghlyl etaavittfl lagrwlerra rrsagaalrs lleagareat
      241 llpgwsqehr edgvertvpv aelavddvvl vrpgqqlptd gvvlsgasai dasvitgesv
      301 pvdagpgdev vggtlnvggr lvvratavge qtrlaqlarm veeaqtgkaa aqrladrisg
      361 vfvpvvlvia latlvgwval tgdlgsavta avavlvvacp cvlglatpta lvagtgrgaq
      421 lgilvrgpea leaaravsvv aldktgtltt grmslvgvva asaeavevhr vagalesasd
      481 hpvaraiaed rpvdgarved fadrpghgvv gtvvspdgta lravvgrpel leregltisp
      541 vlhtaldasr eqgrtavlvg wdgearglle vadtvrdgaa davaelrrlg lrpvlltgdh
      601 eaaargvaaq vgidevvagv vpeekvdavr rlqsdgtgva mvgdgvndaa alatadlgia
      661 mgtgtdaakq agdlvlvrgd lavvadavrl srrtlgtira nlfwafgynv aalplaalgl
      721 lnpmiagaam aassvcvvan slrlrrfr
//
LOCUS       WP_284705088             368 aa            linear   BCT 25-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Flavobacterium
            tyrosinilyticum].
ACCESSION   WP_284705088
VERSION     WP_284705088.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium tyrosinilyticum
  ORGANISM  Flavobacterium tyrosinilyticum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Flavobacterium tyrosinilyticum"
                     /db_xref="taxon:1658740"
     Protein         1..368
                     /product="Glu/Leu/Phe/Val family dehydrogenase"
                     /EC_number="1.4.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016639 - oxidoreductase activity, acting
                     on the CH-NH2 group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39795
     Region          26..358
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mdatfatgke lqkmdpvfgq lsfddheqiv fcndkdtglk aiigihnsvm gpalggtrmw
       61 nyntewealn dvlrlsrgmt fksaitglni gggkaviigd aktqktpelm rkfgefvhsl
      121 sgryitaedv gmetkdmdtv rdvtpyvtgi seerggsgnp spitaygvyl gmkaaaksqf
      181 gtdvlegkkv lvqgighvge tlveyltkeg aqvtisdine eklfqvasky natiytgedl
      241 ytadvdiyap camgatindn tvdkikakvi agaannqlad envhgarlqe rgilyapdfl
      301 inaggiinvy aelanygkae imtkteniyn ttleiidfaa kngitthkaa ltiaqnridq
      361 rrienask
//
LOCUS       WP_284706200              84 aa            linear   BCT 25-DEC-2024
DEFINITION  glutaredoxin family protein [Micromonospora phytophila].
ACCESSION   WP_284706200
VERSION     WP_284706200.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora phytophila
  ORGANISM  Micromonospora phytophila
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 84)
  AUTHORS   Shelton,M.D., Chock,P.B. and Mieyal,J.J.
  TITLE     Glutaredoxin: role in reversible protein s-glutathionylation and
            regulation of redox signal transduction and protein translocation
  JOURNAL   Antioxid Redox Signal 7 (3-4), 348-366 (2005)
   PUBMED   15706083
REFERENCE   3  (residues 1 to 84)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   4  (residues 1 to 84)
  AUTHORS   Fernandes,A.P. and Holmgren,A.
  TITLE     Glutaredoxins: glutathione-dependent redox enzymes with functions
            far beyond a simple thioredoxin backup system
  JOURNAL   Antioxid Redox Signal 6 (1), 63-74 (2004)
   PUBMED   14713336
REFERENCE   5  (residues 1 to 84)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002164
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Micromonospora phytophila"
                     /db_xref="taxon:709888"
     Protein         1..84
                     /product="glutaredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=8808
     Region          9..81
                     /region_name="GrxC"
                     /note="Glutaredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG0695"
                     /db_xref="CDD:440459"
ORIGIN      
        1 msgpggqapv tvysrpgcpy cyllrrglrr rnvaftevdi wadpdaaaav ravangnetv
       61 ptvhvagqwl vnpraatvaq layg
//
LOCUS       WP_284706266             169 aa            linear   BCT 25-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Micromonospora phytophila].
ACCESSION   WP_284706266
VERSION     WP_284706266.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora phytophila
  ORGANISM  Micromonospora phytophila
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Schwartz,C.J., Giel,J.L., Patschkowski,T., Luther,C., Ruzicka,F.J.,
            Beinert,H. and Kiley,P.J.
  TITLE     IscR, an Fe-S cluster-containing transcription factor, represses
            expression of Escherichia coli genes encoding Fe-S cluster assembly
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 98 (26), 14895-14900 (2001)
   PUBMED   11742080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Micromonospora phytophila"
                     /db_xref="taxon:709888"
     Protein         1..169
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=17228
     Region          2..141
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mklsggvewa lhccvvltta tepvpaarla elhdvsgsyl akqlqalsra glvtsvqgka
       61 ggyvltrape litvldvvaa vdgaqpafvc teirqrgpla apqeactrpc piaramagae
      121 aawraalqai svadlassvd edygptalag irtwlngpdh gdtagaeqg
//
LOCUS       WP_284706655             990 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_284706655
VERSION     WP_284706655.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=110129
     Region          2..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvvsfigmat qevpvkanln ivlksdteql eevmvvaygt akksaftgsa atiknekiat
       61 rqtsnvtnal agqvagvqtt snngqpgkda evrirgigsi sasnkplyvv dgvpydgeis
      121 aistsdiesm tvlkdaasna lygargangv ilittkrgks gearvtfdak wgvnkrgvpn
      181 yetitdpatf yelnyssiyn adlkgyaaag dlakanayan qamlsstylg yqvysipqgq
      241 qligmdgkln pnatlgysdg tyyytpdnws deifennlrq eynlsisgat ekmnyymsag
      301 ylddkgivpn sgfqrysarl kadyqvkpwl kmggnvsfth ydsreqdteg gtsnanifya
      361 snimgaiypm yvrdaqgnim vdnrgflryd ygkpgqdsng srntipnanp lasymldkmk
      421 ysgdvvsgkw sadidiwngi kakvnigvdv nnvratemvn pfygqysets gvgglisvss
      481 ertfsvnqqy lltynktfnd vhnvdilagh esydykyqyl ygqreklydp nvpelgngim
      541 nqsnnsysrn yategwlfra qydydgryfv sasfrrdass cfhpdnrwgn fwsvgagwll
      601 skekflenqs widmlkfkis yglqgndnlm fqgglyrnyy pyqdqytlan sngdfstsly
      661 ykgnkeitwe tshsfntgfd fafwggklgg sveyfsrktt dmlyfkpvaa smgysrfpen
      721 vgsmvnrgve ldlysniien knfswnvnfn lthfknkvle lspelngqli dgariyrede
      781 smyqlylpky vgvdsetges lwalvtpden gntvtksysv asenrfasgd ilpkvyggfg
      841 tsvtaygfdl svsfayqlgg rildytyqgl mdvaatgsal hkdmlkawtp enkntdvprm
      901 nindqytnrl tdrfltssdy lslqnitlgy tlpknltrkm qidgvrvffv adnvalltar
      961 kgldprqgyv aadnvyspir tisggislnf
//
LOCUS       WP_284707201             203 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: YceD family protein [Rhodococcus].
ACCESSION   WP_284707201
VERSION     WP_284707201.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..203
                     /product="YceD family protein"
                     /calculated_mol_wt=21916
     Region          16..183
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 msthrrsssr srrdadfvld tvklgrrpgs mrtvervvta prrigldmia ieegseidld
       61 lrleavsegv lvtgsvsadt vgecsrclep fsgsvdlslt elfaypdsat eettdedeiy
      121 rveddeidle pviidavgla lplqplcsdd cqglcpecgv rlaiaesghg hdildprwag
      181 laakfgvesd psknlvnnea eek
//
LOCUS       WP_284708313             290 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Rhodococcus sp.
            MSC1_016].
ACCESSION   WP_284708313
VERSION     WP_284708313.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. MSC1_016
  ORGANISM  Rhodococcus sp. MSC1_016
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Rhodococcus sp. MSC1_016"
                     /db_xref="taxon:2909266"
     Protein         1..290
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31122
     Region          7..242
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 milwggtlsq apvehrlfaa aragfhaisv apmdfgppdr ilqradcvak lanrlnisva
       61 cidpvtswlp lplqagsipt anpaqrrygd lfgrysvsec lrlaerlgst tisaiepygv
      121 dfghqlvvds faalcesaad rgltiqlepm pfssifdlat ahrivadssa knagivfdtw
      181 hfdrsggtrd qlrtlprgiv tsiqlndgrr seaedlweea stqrllpgeg sfgiaesida
      241 lagrladspl igpevisadh rlspvdyvaq iaydaclpya qragldidpv
//
LOCUS       WP_284708892             206 aa            linear   BCT 25-DEC-2024
DEFINITION  dTDP-4-dehydrorhamnose 3,5-epimerase family protein [Rhodococcus
            sp. MSC1_016].
ACCESSION   WP_284708892
VERSION     WP_284708892.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. MSC1_016
  ORGANISM  Rhodococcus sp. MSC1_016
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004867
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Rhodococcus sp. MSC1_016"
                     /db_xref="taxon:2909266"
     Protein         1..206
                     /product="dTDP-4-dehydrorhamnose 3,5-epimerase family
                     protein"
                     /EC_number="5.1.3.-"
                     /GO_function="GO:0016857 - racemase and epimerase
                     activity, acting on carbohydrates and derivatives
                     [Evidence IEA]"
                     /calculated_mol_wt=21985
     Region          1..186
                     /region_name="RfbC"
                     /note="dTDP-4-dehydrorhamnose 3,5-epimerase or related
                     enzyme [Cell wall/membrane/envelope biogenesis]; COG1898"
                     /db_xref="CDD:441502"
ORIGIN      
        1 mkvktrqlqv pgsweitpeq fgddrgafle wfkgsifeds vghslnlaqa ncsvsaagvl
       61 rgihfadvpp gqakyvtcvr gavldvvvdi rigsptfgtw dsvllddvdr raiylseglg
      121 haflsledns tvvylcstgy tpgaehgihp ldpevgiewp tttragapmn ftlsdkdaaa
      181 pslheavqag mlpscdevke wvsgla
//
LOCUS       WP_284708893             115 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: fluoride efflux transporter FluC [Rhodococcus].
ACCESSION   WP_284708893
VERSION     WP_284708893.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..115
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12244
     Region          1..113
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 mvggavgaaa ryqlwrwwpd didefpfttf ainvmgcfif gllfvvipas ahgtialirp
       61 fllfgvmsgf ttfsffavqg vtltsprvgv vyllvtplaa laaamvgarv grlsr
//
LOCUS       WP_284709102             391 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            hygroscopicus].
ACCESSION   WP_284709102
VERSION     WP_284709102.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces hygroscopicus
  ORGANISM  Streptomyces hygroscopicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            violaceusniger group.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Streptomyces hygroscopicus"
                     /db_xref="taxon:1912"
     Protein         1..391
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41222
     Region          1..278
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mnrptarvla lleilqaggt rtvaeladrl gvdertvrry ighlidldvp vrsvrgrygg
       61 yrlapgyrmp plmltdeeal avllglvagr raglvttsva aaesaaakvr rvlpealgrr
      121 ldallttadf taparpvvvp gtdvllmfae aardrrpvai gytgwkgrrs ertvhpygiv
      181 ahsgrwyvtg adsasgevrm frldrietat alpgsfevpe gfdpaarvls glagvpylhe
      241 vslrvrgtvd qvrhrlppgl atvtelpags tretaqaaag garptgadar pgggttehar
      301 gtappgsgta avarrtpqtm rhstqparrd hqtarnrpra arhriravrp stpghppvpg
      361 rgraadgcgs gcgpsgwsgs ppcspgwtsr s
//
LOCUS       WP_284709202             138 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Marinobacter
            sediminum].
ACCESSION   WP_284709202
VERSION     WP_284709202.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sediminum
  ORGANISM  Marinobacter sediminum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Marinobacter sediminum"
                     /db_xref="taxon:256323"
     Protein         1..138
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15050
     Region          1..69
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mnlgqairrl rkqqgmtlae ladrcdshvg nlsriergla rpslellyrl aealdlsltd
       61 ifsvaekkql dseqvalnaa fislleedrq llldfaellq rrstnpmtsv svgqdslpad
      121 ksgsgspkdg iestpkrs
//
LOCUS       WP_284711532             315 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Dyadobacter sp. MSC1_007].
ACCESSION   WP_284711532
VERSION     WP_284711532.1
KEYWORDS    RefSeq.
SOURCE      Dyadobacter sp. MSC1_007
  ORGANISM  Dyadobacter sp. MSC1_007
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Dyadobacter.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Dyadobacter sp. MSC1_007"
                     /db_xref="taxon:2909264"
     Protein         1..315
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36078
     Region          5..194
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 msiffsvvip lynkekyivk tldsvlcqty gnfeviivdd gstdnsvqlv kkyldnrikv
       61 isqknagvsa arntgisnsq ydfislldad dwwgprylen mrnlilkypk adlyaseytr
      121 vfkgrlmpsm svlkdgidhd lvnpliygik ngalplhtss vvirksilkr tglfddrisf
      181 yedydlflri isfgklaygk kggafynidv spddkltgkl pplerhfisy ieklepffke
      241 dkllrlfadr liitsmityh rsgtlkreiv elskkvnsss yylkdkflls lppiiantiv
      301 eakikinelf ekdly
//
LOCUS       WP_284711593              67 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Dyadobacter sp.
            MSC1_007].
ACCESSION   WP_284711593
VERSION     WP_284711593.1
KEYWORDS    RefSeq.
SOURCE      Dyadobacter sp. MSC1_007
  ORGANISM  Dyadobacter sp. MSC1_007
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Dyadobacter.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Dyadobacter sp. MSC1_007"
                     /db_xref="taxon:2909264"
     Protein         1..67
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7257
     Region          1..>58
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mhvggiiker rkllnitqet laemsgvglr tlkelesgkg nptiitlekv advlgmqlll
       61 qiksmnq
//
LOCUS       WP_284713426             366 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Streptomyces sp. G3].
ACCESSION   WP_284713426
VERSION     WP_284713426.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. G3
  ORGANISM  Streptomyces sp. G3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 366)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Streptomyces sp. G3"
                     /db_xref="taxon:690144"
     Protein         1..366
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=36931
     Region          21..365
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mkasgangtd aagdvtadgq asvapgvrfg gvsfvwrpwv agvtlllava gflvfclsig
       61 vgdfpiglpr vvatilgrge qvdefvimdl rmpralaglv vgialgvsgt ltqsiarnpl
      121 aspdvlgits gagavavflv tvsggaatav vdsvglsaaa lagglgtgll vyfmawrrgi
      181 dgfrliligi svnavmqait twllvtadir dvaraqawlv gslddrswse vhvalwctlv
      241 llavvacvaf qfkplhfgde vaaglgvryg avravlllca vllagvavsa agpvpfvalv
      301 apqvamrlar cptpplvasg lvgallltgs dlvartalpv slpvgvvtaa iggpflvyll
      361 vranrg
//
LOCUS       WP_284715008             106 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces sp. G2].
ACCESSION   WP_284715008
VERSION     WP_284715008.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. G2
  ORGANISM  Streptomyces sp. G2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Streptomyces sp. G2"
                     /db_xref="taxon:1684471"
     Protein         1..106
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11784
     Region          45..101
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 msarppastp vrtphptqea sprstsprpq hhltadrpsp fagtwystre latalrvdvs
       61 tlrrwrtsrp pqgppfvsis ervvmysaad vdewlqsrrt apnrka
//
LOCUS       WP_284715311             152 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Streptomyces].
ACCESSION   WP_284715311
VERSION     WP_284715311.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13390132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..152
                     /product="GntR family transcriptional regulator"
                     /calculated_mol_wt=16389
     Region          15..>93
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
     Region          83..143
                     /region_name="WHTH_GntR"
                     /note="Winged helix-turn-helix (WHTH) DNA-binding domain
                     of the GntR family of transcriptional regulators; cd07377"
                     /db_xref="CDD:153418"
     Site            order(103,105..106,114..118,120..121,124,134..135,
                     137..140)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:153418"
ORIGIN      
        1 meggfvpevs prgtylliad alrkdiekgs hggalpseaa lmrehdvsrn tvrralktle
       61 aerlitsvpg tgwrmsaqpi rplvdrmtdl ikedelavgd aypsetklca rfgvsrtavr
      121 ralaqmegtg llatvhgkgr tvralpndpe es
//
LOCUS       WP_284714177             533 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: M23 family metallopeptidase [Streptomyces].
ACCESSION   WP_284714177
VERSION     WP_284714177.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..533
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55866
     Region          <133..>399
                     /region_name="PRK10263"
                     /note="DNA translocase FtsK; Provisional"
                     /db_xref="CDD:236669"
     Region          334..526
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mvndqhphag yagdgahttg gyaadplfgt wsdpgqadhs gqwdlgqyaa tgtydttgay
       61 etgawnttag stpgydttgq wdttgqwata tdaypagtsy gqpeqydttg qwdasawtea
      121 qhtgqfenlh sgayaaqgay gheaydttgq waapafatdt gaydatawnq aadpaeplvp
      181 qqyvpqaehv drtsefafpy epapepetaa yepeaayead tayeaetayg teayepvayd
      241 dapghedpeg pagqdgasda pvaevrtdav agarpvrrss ggsrsrrrtp akrsalltva
      301 vpsacvmgva giaaasvggl tggatestkq kdttalaads aavqqiaant aldtqlsald
      361 advrdfgdra srtqeridlk arqaadkkkr eeeaarkeam rpkfalpvkl hqlsarfgqs
      421 gvnwmsvhtg idfpvmtgtp vmaatdgtvr tqlnyaygnm vivtapdgte twychlssak
      481 irtgsvkagd viaysgdsgn stgphlhfev rpgggsaidp lawlrskgln ptg
//
LOCUS       WP_284715639            1088 aa            linear   BCT 25-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces sp. G2].
ACCESSION   WP_284715639
VERSION     WP_284715639.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. G2
  ORGANISM  Streptomyces sp. G2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 1088)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Streptomyces sp. G2"
                     /db_xref="taxon:1684471"
     Protein         1..1088
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=116302
     Region          1..245
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          129..1075
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          721..751
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          756..789
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          842..870
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(843,846..847,850..851,853,883,886..887,890..891,
                     893..894,923,926..927,930..931,934)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          881..911
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          922..948
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrfavlgpla vtdergaelt pgspklrtll aalllapnrv vpldrledav wdgrppasar
       61 aslhnhvarl rralgdptrv rsrdgglvlr vepgeldadr lvhaldeara arslgdwdrv
      121 arvteevpal wrdtplaefp alatraasdt arwqearlqa leirldaaaq agllhehlpe
      181 lrlltrefpl repfhvhlvl alhhagrrae aleayhalrh alaetlgiep gpagraafqr
      241 aleeepsata parprtpapp avpmalprdp vsftgrapql dailaelipp eedgtdtvpa
      301 tpdvrvyavd gmpgigktaf alrlahrvra aypdgqiflp lhahtagtpp lapedalael
      361 llaagenprr ipeglaarag awrsriagrr mlivlddaag teqiepllpg tpgslvlvts
      421 rrrlealada rpltldtlpe deavglliar sgraditrdd psvarlarmc ghlplalhlv
      481 aarlrhrrhw tpadladdlg saagrtaala aehvsvaaaf elsyraltad crtllrrigl
      541 lpgtdldlya aaalygsdla tvrglvdely drhlidepap grftthdlvr syartlgred
      601 dpavredavd rllahclhta tdaslrlarh rtdppalata rpvrppafad ayeatawftt
      661 ehanlraaft haarhgrhev ttglsaalhd flrssghwde artvhgtala aaraagdlpg
      721 eatalhhlav vdslggryad aeeglrrala lfrrlgdpar egmvlsglgr vlrltgryed
      781 avtaldealp lltdarddlg eanarvesgh vlqltgrypq aasaveaala lyrrsgdtlg
      841 lanacaalad icrslgryah aldhhreald lyrglgnrmg eanvladlgd vlrltgacee
      901 aadalteaar rhhdlgsrlg eaqsltylsr vllrrgapae aaehldrara icasvnsamg
      961 layvrvhtae aahvggdhvr aaeeaeacaa lfrelgdpgg ettathlhal alhaagapae
     1021 alarheaala latrirapye rllahtgiad cltalgtpae aashlrqald latrlgvpea
     1081 gplrerla
//
LOCUS       WP_284716792             142 aa            linear   BCT 25-DEC-2024
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Streptomyces sp.
            G1].
ACCESSION   WP_284716792
VERSION     WP_284716792.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. G1
  ORGANISM  Streptomyces sp. G1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Streptomyces sp. G1"
                     /db_xref="taxon:361572"
     Protein         1..142
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15596
     Region          6..112
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mitvartavr hltvlydasc plcvhirhwl lgqrwlvplr lipaasfeaq rlyprldhas
       61 tlkeitvigd sgqvwtgtda fivclwalae hrpkanwlat aagrpfaraa mytastwrea
      121 vrdgssandg epacddqcsa pr
//
LOCUS       WP_284716957             323 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp. G1].
ACCESSION   WP_284716957
VERSION     WP_284716957.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. G1
  ORGANISM  Streptomyces sp. G1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10648172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Streptomyces sp. G1"
                     /db_xref="taxon:361572"
     Protein         1..323
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35303
     Region          1..248
                     /region_name="YrhO"
                     /note="Sugar-specific transcriptional regulator TrmB
                     [Transcription]; COG1378"
                     /db_xref="CDD:440988"
     Region          260..316
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mgldteaesv yrlmltqqdw gvaeiaghlt cpeesvrgal drlaelnllr rsmqapgglr
       61 pvspdlgfql llqrqqanll aqqqqfaesq aaiskllgey selrtgerhg veylqgidai
      121 qtrleelahr stseclsfmp ggaqsaasld asrpldedlm rrgvrvltvy ldsvrndnpt
      181 veyaqwlhgn ggevrtvpal plrmvlfdre vallpvdpnn tkkgavqltg pgvltalasl
      241 feqmweiaap igstrdrdea gltaqerell rqltqgatde iaakklgigl rtarrmmsem
      301 marlgarsrf eagvlaskag wtd
//
LOCUS       WP_284718210             267 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Sinorhizobium
            kummerowiae].
ACCESSION   WP_284718210
VERSION     WP_284718210.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium kummerowiae (Ensifer kummerowiae)
  ORGANISM  Sinorhizobium kummerowiae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 267)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Sinorhizobium kummerowiae"
                     /db_xref="taxon:158892"
     Protein         1..267
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27929
     Region          1..245
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtqhskgtal vtgassgiga iyadrlarrg ydlilvarnq trldelarrl tdetgrsvev
       61 vaadlgkrtd aariekvlrt dasitmlvnn agigatgpll asdvdkmeem ialnvnaltr
      121 ltyaavpgfv argagaiini asivgiapev lngvygaska fvlaftlslq kelegrniri
      181 qavlpgatat nfwgiagtpv ehlpneivmp aedmvdaala gfdlgepiti pslpdaadwe
      241 ayeaarqklv pnlslsvpaa ryraaaa
//
LOCUS       WP_284718414             410 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium
            kummerowiae].
ACCESSION   WP_284718414
VERSION     WP_284718414.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium kummerowiae (Ensifer kummerowiae)
  ORGANISM  Sinorhizobium kummerowiae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 410)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Sinorhizobium kummerowiae"
                     /db_xref="taxon:158892"
     Protein         1..410
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44864
     Region          29..405
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(140,142,263,265,297..299,340)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mgirkyamlg afalasvslp tfsasaedvt isvwsldrdi qpapnliedf nklntgikve
       61 yrqiqfddvv seamraystg qapdiiavdn pehalfasrg afldlsemia kssvvkpeny
      121 fkgplasvtw dgkyygvpka tntialyynk dmfkakgldp nkppqtwdel veaarkltdp
      181 aqnvygitfs akaneegtfq flpwaqmagg gydninaega vkaldvwkti ideklaspdt
      241 ltrsqwdatg tfnsgnaama isgpweidrm leeakfdwgv allpvpevga erssamgdfn
      301 wavfantehp eeafkvleyf vsqddrmfkd fgqlpprsdi ailatgepkk daalqvfveq
      361 lkyakprgph pawpkiskai qdaiqaaltg qmsskealdq aaekikavlg
//
LOCUS       WP_284718439             473 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Sinorhizobium kummerowiae].
ACCESSION   WP_284718439
VERSION     WP_284718439.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium kummerowiae (Ensifer kummerowiae)
  ORGANISM  Sinorhizobium kummerowiae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 473)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Sinorhizobium kummerowiae"
                     /db_xref="taxon:158892"
     Protein         1..473
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=50289
     Region          7..466
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mkeettreil qraaehaahf rekiaelpqr pelsypaale tfretlperg sagsevigel
       61 aakaepglha mtgprffgwv iggshpvgva adwmtsawgq nagnhhaapa aaaaeaiaan
      121 wlldlldlpr essvgfatga tlanficlaa argevlrqag wdveaqglfg appvavligd
      181 dahatvfsal qflgfghdrv lrvqtddmgr itgpafagaa aqvsgpciai lqagqintga
      241 fddfagimpi arglgawvhv dgafglwara tpgkrgltdg ideahswatd ghkwlqtpyd
      301 cgyaiirdqe ahrramtiaa sylppttege rdpshfvpel srrargfatw amikhlgreg
      361 iaamvdrhcr varaiaerls gedginvlne valnqvlvrf gaampgeegd rltqattarl
      421 qadgilfagg avwrgrkvmr msviswltdd ragevaagai iaawravrdg tev
//
LOCUS       WP_284718451             443 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Sinorhizobium kummerowiae].
ACCESSION   WP_284718451
VERSION     WP_284718451.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium kummerowiae (Ensifer kummerowiae)
  ORGANISM  Sinorhizobium kummerowiae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Sinorhizobium kummerowiae"
                     /db_xref="taxon:158892"
     Protein         1..443
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=48127
     Region          197..417
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mdragygeve ptnavkarvg tvlfmaiflf fwisinpfvd ltgeavldps agnsnrlnqi
       61 islllftgml gyglvhplre ailqpralla ilfswfifvs lvsahpmlgi kgailalmvt
      121 vnagvylllp aserhfakml gigilimlav ayygivfkpl laihqaselr epmnaglwrg
      181 hfphknsaaa amviaafigl yvmntwsrfa givivalsfv flvntggkts tamlpailll
      241 alifekvrfl ripiavggvg lfnlfavgsa vfaplgdfis glgidatftn radiwrfafg
      301 alaeqpltgy gfkafwqtee lvysggsvet wavaaanghn syldialmtg fpglvltliw
      361 ilflplrkia riaperehsh ltrlfvriwl ytifnagles lffeggsllw ftfmvalygl
      421 slqssaelaa apararqgrv aha
//
LOCUS       WP_284718525             447 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Sinorhizobium kummerowiae].
ACCESSION   WP_284718525
VERSION     WP_284718525.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium kummerowiae (Ensifer kummerowiae)
  ORGANISM  Sinorhizobium kummerowiae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Sinorhizobium kummerowiae"
                     /db_xref="taxon:158892"
     Protein         1..447
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47171
     Region          13..444
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mtatevseaa qeiekllalh pkgfdlsldr itrllaalgn pherlppvih vagtngkgsv
       61 tafcrailea aglsvhvhts phlvnwhery rlgvkggkga lvsdpvlada vrrvaeangg
      121 ekitvfeilt avtfllfaeh padvaiievg lggrydatnv iarpavavim pisldhqayl
      181 gdrveliaae kagimkrgcp vvighqeees ardvliatae rlgcpisvyg qdfmaheefg
      241 rlifqdengl adlplprlpg rhqyanaaaa iravraagfd vpeaaiekgl agvewpgrlq
      301 rlaggrlshf gppgaeiwid gghnpgaghv iaeamatfee rnprplflii gmintkepig
      361 yfkafldlte qvftvpvhgs dagldplala adaaaaglea natssvaeal gqiaeltded
      421 pvpprvligg slylvgdvla engtppr
//
LOCUS       WP_284718632             654 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Sinorhizobium kummerowiae].
ACCESSION   WP_284718632
VERSION     WP_284718632.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium kummerowiae (Ensifer kummerowiae)
  ORGANISM  Sinorhizobium kummerowiae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 654)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 654)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 654)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 654)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Sinorhizobium kummerowiae"
                     /db_xref="taxon:158892"
     Protein         1..654
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72434
     Region          8..533
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 maaenrsklv kmtirnlgcv gndgleield nivcivgrnn sgkstllray elakgvvsfv
       61 asedrfqhat ldqpseille vhipdgignv dprwktdrdg lrivksrwqw sapdftrirt
      121 twdptggeng qgdwaadgka ggadpvfssr lprplrigsl ddaqkteeml lalalgplla
      181 sveqertnke salfkaiasv sshidvlsnd htehfndiat kvatgfqgvf pkmdvrlnia
      241 asplvpkisd lvkagssiri kdglsdtmlk qqgtgarral fwamlqvhne ltrdkeirdd
      301 frkrltqdig naerklagkk iaedekagae rlfddlqakl kahdagapip dspddpalpg
      361 ylllidepen alhpmaaraa qrhlyklaes pdwqvlmtth spyfinpfed httivrlert
      421 gddkavavvs prtyrsdrie fdgddkqrlq alqqidpsfa eiffgsypil vegdtehaaf
      481 masvvekqhe linqvtiira rgkailaplv rvmqhfkidf givhdcdppf kkngdtngmw
      541 tenkkirdai laarqagitv rhrisipdfe rflggdeeak dkpltaylri ageqklgdsv
      601 rtlldqlltg eqhepfdvea fpagadymkt lsghiaewag hngladeirf kgkp
//
LOCUS       WP_284718684             267 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium
            kummerowiae].
ACCESSION   WP_284718684
VERSION     WP_284718684.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium kummerowiae (Ensifer kummerowiae)
  ORGANISM  Sinorhizobium kummerowiae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Sinorhizobium kummerowiae"
                     /db_xref="taxon:158892"
     Protein         1..267
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29960
     Region          78..263
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          207..260
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mgidldrlfq amaplvngap mddeavgctf rglmstlmtf dyvvvfayrg keppldlyst
       61 fdaedhvlfv slyqagpyll dpfyhaarap kpgvwrmrel apdrffssey yrtyyvqtgl
      121 aeevgffvpv seqvtvvlsl mrreatgvfs atefallkka eplvaafvrh hwaeldrrfd
      181 talakkgrgr rkaahppadg vwrhlnlter eaaiielvlq ghssesiglk lgistgtvkv
      241 hrrnvyrklg issqtqllsl yiknlgq
//
LOCUS       WP_284718791             471 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Sinorhizobium
            kummerowiae].
ACCESSION   WP_284718791
VERSION     WP_284718791.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium kummerowiae (Ensifer kummerowiae)
  ORGANISM  Sinorhizobium kummerowiae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Sinorhizobium kummerowiae"
                     /db_xref="taxon:158892"
     Protein         1..471
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49183
     Region          1..446
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mntiiaflnt ilwgyvliyg llavglffti rlglpqiihf gemfrvlssg gskdtsgisp
       61 fqalmvslas rvgtgnlagv avalylggpg atfwmwmval vgmatayaes alaqlykvrn
      121 edgqyrggpa fyiahglnap waaaifsvcl iisfglvfna vqansiadav qgafgvpklt
      181 vgfglavlsg vvifggirqi arvaeiivpf mavayllmav yvlianaalv phvlwtivss
      241 afglqeaagg vtggiaaaml ngvkrglfsn eagmgsapni aavatpvphh pssqgfvqsl
      301 gvfidtilic tatsvmills gtldpgsnit gtltqaamnv higaagtyfi aiaifffaft
      361 siignysyae naltflgagn rlgltimrca tlvmvvwgay esiatvfdaa dasmglmati
      421 nliailllsg tiakltkdyf kqrkqglapv fhaadypelq gkidhgiwsr v
//
LOCUS       WP_284718887             585 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Psychrobacter pocilloporae].
ACCESSION   WP_284718887
VERSION     WP_284718887.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter pocilloporae
  ORGANISM  Psychrobacter pocilloporae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 585)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Psychrobacter pocilloporae"
                     /db_xref="taxon:1775882"
     Protein         1..585
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=68045
     Region          4..446
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mkyqlvefri rnyrsisdik lkidndnltv icgsnnvgkt nflralnlff npkidnfdad
       61 rdvpyhiveg srgagyktvl tgrfienkss evleikqsfs ekkgikevvl egkkgrksls
      121 kleiedflns nfsfffieas nidipklise ivndailplg mdkrrgqtqk dsleklnqfi
      181 dlsksavkni endltsifqn llkevdsids dnwklqikfp eydflreais kiieftlydt
      241 nerkletkgs giqriillsl iqyvnsrtkk dviwaidepe iflqaglqks lysrlleesk
      301 dsqilitths hffintqnlk ntflfegtke lkeyarkegf lfyklntmvy egsdfeksqr
      361 ikqnfgiskn dswevmpfnv lvegqedkdi ltflfkkfnl pipniliggg vtkypgylrf
      421 leefcsdley kpkivaifdr dsegrsifns lrgrhykdid lncryiirad gkeyndiele
      481 dfiypdilyd atnkilrrkk ykaikksdrl krtsraynks pildfitdit kqnnpekssi
      541 nftqegmkmi ltntccqiie qsdinemnve ypevlfflkn ilevs
//
LOCUS       WP_284718891             234 aa            linear   BCT 25-DEC-2024
DEFINITION  pseudouridine synthase [Psychrobacter pocilloporae].
ACCESSION   WP_284718891
VERSION     WP_284718891.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter pocilloporae
  ORGANISM  Psychrobacter pocilloporae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Psychrobacter pocilloporae"
                     /db_xref="taxon:1775882"
     Protein         1..234
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=26000
     Region          1..227
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mrldkfiska telsrkeskk imhageitvn eqvvkdpglh vdvindevmw ageplsvatg
       61 nryillykpe gfectlkake ypivteliav pelgslriag rldvdttgal lmsddggwlh
      121 rvtspkheha kvyeltlasa mdsdaqekav kkvaegille gdyeptkpat lefiddthar
      181 ltleqgkyhq vkrmmgyfgn rvtelhrasi ghinldglek gdsrfltpee vakf
//
LOCUS       WP_284718917             402 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin reductase family protein [Psychrobacter pocilloporae].
ACCESSION   WP_284718917
VERSION     WP_284718917.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter pocilloporae
  ORGANISM  Psychrobacter pocilloporae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10937050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Psychrobacter pocilloporae"
                     /db_xref="taxon:1775882"
     Protein         1..402
                     /product="flavin reductase family protein"
                     /calculated_mol_wt=44443
     Region          14..298
                     /region_name="FNR_like"
                     /note="Ferredoxin reductase (FNR), an FAD and NAD(P)
                     binding protein, was intially identified as a chloroplast
                     reductase activity, catalyzing the electron transfer from
                     reduced iron-sulfur protein ferredoxin to NADP+ as the
                     final step in the electron transport...; cl06868"
                     /db_xref="CDD:447143"
     Site            order(72,86..89,120..122,125..128,179)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99812"
     Site            order(86,88..89)
                     /site_type="other"
                     /note="conserved FAD binding motif [chemical binding]"
                     /db_xref="CDD:99812"
     Site            order(125,128,131,138)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99812"
     Site            order(174,178..181,183)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99812"
     Site            order(179..180,203..205,266..267)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99812"
     Region          323..402
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 mangyrpeiv qrafvdfigs rlhpfwsltt pklrliarye msddlialqf etnrafrqqi
       61 skgaddwqgg qyldlrvfid gvyhqrsysl vglanqplww qddavitksa ksqrhtvtia
      121 vkpqglvsdy ltkqlslssi vdtsmplghf tlaqaktsld nrepdnqklh pllfvaggsg
      181 itpmlgliaq aladgyqval lhysrsklpq lqrqwqqlsd typafsyhli htdnpatyla
      241 gerylsaegl lslnlpladt qifacgsqal laglykavse iilpqgnqlr dniivenfgn
      301 alpdfdsggn qvldnalqte shtvylrsrq rqfdsdttll vaaenagirl ahgcrqgicq
      361 lcrcnkvsgv vkniqtgnis sdgyesiqtc iniamtdvvl di
//
LOCUS       WP_284719083             539 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Psychrobacter
            pocilloporae].
ACCESSION   WP_284719083
VERSION     WP_284719083.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter pocilloporae
  ORGANISM  Psychrobacter pocilloporae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Psychrobacter pocilloporae"
                     /db_xref="taxon:1775882"
     Protein         1..539
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=61122
     Region          27..538
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mskttnnngs nnknndssds dsplhylmwf rrdlrihdnt alaalceran ednasvsaif
       61 fltpeqwqqh dtslvqvdhi artlpilakd lksqlnitlt vqlcpsfsdc iesltslckd
      121 ndiscvmanh eyegneigrd eqlceqlakd diefvrwhdq cilpplsitt ndgdsmykvf
      181 tpfykkwrht ldvstiqmhd apavdcddki elkssknsah taddikalse emlgdyqktl
      241 qkedslqhid ikaqltaard aypagesaac qrldefvadd indydvsrdv phlhatsqls
      301 ayltigtisp rlcylqaskv qeklhgndgd nedidrwise lawrdfyrhv lvdkpnlirh
      361 kaykedtdtk vswsyddddf qawctgktgv plvdaamrcl natgfmhnrl rmvtamfltk
      421 dllidwrlge ryfrqqlidg dfasnnggwq wsastgtdsa pyfrimnpfs qgsthdkkai
      481 fiktwlpelk dipastlhse dkmrkalakg gdfanadypa pmvehksark laiaefkke
//
LOCUS       WP_284719128             222 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NuoB/complex I 20 kDa subunit family protein
            [Psychrobacter].
ACCESSION   WP_284719128
VERSION     WP_284719128.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter
  ORGANISM  Psychrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Yu,H., Schut,G.J., Haja,D.K., Adams,M.W.W. and Li,H.
  TITLE     Evolution of complex I-like respiratory complexes
  JOURNAL   J Biol Chem 296, 100740 (2021)
   PUBMED   33957129
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Parey,K., Brandt,U., Xie,H., Mills,D.J., Siegmund,K., Vonck,J.,
            Kuhlbrandt,W. and Zickermann,V.
  TITLE     Cryo-EM structure of respiratory complex I at work
  JOURNAL   Elife 7, e39213 (2018)
   PUBMED   30277212
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Walker,J.E.
  TITLE     The NADH:ubiquinone oxidoreductase (complex I) of respiratory
            chains
  JOURNAL   Q Rev Biophys 25 (3), 253-324 (1992)
   PUBMED   1470679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Psychrobacter"
                     /db_xref="taxon:497"
     Protein         1..222
                     /product="NuoB/complex I 20 kDa subunit family protein"
                     /EC_number="1.6.5.9"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=24802
     Region          16..185
                     /region_name="PRK06411"
                     /note="NADH-quinone oxidoreductase subunit NuoB"
                     /db_xref="CDD:235797"
ORIGIN      
        1 mkytltkanp dadtypaqtr qtvndpiede vnknvfmgrl edlvhstanw grkhslwpfn
       61 fgtsccyvey attltavhdl srfggevira sprqadvmiv agtcfvkmap viqrlyeqml
      121 epkwvismga cansggmydi ysvvqgvdkv ipvdvyvpgc pprpealiqg lmllqesitk
      181 errplgihvn eqgiyqpqmt perdrkqadr iavknlrspd si
//
LOCUS       WP_284719208            1014 aa            linear   BCT 25-DEC-2024
DEFINITION  LPS-assembly protein LptD [Psychrobacter pocilloporae].
ACCESSION   WP_284719208
VERSION     WP_284719208.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter pocilloporae
  ORGANISM  Psychrobacter pocilloporae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Psychrobacter pocilloporae"
                     /db_xref="taxon:1775882"
     Protein         1..1014
                     /product="LPS-assembly protein LptD"
                     /GO_process="GO:0015920 - lipopolysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=113304
     Region          249..993
                     /region_name="LptD"
                     /note="LPS assembly outer membrane protein LptD (organic
                     solvent tolerance protein OstA) [Cell
                     wall/membrane/envelope biogenesis]; COG1452"
                     /db_xref="CDD:441061"
ORIGIN      
        1 mlysplyqsi rlilfgalgl ssltvnaain dadtqtteps sagstssyls dtnnsnvtqs
       61 sdyndirykd arsqldnsqr atpasdfddt rfasdakled sasddvlnit einessdias
      121 tqpsnmldsd qvsrdtrana iatpentaad nrqldindes iqdslvrlae fyeltpetpv
      181 sndvdnieda esdniqstla ptaqtipkvg knlrllpnai dsaqrcegqw vypksnpnyq
      241 ravneaggan gqpvpdvdsi pnnqaplfte sdygyynnin yaelsgnvkv dqgtqhieae
      301 kvvidlsngv aaaqgrvmft dqatgqslqr snvpsnaqas fnerakkggl igvadslnyn
      361 tetgqstand vafasvglqa hgyakrlnkp ndseyeldev mfstcpptnr kwqfdaksid
      421 lntdtgrgea ynttfriadv pvfylpyfnf pidsrrssgf llpsasvsse sgveidvpyy
      481 fnlapnydat lnthvytdrn pmlsgefryl tenygegifn gsylpndkey ndedrksffy
      541 dhywssksip rlsgdakysy vsdadylddf dtlglsdnti nlprrarvny yndyvdgelk
      601 vetfqtldaf tdngealedk dkpysrlpql klnyrlpwak nfditgvhds ayfkksiddg
      661 sedeksgari ynkisavypm ekswgyirpk lslqhlytsy dedsladnni seedgsqsvf
      721 vpqasidagl nfyqagspfg afddtmggyr llsprvkyty spyknqndip nfntriasin
      781 yeqlfsdswf lghdrlqdlh sitpgvnyry idatgvtrfd gsiaeqfyid dgrvtlddeq
      841 rvfnssssgm vwvtstqpyn nfwvdvsgal tndydlnyit telryqpsdn slfnvgyvkr
      901 qrdentdqlp lsaftasavf pinnswrila qgqydynsnk mldsligvdy edccfgfavy
      961 grryyndlnv kdeptqaima eirlnglgsg ssrltrllsd kilgfepvqt awkd
//
LOCUS       WP_284719288             443 aa            linear   BCT 25-DEC-2024
DEFINITION  S1C family serine protease [Psychrobacter pocilloporae].
ACCESSION   WP_284719288
VERSION     WP_284719288.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter pocilloporae
  ORGANISM  Psychrobacter pocilloporae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Psychrobacter pocilloporae"
                     /db_xref="taxon:1775882"
     Protein         1..443
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47791
     Region          123..388
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 msssqntnnt rnkvsllkwl pwvllllvlv afiwlftsmk ssseatwepp rtppaeqqas
       61 epvadtpapi ssyhnavara sqsvvniytt qtmtehpymd dpvlrrffey hggpsqeqgs
      121 tnlgsgvivs edgyivtnah viekadeitv afndgrksra kiigtdpdsd lavikvdmtg
      181 ltplgfredp irvgdlalai gnpfgvgqtv tqgiisatgr tglgvnkfed fiqtdaainp
      241 gnsggalvda rgelvgintv ifsrsggsmg igfaiptslv eqvmnalikd grvsrgwlgi
      301 eiqsqlrdpt qletstgvev lnviegspaa ksglrvgdii ltidgvemtd antliqyvar
      361 kppttelnaq ilrqgknaqv kimleerpvq epierpvvlq gesmdgmggs iqgdeqapmm
      421 seaerdrmre elmklfeqds ltq
//
LOCUS       WP_284719332             531 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Psychrobacter pocilloporae].
ACCESSION   WP_284719332
VERSION     WP_284719332.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter pocilloporae
  ORGANISM  Psychrobacter pocilloporae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Psychrobacter pocilloporae"
                     /db_xref="taxon:1775882"
     Protein         1..531
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=60157
     Region          168..531
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 miktssnpvk spkfkvritl fwrlflslll tilitsllsi mverwlaeke ltarmdvqie
       61 slliqrqemv dalrvgdlia vrqmyrqdrr lmsqirvyde qgaiifpryr drdertqgrg
      121 qsgqqsmera mqqplppppr aydnkpsnln demlikqpsv lheilkpims ssaaiadida
      181 rpeladisve lpdgqsviiq lrphlrfadv velqhgnfpl rllliiafsv lvcvwlsrtl
      241 tqrigrvqst vhrmidgdyq anpalskmgd delgllakdv ahlstrlads elarkqmlsd
      301 ishelrspla rldvateltr dfapnahryl dridkesarm nelieqiihi qslqmqqyti
      361 dnleseavdl seiisdigqd vcfefqhkev rwqwqppeys fandlksawt vqgnqeqlhs
      421 alenvvrnaf mhtaagstvi aemkavqidn kmpaiqisit degggvadnd lerifqpfvr
      481 ldtarhrdtg gyglglaivh avvmahkgyi nahnrrdgvl glvvqivlpi k
//
LOCUS       WP_284719435             217 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Psychrobacter pocilloporae].
ACCESSION   WP_284719435
VERSION     WP_284719435.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter pocilloporae
  ORGANISM  Psychrobacter pocilloporae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Psychrobacter pocilloporae"
                     /db_xref="taxon:1775882"
     Protein         1..217
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24885
     Region          95..201
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mnesfnhagt wglalivivl iswffyryfa pknwrewaga gvvqafiial yaemygfplt
       61 iyllvrffgl dsqyvsaslw stlvglgetg mmismllgya iaflgiglfa qgwrqvhkar
      121 genrlvtdgl yayvrhpqyt glfialfgeg vvhwptlfsi glfpvivlvy twlarreerh
      181 mfeefgkdyl tykqqvpmfi pqwgqwrqla aaarvkk
//
LOCUS       WP_284719477             255 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Psychrobacter pocilloporae].
ACCESSION   WP_284719477
VERSION     WP_284719477.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter pocilloporae
  ORGANISM  Psychrobacter pocilloporae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Psychrobacter pocilloporae"
                     /db_xref="taxon:1775882"
     Protein         1..255
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=28969
     Region          36..253
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mdlfdslptd dsasaltnfi idgkfmqsdy pahihddgkg ividipdgrl yyapryfdst
       61 lsdsiidsll acdgidhsth dwhqqsdiga lpfkniqwqq dsvsmfgkth dlprlsawyg
      121 dndkpytysg itlqpkpwnd illelraalv pickrqfnsv llnwyrsgnd hiswhtdaep
      181 elgtnplias vnfgasrrfl lrrredhtik leiplqhgsi lvmagalqhh wqhsvpkqkk
      241 vkegrvnltf rtiht
//
LOCUS       WP_284719465             368 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Psychrobacter
            pocilloporae].
ACCESSION   WP_284719465
VERSION     WP_284719465.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter pocilloporae
  ORGANISM  Psychrobacter pocilloporae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Psychrobacter pocilloporae"
                     /db_xref="taxon:1775882"
     Protein         1..368
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=41635
     Region          1..361
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mktlklrird khidqlnrls gsvnfvwnyv ndlsykhlkr tgkffsaydl avytkgsgey
       61 lnlhsqtlqa inethaksrk qfkkaklnwr tnnpkakrks lgwipfkksa ikhlatrqsg
      121 kkglkstlql slaegrklii dlwdsynlsl yqintlqivq dsrnrwyaci tvkefpkqic
      181 gidsvgidlg lkesaitsng aklqikqtqk wakklaiaqr aknkkrvkai hakvkntrqd
      241 lihkfttnli kqnalivvgd vksrsftnkk tklakstyda gwyelkrqle ykcenagccf
      301 eivnesyttq ncscckqids nspkgraglg irewtcagcg srhdrdinaa knilavgldr
      361 lvvgipsl
//
LOCUS       WP_284719503             159 aa            linear   BCT 25-DEC-2024
DEFINITION  YkvA family protein [Psychrobacter pocilloporae].
ACCESSION   WP_284719503
VERSION     WP_284719503.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter pocilloporae
  ORGANISM  Psychrobacter pocilloporae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Psychrobacter pocilloporae"
                     /db_xref="taxon:1775882"
     Protein         1..159
                     /product="YkvA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=18203
     Region          36..121
                     /region_name="YkvA"
                     /note="Uncharacterized membrane protein YkvA, DUF1232
                     family [Function unknown]; COG3339"
                     /db_xref="CDD:442568"
ORIGIN      
        1 mftkkndkek tlvsnlkyli gkedklkekl ednsylepfs ddlmlfmsli kdyykgdyrk
       61 ipfrtisagv vgaiytlnpi dlipdsipfi gyiddalvlk fclkqarkdl qkykswkqeq
      121 sgtkstsend kytdkishdn sstddeddne tstdlkkas
//
LOCUS       WP_284719578             586 aa            linear   BCT 25-DEC-2024
DEFINITION  TrkH family potassium uptake protein [Psychrobacter pocilloporae].
ACCESSION   WP_284719578
VERSION     WP_284719578.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter pocilloporae
  ORGANISM  Psychrobacter pocilloporae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Psychrobacter pocilloporae"
                     /db_xref="taxon:1775882"
     Protein         1..586
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=64966
     Region          135..581
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mnaaaryrll nnvtilisvi avaialldsg ftlpiwlqqv fhifylvvil lsfvvtvgry
       61 lytnkprtln kvaifdafts iaivilltah ftdlvrsgld aavdgfvaik iavfvtfire
      121 lsdhnfnlnr tflhpaqffi lsflavvlvg alllmmpnat tqplsfidal ftatsavcvt
      181 glivvdtaty fttfgqviim gliqigglgi ltfvtyfsyf fkggvsyetq asisemsymr
      241 gmgnvvstlk silyvtfave avaaaliyis iydmpdmnws eqlffsvfha isafcnagfs
      301 tfsagmydds lrfnyplqli iamtfifggm gftivvnvlr ylrhraerli yrndrhhiyq
      361 pwllninsri tlittgalll tglvgvmvfe ynnvladhts ffgklitgff taatprtagf
      421 nvidmgeltf ptvmltiflm wigaspnstg ggiktstfai allntlslar gqtkievfkr
      481 qiadisvrra fsiiwlsllv igtgvtlisy dqpeldlikv vfecfsayst vglslnltad
      541 lsdfskvvvs vimfvgrvsm ltifiallkn mrqrnyrypt eeitin
//
LOCUS       WP_284719678             482 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alanine/glycine:cation symporter family protein
            [Psychrobacter].
ACCESSION   WP_284719678
VERSION     WP_284719678.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter
  ORGANISM  Psychrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Psychrobacter"
                     /db_xref="taxon:497"
     Protein         1..482
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51503
     Region          1..448
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 meyiesffal vgdltwgwal vpmliifgll ftivgrfaqf tyfkrmfrvf ktdevgddgi
       61 sarqallvsi ggrvgggnia gvavaislgg pgavfwmwvv aligmmtsiv ecslaqlykr
      121 rdndgnfrgg patyilhglg kdyrwlaviy aialllsfsi gfiafqgntv agsalesfgi
      181 drwisgavlv vaggfivfgg iqriakvadv vipvmaliyi gmaliiivln iadlpalmam
      241 ivknafgies vvgggigvai eqgmkrglfs neaglgsapn iaatayathp vsqgisqsls
      301 vfidtivvcs atafmillsg vyqpgaevdg ivlaqqalta qlgnwsqyvl tislllfals
      361 simynyymge nainflvkkn tktatlvlrv vvvailflga vapaatsvff fadplmgvla
      421 lanllaliml fprakrlldd farqlksgvk eplfdaqeye kldldlsawg kkavkealeq
      481 kq
//
LOCUS       WP_284719682             215 aa            linear   BCT 25-DEC-2024
DEFINITION  M48 family metallopeptidase [Psychrobacter pocilloporae].
ACCESSION   WP_284719682
VERSION     WP_284719682.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter pocilloporae
  ORGANISM  Psychrobacter pocilloporae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Psychrobacter pocilloporae"
                     /db_xref="taxon:1775882"
     Protein         1..215
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=24845
     Region          1..207
                     /region_name="YgjP"
                     /note="UTP pyrophosphatase, metal-dependent hydrolase
                     family [General function prediction only]; COG1451"
                     /db_xref="CDD:441060"
ORIGIN      
        1 meirldtirq qlaqvdielh iskkrvknin frlkphvlmv svplhisdsq aadavarrvs
       61 wainhhpqvl eqhqrkqgal sdlttadqpi ylwgkvqplt lshgekvayy rqqlsdvmps
      121 lfekwqpivg tyaneirvkk mhtrwgscnt rakriwlsvy lpaypiecte yvivhelchl
      181 hhanhspafw qtvasampdy rqwhnilagk rgqld
//
LOCUS       WP_284719019             232 aa            linear   BCT 25-DEC-2024
DEFINITION  ZIP family metal transporter [Psychrobacter pocilloporae].
ACCESSION   WP_284719019
VERSION     WP_284719019.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter pocilloporae
  ORGANISM  Psychrobacter pocilloporae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Dempski,R.E.
  TITLE     The cation selectivity of the ZIP transporters
  JOURNAL   Curr Top Membr 69, 221-245 (2012)
   PUBMED   23046653
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Guerinot,M.L.
  TITLE     The ZIP family of metal transporters
  JOURNAL   Biochim Biophys Acta 1465 (1-2), 190-198 (2000)
   PUBMED   10748254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Psychrobacter pocilloporae"
                     /db_xref="taxon:1775882"
     Protein         1..232
                     /product="ZIP family metal transporter"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23348
     Region          1..230
                     /region_name="ZupT"
                     /note="Zinc transporter ZupT [Inorganic ion transport and
                     metabolism]; COG0428"
                     /db_xref="CDD:440197"
ORIGIN      
        1 mlvfaiilvv sgalvigalw glygympdwi qgnllalagg almssvvlem iqpaigesgl
       61 wttvaftvlg avvftaidyl idekmqnkgg agllaaitld gipenlalgv aliggnalqv
      121 aalagsills nlpeaaggak qmrdggsshk kilmlwigaa illslaaiig ktllkdvdda
      181 visaidcfaa gaviaslate vfpsafkdgn hwagistaig lvlalglnql gg
//
LOCUS       WP_284719771             300 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Psychrobacter pocilloporae].
ACCESSION   WP_284719771
VERSION     WP_284719771.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter pocilloporae
  ORGANISM  Psychrobacter pocilloporae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Psychrobacter pocilloporae"
                     /db_xref="taxon:1775882"
     Protein         1..300
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33804
     Region          8..296
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 msdnsqlide llatialiev tpdvfegksh dyvgsrifgg qvlaqaimaa ahtldqdkpc
       61 hslhgyflrg gdinqpviyq vrrlrdgrsl sarevtaiqy kevrdkapve qvifsmiasf
      121 spmedglayq edmpvypppe dllteqdlke eyvgkvpdal karfmrrrhv eikpvkprnp
      181 inpepmkpkq anwlrirelg nqpvaiqqal lafssdfylv gtglmshgvs fmtsglqaas
      241 idhsmhfhre fdlndwllyd mwsdttsnak glnhgqfwqd gklvatvqqe glmrlrvpks
//
LOCUS       WP_284719876             800 aa            linear   BCT 25-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Polyangium sorediatum].
ACCESSION   WP_284719876
VERSION     WP_284719876.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 800)
  AUTHORS   Pereira,J. and Lupas,A.N.
  TITLE     The VCBS superfamily forms a third supercluster of beta-propellers
            that includes tachylectin and integrins
  JOURNAL   Bioinformatics 36 (24), 5618-5622 (2021)
   PUBMED   33416871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..800
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..800
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=80716
     Region          366..426
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          415..493
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          483..549
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          539..596
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mrrrfaflvl sssaaallaa lgqgcgdggs ssggagaggs gsttgtggmg gssssgtggd
       61 dtlfdagscp tgeacdggvc aggvccavdl acgeaccggg qvcsfqkcvt pgascaesgd
      121 caageycefs lgdpqgtdgg vdagciggaq vpsgkclpkp ptcapgmpap npgdpltcle
      181 scqykpaass fapelkfawg gqlvapfatd vmmspiviel ddddcdgkit akdipeivfa
      241 tftggayqss gilhaisvvg gqvvekwaap gihptkqlaa gnidgaagne vvacaegada
      301 gvralkgdgs llwatppmrc fmptvadldg dgavevvveg gildgvtgav kasfstvlss
      361 sfvvsdvtgd gvldivtgsq vfdaagmlll dtatanqsnf yatqdwkspw pavgdfdadg
      421 kpevvvvdnl nhalvvwryd aaapgkfviv rpaldingpl spslcpagsw gnthgggppt
      481 iadfngdgtp dvamaggvgy avldgkklvd aavpgneafl wikqtsdcss astgstvfdf
      541 dgdgkaevvy sdqqrlrvye gptgnvlwer cnttatlien pvvadvdndg hadivavsna
      601 ygqasaslqc ddgvsiaqsg vrifgdtsgk wvrtrrvwne hayhitnvee dgtipakels
      661 nylqpglnnf rqnkqpgsef aapdavvsla pvcfgpyglv avvrnvgeas lpagvvvgfy
      721 kgnhpngell gqgttskvly paesesvllp lagapgdvvn gtapiyavvd dtsvphpawt
      781 ecrtdnnvsa sasgacnspk
//
LOCUS       WP_284719901             298 aa            linear   BCT 25-DEC-2024
DEFINITION  formylglycine-generating enzyme family protein [Polyangium
            sorediatum].
ACCESSION   WP_284719901
VERSION     WP_284719901.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..298
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=31846
     Region          28..297
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 mrsptrlplg lllvvavtgc grtdaenarr lavsprgarl vsipgatfsf resmavnrtv
       61 vtvqpfqiea tevtvsgyaa cvgakacvap vgegrvekfn epmcnwgkpg rgdhpincvs
      121 paeaeaycqw nggrrlptiy eaywaalgdg rmseaerlge rhrtypwgrd epekiehcwq
      181 rgamggtqgg vvgpitssap paaadlgtcp vasytgdrsp fglydtagnv aefvfdpkpi
      241 tcistageqp cprekmfrvt ggtwhdhglm gnqspadnhp vaserhpwyg frcvvgag
//
LOCUS       WP_284719257             403 aa            linear   BCT 25-DEC-2024
DEFINITION  OmpP1/FadL family transporter [Psychrobacter pocilloporae].
ACCESSION   WP_284719257
VERSION     WP_284719257.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter pocilloporae
  ORGANISM  Psychrobacter pocilloporae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Black,P.N. and Zhang,Q.
  TITLE     Evidence that His110 of the protein FadL in the outer membrane of
            Escherichia coli is involved in the binding and uptake of
            long-chain fatty acids: possible role of this residue in
            carboxylate binding
  JOURNAL   Biochem J 310 (Pt 2) (Pt 2), 389-394 (1995)
   PUBMED   7654173
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Munson,R. Jr. and Grass,S.
  TITLE     Purification, cloning, and sequence of outer membrane protein P1 of
            Haemophilus influenzae type b
  JOURNAL   Infect Immun 56 (9), 2235-2242 (1988)
   PUBMED   2842261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Psychrobacter pocilloporae"
                     /db_xref="taxon:1775882"
     Protein         1..403
                     /product="OmpP1/FadL family transporter"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42740
     Region          41..401
                     /region_name="FadL"
                     /note="Long-chain fatty acid transport protein [Lipid
                     transport and metabolism]; COG2067"
                     /db_xref="CDD:441670"
ORIGIN      
        1 mratfhlktl avavatlsva saasaagldr sgqdvtaflq dgtyaeavyt yidadvtgkd
       61 tsdnkiddia esydffrygv ktdindtfsv gvlydepfga aadytgdnnf vnangegtnv
      121 evrtesitgi lgakfgqnkn fqvyggpvaq rvkadvklrg payeaangyt aninadqdyg
      181 yiagvayskp eialkaslty rseiehnaqa seiypvvgsg lipapvvsal glstnrvdsi
      241 eittpesvnf dfqtginptt latakvrwvp wsdfaivpsl yndvskistq ddkglalvsy
      301 dddqwqvelg lakrvapala isgtvgwdsg agdpvtslgp iegyysaglg akynvtenwa
      361 isaggkylwf gdakgqiptk tivsdfesnd gfvlgvkvsy qaq
//
LOCUS       WP_284719972             129 aa            linear   BCT 25-DEC-2024
DEFINITION  ribosomal protein bL12 [Polyangium sorediatum].
ACCESSION   WP_284719972
VERSION     WP_284719972.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Ban,N., Beckmann,R., Cate,J.H., Dinman,J.D., Dragon,F., Ellis,S.R.,
            Lafontaine,D.L., Lindahl,L., Liljas,A., Lipton,J.M., McAlear,M.A.,
            Moore,P.B., Noller,H.F., Ortega,J., Panse,V.G., Ramakrishnan,V.,
            Spahn,C.M., Steitz,T.A., Tchorzewski,M., Tollervey,D., Warren,A.J.,
            Williamson,J.R., Wilson,D., Yonath,A. and Yusupov,M.
  TITLE     A new system for naming ribosomal proteins
  JOURNAL   Curr Opin Struct Biol 24, 165-169 (2014)
   PUBMED   24524803
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..129
                     /product="ribosomal protein bL12"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0003735 - structural constituent of
                     ribosome [Evidence IEA]"
                     /GO_process="GO:0006390 - mitochondrial transcription
                     [Evidence IEA]"
                     /GO_process="GO:0006412 - translation [Evidence IEA]"
                     /GO_process="GO:0045893 - positive regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=14174
     Region          1..125
                     /region_name="RplL"
                     /note="Ribosomal protein L7/L12 [Translation, ribosomal
                     structure and biogenesis]; COG0222"
                     /db_xref="CDD:439992"
ORIGIN      
        1 msvtreevia ylesltaeel geladelvqr fgllavvepp ryeffmgapp pdpheeitef
       61 svvlldigkd klavvkavra lwempvkeak dlvesapvvv rrwitrdear livdtlttag
      121 asaevrngs
//
LOCUS       WP_284720073             324 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Polyangium sorediatum].
ACCESSION   WP_284720073
VERSION     WP_284720073.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..324
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35679
     Region          38..255
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mipefpraag gpfpfgaqdf svwqaripri eeveinssld gskqrallyd pgrpeprpll
       61 valhswseny lqnigipygi faerngwvli hpdhrgpyrs pastaselaq rdvldaidya
      121 kqrarvdptr iylvgysgsa mtslvlagrh pgiwagvvsw vpiydlvdwy gwlrsnlper
      181 hyahevaaac ggaprpgtaa adecrrrspr shlqaargrv nvylgvglwd qlvppdhalr
      241 afndlaapad qvpvedigri tktrsipetl gapearplye aakakvvfer tseratvvvf
      301 qgghdviyna glswlssqqr tvlp
//
LOCUS       WP_284720084             922 aa            linear   BCT 25-DEC-2024
DEFINITION  Kelch repeat-containing protein [Polyangium sorediatum].
ACCESSION   WP_284720084
VERSION     WP_284720084.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 922)
  AUTHORS   Shi,X., Xiang,S., Cao,J., Zhu,H., Yang,B., He,Q. and Ying,M.
  TITLE     Kelch-like proteins: Physiological functions and relationships with
            diseases
  JOURNAL   Pharmacol Res 148, 104404 (2019)
   PUBMED   31442578
REFERENCE   2  (residues 1 to 922)
  AUTHORS   Gupta,V.A. and Beggs,A.H.
  TITLE     Kelch proteins: emerging roles in skeletal muscle development and
            diseases
  JOURNAL   Skelet Muscle 4, 11 (2014)
   PUBMED   24959344
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 922)
  AUTHORS   Adams,J., Kelso,R. and Cooley,L.
  TITLE     The kelch repeat superfamily of proteins: propellers of cell
            function
  JOURNAL   Trends Cell Biol 10 (1), 17-24 (2000)
   PUBMED   10603472
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18656853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..922
                     /product="Kelch repeat-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=91659
     Region          52..319
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          62..101
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          105..145
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          148..192
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          244..296
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          298..337
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          453..754
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          512..552
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          555..598
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          600..641
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          646..682
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          686..727
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          730..780
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          742..792
                     /region_name="Kelch"
                     /note="Kelch domain; smart00612"
                     /db_xref="CDD:128874"
ORIGIN      
        1 mrmtsifrhl apvllvvpla aalgcngaea ppsrakvygl geaasaltap rwdvappmnv
       61 arsghtatgl sdgkvllagg gsetaevfdp atnawtlvap matartrpta tllpsgkvlv
      121 aggntdavei fdpvantwtp aaplleprer htatllpdgr ilvaggefeg wmlktseiyd
      181 patdswtaaa smiwertsht atllpngkvl vvagmdeggd plnavelydp atntwapega
      241 venrynhtat llgngkvlva ggytdyfgeg fqapnrsaal ydpasgawsa vapmgvvhdl
      301 htatlladgr vliagggatv eaydpatgtw slgkflhtnr sdhtatalad grvlvagggs
      361 tsvevltlap pgeaclfage casgfcvdgv ccnaacdaga cdacavsaga sangtctpls
      421 gavcgsadgc tangvceaga cvgampvgcq fgwtsagsmp vprqagtwae ladgrvlvag
      481 gfdnnwsdtl sahlydpatn awsdvaplsq vrhsaasirv stgeilvvgg dgpstaevfd
      541 pasqtwtltg smvahhdvsa afvrladeri lvagggtdva elydpatkaw aatgslsvsr
      601 ggasavllqn gkvlvsggag dpataelydp atgtfspagt ltfahaghqa trlldgrvlv
      661 vsgngadryd patnawtptq allmppaeft atllgtgrvl vtgaqnipha qvydpatndw
      721 tvtgplevar rrhtatllgn glvliaggte wgggnqcdlr saavynpatn gwstvaamgt
      781 trrypsavql dgnrvlvfgg llgscssgdg dpeahgsaei yeggvtpegs ggsggaggvg
      841 gmggaggsgg gaggmggagg sggaggsggm ggvsgtggag gaggdevpgg gcraaagsme
      901 nsgrglaalv algalfgrrr kr
//
LOCUS       WP_284720089             325 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Polyangium sorediatum].
ACCESSION   WP_284720089
VERSION     WP_284720089.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459648
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..325
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=33509
     Region          <27..98
                     /region_name="PilF"
                     /note="Type IV pilus assembly protein PilF/PilW [Cell
                     motility, Extracellular structures]; COG3063"
                     /db_xref="CDD:442297"
ORIGIN      
        1 mfrkstglsf ftaillgaah vsgqpsaadk avadklfdeg ralldqnrlp eaclkfaesd
       61 rydpsvgtrl nlgdcherqg ktasayghfg eaarlarerg dksretvaee rrraleqrls
      121 riqitasssv tglevlldgk vlgpavfgta lpvdpgshvv earapgragf heekvvpegp
      181 atvevvipel aavapaagkd vvaapksrws llrkaglatg iagvvgigvg agfgaaalqk
      241 naaskekcda gdptrctqeg ytlrneagfs advstvllgi gggmlatgiv lfvvggnepe
      301 apaerawisp ivgrgslgvs agmef
//
LOCUS       WP_284720109             495 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Polyangium sorediatum].
ACCESSION   WP_284720109
VERSION     WP_284720109.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..495
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=52873
     Region          24..456
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mqverrsdss wedepsglpv aigdvldgky rvlrvlgkgg mgvivaavhv elghrvalkf
       61 llksamqnee vvarfarear aaamiqneha trvldigrlp sgqpymvlel legsdlgahv
      121 arngplpied avtyvleace aiaeahslgi vhrdlkpdnl flarrpdgsr tvkvldfgis
      181 klsvdndtsp ergaplttts avigspmyms peqlratrda dprsdiwsig vtlyeliage
      241 gpfpwqslpe lcaailkdpp tplrarlpda ppeldaallr clqknpgdry tniaelaval
      301 apfgkpgaia sseravrlla rgtsaersps trgplstspt ltdprvllpp lhstppvsat
      361 sllerdpaga kwqrilrpvp llaivaafvf vggagirlqr aygspsvlae larggieatl
      421 gpaftkvrpl pasveaaetk ahppvmgear paprprnkap qggfskpwpq stitdktpek
      481 ppssvkrpnp fdgre
//
LOCUS       WP_284720137             282 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase [Polyangium sorediatum].
ACCESSION   WP_284720137
VERSION     WP_284720137.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..282
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=30160
     Region          36..251
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mdwieevkga alrvapregs iaeviagrae waitsgdale flellppaca davwcdppyc
       61 sggffetakr rargmlqaet ikrlgwfvnd nmgttglvwl lrsvavraar alrssghfgc
      121 ftdhrmidal kpalessglr ysnllvwdkl tpglgkgfra qhevvlhfvn rspeyhagde
      181 gnihsvrrvp pkkknhqtpk ppelvarhlr vvappgglvv dpfvggggig vaalrvgarf
      241 igcdvdpgic edarealrae aaalagsgrs kgargrlala ha
//
LOCUS       WP_284720159             277 aa            linear   BCT 25-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Polyangium
            sorediatum].
ACCESSION   WP_284720159
VERSION     WP_284720159.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..277
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29957
     Region          3..243
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mqdaldaltd dvrsthpeqi livtgagvsh asgiptfrgn dpdaiwkrdv telgtraffs
       61 enpagswqwy lsrfdkvsga kpnpghhaia alerfqterg gdfllvtqnv dtlheqagsk
      121 rmvkvhgtsd ryrcsrsgce lgalegsiaa sevdltafra npveanvprc pscgaflrmh
      181 vlwfdevyag hddyqwsrvl daakvqarlv ifagtsfsvg vtelvtqsar arrvpvfnid
      241 ptpriskpgi mpiaagaeva lvevckrlgl aegaawa
//
LOCUS       WP_284720203             339 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Polyangium sorediatum].
ACCESSION   WP_284720203
VERSION     WP_284720203.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..339
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=35057
     Region          47..327
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mvrpqmgdap kggpseasgs ssdlpgnpra rypdrqddhe etatsadvvc vgealwdlst
       61 pqgtslddat qlsltpggga vnvaltlaql glragivapv gddavghalv ahlsrcgvdv
      121 srmratkstr tglvflthap travayravq eealalrdal prsfdasvvh fsgllpshac
      181 llalaqaarh aaregalvtl danlrprlwa gdaleradpr sllggvdvlk vseddlrllg
      241 asdprdlmpl lhaeatvvat fgaantralg pfgevhaggp alavestiga gdafvaglls
      301 vlaregraal rdreaierai qrgnevarss laerslvvk
//
LOCUS       WP_284720264             356 aa            linear   BCT 25-DEC-2024
DEFINITION  HesA/MoeB/ThiF family protein [Polyangium sorediatum].
ACCESSION   WP_284720264
VERSION     WP_284720264.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..356
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36644
     Region          6..249
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 msglserfar halvlgfrqd rlaaatvvia gvgalgnvva qalalagvgk lvlcdpdeva
       61 asnlsraplf rpadvgrpkv laakdtlaal apetvvvarq aalvsgvgla emrdaslvvg
      121 cldsraarms lagraglvra rwidaatsaw ggevrpfldp dgpcyacals peeraksdvp
      181 wscmdprrpa elgssapvag lvgawasala arvimgeaaa tdavvidvlr gaaeplrmqr
      241 apdcplhapi geatriplgs datvgalraa lgpgarplaw spllqrlecp rgdhaeeawg
      301 mpctrgcprc gtlmrarttl lfesapegav lsdlgvapre ilavlgrvgi tyvels
//
LOCUS       WP_284720277             314 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Polyangium sorediatum].
ACCESSION   WP_284720277
VERSION     WP_284720277.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..314
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=32282
     Region          <5..65
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          7..34
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          39..66
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
ORIGIN      
        1 meaaaralfq qadeemavgd fahacprfee vkqlfpvhin tgiklaecyv gqgrpasawa
       61 elsrvkavae gqqkadkvqf iterlavlqv pqmtvdvpae vaaipglvir rnsvelgpgq
      121 wgvplpvdpg myhieatapg rtgwerrvav vpkaapidpp vtvqieappp havaaskqeg
      181 ieitrpvaag vappppssgl rtagivgmgl gaaglgvgai lggvaiarng qsneghcdaq
      241 dhcsrtgyal rkealalgng staafvaggv vlavgvvlfa rsapapagke rdgrggatms
      301 lvirpselvl rgaw
//
LOCUS       WP_284719856            1046 aa            linear   BCT 25-DEC-2024
DEFINITION  efflux RND transporter permease subunit [Psychrobacter
            pocilloporae].
ACCESSION   WP_284719856
VERSION     WP_284719856.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter pocilloporae
  ORGANISM  Psychrobacter pocilloporae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Psychrobacter pocilloporae"
                     /db_xref="taxon:1775882"
     Protein         1..1046
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=114392
     Region          14..1025
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mdinsdlpkp eglferiiqf siqnaiwvll factwiavgi ysyqklpida vpditntqvq
       61 intqakgfta leveqlityp ienamagipd leltrsisry glsqvtiifk dgtdiywarq
      121 qinqriqeaq selpaqiapt mspvstglge iyqwvlkadp nakkpdgtay tpmdlreiqd
      181 wivrpqlqrv kgvaevnsig gfektyvvsp dlnrmqqlni sleqlqqala qnnknrgagy
      241 iedngqqltv rvpgafngls dientmlgsp ngspirvgdi aqvsighdlr tggatyngke
      301 tvlgvvmmam ggnsqtvska vdaklqdiqn slpkgvviet vydrtilvek aiktvqknlv
      361 egailviiil flflgniraa litacvipls mlftltgmaq qnisanlmsl galdfgiivd
      421 gavvivenci rrlahtqqll krpltqserf kevflaarqa rrplifgqli ilvvylpifa
      481 lsgveakmfh pmalavvlal vaaiilsitf vpaavalwvk gdiqekesrw mlwlkakyqq
      541 tldisyqyka vvltfalcll vitgfistkl gsefapqlse gdfaiqqlrs pstgleeslr
      601 iqenteklll ksfpeikavf artgtaevat dvmppnisdg yimlkprsew pnpkesldel
      661 rgrmvtylat ipgnnsefsq pielrfneli sgvrsdigvk ifgddmnvln teatkiskii
      721 qqisgssavk veqtsglpll nvevnktlaa qyglsvrsiq dlvatniggq svgeilegdr
      781 rfdfvirlge qdrsvasvsq lpiqlpnggs illsdvaqvs tieginqvsr engkrrvvvt
      841 tnvegrdlgs fvsdvqtqlk aytlpsgywi eyggqfenla sakarmqivi plalitifil
      901 lmavfhnvke sllvftgipf altggvlflw lrdiplsmsa gigfialsgv avlnglvmlt
      961 fikelrdkyp vhkavwqgai lrlrpvlmta cvaslgfvpm alatgtgaev qrplatvvig
     1021 giisstlltl vllpvlyrwi nekkvs
//
LOCUS       WP_284720281             776 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent helicase [Polyangium sorediatum].
ACCESSION   WP_284720281
VERSION     WP_284720281.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..776
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=86442
     Region          17..697
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mtdlvafppp afpepadeln epqaravaha egplvvfaga gsgktrvity rianllavhr
       61 vppyrvlavt ftnkaagemr rriaslagde iakelwigtf hatcarllrr fhdaaglern
      121 fviyddsdqr avvarvlkel slddkryppr qvlsrihkek qegrgpdafe pqgffddail
      181 kvyegyeryl rkanavdfdd lilsvlriae dpkslagddl rarfrhvlvd efqdvnqvqy
      241 rlvralaasr nlcvvgdddq siyrwrgadv rivrnfrrdf pdaaivkleq nyrstgnvvr
      301 aalgvikpak drepkelwta rdpgepvvvv aaqnehdeaa wvaervreaq argvplgeva
      361 ifyrvhaqsr vleevlraer ipyqivggmr fferaevkdc lsylrildnp ksdvdlerii
      421 nvparkigga tldrltqvan alnvplyeai lpltdrgglg taakksllaf rdlieglrek
      481 aasappsdla revlertgya rmldeddsae sdarkqnlqe lvgsildyea eaaaagqvgt
      541 lsgylervtl ssdidaleda prvsmmtvha akglefdtvf itgmedelfp fkgpdpkrne
      601 dieeerrlay vavtrarerl fvthtarrmi fgntrfgvps rfitdfpvas vkplmtaaas
      661 sersfrdgyr dghrdeparp rgpwshpmdr gsdaparsfs trspstptra pgeryierep
      721 geasseggla rgarvmhekf gvgaiidvdp gddpiatvkf sgwgvkrika rflrte
//
LOCUS       WP_284720295             237 aa            linear   BCT 25-DEC-2024
DEFINITION  YsnF/AvaK domain-containing protein [Polyangium sorediatum].
ACCESSION   WP_284720295
VERSION     WP_284720295.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008079
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..237
                     /product="YsnF/AvaK domain-containing protein"
                     /calculated_mol_wt=26496
     Region          106..233
                     /region_name="YsnF"
                     /note="Stress response protein YsnF (function unknown)
                     [Function unknown]; COG3861"
                     /db_xref="CDD:443070"
ORIGIN      
        1 mvnpfvdqvr egmevrtldg hklgkvvsvh andfvvekgf ffpkdymisc ddiaevreet
       61 lvllrrreel sfeggafssr aathqeplqs alrleeaert eeaarlalhe eqvqatthte
      121 qvgevhihkd vvteerlltv pvkrevvtve rlpvaaqgar tsasegkvfq eesivvpire
      181 evvdlhkrsv vteeivvmra teqteapvst tirrevaevi segevdthev plrktgt
//
LOCUS       WP_284720312             346 aa            linear   BCT 25-DEC-2024
DEFINITION  phosphotransferase enzyme family protein [Polyangium sorediatum].
ACCESSION   WP_284720312
VERSION     WP_284720312.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..346
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=37692
     Region          29..299
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mmetipswil arfrdldqrp haphggglin rtflvegrag kvivqrlhpv fagvvnedid
       61 avtahlaakg lwtprplrtd dgalwvddee grawralsyv egqshdrvpg psfareagrm
      121 varfhaavad lvhdyrhvra gvhdtkkhla tletaldaha ehrlfgevep larrllaeaa
      181 rlpdldqlpl rhvhgdlkis nllfqgeqav clvdldtlgr miwpfemgda lrswcnpage
      241 dvahvaidag tfgaalagyg evargaglvs aeeagavvdg laticlelsa rfladalrea
      301 yfgfdarrfp argehnlvrg rgqlalfdsv qarrteleha araalg
//
LOCUS       WP_284720317             445 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Polyangium sorediatum].
ACCESSION   WP_284720317
VERSION     WP_284720317.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..445
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=47132
     Region          3..437
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 martlgtggm gsvyearhtg tgrrvavkvm sealaandem lvrfqreara lgaietqhiv
       61 qvfdlgvdrs sghpymvmel lagmdldahi krngplppel alrvvaqacl glqkahetgi
      121 vhrdikpanm flaerdggel vvklldfgia rirkhdpsav ttgeltqtga tigspqymsp
      181 eqakglrtld hrsdiwslgv vlykalcgkt phhvhqvigq livaictepa pplqdlapwv
      241 ppevaaiahk alqlnaedrf anvsemlaai qqllpagwnl rkemfsplpe rerlrvaprl
      301 pmagrapmps ttapplaasg plpglaphsq sakvrtavlt fagvvmiais avtlftfkyt
      361 ssstedtaep ktggaesapa appvektapp aeptthasnk apepppsaan vvgtssaqgs
      421 rlrppstata pkpnasanhk irdel
//
LOCUS       WP_284720329             312 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Polyangium sorediatum].
ACCESSION   WP_284720329
VERSION     WP_284720329.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18445993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..312
                     /product="ArsR/SmtB family transcription factor"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34157
     Region          1..90
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
     Region          152..260
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mstymdlagt vgtlnilgde srlrlcalll erelsvtdlv kitgisqsrv sthlarlreg
       61 givrdrrdgq rsfyvlakes lsstaktvld aatrsgdptl erdkrrlsfl ddercgalpd
      121 sfvgemerhy spgrtwqsls vgiaalldlg evldvgsgdg aaagylapyc asltcidtna
      181 rmieaatkrl arhknvraev admhelpfra asfdaivlfh tltyaerpqr aleecarvlr
      241 pngrlvaltl dahehrtita aygerhpgfa prtlkrmlsr agltvtfadv tcrepkkphf
      301 evvlaiatkp na
//
LOCUS       WP_284720352             301 aa            linear   BCT 25-DEC-2024
DEFINITION  formylglycine-generating enzyme family protein [Polyangium
            sorediatum].
ACCESSION   WP_284720352
VERSION     WP_284720352.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..301
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=30082
     Region          93..300
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 mksrsawtlp agmlillvac apelqttgga gsggsggagg igggggiggd gaggsggsgg
       61 tggsggsggg placpdipnt ptmamvqapn ggpfycidst evtnaqylaw tksmpmmaqp
      121 sqcdwnttfl ptnmtpensv pvanvdwcda fafcaahgkr lcgqiaggal pltesagnpa
      181 ksqwhnacag ggakahpygd aynptacngq ssehndvvpv knlptceggf pgifdmsgnv
      241 wewedscdet pgdmpadnsc rrrgggyttl dhdmdcssas ttlargssnp ntgfrccadl
      301 p
//
LOCUS       WP_284720404             336 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA polymerase sigma factor [Polyangium sorediatum].
ACCESSION   WP_284720404
VERSION     WP_284720404.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..336
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=37596
     Region          20..162
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 msapmpmdep rvsepladpe lrrflldfvr rrvspadadd ivqtvlceal iaknrpddga
       61 elrkyllgia rhkvadahrr tareevrdpp elvagpppve eeallrwaer qapateeakk
      121 tlawmarege geklesiaee eqvpaarvrq rvsrmrrwmk erwlaelaav aalvvlavvl
      181 wrvardaedp eailplpdrv papldtpfdr aralradalw wcergsyric veeldaarql
      241 dpkgdeapev qaarerarra ltvpptpttt prdtkdvkge rnedapapkk aapapkpvpt
      301 svkpkldpel ldrgteneka kpsktqkkgd vdflkk
//
LOCUS       WP_284720419             372 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Polyangium sorediatum].
ACCESSION   WP_284720419
VERSION     WP_284720419.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..372
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40313
     Region          151..356
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mkpiasffaa llvasaaplf ascldvaegr arrdldigra sqgavrvdva eglaavrrlg
       61 prelhlwasa ptlsfrlttg aaeggawdvr ienllpdael vaatkagapl pveivaapfp
      121 tertfrlelp aneeitlsla apdralldpw rfavfadvqe aigdvqdiys kmnttpgirf
      181 alisgdltaq gtpeqletfq remktlvfpc yatlgnhelg trddlyheyf grgnytfdfr
      241 gvrftmidsa satldplvyt wldgwlegsr drlhvvtmhi vpidpvgsrn gsfasraead
      301 kllaqlargg vdltfyghih syyafenagi pahitgggga ipermdgigr hfltvdvlpp
      361 grieqvaivr vd
//
LOCUS       WP_284720428             332 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Polyangium
            sorediatum].
ACCESSION   WP_284720428
VERSION     WP_284720428.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..332
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=36787
     Region          10..328
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 meefgistgk vlltgasgfi ggrlqgalas rgvdvvslrr rgsppakqgr sveveyddra
       61 glerligeek pdyvlhvaga tkgvayadfq ranvmptenl lealrkkhpe vrrfvlvssl
      121 asygpssatr phveadaarp iefygqskle aervveragd vipwtvlrpg gvygpgdvdy
      181 fnlfreverg rnvffgnkkr wfsgiyvddl vtatlvaash dgakgraffv cdnepvtwer
      241 fqgaiveasg rrvltmdlpe mlvdvaafgg eiatrfdkkp rlfnrqkakm gaqeawtcks
      301 dalreatgwr skvgvqegvr lalewyrrek wf
//
LOCUS       WP_284720433             498 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Polyangium sorediatum].
ACCESSION   WP_284720433
VERSION     WP_284720433.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..498
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=51324
     Region          12..489
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mssdlaagsi fagryrverr iaaggmgavy evvhletnrr ralkvmhanf lqsddlrgrf
       61 rqearvaaei eseyivdvfd agiddatgmp flvmellrge elgkrlrhtg plppaevvsy
      121 lhqtslaldk thrahivhrd lkpdnlflce redgpprikv ldfgiakiva agstaagatq
      181 slgtplymap eqflmessvs patdifalgm iaftllvgka ywfeesrgga nvfafaaqaa
      241 igprepasar agrlgvslpp afdgwfarat aktpserfps atsavkalae algvaqpglg
      301 gsgvfppgaf prpsfasrps evaistldtq attpmaprra plpsgaefgv mtpvgqagtp
      361 mgpvmtplgs gmtavpagrr sspagliaag vglacllval vlffalssre eaktpepaaa
      421 apsaqpvvat aapvvvpaap vetaevapaa iasasaapvv saaaatptst patttqstkt
      481 sgtpagktak pkstwsrd
//
LOCUS       WP_284720436             270 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family oxidoreductase [Polyangium sorediatum].
ACCESSION   WP_284720436
VERSION     WP_284720436.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..270
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28345
     Region          3..217
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 msvlvltgsa sgigahmtgv farrgdtvva tdvdlaalek raaegawgtn vrlarldvre
       61 aadweaaldl aeregggldv vmniagvlkp gwvpdlgpad vdfhldvnvk gtvlgtraaa
      121 armiargrgg hivnigslas lapvpglsly aaskfavrgf tlaaamelgr hdiavtlvmp
      181 davqtpmldl qvdheeaamt fsgpraltve dveralltev lpkrpleitl plgrgmlara
      241 antapaasrw lepmltkkgr eaqerikqgr
//
LOCUS       WP_284720445             659 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine-protein kinase [Polyangium sorediatum].
ACCESSION   WP_284720445
VERSION     WP_284720445.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..659
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=68061
     Region          12..284
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(12,36..37,66,71,76..79,92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,40,42,74,91..94,98,100,141,143,
                     145..146,148,162..163,166,187..190)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,40,42,74,91..94,98,143,145..146,
                     148,162..163)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(23,98,100,141,143,145,166,187..190)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(162..169,174,183..190)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <249..655
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mrpqvgqvin nkyrlvrvig dggmgsvyea rhevlgttva lkflhpelsr rqglvqrflq
       61 earvsaqiqs phvvrvsdvd qnangqafiv meylegktlq tlyeelyhag qrlsyadale
      121 yasqmldgve aahragvvhr dlkpdnvmit rgskgepllk lldfgiaklk vtgeldrglt
      181 rpgvimgtpe ymapeqaysa davdaradif slgvmvfeml agrrpvggde phqiasaylt
      241 gqiaqltdla phvppelasv vhramgpkpp drynsvaefr salepfamgt rsgaagaava
      301 tpmpgsvtpk pavspaaavt pgetgaspip ktlpptddkp ppgvsepslp pyqvgatplg
      361 gfdaphrgph tsigeplaas ltpsprydat apaaplasht appggydmsp rpggtavgqa
      421 lpsggygpvq tnyggapgyp pangysappg ygpttpmnpi garathqaqq krsggssvvl
      481 mlllaaavtg vvvggvylgq kltsteekgn dpvalqpppt ttvvssdpna qpvqttgpvn
      541 ttptqpspqt tvpkttttvg gtkppttgtg tttspqpsas gstaptgipn pwgsgiplpw
      601 gstqiplpfp mpgqqptaqp tnttpaptat ptnttptprp stsgsgrpri ripipgqnp
//
LOCUS       WP_284720527             526 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Polyangium sorediatum].
ACCESSION   WP_284720527
VERSION     WP_284720527.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..526
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=57354
     Region          10..495
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mlvtgvlfhd ryrvvrsiks ggmgavfevh deptnrrral kvmhpavlen svmrgrfaqe
       61 atvtggiese hlvqvldagv dtstqlpflv mellvgeelg gmvkrrgplp epeavlylsq
      121 valaldktha anivhrdlkp enlfvttrdd grscvkildf gvakvavatt lahttavvgt
      181 plymapeqis gdagirasad iyslahvayt llvgeaywrp ellqlpsvya lfgkiiapel
      241 peaptlraar rgvqlpagfd dwfrrvgare pkerperatt aiglladlfr vplsvppsgp
      301 ilplselppp sqaprrisqr ppvpsvpipi pvprpsrdrl rddptpppsa papgsqkprs
      361 rfsdipasye ptlrsevkgv ldqqglvdil eveyqfsant gipfsvllfq vqeppraegp
      421 rarpfagwgl ertmaelihl aralgpekst igrwpsntiv vvvraslgit lspseardil
      481 afvgkqlagr delpeirsgy sqcwltdrsg mdavdrarfa lkpfnr
//
LOCUS       WP_284720530             666 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Polyangium
            sorediatum].
ACCESSION   WP_284720530
VERSION     WP_284720530.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 666)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 666)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..666
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=71748
     Region          10..626
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mrlstsavll lgasllpaav araeepapng kdkdkgaevv vtgtrmpeqs qratvrvdvv
       61 trdeaerrga tnvaeaiagq pgvqinpsay gdignpsaiq iqgldrqrvl vledgervig
      121 dvggaidlsr mplsdvarve vvagpmssly gtsaiggvvn vvtgqplhpg fsgrvrlegr
      181 nrrgviaqgn aawrgertwa tldgnffrtd gvslledavd lampsrlqgm lgmrlgaeln
      241 artrvqarvr wlhdasegrq sqvvpglgty ridlpqrtnr favhlvelvd lgkgstlrla
      301 lgqqwafdtt qkdryespid etrdreasls sleatgtiad grrtwvvgmr aeveklsqsl
      361 traelisgsv qtstieelvp vtlgsiagya qlgwklfdsl tllaggraem hlryggvavp
      421 rlalsyqplp svtvrasvgr gfrapaakei gfafdhgalg yrvlgnpnls petswgtsgd
      481 vsyrskngfl vrgsvfanwi dglididirp aasqggiddy tyrnigrart fgaqidgact
      541 iagvlraeag ysylwtrdde nqrplegrpp htvvtalrad lplrlelvlr yrmvtdafld
      601 eglrtpgfqt idariarpif rgarayagvl nalgaqkdpt rlgdqrpvqg rtlyfgltad
      661 ipaeep
//
LOCUS       WP_284720534             388 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Polyangium sorediatum].
ACCESSION   WP_284720534
VERSION     WP_284720534.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 388)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 388)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 388)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..388
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41378
     Region          76..379
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mrrdlpvewl dallvascei ppnasaeeaa tslvaaafea lpdsaigvcv pggsegqvvv
       61 rrgarsegae spdptrlfpe yafervvvin adegstlhla sddearfagt gsmdafvdrl
      121 alalgaalrn arihraarah gtevkeleaq viqagklasl gqiaagivhe lnnpltsiva
      181 ysdylhkkal rteadpadve rlarineaae rilrfsrdlm aysrptasvp apvaihdtie
      241 ralvfcdhvl gemhveverq fgdvrlvrgv agqlaqvfvn lftnaahamr eqggrliikt
      301 amsdvgdavr itiqdeghgi daahlekife pffttktdgt gsglglsivr nivashggki
      361 rayahaekgt vfvldlplaa spsepper
//
LOCUS       WP_284720612             189 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin-type N-terminal cleavage/methylation domain-containing
            protein [Polyangium sorediatum].
ACCESSION   WP_284720612
VERSION     WP_284720612.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR02532.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..189
                     /product="prepilin-type N-terminal cleavage/methylation
                     domain-containing protein"
                     /calculated_mol_wt=21043
     Region          1..>49
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
     Region          5..130
                     /region_name="typeII_sec_gspG"
                     /note="type II secretion system protein G; TIGR01710"
                     /db_xref="CDD:130771"
ORIGIN      
        1 merrrgftlt eilvvifmia llaavaspaf irimrdigls rltmqlaevy rrgyvesser
       61 atflvrfrkp sgsvqietir aaldtptptl isprgcntin wddpllerqt yrfastdkkt
      121 lvdvgflgpd nasqevadvc farrtafvry ndgaftqmvg aakvsvknls ngrirrvlvp
      181 sfglprviq
//
LOCUS       WP_284720618             250 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Polyangium sorediatum].
ACCESSION   WP_284720618
VERSION     WP_284720618.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..250
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25734
     Region          2..249
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mrfqgkvalv tggtsglgra taeafarega kvvltarseg pgrevegair aaggeatflp
       61 cdvtderqig alveqtvkty grldcaynna waapkmapls efsaefeanf allrglfacm
      121 kheiaamltt gggvivngss aaaragaafl gpygaakagl esatrtaaae yagqnirvns
      181 lalgafdtpm sretykdapp ealaafttri alrrlghvde aaqtvlflcs pgasyitgan
      241 laidggyflt
//
LOCUS       WP_284720633             492 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Polyangium sorediatum].
ACCESSION   WP_284720633
VERSION     WP_284720633.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 492)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 492)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 492)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..492
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52400
     Region          127..487
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mnlarkrltr kllavfatpv ilgfvvtgvv sirttraslv esseraladn iatlrtaslp
       61 iaatgrteea valvervaae etvhgvafyd ergapfvrss alrsapsald vlaaravatg
      121 dashgtlqig deevlvrvep vrdapglgav vmtrelgpid rmidltlvrl altggaaalc
      181 vslvaiwisr vlgrawgdlv havdrvaagd ldvrveaspe leldrvagav ndmtrslaea
      241 rekllaaeae rtelaarmrh aqalavvgqv agsfaheigs plntilgwsr lsaadddlpe
      301 pvrrqfetia gqceritriv qrmldvsrpp tdhvvpvqla dvvrdvsafl apdlrvrrie
      361 lrlvvaerlp pivavrdrll qvvmnlcina iqaqprggtl rislargeea gperepvlrl
      421 evadagpgip eekrsqvfel fystkvesgg tglglpivad vvrdlggrve igdapeggal
      481 frvllpagss sr
//
LOCUS       WP_284720643             262 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Polyangium sorediatum].
ACCESSION   WP_284720643
VERSION     WP_284720643.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..262
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=28518
     Region          2..212
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mtpvtalrlq aqhirrllsq hpeevparip smvetfdrql grlallcdel lhatqivase
       61 lplacedvdl atlvgeivdr veprpdvral vtikvsgapr gqwdrmlveq lvlhlvrnai
      121 vygegrpvai dvaqveggar llvkdhgigi aeedqarife rferavspsr fgglglglyi
      181 araaaeahgg sirvestpge gatfvvelpt epgvarrare qallphaaha igftregrrr
      241 shprrrtgav araarasrir af
//
LOCUS       WP_284720644             513 aa            linear   BCT 25-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Polyangium sorediatum].
ACCESSION   WP_284720644
VERSION     WP_284720644.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Pereira,J. and Lupas,A.N.
  TITLE     The VCBS superfamily forms a third supercluster of beta-propellers
            that includes tachylectin and integrins
  JOURNAL   Bioinformatics 36 (24), 5618-5622 (2021)
   PUBMED   33416871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..513
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=54867
     Region          46..111
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          <185..230
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mtapsepppg gdvtqappra tppyptepgy rsadttmnsl gaaladidgd gfkdlvvang
       61 ndlnqrpvtv yrndgrgnfp nepswssddt dyhagvavgd idldgfvdva vtvgpwidak
      121 tlgytkvyfn rggalerwps frttdryssf gaalgdydgd gdldlavgva feldterdte
      181 pkpkpgrvri ykndggklsr tpawtssarm haltpkfadi dgdgfldllv aarglplyrg
      241 algedgevhl dtsaawtarv ergiplfvdv gtiggrrgiv tfyndhykdi vppddlapar
      301 ppetppayvg nlypsppppa scasgigsds rlmaywpfss adpiwtsets gwgagvrlad
      361 vngdgaqdll asrwgpqfyg ygaplvmflg tsrafeatpa wssstcgvge aialadldrs
      421 gfteavesfa iekpqagltl saqlveeile irrdgallgr gayvmvpgdn wisfarrlap
      481 gerirvryth spapdialas tmdsndvfyh har
//
LOCUS       WP_284720727             273 aa            linear   BCT 25-DEC-2024
DEFINITION  SirB1 family protein [Polyangium sorediatum].
ACCESSION   WP_284720727
VERSION     WP_284720727.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458474
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..273
                     /product="SirB1 family protein"
                     /calculated_mol_wt=29916
     Region          14..265
                     /region_name="SirB1"
                     /note="Regulator of sirC expression, contains
                     transglutaminase-like and TPR domains [Signal transduction
                     mechanisms]; COG2912"
                     /db_xref="CDD:442156"
ORIGIN      
        1 mvpsrpsltl fahlvsrpep eidlvqaslv faeseypsld varyvstlea lgraaarria
       61 qdaphgttee rvrvvlewly gsqgfrgnae eyydprnsyl nevldrkkgi pitlavvlld
      121 vatragidak gisfpghflv gagdrqkeap rpgfgtryaa kqvetpgvpl vidpfhgril
      181 agqelealha rvtgagprvd prllepcskr qilarmlsnl rsihasrndd erlrnvlehl
      241 vaiapspels reldrlggsr ailarptanr sfn
//
LOCUS       WP_284720891             477 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase C [Polyangium sorediatum].
ACCESSION   WP_284720891
VERSION     WP_284720891.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..477
                     /product="phospholipase C"
                     /calculated_mol_wt=52964
     Region          73..447
                     /region_name="PlcC"
                     /note="Phospholipase C [Cell wall/membrane/envelope
                     biogenesis]; COG3511"
                     /db_xref="CDD:442734"
ORIGIN      
        1 mrrsssllla llptlalvgc tpdeeapppp ppppgpaewn rdvdppsdde aaakrdacgy
       61 tagmlpaetq gkshpygaei pvdhivvvmm enrsfdhyfq klpeygqddv dvapenftnp
      121 ddtgtavatf rdsqlcfvdt nhewtgtheq inggkmdgff ktndgwhelp sagapedmls
      181 grrglgyytq ddlpfyywla nefaiadhyh ssvpgptwpn rmylyaassf gavhntfvtp
      241 dktlfdylel rqvswrvyvs ttpgaaifvd kylqyskdeh ghfvpienyf ydletgnlpq
      301 vvfvdpgiar egyaqndehp pavamlgeqf satvidalak ssawdrsalf ltydehggly
      361 dhvvppaacp pdeitpklep gdtdakfdql gvrvpllvvs pyakkhfvgh ktydhtsivr
      421 fiearfqmpa ltnrdanaea pwemfdfenp phaepptfam ptvdqaklda ckaifep
//
LOCUS       WP_284720963             375 aa            linear   BCT 25-DEC-2024
DEFINITION  lipase family alpha/beta hydrolase [Polyangium sorediatum].
ACCESSION   WP_284720963
VERSION     WP_284720963.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18498059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..375
                     /product="lipase family alpha/beta hydrolase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38757
     Region          85..191
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
     Region          <160..236
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mrffermlaa hvwptcalvl mglaaacgsa getassgipa ggnggnggvl tgvggggqgg
       61 assassssss geggeggvev klgppypivl shgffgfedf agagfvtyfy gvkdhlasqg
      121 eldvftpavd pfnssdfrga qlvehieqil aitghakvni ighsqgglda rvaanlrpdl
      181 vasvvtvatp hggsrvadia ielvsdpaaq dvvsdllali gaplydefge qtnvwkplel
      241 fsqpgiaafn kahpdepgvf yasiagrtdl higgdscdad vslpfiaewk gkldtvdpll
      301 slfesildgg fgdpypndgl vrvvdskrge fwgclpvdhl devgqlfgds agigngwkhk
      361 vfyadvvael rkrgf
//
LOCUS       WP_284721152             412 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Polyangium sorediatum].
ACCESSION   WP_284721152
VERSION     WP_284721152.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..412
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45016
     Region          51..374
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrsfcatlfv gllalagcss sgagdstpvv legpppfpvk prtewptraw ptadpasvgi
       61 dptalkkldd ylfarhgddv drkgqrtnaf vlvkdgklvf ehyargttae tslltwsvsk
      121 sfvntligia alegrfkvdd paskyysalg pdkqnvrltd llrmssgidw netyeaspif
      181 ssvmamlytr gqddmprfva ghglahapgt hwsyssgdtn lllaalratm sdaeyasypw
      241 kalfeplgmt sarferdgag nfvgssylya nardlakwgl lyladgvwdg krllpegwva
      301 ytltmapays ttdvppplwe dnpgaqvyln vgdpkrnipr pwpaappdtf aalghwgksi
      361 fvipsldlia vrmgddreyg csahvqkncv pdrekaftkg yylellsglv kr
//
LOCUS       WP_284721150             450 aa            linear   BCT 25-DEC-2024
DEFINITION  M1 family metallopeptidase [Polyangium sorediatum].
ACCESSION   WP_284721150
VERSION     WP_284721150.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..450
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008235 - metalloexopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47742
     Region          37..>444
                     /region_name="PepN"
                     /note="Aminopeptidase N, contains DUF3458 domain [Amino
                     acid transport and metabolism]; COG0308"
                     /db_xref="CDD:440077"
ORIGIN      
        1 mrigrharlv gigfvalaal gcakdegegn tsnstgtpie pppepsanld rniqrtaltv
       61 dlstmtgtav ldlagsledt gasfeaagle iqsvsraegp lkwtfaqgql dvgvpkslgs
      121 aqitvdytfk eqaqfeglma kgstlvwpyf cgnlfpchsd padgttfelt vtgtpqgmtt
      181 lhppaigida psyqiawatg sytkldvgkt fqgtnlvayy lpgggtdaqk gtavlvdvmn
      241 fyetmlggyp fggeagaiav dwgpgayggm ehhplwhvst iamgdpwiqa heaahgwfgd
      301 gvrpacwedf vlsegtvsyl earaitevmg adegtkvwsh yttrlntama gsapkiawpe
      361 gcgvvdllkd qlfgdiaymk gafffralea kigkakldps lkafflkhkg kaahfqdlld
      421 iiksvggydp tacatawlrs emvpseqvcp
//
LOCUS       WP_284721155             341 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase, partial [Polyangium sorediatum].
ACCESSION   WP_284721155
VERSION     WP_284721155.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..>341
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
     Region          11..>309
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 malepqtatg sasklgkyel tremsgsgva stwlaqtegs tksyvvlrlh khvtkkpeva
       61 eaflrdakng kllthanvvp mvetgvgdge ifvvaehfeg etlsslvtna ktagiplpia
      121 lriglelleg laaahaqsep vahgelspfh vqvgkdgvtr vggfgwaral aklgphgimk
      181 qdrlayappe rvkamsaatp ggptgtidpk gdvfaaavil weiiakqrlf askmeaavvq
      241 kvlsgpiqel ssvmieglpa aleealpkal erdpakrasl dsllqalrsv padklakpee
      301 vgafveklas kpgaapavap aaspavapaa aagpkpvpaa a
//
LOCUS       WP_284721170             381 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Polyangium sorediatum].
ACCESSION   WP_284721170
VERSION     WP_284721170.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..381
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39905
     Region          <115..379
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mspraalpla tlawllactp aadtedptas haassgsesg sgsgngsggg ggsgsggggg
       61 sgggsggnss sgsggggpiv plpttpftlg gqngwehdea qpsgyfhtyd altigpagfa
      121 prkvhvylpr ayaetdaryp vvymndghtt fwpggpgnit wdvdqrlsel yaekaippvi
      181 vvalhpiere reyshvdmgd gkpccdlpey tayvaddvks fidtyyrtkp epantailgs
      241 srgglasfym anrrpdrfgk agclspsfwa gldpvfggnf pggplessvl vttlantlga
      301 pairprlwid wglirtggfh neaieaaatk rgvemvallk qsygyvegke lfwyedpiga
      361 hdeiswnrrf pdvmkalfga p
//
LOCUS       WP_284721181             721 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Polyangium sorediatum].
ACCESSION   WP_284721181
VERSION     WP_284721181.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 721)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 721)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 721)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 721)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..721
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=81409
     Region          1..720
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mvtsqelier vqayqpgadv eliaraydya aeahkgqmrk sgdpyfshpv svagiiielk
       61 ldvasivagl lhdvvedtla tlsdierefg qevaflvdgv tklskinfas kedrqaenfr
      121 kmlvamardi rvllvklcdr ldnmrtlehm kpeaqdrmar etmeiyapla nrlgiarfks
      181 eledlafkyl epeahadlsq kvlgtkaerd kyiadvskil agklaeqgfa cdvtgrakhn
      241 ysiwrkmqsq qcdfdqvydv iafrvqvetv aecyatlgvi hsqytpvpgr fkdyvalpkp
      301 nmyqslhttv igpgreriev qirthemhrv aeqgiaahwk ykerhsggld pkdaarfgwl
      361 rqlmewqkel kdphefldsv kvdlfqdevy vftpkgdvrv fprnatpidf ayaihsevgd
      421 hcsgarvnga ivplrsklrn gdvvevmtnp sqqpskdwld fvttsrarsr irshlradqr
      481 erslklgrel lekefhqrgi smarltknea evrklcehfn aqtfdellig vgygkhspka
      541 iieflappqg ndkeslppps lkesrieslv rkvtgrdnhg irlngiddvl vrytkccnpl
      601 pgdeivgfit rgrgitvhrr ncpkaldtdp errveiswda rakinrpvql rvmtanrpgi
      661 latvgqtfhe qginiseatc ragddgratn tftflcsdla qlkgvirqlq ripgvmaver
      721 t
//
LOCUS       WP_284721237             598 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Polyangium sorediatum].
ACCESSION   WP_284721237
VERSION     WP_284721237.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..598
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=66734
     Region          59..531
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mdatkkgeaa fspealqeky rierekrlrp dgstqylels kvyadfdkdp yvepgftrpa
       61 vtetidvliv gggfggmlaa vrlrqagvhs frvvekggdf ggtwywnryp gaacdvesyi
      121 ymplleetgy vptekyakat eifahcqrig rqfdlykaal fqteveqmdw deeqrrwtvt
      181 tsrgdklaar fviiaggilh kaklpgipgi etfkghsfht srwdyaytgg gpagsmtrla
      241 dkrvgiigtg ataiqaiphl gasakqlyvf qrtpsgvger nnqptdeawa ktlapgwqre
      301 rmvnftaivs grkqdvdlvk dgwtyifdda etrgaqtpae aaklrqlady rkmeeirgrv
      361 dsivkdsaaa ealkpyynql ckrpcfhdey letfnrpnve lvdtdgkgve ritptgvvvn
      421 gkeypvdcli ystgfevsse ytrrlgfdir grggkslres waegpttlhg mhtrgypnll
      481 ifsptqsgwa infvhvldel aqhaayiier clkqgvetie ateqaqqqww evilgslmtn
      541 piafggpect pgyynnegil amslarfaaf nggtleffei lqnwrkaddl aglerthg
//
LOCUS       WP_284721249             415 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Polyangium sorediatum].
ACCESSION   WP_284721249
VERSION     WP_284721249.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 415)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 415)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 415)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 415)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..415
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45002
     Region          1..361
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 mitrfevdgf kslrdfavdl epltvfvgpn gagksnllea mallgrlasm pveeafkkgr
       61 grvldqfsrf ggetsrtirf tvevslgtpi pafedgapsl ptryryelti errardsgie
      121 elaikdeslr vkadgddaae galvlwqarq vgphrllsvl pntgegaeqw fhfpffttlf
      181 phynraqsrg whavigaiar gfdsfrflhl daarlrepse kissgilapd asnlaailad
      241 lpapalgair adlaslvpgl sgfdvvpegd alrldfklsg gehlparlas dgtlralall
      301 tvltvephps vlgieepeng iypgrlrrll silrdtsasd nksqilltth spvvvaafrd
      361 qpqmlrvvdv vvrdgkretr arpvgkpkkp sdsafvaslr evdmllhaad aeaae
//
LOCUS       WP_284721293             711 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine-protein kinase [Polyangium sorediatum].
ACCESSION   WP_284721293
VERSION     WP_284721293.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..711
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=75804
     Region          29..305
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(29,53..54,83,88,93..96,109)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(36..37,39..42,44,57,59,91,108..111,115,117,154,156,
                     158..159,161,176..177,180,206..209)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(36..37,39..42,44,57,59,91,108..111,115,156,158..159,
                     161,176..177)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(40,115,117,154,156,158,180,206..209)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(176..184,202..209)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <337..656
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mtsaqnpigp sdpsaapqgy kptlldgtpy rflaplgrgg mgdvveaehv algkrvvvkl
       61 lqerhasrpd fvdrmrieaq alakithpnl vqvtdfgqta egrtflvmer lhgrdlreel
      121 ehrlffpvae aidvtrqala glaaahdagv vhrdvkldnl flcdapdggr rlvkvldfgv
      181 akvinvmgdn tplplafpta egvamgtprf fspeqargrp vdgradlyav gmvlytllag
      241 rgpfdhittl leltrahafq vpeppsrfat qalpagldai vmkalakepa erfatartfa
      301 aelervadgl sasnirprwd atdvmptvpr mqkaaqpavd depatmrvdt fpksalpkam
      361 pddddeapdt ptrrlvrpmp fmraqraplp lpeaapaiap apapawdakl pttiseppkt
      421 lenipqpfse pstqprsdta tsqpaksqev asfppdpild atltsamrap kppsdtsalp
      481 pdpildatfp sgpraeepaa aripsehppa nrvpsehpsa ptrtgserpt ssgggtgrad
      541 risalpgrnp drpsivpgre grisvlpgrt drtsalptrp drisalparp eptsnvppra
      601 aepvavperp errsnlpaaa plhppaplpe erisvpppap ggvrplrapv pwrrrpaass
      661 tsgaaraaat ttqnkpveve vesgkrqmai laivalvtva vagvllalrf r
//
LOCUS       WP_284721343             346 aa            linear   BCT 25-DEC-2024
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Polyangium
            sorediatum].
ACCESSION   WP_284721343
VERSION     WP_284721343.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..346
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36636
     Region          <30..88
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
ORIGIN      
        1 mlrqglgrrh gprrillagv atalalllvp arpagafphv vragetlaqi aervygrvem
       61 eqilvsanal dagrglsivp gmrleipsvg hhrvaagetw tsladtllgh pdrsdvlalt
      121 neakpwiqpt egqeirvpyn lryvagpgds tltvayrflg qrdkawmldr ynrlggealq
      181 rgdvvlvplt eleltaegkt laasagalvr segagrarda qrrvetdlpq laadvrngry
      241 vdavarasrm lgsgdlsrtq laqihqrlve ayvaldaqgl aetsclawre adptlvldpi
      301 elspkivrac tnastlgaaa pppsvipsas asaapsaprr apaggr
//
LOCUS       WP_284721377             505 aa            linear   BCT 25-DEC-2024
DEFINITION  amidase [Polyangium sorediatum].
ACCESSION   WP_284721377
VERSION     WP_284721377.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..505
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54403
     Region          5..496
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 msfkeyddhd alglaalvkk gevspaelle eaitraervn grlnaivigm hviarararg
       61 elpdgpfrgv pflmkdmata yagvplqaas rlyrgnvpah haelterflr aglvvfgktn
      121 spefgilptt epelygpthn pwrlgyspgg ssggaaaava agivpmahgg dgggsiripa
      181 sccglfgfkp trarnpvgpd vsesfygfaa ehvlsrtvrd saaaldatag peatamyhap
      241 apyqgflaal gsppeklria ftsdpllhga ephpdnrrav eetakllekl ghhveparpr
      301 fearefakgf flhfsalvaa eiraaeaflg rpakredver ttwllnlvgr stdagtfvyy
      361 rrklfdvqra iagffqdhdi lltptigrpp vphgtllakg leegmqelva rldrpellrl
      421 prlldmavdr ayafspftpv fnvtgqpsas vplhwnadgl pigtmltarf gedarlfrlc
      481 aqieevqsfr arrapvhaaa spgls
//
LOCUS       WP_284721428             336 aa            linear   BCT 25-DEC-2024
DEFINITION  formylglycine-generating enzyme family protein [Polyangium
            sorediatum].
ACCESSION   WP_284721428
VERSION     WP_284721428.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..336
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=32998
     Region          133..336
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 mrrdllrral ilgfatlpva vvasqtaagc gaseppdvig qpttsssttg tggtggsggn
       61 ggnggassss sgaggagtgg gsggmgaagg aggmggatss sssgmfidda gakacpsitn
      121 taamvavpgw dgkaycidat evtnaqyatw lerspsvanq satcasnlsf tpstgappkn
      181 dypvgsvdwc dafayckgvg krlcgriggg papyyahdda srnqwfsacs hgdtqafpyg
      241 paydanacnv kdaaygavlp vgtlascggg feglvdmsgn vwewedscvp adggvdvcrr
      301 rggsfsssad nvdcdvassr prdaaeantg frccad
//
LOCUS       WP_284721559             443 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Polyangium
            sorediatum].
ACCESSION   WP_284721559
VERSION     WP_284721559.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..443
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=48054
     Region          18..439
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mprkppalst edviaralea asgaalvldg elrivlstpa asellgieip phasapkllc
       61 gdsekrpvae alaegrpvqa ilpprgssrr lvrvrslpvt qgrarvgtll lledagesfe
      121 ageilfhgmw tqdpamkvmf rvlervagdd vtvlvrgetg agkelvasai halsgrhkgp
      181 fraincaalp shlleselfg hargaftgav rdtpghvqla hrgtlfldei aemplelqak
      241 llrvvetrtv lpvgarepvp vdvrfvsath ralrkeveag rfradlmyrl rvipvfipsl
      301 rerpddipll vekfmalrne tsrrrvdrvs paamallrry swpgnvrelk nvlayayamg
      361 dgptlvpadl ppelldpslf gaeqvapspt peacaehpnp earrilevla raggnrqraa
      421 kilglsrvtl wrrmrelgia gpa
//
LOCUS       WP_284721575             332 aa            linear   BCT 25-DEC-2024
DEFINITION  Rab family GTPase [Polyangium sorediatum].
ACCESSION   WP_284721575
VERSION     WP_284721575.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437803
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..332
                     /product="Rab family GTPase"
                     /calculated_mol_wt=37033
     Region          93..>243
                     /region_name="Gem1"
                     /note="GTPase SAR1 family domain [General function
                     prediction only]; COG1100"
                     /db_xref="CDD:440717"
ORIGIN      
        1 msmliascil lafalaglvl masrhrrttq aeidarkrae vlenenralg aklhvaveed
       61 kkkvgwldhq eqeilwlrae lekrpkitrk tykiltlgvk atgktsltlk wanplidlgv
      121 lagtkidrye rtvshvsqkd vviehvfevg dwggehivda qqeligdeih gllivvdlgg
      181 kdakkvepgr iqeqlqefqs qalkyffgpk tvascktvvl finksdllsg tpleveeqak
      241 klyaplienl mkysmqldir vfvgsanfgh sthllfshfv erilpkhayd sqllqrmvkd
      301 fseapkaats ektiplpavs asseppklsr vn
//
LOCUS       WP_284721595             430 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Polyangium sorediatum].
ACCESSION   WP_284721595
VERSION     WP_284721595.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..430
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45902
     Region          <49..>102
                     /region_name="SdrC"
                     /note="Predicted secreted protein YlbL, contains PDZ
                     domain [Signal transduction mechanisms]; COG3480"
                     /db_xref="CDD:442703"
     Region          113..386
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 myqddalprr pflglelrar paegvseglp vvrvaeggaa alagvragdr llslggatvs
       61 epralvalvr glvpgaplhf eivrdgarvt lpgkatplpv ediagaevcl ghvtvrgswr
      121 qrtllaipts gkppfpgmlf lsglgtgsce lsqdpedpmr rlleglaaag iatmrversg
      181 vgdsegppcq tlgffdeveg araaleslan dprvgrivlf gqslggmiap llagegtrac
      241 gvavfgttsr kwvdcrvraa rfqgslagme gealeehvaa wsemlvsvcr egmfprdvfa
      301 arpelawleg pschgetmfg rhvslfreie rldlpalwrt ttvpvlvlhg rydhaippde
      361 grmiadeiag aspgrsllvl ldqvghdmrr heshvqsytn pragvgdegi lrtmlewlal
      421 aglireeprr
//
LOCUS       WP_284721597             617 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Polyangium sorediatum].
ACCESSION   WP_284721597
VERSION     WP_284721597.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 617)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455327
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..617
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=64387
     Region          <187..410
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
ORIGIN      
        1 msrmsksgts milgslclas vlggggctka apsneeapal appdeantra kgeqgfland
       61 gkqeaqagky dvrggdmtra pgdapaaaek akaggggaap ppaptqalip paandaptid
      121 pngrfattyr pggghlaafe savargiipp gerelvsdvg aryvtgfevp kgkalgiqag
      181 lergklppsg spfhlrltlk sspdkpaerp hlsvhlvldv sgsmqgesik qareaasalv
      241 dklapsddfs lvtfstdaev kipdgpvgar reaikkviae ikegggtnis sglelgyaqa
      301 etksipedav kvvlllsdgr ansgiksang isklaldafq kgiqtstfgl gadydgalms
      361 aiaedgaggy yylrdaaqia palgteldkr ldpaatavev rvrlkkgfdl lkvygsrrls
      421 eaeaqrvraq evaadeqaak rdnikqdrke dneggmrffi pafaagdsha llfqlragag
      481 vgkgqlalve lkykdriskk nvteefpvdi ewadsdaasg atidgsvart iqgfaagetl
      541 araaqnvagg dkqyaisllt eretilreaa ktleeplflk dadrlarmre haaqstgmgd
      601 pllfamllet asrshlr
//
LOCUS       WP_284721660             746 aa            linear   BCT 25-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Polyangium sorediatum].
ACCESSION   WP_284721660
VERSION     WP_284721660.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 746)
  AUTHORS   Pereira,J. and Lupas,A.N.
  TITLE     The VCBS superfamily forms a third supercluster of beta-propellers
            that includes tachylectin and integrins
  JOURNAL   Bioinformatics 36 (24), 5618-5622 (2021)
   PUBMED   33416871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..746
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=71577
     Region          423..483
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          472..532
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          521..581
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          570..631
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          620..680
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          669..729
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mnrasplalv cfgflanslg celiaavdrs qiensggagg atsassssss gtggiggtgg
       61 tggeggegge ggsggsggsg gsggsggsgg sggsggsggs gggsvecrvp adcpgmddac
      121 qtrtcaqgkc gldfapadta lpaqtagdck kavcdgngat iaqnddtdlp ddskpctddv
      181 ctagvpsnpn kaqgttcgag lvcdangaci gcntaadcpg tddeckvrtc tagmcgaaft
      241 eanipvaaqt agdcvtavcd gsgnivatpt ntdlppddnn actdevctag vpsypnkadn
      301 tacddgnact vadtcqagac tsgapmvcta ldqchaagtc dtstgmcsnp vqadgfacsd
      361 gdgcttgdtc qnavctagpp lvcgtgmncv sgacvypact gtnqftgstl pagtsprsia
      421 aldlngdgkt dlatsnfgtn sasvflgngd gtfaamvdyp vgtqpssvtl mdlngdampd
      481 ivvtnvgsdn vsvllnagng tfaakvdyva gtdpissaam dlngdgkpdl avsnlnsatv
      541 svllgngdgt faaktdfpvs ggpglmvamd lngdampdla iptqangggv nvllntgngt
      601 faanvnyptg aaalsvaald lngdsnpdla vanasantvs vllnngdgtf aakvdysaga
      661 gptgvvardf ngdnkpdlva tsaststvgl flgngdgtfa arvnyptgal pysvvashln
      721 gdsmpdlata nangnsvsvl lttctp
//
LOCUS       WP_284721676             400 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Polyangium sorediatum].
ACCESSION   WP_284721676
VERSION     WP_284721676.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..400
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=40643
     Region          <125..321
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mlqrsssstw aallgvmglv iasacgdags sassgggaag atsgaggmgg agggsagaga
       61 gsfgcnpvcv apqrcsaagt cidpgtcava sdcsagmkcd datktcvpgg dcgaqeakve
      121 tvppnmllvl drscsmtalv gnvtkwdiav aainkmttdy tgkirfgltl fpdlvtpncq
      181 qaaipipvgp dnetaiqdll taalakadky fpdgpcvtni qtavtqstte pafddtnrdr
      241 yavlitdgke tcgsdattem eiknlfemrg iptfvigfga gidpaqmnkf aiaggapaag
      301 anqyydasdq asldvalati akktlscayt ldtvppnpne iyvffdntte vsrddtktdg
      361 wtydagknqv vfhgpacdsl kngvvkdldi vlgcqeptpn
//
LOCUS       WP_284721694             328 aa            linear   BCT 25-DEC-2024
DEFINITION  RCC1 domain-containing protein [Polyangium sorediatum].
ACCESSION   WP_284721694
VERSION     WP_284721694.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Hadjebi,O., Casas-Terradellas,E., Garcia-Gonzalo,F.R. and Rosa,J.L.
  TITLE     The RCC1 superfamily: from genes, to function, to disease
  JOURNAL   Biochim Biophys Acta 1783 (8), 1467-1479 (2008)
   PUBMED   18442486
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Renault,L., Nassar,N., Vetter,I., Becker,J., Klebe,C., Roth,M. and
            Wittinghofer,A.
  TITLE     The 1.7 A crystal structure of the regulator of chromosome
            condensation (RCC1) reveals a seven-bladed propeller
  JOURNAL   Nature 392 (6671), 97-101 (1998)
   PUBMED   9510255
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..328
                     /product="RCC1 domain-containing protein"
                     /GO_function="GO:0003682 - chromatin binding [Evidence
                     IEA]"
                     /GO_function="GO:0005085 - guanyl-nucleotide exchange
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33531
     Region          1..310
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
ORIGIN      
        1 mgarhacaal aplpgernar lacwgyahal gladnrgdsp gelgdawpki dmgegtilsl
       61 aagikytcal vedgaarevr cfgeipggke hfvpvqavdf gtkarpfama agnlslsvaf
      121 edghvrslgv vgkdvldapn thvgtellvp lpgrtlalvg gaggscarge dgslrcwdfl
      181 dggaighrhc pvlsapislg kglravsmat sgsrfcaive gesaaprvkc wginqlgalg
      241 vgddldrcks eslgdalpfv dlgtnspvee iavgashtca lfggadagrv kcwgagifge
      301 lgsgeknrsy grssdtmgsh lpfvslpr
//
LOCUS       WP_284721740             269 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA polymerase sigma factor [Polyangium sorediatum].
ACCESSION   WP_284721740
VERSION     WP_284721740.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..269
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=28570
     Region          1..149
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mlqsrsdila tdrmqelmvr glgalsgytp hpdgvrpwlf giaknlrsee krrarrereh
       61 fcpdlgdaer tatpdvspee gafrsearra llsalktlsp eqflvivlvd laestcseaa
      121 elldiplgtv ksrlaaartn mlralgpkeq ylgspgllal fgrrvlgavg eyayplghll
      181 lamlffalpr paphtphava tgaarvigas aadvaraadv sgpltnpepp aaapatttvv
      241 prrgrapepf vvkpsgrrhw lvggngssg
//
LOCUS       WP_284721057             458 aa            linear   BCT 25-DEC-2024
DEFINITION  ParA family protein [Polyangium sorediatum].
ACCESSION   WP_284721057
VERSION     WP_284721057.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..458
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48086
     Region          <94..>189
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          189..433
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 magirescsv cgsdfdvqfr yqmeergggf sfycsqkcle ksqlggegqg dklatcdaca
       61 krfqpelasq vmylggrrty acsmpcrtql qreasgvrlg eiaaevtpqa vapspppqvv
      121 pravatrasg pssattspkr assstspava vpvvpqvank rtapgaqasq atpaapeapk
      181 epaadasvpr ylavfnhkgg tgktttavsi aaglasrgkk vllvdtdaqg nvsvslgatv
      241 erslyhvlvm glrvadatrv vrpnldllgs netlaaaely lagrqnrdrv lcerlsaaaa
      301 gydyvvldcs pslslmnqna lvfadsvlvp vacdylslvg vrqviktvkn vnallhhpvq
      361 iwgvlptlfd srakicreav ttlkqhfgdr clppvraamk vkeapaqgqt ifeyaagtpa
      421 aedygvvvdr iiqsregaak gakdtkdtkp artaaata
//
LOCUS       WP_284721758             535 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Polyangium sorediatum].
ACCESSION   WP_284721758
VERSION     WP_284721758.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 535)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 535)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 535)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..535
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=58836
     Region          8..517
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          289..517
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mrdrpaasrq aesallrgal dvlddaivvv dptgkfvswn rtaarlvgvp vdaspeawte
       61 afgvffpder tpcptesipl wralqgerve dvelyvknpr apqgihvlas arpilgeqgr
      121 vrggvvvfrd vtlakvakaa lghaearmra ivsntpniai egydlqgrvl ywnraaerlf
      181 gwsedevvgk tldgmmldtp stakfvetle eiartgmpng pnewscyrkd gsqvwvysti
      241 fsiptitgac efvcmdvdvt plkhaenrir eqaqrmeaqa tdnanlfhea leaisarddf
      301 lavashelrt pltplklqle rlvrdaraga hqerlapale vayrqvgrla alidrlldvs
      361 ritagkldlc ldeidlcalv hdvvtrfgre iedagcqlsf phdkpilgtw drlrleqvvt
      421 nllgnatkyg rgkpieigle adegtvhltv rdhgvgiape dqgkiferfe ravtnqsfgg
      481 lglglwivrq ivethggavr vesapgkgst fqvelprwrr tldesqgpls isqgt
//
LOCUS       WP_284721765             283 aa            linear   BCT 25-DEC-2024
DEFINITION  Fpg/Nei family DNA glycosylase [Polyangium sorediatum].
ACCESSION   WP_284721765
VERSION     WP_284721765.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Le Bihan,Y.V., Angeles Izquierdo,M., Coste,F., Aller,P., Culard,F.,
            Gehrke,T.H., Essalhi,K., Carell,T. and Castaing,B.
  TITLE     5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA
            glycosylases
  JOURNAL   Nucleic Acids Res 39 (14), 6277-6290 (2011)
   PUBMED   21486746
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Zaika,E.I., Perlow,R.A., Matz,E., Broyde,S., Gilboa,R.,
            Grollman,A.P. and Zharkov,D.O.
  TITLE     Substrate discrimination by formamidopyrimidine-DNA glycosylase: a
            mutational analysis
  JOURNAL   J Biol Chem 279 (6), 4849-4861 (2004)
   PUBMED   14607836
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..283
                     /product="Fpg/Nei family DNA glycosylase"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.-"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003906 - DNA-(apurinic or apyrimidinic
                     site) endonuclease activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008534 - oxidized purine nucleobase
                     lesion DNA N-glycosylase activity [Evidence IEA]"
                     /GO_function="GO:0140078 - class I DNA-(apurinic or
                     apyrimidinic site) endonuclease activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=30682
     Region          2..272
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpegdtlhri asalgprlvg qpvralvlrh qsierlaghl vtkveargkn llvffdegtv
       61 lhthlrmgga whlygeherw rrspasatav lavpalvavc frapvarlvr asllagdaai
      121 grlgpdliap afdeaaalar lrrmagreig dalmdqqvva gignvyksei lfherldpfa
      181 pasafsdeel arllvfarri mvanatakph asgpgahhgh trttregarp gegplavyrr
      241 agepcydcga llemrrqgea rrstyhcprc qpprraaire ara
//
LOCUS       WP_284721776             519 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Polyangium
            sorediatum].
ACCESSION   WP_284721776
VERSION     WP_284721776.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..519
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=55143
     Region          <170..511
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mhqvkrallt wsdagvtgra pshhaprpss drgpvlrlld qdesryevaw vltipegeap
       61 arslcrsiea rigkvelviv pvtdpsdygm lfralgplvg rakaellaan valdvllsag
      121 tpqaqtlwvi lvqagllpar mlqvippafv pvphpkavre vrldiegfpe iralrdelar
      181 lraaaqkgas sllgesapmv elrakiervg asdapvlvlg etgtgkelca reihalsprk
      241 dgpfvaencs vfaegvlsse lfgheagaft gagkrrrgvf eqahggtlfl deigemqprv
      301 qaallrvlqe gtlrrvggeg kvdvdvriva athrelgamv kagafredly yrlrgatllv
      361 pplrarpgdv ellvesflae irgkkggrrl rvtreamral ashvwpgnvr elraevmrwa
      421 vfcddvvnvs dlapeirggg gsgsgsgsgs gsgsdggsgs esgvrplrdv veaaeraalv
      481 aalaaeggnl sraaralgid rntlkrkmra femagadeg
//
LOCUS       WP_284721816             348 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Polyangium sorediatum].
ACCESSION   WP_284721816
VERSION     WP_284721816.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..348
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36699
     Region          46..333
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mrilvllfsl vlliaapasa laapsvavrp vsftvtnple lgalrtvrgs lylpanntqc
       61 rksvmllipg lsygawawdf pfepdtysva ralasqgfpa iaidklgyga sdhpngytlt
      121 vesyaamtsq ivtqlrtgly qtplpslpla fsrvglmghs agteiaelta alfggvdvli
      181 atgythvptp riltdfttgd svraalsdhv yfggtveqrt eymynlaaad pavvaldtam
      241 aeltpsgeil tissqpsrlv mplitapvll vlaeqdilfp psllgvpvge lelalftlss
      301 dkalhvvpga ghsfmlhtna petnavivdw lservpacqa svglpllf
//
LOCUS       WP_284721847             270 aa            linear   BCT 25-DEC-2024
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Polyangium
            sorediatum].
ACCESSION   WP_284721847
VERSION     WP_284721847.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..270
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=28857
     Region          122..224
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mlkhpllafy vlacavtwaf hiplalaavg avgwrlpawv hvlgalgpla aslgmtwatr
       61 gpaglrdlar rattwqggwg wlafallspg acflasgavl slfrgdmtal rgfgyaaelp
      121 qlgwlgtwll wtltfgfcee mgwrgfmlpr lqqgrgayaa tlllgllwaf whvpsffynm
      181 pvnpmvwvaf lisilagsvv mtwlynstgg silipalwhg afdtavagad gmvagavnac
      241 viagaivilr rygpdalspq pkqvvsrgqe
//
LOCUS       WP_284721933             250 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Polyangium sorediatum].
ACCESSION   WP_284721933
VERSION     WP_284721933.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..250
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26245
     Region          3..249
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mllrdkviiv tgatsgigea taleaarqga kvvlagrree kgealaerir geggkalfvr
       61 tdvsvpadie alvartlqaf erldgafnna gipgplgsla dlpldeyrkl mtvnldsvll
      121 cmqhqiramr ksgggaivnc asilgmvgaq tfgaystakh alvgltkaaa ldyaaegirv
      181 navlpgpvet eiwshvnqgd avfaaftsgv pmnryarsee igrpvvflls dwssyvtgts
      241 laidggymir
//
LOCUS       WP_284721985             196 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA polymerase sigma factor [Polyangium sorediatum].
ACCESSION   WP_284721985
VERSION     WP_284721985.1
KEYWORDS    RefSeq.
SOURCE      Polyangium sorediatum
  ORGANISM  Polyangium sorediatum
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
            Polyangiaceae; Polyangium.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Polyangium sorediatum"
                     /db_xref="taxon:889274"
     Protein         1..196
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22187
     Region          16..191
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mrlfpwpwtd pddrhralla raqagdreaf rslyqdlydp vsrfvgrrvr rredaedlvg
       61 rvfhkllehl gdvdlrrgsv rmyvlsmarn avidhararr egtpiddvap iladdrgtpl
      121 dslvqkervr alraavaalp dhvqellalr ygdglehaei aallgestaa vkqrlsraqr
      181 slrevlqege vvdvrf
//
LOCUS       WP_284722063             567 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Methylophaga
            thalassica].
ACCESSION   WP_284722063
VERSION     WP_284722063.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 567)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..567
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=62081
     Region          1..553
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mkyrgqkvhp vgawrlnlvr imfvlmvagl cwrladiqvv npeflrhqgd arhlrqvpvv
       61 ahrgmildrh geplaistpv hsvwlnpqdv latdprlpkl aqllglstqt irekieqnqs
      121 refvylkrri tpelsakvke igiqgvalqr eykryypage vashivgftn vddigqegle
      181 ltydavltgr pglkrmvrds rgnyveggel irpaksgenv qlsidlrlqy ltyqalkkav
      241 tehhaksgta vildthtgev lamanqpsyn pnnraglkps dlrnravtdl fepgstvkpf
      301 tvtsgiksgq fdtttiinth pgyyrvsghp irdfrdygei dlatliqkss nvgaskiala
      361 ldpaklwhdf asfglgeatg ayfpgeamgt mpdpqswrtl diatmgygyg lstsamqlar
      421 aytvladggi lkpvtfiktd kvpqgrrefs adimhevvqm mvkviepggt atraavanyh
      481 vagktgtakk aisggyadkr yqsvfagiip asaprlamvv midepqgeyy ggavaapvfa
      541 evmtgamrll nippddlpmt qmqvahk
//
LOCUS       WP_284722148             128 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Methylophaga thalassica].
ACCESSION   WP_284722148
VERSION     WP_284722148.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..128
                     /product="YybH family protein"
                     /calculated_mol_wt=13927
     Region          2..121
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mtehpiisqi kaadeaiiae dfdtlldiyt ddallvvqpg mnaigkaqir qafekivvyf
       61 qhglqikqaa leiletgdsa lvlantiisa pgaepttrqa tyvfvknsdd iwrcaidnsy
      121 ghailqnk
//
LOCUS       WP_284722188             142 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Methylophaga thalassica].
ACCESSION   WP_284722188
VERSION     WP_284722188.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..142
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=15598
     Region          9..140
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mkvaqtiqhk kpdqddslvp linivflmli ffmvaghisq sdpikvqppl sssetkqieq
       61 plvivvsdng qvaieqdivd dnallpvink qfeaaadkdk frilvkvdgs lpverlqyvl
      121 siikqsgikr vslatqkqae vs
//
LOCUS       WP_284722191             433 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Methylophaga thalassica].
ACCESSION   WP_284722191
VERSION     WP_284722191.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 433)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 433)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 433)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..433
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=49492
     Region          <196..408
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mklklslklw ialsflilgi tivtgysmls ihfffrgmds iisanmenaa edylsgikeg
       61 kanpgnvdny tvtqtweaqt eqiktyfrep krfgvlhkqr kqaepgkrpy lmyfliklkv
      121 egqtyfvsra ftradasplv gqnarqsrql iislsmgitl llalvtwllm krlsqpvskl
      181 tkwthelrpe tlkqsppdfa ypelnemael ikgslssvne smereqkflr ftshelrtpi
      241 svirnnvelm hkiqqkqssa lpdkqqeife rierasltmq nlcetllwln rdetdslvkq
      301 hfrldelidn lvdelryllk skpvtiqvet qacelhessv aariiignli rnafqhtwng
      361 hvsiqqhgaq isirnhstqa dkgnssedqg fglglqlteq lcrklqwqyq nqvnsdghta
      421 tlsiipahsa eqe
//
LOCUS       WP_284722268             450 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Methylophaga
            thalassica].
ACCESSION   WP_284722268
VERSION     WP_284722268.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..450
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=49293
     Region          6..447
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mnrqalvidd epdilelltm tlsgmsidcv taesvaqanq alkqqsfdlc ftdmrlpdgn
       61 gldivrtiqk typncpvavi tahgnidlav ealksgafdf vskplklkvl rdlvnsalnl
      121 splksdvker rsrdkllgdt dvirslrnki sklarsqapv yitgesgtgk elvarlihel
      181 gsrsdeafvp incgaipael veseffghkk gaftgavadk qglfqaangg tlfldevadl
      241 plmmqvkllr aiqekairpv ggneeisvdv rilsathknl aecvkqgsfr edlfyrlnvi
      301 elsvpplrqr kadipllveh ilvqlaaksg elkpvigeda isalreyafp gnvrelenil
      361 eramtwsdgs viheadlmlp eaplnslsad esgfsltadk vdlesqledq erqlivdale
      421 strwnktaaa kklgisfrsl ryklkklald
//
LOCUS       WP_284722365             317 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase [Methylophaga thalassica].
ACCESSION   WP_284722365
VERSION     WP_284722365.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..317
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=35970
     Region          11..312
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mrkyqtenls lhntdclkll ktlddnsidl iatdppyfrv vaeswdrqwk neadffawld
       61 tvleqmarvl kptgslyffa gphmankvei avakhfnmln qiiwrkpsgr hngcskeslr
      121 ryfpqtehim faesmkpvpf gfepirgylh qaiidagvtq kqvdnacgck msghwfgksq
      181 wsmipenhyq tvenligktl kpyadlyaey rslldesnaa rrtfnvnkhv pytnvwdfka
      241 vpfypgkhpc ekpldlmehi itasslpgdv vldafvgggs tpaaciktgr rfigselges
      301 efdmavkrlt emnqqaa
//
LOCUS       WP_284722384             421 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Methylophaga thalassica].
ACCESSION   WP_284722384
VERSION     WP_284722384.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..421
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=48341
     Region          137..403
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mtppihanrq nslrispfhr lcmhllckql arfeegflvi emadlrlefg dptaelkshi
       61 fvihphffea avlggsvgva esymdaewqt ddltrlirlf vrnrhlvdgm eqgiarlagl
      121 lmqgvhwlrk ntragsrkni aahydlgndl felfldrehm myssalyyds aesleqaqsn
      181 klarlcdkld lqpddhllei gtgwggcavy aalhygcrvt tttisqqqyd yairrvreyn
      241 lqdkvtvlle dyrdlegqyd klisiemvea vghhfideff qrcsdllkad giaviqaitl
      301 edhryqqavk svdfikrfif pgsfipcvsv lvnsaakaem klsnledigt syaktlqiwr
      361 erffdklddv kvmgyddrfi rmwefylcyc eggfiersis dvhlvfskpg nrqpswipgr
      421 g
//
LOCUS       WP_284722439             601 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Methylophaga thalassica].
ACCESSION   WP_284722439
VERSION     WP_284722439.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..601
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67692
     Region          6..601
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 msldttdyis iasaqtlygl frerhrktpn stayshfcad tqqwqtttws daaqqiaiwq
       61 halkseglrs gdrvalnlkn cqewvffdqa alslglitvp lypddrpdsl afilqdadvr
      121 clflqnqhqw qrlkpslsde hqlkrviikt tgentldapa vymnewlrtd tnpalidwqa
      181 dphqlatiiy tsgttgkpkg vmlshynils vasaslecfq vrsddlflsf lplshtlert
      241 agyylpmmtg arvafsrgip qlandiqelk psvliavpri feriyqriqs slssqpwykr
      301 lllkltshig wtsflhaqrr hrwspcflfm pvlekivakn iqalfggqlr iavtggaaip
      361 hhvaeffigm ginllqgygl tetspvisvn rtsenepfsv gqpipsvevk igdnsellvk
      421 spgnmlgywn nhkatantid aegwlhtgdq ariaesghif itgrikdilv lsngekvspv
      481 dmemaitrde lfeqalvvge gkpflsalvv lnaeqwlqla qrlkldamnk nsltdkslqq
      541 hiiqrfrgll hdfpayakir rvhltlspwt iengmltptl kikraklvea nqqlidefyq
      601 n
//
LOCUS       WP_284722506             369 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Methylophaga
            thalassica].
ACCESSION   WP_284722506
VERSION     WP_284722506.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..369
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=42104
     Region          1..367
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mrkfwiefhr isglilfipl flqsisgtii vfdhaidewl npqlvlddgi sappapiaev
       61 myaalhalpd vahinslrtp rndkamytaf vemnsqsplh gktievminp ytadvvsvra
      121 wgsyftsmiy lfhftfllgd kmelvlglla mlmlvnvivg vyygwprskk awnwllartq
      181 kssstiarlr rthialglis lpvfiiliit gislifpdqt kwllnrpaka spdvdwlsnh
      241 piqpdnwlis akqywpekqw qriippssqs psveirlnad ndprktsgsf vlwlnpqtne
      301 ilaeqsydtm slrqktafwl fplhsgeafd ltgriivfit giftavlsva ggclwyrrkf
      361 krqhqkrfi
//
LOCUS       WP_284722517             736 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Methylophaga thalassica].
ACCESSION   WP_284722517
VERSION     WP_284722517.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 736)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..736
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=80346
     Region          68..735
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mrmkstcvmm alimggmqvs ladeetsnts tleldtlsvt asadasaegl spafaggqva
       61 eggragilgt kdnldtpfsi tsytnefiqd rqaqsvgdvl rndptvrvar gfgnfqesyf
      121 irgfilnsdd vaynglysll prqyiatelf ervevlrgas afltganpng ggiggainll
      181 pkrapnydln ritlgasind erngsadiar rfgendefgi rvnaahhngg tsiddeqael
      241 nlfnigldyq gdrlrlsadm gyqnhqleqt rtnlrlmnqv ssvpstpnas enwaqpwsys
      301 nekdyfgtfr geydftenvt awaaygmrhg eeenslsnln itngitgngt lsrfdngrid
      361 riqtgevgik gkfktgfikh elvaaysyfv sekknayrfv sipggsnlyn ptyysrpela
      421 dlysprlgsr vrlnsfalgd tlsfmddrlm ltlgarhqtl ktedydyngq tgligkydds
      481 eitpaigavy kltdefsiyt nyiesltkgd tadsttdngs ggtvdvvngg esfapyvseq
      541 keiglkyets sigaglayft tskprsfmdk snpdrpvfrq sgedehqgie ltlygkatdd
      601 lkllggvtwl dakqkdtgns sidgnrvigv aklqatvgae wdvpsvdgla fdgrvnytgs
      661 ryaddantlk vddwttvdig akylvqlanq dltlrarvdn lfdrdywasv ggypgngylv
      721 lgaprtvsis atvdfy
//
LOCUS       WP_284722744             201 aa            linear   BCT 25-DEC-2024
DEFINITION  HD domain-containing protein [Methylophaga thalassica].
ACCESSION   WP_284722744
VERSION     WP_284722744.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..201
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22669
     Region          7..150
                     /region_name="YfbR"
                     /note="5'-deoxynucleotidase YfbR and related HD
                     superfamily hydrolases [Nucleotide transport and
                     metabolism, General function prediction only]; COG1896"
                     /db_xref="CDD:441500"
ORIGIN      
        1 mtdtqqmtdf lmeldalkhi nrrsyitgge rlensaehsw hlamacwsla ahfqldidma
       61 kllqyalvhd lgevdagdtf lysaqrdtan qaerqcverf akhqgngiqd lltvwdeqef
      121 gdsteaklmk avdrllpfll niaaegktwk lhqikasqvh tahafiaatf pelhqwisek
      181 iafateqgwl laddksevas k
//
LOCUS       WP_284722935             361 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Methylophaga thalassica].
ACCESSION   WP_284722935
VERSION     WP_284722935.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..361
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40951
     Region          1..342
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mhrqtfvfld girgiaallv vmthapdffm iwknhtylav dvffilsgfv ialayenklv
       61 skelsffdfv kkrfvrlypi yfvslciafi liivggylsg knlllwagys aaltaffipr
      121 hggammftln tpywslfyef lvnflyaaia pflstrilil ivlsaglsla yisvvnghln
      181 agwgntethy aaglsrsifg ilmgvliyrf rnkliekisf ispwfavlvi vvvllfpsip
      241 kynyiydifi vtiifpltvl iasqlkeskl dpvllmlgaa syplyvlhyp firftetvsn
      301 aygyeyivsd yapytgifll sflvilalfm akfvemplrl wlssyleqkk mkrksatssa
      361 s
//
LOCUS       WP_284723171             418 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Methylophaga thalassica].
ACCESSION   WP_284723171
VERSION     WP_284723171.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..418
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=47608
     Region          3..406
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 makltatqvq syartatank kysdgnglyf cvrksgmpyw mlrytslngr reatlgqyps
       61 mtlaearles skmqlqlqqg edplairaie tipeiqnvsq lfqdwyakdl srrlkhpnip
      121 krvftkeiap vigqlpiqav rpthvrevle riresnrpti andtlmymkq lfrhaikldl
      181 tlnnpaaaft vddaggvess kdrmlskeei hyafsvfhth insfgrdnyl acclflvlgv
      241 rkselceamw remdlttgvw dlpkersktg vpisiplprq aivwfnelqi racgspyvfp
      301 arrashrphm gpdtlnrais klfgrepgrk kqppnkmgkl ehftvhdlrr tfrslaaslg
      361 iagnvaercl nhklkgvegi ydrhdyfeer riahqtvadv veplvnfepa sqhntrgr
//
LOCUS       WP_284723357             385 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Methylophaga thalassica].
ACCESSION   WP_284723357
VERSION     WP_284723357.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 385)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..385
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=43093
     Region          48..344
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mknpespvvh rsedkqyiid tqrlmssdis yqdlvneasy hqradwaahm tpslapysql
       61 gmqlalhhhg nllspelypk lkhaeseikt tlahefgfsh arfthggsys nldalwrars
      121 qsvnkkvvyg seashysirk acdilgitfe aipcntaqqi dlvalekkca qdapiaiian
      181 mgtsatgaid pieeitaist khncwlhida awggsnllid ennlfkqfmp kvdslsfdpn
      241 kslfqprpcs vlfshskpeh thdinylses pekaisgsyg aelfiplwln wkilgkdwfi
      301 dkinyrleqa eyfasqlqkq tkwpiinhgt givcfkadhd allaplvekg tvstinlnqt
      361 cyhrvifagl dtsaekllka lhpfl
//
LOCUS       WP_284723368             377 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Methylophaga
            thalassica].
ACCESSION   WP_284723368
VERSION     WP_284723368.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..377
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=42809
     Region          3..373
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mtkarqlwlk ihtylglsis imlvllgltg silvfylqfd iwlnpdieav stapisqqqa
       61 vfdqlqqqfp trtdswrieq plhpgwpima ryytpvetrd lqfaplmvti dpatleitsk
      121 rfwgefamtw iynlhysvll dktgktlvgi iglislisll sgvilwwpgw hklrqvmawr
      181 lrtsyakkvf dlhilsgsyg fivlfmlslt gaalalptqt qqiirifspl asspilarsl
      241 hqqgkqpvis adtavasafk lfpnaelrwv espgikknsw rvvfyqqgep srrfprtqvw
      301 vnaftgdiva srdgladsag dkvlnwlhpl hngeafgltg riivficgfl plilfitgll
      361 rwqqkrhark rtayrhs
//
LOCUS       WP_284723467             544 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Methylophaga
            thalassica].
ACCESSION   WP_284723467
VERSION     WP_284723467.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..544
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=60277
     Region          5..389
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mkvkadiirt ykslhtwvgi isgmalfiaf yagaltifke pishwatppl qhsesislsa
       61 vpsvlgrvik shpeaaqriq lnlnpethht qqimwtvege kggdhdvssl ryfsaqldeh
      121 qdlvttevyp atvaqfidtl hrvvglpvds dpnrwimgif aifytlalvs gliillpilv
      181 kelfafrlgr kpkrvwldah nvvgvtslpf hlimaitafg fayhdliydv qdklihegql
      241 rqalfssapk pnpeqstdpa tmlspeella tareiapsfv pyqleysgit tprasvmiwg
      301 ndadaiapra pggfiainpy sgevqstdyl pgqqpgemia vssffalhfa tfggspirwa
      361 yfilglagaw lfytgnllwv enrrrhskpd grlfnqrkdv kvmasltvgi clgsvcgisl
      421 mlasskwlal eaqatylhfq wvyyltffat iawsfirgaa rslvellyaa atltvaipvt
      481 sllsiiipat glwmhtdlnt lmvdivafim avgfgllgra tykrvyhsqi idsvwsyrpa
      541 prsl
//
LOCUS       WP_284723530             208 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Methylophaga thalassica].
ACCESSION   WP_284723530
VERSION     WP_284723530.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..208
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=23844
     Region          <13..206
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mavissemrl yspegerlyl saeerqrfld sareedredr lfchvlhytg arpsevlelt
       61 pdrisisekt ltfktlkkrk tdtngksklp qfrtipvpde lidnldlvfd irrierqgkn
      121 shlpiwtmhr atawrmvkrv mkragingkq atskglrhgf giamlsgekp lplnilrdlm
      181 ghtsttttei ylqavgaekr klvmqawn
//
LOCUS       WP_284723564             721 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Methylophaga thalassica].
ACCESSION   WP_284723564
VERSION     WP_284723564.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 721)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20158983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..721
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=81023
     Region          119..>389
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          281..720
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 maislikrls sgtapyfsla flllvlayll saatqdssrl ndlflvifgi gvacllllvg
       61 ilarslfrly rdfkkheags rltvrlvslf vllilvatsi vygfsihflh rginswfdvk
      121 veqalndsle lsrtafgirm rtllrqtrmm agvlselpds elshslrdlt qlsgalelsi
      181 wardgqpias siesptimvp nrpndtimhq llqgedyigm dpsendklql raavripqks
      241 vlaeerilnv lfpindhlsd lgktvqdays dykelsylrk plitvftltl slivfltilv
      301 siwfaiwisr riveplqela qgtqavasgn ynmqltasgh deigflvrsf nqmtqrltha
      361 rnasqrshrl leqqtsyltt vlgslssgvv tvdkrlylht annasskilg vklqqrlesp
      421 lsklaeinkn mktfcemier cavkgiaweq qvelqkqngn qtlichgtel pnnsgwvivf
      481 edittllqaq rnaawgevar rlaheiknpl tpiqlsaerl qrkyaaivpe eqvevvdklt
      541 ntiiqqveam kemvnefsey artpalqlqs ydigqlirev lamyqsnpnh qftllnspes
      601 vavkidvnrf rqvmhnllkn aieacedaql pvdivisyhp lthqqrrwle isvrdygpgi
      661 pfsiidklfe pyattkhkgt glglaivkkm ieehggdvwa enldpegtsi iirlpleesp
      721 s
//
LOCUS       WP_284723574             333 aa            linear   BCT 25-DEC-2024
DEFINITION  FecR family protein [Methylophaga thalassica].
ACCESSION   WP_284723574
VERSION     WP_284723574.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20752687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..333
                     /product="FecR family protein"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0016989 - sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37288
     Region          18..61
                     /region_name="DUF4880"
                     /note="Domain of unknown function (DUF4880); pfam16220"
                     /db_xref="CDD:435227"
     Region          98..325
                     /region_name="FecR"
                     /note="Periplasmic ferric-dicitrate binding protein FecR,
                     regulates iron transport [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG3712"
                     /db_xref="CDD:442926"
ORIGIN      
        1 mvtssspevt dsesivtqaa ewvvlmsdee nppstaqkqa fldwrnqdpq hdeavdklqt
       61 llgdiqqfpr saskaalsvs tskayhqhsw qtlaktfvll mvifipmfvw lpdkvtlmma
      121 dkqtsvgdwq sytladnsvi mlssdsainv dfnhsqrtih llkgeirvkv sknrqrpfvv
      181 ktehgsltal gtefsvdkrs dytllkvies tvaatcqrqg cdvkplqpgq qirvyaehlg
      241 kvsdfsvadv slmwnkhqlm vdgmplnevl tilnrfhkgy fyfdaqqlen yhvsavlpld
      301 npqsalalla dsfplkvthi spwwtaitvv pkt
//
LOCUS       WP_284723587             226 aa            linear   BCT 25-DEC-2024
DEFINITION  OmpW/AlkL family protein [Methylophaga thalassica].
ACCESSION   WP_284723587
VERSION     WP_284723587.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006882
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..226
                     /product="OmpW/AlkL family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24299
     Region          20..226
                     /region_name="OmpW"
                     /note="Outer membrane protein OmpW [Cell
                     wall/membrane/envelope biogenesis]; COG3047"
                     /db_xref="CDD:442281"
ORIGIN      
        1 mktttlaaal lttlglstla apamayeagd wlvrgriinv npnddsgtly vggadsgqkg
       61 vsvnsdtvpe lditymmskn wgvelilgys qhtvksegyw aaqglgdvid tkvlpptltl
      121 qyhfmpdski rpyvgaginy tyffdeevkg pvldvpgakv kldsswglaa qagvdvalne
      181 dwfvnfdvky ididttahfk gtpvgtakid adidpfvwgi gigrrf
//
LOCUS       WP_284723653             580 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Methylophaga thalassica].
ACCESSION   WP_284723653
VERSION     WP_284723653.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..580
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=64943
     Region          34..580
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mtsevstldd laqltsyslm dslncdpdat sngddhyprq vfsghyvpvk ptpienpvyv
       61 shsktffhel gfadsmanse dfvrlfsgdl thvpepirkv gwasgyalsi ygteytqlcp
      121 fqtgngygdg raisvleavi kgqrwemqlk gggrtpycrg adgravlrss ireflaqehm
      181 halgvptsrs fslyastter vrrpwysegs taaepdiiit epvaistrva psfirvgqle
      241 lfarrvvnha henamdelek ivlhvidrey advidnslni etkvillaka frerltslia
      301 nwirvgycqg nfnsdncavg gftldygpfg fceafdpvyq pwigggrhfs ffnqpaaaar
      361 nfamfckale pllkgdqhyl seledvqhgf anvmqmqlek mwaaklgled ynealfseli
      421 slmtltpvdy tiffrelsal pgdigplkks fygelnpaen ginstspnsq dieqhwsawl
      481 dkwqtlvgis dqndgnatss reaissqmkq vnpkyilrew qlvaaykqaa egeytllrel
      541 qevmkkpyae qskdiekkyy rlmptelsdi ggvshyscss
//
LOCUS       WP_284723675             184 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Methylophaga thalassica].
ACCESSION   WP_284723675
VERSION     WP_284723675.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469162
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..184
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=20190
     Region          <23..82
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          85..>175
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          85..111
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(87..88,91..92,94,118,121..122,125..126,128..129,156,
                     159..160,163..164,167)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          116..146
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          155..183
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtnyvsrffv tglmlsvlaa cttspyqpsq ppvddrsnlp pqqptpetha yppveeaipg
       61 qpipshqapp pqaqlpqkqn pavialldra eqarvsgdlr saqnnlqraq riaprdpkvy
      121 yslaqthmsl edydlaeqva lkgvslssgn qvllkrfwql iteirlragd vsgaevaklr
      181 aqky
//
LOCUS       WP_284723802             478 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Laceyella
            tengchongensis].
ACCESSION   WP_284723802
VERSION     WP_284723802.1
KEYWORDS    RefSeq.
SOURCE      Laceyella tengchongensis
  ORGANISM  Laceyella tengchongensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Laceyella.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Laceyella tengchongensis"
                     /db_xref="taxon:574699"
     Protein         1..478
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53886
     Region          6..463
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mtrvdrihll htndlhshld qtskmaplie elraqwqarn ersllldigd hmdrvrmete
       61 gtdgrvngti lermgydfvt lgnnelltfs qdqlaavyrd apyqvlssnv yevkrtgqpa
      121 wirpcshvtl gsvrigmlaa tipyqtvyel mgwdvrdpvs tlaehvrrlr gevdlivvls
      181 hlglmndrml akevpgidli igahthhlle elervgetwl agagkhgqhl ghieievdid
      241 agrvrtirgr vyplagraee remqeliahy rgealenmaq pihqlsrple vdwygesslp
      301 nlladalcdw vgaeaalvnn gqllaeipag svtrqqlhav cphpinpvlm tiegkeirrt
      361 leealldefv tlpirgfgfr gevlgtvsvs gmevfydpea ppfqrikeir ingsrleeeq
      421 lvrlatidmf tfgigymglk egkvqkyylp eflrdllakq lqapaalarc evkrwhri
//
LOCUS       WP_284723832             402 aa            linear   BCT 25-DEC-2024
DEFINITION  thiolase family protein [Laceyella tengchongensis].
ACCESSION   WP_284723832
VERSION     WP_284723832.1
KEYWORDS    RefSeq.
SOURCE      Laceyella tengchongensis
  ORGANISM  Laceyella tengchongensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Laceyella.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 402)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Laceyella tengchongensis"
                     /db_xref="taxon:574699"
     Protein         1..402
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=42698
     Region          4..402
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mrrrevvivd avrtpigryr gglsrvrpdd laahviralv ernsqldeve iedvvfgcan
       61 qagednrnva rmalllagls eeiggvtvnr lcgsgleain qaaaaiqigs gdvmiaggve
      121 smtraplvml kpeqgwargd qalvdttlgw rfinprlavr yepismgeta envaekcgit
      181 reeqdafayq sqqraeqarv rgafqaelvp vpvaeekget vwvsadehpr pqttlaklsq
      241 lppvfrpngt vtagnsagin dgasalllme retairlgcr plarvvafav agtnpltmgl
      301 gpvpavrkvl aregltvddl dlielneafa aqalacmqal aldpdkvnvn ggaialghpl
      361 gasgarimtt lvhelvrreg ryglatmcig vgqgiatvie ri
//
LOCUS       WP_284723845             587 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Laceyella tengchongensis].
ACCESSION   WP_284723845
VERSION     WP_284723845.1
KEYWORDS    RefSeq.
SOURCE      Laceyella tengchongensis
  ORGANISM  Laceyella tengchongensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Laceyella.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Laceyella tengchongensis"
                     /db_xref="taxon:574699"
     Protein         1..587
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=68328
     Region          332..576
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mklekrlmvk flagvfflaf flatsfvtfy yfasllkeeq rsdlfpeeil qrmvaatdie
       61 qgkpvlppsw ekklkkrnew vqilnkdgve vfhyntpdsi pkhytpnqla hyirnsesig
      121 ydihtwyqsi dnhtytwilg rknknelllk ikkhtirhnq titiphplle evkkrkgwvq
      181 iidkngaeiy qyrrpknipt kytpgeyvha krsgsdlhft sgrlsgqevt wimkedilpv
      241 hemeqnkiia llffaslvli plafwlfsyr fgqklgspll flmdwlenls hgiykeptrk
      301 sgpikdpqtg hlkkpyvlyq evfkvveqls frlqevqter erldhtreew iagvshdlkt
      361 plstikgyae lykspsyqws eqemeeyldl virkaediqh liddlnltfr iknnalplel
      421 tyldmkeflr llvadvlnti ateevnihle lphdttvmyp idpqwfkral mnlitnaifh
      481 ndpntpitvr lqettsptpn ttsalkieli dqgcgmdeqt vsrlfqryyq gtrtkrsnrg
      541 tglgmaiakq lielhggkie issqvnrgth vtitlppkrk etpeivt
//
LOCUS       WP_284723914             146 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Laceyella tengchongensis].
ACCESSION   WP_284723914
VERSION     WP_284723914.1
KEYWORDS    RefSeq.
SOURCE      Laceyella tengchongensis
  ORGANISM  Laceyella tengchongensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Laceyella.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Laceyella tengchongensis"
                     /db_xref="taxon:574699"
     Protein         1..146
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16941
     Region          1..139
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 manyanvset kirvryqetd qmgvvyhany ltwfevgrte wirsygisyq qmeqkglllp
       61 vvdihckymh paryddeviv rtsiadlsgg kiafkydvvh aetetvlckg ssvhlwvnke
      121 mkrvnlkqay pelyrtleqi fsverg
//
LOCUS       WP_284723902             258 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Laceyella
            tengchongensis].
ACCESSION   WP_284723902
VERSION     WP_284723902.1
KEYWORDS    RefSeq.
SOURCE      Laceyella tengchongensis
  ORGANISM  Laceyella tengchongensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Laceyella.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Laceyella tengchongensis"
                     /db_xref="taxon:574699"
     Protein         1..258
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27890
     Region          1..250
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mgialitgas egigkelatl faaaghdvvl vardqaklha vaqslkknhg iqahvivqdl
       61 gqphaaetvy rtcqtngwti dylvnnagfg llgpftttnl sveadmitvn vtaltqltkl
      121 fvphmvasrs grilqvasla sfmpgplmsv yyatkayvls fsealqqelr gtgvtvtalc
      181 pgptntkfkh rakmnnpphv dksaldvrrv aqagfngmmk gqtvvipgla yrffvfacrf
      241 lprswvariv hfnqkqrl
//
LOCUS       WP_284723927             216 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Laceyella tengchongensis].
ACCESSION   WP_284723927
VERSION     WP_284723927.1
KEYWORDS    RefSeq.
SOURCE      Laceyella tengchongensis
  ORGANISM  Laceyella tengchongensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Laceyella.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Laceyella tengchongensis"
                     /db_xref="taxon:574699"
     Protein         1..216
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=24799
     Region          2..>201
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          24..54
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          59..84
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(101..102,104,129,132..133,136..137,139..140,163,
                     166..167,170..171,174)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          127..157
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          162..190
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mvaennveea iewvkqarel epdfpiyqie hanylchltr yedaislyqs akkmgvpnpe
       61 lliglanaqy mmgdltssle tltelrmkfp eriegfvdsa miyldhlgep ekakhlllqg
      121 esyqskhply lfqlgrayhe lgetelakch iqkaitidme ckeawielat lyfeeeding
      181 altaisqaik ldpnnpiain nrhifeeyiq erdchd
//
LOCUS       WP_284723932             145 aa            linear   BCT 25-DEC-2024
DEFINITION  dTMP kinase [Laceyella tengchongensis].
ACCESSION   WP_284723932
VERSION     WP_284723932.1
KEYWORDS    RefSeq.
SOURCE      Laceyella tengchongensis
  ORGANISM  Laceyella tengchongensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Laceyella.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Cui,Q., Shin,W.S., Luo,Y., Tian,J., Cui,H. and Yin,D.
  TITLE     Thymidylate kinase: an old topic brings new perspectives
  JOURNAL   Curr Med Chem 20 (10), 1286-1305 (2013)
   PUBMED   23394555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Laceyella tengchongensis"
                     /db_xref="taxon:574699"
     Protein         1..145
                     /product="dTMP kinase"
                     /EC_number="2.7.4.9"
                     /GO_function="GO:0004798 - thymidylate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006233 - dTDP biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=16460
     Region          3..>137
                     /region_name="Tmk"
                     /note="Thymidylate kinase [Nucleotide transport and
                     metabolism]; COG0125"
                     /db_xref="CDD:439895"
ORIGIN      
        1 mkkgrlivle gmsgvgkttl arnwvktltd revpviylhg alsdtpvgrr fkeevrswkl
       61 eltstyyyla dlvqltqsqi qpmlkrgyvv iqdryvdsii sfhraltkmn giiedikpvv
      121 dlytevglla rpeatiwcya snkvi
//
LOCUS       WP_284723732             701 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Methylophaga thalassica].
ACCESSION   WP_284723732
VERSION     WP_284723732.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thalassica
  ORGANISM  Methylophaga thalassica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 701)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 701)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Methylophaga thalassica"
                     /db_xref="taxon:40223"
     Protein         1..701
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=79211
     Region          123..692
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mrdtthsntv iitrnrilag svlsavitvs afflipylfp tvshikwiaa tissvcylfl
       61 ilflsrhlir siqssfddig qltlsvplva skkfieareq cesvnennsd haivnlkqel
      121 cnlatmleal edkvsqrnka vfrahqalkn erdfitqlvd taqmivmtsd dkqvihlfnh
      181 ygeqltgfsr eevegsdvar ffppghwset nnilkellig niqiaqqeae lvdkagslkq
      241 iswfhsrver nneetmilsv gldntqtraa ekrivwmaeh dpltdlcnrr kfteefeksl
      301 qtairyqhns tlllldldrf kdindtsghr agdealklva kalnritrft dfvarlsgde
      361 favimpesde agaitlseki laelstihln yasvrhtisa sigivnyplq dattnelmgf
      421 adlamyraka ngkgryhifs lddqsreqlq krvywkqkie ealenhlfvl yfqpilnlsn
      481 neiqhyevlv rmrnpetqei tlpgkfieia eevgliqsid hyvlhhsikk lgelqkqgsk
      541 vefainlsga vvdtpvllpy lkklikrfdv dpsalifevt etvavanlyq aklmmtaika
      601 lgcrfslddf gvgfasfnym relpidiiki dgifiknldi naddqlfvka lidvakglgr
      661 ktiaefvene ailtilqnyg vdfaqgfyig kpqqdllsgt h
//
LOCUS       WP_284724101             609 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Laceyella
            tengchongensis].
ACCESSION   WP_284724101
VERSION     WP_284724101.1
KEYWORDS    RefSeq.
SOURCE      Laceyella tengchongensis
  ORGANISM  Laceyella tengchongensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Laceyella.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 609)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 609)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Laceyella tengchongensis"
                     /db_xref="taxon:574699"
     Protein         1..609
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=68129
     Region          3..593
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mrkwrtwlis fvmiaafgli vwrlyyiqie atrsftmrnq qvdlirlaee rqreemllns
       61 grgaildrhg erlaggddyh llvfpqtrhl mkakrqqfaq lasfihmplt qlesqlaqir
      121 fpgllsgpag eeivlsqadk eqihrlqlpg vmvvrsdyrm sinhpaqqvl grlvqnpglm
      181 kswypeqvas gkwtpdshlg vtgieaafep flhgnqeerl ayttmgsglp liggemkrtt
      241 sragndehpy tvvttldkel qlrveqilrq envqdgavvv qdvasgdvla masrpavrkg
      301 vhenqpwdnr alletvpgsi fktvvavaal eqgivkpdtv fhcdgeleqa qltddkhggh
      361 grqtfaeaya dscnvvmgmv aqklgaerle ayakrlglaq evlwsgkvfh dehftqlpqe
      421 qkgmvfaktt pkndpgvmaq tgigqrdvrv tplqavnmvt alfhqgkplk prvvkeirde
      481 tgrvvyqfkp qvlpgakplr petiqamkqm mrlvvvkgta rsvagttwsl aaktgtaqig
      541 ldkkrynkwm igfgpferpr vaisvvlrdi sdsedprakr vfravmeeia kqkptdekeh
      601 vakkqsaqk
//
LOCUS       WP_284724270             336 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Laceyella
            tengchongensis].
ACCESSION   WP_284724270
VERSION     WP_284724270.1
KEYWORDS    RefSeq.
SOURCE      Laceyella tengchongensis
  ORGANISM  Laceyella tengchongensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Laceyella.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 336)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Laceyella tengchongensis"
                     /db_xref="taxon:574699"
     Protein         1..336
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38155
     Region          1..315
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mpkakrllel mmtvnrkrkf tvkelaeefg vstrtilrdl relselgvpl ysevgphggy
       61 hvlnerslpp isfteeeafa iffsvyalrh ylsipfeaei ssalnkfasy mtsdirerie
      121 qmknrvdfit parrgesphl srllegavhq qvllieyeak egkvsrhiqp igiyardgiw
      181 ycpaycflrg gyrvfrcdri kavaqassdv kprdlrhvhl gnvqpitqae pemahvrvel
      241 neegvrkcea ewwlanhlhh qedgggwvdg hfpkrdlpfl akffmglged atvrqplelv
      301 hgmkeilsrl mdkyavvpag egsktsegas depsdl
//
LOCUS       WP_284724367             141 aa            linear   BCT 25-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Laceyella tengchongensis].
ACCESSION   WP_284724367
VERSION     WP_284724367.1
KEYWORDS    RefSeq.
SOURCE      Laceyella tengchongensis
  ORGANISM  Laceyella tengchongensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Laceyella.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Schwartz,C.J., Giel,J.L., Patschkowski,T., Luther,C., Ruzicka,F.J.,
            Beinert,H. and Kiley,P.J.
  TITLE     IscR, an Fe-S cluster-containing transcription factor, represses
            expression of Escherichia coli genes encoding Fe-S cluster assembly
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 98 (26), 14895-14900 (2001)
   PUBMED   11742080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Laceyella tengchongensis"
                     /db_xref="taxon:574699"
     Protein         1..141
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=15553
     Region          1..141
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mnsefhiavh slvflaylps rmassellas nictnpvrir kvmnllkaag lvdvqkgtgg
       61 gyilrgnprq itlgsiyrlt sagslvsdwr sgdptmdciv asqigqvmsh ifegaeeqfe
      121 rhldqytiqd llnqmqmnkr n
//
LOCUS       WP_284724467             575 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Laceyella tengchongensis].
ACCESSION   WP_284724467
VERSION     WP_284724467.1
KEYWORDS    RefSeq.
SOURCE      Laceyella tengchongensis
  ORGANISM  Laceyella tengchongensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Laceyella.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Laceyella tengchongensis"
                     /db_xref="taxon:574699"
     Protein         1..575
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=63564
     Region          28..363
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mifvrmlags ifaivfvmgs vssggserar eqagqreplp aqepdafrls fldqikapea
       61 wqafmrrsgs lgtdpfvvav vdtgvdlqhp llrsylvpgv nlrfpdepph drmghgtkva
      121 gviasvwgag qwrtpmgkgr impvkvmedg sdgqmsrtia gireaisrka riivlaqgsw
      181 rhhpalaeav aeaeqqgvli vaavgnakyd eqgrlafdhp lyfpaayptv lavgaatqdg
      241 rhdptsnwgp gidlvapgen irltpeenpl mqngtsfaap qvaavaalvw qlhpeytpad
      301 vrrhlmqtar rtpssawrwd eqmgygqvda aqairgtlhp dpyepndrkd eakpiasgle
      361 vygvsrrgdp difeqpihek gwlelqvsvl gpaselllea ydergrtlsr rrisrqgdvr
      421 fpvgaghvqi gvegldkrea hyrltsqarl gpdamepndd adqaavisvr pgiqiiegtm
      481 drhndrdwle lriaepgrlt levrpftprf dpvlqhpfag rmdvqedqgd egeheeirvr
      541 vrpgryrici sdydgniadr pyhvvmrytp qnkkg
//
LOCUS       WP_284724508             356 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Laceyella tengchongensis].
ACCESSION   WP_284724508
VERSION     WP_284724508.1
KEYWORDS    RefSeq.
SOURCE      Laceyella tengchongensis
  ORGANISM  Laceyella tengchongensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Laceyella.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Laceyella tengchongensis"
                     /db_xref="taxon:574699"
     Protein         1..356
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39246
     Region          8..355
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mlekhllklr qklqergiea llishpvnrr yltgftgsag vvlitateql lltdfryviq
       61 aqeqaphmtl vqhqgvyhtv geqcrklgik vlsfeqdhlt faeflqlkea vgdiklqpts
      121 givnelrmvk dadelavmre aariadqafs kilsdikpgv reneisfkle fymrelgats
      181 ssfdmivasg krsalphgva sdkvlelgdl vtldfgafyq gyasditrtv mlgrpsekqk
      241 eiydivleac nrtiaalrpg mtgkeadava rdyisahgyg dffghstghg lgmevhelpm
      301 lssrgdvvlq pnmvvtvepg iylpevggvr ieddvvitet gcealnqssk dwivie
//
LOCUS       WP_284724518             679 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Laceyella
            tengchongensis].
ACCESSION   WP_284724518
VERSION     WP_284724518.1
KEYWORDS    RefSeq.
SOURCE      Laceyella tengchongensis
  ORGANISM  Laceyella tengchongensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Laceyella.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 679)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Laceyella tengchongensis"
                     /db_xref="taxon:574699"
     Protein         1..679
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=74704
     Region          <115..>230
                     /region_name="PRK11086"
                     /note="sensory histidine kinase DcuS; Provisional"
                     /db_xref="CDD:236839"
     Region          220..677
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mqtflivggg edgktvldml asvdfiavvg mvdaapdapg lvearkrgip tstdmqtfla
       61 pppdvildvt dadevegrlk emappqthvi sgavarlmvk lvgqawkrrq neleaivnst
      121 hdgmiavnqr gevtlfnkaa grmtgvdpak slgkpvtevi pntrlgvvik egiselnrrq
      181 tlengleiit srvpvkapdg kvigavavfr diseikqltq qvldlesmks mlqaiinssd
      241 daisvvdqdg mgilinpayt rltgltpeqv igkpaetdis egeslhkkvl ktrqpargvh
      301 mkvgphhkev vvnaapiiig delkgsvgii hdvtelkqls rdlerarrii rtleakytfe
      361 diignsesmc hslaqakqaa qtratvllrg esgtgkelfa haihnasdrk ynqfvrvnca
      421 tlsesllese lfgyeegaft gakrggkkgl feeasggtif ldeigelsls tqakllrvlq
      481 ekevlrvggt ksipvdvrvi aatnvyleka iqekrfredl yyrlnvlpih iaplrmrked
      541 lydlslhlik kfnqeygrqv eeigedaihv lsqydwpgnv relenvlgra minmafnerr
      601 mrrehippld lsrmiqpsaa psvpdaivgk plkevlaqte rdyilqvvaa cgqnkteaar
      661 rlgisirsly yklerygvl
//
LOCUS       WP_284724593             377 aa            linear   BCT 25-DEC-2024
DEFINITION  two-component system sensor histidine kinase NtrB [Laceyella
            tengchongensis].
ACCESSION   WP_284724593
VERSION     WP_284724593.1
KEYWORDS    RefSeq.
SOURCE      Laceyella tengchongensis
  ORGANISM  Laceyella tengchongensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Laceyella.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 377)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Laceyella tengchongensis"
                     /db_xref="taxon:574699"
     Protein         1..377
                     /product="two-component system sensor histidine kinase
                     NtrB"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009399 - nitrogen fixation [Evidence
                     IEA]"
                     /calculated_mol_wt=42342
     Region          25..377
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 minmnmkslt dhadpscqyl tfypmitver maaqmmanih lgvivldecs qvlelnpaaa
       61 kllrldrarv vyrsfeelva qlglqaqeke qltsfvysaw dgqemdwvwh degeeryftl
      121 rmqalknyeq rlagymlvie ditalrllel qvrrnsrlat igqiaagtah eirnpltaik
      181 gflqvirhkl kdsgqgkecg yidimlkeig risnlvgeil llskprqtdl ravnvikvlr
      241 eilpiiknea llhnidvsfe ksvsalpvvi adgemlkqvf lnlsknaiea mkrggklsir
      301 latmaeerql qveiidsgsg ipeevqekif epffttkeng tglglpicrq ilmelggtie
      361 pdssetgttm rvylpla
//
LOCUS       WP_284724612             429 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Laceyella tengchongensis].
ACCESSION   WP_284724612
VERSION     WP_284724612.1
KEYWORDS    RefSeq.
SOURCE      Laceyella tengchongensis
  ORGANISM  Laceyella tengchongensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Laceyella.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 429)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Laceyella tengchongensis"
                     /db_xref="taxon:574699"
     Protein         1..429
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50003
     Region          92..412
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mqrrmdwlwl iavvlavpla geynvhpfqd dyrvsmsipi yffailwirq yspltiglav
       61 siavvawrsg lhawfyggvd ldvfisdylp sfsyyltyaa llhwvrvrdy hdqpfvilli
      121 gfgtevmsgm velmlrkqfg paefelrrft ylwiiamirn ltvigvyami ifkrerqekq
      181 qklmmlagly eeahymdkll dqakqvshdv kqvqqllqeg stdrdemiqq lrqicvrche
      241 ihkhlevidv glsrlmkreh apdevnvhel leivflagrn yaerkgrrie fmrhvygehp
      301 lyptnmmlsi ltnlvsnave aiersgviki taiydkdwvh fqvwdngpgi rqpvervfve
      361 gyttkwdeqg kqstgiglfh vkglveeagg evkvwsdqqk reteftvslp lplrrperke
      421 enhahlhcg
//
LOCUS       WP_284724629             297 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Laceyella
            tengchongensis].
ACCESSION   WP_284724629
VERSION     WP_284724629.1
KEYWORDS    RefSeq.
SOURCE      Laceyella tengchongensis
  ORGANISM  Laceyella tengchongensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Laceyella.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Laceyella tengchongensis"
                     /db_xref="taxon:574699"
     Protein         1..297
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33101
     Region          1..70
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          <46..187
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <154..>270
                     /region_name="PknB_PASTA_kin"
                     /note="Stk1 family PASTA domain-containing Ser/Thr kinase;
                     NF033483"
                     /db_xref="CDD:468045"
ORIGIN      
        1 msneigyrlr qarellrlsl edveattriq kkylialeqg dfsqfpspay vrayvrayal
       61 avgenpqqll hlyqpgpqpp tgarsvnqrl pqqpvaggqq lrqantrmtp tpsaypnrme
      121 qakslrqmte esaelveqpt lartakgkpr rpqmpadvpd peelgitpsp pepvagprrq
      181 aspplqprrr darrekkkqg svfgkvytim livgavllvl atiafmwyra enaaqlkske
      241 apltvkqnqv keadkplgkp rlsvlstspe gpdryelina helelkiswl resgsaf
//
LOCUS       WP_284724761             888 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Bacillus aerius].
ACCESSION   WP_284724761
VERSION     WP_284724761.1
KEYWORDS    RefSeq.
SOURCE      Bacillus aerius
  ORGANISM  Bacillus aerius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 888)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 888)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14403354
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..888
                     /organism="Bacillus aerius"
                     /db_xref="taxon:293388"
     Protein         1..888
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=96114
     Region          407..681
                     /region_name="Peptidases_S8_Thermitase_like"
                     /note="Peptidase S8 family domain in Thermitase-like
                     proteins; cd07484"
                     /db_xref="CDD:173810"
     Site            order(456,491,554..555,641,644)
                     /site_type="active"
                     /db_xref="CDD:173810"
     Site            order(456,491,644)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173810"
     Region          <742..>876
                     /region_name="Ig_like_BLP2"
                     /note="Ig-like repeat protein Blp2; NF040520"
                     /db_xref="CDD:468522"
     Region          813..873
                     /region_name="Big_6"
                     /note="Bacterial Ig domain; pfam17936"
                     /db_xref="CDD:465576"
ORIGIN      
        1 mfkkqvkscv vvlmaiilcm aalpgyeasa vskgtsvnea iglkdgevis gtlqnekees
       61 wyqitpsadd vakhthmqis vkskqvlsvs vypskdraik ddtysryrvd tasgeteinf
      121 phawsgpyyv kvlylgseed srdeeedaay tigykganlp psepifpeee eptiiiiekk
      181 hgreilqsir tiedkrfnet adgqkltrll qktkpflksk linnqkkqqt vynhlltlks
      241 llndveknga fsghivteke qqairslfdm lkeaspaylk keleavgqkl gidqlegksi
      301 gyvlekqklv peekvntnki ifklkdgqtl qsakkkmkgy giqenrvtsq svnplfkgmy
      361 vydvpagkes agktlkagka vikstarkls sipnvefaep vqtyralsnd aqygyqwplk
      421 nsaqnsgkkg advkfeqmnt ligtskmkqt liavvdtgvd srlsdlsgtv rtdlganlig
      481 rnkdaiddng hgthvagiia akadnhysma glnqhtgiip vkvldaygng dtehialgik
      541 havdkgakvi nmslggyysk vieyamnyaa qknvlvvvas gndgipemgy patskyamav
      601 gasnrmdiaa efssygkgls msapgsdips lmpdgnvsyl sgtsmatpyv aaaaglllsk
      661 nptlkpnqvr nilqntaddi sfkavdgtdd vfydendepv vdpkipgidw mtghgrlnaf
      721 aalsavelna svnkvedqhq kvtgkakaga aisvysgktl lgkgtaskkg tfsvkikhqn
      781 knkvlhikis kgkaatslkt vvkkgkapak pkvnrvtvks ktvkgtagag ltikvknksk
      841 kviqtvktns kgaftakikp qkaktvlyvt asdvrkresk avkvvvkk
//
LOCUS       WP_284724816             233 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Bacillus
            aerius].
ACCESSION   WP_284724816
VERSION     WP_284724816.1
KEYWORDS    RefSeq.
SOURCE      Bacillus aerius
  ORGANISM  Bacillus aerius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Bacillus aerius"
                     /db_xref="taxon:293388"
     Protein         1..233
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=26428
     Region          19..174
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mkifaiqlqp lddrnarkqi eqlkpfvsle kraaaerfrf lidarrtllg evlirhiihe
       61 myalpmeqii fetegngkpv vrqipsfhfn lshsgdwvvg avhdapvgid ieeikpidfa
      121 iakrffsade yqdllsqpae rqeayffhlw smkeafiklt gkgisyglss ftarlsedgq
      181 atlrlpdhea pcvvqtysld payqmavctr kpaaaehvei ltcenmlsrl nnv
//
LOCUS       WP_284724883             189 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Bacillus aerius].
ACCESSION   WP_284724883
VERSION     WP_284724883.1
KEYWORDS    RefSeq.
SOURCE      Bacillus aerius
  ORGANISM  Bacillus aerius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Bacillus aerius"
                     /db_xref="taxon:293388"
     Protein         1..189
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21528
     Region          13..64
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(16,20,46)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(19,45)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(26..27,39,42,46..47)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mqnspynqrn lpeilrkvrk eagysqyqlg kliggrdqrn vsdiengyvr ptpelcinwf
       61 kacgayehid lvhyifkmhp laaapidpal nncahkalin lvqemkdaqk aigelaewln
      121 ntrpgkhgel pmqaikqiyd ltqanktlmy smarefdlki qdltekwskk aivaevamhk
      181 rqdreavla
//
LOCUS       WP_284724963             476 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: SLC13 family permease [Bacillus].
ACCESSION   WP_284724963
VERSION     WP_284724963.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..476
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51908
     Region          91..473
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mivykkvnlt glvlgpiffl lifllipese ltyaprvvlg vtawtatwwv tealpipats
       61 llpiillptl gglsmeqtsr aygdpivfmy mggfmiaiai ekwnlhrrma lhilniigtr
      121 sdrivlgvmm ataflsmwis naatalmmlp valavikevk andilsgasl drfsksills
      181 vaysasiggl atlvgsvpna vfaamskkll dreimffewf lfgfpvaavl lillflyltk
      241 iqfkvehtge mgaafiqkgl edlgkmkqee kwvfaiflmt aflwifkifl fgglpvsdts
      301 iaifgamllf lipatngeri lewqdmkqlp wgllllfggg lslatgfaet nltgwigenl
      361 qhlnglsylm lliiltasil fmteimsnta vanmiipitv glglaigmep yglmaaaala
      421 sscafmlpis tppnaavfsa dvlkisdmvk agfwlnvisi vaivlavyfw lpvvlr
//
LOCUS       WP_284724982             451 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Bacillus aerius].
ACCESSION   WP_284724982
VERSION     WP_284724982.1
KEYWORDS    RefSeq.
SOURCE      Bacillus aerius
  ORGANISM  Bacillus aerius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Bacillus aerius"
                     /db_xref="taxon:293388"
     Protein         1..451
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48092
     Region          1..432
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mgiieqfvtt mnnflwgppl lilivgtgiy ltfrilfiqi rllpyslkla fskqdktseg
       61 dishfqalmt alaatvgtgn ivgvasavia ggpgavfwmw faaffgmatk faeavlavky
      121 rvknekgems ggpmyylehg lkqkwlgvlf avfgasaafg ignlvqsnsi sgvmnstfqi
      181 ptwvtgiiit aftalvilgg iksigrvtsi fvpvmalfyv icgliilvmn adlvpgavgl
      241 ifsdaftgqa vaggaigtvi rwgvargvfs neaglgsapi aaaaaktdmp arqalvsmtq
      301 vfidtiivcs itgitivmad mylteksdal tslsfahflg pagsiivaig lllfaystii
      361 gwsyygekcf tylakdsyvm yyrivfviav ffgavfkndf vwgvadmlng lmaipnligl
      421 iglsgvvvfe skriidkike ekkeknisvs s
//
LOCUS       WP_284725034             363 aa            linear   BCT 25-DEC-2024
DEFINITION  GGDEF domain-containing protein [Bacillus aerius].
ACCESSION   WP_284725034
VERSION     WP_284725034.1
KEYWORDS    RefSeq.
SOURCE      Bacillus aerius
  ORGANISM  Bacillus aerius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 363)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 363)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 363)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Bacillus aerius"
                     /db_xref="taxon:293388"
     Protein         1..363
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41424
     Region          82..354
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mlrdlfinlt ilvtfhyllm lvfkenflkk edtllrqiyk gmisgllgvl lmffsikagp
       61 aiidlrhipl iltafyggia qtfiaacvii igrllieanv asfinifsmi fiatasflia
      121 erhinhvvkm llsitmsnvi atslfiiivn ersfelhaay wmfsyiaglf nfyviehqtk
      181 ayqmlnlykf qahydfltgv lnkrkfdeil sdafslnlkq pihqmsliyl didyfktind
      241 qyghhegdiv lkeigtrlik ntrssdyigr iggeefavll pncsvektwq iaerlrkkma
      301 dhpiylqngt sihitvsigc aydagtsenm kqlpiiadqe lykakqsgrn qvsfsgrkre
      361 hlt
//
LOCUS       WP_284725058             928 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Bacillus aerius].
ACCESSION   WP_284725058
VERSION     WP_284725058.1
KEYWORDS    RefSeq.
SOURCE      Bacillus aerius
  ORGANISM  Bacillus aerius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 928)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 928)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 928)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 928)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 928)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 928)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 928)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18767243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..928
                     /organism="Bacillus aerius"
                     /db_xref="taxon:293388"
     Protein         1..928
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=107982
     Region          1..928
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          1..198
                     /region_name="AAA_27"
                     /note="AAA domain; pfam13514"
                     /db_xref="CDD:433272"
ORIGIN      
        1 mkirslhian fgkfsnqtfh fsddgfqlvy glnesgkttl kafiesmlfg fskshmykpk
       61 hgsfyggslt cldeelgvih iertsdhggq aqvllpngev kdeaflhaml kgtdrrlyqs
      121 iysfdvfglq nvqalnqdqi gefllfsslf gsdaaskmds rllkqqeqlf kpngrkpeln
      181 qqldhvkels gklkqaklve srytekkkeq aeltekveml qhemrqteee iqlltehirl
      241 ypmienkiel kkdlasyper vkrfrpetah eldkleshlh pkkaqvtalk qkldhlqtsl
      301 tqvqplydkd tvlemkrvia essdaelvkk rlaegkteqn slkqkieeas aklkwqrpik
      361 ldqlddsldf ewelkeavsq yvrlmdrktq lddrfdharh eleeaetalk glkeqpvkqq
      421 daedvrgtra tvkqnhsrvw lfplmfvlca viltvlfvla eswvtllfag fsvfvliaiy
      481 pvlkqtqmke andsnayhsf qvqtasaetl vkqkellyer miqqyedwer elepvqqqve
      541 dmrrqlglss elsflveafh ilkqlkanta ayealnkeie mltqqqstye qrvsalmsll
      601 qrkegtiqen isafqeilkd eekrekerqt lhvsiqhveq qlttlegevq yyekqtdelf
      661 rkvgaasked yhvlshlske yrerlynlqq lnqelhksgy ideeevivrk glrtleeqca
      721 qakrhlndmq envtnmkkrl aelaveirqi easgtvsdlt hqlaveqeqa khlakkwaai
      781 qlvrsvirek lnehketrlp allqtasrfi qpltndryev ilfsaeddrl ivkrrdgrlf
      841 rpeelsqatc eqiylsirfa lalshqqdcq lpfmmddsfv hfdhvrldrv lelmseltrf
      901 etqlfyftch hymkqaaedg qitslave
//
LOCUS       WP_284725066             161 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Bacillus
            aerius].
ACCESSION   WP_284725066
VERSION     WP_284725066.1
KEYWORDS    RefSeq.
SOURCE      Bacillus aerius
  ORGANISM  Bacillus aerius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Bacillus aerius"
                     /db_xref="taxon:293388"
     Protein         1..161
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=18635
     Region          66..160
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mnfyitygta dflqkiakkh hlenllytvg keqaalfhet egetvfkaph sydviytkge
       61 lvqsgfvtln hipvklesra lfestfqkkt nmsehqrgfq alrvlrpkkd eevyliltlw
      121 esedlfqdfq eseaffqphe dtgsifsrpa yltsyhavid h
//
LOCUS       WP_284725099             305 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Bacillus aerius].
ACCESSION   WP_284725099
VERSION     WP_284725099.1
KEYWORDS    RefSeq.
SOURCE      Bacillus aerius
  ORGANISM  Bacillus aerius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Bacillus aerius"
                     /db_xref="taxon:293388"
     Protein         1..305
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34423
     Region          1..293
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 maeklleikn lkqhfhtarg tvkavdgvsf diykgetlgl vgesgcgkst tgrsiirlyd
       61 atdgevlykg esvhgkksrq kmlefnrqmq mifqdpyasl nprmtvldii aegidihgla
      121 ktkqarkdrv yqlletvgln kehanryphe fsggqrqrig iaralavepd fiiadepisa
      181 ldvsiqaqvv nlmkelqeek gltylfiahd lsmvkyisdr igvmyfgklv elapanelye
      241 nplhpytksl lsaiplpdpd yernrkriky npsvhkgtnt efrevkpghf vscteeefke
      301 ikakq
//
LOCUS       WP_284725128             148 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [Bacillus].
ACCESSION   WP_284725128
VERSION     WP_284725128.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..148
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17179
     Region          <37..142
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mkredalklr sdikkmiiit gvfesqnlpn gpfekplpts qmmaleeiem ekltvwqlsn
       61 klrletstvs rlvdklvkkg lvyrevnekn rrelflhlte kghitvnrlr eqslafyqri
      121 lnnlseseqk ivvdgfklfi dsisksfd
//
LOCUS       WP_284725144             489 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Bacillus aerius].
ACCESSION   WP_284725144
VERSION     WP_284725144.1
KEYWORDS    RefSeq.
SOURCE      Bacillus aerius
  ORGANISM  Bacillus aerius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Bacillus aerius"
                     /db_xref="taxon:293388"
     Protein         1..489
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=55927
     Region          15..360
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mtqptkyera ivigggitgm laakvlssfy levliiekde lpdapenrfg tpqafhphrm
       61 lplgkqivdr lfpgytkell emggyntwhq tsrfmtkdge lvltdteeta vtrramlewv
      121 lmqrmlredr vqflekheai allfeeettq vsglqvkdrr ikhgiinkms adlvidtsgr
      181 msklpkwlks agrtlpqtde livslgystr yyqippeapn lepmvivgqp nkqiptglfe
      241 rvdhdlvavl lsaaggshyp ttdadqfdee ttrltnpsia eaithlipyt kpkgfrvpac
      301 vrnhyeqmed wpsgllvmgd alctldpihg qgmtkaalea qtlermlkqa qedglisfer
      361 htlqqmqhan klgwwlcaia dmawegvelk gtpishltfv qeffnyyvqy avqtkqpkcl
      421 eayhrmhsfl ieprkiinle qlqdmiqads tgevrnwwqr wdqkndelnr affyeavpdf
      481 qlhlllkst
//
LOCUS       WP_284725199             477 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Bacillus aerius].
ACCESSION   WP_284725199
VERSION     WP_284725199.1
KEYWORDS    RefSeq.
SOURCE      Bacillus aerius
  ORGANISM  Bacillus aerius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Bacillus aerius"
                     /db_xref="taxon:293388"
     Protein         1..477
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=56209
     Region          1..475
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 meivviwfrr dmrlddhial skaityakkh qyrlfafyhl dpfftemeld lnnehffqnl
       61 anfvkeares hmyvhlihdd ilsafqklld aydinavffn edevgngrtr deqvtrflee
      121 kgihvskwqd thlhgardil kvdgshyqvf tpyyqawrkq ekqsvikvdk sflssehtic
      181 deslsekgda klrdiikkct rkfdqigsdk amstlggfiq erlthyhekr dipsvfgtsk
      241 lsrflktgti sirtifhavn eeelfedegk etfmkelawr dfyhmifahy pemkekeins
      301 sfqhikwndd etlfeawckg qtgfplvdag mrqlneegwm hnrlrmvtas fltkdyfidw
      361 rmgeayfark lvdydeasni ggfqwaasvg tdavpyfrif npttqskrfd psgeyirryv
      421 pelkhvnekw ihepskmpid eqmksgcvlg dtyplptvdh qerrkkaisl feeakqt
//
LOCUS       WP_284725436              74 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Bacillus aerius].
ACCESSION   WP_284725436
VERSION     WP_284725436.1
KEYWORDS    RefSeq.
SOURCE      Bacillus aerius
  ORGANISM  Bacillus aerius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Bacillus aerius"
                     /db_xref="taxon:293388"
     Protein         1..74
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8748
     Region          4..>56
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mtpellrtfr vtrnmtqael adklgcstqm ialierqerr ftermanrfm vafnldekkl
       61 qeirklreai vfde
//
LOCUS       WP_284725514             580 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Bacillus
            aerius].
ACCESSION   WP_284725514
VERSION     WP_284725514.1
KEYWORDS    RefSeq.
SOURCE      Bacillus aerius
  ORGANISM  Bacillus aerius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 580)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Bacillus aerius"
                     /db_xref="taxon:293388"
     Protein         1..580
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=65880
     Region          28..557
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mlktrriqwt gviifilllg llfrlaeiql fftesfskld inliqesvrq rteevvisdg
       61 rgefldrnge alltkeepav iifpflqydl phlkqtasil emeedelksq ltetkkplil
      121 kdditkkklk dindmkysgv ygvymkekdk krlalhtlgf tsenpellrk rypdkkelsi
      181 rteigtfgle stfdefllpe qdtkllyhvd grgnplfgmd vkytaeahsf yplqvqttmd
      241 edmqremenv lkaqgvekgg avlldiqnss vlamasvpnv tsknrhearn ymltamapgs
      301 vfktvvlaaa ieknlnqpqt mydcrknlyg epegkqevln lsesfaqscn ytfatlaeql
      361 iqtddqilek tasklglvdr agwegdvyhk qqfkqfdree tgsvwgdkrd khvkkaiaqt
      421 aigqknvktt plqianmmat iarggerkev riadkvmyqn gttmlsfqnk rpdgdsidry
      481 taqtlqkylr qvvtsdkgtg rrfqdlpfhi agksgtaqtg skdkqgnply hkwfagyfpa
      541 ekptyalvvv hldetsgrak tneafydivk kvneiekkqt
//
LOCUS       WP_284725556             376 aa            linear   BCT 25-DEC-2024
DEFINITION  2-methylaconitate cis-trans isomerase PrpF family protein [Bacillus
            aerius].
ACCESSION   WP_284725556
VERSION     WP_284725556.1
KEYWORDS    RefSeq.
SOURCE      Bacillus aerius
  ORGANISM  Bacillus aerius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15201204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Bacillus aerius"
                     /db_xref="taxon:293388"
     Protein         1..376
                     /product="2-methylaconitate cis-trans isomerase PrpF
                     family protein"
                     /calculated_mol_wt=40861
     Region          1..365
                     /region_name="PrpF"
                     /note="2-Methylaconitate cis-trans-isomerase PrpF
                     (2-methyl citrate pathway) [Energy production and
                     conversion]; COG2828"
                     /db_xref="CDD:442076"
ORIGIN      
        1 mrkvpitimr ggtskgvfiq andapyehde leaflldimg spdrlqvdgi gggnsltskv
       61 aiidkatrpd vdvnytfaqv sinerfvdfk gncgnissav gpyaiikglv qavepvttvr
      121 ilntntnkii vaevevenge vkfegqaeip gvkgtgspiy lsfekpegav tgktfptgnk
      181 mdtiqtkfge ipisivdian piafirakdi qlkgtelpee ftdellddle eirsiaaemc
      241 hfapkelatl qspavpklai isepadyvdt ngilrraadm diivrmlsmq rphqalaitg
      301 svcvsascfm dqtlpaqlfe gqddtlrigh pagimqteid isqnrvkvir tareildgva
      361 ftkkdymvqp qikrea
//
LOCUS       WP_284725565             247 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Bacillus aerius].
ACCESSION   WP_284725565
VERSION     WP_284725565.1
KEYWORDS    RefSeq.
SOURCE      Bacillus aerius
  ORGANISM  Bacillus aerius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Bacillus aerius"
                     /db_xref="taxon:293388"
     Protein         1..247
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26764
     Region          4..235
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mkyiesakna hikqwkklht kkertktglf lvegkhlvee alksgvvkel mvatpdmlpa
       61 giepdielye lseeaftamt etetpqqiaa vctipvfeek kyermlllda vqdpgnlgtl
      121 irtadaagld avilgdgtvd afngktlrsa qgshfhlpil kqtlqqtipa lkaqgipvyg
      181 salkdakeyk hiasegpfal ivgnegagid peilqmtdqn lyvpmygqae slnvavaaav
      241 lvyhlrg
//
LOCUS       WP_284725606             250 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Bacillus
            aerius].
ACCESSION   WP_284725606
VERSION     WP_284725606.1
KEYWORDS    RefSeq.
SOURCE      Bacillus aerius
  ORGANISM  Bacillus aerius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 250)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Bacillus aerius"
                     /db_xref="taxon:293388"
     Protein         1..250
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28153
     Region          3..246
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkkitmiggc gvigrlltke lsseydltii dqtrcveevi fanaaieeel fqaiprdtdv
       61 iihllnidmt hdvmnekefa kmnevfwist ynmfrsaarl sipkvifass nhvtdryekd
      121 ghsllgreit tddvpatknv ygilkfaseq lgrlfhdqtg mtvinlrigt vvtdemeglh
      181 tkkrtkrtll shddlfgmik aaietdvpfg tyyavseneg kpwstqstkq elgyrpdvnt
      241 aeilkendqa
//
LOCUS       WP_284725688             584 aa            linear   BCT 25-DEC-2024
DEFINITION  terminase large subunit [Bacillus aerius].
ACCESSION   WP_284725688
VERSION     WP_284725688.1
KEYWORDS    RefSeq.
SOURCE      Bacillus aerius
  ORGANISM  Bacillus aerius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Bacillus aerius"
                     /db_xref="taxon:293388"
     Protein         1..584
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66389
     Region          1..580
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 miepgvnyad iyakqvlsnk kehckavika verylrwkkr kdiwldvdaa nramdfietf
       61 ckhskgelag kpltlelwqk fiytniygfy kkdekgrevr avrtayvqvp rkngktvlas
      121 gsgtyalygd gelgaecyta atdsdqania aqqiastiin spdldevtqi ykgqkgkina
      181 iwyrfsidgv eyanclvpls kntkgldgkg phfvlldevh aqdnadmydi lksgmgsrlq
      241 plmfiistag kgttsvglqi yeyaksllnl rkdeeddtsy ftfitepdkg dkwddrkvwk
      301 kvnpnwgvsv qpsflesefk naqqsaerkd eflakylnif vrstgayfdk divgkmildd
      361 ngeiirdigd ysgsevvlgl dlskttdltc vsinipthdd sgrsrlvvkq myfipdhnie
      421 grektenipy rqmaekgflt fcpgrsidyd mvirymieca qmydviqvny dpalsekiie
      481 sleaegftcv evkqygavln sprddaevlm yeeriktdnp lfiycienvv aeknyqglkr
      541 pskkqsknki dgfsafltah ketmmmmedy ssdeyesmld elyr
//
LOCUS       WP_284725942             293 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Bacillus aerius].
ACCESSION   WP_284725942
VERSION     WP_284725942.1
KEYWORDS    RefSeq.
SOURCE      Bacillus aerius
  ORGANISM  Bacillus aerius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Bacillus aerius"
                     /db_xref="taxon:293388"
     Protein         1..293
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33266
     Region          20..278
                     /region_name="YbbA"
                     /note="Predicted hydrolase of the alpha/beta superfamily
                     [General function prediction only]; COG2819"
                     /db_xref="CDD:442067"
ORIGIN      
        1 mlkrpegmgt enslfgesrp ffipgteqld itahpyrlfi fkpnatppaa gfpvmyvldg
       61 nslfgtmvea irlqsrrpek tgiipaiivg igyqteepyh plrhydltlt apdasigrkr
      121 kdfsnhtygg astffsflek tvkpyieqrf pinqsrqtlf ghslgglfvl htlfehpday
      181 qtyiagspsi hwnkklflek ehqftnyirq vpmdvrllvg vgelekhhpc qmndhansla
      241 nrmlplspyg lhtayhefpe eghtsvlpvl mnyafrfaly hddpltttdm kks
//
LOCUS       WP_284726087             359 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Cobetia amphilecti].
ACCESSION   WP_284726087
VERSION     WP_284726087.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..359
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40135
     Region          25..359
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 msaailkdaq sssqasprvd saelgetlve irdlekrfsl sgdfleqltf ekgrlrrkqe
       61 yvhaingvtl dvkrgealcv vgesgcgkst vartvmgllk psggevrfdg tridnmaprd
      121 llpyrrrmqm ifqnpyasln prmtiqqtle eplrfhqptl kdgevrdkie evmrsvgidp
      181 dwgkrfahef sggqrqrisi aralavdpef ivadepisal dvsiqaqvln lmmeaqeqrn
      241 ltylfithdl avvehfgtrv avmylgtlce ladtrslfar prhpytqalm saiprlhddk
      301 pnhirlegev ptpvnlpsgc vfhgrcphan qrcrteiprl iatdtgqvac haveegrid
//
LOCUS       WP_284726169             318 aa            linear   BCT 25-DEC-2024
DEFINITION  TRAP transporter large permease [Cobetia amphilecti].
ACCESSION   WP_284726169
VERSION     WP_284726169.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..318
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=33417
     Region          1..>281
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mlgflsvgil tlllagipva vtlfllafgi dqfysffplt kalgqnlwsv adsflliaip
       61 lfvlmgeiiv ragiaekayr amdhwlswlp ggllhanitt salfsatsgs svataatvst
      121 vtlpqgkklg ydaklfcgsi aaggtlgili ppsinlivyg fltetsipkl fmaglvpglg
      181 laalfmlasl llcvwkpslg gprqsaswst rikslsfllp llvlfivivg siylgwatpt
      241 eaaaigvlas lglaainrsl dlamisrald gtvkttsmil frqdhlddpv hhhggllpql
      301 ragllrhgpa ghrparsl
//
LOCUS       WP_284726327             204 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Cobetia amphilecti].
ACCESSION   WP_284726327
VERSION     WP_284726327.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..204
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=22697
     Region          2..192
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mtplvlasss rwrrellerl glpftwtaps idetprrees aetlvhrlal gkanavaday
       61 shhliigsdq vavfegeilg kpadlsaasa qlgrfsgrrv rfvtglalid trsarhwvch
      121 edyevvfrsl tsdeieryve rerpldsags frmeglgitl ferlegrdpn sliglplirl
      181 cellreagvd plldaprsre tpqp
//
LOCUS       WP_284726393             286 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Cobetia amphilecti].
ACCESSION   WP_284726393
VERSION     WP_284726393.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..286
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31081
     Region          7..284
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mdsfsqlppi lqaclagifg lligsflnvv itrlpvmmmr qwraeareal eleaedtprf
       61 nllvpasrcp gcdtpikwhd nlpilgwlkr rgrcascntr isaqyplvel aggalgasia
      121 liygleaqsl wifgacltll vlsvidfrtq llpdaitlpl lwaglayqll fqplmlpsav
      181 igamagylvl wsfywlfkli tgkegmgygd fkllaalgaw lgwqwlplll ilsaglgavl
      241 gillqllvpr lrgapmpfgp ylavagwial lfgtplmsly lsviga
//
LOCUS       WP_284726452             110 aa            linear   BCT 25-DEC-2024
DEFINITION  Rieske (2Fe-2S) protein [Cobetia amphilecti].
ACCESSION   WP_284726452
VERSION     WP_284726452.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..110
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=11839
     Region          <7..89
                     /region_name="NirD"
                     /note="Ferredoxin subunit of nitrite reductase or a
                     ring-hydroxylating dioxygenase [Inorganic ion transport
                     and metabolism, Secondary metabolites biosynthesis,
                     transport and catabolism]; COG2146"
                     /db_xref="CDD:441749"
ORIGIN      
        1 maltlddgrp allvmqpdgp rafldrcphq gsrmltedet gdpymdatgg lilchrhqac
       61 fephhgtcis gpcvgqrlta ldvervhnda spvllllwea pgsggelrek
//
LOCUS       WP_284726481             383 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Cobetia
            amphilecti].
ACCESSION   WP_284726481
VERSION     WP_284726481.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..383
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41190
     Region          56..379
                     /region_name="HisC"
                     /note="Histidinol-phosphate/aromatic aminotransferase or
                     cobyric acid decarboxylase [Amino acid transport and
                     metabolism]; COG0079"
                     /db_xref="CDD:439849"
ORIGIN      
        1 mttasprrfl ahlyqdgphn pfpgikaler rlghalpyqy gsnegldmph htlggalgta
       61 ladlsrsyad adawqlrqql aerlgvayen llvdagadsl lalmmratvc agervitsag
      121 typtlayfar glgaevievp ysesfatadd asssrlapdl aallaaarqh darvvylanp
      181 dnpsghlhsd advralrdal pencslllde ayhdfrpdaa hadhapmart frlrtfskay
      241 glaglrlgfm iaepddvaml tkvrihfavs apamaagell lahpeeaaah vagvidcrdr
      301 laehlrslga evlpsatnfl cvrlksaela aqvqqqlmaq gvlitrsphp slghilrist
      361 ledslvpgrl arleqaiaee rrs
//
LOCUS       WP_284726507             627 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Cobetia amphilecti].
ACCESSION   WP_284726507
VERSION     WP_284726507.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 627)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 627)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 627)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 627)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..627
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=68658
     Region          42..615
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mtsnrpqdah resrdssasp ppapaaelts gplpeaplrh llldfftrhw pryllaiafl
       61 igvaglnlll pwaigatida lrdgsldhda llsrllwlvg aglalyalry awrvtlfgta
      121 yqlgteqrda fhakltrldp gfyqrhrtgd lmahasqdid avemaaaegv lssvdgamtf
      181 vlvlgimlia idvpltllal lpfpfmawaf arisrriger freslerfsd lndqtqeafa
      241 girmlrshal ledegarfsq raaaaeavdy rvqkleaafd pvvfialsaa tlltlgvgsw
      301 rylddaitlg qltsftlyla qliwpmfalg wclnilqrga aaarrlatfh aapealedsg
      361 tldevsnhsl rleinefhyp gsqqralgpl slqvaaggsl givgatgsgk stllrllsrs
      421 wpltpeqgvl tlggreasey tlsawrqqfs lvpqdpflfa lsvadnvala cpeasderir
      481 ealraaafee dlrrlpqgle tlvgergitl sggqrqrlal arsllseapi lllddtlsav
      541 dqvtertllk tlarlqqpdh hglkrtliin shrlsavqac qqilvledgc ileqgdhasl
      601 laargayrrl wqaqqinred dakaers
//
LOCUS       WP_284726209             274 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Cobetia amphilecti].
ACCESSION   WP_284726209
VERSION     WP_284726209.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Dean,M., Moitra,K. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Hum Mutat 43 (9), 1162-1182 (2022)
   PUBMED   35642569
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..274
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=29930
     Region          6..266
                     /region_name="TauC"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, permease component [Inorganic ion transport and
                     metabolism]; COG0600"
                     /db_xref="CDD:440365"
ORIGIN      
        1 mkrlinltps rggrwllggl pfallailyi vqsnqrlldn sndrllpsfa smgesfakla
       61 tevnvrtgdl plwtdtfasl erllagvlis aligltvgll tgglpllrak lsplitvlsl
      121 ippmailpil fiafgtgela kialivigit pflirdlqnq alrlpdeqli kaqtlgtssw
      181 qvltrvllpq ltprllsatr lalgsawlfl iaaeaiaaqd glgyriflvr rylamdvilp
      241 yvawitllaf lldrllvtis trafpwyhae esqs
//
LOCUS       WP_284726607             298 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: HAD-IIB family hydrolase [Cobetia].
ACCESSION   WP_284726607
VERSION     WP_284726607.1
KEYWORDS    RefSeq.
SOURCE      Cobetia
  ORGANISM  Cobetia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467317
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Cobetia"
                     /db_xref="taxon:204286"
     Protein         1..298
                     /product="HAD-IIB family hydrolase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32266
     Region          5..284
                     /region_name="YedP"
                     /note="Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP,
                     HAD superfamily [Carbohydrate transport and metabolism];
                     COG3769"
                     /db_xref="CDD:442983"
ORIGIN      
        1 msetqaplll ltdldgslld hhdyspgpar swltrlrarg awivpntskt aaelaplmds
       61 lglagqpwia enggvvalpa dwlsayplee asapdahglc riavamprdr ilavleelsg
      121 efafegfasm pvariseltg lgegdavlag qrdaseplvw rdaperledf rmrlaghglk
      181 ltrggrfhhv tgdsdkgvaa ryliaryrlc ervrpwtlgf gdgandlpll aavdnavlip
      241 gvgdtsqrdr eladypqlad errcfranlp gpqgwveglr hwlangqpee wtsrglga
//
LOCUS       WP_284726642             182 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Cobetia amphilecti].
ACCESSION   WP_284726642
VERSION     WP_284726642.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..182
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19978
     Region          37..177
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mqhdsnppqa adgshtdvgt hadvgthtdv gnhagvvsrt tltvrgyhld gyghvnnary
       61 lefyeegrwe fmlahldlaa lkregiamva vnlnldwhyp atvhdelvit trlaelgrrk
      121 mimrqeihlg errmgevhpr sgalvsradf tfvlmntdtg rampldgeig allgalvsee
      181 ta
//
LOCUS       WP_284726646             267 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Cobetia
            amphilecti].
ACCESSION   WP_284726646
VERSION     WP_284726646.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..267
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29239
     Region          49..263
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mlssplgrlw rgiataisfl tfglggllvg gmwplltlvv rrpekrqkla rsiihhcmrg
       61 fvglmrglgv ldyrlhdcer lqrpgllvla nhptlidvif llaliphadc vvkgrlarnp
      121 ftrgpiraag yitneepqgv leaagaslar gnalilfpeg trsvpgralk frrgaanial
      181 rtpseitpvl idcqpstltk gepwyhipar rvmlnikvlp dmtahvappp atedevplsr
      241 darqltrrla sdfaaelaaf qqrires
//
LOCUS       WP_284726654             820 aa            linear   BCT 25-DEC-2024
DEFINITION  MMPL family transporter [Cobetia amphilecti].
ACCESSION   WP_284726654
VERSION     WP_284726654.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 820)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468174
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..820
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..820
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=87251
     Region          42..795
                     /region_name="COG4258"
                     /note="Predicted exporter [General function prediction
                     only]"
                     /db_xref="CDD:443400"
ORIGIN      
        1 mtspsreprk gldraiwrwl waaalllcal llavkiapqs pwrgaidtri tamlpqqers
       61 plaaraesld dtanrlvilv gsrdasaaar kqrdaaaqal rqalapiarl ddgksleslr
      121 lpaevqpali apslaslsdd dwqaralkql fqpggqrdli rdpfglagaw qswltpanll
      181 lsggqlllra pastgsvsnk qhsdkqhsde qgsdgkgsdq pgngyrlisa tltgsayams
      241 dqqaleqavn gvkadypdvr llrsglvfha sngaqqakqe mstiglgsli gvllllwavf
      301 rtprrlplll vpvatgvlfa lpltwwafgg lhvltlafga sligisidyv lhlecmrrla
      361 thgrgglaal wpgltlglcs slaaylaitl tpmpglrqmg mfaalgliga wlsvrlwlpq
      421 lplpaqatre dspaaraagc laraipgkrs wqalglllma alaslyglrs ddrltqlnps
      481 paslineqre vqrllaepdg lrylivqaet daalltrlha legtfqqlna rqqlghwasl
      541 aqqlptlaqq qanlgamrer trtllpqvls taglppelvk raeqaiagah plrpadwval
      601 pagemgqrlw ldsrtaaigi vrfgdvtahg saalarlaad desleyvdqv arlsttlgri
      661 rsemawlvgg avvlisllla lryrrstwra llpplgglvl tlaaltlagv glnlfhllgl
      721 llvlgiglda gifcaehpar saekgnptrs anekaeqgks eastsrasqa sllaislsca
      781 ssllafglls fsqtpalaal glacllglsa twclvpfars
//
LOCUS       WP_284726660             582 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Cobetia amphilecti].
ACCESSION   WP_284726660
VERSION     WP_284726660.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 582)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..582
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=66434
     Region          1..503
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mrfdslkisn wrsikeidie aqdlmviigr nnhgksnils ailfffsqlk hqdldfncas
       61 evlfveivfn dlsneeksrf tkyltsdnki tvrktaykgg sfeyrgfvek ctiewlreee
      121 assytkrenv edtplidflp aqgritkqdv vnaqtsyiee hrgelefvyq keeteflglk
      181 svaassfgel yfipavkdav sdfsskessv fgriysgvis smsesnndwr makerlaelf
      241 sifninddge hherrpqeit elelslsrel svwgtkidie ikepdidsvi ksntqiwidd
      301 gvrtdivrkg hglqraltla lvqvlaketp grihtdedvr isnskyfife epelylhpqa
      361 qrqlfdsfvr lsdlgsqvii cthssglidl eryrsiyiad ksndesgtvv rkcagdifeg
      421 nekrdfnlty winpdrnelf fakkvilleg atekavipal akrfnifnye yaaidcgskn
      481 sipqyiklln cflipyvavy dldhqldksr davnaadist qkildaiede vgyglalvnd
      541 ieeelglsrg agskpyealn hinsrefqis vrmlekitni ys
//
LOCUS       WP_284726772             418 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Cobetia].
ACCESSION   WP_284726772
VERSION     WP_284726772.1
KEYWORDS    RefSeq.
SOURCE      Cobetia
  ORGANISM  Cobetia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Cobetia"
                     /db_xref="taxon:204286"
     Protein         1..418
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45430
     Region          5..417
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 msdsehteva vigagavgva calwlrrsgh evtmieregi asgtsfgnas tladygclpi
       61 arpeiwrsmp slllspdspf vidwkclprl spwlmrfmgq cnatrfrans emlaqllsht
      121 ytdyqplldd apaaaamiqr kgclyaygka enlqaaqgdi rlrdqlgihq qvltadelia
      181 lepameghta ggvlfpssch lddpqvfidt latplreegr ivsaevtrls rrasgmllky
      241 adgrrlmadr vvlaagawsa hlarqigdri pldtergyhi efdlehspln rptcpvesaf
      301 ymtplhsaeg arlrvagtve lsslagpanp arfdylesrv rkvlgidapv arrwlgfrpt
      361 lpdsvpvigp spneprviha fghqhigvtl agvtgrlvse clakgspewi tpcsaarf
//
LOCUS       WP_284726780             380 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: DegT/DnrJ/EryC1/StrS family aminotransferase
            [Cobetia].
ACCESSION   WP_284726780
VERSION     WP_284726780.1
KEYWORDS    RefSeq.
SOURCE      Cobetia
  ORGANISM  Cobetia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Cobetia"
                     /db_xref="taxon:204286"
     Protein         1..380
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42147
     Region          1..370
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mitvtrpyfp eretfdryvd sifegrwltn hgpleqeltr rletylgven lllvsngtla
       61 lqiayralgi aqmpgqyesa evittpftfi atasslkweg mqpvftdidp dtlcldpari
      121 esaitprtra ivpvhvfgna cdveaidalg eahdlkviyd gahafgvtyr gnsllshgda
      181 stlsfhatkl fhsieggaii fkrkedlera rklinfgitg pecieelgin akmnefqaam
      241 glcvldeieg nlesralvwh ayaqalrgnv qlqtrqtgas lnyayfpiil esesmllevm
      301 qrlqqegyla rryfcpsles lsflgrpaae lqdedvitpq ivhstdiasr ilclplysgl
      361 evseilgavr iivnrhvkaa
//
LOCUS       WP_284726803             157 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: phosphate-starvation-inducible protein PsiE
            [Cobetia].
ACCESSION   WP_284726803
VERSION     WP_284726803.1
KEYWORDS    RefSeq.
SOURCE      Cobetia
  ORGANISM  Cobetia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Cobetia"
                     /db_xref="taxon:204286"
     Protein         1..157
                     /product="phosphate-starvation-inducible protein PsiE"
                     /calculated_mol_wt=17137
     Region          10..138
                     /region_name="PsiE"
                     /note="Phosphate starvation-inducible membrane PsiE
                     (function unknown) [General function prediction only];
                     COG3223"
                     /db_xref="CDD:442456"
ORIGIN      
        1 mnrldkhrer mhkqansign flvegfhylg lfaiggaiai asvsaffemf akgsasvddi
       61 lllfiylelg amvgiyfktn hlpirfllyi aitaltryli gdvshhkapd igllylcggi
      121 fflalsvlav rfasykypss kaidpmggtv gdedsar
//
LOCUS       WP_284726806             659 aa            linear   BCT 25-DEC-2024
DEFINITION  autotransporter outer membrane beta-barrel domain-containing
            protein [Cobetia amphilecti].
ACCESSION   WP_284726806
VERSION     WP_284726806.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009446
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..659
                     /product="autotransporter outer membrane beta-barrel
                     domain-containing protein"
                     /calculated_mol_wt=68189
     Region          8..659
                     /region_name="YhjY"
                     /note="Uncharacterized conserved protein YhjY, contains
                     autotransporter beta-barrel domain [General function
                     prediction only]; COG5571"
                     /db_xref="CDD:444313"
ORIGIN      
        1 mpsrshravf ppasglarrf tltslalais ttllatpaqa ysnlylfgds lsdsgqfpdt
       61 tlgglnslrf tnrsgpdyen saygsvstql latelglaae pstsviyqla gfsdgtnyav
      121 ggyttaqila svtdedgsev vippgstgag tvlrvedgyl vstggtadpd alyyvngggn
      181 dflqgvitsp atavasagnl asavealaaa gattimvsnl pdvgstpagq sagaaqaagt
      241 salvdvfnda lgarlaaldg evniirldtv gileevlasp aefgfasdvp ltqvcfsdsc
      301 nvtpyglgga aedpdkllfn dgvhpttagq eiladyayam laapsvlgla pqlgtgalna
      361 sqrslgdelr pgaqdrrsge gvrvfaigsa sggtgdgets sgqqgfdseq rgagvgvmlp
      421 ldnalgqawg gvavsqrtad fdvddgsele legqvfslfa rqqlgrfgvq avasygdfdy
      481 dldrhvalgq ssrtlsgetd gdgfsaearl dyrltaadsl wynapfvayr htesdidgyt
      541 esgsaanali vsdqtlrdrr veagfmvdra iaegfglyge laygkrlddd adsaevrlas
      601 lptnayraed ldrssdnylr vdggwrmqlg rnamlhlgag ietwdevtar gevgvsytf
//
LOCUS       WP_284726816             213 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Cobetia].
ACCESSION   WP_284726816
VERSION     WP_284726816.1
KEYWORDS    RefSeq.
SOURCE      Cobetia
  ORGANISM  Cobetia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Cobetia"
                     /db_xref="taxon:204286"
     Protein         1..213
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23071
     Region          2..167
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          88..181
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtpilrpair adldalvele evsfdsdwfs rrqlshlilr ahartlviiq pdddviptap
       61 avddvmaalw pagsverdda tplrsvlgyg tvlfrrnsrr arlysfclhp esrgrglaqr
      121 mltsleqlai aqgctqfdle vhtgngaaia lyerhgfekc grlrdyyadg aaawkmrkal
      181 tldspapvae elaagdagea hpgppstvna gaa
//
LOCUS       WP_284726865             414 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: CobW family GTP-binding protein [Cobetia].
ACCESSION   WP_284726865
VERSION     WP_284726865.1
KEYWORDS    RefSeq.
SOURCE      Cobetia
  ORGANISM  Cobetia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Cobetia"
                     /db_xref="taxon:204286"
     Protein         1..414
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44385
     Region          17..405
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 msvasrgars gdaptepapi pvhlitgflg tgkssfiqal vaakpadehw ailvnefgqv
       61 gidqalfagr edvsvkglpg gclccqlafv lqaglvslih qtrpdrliie psglghpagl
      121 idvlrsegla salaleevit lldpralddt rtrehgtfqd qltlaggvvl skrdlateqq
      181 laaaheflag mwprkrwvge lgradgesqs pqarmagqev alidwllsae rvpqrqgggh
      241 gcdahhvsaa redqpeismp aahraardra hlaqasaeps asdmmplpga pvieqaegle
      301 haslgwriaa sevfdldqlt qwldglprew rikgifhtqd gwrsynrang raelapsswr
      361 edsrleliap lggqgqeqeg mmaalpleds rqlnaallac rsdgaarpfn ffge
//
LOCUS       WP_284726385             348 aa            linear   BCT 25-DEC-2024
DEFINITION  ketopantoate reductase family protein [Cobetia amphilecti].
ACCESSION   WP_284726385
VERSION     WP_284726385.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..348
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37715
     Region          14..343
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mhtmtdpedn wlwiigpgai grllaaslma arqrelreqg asalprvlll grqamagqav
       61 mldmttpesl ivssrinhst idtlqdssfr kpsaiwlttk ahgvpavwqq laphitpetp
      121 vtcwqnglsa qpwlaerhan llcasttega wlpaetgast tpdngstadd lqhlgvqhag
      181 rghtwlgawq sggdgdhdsq snqaalmqgd wlkaagface qtpdiqtrlw hklainaain
      241 plvaryrirn gqlrdrpfap mvrqaveeis avldsegipa peegwqalve qviratannr
      301 asmlqdvlag rpteveailg plrstaarhg lalpllddly rqlstpqr
//
LOCUS       WP_284726948             296 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Cobetia amphilecti].
ACCESSION   WP_284726948
VERSION     WP_284726948.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..296
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31737
     Region          24..292
                     /region_name="YbbA"
                     /note="Predicted hydrolase of the alpha/beta superfamily
                     [General function prediction only]; COG2819"
                     /db_xref="CDD:442067"
ORIGIN      
        1 mltsgavsvp alamthaade alpgtttsft qhsrltghdy liqvalpkva pptggypvll
       61 vldgnrhldl ftaardvlgr rgfdkapanl aivavgyags deqaeatrtt vttlrykdft
      121 ppltsgtape gtgggaqfla yltqslppel asrypldlkq palvghslgg lfalhaqqqa
      181 peafgaifai spslwwlqen dqanwplrla cseaagpvli aaggreqspq pqrndpardr
      241 lrvqramidn ahayarqlge rcpqtevqwr ryagedhgsv mwpaarsvme mllger
//
LOCUS       WP_284726951             301 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Cobetia amphilecti].
ACCESSION   WP_284726951
VERSION     WP_284726951.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..301
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33178
     Region          <132..295
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          215..295
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 maraltsdhq cepaegqsgd galignmhlh eaqpglfmrl nrvrkradlm irsriepslk
       61 iavvwrgepk vsfgpdshal apgralcial devtefalks vkgaqehsai lsltpawlkl
      121 hmgvsrasql mpearhlahy vwqpsarlie rleefsrqrp gtlalrlgie slalevisec
      181 laasaslshp tpeglgehwa arledwihsg eaaylsqaem aarlgmsvrq lqrryrdayg
      241 qtlaqdlrrr qltqvahllq drklsieaaa elagyrsaan fatafrrqfg vppsqrpvvt
      301 a
//
LOCUS       WP_284726963             111 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Cobetia amphilecti].
ACCESSION   WP_284726963
VERSION     WP_284726963.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..111
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12752
     Region          1..66
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mihralrtir ryhetprtel ssklgisqaq ltaiesgkkp vqrellekys niydikvssl
       61 iffsetlsth pkknklsenf raafagkvld imewvikkda dqneqpiedk h
//
LOCUS       WP_284726966             551 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Cobetia
            amphilecti].
ACCESSION   WP_284726966
VERSION     WP_284726966.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..551
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=60486
     Region          3..547
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mseldrqilk tiidtahdhy fvvnadgqvm dvspgaaavy gmtreelcaa nvheleasgv
       61 lkpsislevl rtgrtlqmmq ltatgrrvva qahpvfvagk lecvvsrsmd ltdiqllqqe
      121 yavlqqrfsd hlrrnsrgge lsgvsqaegd watagagqsv qateqyaqsq aelrqreqsa
      181 reqaecedaa lelgelqvrs pvmreialll krvaptnatv lmlgesgvgk tafahqlhrw
      241 sqradgpfie vncgaipesl fesemfgyqa gaftgagnrg kaglmeqaeg gtlfldeige
      301 lplatqtkll kviqdgmitr lgdtttrrad frlvvatnqd laarveqgqf rldlyyrinv
      361 lpvslpplre rredipalie qhlsrlnqrh grrklldasl wpilmrqdwl gnirelenwl
      421 erawlsapsd vidsdsvktl lntcstnnan glgnsfgfsn dksngigvte sfttadnshr
      481 pnslsepaae gavampipkl gpnetlkegl arieaqwlre maaelpstya iakragisqp
      541 svvrklknkl r
//
LOCUS       WP_284727004             409 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Cobetia].
ACCESSION   WP_284727004
VERSION     WP_284727004.1
KEYWORDS    RefSeq.
SOURCE      Cobetia
  ORGANISM  Cobetia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 409)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 409)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 409)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Cobetia"
                     /db_xref="taxon:204286"
     Protein         1..409
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45597
     Region          117..395
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mndlmvqvdr qiqqegglgv hfpaeiearf ehdihvahsh klacmsavai siyvlfllnd
       61 wrfrpdhmle aivirvgvmt pialiciyml krgvspvlre mlmtalvcfa miftalliql
      121 svsphsfldl falglivlvg nvlfqlrfwy alcssafhfg vmlylvnahp spyasagfma
      181 lmvflsitlf siisnlrsek aerlsyllll reqlrveeft ekneefrrla sidpltevyn
      241 rrhfdslvss llgkqvdsrl qygvamidvd hfksyndhyg hvkgglclkr iataifesvh
      301 pdvdivarfg geefvvllps sssqqalara eeirrhvrdl alphagssrh givtisigvs
      361 aagtgqgcsf etilkqadea lyrakasgrd rcelfaqqdp qalgrafag
//
LOCUS       WP_284727059             287 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfurtransferase [Cobetia amphilecti].
ACCESSION   WP_284727059
VERSION     WP_284727059.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..287
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31619
     Region          25..286
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mshdssrpsp seadllpliv epqqlaemld hpdivivdvp lkaesharhv pgarlldfkq
       61 lvgsndddip gvpspealsg vmsalgitrd shvvayddeg ggwagrllwt lallghsrys
      121 ylngglhawq gdglplsdta sdwspseyha aymdtsvmat redildrlaa edpqesvvvw
      181 darsaeeyrg ekgqnarlgh ipgavhfewt eamdrernlr irdyaelvte lgarglnpeq
      241 hivthcqshh rsgltwlvgq algfsdvray pgswkewgnr ddtpier
//
LOCUS       WP_284727078             246 aa            linear   BCT 25-DEC-2024
DEFINITION  OmpW/AlkL family protein [Cobetia amphilecti].
ACCESSION   WP_284727078
VERSION     WP_284727078.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006882
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..246
                     /product="OmpW/AlkL family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26087
     Region          29..246
                     /region_name="OmpW"
                     /note="Outer membrane protein OmpW [Cell
                     wall/membrane/envelope biogenesis]; COG3047"
                     /db_xref="CDD:442281"
ORIGIN      
        1 msdvvtrsas lpahltsrsp rsaarpwqll alagltslat lgtapamaad slnassrnsl
       61 sslnygagqf wtragvakvs pksdngrida igadvdvddd safaftlgyr ftdtfgiell
      121 aaqdfdhdis lngqkagsvd hlpptltlqy yplggresri qpyigagvny thfsdetldd
      181 gtklemddsw gaaaqigvdl vinehwaanv aawyldidsd vtvagsvndk veidpivtma
      241 gisyrf
//
LOCUS       WP_284727183            1465 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Cobetia
            amphilecti].
ACCESSION   WP_284727183
VERSION     WP_284727183.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1465
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         <1..1465
                     /product="beta strand repeat-containing protein"
     Region          1..1429
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 tgydsgtvsy tyvedgtaad hsagddsvfd nyavvvtdla gqspsdsldv kildtapvan
       61 ddtytiredd tspdgepvin tsvifsvvgg gqdelgadgv tithldgisl adnegsvtvd
      121 gsygsltint dgtfsydldd araqalgagd lvkevfeyti ldadgdsdta ditinvqgln
      181 dkpvayddgp ivveedtpvs gnvlnndvda dgdelsvvsf tvdgvmydpg ktadlgevgt
      241 llinadgtft ftpgenyngp vpdttyvitd gtefdeails fedvaaiddp vvisaddgav
      301 aedgvteasg tltatdvdsd aptftpatdd sslygtfavd sdgnwtytld ndtavvqglt
      361 sadtineqyi vqlsdgsstt vdivikgtdd alpvissled qsvteatgst ltntftvsaa
      421 agiaavtiag vditdasntp vvisnpdgeg tltvtgydad sgevtytyve dgtaadhtdg
      481 ddsvvdgftv lvtdlagqst sdsldvtvld tapvanadtr sigenrnaav vgnvvdgtsa
      541 tadtlgadav tvtaviagte aapvsdgaaa vitgehgelt laadgsysyq sarddlqyla
      601 agesvtdvyt yeitdadgdt atttltitik gsndapeisv ssgdsaaasl tetdsplsas
      661 gtlsvddvdl snsvtpsvtg vssngdtgtl dnddllallg vdtgaiidde stegtlnwsf
      721 dssaagesfd ylsageslvl tytvtvtdta gatatqdvti tiqgtndapv vtategrvse
      781 egleggiads daadgftdtt dattvtgtvs vtdvdsdsvs lvltapatai tsggsavtws
      841 gggtqsmvat dadgnevatv tiddsgaytf tlsqavdhsg dgedvlsldf gvlatdsega
      901 sstgtltigi eddapeqqea qsfsstlvdt nltivldvsg smasasgigt qtrlesaies
      961 iktlisaydd fgdvrinlvs fsttatsyaa wmtaseavtv leglsaggvt nydaalaeam
     1021 enyaedgale saqnisyffs dgtpygadgn sneldnsldy dsvqyfsggq lipvrdrsdt
     1081 gisnteegiw tdflvdngik syaigmgagv sednlnpiay dgsadedida aivtsfsdld
     1141 dslaatvqsp vsgqlvsgss vdgsllgadg gylqsvtvdg ttysydpvtn tvsatgsdns
     1201 sydadsleli istdlggsml fnlgsgdfty tppdnvsers tdsfdyvtvd ndgdtnassv
     1261 sidvdklavv igtdgndtlt gdgdgpfyad ylvgqggndt lsggegsdrl eggsgndtlr
     1321 ggtgndilsg gegddllvgg agndiltggd gadtfqwlsg hdinseggma tdtitdfsva
     1381 dgdvidlsdl lqsnddadtl ssflhfesdg eggtnieisv dgsdgsnitq einlqdvdlt
     1441 sggdtdtqii qslldsnslk tnvdg
//
LOCUS       WP_284727264             340 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Cobetia amphilecti].
ACCESSION   WP_284727264
VERSION     WP_284727264.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..340
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=37631
     Region          51..285
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 msdlldgasf altdghqpap lvtppaaast vlarvndtal tempqdlyip pealrvflet
       61 fegpldllly lirrqnldil ainvaaithq yieyvelmha mqidlageyl lmaamlaeik
      121 srsllprqpk asdddeeedp raelirrlqe yeqtklaaeg ldemprqgrd wfvatadlpe
      181 letrvvhpdv dlsellgals gllrqadlvq ahtisrevms trermlaimn llthehftpf
      241 eklftleegr agvvvsfmai lelakesmie ivqnaplspi hvrartpepd peddedwlal
      301 efadedevaa dqgafddaas ddaqtspslp psdeqenaas
//
LOCUS       WP_284727288             427 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Cobetia amphilecti].
ACCESSION   WP_284727288
VERSION     WP_284727288.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..427
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=47860
     Region          141..408
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 msqfepappt lattrapadr ltrllrprll rmldkleggs ltvlegrerh vlgkggarnv
       61 tlrihdsraw rrmalggtva aaeaymdgqw etddlvglvr lfaynleqvn dsvdsgtsrl
      121 skwalsvaya larntlagsk rnisahydlg ndlfelfldr ehrmysaavf pypeasleaa
      181 sthkleklfn llelgpqhhl leigtgwggl aihaartrgc rvttttisde qyaytraria
      241 aegledritl lkedyraleg rfdrivsvem ieavghqylp tylktlerll epaglialqa
      301 itirdqrfva asremdfikr yifpggflps haailtamqq dtqlnllqle diglhyaatl
      361 kawgqrfear lgevyaqgyd erfvrmwryy layceggfre rtigtcqlll ggpgarpvqa
      421 glqdwda
//
LOCUS       WP_284727290             612 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Cobetia amphilecti].
ACCESSION   WP_284727290
VERSION     WP_284727290.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 612)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 612)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..612
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=67206
     Region          9..604
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mwpqahfnrp liigalvalt alpwlpglel rlaallpavl agldiarqrr rqllhrqlle
       61 aavhlssdgl visdrhnrvl avnaafshit gyapeeiigr npsllssgrh deefharyrq
      121 alevnghweg evwnrrkqgd eypewlrarr ieqggdvfhv alftditrhk areqdlqrlg
      181 ledsltglpn rrrlgdllvs rlnglragea mdlalidida lksindalga eggdrllqqf
      241 sqrltalarg gvvgriggde fvilrstagg ehtawvdelr qvltkpfeig dqalhlalsi
      301 gscrapedga dadvlmqrle salyaakrhg rntdmrfqpa ldaggdlqlg landlrvaie
      361 iqgqlqlhyq cqhdastgkv asveallrwk hplrgaispa efvplaerhg lmlrlgnwvl
      421 reavqqqasw rraghrlciw vnvsalqliq ggfeaslagl lmeydvpass igleltesvl
      481 lderagdvsr rlaalrargh qiavddfgtg ysslaylkdl pvdklkldra firslpgera
      541 daaitmavla makglgmemi aegvetaeqr eylvsngcgw iqgfyfsrpa pagevierln
      601 gyeagnlaik aa
//
LOCUS       WP_284727292             835 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional diguanylate cyclase/phosphodiesterase [Cobetia
            amphilecti].
ACCESSION   WP_284727292
VERSION     WP_284727292.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12828261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..835
                     /product="bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /calculated_mol_wt=90719
     Region          1..433
                     /region_name="MHYT"
                     /note="MHYT domain, NO-binding membrane sensor [Signal
                     transduction mechanisms]; COG3300"
                     /db_xref="CDD:442529"
     Region          <264..815
                     /region_name="PRK09776"
                     /note="putative diguanylate cyclase; Provisional"
                     /db_xref="CDD:182070"
ORIGIN      
        1 mhgsysyplv alsivvavla shaalqlirq valapsrats lgwlvggava mglgvwamhf
       61 igmlayesqa svtyapglta lsvliamlas glalwvntlp rltpvllmts gtimgggiat
      121 mhytgmaamq mhmpyrydpl lfavsivvav vaataalwlg gfflrqrrpn riyqalaaga
      181 mglaiagmhy igmaamemmp lttpiispag agmnsgqnlw lalaiaiatl avlglallai
      241 saeqrmrrsr hyrsrldgll eyrtrelrhe rdqvavmlds idegvisldr eghiqhinpi
      301 aaelcgwdps largrpwari lqlrhegtlq svasqlegvl qrgevvhmss qtllvardgs
      361 ecavelkasp vrrrsgdveg avlvfrdisy rqamirrlnf qahhdsltgl hnrtafddal
      421 taaladggfh qllyldldff kvvndtcgha agdtvlrels almrahvret dilarlggde
      481 favllyrcsr eqaieraeal caavsayryy degrpfqlgv sigvapaegg vqasevlrqa
      541 dgacymakqs grnqvhayhd gdagferaqr evqwlpllhe alendrftly iqpirslsda
      601 tskpyyevll ryvndsgehl apahfmatae rfglmpeidi wvvtqalqvl esddgriesd
      661 avlainlsgq smgdlrmrdq laalvtqssv mpqrlcfeit etaaisnlaq arefiysmrr
      721 lgcsfalddf gsgmssfayl kelpvnqlki dgafvrnltr dsldaaivsa icgicaqmgi
      781 itvaeyverl elipalelig vdfvqgygig rphpigapli pitprnngpa aslqg
//
LOCUS       WP_284727340             255 aa            linear   BCT 25-DEC-2024
DEFINITION  nuclease-related domain-containing protein [Cobetia amphilecti].
ACCESSION   WP_284727340
VERSION     WP_284727340.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Grynberg,M. and Godzik,A.
  TITLE     NERD: a DNA processing-related domain present in the anthrax
            virulence plasmid, pXO1
  JOURNAL   Trends Biochem Sci 29 (3), 106-110 (2004)
   PUBMED   15055202
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10551559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..255
                     /product="nuclease-related domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28961
     Region          33..144
                     /region_name="NERD"
                     /note="Nuclease-related domain; pfam08378"
                     /db_xref="CDD:462454"
     Region          <211..255
                     /region_name="YrdD"
                     /note="DNA topoisomerase I, ssDNA-binding Zn-finger and
                     Zn-ribbon domains [Replication, recombination and repair];
                     COG0551"
                     /db_xref="CDD:440317"
ORIGIN      
        1 mvvpsniapv msvllclvla sfvsrylksp rmkgrigewr vrwmarrlgk qgyrtlhnvt
       61 lktangttqi dhvllsrfgc fvletknmkg wifgsehean wtqqfprqsf sfqnplrqny
      121 rhlkaleatl cvpfeylhsv iifigrarlk gempsnvtrg tdfvpfvqsf ktpvfseaqv
      181 eamhealltg rlaptratqr ahvqhlkqrn dpqarrecpk cgsrmvlrtv kagvregqqf
      241 wgcsaypacr atqav
//
LOCUS       WP_284727379             233 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: urease accessory protein UreF [Cobetia].
ACCESSION   WP_284727379
VERSION     WP_284727379.1
KEYWORDS    RefSeq.
SOURCE      Cobetia
  ORGANISM  Cobetia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Soriano,A. and Hausinger,R.P.
  TITLE     GTP-dependent activation of urease apoprotein in complex with the
            UreD, UreF, and UreG accessory proteins
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11140-11144 (1999)
   PUBMED   10500143
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Moncrief,M.B. and Hausinger,R.P.
  TITLE     Purification and activation properties of UreD-UreF-urease
            apoprotein complexes
  JOURNAL   J Bacteriol 178 (18), 5417-5421 (1996)
   PUBMED   8808930
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Cobetia"
                     /db_xref="taxon:204286"
     Protein         1..233
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25313
     Region          24..233
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 mstdamaglp aqedlallgl lqlvspalpi gafawsqgle safelgwvtr eqelgewidg
       61 vledglgrce lpllvrlqqa waegdaaald ewdgwlkatr etaelsdeda rlgaallrll
      121 rsleleppva lmpqapgyvt vfawvahqrg vpprqtligf awawlenqla vackamplgh
      181 taaqrlteql rprvveivaq alerldgelg pilpglalas aqhetqysrl frs
//
LOCUS       WP_284727487             586 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Cobetia amphilecti].
ACCESSION   WP_284727487
VERSION     WP_284727487.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..586
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=63413
     Region          1..464
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mastapdldr qiahmddell pvprhklhrw phfaglyaae hvaatefvig atfvalgagi
       61 wdillgllig nglavlsfwl ittpiaietr lslftylhri agdsmsrlyn wanviiftai
      121 saamitvsat avrllfdipa qtqayptsfe fillalavaa ivvlvavygf naltefasic
      181 apwlmlmftv ggmvllpela esvtgetsln sfssfidvag stvftginsq geagigiwev
      241 igfswaantf shfglidmal lryakrmrsg latstgmmfg hyvawisagl mgaataavag
      301 isidvlepge valhalgaag fvivvvagwt tananlyrag laaqsampnl srnkatlavg
      361 icvavlscfp fvyrsmlpll tyaglvlvpv ggiifaehhl fpklgfsryw arykgvkhnt
      421 palatwalsl ifgfglemvd vipfyylflp twfvsiilyt lkarsagaad sypkaeaaer
      481 efqervealh akqaettnha pvkdtsgltk airavwmvlg lavpmvlalr vlfgspdlas
      541 yeanremfyd vtiwstiiyf ifaywelqrs kalfnkqspk qaatas
//
LOCUS       WP_284727385             209 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: TRAP transporter small permease [Cobetia].
ACCESSION   WP_284727385
VERSION     WP_284727385.1
KEYWORDS    RefSeq.
SOURCE      Cobetia
  ORGANISM  Cobetia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Cobetia"
                     /db_xref="taxon:204286"
     Protein         1..209
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22529
     Region          27..180
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 msshshtaka tfptesgegl tatadvtlld rvnrvvercl evftvgllls ltmivlaava
       61 lrtfggslpw ydevasinla wlsfygagla alkrshmgfp glitkapial rsslfitsel
      121 ivigffavvg wfgyqvldvl awdslialpt igldvtqsvi pisaalfilc ellslphawr
      181 kmcagvnsee eeiaeairla eqdlkehrs
//
LOCUS       WP_284727585             309 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Cobetia amphilecti].
ACCESSION   WP_284727585
VERSION     WP_284727585.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..309
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33414
     Region          11..296
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mnakvspqql eeveaalstv lagkprqirl alccllcrgh vliedlpglg kttlaqglar
       61 ligadmqrvq ftsdllpadi lgvsvfdpre gnfrfhpgpv fhslvladei nratpktqsa
      121 lleameerqv tvegetrrlp epffviatqn plqqsgtfpl pesqldrflm rlslgypepa
      181 aereilkgna grqhiealrp lllvsvlkew qaavdrvrls dplldylqal vaatrsspev
      241 ayglstrgvl alasaargwa llagrdyvlp edvqavwapv vghrlsegsv aegeavarhl
      301 lgqvavvpa
//
LOCUS       WP_284727648             227 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Cobetia amphilecti].
ACCESSION   WP_284727648
VERSION     WP_284727648.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..227
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=24360
     Region          73..217
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
     Region          131..168
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          173..199
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mlpsshpsfr visrccrvll sggmalgitl agmtgvhaap gdddifplsk rwaqinyqvs
       61 gdaqekgmea lgkevralad qypdnahvlt wegiilaswa kargglgald lakeakatle
      121 kaisldpkgd nasayvtlga lydkapgwpv gfgddekage vlrkglevnp tgmdtnyyya
      181 dylasegrde ealkharlaq dgpprpnrel adqelqkeia alikrlq
//
LOCUS       WP_284727762             382 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [Alphaproteobacteria].
ACCESSION   WP_284727762
VERSION     WP_284727762.1
KEYWORDS    RefSeq.
SOURCE      Alphaproteobacteria (a-proteobacteria)
  ORGANISM  Alphaproteobacteria
            Bacteria; Pseudomonadati; Pseudomonadota.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Alphaproteobacteria"
                     /db_xref="taxon:28211"
     Protein         1..382
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40582
     Region          23..101
                     /region_name="STAS_2"
                     /note="STAS domain; pfam13466"
                     /db_xref="CDD:433231"
     Region          165..377
                     /region_name="MlaE"
                     /note="Permease subunit MlaE of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG0767"
                     /db_xref="CDD:440530"
ORIGIN      
        1 mksvhpesaa idvedlhddg yrvrlsgawr nnslgvllrd ngqlfpanga ksleidlaav
       61 sdmdmagawl vrrfvtvrek eggkvtltgg tpamrellrv lpedvkrpap appkgpllqr
      121 lfspigkimv dlwfdivamm fvlgsavhga qtklgrgsgv spasvvaqmd hmgvravpiv
      181 almsfligai iaqqgafqlr yfgaeifvvd lvgilqlrei gvlltaimva grsgsaitae
      241 igsmkmreei dalkviglnp igvlvfprlv altivlpllt ilanfaalyg aalvawsysg
      301 itfdvfttrl heaidystva sgmikapfma livgivsave gmkvggsaes lgrhvtaavv
      361 ksifvvilvd alfaifysai df
//
LOCUS       WP_284727794             208 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Sphingomonas psychrolutea].
ACCESSION   WP_284727794
VERSION     WP_284727794.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas psychrolutea
  ORGANISM  Sphingomonas psychrolutea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Sphingomonas psychrolutea"
                     /db_xref="taxon:1259676"
     Protein         1..208
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=23136
     Region          11..208
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 miehskrslp eglryvpdli drrdqedlvt airdiavkap lfvpampgtg kemsvrmtnc
       61 gplgwvtdke rgyryqsthp vtgkpwpaip amllniwdrv sgcdkrpeac lvnfyddsar
      121 mslhqdrdek dfeapvvsvs lgntclfrvg gtsrkdptis lklrsgdvfi iggpgrlcfh
      181 gvdriypats tllknggrin ltlrrvnr
//
LOCUS       WP_284727809             487 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Sphingomonas psychrolutea].
ACCESSION   WP_284727809
VERSION     WP_284727809.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas psychrolutea
  ORGANISM  Sphingomonas psychrolutea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Sphingomonas psychrolutea"
                     /db_xref="taxon:1259676"
     Protein         1..487
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52770
     Region          2..487
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mfafdnsyrr lperffrpae pagaraprli rfntglaetl nldpaaasde tlaaifsgns
       61 lpegaaviam ayaghqfgnf vpqlgdgrai ligevmdrdg qrrdiqlkga gatpfsrngd
      121 graalgpvlr eylvseamha lkipttrala avmtgeavhr etklpgavlt rvaashirig
      181 tfqyfaargd veairtladh viarhypala gveqpylalf savatrqadl varwlsvgfi
      241 hgvmntdnma vsgetidfgp cafldeydpr kvfssidqrg ryafanqpgi aqwnlarfae
      301 tllplfggse eenveaanga laafgpvfqt fwldrfrakl giageaagdl dlvnsllklm
      361 eageadftrt fralgkvagg adigllatef tdptglddwl arwqqrgesd grtaearqve
      421 meavnpaiip rnhrieaaiq aglagdfsvf erlhaalqtp yvedpefvay qrkpetaerv
      481 ertfcgt
//
LOCUS       WP_284727811             335 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Sphingomonas psychrolutea].
ACCESSION   WP_284727811
VERSION     WP_284727811.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas psychrolutea
  ORGANISM  Sphingomonas psychrolutea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Sphingomonas psychrolutea"
                     /db_xref="taxon:1259676"
     Protein         1..335
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36108
     Region          24..324
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mmptpdaplg ekamieaaek aladiaavrq avskvifgqe qvventllai lssghallvg
       61 vpglaktklv ntlgtvlgld asriqftpdl mpsdilgtev mdqdengrrs frfvkgpvfa
      121 qllmadeinr asprtqsall qsmqeyqvti agrpydlpsp fhvlatqnpl eqegtyplpe
      181 aqldrfllqv dvgypelaae rqillettgi neqravgvvn aerlveiqkl irqmpvsdsv
      241 vdgilslvrs arpghgntet dktvswgpgp ragqalmlca raralyegrl apslddvhal
      301 aepvlqhrma ltfaaraegm svrdviaglv krarg
//
LOCUS       WP_284727843             491 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Sphingomonas
            psychrolutea].
ACCESSION   WP_284727843
VERSION     WP_284727843.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas psychrolutea
  ORGANISM  Sphingomonas psychrolutea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Sphingomonas psychrolutea"
                     /db_xref="taxon:1259676"
     Protein         1..491
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=52757
     Region          74..479
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mrhdnrqstp aaprirrraq rvaalasavf agasllglyg iagaqappps atappapvka
       61 pegqaespsd aedaalalrq krdevgkelq elarsmrvsd dkaaeleqsi sklsktsesi
      121 rsaliesagr rkdlerkiaa gekklaelgl kedairasfr grravlaevl aalermgrnp
      181 ppallvsped alasvrtail lgavvpgirh eteklaadla elvrlrlegq ketealvati
      241 asrqeeerhm dlllgendrl sqqnalelat ekrraealaa rassmeglia sleteirsvr
      301 eaaekaraee eklrklseeq rqkarelaas slpdknriap ayafsdlkhk lelptagetl
      361 rqfgdpdgtg heakgmvias apgslvtapa dawvvyagef rsygqmiiln tgdgyhvvls
      421 gmdristaqg kfvlsgepla vmgekrvasa talaletdrp tlyiefrkdg kpvdsrewwt
      481 gsgsgkaqnd s
//
LOCUS       WP_284727908             614 aa            linear   BCT 25-DEC-2024
DEFINITION  PHA/PHB synthase family protein [Sphingomonas psychrolutea].
ACCESSION   WP_284727908
VERSION     WP_284727908.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas psychrolutea
  ORGANISM  Sphingomonas psychrolutea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 614)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 614)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 614)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   4  (residues 1 to 614)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Sphingomonas psychrolutea"
                     /db_xref="taxon:1259676"
     Protein         1..614
                     /product="PHA/PHB synthase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=67861
     Region          66..612
                     /region_name="PhaC"
                     /note="Poly-beta-hydroxybutyrate synthase [Lipid transport
                     and metabolism]; COG3243"
                     /db_xref="CDD:442475"
ORIGIN      
        1 mtstgegaaq ggtkaagfdp slieayvvkd pqaltinvak alenlgkaas iwleprerge
       61 lvdpvsepma elvktmskva eywmsdpkrt leaqtqllag lfgmwtnsla rfsgeadapp
      121 appikdkrft dedwqrnpff dflrqayiil sdwaermvtq aegldehtrh kaefymrqit
      181 salspsnfvm tnpqlyretv ashganlvkg mhmlaediaa gggdlrirqt dtskfkvgen
      241 mavtpgkvia qsevceiiqy eaatdtvlkr pllicppwin kfyildlnpq ksfikwcveq
      301 ghtvfviswv npderhankd weayiregvd faldavekat getevnaigy cvggtllaaa
      361 lalhaqegnk riasatlftt qvdftyagdl kvfvdegqig siedrmkpsg yldgskmaaa
      421 fnmlraseli wpyfvnnylk gqdpmpfdll ywnsdstrma aanhsfylrn cylnntlsqg
      481 kmqlagktls lkdikipiyn latredhiap aksvfvgssl fggpveyvls gsghiagvvn
      541 ppdkqkyqyw tngavkgsye dwvagaketp gswwphwqrw ieamddarvp arkpggealn
      601 aiadapgsyv larv
//
LOCUS       WP_284727914             762 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-mannosidase [Sphingomonas psychrolutea].
ACCESSION   WP_284727914
VERSION     WP_284727914.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas psychrolutea
  ORGANISM  Sphingomonas psychrolutea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 762)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 762)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 762)
  AUTHORS   Nascimento,A.S., Muniz,J.R., Aparicio,R., Golubev,A.M. and
            Polikarpov,I.
  TITLE     Insights into the structure and function of fungal
            beta-mannosidases from glycoside hydrolase family 2 based on
            multiple crystal structures of the Trichoderma harzianum enzyme
  JOURNAL   FEBS J 281 (18), 4165-4178 (2014)
   PUBMED   24975648
REFERENCE   4  (residues 1 to 762)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 762)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14312040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..762
                     /organism="Sphingomonas psychrolutea"
                     /db_xref="taxon:1259676"
     Protein         1..762
                     /product="beta-mannosidase"
                     /EC_number="3.2.1.25"
                     /GO_function="GO:0004567 - beta-mannosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005537 - D-mannose binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=85512
     Region          12..601
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          681..755
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; pfam17753"
                     /db_xref="CDD:465483"
ORIGIN      
        1 mggrarldgg afllpqphce gswyldidyl dtvavvfind vpvlsadncf rryrpdvsta
       61 lqpgenriri lfhssiaaga drqarqpfyi pystnnspia ngnmlrkpqc hfgwdwniav
      121 aplglygtia lkkldparie hleteqvhhd dgsvdlhvrl tlyafepsvv pvhfefdgvr
      181 erldcgipag etviahvfhi drprlwwpag sgeqalytls adipgetltr riglrtiali
      241 tdpdeagsrf afkvngreif crganwipad alfsrtslek tedllqsava ahmnmirvwg
      301 ggfyeqdyfy dlcdrlglmv wqdfmfacnl ypctedflan vaqevdyqvr rlsshpsial
      361 wcgdnelvga ltwfkesrdn rdrylvaydr lnrvieqgvr kaypqalwwp sspasgyldy
      421 gdawhadgsg dmhywsvwhe nksfanyrti kprfcsefgf qsytsmpvie tfadrgdmni
      481 aspvielhqk naggneriag tmfryfrfpk dfanfvylsq iqqglaigta vdywrslkph
      541 cmgtlywqln dtwpvaswss ldyggswkal hymarrffqp vnvvaipsed gtsiafsmvn
      601 dtleeltidm nlfavtldge rlpirtatgt cppdraaell sideteipvd allawsfias
      661 ngmsgeghla lqpykalelq psgletsvap ladgrfeitv satglalfvm leadcpgrls
      721 dnafdlhagi srriiftptt plaegdvpqf riydlqssqq lg
//
LOCUS       WP_284728062             279 aa            linear   BCT 25-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Cobetia marina].
ACCESSION   WP_284728062
VERSION     WP_284728062.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..279
                     /product="isopenicillin N synthase family dioxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31137
     Region          7..279
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 mkvqnvdyrs adaaekfves lrttgfgvir nhpishelve kiyaewaeff asadklewry
       61 dpktqdglfp advsetakgh tardlkeyyh iypwgkipds lranameyyr qaeafaaell
      121 swveahspae vaelyrepls nmikdsgqtl lrvlhyppmt gseepgavra aahedinllt
      181 vlpaanepgl qvmdvdgewm dvpcdpgqlv invgdmlqea sggyfpstth rvinptgegc
      241 sqsrlslplf lhprpqvvls dkhtadsylk erlrelgvi
//
LOCUS       WP_284728199             586 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Cobetia marina].
ACCESSION   WP_284728199
VERSION     WP_284728199.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..586
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=63419
     Region          1..464
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mastapdldr qiahmddell pvprhklhrw phfaglyaae hvaatefvig atfvalgagi
       61 wdillgllig nglavlsfwl ittpiaietr lslftylhri agdsmsrlyn wanviiftai
      121 saamitvsat avrllfdipa qtqayptsfe fillalavaa ivvlvavygf naltefasic
      181 apwlmlmftv gglvllpela esvtgntsld sfssfievag stvftginsq geagigiwev
      241 igfswaantf shfglidmal lryakrmrsg latstgmmfg hyvawisagl mgaataavag
      301 isidvlepge valhalgaag fvivvvagwt tananlyrag laaqsampnl srnkatlavg
      361 icvavlscfp fvyrsmlpll tyaglvlvpv ggiifaehhl fpklgfsryw arykgvkhnt
      421 palatwalsl ifgfglemvd vipfyylflp twfvsiilyt lmaksagaae sypeaeatek
      481 hfqervdafh akqadttnha pvkdtsgltk viraiwmvig lviplvlalr vlfgspdlas
      541 yeanrelfyd vtiwstiiyf ifaywelqrs kalfnkqspk qaatag
//
LOCUS       WP_284728243             224 aa            linear   BCT 25-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Cobetia marina].
ACCESSION   WP_284728243
VERSION     WP_284728243.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..224
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24349
     Region          8..205
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 msrkvfqrls qdqrrrdlle atlscvaqhg lagasvrrva eaagvspgli rhhfgtkddm
       61 vraayaymmg qltsdiadas pasdessacr larfiaaslt qpnlaahkvs lwatfigrvr
      121 hdatysavhq etyrefldll rlliqpvlsa ndlpaddaic eeqaialngl idglwleggl
      181 ehglyaverl paiairaaeg ilrlphgtll ehvemtttpp phrs
//
LOCUS       WP_284728343             373 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Cobetia marina].
ACCESSION   WP_284728343
VERSION     WP_284728343.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..373
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42104
     Region          47..>178
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mlaelsysqa qgtpvtggal eegpipvppa padeatimad wegnlstprv svmcfafnhg
       61 dyiamaldgf lmqrtrfpfe ivvhddastd gtreiieeya arypsiirpi lqdvnqysqh
      121 vwpitfcmpv mrgdiiayce gddywvkadk larqvalfda npratvcfhp aieydehrde
      181 hsiicryads varlspeaii glrggsipsp altfrrvesh vdamlesyrg apimdfflqa
      241 ymallgetly yedaacvyrr nakgswtsqq qdheveqryq rdmlaaidtf ygatrtlpea
      301 dtlyiplyhy fkqyvmapgt tqqrlanfrr glgylhhmqr nkvlslvrrd mfskltrrka
      361 atpgqakdte aaa
//
LOCUS       WP_284728347             448 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Cobetia marina].
ACCESSION   WP_284728347
VERSION     WP_284728347.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..448
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=48923
     Region          1..440
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mkitvfgtgy vglvtgtcla dvghdvicmd vdaakierlk lgeipifepg lesmvarnve
       61 agrlnfttda reavahgvlq fiavgtppde dgsadlkyvl avagtigehm ddykviidks
      121 tvpvgtadrv harvaevlkh rgvsvafdvc snpeflkega aledftrgar ivvgtdseav
      181 rermrecyap ynrnheklmf mdvraaeltk yaanamlatk isfmneisnl aerlgadiee
      241 vrrgigsdpr igyhfiypgc gyggscfpkd vqalartasq igyeaellta vesvnkrqkv
      301 tlfeklsraf dgdlagktia vwglafkpnt ddmrdapsrt lmealwaaga kvqaydpesm
      361 retrriyger ddlvlvadri qavkgadalv ictewkefrt ldagwlktql afpvvvdgrn
      421 lfepsamksa glmyyavgrg dtlaltrd
//
LOCUS       WP_284728365             363 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Cobetia marina].
ACCESSION   WP_284728365
VERSION     WP_284728365.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 363)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..363
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38180
     Region          65..359
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mpdsltspvt spiadwrrrk rhgalwlwts glavlaacll disqgsgelp larllpalwq
       61 saandplaha ilwqlrlpia lmavtvgasl amagaqmqtl lhnpladpft lgvsaaasvg
      121 aglglilhld lvqlvlpswq slagaglgvt lnaflfalga slvlwsaqrl pgvgvqtlvl
      181 lgialmfffn allgvlqfva spealqqlif wsmgslerss wsrlavlslv ialcavvfhr
      241 rrseltalsl geaqaralgv dvrrlrlsgl mctalltata vsfvgsvgfi glvaphiarl
      301 lvgeqqqrll plsaligall lsltsilsrs lipgvllplg mitaliglpf fvsltlkrrg
      361 hdg
//
LOCUS       WP_284725670             292 aa            linear   BCT 25-DEC-2024
DEFINITION  endonuclease I family protein [Bacillus aerius].
ACCESSION   WP_284725670
VERSION     WP_284725670.1
KEYWORDS    RefSeq.
SOURCE      Bacillus aerius
  ORGANISM  Bacillus aerius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Bacillus aerius"
                     /db_xref="taxon:293388"
     Protein         1..292
                     /product="endonuclease I family protein"
                     /calculated_mol_wt=32475
     Region          104..291
                     /region_name="EndA"
                     /note="Endonuclease I [Replication, recombination and
                     repair]; COG2356"
                     /db_xref="CDD:441923"
ORIGIN      
        1 mkrslfgtva agimifgtfa aplppaanaq gftlnepsqt itfsplqlqt etsaqhaktt
       61 assqmdsyyq saagksgpal kkalhdiidd htqlsysqvw dalkktdedp knpnnvllly
      121 sgisrskqan ggnvgqwnre hvwakshgnf gtsqgpgtdl hhlratdvqt nstrgnldfd
      181 iggneykgap gnfydsdsfe phsrvkgdva rmlfymavry egddrfpdle lnnkvnngsa
      241 plhgkmsvll kwhkqdpvdq iernrneiiy qtyqhnrnpf idhpewvsdi we
//
LOCUS       WP_284728373             329 aa            linear   BCT 25-DEC-2024
DEFINITION  YeiH family protein [Cobetia marina].
ACCESSION   WP_284728373
VERSION     WP_284728373.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..329
                     /product="YeiH family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=34396
     Region          4..310
                     /region_name="YeiH"
                     /note="Uncharacterized membrane protein YadS, UPF0324
                     family [Function unknown]; COG2855"
                     /db_xref="CDD:442103"
ORIGIN      
        1 mriimpglli cilialattf iadhyggptl lyallfgmsl hflsedgpck agiefasktv
       61 lrigvallgv ritleqvasl gvgpvitvvl gvvativfga llarvmgldr dmglltggsv
      121 aicgasaala lsavmprnat serhtimtvv gvttlstvam ityplivrll gledteagif
      181 lggtihdvaq vvgagyiise htgdvstfvk llrvamlvpa vmvfmllfrs arqangdegg
      241 kvpmfptflv afvalvlins lgwvpsvave gftdlsrwcl vaaiaalgvk tsfqklavvg
      301 wkpvilmvve tlfllvlvtl cikfglasv
//
LOCUS       WP_284728391             295 aa            linear   BCT 25-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Cobetia marina].
ACCESSION   WP_284728391
VERSION     WP_284728391.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..295
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31627
     Region          35..261
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mptpprsaag ghprastssp tsatasesst tarvdvaewl aqaifenryp pgslipreld
       61 lcdqhaqsra tvrtaiqslv nagiltrttg qgtrvnplse whlldprvtg wmtryamphp
      121 qlardiyafr isiepfvaal aateataqdl saieqaydgm aaavhggsam eefdradiaf
      181 hdaifaathn viwaqlghvl kpsisllvat snhnaselgd slgrhravme airlrqpeaa
      241 haatlhvldr tgrdlglamp evadgphgig raqeplellr rfgqlpslsv plsre
//
LOCUS       WP_284728429             464 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Cobetia marina].
ACCESSION   WP_284728429
VERSION     WP_284728429.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..464
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50452
     Region          38..366
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mesadrsnnp prkeviiiga gpagaaaaaw laraghavrv lershfprfs igesllprcm
       61 qhleacglme aaaaggyqrk tgaaftrrge hrvidfrdkf segpgttwqv eradfdqrli
      121 egaraagaev efgvtvtgft parptqsdta ghaqgprltl tdgrelhaaf vldasgygrv
      181 larlealerd prleprmalf ghvhdgiadl appaegyrrd tiliashplh pdvwywlipf
      241 angraslgvv gpreliepaa eddaqtrlwq wvmeeprlae llrdatpana vqslggysad
      301 vsrlhgpgya llgnagefld pvfssgvtia lesalraapl vareltatrd eqrpdwasey
      361 elplrrgiev frefvtawyd srltdiiyhp rspdrirqmi ssvlagyawd eanpfvsasr
      421 rrltalatls aaqepqaetc epaasalsta gtrqndarkg kvss
//
LOCUS       WP_284728446             586 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Cobetia marina].
ACCESSION   WP_284728446
VERSION     WP_284728446.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 586)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..586
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62644
     Region          50..577
                     /region_name="YnjC"
                     /note="ABC-type uncharacterized transport system YnjBCD,
                     permease component [General function prediction only];
                     COG4135"
                     /db_xref="CDD:443310"
ORIGIN      
        1 mgatlsqltq wlaerwraer pagrlaltpa rllrwavlll llgptalgla glvapafglw
       61 palgfeevsa iawqrwwalp gladglrltl vsgiggtlla vlltmgwlaa aagtrfgerl
      121 erllapvlam phlalalgll wlaapsgvlm rlllapfevl vppqyplpda hgitlalgla
      181 lkeapflmlm aqtalsrlpv taqlqagqal gysipqlrwr ilmpqvmrai alpigavlay
      241 slavvdvaqv lgptrtptla vrlvelwrds dpssrlpasv galllallvi vvmalgaavg
      301 ryllnrhrdw vldnpapraa vrpgrkgqrg rvirvllgtv tavsllafav iavqslarsw
      361 ffpsllparw gleswqqals glggafsnsl wlavlvatla vmlsvavfer erevgrlrgf
      421 vvclylplll pqasflfgfq vgwlslgadp gwvgvvighl lfalpyawlt lagpwarfdv
      481 rleqaarllg rsrlevligi rlrlmlrpla iswavafavs iaqyvptvvl gggrvptltt
      541 etlalatgad prltavaacl qaclpllifl laravpagra lapirg
//
LOCUS       WP_284728470             397 aa            linear   BCT 25-DEC-2024
DEFINITION  PLP-dependent cysteine synthase family protein [Cobetia marina].
ACCESSION   WP_284728470
VERSION     WP_284728470.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..397
                     /product="PLP-dependent cysteine synthase family protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42530
     Region          51..371
                     /region_name="CysK"
                     /note="Cysteine synthase [Amino acid transport and
                     metabolism]; COG0031"
                     /db_xref="CDD:439802"
ORIGIN      
        1 mpttafpprs pcapsslatp segllhrapl eawrqeclaq ltalkaatpv tplrelalcg
       61 lgearvlikd erahasgslk hrlamalfeq alkqgwlspg rpvidassgs tavseawlar
      121 rlglefiavv pkgtacdklk airdeggrvv eienaahlcq saqalaedsg ghflnqfqha
      181 atasdwqset slpgeclaqi aerelpelea vflgagtggs aatfarhlrh kgllrhsgpl
      241 hhrghgarvi gvdpehsvyh acwqhhhthg trmtslpapq apnpiegigr pcvleafdpa
      301 hfddyrriad arsqaaalwl aehaglavgp stgtafagll etlelkharg ealtgswlll
      361 acdhasryas tlgdpvwrae hqprlaphra wierlta
//
LOCUS       WP_284728545             159 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY domain-containing protein [Cobetia marina].
ACCESSION   WP_284728545
VERSION     WP_284728545.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..159
                     /product="PepSY domain-containing protein"
                     /calculated_mol_wt=17220
     Region          61..122
                     /region_name="YkoI"
                     /note="PepSY domain containing protein, regulator of
                     zincin peptidase activity [Posttranslational modification,
                     protein turnover, chaperones]; COG3212"
                     /db_xref="CDD:442445"
ORIGIN      
        1 mptprkaqtg asasrvsqwr qrygwlclgl gglligvlam pphalcdser wrslhdevaa
       61 grvislsell dslerdwlgq vveveledih geliyeveml gpqgqmakft vraadgelre
      121 vrgvnldamr rhaaespagp spslserqpt gglegaedp
//
LOCUS       WP_284728665             422 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Cobetia marina].
ACCESSION   WP_284728665
VERSION     WP_284728665.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..422
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=48058
     Region          45..410
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mekgahggmt aligrlegel anttstaavt qsgdaalika qtdieavaaw lneyrhspqt
       61 lrayrkeaer lllwlraege qgrgaalasl drerlehfea flanpqpaev wigsvrarrh
      121 pewrpfrgpl apasrrqslv ilqglyawli eagylarnpf rlmrdkrrmd nrtlrieryl
      181 erplwdwlwg riearcdavr chvptagsas lerevsrerf iaerqrflfa faylmapria
      241 emaaarmgdi ikregqwwwr vigkgaklae iplpppmlea lvrwrrlrgl sdlpqalpad
      301 eslpllarld gttplgdnql yrlikqtftq aahdmrqqte rpgdaselma rtldqasphw
      361 lrhtaithqa qagvelrfls rsarhsrldt tsrylhaedg ewqqqmarhs latttatpee
      421 ea
//
LOCUS       WP_284728679             265 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Cobetia marina].
ACCESSION   WP_284728679
VERSION     WP_284728679.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..265
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28370
     Region          21..265
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mtrtasphte lpafadfryp dlagasvfit gggsgigaal tegflaqgak vafvglsdas
       61 efcdameary anrplfircd iqdiealqaa vaqareahgp igvlvnnaar dtrhtleewt
      121 veqwdesiat nlrpqfftaq avaadmralg ggaiinlssn symlglggyp tyvtakagim
      181 gltkalarel gpdairvncl ipgwvmterq relwvndkdl necidqqclk eaipvedmin
      241 pclflastas rmmtgqpmvv dggrv
//
LOCUS       WP_284728726             519 aa            linear   BCT 25-DEC-2024
DEFINITION  malonate--CoA ligase [Cobetia marina].
ACCESSION   WP_284728726
VERSION     WP_284728726.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Pohl,N.L., Hans,M., Lee,H.Y., Kim,Y.S., Cane,D.E. and Khosla,C.
  TITLE     Remarkably broad substrate tolerance of malonyl-CoA synthetase, an
            enzyme capable of intracellular synthesis of polyketide precursors
  JOURNAL   J Am Chem Soc 123 (24), 5822-5823 (2001)
   PUBMED   11403625
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11482749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..519
                     /product="malonate--CoA ligase"
                     /EC_number="6.2.1.76"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0090409 - malonyl-CoA synthetase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0090410 - malonate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56741
     Region          7..511
                     /region_name="PRK07514"
                     /note="malonyl-CoA synthase; Validated"
                     /db_xref="CDD:181011"
     Site            order(166,169..174,176..177)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341264"
     Site            order(169,209..210,213..215,255,257,261,283..285,304..309,
                     313,328,388,400,408,411,414,443,481)
                     /site_type="active"
                     /db_xref="CDD:341264"
     Site            order(169,283..285,304..309,328,388,400,408,414)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341264"
     Site            order(209..210,213..215,255,257,261,283,305,307..309,313,
                     411..413,443,481)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341264"
ORIGIN      
        1 mphanhdnly lqfarnfder pdatfldtve ghgytfaear saagqmatal relgvtpgdr
       61 vavqidksce tvilylaclq vgavylplnt aytgeeiryf lgdagphlyv cqpkvletar
      121 algkecdvpr veslgteqdg tlmeqarqcs asseiepraa ddlaailyts gttgrskgam
      181 lthanlasnc qalaetwrft rddhlihalp ifhthglfva cnivltvgas mtflpkfdae
      241 qildlmarss vlmgvptfyt rlleserlnr ettagmrlfv sgsapllset hsefsartgh
      301 ailerygmte tnmntsnpyd gerrpgtvgm alpgsevrit dretgatlpr getglievrg
      361 anvfkgywkm pektasefre dgffitgdlg hidadgylci sgrdkdliis ggyniypkev
      421 elliddmpgv nesavfgvph pdfgegvcav vvmqaghqgs ldeaavltal sdklarykqp
      481 krvffieslp rnvmgkvqkk qlreeyaqlf apeparshg
//
LOCUS       WP_284728727             297 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Cobetia marina].
ACCESSION   WP_284728727
VERSION     WP_284728727.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..297
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32118
     Region          23..293
                     /region_name="YbbA"
                     /note="Predicted hydrolase of the alpha/beta superfamily
                     [General function prediction only]; COG2819"
                     /db_xref="CDD:442067"
ORIGIN      
        1 mvltsgails paaamgdtge sevlqgttta ftqhsaatgq eyliqvalpq vappqegypv
       61 llvldgnrhl dlftaardil grrgfdkaps dlaivavgya gsggrgpdra fiskarfkdf
      121 tpplttgtap egtgggedfl ayltqvllpe ltsrypldle rpalvghslg glfalhaqqk
      181 apeafgaifa ispslwwrqe ndpaswplrl acseaagpvy iaaggreqsp qprrqdperd
      241 rlrvqramid naheharqlr ehcpqaavqw rlfegedhgs vmwpaarsvm erlmrpr
//
LOCUS       WP_284728796             211 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II [Cobetia marina].
ACCESSION   WP_284728796
VERSION     WP_284728796.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..211
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22782
     Region          14..202
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 mqaftsqdps aprvlmidnf dsftynivqy lselgaevlt vrndaitleq iealgathlv
       61 lgpgpctpne agitldvirh fagklpilgv clghqaigqv yggkvvrapq vmhgktsavh
      121 hdnsgvfaal aeplevtryh slvverdslp eclvvtswtg dddvtpqlim glrhreldve
      181 gvqfhpesil tlqghellan flcrgeveka a
//
LOCUS       WP_284728811             430 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Cobetia marina].
ACCESSION   WP_284728811
VERSION     WP_284728811.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..430
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46114
     Region          31..397
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 msattplepa aswyaasana aperpplsge vscdvcvvga gftgisaalh laeqglkvmv
       61 leaacvgyga sgrnggqivn sysrdmdvie arfgartaqa lgdmafegnr iirdriadya
      121 idcdlrdgnl faacnarqlk glkehkalwe rygntslell egdayqrevs aegytgalvd
      181 hsgghlhpln lvlgeaaafe slggvifehs plvslehgsp vvlrtaagai raervvmagn
      241 aylhgvlpel egksmpcgtq iiatepladd vargllpngm avedcnylld yyrltrdnrl
      301 lfgggvnygg edpadiesli rpkllkvfpq lasvridyaw sgtflmtlnr lpqfgvlndn
      361 vyyaqgysgh gvtcshlagr lisevmrgre grfdafanlp hlpfpggrll rvplsavgaw
      421 yyqtrdrlgl
//
LOCUS       WP_284728827             519 aa            linear   BCT 25-DEC-2024
DEFINITION  PhnE/PtxC family ABC transporter permease [Cobetia marina].
ACCESSION   WP_284728827
VERSION     WP_284728827.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 519)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..519
                     /product="PhnE/PtxC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57196
     Region          56..248
                     /region_name="PhnE"
                     /note="ABC-type phosphate/phosphonate transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG3639"
                     /db_xref="CDD:442856"
     Region          <343..507
                     /region_name="PhnE"
                     /note="ABC-type phosphate/phosphonate transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG3639"
                     /db_xref="CDD:442856"
ORIGIN      
        1 mstepglals rlrkpprwwq arsegshllr lgigllaaml ilapfgdlsi tsrepwqelg
       61 rmlnglvmpa psalespvha liltvafalw gtllgallgl plallysrsr alravcaglr
      121 avhelfwall llqvfglsai talaaitipy aatfakvyae ileqvpqapr ralpattsrl
      181 mcfvyaelpl awsrlasytr yrfecalras vllgfvglpt lgfylesafr egryheagal
      241 lwifylliat lpwwghrrll pllgvaslww lgpwpdvnpt llwrflshdi wpaplvnasv
      301 dslisgqlla dlldwashlp hllsalgntl llgllgtags lliamllwpl asrhvgnras
      361 rqatqglmif lrttpelmla filllllgps llpawlalsl hngaiiaflc arhanqiqlp
      421 pgkprgrles wlyeinprva pgmfallfyr aetiiretai lgmlgvatlg fhidssfeyl
      481 mfdqafalll ltailnivvd svarrlrpth eiaedscvr
//
LOCUS       WP_284728844             445 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Cobetia marina].
ACCESSION   WP_284728844
VERSION     WP_284728844.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..445
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=47073
     Region          17..433
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mptrsrsrtr ssagasfahl ddllarreqv gryrrrltld spqgphvsla gqaageevrp
       61 llnftandyl glanhpalve agcraahefg vgsgsahlvn ghqtlhhrle arlaeltgrp
      121 rallfstgfm anlgvidala sasreagrtl eifhdrlnha slldgarlas sgnsavrsrr
      181 fhhrdledle rhlarsqadd rlvisdgvfs mdgdcaditg laracarhga wlmiddahgv
      241 gvlgehgegl vgrdtplaev pvlvgtlgka lgsagafvag sealiesliq larpyiytta
      301 qpphvaaatl aaldiveqep qrrehlaarv rqfregcaal lagsglalgl ppvtagapsl
      361 ltdpmtpiqp lilgsetral awsaalrerg ilvsairppt vpagssrlrf tfsaahsend
      421 vetllaalre vlessttrpt tgaet
//
LOCUS       WP_284728928             242 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Cobetia marina].
ACCESSION   WP_284728928
VERSION     WP_284728928.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..242
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26494
     Region          1..227
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mkqlifdcdg vlvdseiiad gvlkeklplw lpdlgtseqi eheldrclgm mtrdilvdle
       61 grsqhrlpad aleqvrlevd qrlangleam pgvvktlewi rdqrlplavv snssasrmki
      121 nlessglrgi ldeiaaangd relpiftsdd vinpkpapdl yllalktlgr saeeclvved
      181 srtgmqaava aglkvvghlg ashippghae vlrdtgawql ikhwkefper creaghqvqe
      241 pa
//
LOCUS       WP_284728939             436 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Cobetia marina].
ACCESSION   WP_284728939
VERSION     WP_284728939.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..436
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=46904
     Region          198..431
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 malslgaskt gkapasqgia hrldvqrarg cradaetpvr paaipppdlr drhhldaitl
       61 riatcadlee alpsvlrell dmlngcpesg mahssigelc vvhrapgqat havispagia
      121 lsaaarqrlq evvrdigrdp garqqasgia gtpggvlial tdatdsgetg rgatgddwlw
      181 lgepaapaps retplahavi dalsrglalq qqqqarhaed rqaavaqalk nerrqlaael
      241 hdtlaqelsy lqmqsarltr aarhapqevq alaeevhtqa rrafrqtrel ingthatwgd
      301 aplacvleal ieefetrssm vfeldnriqs lhlpdaqslq vvfivreamt nsvrharath
      361 lrlqllyqss gpqpaarvll tiedngcgfd paeipaahfg lgimqdrarh lgadfaitqp
      421 rqggtrvtls werrdt
//
LOCUS       WP_284729088             124 aa            linear   BCT 25-DEC-2024
DEFINITION  Rieske (2Fe-2S) protein [Cobetia marina].
ACCESSION   WP_284729088
VERSION     WP_284729088.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..124
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=13669
     Region          <25..109
                     /region_name="NirD"
                     /note="Ferredoxin subunit of nitrite reductase or a
                     ring-hydroxylating dioxygenase [Inorganic ion transport
                     and metabolism, Secondary metabolites biosynthesis,
                     transport and catabolism]; COG2146"
                     /db_xref="CDD:441749"
ORIGIN      
        1 mtrrllrlpl pelrigcslp irledgrpam lirladglha yldacphrgs rliadpahdk
       61 rehrdpylda tgglilchrh qacfepqqgl clsgpctgqr ltaldvtieq pdgspaqlvl
      121 kswh
//
LOCUS       WP_284729184             171 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Cobetia marina].
ACCESSION   WP_284729184
VERSION     WP_284729184.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..171
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19052
     Region          27..164
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mtdvqasetv igntaplret cegwalpspf llpiavsvea ldgyghvnna eyvrwleris
       61 wahsealglg lehyraqdrg mvvhrheidy lasarladsl mlatwlvacd grlsltrrfq
      121 lrrcsdgltl leartrfvci elssgrarrm peayrecysa alvsedaasq r
//
LOCUS       WP_284729222             281 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Cobetia marina].
ACCESSION   WP_284729222
VERSION     WP_284729222.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..281
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31107
     Region          8..278
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mtdasptple slvtllglet leenlfrghs qdlgfpqlfg gqvlgqalsa atrtvpserk
       61 vhslhgyflr pgdahkpvvy qvdgvrdggs fttrrisaiq ngktiffcsa sfhgkeegft
      121 hqlgmpdies peqlieqgar ieryeghpie flrmkapatt segassappr qrlwfrlsge
      181 lpeddalhry lltyssdfnl latalgghgv rfgspelqma sldhslwfhq dvrvndwlly
      241 emdspwagga rsfsrgslyn rhgelvassa qegltrlrrr s
//
LOCUS       WP_284729357             546 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF2345 domain-containing protein, partial [Cobetia marina].
ACCESSION   WP_284729357
VERSION     WP_284729357.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         <1..546
                     /product="DUF2345 domain-containing protein"
     Region          <1..535
                     /region_name="COG4253"
                     /note="Uncharacterized conserved protein, DUF2345 family
                     [Function unknown]"
                     /db_xref="CDD:443395"
ORIGIN      
        1 lqarmaearq ahglnesahe dyadvgtgqy lidfesqrls qpyrpsldhp rpnlggpqta
       61 ivvgpeneei htdslnrvrv qfhwdrsekg aadascwlrv aqpnagagwg svfvprigqe
      121 vivdflegdv drplitgrvy ngdqtpqwhs ngllsglksk tyrgnkynel vfddatdqer
      181 vrlnseheks qlnlgylihq qgntrgsfrg tgfelrsday gairansglm lsswgqiaas
      241 geqldlspah qqlasayqla ntlsdsatsh naealaartq ikqasddtqg tygaddsgsr
      301 fdgssaqsat nggrgqaarl napwlhltsp agiatstpes thlaqgrsls vtsgedinla
      361 tgrslvgavv ekfslfvqrs giklfagkgk vevqaqsdam dltaekdvti tstendidin
      421 aakeilltcg gayvrlkggn ielhapgkid vkgaqhsfgg ptslstafds lpeskgpyeq
      481 yftlrdkrte kalpyasyrv etaegdiieg radsegrtqk iltlkpeklk atildrfdda
      541 aegnls
//
LOCUS       WP_284729387             236 aa            linear   BCT 25-DEC-2024
DEFINITION  ESPR domain-containing protein, partial [Escherichia coli].
ACCESSION   WP_284729387
VERSION     WP_284729387.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10585893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>236
                     /product="ESPR domain-containing protein"
     Region          1..>33
                     /region_name="ESPR"
                     /note="Extended Signal Peptide of Type V secretion system;
                     pfam13018"
                     /db_xref="CDD:463773"
     Region          64..>203
                     /region_name="Peptidase_S6"
                     /note="Immunoglobulin A1 protease; pfam02395"
                     /db_xref="CDD:396804"
ORIGIN      
        1 mnkiyalkyc yitntvkvvs elarrvckgs trrgkrlsvl tslalsallp tvagastvgg
       61 nnpyqtyrdf aenkgqfqag atnipifnnk gelvghldka pmvdfssvnv ssnpgvatli
      121 npqyiasvkh nkgyqsvsfg dgqnsyhivd rnehsssdlh tprldklvte vapatvtsss
      181 tadilnpsky safyragsgs qyiqdsqgkr hwvtggygyl tggilptsff yhgsdg
//
LOCUS       WP_284729751             255 aa            linear   BCT 25-DEC-2024
DEFINITION  ESPR domain-containing protein, partial [Escherichia coli].
ACCESSION   WP_284729751
VERSION     WP_284729751.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10585893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>255
                     /product="ESPR domain-containing protein"
     Region          1..>33
                     /region_name="ESPR"
                     /note="Extended Signal Peptide of Type V secretion system;
                     pfam13018"
                     /db_xref="CDD:463773"
     Region          64..>203
                     /region_name="Peptidase_S6"
                     /note="Immunoglobulin A1 protease; pfam02395"
                     /db_xref="CDD:396804"
ORIGIN      
        1 mnkiyalkyc yitntvkvvs elarrvckgs trrgkrlsvl tslalsallp tvagastvgg
       61 nnpyqtyrdf aenkgqfqag atnipifnnk gelvghldka pmvdfssvnv ssnpgvatli
      121 npqyiasvkh nkgyqsvsfg dgqnsyhivd rnehsssdlh tprldklvte vapatvtsss
      181 tadilnpsky safyragsgs qyiqdsqgkr hwvtggygyl tggilptsff yhgsdgiqly
      241 mggnihdhsi lpsfg
//
LOCUS       WP_284731143             467 aa            linear   BCT 25-DEC-2024
DEFINITION  IucA/IucC family protein, partial [Curtobacterium flaccumfaciens].
ACCESSION   WP_284731143
VERSION     WP_284731143.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium flaccumfaciens
  ORGANISM  Curtobacterium flaccumfaciens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Curtobacterium flaccumfaciens"
                     /db_xref="taxon:2035"
     Protein         <1..467
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
     Region          <18..465
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 tggagaagsa gsvedvvasf qdveaamteg hpafvaangr igfgldeyrt fapesggrfr
       61 yrwlaarreh thlalaadrt eqahweaels pavvagfraa lerrgldpdd yvwlpvhpwq
      121 wqhriavtfa pdlgrqdlvd lgegpdeyqp qqsirtafnr teparsyvkt alavqnmgfl
      181 rgmspaymrn tpavndwves ivsadpalaa agfsvlreha aigytgdayh rvdvsspqrk
      241 mlaalwresp lprvtdgerl ltmaallhrd aagnavvsal ieasglpadv wvrrwldayl
      301 lpvvhcltvh dlvfmphgen lvlvvrdgvv vravmkdige eaavlgrhdd rpvpadidri
      361 vhpvsddeaa lavftdvfdg vlrfvaaild ddavlpesrf wqvvgecida haaahpdrrr
      421 pldlrvptfe hsclnrlqlr ntlsmvdlad qsasliraga manpigr
//
LOCUS       WP_284729302             297 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfurtransferase [Cobetia marina].
ACCESSION   WP_284729302
VERSION     WP_284729302.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..297
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=32718
     Region          35..296
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mspsssqsts ydptasasfs seqnllpliv epaqllplld hpdivivdvp lkaeshashv
       61 pgarlldfkr lvgsnedeip gvpspqalsd imselgitrd shvvayddeg ggwagrllwt
      121 lallghtrfs ylngglhawq geglalseaa sewqaseyha ayvdtsvmat redilerlst
      181 eapegkvvvw darsleeyrg ekgqnarlgh ipgavhfewt eamdrerdlr irdyaelite
      241 lgargispeq hvvthcqshh rsgltwlvgr algfediray pgswkewgnr edtpier
//
LOCUS       WP_284731549             387 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Planktothrix agardhii].
ACCESSION   WP_284731549
VERSION     WP_284731549.1
KEYWORDS    RefSeq.
SOURCE      Planktothrix agardhii
  ORGANISM  Planktothrix agardhii
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae;
            Planktothrix.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Planktothrix agardhii"
                     /db_xref="taxon:1160"
     Protein         1..>387
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          1..368
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mllgfktqlk vnkqqrllla qhagvarhaw nqglglceqv lihnklnpdd kikfptaidl
       61 hkwlvaavks ihpwyydvsk capqyalryl sdafqsffkk vkgfpnfkkk grhdsftldg
      121 avhidhrkvk vpiigwikty ellpfgykpk svtiskqadk wfiswkieve tsqtpkkqef
      181 vgvdlginhl atlsttevfd gaksykkyeh klarmqylnr hkqvgsnnsr kaqikiarlh
      241 qkianirkdt lhkittyisk nhavigiedl nvsgmlangk lskaiadmgf yefrrqleyk
      301 tqlygsklvi vdrfypsskt csscgekkls lslsqrvfqc nncgfecdrd lnaainlkqe
      361 aarlvvlacg ldsadtsrwk qeekadn
//
LOCUS       WP_284731789             502 aa            linear   BCT 25-DEC-2024
DEFINITION  IucA/IucC family protein, partial [Curtobacterium flaccumfaciens].
ACCESSION   WP_284731789
VERSION     WP_284731789.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium flaccumfaciens
  ORGANISM  Curtobacterium flaccumfaciens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Curtobacterium flaccumfaciens"
                     /db_xref="taxon:2035"
     Protein         <1..502
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
     Region          <53..500
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 pprraatrpr pargrggags agsagsagsa gsagsagsag pvedvedved vvasfqdvea
       61 amteghpafv aangrigfgl deyrafapes ggrfryrwla arrehthlal aadrteqahw
      121 eaelspvtva gfratlerrg ldpddyvwlp vhpwqwqhri avtfapdlgr qdlvdlgegp
      181 deyqpqqsir tafnrtepar syvktalavq nmgflrgmsp aymrntpavn dwvesivsad
      241 ptlaaagfsv lrehaaigyt gdayhrvdvs spqrkmlaal wresplprvt dgerlltmaa
      301 llhrdaagna vvsalieasg lpadvwvrrw ldayllpvvh cltvhdlvfm phgenlvlvv
      361 rdgvvvravm kdigeeaavl grhddrpvpa didrivhpvs ddeaalavft dvfdgvlrfv
      421 aaildddavl pesrfwqvvg ecidahaaah pdrrrpldlr vptfehscln rlqlrntlsm
      481 vdladqsasl iragamanpi gr
//
LOCUS       WP_284728987             205 aa            linear   BCT 25-DEC-2024
DEFINITION  TRAP transporter small permease [Cobetia marina].
ACCESSION   WP_284728987
VERSION     WP_284728987.1
KEYWORDS    RefSeq.
SOURCE      Cobetia marina
  ORGANISM  Cobetia marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Cobetia marina"
                     /db_xref="taxon:28258"
     Protein         1..205
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22807
     Region          5..157
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mpsvlaglsr lnrtlerlly lvllvllasf ivfiiyqias rnlaflprlf wteefsrfaf
       61 qwmvmlgtav gvlhadhfvl eafprgsrad lvtrwirdla clllgvlfiv hgkdfalsgl
      121 rrsamasgls miyvysvftv sgvfivlfsl qrllhawlyg mpameaalnt pneaeelatp
      181 eetqavlspv iaghahdatd rrtlp
//
LOCUS       WP_284732479             145 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Curtobacterium flaccumfaciens].
ACCESSION   WP_284732479
VERSION     WP_284732479.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium flaccumfaciens
  ORGANISM  Curtobacterium flaccumfaciens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 145)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Curtobacterium flaccumfaciens"
                     /db_xref="taxon:2035"
     Protein         1..145
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15331
     Region          12..138
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 mslqtgsqpp tlrvsalllv rdrrvlmvra rardvlylpg gkaephetdl daaireanee
       61 tglrvtaddv dpfgvvlepa hgqapgtmva mtlflvrpgg pldsatpvas aevdevewvt
      121 sadagrcppa gvetlrrlva aerid
//
LOCUS       WP_284732866             185 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Luteibacter anthropi].
ACCESSION   WP_284732866
VERSION     WP_284732866.1
KEYWORDS    RefSeq.
SOURCE      Luteibacter anthropi
  ORGANISM  Luteibacter anthropi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Luteibacter.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Luteibacter anthropi"
                     /db_xref="taxon:564369"
     Protein         1..185
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=19438
     Region          1..184
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mlylasqspr rrellgqmgv afqtldvdve eirqsgespd ayvsrvaldk araghalvaa
       61 dpvarvlsad tevilgdevf gkprdasdat amlqrlsgre hrvvsavwlk daagergeva
      121 istvrfaald daqiaayvag gecfgkagay aiqggaaafi shlsgtysgv mglplyetsr
      181 llrgq
//
LOCUS       WP_284734327             188 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein, partial [Pseudomonas
            aeruginosa].
ACCESSION   WP_284734327
VERSION     WP_284734327.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..>188
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          35..>188
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mpalplsrra laalalvfal palaedwpdt dwpraqqpag paleaferya fgrrddvrrk
       61 girtdavvvi rdgrllyery agpsraetph ltwsvsksll atllgvaege grfqlddpva
      121 ryyppfarhp evtlrhllnw ssgldwqedy efaplkssvv amlytrgrdd magfvaetpp
      181 arppgrrf
//
LOCUS       WP_284734348             360 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein
            [Sphingosinicella terrae].
ACCESSION   WP_284734348
VERSION     WP_284734348.1
KEYWORDS    RefSeq.
SOURCE      Sphingosinicella terrae
  ORGANISM  Sphingosinicella terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Sphingosinicella.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Sphingosinicella terrae"
                     /db_xref="taxon:2172047"
     Protein         1..360
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=40013
     Region          9..342
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mmaepsplvl itgaagnlgr siadilsddy rivgldrqge tdfplievdl tddeaitaal
       61 aqvrerfgdh iasvihlaay fdfsgeehpl ysklnvegtr allqalqpfq verfihastm
      121 lvhaptkpgq qideaspigp rwaypqskae aeaaigeeag sipflilrla gvydeetmvp
      181 tlahqiarif erdiqshfys gatdvgqsml hredmldafr ravdrrddle rretlligep
      241 davgydrlqd vigalihgre qwttlrlpmp vaaagawvqe kleplipdai dkgeapfvkp
      301 fmirladdhy aldvsrarkr lgwvprhrll dtlpamvaal krcpvewyek nnvtapeslt
//
LOCUS       WP_284734367            1152 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Sphingosinicella
            terrae].
ACCESSION   WP_284734367
VERSION     WP_284734367.1
KEYWORDS    RefSeq.
SOURCE      Sphingosinicella terrae
  ORGANISM  Sphingosinicella terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Sphingosinicella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1152
                     /organism="Sphingosinicella terrae"
                     /db_xref="taxon:2172047"
     Protein         1..1152
                     /product="class I SAM-dependent DNA methyltransferase"
                     /calculated_mol_wt=127970
     Region          97..1050
                     /region_name="YeeA"
                     /note="Type II restriction/modification system,
                     endonuclease and methylase domains [Defense mechanisms];
                     COG1002"
                     /db_xref="CDD:440626"
ORIGIN      
        1 mseadtfiaq wrdtggsela ntqsfinglc rligvepphg srtddahndy vferrvfqdn
       61 gdgtlsfgri dcykkgafil eakqgseadr aaaargeddl dlfgqtasar lkrgtarrgt
      121 pgwakamtqa kgqaeryaka lpadhgwppf llvadigyci evyadfsgtg kayaqfpdrs
      181 ryrimlddlr daevrarlaa iwdapfsldp aaraarvtre iadllatvar rlekrghape
      241 rtsgflmrll ftmfaedsnl ipeksftell rnqrtaphhl ehqlsalwaa mdrgdfspal
      301 gvplkrfngy lfkdrtaipl eaeelevliq aaehrwteve paifgtller alnpkerakl
      361 gahytprayv erlvgptime plradwagvr vaaselidqg kadearrtve afhtklaqtr
      421 vldpacgtgn flyvamarmk elegevldll vdlgddqyla eltghtitpe nflgieinpr
      481 aaaiaqlvlw igylqwhfrv ngrdrpppep ilrdirtien rdaliewddk vterdehgap
      541 vtrwdgetmk phpvtgkpvp denarvevyr yanpraakwp kadfiignpp figkvglraa
      601 vgdgyfnalf sttdvpesad lvmhwwnkaa nvvrrgeakr fglvttnsit qsfsrrvvnk
      661 hvdakdrlsl lfaipnhpwv nerdgaavri amtvgekgtg rgrllevvde sgapeqitfd
      721 tqdglisgdl rvgadvaqaa plraneriss lgfalygngf ivdddearrl grgidpiadq
      781 lireyrngrd ltakprnvfv idafgysedq lrmdaptiyq hlalhvkpvr dsnrrdsird
      841 nwwifgwprp eirkalqgld rfivtvetmk hrifqflpsk iapdnkltvi atsdayhigv
      901 lsskyhvtwa saaggrlgmg ddlvyvkshc fdpfpfpadv peplkacira eaealdalrk
      961 rvlaehpdlt ltrlynvlea lregraltpq erdihdrglv slirqhhdei degvadaygw
     1021 gdeqragtlg eetilarlva lnkeraaeea rglvrylrpe yqdpgyrtpv aatldlgeaa
     1081 alpasnvipw patlpeqvga vqsilaaapa plaaqdiars fkgkraatvr pvldalaglg
     1141 marrledgry aa
//
LOCUS       WP_284734381             460 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Sphingosinicella terrae].
ACCESSION   WP_284734381
VERSION     WP_284734381.1
KEYWORDS    RefSeq.
SOURCE      Sphingosinicella terrae
  ORGANISM  Sphingosinicella terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Sphingosinicella.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Sphingosinicella terrae"
                     /db_xref="taxon:2172047"
     Protein         1..460
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48598
     Region          247..459
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mnaelqrdrp vtgrvdsagr lvaadaplae lnaragggea gmlsvpqiaa larlarrlgi
       61 tvsraaiaad gdrdidlwvr aepvgedvel titgwgqraa qpaapaptee readflrasa
      121 dwtwetdeal rltalsgaaa aglgrasael igqqltrlfr fregesgalp iltalaehkr
      181 fdgqvaelra grkgryllsg vplidgmgrf agfrgaavsm psgrtvpqpl aggerasafg
      241 erldqalrap laaivdnaer lraqpegplr hdytgyaadi aaagrhllsl vddlvdlqai
      301 erpdfapeae avdladlarr asgllavraa dlgveidppa sdealpatgd ftralqvlmn
      361 linnairysp qggqvwirtd regdlaaviv adqgkgiade dqqrifdkfe rvdpaepggt
      421 glglyiarrl aramggdvsv hsapgqgsrf tftlpsrksl
//
LOCUS       WP_284734424             286 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Sphingosinicella terrae].
ACCESSION   WP_284734424
VERSION     WP_284734424.1
KEYWORDS    RefSeq.
SOURCE      Sphingosinicella terrae
  ORGANISM  Sphingosinicella terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Sphingosinicella.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Sphingosinicella terrae"
                     /db_xref="taxon:2172047"
     Protein         1..286
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31944
     Region          2..274
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 meisqssqri laslleartg qqitfnrrwr idsalssimr erdfanvdql varlvagrdp
       61 altesvieal lnnetyffrd klpfdllfgg pvkrleqarq rekrlsiwca gcstgqevys
      121 lamsfadekt rwqgwkidiv gtdlsrrtie karagiysqf evqrglpvvq mirhfdevgg
      181 rewkispvlr davrfearni sdapphpgkf diilcrnvll yfspemkrla ftrlsqaiaa
      241 dgslmlgage tvigltdrfv sdpenrglyv papgvgigas paarva
//
LOCUS       WP_284734463             427 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Sphingosinicella
            terrae].
ACCESSION   WP_284734463
VERSION     WP_284734463.1
KEYWORDS    RefSeq.
SOURCE      Sphingosinicella terrae
  ORGANISM  Sphingosinicella terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Sphingosinicella.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Sphingosinicella terrae"
                     /db_xref="taxon:2172047"
     Protein         1..427
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46172
     Region          134..403
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 maagykaqfl csglwnggrt qtqieadela giyeriqaiv ptlpaeidqe rrqvrvafge
       61 ampprtaqwr pglgcaslpi gaspeagahv palapdfdia afdsrpwpmg dgrgrigata
      121 gtsglqllas sviaqdqygg rssavlvvhr griaaegygr ghdlhttqrt wsvakslagt
      181 lighavqrgl irtdapadla awrspgdpra aisvdqlmrm asgltsdtag nrtddlymgg
      241 tavtdrsprw pllhppgtrf ryanndtlla tmalmerlpt eerlgfpiaf frrigmtrti
      301 aetdwqgnfi lssqvwtsar dlarlgllyl ndgiwqserl lpegwrnhvt rpsgpqpege
      361 fgygatfwlm srsegvpada faafgnrgqy lvivpsrdlv ivrrgydtsa erfdvaafta
      421 avvaale
//
LOCUS       WP_284734486             124 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Sphingosinicella terrae].
ACCESSION   WP_284734486
VERSION     WP_284734486.1
KEYWORDS    RefSeq.
SOURCE      Sphingosinicella terrae
  ORGANISM  Sphingosinicella terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Sphingosinicella.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 124)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 124)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007442
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Sphingosinicella terrae"
                     /db_xref="taxon:2172047"
     Protein         1..124
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12601
     Region          44..121
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
ORIGIN      
        1 miaaarampa tllllaackp ppegrhpmag adaaagravv ervgcgscha fpdiawprga
       61 vgpdlsrfas qtmiagrvpn rpdllaafvr napavvpgsa mpampideae ardvaaylyt
      121 lgae
//
LOCUS       WP_284734490             574 aa            linear   BCT 25-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Sphingosinicella
            terrae].
ACCESSION   WP_284734490
VERSION     WP_284734490.1
KEYWORDS    RefSeq.
SOURCE      Sphingosinicella terrae
  ORGANISM  Sphingosinicella terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Sphingosinicella.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Sphingosinicella terrae"
                     /db_xref="taxon:2172047"
     Protein         1..574
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=61037
     Region          32..563
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mkrrwtgaig rpwlmlalla sagaqattpa ptydivirgg tvydgsggep yvgdvavedd
       61 rivavgrveg tgrqeisaag kavapgfinm lswatrslle dgramsdlhq gvtlevfgeg
      121 wtmgpineam rvrlrerggd giaatwttlg eyldhlerrg ispnvasfvg attirihelg
      181 eadvdpspeq larmralvrq ameegalgvg saliyapgny aetpelaala geagrcggmy
      241 ishmrseadd igeaidevvt iaregdvpae iyhlklagtr nwdrlpqiva qieaarragl
      301 ritanmyhyt aggtgldavm ppwvqdggse aflarlrdpa irarllaemr apesdwenll
      361 rasgggegvl lvevanetlr plvgktlaev aamrgtgvee taidlvleds rigaiyfmms
      421 ednvrrqtal pwmsfgsdag apaaegetle saahprtygn farllghyvr eqralplaqa
      481 irgltslpaa nlglrdrgsl apgqhadivv fdpatiadha tyadphryat gvsdvfvngi
      541 qvlaegrhtg atpgravrgp gwtgwpdggg cgrr
//
LOCUS       WP_284734501             421 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Sphingosinicella terrae].
ACCESSION   WP_284734501
VERSION     WP_284734501.1
KEYWORDS    RefSeq.
SOURCE      Sphingosinicella terrae
  ORGANISM  Sphingosinicella terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Sphingosinicella.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Sphingosinicella terrae"
                     /db_xref="taxon:2172047"
     Protein         1..421
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=45439
     Region          39..398
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mtfqspassv aprpaaitpq pvpavragtr rraggtaarr trallrqlhl wmglviglpf
       61 allgltgsal vfyveidall tpeiraasea papdwsspaw dralatvqaa wpdrigkwtf
      121 eangepgaip arfyeaagvh ghgarplmvw vsadgsrvvr harwgdylmt wfydvhrnll
      181 agdtgnrvvg wlgvamllll atgmaawwpr gswrkalafr raapplrrlr dlhkllglst
      241 lallfvltat gallalpaer dllldrtvap vvpvpapvsa ppsgrriaiv qalaaarqal
      301 pdarlawidv pgapegvfrl rvqvpgdpnr rfpqsyvfvd qysgtvlavh dmrrgtastt
      361 aaawlrplhd asvgglatri lgvvvglvpa alfltgllrw rrrraaasvr pvrpseertn
      421 p
//
LOCUS       WP_284734512             370 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha
            [Sphingosinicella terrae].
ACCESSION   WP_284734512
VERSION     WP_284734512.1
KEYWORDS    RefSeq.
SOURCE      Sphingosinicella terrae
  ORGANISM  Sphingosinicella terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Sphingosinicella.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 370)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Sphingosinicella terrae"
                     /db_xref="taxon:2172047"
     Protein         1..370
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41718
     Region          3..363
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
ORIGIN      
        1 merslpssdy ltpkafeldr esifarewfc aareedvpgp gdhrvieyag eslllvrtka
       61 gvlkahynvc rhrgaricds darwdlqlrg giaqgmircp yhswcysldg dlvaaggmge
      121 gpafdkaafg lypagvacwg gfvflnlmpg eapdfgealg eaprrlanyp ledlrtarsi
      181 dyevganwkl ilenynecyh cgpvhpelca lvpefrrngg mhldwelgip hrdgattytr
      241 tgttdracfp glseeekvrh kgellypnlm fsvssdhaaa filwpmgpdr trvqcrflfh
      301 rdeigkagfd pldavefwdl vnrqdwavce rvqrgigarv hdfghysple dysldirryv
      361 tdrrqrlrga
//
LOCUS       WP_284734546             880 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Sphingosinicella terrae].
ACCESSION   WP_284734546
VERSION     WP_284734546.1
KEYWORDS    RefSeq.
SOURCE      Sphingosinicella terrae
  ORGANISM  Sphingosinicella terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Sphingosinicella.
REFERENCE   1  (residues 1 to 880)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 880)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 880)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 880)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..880
                     /organism="Sphingosinicella terrae"
                     /db_xref="taxon:2172047"
     Protein         1..880
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=94865
     Region          98..767
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mepvgleaed rpslrrlliq dfqplanerd egiarerlra lapvpgfflv vhlvcaaail
       61 lalgteamrq pvvtaplasl lvvdillwal arrggifriq phlalraaaf ysllvgalig
      121 tvvaglgtvr dggmplltlg lagavfalpl afllfpglag lgcigalmaw llvtgdavst
      181 alagivgiai lrlslnraae klsqlkrrem idwnaqrasr fieefeqagr gwfwetnsrg
      241 alsyisdqla adlaipaael igrpftdlig sdasgsadss ertlgfhlsa rlpftditvr
      301 anasadtwws lsgtpsfdey grflgfrgig tdlteqrrse deinrlakyd sltglpnrml
      361 mrrtldetlq anstsgnalf lidldrfknv ndtlghpvgd allkqvgqrl asvigdrgqi
      421 grlggdefka vlpgvtdeps lgalaarliq qvsmpylieg hnisigasvg iaiappegcc
      481 gdalirdadl alysakaagr gtycffapem hseaqdrqml endlrkaigr gelelyyqpv
      541 vdtksealsg fealvrwhhp trgmisptvf iqlaeesgii lqlgewvlrt acaeaakwpe
      601 niriavnlsp vqftdaslpn tivsalanag laprrlelei tegvflvese stddmfarlk
      661 aigvrlaldd fgtgysslgy lrktpfdkik idqsfvrgaa mrgsrnaaii raivtlaesl
      721 gmdttaegae thdelalire lgcshiqgyi fgrpmiaeea lklaadnetv aadgfqfnrp
      781 prqgllkvat lqwngmqipv rvrnistgga llesdrtvpv eakvqldlpg cgslgaevrw
      841 sesrrtgiqf eeefdlrrlv pgktrgfgvr lagggqraag
//
LOCUS       WP_284734595             705 aa            linear   BCT 25-DEC-2024
DEFINITION  autotransporter assembly complex protein TamA [Sphingosinicella
            terrae].
ACCESSION   WP_284734595
VERSION     WP_284734595.1
KEYWORDS    RefSeq.
SOURCE      Sphingosinicella terrae
  ORGANISM  Sphingosinicella terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Sphingosinicella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Sphingosinicella terrae"
                     /db_xref="taxon:2172047"
     Protein         1..705
                     /product="autotransporter assembly complex protein TamA"
                     /GO_component="GO:0097347 - TAM protein secretion complex
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=76798
     Region          <28..>109
                     /region_name="PRK15313"
                     /note="intestinal colonization autotransporter adhesin
                     MisL"
                     /db_xref="CDD:237940"
     Region          110..705
                     /region_name="TamA"
                     /note="Outer membrane translocation and assembly module
                     TamA [Cell wall/membrane/envelope biogenesis]; COG0729"
                     /db_xref="CDD:440493"
ORIGIN      
        1 mwaaiaggvl atpyavqaqq ptpdnqavrd depivpdsaf eealppldpa liepleplea
       61 iepdaspfpp vpgpvedtpl gdpalseplp plsvsdvepr sidpvedeqt aepvpirytv
      121 ivegleetgl edrfrdlsal edargeavng amiearaeed elllvrllrs egyydavvas
      181 aienvveepg alrirltaap gpvyrfgeir iagaqtvppg larealplqs gepiiaeeve
      241 aaeanvllrl pqqgypftev glrdieldpa telglytlpv elgprasfgg fttegdlafd
      301 aehvgvlarf rrgelydrrk vddlreamvs trlfdsvsae tvrtgeiapd gteyvnilvr
      361 qdagparsid anagystgeg lrlegawehr nlfppegslr iaaiagtaeq nlslrfrrnn
      421 whqrdralll qieagqrdye afqgytarlh glvtrestpi wqkrwtyayg aeilatnesr
      481 vgrarlslsd ayfiggligq lgydrsnsll dptrgfrlls rvnpeasfgn gdfyyirnli
      541 egsayfpagd sfviagrarf gsiygiprde lapsrrfyag gggsvrgfgf qelgpreivp
      601 npdfdpeepd kepatisvpl ggrslaefal egryrfgnyg vvafvdagqv yesqfptfss
      661 mrfgvgvggr lytnfgpirl dvatpigrre gesrisvyis igqaf
//
LOCUS       WP_284734620             196 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Sphingosinicella terrae].
ACCESSION   WP_284734620
VERSION     WP_284734620.1
KEYWORDS    RefSeq.
SOURCE      Sphingosinicella terrae
  ORGANISM  Sphingosinicella terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Sphingosinicella.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Sphingosinicella terrae"
                     /db_xref="taxon:2172047"
     Protein         1..196
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21272
     Region          57..193
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 miasllalgl glplagcdrq tatvpqgeap artdaaqaae sapprsyptg rldrshagaq
       61 apdtifedpq gdparmadfr grpvlvnlwa twcgpcvvem psldglarre gdrvavlals
      121 qdmqgrqkvt dffaardfak lepyldpnld fmtslridtl pttilydaeg revwrmtgma
      181 dwesdravrl lreagt
//
LOCUS       WP_284734627             317 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein
            [Sphingosinicella terrae].
ACCESSION   WP_284734627
VERSION     WP_284734627.1
KEYWORDS    RefSeq.
SOURCE      Sphingosinicella terrae
  ORGANISM  Sphingosinicella terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Sphingosinicella.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Sphingosinicella terrae"
                     /db_xref="taxon:2172047"
     Protein         1..317
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=35078
     Region          20..312
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 msrppparsg rprntatlav tggtgfvgah lmrvaraggl svraltrkwr ppeegvdwie
       61 galdrpdsla rlcagadavi hvaglinaat rdafdsvnvg gtanmvdaar haglrrfvhv
      121 sslaarepdl sdygwskars ervvaasgld wtiirppavy gpgdretfel frmarrglva
      181 lpprgrfsvi hvedlcrlil avidepdthf etyepddgtd egwdhrhfar tlgrvlgkrp
      241 atlpmpklvm qgasrverlv rrdrakltad rvryfchpdw vvtarhrppe slwkpeirtp
      301 tglkdtaewy kaqgwlk
//
LOCUS       WP_284734651             145 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Sphingosinicella terrae].
ACCESSION   WP_284734651
VERSION     WP_284734651.1
KEYWORDS    RefSeq.
SOURCE      Sphingosinicella terrae
  ORGANISM  Sphingosinicella terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Sphingosinicella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Sphingosinicella terrae"
                     /db_xref="taxon:2172047"
     Protein         1..145
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=15597
     Region          15..138
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mtyafpgrdp aafadpapmm nttplidlml vllvmfivsi piathkvpld vstgptppse
       61 rppahrldld aagraswdgr pvrdaqlsll ltrlaadpaa pelhiavaae tryervdhvl
      121 aeilragvtr tgfignerfa qaldr
//
LOCUS       WP_284734717             558 aa            linear   BCT 25-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Sphingosinicella terrae].
ACCESSION   WP_284734717
VERSION     WP_284734717.1
KEYWORDS    RefSeq.
SOURCE      Sphingosinicella terrae
  ORGANISM  Sphingosinicella terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Sphingosinicella.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Sphingosinicella terrae"
                     /db_xref="taxon:2172047"
     Protein         1..558
                     /product="long-chain-fatty-acid--CoA ligase"
                     /EC_number="6.2.1.3"
                     /GO_function="GO:0004467 - long-chain fatty acid-CoA
                     ligase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=59746
     Region          20..541
                     /region_name="FC-FACS_FadD_like"
                     /note="Prokaryotic long-chain fatty acid CoA synthetases
                     similar to Escherichia coli FadD; cd05936"
                     /db_xref="CDD:341259"
     Site            order(201,204..209,211..212)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(204,321..322,343..348,428,440,443,454,534)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(204,246..247,294,296..297,300,321..322,343..348,428,
                     440,443,451..454,515)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(246,296..297,300,321,451..453,509,515)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mnpamasgma fdftprlvtd mfdetvrrhg grpavdfmgr rtrydelsal vekaaaglqa
       61 igvvpgsrva lclpnvthyp vlflatlkag givvnvnply verelahlle dsgaeiiatc
      121 dlpeihgrva saaarlglrh vvtcpiaeal splkafgykl fkrrdiaalp ddphhlsfae
      181 lvdrgsafrp vdvtpdatav lqytggttge pkaamlshan lvanadatla fsggeraepd
      241 rvlgvlplfh vfalttvfsf airtgaemvl lprfnleqvl ktiartrpty fpavptifat
      301 iagiaaqrki dfsdmracis ggaalpaevr laferttgar lvegyglsea spiitcnpid
      361 giskagsagp pypgttieir drddssrlta igepgeicar gpqvmkgywn rpeataavfv
      421 dgalrtgdvg yldeegylfi vdrikdviia ggynvyprvi eealyehpav aeavvigvdd
      481 pyrgqapkaf vtlvageaat pealrdflrd kvskielpre veirdslpkt ligklskkel
      541 vaeekakaal aqppedav
//
LOCUS       WP_284734735             158 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF2269 family protein [Sphingosinicella terrae].
ACCESSION   WP_284734735
VERSION     WP_284734735.1
KEYWORDS    RefSeq.
SOURCE      Sphingosinicella terrae
  ORGANISM  Sphingosinicella terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Sphingosinicella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Sphingosinicella terrae"
                     /db_xref="taxon:2172047"
     Protein         1..158
                     /product="DUF2269 family protein"
                     /calculated_mol_wt=17221
     Region          3..154
                     /region_name="COG5528"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:444279"
ORIGIN      
        1 mieylilkwl hvigstillg tgagiaffml mahrtgdpaa vaatarivvi adfvftatav
       61 vaqpvtgill vrsvgysfae gwilasialy lftgafwlpv vwmqvrmrdl ataavaagap
      121 lpaayhrlyr lwfafgfpaf favlaifwlm iarpeinw
//
LOCUS       WP_284735446             503 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Nonomuraea sp. NEAU-A123].
ACCESSION   WP_284735446
VERSION     WP_284735446.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NEAU-A123
  ORGANISM  Nonomuraea sp. NEAU-A123
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Nonomuraea sp. NEAU-A123"
                     /db_xref="taxon:2839649"
     Protein         1..503
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=49925
     Region          1..503
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mtrplaarll pagpptagph maakppqggs laamlplags llagflvagp laagllvvga
       61 gpsssddvgs varagqwqla tlrlpeawrl srgdgvlvav ldtgvnarhp dlagavitgp
      121 dltgdagepv mwghhgtama sliaghghna attgdpaqsg httsatdept qsvhmtpqtr
      181 dpaqsgrsal atgdaaqsga fatgslarsg saasgsaadg saaggsadsg vigvapaarv
      241 lsirvtleng dplrdkqrag grdalargir yavdhgadvi smslgggsga wegsaaeeea
      301 vqyaishgav lvassgndgn ttnrknfpaa ypgviavgav drrlevaafs nrqdylsvva
      361 pgtgivtadg adsyvvgdgt ssaaamvagi valikaahpd lspyhvrtai elgtrrrpad
      421 gysrasghgv anallalraa drlanpatps aaggvgtggy fgdgpvsrpp ssrlpvvlgm
      481 vlltavmsar vlvrhrwrgr dlt
//
LOCUS       WP_284735583             383 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Dongia deserti].
ACCESSION   WP_284735583
VERSION     WP_284735583.1
KEYWORDS    RefSeq.
SOURCE      Dongia deserti
  ORGANISM  Dongia deserti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Dongiaceae; Dongia.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Dongia deserti"
                     /db_xref="taxon:2268030"
     Protein         1..383
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=41171
     Region          17..377
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mmhdnpfsea eiarrlaafr tgllqrgldg avvaapenvf yltgldhwgy faphllivpl
       61 agtpvlvtra mervsvekqv kaaefrghsd setaadvaar vlrdqklagr rlgleywtag
      121 fshglamslq aqaeaqwqdi sgliddlrlv ksteeqtlmr raaavtdaaa gaaieviadg
      181 aperevvaac vaamtraggs ppafgpfirp gsrlgeehtt wgdgryksge pvflelsgca
      241 sryhaplgrl vhigsipdpd armaetsqqa fhavlgalrs garardvyaa wqqvvdeagl
      301 pryrrhhcgy cvgiglsptw tggnkvvglr hdsemeireg msfhilswlm gtgrgdyfis
      361 ntvllgaggp evltrtpdgp ivr
//
LOCUS       WP_284735659             285 aa            linear   BCT 25-DEC-2024
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Dongia
            deserti].
ACCESSION   WP_284735659
VERSION     WP_284735659.1
KEYWORDS    RefSeq.
SOURCE      Dongia deserti
  ORGANISM  Dongia deserti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Dongiaceae; Dongia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439579
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Dongia deserti"
                     /db_xref="taxon:2268030"
     Protein         1..285
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31091
     Region          1..259
                     /region_name="PssA"
                     /note="Phosphatidylserine synthase [Lipid transport and
                     metabolism]; COG1183"
                     /db_xref="CDD:440796"
ORIGIN      
        1 mrrtrlrdhs inrlipnmlt lfalcaglts ikfaldaqal mdvtaytdps avanaaarkw
       61 elaciaiiva avfdaldgri arlldstskf gaeldslsdf iafgvapsvi lyvwtmdqag
      121 rigwgltllf sacmalrlar fntkldnadv pawtmrfftg vpapagaglv lmpviayney
      181 gggiadspwl vgswmvivsg llvsriptfs fkrlaitqrw vlpamvvvav fvallvsetw
      241 ntalamgaly lasipfsyrq yqrlavqrph aptieqraeh dldlh
//
LOCUS       WP_284735817             288 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Dongia deserti].
ACCESSION   WP_284735817
VERSION     WP_284735817.1
KEYWORDS    RefSeq.
SOURCE      Dongia deserti
  ORGANISM  Dongia deserti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Dongiaceae; Dongia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Dongia deserti"
                     /db_xref="taxon:2268030"
     Protein         1..288
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31441
     Region          25..275
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          186..268
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtciaqsksl aiydyrcrig lgatpfverh nrssisfvrk gsfgyhtrgk yfelvagsvl
       61 igragdeyvc shdhvcgdec lsfqlapelv aaigdddtiw svgalppvpe lmvvaelaea
      121 aaarqsdval deagllmaar fveiagsthr aksaaaeqkp vvtatrdrrr aveaalwlee
      181 hahqaidldr vsrqaglspf hflrlfarvl gvtphqylvr crlrhaarll adparsitdv
      241 afdvgfadls nfvrtfrraa gvsprvfrka akgerkilqe riaayalg
//
LOCUS       WP_284735892             384 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein [Dongia
            deserti].
ACCESSION   WP_284735892
VERSION     WP_284735892.1
KEYWORDS    RefSeq.
SOURCE      Dongia deserti
  ORGANISM  Dongia deserti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Dongiaceae; Dongia.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 384)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Dongia deserti"
                     /db_xref="taxon:2268030"
     Protein         1..384
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=41399
     Region          3..377
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mtasamnsnc ggrdhgaihv eravidwtrr ifgfpegtsg lltsgtsqst iialaaarih
       61 algrdvrang lrdapdhvay assgahsanq kalellghga qavrripatg tnggmdlakl
      121 raqlasdraa gkrpfcvigt igsvdtgacd dldaladlca qeglwlhvdg afgcwariad
      181 hpwrdlargi eradslafdf hkwmyvqydc gavlirhgda hraafamrpd ylegqedglg
      241 ggdpwycdyg ielsrgfral rvwsclrayg ldrlarkisd ncrqaarmaa lvetadelel
      301 gapvvlnvcc fryapkdvda grqdmlnrql atrlqlggev vfsttklggr tflraaivnh
      361 rtrdqdidra iaavreacga lgrq
//
LOCUS       WP_284735914             471 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Dongia deserti].
ACCESSION   WP_284735914
VERSION     WP_284735914.1
KEYWORDS    RefSeq.
SOURCE      Dongia deserti
  ORGANISM  Dongia deserti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Dongiaceae; Dongia.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Dongia deserti"
                     /db_xref="taxon:2268030"
     Protein         1..471
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=52670
     Region          3..301
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(71,74,149..155,184,208..213,244,270..274,276)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 maaqagnrle iqavnpaara lglkpgmava darawvpqvv vlpldpeada adlkrladwt
       61 trfsplvaid gtdglmldia gcahlwgset rmladldrhm rtfglhyrva vadtigaawg
      121 aarfgagtnp ivphgqqraa ladlppqalr lpgelcaqlq rlglkriadl ctlpraalar
      181 rfgtglmdrl dqaldrqdei lspllpppqc yvrmdfaepi tqradidral tlllkrltea
      241 lrphesgprk ldlscyrldg etqrltigta raslnaahlf rlfeeklnql hpddgfeamr
      301 lsgremerlt tqqhdfeags airhdlapli drlsnrlges avhrvetces hiperavrrl
      361 pplaesprlh wpkasqrpir llphpepiea vapipddppv qfrwrhvlhk vraaegperi
      421 apewwlpgge daeirdyyrv edsegrrfwl yraglyqttp tprwfmhgmf g
//
LOCUS       WP_284736057             426 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Dongia deserti].
ACCESSION   WP_284736057
VERSION     WP_284736057.1
KEYWORDS    RefSeq.
SOURCE      Dongia deserti
  ORGANISM  Dongia deserti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Dongiaceae; Dongia.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 426)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Dongia deserti"
                     /db_xref="taxon:2268030"
     Protein         1..426
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47314
     Region          24..415
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(135,137,270,272,307..309)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mitrrvllgs alaigfafpa yaetlnvlme gvpdtefvkq vlpefeaatg hkvnlevvny
       61 aemhtklvpq lvapkgsysv ivvdfywvge ftkagwlqpl ddrikadnvd tsvyipalmd
      121 lvgkvdgvty mlpfynyamg ltyrtdllad pknqeafkak ygmdlqppkt wdeylkqmef
      181 ftrdgmhgvv nqglrpdpia mewsnylfan gaeyhdanwn ptfnnekgvk avqqyadaid
      241 kygpvgsasf sfdeafnvma qgkaysyity nffrtayddp skssvvgkve impvpgptad
      301 tggslngawg waipksspnp daawefikwv espeiakkra llggsptrtd vfedpelnqk
      361 ypyaqalksm lltshnfpvf tytpqlvevl grelslavag eksaqdaltq iekefvdlak
      421 kdgklk
//
LOCUS       WP_284736883             112 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein, partial [Escherichia coli].
ACCESSION   WP_284736883
VERSION     WP_284736883.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>112
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
     Region          <6..>110
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 fdlpvgwldq ehqttnitkk pdvsitnkqi tlvpviswvq agawkevgys evdlstaety
       61 pcpvpcgemt yilrvigdsm ideyrpgdmi fvdpevpach gddvialmhd sg
//
LOCUS       WP_284737153             123 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase, partial [Escherichia coli].
ACCESSION   WP_284737153
VERSION     WP_284737153.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>123
                     /product="DNA-methyltransferase"
     Region          11..>117
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mfkttnihga qlvcadslqf iktipdnsvn liatdppyfg vkanawdnqw dsdadflgwi
       61 deflaefwri lapngslymf tgsrlaskie lltrdrfnvl nhiiwakpsg mwrgchkesl
      121 ray
//
LOCUS       WP_284737471            1472 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Escherichia coli].
ACCESSION   WP_284737471
VERSION     WP_284737471.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1472
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..1472
                     /product="beta strand repeat-containing protein"
     Region          4..1435
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 gdkaivnndg dstildggtg tritgddata nnsgnttvdg qgstgteiag nnavvnqdge
       61 ldvsggghgi ditgdsatvi nkgnitvtdk dsvgvlingd ratfantghi dvnnsatgfs
      121 iatsegvisl tgsmdvgdis tgmvlsgdgn svtlavedln vtgqkamgvd isgdsndidi
      181 agnilvdkdq tadnaadyff essvgvnvtg nnntvslnge ltvvsdselt srshgkrdgs
      241 qenisglivs gdnntislng giqfigeqki ladgsdiasl rkgfsdtsii svdgnssvyl
      301 ngtstiggdl plgytsiiql knkaileigr dallgvkdik sfnnyyepvp kiikattgsk
      361 vinngnidiq nigfisvsge dtsgtnngni tlsqydygnm msgtnallst dggsvvnngt
      421 iigkvmeqss vinrfettdv tydelfnnsv tgitgmlskt gamginnvng iidmygrgsv
      481 gmlavtqaii enagtiklds lwvdandtta lpdniaisna ryygagmavg sdsygspdan
      541 vtainqlggv isvynagvgm aayggsnmvi nqgtinlekn enyssslsan tlvgmavyqh
      601 gtaindktgv ininvdtgqa fyndgtgtil nygeinllgs pmdsadphmg atpdnldlls
      661 altgsgetdm rtassggfvt tkalanygne tlnsnvtaka wlynqdkanl tingelsvgq
      721 glensgllds dtisaaanvy nrasgsiitd llmltsgnsf fnegnfsgsi vgnsyrqnvv
      781 ntgsmtvtad gtsliggsfv lyneagails nsnsavsgge naivnitrts dslaqvnrgt
      841 itatngysai ktastgsnsn gkwiwntdtg visgvnpnap lidlgrgynf anagtinvqg
      901 dgavaisggt tsytvqlvns gtinvgtaqg kadgtngtgl igikgngret tinnaqsgvi
      961 nvyadnswaf ggqtktiinn geinllcdmg cdiyapgttg tlndhnsttd iivpaatstp
     1021 tqgsvptvpa dssaqqkltn ytigtnsdgt sgmlkannlv isdnvkvntg fsagtadttv
     1081 vindvfkgen isgaenisss tvmwnaqgst dasgnvdvtm tknaytdvvt dssvnnvaqv
     1141 ldtgytnndl ytslnvgtta elnsalkqis gsqattvfne arvlsnrfsm lsdaapevan
     1201 glafnvvakg dpraelgnnt qydmmalrks mtlteyqnls leygiarldg ngsdtagdng
     1261 vtggysqffg lkhqmafdng mswnnalryd vhnldssrsi aygdvnktad anvkqqylef
     1321 rsegaktfel reglnvtpya gvklrhtleg gyqernagdf nlsmnsgset avdsivglkl
     1381 dyagkegwsa natleggpnl syvksqrtas isgagsqrfn iddgqngggf nslatmgvky
     1441 ssqesalqvd afhwkedgis dkgvmlnfkk tf
//
LOCUS       WP_284738151             341 aa            linear   BCT 25-DEC-2024
DEFINITION  DODA-type extradiol aromatic ring-opening family dioxygenase
            [Serpentinimonas maccroryi].
ACCESSION   WP_284738151
VERSION     WP_284738151.1
KEYWORDS    RefSeq.
SOURCE      Serpentinimonas maccroryi
  ORGANISM  Serpentinimonas maccroryi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Serpentinimonas.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Vaillancourt,F.H., Bolin,J.T. and Eltis,L.D.
  TITLE     The ins and outs of ring-cleaving dioxygenases
  JOURNAL   Crit Rev Biochem Mol Biol 41 (4), 241-267 (2006)
   PUBMED   16849108
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Siegbahn,P.E. and Haeffner,F.
  TITLE     Mechanism for catechol ring-cleavage by non-heme iron extradiol
            dioxygenases
  JOURNAL   J Am Chem Soc 126 (29), 8919-8932 (2004)
   PUBMED   15264822
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Serpentinimonas maccroryi"
                     /db_xref="taxon:1458426"
     Protein         1..341
                     /product="DODA-type extradiol aromatic ring-opening family
                     dioxygenase"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016701 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36828
     Region          74..337
                     /region_name="45_DOPA_Dioxygenase"
                     /note="The Class III extradiol dioxygenase, 4,5-DOPA
                     Dioxygenase, catalyzes the incorporation of both atoms of
                     molecular oxygen into 4,5-dihydroxy-phenylalanine;
                     cd07363"
                     /db_xref="CDD:153375"
     Site            order(78..80,116,181,237,295,332..333)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:153375"
     Site            order(78,116,295)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:153375"
ORIGIN      
        1 maigagaals pmrwvcllqr asaaaelryi gnvtfpvkpm qsatsthtsp srvssseplr
       61 qaaaapqarp spalfishgs pmlalepgqt gpalaawaqa ecerqrpsav lvlsphwmad
      121 caavmthpqp atwhdfggfp eplyrlqypa pgapalaqqv lqllqaagia trpdaqrpfd
      181 hgawvplryl lpkaevpvlq valphgygpa evyamgqala plrqqgvwlv gsgsmthnlh
      241 effssrpaqd aepadyvsaf prwveqrlla hereallnyr elapqaarah ptdehflplf
      301 falgaaawgq saasqaepap phyltrevmh rylamdalvl q
//
LOCUS       WP_284738199             189 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II [Serpentinimonas maccroryi].
ACCESSION   WP_284738199
VERSION     WP_284738199.1
KEYWORDS    RefSeq.
SOURCE      Serpentinimonas maccroryi
  ORGANISM  Serpentinimonas maccroryi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Serpentinimonas.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Serpentinimonas maccroryi"
                     /db_xref="taxon:1458426"
     Protein         1..189
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=20258
     Region          1..189
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 midnydsfty nlvqylgelg aqvlvrrnde igleeleqrv aageierlvv spgpcspaea
       61 gvsvaaiqal agrvpilgvc lghqaigaaf ggrivraqql mhgktsliht tqegvfaglp
      121 aqftvnryhs laieratlpe claisawsdd geimgvrhrs laiegvqfhp esilsehgha
      181 llqnflaqr
//
LOCUS       WP_284738321              85 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase, partial [Klebsiella quasipneumoniae].
ACCESSION   WP_284738321
VERSION     WP_284738321.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella quasipneumoniae
  ORGANISM  Klebsiella quasipneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Klebsiella quasipneumoniae"
                     /db_xref="taxon:1463165"
     Protein         <1..>85
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
     Region          1..>85
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 nveigprcyl nsgvviysgn gvrmgegvli aanttlaptn heyrsrerti iaqrfmpsrg
       61 givigddcwi gancvlldgt vlgtg
//
LOCUS       WP_284738796             288 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Pseudomonas marginalis].
ACCESSION   WP_284738796
VERSION     WP_284738796.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas marginalis
  ORGANISM  Pseudomonas marginalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Pseudomonas marginalis"
                     /db_xref="taxon:298"
     Protein         1..288
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31649
     Region          9..283
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mslllveqpw afvamagvlg livgsflnvl vwrlpkmler ewraqahevl glpaepagpt
       61 ynlmhpnscc phcnhpirpw enipllsylf lrgrcahcqg pisaryplte lacglisawv
      121 awhfgfgwqa gamlvlswgl lamslidaeh qllpdalvmp llwlglivna lgllttlpda
      181 lwgavigyms lwsvfwlfkl atgkdgmghg dfkllallga wggwqilpmt llisslvgvf
      241 vglilmrlrk arastpmpfg pylaiagwia llwggqitdf ylqsvgfr
//
LOCUS       WP_284739071             492 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Pseudomonas sp. CG7].
ACCESSION   WP_284739071
VERSION     WP_284739071.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. CG7
  ORGANISM  Pseudomonas sp. CG7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Pseudomonas sp. CG7"
                     /db_xref="taxon:191007"
     Protein         1..492
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=53509
     Region          7..>484
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mnsfvkpdse pavsfgpfaf yrqqrlvtra gqplalggra ldvlqvlveh agryvskqtl
       61 iahvwpdsvv edinlrvhia alrrafgdgr dgaryilnhp rqgyclavhe dieapfsppa
      121 erhnlptrls pvvgrdrilg rllaqvprqa lttvtgpggv gkttvvlrva qlllehfddg
      181 awfvdlaais epsqvtaqga galglanetl grrlescrml lvldgceqvl gacrelaqal
      241 avtapgvall cssreplels gekivplpgl avasplepeh qivacpavql liervgarqq
      301 dfkphgrdwl ilsqicqrld glplalelaa aqvdalgvag vleqldygls llshgrrtav
      361 arhrsleavl dssverlsad ertafqrlav fegpftlkaa qaviscaeln vgqvprlllr
      421 lasvsllmve plaeggrfrl lhttrayamd klrrsgqwpv fhrryvlqga wgarrsrpqp
      481 asqrleqrvg fq
//
LOCUS       WP_284739922             135 aa            linear   BCT 25-DEC-2024
DEFINITION  histone-like nucleoid-structuring protein Lsr2 [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284739922
VERSION     WP_284739922.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Gordon,B.R., Li,Y., Wang,L., Sintsova,A., van Bakel,H., Tian,S.,
            Navarre,W.W., Xia,B. and Liu,J.
  TITLE     Lsr2 is a nucleoid-associated protein that targets AT-rich
            sequences and virulence genes in Mycobacterium tuberculosis
  JOURNAL   Proc Natl Acad Sci U S A 107 (11), 5154-5159 (2010)
   PUBMED   20133735
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18741]
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Gordon,B.R., Imperial,R., Wang,L., Navarre,W.W. and Liu,J.
  TITLE     Lsr2 of Mycobacterium represents a novel class of H-NS-like
            proteins
  JOURNAL   J Bacteriol 190 (21), 7052-7059 (2008)
   PUBMED   18776007
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Oshima,T., Ishikawa,S., Kurokawa,K., Aiba,H. and Ogasawara,N.
  TITLE     Escherichia coli histone-like protein H-NS preferentially binds to
            horizontally acquired DNA in association with RNA polymerase
  JOURNAL   DNA Res 13 (4), 141-153 (2006)
   PUBMED   17046956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10570331
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..135
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14537
     Region          1..110
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 maqkvlveml ddidgtpaah tipfsldgvt yeidlsddna aslrdglary igagrrtggr
       61 kvrvatgqpt ttasdrernq qirawanang yevsergrls seviaaydaa qlqeaepvka
      121 trkraprkkv aaark
//
LOCUS       WP_284739923             472 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284739923
VERSION     WP_284739923.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..472
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=48256
     Region          67..>470
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 msrirhllvp alvavagsvl vapsasaapa pqcnttnkqf tyvvlydpgt pelqvdtelr
       61 akcgekvayh paigvavats rnadfqakig afraysggrd valsswtsgs snssnlvgak
      121 eneettdtvv adklsaqqwd mraihapean kisggspsvt vgvldsgidp thpalknald
      181 pkasagctsg apdttpaawa pttsdhgthv agtiagkdte hdftgiapgv klasvkvvnd
      241 nglifpeaav cgfmwaanhh favtnnsyyi dpgmfycske pgdaaayeav rravvhstgq
      301 gvlniaaagn sgfdvtqqts dpnrphavda scgilpkaie gvvtvsaigy sgtkspysnf
      361 gpgqievtap ggayydtppa gqgascplst vlngaygtkc gtsmasphaa gvaallasrf
      421 pgappqkltr lleeqadpvp cdtvtaaqac adpaqnkpyy ghgrvnalda vq
//
LOCUS       WP_284739957             407 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284739957
VERSION     WP_284739957.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 407)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..407
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43448
     Region          33..262
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mdisseaahl rpldvaadll tllhdtttep radtqlealt lavsadlpvl lwgepgigkt
       61 aalnqlaeal dlplttvias vhepsdfsgl pvvgddpatq gvpmappewa vrlvragrgl
      121 lfldelstap pavqaallrv vlerqvgalr lppgirivaa anprssaadg welspplanr
      181 fvhlqwtydh dvvlrglggt wpkaelprld rerlpdavtf arravcglla arpelvhqlp
      241 knearrggpw psprswemal rliafttaag vsrdvlsmlv rgavgdgpgl ellagldrmd
      301 lpdpetllad peaavlperg dlrrtvldgv vaavrkrpel srwnaawsll vraletgapd
      361 lvvvpaatla alrrddwqvp aaierlsvav slsrradeaa agvgerr
//
LOCUS       WP_284739991             457 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284739991
VERSION     WP_284739991.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..457
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=48877
     Region          30..386
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msatqtapah rarrpspspr lstvlqlvsr rlhflagivv apflavlclt glvyvfspqi
       61 hdslyrtdlh vneagdvrrp laeqiraalt ahpeatlksv ltppaadrtt rvvlsvpgpa
      121 gtpdrtvfvd pytalingel atvenrlpan twlrqlhgnl qlgtpgrlya elaaswlpli
      181 vvgglvlwla rtrrkrrlre vlapstrdkt gwtrlrvvhg saglwlavgl llvgvtglam
      241 sqfaggradr aadpihlrap vltaapvpvp pgaqpigldr avaaaeaagl sgelavnppt
      301 vagapftvte iaeglpihrg avaidpytar vteqigwgdy swvaklsalg tefhtgtlfg
      361 lanqlvlaal avatlvllal gyrmwwihnp yrgrwtslpr pvwrqlagwp liavllgval
      421 lawrlpvlga slpvflavda glsrfkrrtk paelsta
//
LOCUS       WP_284740048             178 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284740048
VERSION     WP_284740048.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..178
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=18687
     Region          39..173
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 msggrlrrel rieftmltrr allnvvagss lvprplrwli yracgadvrs pnvfpgleia
       61 grpgnltlga gtfvntgcff elvapvsigr dcqlgmrtmv vtshhettaa gtsrrpvglp
      121 vrigdrvwtg arvtilpgvt iaddvvvaag avvtadcpep gvyagvparl irstagar
//
LOCUS       WP_284740056             384 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284740056
VERSION     WP_284740056.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..384
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39985
     Region          1..363
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mkvivvgagv lgtavarala vageevllld rgrpgtgtts ttfawtnanr kldpayhrln
       61 vagmaehadl arqlpgaaay fpsgalhwan sasapwltdn vdrlralgyp vrwverdeas
      121 riagalrips davsfahfps egyvlpdrll gnlladaerh gatfaigeva giddgpggva
      181 vtlaggevrt adrvvlatgr wserlaagag ialpmlagve rgspavgllg yvrapgidlr
      241 cvvhspglnl rpaagghtvv qaldlnadvd padppspdgp iareitrrls avlpepvsdi
      301 dlrvgfrslp adghtiagfg sprvyclvsh sgvtlgpllg rlvatelvtg rgddlldafr
      361 parfagrrra dfdadqhatr lgeq
//
LOCUS       WP_284740071             650 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284740071
VERSION     WP_284740071.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 650)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..650
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..650
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=67505
     Region          1..451
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          584..649
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(606,615..617,624)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            616
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mitkllvanr geiaarvlrt ahdlgistva vysdpdagap farladeavr lpgsapadty
       61 lradlviaaa ratgadaihp gygflsenag faracaeagl tfvgpspeai asmgskieak
      121 almdaagvpv lpgatvtdet dlaavaasig fpvlvkaafg gggrgmrvvh deaglsdave
      181 garweaasaf gdgtvflerf vvdprhievq ilgdahgevv hlferecsiq rryqkiveec
      241 pspavddalr aelgaaavaa gkaigytgag tvefvldadg rffflevntr lqvehpvtel
      301 vtgidlveqq lrvaegealp pevtgaritg haievrlyae dvpagflpat gtlhrfhvpa
      361 lrgvrvdsgv tdgsvvgphy dpmlakviah grtrreaart laralrhael hgvttnrnll
      421 agilaepefl agrtdtgylt rhdpaalgas sggarqaaaa alaaqarnrr aarvvpemps
      481 gwrnvggasq rvaytvgpet levayslrrs rlrvrvngep lggsvrllsa spslveleid
      541 gvhlayavrt yagvsyvdgp dgsvaltevp rfadpdaata tgsllaampg avvrvfaasg
      601 davtagqpll vleamkmeht vaapadgvls dlrvrqgdqv dtgqvlavvs
//
LOCUS       WP_284740107             108 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284740107
VERSION     WP_284740107.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..108
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11717
     Region          7..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mgtsttldat faaladptrr ailarlatgd atvtelaapf amsqpavskh lrvleraglv
       61 krgrdaqrrp chlvaeplka atawlagyrd yweasyrqld dllkdlqp
//
LOCUS       WP_284740159             222 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284740159
VERSION     WP_284740159.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..222
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23541
     Region          <2..220
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mwrtfptraa lleairttpl pappgsrvey ssqgfillgv iasaasgrpl drlvadlvtt
       61 pagmrdttfg paddavated cpwrgrvvtg evhdenavvl ggicghaglf apladvarlg
      121 rilaagaspl lkpqthaemi achtrglrrg lawqgldvpg spvgtalqpd syghtgftgt
      181 slwveparrr yyvlltnrvh psrardvsai rhafhdtaar is
//
LOCUS       WP_284740244             105 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284740244
VERSION     WP_284740244.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10601889
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..105
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11310
     Region          4..72
                     /region_name="HTH_26"
                     /note="Cro/C1-type HTH DNA-binding domain; pfam13443"
                     /db_xref="CDD:433211"
ORIGIN      
        1 mrwnlrmkaa ecgiwksael rrrladagle isagkmsalw agtpttirld dldvictvld
       61 ceptellire pekvaalrpa kaatnqagpt pvtprlghpr stppv
//
LOCUS       WP_284740257             369 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284740257
VERSION     WP_284740257.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..369
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41383
     Region          29..357
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 masddrlags aglhlatgvp llhpeeqvfa amldgwcnql larnlarstv asaqrvvrqf
       61 gehsgtypwl wtpqladewf adlravrhls lstvrnyqga lrrfgafvtd paygwaaece
      121 rrfgthpvkv inevnaavhv adseadaskr afsrvelqal fdyaddevdr kraagrkgwl
      181 tafrdatcfk vaygfglrrn etrmldvvdf grnphgpefg gygvldvrhg kakkgsppkr
      241 rsvlcvwewv aevveqwste vrpllgvdgn paqwpsergl rignkqlnrq latyrdalgl
      301 dpaldfhslr rayvthlied gwdprfvqeq vghdhastts iytcvssdfr trtlrrvldg
      361 tinralgwe
//
LOCUS       WP_284740276             736 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284740276
VERSION     WP_284740276.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..736
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=83672
     Region          <414..603
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mlhwlsampg tgwqqqwasa gcdhhsrwvd qaaegdprdr etslaefrag mnwlflarii
       61 qpsydyflhc ktytlfevap rvfsvdlfar ladsaakipt msvghyaaas ntlvkvvlht
      121 gkdlehlcak dllefrdwhr grqkkpegin tawdllreag vldsdramft mnrqgqrsts
      181 elvdfygirs nsirqvliay leerrpqvdy aslrgiagal agtfwadier hhpgidsldl
      241 pdtvatawke rlavirtadg qtrprksvld iftavrafyl diqewahvda swarwavrcp
      301 irrgdtngiv karqqataqm hqrvrerlpq lhvlvdtaer hlahqqallt agrvivgegl
      361 fthdgqlyrr iipvdelkkn prhrnhnrla vehvgtgars dliqseqdaf wswaiietfr
      421 htgvrieell eithlalvty plpdtgeivp llqivpsksn eerlllvspe lasvlatiit
      481 rlrrengstv altarydihd ringpalphl fqrrignnwr vfsyytvqrl lsdtvartel
      541 rdaageplrf tphdfrrifa tdavtgglpv hiaarllghs svattqsyla vfqddlvrsy
      601 rsfldnrrav rpeaeyrept sdewrefeqh fqlrklelgt cgrpygspcq hehacircpm
      661 lrvdpqqrhr lvaisrnlsd riaeakqnhw lgevrglets laaanaklls ldrtartttg
      721 sltdlgipql pprhqh
//
LOCUS       WP_284740331             447 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284740331
VERSION     WP_284740331.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..447
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46315
     Region          6..336
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtwpvdaddl sglltglvre ygvpgaqlav rwrsrtvtae ageetagtgh pvartsafpv
       61 gsltkpftat lvmllaedgd veldqpvaky lpqlgsatsg agqvtprqll shtgglvanl
      121 geqapgtdrr rwleggpape lvhppgtafs ysnagyllag clveaitgms waeavesill
      181 rplgitpssa lgaarppvtg hvvrpggrvl pvaeqtvtal eepvaalaag aadlvafaaa
      241 hlptaagpvd rrtaeamrnd qtagltagpf gladgwglgw slyrgtgarw fghdgtgdgt
      301 wchlraepds gtvvalvtna sngvflwdal verlrasgla vgscsmvapa eprdpvagra
      361 ecagrycngd ttytieaeng rlfltvdaep ateltcladl rfttvgptpl lgrfgrdpet
      421 gavdhvqitg rlarragtgh rrkdeea
//
LOCUS       WP_284740385             452 aa            linear   BCT 25-DEC-2024
DEFINITION  MBL fold metallo-hydrolase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284740385
VERSION     WP_284740385.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..452
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48331
     Region          3..182
                     /region_name="POD-like_MBL-fold"
                     /note="ETHE1 (PDO type I), persulfide dioxygenase A (PDOA,
                     PDO type II) and related proteins; MBL-fold
                     metallo-hydrolase domain; cd07724"
                     /db_xref="CDD:293810"
     Site            order(55,59,112,134,137,141..143,182)
                     /site_type="active"
                     /db_xref="CDD:293810"
     Region          253..>287
                     /region_name="RHOD"
                     /note="Rhodanese Homology Domain (RHOD); an alpha beta
                     fold domain found duplicated in the rhodanese protein. The
                     cysteine containing enzymatically active version of the
                     domain is also found in the Cdc25 class of protein
                     phosphatases and a variety of proteins...; cl00125"
                     /db_xref="CDD:444705"
     Region          350..450
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mieiiaidtp slgdrsylve dgetafvvdp qrdidrvlgl aqvrglritd vfethihndy
       61 vtgglalarv tgaayhvnaa dpvsfertpi edgdvidvgp hmrvralatp ghtfthlsyv
      121 laapgrvpav ftggsllfgs tgrpdllgpa htgelvkrqy asahrlaevl pddaeiypth
      181 gfgsfcsatq seadrstigr ekqvnpvltl qerdyvdgll agldaypayy ahmgpansag
      241 pdapdltppe tadpvelrsr iekgewvvdl rsrtafaagh vagtlnfgad gsfatylgwl
      301 ipwgtplsll gdtaeqvada qrelvrigid rveatatgtp dawtgdvplg sfpradfgel
      361 amvrhhrpvt vldvrrnqew tqnhidgalh ipihdlldrl gevpagevwv hcqagyrasi
      421 aasvlaaagh qvvavddefd raaraglpla vg
//
LOCUS       WP_284740414             113 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284740414
VERSION     WP_284740414.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 113)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 113)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 113)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..113
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11999
     Region          16..99
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mpsppdpepl ppellqdaaa sfgllsatvr lhllwllsqa ehdvgtlada tgqsvatvsh
       61 hlgklklagl vrarrsgkhq ihyvddphva rlvqlaiehh rgapahqpra hga
//
LOCUS       WP_284740415             411 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284740415
VERSION     WP_284740415.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..411
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44081
     Region          52..395
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtrgnetnsg gmprvfqrvg vtalavtlla gvsaaggtav agaaarqgrp elqetiqaiv
       61 dsgfagvqlr vhdqrgdwvg sagvrkldep akpptdgrfr igsttktfta tvvlqlvaeg
      121 kigldtpvdd ylpgfgfdrr itvrmllqht sglfnytgey ypdgtvvpgi pwsgkewvdn
      181 rfhtyrpedl vrfalakpar fapgtdwsya ntnyvvarll iekvtgrsya demqrrilrp
      241 lglrdtvvpg tspeiagpha hsyyryqdag qwktvditrq npswissage misttkdlgt
      301 fisallggkl lpapllaeml ephatpdpts dyglgvfelh adancsgtml inhngsvqgy
      361 gtlmystpdg sktleasiny vdtgvapaea yqkavqslie kvfcggragg a
//
LOCUS       WP_284740456             790 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-glucosidase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284740456
VERSION     WP_284740456.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 790)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 790)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 790)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 790)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 790)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12807938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..790
                     /product="beta-glucosidase"
                     /EC_number="3.2.1.21"
                     /GO_function="GO:0008422 - beta-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0030245 - cellulose catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=82304
     Region          26..385
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          58..757
                     /region_name="PRK15098"
                     /note="beta-glucosidase BglX"
                     /db_xref="CDD:185053"
ORIGIN      
        1 mssfvdsald lpakvalltg asmftlrpep aiglaelrls dgptgvrglt fsggpavtlf
       61 pnatllasaw ntgtayevgr llaeeaaaqg ihvvlgptin lhrsplggrl feaysedpll
      121 sgalaaayvr glqdngvgac lkhlvanese terhavdcvv deatlrevyl lpfeiavada
      181 dawsimaayn rvngtpateq ahvitdivkg ewgyrglvvs dwwattstap sanagldlvm
      241 pgpagpwgrq lvdavkagev deaviddhlg rllllaervg apqpsrevpa pdspvrraql
      301 trlaaegmtv ltneggvlpl rrdttvalig rhavdtidmg ggsaqvnppy qvsvaeglte
      361 llavtvvdgv evrerpvpag pefavhpdtg epgmrvtlha adgsqleerd cpaastmigi
      421 dddlpepprv vrlsarlprg grmlvggigi gtwevraggq tvrfelglts gdvgeavlrp
      481 pggtvlvdve pgelfeadva ldagrglygl varpapddva dvvgravaaa rsvdvavvvv
      541 glteeqetea vdkttlrlpg aqddlvaava avaphtvvvv naatpvlmpw ldqvdavlwa
      601 glpgqeggha vaaallgdie pagrlvttfp aadgaspaws vtpvagrley aegpfvgyrg
      661 haadkapapa fwlghglgys twaysdaaal ddvghrvavt vtntggrtsr evvqvyfrpa
      721 dedqpvrlvg wgaatvepgq sarvevtgdp rlrrrwdtaq gswadlpreg elllarglgd
      781 vratlrlgsa
//
LOCUS       WP_284740479             932 aa            linear   BCT 25-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284740479
VERSION     WP_284740479.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 932)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 932)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   3  (residues 1 to 932)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 932)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..932
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..932
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=99224
     Region          5..241
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          109..928
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          707..733
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          738..773
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          787..812
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(788..789,792..793,795,825,828..829,832..833,
                     835..836,865,868..869,872..873,876)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          817..853
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          864..892
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mgtvvrllge vdvlvngrpv dlgtprqrcv lavlaleagq vvradrlier vwgadatprt
       61 rttlhgyisr lraalapadg vtlarrsggy vlvtepevst vdlfryrelr adaradeera
      121 tallteavgl wqgealiglv gewveaerer lererlataq dladarlrlg lgedvvdela
      181 graeahplde rtagqfllal hqagrtaeal dhyrrvrarl veelgtdpgp alqelhrrll
      241 ttgtgrpgrp prsavprelr aapasfvgra ddvhrldatl daaraggtmm lavvrgtggl
      301 gktwlvlhwa hrrlgrfpdg qlfadlggfg agapmtpaaa lfgfltalgv epgsippdlh
      361 grsalfrtlt agrrllvvld naagtdqvvp llpggascav vvtsrnglag lvaahdarsv
      421 algvlpaada rellaarlga arvdaeretv delvglcggl plalsvlasr agarlsvlag
      481 elresgldsl adddpaaslp avlsssydal tedeatvfgl lalapgpdaa lataanltgl
      541 ppararavlr gleqmslleh dpdgryrmhd lvrayaaeta rtlpggvrda avrraldfca
      601 htayhaglll dthrgpvdlt ppepgpyvle lsgaeaamvw feaeratlla vqdaaasrde
      661 hetvwwlals tdtarqrrgh rddrlagwra avhaatslpg pvpalvahrh lgracaasgl
      721 reesarqlrh aiglagdhdd ryelghahqa lartlerhdd elalthaira lrlfedlglp
      781 vctahghnav gwhaarlgdh dtarghfdaa ltlhrengna ageadsldrl arlehdagnh
      841 deaiglhrra ltlrrglghl pasaetldhl glshaalgrt geareawqea lelyrcqgra
      901 eegervehql gglaaarpgh trasavhqkg ek
//
LOCUS       WP_284740564             173 aa            linear   BCT 25-DEC-2024
DEFINITION  flavodoxin family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284740564
VERSION     WP_284740564.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..173
                     /product="flavodoxin family protein"
                     /calculated_mol_wt=17883
     Region          3..164
                     /region_name="FldA"
                     /note="Flavodoxin [Energy production and conversion];
                     COG0716"
                     /db_xref="CDD:440480"
ORIGIN      
        1 mrivivfesm fgatekfara vadgiavsag aevlnvddap tdftgvdllv vggpthvhgm
       61 traatrksaa dqvayemrsk tgirewlgsl gplphdlvva afdtridkpr vftgaaslgi
      121 akrlsrlggr laapaesffv gtepvdvgpe pgelaraeaw gaalgaavlr tvs
//
LOCUS       WP_284740636             461 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284740636
VERSION     WP_284740636.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..461
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48759
     Region          9..352
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mskltelsaw lesrlpalla ehhvpgasva vyaggeiidh aagvlnkgtg veadaaslfq
       61 igsitkiwtt tlalqlvdeg tldldepvrt hlpefklgde daaaritvrq lmchtagfeg
      121 diftdtgrgd dcveklvatl gdvpqlfapg emfsynnagf cvlgrvvevl rgksyndcla
      181 ehlfvplglt haaaspyeai rfraalghva pepgaepepa giwalapsna pagsmlamrp
      241 rdlvtfagmh lrdgegpdgt rvlsaesara mrarvvelpd lglmgdawgl gwslfdwagg
      301 evvghdggti gqssflrlap ghdvavallt nggdpvpvyt eivghllkel tgialavppv
      361 pdraaprida tryvgeyass vaditvsqdd dgrvwvervp kgifaelakp ektelvamng
      421 dtlilaepmq gmylphafvg ddgtgralyl htgradrrvs v
//
LOCUS       WP_284740648             402 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284740648
VERSION     WP_284740648.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..402
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42958
     Region          8..402
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mtvsrdrstg alaglrvvda stlfagpmaa mhlgdmgaev ikiehprkpd psrthgaakd
       61 gvnlwwktlg rnkrtitadl gseggrevfl alattadvvi enfrpgtler wnlgydelas
      121 wnpklvlarv tgfgqlgpyr srpgfgtlae amsgfaattg epdgpptlpp fgladgvasl
      181 atayaimval sarantgrgq vvdtaiiepm lamlgpqitr wdqlrtvqpr tgnrstnnap
      241 rntyrtadgq wvavstsaqs iaervvrmvg rpdlaaepwf atgadrarha deldeavgkw
      301 igqrtrdevv tafeaaqaav apiydaadiv edpqfralgt iheiddadlg pmlmqgplfr
      361 lsghdcvigf tgrphgadtd avleelgfsp ervaelrerg av
//
LOCUS       WP_284740683             609 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 35 protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284740683
VERSION     WP_284740683.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 609)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 609)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 609)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..609
                     /product="glycoside hydrolase family 35 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65562
     Region          40..354
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
ORIGIN      
        1 mnsvsrrsfl ggaaaitaga vlagpagaag rrglsvsgdr flldgkpfqi vsgaihyfri
       61 hpdqwrdrll rlkalglnti etyvawnfhq pargradfsg wrdlpafvrl agdlgfqviv
      121 rpspyicaew efgglpawll adrnlelrca epaylkavde wydqliprlv pleaqhggpi
      181 vavqieneyg sygndtsyla hlrdglrsrg mtsllfaadg aseffmrfgs lpgtlevgtg
      241 dgdpapsvaa lkkfqpgapv mmaeywdgwf dhwgeqhntr dpaqmasyvd sllatgasvn
      301 lymacggtnf gftagantsg ttyqptvtsy dydspvgeag dlgakftsvr avltkytgvp
      361 agpipgrsar lpaqtvtpsg avslldslpv lsspvrsaqp vpmervgqst glihyrttvq
      421 gphsgplsih gladralvfv dgaylgvldr nqpsgtlnls ltaastrldi lvdamgrvny
      481 gpyladrkgi dgwvamstqq klfgweirpl pledlsrlrf sagavsgpaf hratvsvgdp
      541 edgfvalpgw ekgvvwlngf nlgrywkvgp qrtlyapkpl wrrgvneivv lelhqpgavi
      601 evrpeadlg
//
LOCUS       WP_284740760             134 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284740760
VERSION     WP_284740760.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..134
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14464
     Region          33..77
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(34,38,63)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(37,62)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(44..45,56,59,63..64)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 misnsqvvva sqnegsrmse rgsfdaaaff aalnaerear gllwkhvaeq akvsqstltr
       61 laqgkrpdvd slaalvdwag lraddyvvrv lnkteaepia mistylradp nlspaaaeam
      121 etvvratyqa lren
//
LOCUS       WP_284740802             517 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA synthetase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284740802
VERSION     WP_284740802.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..517
                     /product="acyl-CoA synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016405 - CoA-ligase activity [Evidence
                     IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0032787 - monocarboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=55528
     Region          7..500
                     /region_name="FACL_FadD13-like"
                     /note="fatty acyl-CoA synthetase, including FadD13;
                     cd17631"
                     /db_xref="CDD:341286"
     Site            order(162,165..170,172..173)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341286"
     Site            order(165,278..279,299..304,391,403,406,417,497)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341286"
     Site            order(165,205..206,251,253..254,257,278..279,299..304,391,
                     403,406,414..417,478)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341286"
     Site            order(205,253..254,257,278,414..416,472,478)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341286"
ORIGIN      
        1 mslyfylekg asldpdapcl tldgssvsyg qvvelaeava ralrhsgvrp gdkvgilsan
       61 dptaftcvfg iaragavwcp inprnaagen aelldlfdca tlifqpgfed lvrqiapklp
      121 klttlvrlge gddfapgfpd wldaarddpg veaaqpgdvv alvgtggttg rpkgvmltgr
      181 nleamsaitl msypfegrpv ylalapltha agvlcfpila rggevvimak pdvgrfleli
      241 erhrvthtfl pptliymvlg healdrtdls slqcfwygaa pmsttrltea lgrigpmaql
      301 fgqseapmmi stmspadhrr pdgtvhtgrl ssagrpsplv tvaildedgr pvpkgergei
      361 cvrgslvmag yyrnpeatae asvhgwhhtg digflddegf lhivdrakdm vitggfnvys
      421 aeveqavmah davrdcavig lpddkwgerv tavvqlqpgr eldtgeliaf vkdrigsvka
      481 pkqieiwpel prstvgkvlk adirstfter skeavrp
//
LOCUS       WP_284740808             490 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284740808
VERSION     WP_284740808.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..490
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50333
     Region          13..490
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mvesgqvpga svadtvaspq rsgaletrgi epvpagerhg hpmqlfwvwf aanisilglp
       61 lgatlvavqh lafwqaalva vlgavgsfav vgvvsiagrr ggapgltlsr avfgvrgnig
      121 ptvvslvsrl gwetvnttta afaflslcai lfganadaka spvltiagva lfvlltvtvs
      181 glghavlvav qrwstwifga lnvvvavsli trihwgqvfa aspapvgami agvgtiaagt
      241 gigwanasad msryqsptvr agslvasaaa gagiplvlli slgslvsadd pslasagdpv
      301 aairellpsw mavpyliaaf gglllsnhls vysaglttlt lgirlkrvya vvvdiivtfl
      361 gslyfmlvad gfygpfiafi sllavpitaw vgvfvvdmvr rrdydpaalm dvhrtsaywy
      421 ragceprall awaaaivagy lfttagtgdd awftgplagt wlgvnglgwv vtfavgagly
      481 aalggarirr
//
LOCUS       WP_284740817            1323 aa            linear   BCT 25-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284740817
VERSION     WP_284740817.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 1323)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 1323)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 1323)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 1323)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1323
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..1323
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=141779
     Region          31..1321
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 mttfdtrpea daeraarlra avlakrlrgr atapvrtfgr adrdiplpls agqqrlwfld
       61 rldpdsaeya vplllrldga ldidalqhal delvarheil rttyvaednk prqvigapap
      121 velpvldgdl dvvladyvsr pfdlaagpvf rallireape rhvlalnvhh iacdgwslpi
      181 lledlrklyt gaepppiels yadfavweqs rvdahdadla ywkdrlggle tlelpadrpr
      241 paqrdhhgas arftipasaa eavlnqgkst gatpfvtlla aayvvlgrht grqdiavgtp
      301 vagrgraele hmvgffvntv vargdlsgdp dfvaladrvr varladqahe dlpferlvqe
      361 lsperdlaht pvvqvmfavy dasegegalg dlavssvdlp sstakfdlmi sfvrqadgsv
      421 egvleyatal fdqarmdrmg ehfvrlftel aakpgvrlse vdvlgaderk llletwnata
      481 epylrgtlhg riaeqaasnp daiavrcgga eltyadletr atrlaqrlra hgvgvetpvg
      541 vlcergplll pvllailktg ghyipldpay pqdrkeymlr qagarvlvtt rryanenlgd
      601 vlvfadepva ddpvpwadpv vdpedlayvi ytsgstgrpk gvmishrgvl hyldwcrqay
      661 radegdgapv hsslafdltv tglflpllcg ttvtlvpede hpvagladvl ssgrkfsfvk
      721 ltpahleplr rclapeaaaa aahlvvggeq ltaealefwr enapevvvan eyghtetsva
      781 nvinllpaae cvttpisvgr piwntevyll dehlrpvpvg vtgelyagga gvargfagnp
      841 gltaakyvan pfgpgrlyrs gdlarylpdg rlefvgrtdh qvkvrgyrie lgeieaalvg
      901 gpgvteavav vrdgalagyv apstvdseal rahlserlpe ymvpstlttl atlpltsngk
      961 idrvalpapd atpvatsgvl prdelemala klwedllgrr vgvtdgffdv gghsllavvl
     1021 vdrikaelga tvglaevfra ptiraladhl ragesggglv vplspgragv aplfllppta
     1081 gspfpylqlv aeldpalpvf glqapgfapg edpvhtieel aaafiadllp vagdrpirla
     1141 gwsqggsvaf emaaqlekag ravehlcvid atvlgvddyg nplpevdtsd plawfgeavl
     1201 klepgvdtld emlaeardrg mvsevagnav veqmarvyla gkdaveayrc ravvdagihl
     1261 itstgshpvk grpevrpesw rartrgeltv tpvpghhwdm vepphvaela ravlaglavt
     1321 ade
//
LOCUS       WP_284740873             947 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284740873
VERSION     WP_284740873.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..947
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..947
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=99106
     Region          <4..911
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mssripfpsp parlvgrrre ldrftesrry agdghghall vrgpagigkt sllaaalhda
       61 aadlpapgri ltaaaarkda ntaygvvrdl faplglagea gesllqgsar farhalttda
      121 vaeplavssy avqhglywla atlatpgpli lvvddvqwcd esslrwlefl vrragdlpll
      181 vvlaqrsgta isadgtlaei agahdtrtld lgplpfdava elipeplata dglfartcfd
      241 etggnplllr rmlgelarar tgdeplslss vagsgravla tstldrlsap travamavav
      301 lgddepglla klaevpgtvv staletlqah eilldgtref vhelvraavl daggagepdr
      361 whrraarlls dagrpaeeva ghllllpeld egwmagimre aarsatgrga pgtaarylkl
      421 alvfapadvg lllelaaala padpvaafdl lqqarglagd vrerariavr lgmvalavqr
      481 apeavtvlrd vageldarlg eprsvadagl rtlvesmali tgldekgtvp aalarvreqp
      541 tpagddpaec qllgmraaar alegdsaama aaeatralrv dpaglggwaa lgaglalqla
      601 delkpaqdal grliehasga gdawtyclgq ctramfwhwa gdlteagada qvsydlahqe
      661 swgetttmpr ialatvlapr geaaraeell dgitrpridr faleyhwylm araaaraglg
      721 dpsgaleylr rcgeslsgag manpvfapww legacllael grfsegrela ehgqalaerw
      781 gtpravgmgl laagvttsga egvellteaa rtfeggpglr ehqraeyllg rallarddrr
      841 garehlrrav dgctrtgdrl lldaartall aaggrpgpqg gsaldtltgs errvaelaag
      901 gdgnraiaea lfvtvrtvem hltsvykkls iagrpdlaaa larrdav
//
LOCUS       WP_284740886             241 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284740886
VERSION     WP_284740886.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18629734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..241
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26391
     Region          43..217
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          158..220
                     /region_name="GerE"
                     /note="Spore transcriptional regulator GerE (stand-alone
                     HTH domain) [Cell cycle control, cell division, chromosome
                     partitioning, Transcription]; COG5905"
                     /db_xref="CDD:444607"
ORIGIN      
        1 mpeiqvhgsv tdsrfspdqe keiggeyqrm fssflensdv ssailddrlr vvaanrella
       61 lfgrsaaevc radlpgllhp fvservqrrl trlvlegerg frerftplvp aagalpvtli
      121 aaalpgrrpa aaaalllflp drvqrrsidp agrnramsei etqilqgvaa gastaelarr
      181 lylsrqgvey hihrmmrflk vknrtelvsr ayvagllapd vwppqvlpgr avagraavpa
      241 r
//
LOCUS       WP_284740961             412 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284740961
VERSION     WP_284740961.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..412
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44147
     Region          131..389
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtehkpggdl tlggqrvher ltqeepelia rvltriqadv adyrrlpvee lagdiaritr
       61 qavrafarsl redrqlndae lrqigasavr raeegfplea vltayhvgar eifavgsada
      121 tgtdvadvld vadrvlafvg titgavtrgy leelrtkvgq ehtarrtlls vladggpvdv
      181 varsagitlp arylvlsvel gphadeaspg vdadiairrk lrrflaafeq scgdgvlasl
      241 dgpgglvllp lagrlsavpe wgalldtagr aagvdvlaaa dtaapsevre aagltgevld
      301 vlrwfgrspg lyrlddvlme yqltrpgaar drlaaalapl dahpelvetl styleldtnr
      361 rrtaaklhvh pntvdyrlrr vrdltdidpl hpaglpriia alaarrattp pp
//
LOCUS       WP_284740966             563 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284740966
VERSION     WP_284740966.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..563
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=61971
     Region          47..540
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mtsavptaih hdepagrpit mfgpdfpfay dehlahpagl gsvpahrhgt evavigggls
       61 givtayelmk lglrpvvyei aeiggrlrtv rfpgcpddvv aemgamrfpp astalfhyid
      121 kvglettpfp nplapetpst vvdlkgeshy artpgdlpav fadvaaawdr tlaehasfae
      181 mqtairdrda ktikrlwnel vpkldnqtfy gflcdspafa sfrhreifgq vgfgtggwdt
      241 dfpnsileil rvvytgadde hrsiaggsrq lplrlwdhap selafwpagt slaslheggp
      301 rpgvtrlhrt apnnitvtda sghirtypaa vftaqswmll skiecdealf pidhwtaier
      361 thymesskvf vpvdrpfwld rdpatgrdtm smtltdrmpr gtyllgddps kpaviclsyt
      421 waddslkwlp lsvservevm lqslreiypg vdvrrhiigd pvtvsweaep hfmgafkanl
      481 pghyryqhrl fthfmqdela erhrglflag ddvswtagwa egavqtalna vwgvlhhfgg
      541 etdpanpgpg dcfadlapit lpd
//
LOCUS       WP_284741090             364 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284741090
VERSION     WP_284741090.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..364
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=38459
     Region          1..336
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mtvtiigagl gglvlarvlh rhgilvtvye aepspaarrq ggmldihpwn gqpaleaagl
       61 iegfrelvlp gresyrvvdr ngavltdrpd dgtgerpevq rgelrqllld slpqgvirwg
      121 hkvtgvrplg dgchevslad ganvvtsllv gadgawsrvr pvlsdaspsy vgftvvetfl
      181 fdgdarhpaa akvvgagslf alapgkgila hresggtlha ytqlrkpsdw ldgtdparvi
      241 eefadwapel talitgsdvp pvvrrlftlp aghrwdripg vtllgdaahl mppngeganl
      301 amldgaelgq slaahpddve talaeyekam feraaaeadd ediyavmfgd daphsmaall
      361 tgae
//
LOCUS       WP_284741122             104 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284741122
VERSION     WP_284741122.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..104
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=10513
     Region          2..104
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mgwatlicag lveiawsqsi kptenftkpw ptllcfvlga aavyllsram dtvpvgtaya
       61 vftgigavga ivlgvvvtkd plsvgrvaal alivggvvla rvts
//
LOCUS       WP_284741140             376 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284741140
VERSION     WP_284741140.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..376
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39524
     Region          2..368
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mltellkqha advpgavalv ahgdqveaaa vgsadaggtv pmardslfrv asltkpivaa
       61 avmllvddge lalddpiarw lpelaspvvv rtpagpvddv vpaarpitva dlltfrcgyg
      121 laadmtlpav dlllqvlghp aaasralapd awtaalaqvp llhqpgeawl ydtgsdiqgv
      181 lvarvsgrpl peflaerlfe plgmadtgff vptaalgrft sayrrgeagl rlidspegrw
      241 saappfpsgs aglvstaddl lafgrfllae gragdhrllt pesvrrmttd hltpaqreag
      301 rvflhgqgwg yggavdveak qlwqvpgryg wvggagtawh llpatgtvtv lltqvemtsp
      361 eptrlmrefw tyaass
//
LOCUS       WP_284741174             255 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284741174
VERSION     WP_284741174.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..255
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27191
     Region          5..249
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mgvlagaepf ghtgsaetgf llchgftgtp asmrawgdhl agagftvrcp llpghgtrwp
       61 dlnrttwedw ygavrealla llstcktvfv gglsmggtlt lrlaeefgdr iagivlvnps
      121 vtrlkwdtkl lpvlgkivps vpaiandikk pgetelaypr tpvraaasla klwalvradl
      181 pkvtqpvlll hssvdhvvep ensrlvlqgv sstdvtevvl ensyhvatqd ndaeviftrs
      241 vefakahaaq peeta
//
LOCUS       WP_284741191             300 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284741191
VERSION     WP_284741191.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..300
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33143
     Region          13..75
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(19,23,48)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(22,47)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(29..30,41,44,48..49)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          96..277
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 margqsptvr rrrlagelrr lreaadltid evgeklecsa skvsrietgh vgvtprdard
       61 mlalygivgd eqealvqlar earkrgwwha ynevftgtfv gleadasslr afqallvpgl
      121 lqteryarav iralrpdaed detrrrvaar marqellsdt pppeywavmd eavlrrvvdg
      181 pevmaeqlyr mvalaekpnv tiqvvpfgag ahpgmegpfl imgfpeqadp dvvyvddsts
      241 sglyleeptd vrryglmfdh lraaalkpdd sveliaeaag rfaeqaaapa pvhqleprtq
//
LOCUS       WP_284741224             461 aa            linear   BCT 25-DEC-2024
DEFINITION  WS/DGAT/MGAT family O-acyltransferase [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284741224
VERSION     WP_284741224.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Stoveken,T., Kalscheuer,R., Malkus,U., Reichelt,R. and
            Steinbuchel,A.
  TITLE     The wax ester synthase/acyl coenzyme A:diacylglycerol
            acyltransferase from Acinetobacter sp. strain ADP1:
            characterization of a novel type of acyltransferase
  JOURNAL   J Bacteriol 187 (4), 1369-1376 (2005)
   PUBMED   15687201
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Kalscheuer,R. and Steinbuchel,A.
  TITLE     A novel bifunctional wax ester synthase/acyl-CoA:diacylglycerol
            acyltransferase mediates wax ester and triacylglycerol biosynthesis
            in Acinetobacter calcoaceticus ADP1
  JOURNAL   J Biol Chem 278 (10), 8075-8082 (2003)
   PUBMED   12502715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496208
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..461
                     /product="WS/DGAT/MGAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0045017 - glycerolipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=49744
     Region          4..460
                     /region_name="acyl_WS_DGAT"
                     /note="acyltransferase, WS/DGAT/MGAT; TIGR02946"
                     /db_xref="CDD:274360"
ORIGIN      
        1 mqrlsgldas flyletpaqv lhvcglmtld gstvpggytf akleekleer vrmipafrrk
       61 lhnplwnigh pvwvededfd ldhhvhrigv papgdraela elcahiagqq ldrahplwql
      121 yviegladgq iavllkmhha svdgvsgasl itylaglepd apapeieepr npampsplnl
      181 lrtsvesfak rpaeivrllp dllglvpqwl gkalrgkgmp ipftaprtsl ngtitghrsv
      241 afaqldlddv kaiknafgvt vndvvlalva galrefldar gelpddplva tvpvsvhdrt
      301 erdhgsnkvs affaslpthl adpaarvffl aeanrlskdh hydidadmlq dwaqfsaata
      361 fglavraysa lrlaekhpvv hnlvvsnvpg ppmplyllga ritglyplgp vfhgaglnvt
      421 vlsnagklhv gllgarelvk dlwpladalp ealaellkaa g
//
LOCUS       WP_284741211             187 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: GTP-binding protein [Amycolatopsis].
ACCESSION   WP_284741211
VERSION     WP_284741211.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis
  ORGANISM  Amycolatopsis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Takai,Y., Sasaki,T. and Matozaki,T.
  TITLE     Small GTP-binding proteins
  JOURNAL   Physiol Rev 81 (1), 153-208 (2001)
   PUBMED   11152757
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006198
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Amycolatopsis"
                     /db_xref="taxon:1813"
     Protein         1..187
                     /product="GTP-binding protein"
                     /EC_number="3.6.5.-"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /calculated_mol_wt=20357
     Region          1..184
                     /region_name="Srp102"
                     /note="Signal recognition particle receptor subunit beta,
                     a GTPase [Intracellular trafficking, secretion, and
                     vesicular transport]; COG2229"
                     /db_xref="CDD:441830"
ORIGIN      
        1 mtsakivvag gfgagkttfv gsvseivplt teammtdasv gvdnldhtpg kstttvamdf
       61 grvsldadli lylfgtpgqq rfwfmwddlv rgaigavvla dtrrladsfa pidffedrgl
      121 pyivgvntfd gvlehdindv realsidpni pivrcdardr estkqtlitl veyamrqwia
      181 lraaknr
//
LOCUS       WP_284741248             340 aa            linear   BCT 25-DEC-2024
DEFINITION  fatty acid desaturase family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284741248
VERSION     WP_284741248.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..340
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37708
     Region          2..339
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mtttenpvst gsdfarlsqr isaaglmvrr pgyytarfai vgglfaagwv afallgnsww
       61 qlavaafqav mfaqiallsh dlahkqvfrr rrpteiagml vgnlgigmsy gwwmdkhtrh
      121 hanpnheeld pdvdpdifvw skgqakeasg varfigryqa flffpmltle glnlhvsgir
      181 avckpglrrr wveasllath vvvylvalft vlspgmallf lavhqalwgi ymgsifapnh
      241 kgmptltgqp eldflrkqvl tsrnvrgggv tdvalgglny qiehhlfpsm psrhlrlaqp
      301 ivqeycaeld ipyletslie syrqalthlh eagaplrnrs
//
LOCUS       WP_284741271             263 aa            linear   BCT 25-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284741271
VERSION     WP_284741271.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     BTLCP proteins: a novel family of bacterial transglutaminase-like
            cysteine proteinases
  JOURNAL   Trends Biochem Sci 29 (8), 392-395 (2004)
   PUBMED   15288868
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..263
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=28385
     Region          56..206
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mapratvdve fsvrvtepga aaisvaaaha dteelavswh geselvefeh gtraevfefp
       61 agehrvtyha ervlaepepe pvtradaavf trpsrycpsd riaglvppel fslestkkkv
      121 dtivrnvher lsyvvgsgrp tddaidtlla gegvcrdfah vcitlcrfld iparyvgvya
      181 pglspmdfha vfeagvdghw yvfdathlap rrtmlristg rdaadtsfla tlgceldflg
      241 stvfattdaa lpvddgtelv vlg
//
LOCUS       WP_284741278             254 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284741278
VERSION     WP_284741278.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..254
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27888
     Region          25..249
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mmdrwtplet egelltrrqm iaygrrfara grgawysfai evvwqflvqt trfrvrgshh
       61 ipksggvlva snhlsfadpa tltafclaag rvprylakas lwklpvlgrv mrsgrhipvy
      121 rgaataaeay rdlvasvrdg ecvavfpegt fsndpagwpm rgktgivraa letgapvipv
      181 anwgthhllp stawfprglp rktvelvagp pvdlsdlrdr pltrevleea tarimaevtt
      241 llesirgerr pvaa
//
LOCUS       WP_284741524             273 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284741524
VERSION     WP_284741524.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..273
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28044
     Region          4..267
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 msevlrswly vpgdrpdrit kalsgpadav iidledavaa aakddarrnt laalgdgata
       61 fvrinapgtp ageadikala slapagvrvp kcedpgelrr vadalgvpvy pvlesalgve
      121 nalaiatahp lvagislgea dlaadlrvtg gdaltwprsr vvvaaraagl pspvqsvwta
      181 vrdldglrts teagraagff grsvihpaqi pvvheacapd paetawasal ldrlatdgaa
      241 awidhhgqfv daaivararw vlalagereg qhs
//
LOCUS       WP_284741611             403 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284741611
VERSION     WP_284741611.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..403
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43020
     Region          144..397
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mgearadard tawslaarvl deldeltgal vaviveqnpg yrvvdvvpdd dlwrschdnl
       61 rrvlqligrg aetsedlyda akatgrrrae qqlplddvlr sfriggrlvw qaltakarat
      121 gyvnneamld latrvwevvd atsaqvalay haaersfvra deqrraslwe gllqgratda
      181 gfayeagral rlpisgpyvv vaaagpgdaa faeplgstle dagsasawqs radvlvglvs
      241 lpgrevaeav eaigsvltvp agvslvvdgl aavhtayrqa vlamrtvppg raavvclaer
      301 lpealllssp elteslqqnw lgglldlrav ergplletla twvrtggsat rsaqalhchr
      361 ntvlnrihri eeltgrsltg gdlalelalv vralpflppp rvp
//
LOCUS       WP_284741623             233 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284741623
VERSION     WP_284741623.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..233
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=25615
     Region          171..222
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(175,179,204)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(178,203)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(185..186,197,200,204..205)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 maltivdpft agarrghrsp vrqvrqdrrt lliapagqnr afhasrfrdy tehlggrtli
       61 emesagrsqg tsievvavei vtkifparps avprirefvq eclgeaplad aedreignti
      121 lralltaagp sgvlevscrk ypgrvefdvl psrgrpaspa strpepaasf aewlaealrs
      181 rgitkesaae qldvspktlt rwlggqtepr lrdlrriedr fgdvrlrrgt evt
//
LOCUS       WP_284741634             733 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284741634
VERSION     WP_284741634.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 733)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 733)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 733)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 733)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..733
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..733
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76228
     Region          1..723
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtcgscaari erklnrvdgv ratvnyatgk aavsvpaslt vedvvaaiea agytaqlpap
       61 peqepvpgad plrqrllvsa vlavpvivla mvpvlqfpaw qwvslvlatp vvawgagplh
      121 raawanlkhr tatmdtlvsi gvaaaylwsl yalllggage igmrhefdfs laadhdvdgi
      181 yfevatgvtl filagrffea rsrrragaal ralldlgaks vsvlrdghee ripidelrtg
      241 drfvvrpgek iatdgviedg tsavdlslvt geavpvevaa gaevvgatvn msgrlvvcat
      301 rvgadtrlar iaamveraqs gkadvqrlad rvsavfvpvv malslatlvf wlvsgaetaa
      361 aftaavavli iacpcalgla tptallvgtg rgaqlgvlvk gpemlestrr vdtvvldktg
      421 tvttgkmsla avrtddgtpr dlalqlagal enasehpiav avtaaavkrf gwvgqvrefr
      481 tvagfgvlgr vdghrvvigr pellrrlnvr lpqsllrake raeqegntav ilawdglaha
      541 vlvvadsvkp tsapavfqlr rlglnpvllt gdnetvarai greagitdvi agvspeqkve
      601 viqgmqaegr vvamigdgvn daaalatadl glaigtgtda aieasdltlv rgdllaavda
      661 irlsrrtlat ikanlfwala ynvaalplaa agllnpmiag aamamssclv vsnslrltrf
      721 rgsatgelpe par
//
LOCUS       WP_284741703             371 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284741703
VERSION     WP_284741703.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..371
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=39571
     Region          21..356
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mirhaivagg giaghaaaia lrkagidvtv leqrhaedgl gsfmrlnpng ldalaaldvl
       61 dpvmnvsfpm thveaygpdg tllvnrplsd pvperglgar fvtwtnleqa lraeavrrga
      121 svrhavrvtg atgaddgvaa lladggrvdg dvligadgtr sviraaidde apapeycgsr
      181 tvygytpktp advppapaql rayrgegrll ahiddpvtge qywftnlktp dqlpepgpst
      241 dewrdqllal wpdadapaag iiaaassira addkalhhlp rwhtdrlvvi gdaahaappa
      301 teqggaiale daavlgqclr dlelplalar feqlrrdrve kiigfatgrl tttespnwsy
      361 hhhidwsrqi r
//
LOCUS       WP_284741887             225 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284741887
VERSION     WP_284741887.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..225
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24241
     Region          44..145
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mtttywnrya lgaanaaadd esaptfrwtq ypshgpgiel lgdprssvel gcgrgdavaa
       61 laargvaatg vdlsgtqceq arhrwghvag arfehtdvld flaatdrtwd aiysiwgaiw
      121 fldpalvlpl arerlapggk lvfshappvp gaygiqgmyg aaftadplwv yrwsyepdvw
      181 aellrrhgfg niharveaap epgklgtliv eaerrpdpar vsahg
//
LOCUS       WP_284741896             110 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284741896
VERSION     WP_284741896.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 110)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 110)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..110
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11766
     Region          5..110
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mastppqart eelvramraf gsasrlellr amldprqlda apgevsehgv clallartvg
       61 iagptalqhl sklveaglcv ktadrrgggf tfyrrdenai tdvadrlrhv
//
LOCUS       WP_284742063             516 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284742063
VERSION     WP_284742063.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..516
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56425
     Region          8..504
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mtepthhsrr tllkagltga aatlvlpsta faatpllrgd rpvlthgvqs gdvtpgsaiv
       61 wsradrpsrl vveiardpsf rharrvpgal agpatggtgq vrvaglapgt eyhyrvtaes
      121 ldgratsepl tgrfatapvg rrdtrilwsg dvvgqnwgin pdlggmtifs amadrrpdlf
      181 lhsgdtvyad gpltetvslp ggrtwrnvvt aekskvaetl deyrgqhayn rldahfkrfa
      241 aqvpvyaqwd dhevlnnwyp geildlpayt ekrvdvlapr ayqafhewhp idsrqavdgr
      301 vyrsfkygsr aeifvldmrt yrnantadqt kpgyilgdkq arwladalgr statwkivqa
      361 dmplglvvpd gtdieavann lpgapggret elawvlreiq rrrvrnvvwl tadvhytaah
      421 hyspdraafq dfdpfwefvs gplnagafgp naldptfgpe avfvhappva ntapidgfqh
      481 fgelnidggs gdltvdlrda tgvslwskkl hpqgrr
//
LOCUS       WP_284742066             103 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284742066
VERSION     WP_284742066.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 103)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 103)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 103)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..103
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=10921
     Region          12..90
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 miedalttal pvlralgeat rvriigvfld rggsatvgev qselglpqst vsrhlrilld
       61 arlltvgrag pnriyrldvp adaldaldav ttrvrecqsa php
//
LOCUS       WP_284742097             630 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284742097
VERSION     WP_284742097.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..630
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64045
     Region          19..>245
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mtalasrett avtpsppapr twhrpalavl llgtavlylw glgasgwana fysaaaqags
       61 eswkalffgs sdaanaitvd ktpatlwvms lsarvfgvna wsilvpqalm gvgsvwllha
      121 tvkrtsgpaa glvaglvlal tpaaalmfrf nnpdallvll lvagaycvvr alekasprwl
      181 alagvavgfg flakmlqafl vlpafavayl vaapvslgkr llhllgalaa tvvaagwylv
      241 vvalwpaadr pfiggsqtns lwelvfgyng fgritgdevg svgggggrgw gstgltrlfg
      301 semaggiawl ipaallalga glwftrrapr tdrsraalll wggwllvtal vfsymggiih
      361 pyytvalapa iaalvgtaav qlwrlrarps asgllsggva ltaltaylll sgsswqpwla
      421 pavlvgglla avglffashl trwaassvav lglvvllsgt gaytlataat thdgaipsag
      481 pssgfggfrg gtggpggpgg fgggrgggpg sllsttlpga sltallrqda shytwtaatv
      541 lsnaaagyql asgapvmavg gfngtdpypt laqfqqyvaa grihyflgdg mtmqgstgsd
      601 aaqqiaewva styrattvdg vtvydltaaa
//
LOCUS       WP_284742134             333 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284742134
VERSION     WP_284742134.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..333
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37358
     Region          4..317
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 marpltlftg qwadlpfeev celasgwgye gleiacwgdh fevdravaed gyvrakletl
       61 akydlkvwai snhllgqavc dhpiderhea ilpvriwgdg epegvrqraa aemkttaraa
      121 aklgvstvvg ftgssiwhtv amfppvppsm iergyadfat rwnpildvfd evgvrfahev
      181 hpseiaydyw stvrtleaig hreafglnfd pshfvwqdld pvgflwdfkd riyhvdckea
      241 rkqlngrngr lgshlpwadp rrgwdfvstg hgdvpwedvf rmlnaigydg pisiewedag
      301 mdrligapea lefvrklnfs pptaafdaaf ssk
//
LOCUS       WP_284742176             139 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284742176
VERSION     WP_284742176.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..139
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15276
     Region          1..134
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mtyvahvrpr wtdmdvyghi nhakmvtlle earipllfkg aveagleelp kgivvvklev
       61 aykapivvsg qelrvdidlt elraasfrlv yrvhtgpaes dpvavtaetv lapydtvalr
      121 prrlsppese flkqgfada
//
LOCUS       WP_284742178             839 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284742178
VERSION     WP_284742178.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 839)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 839)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..839
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..839
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=89851
     Region          <249..>357
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          <408..677
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 measkqhrtg plshesgraa naggtlsavg rlieradalh lrapelalvl geraaalsea
       61 agadeqwirs eslvvsarvr lgerpstvgr avaalraaeh agygdiaarl ridlavcars
      121 lgvpltglaa lrpvltdpvv spvhraaalt hlvgclgllg rkaeldralv eadklvlgde
      181 slgadtqllv rallrvgtaa hrrrhgdlta aadaartglg flekldnpad dgglvrirlv
      241 lllvstlldr gdaemayeia epilaepvra agvapmgwlr lavatrihls sgsgeaaiel
      301 vreavastdr hglsaitarl wlelaqleer fgqpeeaiac lyrsraaeql hararrqacg
      361 vlagefgtge pasvdldevl kavpsrpvpv vaevvaapep slrtpgwsfg reetpkpepr
      421 qpapawsfer prvtadaaet slmpavrdep aeprvrpepv vverrrpepv eaqpagrrep
      481 epievrsasv epvrrsesvd pprrelepie vrsasvepvr rpesvepppr elapievrsa
      541 pvdppwrres pgqarpipat pepavaqpsg rrrapevpae pievrtaper raepaetraa
      601 apeppaprei ektkfswaal aearlretaa eresaptrit palplapepa aereprrepq
      661 pstrhdaehg seaaqsvldr lgisssagas ggrrraedad sraddsprre raepelappp
      721 rpedeppsvp dyrdeaepwl prlrmppsle pmedfghwtp atapfpesya raiaedeppp
      781 dagladllar alaehqagta saaalvkqlg skdtgrrngh grnghgaevp dsrrhgsgd
//
LOCUS       WP_284742186             414 aa            linear   BCT 25-DEC-2024
DEFINITION  cytochrome P450 family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284742186
VERSION     WP_284742186.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 414)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..414
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=44687
     Region          16..405
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(52,59,88..89,96,100,107,237..238,241,245..246,249,
                     282,287..288,291..292,294,318,346..348,351..352,354..356,
                     360)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(59,82,84,87,89..90,175..176,185,236..237,240..241,
                     245,288,291..293,395)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mesrcpvldt tgrdihgeaa rlralgpatr velpggvlaw svtraevikk lladsrvtkn
       61 arnywpkfin geippdwemi swvamdnmvt atgkdqvrlr rlvgkaftpk rteairpriv
      121 altnmlldal aaagpdevvd lrerfayplp amlvaeligm deqaraatak vidmmvdttv
      181 tpeqaqsvla gwrgamdeli atkranpged itsdliaard edgsrlseqe ladtifailg
      241 agsettinff dnaitallth pgqlelvksg evawsevide tlrvesplas lplryamedi
      301 dlgdgvtipk gdpilvnyaa igrdpamhge sacefditra dkehlsfghg phfclgagia
      361 rlvatvglss lferypnlal avepaelepl stfimnghra lpvhlkgaes aaaq
//
LOCUS       WP_284742201             406 aa            linear   BCT 25-DEC-2024
DEFINITION  cytochrome P450 family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284742201
VERSION     WP_284742201.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 406)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..406
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=44693
     Region          15..404
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(52,59,88..89,96,100,107,237..238,241,245..246,249,
                     282,287..288,291..292,294,317,345..347,350..351,353..355,
                     359)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(59,82,84,87,89..90,175..176,185,236..237,240..241,
                     245,288,291..293,394)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mdkcpyvldr sgsdlhqenk nlrargpvtq velhggytaw svtgyeearq llvdpriakn
       61 tkdnwpefqa grvpqdwelf twvamdnmqt rdgaehdrlr klvaraftsr qvaksrpiie
      121 givnrlldel atvpadevvd vkgrffypls tilvcdllgi reedqkamlq gaqvnaktdn
      181 taeeaeanlh qwhealgrlv etkrrepgdd lttiiikate ddeapltdee vvgsvhllig
      241 ggtettanvl chtlvdllth pdqlaairsg easweeawde evrkdgavgs mpfrcaledi
      301 eiggvtiakg dlvlinylaa grdpakygdt adefditred ksslgfgygr hrclgpalat
      361 meamvalpal ferfpdlkla vpatelkpaa tfifngpaev plllkg
//
LOCUS       WP_284742469             291 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284742469
VERSION     WP_284742469.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..291
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=30909
     Region          3..288
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mkpakfayhr pdratdaval lgklgenakv laggqslvpl lslrlayfdh lvdisrlpel
       61 qgvrrtgdav rvgagtteaa vgrddnlrts vpllsrvtpf ighfqirnrg tvggslahad
      121 paaeypavav aldaefdvls ladertipas efftglwsta lepgellvav rfpvwsgrcg
      181 faveefarrh gdfaiagavl gvqvaedgrv rrcaiglmgm gstpkrarqa ehsatgvlls
      241 evdprelgel aasgwddtps dlqgtadyrr kvcasmvara wgrateeath g
//
LOCUS       WP_284742349             985 aa            linear   BCT 25-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284742349
VERSION     WP_284742349.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 985)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 985)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   3  (residues 1 to 985)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 985)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..985
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..985
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=107386
     Region          3..242
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          108..985
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          700..726
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(702..703,706..707,709,739,742..743,746..747,
                     749..750,779,782..783,786..787,790)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          737..767
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          778..806
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          812..849
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          858..886
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mnfsvlgpvr afldgspvdl gvrkqrfvla vllleankhv padrlielaw pageapdtar
       61 avihtqisrl ratfagredv tlvregsgyq lrvdpmrvdv frfralcawa ragtderrie
      121 lleealalwd gpalssvate dvrlrvaapl eearlgaled rfeaylrlgr eaeiihelae
      181 aaieqplrqq lvakvmlalh rldrtpeala tyqrlyqhld eelgiepapa vrqlqlrilr
      241 ddpslmlftg prqlppdvnh fagrrdhldt laglfdlgdq apavvaitgk pglgktalav
      301 raahrlaarf pdgqlfvdlh gagpqprapa evlarflrdl gvagadlpas leeriglfrd
      361 rtatrhilvv ldnaageeql rplipgnpec gvlitsrrrl tgldmrglid ldgladadal
      421 alltglaprv pageeaarki vrlcgglpla lrivgaklrs rphqtvadla arladerdrl
      481 delvggdrev ragfllsytg lepaqqrafr llaampdtgf aawaasaalg edfrttegll
      541 eslvdvnlle cgrgeftptr yhfhdlirly ameklsppdr aavwsrltda ylylgkrada
      601 rlefgglhqf tppplaldap rlvadvesna pawladehas iaqavelsaa agddattcrl
      661 satvaaffel raqwsdlkrv aelshvaatr idspywtgfa lfalglaare trdfatsers
      721 frdglavlpk agdpllevvi llsvgvshrl lgrwdeaasy fagclsrlds laaprwraya
      781 lreygvlhry rgqwakakef lteaiatyrs lgdvrweaas grelgivhqd egnhaaaveq
      841 ltisrealrs vgdhrreaat lrclgwvale agalpealay arqaretlrr tldthglaca
      901 evllgdiqla mgdpvagrah ldrgvayldt sgdprwrgks mlslgchlaa agdhagaraa
      961 wekasddlsr igaheaatvr alldr
//
LOCUS       WP_284742549             623 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284742549
VERSION     WP_284742549.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 623)
  AUTHORS   Geistlich,M., Losick,R., Turner,J.R. and Rao,R.N.
  TITLE     Characterization of a novel regulatory gene governing the
            expression of a polyketide synthase gene in Streptomyces
            ambofaciens
  JOURNAL   Mol Microbiol 6 (14), 2019-2029 (1992)
   PUBMED   1508047
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18715624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..623
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=65376
     Region          70..249
                     /region_name="PtsP"
                     /note="Signal transduction protein containing GAF and PtsI
                     domains [Signal transduction mechanisms]; COG3605"
                     /db_xref="CDD:442824"
     Region          337..621
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtavtaptda lrrlldllas gasseqlahv vvaaraegal gpaeltalas agelalrire
       61 tlaehrrrea qlgalfdtas elaalsdpdt vlrsivrrar allnvdvsyl slndeaenrt
      121 yvrvsdgsvs aefqqivlgm geglgglvaq tarpyatady fhddrfkhth hidsgvqdeg
      181 ltailgvpla igpkvlgvlf asdratrefs adevallssl adhaaialds anlldqtrra
      241 vaelneanat irahteamer aqdahdrltd lvlrggdvpe vaaavagvlh gdltvydadr
      301 tllassaspa aldpdalaaa raagravstk dtwvcavqag pellgslvla grdgltdpdr
      361 rlferagvvt alllmlrrsv vraedevrge lltdlltapd rnprallarg rrlgidlsap
      421 havlvahadg gsrrrvasaa arhatlvgvh aeevvllgeg dpdelarrva adlgaatgrp
      481 vtvgaagpas gpsaiaaahg eaarcvrall algrtgegaa maglgflgql lgdhadldvf
      541 vrqtlgpvld ydarrgtelv atlrayfasg sqlartkdvl hvhvntvvqr lervasllge
      601 ewqapdrale iqlalrvhrl rea
//
LOCUS       WP_284742655             716 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284742655
VERSION     WP_284742655.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 716)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 716)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..716
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73737
     Region          10..715
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtlqlekapa eielaitgmt cascamrver klnkldgvta tvnyatekak vvyggdvape
       61 dlvaqveaag ygaalpqaep devpaddpar tlrqrllgsa vlsvpviala mvpawqftyw
      121 qwisltlaap vlvwgawpfh raafanlrhg aatmdtlism gtlaafgwsv yallfgsagm
      181 pgmkhpfeft iermagdgai ylevaagvtt filagryfea rskrragaal ralldlgakd
      241 vavlrdgger ripigdlavg drflvrpgek vatdgvvedg gsaidasllt gesvpvevgp
      301 gdtvagatvn aggrlvvrat rvgadtqlaq tarlveeaqt gkarvqrlad rvsaifvpiv
      361 ialavatlaf wlgaggtpsa aftaavavli iacpcalgla tptallvgtg rgaqlgilik
      421 gpevlestrr vdtvvldktg tvttgrmtlv egdgevlrla gaveaasehp varaiadaar
      481 erfgtlpsvv dfrstpglgv egvvegrkva vgraasdsal ttvavtwdge vrgtlavadt
      541 vkptsaeair rlrglgltpv lltgdsavva ravaaevgie rviaevlpkd kadvvrglqe
      601 dgkvvamigd gvndaaalaq adlglamgtg tdvaieaadl tlvsgdlraa adairlsrrt
      661 lrtikgnlfw afaynvaalp laaagllnpm lagaamavss vfvvtnslrl rgfsag
//
LOCUS       WP_284742687             469 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284742687
VERSION     WP_284742687.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455327
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..469
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=50832
     Region          <30..225
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
ORIGIN      
        1 mpetpsftlq lsqnkylaps dermdavltv rvgdagataa dgppqtaell lvdcsssmdw
       61 pptkieaarh acrvavdslr dgvlfgvvec tahaelvypa tpelavagpr trheaktavs
      121 gliagggtam sqwlelarel fernhpeirh avlltdgkne sdrmgaldaa ldrcrgefac
      181 dargigddwe prdlqriasv lrgsadavle daelagdfrr lveqamgrtv pdlrlrlttm
      241 pysrlrfvkq vfptevdlta qcrssgrvle lptgawgdeq reyhlcldve ateltrhedr
      301 llgtvtlleg aetvvseqlp vvgyltddla lssvpdenva ritgqaelgr avragwdafe
      361 redraeaare wgtayrlatd lgnaeilkrl grmidvrdga vaikegvrpr dgfslvlgst
      421 istytaepva pvarsedgga prkcvhcghk arpaakrcgr cgepfedps
//
LOCUS       WP_284742770             113 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284742770
VERSION     WP_284742770.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 113)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 113)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 113)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..113
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12296
     Region          3..103
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mwttgdellr qlgalgnphr lrivaalrae rtyvsklare lrisrallqv hlrkleaagl
       61 veasfevged gktlrfyelt pfsvvltpet iaaavptltt pesvqgdgqe grt
//
LOCUS       WP_284742868             171 aa            linear   BCT 25-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284742868
VERSION     WP_284742868.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..171
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=16454
     Region          62..170
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mistrtriaa avaglaavga ttvgavsata apappkgviq tshlsiasaq kaaqaaldaa
       61 gkagqhvsva vvdrdgntil tlrgdgagpq syssaqekaf tavswnakts elvgrlqqtp
      121 tlkdidgtlf lagavpvtag sapiaavgva gapsgaqdea faqagvdalg k
//
LOCUS       WP_284742922             192 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284742922
VERSION     WP_284742922.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10582168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..192
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21447
     Region          14..102
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mverperrvl tgadlkafyk alanpvrrdi lsylgkhgea nstsvakalg estgttsyhl
       61 rrladlelia eieerstgre rwwkslmkdi ytppglemtp derdaarklg alkmshdlgl
      121 vtrayagyds gegwnqifra gltltkeqit sfveeyqsll wkyvtepghh apgsralavr
      181 livvpeeest ed
//
LOCUS       WP_284742972             557 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284742972
VERSION     WP_284742972.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..557
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58476
     Region          28..465
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mteilsnaee sappkrryap laanenredy slrfaahsfr kwspfvvatt alggiaylad
       61 faigasivls ygftsgilai laaavvifgt gvpiaaacak sgvdmdlltr gagfgyfgst
      121 ltslvyasft viffslegsi mgqafelalg iplpigylla tlivlpfaly gmgavakmqt
      181 wtqplwiagl vlpfvvvlvr epgkfaefth fggtegagag fsaigfgfgm gvalsligqi
      241 geqadylrfm pektaenkrs wwaavlaagp gwvilgaakq iggallafla lgvvgkshal
      301 epiapyleav kpalgpvalt faalfvvvsq ikinttnays gslsfanffs rvlhkhpgrv
      361 wyvlvncgia lalmefgafg flnkilgfys nvaiawigav cadlviakpl glspkyiefk
      421 raylhkinpv gfgsmlvast vsiaayfgaf gqflaafspl lalviavvlv pvlavatrgk
      481 yylarpntva gpdsdvdlra thtcsvcgdp yelpdvadca kqdgpicslc ctldnschdm
      541 cqttgpvslg lpaprqa
//
LOCUS       WP_284743091             487 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284743091
VERSION     WP_284743091.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..487
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=54423
     Region          2..445
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 msssakgpsv livgtgfggi gtaielkrag ftdftilesa aepggvwrdn typgaacdip
       61 splysysfep nprwpkrfsy qpdilaylrd vitkygleph iryrtevtaa afdeergvwr
      121 vetqggetye anvfvpavgq lsrpilpdia gresfagdaf hsarwdhdve lagkrvavig
      181 tgasavqfvp elrkhakrvt vfqrtppyvm aksdpsyrrw qhwlfehlpp tqllgrlrif
      241 llaeyatyam tkhpvlakmf elrtaqlrrr hikdpelrak lkpayplgck rilfsneylp
      301 alaqpnvdve arpiasitps gvrledgtev eadvlvygtg faateflgrm tvtglggrsl
      361 rdewaggara ylgmavpgfp nmfcvygpnt nlgagsiiym ierqaryirq aveqltrpgv
      421 syvdvradve erydrevqkr lgdsvwsact swyrqadgrv ttnwpglvte ydrrtrrlda
      481 sdfrvva
//
LOCUS       WP_284743148             181 aa            linear   BCT 25-DEC-2024
DEFINITION  cysteine dioxygenase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284743148
VERSION     WP_284743148.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Chen,M., Zhu,J.Y., Mu,W.J. and Guo,L.
  TITLE     Cysteine dioxygenase type 1 (CDO1): Its functional role in
            physiological and pathophysiological processes
  JOURNAL   Genes Dis 10 (3), 877-890 (2022)
   PUBMED   37396540
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Joseph,C.A. and Maroney,M.J.
  TITLE     Cysteine dioxygenase: structure and mechanism
  JOURNAL   Chem Commun (Camb) (32), 3338-3349 (2007)
   PUBMED   18019494
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14410663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..181
                     /product="cysteine dioxygenase"
                     /EC_number="1.13.11.20"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0017172 - cysteine dioxygenase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19583
     Region          67..156
                     /region_name="cupin_CDO"
                     /note="cysteine dioxygenase, cupin domain; cd10548"
                     /db_xref="CDD:380416"
ORIGIN      
        1 mttsiarpav eihpqltdpl lpellhpsrl lwtpreladl tatvttelta nvkdilrfde
       61 drrwwarlal tdgvelwlls wlpgqhtkph dhggasgsft vlqgelgeey rypggpirrr
      121 thvpgegigf gagrahqvtg igdapaasvh ayspplvptr eyatladvpa eipplpaivh
      181 g
//
LOCUS       WP_284743209             294 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284743209
VERSION     WP_284743209.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..294
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31437
     Region          44..>213
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mkhawmpasp cgdgcltdgd pvvgfprrvl rvtaaifvvf salltsplll vswgrerrir
       61 lifrgvlraf gvrldvrgge dfltapagrg alvvnnhisw ldivainalr pmralakkei
      121 agwpvlgglv rrggsifldr erlttlpatm asladalrtg slvsvtpegt twcglasgrf
      181 ttatfqaaid ggvpvrpial ryrladgret srpafigpes liaslrrvaa lrglvleihi
      241 cpeiapgrae nrrelaalae aavhsalgtv qipaqqrrrt prpqpvplas ppak
//
LOCUS       WP_284743211             427 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284743211
VERSION     WP_284743211.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..427
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45553
     Region          235..419
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          357..414
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mdaswsdprh vldvverlls aprphllhqf saelgkliph raaamqtgdc prsplkvvgd
       61 qaiadavtsv elqrlvdrse pgkalvidgv lggverrlvl lssmpavgrg avlavvpedt
      121 elpttelela aqlwhilstd agqratdpgp dvlasnlaaa taraqaitdl gqthaatltt
      181 llavlrsgrl sdavarrtaa dlatdallel kgvvdrdqal seeragaafa vlrtqladlv
      241 rhtdvdvdlv dpagdaslpq diahtartmt rglvlaaldr pattrlrasw rldglvlrit
      301 vrddspevad aiparglter ltalgghwev davpgwgttv tavlplgvae ppelrpldrl
      361 nprevevltg isqglrnrqi aeqlqlseht vkfhvrnild kldvssrgea aalardlrle
      421 pvarrta
//
LOCUS       WP_284743342             434 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284743342
VERSION     WP_284743342.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..434
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=45063
     Region          5..425
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mtparivvvg tgyvglttga claglghyvt cvdvdrakvs rlsagrvdil epgltdlvar
       61 giaagrlqfv vgardavrda qavflcvptp mgaggsadlr aveavaaeig dvlpagcalv
      121 tkstvpvgts krieemlgrt dvpvvsnpef lregtavadf lgpdrivvgs ddraaahwvg
      181 elyaeldapv vvadaasael vkyaancyla lklsyvnsia elcerlgadi dlvtegmghd
      241 rrigrtflkp gpgwggsclp kdtsalvkva esvnydfrml tsaideniaq rdrivakiag
      301 avggtlagar igvlglafka gtndlrdspa lavssvlcal gaeliaydpa vdggidgmtv
      361 vddayqvakd adavvvltew aefkhldwaa maelmegidv vdtrnlldpr vivdaglswq
      421 gvgrpraaar ikvs
//
LOCUS       WP_284743508             212 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284743508
VERSION     WP_284743508.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..212
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22322
     Region          1..205
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mdavifdldg vlvdseriwd evrrtvvaeh ggtwreeatr aqqgmstpew arylveelga
       61 rltppeiatl vvkrmaarya kepplipgav evvravakrw pvaiassspv ilikgfldvt
      121 glpvgaavss eqvgagkpap dvylraaell gvapgdcaav edttnglrsa laagmavyav
      181 pnphfppdpe vlkqatavve kitdlpgsle an
//
LOCUS       WP_284743720             426 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284743720
VERSION     WP_284743720.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..426
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46233
     Region          171..396
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msvergfdha apppaalprk ladilrpela slaaeivdei ratipayarp ldgpygksir
       61 agveyaitlf vaqiadptvs keqshevhhr lgqnemregr sldtlqsayr vgarvswrri
      121 mrvgrrsgls savmsqlada mlafmdelas valdgyleak artagaldtw rrkllhlile
      181 tppaspkaia elaqligwpv ptdatpvavc padgvaparr hagldadila eldtpdpklv
      241 ipgelsgarl atlqvalpdc rlsigpcvpl asvadslrwa rnalhlaerg vlmprpvlra
      301 eehlatllvn sdtglvgtlr hrlfapladm tgkqqerlle tlrawldsqg nvveiaerlg
      361 vhpqtvryrm rqlqatfgds lrdpaarfem elalragaap lplrypvtel lpaprsgglh
      421 pqwtpr
//
LOCUS       WP_284743775             707 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284743775
VERSION     WP_284743775.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..707
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=75013
     Region          8..354
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
     Region          373..697
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mrkavlltvt alalgsaapa sasptlslar ptgaqpvgit slylkdtsrp dpwvetvpyr
       61 elmvslfypa vsaqgpkkqf mteaeaqavf deagitgipa svmttvhtda avdaqpaghh
      121 lplvvlspgf krpraeltsl aedlashgta vvvvdhtyen vattfpdgrv tgcaacgsyd
      181 dafwkklqrg raadvsfvld slthskwasl idasrigmag hsvggasald amvgdprika
      241 gididgttdd pllapgldrp flflgradmy tpgtgqesgt wqrdwaqltg wkrwlvvagm
      301 ahpsftdigl vgeqlgldfg attpaargqa itaayvraff dqhlrgqaqp lldqpspryp
      361 evsfamtstp ylpaptgnrp vgstqvylkd tsrpdpwvps vpyrelmvsl fypavsaqgp
      421 kkqyltaaes aallsgsgld vppdlltrlv tnsvagarpa gshlplvvls pgytkpratl
      481 salaedlash gyavalvght yenagqsfpd grfagcasce vphdsafwtk velgraadvs
      541 fvldsltrsk kwaplidasr igmaghsmgg astlptmvad prvlagidid gttevpltpp
      601 glsrpfmfms hqlaatacap nvpwerdwaq ltgwrrwaev agtqhasftd vglvgdqlgv
      661 dtgttttaar tqeitrtyvn affdqhlrge arpvldepgy pevsfch
//
LOCUS       WP_284743816             294 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284743816
VERSION     WP_284743816.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..294
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31397
     Region          4..279
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mpvyhypdtl geacslmaag edamvygggt avqillkqgv lfasdlvdig avpglgeltr
       61 tkdglragpl vtlrqmetsp lvrevaplaa evygrvanpr vrntasvggn lahgdyrldp
      121 ptalmvldar veltssrgkr tvpareffvd fqqtalrpge iitaveiprq pedagahfak
      181 lsslavndwp aasaaalvvp asrgrrqvrl glgalahvpv ftqfeipgdt pvddvvatak
      241 evagplidpl pdvrggsayk trlglvavee avrgswkerd derripflgr rrrr
//
LOCUS       WP_284743833             253 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284743833
VERSION     WP_284743833.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..253
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27465
     Region          32..145
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 msddtwaala gqfaddayas vkgrvrtyvl hrqllehlpp ppatvldvgg gtghqsfpla
       61 ragydvtlld sspamlekar qrltservtf veadgqhaee avdgrrfdav lchgvlgyld
      121 rpdpvvdqlc rcaatggvvs imtgnahtma vrpaleqrwe dalaafesrs elgvlgvptr
      181 adtveelgel lrsrgvepvr wygvwlfvdw lgfggaevdp adaervaave feagrrdpyr
      241 glsrvfhlvg rka
//
LOCUS       WP_284743838             374 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284743838
VERSION     WP_284743838.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..374
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39293
     Region          30..369
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrksaviltv agllgglttt aaatntkppv qesldalvsq qkfpaalawv grdgagtslv
       61 agsarldrrv pvprdgrvra gsntktftav vvlqlvaegk veldapieky lpglvrgegi
      121 dgnaitvrql lqhtsglpny teyigvenfe dvqhkffqph dllaaalahp akfapgakwe
      181 ysntnyllag lliehvtgrp vqeqitkrvi akaglrdtyw pqpgdetiqg phphgyalan
      241 stgtkvvdat emdpswggaa gqlistpsdl aklsrallgg ellppaqlae mrktvdaplf
      301 pgwqyglglf rvplscggay wghggdidgy etrggatedg rsvglavtal pgtfgdgeqa
      361 avavlstvdt afck
//
LOCUS       WP_284743894             405 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284743894
VERSION     WP_284743894.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..405
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42519
     Region          1..362
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtararltil ytalvlaagi lltgltyllm rrnaghrtsv ivlsppsgpt eipplppgvk
       61 eitfadfvaq aaialalvtv laavlgwlva grvlrpirti satarrlsae nlservpitt
      121 padelatlag tingmldriq egvterdrvl asqrmftana ahelrtpltt mrtaidvtld
      181 srpgteella mtgdvrtave qsqrtldgll alarsqagag pphrvdladl vannldagdl
      241 tvrtdlraap vsgepvller mcgnlvenav rhnhtgghie vatgiadgra flrvgnsgal
      301 iapetverlr epfvrgegar irsnrspglg lsivdaivta hrgeiviaar saggldvtvr
      361 lpsepcapva tsvsagarss rwrnpqvgfd svgcairdsn pepag
//
LOCUS       WP_284743923             246 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284743923
VERSION     WP_284743923.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..246
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=27212
     Region          2..242
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mvrqlpiasv dcvvtsppyw glrdygserq lgaeatvqqy varlvelfde vaqvlvprgt
       61 vwlnlgdnyg gswghyvaag svsrtaevrs rtpygthrpp qascrskdlv gvpwrvalal
      121 ldrgwharre ivwhkpnarp esvrdrfshc yenifvlsrd pcetaetevw svssdrgrvs
      181 hpakgtleia rrcvrlgcrp ggtvldpfsg sgttgiaare hrcrfigidl dprchdlalq
      241 rlglsa
//
LOCUS       WP_284743936             300 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284743936
VERSION     WP_284743936.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..300
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=32281
     Region          46..289
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mtisllgsei tvhgefdlaa aarfltgfap agqpeaerga lrvafpldge wtpvgavlrq
       61 rspgevvvev hgpppqadav laqvrrmcsl dvdgtgfaev gardpvvslv qgmhpglrpv
      121 lfaspyeaac wavlshriwm tqavrlrrrl aerhgtevdv ggsvltsfpa pavlakleyl
      181 pglsgpktqr lrgigeaaad glldaatlra mpadealkql qllpgigrfs aelilirgag
      241 hpdvfpraet rlheimrday hvpdagveel aeiaeawapf rswvsflfrv egearmresr
//
LOCUS       WP_284743979             315 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284743979
VERSION     WP_284743979.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..315
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32873
     Region          11..310
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mttelpvlap prvahrgrgt tlvllaalff stsgtlgksa msagftpeqv aamriglagl
       61 vllagvalva prklrvrrse lpvlagygll gvagvqllyf vaagripvgi aillefispv
      121 lialwvrfvr rhrlprsvwg gialamagls lvaqvwqgvt lngvgllagf gaalcsagyf
      181 llgeravadi dplglvtwgm vigavlislv appwtwpvgl lavdvefgaw hppvwllmvl
      241 lvlvatvlay vcgisslrhl pasvasvlgl vepvittvaa waligeeltw pqllgsaill
      301 agaylvqrks eilts
//
LOCUS       WP_284743981             271 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284743981
VERSION     WP_284743981.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..271
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29072
     Region          14..246
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mvalhsdnts rrapaiwrtm lnidrglvnl vgrltvsgri paqlrgkpll mtanhigvfd
       61 afvlmaackr iginprfmla ggildapvig palrvsghlr vdrkvaatav gqfteaveal
      121 kttrepiivy pegrishdpg lwpergktga arlalaadvp vipisqwgah eavywgtetv
      181 ngpadlvpla rsglsaplrr pkfrvhfgdp vdlsgveper pgagvrahak imqaitdgli
      241 plrageldrp rfhdptrptd tvspwkpksg s
//
LOCUS       WP_284744042             227 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284744042
VERSION     WP_284744042.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 227)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..227
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23562
     Region          15..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 metialaeva avladpsrat mclalldgra wtvgelakaa gialstaseh vsrlvdagfv
       61 arvkqgrasy vriadprvae liehlaqhae hrpvtglkss lrvkrlgfar tcydhlagvl
      121 gvalrdgmla tglidadggl altgrgravl aelgvpvapg rrsplrdcld wterrdhlag
      181 avpaallera vgagwvgrdg hravkvfpaa ekpfaalgvd ltalggp
//
LOCUS       WP_284744092             461 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284744092
VERSION     WP_284744092.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 461)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..461
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=48865
     Region          11..460
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mhprlaedlk slpelldaar klagealagl perpaavppg dlvraplple gaggrgalee
       61 fsqrweagfa gsagprylgf vtggatpasl agdwltatyd qnpasgmdss aqdleretvg
      121 wlaelfglgr efsgafvtga tmstvtglai arewlgerag vsvsddgaaa lgpvtvlsgs
      181 phssilkals flgmgrtalr kvpvlpgrea vdvaklaeal esldgpavvv anagtvntvd
      241 fddlraiaal kqrydfwlhv daafggfaal spehaaltag ldqadsvvvd lhkwlnvpyd
      301 savqftrrrd lqlrvfsnna aylgeigetp dflhltpens rrlralpawf slvaygrdgh
      361 reivercvsl ardlgarldg sprwrllapv rlnvvcfapa edvtqdrida lvraiaedgt
      421 tfltptvydg hpalraafsn wqttaadvdr vfaaiervaa g
//
LOCUS       WP_284744107             332 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284744107
VERSION     WP_284744107.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..332
                     /product="zinc-dependent alcohol dehydrogenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=34870
     Region          1..331
                     /region_name="MDR7"
                     /note="Medium chain dehydrogenases/reductase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cd08276"
                     /db_xref="CDD:176237"
     Site            order(36..38,41,137,141,162..167,185..186,190,205,
                     230..231,233,253..254,278..280)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176237"
ORIGIN      
        1 mrvyrpesgs lvqreeptpe pqrgevlvrv ratslnyrdl lildgdhftn gpgslipvsd
       61 aagevaavge gvtrfkagdr vvnafhsgwi agrlpdtlag ygngqdgwla eyravgehal
      121 valpdslsye qgatlpcaav tawtslnggt plrpgevvlt lgtggvslfa lqlakqhgar
      181 vvattssaak aakltelgad vvidytatpe wgkavldatg grgadrivev ggpgtfaqsl
      241 vaagthhadi alvgfvgrsg ppvdfmdlfr sgatirkiwv gsredtedll rwlavrplep
      301 vvdsvfpfdd agaalerfrs rrnlgkvvvt vp
//
LOCUS       WP_284744224             372 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284744224
VERSION     WP_284744224.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..372
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39894
     Region          6..312
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mqkpldnael daalenvcqa gmpgvfaevr agddvwrgaa gvadvetgrp vtadlrhrvg
       61 sitktftaaa vlrqvengei gldtpighyl prlvpgergd aitvrmlldh tsglaeylpy
      121 aypslsafpd laktgpesfd dhrftrfdpv dligmgvaap avgtpggtpg lysntgylll
      181 gqllehvtgt aaekhitrdv ieraglrdtg fpegahvdgp hsrlyeswfg midpprdysv
      241 fdmswvgpaa alvstvadln rffrllhage ivsrtsleqm rrtvrvisqe gklidyglgl
      301 hpveapgqar fwghggtvwg ggalaairad gerqlavgmn lqrwnrldta gapqphaidr
      361 alaafqqvam yg
//
LOCUS       WP_284744263             397 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284744263
VERSION     WP_284744263.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..397
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42386
     Region          9..395
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mpadraglrp ldgikvvdls rilagpyctq ylgemgadvv kveppghgdd trgwgppfvg
       61 esdeavyyla anrnkrgivl dlksdrgrea lrrlvadadv lvenfrpgtl ekwglgyaal
      121 sdlnprlihv sitgfgqtgp yrdragydlv aqalggvmsl tgepdgapak vglpvadlna
      181 gtwaiiavlm alqarhttgr gqyldvslld sqlawhvyaa gavfydaprp rrmgsahpsi
      241 vpyqaysvsd gwliiavgse klwhafcgvl glaiasdarf ssnalraahr delnallepv
      301 lltrtaadwm ksfdaagipa apineiddvy adpwteardq vvrlphptvg tyvgtgfpvk
      361 asdtparpts apptlgqhta evlaelgysa eeiaefl
//
LOCUS       WP_284744274             454 aa            linear   BCT 25-DEC-2024
DEFINITION  WS/DGAT/MGAT family O-acyltransferase [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284744274
VERSION     WP_284744274.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Stoveken,T., Kalscheuer,R., Malkus,U., Reichelt,R. and
            Steinbuchel,A.
  TITLE     The wax ester synthase/acyl coenzyme A:diacylglycerol
            acyltransferase from Acinetobacter sp. strain ADP1:
            characterization of a novel type of acyltransferase
  JOURNAL   J Bacteriol 187 (4), 1369-1376 (2005)
   PUBMED   15687201
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Kalscheuer,R. and Steinbuchel,A.
  TITLE     A novel bifunctional wax ester synthase/acyl-CoA:diacylglycerol
            acyltransferase mediates wax ester and triacylglycerol biosynthesis
            in Acinetobacter calcoaceticus ADP1
  JOURNAL   J Biol Chem 278 (10), 8075-8082 (2003)
   PUBMED   12502715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496208
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..454
                     /product="WS/DGAT/MGAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0045017 - glycerolipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=49859
     Region          8..453
                     /region_name="acyl_WS_DGAT"
                     /note="acyltransferase, WS/DGAT/MGAT; TIGR02946"
                     /db_xref="CDD:274360"
ORIGIN      
        1 mammpvtdsm fllvetrehp mhvgglqlfk kpdgagpdyl rdvrrslles dnmrsvfrrr
       61 parpvntmgh vawraetdle ldyhfrhsal pqpgrirell eltsrwhstl ldrhrplwet
      121 hliegladgr favytkvhha lmdgvsalrq lqgtlsddpa dldcppwwgs rrkpgekpak
      181 rprsfletag ktanqlagla paaikvarea fgehtvtlpg qaprtmfnvp iggarrfaaq
      241 swsldrvrkv ataagvsrnd vvlamcsgal rdylieqral pdaplvamvp vslrrqndpg
      301 eaagnnigal lcnlatdlpd agkrlltihq smrngkrlfs eltplqtlll savnvaqlgi
      361 spipgivnnt rppfnlvisn vpgprkqmyw ngaqldgiyp asvlldgqav nitltsngdn
      421 ldfgvtgcrr svphlqrilt hldtalvele aavk
//
LOCUS       WP_284744280             174 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284744280
VERSION     WP_284744280.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10582168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..174
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18960
     Region          6..72
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mphdnlrvla hplrmrilsl ltgaamsaae aarelgetqa nisyhlrrlh eaglldvaee
       61 vtirggrakr yrhdpesgrr lttrnpaeqq lltkavagel lrragsrapg rrasltdael
      121 wvdpeiwarl leraselsqd lhaaaqpprs pgtvrvsasv alfeladags eear
//
LOCUS       WP_284744400             290 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284744400
VERSION     WP_284744400.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..290
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29622
     Region          2..281
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mvigatgvlg vpavarllaa ghevsglsrd asrapaieat gakpvpgdlf sasslvtalr
       61 ghdavlnlat riprkvtsks awaandrvrl agsaalaaav reveelrivv qegisfvyad
      121 ggdrvlaeda plrprgvtas svvahenvaa ltdrtvvrlr igtlvgsdtl taallasarr
      181 gaplimgsrt dwttaihpsd agaaavaald apsgvynvga pavrkgelge amaaaagvrk
      241 aravpkwvls rvamaepmar sqrvdsgklm avtgwrcerp vpgpdwftag
//
LOCUS       WP_284744419             368 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284744419
VERSION     WP_284744419.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..368
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39298
     Region          1..366
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mipitvvdvr daedlvvevl rsgaiaqgpm vkrfedafaa vsgtkhaiav nngttalvas
       61 lqvldlkpgd evitspftfv atlnaileag atvrfadirr ddfaidpdav akvvtdrtkv
      121 lmpvhlygqt admgklapla aehglkvied saqavgasfe gkqagsfgig cfslyatkni
      181 ttaeggvitt dddaladklr vlrnqgmrar yqyevaghny rmtdlhaavg ipqlakldql
      241 taarqanakr lseglagtpg ldipqvlpgr ehvwhqytvl vgphaflsrd elaaalterg
      301 igngiyypki vfdyecyadh dlipgarved fpvaqavanq alslpvhphl tesdldtiie
      361 tvrevlga
//
LOCUS       WP_284744428             564 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284744428
VERSION     WP_284744428.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..564
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59455
     Region          <85..>261
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mvyavvvawl vlaaivvltw grldtdrgwr gfvltltlgl sllhqllfat vtedalvsfr
       61 yaqniadgng pvfnpgerve gytnffwlvl ialpraafga dvqttavvfg vlaalgcvlv
      121 ayllvnriva gadaewrpai gvaaavltas agglavygps gsevplfvll llavcyslaa
      181 rrpvvagvlv afavmtspeg lvvavlgglw lagaalrkkh swwapvgyvl galvfliprl
      241 awratfyqhf lpaplaaklg gpfgsqvasg wpylsgfala hqgflllglv aavalllrrt
      301 qpafrgfrva eppvgtdvea raliwllfat aatvaaaavl iggdpgpswr llapvpplia
      361 vaavsaygvl tvdadakpsp rprawpaatr lvpvtacgla giavlvsvfs pemldrvrdw
      421 rahgaeltev ggwlgrylpp gsvvsaaapg alaahggqll iidvlgrtdd hiaregrhdd
      481 gvatdydyvv ngrrptvavp adsgyadrqh caidpvyagk yevatfrrvg tpywvsvypr
      541 teqaksvvtd ldkgpdfryv pcpt
//
LOCUS       WP_284744430             242 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284744430
VERSION     WP_284744430.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..242
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26565
     Region          4..210
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 madlvyppvi aaartmfrvl dnritiegae hiprrggavi acnhvsyldf ifcglgarpa
       61 krltrfmakk eifdnkiagp lmrgmhhisv drsaglasyr ealeklqage vvgvfpeati
      121 srsftvkeik sgavrmaaaa dvpvvpmalw gtqrlwtkgr pkdltrrhvp vsiligeplh
      181 pakgddwdvv tkelrtrmsa lvdraqaeyp dqpasdeerw wlpahlggta ptpeeaaeld
      241 rg
//
LOCUS       WP_284744682             261 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284744682
VERSION     WP_284744682.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..261
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26424
     Region          1..236
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mnrrqlvdlm aagrpalgtf vnlgsplaae acalggaswl lldlehgtge hallpqilaa
       61 eahgvaalvr vetadrirag rvldlgvtgv mfpridtveq aaeaiahlry ppegdrgvat
      121 ynracgfgld tgaldrange vlgiiqiesp eavanaaeia avpgvdvlfv gprdlshamg
      181 ipgqvrhpdf vaamehvlaa agkagiaagt laatpasaag yvadgftfvg vgsdssilag
      241 avadairttt daatrlqkev s
//
LOCUS       WP_284744689             289 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284744689
VERSION     WP_284744689.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..289
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30602
     Region          23..287
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mimdrvagap iswgvcevpg wghqltpdrv lsemkdiglv atefgpdgfl prdpaakaak
       61 lrelglsavg gfvpvvlhda grdplpeidr eldgfvaaga gtivlaaasg ldgyderpel
      121 derawrtlfg nldriadrar ergvaaalhp hvgtmvenra evervlagst vplcldtghl
      181 liggtdpvel aksvpdrish thlkdvdvtv aekvragelt yadavrggly rplgagdvdi
      241 aaiigvlesh gyrgwytmeq dtilagepeg egpgadvras vaylrslpw
//
LOCUS       WP_284744722             332 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284744722
VERSION     WP_284744722.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..332
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35526
     Region          3..328
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mplklgayta clhdrtltea ldvlqenglt svevntggfi psphcpvdll lssataraey
       61 laifaergme ltglncngnp lnplpgvgpk haddlrrtir lagllgvkhv vtmsgtpgsd
      121 pdaqypswvv npwdgvyldv ldyqwgvava fwteidalar endvrvaiem hphnvvfspv
      181 tlkrlvdetg atnvgaeldp shlmwqgmdi vasikwlgpl vfhaaakdam lcpgadirgv
      241 ldtsftrvpa dapgkvptgy gfwcaawpen pawkfvavgi ghdvgywtgf lraladvdpd
      301 mavnieheda aysrteglal aakslhsaat gl
//
LOCUS       WP_284744746             929 aa            linear   BCT 25-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284744746
VERSION     WP_284744746.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 929)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 929)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   3  (residues 1 to 929)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 929)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..929
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..929
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=100914
     Region          2..244
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          114..922
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mtvefrllgq vevrldgepi dvgyaqlkav lalllvevnh vvavdrlvdr vwgdrrlpqr
       61 prgaiqrsit llraalapvp gfaitwqqpg yrltaepgsv dlhrfhrlia dartagddpr
      121 avalfgeale lwrgepfagl dipwltecrt slfqqrqaae leltdirlrq gdhaellpgl
      181 aertrddpld erlaaqlmla lyrngraaha lehyqrfrtr laeetgtdpg pplrrlhhri
      241 latdpaltvp spttapvprq lpaaprsftg raaaladvna tltergravp vavvtgsggi
      301 gktwlslhwa hehaeafpdg qlyvnlrgfd pgseplpaat alrgfldalg vaveatppew
      361 eaqiglyrsv vagkrllivl dnaratdqiv pllpgsptca vlvtsrhrld glvtshgara
      421 valdvltgte arqllvghlh rhriaaepda vtellgycad lplaigivaa raghhpgfpl
      481 salaaelrdq agrlaaldta dadvnlravl swsyralspe aatafgllgl aagpdislpa
      541 aasllarpat gtlgllrele haslvqqydp grirmhdlvr laaaqhaeqd lpepdrtaal
      601 rrladfylht ahagdrllqp llppirlaep htgcqvvpla dqaaalawft aehpnllalq
      661 rlaaargwaa vgwqlawlqt tflyrrgrfh aaldawkagq eaakelddpa vhagthqllg
      721 aiftelgqht eaghhlalae rsgdlpaqay thhalgwsws lrgadrrale hateslrlyr
      781 alglpagetr eltvsgwyra rlgdfaeaga haeaalvlar rhgfredegl atgilgflaq
      841 htgryrdavn hyrdaagvll eagntyfegt vlefagqtyl aldepeaahr twqealelyr
      901 vqartadadr vrryladlge wlpapaptr
//
LOCUS       WP_284744770             318 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284744770
VERSION     WP_284744770.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..318
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34497
     Region          21..316
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mygtserllr llsllqarrd wpgadlasrl evdvrtirrd verlrslgyp vhatpgvagg
       61 yrlgagaalp pllldddeav avavglrtaa sgtvsgieet svralakleq vlparlrprv
      121 galsaatmsl pgagptvdae vltviaaacr dherlrfpyg drsgaeters veplrlvhtg
      181 rrwylvafdl drtgwrtfrv dritgvpaps frftpreppa edlaayvsqq issapyphql
      241 vlrvaapase lshrvpptsg avepidehsc rvrtgantld tvpyylaqwg ydfvveeapp
      301 glvellreva erfaravg
//
LOCUS       WP_284744772             321 aa            linear   BCT 25-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284744772
VERSION     WP_284744772.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..321
                     /product="isopenicillin N synthase family dioxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35333
     Region          2..318
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 mpstvplvdl spwfagtseg raevaaqids alresgfllv tghgvpddlr rrtrelaref
       61 falpedvkqr yavtvggrgw lppgveangy aegtetppdl kesysagadf gvgdaeidgf
      121 wfqpnlwpde vpglaetate ymrrmralsd hlleicaaal glaeshftrh tahptytfni
      181 nwyppmahvg apepeqfrig phtdfgtvtv ldrqagvggl qvytddgewa dapfhpdaft
      241 inigdlmarw tgdrwrstrh rvlppaasap dedlvsliff yetdhdarit slapplgkrt
      301 ypeviaadyl rekldaitvt q
//
LOCUS       WP_284744783             277 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family oxidoreductase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284744783
VERSION     WP_284744783.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Persson,B. and Kallberg,Y.
  TITLE     Classification and nomenclature of the superfamily of short-chain
            dehydrogenases/reductases (SDRs)
  JOURNAL   Chem Biol Interact 202 (1-3), 111-115 (2013)
   PUBMED   23200746
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10793067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..277
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29369
     Region          1..274
                     /region_name="PRK08278"
                     /note="SDR family oxidoreductase"
                     /db_xref="CDD:181349"
     Site            order(13,15..16,18,37..39,97..99,147..149,165,169,
                     195..198)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187663"
     Site            order(121,149,165,169)
                     /site_type="active"
                     /db_xref="CDD:187663"
ORIGIN      
        1 mstldgktii msggsrgige aialraakdg anvallakta ephpklpgti ytaaeaieka
       61 gghalpilgd vrdddgvaaa vaktveqfgg idivvnnasa idltpteqvs mkrydlmqdi
      121 nargtfllsk laiphlrqgm nphiltlspp isldekwfta ghlaysiaky smslvtvgla
      181 aelkkdgvav nslwprttid taairnvvga eladrsrtpe imadaayail tkpsreatgn
      241 fflddevlra egvtdfakyr iggseedlql dfwvdpa
//
LOCUS       WP_284744814             551 aa            linear   BCT 25-DEC-2024
DEFINITION  nickel ABC transporter ATP-binding protein NikE [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284744814
VERSION     WP_284744814.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF007739.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK10419
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     gene            1..551
                     /gene="nikE"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Protein         1..551
                     /product="nickel ABC transporter ATP-binding protein NikE"
                     /calculated_mol_wt=58218
     Region          1..542
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtspllqlkd lnvtyvvgeq dipavrgvgl tldpggtlgv agesgsgkst vamsvlrllp
       61 rtakisgeil legedvttmn wgrlravrwa easvvfqgam halnpvrkig dqiaeplrlh
      121 ppeggkaltd aavdarvael ltqvdlppgr agayphelsg gqkqrvmiam alacsprlii
      181 adepttaldv ivqaqvldll srlvaeqdig limishdlsv laatckriav mydgqiveeg
      241 lsaevmaapk hehtralaaa fptvgdpvsr fapatstplp pepedrvagg epllaaenlr
      301 vsfrdrtgkr inavagvdla vardeivalv gqsgsgkttl artllglqkp dsgvvryagn
      361 pvphggaglk ayrrqvqlvl qdptsalnpa htvyeavaeg prihklader avvhraleaa
      421 elrpaekyad rlphqlsggq rqrvviagal alepsvvvad epvasldasv rgeilglllr
      481 lrrelglaal vithdlglaw niadrvavmy rgelvetgtv eqvlldpqhe ytksllaalp
      541 ggtaqrrtvg t
//
LOCUS       WP_284744943             386 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284744943
VERSION     WP_284744943.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..386
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41011
     Region          4..386
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mghsaagpls gllvadfsrv lagpyatmll admgaevvkv egpqgdetrt wmppvrgdvs
       61 tyylgvnrgk rsialdlree adaavarela aradvvienf kpgglakygl dydsvraanp
      121 gsvyasisgf gsgegrhvpg ydlmvqaisg lmsltgdpdg ppyragisvf dvmagnhavi
      181 gilaalrhrd atgegqhvev nllssaltgl vnhssayaag gvvpyrmgna hpsvfpyepl
      241 ptadhdliva aandgqfrrl cevlglpdvp ddprfarnad rtknreelrp ilverlkerg
      301 avewfdaltk vgvpcgpint idggfamaer fgldpivevg dgdravpttr hpirfsatpa
      361 ayrlpppeld ehgaelrawl tettdd
//
LOCUS       WP_284745008             224 aa            linear   BCT 25-DEC-2024
DEFINITION  SGNH/GDSL hydrolase family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284745008
VERSION     WP_284745008.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..224
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=24385
     Region          1..223
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 mtiklkpgst vmftgdsitd lwrppgedrc gypllvagew cfrhpgcpvt wlntghagdk
       61 vmdlearwee vldarpdvvs ilvgandmgw htldprgrvi pveefaacyg rllaplaslg
      121 telilvepfl vpvkgvverv lhgvdgervv viddavreew rgdldakira vrelageyga
      181 hllaadrmfa svvgedpgrw sedgihptpa ghgalaeawl rlvv
//
LOCUS       WP_284745023             163 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-class carbonic anhydrase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284745023
VERSION     WP_284745023.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130171
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..163
                     /product="beta-class carbonic anhydrase"
                     /GO_function="GO:0004089 - carbonate dehydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18181
     Region          27..162
                     /region_name="beta_CA_cladeD"
                     /note="Carbonic anhydrases (CA) are zinc-containing
                     enzymes that catalyze the reversible hydration of carbon
                     dioxide in a two-step mechanism in which the nucleophilic
                     attack of a zinc-bound hydroxide ion on carbon dioxide is
                     followed by the regeneration of an...; cd03379"
                     /db_xref="CDD:239474"
     Site            order(27,29,36,38..40,52,55,74,79,89,92,152)
                     /site_type="active"
                     /note="active site clefts [active]"
                     /db_xref="CDD:239474"
     Site            order(36,38,89,92)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:239474"
     Site            order(37..40,46..47,52..54,56,58,69..70,73..74,152,
                     154..155,157,159)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239474"
ORIGIN      
        1 mtsidvllkr nqelgevtpg drsspkpslh vailtcmdar irvfelfgll qgeshvlrna
       61 ggvvtddmir slalsqrklg trevlivqht ecglsmvted dfkdelesdt glrptwavea
      121 frnvensvrt svervrrsdf lphtenvrgf vydvktgklt evq
//
LOCUS       WP_284745030             103 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284745030
VERSION     WP_284745030.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..103
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=11052
     Region          3..100
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 msvvkinaie vpegagaele krfaarlhav dqqpgflgfe llrpvsgetr yfvytkwete
       61 ehyqawakgg paaaahsger akpvstganl lefevvlgsq pge
//
LOCUS       WP_284745140             232 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284745140
VERSION     WP_284745140.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..232
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=24298
     Region          42..193
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 migplvepes vpewlrplvk vsaevdsktf trfsppeaay traaavlilf gereadgepd
       61 vllqrradtl gshagqvafp gggaedgdgg pvgtalreae eetgvvpsgv rpvavlpelf
      121 vpvsgfavtp vlahwaepsp vhavdpaeta svarvaiadl vdpanrftiq kagmpwkgpa
      181 fevgglfvwg ftagllsvll glggwerewd sddvrdldea laafrarltg ge
//
LOCUS       WP_284745141             199 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284745141
VERSION     WP_284745141.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..199
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19945
     Region          72..196
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mttvtkwala aavlavaliv allprggdds aakpsgdlap arsaaalqpc paagpaqpvk
       61 qlegvkadcl gdgasvdvgk alagapvlvn vwaswcqpcr telpvlqeya kqpgaarvlg
      121 vqvqspaedg lnllaklgvh lpsvfdgdgp sgpvrtalkv psslpasylv taagevrfia
      181 nprtfgntdq vraavegas
//
LOCUS       WP_284745251             218 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284745251
VERSION     WP_284745251.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..218
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=23309
     Region          <1..201
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mrvaiagaga vgrsiateli dgrhqvmlie readqfepqt veqadwvlgd acevsilees
       61 gieqcdvvia atgddkanlv vsllaktefa vrrvvarvnn panewlftda wgvdvavstp
      121 rmlaamveea vsvgdlvrlm tfrqsnanlv eltlpaetpl agkpvsdlal prdaalvtil
      181 rgdrvivpqp edplepgdel lfvatadvep eirtalgy
//
LOCUS       WP_284745259             216 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284745259
VERSION     WP_284745259.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..216
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23464
     Region          <50..149
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 msiteassga glpqrpydrl ylsraglplw gdspgrlvgg lsyqgqskia ldagcgdgkn
       61 aihlerlgfd vigidhsdva ikllherfhs ngrpvlgsys vadvrtwrpv glevdvlvsy
      121 glyhclpqnd rathehllnl irpggtllfc sltdgvpmgd ehctpgielp svkevdehlq
      181 gftilersve kfdgshpplv gphrheaiwi sarrpt
//
LOCUS       WP_284745297             517 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284745297
VERSION     WP_284745297.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..517
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=54524
     Region          219..517
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtslrhvlat lgeplvevvv aphglgvpvg dvvildpedp leagpgdlvl vigargraaa
       61 pairaagrgg aaavavkgat gadvaadagi alltvgaear weqveslarg vveaaragge
      121 aasgevlgdl falaqtiatl tgglvsiedt anrvlaysra gdevdelrrl silgregper
      181 ylamlrewgv yqrlragegi vriderpelg irrriaagih agkqplgtiw vqegaqplte
      241 raetallgas rtlapqlira rtlpspelrl redllaslle grldaesvad digadparpa
      301 qvlafslers dnrqlrrael vhliavhtaa yrrsalvsvi ggrvyallpd lpehsdaavl
      361 alakeivgta rrhldvpvra alggvvprls daaasrgdad rvlaamvrgh wpadvaslad
      421 vraevllsev laflggqpri rdprltslve hdtehggilv pavlawldaf gdvraaarll
      481 nihpntvryr vrraaevsgv dfadpaqril tqlqlrl
//
LOCUS       WP_284745327            1017 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284745327
VERSION     WP_284745327.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..1017
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=108199
     Region          6..1006
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mlrvsllgqq viaddetgav ltrsprsval vahlvvhagl aqprrliagl fwpdstdaqa
       61 ltnlrrelhq lrrvlgdpps lavtgrdlcw rdtpssrvdv refdlarqaa laaadpgelv
      121 ahaqtafaay rgellpglad dwvlaarael drqcvelcdl lcrtpsgdpa valeaarrri
      181 rlrpleetgy rtlmglqada gdragavsty hrcasvlere lgvvpaeptr aalrrllalp
      241 dpeprraaap glvgraaela rlgerwraaa agragivlvr gdagvgktrl aaelaavara
      301 egatvavgrc fgtagrvala pvadwlrtpa vqraataldp vwrtevdrll paarpaaagh
      361 ptvdawqrlr ffeglaralt aggrpvllvl dnvqwcdeet raflafclgl lpaapllvag
      421 tlrdgdldpg vaawttqlrd dgkltelplr pfdadgtahl geavagrpls asdravlhaa
      481 tggfplyvve alrtndspps grltgvlrar leqpgpaare vaglaaaagr dftlelltea
      541 sdldadtvvd avdelwrrri vrefaggydf ahdllreaay qqvspprrwl lhrrlaqgme
      601 llhaddtdav aaqlaeqyar ggrpdravah yrraaavaag tfahaeairl lkaalalvra
      661 rpasgnrdra elevlealag plnahhgyss pelqhvlers lalaessgsk eaaltallel
      721 wssrfvqgrt aeaheaaera lallapgtsa eqdgsahfiv agsslslghd paealrhfel
      781 gadrtrgass wpigtrpdvh gpawaahahw llghddaava ssvaaitlar eieqpyslai
      841 alayagithq mrrdrralwa avselhtlcd rygfayyrew alvlggwsrg gaaglaaaqe
      901 gvahlkaega farmpywlsl vaelsgpeaa ratldaalaa gearddrwwl pdvlrlrath
      961 dadpvprlra aaelarvqgs valrrraead lgafggpggg apgsgrspgs rsvrpvp
//
LOCUS       WP_284745362             268 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284745362
VERSION     WP_284745362.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..268
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27102
     Region          2..267
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 myagaaiavg lfghatpagv awlrclgaav vllawrrpgr aawrghrlal aiafgvvtag
       61 mnvlfyeaia rlplgtvvam efigpvlvaa fgsrtprdvl avvlvacgvv aiadvqlsgs
      121 vlgvvfalga aaawagyill gkrvasaegs gidslaigfa aatvvlspla fgtgevwssp
      181 rmlllgvgvg vlstvvpyal dqvvlrrlgq arfavllall pvtagvmgfv llgqvpswpe
      241 algtlavvgg valrsrdeav rpvpeppg
//
LOCUS       WP_284745360             213 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284745360
VERSION     WP_284745360.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..213
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22501
     Region          1..>55
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 msedpfatfd aayvlgalsp edrqrfeqhl rtcdrcaasv rdmaglpgll arvdappvvp
       61 dvgppppdll ptvlrrvrrg rrirlavtsv saavavsacv alavvaswpp aapppsiamt
      121 algqfpvrad arldafewgt qvdmscsytg erssgeyvlv aisrsgtetq latwkavpdn
      181 tarivigtal krtdlaalev rggsgrallr ltl
//
LOCUS       WP_284745513             258 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284745513
VERSION     WP_284745513.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..258
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28159
     Region          14..258
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          174..254
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mahveawrpa vpgiaevfha rfithayplh thdtwtlliv ddgvisydld rhhhgalgpa
       61 vtllppnvah dgraatshgf rkrvlylets vlgedligaa vdqpsvadgl lrtrihqlhv
      121 slaepgdale aesrlalvae rlhthlgrpa vhepkrglad dlrdlldarl pealtlaeaa
      181 etlgahpahl vrcfgarfgl pphryltgrr vdrarrllld gspaaevaav agftdqahlt
      241 rhfkrylgtt psryskar
//
LOCUS       WP_284745552             134 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284745552
VERSION     WP_284745552.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..134
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14772
     Region          17..111
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mseapewlde hgqvvfdvfa qactsratle hitgrwgila maalhdgtlr fnalrrrvsg
       61 vsekmlaqtl qalerdgfvh reaqptippk veysltprgr rtaalllali qdvegqmpev
      121 maanseydaa kres
//
LOCUS       WP_284745558             351 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284745558
VERSION     WP_284745558.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..351
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=36377
     Region          10..343
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mktaltelvg iehpvvqtgm gwvagprlvs ataeagalgi lasatmtyge leaaieevkk
       61 rtekpfgvnl radaadagdr vdlliregvk vasfalaprk emiaklrdhg ivvipsigaa
      121 rhaekvaawg adavivqgge ggghtggvat tlllpsvlda vdipvvaagg ffdgrglaaa
      181 laygaagvam gtrfllskes tvpddvkrvy leqgltgtvv trrvdglphr vlrtdlvekl
      241 ertgrlrgla qaarnalrfr nitglspvam vkegfamkhg ndltwsqlvm aantpmllra
      301 glvegrtdag vlasgqvvgm ihdlptvagi vegtvaeage ilrrlgretg g
//
LOCUS       WP_284745568             604 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284745568
VERSION     WP_284745568.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..604
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=66901
     Region          184..>516
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mtqtlepaaa vdarqrvegw lagfeaalaa rdadraaalf attsfwrdli aftwnlktve
       61 nrdgvkdlll atmdtadahg fhateeptes dgvveawigf etvagrgrgh lrltgegaft
      121 flttlhelkg heeplgttrp kgaehgvnre rvtwsearqa eadelgttrq pyvvvigggq
      181 ggialgarlr qlgvdhvvvd ryarpgdqwr grykslclhd pvwydhlpyl dfprtwpvfa
      241 pkdkiadwle mytrvmevny wssttctsas ydeetkewtv vldrdgeevv lkpkhlvlat
      301 gmsgkpnvpv lpgqdrfrge qhhsskhpgp dayrgkkavi vgsnnsafdi cgalweagad
      361 vtmiqrstth ivksdslmdl glgdlysera laagmttqka dltfaslpyr imhtfqqpvy
      421 aaikdrdqef ydrlegagfr hdwgdddsgl fmkylrrgsg yyidvgaadl vangdvklah
      481 gqvveltens vkledgtele adlvvyatgy gsmngwaadl isqevadkvg kvwglgsdtt
      541 kdpgpwegeq rnmwkptqqe glwfhggnlh qsrhyslyla lqlkaraegi ptpvyglqer
      601 hhls
//
LOCUS       WP_284745581             254 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284745581
VERSION     WP_284745581.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14398448
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..254
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27850
     Region          16..109
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          176..252
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mrnvhvdtvd dldrdvvaig tdyppghvla ehrhrraqvl ygvtgsmrvd tadgawtvpp
       61 qravlipagv phavrmdgvs trslyvepra vpwfparcrv vevtpllrel lreavdvepr
      121 yaprgrdaav lqlalhelrr aaplpldlpl padpalrrlc tdflaeprid vrpaawaarl
      181 hvaertlhrr fraetglala pwrrracvlh alpllaagtp vaevaaalgy agpgafttmf
      241 hrllgvppse frgd
//
LOCUS       WP_284745605             364 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284745605
VERSION     WP_284745605.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..364
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38213
     Region          27..359
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mrkallagla galvvtaapa atattrpelp aptgpyavgs telhlvdhar pdpwvagttr
       61 elmvtvrypa rpgggpkapy ltpgaaaiva dedarqlgis adrldytfpt hartgapaag
      121 gprpvvlysp sakyprsvgt aqleqlsseg yvtvaidhth eaaavefpgg rverralppg
      181 tdgklviatr vadvrfvlde lellsregnp aglsldltrv gmfghsaggf ttgetmvsdp
      241 ridagadldg smaysqsard fgrvanegld rpflllsagd hsaasdaswq eflshqrgpv
      301 rqahladgeh fsytdyqall prlgldpasi apfigtidag rsiatqrasl saffaryvpr
      361 cdvr
//
LOCUS       WP_284745825             506 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284745825
VERSION     WP_284745825.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 506)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 506)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 506)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..506
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55269
     Region          11..500
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 msaeargwti rrwltllavt eavlllaala gggmamnnlt darnrlldvi gaqrlaaiql
       61 stallnqetg vrgyqlgrqp dfltpytdgv rsqadavtql rrlgatpgtq igddldrvqr
      121 aastwqatia ptitpaappv tpaqadrsrt qfdavrgald aqaahlatlr negradldsa
      181 asfltamlia vavlvvllfv vlflglrrvi trpilrlade vrhvadqdvh rpvngngpre
      241 iaqlgadvea mrqrildeva elerahamld rrtrelersn adleqfayva shdlqeplrk
      301 vasfcqllqk ryqgllderg eqyieyavdg akrmqvlind llafsrvgrk pgehvvveag
      361 rlvddavanl evalslsagk vehgelpevr vepalmtavf qnlignalkf kgetppevrv
      421 sadrdgedwv fsvsdngigi dgeyaervfa lfqrlhtrsa ypgtgiglal crriveyhgg
      481 riwldteadd ttfrftipva gdegda
//
LOCUS       WP_284745843             430 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284745843
VERSION     WP_284745843.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 430)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..430
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44958
     Region          37..424
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(151,153,280,282,311..313,357)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mayrrtrlla aaalsavala stacsggagd dtnialrmtv wttdknqlal fdsiaaeyrk
       61 ahpevasvkf dvvpgdtsay saalttqlsg gnppdlawil erdapdfvqs galtnlkptl
      121 daaagynage lvpsatklwt kdsglyaypf stspfgmfyn knlltqagit etpdqllasg
      181 rwtwdaakqi atqvaakdtg kaglvirefe ykqwvllasv wrgfgadawg pdgktcgfat
      241 pemtsamtfl hqaiftdkal pgpgttadff agesgltiaq isragllkak pfewgivplp
      301 agpkanaqvi gqagigvpvk gkhakaaadf lafftdpans aklgqyfppa rdsllnaatl
      361 akanplfsqe qlqnvvvngi ktgavlpsht gsariaslvq saldpmwkpd anvpaalagv
      421 cqaidpalsq
//
LOCUS       WP_284745846             634 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284745846
VERSION     WP_284745846.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 634)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..634
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=66679
     Region          <291..580
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtrsfplrrs lvvrltavsl lialgsiaat awlavqtttr aiqqeqgqal sgdatiytev
       61 lgfaaanhtw dqvgpklkal sdqtgrrivl ttldrrvlgd sggapvtlpv katasvdplh
      121 vdavllpqag tsgidpravg pfrlppkerd dvdglarkai acleslgidg qvresasgra
      181 qltgtdplsv ryfaakcgiy elaiptpteq aaldslneav nrclqsqgad pvkldldlel
      241 lagsdqgasq rcldsarreq ltpfvappal lftlgpggsq lptftlsqen ltrilavtgg
      301 vlvlaaaitv lvarrlsrpl ralteaaqqd rpapvksrde vgylatafnd ltarreriee
      361 qrkamvsdia helrnplnvi rgrleaaedg hlpfdralst slleetvllq hivedlqdla
      421 aadagrlrlh pepvdaaela ghvaaahadr aaaagvtltv sphgetglea dpvrlrqivs
      481 nlvtnavrht paggrvtihv sstvdevvia vadtgagiaa adlphvfdrf wraeksrnrq
      541 tggsglglai vrhlveahgg tvtaesevda gstftvrlpk pdlrgegpgv rdaqdvqppg
      601 avaqegdggg gdgraqgrap adrdrraaaa drqp
//
LOCUS       WP_284745935             749 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284745935
VERSION     WP_284745935.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..749
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=80912
     Region          21..738
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          575..609
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(576,579..580,583..584,586,616,619..620,623..624,
                     626..627,650,659..660,663..664,667)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          614..644
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          649..683
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          695..721
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 myrkhetgga egekrksfas elrdvriarg lslaelaart hysrahlanv ehgrraatae
       61 laaacdnale adgellalip rprpgdpdav trpaqlpaap grfvgrgdql stldrvaaqa
      121 drlsiatihg ppgvgkttla lhwahreidr fpdgqlfadl rghsgnqvpa spsevledfl
      181 islgltpadv paseekraal frtmthnrri lvvldnavss dqvrpllpga agstvlltsr
      241 vmltglavra gatllalapf qaddslrflr evvgprvdde peaaravldr cghlplavav
      301 aaeriaahpi rlselaedla eehqrlaala adgdadvrav fswsyralpe aaarmfrllg
      361 lhpgkeisva aaaaladtqs eqalnilral atchlveeag rdrfwlhdll rvyaseqala
      421 ldtpqdieqa qvrelswylr tadeagralg pfrppasdts aldyaaaftw ceqeladfps
      481 vvglalktgh pglacrisqa lfsyfhlrkp wtiwnhtyhl gleaaaklge pslqadmltg
      541 lglvelglgr pecgrdaflr gldllenhde asrsawchig iglahadmed fhlarssler
      601 gmvihraqnd qhaesvalvh ladlcreeqh tedalryagr alslcrsidd rygeglslyq
      661 igmthlaanr feaaaqqleg alsvqraahd dkgqadtlwa lartliacgd ssgartrlee
      721 aasileqrgd paesavraci dnlesgrds
//
LOCUS       WP_284745946             164 aa            linear   BCT 25-DEC-2024
DEFINITION  glycine-rich domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284745946
VERSION     WP_284745946.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..164
                     /product="glycine-rich domain-containing protein"
                     /calculated_mol_wt=17992
     Region          19..144
                     /region_name="COG4278"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443419"
ORIGIN      
        1 msittsthrt grslvshdlf hrltdrivkt esferdlaer imdqalafll acatnvgapl
       61 apselvdigw htflldtsey atfcdraagr fihhvpndne htgkspddvl artvtamrtl
      121 gfhlddalwp rtalssctgc hngchddppp tsqedaqhap qylg
//
LOCUS       WP_284745959             282 aa            linear   BCT 25-DEC-2024
DEFINITION  amidohydrolase family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284745959
VERSION     WP_284745959.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..282
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30832
     Region          2..281
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mrvdahhhlw rlsarpqpwl dgeetsyirr dfgvpdlqka agsagigqtv lvqvlpdlde
       61 tieflalaee npliagvvgw adltsstvds dlerlravpg gellvgirhl vqaepdprwl
      121 vrddvlrglr avrdaglayd llvlphqlpa aieavravpg ltfvldhlgk ppiatrevnp
      181 waihlktlad epnvaakisg lvteadlehw ttedlrpyve talaafgpdr lmlgsdwpvc
      241 llaagyetvw rtteslltrl tdaeraeisg gtaariyrld qp
//
LOCUS       WP_284746021             541 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF885 domain-containing protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284746021
VERSION     WP_284746021.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..541
                     /product="DUF885 domain-containing protein"
                     /calculated_mol_wt=59668
     Region          21..539
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
ORIGIN      
        1 mtseaialad elldvlgtwm pleatfvgvp ghdaelpdps eaghqrlrar aagirarara
       61 sadddhvtlg vvvqqaevvl tqldarvvef tladpmfata mshlaflpql tpageraeed
      121 flarlaafpa fydavarrqr dglragrtpv drmahnaigf ldrflaqetp fpqpltgdrg
      181 errdrlvaev vrpaltryre flatevaghg rsddrpglcw ledgeahyaa larmhtttdh
      241 tpeelhqlgl dvlagleaey aeiggrefgl tdpaqvrrrl rtdeslrwrd aeemletara
      301 aiarataaap dwfprvpdae cvvravpead apvaaaayym ppaldgsrpg vyytnthevh
      361 trdrfiaetv afheavpghh faealaqelt glprlrrial itaysegwal yterlademg
      421 lfssdvmrlg mvaedsvraa rlvvdtglha lrwtreqcve flrahtvlse vevqsetdry
      481 iespgqalay mtgrleilrl rrfaeeklge afaikdfhdv vlgggplplk vlgdvvrawa
      541 g
//
LOCUS       WP_284746043             373 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284746043
VERSION     WP_284746043.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..373
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41294
     Region          13..370
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
ORIGIN      
        1 mtttdlppsl latlpgtyyt dpaifaleqs kifeadwfca vrsadlagpg afetvqvgke
       61 svlvsrgrdg kltaflnvcr hrgarlcted sgtvkrafqc pyhawtygld gkliaapnlt
      121 gmpdvdrtaf gltkvhlrew lgyawvclad epppfdgtvv aavterlgge saieaygvdg
      181 lalgkrieyd vkanwkqiie nfmecyhcat ihpeltevlp efadgyaaqy yvghgaefgg
      241 dvqgftidgs egvdrlpgvt edqdrkyyav tirpqvfvnl vpdhvilhrm fplapdrtlv
      301 rcdwlylpgv vesgkdltrs ielfhrvnqq dfeacercql amdsrsyang gvlvpsehhi
      361 gefhdwvrtr lgl
//
LOCUS       WP_284746206             538 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 27 protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284746206
VERSION     WP_284746206.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Bhatia,S., Singh,A., Batra,N. and Singh,J.
  TITLE     Microbial production and biotechnological applications of
            alpha-galactosidase
  JOURNAL   Int J Biol Macromol 150, 1294-1313 (2020)
   PUBMED   31747573
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Kitaoka,M.
  TITLE     Diversity of phosphorylases in glycoside hydrolase families
  JOURNAL   Appl Microbiol Biotechnol 99 (20), 8377-8390 (2015)
   PUBMED   26293338
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19064013
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..538
                     /product="glycoside hydrolase family 27 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56508
     Region          33..316
                     /region_name="GH27"
                     /note="glycosyl hydrolase family 27 (GH27); cd14792"
                     /db_xref="CDD:269893"
     Site            order(40,75..76,117,158,160,194,216,220)
                     /site_type="active"
                     /db_xref="CDD:269893"
     Region          328..402
                     /region_name="Melibiase_C"
                     /note="Alpha galactosidase C-terminal beta sandwich
                     domain; pfam17801"
                     /db_xref="CDD:465512"
     Region          409..537
                     /region_name="beta-trefoil_Ricin_XLN-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold,
                     found in Streptomyces olivaceoviridis
                     endo-1,4-beta-xylanase and similar proteins; cd23418"
                     /db_xref="CDD:467297"
     Site            order(425..428,438,440,443,447..448)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(434,467..470,480,482,485,487,489..490)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(453,457,459,463,467..469,480,482,485,489)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467297"
     Site            order(510..514,523,525,532..533)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
ORIGIN      
        1 mpvrlrhllt aaatalavap aavaapgspa ltpplgwnsw nsfgcgvtet airqaadamv
       61 ssgmkdagyq yvvvddcwfd pqrdsqgalr assskfpsgm kalgdyihgr glkfglyqvp
      121 tdrtcaqrtg typgstgsag hevqdaatfa swgvdylkyd wcspagtrde qvarftvmrd
      181 avratgrpiv ysinpnsyha itgdkydwgq vadlwrtted lldiwqngnt nsypmgvgnv
      241 ldvtaplaaq agpghwndpd mlvvgrpgls ltesrahfal walmaaplma gndirtmsad
      301 isavlrnprl laidqdrlga ggrrvrddgn vevfakplad gsvavgllnr gsatttvstt
      361 aaqiglsgta ftltdlwtga tsttggaisa svpahgvaay rvsggapfaa ttsrlrgags
      421 grcldvdnas taagagtliw dcqtaanqlw tswengeirv fgdkcldadh qgttngtrvi
      481 swpcsgqdnq kwtlgtdgsi rnvhsglcld aegaatangt hailwscngq pnqrwara
//
LOCUS       WP_284746091             766 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284746091
VERSION     WP_284746091.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 766)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 766)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 766)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..766
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=81498
     Region          100..759
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mtvrrypvav llvvvtvalv vvngfafwgd tfalwvddam qlsagvaavv cgvlvarrvr
       61 ghqrwwrvlv algmagwslg qcawswyqlv dgrglpspsl advgylsfpv falaalfvla
      121 rarirpdrer fqpaqwtahf gvavvldgli vtgslfiltw taalgqlvra tapdkltwsv
      181 aisyplsdlv ivvvavllvv fdrvdrpyra nlllaavgiv alaasdsvfa ylvsigaesm
      241 kpwsdggfvl gplfiafall vtpgqrrrde aspaggvdww qlalpyvpvt avallitgql
      301 lagagpdgve vfvgvlvvfl vlarqllsll dnrlllrrvy dgqqqlthqa yhdpltglan
      361 ralfadrldr aveipdrplv lifvdlddfk evndrfghag gdvllhavaq rllscvragd
      421 tvarlggdef aillegelda pqavadriqg vlrrpfavhg tlvsvrasmg lvvpdpaepl
      481 vtsdvllgra dtsmyagkrl gkdttvvyrp sqdgppdfps alrrakggip egfglvfqpi
      541 vrladetpaa vealarwttp dgtavspetf vraaegaglg aeldalvldl acreitaagl
      601 dltvhvnvca srlgaaaler svasaldryr lpasrlvvei tetvpvpdla agaaairrlq
      661 elgvrvaldd fgagyssltv lhalpvdlik ldrslttgvq perdaalcra lvglcadlel
      721 dvvaegieta eqaslvtrag cttaqgylyg rpaplsalrl stipag
//
LOCUS       WP_284746239             954 aa            linear   BCT 25-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284746239
VERSION     WP_284746239.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 954)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 954)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   3  (residues 1 to 954)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 954)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..954
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..954
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=100352
     Region          1..237
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          108..935
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mleatvlgpv garvhgtpvp vkgrlgrtvl aalalacrqp vsverlidal wgelppatar
       61 tqvhiqvskl rasldrvgag gavvtvssgy lldcvadvde vrqllvtara agdpadtagl
      121 lraaldhwtg tplggvtahl agaelprlde lriglaeewi daeiacgraa rllpeltalv
      181 qahplreglh hrrmlalhra grradalaaf qearrvlrde lgmdpsrell aleaeilsve
      241 tppavtvvpa qlpprtsgfa grdaessair talarrtdap plvlitgmpg igktalalha
      301 gaasahaypd gqlyadlrga dtrpaaphei lagflralgv parsmpatve ertaefrsrt
      361 agkrvlvvld naataaqiep llaadpgcat ivtsrsvlpd veqavrvpla plsdrvagtv
      421 lanvagaarl gededtvatv leacggvpla lriagaqlaa ypklsvaela arlsdesrrm
      481 reltvgqrsv rdsldasfrl ldrearaaml alaaigaptf tgwplapvld vplprtdevl
      541 ahlcamslld qagpgrdgvp ryrmhdlvra ycrtvgpslg shaldrlagw avaltrhaye
      601 gmlgmrvgya vlaetaaplg qdvvghvvke plpwvgadvd vllavfglav rggllrpaaa
      661 lllvlraplv rldlsdhgar aaarlanvag sdpvvrvtaa lvaatarmhr sryadvvail
      721 tevplagvdl alraevltkl gdayercrdw hraitamrea vvcfrksgnl agmsgchgtl
      781 aalyrdhlgd lraatahgtk alrladaagd wktraqvrlv vlrtalacgd atfaaelaeq
      841 arclserngd pigqtwclta eadahrangd lsaarrsadr alglarrirr pdaesaalla
      901 lasielaagd raaarriaha alrlqdrfds pveragvekv laeidcqlps gaer
//
LOCUS       WP_284746247             928 aa            linear   BCT 25-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284746247
VERSION     WP_284746247.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 928)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 928)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   3  (residues 1 to 928)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 928)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..928
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..928
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=99639
     Region          1..242
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          110..921
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          714..738
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          749..779
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          790..818
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(791,794..795,798..799,801,825,834..835,838..839,
                     841..842,871,874..875,878..879,882)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          823..859
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          870..898
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mefrllgavv avvdgtvvel gpvrqqcvla alavdapgvv svdrlvdrvw gddpplrark
       61 tllnyltrlr halatagpad avirrhaggy slrldpaeid vhrfrrlcsr aragdarhaa
      121 alleealglw hgdavagltg ewvtaererl hrerldaehd ltgallalgh gedlvtglaa
      181 raaehpwder aaghyllalh ragrtadala yyrrlrerlv aelgtepgta lrdvhrrilg
      241 adpaldarsa aapvvpprql pavpasfvgr daelgfldaa lddakpgrvv vlaiagaggi
      301 gktwlalhwi rrrldrfadg qlfvdlrgfs pagqpmdpav avrgflgalg veparipagt
      361 qaqaalfrsl vadkrmllvl dnavdteqvv pllpgggsct vvvtsrtqlp glitghgarh
      421 lpldvlsgde atalladrlg dartraeqaa vdrlagfcgg fplalgivag raatrphasl
      481 aglvselres glralegvep tsglpavlsw slhaltedqa taftllgiap gpdiglpaaa
      541 alvgsppeac rttlrvleqs slisqdargr yrmhdltrry atdiacelpe garrealrrv
      601 ldfychtaft adrrlaphrh pieldpaaag agpgrpadda aamawfdsey anllaaqhaa
      661 vaqkrhttaw qlawalttfq hrsgrredhl agwqlaaett aslpggatgs lvqrllggay
      721 aelgrfeeat rhldralala vehgddiaha yahrvlaltw arqgddklaa mhaadaldlf
      781 rglarpvwea ealnalgwyt arlgdhdtal thclagldlf rgnhdpsgea atldslgyiq
      841 dhlghhreav eyyeqavrvl rglgytfeia ntldnighpy aalgdverar aawseahely
      901 rrqdrpdeae rvrqrldalg epgesqvr
//
LOCUS       WP_284746344             358 aa            linear   BCT 25-DEC-2024
DEFINITION  fatty acid desaturase family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284746344
VERSION     WP_284746344.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..358
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40525
     Region          19..354
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mttsakelgh aeieklgiel delrlrvaad lgaedadyih nvvavqrfce vsgrlllfag
       61 wfppawaggv aalalskild nmeighnvmh gqydwmkdpa lnsrtfewdm vcpgeqwrrs
      121 hnfmhhtytn ilgqdrdvgy gilritddqp whpyylgnpv yaaaqalffe ygimlhdlev
      181 drivqgrrhw advrpllkpm lrkvarqagr dyvvhplltg plapltltan vtanvvrnlw
      241 afsiifcghf pdgaevftee esedesrgqw ylrqmlgsan itgspvfhvl sgnlshqieh
      301 hlfpdlpshr yprmaaevre iceryglpyn tgslsrqlgs varkifrlal pakrpirp
//
LOCUS       WP_284746258             340 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284746258
VERSION     WP_284746258.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..340
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37841
     Region          <1..>172
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
     Region          <269..316
                     /region_name="FNR_like"
                     /note="Ferredoxin reductase (FNR), an FAD and NAD(P)
                     binding protein, was intially identified as a chloroplast
                     reductase activity, catalyzing the electron transfer from
                     reduced iron-sulfur protein ferredoxin to NADP+ as the
                     final step in the electron transport...; cl06868"
                     /db_xref="CDD:447143"
ORIGIN      
        1 mlpwdgdlag rldrhtvesa llrdnplgdp herplwvyvp pgyddgaery pvvyviqgyt
       61 ghlsmwanrt pfrqpfveta davfaggapg cvvvyvdawt ayggsqfvds pgtgryhsyl
      121 cdeivpwvdv hyrtipdres raiagkssgg fgamitpmlr pdlfgalath agdslyelcy
      181 vpdfgkavra lrgydrdiqa wwadfrarpa ftrpedatll qligvsacfs agpdgtpelp
      241 fdpatgvlrp evwqrwldwd pvrmvpdrae avrswravwi dagtsdeyfl dvgaeafrae
      301 vvkaglaedr ihfelfeagh aaidyrypls lawlaerlar
//
LOCUS       WP_284746383             290 aa            linear   BCT 25-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284746383
VERSION     WP_284746383.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..290
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32219
     Region          21..285
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 meqyeldavk rittrpprdf rtlavrgltp vigaevtgld ltrelteeql telktafldh
       61 hvlvfrdqdi tpddhqrlaa nfgelrpvnp ppehgnpyil evatapesat vfgngwhadg
      121 tadaepslgs mlhitrmpep gsggdtlfan mhlaydmlsp klkellaglt aihdgahafr
      181 ghkipegyep pvsehpvvvr hpetdrplly vnpaytsrip qlsgdesqav ldllfsvvpn
      241 rpmlacrvrw epntlvfwdn rcvqhhatyd yypytrfgnr vainggplkg
//
LOCUS       WP_284746409             282 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284746409
VERSION     WP_284746409.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..282
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28736
     Region          8..279
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mrsstrdgaa favaamlcvq lglavsvglf drigpegaaw lrlawagvll vvvvrprpas
       61 frratfaacc algvvtagmt mlfmeavarl plgtasalef lgpltvavtr grgskrlwpv
      121 laalgvvllt epwrggadla gvgyalasav cwagyilltq rvgdevagvr glavsmpvag
      181 ivatlaygpg vlghltgell liglglaill pvvpfsleml alrrlntsaf gtlmslepai
      241 altiglvvlh qvpdlaaaag vlfvvaagig aertgarepv vl
//
LOCUS       WP_284746483             405 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284746483
VERSION     WP_284746483.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..405
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42964
     Region          1..400
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 msyiigvvlf algicvsval heaghmvtak afgmkvrryf vgfgptvfsw rrgeteyglk
       61 wiplggfcdi agmtaldevt pdeapramwr fktwkrtvvm sagsvthfil gfvvlylmav
      121 tmglpnlapa ttepvlaats carsttteae aeaqdiscpp galtpaktag lqvgdkvlsv
      181 ggkpvatwda mlaavqatsg ptafqvlrdg ktlnltvdvp kvkrwtsagv kevgmigasa
      241 qppalttqyg pvaavgatfs ftgtmfseta qrlvefperi pavvtaifgg erdpntpvsv
      301 vgasriggea vergiwvlff fllaslnffi gvfnllpllp ldgghiavvw yervrdwira
      361 rrgkaaggpv dytklsgitm vlvliggavt lltvtadivn pirlq
//
LOCUS       WP_284746507             510 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284746507
VERSION     WP_284746507.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..510
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53811
     Region          12..508
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mdsydvvvvg gghnglvaaa ylaragrsvl vlerrgetgg aavsfrafdg vdvrlsrysy
       61 lvsllpkkiv adlgldvrlk rrrmssytpt ggsgllvdtg ddgrtaasfr avtgatsdfa
      121 awqrfyelte rvaersfgtl tepllsevdf rdrlgdgeaw sllferpige tltsrfgddl
      181 vrgvvltdal igtfaaagde dlrqnrclly hvigngtgdw dvpvggmgav tgslaavaaa
      241 agarlvtgae vlsidpggev ryrrddaehv vrgghvlanv apstvarllg eepperpega
      301 qlkvnmvlsr lpklrdphvd paeafggtfh vnetftqlet ayreaaagki ptlppceiyc
      361 hsltdpsilg paeraagvqt ltlfglhmpa rlfeghneea reaalratla slnsvlaepi
      421 edclltgpdg kpcveaktpl dleaelglpa ghifhrdlaw pfatdpaqag kwgvetaher
      481 vllcgagavr gggvsgipgh naamavlgad
//
LOCUS       WP_284746512             356 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284746512
VERSION     WP_284746512.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..356
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=36605
     Region          1..355
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mrvlvigsgi ggaatawhla grgaevvvad aarpgtatea gagivspwts rwedalypla
       61 saagryyref taeledssfe vvggmvvsae eselaevher ltaraadape igeirrldpd
      121 qarelfpala pglgavhlag agrvdghrlr gallaaaerr gakfvegeva fradgtvvsa
      181 sgpleadsvv vaagawsrel laplgidlpv tphrgqishf dlpgtdtsaw pvvlprtshy
      241 llafgggrvv agatreaeag fdyrvtaagq revldnaltv apgladatla etrvgfrpgt
      301 pdglpilgsl rpglavstgf gaggltnapf agklvaaial redpgfdltp fapdrf
//
LOCUS       WP_284746533             464 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284746533
VERSION     WP_284746533.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..464
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47848
     Region          3..462
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 msaqtfdvvv igagpvgeva aeraargglk valveherfg gecsywacip skallrpgnl
       61 laaakripgv pvgdrldpaa vfarrdwftg kgddsgqvew argagiepir ghgritgere
      121 vtldgdrvlt arhavivctg svpstpsipg ldtirpwgsr eatsaesvpa rlgvlgggvv
      181 gvemaqafas lgsevhlvit gerplprnaa iagdlvlhgl reagvyvhtk sgiigvsdtg
      241 ngtevvlkdg erlvvdeflv atgrrpatag lgleafgvea ghpltvddtg rasavdggwl
      301 yaagdvtgra plthqgkyga raagdtvaal aagkpvstea wspftatadh savpqvvftd
      361 pevaavglad arpgsadrvv didiavagss lhadgytgka rmvvdternv llgvtfvgqd
      421 vsellhsati aivgevpldr lwhavpsfpt isevwlrlle aygl
//
LOCUS       WP_284746540             404 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284746540
VERSION     WP_284746540.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..404
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43103
     Region          159..398
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mdgttsprrv pkhhglsakt lrrlehasgs lasasiavme rrltwfprlp adqrasvlli
       61 tqagaagfvd wlrdskealq ltteafrdap aelsrwvslr qavgmvrlai evfeeqlpef
      121 aaneaeraal iegilrygre iafaaansya aaaeargawd arlealvvdg ivrgdaeesv
      181 lsratalgwe psaaatvlvg nppsedpptv vfevrsraar vgrpvllsvq gsrlvvvvgg
      241 pteggvkere ilarmsvafa egpvvagptv pslaeahhsa tealsglrav vgwpgaprpv
      301 rsadllpera lsgdaeaerl lvdtiarple eagptlqrtv eaylesggvl etcaktlfvh
      361 pntvryrlrk aadltghqpt dprdalvlri altvgrlara rglw
//
LOCUS       WP_284746592             471 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284746592
VERSION     WP_284746592.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 471)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..471
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=48778
     Region          3..382
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mnppedvlaa lrelragdlp thggrtlayv ydsglsevdt lgaaahalas sangldptaf
       61 psllrmendl vaaasallgd vpgvvgsvts ggtescllav laardahpei aspsivlptt
      121 ahaafhkaah lfglrridvp vdpvtfradp aamaaaidds tvlvvasaps yahgvldpis
      181 eiaaaasarg vrmhvdacig gwvlpyfarl gadvapfdfr vpgvtsisvd lhkyaycpkg
      241 tsvllhasae lrrshyfasa awpgytmlnt tiqstrsggp lagawavvrh lgedgylrla
      301 tstreavsri ragieelpgl rvlgdpvstl iaftgddgfd lftvademkt rgwyvqpqfa
      361 hlaspvnlhl tvtaanhgte kefladlaas ldaarasgpv vidpavaefv aaldpatlts
      421 eqfagllvaa glggasglpe rmapinalla tapaplrerl lleflgalyt p
//
LOCUS       WP_284746724             306 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284746724
VERSION     WP_284746724.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..306
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32660
     Region          16..306
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mergtttddv relrltvpaa dglalastlt lpagdgphpa vlclpgsgkv drdsnagrvr
       61 mdlgrplaat larhgiaslr ydrrgvgatp gdwhsvgfld nradgeaaln alrghpeirs
      121 ravgvlghse gavhamwlaa haqpaaavll agyarpgeqa lrwqgtrlad slprpllpll
      181 rrvatrqlar laatttdtar igglrinarw wreqlaydpr pdlaripvpv lavtgakdvq
      241 vdpgdldvia qlvpggaeth rapglthilr rtdgpasvfs yrrllrdpvd eellttvagw
      301 latrlr
//
LOCUS       WP_284746756             320 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284746756
VERSION     WP_284746756.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..320
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=34359
     Region          2..319
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrylitggag figshltehl lerghevval dnlstgtldn lagvrdnpgf rfvrgsvtdp
       61 saveacmagi daifhlaaav gvftildktm eslrtnlhgt etmldaalqh dvpilvasts
      121 eiygkntadg ltedadriig splknrwsya eakaldetfa ylyavehglr tvivrpfntv
      181 gprqtgrygm viprfvkqal agepitvfgd gqqtrcfchv hdvvpalval ladetayskv
      241 fnlgsteqtt iaqlaervis atgsastiak vpyeeaygdg yedmqrripn cekalgqigf
      301 sptrtlddii aavvadqrgs
//
LOCUS       WP_284746758             862 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284746758
VERSION     WP_284746758.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 862)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 862)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 862)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11971133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..862
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=91232
     Region          <17..859
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          798..852
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mgaiwgqnrr enpqgalafl edlliecdag vgetvlvggg pasgkthlqh qvvvrakelg
       61 ivtltaagaa derdvdggvi dqllaspllp psltgrpadg dgrdvderia elcsaihrla
      121 reravlvavd dlhhidetsa rlllrlqrra psaalllvln hadgsyadsp ftslphrhve
      181 ltplsvqaia elvqgdglpe rihelsagnp llvralvdah rgsadtgsay seavqrllhr
      241 ygsplrevat aiavldsdvt teavaivagv dpleaeastg rladaglvag vrfrppaaaa
      301 vvgglrgpek vrlhvraaev kharglspae varhlvaage aeadwalpvl vaaaeqvmlg
      361 ddiefatrcl klaasvakar weqqtisqll akitwrvnpa aaaphlrslr eagsldasdr
      421 iglarqslwl gdrdtfersf aaletdvepl dprtsaelil agywhygvst ttadpgdpwl
      481 htanslaamw rtggtettsa caerilqncr lsdtsleala tailalahdd kadraegwct
      541 slseeaeyrg aitwkamlda igaslrlrrg dvpgavdlgt ralgmldapn wgvaisypla
      601 tlliahtaag afkdaaavlr hpmpdavwat lggvrylrar ghfhlatnrg laavsdlqqc
      661 rrilheqdle lpavlpwqad laeanlglgn tamavelarq slagpadays rgsalrvlal
      721 agdaaarpgl lnraaeafka sgdrlelakt mrtinhlsqr aeragslvka vhvprqgrsr
      781 pavprpvarp epvaspsasv lseaelrvae lavegrtnrq iaetlyitvs tveqhltrvy
      841 rklgvagraa lagefadaeg gq
//
LOCUS       WP_284746858             491 aa            linear   BCT 25-DEC-2024
DEFINITION  WS/DGAT/MGAT family O-acyltransferase [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284746858
VERSION     WP_284746858.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Stoveken,T., Kalscheuer,R., Malkus,U., Reichelt,R. and
            Steinbuchel,A.
  TITLE     The wax ester synthase/acyl coenzyme A:diacylglycerol
            acyltransferase from Acinetobacter sp. strain ADP1:
            characterization of a novel type of acyltransferase
  JOURNAL   J Bacteriol 187 (4), 1369-1376 (2005)
   PUBMED   15687201
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Kalscheuer,R. and Steinbuchel,A.
  TITLE     A novel bifunctional wax ester synthase/acyl-CoA:diacylglycerol
            acyltransferase mediates wax ester and triacylglycerol biosynthesis
            in Acinetobacter calcoaceticus ADP1
  JOURNAL   J Biol Chem 278 (10), 8075-8082 (2003)
   PUBMED   12502715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496208
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..491
                     /product="WS/DGAT/MGAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0045017 - glycerolipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=52989
     Region          4..484
                     /region_name="acyl_WS_DGAT"
                     /note="acyltransferase, WS/DGAT/MGAT; TIGR02946"
                     /db_xref="CDD:274360"
ORIGIN      
        1 mrqltpldvq flnaestttt ghvgglsild pstapngrlt lddlreligs rlhlakplrw
       61 rllpvplgld hpywiddpef dleyhvreia lpapgderql aeqisrltar pldrrrplwe
      121 aylvhglqdg nvavytkvhh saidgvsgae ligvlmdtta epppqkppkt pqkeplptpl
      181 alalngtkkl alhpvkaalq vpkllqhlde vpglgrypgv gllakagsvl nrvtrqgsgr
      241 headrprlva pdtpfngpis phrrfaygsl pldevkhvkn tfgvtvndvv malcasvmrr
      301 wlvdhdalpd qplvtlvpls vrtpeqakda gnqvsvmlap lpthladpaa rlaevttamv
      361 aakqryqplp aswlvdfsgm lpaalgglaa ratmkflgat apvvnlvvsn vpgsqsplyl
      421 agarllanyp vsaitdasgg lnitvmsydg kldfgfvacr elipdvwdli dhlhdalael
      481 tklaaehtre a
//
LOCUS       WP_284746883             118 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284746883
VERSION     WP_284746883.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..118
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13106
     Region          3..110
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mdntetppad mcslrevldl vgdkwairvl vqlgdgprrf seleraltgv srrmlsltlr
       61 glernglvtr kvypevpprv eytmtphaae ldeplhalsa waakhrekvg aarlayds
//
LOCUS       WP_284746916             422 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284746916
VERSION     WP_284746916.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..422
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44919
     Region          23..270
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 milavtaaqp pasaadssdv tftnggvtlh gtvvappggs klpglvmvhg sgahsredyr
       61 eqaeafareg iatliydkrt egyslfsrsy stladdalaa vealrkrpev dparvgvwgl
      121 seggwvapla asksadvafv vtlgangvep srqqawaien qlrrlgmdgs mvgmasstmm
      181 rqlvgggvfp eahydsvavl kslrqpvlgl wgakdvltpp geavrifqes lahytlrvfp
      241 daqhqlrrtt dgydklpgya pgylelvgtw vhampaassa dappvqdrps favtplswye
      301 stwlqlavll flvlafafyp lfrrgpsaas arwltatgll avlgflafdv liqvtmgrnl
      361 gpvlagrplp wlvlqllslg avaaaigtav awwrhrtprl gvllaggvvf vpwavywgll
      421 gi
//
LOCUS       WP_284746992             207 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284746992
VERSION     WP_284746992.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..207
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23291
     Region          <46..152
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mshthdqpmt venmlkqefw etlyqrddhq iwsgnvnrnl ssevtglkpg raldlgcgeg
       61 gdaiwlaqqg wtvdgadist lalaraeaag kergvdvrwl hrdildwrpe etydlisaqy
      121 mhlppdlrrk vftaaaaavr pggsllvvgh spkamrefeg qkppeelffe peeitnflgd
      181 awewivetce trgeghhtda vyrakrl
//
LOCUS       WP_284746457             163 aa            linear   BCT 25-DEC-2024
DEFINITION  EXPERA domain-containing protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284746457
VERSION     WP_284746457.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Sanchez-Pulido,L. and Ponting,C.P.
  TITLE     TM6SF2 and MAC30, new enzyme homologs in sterol metabolism and
            common metabolic disease
  JOURNAL   Front Genet 5, 439 (2014)
   PUBMED   25566323
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526086
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..163
                     /product="EXPERA domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0032934 - sterol binding [Evidence IEA]"
                     /calculated_mol_wt=18494
     Region          45..143
                     /region_name="EBP"
                     /note="EXPERA (EXPanded EBP superfamily); pfam05241"
                     /db_xref="CDD:461600"
ORIGIN      
        1 mnlplrdrki dvffavlfsa ftvtslisdl lptvgvdfsk psdnffvnsn ywyahdadpl
       61 fmhppdwmri vtglsafvym pfyvvlvfal lsgrnwiqlp sviyatmivt ltgvvvfgve
      121 ffgdpafrtg npakflafnl pyvlvpllll vrmrkplpft rrf
//
LOCUS       WP_284747068             181 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284747068
VERSION     WP_284747068.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 181)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..181
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20233
     Region          1..>81
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mteprrrrpa tpeeakalgh plrlrimrmc lveeltnkql adrldrdpgt vlhhvrqlvs
       61 agllepapvr tgasgalekp yksnnetwwl dgpladadae trfapieifq eeiraagpes
      121 vavhekfllh lspdevgeld rrilavldey vatdherldr palggifvlh hvtreapdek
      181 p
//
LOCUS       WP_284747123             233 aa            linear   BCT 25-DEC-2024
DEFINITION  S1 family peptidase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284747123
VERSION     WP_284747123.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Perona,J.J. and Craik,C.S.
  TITLE     Evolutionary divergence of substrate specificity within the
            chymotrypsin-like serine protease fold
  JOURNAL   J Biol Chem 272 (48), 29987-29990 (1997)
   PUBMED   9374470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475742
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..233
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=23784
     Region          31..233
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mriartgvvv sgvllsalaa aapsvaaqpa iidgsnadsl hsaarmfagg qeicsatiia
       61 pdwvltarhc tqgadgkpis fhvgdldqtk gttvnatsvh eapdsdialv qidqqvqtey
      121 aplgsegdvk vgdqaevygw gatctdkpei ecqsqllkva kvsvtsidcp dgaagvsvca
      181 nrgdgitagg dsggpmyang kqvgvastsd rqsytayini tkyrdwisqt agv
//
LOCUS       WP_284747208             319 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284747208
VERSION     WP_284747208.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..319
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=33521
     Region          13..301
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mpftslvarl pypsatvqra vgiaavlaqa ligvtgsivr vtgsglgcpt wpqcvagslv
       61 pvnhpgihal nqwiefsnrm ltgvviavaa iavltawrvq idhpgrtrlv klawtmpggv
      121 vlqavvggmt vlaklewwtv aihflattpl vwlavlllra fregdeparp lvpgrsvlva
      181 lavvmwlvla agttvtgagp hsgdinthrl avsvetlaqv hggllvlyml llavfglqll
      241 ragapkslwq ryiwvwvial aqgglgslqy vlgvpeamvs fhvlgamavi vatatlwtgs
      301 rdrgpvtsle aaprelaaa
//
LOCUS       WP_284747227             363 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284747227
VERSION     WP_284747227.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..363
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=38348
     Region          4..363
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mnsiaivgag lgglacarvl qlhgldvtvf eqeasagart qggtldlhgd tgqvalrtag
       61 lhdefralar pegqqmrald phsaevvmde vpaegddfrp eidrgqlrgl llgslkpgtv
      121 qwgqpitdvt tagrltfadg tardfdlvvg adgawsrvrr altgvrpeys gvtfvelgld
      181 dadrrhpdla altgqgtmmt kidgkalvaq rnsnghircy aifyasedwa agldfadtaa
      241 vrahllerfa gwhpsllgfl hdldggftnr plhvlpvpha wthtprltll gdaahlmppl
      301 gvganlalld gtelatalat apsvgeavrt yeagmlprsi etaqacatgl hdllsddlrs
      361 maa
//
LOCUS       WP_284747234             108 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284747234
VERSION     WP_284747234.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..108
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11608
     Region          19..>79
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mttararglt hgvpaevslq dalaavadpv rrnilrelaa vpewtkacgt fdlpvakatl
       61 shhfsvlraa glieqrdagp rrlnrlrrpe fdaafpglld lvlshpgr
//
LOCUS       WP_284747382             306 aa            linear   BCT 25-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284747382
VERSION     WP_284747382.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..306
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34858
     Region          37..305
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 msvdlparip lreavtpddg ivegprvlhr cesepyerft lrplgrviga eidgvdlaep
       61 ltpelredln rallewkvif frdqditsaq qrafaanwge letnpfipkg dddavtrfer
      121 taampgyeni whvdvtwrpn palgsvlrli evppvggdtm wadmaaaydn lpedvrarid
      181 gltavhdylp gfdrfadpal larwqdefpp vehpvvrthp etgrrtlfvn qaftthvvgm
      241 drdesdrllr ylflqahtpe fqvrfgwrpn svafwdnrat qhyavndyhp hvriaervai
      301 agdrpr
//
LOCUS       WP_284747410             506 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284747410
VERSION     WP_284747410.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..506
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=53597
     Region          172..504
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 msssqraerr rfraqrpwsl rrrlivqlaa llalvclvvg vvtefalsef lvgqqdkrla
       61 aatdraahga drpppwtydg eapppdplra lgqgegtlav vqigsratgs vidstvtssl
      121 pkrrapfrni ekgqtlalla lpsdgkpysi dlggklgdyr vvsttspgge ktviglpltd
      181 vnetlwrlgf ilggvalagi lvagavgaat irrtmkpldr laatatrvse lpldrgeval
      241 servpdadtd pgtevgkvgs alnrmlqhva nalsarhase nrvrqfvada shelrtplaa
      301 irgyaeltrr sgeqvppdva famsrveses rrmttlvedl lllarldsgr qvvhewvdlc
      361 rlvadavada hvagpghkwl mdvpgepigv lgdagqlhqv vinvlanart htpagttvtt
      421 slstsdgklr lrvaddgpgi ppdilpdife rfargdnsrs raagstglgl aivaavvaah
      481 ggrvgvqsrp grtefeitfp eapape
//
LOCUS       WP_284747614             970 aa            linear   BCT 25-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284747614
VERSION     WP_284747614.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 970)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 970)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   3  (residues 1 to 970)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 970)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..970
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..970
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=103578
     Region          1..240
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          110..898
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          686..714
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(687,690..691,694..695,697,727,730..731,734..735,
                     737..738,758,761..762,765,768,771)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          725..752
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 masfavlgpl aiesppghwv alrgdrqrtl lavlllnanq hvhvdvlvea lwperppksy
       61 asnlhtylsr lreridglrv ehgplgyrlc veraeldllv fraavadgqr agdalaasgh
      121 yrqalaqwrg pvlaglhvpp ldadvarles erlavfedcv daeltagrhg evtgelqami
      181 tehplrerla aqlmialhra grqgdsleiy rrlrttliee lgvepgaevr rvhaavlrge
      241 dpvprmpppv wpvcqlppdi adftgrdael aeltavlgsg agvpvavlsg epgagkstla
      301 vraahrlrar fpdgqlyvpl ggreigevla dllralgvpg pavpddvrar tavfrgrltd
      361 rrvlvvldda gdpehvrall pgtpgcavlv tsrqrlsgla gahrlslgpl sdaeatelln
      421 rlagarvare radagriiaa carlplalri agsrlairph lrlgeladrl edevrrldel
      481 tvsdlavrss ialsheglrp parrafrllg qcrladlpaw avttligepd adeaveelve
      541 asllearepd atgegryrmh dlvrlyaaeg ppvaggaatv laatlalada aaarlprtvp
      601 mpamaheafp qplpdalver llarpeewfa aeranlvrli gslgarkall lldklsvyly
      661 lhghyadmra ayetvlaate drpsaaiaea nlallrharg qyeeaaaayr ecakeleahg
      721 dhrthawvsa nlahcliglg raeealqtar slstlddqfl vreaesaall rlgrvaeare
      781 vdllalasar ssgdprrigt alhgfawssl ltgddaeaat aiaesvellr gtvarsalak
      841 slrtlgaiaa atgsrdrata afeeartlar dlderprels ctraiaaswi gagraaqaip
      901 vlracldefr emggkpatgl twlvlsrace aageeeaaae aaaeaaslad srdasaaalr
      961 rallaltepa
//
LOCUS       WP_284747643             253 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284747643
VERSION     WP_284747643.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..253
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26041
     Region          16..253
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mgdestispk drfltvygrk pvlealadgg lrvdkvilad targpgaaei qraakeagva
       61 vqrasahrvk vlagngkqdq gvladvvapr mraleaalsd rrppsrvlll dgittpanvg
      121 milrtataag ldgvivprrg vaaldplvvk asagvafrap vlrcgsarda aemlteagyg
      181 lyalgasakt tifeidlpqr aafvlggetg gvgtevgelv tewvsipmpg dveslnvsaa
      241 aavlsfelvr rar
//
LOCUS       WP_284747792             339 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284747792
VERSION     WP_284747792.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..339
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=36250
     Region          2..305
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrvlltghkg ylgtvmapvl aaaghevvgl dsglfeqcll gpapadpggy vvdlrdvtak
       61 hvtgvdavih laalsndplg slapeltydi nhhasvklak lakdagvgry lyastcsvyg
      121 aggdnlvned aplkpvtpya eskvrveadv heladndftp vymrnatafg ysprlrgdiv
      181 lnnltahahl sgevlvlsdg tpwrplvhaq diaraftaal tapkeavhnk afnigtednn
      241 vtvaeiaqev veavpgstln itgeagadpr syrvdfsrfr eaipgfacew svkdgaveli
      301 eayrkfgltr esfeklftrl awlrsegaag rvddtlrrh
//
LOCUS       WP_284747973             371 aa            linear   BCT 25-DEC-2024
DEFINITION  C45 family autoproteolytic acyltransferase/hydolase [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284747973
VERSION     WP_284747973.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   True,J.R., Yeh,S.D., Hovemann,B.T., Kemme,T., Meinertzhagen,I.A.,
            Edwards,T.N., Liou,S.R., Han,Q. and Li,J.
  TITLE     Drosophila tan encodes a novel hydrolase required in pigmentation
            and vision
  JOURNAL   PLoS Genet 1 (5), e63 (2005)
   PUBMED   16299587
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tobin,M.B., Cole,S.C., Miller,J.R., Baldwin,J.E. and
            Sutherland,J.D.
  TITLE     Amino-acid substitutions in the cleavage site of acyl-coenzyme
            A:isopenicillin N acyltransferase from Penicillium chrysogenum:
            effect on proenzyme cleavage and activity
  JOURNAL   Gene 162 (1), 29-35 (1995)
   PUBMED   7557412
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Tobin,M.B., Fleming,M.D., Skatrud,P.L. and Miller,J.R.
  TITLE     Molecular characterization of the acyl-coenzyme A:isopenicillin N
            acyltransferase gene (penDE) from Penicillium chrysogenum and
            Aspergillus nidulans and activity of recombinant enzyme in
            Escherichia coli
  JOURNAL   J Bacteriol 172 (10), 5908-5914 (1990)
   PUBMED   2120195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF040521.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..371
                     /product="C45 family autoproteolytic
                     acyltransferase/hydolase"
                     /calculated_mol_wt=38193
     Region          27..321
                     /region_name="C45_proenzyme"
                     /note="C45 family autoproteolytic
                     acyltransferase/hydolase; NF040521"
                     /db_xref="CDD:468523"
ORIGIN      
        1 mvatvrehri gdvrwtvvsg preaafralg syaaadirtv laglpswpva erarrspvlf
       61 raiesasqve hpdayaelta laagagvpfd dlllanlrgd lgagdgtgct dlawvgspsl
      121 lghnedgapv fdgigrlltl lidgepgvcv wwypgflpan tvtltthglv wgidsvsvvt
      181 pspcagrhfl artaqrassv aeavsvlrsr psaggfaytm gqvgspavtv vekagsetav
      241 ttvgsglswh tnhfrqlspq wdvapeesla raevcahlap aepdakwlvs altgevyrsa
      301 sggdplmtls tvvtdladgt vtvvprggap lrarvadlas gdvdavgaln gatvpggsgv
      361 svevrptweg p
//
LOCUS       WP_284748011             396 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284748011
VERSION     WP_284748011.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 396)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 396)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 396)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..396
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42232
     Region          68..390
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrpdpeeral rrarwaitaq vavvvsmlva iaggiayaml lsrqhaeadr tlarttelgp
       61 aatppgcvwl ftpvlhapag appagmpiaa lnatvpapgd vhterrpigg mtytirvenr
      121 ggvvsqayfe elyqiqdrss lvsglvvaev lallaavlcg rvlacrairp ladalrrqrt
      181 fvadashelr apltrlhtra qllarrasgr dahdleqlvr gtrelgevve dlllsaqacd
      241 rpefelvelg glaeeavaae avragegkvr lavsrerrpy vvqgvptalr rvlsalldna
      301 lghtppggsi evwlgvpder hvelrirdtg igfpsadaer iferfargsd gdgrrfglgl
      361 alvrevvtgh ggtiaaagrp gdgatftlrl lradpa
//
LOCUS       WP_284748073             459 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284748073
VERSION     WP_284748073.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 459)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..459
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48336
     Region          7..456
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mekltadvlv igfgkggkta ahalsdagkr vvlveqsanm yggtcpnvgc vptkmlvhys
       61 narrleddaq effahsiagv raltsafrag nfasldgkdt atvitgtarf adphtvdige
      121 gddrisvtap tiilstgsap vvapipglat skhlvsstel tqaatlperl ivvgggylgl
      181 efaaiyqhfg thvtvlegad rllprededi aatareileg dgiriitgak itkvedsgav
      241 akvvyekdge theveasall patgrrpvtd glrldaagvr ttpngavevd ehlrtnqphi
      301 yavgdvnggp qftyvaldda rivldqllge gkrttgdrva vphtlfitpp latvgltere
      361 artlglnikv arekvadiva mpraytveet rgvmkfvida dtdlilgaal lsidaqeivn
      421 tvalairhhv tatelrtaiy thpsstealn evlgkvvsg
//
LOCUS       WP_284748129             110 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284748129
VERSION     WP_284748129.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..110
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12173
     Region          18..107
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mttplpgrpv rgsttgrpim alldllgrrw tlrilwelrd gakptfrelq qrcdgvsssv
       61 latrlrelge adladhagdg yalteqgksl fetlvrldaw aadwrprqss
//
LOCUS       WP_284748132             270 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284748132
VERSION     WP_284748132.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..270
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29180
     Region          10..262
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 marvtdekpv pvglstasvw plkagtafel aaelgydgve vmvwadpvsq dvsalrrwsr
       61 rtgvpvlsih spsllitqri wspdpvvrlr msveaaaelg artvvvhppf rwqrrygdaf
      121 gdlvdelees sgieiavenm fkvrppggsk nsrvsafrps idptdvgfrh ytldlshtaa
      181 agmdalvlaq rmgeglshvh ladgtglpkd ehlvpgrgdq pcaelleklv ssgfagqivl
      241 eintrhagtg aqrvrdlaea llfarfhlgq
//
LOCUS       WP_284748194            1239 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284748194
VERSION     WP_284748194.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 1239)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 1239)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1239
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..1239
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=128907
     Region          301..750
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mieavadhqh gigplvryad gtsllltrpl gplrtrdara aglvaklvtk avvtreqaml
       61 svrqlsvcdg grvtlvtvvp rtaipadael rflaglpyar aagarqdkil evaepggapf
      121 dlavpeavle tggslsaagl litsgaglrv vnsaagrpag aprnsakisc nqtsdlgtvy
      181 regirlggcm swrhpvaavl avvlatsgti twteaeaeaa asgpvltrti tlitgdrvvl
      241 ggsrvvsvqr gagrskmafe qhtdvtgdvy vtpedalpav rsgqldphlf dvtklieygf
      301 ddqtrddlpl ivssglavar esglqavrel kslgatavra vkgsglwart qraaapriwl
      361 dspvqgtldk svpqigapta wqagltgsgv kvavldsgid ttnpdlsdvv adakdftgsa
      421 sgttdrwghg thvasivtgr dakyqgvapg vrllngkvlg dtgfgpqssv iagmewaaad
      481 gakvvnlslg tgfpsdgtda msqavnrite qagtlfvtaa gndsslvssp gaatdaltvg
      541 avdrdetlap fsnhgprlgd gaikpdltap gvgiaaakah dsvlgaseps vdeyhmrlsg
      601 tsmaaphvag aaailaqqhp dwkapelkaa lmgsakpgtg msvfqqgagr vdvakavaqq
      661 vlagpagisl gtarwphddd qpmvttmtyr nagtapvtvn laadvrgpdg aaapagmftv
      721 tpgsmmipag gtaqatvtad tkvtgpdgvy qgvvlagdvr tpiavtreae sydvrlnfld
      781 ekgnptqnfs ydftdidhpr dfggggdtvt arlpkgrfyf qsttwsddrr yvfavepelv
      841 vngstqltvd artgaaadvr fadrpsakig raaygferda nwgristwmy ipdftdfrvr
      901 psttsassfd laieaqaaep dgeggfstss ylynvrkhvs gsvpatpgft vrdketarvr
      961 seeavtkpgs tgtregivtr plpygldefy tpgeqwyplf sedgvnllld avprsyrlgr
     1021 pvlerwnaav fgpafpagpr srasrqgeti avnvpmfadq hagriadgpa asahttlsrd
     1081 gkeigtsgia gqgtfvvppd pgvyvlhada trdnalssev vadwtftsat vtgatpaalp
     1141 llavryapdv dawnqvpgrl ptyvpitvdn naggtgrlta lsvsydkgvt wravpftdkg
     1201 allvhpvdak tvslkasatd qagnkvdqti vdaflisir
//
LOCUS       WP_284748207             734 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA-transferase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284748207
VERSION     WP_284748207.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20169552
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..734
                     /product="CaiB/BaiF CoA-transferase family protein"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=78104
     Region          1..320
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
     Region          342..732
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mrvldltdel arqgarllvg lgadvvrvdd dltgherthw hagkklaaaa dldalagetd
       61 vvlesgpvak lrglhadgts rwphavhvvv tpfgltgprr gwvggdlvla saggmtwlgg
      121 kpgeqpkppp reqacqlaga hgaiaallgv lagggqlidv saqeavaatl etgaiswiha
      181 grfpvrnggv yehvahrife aangyvaggy sgsermwtgl qtwlaeegeg dagdlleerf
      241 adqvvrwaer phvdeviarf vakrtareva eqgrsralpw aevtppaelt dnpqlrdrrf
      301 fvsvdgtena gfpwdapglp rpvtlsplve gtwtseprpr aamgrgpldg vrvldltwvl
      361 agpyatkila ehgadvvkve srhrhdptrf spsmrlrpda gpddsgyfln fnrgkrsval
      421 nlrtpegqav lrelaarcdv ivenfspgvl akwgldyasl reinprailv smsgvghtgp
      481 wrkavtfadt laamsglsae tadpgeppqg lvfglgdmva anaavlgald llvrgygghv
      541 dlsqleamaa tmgpavlddg dddprtaahp nrsrhavphg vypaagedrw vaitaqdeaq
      601 waalrdlagl peyrdrraae deidaalagw trgqdateva arlqaarvaa avvatgrdiv
      661 edehltergf yqklthpiag dvlhegivar ltatpgalts papllgehte avlrelldid
      721 ddrlaalraa gite
//
LOCUS       WP_284748254             385 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284748254
VERSION     WP_284748254.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..385
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41434
     Region          1..385
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msrhiergal pgaitlvsrh gevhvdvlgt mdlggdrpmr rdaifriasm tkpvvavaal
       61 ilveecrlrl ddpvdpllpe lanrrvltal daqltdtvpa rrpitlrdll tfrngfgtan
      121 gaseeypiaa aaaesglagg ppgpakrpap dewlrrlgdl plmaqpgekw lyntgsdilg
      181 iliaratgqp leeflrerif eplgmrgtgf svpdadigrl ptgyladpga sdispfdpal
      241 ggqwsrrpaf qsgsagllst vddyfafatm llslgrhgqe rilsrptvlt mitdqltpaq
      301 kaasgffpgy fdnrgwgfgv svitgrdels gspgrfgwdg gfgtswwsdp aenltgillt
      361 qrgefpavsg lhrdfwtsvy qaldd
//
LOCUS       WP_284748294             474 aa            linear   BCT 25-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284748294
VERSION     WP_284748294.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 474)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..474
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=49433
     Region          1..473
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mlidgewtip saattpvfdp stgdvianvp dggaeavdta vaaarrsfde grwrglsgte
       61 rgavlwragd lmreraddla sleslnlglp vaqakamvle aagqfryyag wadkihgrti
      121 dlgpadrrvq gytlrepvgv aglitpwnap lsmaakklap alaagcscvl kpaeetplts
      181 lwlgqlllea gvpagvvnvv tgvgeragaa ltehpdvdtv sftgstevgr livqaatgnm
      241 kklslelggk spvvvfgdad laaaipgaas avfwnsgqvc aagtrlfvhe svfdevvrgv
      301 aeigrsmrlg agsdpaadlg plisqkqler vsgyvehgvk dgarvvsggt rvgdrgyffe
      361 ptvlvdvdqs mtvmreeifg pvlgvmpfsd vdeavaland ssyglassvw trdgalahsv
      421 arrlragrvg invhraggay mpaggyrqsg wgresgpeal enyletksvv sqll
//
LOCUS       WP_284748613             292 aa            linear   BCT 25-DEC-2024
DEFINITION  S1 family peptidase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284748613
VERSION     WP_284748613.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Perona,J.J. and Craik,C.S.
  TITLE     Evolutionary divergence of substrate specificity within the
            chymotrypsin-like serine protease fold
  JOURNAL   J Biol Chem 272 (48), 29987-29990 (1997)
   PUBMED   9374470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475742
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..292
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=30018
     Region          92..292
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mrtipdrrrr fraravavav lvgagiafan aaigapagpa laaalgghsl pdttalgrdp
       61 apapptstkp apnpilpfna kltsddipve gggvrdgacs gslvapqwvv taghcfhdik
      121 dariggrppy tmtvtigrlk dsdpgghtav vvdvrqspvn dlavaklsap vdditpvela
      181 tkrpsvgeel qfagwgshsa tvlgpsdhlk rgrfrvsgia sstlealpig trtvdngpcp
      241 edsggpffvs ddndrtarli aivntgppcp qpgaetiarv dvvanwireq tg
//
LOCUS       WP_284748655             323 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284748655
VERSION     WP_284748655.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..323
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31800
     Region          6..264
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mtsegrrrga almlgsglsn qvgasvaala fpqlgpagvv avrqwvaaav llatarprlr
       61 aftaaqwrpv lalalvfgtm nlslysavdr iglglavtle flgplavala gsrrrgdllg
      121 alvaaaavvv lvrprpstdy lgiglallaa acwaayilln ravgaripgv agsaaaagas
      181 glayvpvgvw amiahrpglg avlaavtagv lssavpmlad lltlrqvpas vfgtvmsvnp
      241 vlaalvgwvv lgqsldalsw aaigvivavn vlvvvrppat pvpsspsaag paapptspgs
      301 peppgaaaas ssgsscpprr saa
//
LOCUS       WP_284748697             176 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284748697
VERSION     WP_284748697.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..176
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19114
     Region          7..101
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 malpstyads ncslarslei vgerwtlmiv rdaffgvrrf gdfaaqlgip ravltsrlks
       61 lvqedvlvra esggvveyrl tekgialwpi vralmswgde yyspggekrt trhdedggrl
      121 dpdgrctecg alvpvpeiri epgpgfdprp gapdpvsaai ntprrllepl partav
//
LOCUS       WP_284748826             739 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284748826
VERSION     WP_284748826.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..739
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=79343
     Region          8..739
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          613..638
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(614..615,618..619,621,645,654..655,658..659,
                     661..662,691,694..695,698..699,702)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          643..679
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          690..718
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdsfgttlrr lrraaeltqe alaeksglsg qaigalergd rryphrdtld rladalglag
       61 ddraefaaaa arpgsparad adavprelpg giavftgrea eldrilgllg eprqggvvai
      121 agmagagkta laleaghrla rrfpdgslhl dlrghaadpp dpldlldrli relggepptp
      181 lsldsasarf rtllapkrvl llldnardaa hvapllpgag gsaaivtsrv altdlpqahq
      241 vlldvlpead alrllaaeig aervaaepta arnvarlcgy lplalhlvga rlatrprwpv
      301 ahlahrldde rrrldetgvr tsfalavgal ddtaaraypl lslldvpels vpvasrllda
      361 peratealle rltdehlltt papgwyrlhd llrlfareha arlpageraa aitrvvelca
      421 amawqsmglv saashrhdwa agrwadagpa saeevfawld rhqahlvtvv rqaaatpgvp
      481 peaiaavglg lyeyhrarar wrdaiqvdev alelvdgvdp vaaatlrndl gvaeaelasg
      541 geaagfrrsh aflrrsladw eaigderqla gilnnlcfvy glgddvdaai gfgerslaln
      601 rslglryvet lnlvnlavly grqgdrarel ayateavsvg eesgdvrgta ygrmrigivh
      661 relgrfdvav eelsrsadlw reagvrlyea mtlaelgrah lgradrdrar evltdalelm
      721 reyggeeraa evraeldrl
//
LOCUS       WP_284748872             782 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284748872
VERSION     WP_284748872.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 782)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 782)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 782)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 782)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..782
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=86159
     Region          50..780
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 msqeldaavp akegapqngq aaaqppkpng aapnpsatrr vrarlarrit aqraapvkqv
       61 leplavihre lhpnadlgll qraydvaeel hrnqrrksgd pyithplava tilaelgmdt
      121 ttlvaallhd tvedtgyave slkadfgekv aelvdgvtkl dkvklgtsae aetirkmvia
      181 makdprvlvi kladrlhnmr tmrflppekq arkaretlev laplahrlgm atvkweledl
      241 afailqpkky deivrlvadr apsrdiylrs vitdltsnlv ssritakveg rpkhyysihq
      301 kmivrgrdld dihdlvgvri lvedvrdcya amgvvhalwq pvpgrfkdyi aqprfgvyqs
      361 lhttvigpdg kplevqirty emhrtaeygi aahwryketk gthngnavdv demawmrqll
      421 dwqreaadpg dfleslryel asreifvftp kgdvitlpvd stpvdfayav htevghrcig
      481 arvngrlval erklengevv eiftskaena gpsrdwlqfa gspkarakir qwfakerrde
      541 aieggkeait keirkvglpi qrlvsaesmg avatelrhad isslyaavge ghtsakhvvq
      601 rlvaliggvd aaeeelaera tpstvtrrrg sndvgvvvkg asdvwaklar cctpvpgdei
      661 lgfvtrgggv svhrtdctna gdlqsqperl vevewapsas svflvaiqve aldrhrllsd
      721 vtkvladekv nilsasvtts rdrvavsrfs femgdpkhlg hvlkvvrgve gvydvyrvts
      781 as
//
LOCUS       WP_284748897             435 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284748897
VERSION     WP_284748897.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..435
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=45151
     Region          82..276
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 masrarelld rsrvlldrsr vaaaqyltap pkhpehpgya paagpaltql apvvvpaapa
       61 deavlaeica svalrdlnll dqllarleel eageedhhrl aelyqldhla trlrrnaenl
      121 rvlagqetad daaratsvvd vmraamssid hyaritigrv vnlgvvgfaa edlgrvlael
      181 fdnaanqssp sspvnvsahl teqgsvlvri eddgigipad rvdglnarla aggelddaaa
      241 rhmglavvsr laarhdvtvr ldrrsphgtv atvllptgiv telaenawsg trtvagsgdr
      301 vakppargea qggavtgepv kaaagepaaa gglprrrpgt fpqeepvtai prkptprprp
      361 veqtggttan glprrvpgsi rgaapepppt ppapaspagh drlladlgaf adgeraalae
      421 nnrssqdetp ggtas
//
LOCUS       WP_284748899             208 aa            linear   BCT 25-DEC-2024
DEFINITION  GTP-binding protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284748899
VERSION     WP_284748899.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Takai,Y., Sasaki,T. and Matozaki,T.
  TITLE     Small GTP-binding proteins
  JOURNAL   Physiol Rev 81 (1), 153-208 (2001)
   PUBMED   11152757
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006198
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..208
                     /product="GTP-binding protein"
                     /EC_number="3.6.5.-"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /calculated_mol_wt=21688
     Region          14..197
                     /region_name="Srp102"
                     /note="Signal recognition particle receptor subunit beta,
                     a GTPase [Intracellular trafficking, secretion, and
                     vesicular transport]; COG2229"
                     /db_xref="CDD:441830"
ORIGIN      
        1 mgssgsppeg elltisakiv vaggfgvgkt tfvgsvsevp pmsneawmte agqgvdeipp
       61 ggkstttvam dfgritlrpd lllylfgtpg qarfwflwdd lsrgalgavv lvdtsrides
      121 faainyfend selpfvvavn qfegmpvhdl devrdalald pavplvtcda rdrastiatl
      181 telvghtlsl avlsgpagre lagsapha
//
LOCUS       WP_284749095             310 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284749095
VERSION     WP_284749095.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 310)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 310)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18123688
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..310
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33292
     Region          6..222
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          <244..300
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mielvltaag aqrvrfaisp leevlgavqt llgvrrhpah lpwladapdv pelaavlsar
       61 hyiteflspp pdgpettvea qlravratpp hqvalelgmv dadlallpdd paaardllad
      121 qlatvwdall apewprlrel laadiahrtr qlgsgglasm laglhprvrl sdtsvlvdlp
      181 arerleidar glllipavfa wpnvgvvtvp pwqisllypa rgvvslwtss aappeplvev
      241 lgrtralllt tldrpaatte larrhdlapa tvsahltalr sagllaserr ghrvlyrrte
      301 lgdalltgrl
//
LOCUS       WP_284749130             192 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284749130
VERSION     WP_284749130.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..192
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20952
     Region          1..187
                     /region_name="HAD_sEH-N_like"
                     /note="N-terminal lipase phosphatase domain of human
                     soluble epoxide hydrolase, Escherichia coli YihX/HAD4
                     alpha-D-glucose 1-phosphate phosphatase, and related
                     domains, may be inactive; cd02603"
                     /db_xref="CDD:319790"
     Site            order(7..11,106..107,138,162..163,166..167)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            133
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mnwivfdygd vlskpsaarp amaaamgapl pefekaywdy ripydagstp leywqtvgka
       61 lgvsvgeels deltqidveg wshlepssqa lfetlseaga slallsnapv vfgewvraqe
      121 warhfrvtlf sgdvrcvkpd akifrlllde lgaepadclf fddrpsnvdg aravglkaqv
      181 wngadaaqaw ld
//
LOCUS       WP_284749212             289 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284749212
VERSION     WP_284749212.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..289
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32544
     Region          12..74
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(18,22,47)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(21,46)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(28..29,40,43,47..48)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          98..285
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtqdapsare rqlarelrql rstvgltgkd vaerlgwsts kvsrietgri gigqddlesl
       61 fglyevledk aeylrglaas araqgwwday annlssgyss liklesgsve lrcycalvph
      121 allqtpeysr hviqstlqvp apteidrrvd iarrrqavlr renppmrlsa videaafrrh
      181 irtpdgridn gvtraqfrhl adlaawpdis irvllfksgi ppvtsgsfsi lesmathrpd
      241 vvylenktrf ffidtenevh qyvqefells smalneddsr afleraasr
//
LOCUS       WP_284749271             491 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284749271
VERSION     WP_284749271.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..491
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=53977
     Region          1..444
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mtehvevliv gaglsgvgaa hhlrtafprk tyailearea iggtwdlfry pgvrsdsdmq
       61 tlgyrfrpwt sekaiadgps ilkyvrdtaa dagidrhirf ghkvvraaws tenaqwtvea
      121 thegepvrft akflylcsgy ydyagghtpe fpgiedfggt vvhpqhwped ldyagkkvvv
      181 igsgatavtl vpamtdraeh vtmlqrspty ilslpsedal anrlrgllga klaypiarwk
      241 nvavstliyq lsrrrpgvvk amirkaamkq lpagyavdth fkpryqpwdq rlclvpdgdl
      301 frsikrgdas vvtdriasft kdgirlesgd elpadvvvta tglrllafgg idlvvdgepv
      361 klpetmaykg mmlsgvpnfi ftigytnasw tlkadlvgey fvrllrhldr gghdqcvpvn
      421 ddpavterpl ldfdagyvlr sidafpkags rapwtlgmsy ahdvvklrhg riddgalrfs
      481 rrkagagrls a
//
LOCUS       WP_284749302             277 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284749302
VERSION     WP_284749302.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..277
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31784
     Region          8..249
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mphlfatsdl hvthegngpi lddvvpespg dwllvagdva eraeatigtl ktlrerfakv
       61 vwvpgnhelw ttkndecqlr gqaryeylve qcraidvltp edefpvwrqg grpltiaplf
      121 llydyswrtp eaegksleea lsqartagvv ctdeyflhpd pypsrqawca drlkisterl
      181 daipedhgti lmshwplhrh ptaplywpef alwcgttkte dwhiryraei avyghlhipr
      241 tteadgvrfe evslgyprew rkrargavpm rrilwps
//
LOCUS       WP_284749304             195 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284749304
VERSION     WP_284749304.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 195)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..195
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21063
     Region          6..82
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 maelpprkri edvellrals hplrsallhh ltsvgprtas ecaeavgsta sncswhlrql
       61 aqfglverte gddgrerpwr arqvgldlgd ldgdpvrraa qlgvvgasla neqeltqryl
      121 dsldgldpaw qaaaglisys lrvtpaeltr ltdaidalvr pyvgairtda ptgarpvhvg
      181 lrafpriehs gkaee
//
LOCUS       WP_284749444             385 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284749444
VERSION     WP_284749444.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..385
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=40943
     Region          1..381
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 msvviigagl gglslaqglr ragipcqvye rdpspefrkq gyrlhidgag dtalravlrp
       61 elhelfrata gralphtnvy derlrlltrl edegthlnvn rftlrqvllh gqevaygkrf
      121 thhatdedgv tahfadgtsa rgsllvgadg instvrqrhl phaevvdagl vhlygriplt
      181 pdtralfape mfavfsmmvg pdrtmagfap vdypepvada carlvpdlrp rdaepymtcs
      241 vgarwevvgh teadlaamtp gdlqkvalgl veswhplaga mvghwdvpat fpqpirtsvp
      301 igpwepsrvt lvgdaihams paggaganta lrdgaalasa lagaplleav aayesamvgy
      361 gfaavresae ngrrflgqnp lttga
//
LOCUS       WP_284749445             288 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284749445
VERSION     WP_284749445.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..288
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29412
     Region          45..156
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mrvtnggvkr tlavlaaalt fgavapavae aapssgwndw gcrpsaahpe pvvlvhglga
       61 ndtvnwffha pkiaaqgycv fsltygtgil gpgvgglasm rdsaaqlgrf vdrvrtttga
      121 akadivghse gstmpayylk ygggaakiah fvgfganyrg ttlggldkla kallttvpgl
      181 glilktacgs cteylapsaf lddlarggvh vagpaytsiv skydevvtpy tsgilnepga
      241 tdivlqdfca sdasghlsqa vdpnvtglil haldasytpk ctpftlpl
//
LOCUS       WP_284749480             454 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284749480
VERSION     WP_284749480.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..454
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48928
     Region          27..437
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 marqvsgheq pvgttrtles tpdgavvkrs vlpgglrvit ehvpasrsat vglwvgigsr
       61 depvavagaa hylehllfkg tkkrdatqia eeidavggef naftakehtc yyaqvldadl
      121 plavdlvtdv vfealctdrd mdmersvvle eismrdddpe dllhetfvsa ilgdhplgrp
      181 vlgteksiie mspaalrtfy krrytlprmv lavagnvdhg qvlrlvrkal kerlagtatp
      241 vapregrari ktlpklalht ddteqahvml glrslsrhde rrfalsvlna algggmssrl
      301 fqeirerrgl ayqvyssvas yadtghmavy agcqpeklgd vagvirevld kvgvdgltda
      361 evarakgqlr ggivlgledt ssrmsrigks elnyghylgv detiaridav tteevcalar
      421 tlfarpggvs aaavvgpyah addlpddlhe vias
//
LOCUS       WP_284749483             157 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Amycolatopsis].
ACCESSION   WP_284749483
VERSION     WP_284749483.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis
  ORGANISM  Amycolatopsis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Amycolatopsis"
                     /db_xref="taxon:1813"
     Protein         1..157
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17302
     Region          22..>59
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 medhkivqrn ialqrewyge plgdrvrrlv vafdvsqafl aevlgisapm lsqvmsgrra
       61 kignpvvlar mimlerkilv pevaagnrda mlaamedvrd srptvgrdni pvvnedqkvl
      121 aylrdlaede dlgeaakrld defpaiadll rragnga
//
LOCUS       WP_284749490             343 aa            linear   BCT 25-DEC-2024
DEFINITION  TRM11 family SAM-dependent methyltransferase [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284749490
VERSION     WP_284749490.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Kozbial,P.Z. and Mushegian,A.R.
  TITLE     Natural history of S-adenosylmethionine-binding proteins
  JOURNAL   BMC Struct Biol 5, 19 (2005)
   PUBMED   16225687
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437146
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..343
                     /product="TRM11 family SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=37173
     Region          106..338
                     /region_name="Trm11"
                     /note="tRNA G10 N-methylase Trm11 [Translation, ribosomal
                     structure and biogenesis]; COG1041"
                     /db_xref="CDD:440663"
ORIGIN      
        1 mpeyvilvhp sanrvyaass pallraelav fgaalsaels gieevelggv gyvrftssap
       61 lggsdlalls nlsslyalfe lgdgvlrpvt vtplakadsd lltiqkyagk tnesftklll
      121 nvtllatadp fsgkpkylld plcgrgttln qaimyglhat gldvdakdfe ayeafiktwl
      181 rnkrvkhtad sgqlrrnkvr lgrrldieya ltkddykagd trkltyfnad tlttdevlra
      241 nscdvivtda pygvqhgshr eaglqrsprd llaaavpvwt rvlrpggalg iswnttvlpr
      301 eelvavlrka gldvredgpw aefthrvdqa ilrdlvvavk pas
//
LOCUS       WP_284749561             514 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA synthetase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284749561
VERSION     WP_284749561.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..514
                     /product="acyl-CoA synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016405 - CoA-ligase activity [Evidence
                     IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0032787 - monocarboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=54993
     Region          17..499
                     /region_name="FACL_FadD13-like"
                     /note="fatty acyl-CoA synthetase, including FadD13;
                     cd17631"
                     /db_xref="CDD:341286"
     Site            order(167,170..175,177..178)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341286"
     Site            order(170,283..284,306..311,393,405,408,419,496)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341286"
     Site            order(170,210..211,256,258..259,262,283..284,306..311,393,
                     405,408,416..419,477)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341286"
     Site            order(210,258..259,262,283,416..418,471,477)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341286"
ORIGIN      
        1 mpedvrprvr lfgellahwa reragdtali fgdrswtwae fddrvrrlsg alagagitrg
       61 drvafvdknh paclettfaa agvgaanavv nwrlsgdela yvlkdagakv vfvgaelvpa
      121 ldavrdrlpa lervvvvggd hdeyepflas gephtgsgld eddgvlimyt sgttgfpkga
      181 vlthhsviah glaagtafpi gpgdvnlvam plfhvggscy avsgflygep syltrepdaa
      241 slfaalqagi thaflvpavv agiaqageaa lkafsrlkyl cygaspmplp llrtalaawp
      301 dvrfaqvygm telsgavtal dpeahrdash perlasagta lsgvdirivd pvtaedaavg
      361 evwirteqrm agylgkpeat aetivdgwvr tgdvgrlddg gflfledrvk dmiitggenv
      421 yspevervva efpgvaevav igvpddrwge qvkavvagdq ldadklmefc rerlahykcp
      481 rsvdvvealp rnatgkilkr slrepywrdr drnv
//
LOCUS       WP_284749630             320 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284749630
VERSION     WP_284749630.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..320
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=34344
     Region          <109..188
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
ORIGIN      
        1 megsggrddq rgarvgladv rrledvvael rgldyryggg acrravesrl paavallegv
       61 tktvvlarlc tavadlynla gwtnfdqdrp aaalaafrra lelaiqaend dlqaniryri
      121 grlhlhygav daaleefarg reaalqahsk laqailsanq awahakkadv aealtylrra
      181 reefaeaegr epspwdsffg atdmaamvgt vhgelaqvvd irhgrdgipa ltdaiagygt
      241 gmtrsrsltl iwlatvhald gdldvatavg eeaielagal rsprtrqrlr slsaaarrfs
      301 gnadareivd rlgdlghsgr
//
LOCUS       WP_284749649             977 aa            linear   BCT 25-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284749649
VERSION     WP_284749649.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 977)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   3  (residues 1 to 977)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 977)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..977
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=105059
     Region          13..256
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          130..960
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          724..752
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          764..792
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(765,768..769,772..773,775,805,808..809,812..813,
                     815..816,845,848..849,852..853,856)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          803..833
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          844..872
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          924..952
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mgeligqvea tsltirvlgp levtasgqvi plggpkprll laalalqpnv vvsadvlvev
       61 lwpesaprsa aanirtyvhs lrrrfaeldp glgdrissra sgylltaspe eldhlaftal
      121 ageaqealdr adaesalkll draealwrge vleglphdhs wgasvarlae lrlsvqeqrl
      181 raridlgrcg eavaelrglv tehplreelw aqlivalraa grtadaveay esaervlree
      241 lgaepgsqlr elratlvses vpagrpvdfv pvcqlpldlp dftgrddvlr evagllrera
      301 dsgtpavvvl sgapgvgksa vairiahavr ddfpdgqlhv dlagtssspr apmgvlaell
      361 ralgipdagl prepaersal lrsrlagrrm civlddagsa aqvrpllpga gacavlvtsr
      421 lrlpglpgat pvdvdllpea egarllqgiv gaervaaepe saaailrqcg hlplairvag
      481 akltnrpgwt lrlladrlrd ehrrldelrv gdlavrasvt lsydllpmsa atafrglgll
      541 gpvqfpawav aavlgrrdae dvldvlvdgh lvelvgsdsa gqpryrlhdl lrvyavelae
      601 qsdaaktraa lrrvlegyla laleaarrmp lhffgmycde elprpavpad vlpddpaawf
      661 aaerhtsvaa vslaaeqgfd dlawqlasal tpyfdlrghq ddwhsthtia laaarrtgsl
      721 raeaivqrnl gqyllyqdey agsrvafees kalfervgda qgvaialtgl atilridged
      781 glaldhchea lklfaeegdp ngeavarlga gavwmsrgcy aaakrwftda lelsaaigdr
      841 hreahaykrl gllfqhqgnl aaarehvdqa iaiftelgdd hcvgyanqnl gelclhsgdf
      901 ahaqlllvns lsvhrrngdr rseaevsqll gelhralsqp ersrdysera laiwrelssr
      961 ppepvtsvee pphiasa
//
LOCUS       WP_284749651             523 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284749651
VERSION     WP_284749651.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..523
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56867
     Region          4..522
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mvqvnrrkvl lgglaavtat aasaalpswa narttaaapt ihdpfqlgva sgdplpdsvv
       61 lwtrlapapl nadgyggmpd atyavdweia ndeafssivq tgsvnavraa ahsvhiepvg
      121 lqpareyfyr fkssgyispv grtrtapaag aavnqlkycf tscqhweegy yhaykgvvad
      181 dpdlvlflgd yiyekksgrv aaernprsla vpddtttlal yrarhgqhkt dadlqaahai
      241 apwvvvfddh evmnnwngtt spasaarkaa gfqafyehtp irstakpnga siqlyrqlmw
      301 gnlarfhmld trqyrnaqva dpsgsagpac tdmrntsrsi lgsteeawll kqfeshpatw
      361 dflgqqvffa trdgdgdkat cespdswqgy easrdriakg wvdrkvanpv vltgdvhrhw
      421 aadlrldyfd hsdpligsel vttsvtsnsd tatppsaawl annphikyck gergyvrvtt
      481 tpgqmradfm ttsdtsvydp asvvikndvs yvvqagrpgl qkv
//
LOCUS       WP_284749821             396 aa            linear   BCT 25-DEC-2024
DEFINITION  Kelch repeat-containing protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284749821
VERSION     WP_284749821.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Shi,X., Xiang,S., Cao,J., Zhu,H., Yang,B., He,Q. and Ying,M.
  TITLE     Kelch-like proteins: Physiological functions and relationships with
            diseases
  JOURNAL   Pharmacol Res 148, 104404 (2019)
   PUBMED   31442578
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Gupta,V.A. and Beggs,A.H.
  TITLE     Kelch proteins: emerging roles in skeletal muscle development and
            diseases
  JOURNAL   Skelet Muscle 4, 11 (2014)
   PUBMED   24959344
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Adams,J., Kelso,R. and Cooley,L.
  TITLE     The kelch repeat superfamily of proteins: propellers of cell
            function
  JOURNAL   Trends Cell Biol 10 (1), 17-24 (2000)
   PUBMED   10603472
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..396
                     /product="Kelch repeat-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=41244
     Region          15..320
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          35..75
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          79..129
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          132..184
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          186..243
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          246..300
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          302..350
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
ORIGIN      
        1 mtaqtelptt tttgwaptgd lpwprqwdhp yegpvllhdg rvlaagggnn rgsqtfadaa
       61 lydlatgqwt ptgpmltsrr ihtlttladg rvlavggghg hpsvkpfila saeiydpatg
      121 twtetgslhq srclhsatll pdgrvlvagg atdqpplpaq ivtttaeiyd patgqwtpaa
      181 pmlhprasfs avllpdghvm avsglvetgg dlagltfcet ydptagtwtp tdpigtpvpl
      241 etgtprvnaq avalddgavl ltgghqggpv nwsyspfsls dterydpatr rwaptasmkv
      301 ardefrmikl dsgkviaigg leyggydtgy qnsetydpat rtwappigls agrakfgavk
      361 ladgrvliag gatvlgaagp dgentvlits tdlftp
//
LOCUS       WP_284749840             255 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284749840
VERSION     WP_284749840.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 255)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 255)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..255
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26704
     Region          1..243
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtttavitga tagigaqfar tlaaekydlv lvardvtrle ayaaelrekh gvgvevlpad
       61 lsevdgrtav eerlaagpvd llvnnagfgl ngdfwtippd alqrqldvnv tavlrltrav
      121 lpgmierghg eiiqvssvag ffsgrgstyt asknwvtsft egiaaslpkg vrmmalcpgf
      181 tatefhqrag igkpgpkiaw lgveqvvgea ladlrrgkvi svpslqykav vaiggllpra
      241 vlrrisggfg gkgrt
//
LOCUS       WP_284749886             248 aa            linear   BCT 25-DEC-2024
DEFINITION  SRPBCC family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284749886
VERSION     WP_284749886.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..248
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=26761
     Region          10..136
                     /region_name="SRPBCC_CalC_Aha1-like"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of Micromonospora echinospora CalC, human Aha1, and
                     related proteins; cd07814"
                     /db_xref="CDD:176856"
     Site            order(11,20..22,24..25,30,40,46,48,50,52,61,64,70,72,
                     82..83,85,87,100,102,104,106,115..123,125..127,130)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mghefeaidt aevdatpeql weaiatgpgi dswfmgrnev eggtggvvrg afggyrpeyg
       61 ireweplekl vygnepgpdg rkiayeflie greggssvir cvtsgflpgd dwedefeamt
      121 aggamffrtl veyvthfagr tavpvtafgp pvgdwpaawa rlgtalglsa rpaegdrvrv
      181 elpgrapqeg vvyavneqna girtadamvr flrgfhgpmv aahhvftpga daeaeekaws
      241 ewldrvfg
//
LOCUS       WP_284749920             146 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284749920
VERSION     WP_284749920.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..146
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16034
     Region          8..105
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mvrrgrecsv aealevvger wsllalreim lgerrfnqia entgasrdil aarlrklvda
       61 gvlekvqyea hpprheyypt eagralqpil lglmawgdky vhqgepptlw rhacgevlep
      121 atvcahcgep vnapgthair lgavhs
//
LOCUS       WP_284749887             199 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284749887
VERSION     WP_284749887.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 199)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 199)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..199
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21196
     Region          18..>87
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mfsvavieda saaevsldpv rarllaelae pasatmlaar vglprqkvny hlrtleahgl
       61 velveerrkg nvtermmrat assyvispaa laavqpdpaq spdrlsarwl lavagrlvrd
      121 vgllitgaak akqrvatfai dgevrfaspa draafaeelt taittlvgky hdetaekgrn
      181 hrvvvavhps vpeetedga
//
LOCUS       WP_284749948             259 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284749948
VERSION     WP_284749948.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..259
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27807
     Region          27..257
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mpesrqaspp pakpggvtpr gggwlphgfh lgthshpdgq lvyaaagala tttergtwva
       61 pasrvtwtpp gfdhshrfyg rtdarlvaip adecgslvay psvfavspll reallaltgr
      121 drrppeaekr lravvvdelg etpqqslhlp eprddrlrvv tdllradpgr attlaelgra
      181 agasertlsr lfhadlgmsf hrwrtilrih halvhltdgq svtdtavacg wsnpstfiea
      241 fsavvgqtpg ryqaglhgd
//
LOCUS       WP_284750040             447 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284750040
VERSION     WP_284750040.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..447
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46708
     Region          <154..>447
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mrrailvata mlglsaapst atadplvmph vvvahntwwa eltvhraggt vvasypqigv
       61 vvaytakddf aakvrktpgi davgatrtak ipkeffaprk dvrytgpnsp nsgqvppegt
      121 awdvpalhlp eahqvtegsr rtvvgvldvg vddthpdlkp afdakdsvsc lsgwadrspg
      181 awrptldghg thvagtiaaa rngsgvvgva pgvriaavkl aelddtetae smvcgfvwaa
      241 ehgfaitnns yrsipwrync ddqpdqaaak lavgravaya qrrnvlvvas agnagidldt
      301 rsvdrespad stpveraidp tctrlphelp gvvgtgalde kllkasfsny sasrisvaap
      361 garvwstwpn geyrsasgts maaphasgva aliasehprw saerikraly dtatplpcpd
      421 tvckstkqgt tyyghgmvda gsavgag
//
LOCUS       WP_284750158             262 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284750158
VERSION     WP_284750158.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..262
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26741
     Region          7..254
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mdpftertpr vvaarkltrr aerdktgrfl aeganavgaa laggpvhelf vtehaaaqha
       61 dlvdaaraag vavspitdra adglsetvtp qgivavcall drsleeavtp garlvvvlvd
      121 vadpgnagtv irvadaagad avvlagdtvd phngkcvraa agslfhlpia rvrdvpaala
      181 acsaaglrtf aahgyadael drvdltepta wvfgneahgl padvldrtdl avriplygka
      241 eslnlataaa vcvytsamaa hr
//
LOCUS       WP_284750167             531 aa            linear   BCT 25-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284750167
VERSION     WP_284750167.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..531
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=56468
     Region          1..530
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mdvvvknvlv adgtgdamtr hdvgitgeki asvgeagsla grrnidghgl vlapgfidmh
       61 shsdlqllan pdhaakitqg vttevlgqdg lsyapvddav lealrqqlag wnddpagfdw
      121 nwrsvgeyld rldqgiavna aylvpqgtvr mlavgfddrp atdaeltrmk elvatglaeg
      181 amgmssglty tpgmyaetse lvelckvvae gggfysphhr sygkgaleaf aemidvsrrs
      241 gcplhlahat mnfsvnkgka pdllklldda lddgcdvsld typylpgaty lsallpswat
      301 eggleptlar lsdvdereri raaieesgsd gahgvpidwd aieingvrnd hnahlvghsv
      361 agsaraagle patlyfdtll derlgtsclm hvgheenvqa imrhrthtgg sdgllvgarp
      421 hprawgtfpr ylaryvrelg vldlaecvah ltgraarrlr ltdrglvrag yaadlvlfdp
      481 davadtatfd dprqpaagit hvfvngvaal ddgrptgala grslrnpgra r
//
LOCUS       WP_284750256             137 aa            linear   BCT 25-DEC-2024
DEFINITION  SRPBCC family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284750256
VERSION     WP_284750256.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..137
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=15349
     Region          17..121
                     /region_name="SRPBCC_CalC_Aha1-like"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of Micromonospora echinospora CalC, human Aha1, and
                     related proteins; cd07814"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mtssvgktad vgwnigvsrt lpyraekvwe flvsrdgvai wlgpgvelpr etgaeyetan
       61 gtvgeirgfv egdrvrltwr psdwdhdstv qvrlsgsgak ttlrfhqewl sdaeereeqr
      121 aywqdvterv vaalaer
//
LOCUS       WP_284750257             400 aa            linear   BCT 25-DEC-2024
DEFINITION  cytochrome P450 family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284750257
VERSION     WP_284750257.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 400)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..400
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=43305
     Region          21..399
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(51,58,89..90,97,101,108,233..234,237,241..242,245,
                     278,283..284,287..288,290,313,340..342,345..346,348..350,
                     354)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(58,83,85,88,90..91,173..174,182,232..233,236..237,
                     241,284,287..289,389)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mttievaedf aqdahlfagl lradgparrv rmprgldcyi itdfaqaral ladsrlhkdn
       61 rrayelfesk lpagatnqgg fgealgrhml ntdppdhsrl rklvnkaftg rtvarlrpri
      121 eeitaellda lagqeradll psfaaplpit vicellgvap edrtefsaws ktllssstpe
      181 daqhaaqsml tyltalvtqk raepaedlls dlvhasddgd slsqdelism aflllvaghe
      241 ttvnliansv lallrepeql allradpalm pgaveeflrf dgpihlatlr fteeaveagd
      301 vtipagefvl isllganrde erfpeadrld vtraagghla fghgihycvg aplarleaei
      361 alagllarfp glaldakpde lvyrssslvh glealpvrlr
//
LOCUS       WP_284750315             126 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284750315
VERSION     WP_284750315.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..126
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13893
     Region          5..110
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mgaahdllat rcpsrdvlnr vgarwvptvl naldagsmrf telkkvvegv takaltetlr
       61 aleydgiidr vetpsvtppr vdysltplgr slfealnpvr ewaerhvgdi aearrryeln
      121 sqaeah
//
LOCUS       WP_284750323             380 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284750323
VERSION     WP_284750323.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..380
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39096
     Region          2..376
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mqsveyavig ggvagtataw nlarrgaetv vleadelasg asggpgrrgv raggrdlrel
       61 plarramelw peldsllgap tgyrrnglls vydvevagvs gwqslparaq aqqaagipcs
      121 ivdreqldam qpglaadirv alftpedgtg dhpattrafa kaaaelgarv lehtavtglv
      181 phpdgsvtlr laegdelrvt rgvvlaanra vprlladsfg lslpvwekat qvtfvapppg
      241 falnhqvght rrslsvkltd egrvmlsggr pggwdaasgv gtpdpavlra tladvaatip
      301 alagaevlav dnsradtsti dlipvvdkvp ghgavfagtg wsghgfalap avgealaswa
      361 ldgerpealr pftferlgvg
//
LOCUS       WP_284750320             202 aa            linear   BCT 25-DEC-2024
DEFINITION  GTP-binding protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284750320
VERSION     WP_284750320.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Takai,Y., Sasaki,T. and Matozaki,T.
  TITLE     Small GTP-binding proteins
  JOURNAL   Physiol Rev 81 (1), 153-208 (2001)
   PUBMED   11152757
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006198
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..202
                     /product="GTP-binding protein"
                     /EC_number="3.6.5.-"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /calculated_mol_wt=21891
     Region          22..201
                     /region_name="Srp102"
                     /note="Signal recognition particle receptor subunit beta,
                     a GTPase [Intracellular trafficking, secretion, and
                     vesicular transport]; COG2229"
                     /db_xref="CDD:441830"
ORIGIN      
        1 mdsaisetde rlpladtasd glkivivggf gvgkttmvrs vseirplste etmtqagvgv
       61 dstrgvhakt tttvafdfgr islddqlily lfgapgqerf wflwdslfag tlgavvlvda
      121 rrladswyai drlehhgtpf ivarnnfgpp khslddvraa ldlsdevplv dcdardrdsa
      181 kqvlislvdh lytlskvreg as
//
LOCUS       WP_284750334             383 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284750334
VERSION     WP_284750334.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..383
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=40159
     Region          21..371
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mkngdegmrv vvvgaglggl tlahglrreg idvvvyerda asgrpqgvsl hvdergasal
       61 raclppahva mveataggpr ertltlsdvd gelavtgaqp adgtagrarp grqvhrpllk
      121 evlltglddv vrfgaeftrf eqradgtvgv wfadgradta dvlvgadgig savrrrylpe
      181 arvvdtgrrm imgatplrav lgtglpglig dspaaahvrg tmlalgvlrf teppvlarqr
      241 wlpalrhsav aeledyvmwa lpvtrerlgs asvwrragel aadlppalrl vvaeawpevt
      301 valrigtipp ipawpaspvt vlgdavhlap gfggnlamrd ahhlgealag ayrgrvglld
      361 aigayedtmr rgsfpavvvk agk
//
LOCUS       WP_284750340             455 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284750340
VERSION     WP_284750340.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..455
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=47676
     Region          161..350
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mgvlvtavvv gaiwtgvsls isggqgilva vagavtgiva cvavffalrr gdqvanatar
       61 teaaldearr aresvqfggh elarlldetv pdavrrlrgg apadsvlaev prpaddqhqr
      121 vlrllvdeia vgerrraaat aacanaagrl qalatstlgd lremenrssd amlgdllkvd
      181 hstaqagrla dsiavltgar sgrrwtkpir mesilrgalg rigayqrvrv hsasgvavvg
      241 yaaedvmhal aelmdnatkf sapseevhvy vedlhngavi tiedgglgmk aqalvraera
      301 vsldrpldlt smsgtrlgla vvgslarkhq lhvffrpssr ggigvvmrip tqlitqprpe
      361 alpeadepaa tvvwpgpadt shevagdlse pselpkrsrg qtltaasrrp psptpspara
      421 erdsgsrfga fqqrrsggat psrhaasppd tgeda
//
LOCUS       WP_284750530             290 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284750530
VERSION     WP_284750530.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..290
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30456
     Region          44..152
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 msvhthddid wadrlaqlrm adsldagala pvarrlvgrl parptvldvg cgaggmsvlf
       61 arelsradgg tvvlldatpe llaearravt gaaggdvevv gvhgdladpr laervpaadl
      121 vwasgvvhhv gdqqaalcal arllrprgvl aigegglemr clpwdvgvgr pglehrllaa
      181 raewfagmra glpgsvalpy gwpralreag ledvesfgal idhpmpgsdl lreyvvqrvg
      241 wlaesagdrl daddraavaa lidpdgpgfl arrddlflfg akaihcgrlp
//
LOCUS       WP_284750652             676 aa            linear   BCT 25-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284750652
VERSION     WP_284750652.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 676)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   3  (residues 1 to 676)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 676)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..676
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=72434
     Region          2..239
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          105..>615
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mpvrfrllgd ieahvdgrpv dlghvrqrgv laalladvnh pvsvdqladr vwagrpphra
       61 rrslasylsr lrrvlagaed vviaygpggy vvrvapeaid lhrfrtlvae arenqelarf
      121 dealrlwhgd afagvdtpwt eamrrtlaae reaieldrtd ltlrlgkhna vlaeissrva
      181 anplneraag qlvlalyrgg rqadaldhye rtrrrlaeel gadpgpalre lhhkiltaap
      241 eldppsevav prqlpaapgw lvgrdaelav ltrvvaaggt vpvcaiggpa gvgktalalr
      301 wahdhlarfp dgqvhvdlrg fdpsgepmtp kaavrrllga lgadpatlpp dedelvahyr
      361 slvagkrllv vldnardaaq vepllpgset cavlvtsrhr ltglgvrgar lvdldplsea
      421 dardllarhi gpepvadead avadlvrwca glplavgiva aratarpgfp ldvlvkecrd
      481 asarldalda gdltsnlrav fswsytaldp aeaevfrllg vapgpdialp aaaaltgldg
      541 rqvrsvlrsl vganllqepv pgryrmhdli rlyaaelage eargaaldrl telqlhtars
      601 aahllrpehp vielataagc appefehraa alawfeaeha gllalrraaa ahgrhraagq
      661 lawflsayhi srglta
//
LOCUS       WP_284750630             316 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Amycolatopsis
            ponsaeliensis].
ACCESSION   WP_284750630
VERSION     WP_284750630.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..316
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=33083
     Region          12..306
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 masahgpdrt svvvtggggf igravvralr drgvpvtvvd rvpfpdddgd gvrvvtgdlr
       61 eaavreeavt petagivhla altsvlksve lpedtfadnv lvtqellela rrrevpkfll
      121 astnavignv gtatitpdlp lrpltpygat kaacemllsg yagaygmttc alrftnvygp
      181 gmshkdsfvp rmmraaltgt gvkiygdgrq rrdlvhvddv vralllalds ghtgraivga
      241 grsvsvlemv eavrevtgae lpvehveapa gempavvvdv sasaetigye psvsltdgla
      301 tawkyfsgld rpnatp
//
LOCUS       WP_284750689             180 aa            linear   BCT 25-DEC-2024
DEFINITION  HIT family protein [Amycolatopsis ponsaeliensis].
ACCESSION   WP_284750689
VERSION     WP_284750689.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ponsaeliensis
  ORGANISM  Amycolatopsis ponsaeliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Amycolatopsis ponsaeliensis"
                     /db_xref="taxon:2992142"
     Protein         1..180
                     /product="HIT family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19637
     Region          45..171
                     /region_name="FHIT"
                     /note="FHIT (fragile histidine family): FHIT proteins,
                     related to the HIT family carry a motif HxHxH/Qxx (x, is a
                     hydrophobic amino acid), On the basis of sequence,
                     substrate specificity, structure, evolution and mechanism,
                     HIT proteins are classified into...; cd01275"
                     /db_xref="CDD:238606"
     Site            order(70,72..73,80,82,128,136,138,142,144)
                     /site_type="active"
                     /note="nucleotide binding site/active site [active]"
                     /db_xref="CDD:238606"
     Site            order(140,142,144..146)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238606"
     Site            142
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238606"
ORIGIN      
        1 msdgpelveq qgvgvqdafq rlwtphrmay ikgqdkpdgd edtgcpfcri pslddktgli
       61 vargeavyav lnlypynpgh lmvvpyrhva dyteltveet revaeftqha mkviravsga
      121 hgfniglnqg viagagiaah lhqhlvprwg gdanfmpiig qtkvlpqllg etrdlladaw
//
LOCUS       WP_284750902             240 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [Arthrobacter].
ACCESSION   WP_284750902
VERSION     WP_284750902.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter
  ORGANISM  Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Arthrobacter"
                     /db_xref="taxon:1663"
     Protein         1..240
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26965
     Region          27..121
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mtiaehftre hdelanatgr msadywsisq glrlvgdrws llivrellgg emgfndmsra
       61 lpdisrtlls qrlkrlvqle lvirndeagp rgsrryrltp sgyglrqtle slglwasqwq
      121 apfendlrag lgnllehmgr slvtdslprk sivlafefdn vrgapfqgli crennkttss
      181 igrseripdl qihvaprvly dlwwglrrce darklgsigf vgpeewaaaf sgwfapraas
//
LOCUS       WP_284751019             130 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284751019
VERSION     WP_284751019.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..130
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14378
     Region          9..112
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mdtddlpanv ldpdcpsrvi fqrigdkwas lvvqvladgp irfselrkmv hvvtpkvltq
       61 tlrtlerdgl itrtvhaqvp prvdyeltel gasllepltl lrlwaedhvp silkardayd
      121 daqdeavigg
//
LOCUS       WP_284751529             334 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. efr-133-R2A-120].
ACCESSION   WP_284751529
VERSION     WP_284751529.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..334
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37241
     Region          4..317
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtrpitlftg qwadlpfeev arlagewgfd gleiacwgdh ldpyrasvdd gyvqerldil
       61 eknglkvfai anhltgqavc ddpiderhrd ilsdeiwgng eaegvrqraa eamkataraa
      121 arlgvktvtg ftgssiwkav amfppasesm iergyqdfad rwnpildvfd evgvrfalev
      181 hpseiaydyw ttkrtldavg hresfglnfd pshfiwqdld pvmflqdfap kifhvhvkes
      241 irqlngrngr lgshlpwadp rrgwdfvtag hgdvkwepif rtlnaigyeg ptsvewedag
      301 mdrlvgapqs lamvrelaai appvaafdaa fssr
//
LOCUS       WP_284751682             420 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase family protein [unclassified
            Arthrobacter].
ACCESSION   WP_284751682
VERSION     WP_284751682.1
KEYWORDS    RefSeq.
SOURCE      unclassified Arthrobacter
  ORGANISM  unclassified Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="unclassified Arthrobacter"
                     /db_xref="taxon:235627"
     Protein         1..420
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=44819
     Region          13..400
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mkkiveplps wgrrlagieg lraaaalsvl ayhvglmasd evhlgpvgqv flpllgqglp
       61 lffvlsgfll frpfvtsimr gkelpsirry aanrllriyp aylvilgata lvmgsvyikg
      121 sthgfgpdni grltepikfl anallvhmfi pqfvmsglpv awsltaeitf yvavplmall
      181 sarlvrlgts kavalaiapv alvviglgvt swghaaadhl dytqrvdfaf gqtgtavllr
      241 sflgqadlfg ygiaaalvvv aldergvqrv aawvkvvlla aavaaiwagm sgtmpylsnm
      301 agvasalvll avvlpssrdg ganrlallfe wrpirftgti sysiylwhlp vifwlmthkl
      361 tvggtvlalp fntilvlgiv lplsaltyyl verpamlrkk pspqgesssq kvplatsaap
//
LOCUS       WP_284751690             281 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. efr-133-R2A-120].
ACCESSION   WP_284751690
VERSION     WP_284751690.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..281
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29623
     Region          9..246
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtetnavwsl sgfgdevdpd pvvqaavlla lgashievrs awgtnvsele petverlkai
       61 ldekglkvsa vaspigkvdv sipvehelar lrqivsvakg ldtkyirifs fyraegqspe
      121 dirdsvmerm taltneaaas gvvllhenek giygdtperv ldimetvdsp alrvawdsan
      181 fvqvgvkpyt egyavlrpyl eyfqvkdavs gtgevvpage gdgeldatia alkadgfagf
      241 aslephlast helggfsgpv afgaaarafa alaakngval p
//
LOCUS       WP_284751851             413 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284751851
VERSION     WP_284751851.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..413
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41420
     Region          6..408
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 mgrnevvvtg lgaitplggd vrstwealla gesgirgkvl pghedgelag tvagtmaidp
       61 aerlspvqar rldrsqqaal vaaaeawada gapevdperl aaaigtgigg vqtllgeddv
      121 lelsgarrvs prtvpmlmpn aaaalisiay garagvytpv sacssgaeai algarlirag
      181 eadvviaggt eaaitpitva gfkqtqalsr htaepasasr pfaadrsgfv laegaavlvl
      241 esaehaaarg arvhavlaga giaadahhit apapdgsgqi samrkalaqa glspkqighi
      301 nahatgttvg daaesraire vfghatvtap kaalghlfga agaiealiav lsvkhdvvpp
      361 trnltptdvd pdinldvvtq rrnlpqhavl snsfgfggqn vslvvtavta sys
//
LOCUS       WP_284751828             257 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284751828
VERSION     WP_284751828.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 257)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 257)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..257
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26907
     Region          1..227
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 msklalitga ssgigwafae rlsaddydlv ivgrrqerld qfadshpqtr vrtvvadlst
       61 tagidavaei catepvtmlv nnagvahymp faelpadkat elvnvkvlap tmlsraaipg
      121 mqergegtii nvsgmiafgg paphsqmprr vvyggslayl vamsqtlsae lkgtgitvqv
      181 vcpgvvatef herqgmdlsm mprmsaadvv taslrglelg etvcapgved ggvldavfqa
      241 dlaafgaqsp elatryr
//
LOCUS       WP_284751858             446 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284751858
VERSION     WP_284751858.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..446
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45006
     Region          35..387
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(45..46,49..50,53,87,137..138,140..142,145,165,
                     168..169,172,253,256..257,260..262,265,292,296,345..346,
                     350,354,370,373..374,377..378,381)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mnhtpsaaap ertqdgvhhf pgasarfskr saaavlvcwl lvvfdgydli vygtvqssli
       61 tdtgwgltka tagtvgsmaf lgmmigaifa grmsdswgrr rtiiacaalf slftilcafs
      121 pnaavfgglr llagiglggl vpsanalvae lvpakwrsti atlmmsgvpi ggsiaalagi
      181 pliptfgwpv mflvaavall vvvplgmrfl petlpetlpg tpptakdakq aagfksllra
      241 pylgmsllfa istlvtlfaw yglgtwlpnl mqlagynlgs altfalalnl gavvgsvata
      301 wagtrfgpip taivaaavaa vglavlvagp pvglvyvmlv lagvgthgtq cliiaavash
      361 ypahlrgtal gwalgvgrig avaapqvggl llaaglgvns nflafagaaa vaaillgaig
      421 tkiktakint aniqskntts vgasnv
//
LOCUS       WP_284751979             174 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284751979
VERSION     WP_284751979.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..174
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18170
     Region          55..168
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mtasgdaard krlaeigtav faaapatvag llpwvltrwk vrrpvpggla aqcagvllig
       61 agaavitnsf arfalegvgt papfappknl vvsgfysfvr npiyvgigaa itgqglllgq
      121 pklfglaalg avpvvafvrl yeeptlarkf gaeyesyran vprwlprltp wrqg
//
LOCUS       WP_284752055             516 aa            linear   BCT 25-DEC-2024
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284752055
VERSION     WP_284752055.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..516
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=54805
     Region          64..516
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mnesgrrgpn nggnrdgggh gnrgprgesn rnaqgrernr gpqrgfsana psqrtrradp
       61 arlvafevlr avasedayan lvlpsrirhh hldkrdagfa telsygalrg qgmydavlak
      121 cvdrplaqld pavldalrlg ahqllamrvp ahaaldqtvg laravigagp sslinavlrk
      181 vtartlpewl dhllenetde triasvrhah pewivralrq slvmhgrpas einelleadn
      241 aapvvnlval pgignldeal engatpgelv idsalssggd lgrmssireg ttrvqdvgsq
      301 lvaravagvd lgqaakdgek wldlcagpgg kaallaalah qegatllane paehraklvs
      361 qaltavpada wsvrvgdgrd vgkeqpetfd rvlvdvpcsg lgalrrrpes rwrrtpkdla
      421 dlgplqrell nsaidavkpg gvvayvtcsp hpaettavvs dvlrkrddle qidagaalda
      481 islngnlgag heltaqlwph vhqtdamfla lirkkp
//
LOCUS       WP_284752108             200 aa            linear   BCT 25-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284752108
VERSION     WP_284752108.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21678
     Region          12..169
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpvapqplgr rernkqlkld ritaaasalf aehgveevtt qqiadkadig tgtlflyakt
       61 kgellllvqn ahyaealerg radaetipna ldavmaivrp ivecnrvqvd ngrtylremv
      121 fgdatephhs ealsivaqte eviaavlvrd dllsaddaat tarivsaimf lsmavnanpa
      181 lrtedivqdi stqirlllpr
//
LOCUS       WP_284752123             229 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284752123
VERSION     WP_284752123.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14302692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..229
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24776
     Region          22..93
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          122..203
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(137,139,146,149,153,188,190,202)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mknpvdvars ggegtgrapa idrqialmgr rvrvlrkdkg ltlvqlagat dlshsflsql
       61 erglarpsms sldrishalg isqielmlaa esrgassddh gsvhvvrade gvrgptrkge
      121 artlargnrg vmtlewrdss vepgrffvhd edeflfiisg svlvdlddrg cellhagdsi
      181 hypggtrhrw sspdgsvyra ivvkedrslt ggtgdvhfer adadldrks
//
LOCUS       WP_284752136             277 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284752136
VERSION     WP_284752136.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..277
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28647
     Region          5..251
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mtenfqgrva vvtgagrglg eavvgrlvga garvvvvdre gddaaavaer ygrqaisvqa
       61 dvsteagveh yisagldafh ridmyhlnvg ivgsparlvd lslddfrhvm dvnvistflg
      121 iraalrqfes qggggtvlat csiagthgsh diipyqaskg avlsllrgsa mygapmgvrv
      181 nglapgliat qqafdgvlid avqenllrrg gtvplrragr pgeiadaaaf llsdrssyit
      241 gqllyvdgga sqvcsvrgag gagmwdtapi ddyvrgr
//
LOCUS       WP_284752140             404 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284752140
VERSION     WP_284752140.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..404
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43214
     Region          1..389
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mktiviagss vaglsaarel rqggfggrll tvdrdpqvpy rrpevskgll sgalpagkva
       61 mgwadelrae risgglegld lerrtirgih adgrpfaeqy dglviatgtm arpspfaklg
      121 gvhslrtwad shnmrgdlae aqrvvivggg figlevasva rklgkevtvi epmqaplvhi
      181 lgqtfsaalq akhenegvrf vlgqtvrele ghesgsirrv hlsngdslda dvvlvaigsv
      241 pavdwlldss ldverglvcd ttcsvagted vvaagdialw hnplyerlmr vehwtnaveq
      301 gtyaakrllg thdaggfvsa pyfwseqygs riqsigsnlg hdqavvlddd perlfvaylk
      361 egrllsvagm aagasifqfr nlvlarapih dvrahfaslr qpas
//
LOCUS       WP_284752167             447 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284752167
VERSION     WP_284752167.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..447
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48169
     Region          <139..311
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mktlttgvke hfpfigtqkv ddgylarvle lmlattnean qaqrleassl gyvnllhiav
       61 tlagipdpsk spettsenap adssgaadga vgvnqslgdi nqpapadnae darrklemrs
      121 eeaedqldsf fpqlfhatvl ieepeahlhp qlqhgliryl rkvtvarpdl qvivsthase
      181 ivaackpeem vvvrreygrv vtrtlanipw keadrkkitr mtalhldasr sgalfadrvv
      241 lvegiteaal vrafgrawas ldgakfafid alsivpignk vgewpvrlla hpgwelasqv
      301 avlsdtdkrd dplpepspta wqsgfadstr fkvfwsrptl eptlvdgndl liekalaslg
      361 qsvigpltsk siddlfltss gkkakgefaf elaalvdeta stvqvpeqlv elfdwlwagh
      421 vavedggdgd gemtkesgae sgpggqi
//
LOCUS       WP_284752180             398 aa            linear   BCT 25-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284752180
VERSION     WP_284752180.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..398
                     /product="metal-dependent hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42264
     Region          15..>77
                     /region_name="COG3964"
                     /note="Predicted amidohydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443164"
     Region          56..379
                     /region_name="Met_dep_hydrolase_A"
                     /note="Metallo-dependent hydrolases, subgroup A is part of
                     the superfamily of metallo-dependent hydrolases, a large
                     group of proteins that show conservation in their
                     3-dimensional fold (TIM barrel) and in details of their
                     active site. The vast majority of the...; cd01299"
                     /db_xref="CDD:238624"
     Site            order(74,76,219,239,311)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mavrsdpgrs raativlrra hildvasgel spprtivsrd giiteisdst rtvadaveid
       61 vagqtvlpgl idahahvtqa sgdfneilsw spqyhaarta rvlhemllrg ftlvrdmgga
      121 dtglaravde rlvtgprlka ggpifaptgg hvltkvcdge velrralrae frdgadhakl
      181 tlsggvvskm rlealgfsda evlaavdear lahryiaahv ytaeavaral rlgvrtiehg
      241 nllddecirl flerdafyvp tlatywails gvtghgldaa kraavedife rgleslakas
      301 vagvrigygt dlhgeglplq leefrlrarv qeplevlrsa tivgaeivge agragvvgeg
      361 gyadlivvdg dplsdigvla dgrslrlalv dgdpvrpe
//
LOCUS       WP_284752294             334 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284752294
VERSION     WP_284752294.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..334
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=34098
     Region          32..334
                     /region_name="Tdh"
                     /note="Threonine dehydrogenase or related Zn-dependent
                     dehydrogenase [Amino acid transport and metabolism,
                     General function prediction only]; COG1063"
                     /db_xref="CDD:440683"
ORIGIN      
        1 msaptlarrv awtgaerlvv eprpaptppg pdeivirves vgvcgtdaai wrghnnrvri
       61 gttlghefgg tvvevgpnvt irtvgqqvav dpnrvcgecr ecatgsrglc rrrelmgldv
      121 dgglqsyvtv davntvavpg aadpralali epiavgvrac aranvspgar lvivgggaig
      181 masalqarsl gaksvtviep davrratitd hgviaiapge gaaerwdvai dtvgsgtsvs
      241 avmellepgs ticvaglakg galpptedlv rreltltgtf cytsedlsta aalvarhgla
      301 aipndivqgl ndapaaieaf aqgrlgrgkt liip
//
LOCUS       WP_284752313             385 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284752313
VERSION     WP_284752313.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..385
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=41329
     Region          34..348
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mkskdiknln iaiigagygg aaaakalsll ganvnvyeqa sqmrevgagi glrpatmdrf
       61 skwgifdaia kvsspsdyfe iltasgepil kdtwpefggq ahtylihrgd fieallgvlp
      121 kgmvhlghkl ekieemdgrs vlsftngntv eadlvvgadg iksvvreqlf sdkgpvfsge
      181 hayrvvisad dahglvvddn lrmyigkgtk vyllplrhrn qvsfditaln pdgtwapkvc
      241 keslletvsg fderivnitr gldmnavnvr avydiepvds whtdsvvlvg daahsmlhhq
      301 gqgansaied agaladaltq aatvkealal fqatrkpvtd elqrisrqgw sekevndvfp
      361 gqkptsqkpt sqkptsataa aeara
//
LOCUS       WP_284752356             126 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284752356
VERSION     WP_284752356.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..126
                     /product="YybH family protein"
                     /calculated_mol_wt=13701
     Region          1..124
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mtmtaadaei lrsvldpwia aidahdpegi aelftedavf qglhpytvgr qgvadyyasq
       61 plgltaeyri letrrpasdf vygylsvefg fadgrptlpv ligvaaqrsg ddwmlalyqv
      121 shrpgl
//
LOCUS       WP_284752523             893 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284752523
VERSION     WP_284752523.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 893)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 893)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 893)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 893)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11971133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..893
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=95466
     Region          <10..844
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          832..882
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mtevvstdal vgrfsvmaav vdclldvngp gvllfgdagi gktalinevv helgqrvrpf
       61 rvfagptlas vpfaalapll taltpsqine plsvlravva alnpagqphp apavliveda
      121 hhiddssvav laqlaaaeaa kvvflcrpyp appaevfsmw seglvdrfdl qplneqevnq
      181 lcaqaleapv vqgtsavlck ysggnpmfll eliehakslg qlvcrndawm lsgelrgtsv
      241 rlmdlvrnqi lmlgaaqret letvalaepv plnvvqqacd ssavdelqel hfieiasdpa
      301 rhvrlaqplv gevirqlvpt ahsmtirrri velmgakpqt mdgllrfvsw glesgtevpd
      361 sdileaaqla nrlfipsyve rvagaikdps lrlaaqveva rakwyrgdir gsvsslagvv
      421 drtndprtvr qasmlaaqla grqgvgpnai kqaayeweaa larlaesrqg idpgelergk
      481 lgsrllsleg lqaeghyvet erelrqiwke tdddesrlva gtllaealav tgrpvsaiqi
      541 lmeiqemvst sgdwslqyag mvmrryilal hqagefgvle tflknhvsqa pnsliysggm
      601 lhlaagmvdl rrgdlgvalp rlrqavsmlr vsdmgsdlpd avaaaayaas ilkrrdtamt
      661 ysseydalir egvhpsllaq ghaavaraeh tgsqtaiarl msladsaaad gaigaeidil
      721 mlilrlgdtg varrliavae gsegrtaefa lsvglalahk dadrlielse saardglela
      781 aadcaghalr ilesrgdkar qlegqrllkr rtaaldkagp vleggspdlq kltrreqeia
      841 tlvqsgssnk dialslglsl rtveghlyrm faklgishre dlmngahgtq glg
//
LOCUS       WP_284752341             266 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family oxidoreductase [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284752341
VERSION     WP_284752341.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 266)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 266)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..266
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28048
     Region          4..215
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mnstilvtgg tgtlgrlvas rlrgggysvr vagrhapppe qdiefaqcdl dtgdgieaal
       61 sgvrtvvhca gtqkgdgdka rhlvaaasra dvthlvfisv vgadtipvks rfdraafgyf
      121 askrdaeevv agsgipfstl ratqffelsl ltvramaklp vipvpkgfrf qpvdagevad
      181 rlvelalaqp aglvpdlagp vcypmgelir sylaaaglrr llvpvhmpgh aakairagan
      241 lsedravgrr tweeflteqv stavrr
//
LOCUS       WP_284752725             172 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284752725
VERSION     WP_284752725.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..172
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18605
     Region          7..168
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
ORIGIN      
        1 mfneagavli rpmshedwpe vraiftegie tgqatfeaaa peweqfngsr lpdhrfvava
       61 sgrvvgwtav savstrpaya gvvehsvyva gsargrgvgs lllqalaast eehgiwtiqs
      121 sifpenqasi rlhqangfti vgrrvriarm sagplagqwr dtlllerrsl rv
//
LOCUS       WP_284752756             229 aa            linear   BCT 25-DEC-2024
DEFINITION  IMPACT family protein [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284752756
VERSION     WP_284752756.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Park,F., Gajiwala,K., Eroshkina,G., Furlong,E., He,D.,
            Batiyenko,Y., Romero,R., Christopher,J., Badger,J., Hendle,J.,
            Lin,J., Peat,T. and Buchanan,S.
  TITLE     Crystal structure of YIGZ, a conserved hypothetical protein from
            Escherichia coli k12 with a novel fold
  JOURNAL   Proteins 55 (3), 775-777 (2004)
   PUBMED   15103642
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Okamura,K., Hagiwara-Takeuchi,Y., Li,T., Vu,T.H., Hirai,M.,
            Hattori,M., Sakaki,Y., Hoffman,A.R. and Ito,T.
  TITLE     Comparative genome analysis of the mouse imprinted gene impact and
            its nonimprinted human homolog IMPACT: toward the structural basis
            for species-specific imprinting
  JOURNAL   Genome Res 10 (12), 1878-1889 (2000)
   PUBMED   11116084
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..229
                     /product="IMPACT family protein"
                     /calculated_mol_wt=24546
     Region          12..214
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 maeqeesrat ayttlapgdd frheleikrs rfitvlrras dedaaralva elrkefhdar
       61 hhcsafvlgp drviqrsndd gepsgtagip mlealikret lpgvtdlsdv savvvryfgg
      121 illgagglvr aysesvsaal dsaplvqrrr lricdipvph haagrlendl rsaghvmaet
      181 syepsetilr valpddpgai adagerlasm tggasglqlr gtvwvdvqa
//
LOCUS       WP_284752905             419 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284752905
VERSION     WP_284752905.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..419
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44705
     Region          15..398
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mtqpeypghk qdhkgplagk lvvdlsrala gphagmmlgd lgarvikven pdggddtrgw
       61 gppfvdipeg restyflscn rnkesirldl kaaegkaalr ellrqadvlv enfrpgtldr
      121 lgfdpaslek lnprlvvlai sgfghdgpeg hragydqiaq geaglmsltg sgprdpqrvg
      181 vpigdvlagv hgacgvlaal lerertgrgq ivrtsllssi vsvlafqgtr wtvggevpqa
      241 qgnhhpsiap yglfrcagga vqiavgsegl wrrfagefsl pvdderwrdn qsrvahqael
      301 idaieaafse sdaeellarl eaagvpggrv rsldevfawe qtrsqhlale lqhptlgrie
      361 vpgsplrffq qdgtettrlr hsapprlgeh ddavrawldg aglpgdalpg gallasras
//
LOCUS       WP_284753070             695 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284753070
VERSION     WP_284753070.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 695)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 695)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 695)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..695
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72590
     Region          86..354
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
     Region          421..687
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
ORIGIN      
        1 msvateranr rrrsggarpd spggrtpatp sggpavlgfc rrhwrpvslv gicvvwlvlw
       61 atlkgldtle lggadktdfq lwlnsvrdaf dsartnsfvf qhivqpitdg vnglvtslqg
      121 ifsqasdgrp vpeigwlgvv allawlalaf agvrsmllvg vcvllfgffg ywaqsidtli
      181 vtffavgict vaglplgivm arsrrvsaav splldlmqtl psfaylapla lvfgigpaaa
      241 ivttiiyslp plvritehgi rgvspatlea vtsmgstpwq alvkvqlpma rrtivvginq
      301 ctmaalsmat iaalingpgl gtpvlqalqs ldvgsafvsg laivlmaiml drtttraser
      361 sgiearilrg sgmaqagtfg gqqmrrtvii agavvaavai ylshiylals kfpawpdlgt
      421 plakavstat dwtvgtfsgf tewlkntvta llvdplqsvl aqspwwamal vllgiafvla
      481 grraatvtiv ceavilgsgl wnesmktlat tlvasfvvvl vavclgvwmg rskpadsvir
      541 pvldafqtip sfvylvpala lfgptrftai vaafaygvpi atklvadgir gvspvaveaa
      601 eslgttsrqm iakvqlpmar aavvlaanqg llyvlsmvvv gglvgggglg ylvvagfsqs
      661 qlfgkglaag iaitalgvml dritqhatar fgstr
//
LOCUS       WP_284753085             326 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284753085
VERSION     WP_284753085.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 326)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..326
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35124
     Region          35..323
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mssttaqsgl ararrglapg gpgggsqhrs gglnrkskls gqtkrtffwl llpsivllvl
       61 ingypliyag vqathdgsli dtgnfvgvdn fatvlsspaf wkaaqftlwf tivgvfgswl
      121 vglglalllr tkipaggtfk vllllpwvvp ivvsstawnw lvatpeslip sifrnlglgt
      181 plfladphla avmvmvfkvw vsfpfmmmmi saalasvdtt vyeaasmdga skwqqftqit
      241 lpmiarstyi swilmtifcv ndfptiyllt gggpvdatts lvvlayrsvf qdfqtgpgva
      301 iaflmtltlv vvsvflyrqi rkssve
//
LOCUS       WP_284753086             436 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [unclassified Arthrobacter].
ACCESSION   WP_284753086
VERSION     WP_284753086.1
KEYWORDS    RefSeq.
SOURCE      unclassified Arthrobacter
  ORGANISM  unclassified Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 436)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="unclassified Arthrobacter"
                     /db_xref="taxon:235627"
     Protein         1..436
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46521
     Region          45..353
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mnvqseasrn fsrrgflglt aaaaavplla acgggsssss aggaikfwdm pwatpaynda
       61 akkitegfsg anskasyqii qwnnfyqtfs saiasktgpa vstgggfqaf qfeqqgqiay
      121 adkvidalkk ngqfddflpg vlepfksdkg yvavpwqldm rplwyrkslf dqagvavptd
      181 wpslleagkk lkgigavgfa tgsgagnnig nhlmimmmin ngggvftkdg qldvmndrnv
      241 eatefllelv sngiidpaav sytsdnldaq wknkkaafgm yvlgvpqrvg dtsgdllvas
      301 pmagphgdka tlvfpnnimm ykntpsqdas eafltyymgq lkslwqqklm nalpvfksit
      361 elpefasdpn nvkivkeyqp iaktfaaqgt slnanlavld ggqalnqftq tiltgktdak
      421 saltafqtgl qsvlkk
//
LOCUS       WP_284752647             188 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA polymerase sigma factor [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284752647
VERSION     WP_284752647.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..188
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21366
     Region          11..161
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mrqpskapdr ertfrllyel vhpelmrfvq rrahpdhaed vvadaflvvw rrldelpsrh
       61 ddarawifgi trnillnthr gerrrlalgv rladaaalay ldedadpivn ridlgkawca
      121 lsethqealg lvvfedlnap qaaavlgisp vafrlrlsra rralrllleh lprhsripaa
      181 sfertttp
//
LOCUS       WP_284753088             370 aa            linear   BCT 25-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284753088
VERSION     WP_284753088.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..370
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39272
     Region          15..>148
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msshsqatsl gspqplgvgi lgagpvtqai hlpslarlrn ilevrhimdv davvaesvaa
       61 rvganhstsm dallgdpdvd ivaicsphqf hadqviaacr agkkavlcek pfamsgeeaa
      121 risavseetg vpiivgamht fdpgwlaaeg nwgdlpenvh tirssivlpp narfedfate
      181 iitrpaggtp dysdievikn alrggimgla ihdlplvrrf tpdfedlevl qarhvrpfgy
      241 vislrsgkqg agdriielra amnktwkpew vfeaisddaa lrmdftpsyv qagsavatit
      301 rgststtygp fehngyegew relaqlalgt kqppsaesli ndltfaiaia datvdvaaae
      361 hanshagahs
//
LOCUS       WP_284753101             200 aa            linear   BCT 25-DEC-2024
DEFINITION  YdeI/OmpD-associated family protein [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284753101
VERSION     WP_284753101.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Pilonieta,M.C., Erickson,K.D., Ernst,R.K. and Detweiler,C.S.
  TITLE     A protein important for antimicrobial peptide resistance,
            YdeI/OmdA, is in the periplasm and interacts with OmpD/NmpC
  JOURNAL   J Bacteriol 191 (23), 7243-7252 (2009)
   PUBMED   19767429
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..200
                     /product="YdeI/OmpD-associated family protein"
                     /calculated_mol_wt=21977
     Region          1..191
                     /region_name="YdeI"
                     /note="Uncharacterized conserved protein YdeI,
                     YjbR/CyaY-like superfamily, DUF1801 family [Function
                     unknown]; COG4430"
                     /db_xref="CDD:443542"
ORIGIN      
        1 maveleeliv kdaaewrswl ekngahspgv wlvlhkkggn vteldyaaal dealcfgwid
       61 gqgrrrddes vfqrmtrrgp kspwskrnvg hiarleaegk mtpagwaavd gakadgrwea
      121 ayvgqsdaev pedlaaaiaa vpeaqamfdv ltavnrysli yrtnsvkkae trarkiagfv
      181 emlarqetpy pqkkkpavae
//
LOCUS       WP_284753228             256 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family oxidoreductase [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284753228
VERSION     WP_284753228.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..256
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=26381
     Region          16..254
                     /region_name="fabG"
                     /note="3-oxoacyl-ACP reductase FabG; PRK05653"
                     /db_xref="CDD:235546"
     Site            order(21,23..24,26,45..47,100..102,149..151,164,168,
                     194..197)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187535"
     Site            order(124,151,164,168)
                     /site_type="active"
                     /db_xref="CDD:187535"
ORIGIN      
        1 mveekivadq ssarpvalit gasrgigqss avamaeagfd ivgfsqsgds gnsetcrlvn
       61 laggayvthk vnvavesdvr safrslltan grrlhavvvs agitsdglaa tmsadrfdsv
      121 iavnlrgtfl vcreaikamr ktggaivlls stsgvsgqag qvnysaskgg vnamtqalak
      181 evaglgirvn avapgftetd mfrrmdvkar ngliqhiplq rvakpeevar avrflatees
      241 syitgqilpv dgglta
//
LOCUS       WP_284753286             300 aa            linear   BCT 25-DEC-2024
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Curtobacterium
            sp. ME-Dv--P-122a].
ACCESSION   WP_284753286
VERSION     WP_284753286.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..300
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=31643
     Region          133..232
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 maagarqste taagrnpwqr fwnrggwwra vlavilylav yeglgwlnah tlasgitade
       61 lfasprgavv gvalpiivmg lltlvfvrtl gwgrevfgrq plpgrgwmwi avvlllvpiv
      121 irlvatnwss ysvsvvfavl flglcigfae eliargvavn llrrghhter tvallssllf
      181 glmhasnaig gtplvtvavt vvytfgagmm fylsmrvtgs ivpamllhaa tdpttilatg
      241 gidttaaaag dagligfagi fnfaypvlal lvlffikgrv sspetgtgte tetdqqgvaa
//
LOCUS       WP_284753338             330 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284753338
VERSION     WP_284753338.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..330
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=35135
     Region          25..308
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mtivdvppaa aaaadasvrw hacgpfdllq tlgilmrgng dpsfaarqdg vwmafttpdg
       61 pvtlrltaag ngqdrhvdaq awgvgagsai asvpallgsg ddwsgfdeaa fhatlprmvr
      121 earrrnlavr lpttgrvvds lvptileqkv ttiearrgyr ylmyrygtsa psagrlstsg
      181 lpsgllvppt asqwlavpsw ewhkagvgpq rsatvmralr savalerlas lsaaeagakm
      241 qtipgigvwt aaevvqrthg cpdsiavgdy hlasyvgyal tgrktddagm iallepwrgh
      301 rqrvvrmlgl sgfrkptfgp rmtiqdhrgh
//
LOCUS       WP_284753423             294 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284753423
VERSION     WP_284753423.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 294)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..294
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31560
     Region          2..293
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mprkrrplrn vgravplipa lvllvifllg pvissfygsf tnsaltgasa adqqfvgfqn
       61 yvelfqdpdf pksviltvvf llasavvgqn vlglglallm rsankavrai vgtfvvaawv
      121 lpeivasfaa yaffndegtl ntflasigit ganwlytypm favilaniwr gtafsmlvys
      181 aavqevpeei tesaevdgat gwqrlvyitl pvirrsistn lmlttlqtls vftlifvmtg
      241 ggpgtnsstl pilayqeafk fsqlgfgtai atillvvgav fsiiyiralk pevd
//
LOCUS       WP_284753459             486 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284753459
VERSION     WP_284753459.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..486
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50894
     Region          7..484
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 maeenirefd vivigagavg envadrvvrg gltaaiveae lvggecsywa cipskallrp
       61 gtalhtaqsv pgasdsvtkv ldpapvlkyr dyftnkwqdd gavqwlvdtg ielirgrari
      121 tgprevqvdg kdgnsyslka hhavvvatgs tpvipkvdgl rdvpywttrg atsaryipar
      181 fvvlgggvas velaqafarl gssvtivarg rllsafpeea adlvaaglra dgvdlrlgtd
      241 ttlvehnpdr afsvtlgdgt vlnsdellva tgrrpaldnl glenvgldae egkalrlttd
      301 ssglvegaas dgtsglwlya agdaagsvfl thqgkyeara tgdaivarak gtlhgtpkpw
      361 salaktadey aipsvvftdp evasvgpslk qalqkginas svelpinvsg sqlhsenyeg
      421 waqlvvdedr kvvvgatfag pgvaellhga siaivgevpl drlwhavpsy ptisevwlrl
      481 lekygl
//
LOCUS       WP_284753460             260 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284753460
VERSION     WP_284753460.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426811
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..260
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27909
     Region          5..242
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 maelvdiagh ptwvedrggp gepllllhgg lsnsddllrs igpglserfr vvafdrrghg
       61 ytadtdaefh yadmatetvr vledviggra hlvgwsdggi vgllvalrrp elvsklvvig
      121 tnyhyngtvp femdqdspia qelgkayier spdgpehlev vfgksvamft sepeltttdi
      181 ahitqpvlvm vgdddvvtlp htlslyealp qgqlavipga shglpleqpe vvtglianfl
      241 aaeepprtfm pvrrakpaeg
//
LOCUS       WP_284753486             689 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284753486
VERSION     WP_284753486.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 689)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 689)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 689)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..689
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..689
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=70612
     Region          61..>285
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mttsystdtg skagqsapps rsveppeaaa prggggrara gvtrksrsnr glgalrhrve
       61 lgivliatav lylwnlgasg wanafysaaa qagsqswtaw ffgssdaans itvdkppasl
      121 wimdlsvrif glnswsilvp ealmgvataw llylavrraa vpasgdprla hragllaavv
      181 maitpvatli frfnnpdall vllmtaagya tlrsiqdnkl rwllfagvfl gfgfltkqlq
      241 vllvvpgfiv ayvvaaqggv grrllrllaa gaamvvsagw wlavvelipa nmrpyiggsq
      301 nnsileltlg ynglgrlsgq etgsvgggng wgvpglfrmf nsefggqiaw llpsvlilga
      361 gllwlgrrap rtdsvrasvi vwgswvlvtg lvfsfmagii hpyyavalap giaglaglgg
      421 vllwqhraql vaavmlamav aaagftafdl lgsttaygpl lrwavllgal aaaagvllsg
      481 rfpsrilqrt tavlalaasl agplaysist asvthsgaip sagptttfgg fggfggrggf
      541 gqgaqntppq alqqpgaqgg gfggnrqggg mggllgattp ssemvaalks gasnytwaaa
      601 vvgsnnaagy qlatelpvma vggfngtdps ptleqfqqlv aqgkihyfia ggtmqansgs
      661 dapaqieqwv aanfqsqtig gttvyalag
//
LOCUS       WP_284753602             165 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284753602
VERSION     WP_284753602.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..165
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18424
     Region          16..157
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msntpddape tveagdnvda alqqvehqls mfwrrarsls hqlsrqvhpd mepaaygllt
       61 iirkegpirl telascigvg kpsvsrqiaf lesigmvyke adpqdgraqs irltpkgeek
      121 mhqvqdarrq vfrerlgewp leeiqtlady ierlnaayge gigkd
//
LOCUS       WP_284753630             344 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284753630
VERSION     WP_284753630.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..344
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33833
     Region          35..339
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mppststppa pssvprlvga tvlavvvlav acalsiaygs rpiplgtvld tvmhpgrsde
       61 vglivlgnrv prtvvgllag aalgvagavm qgvtrnplad psvlginsga tlavvagiav
      121 fgvsgtaayl pfafigaala avlvygiatv arrglspvgl alagavvaaa lssvttavlv
      181 tdqslldqlr fwqvgalagk dlgtagiita pvlvglviaf glgrslntla lgdelaaslg
      241 qrvvlvravg glvavllags avaaagpiaf vglavphavr rlsgpdhrwt illsaivapa
      301 lllvadvigr vvaypgelqv givtaligap vfialvrsra vrgl
//
LOCUS       WP_284753639             248 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284753639
VERSION     WP_284753639.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..248
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24630
     Region          13..226
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mipantphtn nrlgawltfl dahgvealsg sgfdwigidl qhgtatldgl pgllraceln
       61 rtpalvrtsg hsaaeigral dagaagvvvp mvesaaqaaa iaaactfppe gvrssgasrs
      121 aiaapsplqp egkvlclami esaaglanag aiaqadgidg ifvgpydlal slgadgvtdp
      181 ktldaighvl avarnhgklt gafsgsaels galrdadlla vdsdlaflrs gaeaklaatr
      241 aalstarq
//
LOCUS       WP_284753678             589 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284753678
VERSION     WP_284753678.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 589)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 589)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..589
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=62287
     Region          1..573
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mtktirnrrl rysivmlavi alvgvfvvrl vdiqvvqase lnkasaqkrs ipvtiygtrg
       61 sivdrngtel adsvtrynit tsprlvkqfk gklggtrikn vsvgtalsal akasggdvat
      121 mrkniaanpk sdfaylvkgl dvqhyeavra lgipwlypep qaarvyptga ttgnltgfmg
      181 tdgaqagley synqclagtn gsetyerged gvqlpgstvt tkkakdggtl ettidsdlqy
      241 maqqtiasaa ktlqaesata tvtsvktgel lavadyptvd pndvdattdk gafgsralta
      301 syepgstika aiaaalldqg ksnptdqavv pysrtfpwgg tihdsefhpt enltltgilq
      361 nssnvgitel garltaqqrf dymkkfglfe petaidypgq psmdygtspn wdqqtninsm
      421 fgqgisttav qvasvfqtia ndgvriplhf vkgcttadgk tidapdvqkq rvvsaaaatq
      481 vtgmlqsvvt ggtlvgmkpi sgyniaaktg taevaegsqg yggqritsva gmapaedpqy
      541 vvtvtftkpq tnkwssgaap afrtlmsqvl ekyrvapsas eaklypstw
//
LOCUS       WP_284753725             225 aa            linear   BCT 25-DEC-2024
DEFINITION  FMN-dependent NADH-azoreductase [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284753725
VERSION     WP_284753725.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..225
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24003
     Region          1..210
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mptilhinas prdshsgslr larhfidevq sagdgtfeve tvnlfdagvl pgfgriaaaa
       61 kmavfsgqdq tseqmnawea aravfeqfaa adayvfnipm wnagvpyvlk qwidivtqpg
      121 wsfgfdpatg yrgllegkqa laihtsgvya pgvpaafgqd fsstffadwl nfvgiedath
      181 vrfaptvlng dvdgtrraae telsevattf agklsaagll qlvnd
//
LOCUS       WP_284753727             138 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284753727
VERSION     WP_284753727.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..138
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15403
     Region          22..120
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msltvelkrq aaqteynael ihcparhlle aisskwvtlv mlalaegplr hselrkripg
       61 asqkmltstl rslerdgivs rcitvsvpvr tdyeltpvgh sllsvvhdmk ewaeanmddv
      121 aharlehdrr asisgdrr
//
LOCUS       WP_284753776             336 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284753776
VERSION     WP_284753776.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 336)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..336
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37013
     Region          52..334
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mslttdssqa nqqarsranq rakpgsdsvr areespsprr rsrkrrerlf qwlflvpavi
       61 ymalffgypv vknivmsfqd yttatfftge apwvglanya kvlssslfst slvntalftl
      121 gsilgqfvig lalaiffqrk fplngilrsl lllpwllpli vssavwrwil dkdsgalnrf
      181 lgelhivntg vpwltstsla liavvgvniw igipfnltil ygglqeipde lyeagsldga
      241 tgwkafrhit wpmlrpvvsv vlvlgvvytl kvldiilglt nggpanstqt iatqsydlsf
      301 hefkfgegaa lgnvlvvisl vfavlylras rrsvde
//
LOCUS       WP_284753780             197 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284753780
VERSION     WP_284753780.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..197
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21618
     Region          7..181
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mtliapvtld grfvtlepls aehhdglvda akdgelwnlw ytsvptpegm aaeidrrlgl
       61 qeqgsmlpfa trlkangkli gmttymnida atprveigst wnaasahgsg snpdskllll
      121 rhafetlgcp avefrthwln hqsreaiarl gakqdgvlrn hsrtldgvlr dtvvfsileh
      181 ewpavrtgle frlakrs
//
LOCUS       WP_284753857             835 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional lysylphosphatidylglycerol flippase/synthetase MprF
            [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284753857
VERSION     WP_284753857.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458459
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..835
                     /product="bifunctional lysylphosphatidylglycerol
                     flippase/synthetase MprF"
                     /calculated_mol_wt=87116
     Region          216..808
                     /region_name="MprF2"
                     /note="Lysylphosphatidylglycerol synthetase MprF,
                     lysyl-tRNA-binding C-terminal domain [Lipid transport and
                     metabolism]; COG2898"
                     /db_xref="CDD:442143"
ORIGIN      
        1 msavvaalaw ahprrlvpaa rrypltsvvs altivagiaa vvlrclgtkd grtpdtlggt
       61 mgplgvvavt ssvvgflvtf vavvvctaas erllgwrrtl lamvvttvvg tglgallqlf
      121 dgapanrgfl vhlghvgpwt wivgtivtas afagalwrrr irvvsiavva alllyaghas
      181 dlhaalalvv glvlgrvlrr spvrsgwtrs ssretrvllv aavtvsavgp vlalvtgaqf
      241 gllaplavvl dtgptgrmph csvtgvtasc vralaevhph glfhsllavm plvvlavgav
      301 glrrgsrfal wlvatvdlvs gvatavsygv lperhhavvq rlasdhlavs lsivasvlvp
      361 iatavvlvlr radfpvrtdr rrlrtfvltv agsavvlavv vvgvavasgd svreplhlal
      421 avlgpiapvt lpthlaqaep alrfvvgvsg pllwlavaia avrptgagrs dsdldgqdaa
      481 rvaarallva gggdtfgwmt twpgneywft edgragvayh rtgsvavttg gpfghedarl
      541 aalegfaraa ddhgwtpvfy gidatlgaal arlgwttlpv aedadldprt wtttgkrkqd
      601 vrtavnkaar sgttalwadw aslpgsvtrq ieaiseewva erelpemgft lggidemrdp
      661 avrtlvalge dgtvlavtsw lpayragqvv gwtldvmrra pdapngvmef lvasavdrmr
      721 tdgaerlsls aaplassaep qgagrggves vldvvggale pvygfrsllr fkakfgpdlh
      781 plvmaypdpv alptigvaiv rtylpglslr qavaivrerr pahgvraeqp gervg
//
LOCUS       WP_284753914             191 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284753914
VERSION     WP_284753914.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..191
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20395
     Region          4..170
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mqpvtlrter lvlsvpelgd addvvayand pdviastpvp vpyghaeary wisdvvgagw
       61 aadtryefgi rraddlrllg tvglfafadg aaeigyamhp dgrgsgimte aaervlqwaf
      121 agppeglglv rvqwraiatn tasaavaqrl glrfegrtrs svlhrgsrhd qllaaalldd
      181 drsaatvwpt s
//
LOCUS       WP_284753922             955 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284753922
VERSION     WP_284753922.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..955
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..955
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=101241
     Region          <2..953
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 maavltdeel lprgdevsvp vsavprsglp irgrsieqav vadalvglar gagdvlvvrg
       61 aagvgksrll edvvdqatav glrvavgrtd rdarliplap imdalgagpr pisdrvrlsa
      121 vtldpearyw llqqlqddle raaasdgvvv vvddlqwcdt ttlavlrsls rrladvpvlw
      181 vvavrtehqd ppvtaivdel aatgrivdld pldeqataam iadlvgatpd gsvlraarrt
      241 ehipilvael vrglvdegll aivdgvatmp gaalparfga sireglrrls kptqqlvqvg
      301 atlgrsfsvr slsamldqpv qrllpglqea ieagvlvddg tdlsfrhdvl reaaesmvpa
      361 avrddllrqa vdellrqgvp pvsiaariat vaqrgdvraa evlrtvaidl astdpteaga
      421 lalraadvah gtpalpgivv dvlpllwhsg rtaearalld dlqgrlaped darlhltlar
      481 lqtegstpea lqtvesalal pgvsagvrsr llavralnla qagrhadlat alrearatvd
      541 gdadpvavat feasasvlaf negrfadatq aitsamsria atggssstwl peglwvafla
      601 galgdtdrag riaeanaiet rrnhlarpsa awmmlrtrvl fdqgrledak tsaesvldla
      661 edlelgqfaa ltagtvlfrt allqgdrsaa drtrhfaeal hadpafarsg swllaleada
      721 hgdvraavdr sevawrslee piasmsspad faddvhlari airggrrdrl eriervarlr
      781 atanpdndlc ggtwlhvhgl vhdsvehlga aaerlrrvdr rlvlaaaled lgsalrrrsv
      841 paavevwrea ttlfdsagal reaersrrhl rgvgvtvraa tadpaasgas glpgltarea
      901 qvvervaagl ttqqiasdlf isthtvtshv rhvyakwgva srrelaarfr qhrsg
//
LOCUS       WP_284753973             451 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284753973
VERSION     WP_284753973.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 451)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..451
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48039
     Region          33..357
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mktrrlqvrt lvgavavval aalslqgcav vngsgddpnt lrvmmgadtt ypkerkqwqr
       61 etaaefkrtt gadiqwetys saqeeltaiq tsvisgqgpd vyaigttftp tayatgafve
      121 mgakewdaig gkdqfdpasf gisgpspskq igipfasrpf vmavnkdlla kagitdmptt
      181 wdeltadaka ttgdgrhgma iayadgfdpw kfvwgmaqna gntivdgska eidskavena
      241 yrtyfdwvtk dgvvdpaaig wnnaqalaqf tegkaaffpm ttttainsft gtkvdgkyef
      301 allptvppga terpsdgiea asilsgdnwv vadygtkqel sfafvkqlsa pkaqleyydl
      361 fgnlptnasa aadlaadnpq lkpiidagrl skptaftgaw sdiqlalvdv vvqsipslks
      421 gevtddqlrk rlqdaqkdaq atldrqkngg l
//
LOCUS       WP_284753990             563 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC1 kinase family protein [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284753990
VERSION     WP_284753990.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..563
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0004672 - protein kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=61845
     Region          20..474
                     /region_name="AarF"
                     /note="Predicted protein kinase regulating ubiquinone
                     biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport
                     and metabolism, Signal transduction mechanisms]; COG0661"
                     /db_xref="CDD:440425"
ORIGIN      
        1 mptpprlsdl sgprdadtgs lrsrgrrfte llsiarrhhl vpfrrldfsh dpatsdlrrd
       61 qaehlrrale eagggfvkmg qllstrddll peewteglah lqrnvtaapa devralleqe
      121 lgapidqvfa tfdpvpvaaa siaqvhrarl pdgtavavkv qrpgidaavr rdvdialrvv
      181 rfmarwstea rqvgvqdiag qyaddlirqv dfvselrnlt alraaqarsa rpdevrfpdp
      241 ypdlsgrrvl vmeflegdtl sairaerser dldapmrail raflrqvvfd glyhadlhpg
      301 nvlvlrdgrp alidfgsvgr ldpglrdtvq dllaaylqdd tsriadavlr mapvrdahde
      361 pdfrrdiarf vadelgpgar igvdtvddav evfgryrlkp ppdfvaaara laifegtlrt
      421 lapsfdllee srglareqit dqlrpgklrd laakellgvv saarrlprrv drigeaietg
      481 rftvnirlfa dsrdrqlvsg mirrillvll gagagilaiv ylslparpta alstgvaggl
      541 lggaavvllg waaidawlar rrr
//
LOCUS       WP_284753997             522 aa            linear   BCT 25-DEC-2024
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284753997
VERSION     WP_284753997.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..522
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=55011
     Region          22..522
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mspqtkpqga rrgprpasar rvafdvlrav qvddayanll lptrirragl tardagfate
       61 ltygsirmlg rydviialas grraeniead vldvmrlgah qllamrtpth aavdatvela
      121 revgarratg fvnavmrkia artdqewdal itegragdal latrwshpvw vvsalrdala
      181 aersrdelaa llaadnaapr vqlaalpgla tdediatata rtapdddtda afadatgadd
      241 vpaalvpadd epeadgatgt vppvrtdepv vqadaapvsp vgirgisgdp arvpgvaagr
      301 lrvqdegsql aalalsrssd vragerwldm cagpggkaal laaearqgga tlvanelvpa
      361 raglvrnalg vfgdhvrvve gdarrygrdg tgmtfdrill dapctglgal rrrpearwrk
      421 lpedveelaa lqtelldaav rvlapggtla yvtcsphlae trgqvdalmg rhgdrleqld
      481 tativrgvaa rdpeiadgat aqlwphrigt damfialfrr vd
//
LOCUS       WP_284754026             410 aa            linear   BCT 25-DEC-2024
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Curtobacterium
            sp. ME-Dv--P-122a].
ACCESSION   WP_284754026
VERSION     WP_284754026.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..410
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43567
     Region          50..402
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 msrvvrrprs avrrpvtisv vavlllvagy lvaaavvpfg pasastttys apkttvpals
       61 fpgygatave atdfpeslrt sgdtkprsia sitkvvtalv vldekpmaag esgpsirftk
      121 qmeglyakya aqngevapmp aglkltehqt fqvmlmksan nyagalaiwa fgsiaayera
      181 andwldehgl ddttiheptg ldpdntstat dlvelgqlal anpvvkdivg tqdvtiptvg
      241 eiensnkllg ldgiegiktg tldeagacll faatyerggk dvtvvgvmlg gvdhdsldvd
      301 vqrllrsvad nfqvvtlthq gqtfgtfstp wqdeadavtt kaaevlvwgk ttvtakakle
      361 qvtfgtkger vgqvrfrisd hdpvtvplvl ertiddpgvw wrwtnpfqga
//
LOCUS       WP_284754070             234 aa            linear   BCT 25-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284754070
VERSION     WP_284754070.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..234
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24611
     Region          2..222
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mrthelvlsw iekqlsdghl vlggrlpaer alaeqlevsr tsvreairil eamglvragv
       61 gsgkdagtvv iaepaaalgs alrlhvatqh lpvadivetr vlleswavsr akadapelke
      121 aarlldemdv saavddflal dvafhlalae aagnavvsti mgslreaieg yaaaltanlp
      181 dwdhtadrlr sehraileav ndgdggraat lvaahiegyy reaglgkapa etkp
//
LOCUS       WP_284754103             141 aa            linear   BCT 25-DEC-2024
DEFINITION  Fur family transcriptional regulator [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284754103
VERSION     WP_284754103.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..141
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15082
     Region          9..130
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mnavqktkrn twqreavrga ldstdgfvsa qalhqhlrde gstiglatvy raladlateg
       61 dadslqqdge slyracttda hhhhlicrnc grtveieadp veqwaqdvaa angftnashv
      121 vdifgecavc taarttdstg e
//
LOCUS       WP_284754144             203 aa            linear   BCT 25-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284754144
VERSION     WP_284754144.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..203
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20768
     Region          19..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtrparrarp paeeinggvl ditagliarr gikdtavqav adqagyskag ilarftskel
       61 lveaalaqct aqteairaaa taapageprd aaalagiadl alvrpgwael alaaftlrrg
      121 ddvgvrlepv aatlldvfgi dmadatatpl drrarvsgaf gaivmlalty eteasaaear
      181 phmlqigwda lghdgpvplg vvg
//
LOCUS       WP_284754232             353 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284754232
VERSION     WP_284754232.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 353)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..353
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=36646
     Region          7..324
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mtenpdqatl rkaslkiavr isaactvlvl cllaaaaiyl fnqaqhptlp gpgetdsvya
       61 yldtkdllkv mivagiagil lagaigwlsa rsairplgea lalqrrfvqd ashelrtpla
      121 ildarvqlaq rdapadsktg ealarirndt atltgivnel lvaatgsppd ataepsdlak
      181 vagavveslq qlagekdvrv tltekdrpfa lidsnafrra llaladnala htpvggqvgi
      241 ttavlgnrav vtvsdsgagi kgvdqtrifd rfvrthspeg spgqrsfgig lalvreiitg
      301 argtvevers gprgtvmkit lplapkaagp kdaapkdtgp kdtgpkdtws gsa
//
LOCUS       WP_284754241             489 aa            linear   BCT 25-DEC-2024
DEFINITION  rhamnulokinase [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284754241
VERSION     WP_284754241.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167330
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..489
                     /product="rhamnulokinase"
                     /EC_number="2.7.1.5"
                     /GO_function="GO:0004370 - glycerol kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008993 - rhamnulokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006071 - glycerol metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0019301 - rhamnose catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50831
     Region          11..474
                     /region_name="ASKHA_NBD_FGGY_RhaB-like"
                     /note="nucleotide-binding domain (NBD) of rhamnulokinase
                     (RhaB) and similar proteins; cd07771"
                     /db_xref="CDD:466791"
ORIGIN      
        1 msgketgggv faaidigass grvmlgrvtg gpasgktvsl etvhrfpngv veldgglhwd
       61 fealfdevlt glaaaaetaa asgkriasig idtwavdygl vdasgalrtq pfsyrdergr
      121 tavadvhkvl dparlyattg lqflqfntly qlaterelrg vqallipdli aftltgqrrt
      181 eatnasttgl fdavagewat esfkalglpk nlfpaiiqpg etvgtllpei aartglaaet
      241 avvavgshdt asavaavpar qedfayissg twslvgveld npvldessrl anftnergvd
      301 gtvrylrnvg glwllsecqr twaaeghrqe laallesaaa lpaggpqina edpafiapds
      361 mperirsavr aggavlpdrp aaivrcilds laaayartla raeelsgkqt svvhivgggs
      421 qnrllcqlta datgktvvag pveatalgnv lvqaraagav sgglselral vrasvglesy
      481 epklvfhsp
//
LOCUS       WP_284754246             219 aa            linear   BCT 25-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284754246
VERSION     WP_284754246.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..219
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23620
     Region          37..219
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mtstfervld qvgaavvsga vavgsrrsvd dlvtwtgasr sivreavrvl valgllsarr
       61 rvgvtvldvr ewdvldprvv rwrlrgpdgd rvaaelrelr aavepaaaaa aarraaldec
      121 adrrealrtt adelaaaatr ddrpdfvaad vrfhalvldl sgnalyrrlh qvvgqvlrer
      181 gsirpdrhdv glhlaladav ldgrpddaas tmqaivdrt
//
LOCUS       WP_284754350             347 aa            linear   BCT 25-DEC-2024
DEFINITION  HoxN/HupN/NixA family nickel/cobalt transporter [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284754350
VERSION     WP_284754350.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..347
                     /product="HoxN/HupN/NixA family nickel/cobalt transporter"
                     /calculated_mol_wt=36371
     Region          16..336
                     /region_name="HoxN"
                     /note="High-affinity nickel/cobalt permease [Inorganic ion
                     transport and metabolism]; COG3376"
                     /db_xref="CDD:442603"
ORIGIN      
        1 mtslaefasm yrqrehlpmk srlafmfgsv vllhlaavvf llvggagggq plalglvlta
       61 yvagikhsyd wdhiaaidns trkfvaqhkd pvsvgfafsl ghssvvilag vmvvggaslv
      121 gqlmedgttg hlvlgligsg vsglfllamg ifngsaflrt mqlyraaqag geiavddlet
      181 kgfiarllak plskvqrprn iyvigflfgl gfdtattigl lvlttaasla gvsvlallal
      241 plaftaamtl cdsingvamm rmyksaihdp qrklgfnaii tgisafsalf isvitlggfl
      301 naafglsdpv ttwlgeidlg daglvlialf avvwvvaalr fraarrr
//
LOCUS       WP_284754352             356 aa            linear   BCT 25-DEC-2024
DEFINITION  lactonase family protein [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284754352
VERSION     WP_284754352.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..356
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=36901
     Region          1..355
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 maenidgtli wagaytadsd gngmgigava aredgsiawl gtaveapsps flavhpalpv
       61 vyavaeaaqt irayrrtglf gleplgeawp agaaachvav dpsarfivvn cwgdgnvlly
      121 gldddggits rfaappakdp hagvdggidi atggarvsra haslmledgr imttdlgfdl
      181 vrvwnyfpdt gllkdheval pvgsgprhlv qhpsadavfv vteysievvv llpgadgrfv
      241 lhrrgpatag gaadgdaaae ialspdnrfv ytgirgsnri svlavegsgt rlrpvadvps
      301 ggdwprhhlv rdgwlhvahe rsnqvttfal dpatgipgev ldqlntgspt alviap
//
LOCUS       WP_284754376             448 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284754376
VERSION     WP_284754376.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..448
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=47997
     Region          24..329
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mgfsrqqkts agmaafgrsr dpvidlarff clilvvlshc mmvspvlhpd gtvttentlm
       61 eqhwfepvlw vfqvmplffv lggitglesw rrlrarggsg vdyaqlrllr lirpatalla
      121 smfvglwaas llgvdpevvq liatgagmpl wflaaylatq lsvpllarlh ghspwltlsg
      181 lvaavitlds lrgafpmlaf vnmlfvwcav qqfgffiadg ifagrsrgwf aglivgsnll
      241 lgfvtgigvy sgnmivdlnp pnfcmlllgl sqaatlqllr palawaagvr wirwmvtvag
      301 rrsmtvylwh lpllaamsgl llltdfpkpa agtaewwwar plvllgvlll llpvlllcgr
      361 leerptaash argrthvavv tagvmvfipv vdaafngltl tllaggaacf algvlllgrv
      421 pagvlspavp gapavplpep glranlds
//
LOCUS       WP_284754517             124 aa            linear   BCT 25-DEC-2024
DEFINITION  TadE/TadG family type IV pilus assembly protein [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284754517
VERSION     WP_284754517.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..124
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=12570
     Region          3..>97
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mprasergav avefailapl limlllgime fgraynvqvs lsnaaregvr vmaisndqta
       61 aktaaknaav slnpgladtn ftfsaascts gaqmsvtiky tlstltgiag pfpmqgvgvm
      121 vcgg
//
LOCUS       WP_284754538             157 aa            linear   BCT 25-DEC-2024
DEFINITION  heme-degrading domain-containing protein [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284754538
VERSION     WP_284754538.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..157
                     /product="heme-degrading domain-containing protein"
                     /calculated_mol_wt=16392
     Region          8..157
                     /region_name="COG4702"
                     /note="Uncharacterized conserved protein, UPF0303 family
                     [Function unknown]"
                     /db_xref="CDD:443737"
ORIGIN      
        1 madiatleal etlkrqeeel ifasfdhgda wrlgsrltgm aqaaghaigi dirrpglilf
       61 raalpgitpd qeswiarksa lvlrmeassa lvearlssag idpvasgwlg adyavtggsf
      121 pvrvhgvgvv aavtasglss qedhdliveg irqhlaa
//
LOCUS       WP_284754554             438 aa            linear   BCT 25-DEC-2024
DEFINITION  protoporphyrinogen/coproporphyrinogen oxidase [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284754554
VERSION     WP_284754554.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Pawelek,P.D., Cheah,J., Coulombe,R., Macheroux,P., Ghisla,S. and
            Vrielink,A.
  TITLE     The structure of L-amino acid oxidase reveals the substrate
            trajectory into an enantiomerically conserved active site
  JOURNAL   EMBO J 19 (16), 4204-4215 (2000)
   PUBMED   10944103
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440906
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..438
                     /product="protoporphyrinogen/coproporphyrinogen oxidase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006779 - porphyrin-containing compound
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=44467
     Region          10..438
                     /region_name="HemY"
                     /note="Protoporphyrinogen oxidase HemY/PPOX [Coenzyme
                     transport and metabolism]; COG1232"
                     /db_xref="CDD:440845"
ORIGIN      
        1 mtdvvvvggg vaglvtardl akggahvvlv essgelggmi rrhtvggidl dmaadsfatr
       61 tdavgrlaie lglgndvvap dprgawlmtr dgrtspipat gllgipstpm aadvlavvgq
      121 kgglraqmds llpapvgaka sslgelvrrr mgervlddlv vpiaggvhst hpdqldpdrv
      181 apglraallr egslaravls lraraaagtp vqgirggtvr lvdelvadma tygvdvrlht
      241 ratrieahav eivgadgtte rlpaqhtlss vadpertaap drtgiqlvtl vvdqpeldaa
      301 prgtgmlvhp daqavsakal thatvkwpwl advadgrhvl rlsyattatd pagvatslpv
      361 dptdpvgsra lqdastllgv aitadrvsga arvgwygpdl aaaglaegvv gigeastgrg
      421 lagiiaaark aadeilgs
//
LOCUS       WP_284754611             341 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284754611
VERSION     WP_284754611.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..341
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37003
     Region          45..331
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtlvkaktlr vgdgasavvv pdtappvykr rrkpltfdki sffvvflgvp laiyllfviw
       61 pfiqafgysl tdwsgfspkq nfiglqnyqk lftddifmka mgnnillvif lpiitivlsl
      121 vlatlvtvgg sskgqikglr nssfyrvvsf fpytipaiai gimwgqiydp sggllngilt
      181 slgmdqfksy awlgdkntam iatmfvivwg figfymvlfv agikgipael feaaridgag
      241 rfrtavsiti plirdniqta yiymgilald afvymaalns gggpdnstlv msqqlfftaf
      301 tkgqfglasa mgvvlavatl ifsglvflvn rltggdkdvs l
//
LOCUS       WP_284754628             178 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284754628
VERSION     WP_284754628.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..178
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19288
     Region          28..160
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mpltvvrreh vhlyarepes gvaktavdal lrlqhaedqq iesariesgl skneflavry
       61 mlqahrdgrt mgpkdlavml avsnasvtki vdgleqkgll srtahptdrr aqvlaptdra
      121 aekidasyar fhaavvevle qlpdtdnavl adsltkivda laagtpapvd eytvddqd
//
LOCUS       WP_284754632             407 aa            linear   BCT 25-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284754632
VERSION     WP_284754632.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..407
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42118
     Region          15..379
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msevanapgt pgaeiraaiv gcgvigrths aavrefpelv italvdvvae asealaakie
       61 aqgdpkptvf rtlaealaaa pvdlviistp sglhiqqale aldagkhvvi ekpldvdlsk
      121 adeilaaaka aeakglvatv isqhrfdpas rvvdearrag rfgtltsava svswwrsqgy
      181 ydsgawrgtw amdgggaimn qgvhtvdlll wflgrpveis aktallaheg vevedtavat
      241 vafesgalav lhattaaypg ltvrlqvmgn kgsavidndd layfhasdaa dpsessamgi
      301 lgggnqaave lakypddtve aldptvypag hvrqyrdiia airagrpagv tvrdavtala
      361 tvralyvsat lgqpvliddv iagkynnvev rtggtashpd areevsa
//
LOCUS       WP_284754646             463 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284754646
VERSION     WP_284754646.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..463
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=51534
     Region          1..461
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mkpsivwfrd dlratdnpal raaaddgaav alyvldeesp girplggasc wwlhhsllsl
       61 redlaalgvp lllrrgpvae ivretatamg sgslywnrry gepermldag iktsaresgm
      121 haesfqasll hepwavttkq ggpfkvftpf wrtvsgldfr epleapepgr gfsgqlpese
      181 eldtwgllpr npdwsaglse swqpgsaqah ellddflehg ladysvnrdr pdlpgssrls
      241 pflrwgqlsp fevwhaqqgr rrelgdgaav faselgwref cwhqyfhhpd latanlrpgf
      301 dhypwawpgg qgagspdaaa qettflrawq egrtgfplvd agqrqlwhsg wmhnrvrmvs
      361 asllvknlgv hwqvgeqwfw dtlvdadpas npanwqwvag sgadaspffr ifnpetqaak
      421 fdphgsyvgq wipelstady pepvvdlkas rrealdayas lpr
//
LOCUS       WP_284754713             454 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284754713
VERSION     WP_284754713.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..454
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=48126
     Region          32..406
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 msgyrgvsfw ldqlastgrd dltprppldg dttadvaivg ggltglwtaw ylhqadpglq
       61 ivvlereiag fgasgrnggw csalfprsas aiaeehgrda alalraamrd tvdevgraas
      121 eaevdcdyvk ggtvlyarsa vqeraahdev assatwgddm ewraarpgda agsagvawtp
      181 dcarvqpaal vrglaaalea rgvriaehtp vsswdrgrvv tsrgtvtagt vviavegyga
      241 qleqtkrril plyslmiata plpasaweri glehgqtfsd yrhllvygqr taddrlafgg
      301 rgaryhwgss itpgydrvpr vfehlrkalv dlfpvvadap vthtwggplg vprdwcasvt
      361 wdghvgsagg yvgdglsttn lagrtladlv rgestaltal pwvnhrspdw epeplrflga
      421 naglvatdla dreealtgrp slaarlmapl tggh
//
LOCUS       WP_284754799             240 aa            linear   BCT 25-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284754799
VERSION     WP_284754799.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Niehaus,T.D., Elbadawi-Sidhu,M., de Crecy-Lagard,V., Fiehn,O. and
            Hanson,A.D.
  TITLE     Discovery of a widespread prokaryotic 5-oxoprolinase that was
            hiding in plain sight
  JOURNAL   J Biol Chem 292 (39), 16360-16367 (2017)
   PUBMED   28830929
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Fan,C., Li,Z., Yin,H. and Xiang,S.
  TITLE     Structure and function of allophanate hydrolase
  JOURNAL   J Biol Chem 288 (29), 21422-21432 (2013)
   PUBMED   23754281
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Wang,L., Grau,R., Perego,M. and Hoch,J.A.
  TITLE     A novel histidine kinase inhibitor regulating development in
            Bacillus subtilis
  JOURNAL   Genes Dev 11 (19), 2569-2579 (1997)
   PUBMED   9334321
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005226
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..240
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=25667
     Region          5..233
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 mssltaapte iyesgdsalr vvalaeased nwltvhrlad wlescgaegl hgavptydsv
       61 lvefdpvlvs arqvrafvkl gllemgrsag seatprefdv pvvyggdygp dlekvaeyqg
      121 isteevirlh tektytvrcl gapagspmmd gpafpkpvpr lkdprlsvpa gavavagrqa
      181 viapasapgg wcvigqtplt vlnirreplv pykpgdilrf rrieagefds yvgkeleprp
//
LOCUS       WP_284754958             340 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284754958
VERSION     WP_284754958.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..340
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36673
     Region          1..316
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mdtqailqve nlqkhfpikg glfspkgski vkavdgvsfs largqtlglv gesgcgkstt
       61 grmiarlmdp tggrilidgv disqlggrdl ynfrrkvqmi fqdpfaslnp rqtvgtaiaa
      121 pmlaqkinpa gglknrvkel leqvglkpeh ynrfphefsg gqrqrvgiar aislnpsviv
      181 cdepvsaldv svqaqvvnll qeiqrdtgva yifiahdlsv vrhishevav mylgkvveqg
      241 treelfrepr hpytqallsa vplpdpraar qqqkirlrgd lpspanppsg cvfrtrcplf
      301 gtlgaelqqr ciseiprpas aaapachhag lesaapagvq
//
LOCUS       WP_284754988             481 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284754988
VERSION     WP_284754988.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..481
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50665
     Region          1..467
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mvdavvvgag pnglaaavtl araglsvevv erndtiggga rtaeltlpgf lhdvcsavhp
       61 malqseffrl frmeerielr lpevqyghpl dggragiayq dldrtaaelg vdgpafkqlm
      121 aplaenadqv adfatdallh vprhpltvlr fglraleqgt aawnlrfrge aapamvsgva
      181 ahsiqhlpsl staaaalslg syahargwpv piggsqaivd alaadlvahg grivtgqevr
      241 slgdltpaka vlfdtsvpgm lriagkqipt prrgalrrfr fgnaaakvdf alsdpvpwtn
      301 eslrkagtvh iggtrqeiaa aeravangqh aerpyvlgae ptvvdptrap kgkhvfwaya
      361 hvpagsdvdp teavtrqier fapgfrdtil ssssrtavqm geynpnyvgg diaagaasfw
      421 qlvkrpvlss dpwrmgggmy lcsessapgp gvhgmagwha aksalrhtfg lledvdltpe
      481 g
//
LOCUS       WP_284755038             324 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284755038
VERSION     WP_284755038.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..324
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34968
     Region          14..324
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msasrakmda magpsarmla llsllqvhrd wpgdelagrl evsprtvrrd vdrlrglgyr
       61 vealrgpagg yrleagsdlp pllfdddqav aialalavap asgadvaepa aralatvrqv
      121 mparlrsrvd avqavtatsr tttdpevlva vseavhlhev frfgygddet phrvephavv
      181 arngrwylld wdaarddwrt hridriaprm rtrvpftprp ipggdaaafv sarfkgsavd
      241 dvwpctgsvs mtaddarria pylpedavve qleddrarvt lgswswdgla gviaglavpi
      301 rvegpdalrr avralstrla taad
//
LOCUS       WP_284755105             555 aa            linear   BCT 25-DEC-2024
DEFINITION  GspE/PulE family protein [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284755105
VERSION     WP_284755105.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..555
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=60232
     Region          4..554
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 matlseilil ngalpiehld amtgdedlde rairglvdqg vvseaqfita raasnnsrtv
       61 plsdypvdgt avsilpaalc rrhgvlgvgf egdllilamv nptnvlaidd artasgraik
      121 plqveerdlv aaldrylrad delndltssl eeeasttska qvdiadgald dvpivrfvnl
      181 lvsqaiqdqa sdihiepgeh evriryridg vlhemapapk niqngvisrl kimsdidiae
      241 rrkpqdgrms vrhggrqidl rvatlptvwg ekvvmrildn tntsltlkdl nlleqnfqay
      301 qrsyskpygm ilvtgptgsg ksttlyttln avakpeinvi tvedpveyrm aginqvqvnp
      361 kagltfasal rsilrsdpdv vllgeirdhe taqiaieasl tghlvlstlh tndapsavtr
      421 ltemdiepfl vgsaldsvva qrlarrlcdr ckapavyeie qlralgflap gdempaffap
      481 vgcavcsntg yrgrialhev mtvteeierl avgrassaei srvaqqqgml tlrqdgfekv
      541 klgmtsvdei lrvva
//
LOCUS       WP_284755137             474 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284755137
VERSION     WP_284755137.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 474)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..474
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=50466
     Region          16..461
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mtppielltt ataeryrsav tstvdrladr faaadrpttd tapevlrarv qdvdldaepl
       61 gtdralaeld elfvreavwf hdpaylahln cpvalpavaa esvlaavnps vdtwdqsrig
      121 teierhvvaw lagrigfaag dgiftsggsq snlqalllar ealgtsgtvf ttaethfsia
      181 ksarllglea vvavatdhag rmvpaalaea iaaaraagqt pmavvatagt tdrgvidple
      241 piadvcdleg vwlhvdaayg cgllvsptrr hlldgverar svtadlhksf fqpvsssall
      301 vqrpedlrrt awyadylnpe daaepnqvdk slqttrrfda lklwatlrat gadaigsafd
      361 avidlavvth riveehpdlv lvaptqlstv lfrwqpagmt deaadalvap irsallaegr
      421 vliaktvidg rpcnkltlln pettpdqmra slehvvataa rvratttkte ganr
//
LOCUS       WP_284755159             363 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. efr-133-R2A-120].
ACCESSION   WP_284755159
VERSION     WP_284755159.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..363
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39423
     Region          36..269
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtqithllpd sravgtgelp etrlgvqftr ypghedrplv eslraalddg ftlvvlnsia
       61 aelsgeapde lnevaeearr advelqlglg cagpfvdpar iraglnrtla rglelgvtef
      121 fvytrsvreg aveqgrfldh paqlrliran lealapaard akvrinvkth edlaspevqt
      181 lvqaldpavf gigfdvanlv vrgedpveaa rvlgpqvrmt hledavlfpl phgyrrrlra
      241 igegvfdwea ilghlfragv rdftleqhrg kfdapvfdrs wfthephlda aglgqlarlg
      301 vathdgvarg hipaladwdd epapaerrrq llhsaatvrt iltsigagvk klatilsgee
      361 gls
//
LOCUS       WP_284755173             449 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: cryptochrome/photolyase family protein
            [Curtobacterium].
ACCESSION   WP_284755173
VERSION     WP_284755173.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium
  ORGANISM  Curtobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Curtobacterium"
                     /db_xref="taxon:2034"
     Protein         1..449
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=51185
     Region          1..447
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mtgaivwlrd dlrlsdnpal raaidhggdv tvvvvldeqs pglrpigaas rwwlhqslta
       61 ldadlrergs rlvlrrgaaa tvidqlvadt gadavywnrr ygaverdida giktalhdrg
      121 veahsfaanl lwepwtvltg qgepykvftp fwnavqalpe prhplpdpdd lpapadvtgd
      181 aladwallpt kpdwagglrd awtpgehgaq qqlehfveha ledydqrdep ameatsslsp
      241 flrwgeispy qvwhrlherl epaqrqnaaa flrqlawref nwneyfhcdd iatvnvrrnf
      301 dafpwrdpea aeldrwrqgl tgfdlvdagm relwhsgamh nrvrlaagsf lvknllvdwr
      361 vgeqwfwdtl vdadpannaa nwqwvagsgf daapyfrvfn pdrqlerfdp hreyvhrwvp
      421 adelrpepmv dlkasrqral dayermrrs
//
LOCUS       WP_284755223             257 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NUDIX hydrolase [unclassified Arthrobacter].
ACCESSION   WP_284755223
VERSION     WP_284755223.1
KEYWORDS    RefSeq.
SOURCE      unclassified Arthrobacter
  ORGANISM  unclassified Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 257)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19108954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="unclassified Arthrobacter"
                     /db_xref="taxon:235627"
     Protein         1..257
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27460
     Region          32..206
                     /region_name="NUDIX_AcylCoAdiphos_Nudt19"
                     /note="Nucleoside diphosphate-linked moiety X)) motif 19;
                     cd18870"
                     /db_xref="CDD:467582"
ORIGIN      
        1 miqqnvtqqa gkgavlagmg eansttvaep rlaasvillr daavpgrsgd aaqalevfvq
       61 hrvstmdfaa gmvvfpggrv dqadssgwdf tddvverhaa awhrssiave pssarfnagr
      121 vlaaaqrevf eeaglkldaa tlrpwanwvt ppdqpkrfdt yfylacpvsg aeprhqttea
      181 ssslwmpvrg ildaeaagtl klmpptlall dellalgtve avlaedrdiv pvrpkpgalq
      241 effrlrrqap svapelp
//
LOCUS       WP_284755253             406 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284755253
VERSION     WP_284755253.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..406
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42077
     Region          155..388
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mlgipthlap rvnawstvra fhagaigsll aaaitlvlyg lsepgvqvvg talavvpmla
       61 migvhvqfgt rvsaiaflav ggvcawwfav gvqqqvptgw vtsylmslvv iplilvggag
      121 avpsrvvlws fvgfltgrla twiaivqadq sprplilawv tlgfvvalvl fttrstgrse
      181 rvqpellrsa reehvsayra gveaeasail hdtvlnhlga ialapdgpmd phlaetvdad
      241 vavltgkgwl apaarpspga aaeafgtmvd ehrtlgldvt vsgdtsaler ldqralsavv
      301 ravgqclanv rkhagtdaae vsvfddsasc tvmvvddgrg fdedatgadr mglrgsvrer
      361 igrvggdvqi wsspgsgtsv mmtvpygpvt gavtvpavsd grgter
//
LOCUS       WP_284755293             209 aa            linear   BCT 25-DEC-2024
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Arthrobacter
            sp. efr-133-R2A-120].
ACCESSION   WP_284755293
VERSION     WP_284755293.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..209
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=21389
     Region          70..205
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
ORIGIN      
        1 mgggatqgdg lkayirtgsf hvrtigslsl laasamllas caysepapsp sispspqaav
       61 asassssapl pevagkvsls syklpvkytt vagdtwasia kafelkeesl kafqakaida
      121 epapgtvvdl rgvdyqrpga sgeyekdasg qpdvyivqag dnpgavaarf gipvrqlvtd
      181 nklpgmfsls pedtasfkpg mklklqnps
//
LOCUS       WP_284755295             521 aa            linear   BCT 25-DEC-2024
DEFINITION  chitinase [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284755295
VERSION     WP_284755295.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10158442
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..521
                     /product="chitinase"
                     /calculated_mol_wt=54737
     Region          48..356
                     /region_name="GH18_PF-ChiA-like"
                     /note="PF-ChiA is an uncharacterized chitinase found in
                     the hyperthermophilic archaeon Pyrococcus furiosus with a
                     glycosyl hydrolase family 18 (GH18) catalytic domain as
                     well as a cellulose-binding domain. Members of this domain
                     family are found not only in...; cd06543"
                     /db_xref="CDD:119360"
     Site            order(52,78,123,159,161,163,233..234,285,319)
                     /site_type="active"
                     /db_xref="CDD:119360"
     Region          391..437
                     /region_name="ChiC_BD"
                     /note="Chitin-binding domain of chitinase C; cd12215"
                     /db_xref="CDD:213178"
     Region          459..505
                     /region_name="ChiC_BD"
                     /note="Chitin-binding domain of chitinase C; cd12215"
                     /db_xref="CDD:213178"
ORIGIN      
        1 mskrfpgrrl svlrlgilcv ivvaavtagy lglrnvqdvs aaasmpsvfs gyvdvtatpr
       61 fafedpavps akavvlsfvv adpkqgcaps wgaayspdqa asdldldrri arlrqlggat
      121 avsfggmnnn elavsckdtk altdayrqiv drydvatvdl dvegvalgdi aaadrraqai
      181 aalqkerkas gkplavwltl aadpdgltsq gqvivahtla ggvelegvni mtmdfgaskp
      241 aawsmsraae saadaahgql aalyrnagtd fgsetlwrkl gltvmvgqnd iageiftldd
      301 aatmnsfvkd kglgrlsmws mnrdrtcspn ypdlskvsds csgvvqgsql fsatlandva
      361 lptpavvpsp tatastsatp ttddpatspy piwstyaayt aadrvvwhgs vyeakwwtra
      421 dvpdnpvlqg gatpwklvgp vlpgdrpspk atvppgtfpa wapetiyhkg drilfegsaf
      481 eakwwtqgds peaaiqgapd spwakltpaq iltpspttpa p
//
LOCUS       WP_284755317             264 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284755317
VERSION     WP_284755317.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426811
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..264
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28589
     Region          13..261
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mgaevldlrl ttgiripciv hgdadakpll llhawgesrr sfdrllplvt dfrvyapdlr
       61 gqgdaekpeh gyslieqaed aaaildalgv hrafvlgsss ggyvaqqlai gypdrvaalv
      121 lvgtplslrg rpafadqvat lqdpidedwv rnslawfpll haipawfied rvrdgvrmpa
      181 hawkrildgl rtatpptesg tilaptlilw gahdavlprr hqealaarip gavlkvypgv
      241 ghlvlwecpd qvaadtaafl npld
//
LOCUS       WP_284755318             430 aa            linear   BCT 25-DEC-2024
DEFINITION  lipopolysaccharide biosynthesis protein [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284755318
VERSION     WP_284755318.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..430
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44559
     Region          12..375
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mrssprrrlp aiatilvgtv lgqglvvais plltrlytpa dfgtlavvta vasilgagat
       61 lgtdralvva hdrvttdalv tlgllstlvv gagtawaawv lrgdaarwft apaledlwwt
      121 vpvtvvavga qriasavlar rqqhrsiavr nacqgigqsv wnlamaaagp vglvgglavg
      181 riaavlgmar frrsdgerit pralssaarh hrrflvitpw ssmlnvvgqq apglliaalh
      241 gsvaagfval tmrvlgapvg mvadataqya agafglrirs adpvrgllvr lvvrlalaga
      301 vaavvvvllg pavfstlfgp ewavsgtyaq vlvpafaiqv avspvtqvls mlqrqgaqla
      361 wdgarlalsa savlvpsllg apmlvvllsl asamaisyaa vllmvlraar ihdrgasgrr
      421 atrrrreydm
//
LOCUS       WP_284755348             904 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284755348
VERSION     WP_284755348.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 904)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 904)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 904)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 904)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..904
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..904
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=98505
     Region          10..>662
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mtlereelrd dwtvtlaggt gapdgvagrt ipatvpgqvh tdleregllp dptfhlneqp
       61 akwvgradwa yrrtvdvdpr ghervdlvcd gldtvaelsl dgvvvgttrn mhrryrfdar
      121 vqtgsggttk dleilfespy reagrvaaka gsmpgpydep fpyvrkmasn fgwdwgltav
      181 tsgpwrpvai erwstarlre vrplvdveag egvldahitv ersgmndldq dgedddlvlv
      241 vtvsgetedg gttrqrsraq ltpkddetvv tvrvpearrw wprgygaqpq ydvvvelqtv
      301 dgevldrdtf rtgfrstrie tqvdgigrpf avhvngtlid vrgvnwipdd vivsrvdrar
      361 lesrlgaaas lgtnlvriwg ggvyesrdfy evcdelgllv wqdfpfacsa ypevepirse
      421 viaeardnva rlarhpslvv wngnneniwl hdadgwgeel gdrgwgldyy ldllptivda
      481 vdpsrfytva spwsgseslp anevdhethh swdvwnrlpd tayresvprf vsefgwqapp
      541 awrtlrdavt daplrvdspg vvhhqkaadg maklarglep rfgavdpaaf dawhyltqlq
      601 qaraiatgie hwrthwprnt gvvvwqlndl wpvsswsaid sagrlkplah elrrlyddvl
      661 ltirpvssva vtpgaastag aagtagasga vaasgaertg gpdhpgaspa vgetadlgel
      721 adtlslgvsp gafgsspvev avrstrtghd svvrvrritt agtilaeasl pvrlssagva
      781 vvalpesvgv vddpanelvi admdwrravw tpgpdaemrw eparyrtsfa vvdggldltv
      841 eadslvrdll vqpdrvaagg tvdrgfmtll pgervvfrlg gvteadipal reapvlwsvd
      901 gvlr
//
LOCUS       WP_284755408             296 aa            linear   BCT 25-DEC-2024
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Curtobacterium
            sp. ME-Dv--P-122a].
ACCESSION   WP_284755408
VERSION     WP_284755408.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..296
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=31786
     Region          122..223
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mtttaparvr rrrwpvppsl llglapivvf aaisawrsrp sddyatlgqt vdsvvhalvi
       61 pegiavvala lfvtalgwwr iatvdpvrtr lrwtmlapil vlvvcvvrlp lidwtalpah
      121 yflllavgvl fvgvfeelma rgtllvglrr rlpemgvwal scalfgllhl lnalagagig
      181 ptliqvvfaa sfgstlyvar rltgsllapm llhafwdfgs igfsatsdpg dfgkltllgl
      241 iglfsfgvla fgivaggiia wyddrprrla krwrtvppmg avvvpggepr lpadvv
//
LOCUS       WP_284755465             189 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase [Curtobacterium].
ACCESSION   WP_284755465
VERSION     WP_284755465.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium
  ORGANISM  Curtobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Curtobacterium"
                     /db_xref="taxon:2034"
     Protein         1..189
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=19741
     Region          26..163
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mirgmltgir rrrwfralpt tvacerglrf garvrlwapt sltigsdvhl gsdvrievdg
       61 sigdavlian raaiigrrdh dmtvvgvpit aspwvgdtpa lsavttigsd vwigfgaiil
      121 sgvtvgdssv iaagsvvtqd veantvvagn pakvlrprfr egelsahwda lrgqgvrlav
      181 deaagapdv
//
LOCUS       WP_284755477             137 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284755477
VERSION     WP_284755477.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 137)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 137)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..137
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14703
     Region          28..118
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mavreaadec gvklvdpdkv elvraalpsd hdiaeladvf sllgdpgrlr lltsllegge
       61 lcvcdlaatt amtesavsha lrllrahrvv svsrrgrmay yrlddahvrm lldlglthtg
      121 htvavhpert akkdggq
//
LOCUS       WP_284755491             288 aa            linear   BCT 25-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284755491
VERSION     WP_284755491.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Bagautdinov,B. and Kunishima,N.
  TITLE     Crystal structures of shikimate dehydrogenase AroE from Thermus
            thermophilus HB8 and its cofactor and substrate complexes: insights
            into the enzymatic mechanism
  JOURNAL   J Mol Biol 373 (2), 424-438 (2007)
   PUBMED   17825835
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..288
                     /product="shikimate dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30043
     Region          7..277
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 maftdpgrth lavlgspiah slsptlhaaa ydaldlpfty grhevasgel aafvaglgpe
       61 wrglsltmpl krevlplldr ttplvdelgv antvafrheg stlvragant dvqglvrpve
      121 alghlpgeat vlgggataas altaavrlga slvrvfvrdt akthalvdla vrlgvtlevh
      181 plaelagthh gfvlstlpgg aadplefrps gldavlfdva yepwptvvas rwteaggrvl
      241 ngldmlteqa igqirffltg dedellpdea gvrramrtav dlpavigs
//
LOCUS       WP_284755505             996 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-mannosidase [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284755505
VERSION     WP_284755505.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..996
                     /product="alpha-mannosidase"
                     /calculated_mol_wt=110110
     Region          248..996
                     /region_name="MngB"
                     /note="Alpha-mannosidase [Carbohydrate transport and
                     metabolism]; COG0383"
                     /db_xref="CDD:440152"
ORIGIN      
        1 mhddtsltig rvkrvleeri lpaihsasvp laveiheldg epispadgla ldyapwcvga
       61 pwgpawgttw frltgrvpae wagrtveavv dlgfdvnmtg fqceglvyra dgtpvksinp
      121 rnqwvpiaep adgdepvely leaasnpvll dyhpflpthe gdiltssaep lyrarrmdlv
      181 vfekevfels ldldvlfelq aelpdtsprr mrilqamdda ldaldlqria ataadarakl
      241 avvlaapaea sahrisaigh ahidsawlwp vretirkvar tsssmvalle eqpefqfgms
      301 saqqyawlke hrpevfervk aavaegrflp lggmwvesdt vmptgeslvr qfshgqrffe
      361 refgfrskgv wlpdsfgysp alpqlmrrag fewfftqkis wnqqnvfphh tflwegidas
      421 qmfthfpsmd tynsqlsgme vakasrqfke nrvssrsiap vgwgdggggt tremtgrarr
      481 lqnlegsaqv vwehpdvffd aakaelphpa vwvgelylel hrgtltsqhg tksrhrraeh
      541 alieaelwaa tdavrtgtay pqaelehlwq qvllhefhdi lpgtsiawvh reavavledv
      601 idraraisda arrslagegd relvfsptsv agplplgatl avasddrvtl ddsgegivle
      661 nalvrvrisd eglivsavdl gtgrdavadg raanllqlhq dfpnmwdawd idryyrnsvt
      721 elrdvtsics rlteagaevv idrtfsksti tqtitlapgs rtlhivndid wnetekllkl
      781 afpldvqaah seaetqfgyq srvthtntsw eaakfetsmh rfvlvreadf gvalvndsiy
      841 gydtsrevad dsvtttvrls llraprfpdp eadhgrhvit igmvigagpa eatragieln
      901 apgtvvrggh dvaplvsvqg egivvsgvkl addgsgdliv rvyeslgrrt ngelsvdfph
      961 revrevslie daldearlgg elrlrpfevr tlrvvr
//
LOCUS       WP_284755506             327 aa            linear   BCT 25-DEC-2024
DEFINITION  HNH endonuclease, partial [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284755506
VERSION     WP_284755506.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         <1..327
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
     Region          <48..224
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          208..267
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 rlnewratll vketaclsae nrcavdeela adtgtfdgag drtiisiara aayrrdprsv
       61 tqrashaate rhvslrpapd tmtyltalvp vaqgvavhaa lsrhadtlrn tgdtrtrgqi
      121 madalvertt gtpggisgvd iqlvmtdrtl fqgdseparl tgygivpagw arellsages
      181 egsrelklwl rrlytapgtg dlvaadsrar lfpaglrrfi qarddtcrtp ycdapirhfd
      241 hvvawqaggp tsqangaglc escnytkerr gwtartrpgt rhvveirtpt ghhyqstapp
      301 lpgtdppirr hripdtigan yatkprr
//
LOCUS       WP_284755514             437 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284755514
VERSION     WP_284755514.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..437
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=46242
     Region          58..338
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mstsqglpeq anstadvrgi iakrdlvvdl irtacvvlvv ivhvtmvgva addqgvrvts
       61 plqelpwyva atwvgqvmpl ffvvggfasa vgwrstvarg apspardyla irlvrlfrpa
      121 vplfvflalg lgvataagtp pellaevafg igsplwflaa ygitqccvpv mmrlherapw
      181 atlavllvla gavdavrlat gvaevgllnl gpvwlfaqql gflwadgwfa rrskvlllgi
      241 avvayavlvp mtsvglwapd mlqdlnppml plaflaiaqa clvqlvhapl trlmrtraal
      301 gavfvlgrdg mtiylwhlpl fialngiall vgvpfpapgs gpwwasriva lvvvlavaig
      361 varalrwfdr plprllpsad rpswpvvava alctigpafl vmqlhlsfav alvgavavpv
      421 gvwllsrtvp apgvari
//
LOCUS       WP_284755517             156 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284755517
VERSION     WP_284755517.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..156
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16917
     Region          31..128
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtehaeavag rnldpvtqwg lviegfqitn rklhravaaa fsldpaetet llrltrsper
       61 rmsmaalare aafstggftk iadrlakrdl vvrtpcaddr rvvyleltaa gvkladelqn
      121 lvadivrkty idvlgadraa vvaeamaelr eanstl
//
LOCUS       WP_284755539             410 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Curtobacterium
            sp. ME-Dv--P-122a].
ACCESSION   WP_284755539
VERSION     WP_284755539.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..410
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=43386
     Region          15..397
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mqpetamsvp attgahavrr aaliaaldvv dggveerfer itriarealg vsgsflnlag
       61 ettltiksqq sdaafgpvip lqdtfcgrtl geqgpvvvpd arvdaryadl pmvlgdpnvr
      121 fyagvglrag dddlkigtlc lidpeprtld adelellqel giwaerella gadedrlrtv
      181 lnglqpaevq vpgyritgms iphglvsgdf hdwhrsgeds vhltvsdvmg kgmsagllaa
      241 nirggllarg dqdpgtavae leaqvapels raesfatmfh grltpstgrl dfadaghglv
      301 lqlrddgaer ilrssdlpig lhpagmpraa gslvlrpgdv livvtdgale lwdstlaals
      361 elgslyresp dvetflqrvr arvaehdpgd dltvvvvare avgaleales
//
LOCUS       WP_284755577             192 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284755577
VERSION     WP_284755577.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..192
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20442
     Region          43..165
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtdtdpvvlp phapavptar vapstppapm spdvtaldpv tvdtdpdadl prlltafrvl
       61 qmqharvlhh estsrglnat dtrfvfflna agghgvtpkq ageylelttg amtslidrle
      121 khghlerrpn pedrrsvllh ltpsgtavar evgavysqaf qqvvapsdra vvaaafegfa
      181 aalerhhrss ta
//
LOCUS       WP_284755592             382 aa            linear   BCT 25-DEC-2024
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Curtobacterium
            sp. ME-Dv--P-122a].
ACCESSION   WP_284755592
VERSION     WP_284755592.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..382
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=41027
     Region          180..269
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 msvpyqrlpr idgrwrwwrp lvalaflagw ylvsqiviav ayfvpilraq gadgliqlqn
       61 dlasgaldpt dpvvlsmslv slvvllpgil lavkiarigp agilsstrfr vrwawtawcl
      121 lptlviaafm fvwqtglfwd ggmittdggf awnhdaigqs tvslgtlslt ivlvvllvpf
      181 qgaaeeyifr gflmqtvasw iprrvgtvia vavstvvfav lhipngynvw gildvgsfgl
      241 iaaiivlrtg gleatvlqha fnnimifvlq apgwsgidlt ssdangtwqg tlvtlvtsla
      301 fwgmveflaw wrgldrrfag heaprfrgvt pawaggvrwt rpggtgwatt paraddvagp
      361 dhragsgtdg avdsavgvag rp
//
LOCUS       WP_284755608             300 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284755608
VERSION     WP_284755608.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..300
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=33460
     Region          11..274
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mrrgddrgpd rvvlgdaldv vpaypdgsft lvyldppfnt gryqrrhats avpkadgpvm
       61 gfhgrtyerv rgdlmrfddr fedywsflep rlieawrlla tdgtlylhld yreshyakvl
      121 ldalfgresf lneivwaydf gaksktrwpt khdtilvyvk dpsrywfdse avdrepymap
      181 glvtpekrer gklptdvwwh tivsptgrek tgyptqkpeg vlrrivqass regdwvldff
      241 agsgttgava qalgrryvlv ddnpaaidvm rkrlpgasfe vaaagagags aaagdaapav
//
LOCUS       WP_284755634             362 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284755634
VERSION     WP_284755634.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..362
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=39447
     Region          1..71
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          168..270
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mtaeigqrva gllpegrtqr evaadvgmtp dafsralrge rgfaaielak ladvlgadlh
       61 flitgapdpn rvvasarhsf dqetrqhhip gkdvdlpqle avllayeqvq gdlpnssvpt
      121 slsearaalg dgfirpfadr ldalgidvvr lgdltsaysf wfggravivl katgnwfwen
      181 wslahelghl ttqaddierg rgiertsner danafaaell lpaewmrsvd wasaseaqva
      241 syvwdrgvsi dalakrvaal hlttsknlel wmgqptqrll rrrwtatepg dpitarmdaa
      301 strrfplslq dahlariadg kvrkdtlawm lgvdptelev depsdettlt sdalsdllgl
      361 gv
//
LOCUS       WP_284755652             375 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284755652
VERSION     WP_284755652.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10617647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..375
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39254
     Region          19..315
                     /region_name="Pyr_redox_3"
                     /note="Pyridine nucleotide-disulphide oxidoreductase;
                     pfam13738"
                     /db_xref="CDD:404603"
ORIGIN      
        1 mpaphptetl dalvvgagpa gvgtglalha vdgllfgvve rgvvgdtfrr wpehqrfltp
       61 sftgngfgat dlnavhprts payslgtdyp sgpeyarylr gvvaafhlpt lldteverie
      121 pdddgfrvtt srgpvitrnv vwaggefsdp ilprcagtsl gvhasaeaaw varsghvvvv
      181 ggfesgidla chhveqgatv tvvdpshpwd agsgsdpsfr laprtrqrla aarasgrltl
      241 vddgqvtgik rsgdgftvgv agrtalvada ppilatgygp glgpaaslfd tradgwpllt
      301 eddestttpg lflagtalrh gglqfcfvyk frqrfahvar vigeragrdc salqewddag
      361 mltddlsccg vecac
//
LOCUS       WP_284755695             510 aa            linear   BCT 25-DEC-2024
DEFINITION  lipopolysaccharide biosynthesis protein [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284755695
VERSION     WP_284755695.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..510
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53189
     Region          51..444
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 msfppqtrre araareaeva apvplaaepi apvpesldtg siavrkgasv lfgrgllyvv
       61 vwsmqlvvss lispvlahlm ppaefgvlas aialyqalvv lavlgidqas vlqraedgdd
      121 rrargllavg mvtaivvtva alttipvwad aagfvgnhpl llvavlwtgp aaivqislal
      181 lvaqdrirvf avtsllssig gsaiglgllt wvqadattya wggvvaqgva mvigiaatrp
      241 rlaglfdrkt tarafrlgvp ialgnlsyfv lnagdrivvq rllgpdevar yqiayvvgsa
      301 villltftnq awaphfaalr dpvarrqlam hsrdelykml gpvllavtlv spvalpilap
      361 asyrvqelsv vvfvvaitaf pvvasgatgr lllverrgva vgviaaiaga vniganlvlv
      421 pvlgiagagl atvvayaila amqllalpdr rewrgpgari vlttlaalvv aaaslllpqd
      481 vlwnwvriag vvaclpwflr rlktarggvs
//
LOCUS       WP_284755737             339 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284755737
VERSION     WP_284755737.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..339
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=33867
     Region          7..337
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mnprsrtall gagvvilfav tvllgsytvt ipdffriiav qlaggekipg asfivmenkl
       61 pravlgilig vafglsgglf qtmlrnplas pdvigisyga saaavlaivv fgasgaavsa
      121 aalagaigva vviyaisrgg sgsrrtnaag nrlilagvgi aaalgavvnf lmtwadirta
      181 sealiwlngs lnsanwervg vllaslavlv palallagpl rmlelgddaa aglgirvnav
      241 rfglvitava laavataaag pvafvaflag piarrvvgwp slpasaftga livlaadyfa
      301 ynvaplilag tvlpvgvitg algapfllwl latsnrkea
//
LOCUS       WP_284755834             417 aa            linear   BCT 25-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284755834
VERSION     WP_284755834.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..417
                     /product="metal-dependent hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44014
     Region          7..>65
                     /region_name="AdeC"
                     /note="Adenine deaminase [Nucleotide transport and
                     metabolism]; COG1001"
                     /db_xref="CDD:440625"
     Region          47..383
                     /region_name="Met_dep_hydrolase_A"
                     /note="Metallo-dependent hydrolases, subgroup A is part of
                     the superfamily of metallo-dependent hydrolases, a large
                     group of proteins that show conservation in their
                     3-dimensional fold (TIM barrel) and in details of their
                     active site. The vast majority of the...; cd01299"
                     /db_xref="CDD:238624"
     Site            order(63,65,224,244,316)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mttperltir nalifdgesp eliegsisir dgriiavgre veetgavlda ggrtvipgli
       61 dahfhayals ltsarnetgp lsysalvgar rlaatllrgf tsvrdvaggd vglasaieeg
      121 lypgpryfft gpalsqtggh gdirpandgg cfhgghmcev vdgaedllrt vrhrfrtgas
      181 aiklmtsggv vspvdpirvp qysaaeirvv teeasrrgsy atahayspea irhsvlngvr
      241 ciehgnllda etaqlmannd vylvptlvty eamerrgkev gltevgaakn revleagrna
      301 valardagvr igfgtdlmge ledeqlaglr lqcevlgvyg alrsatstna allrrgdlgr
      361 iavgfcadlv vldgnpfcep silwdesktr tvikdgqiis tgalrgaadl tlnvpva
//
LOCUS       WP_284755880             324 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284755880
VERSION     WP_284755880.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..324
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34986
     Region          29..320
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtstsiaesv krarrgvgpa gagrkpgpap agrarkrftp rtwtliafaa pslillllln
       61 vyplvyaliq alhdgtllet gpfvglknfg dvlalpsfws atsftvvftv vgvfgswlvg
      121 lalslllrth ipagglfkvl lllpwivptv vsatswnwlv atpqspfpvi aehlgfgnvl
      181 fladpmlaqv vvclfkvwis fpfmmmmmss alasvdtnvy eaakvdgatg wqsfrlitlp
      241 liarttfvsw ilmtifcvnd fptiflltgg gpahattslv llayltvfqn fqtgpgvaia
      301 flmtfvlvvi svvlyrqirk vnve
//
LOCUS       WP_284755883             365 aa            linear   BCT 25-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284755883
VERSION     WP_284755883.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..365
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38913
     Region          4..348
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mgvpltvgvi gvgkiseqyf eslpklpglk lvavadinee rahevaaeqg vealtvdell
       61 ahdridsiin ltipaahvev gtralhagkh vfaekplals peealpmlel adslglrvgs
      121 apdtvlgtgv qtalqllnsg aigapvaaqv hwsapgherw hpsplfyyqp gggplfdmgp
      181 yyltslvmff gpvvrvsgva trsdrartve tgplagtpip veidthvsai lehangvttt
      241 itvsfevwat rtplfeiygt dgtiavpdpn lfsdpvelvt revperrevp tsagyedagr
      301 gygladmara ietdrphras grvafhvlev mdaitrasre rrvievdstv drpavvpfga
      361 apdtw
//
LOCUS       WP_284755963             320 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284755963
VERSION     WP_284755963.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 320)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..320
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33927
     Region          24..318
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mtttlhkpae lqqtvppagv trpkrlgqra vgffmalppi lliaifvgfp ivlafgfsig
       61 ltgglnhtia tigqnvhead awwgtlaayq emftnkrflg dllvtvivtl vstatvifla
      121 lgiglylklk ggrmarllsg laivplfipv viaswailtf ysgtgflrsv falfgvdfpv
      181 waftmvtvii gsvwtslpfa vlmvssglqs vpnamieaar dagagslrti vsvivpmaav
      241 piiiattfta igivgsftvp yftgpnspnm lgvdmsnyfs afnqpqqsav maftvflias
      301 giaalyvwan frsakeqgka
//
LOCUS       WP_284756017             316 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284756017
VERSION     WP_284756017.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 316)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..316
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34273
     Region          21..313
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mstsvrrtel pltvrtpthe plnrrrrstp grapatklfl ilpsvvilil tnaypiayaa
       61 fqalhngsli spgefvgvdn fakvladpaf wraagftavf avagvfgswi igiaialllr
      121 tripakgllk tilllpwvvp ivvsamswnw ligtssspvp tifhalgfgd aiflsdplga
      181 qitvclfeiw vnfpfmmlmm saalssvdes iyeaakidga gawqqfrymt lpiiakptyi
      241 swvlmaifcv ndfptvyllt hggpvgatnt lvvlayktvf qnfqtgpgva iaflmtlala
      301 ivavllfrqi rkstsq
//
LOCUS       WP_284756081             243 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284756081
VERSION     WP_284756081.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..243
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25903
     Region          2..211
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mkiavfgang ptgriltaqa ldaghvvtav trrphefpis apglsvvgad vynfeyvsav
       61 vegsdavlst lgvpysrqpi tvysvgtgni iramgnhgvr rlvcvsssat dttagphggf
      121 lfekllqplv tkllgktlye dmrrmesava asgldwtimr psglfetdsv teykmavdyi
      181 ngtftsradl adsmlrqlts defvrknvav atfsqkpsli qllfreassk kaapdsvpeg
      241 kls
//
LOCUS       WP_284756147             396 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284756147
VERSION     WP_284756147.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..396
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42626
     Region          72..390
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msrittgqsr vtvdnwqepa nlpwsflhmd elfanaaira vakdsasplq rampedplgl
       61 rgvvvrlpdg sdrtveevla atstdawmvl hgnevlveey fgamshdtrh llmsvsksiv
      121 ssvvgvlvaq gkidtaqpie hyvpelrasg yggatvrdil dmrsgikfse eyldassevr
      181 kldeavgwap rnggagtlke flltleqvre hgghfeyrsc etdvlgwlce aasgkqfael
      241 asevlwsrmg arhdafisld aagtgmfdgg icatlgdmvl fggmirdggv slnderiles
      301 dwvddiftgg pdsatafaag dhaeempggk yrsqfwflsd dadtayclgi hgqmvyinrr
      361 sgvvgvkfss talpvdpaag paaaamfeai srrltp
//
LOCUS       WP_284756154             213 aa            linear   BCT 25-DEC-2024
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284756154
VERSION     WP_284756154.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..213
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23055
     Region          8..205
                     /region_name="YdeN"
                     /note="Predicted esterase of the alpha/beta hydrolase fold
                     [General function prediction only]; COG3545"
                     /db_xref="CDD:442766"
ORIGIN      
        1 msrprpwviv pgiwnsdpdh wqsvwereqq derdehgqrd ehgqrdqrdq yqqraavria
       61 ptswsdpdpd dwraaistav ascteppvli ahslgvlava dwlattadas tlvagaflva
      121 ppdplgdtfp deasgfvapr pvpsaqrvpt rlvvsdddpy csadravvfa damgadvvrv
      181 galghvnvas gvgdwpagre llrafedglr ppr
//
LOCUS       WP_284756197             326 aa            linear   BCT 25-DEC-2024
DEFINITION  GDP-L-fucose synthase family protein [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284756197
VERSION     WP_284756197.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..326
                     /product="GDP-L-fucose synthase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35662
     Region          21..318
                     /region_name="GDP_FS_SDR_e"
                     /note="GDP-fucose synthetase, extended (e) SDRs; cd05239"
                     /db_xref="CDD:187550"
     Site            order(24,26..29,50,53..56,76..78,80,100,119..121,150,154,
                     177..178,180)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187550"
     Site            order(97,121,150,154)
                     /site_type="active"
                     /db_xref="CDD:187550"
     Site            order(121,150,179,198,215,223)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187550"
ORIGIN      
        1 mkvkswteft pgkldrssif yiaghrglvg saiwrnleae gfdklvgrts aeldlknred
       61 vfsffeatkp ryvvlaaakv ggilanstyp vdflsdnlri qvnvldaale ygverllflg
      121 ssciypklae qpiredsllt ghleptnday aiakiagimq iqavrrqygl pwisamptnl
      181 ygpgdnfspe gshvlpalir rydeavrsga rtvtnwgtgs prreflhvdd maaaclylle
      241 nydgpaqvnv gtgtdvtire lasivadavg yqgdmlwdts kpdgtpqkll dvsqlaqsgw
      301 sssiglkdgv rqtvdwfran vgdvrs
//
LOCUS       WP_284756322             467 aa            linear   BCT 25-DEC-2024
DEFINITION  xylulokinase [Arthrobacter sp. efr-133-R2A-120].
ACCESSION   WP_284756322
VERSION     WP_284756322.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437490
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..467
                     /product="xylulokinase"
                     /EC_number="2.7.1.17"
                     /GO_function="GO:0004856 - D-xylulokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0005998 - xylulose catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0042732 - D-xylose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49278
     Region          6..410
                     /region_name="XylB"
                     /note="Sugar (pentulose or hexulose) kinase [Carbohydrate
                     transport and metabolism]; COG1070"
                     /db_xref="CDD:440688"
ORIGIN      
        1 marpvlvagv dsstqsckhi tvdaatgevl sstalphpdg tavdprrwwd aldgvgatrl
       61 qgiaavsvsa qqhstivlga deqpvhdail wndhratqsa lelrhefgqd rwlrelgmvp
      121 taahpvsklr wlsdhepeaa nrirrvmiph dwltwgllgq rgepmtdrsd asgtgywssa
      181 nseyrndliq lalgrgvkvp kvlgpadrag itargvvvga gcgdnaaail glgakrgeav
      241 vsigtsmtvs mvedshvndp schvadmana sggqlplvat lngartltam admlrlslge
      301 mevlsaaapq daggicfvpy ldgerkpllp esqgaltglt rrsmtpenlg raailglaca
      361 iadavedlig aglvvdtvtl igggsksrsl rqavsdltgr tvgwpeprey aalgaakqaa
      421 waltgelpqw dqpnytliqp salrewvpav rnrysaaskr ifgaelh
//
LOCUS       WP_284756329             416 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Arthrobacter sp.
            efr-133-R2A-120].
ACCESSION   WP_284756329
VERSION     WP_284756329.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-120
  ORGANISM  Arthrobacter sp. efr-133-R2A-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 416)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Arthrobacter sp. efr-133-R2A-120"
                     /db_xref="taxon:3040277"
     Protein         1..416
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44003
     Region          37..411
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(143,145,268,270,298..300,344)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mnkkplaslg laltailams gcgsaassnv sstekvtiky snfisnggne knldtivqaf
       61 ekanpnitvq vttlpykdyt talqtdlaag tqadtfdiey anlrsyvang avaplegvdg
      121 skykqsllqs yqsdgkqyal pssfsdvily ynkalfdaak vayptaswtw adetaaakki
      181 tdsaagvygd fqnvsfyefy kalaqtggkf lnddgksvaf nspqgikaae wlagksgttm
      241 ptpaqgagtp dfdtklfkdg klgmlhsgiw vassfadspk swdiavepgd tqkasaefsn
      301 aigvsanskn kaaaqkwaey mtssdvmaqt risagwelpa tsddsvlkpy lakdkpanrk
      361 aifdaldnva lppvigdnqq kmvdiinnal geveakrssa adalkgaadq inallk
//
LOCUS       WP_284756368             313 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284756368
VERSION     WP_284756368.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..313
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33598
     Region          7..299
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mrdafgrvrt evakavvgqe gavsgmivgl laqghvlleg vpgvaktllv rslaaamtld
       61 tkriqftpdl mpgdvtgslv ydastgtfpf regpvftnvl ladevnrtpp ktqsalleam
      121 eerqvsvdgd aralpdpffv aatmnpiefe gtytlpeaql drflmkltld vpprdvewqv
      181 lrrhadgfvp rdvrsagitp vvgvdevvra qravrgvgar ddvlayivdl aratrqapsv
      241 rvgvsprgat allaaakawa wltgydaitp dhvqamalpv wrhrlrvaad aelegvgadg
      301 vlqqvleqvr vpi
//
LOCUS       WP_284756424             276 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284756424
VERSION     WP_284756424.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..276
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29838
     Region          23..273
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mhqdtievad dridgphgpv pvrryrpldr sagtgaptlv gvhgggffrg dldlpesdav
       61 aralaerglp vvtvdyrlgp lpglpwlgrg gprgrrraph ardeivavlh hlhdeapsag
      121 lllggasaga claastvata pplvglvlty gffharlprd ralqrlvrgh rrlthaplll
      181 dlsnrayagg rptavypesd dlggfprtll idaerdvmra sgerfadela aadvevever
      241 hvlpdsrhaf lnrpgtrdfd dtierivdwv drtpir
//
LOCUS       WP_284756459             404 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284756459
VERSION     WP_284756459.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..404
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41701
     Region          137..404
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtstalpavp lgqrvwsqtw rvavaaltgl ltaglvwpsm dtrgwsdlhv galllgdvga
       61 glaalvllpf rhrapllitv viaalssvst lavgaaaiat vslatrrrav elavagavll
      121 gatvlydvvl appaddmplw qilvagivai allvvigiai gqrralllsl reraallerd
      181 qqlredrare qerahiarem hdvlghrlsl valhagaley rgpgltpdet aaaagvvrae
      241 ahsaltdlrd vlgvlrdpaa tggdevtgta ppqptlvdlp alldqaragg atvrarvdad
      301 gaavptavgr hayrivqesl tnarrhapgq pvdvvvetvp gpgvrvvvsn tltdgpapad
      361 asgktaghgl rglaerarlv ggsfragsdd grvhvveavl pwtp
//
LOCUS       WP_284756463             415 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284756463
VERSION     WP_284756463.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..415
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=44218
     Region          34..381
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 matttlthap tqaqpqhrta tpahseagsp qapppplthr apaldglrtl ailvvvlyhl
       61 hvpqfeggfi gvtvffvlsg flittlllge rrrtgrvrlg sfwvkrllrl ypallafvvv
      121 glllwnwvgd ykgaslqsge aafialtytg nlfrafwdts qgvfahtwsl smeeqfylvw
      181 ppvlvllaal rvrrrwlltg lgvlvvgasa aswasyrsps ggatpdvyfs pvlgvvplai
      241 gcglallldd ervrvraagv lghvatwlgl vllvgvllwi dddwtqhast fgivlpltgl
      301 iaavtigglv svrspvsaal awtpvswfgr rvsysaylwh plviallgtf aigpwgtvgl
      361 vgavaivsig aayavevpve rfrarvragr raaahaapap apatatapap aqrie
//
LOCUS       WP_284756467             342 aa            linear   BCT 25-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284756467
VERSION     WP_284756467.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..342
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35381
     Region          1..338
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtlrvgvlsf ahthaisylg alaampdvev rgtdpggvst gtelgdlrga elaralgagy
       61 aesvdellaw gpdavivtse narhrefvel aaaagahvlc ekplatswqd glairdavdr
      121 agvllmmafp vrfasafdrl ratrdsgalg tvfsvrgann gmlplardwf tdvrlsggga
      181 lvdhvvhvad lidgltgaap vsvtavanrv lhadranaet aglvtitydd gtiaaidcsw
      241 srpdtspvwg gltldvagtg gtvsvdffga aargldavgg rpielrygpd hdlpmlrtfl
      301 aavrfgeqpq pdvgvglrtl sivlaaqesv rtgrtvpvqv ag
//
LOCUS       WP_284756471             610 aa            linear   BCT 25-DEC-2024
DEFINITION  thioredoxin domain-containing protein [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284756471
VERSION     WP_284756471.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442502
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..610
                     /product="thioredoxin domain-containing protein"
                     /calculated_mol_wt=64466
     Region          4..610
                     /region_name="YyaL"
                     /note="Uncharacterized conserved protein YyaL, SSP411
                     family, contains thoiredoxin and six-hairpin
                     glycosidase-like domains [General function prediction
                     only]; COG1331"
                     /db_xref="CDD:440942"
ORIGIN      
        1 mndnrlgttv spylrlhadn pvdwrewgpe afaearergv pvlvsvgyat chwchvmare
       61 sfddpeigel lrrdfvsvkv dreerpdvda slmasasaft qqlgwplttf ltpdghvffa
      121 gtyfpptpvg qvpafrqila avldawterr hevdanasai atairqgava datarsgegg
      181 agadpglpsv dairavtdql sqaedttygg fggapkfpst pllefladaa adgdaeadgl
      241 ldrslhaira seltdadggv fryatkrdws vphyermlyd nagllavaga eqargiadfl
      301 rdtlrradga fvaaqdsest idgrrvegew yrrpvaeraq ldppplddqv ltgwnglair
      361 glaiagarhg dpelvalarg aadavlaahv qdghvtvrss tprgvssapa tvedvgllae
      421 gllelalvtg evsyatvars lvddglaerf dvdpvlasag tatgeqpqta mrsgtvalas
      481 aaatlgaltg dealrgaaar lvadrartgt erplghadal gvalalqrps reivvvtsdt
      541 ddpmravahr arrpgtvvaa ttpeqardwa eagfslfegr dvldpaayvc hdrvcelpsr
      601 sadalarqia
//
LOCUS       WP_284756481             439 aa            linear   BCT 25-DEC-2024
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284756481
VERSION     WP_284756481.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..439
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=46017
     Region          8..437
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 mgatptnaed gwafetrqir agfkadpgwg anvppiaqsa ayvypsgeda aarfmldapg
       61 htytrvnnps aaalerriad leggigalal asgqaatsla vlgvaragdh vvssaslyga
      121 tytlfastlr dlgitftfvq dptdlsewaa avrpetkaff gesipnprgd vldfagvagv
      181 aheagvpliv dntiatpylv rpiehgadiv vhsatkylag hgsaiagliv dsgnfdwaah
      241 adaypqlatt eqsefantnf aekfgrrafi qrtrsklsad lgpaiapfna flvlqgiqtl
      301 slrmdrhvsn aatvatwlda hdqvehvhya glpdspwhhl qqryvpkgps avlsfdlagg
      361 vaagrrfvaa lelfdhvsnl gdvrslvvhp astthvqmts aeraaagvgd glirlsigle
      421 hidditadla rgftaaaag
//
LOCUS       WP_284756505             355 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Curtobacterium
            sp. ME-Dv--P-122a].
ACCESSION   WP_284756505
VERSION     WP_284756505.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..355
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38325
     Region          1..315
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mklglynail hdrpladalr viaangltgi elntggflpp vhvpdidail qddgardafl
       61 aqfagtgvei aglncngnpl hpdpaigpah aedvrrsirl aarlgqdrvv tmsglpagep
      121 ggtrpnwivn awnsaaldvl ehqwsvavpf wqeidalare hgvkvalelh pqnlvfnpas
      181 irelverggl tnvgveldas hlfwqqmdpv avahdlgplv fhaaakdvri nphaaingvl
      241 dnsfrrlspd esrtnlggde wanewpkpsa wdfvalgkgh deaywttfle alraidpdmw
      301 vniehedtel greeevavaa rvlraadaal aptvltvrqp trslpggpwt vprtg
//
LOCUS       WP_284756499             672 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284756499
VERSION     WP_284756499.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 672)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 672)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469209
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..672
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=73564
     Region          301..660
                     /region_name="COG4867"
                     /note="Uncharacterized conserved protein, contains von
                     Willebrand factor type A (vWFA) domain [Function unknown]"
                     /db_xref="CDD:443895"
ORIGIN      
        1 marqnrrltr dtrygrytdg pdplaapvdl aealdaigqd vmggtspera mreflrrggr
       61 tqrglddlar rvaerrrelt srnnldgtlq qvrelldqal laergelarn vdlddgdral
      121 aelqldslsp spaaavqelg dydwtspaar qkydeikdll grevldqrfa gmkqalegat
      181 dqdraavsam mqdlnallea hargedtqqq fddfmdqhge yfpsnpanvd ellddlaara
      241 aaaqrmrnsm tqeqrdelda laqqafgspd lmeqlsqlds tlralrpged wggfermhge
      301 qglglgdgtg vfqdiadlda ladqlaqsgp gselddldld alsrqlgdea avdaktlqrl
      361 eqalrnsgam rrgadgqlrl tpkamrqlgk sllkdvaqrm sgrqgardlr rsgaagepsg
      421 asrqwafgdt epwdiprtit navvrtaasg rqgagvrlsi edvevqetea rtqacvallv
      481 dtsfsmamed rwvpmkrtal alhtlvstrf rgddlqliaf greaevmdve qlvgldamwd
      541 kgtnlhhall lanrhfrkhp taqpvllivt dgeptshlep ngqvwfdypp dpvtialtvr
      601 elenagrlga qttffrlged pglarfidam akrvdgsvva penddlgvav vgsylgsrrg
      661 aggalfrddw gl
//
LOCUS       WP_284756529             353 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284756529
VERSION     WP_284756529.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..353
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35586
     Region          1..349
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mrtpgragir igpvglawrp rvfwytvgsi atvlvlivlg tavgstwiap gvvirsllgl
       61 esgpdafiit tlrlprvltg alvgltlgva galtqtftrn plgtpdiigv tagasvgava
      121 aivlgggtys vsslvlgggi pvaatigalv aavlvyglgw rggvqsyrlv lvgigvsatl
      181 davtsyllvr akitvataas qwlvgslsst swesvwpllv vavvavpial atsaalgigq
      241 lgdevatgvg lgvqrhrllv ialavvltaa avaaagpvgf vafvvpqvgl rlagtnrppl
      301 llagalgavl vlaadllsrs afpwqvpvgi ittvigapyl iwllvrhrke msr
//
LOCUS       WP_284756561             210 aa            linear   BCT 25-DEC-2024
DEFINITION  O-methyltransferase [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284756561
VERSION     WP_284756561.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..210
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22254
     Region          38..207
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 msekesnwkf aedivsetea iararehsle lgveaispai gaqigviaaa sratsiieig
       61 tglgvsglyl ltgapnatlt tidvevdhqq fardayisag taparirlip granqvlprm
      121 neasydvvlv dadpehviey vehglrlarl ggtvlvphal wrgrvadpvk rdrattdfrl
      181 lltevstsga vrsalspagd gllqltkvtn
//
LOCUS       WP_284756621             285 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284756621
VERSION     WP_284756621.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..285
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29145
     Region          3..284
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mnrvpaplla ltamvsvqlg aaiakthfdd vgavgaatlr lvigavvlal vvrprvrhwt
       61 raqwlgavgl glalggmnvf iylsfasipi gvavtieflg plalslvhtr rwrdalwavl
      121 alagvvllgv gptavtevgg vvwavlaaac wagyivmnrh vgaaipgvdg lvvsmvvaml
      181 vslpfglrsa vdgvlreptl livfgavavl ssvlpyalem lalrrmptrv fgvlqslgpa
      241 iaalaglvvl aeglsvletv alacvtaasv gvtlsarrrr ggpvg
//
LOCUS       WP_284756625             292 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284756625
VERSION     WP_284756625.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 292)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..292
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31584
     Region          2..291
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mranrwytpw llvlpaliwl vafslwpsin tvrlsftnas plggvsqwvg aqnfetllad
       61 pqvweallns viymavclpl ltvlplliav lvqqklpgia ffrtafytpv iasavvvgli
      121 wtwilddrgv inemaqalgv vqgsvpfltd rwllllsais ltvwkglgyy miiflaalgn
      181 vgkdlheaaa ldgagavrrf wsvtmpgvrg tmtlvgilvc vsalrvfsel yiltngtggp
      241 ggqdnslvml iqqyargftg nlgyasalsl llfvvtlvpm lalarmnska dk
//
LOCUS       WP_284755650             340 aa            linear   BCT 25-DEC-2024
DEFINITION  arsenic resistance protein [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284755650
VERSION     WP_284755650.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Ben Fekih,I., Zhang,C., Li,Y.P., Zhao,Y., Alwathnani,H.A.,
            Saquib,Q., Rensing,C. and Cervantes,C.
  TITLE     Distribution of Arsenic Resistance Genes in Prokaryotes
  JOURNAL   Front Microbiol 9, 2473 (2018)
   PUBMED   30405552
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Achour,A.R., Bauda,P. and Billard,P.
  TITLE     Diversity of arsenite transporter genes from arsenic-resistant soil
            bacteria
  JOURNAL   Res Microbiol 158 (2), 128-137 (2007)
   PUBMED   17258434
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Mansour,N.M., Sawhney,M., Tamang,D.G., Vogl,C. and Saier,M.H. Jr.
  TITLE     The bile/arsenite/riboflavin transporter (BART) superfamily
  JOURNAL   FEBS J 274 (3), 612-629 (2007)
   PUBMED   17288550
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Rosen,B.P.
  TITLE     Families of arsenic transporters
  JOURNAL   Trends Microbiol 7 (5), 207-212 (1999)
   PUBMED   10354596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..340
                     /product="arsenic resistance protein"
                     /calculated_mol_wt=35409
     Region          18..310
                     /region_name="ACR3"
                     /note="Arsenite efflux pump ArsB, ACR3 family [Inorganic
                     ion transport and metabolism]; COG0798"
                     /db_xref="CDD:440561"
ORIGIN      
        1 mpaqraarpa garlwatpai vggaillgsv iggispsagd amgsvvdvlv itlvvalfvd
       61 vplhrlprtp gawkvigiaw smnfllaplv aflltrvalp ghpavqlgvm lyflapctdw
      121 flaftrlsdg dtaagatllp inmvtqlllf pvwitvlggn agidavgtig tllqwfvlpa
      181 aiavvirlgv sllpdgargr aaalpgravp wivgamvagl fashiallla nlpvfvavlg
      241 cavvffavmf iaadwasrla alsyprsall amttaarnap lmigltsaal phqplvttai
      301 vvgmlvefph llavrhlllr rrrgqhagrr lrgtaawghp
//
LOCUS       WP_284756645             517 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284756645
VERSION     WP_284756645.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..517
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54438
     Region          52..512
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 msdhdqyddh eaneefvghd eldgrdedgi ripvgpsgda psdavpyggd ddevrrveaa
       61 lyarigeqap errltatrra vellgdphla ypvihvtgtn gktstartie sivrahglrt
      121 glmtsphlvs irerivvdgq piaadrfven wddiapvlei tdreladkge lpltffealt
      181 vlalacfaea pvdvavievg mggewdstnv vqsqvsvftp iaidhakqlg atvaeiartk
      241 sgivkpssav vssrqvpeal aeleraaelt estlavegtv gpfepvpdrr eaagrpssqg
      301 fsvvdvtpav ggqlitvqgi agryddlflp lfgrhqaena avaiaavesf lgrgaqalde
      361 dvlsegiagt tspgrlqpia tdptvvvdaa hnphgakala ealpvafpse hvvgvvgilg
      421 dkdargfvra lkdtvatfvv tqppgerald adefarvvvd evgedrvvve pslasalqea
      481 rsladeadae dalvlvagsi vmvgavmdlv hregeak
//
LOCUS       WP_284756769             975 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284756769
VERSION     WP_284756769.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..975
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..975
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=102908
     Region          <117..231
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <436..916
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 maggtksttr srastssrgn gtrgssrtqa ttkklpqaap tpvfreqnpl vtfwlamahg
       61 vgamfrllgk etlekdqrrd gfpfllflla iaggvvewln ptnsvsvald aytfgglfgr
      121 lafalpvimi vfagwlfrhp asvhdntrig iglgilivsi aslchvfggr psaadgmpal
      181 aaaggvlgwv vigwlvtiat awvavpvaiv llvlslfiit ktppnklgrr lhelyaylfg
      241 apapaaepea daaavaepaa rartskrgkk gdtdfqlfdd lgfgdeqaaa daggdnvpww
      301 rrnksgreed paydspvlpp atgvapaaaa vapaapvvpa apavspnaga aaglvdltpa
      361 epasvnlnds veqdlqdaeq alrafgtdvp arpeptadir pavpevlsep eivdepedid
      421 aaaelsaaaa gagddpskpy rlpaattlss gtpsvarsqa nddivaaitg vltefkvdak
      481 vtgfsrgptv tryeielgpg vkvervtals knlsyavasn evrilspipg ksaigveipn
      541 tdreivslgd vlrsnaarks khpmtigvgk dveggfvvan lakmphllva gstgsgksvf
      601 insmitsllm rakpsevrmv lvdpkrvels iyagvphlit piitnpkkaa ealqwvvkem
      661 dmryddlasf gfrhvddfnk aienneivlp agserklkpy pyllvvvdel adlmlvaprd
      721 veesivritq laraagihlv latqrpsvdv itglikanvp sriafavtsv tdsrvildqp
      781 gadkligqgd alflpmgssk slrvqgawvq egevaevvqh vtrqaqpeyr qdvqavverk
      841 eidadigddl elllaaveqv vstqfgstsm lqrklrvgfa kagrlmdlme srdivgpseg
      901 skardvlvta dqlpavlakl rgeeppaaaa paapaptpsg dgdrygadpv gdmtrgydev
      961 hdepdedawg ltgre
//
LOCUS       WP_284756779             405 aa            linear   BCT 25-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284756779
VERSION     WP_284756779.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..405
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=41450
     Region          44..352
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mrltpsrgvl vaaavvvgal vapaltaapa nateyptwqd vqrakgneta kraevqkvqa
       61 alqsaqdeaa aksqaalvas skadaaesel asatqaatsl qaqaqhaset adraqqragq
      121 laanlyrdgs tnqmttriat aknpdqllyq lgaldqlset wagvmddasv aagtasslhe
      181 qaeraetera traqaaeers aaaksaeqaa daavesteqh sdelyaqlas lkdstakqea
      241 gyelgqrvaa qkaeqqrkra aaaaaeaaan aaaanagssa sggsatsggt gssypstggv
      301 avdpaaaqay arsalgsygw gsdqfsclvs lwtqesgwra nalnassgay gipqslpaek
      361 mavagadwrt nantqidwgl ayiksaygsp cgawghemsv nphwy
//
LOCUS       WP_284756851             271 aa            linear   BCT 25-DEC-2024
DEFINITION  triose-phosphate isomerase family protein [Curtobacterium sp.
            ME-Dv--P-122a].
ACCESSION   WP_284756851
VERSION     WP_284756851.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..271
                     /product="triose-phosphate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0004807 - triose-phosphate isomerase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006094 - gluconeogenesis [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27999
     Region          12..258
                     /region_name="TpiA"
                     /note="Triosephosphate isomerase [Carbohydrate transport
                     and metabolism]; COG0149"
                     /db_xref="CDD:439919"
ORIGIN      
        1 mpattaaapv tigvslkmyf shartlewta avadiarshp avrsgvvelf viptfpalvp
       61 vravigdapv tlgaqdlawa dsgaftgevs gaelreigvd lveiahaerr elfhetdhei
      121 agkvqaayrn hlrplicige teraadgdpa aaiaevttql drftataiad giagpliaay
      181 epvwaigapq papdehivav lagieqhlan rpelagsvai yggsagpgll trgagriggl
      241 flgrfahdpe airtildeve alaatqdgap a
//
LOCUS       WP_284756941             360 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284756941
VERSION     WP_284756941.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 360)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 360)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..360
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=38127
     Region          16..342
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 migttwhrlv davarwslrr epdqdadrla srrsvigiav rvaavsaalv vgiialvvay
       61 vvwqltpgqq reqagpldvh itldtvdltv aiagvgglai vfagvaswli arravrplte
      121 alrvqrtfva dashelrtpl avlharvqrl rmqtpaddpr rgivdevtgd trilidivdd
      181 llgaaagtpt epgvtrledg lavlrrdmsv laaerqvrlr vadhsatval tptqlhrclv
      241 altdnaight ppggtvtvtt tsepdrvcvr vqddgtgitg iaparvferf ahgtgpgper
      301 aatrtgygig lalvreiavr aggavtvest gdqgtvfalr ipthrtptdi ptttrtiaeg
//
LOCUS       WP_284756881             398 aa            linear   BCT 25-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284756881
VERSION     WP_284756881.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..398
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42103
     Region          10..393
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 masestvqqr lrvamvghgf mgaahsqawr taprffdlga epemavvvgr dpgrteaarq
       61 qygwqaastd wraviadpdi dvvdvvspgs shveiaiaal qagkhvlcek plantvaeae
      121 amtaaadaar aqgvramvgf syrrvpaiaf arqlvqdgri gtvrqvraly lqdwladedg
      181 pmtwrldksl agsgalgdig ahaidlvehv tgaslatvsg tletfvterp lmaegvglsg
      241 tassergqvt vddaafftar lgggaadgai gtfeatryat grkngltlei sgsegaiqfd
      301 leamnelrly esnapageqg frrilvtepe hpymaawwpt ghligyehtf shqvkdfvda
      361 ivagtdpsps fadglhvqrv ldaversaaa gstwtats
//
LOCUS       WP_284756972             282 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Curtobacterium sp. ME-Dv--P-122a].
ACCESSION   WP_284756972
VERSION     WP_284756972.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ME-Dv--P-122a
  ORGANISM  Curtobacterium sp. ME-Dv--P-122a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426811
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Curtobacterium sp. ME-Dv--P-122a"
                     /db_xref="taxon:3040286"
     Protein         1..282
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29365
     Region          3..258
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mlehldtegg tiaynlsgtg plvvlahgmg dsrhayrfvv pelvaagyrv anvdlrgcgd
       61 sstgwdgyqr tdiardlvav arhlggpavv vgqsisggaa tiaaatapdl vagivelapf
      121 trkqsvdlgg llrnrrhrag tvqlarvmts gslpgwlayl diavptkpad watersriet
      181 tlrqpermaa lramtrtspa dageqlgavr cpvlvvegsa dpdwavprae geriladlpd
      241 glgelavidg aghyphtetp aallalllpf lartlpvagp va
//
LOCUS       WP_284756957             377 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein [Agrobacterium sp.
            fls2-241-TYG-188a].
ACCESSION   WP_284756957
VERSION     WP_284756957.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. fls2-241-TYG-188a
  ORGANISM  Agrobacterium sp. fls2-241-TYG-188a
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Agrobacterium sp. fls2-241-TYG-188a"
                     /db_xref="taxon:3040275"
     Protein         1..377
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40904
     Region          4..354
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 maldripvsi itgflgagks tllnrllkdp amqdaaiiin efgdvsidhl lversgdgii
       61 elaegclcct vrgelvdtla elmdgiqtgk lkpvnrivie ttgladpapv mqsiignpvi
      121 aqnfslngmv tvvdaangaa tldrhpeavk qvavadrlvl tkrslaeeaq vaalkerlsa
      181 lnprapvedg daedwsaval lenglydagn klgdvsrwlg deaahddghh hghdehghgh
      241 hhhhhhddvn rhnasirsfs iihdkpidpm aidmfidllr sahgekllrm kgivqlsdnp
      301 drplvlhgvq sifhppqrla awpdpadrrt rmvlitdglp eefvkdlfga figsvridkp
      361 drqavvdnpl avpgmrf
//
LOCUS       WP_284757042             219 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Agrobacterium sp.
            fls2-241-TYG-188a].
ACCESSION   WP_284757042
VERSION     WP_284757042.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. fls2-241-TYG-188a
  ORGANISM  Agrobacterium sp. fls2-241-TYG-188a
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Agrobacterium sp. fls2-241-TYG-188a"
                     /db_xref="taxon:3040275"
     Protein         1..219
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=23829
     Region          6..>193
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mtqidapqrf vlldgvrgia avaivhrhae affgrpeass ylavdlffal sgfvlahayg
       61 eklagrsvtp fafmkarflr lyplyaiall smalffatly yldlptpidd lhrkislael
      121 afalltgvmf lpapftltln galflispaw slfnelvvnl ayaikgarag tkgiavvlga
      181 savvlifaaf hsgklhlgfr whemyagmgr vfsrflpvs
//
LOCUS       WP_284757212             132 aa            linear   BCT 25-DEC-2024
DEFINITION  6-pyruvoyl trahydropterin synthase family protein [Agrobacterium
            sp. fls2-241-TYG-188a].
ACCESSION   WP_284757212
VERSION     WP_284757212.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. fls2-241-TYG-188a
  ORGANISM  Agrobacterium sp. fls2-241-TYG-188a
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Phillips,G., Grochowski,L.L., Bonnett,S., Xu,H., Bailly,M.,
            Blaby-Haas,C., El Yacoubi,B., Iwata-Reuyl,D., White,R.H. and de
            Crecy-Lagard,V.
  TITLE     Functional promiscuity of the COG0720 family
  JOURNAL   ACS Chem Biol 7 (1), 197-209 (2012)
   PUBMED   21999246
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Colloc'h,N., Poupon,A. and Mornon,J.P.
  TITLE     Sequence and structural features of the T-fold, an original
            tunnelling building unit
  JOURNAL   Proteins 39 (2), 142-154 (2000)
   PUBMED   10737935
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Agrobacterium sp. fls2-241-TYG-188a"
                     /db_xref="taxon:3040275"
     Protein         1..132
                     /product="6-pyruvoyl trahydropterin synthase family
                     protein"
                     /EC_number="4.1.2.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14263
     Region          1..132
                     /region_name="QueD"
                     /note="6-pyruvoyl-tetrahydropterin synthase [Coenzyme
                     transport and metabolism]; COG0720"
                     /db_xref="CDD:440484"
ORIGIN      
        1 mfavevrdhi miahslprpv fgpaqgmhga tfvvdaafft kdvdedglav digaattvls
       61 evlkplnyqn ldeldvfkgk istteviakh ifdelsgava dkrlgpgshr iarikvtlhe
      121 shaargwyea dl
//
LOCUS       WP_284757224             455 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Agrobacterium sp.
            fls2-241-TYG-188a].
ACCESSION   WP_284757224
VERSION     WP_284757224.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. fls2-241-TYG-188a
  ORGANISM  Agrobacterium sp. fls2-241-TYG-188a
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Agrobacterium sp. fls2-241-TYG-188a"
                     /db_xref="taxon:3040275"
     Protein         1..455
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=49809
     Region          188..418
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 msgpsfsrlf vlnalmgicw lvmmsvtlve sdayryaals viiifvfflp kednanlhdw
       61 lavlcvacgs ialfrflyql imtgekgase wlyafpllfp llgralygsr silrvviacf
      121 fciallllli stdfaraltg erifplfhqn pihgavgcgf lvigafywas hnyemgstra
      181 vrtavtsiam lviaialfni wgskskgvwl aliptflliv ssaflflrrk evlvslvagv
      241 lllgsgvfla hqnilavvgp taktvvtlyd dfvggrsvss flgdaiaspe tpfsvderlq
      301 lwsnaseiia aspifgsgnh wlaiwhtthy agipytlmhn gylevlvrhg fvglaiygli
      361 fvasiyrvfr askqgllsks aflcyfvcai yfaftilsns nnrlalgesy vllfsavcfa
      421 ctismkmarp dvestpqsga tvaeasmdrk rqtya
//
LOCUS       WP_284757276             406 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Agrobacterium sp.
            fls2-241-TYG-188a].
ACCESSION   WP_284757276
VERSION     WP_284757276.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. fls2-241-TYG-188a
  ORGANISM  Agrobacterium sp. fls2-241-TYG-188a
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Agrobacterium sp. fls2-241-TYG-188a"
                     /db_xref="taxon:3040275"
     Protein         1..406
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=46262
     Region          134..400
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mshaerenls lildraplwq kmicrrvnnm thgrltlvfp ggseyvingq qpgphgvlcl
       61 nrgrvvrrlv tggslgfaqs ymdgdwdspd latllelaia nedswkavse psrfisalal
      121 lrhrlrrnsk agsrrniafh ydlgnrfysa wldetmtyss alfekpgqtl adaqnakydr
      181 iveqlqigpd dhvlevgcgw ggfaeyairk tgcrvtgltl sreqadfark rldaagfanr
      241 sdirledyrd cqgqyskivs iemfeavgee nwptyfqrlr tllaqggeam vqvitideer
      301 fdeyrrtadf iqtyifpggm lpsitafkda aatqgfavpd llrfgkdydr tlmqwdrafi
      361 snwhrieplg fderfrrmwq yylhycsagf ragridvvqf klvpas
//
LOCUS       WP_284757315            2391 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Agrobacterium sp.
            fls2-241-TYG-188a].
ACCESSION   WP_284757315
VERSION     WP_284757315.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. fls2-241-TYG-188a
  ORGANISM  Agrobacterium sp. fls2-241-TYG-188a
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2391
                     /organism="Agrobacterium sp. fls2-241-TYG-188a"
                     /db_xref="taxon:3040275"
     Protein         1..2391
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=236700
     Region          361..2004
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mtsiissfap sqiskmttsa lsawttedma elsteqikal sskqinvfss qqiaaleved
       61 lramstsqln gistsgmvgl tldhiaalnr isvaslgsgq iaalttdqvk nlsteqseal
      121 tpaqiaamss dqiaaldied llefstsdfa aislkgiagi gtqgvhlfsn eqigalspna
      181 isgmntdtlv alseeqvaal stasisrltt dqlvrlettq lsaltssqva slkaaqital
      241 spdyvaklsa sgiaglstts iasltpeqls gmstvqfagl ttkqinalks sqleslptth
      301 laalspaqia alntraipgl tpaqvevfsa tqaealtpaq vkamtasqle tfaedeirqf
      361 stadiaaisa stfaelsttt lgafttaqia sigastfskm tieqlnaldg eqlgaltstq
      421 maaltslqas slstdevafl stsalaalsg ksiagfatdv vakwtpeqia alstgaivkl
      481 tsdqlatlst aqvealtsaq ikvlssvqig alsaaaigtf tpsevaaist kalsalrtda
      541 vagltndhii alsgssvaam ssdqfaalts dqlsvltskq lgalkttqik alsseaiagf
      601 staqisslst saiaglsasq faalqddkid altslqikal nsaqlavlgt ddiakfstae
      661 maainsrait glsgenlasl tsaqmsaisa aavsalkadq vaaltatqia aisasqaaal
      721 tsgqlavldk adisalstta iaalgtkais gispalvael ttaqaaalna savskmstdq
      781 iealtpsqva vmttaqikvm sssqvgafsa saiaaltstq iaaiptksla gltatdigdm
      841 ttiqlaaltt aqiaalsssq lsglksedia afslddirai gaagiggfst dviaaldskq
      901 iaalsvaaig sltsdqvaal stlqvdsltt nqiaamkstq taalgvedlk tfssqdiaal
      961 saraiggfgt gvlasletvl vaafstasia sltteqldal tsqqfvamkt sqiaalssaq
     1021 asainptila slssgqiaal gsvavtnltg aqiaaltstq lsslstsqma alssaqvnal
     1081 stehvaalst gqiaaigtng iaglsskqia alttdqaaaf tslqvrvlse dqiaalgadd
     1141 iatfttkeis ligtaaiigl ssatleslst dkiaainads laalttrhia slgsaqigal
     1201 ttkqlsglta dqvsvlstad isalstskis alsaagisgl tttqlsklst sqiealtniq
     1261 vgaltsaqlg aiglegiskf ssadiaaina niigslptst iagltadqis flsaqaiagl
     1321 ttnqisvlst gqvaslgtkq iaamtssqva algtddlasl kdaaigaigs saisglstet
     1381 lgkltgsqll aistaavsgl sanqigalts sqiaslsnkq iaaltsrqva algtagvaal
     1441 dtnqisalss sgvvglsteq idkltvaqae altadqaavl ssaqvsalgt ddlsrfsske
     1501 iaslssgsla glstekiasl dpliigalss vaipglsttq vaylnsaqla alntaqvgam
     1561 ssrqvaalgt ggitvlsssq iaalstagip gltaeqlgam atdklealtt tqvavlnsvq
     1621 tgalgtedla vfskaelavl sssavlglst avlaslsadr laalgtasls glssgqlssl
     1681 tteqvqglst lqvaalsskq laslstagaa afspsqiaal ssgaiagltt aqiaalsvaq
     1741 ieafntgqva altstqlsaf gtediaalst eelaaltsna iagllpgtia alplerisvl
     1801 gtasiaglts aqisalttqq leafstaqig algskqiavl gtagvaamsp aqiaalstsa
     1861 iaglssaqid alssdkveal tptqiaalts vqlsvfgvdd idlfstddla aipahviqgl
     1921 staalaampa skiailstsa vsgltsdqmr altadqveaf tsdqvgalgs kqmaglsldh
     1981 lksftkaeig aisagaivgi staimaalpq divsalsasg vsglstaqvr altvdqltal
     2041 sptqvaafts qqvaafkasd lptfstaqia aisaagiagm ssdqvaalnl eqlhvlttsq
     2101 vnaltssavs glsaeeletl saaqiaaiss saigglttef igglsatela rlgtagisgl
     2161 tgkqvaalsr dqldslstaq iaalsadgls glttegmstf saseiaaisa ssirglstqi
     2221 isrltnaeiq vltpaqigam gynqivalst sqvdalttaq lgglnaiqaa algtedislf
     2281 ttedisalgt savsgltvgv iailttaqse altpgqvnal tsgqvaalsk dnlakfstad
     2341 iaafnssgvt glstdtlvsl ssdqigtlmg thmgsltpaq isaiisvyva g
//
LOCUS       WP_284757365             268 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Corynebacterium sp.
            UMB9976].
ACCESSION   WP_284757365
VERSION     WP_284757365.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..268
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=29610
     Region          11..254
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 mtdpqqpelt gfrvalanfd gpcdlllqli hshklditei alaevtdefi aytrglsqsa
       61 edldevtefl lvastlldlk aarlvprgev ddeadlelle srdllfarll qykaykqvad
      121 lfaewqrgaa rsypvalsle dryanllppv eikhtkesfa elaahvfrpr pegvqtghvh
      181 apavsvpkqa gkilntlkia genkwvnfds lisdaeesiv vvgrflalle lykaraigve
      241 qpmpleemlv awtgldvdpq vvaasnwd
//
LOCUS       WP_284757370              87 aa            linear   BCT 25-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Agrobacterium sp.
            fls2-241-TYG-188a].
ACCESSION   WP_284757370
VERSION     WP_284757370.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. fls2-241-TYG-188a
  ORGANISM  Agrobacterium sp. fls2-241-TYG-188a
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 87)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Agrobacterium sp. fls2-241-TYG-188a"
                     /db_xref="taxon:3040275"
     Protein         1..87
                     /product="type II toxin-antitoxin system RelE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0017148 - negative regulation of
                     translation [Evidence IEA]"
                     /calculated_mol_wt=10395
     Region          3..87
                     /region_name="RelE"
                     /note="mRNA-degrading endonuclease RelE, toxin component
                     of the RelBE toxin-antitoxin system [Defense mechanisms];
                     COG2026"
                     /db_xref="CDD:441629"
ORIGIN      
        1 mnwtieydil vqkqikkldp qtrirsflhe rlaqldnprk igealqgsel gnywryrvgd
       61 yrilcdiqdn rlvvlvieig hrrevyr
//
LOCUS       WP_284757407             229 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Corynebacterium sp. UMB9976].
ACCESSION   WP_284757407
VERSION     WP_284757407.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 229)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..229
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=24918
     Region          <20..215
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mvnpldkllp sarpidlppv aiiglgrfgs amaeelhshg vdvlgidvee kllhdsdphl
       61 tdsfiadatd pealkqlgvk dfqqvvigig ssleasilta snlvelgvkd iwakadsdah
      121 ariltrvgvn hvvrperdtg rrvahllsgr fqdytvfdqg yamitlrapk elvnhslnrh
      181 slwakhrvql vavhsgnqwa ppfadhqlsp dddvilagap adlekfgrr
//
LOCUS       WP_284757416             911 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium sp. UMB9976].
ACCESSION   WP_284757416
VERSION     WP_284757416.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..911
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=101067
     Region          14..910
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mansatcnak nyptlveefr keydfeldef qldaaaaiae grgvlvgapt gagktivgef
       61 avymafhggg acfyttpika lsnqkyhdlc asygeenvgl ltgdvtlnpd apivvmttev
      121 lrnmiyadsd rlaslthvvm devhfladrw rgpvweetil nldhsvtlvs lsatvsnvee
      181 fggwlrtlrg etdiivtdkr pvpltqymmv gskimrlfsk naehlagedh pgainrslls
      241 avgkaeaygn qrgprredvv rhleqakmlp aiyfifsrig cdkavqqlli rkvelttpde
      301 areigdiide gvagleaadl hmlgfrqwrr almrgfgahh agmlpafrhi veklfsrgll
      361 kvcfatetla lginmpartv vlekmtkfng eahaeltpgq ytqltgragr rgidtvgnav
      421 vlwspqvdpy avaalasart ypldstfrpg ynmavnliat kgwaeahril ersfaqyqan
      481 dtiverahav elrrqdfdre raelealvgr teaaqradaa elteqvldya elrrtlshee
      541 rrakrdaale rqqevehllr tinvgdvlal ptgknpvtav vvrsdsgrnp rptlvlddgw
      601 vervaadmfr ntpviighmr ihrgverapk rharavasql rrmhldkpkk irpharggsk
      661 kaaelrnqlh vhpvhawaer eelakkaqsv lkagrrweyq kqeseqpgds ltatfdriia
      721 lleelgyvet wtaeggtpaa kvteegekla rihhesdllv aqclrrglwd dldpaelaaa
      781 vsacvfenrr estertqlpt daleeavaht lrvykelvsd eerhrltatr epqlgfatav
      841 hqwvagaple yclqaaeasg avltpgdfvr acgrvkdlld qikmtgysnd vrksarkavd
      901 amqrgvvaid v
//
LOCUS       WP_284757500             203 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Agrobacterium sp. fls2-241-TYG-188a].
ACCESSION   WP_284757500
VERSION     WP_284757500.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. fls2-241-TYG-188a
  ORGANISM  Agrobacterium sp. fls2-241-TYG-188a
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Agrobacterium sp. fls2-241-TYG-188a"
                     /db_xref="taxon:3040275"
     Protein         1..203
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22659
     Region          4..197
                     /region_name="HAD_sEH-N_like"
                     /note="N-terminal lipase phosphatase domain of human
                     soluble epoxide hydrolase, Escherichia coli YihX/HAD4
                     alpha-D-glucose 1-phosphate phosphatase, and related
                     domains, may be inactive; cd02603"
                     /db_xref="CDD:319790"
     Site            order(10..14,110..111,143,167..168,171..172)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            138
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mtkinhivfd igkvlihydp nipysrlipd aaerawffen vcthewnleq drgrtwadae
       61 alllqdhpdh eetirafrlh whemvshsyd dsvailkgli dgghdvtmlt nfasdtfrea
      121 qkmypfltls rgvtvsgdvg likpdvaiye lhaqtfgldp assifiddal anvegakaag
      181 wqavhftgae klkadlaefg ikv
//
LOCUS       WP_284757722             357 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Corynebacterium sp. UMB9976].
ACCESSION   WP_284757722
VERSION     WP_284757722.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..357
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=38307
     Region          50..337
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mdpisqqaaq tnnplsraml klyaaiyrad rkvglprqvd sdgnkavkvp rlktqwvltl
       61 illicqtgit ftgslvrvtg sglgcetwpq chpgsfvpvp gsapwihqii efgnrmltfv
      121 laaaalaafi allragrrss ilhlsfiqgl giiaqavigg isvrldlaww ivaahflpsm
      181 llvflaavll vkvtedddap ikeqmpaalr vlttmnaval avtlftgvlv tsagphagde
      241 aikpehrlqv slesiahiha hamylylglt igliaaliav vaaprvrkaa awmcagilfq
      301 avvgiiqfwl gvprwtvpvh vigsglvtla tgylwalryq ktheeqsetv shavqgd
//
LOCUS       WP_284757831             236 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Agrobacterium sp.
            fls2-241-TYG-188a].
ACCESSION   WP_284757831
VERSION     WP_284757831.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. fls2-241-TYG-188a
  ORGANISM  Agrobacterium sp. fls2-241-TYG-188a
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Agrobacterium sp. fls2-241-TYG-188a"
                     /db_xref="taxon:3040275"
     Protein         1..236
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25341
     Region          1..93
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtsiaspnti aaianlmgdt tranmlcalm ggqaltagel srqagvtpqt gsghlakmvd
       61 anllstvkqg rhryyrlasa qvangidalm niaadgpkrh hpvgpkekdm riarscydhi
      121 agrlavamad slsenghill sdegalltek gnaflrefgi dldkgthskr plcktcldws
      181 erryhiagrv gaalldrtle lgwlarrads ralritpags kgfreifclp aewnal
//
LOCUS       WP_284757892             424 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium sp. UMB9976].
ACCESSION   WP_284757892
VERSION     WP_284757892.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..424
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44258
     Region          15..424
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mtsasnspip ttvtpravgi wvtgvlvyvm avlgrtslgv vsvdaldqfq inagqlavft
       61 tvqlatyafa qipagllvdr lgprkmmlyg avlmavgqvl lafttsfpva vaarvlvgag
      121 dataflsvmr iipawfplrt aplfgqatga vgqlgqflsa vpflalvgsa gwsigfvslg
      181 avgllvgiva fvvvwdtpge lasgrrggve nqedgpgpsp mvavkyalgn rtawhgffih
      241 wsglsllvvf tllwgmpimt lgmgmdkpta gwaisastla mavcgvlvgf lsarlgrsrw
      301 kaivvgtslg aaawllffis peprtaaaaf vmnvvmgvvs planigfdsv reecrrefva
      361 tatglanmgg wlagmaanqa mgiyltlaap ngdytwaefr fgwfvvlgvw alglvgvvat
      421 rprr
//
LOCUS       WP_284757913             293 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium sp.
            UMB9976].
ACCESSION   WP_284757913
VERSION     WP_284757913.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..293
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31429
     Region          50..293
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtdsaitdvl nqvadwpvnn vaaaaitlgg ggdadgtgge advvthgdme hvfqlasvsk
       61 litayatlma veegafeldd kvpaelvpsf eepptvrell shasgiefrk hrqmrpahtr
      121 riyssagyev lasfieqate msfaeyvrlg iceplgieit vegsaghgfs asasavttlt
      181 eeflrpklla gqtvaealtv qfpdlvgvvp gygrqtpcpw glgfeihgek hphwmgenmp
      241 atvaghfgqs gtflwfapdq glaavvltde pfgdwskdrw pefnaqlwea mad
//
LOCUS       WP_284757924             813 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium sp.
            UMB9976].
ACCESSION   WP_284757924
VERSION     WP_284757924.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 813)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 813)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 813)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 813)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..813
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..813
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=84277
     Region          27..804
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 menlsqhqds satevgaiga aqpvldldyq itgmtcasca nrierklnkl dgvtasvnya
       61 tekahveqdg aaeavtdeqi reiiadmgye aqlsqplasq pgagdpqgga geqgaadaaq
      121 pgaeptsqts aeqaaerele glrsrligsl wlaipvivla mipnlqftnw qwlsltlaap
      181 vivwagypfh ratwlnikhg avtmdtlitv gtgaaflwsl valffgsage pgmshtwslf
      241 nthsdpmgdi ylevaagvim fvlagryyek rakhrageal ralselgakd vavvddaqgg
      301 nerripigql aegmyfvvrp gekiatdgrv vagssavdes mltgesvpve vapgdmvtga
      361 tvnasgrliv eatrvgsdtq laqmaklveq aqsgkadvqr ladrvsavfv pvvialavit
      421 lvawllitgd vgaamasava vliiacpcal glatptallv gtgrgasmgv lirgpetleq
      481 trgvdaiild ktgtittgem tateawlapa adsiadgsgk agfseadlwr iagavenhse
      541 hpiaqaiaer areeiggelp eaedfesvpg rgvtatvdgv tvqvgrgfet sdgttvgaei
      601 versglggtv vpvlvdgqla gavavedavk pdsaeaiaql nelglepmlv tgdneqvare
      661 vaglvginpd nvragvmpad kvtavkdlqa egkrvamvgd gvndaaalaq adlgiamgtg
      721 tdvaieaadi tlvraemsav vdsirlsrkt lrtikmnlfw afaynvaaip laafgllnpm
      781 lagaamalss vfvvsnslrl rgfksiqpev ees
//
LOCUS       WP_284758138             226 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Corynebacterium sp. UMB9976].
ACCESSION   WP_284758138
VERSION     WP_284758138.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..226
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=24965
     Region          1..222
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mlfddlprdd aritpgvvhl pgwlelgqqa avisqlreva relagtplsm srpqlksgrm
       61 qvfmlhlgrm wvteptyryv thvaghrvpq vpknlaeiar qalasaaryd aalsawaetf
      121 rpdmalvnyy ppgasmgmhq drnenslapv vslsigdeal frigstetrn qpwdevtlis
      181 gdvivfggpk rlafhgvpqt rpetlpdgcg lkegrinitf rqlddr
//
LOCUS       WP_284758244             151 aa            linear   BCT 25-DEC-2024
DEFINITION  Rieske (2Fe-2S) protein [Corynebacterium sp. UMB9976].
ACCESSION   WP_284758244
VERSION     WP_284758244.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..151
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=15322
     Region          57..149
                     /region_name="NirD"
                     /note="Ferredoxin subunit of nitrite reductase or a
                     ring-hydroxylating dioxygenase [Inorganic ion transport
                     and metabolism, Secondary metabolites biosynthesis,
                     transport and catabolism]; COG2146"
                     /db_xref="CDD:441749"
ORIGIN      
        1 mssqssspqf tspsatgagq fscsrrsllr gaalataata agallaacag eetvakaakt
       61 dipvggakii dnwiiaqpek dkfmafstec phargridqi aeqdgmtvai cpkhgsvfdt
      121 atgdvvegps rdpmalssdv qvngdavevi n
//
LOCUS       WP_284758302             277 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium sp. UMB9976].
ACCESSION   WP_284758302
VERSION     WP_284758302.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..277
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28923
     Region          40..275
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mnpgnvnkrq petstsgqgs gtadadlpdl clpdlwqyga ilfdldgvit ptadlhreaw
       61 ahmfteyfre lgaggqsvae ytdqdyydyl dgrprtegia allrsrgidl ptgseadtaa
      121 entvyglger knaeflrllg qgiaaypgsv qlldslaapk ggvtpprlai vsssknarpv
      181 leaaglldrf elvvdglvga elelpgkpap dtylhaatwl gvpaekavvv edalsgvasg
      241 rngkfglvvg vdrgagdqel ldagadtvva dladfvg
//
LOCUS       WP_284758341             226 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Corynebacterium sp.
            UMB9976].
ACCESSION   WP_284758341
VERSION     WP_284758341.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..226
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24269
     Region          72..216
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 msrrgahlrs trpnlrsrsr aalaalltaa islggltacg egatgddava vggtfefvsp
       61 ggqtsisypq eerkevanlt geslmeegeq inledyagka vvlntwgqwc gpcrseaddl
      121 ervheklekr gdgtvlginv rdpsrekpkn fvrtygityp siydppfksa lrlggipasv
      181 ipttivldkq hrpahiflke itddelwkvl epilneddga aagega
//
LOCUS       WP_284758403             105 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsB family cell division protein [Agrobacterium sp.
            fls2-241-TYG-188a].
ACCESSION   WP_284758403
VERSION     WP_284758403.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. fls2-241-TYG-188a
  ORGANISM  Agrobacterium sp. fls2-241-TYG-188a
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Agrobacterium sp. fls2-241-TYG-188a"
                     /db_xref="taxon:3040275"
     Protein         1..105
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=12202
     Region          13..101
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 mwtkhhkkrr fgrlvvpait vaflsyfgyh cihgdfglqa terlerqria rtaelakltk
       61 grvalerqve lmsdgslerd mideisryql nmsradeivi mntyf
//
LOCUS       WP_284758425             112 aa            linear   BCT 25-DEC-2024
DEFINITION  histone-like nucleoid-structuring protein Lsr2 [Corynebacterium sp.
            UMB9976].
ACCESSION   WP_284758425
VERSION     WP_284758425.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Gordon,B.R., Li,Y., Wang,L., Sintsova,A., van Bakel,H., Tian,S.,
            Navarre,W.W., Xia,B. and Liu,J.
  TITLE     Lsr2 is a nucleoid-associated protein that targets AT-rich
            sequences and virulence genes in Mycobacterium tuberculosis
  JOURNAL   Proc Natl Acad Sci U S A 107 (11), 5154-5159 (2010)
   PUBMED   20133735
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18741]
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Gordon,B.R., Imperial,R., Wang,L., Navarre,W.W. and Liu,J.
  TITLE     Lsr2 of Mycobacterium represents a novel class of H-NS-like
            proteins
  JOURNAL   J Bacteriol 190 (21), 7052-7059 (2008)
   PUBMED   18776007
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Oshima,T., Ishikawa,S., Kurokawa,K., Aiba,H. and Ogasawara,N.
  TITLE     Escherichia coli histone-like protein H-NS preferentially binds to
            horizontally acquired DNA in association with RNA polymerase
  JOURNAL   DNA Res 13 (4), 141-153 (2006)
   PUBMED   17046956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10570331
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..112
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12498
     Region          1..110
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 markeitqyf ddidnaplaa edvnvvefav dgvtysmdvs tanrekfeea lapyiavarr
       61 vqrtnarrap qstnspernr airewaqang lqvsdrgrmp qdivdkydaa hs
//
LOCUS       WP_284758442             302 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: lysophospholipid acyltransferase family protein
            [unclassified Corynebacterium].
ACCESSION   WP_284758442
VERSION     WP_284758442.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..302
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=33827
     Region          43..249
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 maklpallsr vgsifsidrw tdsaftltsk gvetpkhpes qelvygriii raakllmryi
       61 qrlevvvmhh eripaeggal lavnhtgywd fvyggipahf rgerlvrfma kkeiwdnkfa
      121 kppmeacrhi pvdradgqas vneaierlkv gelvgifpea tisrsfevke lrqgaaiisr
      181 dsgaplipma iwgsqriwtk ggknnlrpkn aklvisvgep vevtedsiet terlheamka
      241 qldeaqqeyv rrygpmpkge awvparfggt aptleeataq dradqaerkr kreqqaqqgr
      301 kn
//
LOCUS       WP_284758429             257 aa            linear   BCT 25-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Corynebacterium sp.
            UMB9976].
ACCESSION   WP_284758429
VERSION     WP_284758429.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..257
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28145
     Region          5..247
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mqhevkiiah rgaskhrpeh tigayelaaa qgadgyecdi rltrdghavc ihdrtvdrvs
       61 dgtgavsrmt laelkalnfg tstrpagvle lrelleflqd mrhsaeagkp elfietkhph
      121 vrslqveaem hrqleaagla ggegiylisf dswslwrsrq inpqveriql rrkyhpparp
      181 llrgsgiarh agwsieqama slrgeggsap adyiwtvdqa eqlrwiaqrg arwvatncpg
      241 eaagwlqnsv gggagqa
//
LOCUS       WP_284758483             687 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Corynebacterium sp. UMB9976].
ACCESSION   WP_284758483
VERSION     WP_284758483.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 687)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..687
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=73365
     Region          8..273
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mrarhqhatp reaslapaat trpernpgha grarssatlh ssvnlrsnmk hrsamavaia
       61 lllslagvvv pfghpqaaae akdipptmli ldasgsmmar dadgqtrlda akeasknfsr
      121 svskdselgf mvygtkvgns peereagckd vttllpvgkg nagkipgevd kvnasghtpm
      181 gpalkqaake lpnegersiv lvsdgedtca pppvcdvakd lhkqgidlti ntvgflvdpa
      241 arkelqciae agggeyldak dseslaesmk vlatrtaqta esnapeikgr ddaasatevp
      301 edvelfstpl reksggaknd edgaeyfstp iaegerlaig vatmpppsqg seigfgknfs
      361 vkvevdeplc ylandndvgi idsngpffas wttqqagedc pagdfrfkvv rksgpykgke
      421 ipaevsikrl pnedlsevpe pfavdkvenr kepsaagkpr kvtpgawfdn atelnpdake
      481 tvsadivpge ahvykiktdy gqqlrggikv tsepprdhya eikqldinvl nsarqkaaia
      541 esvhvregds kafgnpvrvn yrnmvgdgke qpsdvesqka wldgeqyivi flnkslkaga
      601 nrdiskekna tatyelttel vgekipgpsf ekvsndteie esekaeepke teqaaaeeds
      661 sinwfligag vlvvlavalv altrrgr
//
LOCUS       WP_284758548             287 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Corynebacterium sp. UMB9976].
ACCESSION   WP_284758548
VERSION     WP_284758548.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..287
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30255
     Region          52..154
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mspstprnpg rspilhsglg qeatprrsll ahipdlgewn espthrvlps eprpivvvhg
       61 tvggrgnfar mvpylrstfd grdrrvfsvs ygdngttpla qsiaqtraqi aalqeatgae
      121 sfdlvahsqg glislavasr pggeavnhiv glgadfrgvh mpwsgtaret lvnrvistvm
      181 apafaeqvvg spaladalap agectvpitq iasdydrlvp lnaafalgda eptggipqhp
      241 gplrlvrvqd fypqlqvahn mlprnqkvsl lvkfalenpp apraaap
//
LOCUS       WP_284758613             600 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acetyl/propionyl/methylcrotonyl-CoA carboxylase
            subunit alpha [Corynebacterium].
ACCESSION   WP_284758613
VERSION     WP_284758613.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..600
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=63533
     Region          14..473
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          533..599
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(556,565..567,574)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            566
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mstfyneqpt palplkkvli anrgeiavri araardlgie svavysdada dnqhpvfade
       61 ayplrgesaa dtymnipall diaarsgadc vhpgygflae nadfaravqd aglvwvgpsp
      121 eaietlgdkv aarqlatkvg aplapgtdqp iesweeardf aaehgmpiai kaafggggrg
      181 lkvvheeadi eegfasagre akaafgrgec yvekfltkpr hveaqvladt hgnvrivgtr
      241 dcsvqrrfqk lveeapapfl tdeqntsiye gareicreag ytgagtvefi vaedgtvsfl
      301 evntrvqveh pvtevvsgvd ivqeqfriaa glelsfdadp vptghafefr inaedaangf
      361 vpcpglvrtf epptgpgvrv dtgvrsgsti pgsydsliak livwgpnrqv alrrseealr
      421 dlkiegvrtv ipfhkdiihh pafaedhldv ytdwvdkeyv pgfgdgntdv eaaytertev
      481 nieidgklhr vglpmsvlsg lgaapaqgaa gsesaaaqss agsaasepag edaitspyag
      541 vliswkvedg aevaegdtva iieamkmesp vkaptagtlr rsdiaeggsv aqgevlaris
//
LOCUS       WP_284758604             286 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium sp. UMB9976].
ACCESSION   WP_284758604
VERSION     WP_284758604.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..286
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29874
     Region          8..285
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mhlapiaitd padprlddfr dlnssdsrpd lpggkglvia egslvvprll asgypvrsvv
       61 gfegklsvlq dvtcsasqpa ggpvvyqvsr dvlrevagfd mhrglvaaad ripersvpev
      121 lagipagpsv iailegvgdh enigavfrna aglgvdavlf gaatadplyr ravrvsmghv
      181 lrvpwarfsg kttnwqngld avreagfqii amtpdtelsl adavhavrre qgegariaim
      241 vgaegpglte hamraadvra kipmmpgtds lnvataaaig fyasry
//
LOCUS       WP_284758680             351 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium sp.
            UMB9976].
ACCESSION   WP_284758680
VERSION     WP_284758680.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..351
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35288
     Region          31..344
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mqkrrlsspa vaiaiaaila ailfiaalai gpvtiavpdv lasvwaqitg rgeiarqdpa
       61 lgsaynvvat irlpraiiaa lvgaalavag tvmqavfrnp ladpgiigvs agaataavla
      121 ivtgfsavaa walpasaflg algavaivql aaamrgggpa tlvlvgials aflgavtsaa
      181 ianapsdsdi rgvafwlngd lvartwehva iaslpivlgi vllllfsrdl nillmgdqaa
      241 rttgvnvrrv rvvtltvaal itasavavsg vigfvglvvp hlirliigpn hksllptaal
      301 agaafllaad tiarmlfapv tlqtgtvvaf igspiflwll lrgrrpagws a
//
LOCUS       WP_284758839             402 aa            linear   BCT 25-DEC-2024
DEFINITION  proline-rich domain-containing protein [Corynebacterium sp.
            UMB9976].
ACCESSION   WP_284758839
VERSION     WP_284758839.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12172186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..402
                     /product="proline-rich domain-containing protein"
                     /calculated_mol_wt=43366
     Region          <2..51
                     /region_name="Pro-rich"
                     /note="Proline-rich protein; pfam15240"
                     /db_xref="CDD:464580"
ORIGIN      
        1 mnspnqnqpy dwgvpsqpan gpaqqpagng apppqgsqgp qgpvggqppq gqqdkprknl
       61 kpwaftalav vviaalvyag lwvyqstrgt ekgplgwdne qiakhvsknk ladcdlgeef
      121 wnsvglkdvq vsgdeetcqg wyetadggev lvtmeidsss ssfsvpddsv slssdglrgw
      181 taqeksedgy lsteptekct yysksglfvg tlstpatcda lkplasqltn ldiqdreata
      241 skdltdfdsp eylpvnvepv evssplwekl gknvaktgea qkvkddgysg skitvdkidv
      301 dkaqvcadat frlgretdrf afqfhvpdmr vvfptgsalk ldrdperlrl kegatkklsy
      361 cgdledaeyv gyrggqaylv sdldssgdle gsawkfdlat qd
//
LOCUS       WP_284758825             236 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium sp. UMB9976].
ACCESSION   WP_284758825
VERSION     WP_284758825.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 236)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..236
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26681
     Region          57..230
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mrrwtglnva errqlgptva vstvafaidp phvegaspal wvplvrrirp pfegawalpg
       61 gptewnktlt etalenlvaa aqaepnyleq lyafgsvers aeaqrtvtia ywaqfrdsdf
      121 qqqcrpeqqn iawfrtddlp plafdhaeii aagidrlrrr tekalvahrf ledsftiael
      181 rqvqevilgk kldpanfrrq vlasgdveet gkhqegtkhr pakyyrfvpe sdrpel
//
LOCUS       WP_284758878             375 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium sp. UMB9976].
ACCESSION   WP_284758878
VERSION     WP_284758878.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..375
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40112
     Region          7..368
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mnhgpgltfr flaaqvlvvv islmvaaava ttvgptlfhd hmlmagredp slelfhaeqa
       61 yrdanlitla valptalisa llaslwlsrr lrtplqdltr aatsltagns rirvpagkag
      121 pevttlahaf ntmadrleht eqlrrqmlsd lahemgtpls vltvyldglq dgvvdwnnat
      181 htimadqltr ltrlmedidd vsraqehrid ldlaeeelgd llrtaaaaag eayadkgvdl
      241 qvetitdtdr vlvdrqrfgq vmsnllsnal rhtpaggqvr isvhrqgast alihvaddge
      301 giptdqlghi ferfyrgdaa rsrnnggagi gltiskalie ahggtltats pgpgrgavfa
      361 lclplsppds eeaar
//
LOCUS       WP_284758958             297 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [Corynebacterium].
ACCESSION   WP_284758958
VERSION     WP_284758958.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..297
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32817
     Region          22..243
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mtplprisnr iasrrtapgr tarrtlavfd ldktivdtsa smaygrpmak rgiittgeml
       61 rigamlfsym ltthtdenld atkdalssmi rnrpaaslra iaedalqevl ipyvyaeard
      121 fifehhklgh dvaiitasar vlvdpiarel qadyliatel eeidgtytgk vlhfnkgqak
      181 vdklmelver ggydlsrsya ytdshtdlpl leavghpyai npdrqlrkia rerdwpieyf
      241 skpeplfkpg kvlagagtla flgaaatgvv lwlrqraqdv gsastpqlla rlmprra
//
LOCUS       WP_284759135             212 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Agrobacterium sp. fls2-241-TYG-188a].
ACCESSION   WP_284759135
VERSION     WP_284759135.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. fls2-241-TYG-188a
  ORGANISM  Agrobacterium sp. fls2-241-TYG-188a
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Agrobacterium sp. fls2-241-TYG-188a"
                     /db_xref="taxon:3040275"
     Protein         1..212
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23564
     Region          51..206
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mtvsamdfsa edfrrrvlee gqgvaerdvd dngdhvlnpg vrlagdgirl kdaavlvpvv
       61 dyghharvif tlrtatlrkh sgqisfpggg idaedaspee aalreteeei glsrsyieav
      121 grlpdyvsgt gfrikpvlav vkpgfeltln ptevadvfev plgflmnpen hrrasrifqg
      181 rerffyempy geryiwgita gitrsiyerf ys
//
LOCUS       WP_284759260             267 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Corynebacterium sp.
            UMB9976].
ACCESSION   WP_284759260
VERSION     WP_284759260.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB9976
  ORGANISM  Corynebacterium sp. UMB9976
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 267)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Corynebacterium sp. UMB9976"
                     /db_xref="taxon:3046354"
     Protein         1..267
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29035
     Region          1..266
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 msvvlitgag rgigaatara aaqagydvav tdingdaars vaeelprnvr aigvdhdvrd
       61 eeawstvfre verqlgpvdi lvnnagmiht gwardltndq hrqmmdvnff gpmygtleam
      121 rymkdrgghi vtvcsmtsfl plpgyssyga tkhalrafin tvaieerasr vaftlvhppg
      181 vrtemleqek rdpsavaafa eksvgpevia etivrsfkkr plfgrpaeiv fpalggrfqr
      241 wvgaqavlmr lampfvlasg rralrkg
//
LOCUS       WP_284759429             412 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Agrobacterium sp.
            fls2-241-TYG-188a].
ACCESSION   WP_284759429
VERSION     WP_284759429.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. fls2-241-TYG-188a
  ORGANISM  Agrobacterium sp. fls2-241-TYG-188a
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Tomich,M., Planet,P.J. and Figurski,D.H.
  TITLE     The tad locus: postcards from the widespread colonization island
  JOURNAL   Nat Rev Microbiol 5 (5), 363-375 (2007)
   PUBMED   17435791
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18792929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Agrobacterium sp. fls2-241-TYG-188a"
                     /db_xref="taxon:3040275"
     Protein         1..412
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=44079
     Region          5..>56
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
     Region          <140..400
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mmferfdtmr clrrlladrq gnfamitala lpmlmgaagv gleftramqv ksdlqnaada
       61 atlsaatqfr esegkksdee lkaqvaqimm gqsvtkelse aeakilensi nsvtsrnett
      121 kgtnfkistt vnyrlplnpl lglvgatslt lsatstaess fnngaplsly lvldhsgsma
      181 fktdsidsrk stcsnydeas wpkpmrsnrp cyidkmtslk tavsflldtl nksdptaksn
      241 gnpasqlvrt savayndkas ptqgldwgtk rasgyvnals atggtdatga lnaafnalks
      301 tnaseieahk qagnksfqri ivlmtdgemt gnsaswsypv dnavrttcaq akaddikift
      361 vafmapdrgk sllqacatsa enyyapenme eiveafgdia rkasgnvsrl tn
//
LOCUS       WP_284759586             482 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Agrobacterium sp.
            fls2-241-TYG-188a].
ACCESSION   WP_284759586
VERSION     WP_284759586.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. fls2-241-TYG-188a
  ORGANISM  Agrobacterium sp. fls2-241-TYG-188a
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Agrobacterium sp. fls2-241-TYG-188a"
                     /db_xref="taxon:3040275"
     Protein         1..482
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=51740
     Region          215..455
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mrshyvalsv ywvslsvall nygsvelltv tllalptffl fmvllstggi pthtgstlwa
       61 aaslmvllla wigaqtvipl dapfsegawk eiqaflpgaa stisvspadd raaamriavp
      121 fgifmvglll fstderasga lrllsglsgl isifsivqft iapdqllfda kraylssltg
      181 ifvnrntaat ffglalllna siveasfgki gfrrvssail agarlspamq tqlwfaafhv
      241 vllfstltal mltksrggvv aaliaaccll llkafsrfqk qeksglapak errwirilig
      301 asillaivii ffslgqrvll rsqiqstfed grfcvlpgiv tavwdnlplg aglssfptvf
      361 payrdatcgi agvwdrahnv yleglltlgi vfpllallfs lwlsavfiig irrrrsarya
      421 gelgiaslvl iaahsaidfs lqisglaiyf aamlapivtl slrppgkkrt lkeqstrhsi
      481 ta
//
LOCUS       WP_284759593             337 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Agrobacterium sp.
            fls2-241-TYG-188a].
ACCESSION   WP_284759593
VERSION     WP_284759593.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. fls2-241-TYG-188a
  ORGANISM  Agrobacterium sp. fls2-241-TYG-188a
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18827174
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Agrobacterium sp. fls2-241-TYG-188a"
                     /db_xref="taxon:3040275"
     Protein         1..337
                     /product="ArsR/SmtB family transcription factor"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36922
     Region          8..78
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(12..13,15,18,21..22,25..26,29,59,79..80,82..84,
                     86..88)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(13..14,18..20,33..35,44..47,49..50,53..54,56..57,
                     63..65,70..72)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(33,36,79)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
     Region          120..276
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mtlgldnlvg llkaageptr frllallsag dltvtdltei lgqsqprisr hlkllaeedl
       61 idryqegawa yfrlkqdgkg aevikqllsv asstdavllr dyerlsgvkr vraeraqdyf
      121 srnasawdel rrlhvsddav egallkligt tpvdsmldlg tgtgrilqll sgiyrraigv
      181 dasrdmlava ranldkagva hasvrhgdil nlplegqdfd lvvvhqvlhf ldqpemalae
      241 aarmlrpngr lvvidlaphs leylreehah vrlgfshqtm eewlkkagln peqavdlhsg
      301 nasaqsldvt iwvardprll iageepieap llsagra
//
LOCUS       WP_284759657             441 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Agrobacterium sp.
            fls2-241-TYG-188a].
ACCESSION   WP_284759657
VERSION     WP_284759657.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. fls2-241-TYG-188a
  ORGANISM  Agrobacterium sp. fls2-241-TYG-188a
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Agrobacterium sp. fls2-241-TYG-188a"
                     /db_xref="taxon:3040275"
     Protein         1..441
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=48178
     Region          150..354
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mkilkstlid pdhnkiygif amassflvfa ysqqigaiav vfyyglwisl vfvdyrrvlg
       61 nysryfwifa favfcflsaf wsqapgvsfr aaiqylshia caliamrvls tatltqggal
      121 gcaavlvysl ifgryesdal dgsytfvgaf asknqlglfa slgcllsygt lilsarkgwv
      181 fialitgals fynllasqsa tsiittmavl alsvamqstl vlapkhrvil clmvflgall
      241 cgtvvlqigg tgslleafgk dstltgrtyl wqqgiaalse splfgvgyqg ywvtgladae
      301 rlwdefyips rngfhfhnty ietavesgif gtvclilvvl ttlwghlarf ltrrrhvesl
      361 llfavaallt crsfveidvl fayqigsfll yfvagkltvc ravivrpvtr tirtvryact
      421 kdtwaegsga kilsslshia d
//
LOCUS       WP_284759704             417 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Agrobacterium sp.
            fls2-241-TYG-188a].
ACCESSION   WP_284759704
VERSION     WP_284759704.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. fls2-241-TYG-188a
  ORGANISM  Agrobacterium sp. fls2-241-TYG-188a
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Agrobacterium sp. fls2-241-TYG-188a"
                     /db_xref="taxon:3040275"
     Protein         1..417
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44764
     Region          6..415
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mkssgkcdvl vigtgiigvm salylqnagr svtflergei argasagnag ilafpeiipi
       61 papgimkkap rwlvdplgpl svppayamki apwlwrfwka ssprrfqygl dvqmrmmala
      121 asemqkvaav pelaghisnt gtldlydnrt sfdaarhdwd lkekagiafs rvdrseierl
      181 qpglapqfqh amftpgglqv adpyeftrsi adlvlargat lhkgeatrie mvgestivsl
      241 ksgekidadk viiacgawsk tlaaslgdvv pletergynt tlpegafdlt rqlyfndhaf
      301 vvtplssgir vggavelggl dlppnfrrse allnkakrfl pglkteggkq wmgfrpslpd
      361 clpvigpsra snsviyafgh ghlgltqsaa taklvtdlvt gahptisvdp frasrfg
//
LOCUS       WP_284759859             473 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Agrobacterium sp.
            fls2-241-TYG-188a].
ACCESSION   WP_284759859
VERSION     WP_284759859.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. fls2-241-TYG-188a
  ORGANISM  Agrobacterium sp. fls2-241-TYG-188a
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Agrobacterium sp. fls2-241-TYG-188a"
                     /db_xref="taxon:3040275"
     Protein         1..473
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=51312
     Region          59..464
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 madaprsnrw talsgamlaa cmvvsfpylh afaqedvapp astqdatqds aqpaddvdal
       61 errrdqnrqd lqelvdsigl sedksrqlqd siaalnqdta rikdeliasa arrkdleaki
      121 sdgedrlakl giredavkas lrerrdvlae vlaalqrmgr npppallvsp edalasvrsa
      181 illgavvpgi rsetdklvfa lkeltdlrqa iavekeqltg tmtasleeek rldllrlene
      241 krntqtasal eaerkrseel aakatslegl vssleneiss vreakekerl eqerlaalsq
      301 serdkveaqt dagmpdknri apayafsslk gklampvsge vlrrfgdadg tghfskgivv
      361 atgpealvta padgfvvfag efrsygrmii lnagdgyhlv ltgmdnvrtr qgmfvfsgep
      421 iasmgakrva saaalaletd kptlyiefrk dgvpvdsqpw wtakntgrar nds
//
LOCUS       WP_284759864             303 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Agrobacterium sp.
            fls2-241-TYG-188a].
ACCESSION   WP_284759864
VERSION     WP_284759864.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. fls2-241-TYG-188a
  ORGANISM  Agrobacterium sp. fls2-241-TYG-188a
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Agrobacterium sp. fls2-241-TYG-188a"
                     /db_xref="taxon:3040275"
     Protein         1..303
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32864
     Region          8..300
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mvdfyfnntv rprrsllsvp ainkralakl ktldcdgvif dledsvapdl kdearnnlla
       61 ffkdtplagr etiirinpvs vnvgqrdlia alecgpnail lpkveqpsqi qdvadllaea
      121 dapddikiwa mietpkgiln aasiaessht eaarlgafvv glndlrkath vpaqpgrayl
      181 vpwlmqtvla araygldvfd svsndfhdld afaaecdqgr amgfdgkmli hpaqidaanr
      241 afapteeala eareiiaafa kpesvglnvi nsngrmierl hvgqaerlva maeiidhrka
      301 ekp
//
LOCUS       WP_284759937             170 aa            linear   BCT 25-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Agrobacterium sp.
            fls2-241-TYG-188a].
ACCESSION   WP_284759937
VERSION     WP_284759937.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. fls2-241-TYG-188a
  ORGANISM  Agrobacterium sp. fls2-241-TYG-188a
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Schwartz,C.J., Giel,J.L., Patschkowski,T., Luther,C., Ruzicka,F.J.,
            Beinert,H. and Kiley,P.J.
  TITLE     IscR, an Fe-S cluster-containing transcription factor, represses
            expression of Escherichia coli genes encoding Fe-S cluster assembly
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 98 (26), 14895-14900 (2001)
   PUBMED   11742080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Agrobacterium sp. fls2-241-TYG-188a"
                     /db_xref="taxon:3040275"
     Protein         1..170
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=17661
     Region          2..140
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mklsegveqa ihctaflagl sedgvlsaaa laelhgvsts yllkhlqals gagivattpg
       61 prggyrlaka pkdislldiv lavegpapaf rcaeirqrgp nplpqryftk pcqinaamlk
      121 aekayraela kvsvadllan lgadddggia argcaflelh erktgnrass
//
LOCUS       WP_284760194             220 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Curtobacterium sp.
            MEB011].
ACCESSION   WP_284760194
VERSION     WP_284760194.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. MEB011
  ORGANISM  Curtobacterium sp. MEB011
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Curtobacterium sp. MEB011"
                     /db_xref="taxon:3040285"
     Protein         1..220
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22705
     Region          <65..158
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mtmhapvsfg agggepyara lrtdghlrlt dadrpdavtt mdvgrwsaaa drvdrslldd
       61 vdggvidigc gpgrmlvaar srgipalgvd vsaeavaiaq rsggtalqgs vfdavpdegh
      121 wdtalvidgn igiggdptal larcraivrt ggrvivetnp evaadrvyta rvvdadgnes
      181 agfpwaevgl dalhrhaaea glvarqswta egrnfcella
//
LOCUS       WP_284760280             318 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Curtobacterium sp.
            MEB011].
ACCESSION   WP_284760280
VERSION     WP_284760280.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. MEB011
  ORGANISM  Curtobacterium sp. MEB011
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Curtobacterium sp. MEB011"
                     /db_xref="taxon:3040285"
     Protein         1..318
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34334
     Region          4..312
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 magpsarmlt llsllqvhrd wpgdelagrl evsprtvrrd vdrlrglgyr vealrgpagg
       61 yrleagsdlp pllfdddqav aialalavap asgadvaesa aralatvrqv mparlrsrvd
      121 avqavtatsr tttdpevlva vseavhlhev frfgygedet phrvephavv arngrwylld
      181 wdadrddwrt hridritprm rtrvpftprp ipggdaaafv sarfkgaavd dvwpctgsvt
      241 ttagdarria pylpedavve qlegdrarvt lgswswdgla gvvsgfavdf vvagpeelve
      301 avadladrlr tagtrrpa
//
LOCUS       WP_284760414             486 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Agrobacterium sp.
            fls2-241-TYG-188a].
ACCESSION   WP_284760414
VERSION     WP_284760414.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. fls2-241-TYG-188a
  ORGANISM  Agrobacterium sp. fls2-241-TYG-188a
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Agrobacterium sp. fls2-241-TYG-188a"
                     /db_xref="taxon:3040275"
     Protein         1..486
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=54077
     Region          112..486
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 midlfttywp hllaalslfm gasaaihatm tkqevrtalg wvgvivlspv igaviygiag
       61 inrirrsalg qqrslmhgti mdrvarfdad salvakrfgr rfvsmknvgd rvtrnalttg
      121 neidvlpsgd iayremldai daakrsiile tyifdqdrig lrfvealsra rdrgvevrvl
      181 vdavgarysv psimpsleka dvraavfngn viiglrlpya nlrthrkilv vdgrlaftgg
      241 mniregftae fspenysrdt hfkvkgplvf dlfsvaaedw rfatrelldg pvwdvtlpes
      301 kpgspvvgrv vasgpdnsie tshkllmgaf siarssirim spyflpdrel isalttaarr
      361 gvqvdiivpa nnnlklvdya mtaqfdqilr nqcriwrgag afnhskllvi derwayvgss
      421 nldprslrln fevdievidd rfaqaiserm aqamenanpv kledlrarpf vlrlfervlw
      481 laspyl
//
LOCUS       WP_284760566             424 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Curtobacterium sp. MEB011].
ACCESSION   WP_284760566
VERSION     WP_284760566.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. MEB011
  ORGANISM  Curtobacterium sp. MEB011
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Curtobacterium sp. MEB011"
                     /db_xref="taxon:3040285"
     Protein         1..424
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=44773
     Region          38..386
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 matttlthap tdaptsarpq hrtaaparag tgapeapppp lthrapaldg lrtlailvvv
       61 lyhlhvpqfe ggflgvtvff vlsgflittl llgerrrtgr vrlgsfwvkr llrlypalla
      121 lvvvglllwn wvgdykgasl hsgeaafial tytgnlfraf wdtsqgvfah twslsmeeqf
      181 ylvwppvlvl laalrvrrrw llaglgvlvv gasavswasy rtpsggttpd vyfspvlgvv
      241 plaigcglal llddervrvr aagvlghlat wvglvllvav llgidddwte hastfgivlp
      301 atglvsavai gglvsvrspv saalgwtpvs wfgrrvsysa ylwhplvial lgtfaigpwg
      361 tvglvgavvi vsigaayave vpverfrara raarsasapm paaapvpapa papsseqktp
      421 gtar
//
LOCUS       WP_284760544             793 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Curtobacterium sp.
            MEB011].
ACCESSION   WP_284760544
VERSION     WP_284760544.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. MEB011
  ORGANISM  Curtobacterium sp. MEB011
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 793)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Curtobacterium sp. MEB011"
                     /db_xref="taxon:3040285"
     Protein         1..793
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=80328
     Region          44..550
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mntshttgsa gattrrrlga gaalatagvl valsvpsaav aaegdttidi idvndfhgri
       61 esegtaadka agaaklagvv qsyreanpnt ifasvgdnvg astftsliqq daptidalna
      121 mdldvsaign heldkgqsdl tgriedraew pyvsanivka gttdpaftpy sivekggvki
      181 gfigattedl ipglvspggv eglamapivs qvnkyaeqlt dgkddndead vlvllvhega
      241 ptnvladatg sgvfgeitsg vsskvsaivs ahthatynhs iagpdgtkrp viqagsygva
      301 fghlqltvda dkqltgitse vksvngetrv ptdptsvnav adivtaakav advegskklg
      361 titgdlrrav qsdrttenrg gesvlgnyia evqrsatern gsqvafmnpg glrtdmiaas
      421 sgagdpdgtv tykeaalvqp fantlvtedm tgqqiknale qqwqpdglpr pflklgvsdg
      481 faytydpskg rgdritgmtl dgepialtdt lkvtvnsfls tggdnfgafa tgtniadsgq
      541 vdlqaqvdyf lanptvtppt dqravgvtvt ptpsdgfqpg deieldlssl vfssedpaka
      601 gtvsvsadgk elasaaidpt iidtndeqgr atltvtvpdi eapaaraaar tagsvslaav
      661 aepvattdap lvvslpgdqt vtlavtipva aavdptdptd ptdptnptdp adptpgtggg
      721 vtpgpgagtg ddagiggvgg tdddpraggd laytgadlta paiaagllll agttalvvlr
      781 rnrarraamv ltd
//
LOCUS       WP_284760586             357 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Curtobacterium sp. MEB011].
ACCESSION   WP_284760586
VERSION     WP_284760586.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. MEB011
  ORGANISM  Curtobacterium sp. MEB011
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Curtobacterium sp. MEB011"
                     /db_xref="taxon:3040285"
     Protein         1..357
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38504
     Region          13..354
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mtlrlhdldl rgfasdnyag vhpeilaaia eandghqtay gedvytarlh evvrqhfgsq
       61 aeafpvfngt ganvvglqsm lprwgavvct stahihtdea gaperiggik lltvdapdgk
      121 ltperidrqa wgwgnehraq plvvsitqtt elgtaytvde irtiadhvhs lgmtlhmdga
      181 risnaaaslg vplrdfttda gvdvlsfggt kngmlygeai vvlnpsaseg lhylrkmnmq
      241 lsskmrfvsa qlvallsddl ylrsaghana maarlrgale agiadgsirg vgfsqqtqsn
      301 gvfatlpagv adrlrehfrf ydwdasrnev rwmcaydtse qdvddfvaal treldaa
//
LOCUS       WP_284760575             743 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Curtobacterium sp.
            MEB011].
ACCESSION   WP_284760575
VERSION     WP_284760575.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. MEB011
  ORGANISM  Curtobacterium sp. MEB011
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 743)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 743)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Curtobacterium sp. MEB011"
                     /db_xref="taxon:3040285"
     Protein         1..743
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=75798
     Region          4..742
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtdrtveldi tgmtcascan rierklgkmp gvtatvnyat ekaqvqvaad gtadpqslia
       61 avesagygat vpappaaada eptadqdrae plrrrlvvsa vlavpvvvls mvpalqfpnw
      121 qwlaltlaap vavwgalpfh raawvnarhg aatmdtlvsv gvlaafgwsl yalflgdagt
      181 tgmhmtfswf atdpeaadly levatavtvf ilagrymear aktqsgaalr allelgakda
      241 avlrdgaehr vptsslvvgd vvvvrpgeri psdglvqdgs savdrsmltg esvpvevgpg
      301 drvtgatinv ggrlvvavtr igadtelarm grlvedaqtg kaevqrladr vsgvfvpivi
      361 alavlafvgw lvlggsvtaa ftaavatlii acpcalglat ptallvgtgr gsqlgiligg
      421 pqvlertrgv dtvvldktgt vttgsmtlrs vtvvdeteda vlrlaaaved gsehpvarav
      481 ttaarargad lpaaeqftat agagvqavvd gdvvlvgttr wladawsitl ppvladavdg
      541 aeadgatavv varngsalgv vvvgdtvkpe aadaitrfra lglrpvlltg dndgaarava
      601 arvgidevha ratpasklet vrrlqsegrs vamvgdgvnd aaalaaadlg iamgagtdaa
      661 iaasditvvs grltvvadav rlsratlgvi kgnlfwafay nvaaiplama gllnpvlaga
      721 amafssvfvv tnslrlrrfa pqs
//
LOCUS       WP_284760655             681 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Alloscardovia omnicolens].
ACCESSION   WP_284760655
VERSION     WP_284760655.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 681)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..681
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=74574
     Region          12..605
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mlreyttepv ytttdddtif klltdraase pdsvvaqalr gprrqwvdit asqmlddvrk
       61 vakgllamgi skgdsvliys ptcyewgvvd facasigais vpvydtdspk qvaqivsets
      121 pqvafaggde rsltleamrq spdnsvrysf nmqsnglqav tdwgkkvsde tldeaiahih
      181 addpltiift sgstgkpkga lishrnfvht vksgwavlpt mlmadptrll lflplahafa
      241 ryiqytaiga hgvvgylsdt khlladlrgf rptymlavpr vyekvynaas qkagnglkgh
      301 vflvaykhfv qwskdeqegk ahtwrqklhh kffmsvvgss ihsamgngmr fmacggapmn
      361 vdlahffngi ddltfiqgyg ltetsapcmv nfeaknhvgs vgrvgpgfsa rltdedelei
      421 kgpsvflgyi napeqtadvm ngewlrtgdl asidddgyvy itgrkkdlii taggknvspa
      481 plediiatcp ivshavvvgd nkpfiaalit lepdmlrqwl eghgldanmt pleaakneav
      541 rafiqeyidh ananvsraes vrkfvvlpse fsqeagtltp slkivrprvi kqygqvidei
      601 lyapkpsamt daatakimaa aeqfnkqvqp tvkaardmie pmynkamenv kdnvaefseq
      661 lserlrstat hddaetenee k
//
LOCUS       WP_284760685             686 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Alloscardovia omnicolens].
ACCESSION   WP_284760685
VERSION     WP_284760685.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 686)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 686)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 686)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..686
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76329
     Region          1..503
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mgsflliiqi giavvissll spyiprvsmp lvqiflgilw ffipglplin ldseffllvf
       61 iapllyfeam hisrsglrkn lgitlslavg lvllsiviag ytltfsmadi plaaafalga
      121 tlsptdavav sqigadaqlt erqetvlate slfndasgiv sfqfalatli tgtfsplkfs
      181 lnvlysfigg aavgavlgim lnhlivrlrr mrletttnri lielmfpllv fgvaddifea
      241 sgviavvaag lvaryhrvgv gedlaevnrv sgavwdvvaf vlngsvfvll gielplamrq
      301 tivndkvntv gmvltamvlc mvlylvrffw iaatlrttks hetglrrkmt kerwhsaavm
      361 tfsgakgtis lilafslpsq ldtmtdfpvr taflfiaavy iilslliani ivpilapaek
      421 dedghkfala nlemlnrtlv aisridnpdq hiaieavmrs ynariarqrg kvltpeelat
      481 lhsariemrh wqstwlenya rrnpqytdac qrllapieys lthdgagwfk hvrtrmyflr
      541 lktvvwirvm raairflwtr tvqvttrsed veyrrsevtr iqlqllqdsi hhafilinyd
      601 qvppvvgsti vselrtliks lqmpsmakpg attfesfphq fnevlsqaya ieletirtma
      661 dkkeitreqa rtmrhnvflm qsdsva
//
LOCUS       WP_284760784             221 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Curtobacterium sp.
            MEB011].
ACCESSION   WP_284760784
VERSION     WP_284760784.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. MEB011
  ORGANISM  Curtobacterium sp. MEB011
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 221)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Curtobacterium sp. MEB011"
                     /db_xref="taxon:3040285"
     Protein         1..221
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=22628
     Region          6..211
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mplitiigag pglgleiara fgkkgfdval varsqakvda lasalvaegi qargftadvs
       61 epdtirgalr sireslgpid vleyspadra lesvdavdvt mdnlqpqidf ylggaiaavg
      121 avlpdmiaag rgtvlvttgg galartpvrg nvniaaaglr nwilnlgaav aekgvyvgfv
      181 aitaligggr pdaepaviaq syvklhderr daelhyvayd g
//
LOCUS       WP_284760799             368 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Curtobacterium sp. MEB011].
ACCESSION   WP_284760799
VERSION     WP_284760799.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. MEB011
  ORGANISM  Curtobacterium sp. MEB011
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Curtobacterium sp. MEB011"
                     /db_xref="taxon:3040285"
     Protein         1..368
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36704
     Region          51..362
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mpdrlstvlp apsrsgrida vlclmrrarr raavriavla vvlalvtvaa mmigpvpiap
       61 thvigilveh vsgaraghws asadeivwgt raprvvmgii agavlavaga vlqalvrnsl
      121 adpyllgins gastgvalvv lvigsgsalv fsgaalagai gavllvvala gtasrrgplr
      181 lvlaglavgy alnaatsflv fwsdspeaar svlfwllgsl tsvqpialaa aaitggvglv
      241 alvviapfid alasgddsar sagidperar lglmvavsam vgvivaavgg vgfiglvvph
      301 larqlvggrh ravlpvsall ggsllviadt variafapqe ipvgvvtgvl gapfllvllr
      361 rtapatap
//
LOCUS       WP_284760815             975 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Curtobacterium sp. MEB011].
ACCESSION   WP_284760815
VERSION     WP_284760815.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. MEB011
  ORGANISM  Curtobacterium sp. MEB011
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..975
                     /organism="Curtobacterium sp. MEB011"
                     /db_xref="taxon:3040285"
     Protein         1..975
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=103064
     Region          <117..231
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <436..916
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 maggtksttr srastssrgn gtrgssrtqa ttkklpqaap tpvfreqnpl vtfwlamahg
       61 vgamfrllgk etlekdqrrd gfpfllflla iaggvvewln ptnsvsvald aytfgglfgr
      121 lafalpvimi vfagwlfrhp asvhdntrig iglgilivsi aslchvfggr psaadgmpal
      181 aaaggvlgwv vigwlvtiat awvavpvaiv llvlslfiit ktppnklgrr lhelyaylfg
      241 apapaaepda dtaaavaepv artrtskrgk kgdadfqlfd dlgfgdeqaa adaeaggdnv
      301 pwwrrnksgr eedpaydspv lppatgvapa aapvapaapv apvpspnaga aaglvdvtpa
      361 epasvnlnds veqdlqdaeq alrafgtdvp arpeptadir pavpevlsep evvdepedid
      421 aaaelsaaaa gpdddpskpy rlpaattlss gtpsvarsqa nddivaaitg vltefkvdak
      481 vtgfsrgptv tryeielgpg vkvervtals knlsyavasn evrilspipg ksaigveipn
      541 tdreivslgd vlrsnaarks khpmtigvgk dveggfvvan lakmphllva gstgsgksvf
      601 insmitsllm rakpsevrmv lvdpkrvels iyagvphlit piitnpkkaa ealqwvvkem
      661 dmryddlasf gfrhvddfnk aienneivlp agserklkpy pyllvvvdel adlmlvaprd
      721 veesivritq laraagihlv latqrpsvdv itglikanvp sriafavtsv tdsrvildqp
      781 gadkligqgd alflpmgssk slrvqgawvq egevaevvqh vtrqaqpeyr qdvqavverk
      841 eidadigddl elllaaveqv vstqfgstsm lqrklrvgfa kagrlmdlme srdivgpseg
      901 skardvlvta dqlpavlakl rgeeppaaaa paapaptpsg dgdrygadpv gdmtrgydev
      961 hdepdedawg ltgre
//
LOCUS       WP_284760868             285 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Curtobacterium sp. MEB011].
ACCESSION   WP_284760868
VERSION     WP_284760868.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. MEB011
  ORGANISM  Curtobacterium sp. MEB011
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Curtobacterium sp. MEB011"
                     /db_xref="taxon:3040285"
     Protein         1..285
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29115
     Region          3..284
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mnrvpaplla ltamvsvqlg aaiakthfdd vgavgaatlr lvigavvlal vvrprvrhwt
       61 raqwlgavgl glalggmnvf iylsfasipi gvavtieflg plalslvhtr rwrdalwavl
      121 alagvvllgv gptavtevgg vvwavlaagc wagyivmnrh vgaaipgvdg lvvsmvvaml
      181 vslpfglrsv vdgvvrepal llvfgavavl ssvlpyalem lalrrmptrv fgvlqslgpa
      241 iaalaglvvl aeglsvletv alacvtaasv gvtlsarrrr ggpvg
//
LOCUS       WP_284761044             489 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Curtobacterium sp.
            MEB011].
ACCESSION   WP_284761044
VERSION     WP_284761044.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. MEB011
  ORGANISM  Curtobacterium sp. MEB011
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Curtobacterium sp. MEB011"
                     /db_xref="taxon:3040285"
     Protein         1..489
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51241
     Region          1..365
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkdaplanda hpavaavvdq vdelfrarve qgiapssvwg vfdrsglvas gghgdrgdgq
       61 rpdadtvyri asctksvtaa tlltlvargl ldldapitdf vpafdavalp tpdfpvptvr
      121 mlltmsagfp tddpwadrqe sisdaeldqv lragllfdsl pgtrfaysnl gyallgrvvs
      181 vvtgqpftqa aseivlrplg ladtvfrade ssgfvvtgvr ghegdweplp mtgpgafssi
      241 gglfstvrdl arwathlgsg fsgapepgpv spadrrlmqq amrvvppsvv pgspratayg
      301 fglfveqddr fgelvshsgg ypgfsahmrw svrdglgvva fenatqakvs aaaqqahdlv
      361 lgaalttdap aatgpstgaa vtsratraaq aavmrlladw rddladaict pnvamdvpyd
      421 rrrravaqav sevdadlaat pvaesssaps hlrwwmpgac grlrveirla pvgaglvqtl
      481 nvvaepser
//
LOCUS       WP_284760965             234 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Alloscardovia omnicolens].
ACCESSION   WP_284760965
VERSION     WP_284760965.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 234)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 234)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 234)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..234
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=26522
     Region          1..222
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mrvaiiddvm qeaedtktlv lsrdaasnti ifssgtefvq aykdkhdfdv ifldiemhgl
       61 dgletarair eydqqvvivf ttrmaqyava gyevdaisyl vkpisaesfs lawrkierii
      121 ssradehial ettdgnlyvk tsdiyymevr shklyyytah gvltawnslk aaftqvknsn
      181 falisrynvv nlahvnkydp vsgdimvhdt llhvsrsarr eisnkllefh arna
//
LOCUS       WP_284760880             486 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Alloscardovia
            omnicolens].
ACCESSION   WP_284760880
VERSION     WP_284760880.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..486
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51363
     Region          2..481
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mtydydvlii gsgpggyata lrtselglst aviektdvvg gtclnrgcip tkayltaaht
       61 lhdvhragsw gldisvnsin mpalktakdk tvagvvkglt qhmkarsidi ihgegslsga
      121 hnvsvtdges trelsahhiv latgsyatpl pgfdffhets tavseaiadk kvpvlssdea
      181 ldldiplnni vivgagaial efaqfwnalg thvtvllrkd tplsrwdshv sstlmrtlkr
      241 dgvrfeshst ltgagdgevt ysiadpkkdt vtektipadf vlaaigrspr ttaswlkqag
      301 ialtstnrvi tdeygrtnle nvwavgditd gymlaheafe qalvvsesia glptqpvdpl
      361 tipqvvygmi davsvgytss qaqnagfeqv eetvvpqlsn prvamlgsng ttvivsalns
      421 ektervvlgv hmagpqasei agaareiiqn riplsqaara lfahptises lgesllkadg
      481 rplnvr
//
LOCUS       WP_284761059             509 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Curtobacterium sp. MEB011].
ACCESSION   WP_284761059
VERSION     WP_284761059.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. MEB011
  ORGANISM  Curtobacterium sp. MEB011
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Curtobacterium sp. MEB011"
                     /db_xref="taxon:3040285"
     Protein         1..509
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=53158
     Region          128..470
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtlrrrlvls ivalvvavsa vigagsiial fsiqrsaide qlqfatnraq rsveqqggsg
       61 pgldigrpsg qasgtltvyf lngdvivgsv ldnaggierl sapvvaplgg vhvdgrphti
      121 dlggdlgryr vtaatvgpav lvvglpmapv yesvwkllgv vlvvtglall aaslvaalvv
      181 rrslrpldrv aetastvarm pldrsdaldg vrvpdtdprt evgrvgsafn rmlghigsam
      241 qarerseqkv rqfvadashe lrtplasvrg yaeltrrmgg dlpkdvvyam sriesesirm
      301 tsmvedllll arldegreiq faevdltglv ldavndahaa spehpievdv ppepvtitgd
      361 aarlhqvivn lvtnarthtp egtritvgla pvdggvdltv rdtgqgidpe flpklferfa
      421 radssrsrtv gstglglaiv aavvqahggr vevtsepgdt vftvhlprdp aaaaaaagsv
      481 asssssaepa eragsadwsa tpaavdrth
//
LOCUS       WP_284761112             334 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Curtobacterium sp.
            MEB011].
ACCESSION   WP_284761112
VERSION     WP_284761112.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. MEB011
  ORGANISM  Curtobacterium sp. MEB011
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Curtobacterium sp. MEB011"
                     /db_xref="taxon:3040285"
     Protein         1..334
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=35497
     Region          12..327
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mptppnehgp lraavvvnpt kidaarlrav lrteerahgw deslwlttsa dddgraaara
       61 acaahpsvvl vaggdgtlri vaeelrgtgi pvallpsgtg nlfarnlglp lgdlqrsvra
      121 gltgvdrpid vgladltdpa gvttshaflv mtgigldasm aadtnawvkk rlgwvaysdp
      181 iarsvignrq ipvhygidda plrsmsahti ivgncgtlta gilllpaarp ddgvldavaf
      241 rpagwfgwtk vgyaltlnrf fsrtrfgrll arvlptsral rytrartlrl tvdtpervql
      301 dgdafgevva vtlttdhhgl vlrtepdgpr trra
//
LOCUS       WP_284761126             387 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Curtobacterium sp. MEB011].
ACCESSION   WP_284761126
VERSION     WP_284761126.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. MEB011
  ORGANISM  Curtobacterium sp. MEB011
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 387)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 387)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Curtobacterium sp. MEB011"
                     /db_xref="taxon:3040285"
     Protein         1..387
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41292
     Region          56..362
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mriaalrrls irarltltyt alilltgavm lavvfavlai vpgyaftagp fpygsthdvy
       61 eitgrddvlr lfvivsvpal lvvggtggvv swlvagrllr plrdiittad rlgagtldar
      121 vdvsgppdei rdvgatlnrm ldrletafvs rsrfaanash elrtplatmk tmlqvalrap
      181 dgpdrtqtle rllvttdqmi rmttalldla rgdepidarp vslrdevaaa llavdaerla
      241 rrivvsvqld dvvvlgnrpl lgqlvgnlir navvhnvsgg slrvvldaga selrvendge
      301 viptdeahel tepfrrrhrt rtdgsghglg lplvamiaav hgaeltltar avggltastr
      361 fpdrqppdpa gpsrsaprvl gdhpgvr
//
LOCUS       WP_284761164             479 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Curtobacterium sp. MEB011].
ACCESSION   WP_284761164
VERSION     WP_284761164.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. MEB011
  ORGANISM  Curtobacterium sp. MEB011
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Curtobacterium sp. MEB011"
                     /db_xref="taxon:3040285"
     Protein         1..479
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51228
     Region          25..454
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 msrivvvggg iggltaaall araghrvtll essaelggks rrihlgadri dtgpslmtfp
       61 avwdellrrl gdgadagape rtrdaghldl vrmpevgryy hdgeetslpv apdhpwypaw
      121 rrfsdlhapl addvtellla dpldraalpa lrrllavygs rlttrayldg lpwlpdglre
      181 iiaihtlnag vspartpaly asmpaimaet gawvprggiy eivlalgrla eaagaevrtg
      241 eavtriergw vttevgrypa dlvvsavdad rlttltgpsr ipplprlrpr tlscsavavy
      301 gvlrqelpad laahsvvlpt kpaalhrsle agdepadtmv fvnqyragev ypngrstagi
      361 lltapadggh ytaehpfvrr evdrvsramg ldgpltdlld eqvvldpqyy geggephgal
      421 ygaarppwls gpfhrpsynd pwrpwlwrvg asvhpgggvp avvggamiav nrllkstpa
//
LOCUS       WP_284761254             442 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Curtobacterium sp. MEB011].
ACCESSION   WP_284761254
VERSION     WP_284761254.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. MEB011
  ORGANISM  Curtobacterium sp. MEB011
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Curtobacterium sp. MEB011"
                     /db_xref="taxon:3040285"
     Protein         1..442
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46468
     Region          17..436
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 mtvesvllfv lgvvvfiigl lvsiglhelg hlsfaklfnv kvtqyslgfg kamwsfkrge
       61 teygirpill ggyismvgml kprasgreit ntgmysafvq darqasaeqi adsggddsra
      121 fyrltpwkri ivmvagpamn lvigivlfgv llcgfgaptt tftssvgcvl pnsrttecsp
      181 gdavspakqa giesgdvvls vngeqdptit rvsqvfqesa geqvtvvvdr dgarktleit
      241 pttatrdvyd aegkvvkndd gttktqrvgv vgvsigqslv rqspaavlpa tgaqiaasah
      301 liidlpqrlv avwnaafgaq ersqdspvsv vgvgraigev ssmsgvpvvd kaytilglla
      361 slniglfvln mvpllpldgg hiagalweai krrsfklvgk tdpgpidlak tmpltmvvvv
      421 llagmsalli yadivrpvnl fg
//
LOCUS       WP_284761344             457 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Curtobacterium sp.
            MEB011].
ACCESSION   WP_284761344
VERSION     WP_284761344.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. MEB011
  ORGANISM  Curtobacterium sp. MEB011
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Curtobacterium sp. MEB011"
                     /db_xref="taxon:3040285"
     Protein         1..457
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49440
     Region          1..314
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mttfprttps aldvdargvl afvdalestp gvephsfmll rhgqvaaegw wqpysadrvh
       61 llyslsksft aaavgiavrq glvdldatvl syfpeldadv tdersrrmrv rhllamasgh
      121 reetleraea ldptntvrgf lllppdeepg svfaynqpct ytlasivrrv tggslvawlr
      181 phlldplgid dlawrrddtg aefgfsgcya ttdavaklgq lylqdgvwng erildadwve
      241 qatstqvanp deanpdwskg ygfqfwmarh gfrgdgaygq fcvvlpeqdv vlaitgqtvd
      301 mqavldaawq hllpavdgtt dtdadtalea rlaslglppv qggrlpehla dvelrsrpgg
      361 ildaatftrg adgirltitd dgrsesvplg eglwavegal aasaatepeg tvlvavrfle
      421 tphllhlrid ldagtvgakw kteplhdgpm tlrrpad
//
LOCUS       WP_284761377             613 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Alloscardovia omnicolens].
ACCESSION   WP_284761377
VERSION     WP_284761377.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 613)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 613)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..613
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=69354
     Region          26..516
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(39,41,43,47)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(78,81,118,121,168,187,191,223,292,455)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(223,292,366)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          524..>562
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; pfam16657"
                     /db_xref="CDD:435493"
ORIGIN      
        1 mvtadrmhls dtirtngatp npwwsnavvy qiyprsfqdt ngdgmgdlkg itsrldylad
       61 lgvdvlwlsp vfkspqddng ydisdyqdid plfgtlddmd ellaqaherg lkvvmdlvvn
      121 htsdehswfq asrdkndeha dwyiwraard gytpgepgae pnkwgsyfgg sawqfdekrg
      181 eyflhqyskk qpdlnwenpa vrqavyammn wwmdrgidgf rmdvitqisk pydtqgrlpg
      241 edgseledfp agsdgysspf pfcsdgprvd eflaemrrev fahregfltv geapgitpkr
      301 nehitnpdng eldmlflfnh vdvdcengtk wnptplrlte lkrtlseqqq avknngwasl
      361 ffnnhdqpra vsrwgddste esrslsakal glllhmhrgt pyiyqgeelg mtnahftrle
      421 qyrdlesinm yhqrvdeagi qssesmmdal arrgrdnart pmqwdasrya gftaedapte
      481 pwisvnpnhe hinaveevcd snsvysfykq lialrhtnpv isagdwqild asneqiyaym
      541 rslgdervlv lvnvsgsavd vpaesaavla asgldehsin qrlllstyes nhavssvlnq
      601 rleawegivl rid
//
LOCUS       WP_284761444             218 aa            linear   BCT 25-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Alloscardovia omnicolens].
ACCESSION   WP_284761444
VERSION     WP_284761444.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..218
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23564
     Region          23..150
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 makhrtasra rkprvnrtpl tdiwmylvvf vggalgtaar ygisssmntl phplsirwgt
       61 ftanviaafa laaitaalsh tllsehapas qkragelisk glgmgvcggl stmstlalei
      121 aasdygwsya ivslaagivs ailgalfgmw asgakraqrr aqqhqqqqtl rrsrvsarrr
      181 ahiqnksqnk svtrrvsrat qkasensqrv rarkhrkh
//
LOCUS       WP_284761516             677 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Alloscardovia omnicolens].
ACCESSION   WP_284761516
VERSION     WP_284761516.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 677)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..677
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73422
     Region          1..455
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          555..621
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(578,587..589,596)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            588
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mkkllianrg eialrvirta remgiatvai ysdqdrnapy vdradeafhl pgdtynetyl
       61 nmdrivdice rsgadaihpg ygflsenstf aqkvldadiv wvgprpevld dlgdkiiarr
      121 faeraqvtpv pgisdpvsdv htlisfcdeh gypammkrad ggggrgitvv rteddlrtff
      181 mshdslqggd ldkyfiekfv searhvetqc grdsfgtftv ystrdcsvqr rnqklieeap
      241 apflsdvvee klrvfsqrlf dtagyeglgt cefmvtphdd vyflevnprl qvehtvseev
      301 cgidlvreql tiasggsltv pdkmrghsfe lritsedpek nltpgsgvie kialplgpgi
      361 rvdfgvaqgd tispkydsmm gkiivtaatr dmaiarvhra isefelegvp tpialydeif
      421 ahddftakgr saqfnvttkw lentfmneha katragqphs vfdrsvnsve pselgsmran
      481 sqigssrdvh nttfvvevdd rrmkisvpdy viaavstshr pianrktqpl rgaglnitas
      541 ssenthgslv gsngeikapm qavvtrvnva vsqqvakgdl lvvlesmkme nyvyspiagt
      601 iseiyvgpad gvdagesllk vdmnaanksa esgdnekskd gavgeganlg assvavsgas
      661 svaisgasnk sankeek
//
LOCUS       WP_284761657             475 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Curtobacterium sp.
            MEB011].
ACCESSION   WP_284761657
VERSION     WP_284761657.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. MEB011
  ORGANISM  Curtobacterium sp. MEB011
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Curtobacterium sp. MEB011"
                     /db_xref="taxon:3040285"
     Protein         1..475
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=49343
     Region          19..453
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mseskkstas adtrpapvis vigtgylgat haaamaemgf etigvdidps klaalsagev
       61 pffepglpel itkhvasgkl rftadtasav aaadvhfvcv gtpqkagsha anlayvesat
      121 rgvaenlthp glivgkstvp vgtasrlrgi vreftpagid aeliwnpefl regkavedtl
      181 hpdrlvwgga seaadavire vyaapinegt pvittdlata elvkvsanaf latkisfina
      241 isemcaitga dvstladalg hdarigrkfl naglgfgggc lpkdiralmy raneigagqv
      301 vglmqqvdei nmgqrqrvid maidsaggsv lnrrvaviga afkpltddvr dspalnvaaa
      361 lhlrgaqvtl wdpeamepak rsfptlsyae smtdaiegad vvlvltewdd iitadpvalg
      421 dlvgrrvvid arnclpvadw vkagwtvrsl grptpvtgap vsvaagtnda latsr
//
LOCUS       WP_284761768             230 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Alloscardovia omnicolens].
ACCESSION   WP_284761768
VERSION     WP_284761768.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..230
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24809
     Region          12..217
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mnnatskstt lpaavmwdld gtlvnsepyw geseralldr aggtwtpdia aqlqgsslaf
       61 vanfmiqagv kdmgaediah fmvefvykke verlpwlpgv ydlitavrda gipqiivtss
      121 pekmarnvke qapegafmay vcdnddvphk pspepyllaa rtmgvdikdc lifedsvpgl
      181 taaaasgasw vsvtgyssid arerglasqf vrdyeglgid diarffahkg
//
LOCUS       WP_284762104             128 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284762104
VERSION     WP_284762104.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..128
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14040
     Region          9..108
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mtycadhwpd cgvarfltll dgpwatlivr qllmgparft elrndlpgis ahtltnrlrq
       61 fqayglvtrt ayaeipprvv yeltelgagl rpvlasmndw aqhvpkkesg nepqersvah
      121 qaigtasg
//
LOCUS       WP_284762106              97 aa            linear   BCT 25-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284762106
VERSION     WP_284762106.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 97)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..97
                     /product="type II toxin-antitoxin system RelE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0017148 - negative regulation of
                     translation [Evidence IEA]"
                     /calculated_mol_wt=10843
     Region          11..95
                     /region_name="RelE"
                     /note="mRNA-degrading endonuclease RelE, toxin component
                     of the RelBE toxin-antitoxin system [Defense mechanisms];
                     COG2026"
                     /db_xref="CDD:441629"
ORIGIN      
        1 mtgaeatgpa pwnvevtspa lkrflrlpqk aataivefvt galadnphrl skpltnellg
       61 lrtarrgdyr vlftldieeh ilyvhriehr sdvykpr
//
LOCUS       WP_284762130             457 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Arthrobacter sp. efr-133-R2A-63].
ACCESSION   WP_284762130
VERSION     WP_284762130.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 457)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..457
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=49007
     Region          42..395
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mraqdvrldd tvieelrqra kdleaystlw aggpaidssg taalsslver lanmypygda
       61 kyigqllkpp hpvawvaqai talinpnnha mdggpatavl ekevvaklaa mfgyeehlgh
      121 ltssgtianl ealwvarelh pgkvilsgtn ahythermcr llgtphetip eddlgrlsma
      181 dlrirlargg vgtivvtlgt tglgaldqvh eaadlaaefg arlhidaayg gfhtllatgp
      241 eplvdpapfl airradsivv dphkhglqpy gcgsvlfadp svgrlyshns pytyftssdl
      301 hlgeislecs ragasaaafw atvealglsr egmgsiiadg rkaalqiagi iraadgaelv
      361 vepeldivca fprrpttgqi saatedafaa mardgwhlal yrvdskwlar khpwvvvdsd
      421 yttvlrscam kpehlqvaqe fshrliasve qqpsrts
//
LOCUS       WP_284762161             521 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Corynebacterium sp. UMB6689].
ACCESSION   WP_284762161
VERSION     WP_284762161.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB6689
  ORGANISM  Corynebacterium sp. UMB6689
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20358183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Corynebacterium sp. UMB6689"
                     /db_xref="taxon:3046341"
     Protein         1..521
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=56050
     Region          43..280
                     /region_name="SBP_bac_11"
                     /note="Bacterial extracellular solute-binding protein;
                     pfam13531"
                     /db_xref="CDD:463911"
     Region          <300..518
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mfrslrvlli lvgtmaltac smgdllddsq kpgagnsfsg glrivaatel eplepvlaea
       61 sqdlgfditm ttedgtlans rtlkqggfeg tydatwfatn ryariigadg qlgrehsvar
      121 spialgvqts vaqeqgwtgk qptwqeians gitfgmtdps tsnsgfsals aattafadtg
      181 raltekdirq stgkvqklfg nqtltsgssg wladrfrehp eqadaifnye svlyqlkdeg
      241 adievvipsd gvisadypls slgsssdkda eakvqalaew faehpdklts fhlrvdnsdl
      301 pgtifelpyp aneqtvdale aafahelrnp gntalvldts gsmegermdl lkssllplid
      361 gsadgtpdge gqvafrnreq iklipyssep qqptrarvdk dkpattkela drverlvadg
      421 dtatfeavln afdevdtsgg digtvvlmtd gevtrgrtfa qfkeayeqlp edkkeipvfv
      481 ilygeaniqe meelaqltgg ktfdalngdl aaafeeiray q
//
LOCUS       WP_284762209             262 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284762209
VERSION     WP_284762209.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..262
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=28596
     Region          <63..216
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mpwsgfdlin afnawkrsda agrvfavdga gavesvvtgl swrtrvcqqv feeaalpgig
       61 tlrvhddtrp lrrilaknrr lskavsrkkk gsknrakavt rlarhhehir nrrqhfrhqa
      121 snelakthar laiedldvtg mlanhhlaaa iadatwaela rqlaykqswr ngelalvdrw
      181 fpssktcsqc gharpglglg erayecgncg laidrdlnaa anlaawaqkh haqapdpear
      241 agtptpadtk alapapartk ps
//
LOCUS       WP_284762246             765 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Corynebacterium sp. UMB6689].
ACCESSION   WP_284762246
VERSION     WP_284762246.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB6689
  ORGANISM  Corynebacterium sp. UMB6689
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 765)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 765)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 765)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 765)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 765)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Corynebacterium sp. UMB6689"
                     /db_xref="taxon:3046341"
     Protein         1..765
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=84439
     Region          34..765
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mttekqdkta wrpgsvrgms arlarsltgg rvkinpaldp lmsihrefhp kadaellnna
       61 yttaqrlheg vfrksgepyi thplavatia aeigmdtttv aaallhdtve dtdysledlt
      121 rdfgpevarl vdgvtkldkv algaaaeaet irkmivamat dprvlvikvc drlhnmrtmr
      181 flppekqakk arqtldviap lahrlgmasv kweledlafa ilypkkydei vrmvadraps
      241 rdralkeika qvgqalkang ieaevmgrpk hywsiyqkmi vrgrdfaeif dlvgirilvd
      301 dinscyaaig vvhslyqalp grfkdyissp rfgvyqslht tvigaggstl evqvrthemh
      361 ynaefgvaah wryketkgkn sghqeevdqm awmrqlldwq keaadpnefl dslrydltak
      421 qifsftpkgd vvnlpagstp vdfayavhte vghrcigakv ngklvalese lksgdkveif
      481 tskdpnagps rdwqeflvsp raktkvrqwf akerreehle agrdalaaev qrgglpmhrl
      541 ftassmkqva eqlhypdvda lytaigaghv saqhvanqlm alfgdqddav dalasrtpls
      601 elensraqht kdsatgtgil vegspdvmak lakccqpvpg daifgfvtrg ggvsvhradc
      661 tnaeklksep ermmqvewag gpkssgafaa tlqleaidrq gllfeltrif seqslnvlsm
      721 tsnrgddhia tvrfsfsvsd tkqlgqlmtt lrntegvfdv yrvta
//
LOCUS       WP_284762386             575 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284762386
VERSION     WP_284762386.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 575)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 575)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..575
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=60420
     Region          20..258
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 maspqasegk slppelplim ryaarsdvgr vrsknddsay agrhlavvad gmgghaggdv
       61 asastvldmi hldhdsypdg aetvladeiq tansllselv hvdpklagmg ttvtallleg
      121 rrlhfahigd srayrlrngk feqvsvdhtf vqrlidegrl rpeeaethph knvlmrvlgd
      181 vdaspeldld eldvepgerw llcsdglnyv qgavveqvvr etkdlaecae llieltlang
      241 apdnvtvvll eiveetgdnl staavdvvpe apapanaaea akaaprkdgh gsdasapake
      301 sganapatgr vpprettsda gpsaaaakpt apaepeagap anpagttepp tatdphlgeh
      361 lsaeilreel ssrphelvga aataadtgsi ptiagrsvar raatvlthka eqdrqdpqpi
      421 varkrrwltp aiaavlaifv iaglwlgyaw tqtryyvgef nqhvaifngi sqslgpfqls
      481 kveattnirm dslpeytqqt lrqtvpardl sdaqqivksl qengttglpa ncptatatpt
      541 asltptaspt pspspsnrpt ssptstpvps cavsr
//
LOCUS       WP_284762387             463 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284762387
VERSION     WP_284762387.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..463
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50043
     Region          5..453
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mlnldrdvvi vgagpsglta arelkkagls vavleardrv ggrtwtdtid gamleiggqw
       61 vspdqtalmg lldelglkmy sryrdgesvy lspdgtrtry tgtsfpvset taaemeklta
      121 ildglaaeig peepwahpka reldtisfhh wlrqnstdee acnniglfia ggmltkpaha
      181 fsalqavlma asagsfsnlt dedfildkrv iggmqqvsll iaaelgddvv lsspvrtinw
      241 eaageghrvt veseratvna rfvimavppn lysrvsfnpp lprrqhqmhq hqslglvikv
      301 havyrtpfwr edglsgtgfg adalvqevyd ntnhgdargt lvgfisdeka davfelsagd
      361 rkkkvlesia gflgdkalda evyyesdwgs eewtrgayas sydlgglhry gkdqhahvgp
      421 iywsssdlaa egyqhvdgav rmgqataari vtansrvvav pva
//
LOCUS       WP_284762431             213 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284762431
VERSION     WP_284762431.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 213)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 213)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..213
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23313
     Region          30..100
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mnedngvstg lasakrrkrp gktveitdpk airalahaar leviselyst qlsrtatela
       61 aqtgltpsam syhlralqkw givtaadneg darerrwkaa gsdftiksgg napspeiavv
      121 eleldafrrr ataftrarge rrlrgetane aaamvlssdl lyltpdqrtd lkakfqdlir
      181 sydledptri pegavriatm wsmipddrtp tst
//
LOCUS       WP_284762468             247 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Arthrobacter sp. efr-133-R2A-63].
ACCESSION   WP_284762468
VERSION     WP_284762468.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..247
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26293
     Region          14..228
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mlasatqpfv kaelkaalwd mdgtlvdtep ywiaaeralv eshggawshe qamqlvgqsl
       61 mhsagilqta gvnlekreiv dslsarvidr lrvevpwrpg akelldelfq sgvrcalvtm
      121 segpmarevv anlskpyfef litgdtvsqg kphpeaylaa verlqdtdpg ltadhcvale
      181 dsvpgvasai asgvvtvgip hqmplpedpr ratwdtlqgr tvadlealva arasanapag
      241 tllgran
//
LOCUS       WP_284762488             314 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Arthrobacter sp. efr-133-R2A-63].
ACCESSION   WP_284762488
VERSION     WP_284762488.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..314
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=33062
     Region          20..309
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mstasrlpks iqqladklpt evnstirrla mlsligqvvl vvtggavrlt ssglgcptwp
       61 rctsgslvnt pemgihgfie fgnrmltfal aavavlmlvy lwnlrkerrd lfllavglla
      121 sipaqaiigg itvlsnlnpw vvglhflvsm alvvfstllv nraygrtgrf mkrpleaipg
      181 amspvmtava ffsavavclg vivtgagpha gdanaprndl dwdlvshtha vpaylitaga
      241 vfavyfvlrk gitglfrtaa llllavtvlq avigftqyyn gipallvgah mlgaallmga
      301 atnaadvarf spkl
//
LOCUS       WP_284762534             343 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Arthrobacter sp. efr-133-R2A-63].
ACCESSION   WP_284762534
VERSION     WP_284762534.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 343)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..343
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=35553
     Region          7..324
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 msenpdqatl rkaslkiavr isaacavlvl cllaaaaiyl fnqaqhpslp gpgesnsvya
       61 yldtkdllka mivagiagil lagaigwlsa rsairplgea lalqrrfvqd ashelrtpla
      121 ildarvqlaq rdapadsktg ealarirndt atltgivnel lvaatgspad apaepsdlak
      181 varavveslq qlageknvrv iltekdrpfa lidgngfrra llaladnala htpaggevri
      241 ttavlgnrav vtvadsgagi kgvdqtrifd rfvrthspeg apgqrsfgig lalvreiita
      301 argavevers gpqgtvmkit lplagkdtta kdaspkdtap gpa
//
LOCUS       WP_284762556             423 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Arthrobacter sp. efr-133-R2A-63].
ACCESSION   WP_284762556
VERSION     WP_284762556.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..423
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=46345
     Region          42..422
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mfsvispphr aptanptagn pdtdsapplg sgpenrlpts apkqsrpdla tltalrfvaa
       61 lwvvffhlqa mqqtflapvy elfrpiiang dlgvdvffvl sgfiitytyl drlgprfrwr
      121 aaadfvwarf armwpafalv vgvlglwfvy gtaqesvrew slqtqapdls pwglakqllm
      181 mhlwfqpgtd gaswfgpgwt vsaewlayla fpllalvlfr lrrlhplaal aasvlvllpt
      241 avwgpdlpia ttehqpyewl lriaccfvag alaciaarna drmkfnpala gpgalltgta
      301 vvvflatagk pgpgrlavla fplliallsl trgwlrsals arwlqygghs syslylvhmf
      361 fiylfywlir dwpqgaspla enllaaacll gialathllf kyveeparlr lralvpraap
      421 asg
//
LOCUS       WP_284762592             453 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Arthrobacter sp. efr-133-R2A-63].
ACCESSION   WP_284762592
VERSION     WP_284762592.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..453
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48041
     Region          6..450
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 msdefsvesv yaellgrape nkmeprlapl yramdvlgep nkafpiihit gtngktstar
       61 mieaglrahg lstgrytsph lskvterisi dgepvsdetf vriwdeirpy leivdkelea
      121 dgqprltyfe cltilgfavf adqpvnvavi evglggitda tnvgdgqvsv vtpisldhtd
      181 llgdttedia hekagiikpg gflisaaqpv daaqvlleka revgvpfrfe gvefgvesrs
      241 vavggqvlti qglagryedl llplhgahqa enaavavaal eaffgggeke ldgdvlreaf
      301 gnvtspgrle vvrtaptiiv daahnpdgir vsaeaieeaf sfsklvvvlg vlkekdaeei
      361 lrqlkeslgg laeefcftqs sspraipaaq ladlavdlgf gadnvhiaek lddaiewave
      421 raeanddlag gvlvtgsitv vaearmllgk vgs
//
LOCUS       WP_284762760             373 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Corynebacterium sp. UMB6689].
ACCESSION   WP_284762760
VERSION     WP_284762760.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB6689
  ORGANISM  Corynebacterium sp. UMB6689
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Corynebacterium sp. UMB6689"
                     /db_xref="taxon:3046341"
     Protein         1..373
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39446
     Region          1..372
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mihfgndyhr sahphvldai agaggayagy gtdelcntaa ariraacqap naevhfmvgg
       61 tqanatiiah rlrpwegvia adsghiathe tgaiehtghk vitlpnqlgk itaaqvracm
      121 deyrasgvee hmpepalvyi tqptefgtty sraelvalra vcdeyglglf vdgarlgygl
      181 sasditlpdl aalvdvftig gtkcgalfge aivfpagapr frnamkqsgg llakgwllga
      241 qfaalfsapp tvsadalaes natctraqaa tpgnevnsaa attlyeqica ranaqaqria
      301 eafraagidm lfdsptnqqf alltreqedk lsqdfvcqff eeheglrvvr fctawsteeg
      361 dvdklcaais alk
//
LOCUS       WP_284762842             527 aa            linear   BCT 25-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284762842
VERSION     WP_284762842.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10594375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..527
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=57253
     Region          296..404
                     /region_name="SIR2_2"
                     /note="SIR2-like domain; pfam13289"
                     /db_xref="CDD:433090"
ORIGIN      
        1 mtqphvfvam adilnlrcda wllptdstvn ierpwlaayp dlrtraatsa seyfrsgsal
       61 aeavhpwerg fprpimtavp ddghwgssvv aerleefvrc avkntpapdd rpyrllalpf
      121 fgtaaggagn hlgaalrdil daaielssry gvdivlvlrd raafslaqkl rrevrddssw
      181 ptlgaqrhee akslgkkars ghlvpflgag vsvsagapsw gqlldklrtg iqlkeseana
      241 feglsmldra gvleqlyalq hgskqafgea vaaavdlpry glapalltal psagaitlny
      301 drlfemackd aqrprtvmpe nipaegsswl lklhgsvsqp esivltrddy lgynsnrdal
      361 salvkahllt hhllfvgfgl addhfheivh dvrralpvda skqhrmgtvl slfqeplqkl
      421 vwegklgilh madapapdat aaelrasiar agreleifld mlaayatdnh syllapayng
      481 gladdelilr rqlldmaywp rsagtaevwg vldnalkelg fagmsea
//
LOCUS       WP_284762857             328 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Arthrobacter
            sp. efr-133-R2A-63].
ACCESSION   WP_284762857
VERSION     WP_284762857.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..328
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=35569
     Region          2..313
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkviviggsg higsflvprl vrdghevini srgthksygd apeweqvrqv vadrqqedrd
       61 gtfgdrvaal qadvvvdlvc ftfesasllv nrlrgeaghl lhcgsvwryg qslklpiaeg
      121 sgsaaapfge ygiqkdriar mlkeetddgg lvttsvhpgh ivgpgwhpig plgnldpavw
      181 ytlsagrplq vpgsgaelmh hvhaddvaqa fekaiqnrda aagedfniva ptaltvrgya
      241 diaaawfgqs atletvtweh fresttpeya esswghlyrs hcftiekats llgyapryep
      301 eqavlesitw liergqfrva nplsvpas
//
LOCUS       WP_284762920             489 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284762920
VERSION     WP_284762920.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..489
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=54628
     Region          48..461
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 milsffssqg weswevdcrp lipermpvlv dedlrfegsp gtprptvavn rwlrelpasg
       61 apspntwaay araikewmef laehgvglfd srdrlklgls ryaehraagp lkhrfaattw
      121 gqhmsilslf yrwameegha eaepftyrta ralfrgtgrd vrvnlavrrt pkphvtikyl
      181 epdftglfln glrglapdga ldagyrgrel arnaavggla latglraqef tylltyeipa
      241 lpprpvaipi pfpvpagitk grkfrttwis yealaavhhy leldrvvtvd gsawrpprrw
      301 gepllvtnpd arggqingir rrwdtltpde rrrlvapggg scllalrngg gpftawatvf
      361 ertadrirar feprfphihp hrlrhsfsmr tleylvtghy rqaaklvkdt dadaalvfyl
      421 skadpllvlr dllghssvlt tekylkrldt triyrdayds agiadgllae aaaeqeaaae
      481 fddgesglc
//
LOCUS       WP_284762929             110 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Arthrobacter].
ACCESSION   WP_284762929
VERSION     WP_284762929.1
KEYWORDS    RefSeq.
SOURCE      unclassified Arthrobacter
  ORGANISM  unclassified Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10601889
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="unclassified Arthrobacter"
                     /db_xref="taxon:235627"
     Protein         1..110
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12267
     Region          10..74
                     /region_name="HTH_26"
                     /note="Cro/C1-type HTH DNA-binding domain; pfam13443"
                     /db_xref="CDD:433211"
ORIGIN      
        1 mkreidyrwr laelmaargm hnstdlspll kergielsas qvyrlvtqrp ervslmmvsa
       61 lcdifacgpe dlitvtaada kvrkiasnan vvdlnktirp krarvirddg
//
LOCUS       WP_284762953             597 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Corynebacterium sp. UMB6689].
ACCESSION   WP_284762953
VERSION     WP_284762953.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB6689
  ORGANISM  Corynebacterium sp. UMB6689
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Corynebacterium sp. UMB6689"
                     /db_xref="taxon:3046341"
     Protein         1..597
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=63076
     Region          1..483
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          531..596
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(554,563..565,572)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            564
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 misavlianr geiavriart ardlgirsia iyseadagal htqvadeaya lpgnsaadty
       61 mnipalldia vragadaihp gygflsenad fartvaeagl twigpspesi ellgdkiaar
      121 rvaeevgapl apgtsdpidd wqearafaee hglpiaikaa yggggrglkv venledieaa
      181 fnsagreake afgraecyve kflthprhve aqiladthgn vavlgtrdcs tqrrfqklie
      241 eapapalsde qrtgihegar aicakvgytg agtveyivse dgtisflevn trvqvehpvt
      301 emvtgvdiia eqfriasgep lsfvsssssd aseahaseah asdpemdgha fefrinaedi
      361 lngfapcpgt ivrfepptgp girvdsgvrs gsivppyyds lvakllvwgp treialkraq
      421 qalqefdieg vrtvlpfhrd mvssqvlvdh gdadaaagiy tdwldhnyrp saeatsttvp
      481 veaiyaqrtr valeidgklv svgfptdmls qgpvkgasas aasgasdsgn evtcpyeanl
      541 vawnvedgem veegqaiati eamkmesavk asssgklsrv akegsrlepg aviatis
//
LOCUS       WP_284762996             373 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284762996
VERSION     WP_284762996.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..373
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39248
     Region          7..371
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 msstpptkhv vvigggilgv stavhllreg asvvlltekg laseasgrsl swlnsagers
       61 tpyhqlrlag vdryrtlfaa dphrewlqfg gglmwnaagq qaatesrhay eksvgydskl
      121 ltpeeidfat pginagavpe faifnpgegw vslpeliefl leefharggq lvlnagkasv
      181 tvdggratgv etaaggtyra davlvacgaa tpavvaplgv dipnaspvsm lvltkavdhe
      241 vravmntpra airpnpentf aldhdwyeeh itehedgsfs ipdgivqela deaskliagr
      301 pelkpaswki gykpipgdge pvlgelghvp gcyvafthsg atlglivgel lageiltgsk
      361 hpmlstfrpg rfs
//
LOCUS       WP_284763004             113 aa            linear   BCT 25-DEC-2024
DEFINITION  YegP family protein [Arthrobacter sp. efr-133-R2A-63].
ACCESSION   WP_284763004
VERSION     WP_284763004.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..113
                     /product="YegP family protein"
                     /calculated_mol_wt=12219
     Region          2..58
                     /region_name="YegP"
                     /note="Uncharacterized conserved protein YegP, UPF0339
                     family [Function unknown]; COG3422"
                     /db_xref="CDD:442648"
ORIGIN      
        1 magkfelfvd areryrfrlk aadgtvmavs kdfetkraav agirevraca gmglitdlcp
       61 aqpatsvaap etsppalsea vpprgrhwlg rtfivrrrgh kalasarwln sve
//
LOCUS       WP_284763194             548 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284763194
VERSION     WP_284763194.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..548
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60263
     Region          27..526
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mlnpdfpfpy ddylthpagl gavpehmhgt eiavigagls glvaayelmk mglkpviyes
       61 sriggrlrag rpegqagpva dlggmrfprs grsffhyadk vgietqpfpn pltpaagstv
      121 ielggrahya etaadlpqff gdvaaawddc leerahftam qdairnrdla tikrlwnelv
      181 pkfddvsfsg ylatskafsa lpfeyreafg qvgfgtggwd tnfpdsflei lrvvyvdada
      241 dqhriiggaq lvpeclwqha penlthwptg tslaslhggh prgavaavar vkndggapsd
      301 iavtdrwgrt aeypaviatc qswllsarid vdeslfshkl wtaiershym qssktfvvvd
      361 rpfwkdidpe tgrqvmsttl tdrltrgtyl ldngpeqpsl iclsytwndd alkwlpldad
      421 ervrlmlhsl kqiyptvdia shiigdpitv sweddpnfmg afsdnlpghy ryqerlythf
      481 mqeghppehr giflagddvs wtggwadgav ttglnavwgv mnqlggsspa enpgpgdrfe
      541 elkpirlp
//
LOCUS       WP_284763132             256 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Arthrobacter sp. efr-133-R2A-63].
ACCESSION   WP_284763132
VERSION     WP_284763132.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..256
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27853
     Region          169..241
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mslvlvealm dqawpaldre dtggwvmraa ggvtqransv wpreeaddhe savraasqwy
       61 rsrrlplifq vfddersagl navldaqrft rqsetlilvr aadtppgapr gdlpndveis
      121 eepseewlrl wwsvdgrggd aeleiarkil vscpsvyalv tdddgvpaav grlalvdgrg
      181 giycmataag hrrrgfgrqv ldalltaggh rgvsgfwlla masntaaqal yegagfterg
      241 rylyrqarpq ralsgc
//
LOCUS       WP_284763196             258 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284763196
VERSION     WP_284763196.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..258
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27920
     Region          9..245
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mttranelta lvtgataglg aqfarqlaes ghhlvlvard egrlrasaev lerdfsisve
       61 vlpadltsdv gvaavaarlr dasrpvdvlv nnagigllns fekndvedek rhlrvhvqtp
      121 lelchaalev mlarksgrii nvasvaafan rgsysaakaw qvsfsrwant ayarsgvkvt
      181 avcpgfthte fhdrmgmdks vaprflwlka ervvregled nakgkgvsip tkrykaitav
      241 mrflptklts gpprrplk
//
LOCUS       WP_284763201             448 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Arthrobacter sp. efr-133-R2A-63].
ACCESSION   WP_284763201
VERSION     WP_284763201.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..448
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=47907
     Region          24..329
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mgfsgqqkts agmaafgrpr dpvidlarff clilvvlshc mmvspvlhpd gtvttentlm
       61 eqhwfepvlw vfqvmplffv lggitglesw rrlrsrggsg idyaqlrllr lirpatalla
      121 smfvglwaar llgvdpevvq liatgagmpl wflaaylatq lsvpvlarlh ghspwltlgg
      181 lvaavitlds lrgafpmlaf vnmlfvwcav qqfgffiadg ifagrsrgwf vglivgsnll
      241 lglvtgigvy sgnmivdlnp pnfcmlllgl sqaatlqllr pgldwaagvr wirwvvavag
      301 rrsmtvylwh lpllagmsgl llltdfpkpa agtaewwwar plvllgvlll llpvlllcgr
      361 leerptaaih argrthvavv taavvvfipv vdaafngltl tllgggaacf algvlllgrv
      421 pagvlaaavp dgpavplpep glranlds
//
LOCUS       WP_284763357             353 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Arthrobacter sp. efr-133-R2A-63].
ACCESSION   WP_284763357
VERSION     WP_284763357.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..353
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=37602
     Region          8..343
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mdqqrkessl gyvpaldglr giaillvlah haygawdags vgvdvffvls gylittillk
       61 eldrsgrisl whfylrrlfr lypallvvil avaaltpivg snwialfaag tyttnigtvf
      121 lhldlgplkh twslaqeeqf yliwplflii asrfqmprka qflvtvlass gcialfvvat
      181 gsgtatlnpi armggiaagc vvalalntgi irtvrawlmw agagvgicai imnstglvda
      241 ailapvvilg clpllaglma gpggaiasil scpplvyigv isyslylwhy plfyfaqslh
      301 lgtwltaaia lpvsfglaal srrfievpgm algvsrvklr tsprntekag apv
//
LOCUS       WP_284763292             448 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium sp.
            UMB6689].
ACCESSION   WP_284763292
VERSION     WP_284763292.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB6689
  ORGANISM  Corynebacterium sp. UMB6689
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Corynebacterium sp. UMB6689"
                     /db_xref="taxon:3046341"
     Protein         1..448
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=47944
     Region          1..443
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrmtvigtgy lgathaacma eldhevlgvd vdehkiealk ngrvpfyepg lpevlernie
       61 agrldfstsy ddaaefanvh flgvgtpqth gsyaadltyv ksvitelvpr lkgehiifgk
      121 stvpvgtaae lqqmadelas ggtsveiawn peflregyav kdtitpdriv lgvgeagrad
      181 gessaeevar evyaqplaqn tpfivtdlqt aelvkvsana flatkisfin avseiceiag
      241 advvkladai gyderigrkf lgaglgfggg clpkdirafm aragelgadq altflrevda
      301 inmrrrdrvv dlakqafdgs llghrvtvlg cafkpnsddv rdspalsvag slslagaavt
      361 vydpqgmena kkvfptlnyv asasealkdt elvilatewq efrdldpaea gelvarrhii
      421 dgrnvlsvda wrevgwtvea lgrvlpaq
//
LOCUS       WP_284763359             448 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Arthrobacter sp. efr-133-R2A-63].
ACCESSION   WP_284763359
VERSION     WP_284763359.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..448
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=47118
     Region          181..416
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 matygmikgg skapyivfgg liaifaiaam mkrpylapfl vivaavydrh iyygldslel
       61 ttllivlalt apvfaaaair rgglsayvvv gslllaiglv aaalgaqdgt eatlgtvrwl
      121 lvlnmivgta amcgarpnlt rqltwwmvtg gavaaifgil qrsgkyflvg ppyadgvyns
      181 tfgyytnfan fmalasvlgl glllelrrth rrggfwalam tvlcaisvvq slsrgalicm
      241 ligiavimfr qvtrpgrflg ilatlgglgg iiwlvipead qtalinrfiv qpggdvvreq
      301 mqaggmqlat ehplgigfnn fqayvstgiv daskalahsh ntflqmalda gwigfagfvi
      361 ltvgacfaai rakhnalrlg agaaligflg qvtqdffffe aasltlfglv lamsaakthv
      421 tvqapeeppa ptangangak lddralvq
//
LOCUS       WP_284763428              94 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284763428
VERSION     WP_284763428.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 94)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 94)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10601889
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..94
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9751
     Region          20..72
                     /region_name="HTH_26"
                     /note="Cro/C1-type HTH DNA-binding domain; pfam13443"
                     /db_xref="CDD:433211"
     Site            order(21,25,50)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(24,49)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(31..32,43,46,50..51)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mptgkqpeag pfaraisaei resmarqrvs gpmlagrtgi sqsylsrrll dkvaftandi
       61 eaickalged ilaliaaavd aaglstetpp erps
//
LOCUS       WP_284763459             131 aa            linear   BCT 25-DEC-2024
DEFINITION  6-pyruvoyl trahydropterin synthase family protein [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284763459
VERSION     WP_284763459.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Phillips,G., Grochowski,L.L., Bonnett,S., Xu,H., Bailly,M.,
            Blaby-Haas,C., El Yacoubi,B., Iwata-Reuyl,D., White,R.H. and de
            Crecy-Lagard,V.
  TITLE     Functional promiscuity of the COG0720 family
  JOURNAL   ACS Chem Biol 7 (1), 197-209 (2012)
   PUBMED   21999246
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Colloc'h,N., Poupon,A. and Mornon,J.P.
  TITLE     Sequence and structural features of the T-fold, an original
            tunnelling building unit
  JOURNAL   Proteins 39 (2), 142-154 (2000)
   PUBMED   10737935
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..131
                     /product="6-pyruvoyl trahydropterin synthase family
                     protein"
                     /EC_number="4.1.2.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14018
     Region          1..128
                     /region_name="QueD"
                     /note="6-pyruvoyl-tetrahydropterin synthase [Coenzyme
                     transport and metabolism]; COG0720"
                     /db_xref="CDD:440484"
ORIGIN      
        1 mfsltvrrhf miahslprks fgpaqglhga tfvaevtfrr aalnddaivl digaagtild
       61 evlaglnykn ldehpdfagq ltttevlarf iaeavaakvr esddggalag vdvvlrehpd
      121 awagfsldfe r
//
LOCUS       WP_284763567             494 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Arthrobacter sp. efr-133-R2A-63].
ACCESSION   WP_284763567
VERSION     WP_284763567.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 494)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 494)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 494)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..494
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52054
     Region          2..487
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          250..488
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 maaadvnaig lplravkgig rrrilaglal alllpvaiev lvsalqyrnf amimlfqlav
       61 saavaaiggl wpavvsavlg smllnyfsad pvgslsiadp atlltlvifl avacgvalav
      121 glatrraqea ahsgaearal selalrilss dgslesfldk irvnlgmeam tllatfdspd
      181 apgpnwqvla ssgiqppvth aaanhaavvd rnytlllrgg plseqhrrml aafgafvval
      241 rerqqlvksr qdnvrlaegn kmrtsilrav shdlrtplag iklavsslrq edvtfapede
      301 rellatiedy adrldhlvdn lldmsritad avnpllrglg whqimpealr gvpgerirne
      361 lpanlpqiea dagilervva nlvenavkya pdsdvvlvar tgagitvdgr paselrvmdh
      421 gsgiapaavl elfqpfqrld dspssrdgrs giglglavak gfteamggtl maeatpgggl
      481 tmvvtlplwt ggrp
//
LOCUS       WP_284763611             365 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284763611
VERSION     WP_284763611.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..365
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37874
     Region          3..327
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 maanydvviv gggiaglsla salagqcsva lveaeqtlay htssrsarql ipsygpavvq
       61 eltvrtlelm aardaalpvp vleprsfmlv gdeatvkaea sghmhpitha ealklcpaln
      121 pgaftaagld tesfacntpv lledhrqrae aggvdiitga kvhsaqrlgs gwqvgaglea
      181 fqsavvvnaa gawadelavl sgveklglqp frrtaaivdv ehplppgspm vcaaddtyyf
      241 rreggqvlis psetvpsgpe daqprpgdve elvtrlnsit slgiravaka wtglrteaad
      301 gvpvvgfdae apgffwlagq ggygfqtssa iaelaaaeil dytsgtspas rtprelaaar
      361 wsirr
//
LOCUS       WP_284763676             278 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284763676
VERSION     WP_284763676.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..278
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28850
     Region          1..276
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mtftmgpall fcpadrperf qkaaersdav ivdledavap adkkrargai laqlgsgget
       61 aeldpsrtiv rvnpvgtadf ekdlhclaht pyrtvmlaka etgeqlkale gyhvialcet
      121 aegivnaaei aqapnvvglm wgaedliasm ggtssrkddg gyravamhsr stvllaakaa
      181 gkeaidsvyv dipdlaglav esadavasgf gakacihpnq vavvreayap speavagard
      241 lldaaaaagt gvfqykgkmv dgpvlkhaes tlrrarls
//
LOCUS       WP_284763673             723 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Arthrobacter sp. efr-133-R2A-63].
ACCESSION   WP_284763673
VERSION     WP_284763673.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 723)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 723)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..723
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..723
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76945
     Region          6..475
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          630..695
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(653,662..664,671)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            663
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mtinsfdtvl vanrgeiacr virtlkamgi rsvavysdad agarhvread aavrigtaaa
       61 adsylridai ieaclqsgaq avhpgygfla envefakald aagiafigpg idaieimgdk
      121 irsknhvmsy gvpcvpgiae pglsdeelid aapgvgfpll ikpsaggggk gmhiverled
      181 maatlltarr vaasafgddt lflerliqtp rhievqvlad nhgnvihlge recslqrrhq
      241 kvieeapspl leslangaev rarigaaacq aarsvnysga gtveflvsde dpehfffmem
      301 ntrlqvehpv temvtgvdlv ewqvrvaage vltvaqsdvv ldghavearv yaevpergfl
      361 psigeivtlr erasndphvr vdsamlpglt vtgdydpmla kviawgpdrk aaldtldhal
      421 gdyallgvht nveylrllin dddvragrld tglierkldg lefrqasdve liaaallnrt
      481 ellnrtelln rtellgrpep apagtaapwn tadgwrvgap apwkatigrp dgglatvglt
      541 vkgqgftarv ddgvehsaal rpgsaghavl vldgaehpfa ygspspvagt relwlgsdgw
      601 scrleildre triqrilavi qreesaadpe vrspmpgtvv svsvndgdqv eagqvllsve
      661 amkmehqlva svsgtvhlss ktgdlvkadq vlatihvlae ptseaasepa peltaenqkd
      721 eev
//
LOCUS       WP_284763626             394 aa            linear   BCT 25-DEC-2024
DEFINITION  integrase catalytic domain-containing protein [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284763626
VERSION     WP_284763626.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Ballandras-Colas,A., Maskell,D.P., Serrao,E., Locke,J., Swuec,P.,
            Jonsson,S.R., Kotecha,A., Cook,N.J., Pye,V.E., Taylor,I.A.,
            Andresdottir,V., Engelman,A.N., Costa,A. and Cherepanov,P.
  TITLE     A supramolecular assembly mediates lentiviral DNA integration
  JOURNAL   Science 355 (6320), 93-95 (2017)
   PUBMED   28059770
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (5), 302-307 (2001)
   PUBMED   11774877
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Dyda,F., Hickman,A.B., Jenkins,T.M., Engelman,A., Craigie,R. and
            Davies,D.R.
  TITLE     Crystal structure of the catalytic domain of HIV-1 integrase:
            similarity to other polynucleotidyl transferases
  JOURNAL   Science 266 (5193), 1981-1986 (1994)
   PUBMED   7801124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10461024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..394
                     /product="integrase catalytic domain-containing protein"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016893 - endonuclease activity, active
                     with either ribo- or deoxyribonucleic acids and producing
                     5'-phosphomonoesters [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=44271
     Region          168..259
                     /region_name="rve"
                     /note="Integrase core domain; pfam00665"
                     /db_xref="CDD:459897"
ORIGIN      
        1 maqrqavtkk kalaykgadr agksrilnel veltgwhrdy araalrdalv lkivrprpgr
       61 tpvygpdllp alikcwavlr apagrllapm lpvlvpllrr dreleltdeq agllmrmsaa
      121 tidrklager aklfprgrsh tkpgtllksq ipvrtwaewd davpgfveid lvgheggnsf
      181 gefcctltvt diatgwtvnr svrnkaakwv fealehvtav fpfpiigids dngsefineh
      241 llaychahei tftrsrpgnk ndgahveqkn warvrelvgy lrydtpaela klneiweldr
      301 vltnyllpqq kllfkqrhga kvtkkhdapa tphqrairhe rmhkrpviqm naafkrikpg
      361 alsrqilalt gqletlalak kpaplkpvnr awnh
//
LOCUS       WP_284763581             602 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Arthrobacter sp. efr-133-R2A-63].
ACCESSION   WP_284763581
VERSION     WP_284763581.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 602)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..602
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=63228
     Region          12..475
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          535..600
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(557,566..568,575)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            567
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 msanpaqpis spltkvlian rgeiavriir aardegiasv avyadpdrda lhvrladeay
       61 alggntaaes ylvmdkliev akqsgadaih pgygflaena efaakvidag itwigpspda
      121 isalgdkvqa rhiaekvgap lvpgtadpve sadeilafaq efglpiaika ayggggrgik
      181 vartieeipe lfesavreai aafgrgecfi erfldsprhv etqcladayg nvvvvstrdc
      241 slqrrnqklv eeapapflsp eqnerlyess kailkeagyl gagtceflvg qdgiisflev
      301 ntrlqvehcv seevtgidlv reqfriarge klgygdpevr ghsfefritg edpgrnfmpa
      361 pgtistlknp tgpgvridsg veqgdvisgn fdsmlsklvv tgatreqalq rsrraleemv
      421 vegiptvipf dlavvtdpaf apaegpfkvh trwietefvn nvpawtptgt gteaadager
      481 qrvvvevggk rlevvlpatl gsvsaassag tkgakvkkrs rsagataava ggnaltspmq
      541 gtivkvavaa gdvvaegdli vvleamkmeq pltahkagti hglvakaget vsagaviati
      601 ed
//
LOCUS       WP_284763746             344 aa            linear   BCT 25-DEC-2024
DEFINITION  trypsin-like serine peptidase [Arthrobacter sp. efr-133-R2A-63].
ACCESSION   WP_284763746
VERSION     WP_284763746.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..344
                     /product="trypsin-like serine peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=34756
     Region          135..333
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mtrtktlats llsltaaall slgagsgasa apstshgada stvssnpasd gntadywtpe
       61 rmknavsgdv latkaltraq aalgladlpv spdqvfpglg salttiegqq aaspatqspa
      121 vdrkanggea pvphigkvff tlggvnyvcs gnsitsanrs tvstaghcln egpgafasnf
      181 tfvpayqngv apygkwtaka lyttsqwsss gamqydtgfa vmnplngqkl advvgasgvq
      241 fnaarglayk sfgypaaapf tgeslmscsg taandpynpq yntqgipcnm tggssggpwf
      301 tgtssagyqn svnsygygsn stnmygpywg sviqgtyqna stap
//
LOCUS       WP_284763861             148 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Arthrobacter sp. efr-133-R2A-63].
ACCESSION   WP_284763861
VERSION     WP_284763861.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..148
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15912
     Region          13..140
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 megteapset qasidrtvew vdtdasghqh nsaimrwvea aeadlfrnlv lpeyfpsapr
       61 vqqvvnytak lwfgqrvtat vriqklgrts mtlafevygh ahpnspggla ahgtlttahv
      121 pagsataqpw perirqaaga tvpkglnl
//
LOCUS       WP_284763998             311 aa            linear   BCT 25-DEC-2024
DEFINITION  lipid II:glycine glycyltransferase FemX [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284763998
VERSION     WP_284763998.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Rohrer,S. and Berger-Bachi,B.
  TITLE     FemABX peptidyl transferases: a link between branched-chain cell
            wall peptide formation and beta-lactam resistance in gram-positive
            cocci
  JOURNAL   Antimicrob Agents Chemother 47 (3), 837-846 (2003)
   PUBMED   12604510
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Hegde,S.S. and Shrader,T.E.
  TITLE     FemABX family members are novel nonribosomal peptidyltransferases
            and important pathogen-specific drug targets
  JOURNAL   J Biol Chem 276 (10), 6998-7003 (2001)
   PUBMED   11083873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006395
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..311
                     /product="lipid II:glycine glycyltransferase FemX"
                     /EC_number="2.3.2.-"
                     /calculated_mol_wt=34083
     Region          4..311
                     /region_name="FmhB"
                     /note="Lipid II:glycine glycyltransferase (Peptidoglycan
                     interpeptide bridge formation enzyme) [Cell
                     wall/membrane/envelope biogenesis]; COG2348"
                     /db_xref="CDD:441916"
ORIGIN      
        1 meyflqtpaw asfqrslgrt vheesgpgwr flaveetnpa gkviytpygp vadsleafde
       61 avaalvaiar rsravfvrme pvtagfeaad agavlrergl qpapsnqqpe lswivdlegd
      121 fkdvlagmkp tnrnlyrnih kkgvtfrssq dpeeisvlld flhmtaarng fkpqsddyls
      181 avaqslmpag agtlfiaeld gepiaaalay dsadtrtyah aalddthrkl sagipllvtl
      241 madakdkglk hvdlwgvape dhpdhkwagf tafkksfggr eiaypgtwdl pvnklrygay
      301 qvarklrdkl r
//
LOCUS       WP_284764011             265 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284764011
VERSION     WP_284764011.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..265
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27624
     Region          18..250
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 msasggsnyd ggpldggrlr rrlaagevtv gtfvgmasat avevcaaaga dwvlidlehg
       61 sggedavrdg vlaagsygvp tlvrvesger irigrvldqg aagimvprln tveeakqtvk
      121 hmlyppygdr gvatynrscr wgmdraplsa dqqstvgivq ietldalehv eeiaaqdgvd
      181 vlfvgpmdms falgvpmqld ssafqealqr vvaaaqlhnk aagilavdgv aaakyvrqgf
      241 rfvaigsdst imaaafrvaf dtarn
//
LOCUS       WP_284764030             455 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Arthrobacter sp. efr-133-R2A-63].
ACCESSION   WP_284764030
VERSION     WP_284764030.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..455
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=46869
     Region          220..446
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mrrwfgtlag rttaviaava tvavllagll aaqlvnatav deakkylave adslskqssl
       61 gslqdlradl lthgarlaqi stdgrvsggg arlvdaktva dvlagksvst svngpqntvv
      121 learplaagg gvvlaqpvse iraaaaplls rmlvalavcl vfaivaggll aqwlsrplvr
      181 tahsahrlaa gersvavapg gpaevvevsq alaaldaalr tsegrqrefl lsisheirtp
      241 ltalrgyaea ladgvvsgdd vsgvgqtlva etnrldrfvr dllelarles ddfrvelqlv
      301 daslilresw qawqavciqn giagrlelpl gplpvrsdgq rlrqvvdgll enalrvtpes
      361 apvvlaayat gsgltvevrd ggpglteada avafergalf arysgerpvg sglglsiaar
      421 ivqrvggris vrvapeggaa fvvelpgipa gapqt
//
LOCUS       WP_284764102             303 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. efr-133-R2A-63].
ACCESSION   WP_284764102
VERSION     WP_284764102.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..303
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32395
     Region          1..288
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mkfsvftast pewspqeaat klaaqgwdgi ewrvtdqada aepgfwagnr atwpmtgled
       61 sipeiarlta daglefsglg gyarcdnhad vdrvlaataa lgarqvrvnv lplgnsnmgg
      121 peptglsype lfaatrehye wvasraahhg vkalvelhhg tvtasassar rllegldpqh
      181 vgvihdlgnl liegwesplp alqllgpyla hvhvknarwv rtdskdesga avwvnewapl
      241 aegqasvlay fraladvgyd swvtledfst elpleertas nlayvrkaaa lagfavvdpa
      301 sap
//
LOCUS       WP_284764215             364 aa            linear   BCT 25-DEC-2024
DEFINITION  LolA family protein [Arthrobacter sp. efr-133-R2A-63].
ACCESSION   WP_284764215
VERSION     WP_284764215.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Tajima,T., Yokota,N., Matsuyama,S. and Tokuda,H.
  TITLE     Genetic analyses of the in vivo function of LolA, a periplasmic
            chaperone involved in the outer membrane localization of
            Escherichia coli lipoproteins
  JOURNAL   FEBS Lett 439 (1-2), 51-54 (1998)
   PUBMED   9849875
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..364
                     /product="LolA family protein"
                     /calculated_mol_wt=37114
     Region          <101..268
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mvrevvmtrv wlrwlpavla pvalaaaala gsyqagaats lphktaaevi amigradvha
       61 lsgtlqqssd lglpklpsvg ptasqgpasv mellsgshta rvymdgpaka rfqvmdmlae
      121 rdvvrngndl wlynsadnsa ahmtmpaepa rsaaphatpt pgvttpdvva qhflaavgpt
      181 tdvavgdgtt vagrtayqlv ikprstgtlv dsvtiavdsa lglplgvdvr argqaaaafs
      241 laftdvslsa pdaalfsftp prgaaveeka tpqlrslpgk tgqpkataar ptitgtgwda
      301 vmglpagtvp ndvrsapmla qltqpvaggr alttslatvl mlddgrvfag mvplerlqaa
      361 aaak
//
LOCUS       WP_284764262             430 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Arthrobacter sp. efr-133-R2A-63].
ACCESSION   WP_284764262
VERSION     WP_284764262.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 430)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 430)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 430)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..430
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=45559
     Region          91..406
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mkgqaedelq rsswrlalqt gallvlllva iagsvllivs tsqasaaqrl lttatehvds
       61 ivdapagtwl aisnqgvltv spgmpsglpd lkaieavaas gdaaqedvsi agrpytvrta
      121 dsgnrvvqav fdrhenleel nrlglalllt cggavvlasl lavwlarram rpmaealdrq
      181 rrfvadashe lrtpltllsm raqmlrrrva ssplqeppas ieadvdamve dsrsltrlle
      241 dllisadsrr ielteidvva laddvvesfs vsaarrgvtv ersgltgplg iiaaptalrr
      301 lfvalldnav rfarervdva vtadartlvi tirddgpgfa ddvrprafer fatappadaa
      361 pedgtaarhy glglalvaev aaqhggraei aaqpsgaavv vhlpirrnqg nspaagswls
      421 afvsrvrrmf
//
LOCUS       WP_284764337             365 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284764337
VERSION     WP_284764337.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 365)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..365
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36701
     Region          57..361
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtqstttagp psadgparel aapaphsdsk ghdqpvraka awlvaavvvl glvcaaslat
       61 gargmsletv wqaltqfnpa dgnhavvhtr iprtvlglva gaalglagaa mqgvsrnpla
      121 dpgimgvnag aalavvagiy lfgisgasgy iwfafvgaaa aavvvylias lgrdgatpvk
      181 lalagaalsa glysltnvil vssqdtldrf rfwqvggiag tdwsivlngl pflllgaviv
      241 lgsgrtlnsl algddvargl gqnvalargv aalgivllcg satamagpig fvglvvpham
      301 rfftgpdyrw ilpfsmvlap alllvsdvig rvvllpgevp agimtaivga pvfvwlvrrg
      361 kgvsl
//
LOCUS       WP_284764353             306 aa            linear   BCT 25-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284764353
VERSION     WP_284764353.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..306
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33609
     Region          7..282
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 msvitetkle faklgsriga eirgfdlsge lspetvaqir aalnehkalv freanilsde
       61 aqvkfashfg plttahptva svegeenvlp vdsengsann whtdvtfvvn ppqastlrsi
      121 dlpsyggetl iassagayad lpdelrnfad tlwaihtndy dysvpknleh enaderrkef
      181 trikfetahp vvrvhpltge rglfiggfaq rlrivglsnt eskdiirllq ayvirpeniv
      241 rvnwepnqlv lfdnritqhy apdnydgqpr klnrvtiagd ipvgvdgkps qsiqgdssay
      301 svvapv
//
LOCUS       WP_284764447             723 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium sp.
            UMB6689].
ACCESSION   WP_284764447
VERSION     WP_284764447.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB6689
  ORGANISM  Corynebacterium sp. UMB6689
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 723)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 723)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 723)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 723)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..723
                     /organism="Corynebacterium sp. UMB6689"
                     /db_xref="taxon:3046341"
     Protein         1..723
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=75294
     Region          3..722
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mttsltlgit gmtctscssr verklnkldn veatvnfate sasvsydpat ttpadlidvv
       61 egagygaftm dgegeepast aedareseas dilqrtllsa alslpvmlls mvpalqfqhw
      121 qwaclmlttl vyviggapfh ratwanlkhg aatmdtlitl gttaafgwsl yalffgdagm
      181 pgmtmhmtlr sndaqmdhiy lesvgmvitf lllgrwfelk akgrssealt tlltmgakea
      241 tvlrdgtetr ipaselhvgd vfvvrpgeki atdgvvlsgh savdeslltg esmpvevspg
      301 stvtgatina sgrlevratr vgsdtvlaqm galvtaaqts kapvqrladr iaavfvpivi
      361 giallalvah llfggiapaf vaavsvliia cpcamglatp tailvgtgrg aelgilikgp
      421 eilestrqid tivldktgti tegqmsvgai qstaghtqqd vlrlaaaaeq gsehpiarai
      481 rtaydgelpt aedfhelpgq gieatiegah vrvgrppagy egtgtqvgvy vddtlagtie
      541 lqdrikessa aaiaamhklg ltphlltgdn agaaravara vgiddanvta evmpadkvdt
      601 iarlqeqgrt vamvgdgvnd aaalaqadlg iamgagadva ieasditvmn ndlrsvaeav
      661 rlarstlrii kgnlfwafay niillpvaaf gllnpllagl amalssvfvv tnslrlksft
      721 pee
//
LOCUS       WP_284764485             117 aa            linear   BCT 25-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Arthrobacter sp.
            efr-133-R2A-63].
ACCESSION   WP_284764485
VERSION     WP_284764485.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-R2A-63
  ORGANISM  Arthrobacter sp. efr-133-R2A-63
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 117)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 117)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 117)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 117)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 117)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Arthrobacter sp. efr-133-R2A-63"
                     /db_xref="taxon:3040278"
     Protein         1..117
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12607
     Region          5..114
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mvdakrfrvl leeerdrkva llkallgdit svnvarqdan vddehdpegs tiafelsqas
       61 almeqsrvgl eqieaallri asgsyglcav cgkpiaearl earpwtpyci ehasgqg
//
LOCUS       WP_284764621             433 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium sp. UMB6689].
ACCESSION   WP_284764621
VERSION     WP_284764621.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB6689
  ORGANISM  Corynebacterium sp. UMB6689
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 433)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 433)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 433)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Corynebacterium sp. UMB6689"
                     /db_xref="taxon:3046341"
     Protein         1..433
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46323
     Region          12..419
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 msvphprnvi ttkalsvwva avlvyivait grtsfgvagl eaidrfdvda sriavftsvq
       61 lgiyslaqip tgmlidrfgp rrllvigsvi mgigqvvlgf tsnywvaiaa rlligagdat
      121 aflsvmrilp ywfplhrtpm ftqvtsslgq lgqfmsalpf aillgwggwt mafvtlgavg
      181 iliavaaava vadspeslgi vpkpkekpna kpestaalls tvflspvawq affihwiglg
      241 atnvfvmlwg vplmtagmdf sktsagwvlt wfsvcmvlvg plhgrlssra rgfrpwlalg
      301 fvaihcavwv lffffggsyl slfilisvvs lctpvanygf divrenldrr vvatatglgn
      361 mggfiatvig aqlvgmvldh lgngpdypyh dfrlaawavf gvwcigivgv lithilrsrg
      421 geegphariv qvg
//
LOCUS       WP_284765263             323 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Corynebacterium striatum].
ACCESSION   WP_284765263
VERSION     WP_284765263.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..323
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34255
     Region          3..319
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(40..41,45,118,122,125,143,146..148,167..168,172,187,
                     210..211,232..236,257..260,307,309)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(130,225..226,239..244,252..259,262..263)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 myaiqvnqtg gpevleyvev paptptedqv lvdvivagvn yidtyyregi ynaatpfalg
       61 legtgrvvhd pkgeiaegtm vawdhgfgsy aeqvcvsrdr ivavpddfpp evagsmllqg
      121 mtahylangv yqlgegascl itagaggvgl iltqmakalg atvytvvstd ekaqlsyeag
      181 adqvfrygeg laeqvrrfng grgvdvvydg vgkdtfnesl evvrprgtva lfgaasgpvp
      241 pmdpqllnkh gsifltrpsl gawtaqegef qmraqavvqa vtdgavtfnv tasyplkdaa
      301 qahrdlhark ttgsivlrvr edn
//
LOCUS       WP_284765455             744 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium striatum].
ACCESSION   WP_284765455
VERSION     WP_284765455.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 744)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 744)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 744)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 744)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..744
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77424
     Region          6..742
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtnlvhldlg vsgmtctscs srverklnkv dgveatvnfa tesasieydp ststpdslie
       61 vvrgagydaf alteeqkads eetanpvdea raqeakdllr rtiisaaist pimvvsmlpa
      121 lqftnwqwaa ailativyif ggapfheatw anlkhgsftm dtlitmgtta ayfwslyamf
      181 fghaghpgmk mhmelvsnna emdhiylesv gmvitflllg rwfevkakgq ssealrtllg
      241 mgakdatllv dgaekrvpik dlkvgdvfvv rpgekiatdg vvnagasavd esmltgesvp
      301 vevkegdhvt gatinssgrl evratkvgad ttlaqmaklv teaqaskapv qrlvdkiaqv
      361 fvpiviaisv ltliahliig gaaatapafv aavavliiac pcamglatpt ailvgtgrga
      421 qlgllikgpe ilestkqvdt ivmdktgtit egkmsvagvh aaqtsdqdat qvlklaaave
      481 agsehpiaka ivhaasdvtp asdfasvagr gvegtvegqr irvgrvegel gslseafraa
      541 eaeggtpvav yaadaligii dvrdtvkess aaavaqlkel glvphlltgd nesaaqavaq
      601 avgidpenvt agvlpedkvd vvkqlqssgc nvamvgdgvn daaalaqadl glamgagtdv
      661 aieasditlm sddlrsaada irlsrrtlri ikgnlfwafa ynvilipvaa igllnplfag
      721 iamafssvfv vsnslrlrtf qpta
//
LOCUS       WP_284765631             437 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Corynebacterium striatum].
ACCESSION   WP_284765631
VERSION     WP_284765631.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..437
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=49163
     Region          1..437
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mttlhwfrdd lrlhdnpalt waasrgevia cvldepaypg srplgsataw wrerslsrla
       61 anlasynvpl yrlngdarsv lpafaathkv savcwnrryh lptidaavkd tllaqgleah
      121 sfaahclvep havkpfkvys afaraarevl qdtlesalnv palqgpgaia weelpspgwa
      181 aslaeywtpg ekaardrlas ldlsdydkgr dfparpatsr lsphlrwgev sarevwqfas
      241 alptdassfh sellwrdfaw hrlyhvpdla tepvrekfrn fdwywdgggi dtsgkdsrph
      301 plpelqawrt getgiplvda gmrelwqtgy mhnrvrmvvg sfltknlgih wrhgeewfwd
      361 tlvdadpasn pfnwqwvagc gddaspffhi fnpqlqaskf dpdgtyvrqw applspppiv
      421 dlkesrqaal dayqeir
//
LOCUS       WP_284765709             332 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Corynebacterium sp. MSK195].
ACCESSION   WP_284765709
VERSION     WP_284765709.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426811
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..332
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=35879
     Region          46..332
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 malrkrssvv arswlkrlrp shraelekly gglhdpstep glthisasgt vdhdgldiaw
       61 yevgqqdapv tvvfihgycl sseayydqan ylrgrnaral lvdlrghgqs stvapgectv
      121 daaaddvlav ireraphgnl vivghslggm valnlirrap aevyerikga llistsmrrf
      181 aakgvaqilq skslhalyrl clrlpgrvds arfevarfia plfavtlagf pqmeklqfhv
      241 amlldtplas ysgffddlle haeygaaerl aklhgevvvg tadivtprsq sevlcenwpt
      301 aslqtvggsg hmviledpea isaalgrvld av
//
LOCUS       WP_284765727             181 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium sp. MSK195].
ACCESSION   WP_284765727
VERSION     WP_284765727.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 181)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..181
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19518
     Region          4..156
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18879"
                     /db_xref="CDD:467590"
ORIGIN      
        1 mptpdfivql rekighdqif vpacsaiiir dvpadaalwe vpsvllvkrs dngawtpveg
       61 icepgeeitt talrevkeev gldakveall gvgqsgpvty pngdectfmg talrvsvadg
      121 aepvisdeen teagwfsvak lpdsvsrrhr lmiadavaqm khprgfaprm gwmkrseqpg
      181 l
//
LOCUS       WP_284765750             246 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: lysophospholipid acyltransferase family protein
            [Corynebacterium].
ACCESSION   WP_284765750
VERSION     WP_284765750.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..246
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27534
     Region          1..223
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mknkwywafk hiffgpalrv wnrpwtegie kipaegpail vsnhqavmds fffplvcprq
       61 itfpakseyf ttpglvgslq kwfftsvgqv pierdsedag daivetaegi lsrgdlfgiy
      121 pegtrspdgr vyrgrtgmar iametnqpvf piaminsrka npigswiprp fkvgvrvgdp
      181 iwphewaker gmnpaeheti raftdfvmrn laelsdkpyv dvyasdvkas lkaghgypag
      241 aeykgr
//
LOCUS       WP_284765764             223 aa            linear   BCT 25-DEC-2024
DEFINITION  cell division protein FtsQ/DivIB [Corynebacterium sp. MSK195].
ACCESSION   WP_284765764
VERSION     WP_284765764.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..223
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=23685
     Region          26..222
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mrvsakliag viaaivaval iaaavmwtvp vlkvrnfqve gvhqldpaqv eeasgvpege
       61 nllrvnarea asgvagldwv dsvtvsrdfp stltinvseh kavafvkrdd kpfliddkge
      121 eftsaeppag avevtgsvds gspqtqdavr aiaalsddvr nqvaklevag eysltfttkd
      181 grrvfwgasd sndedkahaf atvlkmegre wnisnpelvt trg
//
LOCUS       WP_284765885             376 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Corynebacterium sp. MSK195].
ACCESSION   WP_284765885
VERSION     WP_284765885.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..376
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41354
     Region          230..363
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mhlvhiarpp rpahsptaha qpsepadcir sfvfwanlaa qeasgdaaas tspgrvvqrl
       61 qgssesqthl favvdgdstl gevsdlglpl ipsvepspel dylgfihisl plleereaae
      121 iecvlcdlpl pgeqldeegr kvaewmgtka lelarklgrt vahvgllhpp gadpdydamg
      181 siyrelgftq rhaehqlvmd ipespvaall pagitarvwp dydipegyld evmrllslas
      241 tdaetgdltv epivwtrarl reahsrlrsr rghtllialt aedgsilalt emarhedanp
      301 evcewtltvt drphrrrgla qlakltalhe varywprvrr cycsvaakda amnaiyrslg
      361 arelsrssaw elrlrd
//
LOCUS       WP_284766098             444 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF445 domain-containing protein [Corynebacterium sp. MSK195].
ACCESSION   WP_284766098
VERSION     WP_284766098.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..444
                     /product="DUF445 domain-containing protein"
                     /calculated_mol_wt=48831
     Region          34..443
                     /region_name="YjiN"
                     /note="Uncharacterized membrane-anchored protein YjiN,
                     DUF445 family [Function unknown]; COG2733"
                     /db_xref="CDD:442039"
ORIGIN      
        1 mthradegle sapatassga apvpqagnqe arradlrrwk aialsfliga aviflgcsww
       61 qasesgapvw vgyvraaaea gmvggladwf avtalfrrpl glpiphtali pnnkdrvgda
      121 lkdfveenfl tadalsakvr eaelplwlar qgvepgkaee vsawigeraa svvedldpee
      181 aeqfirtqvm drlaepewgp plgrllegyi adgkarpled dliewahgki lsmeptvvta
      241 idermpgwap rfaremvgek vytelvefad evrrngnhea rlairrnlsk laadlqwdad
      301 mrgriegikq emltsdqaqq apaamwrtvs ttlidqlndp esflrlkita kvkelahrll
      361 edseflaqan alvdkaarya vekfapeiia iipetikrwd aeeashniel mvgkdlqfir
      421 lngtivgsla glvifainhl ifga
//
LOCUS       WP_284766102             461 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium sp. MSK195].
ACCESSION   WP_284766102
VERSION     WP_284766102.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..461
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48570
     Region          97..397
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mhtlrsigss vagiaiaagv lsapiasave paeiqgdatp stirevnltd padpeninya
       61 ittkgdsrvv diaglkdkdk wkgyafghks kagkhygnhv ktltatsaam ggrevplavi
      121 tpdgdfekkr ptlyllngag gaeqgmdwlt atanhdidpe tegvqdmvdf ytskdvnvvi
      181 pqagafsyyt dwvsspnsgy lkgpqkwetf ltkelpdale khiggngkrg iagmsmsats
      241 slllaehnpg fynavgsfsg caatsrplpr lytqltvnrg ggsadqmwga mgseynvynd
      301 alvnanpnnl gksetyvsvn sglggandwg vpgsstlive ggvieaamns cthdlkakmd
      361 sqgmdadwnf rntgthswpg wrndlftswa tfergfnkda aeapaepevk pnelsieapq
      421 aeenaqvkda psaadqspdk dfvegmdaeg aaaaeaavaa e
//
LOCUS       WP_284766128             304 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Corynebacterium sp. MSK195].
ACCESSION   WP_284766128
VERSION     WP_284766128.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426811
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..304
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=33350
     Region          18..303
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mafaplppst veldgpyahe fvhtrgirlh vatagdstqp lvvlihgafg gwfdyqdvia
       61 piaqrgfhva avdmrgfgms dkppidagqd irtlvgdisg liqalghdda fvvgadtgga
      121 vawclaaerp ervrglasis aahpvdlrra iaarpwdfgw inlrsllcrl prvtraqnll
      181 lsprayrkel eldtgpslad atldrildlr lrasrigsvr rgilwnhrmr tavvpltwie
      241 ltverpvlfi haqqrlwnpv vrraasrarr gftattvpga knlphleapa dfvstlaawl
      301 qehr
//
LOCUS       WP_284766262             278 aa            linear   BCT 25-DEC-2024
DEFINITION  spermidine synthase [Corynebacterium sp. MSK195].
ACCESSION   WP_284766262
VERSION     WP_284766262.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..278
                     /product="spermidine synthase"
                     /EC_number="2.5.1.16"
                     /GO_function="GO:0004766 - spermidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29923
     Region          32..231
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mgrkrastdp gitgtyeist gtaevvpdef rdgayilnvn gvpsshivlg epeelefeym
       61 rwiaaavehl nsrpanklrv thlggagcsl pryfasklpg srhtvvelda klgelvrtlf
      121 dvprsptvki ragearkete gflpssrdii irdvfagdkt panlttveff qaakqslapg
      181 glyvancgdh sdlqlaksel agldkvfdhl sviadppmlk grrygniilv asdtempaeg
      241 smeaaqlakt llggavpahy kdeewtrtff agataard
//
LOCUS       WP_284766395              59 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium sp.
            MSK195].
ACCESSION   WP_284766395
VERSION     WP_284766395.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 59)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 59)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 59)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..59
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..59
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=6513
     Region          1..57
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 msqvpmeylt kaqvveltgl santitkran dgllhpikst rdtrmnlyrr aevealltp
//
LOCUS       WP_284766420             458 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium sp. MSK195].
ACCESSION   WP_284766420
VERSION     WP_284766420.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..458
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=49093
     Region          8..399
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mtisthgals rlhkfagvii apflivaals gflyalaptf epwiyhdevt ataqgsprsl
       61 deqiaaaqrq hpdgtvvrve psedpqettr vlfddptapn ssythavfvd pvdlhitgel
      121 qqyggsralp frtwasnghr tlwlgepgrl yaelaaswlg alsilglylw lkrkqrnkkk
      181 rstvlalhar vgawllpgfl fltvtgltws lvagtgigkv reelnwkeps vatsvaeaga
      241 stgagehanh aghaghaght ghhgaaelag aqtaestars qgltgvlemt ppekpgdawg
      301 vrearaafkl rsdavavtpn gevidrinsa dwplaaqlts wliqlhmgtl fgiysqvala
      361 vlalgllvvs iaglwmwwkk prrslpelki tpavlagvma ysiiaplfga slvifflgdw
      421 vvrrlrapqr grgaaagett prprgesssr slstdrng
//
LOCUS       WP_284766402             524 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Corynebacterium sp. MSK195].
ACCESSION   WP_284766402
VERSION     WP_284766402.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..524
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55423
     Region          128..515
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mttphthest ahtegdeapg aprsewrrqf iglfiglgla vlvffifpsn aietvqgsag
       61 adpeaeytls airtvaavti lmgvwwmtea iplaatallp liifplagvg tikevgapya
      121 satiflfmgg flialalqrw nlhrrlalyv vkiigtspkr lilgfmlatg flsmwvsnta
      181 tavvmlpigt svlaltaetv ggwekqkkfa talmlgiays asigslgtli gtppnaflna
      241 ymadtwdvtl gfgrwmavgv plavtfllia wallitvfkp emkdipggre lindeikalg
      301 pwtrpqimtg iifvlaaaaw vtlplvlkef enyddaivgi aagillfilp adnqrrirll
      361 dwktanempw dvlllfgggl slssvfnasg lslwigemak glsvlpvvli vsavaalvlf
      421 lteitsntat aatfipimgg vavgvgltad gdinvlllti pvalaatcaf mlpvatppna
      481 iaygsgyvki gemikgglgl niigiflitl tvyllavpif glsi
//
LOCUS       WP_284766421             297 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium sp. MSK195].
ACCESSION   WP_284766421
VERSION     WP_284766421.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..297
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31902
     Region          109..>199
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mtnadanqdp hrplepgqew higgqdrqme ekeqleqlva yidahydtpd frppwagggs
       61 peadqycall pdrithaamm vlgtavdhal pgtaytedis veesevgaif rpstptsrwa
      121 vslhsggwwr gdgqalemqw rpevaaaaql sgttiidvdy plapehtvae mvtavqqaid
      181 yarvqgassv ttwgyssgga laalapadal lltfpdfgal anlpkdlrag yaipadlskl
      241 cpdifvqtat edeiaarvsv psavardyvs thrvstpava rqrvrdaaaf larelek
//
LOCUS       WP_284766512             342 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: COX15/CtaA family protein [unclassified
            Corynebacterium].
ACCESSION   WP_284766512
VERSION     WP_284766512.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..342
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=37070
     Region          16..305
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mlcvnywtki krffkeaapt lqqqrliali lllcqggitv sgsivrvtgs glgcptwpec
       61 qpgslvpmeg aapalhqaie fgnrlltfvv taaavaavia mrmarrrael kvyawlnvag
      121 ivlqaiiggi svhldlrwws valhflpsml lvwlaamlys rilepddgtp rarfprairl
      181 laavatvals ivlitgtmvt gsgvhsgdsg vgmegrlqvd teamavtham cmyvyltltv
      241 itvfllyknr apqdakkagw vlvvciliqw avgvyqfyms iprwtvpfhi glssfvtayt
      301 allwahgvrr tdgtadlitg spsgdekyaa rqasleqela ta
//
LOCUS       WP_284766592             528 aa            linear   BCT 25-DEC-2024
DEFINITION  inorganic phosphate transporter [Corynebacterium sp. MSK195].
ACCESSION   WP_284766592
VERSION     WP_284766592.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10475700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..528
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006817 - phosphate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56242
     Region          62..511
                     /region_name="PHO4"
                     /note="Phosphate transporter family; pfam01384"
                     /db_xref="CDD:460184"
ORIGIN      
        1 mtdieavngk gndwiwhaif ggltavtlig fmvwghdyvd gskpillgta ilfalfmafn
       61 iggndvansf gtsvgagtls mkqalvvaai fevsgailag gevtdtvrsg ivdldaidgl
      121 dpmefvyimm asllgaaiwl lvatrmgwpv stthsivggi vgaaltvgfv tgkgswnmvq
      181 wgeigtiais wvlspvlggl aafilfkwik tsilvyneea drklreiktr raelrqehks
      241 rfarlneiqq isytnamard aalvaeedfd peqleseyyr dlynlnkdmd dvkahrales
      301 wvpvlaalga iiisamvmfk glkhtgldfs vlqnllvmgm vgavvwmavf ifarslkkks
      361 lakstfllfs wmqvftasaf afshgsndia naigpfaavi dvlktgqvnd eaavpvavmi
      421 amgialisgl wfigrfviqt vgsgltqmhp ssgfaaelaa aavvmgssil glpvssthil
      481 igavlgvgiv nkaanwnlmk pialawvitl paaaviaait vsvlrvvf
//
LOCUS       WP_284766638             386 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium sp. MSK195].
ACCESSION   WP_284766638
VERSION     WP_284766638.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..386
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=42554
     Region          23..344
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 msnqfqvdpg lgasvqpqas vksvpqhlpe ldglravasl giivthvsfq tgtgwgfagr
       61 fdffvavffa lsafllwrrr glhtlsgyar srvarllpay yacvvavmll lpdahsltlt
      121 qllsnltstq iyvvdglapg lthlwslcve fffylalpvl vwllgtlprr wrvaaialga
      181 viswtwgfvp fvadyakdqv nsqiwppaya swfavgmlaa eceeagvsrr vqrvlrprwa
      241 wwlvaavvlw issrewfgpq glihpepaef srriiagaaf aavvvipval aprdkswlts
      301 plmqalgaws ysiflwhvai lglafpltgv plfsgkpldf wvilavtvva tvvvsaasyt
      361 lierpgrdll lgrrrkdrpr prhtss
//
LOCUS       WP_284766617             337 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase [unclassified Corynebacterium].
ACCESSION   WP_284766617
VERSION     WP_284766617.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..337
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36442
     Region          55..328
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mtasikgrvl svimavaval glavvagsqp aeaanrdwlr rdatgtcewd kvgwwvqrcd
       61 vwsqamgrti pvqvqpakrg gnaalylldg lratertnaw vndvnaakty ephnitlamp
      121 vggaasfyad wqgpatydle npvnykwetf ltselpgyle rnfgvarnnn siaglsmgag
      181 aaltlaakhp nqfrqalsys gfltttvpga qtfmrlamld aggfninamy gslfnpkrfq
      241 ndplllipkl rntnlyisaa sgvpgagdsh ylpehqaaga alevgsnitt rvwegaarlq
      301 glnptvsypa qglhnweqfg yqlnrskpqv lnvmnaw
//
LOCUS       WP_284766696             201 aa            linear   BCT 25-DEC-2024
DEFINITION  LGFP repeat-containing protein [Corynebacterium sp. MSK195].
ACCESSION   WP_284766696
VERSION     WP_284766696.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..201
                     /product="LGFP repeat-containing protein"
                     /calculated_mol_wt=22138
     Region          <18..159
                     /region_name="Psp3"
                     /note="LGFP repeat-containing protein, may be involved in
                     cell wall binding [Cell wall/membrane/envelope
                     biogenesis]; COG5479"
                     /db_xref="CDD:444230"
ORIGIN      
        1 mllllvlvfq vprffhghwi ggrieeayhr lggwktfgda ttdervaknn grfqvfakda
       61 siywhagvdn giahqvggri rnkwgdlgwe gaalgypitd elktpdgkgr fnhfqggsiy
      121 wspetdahqv wggirdkwaq qgwetgelgy pttdelltpe rlgattifka dlstghklag
      181 sivflapfgi fgevrdgsva l
//
LOCUS       WP_284766715             320 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium sp. MSK195].
ACCESSION   WP_284766715
VERSION     WP_284766715.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..320
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32044
     Region          49..308
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 maprtkasac lvlataaaaf vwwwrlrhvq vpvdtpwlee elhsvafdrl lattvvgial
       61 gvgglllrta tanpladpsi tgvnsgaalg avatamfigs etsrvdqlpg allgagiavg
      121 vtvgvgksga iqrmvlvgva vsalcsalts iflvvdeaql atvmswlsgr lagvrlsgim
      181 paliavlvvv pltlvgaktl dllvagdava gavgakperi rlaaivaavv liapavaatg
      241 pigflglmaa avawrvcgph hrmglcvagi vgaavllvad svgqgiwapa etpvgivtsl
      301 agmplvlwsv halgrrkhaa
//
LOCUS       WP_284766763             516 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Corynebacterium sp. MSK195].
ACCESSION   WP_284766763
VERSION     WP_284766763.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..516
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56886
     Region          54..487
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 msdsnsrpsf nrrnflqiag vsaaavaagi napaqasaqs slsswgssqg gdhpqdself
       61 glgvaagtpr hdsmilwtrl apeplaedgh ggmtggdvrv gwevakdegf gdvvkqgeal
      121 aqrelahsvh pqvtglepat eyfyrfrvdg kvspvgqfkt lpapdakvdd ftftvascqa
      181 wyhgyftpwk hiaqepdldm tifvgdyiye ygivegdnlw rqgasvpdvf kakvetleqy
      241 rlryslfksd ehlqaahara amaivwddhe vennyagnws eigtkaehfl yqraaayraf
      301 yenlpvappa lpdgpnnriy dsfdvgtlmr fnlvdtrqyr eesaedasil gaeqeqwlnd
      361 klatspaqwn vvvnsvvvvp iadstdqwdg fpaarhrlie slskvsdpiv ftgdihqhca
      421 aeiqsesgqp vgvelvatsi asdgdgfags kstewlekpy vkamdkrrgy ikvrasrehl
      481 dsefvvvpwi erddtapret afsfrtnage htlrsl
//
LOCUS       WP_284766864             164 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Corynebacterium sp. MSK195].
ACCESSION   WP_284766864
VERSION     WP_284766864.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..164
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17968
     Region          1..163
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
ORIGIN      
        1 mlirpaglad vpamtetlnw aiehtdvifr aspasiaere aylrhiweeg cpcliaesds
       61 gaylgwalyh pyrdpqvwtg cyettiylsp aaqgqgvgta llgalvntar addkvhslla
      121 livstnaasl klhekfgfen vgtlkevcyk fdhwlslthl qllv
//
LOCUS       WP_284766422             644 aa            linear   BCT 25-DEC-2024
DEFINITION  M13 family metallopeptidase [Corynebacterium sp. MSK195].
ACCESSION   WP_284766422
VERSION     WP_284766422.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Bland,N.D., Pinney,J.W., Thomas,J.E., Turner,A.J. and Isaac,R.E.
  TITLE     Bioinformatic analysis of the neprilysin (M13) family of peptidases
            reveals complex evolutionary and functional relationships
  JOURNAL   BMC Evol Biol 8, 16 (2008)
   PUBMED   18215274
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..644
                     /product="M13 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71332
     Region          3..644
                     /region_name="PepO"
                     /note="Predicted metalloendopeptidase [Posttranslational
                     modification, protein turnover, chaperones]; COG3590"
                     /db_xref="CDD:442809"
ORIGIN      
        1 mkdlyqlvng pwleshvipd drgvdgtfha lrdeaeelvh eivdqdtgrp gklyasfmdt
       61 egvnaagmap ldadldrlsa adpeelaqrl gelertgvgs pvtfwvskds gsedaiayvi
      121 qsglglpdea yyreeahaet lsayekhvae mlefldparl fglgaevaaq rivslekela
      181 aghwdvvstr davktynpce fselptmtra llsggnlpeh rvvnmmpsyl ehfeslftta
      241 rmadwqlwat whilrsraam lpeevgaknf efygtklsga tqqrdrwkra vglaeslvge
      301 eigqvfvdkh fpasskremd elvdyliaay rerisqlewm tpatrerale klsqfkakig
      361 fpdswrdysg levsgkgadl lanaragsaf shdfelakig kpadrdewvt tpqtvnafyn
      421 pvvnditfpa ailrppfynp eadaaenfga igavigheig hgfddqgsqf dgqgnlnsww
      481 seedrtafdk ltaklveqfn gqvptvlkea gidstgvngs ftlgenigdl gglgiavvaf
      541 knycadkgid lqgkeekfev dgaepelaeh tytglqrffl swarvwrtai rpematqyla
      601 idphspaefr cnliaaniae fyeafdvaed samyiapedr vtiw
//
LOCUS       WP_284766894             392 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium sp. MSK195].
ACCESSION   WP_284766894
VERSION     WP_284766894.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..392
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42680
     Region          147..386
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mstdtaarar lgdkiltava vlialfyvis aaknpsiiei iqaglsllfl pfmwvwrsrp
       61 vlsatgfivl laawavawms qlptnlgltp waltapmavy atsryvtrrv iprtvlalai
      121 lgsfispvmw ridpesfllh yqldrrflam lvvhwavlgs tyfiaaryfd larqqerlaq
      181 erfhqaqeee rlliarelhd vlahsltlik vqanagiiag rvdseaaqda latiregads
      241 aleevrgivt alrstgpsal kpteqlehie giidgfraag leitaglpet yeapaltqla
      301 lvriiseglt nalrhqgpgt hievelalvd aaritltstn psptpsevtg sgvgligvee
      361 rahalggrle rsgdakkfil raelplwkes rv
//
LOCUS       WP_284766929             262 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Agrobacterium sp.
            CFBP2214].
ACCESSION   WP_284766929
VERSION     WP_284766929.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. CFBP2214
  ORGANISM  Agrobacterium sp. CFBP2214
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Agrobacterium sp. CFBP2214"
                     /db_xref="taxon:3040274"
     Protein         1..262
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27701
     Region          7..229
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 msqipavlit rastgigaty aerfarrghd lvlvardavr mealasrlrq etgvaidilq
       61 adltkaedlv kvetrlrdde rigvlvnnag aaiggtfvdq naddmtklva lnatalvrla
      121 saiaprlana gegaivnigs vvglvpefgm tvygatkafv lflsqglahe lgpkgvyiqa
      181 vlpattrtei wdhvgadvna mnnvmevgdl vdaalvgfdr repvtipplh dgsqwdaldg
      241 arkamlgnlv nalpaeryrt qa
//
LOCUS       WP_284766948             403 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium sp. MSK195].
ACCESSION   WP_284766948
VERSION     WP_284766948.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..403
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=44041
     Region          159..401
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mklfrkfdam lqrplwqklv iaavavigdf lvasvhlsss evvedrlvpt faamlgtwil
       61 lpfalrhaar erdprstqpg prsalvaati isatvsiaef rpsvfmaafs aasrrsrlwm
      121 avvcvamlvs klaatdisip agesfayklg yfgslvypal ivlvvglvrs nqkertialq
      181 aqaeltheem atrenfarqe erdriardmh dtlshrlsmi avyagglayr kdldpeetrk
      241 sartirdeae aavgdlreal hslrsegrid pregvdslve rsrragmdve vrykqgtgpq
      301 slaelstmag halnravqeg ltnarkhapg epvtitiaal adallitmsn pvapaekkrs
      361 gnsggygivg mrerasvvgg slqvndeddr fswslrlprk evq
//
LOCUS       WP_284767011             700 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Corynebacterium sp. MSK195].
ACCESSION   WP_284767011
VERSION     WP_284767011.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..700
                     /product="PhoX family protein"
                     /calculated_mol_wt=76790
     Region          46..692
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 malkgrnlls slfassrssl tctykcgnac fgecenksnn pyfadqfsrr talragslsv
       61 vtvgggaala acsnpddasn easssegkgg ktseanvelt saegmkfdpv qpnekdevvi
      121 pdgyeqsvli awgdplfeda pefddknqta eaaekqfgfn ndfagliehp nddnrliyvc
      181 sheyttepqm fpnydadnpt eeqakigwag hghsivevsk vgktgelkre fgplnrrita
      241 tteftlvgpa agsdyvktsa dktgkkvkgt lnncsggitp wntmlsgeen fdqyfahakl
      301 ddkkaqesle rfgmedgesq rkwerfdkrf dvskepnepn rfgwiveinp ldpkstpvkh
      361 talgrfkhea gnihiasdgt vvcysgddsr feyiykfist kkykegdieh nlsildhgtl
      421 yvakmegnsp edeidgsgvl pedgafdgkg ewiklltsdt ennkfeshvd gmsaeevavy
      481 treaadkvga tkmdrpedmq vhpdsekvyv altnnkyrga tgenakknke epmewapike
      541 nknglvmeie ddhagekftw nlflvcgdpk eantyfggfd kekvspiscp dnlafdshgn
      601 lwistdgnal esndglyavt tegdtrgelk cfltvpagae tcgpivtder vmvnvqhpge
      661 tddatfekqt shwpeggkst prpavvvvwk kdgnigvdkk
//
LOCUS       WP_284767093             138 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [unclassified Corynebacterium].
ACCESSION   WP_284767093
VERSION     WP_284767093.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..138
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15566
     Region          4..132
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mmatpsvhty riqtrwsdfd myghmmnany ielaqearla fakehiyskg ldfiafvrhl
       61 dvdflrpief kdtttvevdt avsqigttsf tttqqvknaq gevaatvdcv qvvidrqqqt
      121 prpltdqekd ilhntaan
//
LOCUS       WP_284767083             351 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium sp. MSK195].
ACCESSION   WP_284767083
VERSION     WP_284767083.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..351
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36761
     Region          40..346
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 megaevaala rqhkkltwqr igivagltli aaaafvisnf vgaidispae vikgivnpag
       61 ledqtrtvlw qlrlpmavma vligmalsla gaemqtilnn plaepftlgi saaaafggat
      121 sivlkwqlia qpqfnlalma wlaaavatai iviaavirga kaetmvllgi glvfffqaml
      181 aliqyqssae alqqivfwsm gsltranwaa ngvlaavlii alpilwalgw rltalrlgda
      241 ratamgints rlrivvlivv slvaattvaf agiigfiglv gphiarmlvg edqryflpas
      301 maagaavmca ahavslmikp glaipigivt sllgvpffia ivmtrrralw t
//
LOCUS       WP_284767197             212 aa            linear   BCT 25-DEC-2024
DEFINITION  DedA family protein [Corynebacterium sp. MSK195].
ACCESSION   WP_284767197
VERSION     WP_284767197.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK195
  ORGANISM  Corynebacterium sp. MSK195
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Corynebacterium sp. MSK195"
                     /db_xref="taxon:3050216"
     Protein         1..212
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23070
     Region          11..208
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mdflsslhnl mdagsllqsf gpyillgvav vifiesgvlf pflpgdsllv taailrheld
       61 inawllfvva avaafagdqv gfylgrrfgr klfkddarvl rtehldsaed ffqrhgpval
      121 vlgrfvpivr tfvpfaagta emgyssflrw nilggvgwvg smllvgvllg gipgiahsid
      181 iimliivais vlpmiiswin krrkekheip at
//
LOCUS       WP_284767353             741 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium sp. MSK158].
ACCESSION   WP_284767353
VERSION     WP_284767353.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 741)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 741)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..741
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=81454
     Region          14..734
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mnsashkhat aagssereai ateqdyvdgl farlddevaa anerlnevqa dvdpstpdad
       61 alvrreteyh glqakldrln vaqmglvfgr ididapgdnp tpegldrryi grmgldared
      121 dyrtllldwr apmarpfyla ttaqpegvht rrqirtkgrt vtgihdevla gpgvreeeag
      181 vasesalyha mqrartghma sivetiqreq deiirdntrg vmvveggpgt gktavalhrv
      241 ayllythrel lsatgvlivg pnssfldyis rvlpelgetg vvlstigglf pgiepsheen
      301 lvareikgsd amveilstav kdyqllpddp relvvdglal evtpsmvksa rtrarrsrkp
      361 hneargafie hlvedlaqqm aekvgadplg gknllsradi dqfhddlaed aavtalidef
      421 wpelhptdvl aalvssrkli asaahgydee tqealyraeg rawtdsdaal ldelavligl
      481 pnpeekkaad daawreqvad aedaldilss sestdndddm feaeilsahd vidaetlahr
      541 qevrdkrtta qraredhtwa yghiivdeaq eltpmewrml frrcpsrwmt lvgdtsqtgs
      601 pagvddwgea lepfvaqrfr hhfltvnyrt pqpitelang lleminpdai patairdgvq
      661 vrrlekgtyt pgvhseedgr ltavidaata erykglefdh vvvldpqriv daspqglqnl
      721 yvcitratqs ltlvgdcgev l
//
LOCUS       WP_284767370             785 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Alloscardovia omnicolens].
ACCESSION   WP_284767370
VERSION     WP_284767370.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 785)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 785)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 785)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 785)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 785)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..785
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..785
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=87996
     Region          33..771
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 madtnftqhd anaptsrilg aeissdplnp llpiiqvctf hhpdadtdll qrayeravvq
       61 hapqrrrsge pyiihpiava qiladlgmsp kviaagllhd tvedtdftld qcreefgdti
      121 aglvdgvtkl tkmdvgdsaq aetirkmiva msrdvrvlvi klsdrvhnar twryvkpksa
      181 ykkaqetidv yaplanrlgm naikteleel sfktlqpkiy deivelvrhr agqrelylqq
      241 iiadiredld eqnvhaning rpkdyysiyq kmivrghdfg diydlmgvri ivdsirdcya
      301 algavharwn pvpgrfkdyi atpkmnmyqs lhttvvgpgg kpveiqirtw dmhrraeygi
      361 aahwkykeng ragralsapd kqdaergkki daessdffeh dnlqwikqla dwqsevpdsd
      421 eflgflkddl gasqvyvftp kgkivsvpqe gtpvdfayav htevghhtmg aringrlmpl
      481 dtklqngdtv eiitsrgena gpshdwlnfv kspkarnkir qwftkerrte nmeegrdelt
      541 ralrkrnlft qnytrlevfv avaddlgypd vdslytaige gqvstqnvit hilkfvddda
      601 despeqnivp lrrrsgsgpr rtksvgvsvk gvddvwvkla kcctpvpgdq ivgfvtrgag
      661 vsihredcvn vaslkknqpe rlvdvswtsa qgvflvkiqv ealdrgrlls diarvlsdag
      721 vnivagtist gddrvaisqy sfemadmshl nqllasirki dgvfdvyrlt gtkddsklri
      781 rhidk
//
LOCUS       WP_284767392             332 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium sp. MSK158].
ACCESSION   WP_284767392
VERSION     WP_284767392.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 332)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18950610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..332
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=36833
     Region          40..163
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
     Region          176..319
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mpnikkmhet dkdqqheefi sgrhqeipvd pakefhrttl aagaviwrgs pqdpeialih
       61 rphyddwslp kgkvdpgesl pttaareile etgfsvrlgk ligkvtypvq grtkvvyywv
      121 akylggtysa nsetdelrwl pideaqdlls ydvdtavvak aakrlriapa trvlyvrhar
      181 ahdsgswegd dnlrpldkkg rrqaemlvpm lsafhptaiy salpqrcqqt aapladelgk
      241 disinknfgd eawendpeaa kkafrrvvne ggvpvivsqg atipgiiedl apkflkkpvd
      301 klkfkkasvw vlsfnngelt gadylasplp vr
//
LOCUS       WP_284767400             648 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Alloscardovia
            omnicolens].
ACCESSION   WP_284767400
VERSION     WP_284767400.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 648)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..648
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=71579
     Region          294..643
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 maegsshgrr rfsdkwgkhe ldvlavlssa fpqwltsrqi aqrvkayads ygeladqaak
       61 aafakqfqrd rakltamgia iesrqpeyss ksegqdfasy rlqlgdeprt rmhfeaeelp
      121 ilaaanylar slamsaksde kkaedkrnhk asrtqphvaq tptpglglds iapglgtqti
      181 penlmrvvds rrftatvmvd geninvaytd sddlasyvle hpgatiispq eavdafvrrl
      241 naavafeevt vpaesenlia aselrkklee qnededgdsk serkgssfqt gsevdrrlrl
      301 mlflsahlge eyllselaer fiavphtpee ekknvqiirk digtlttvsd dgelagsqff
      361 didwsllese givaatnslg lerlagvsaq ymslltasvs ylahsplmse syrksaevlf
      421 erlqeendna aqnstawlsl tgyelepasy qvvhdaierg klldmdytdg agrtrhklva
      481 paqiyvdegv yyaavwtgvs dedrkepstr sydadsprht pirneasaqw qtlrlarigr
      541 vesvepshdi dipdvplael rewsfengtp avfvtaqknl pfilnlpdak vedsgegqkv
      601 hltvssdswf vafciaharh itavgpatlq smciaraehe lsmntqae
//
LOCUS       WP_284767455             278 aa            linear   BCT 25-DEC-2024
DEFINITION  spermidine synthase [Corynebacterium sp. MSK158].
ACCESSION   WP_284767455
VERSION     WP_284767455.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..278
                     /product="spermidine synthase"
                     /EC_number="2.5.1.16"
                     /GO_function="GO:0004766 - spermidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29896
     Region          32..231
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mgrkrastdp gitgtynist gtaevvpdef rdgayilnvn gvpsshimlg epeelefeym
       61 rwiasavehl ntrpsnklrv thlggagcsl pryfasklpg srhtvvelda klgelvrtlf
      121 dvprsptvki raaearkete gflpssrdii irdvfagdkt panlttveff qaakqslapg
      181 glyvancgdh sdlqlaksel agldkvfdhl aviadppmlk grrygniilv asdtempaeg
      241 smeaaqlaka llggavpahy kdeawtraff tgataard
//
LOCUS       WP_284767486             219 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Corynebacterium].
ACCESSION   WP_284767486
VERSION     WP_284767486.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..219
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23324
     Region          10..219
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mpdslprptt elfpealnls pkqrevltav qrhpegakag tvaeelgmhv ntarghidel
       61 vnagavnvvs apskgrgrps lifqaripdn kavaeeyitl vevlttmlad keelddaasa
      121 kaleigrrwa raagadasdg aldtlfatlr dmgfdpatkp dstdielhac pfvssgleps
      181 pflcavhagf lqetsdddts itlvprqhpn vcrlkikpa
//
LOCUS       WP_284767538             182 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Alloscardovia
            omnicolens].
ACCESSION   WP_284767538
VERSION     WP_284767538.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..182
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=19983
     Region          <7..182
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mfddqgrald iaakqwhfnn aagigfdadv cvkvlhsdvs drlsrlhlsq laylcaalpg
       61 ffkhrgfsvs vdidgevcry ddtlfvavmn epyegggfkf cpqaspydgq ldsciaqgik
      121 ktelvhlipr vmkghhtssr gvhmargrvy rittnvpvwv qtdgevayks ndisisllpq
      181 av
//
LOCUS       WP_284767562             761 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Alloscardovia omnicolens].
ACCESSION   WP_284767562
VERSION     WP_284767562.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..761
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=84408
     Region          1..757
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 msdyseqlre eqsmvdvaya rldeirkqtq drlsevrsrg ahgsptqrse rdsfatmyed
       61 rlyqlrlved rlvfgridtd ddtrlhigri glqstdheai vvdwraeaar pfyeatplhr
      121 gniairrhit lkfrdviale devlnidssq vsqasasgtl tgegallasl atrrtgkmsd
      181 ivatiqgeqd riirssakhp lvvqggpgtg ktavalhraa yllythrstl qrsgvlvvgp
      241 spaflhyidq vlpslgetgv isrtlgnllp gistdvtdnp faarlkgdcr madviahavs
      301 mrvripsqlp vlkingvrvp itradieeaq gnarrshqph nlarntfvks mislltnrfk
      361 eqldyepeys evenaretir msedvkrtln tawlpmnaqw lindlfskph rlkqcapwlt
      421 dtdiaalirp sgsaltvsdi plldeayell gpdpleqqka narssaqsae eryvnemmds
      481 fglknsgisa qtvlshmnns ddsslaerag adrewtyghi vvdeaqelta mdwrmlmrrc
      541 psrsftivgd vaqtsalggt hswnhmldri fgadgwdmhe ltvdyrnpqe vsdiagrfaa
      601 seglyistvs avravddsvv ikklsdmpav isssifhtvd lltqyvssdg sgrvalicde
      661 svrdavdkql rlslkntdai senefdrlts qprwdaqigv ytptevkgle fdavvlmepg
      721 lisenspsrl taaadlyvam trptqklviv qtqedteris l
//
LOCUS       WP_284767693             236 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Corynebacterium sp. MSK158].
ACCESSION   WP_284767693
VERSION     WP_284767693.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..236
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26227
     Region          45..220
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mldpfgnaad rfrhpatgpt damhpgwpes tpfvqlppss vfpsgarmrl rpllrsdghe
       61 wrrqridden flrpveptqa apwaeahsqq awwnhlmylr tavrealvvp lvievegkfa
      121 gqvtlgniqh gsirdcwigy wvysavhgag vataatalgv dhafgrvglh rvtatylehn
      181 pasgrvlaan gfrhegylrr nlhidgawqd hhyvalvked fastaverlr qagrla
//
LOCUS       WP_284767909             199 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Corynebacterium sp. MSK158].
ACCESSION   WP_284767909
VERSION     WP_284767909.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..199
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21189
     Region          10..>187
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 msdlisrpsf nrrsflqiag vsaaavaagi napakagaqs slsswgssqa gdhpqdself
       61 glgvaagtpr hdsmilwtrl apeplaedgh ggmtggdvrv gwevakdegf gdvvkqgeal
      121 aqrelahsvh pqvtglkpat eyfyrfrvdg kvspvgqfkt lpapdakvdd ftftvascqa
      181 wyhgyftrgs tlrknqtwi
//
LOCUS       WP_284768003             336 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Alloscardovia omnicolens].
ACCESSION   WP_284768003
VERSION     WP_284768003.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..336
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36246
     Region          14..301
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mkklivklln tspvlcvlav qtiaiscane iskiaftqie pllvswwrma ftvlimvlwr
       61 rpfsirkran lpkdaktwii lgalgvavag mngvfyiain tlnsgvavai efigplavav
      121 ftgrtwreym gaflafagll tlagaalfsv gpssipglva iiasgvlwgi yivlgrhvah
      181 gssgldnlti slligwiiqs cfigfpavka vivpaqfatw aradggwfkl lvllfimtlg
      241 asivsyifdq vlmrrvsvnr fsvmqsvlpa vnliismffg drpgvmdfvg vgiivfavii
      301 sfssdndplp shdltsrhha kitdeegnie tidvld
//
LOCUS       WP_284768082             110 aa            linear   BCT 25-DEC-2024
DEFINITION  HNH endonuclease [Corynebacterium sp. MSK158].
ACCESSION   WP_284768082
VERSION     WP_284768082.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..110
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12255
     Region          25..91
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mtspqtprkk rdktnapyaf shswrkkvtt wrrklerdpa lavcwlcgga idmnlppthg
       61 raftldhlvp lsqggdlmge vkpahrscns argdgrrsrr gpnpptlldw
//
LOCUS       WP_284768013             762 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Corynebacterium sp. MSK158].
ACCESSION   WP_284768013
VERSION     WP_284768013.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 762)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 762)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 762)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 762)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 762)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..762
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..762
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=84114
     Region          31..762
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mdkpvkrqsg ggmrsmsarl arsltggrvk vnpvldplms ihrkfhpkad adllnraydt
       61 aerlhegvfr ksgepyithp lavatiaaei gmdtttivaa llhdtvedtd ysledltrdf
      121 gpevarlvdg vtkldkvalg saaeaetirk mivamatdpr vlvikvsdrl hnmrtmrflp
      181 pekqakkarq tleviaplah rlgmasvkwe ledlsfaily pkkydeivrm vadrapsrdr
      241 alkeiisqvs galkengiea evmgrpkhyw siyqkmivrg rdfaeifdlv girilvedvn
      301 scyaaigvvh siyqalpgrf kdyissprfg vyqslhttvl adggatlevq vrthemhyna
      361 efgvaahwry ketkgknsgh qeevdqmawm rqlldwqkea adpnefldsl rydltakqif
      421 aftpkgdvvn lpagstpvdf ayavhtevgh rcigakvngk lvalesklks gdkveiftsk
      481 dpnagpsrdw qdflvsarak tkvrqwfake rreehleagr dalatevqrg glpmhrlfta
      541 ssmkqvaeql hytdvdslyt aigaghvsaq hvanqlvamf gdqddaidtl asrtplseie
      601 hsraqhteds asgtgilveg spdvmaklak ccqpvpgdai fgfvtrgggv svhradctna
      661 eklkaeperm levawssgts atgafsatlq lealdrqgll seltrvmsdq ninvltmnsn
      721 rgddhiatvr ftfsvsdtkq lgtlmttlrn tegvfdvyrv ta
//
LOCUS       WP_284768100             376 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Corynebacterium sp. MSK158].
ACCESSION   WP_284768100
VERSION     WP_284768100.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..376
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41288
     Region          230..363
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mhlvhiarpp rpahsptaht qpsepadcir sfvfwanlaa qeasgdaaas tspgrvvqrl
       61 qgssesqthl favvdgdstl gevselglpl ipsvepspel dylgfihisl plleereaae
      121 iecvlcdlpl pgeqldeegr kvaewmgtka lelarqlgrt vahvgllnpp gadpdydamg
      181 siyrelgftq rhaehqlvmd ipespvaall pagitarvwp dydipedyld evmrllslas
      241 adaetgdltv epivwtrarl reahsrlrsr rghtllialt aedgsilalt emarhedanp
      301 evcewtltvt drphrrrgla qlakltalhe vagywprvrr cyssvaakda amnaiyrslg
      361 arelsrssaw elrlrd
//
LOCUS       WP_284768129             402 aa            linear   BCT 25-DEC-2024
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Alloscardovia
            omnicolens].
ACCESSION   WP_284768129
VERSION     WP_284768129.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..402
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=44878
     Region          198..295
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 maavptkakk inirpalsyt aprvpepvqt tytrpwelir rndwykghgy aatlrdtfrn
       61 pwwkpvattf ifvlfyllvs lalyvvagla afgqlsiyty qqymglspen flanpasptv
      121 illtfggvai mlpalwwtih tlksqsfgsl ssvyghlrws amfkstavsf iffallnlas
      181 iivaiasgek vtphapsivs llliitvipi qcateeyvfr glllqamgrw lprithvlvp
      241 iipaliftam hdydligltt ifslgiitgy lamylgglea gigmhiannv simlfaafgf
      301 adggdsdsat spifasidia vqitiaviiv ylavkrgwfd apgrdyaref ydgmmqsvts
      361 wkqrrsmrkq mkryyqqqrq qqmyfaypqq psapvppqpp yr
//
LOCUS       WP_284768293             256 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium sp. MSK158].
ACCESSION   WP_284768293
VERSION     WP_284768293.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..256
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27900
     Region          1..244
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(17..18,20..21,24..25,62,67..68,71..72,102,106,113,
                     116..117,122,138,142..143,145..147,149..150,153..154,
                     157..158,178..179,181..183,185..187,189..190,192..193,197,
                     200..201,207,209)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(141,145,148..149,151..152,192,195..196,198..203,
                     206..208,216,218)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(162..169,180,183..184,187)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mpnllrganp lsriflmfiw vtpllgsidw vsaavslalt lilaplcgvs wvrlfkagwf
       61 lfliapisgi smllygepgg rqyfswwlia vtqnsltlai aitlrvfava lpmvvlardi
      121 dptelgdals qilklpsrfv vgavagvrmm tlfqsdwqsl gmarrarglt dvgklkhllt
      181 msfgllvial rrggklatam eargfgrtpp rggartware srlrardgwi malgtvfafv
      241 pvvvsvltga wrffgl
//
LOCUS       WP_284768271             294 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Corynebacterium sp. MSK158].
ACCESSION   WP_284768271
VERSION     WP_284768271.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..294
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30721
     Region          5..282
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(34,231,234)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(181,202,229,232..233,236)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mtihvcgegl vdlvpvapgs lndhtpalgg gpfnvaiaaa rlgadvefqs ristdgfgqe
       61 lvgrleaegv ttshlqrgde pttlavttih edgsasynfy iegtadrlve prlvpadiac
      121 fgtvslalep gasryaqllk dfaaqgtlva ldpnirpfya taehreflae llpyvtllkl
      181 sdeqveflgd dlisqvpivv vtrggeglsv ragdttltvp aaqvtvsdti gagdtimaal
      241 ltqidergld ssalaqlgaa ewkellsfaa aaagitvsrr ganpprreev essl
//
LOCUS       WP_284768312             299 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Alloscardovia omnicolens].
ACCESSION   WP_284768312
VERSION     WP_284768312.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 299)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..299
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33184
     Region          1..295
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msnvdtvptn krhgdwrgwk fvwpfscafi fvfivpvlya iwisfyqnrm vggnkfvgfa
       61 nyqrllsdaq fwsavghval ftvvqvpiml clsvmmalal dsmklhgtkf frivtflpya
      121 vpavvstliw gfvygakygl vgsinswfgw hvdvlspnvl lasignivtw gyagynmlif
      181 ysslstiphs lyeaasidga sewqviksik lpelrgslai tvifsiigsf qlfnepsilq
      241 nmvpgnavtt yytpnmyayn lsfsgnqsny aaalaivmai itmavayavq lrgmkdqmk
//
LOCUS       WP_284768341             236 aa            linear   BCT 25-DEC-2024
DEFINITION  metal ABC transporter ATP-binding protein [Corynebacterium sp.
            MSK158].
ACCESSION   WP_284768341
VERSION     WP_284768341.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..236
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25375
     Region          1..232
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mlrathltag yprtpllada tfaltpatit glvgangsgk stlvrtlvgl lpplnceslt
       61 fdgtnlahfr hrlgympqha didwdfpata fdvalmgrta glrwwqwpsr adkraahdal
      121 artgmqehsh lpisalsggq rqrvllartl vsdpeliild epfagvdaas qraimdvlrq
      181 lradgatill vhhnlaevad fcdevlmvgq grliaagptk qvltesaiad mfclps
//
LOCUS       WP_284768706             140 aa            linear   BCT 25-DEC-2024
DEFINITION  dUTP diphosphatase [Corynebacterium sp. MSK158].
ACCESSION   WP_284768706
VERSION     WP_284768706.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10786453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..140
                     /product="dUTP diphosphatase"
                     /EC_number="3.6.1.23"
                     /GO_function="GO:0004170 - dUTP diphosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006226 - dUMP biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0046081 - dUTP catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=14801
     Region          6..138
                     /region_name="Dut"
                     /note="dUTP pyrophosphatase (dUTPase) [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0756"
                     /db_xref="CDD:440519"
ORIGIN      
        1 mlyysldrda yqprfayegd agmdlalshd ltvpvgahrm gdtgvhvaip eghvgmvfvr
       61 sstgiknhlv lsngtgiidq gfrgaikisl hntgdtkqhi pagayiaqlv tipiapndia
      121 earelppser gekgigssnk
//
LOCUS       WP_284768738             351 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium sp. MSK158].
ACCESSION   WP_284768738
VERSION     WP_284768738.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..351
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36745
     Region          40..346
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 megaevaala rqhkkltwqr igivagltli aavafvisnf vgaidispge vikgivnpag
       61 ledqtrtvlw qlrlpmavma vligmalsls gaemqtilnn plaepftlgi saaaafggat
      121 sivlkwqlia qpqfnlalva wlaaavatai iviaavirga kaetmvllgi glvfffqaml
      181 aliqyqssae alqqivfwsm gsltranwaa ngvlaavlii alpilwalgw rltalrlgda
      241 ratamgints rlrvvvlivv slvaattvaf agiigfiglv gphiarmlvg edqryflpas
      301 maagaavmca ahavslmikp glaipigivt sllgvpffia ivmtrrralw t
//
LOCUS       WP_284768744             476 aa            linear   BCT 25-DEC-2024
DEFINITION  peptide MFS transporter [Corynebacterium sp. MSK158].
ACCESSION   WP_284768744
VERSION     WP_284768744.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..476
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49739
     Region          2..466
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mtiikqrsir rlpaalpava giemwerfsf ygmqailayy lystsgglgm dqaqatalvg
       61 aygsllylct fvggwvsdrl lgaertllag avllicghfs lslvpgaagl vagllplalg
      121 sgllktaait ilgaafppaa gardgafqif ylginigall gpmltgwlaq eygyhagfla
      181 aailmccgca lygtlrrrvv aefdsrppnp tttpgraaai alaavvggvv vavtvspdkl
      241 avllllttit aalalfasml rsprvsaper rkvvayiplf fcstaywtlq pqiygvlavy
      301 sdqrvnrmvg gfeipaawtq slnplfilvl slplaagmar warsrrllma vgimvagsgm
      361 fvllpfvggg enstpfavla ltiflmslge lfigpvgmaa saahapraya trfsalyflt
      421 maigtslagt lstlydpssa daernylliv givpvalglm llvgrkdvvd evsggv
//
LOCUS       WP_284768791             399 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Corynebacterium sp. MSK158].
ACCESSION   WP_284768791
VERSION     WP_284768791.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..399
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42921
     Region          27..225
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mlegmseake rvstrqklrv idrsvlsrvn rirsrfvyii qatigaalay wvagdvvghp
       61 qpffapisav iilglsggdr mkkalemsig giigvavgdl lfqivgqgpf qiffivgagl
      121 vvgsfltksp lvtnqivfga iliatifppt egpgglhrai damigsgigl itialipnsp
      181 lvearrevsk vlkiassila dvtygirhqd pavirdarea vrgtqnsint llsaaqsgre
      241 asevspllwa srrsirsler ilmpvdnavr gvrvlsrqal gltedrdkvs deqlelldel
      301 sdvilaisel ygqgkqhghd eaieipdlvq rlrivggrag ldiidkegtl saymilgqtr
      361 sivvdmlmvc glsresavah lvptsqhpay ppevwgred
//
LOCUS       WP_284768841             700 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Corynebacterium sp. MSK158].
ACCESSION   WP_284768841
VERSION     WP_284768841.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..700
                     /product="PhoX family protein"
                     /calculated_mol_wt=76719
     Region          46..692
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 malkgrnlls slfassrssl tctykcgnac fgecenksnn pyfadqfsrr talragslsv
       61 vtvgggaala acsnpddasn easssegkgg ktseanvelt saegmkfdpv qpnekdevvi
      121 pdgyeqsvli awgdplfeda pefddknqta eaaekqfgfn ndfagliehp dddnrliyvc
      181 sheyttepqm fpnydadnpt eeqakigwag hghsivevsk vgdtgelkre fgplnrrita
      241 tteftlvgpa agsdyvktsa dktgkkvkgt lnncsggitp wntmlsgeen fdqyfahanl
      301 ddkkaqesle rfgmedgesq rkwerfdkrf dvskepnepn rfgwiveinp ldpkstpikh
      361 talgrfkhea gnihiasdgt vvcysgddsr feyiykfist kkykegdieh nltildhgtl
      421 yvakvegnsp edeidgsgvl pedgafdgkg ewiklltsdt ennkfeshvd gmsaeevavy
      481 treaadkvga tkmdrpedmq vhpdsekvyv altnnsyrga tgenakknke epmewapike
      541 nknglvmeie ddhagekftw nlflvcgdpk eantyfggfd kekvspiscp dnlafdshgn
      601 lwistdgnal esndglyavt tegdtrgelk cfltvpagae tcgpivtder vmvnvqhpge
      661 tddatfekqt shwpeggkst prpavvvvwk kdgnigvdkk
//
LOCUS       WP_284768821             356 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium sp. MSK158].
ACCESSION   WP_284768821
VERSION     WP_284768821.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..356
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38467
     Region          58..339
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
ORIGIN      
        1 mftvgavaqg apapaadqkp dvlgrptvsd kqvsdedgyf dsqrgqgvki yyrkqkvanp
       61 rgavvlahgv sehsgrydyv akrlldagyn vyrvdhrghg ksaggsvpmg hidnfqyild
      121 dfdrvvdmak genqgvktfl lghsmgalav eaygirepgk vdgiitnggg aplnlsgknv
      181 agknitpddi setqkkldpt iferlplaql tsfnahyaqn liphrteiga qspewskdiq
      241 lsnpftdgis tsqavkdeya sspliaqkts agtalqlaaf atydavnadl fsaptlimhg
      301 tkdgivppyf sqdwynsiss edveyvtweg qkhevfnepa adqaldtvvd wldrha
//
LOCUS       WP_284769006             938 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium sp. MSK158].
ACCESSION   WP_284769006
VERSION     WP_284769006.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..938
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103619
     Region          4..936
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtethldsft aalpypldef qvkgcqaved ghgvlvcapt gagktivgef avslalsrgt
       61 kcfyttpika lsnqkyhdlv eehgeeavgl ltgdvsinsd aeivvmttev lrnmiyaesa
      121 aldrlthvvm deihfladas rgavweevil nladhvsiig lsatvsnsee fgdwlstvrg
      181 dttvivsehr pvpldqwmml grkiyplfep esggqvnael errihrleag dtddgradyk
      241 sgkgfrarar hkgggrsefh gkgrgrsgaa rqqdryrplg rpevlkvlqs qdmlpaitfi
      301 fsragcdgal yqclrsrmvl tsqeeaqhik divdagvegi peedlqvldf krwrealsrg
      361 faahhagmlp afrhivedlf vrglvravfa tetlalginm partvvlekl ikfngeahvd
      421 ltpgqytqlt gragrrgidt lgnavvqwap amdprqvagl astrtyplis tfapgynmai
      481 nllgmlgfed slrlleksfa qfqadgsvve etreieraeh rvrelrnqld davvslappa
      541 kdgedpaevl mdyvrlrrel taeekqskid svnqrnqevi avlgrlqlgd viampgkkrp
      601 ilaavvtpan qtadprpwit tesgwsgrid aaginnapiq vgsikipkpv rknprrntry
      661 vqdvlhrehf drpkrmksht rarpnkrvgq lrdalrahpa hdwpatdreq laglaqklar
      721 rerdrdklqs kvnkatdtlg rtferivdll aemdyveftg vgadrtpvit eegerlakih
      781 sesdllvaqc lkrgiwdeld paelagvasl ccfenrkats gqpeaaterm adamnatwrv
      841 yteltadeqr hrlpptrepe agfalavhqw aagaplgycm aaaneagael tpgdfvrwcr
      901 qvidllqqva ktgydgeiqr narraidaiq rgvvaiga
//
LOCUS       WP_284769028             230 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: energy-coupling factor transporter transmembrane
            component T family protein [unclassified Corynebacterium].
ACCESSION   WP_284769028
VERSION     WP_284769028.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..230
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23988
     Region          1..227
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(13..14,16..17,20..21,58,62..63,66..67,91,95,102,
                     105..106,111,126,130..131,133..135,137..138,141..142,
                     145..146,165..166,168..170,172..174,176..177,179..180,184,
                     187..188,194,196)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(129,133,136..137,139..140,179,182..183,185..190,
                     193..195,199,201)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(150..157,167,170..171,174)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mqglhpatvv tiaacgwilt laldtpvasa svvllalacg taatrnasvi lttmalsapa
       61 alsmlvihap ygddpvlplv tsdglvlaat lslrfcalma cfiaamaalr iadiakwlqv
      121 sraghkvayi vgaslqtlpq gahawrcvre anqlagitvt wrntisrvii pviarlltqg
      181 tqrgqalaav gfdqegqrtl lrpvadsivs rvvrlviplv sfavviatwi
//
LOCUS       WP_284769152             396 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium sp. MSK158].
ACCESSION   WP_284769152
VERSION     WP_284769152.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..396
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=43260
     Region          140..389
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mdrtvskpsq pplhqriraa mtlqrtaalt avicvaltll gafltpteyq lsaailglil
       61 tvistsayrw plgmaatfvi twiiaailtr tplissvfla pvflavvayh grhgrtvaig
      121 filwfcglvd pvsfklslhl apaltwgmli gvggvigaif ahsadryrsa mvewnddvkr
      181 rqsdlaetlh nsvvsnltvn tmqlealsle yskhpelakk ldelsdsmrs smsevraltk
      241 vlrnnidgin dgmsfgsttk ptsfaqlise eeerlsrlnr spvvevkgee fapefpqeil
      301 epiaaittea clnavkyspp gaeivisvrp hmgwtvitit npvakptskn iemssgigms
      361 smnriaatid arldtelese kwelnlflpp sahkrr
//
LOCUS       WP_284769219             325 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Corynebacterium sp. MSK158].
ACCESSION   WP_284769219
VERSION     WP_284769219.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..325
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34451
     Region          2..319
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(40..41,45,118,122,125,143,146..148,167..168,172,187,
                     210..211,232..236,257..260,307,309)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(130,225..226,239..244,252..259,262..263)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mhaiqvteag gpevlrytev paptpnndev lvdvimagvn yidtyyregi ynaatpfipg
       61 fegtgrvvyd pkgeiaegtm vawnqafgsy aeqvcvprea lvavpddfqp evaasmllqg
      121 itahylahgv yqlgegascl itagaggvgq iltqmasslg atvytvvstd ekeelsyaag
      181 adkvfrygdg laeqvrryng dkgvdvvydg vgkatfqesl eavrprgtva lfgaasgpve
      241 pidpqllnkh gsifltrpsi gawtaqegef qmraqavvqa iidgdlnfnv tasypledaa
      301 aahrdlqerk ttgsivlrvq agdka
//
LOCUS       WP_284769271             461 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium sp. MSK158].
ACCESSION   WP_284769271
VERSION     WP_284769271.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..461
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=49318
     Region          8..401
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mtisthgals rlhkfagvii apflivaals gflyalaptf epwiyhdevt atapgnprsl
       61 deqiaaaqre hpdghvvqve psedpqettr vlfadpsapn asythavfvd pvdlhitgel
      121 qqyggsralp frtwasdghr tlwlgepgrl yaelaaswlg alsilglylw lkrkrknrkr
      181 lskpltlhar vgtwllpgfl fltvtgltws lvagtaigkv reelnwkeps vatsvtevga
      241 stetgehsgh aghkghggha ghagheggak lvgaqtalsa arsqgltgvl emtppekpgd
      301 awgvrearaa fklrsdavav tpngevidri nsadwplaaq ltswliqlhm gtlfgiysqi
      361 alaalalgll vvsgaglwmw wtkprrglpe lkitpavlag vvaysiiapl fgaslviffl
      421 gdwivrrlra pkrgrgaaag etiprprges ssrslatdrs g
//
LOCUS       WP_284769406             268 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium sp. MSK158].
ACCESSION   WP_284769406
VERSION     WP_284769406.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..268
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28607
     Region          3..262
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mlitdptdpr lndirnlnks dksgeglvia egplvvsrla esrfpmrclv gfpkkveayi
       61 seygepecpi yevsretlae vagfdmhrgl vaaadrapep evseivesak tiavlegvgd
      121 henigaifrh aagmgvdavl lgsgaadply rrsvrvsmgh vlrlpfahle ggfttwqrsl
      181 qaladasftl isltpnpqav hlaeamhgld kvamlvgaeg pgltehamka tdiraripma
      241 pgtdslnvat aaaisfyerq rslsdlnv
//
LOCUS       WP_284769422             375 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium sp. MSK158].
ACCESSION   WP_284769422
VERSION     WP_284769422.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..375
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40046
     Region          7..368
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mnhgpgltfr flaaqvlvvv isllvaaava tmvgptlfhd hmlmtgredp slelfhaeqa
       61 yrganlitlv valptalica llaslwlsrr lrtplqdltr aatgltagns rirvpagkag
      121 pevttlahaf ntmadrleht eqvrrqmlsd lahemgtpls vltvyldglq dgvvdwnnat
      181 htimadqltr ltrlmedidd vsraqerrid ldlaeeglgd llhtaaaaag eayadkgvdl
      241 qvetitdtar vlvdrqrfgq vmsnllsnal rhtpaggevr isvhrqgast alihvaddge
      301 gippdqlghi ferfyrgdaa rsrddagagi gltiskalie ahggtltats pgpgrgavfa
      361 lrlplsppds eeaar
//
LOCUS       WP_284769413             524 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Corynebacterium sp. MSK158].
ACCESSION   WP_284769413
VERSION     WP_284769413.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..524
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55340
     Region          128..515
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mttphthest ahtegdeapg aprsewrrqf iglfiglgla vlvffifpsn aietvqgsag
       61 adpeaeytls airtvaavti lmgvwwmtea iplaatallp liifplagvg tikevgapya
      121 satiflfmgg flialalqrw nlhrrlalyv vkiigtspkr lilgfmlatg flsmwvsnta
      181 tavvmlpigt svlaltaetv ggwekqkkfa talmlgiays asigslgtli gtppnaflna
      241 ymadtwdvtl gfgrwmavgv plavtfllia wallitvfkp emkdipggre lindeikalg
      301 pwtgpqimtg iifvlaaaaw vtlplvlkef enyddaivgi aagillfilp adnqrrirll
      361 dwktanempw dvlllfgggl slssvfnssg lslwigemak glsvlpvvli vsavaalvlf
      421 lteitsntat aatfipimgg vavgvgltad gdinvlllti pvalaatcaf mlpvatppna
      481 iaygsgyvki gemikgglgl niigiflitl tvyllavpif glsi
//
LOCUS       WP_284769383             192 aa            linear   BCT 25-DEC-2024
DEFINITION  LURP-one-related/scramblase family protein [Corynebacterium sp.
            MSK158].
ACCESSION   WP_284769383
VERSION     WP_284769383.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Bateman,A., Finn,R.D., Sims,P.J., Wiedmer,T., Biegert,A. and
            Soding,J.
  TITLE     Phospholipid scramblases and Tubby-like proteins belong to a new
            superfamily of membrane tethered transcription factors
  JOURNAL   Bioinformatics 25 (2), 159-162 (2009)
   PUBMED   19010806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008917
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..192
                     /product="LURP-one-related/scramblase family protein"
                     /calculated_mol_wt=21581
     Region          9..192
                     /region_name="YxjI"
                     /note="Putative phospholipid scramblase YxjI, Tubby2
                     superfamily [Lipid transport and metabolism]; COG4894"
                     /db_xref="CDD:443922"
ORIGIN      
        1 mtqnlftlde lvitqtksfl ndqfmitdid gtpvgtilqs tslkdmvfks srslevaitd
       61 aegnplqtvm tisdppnflr dtyevhlpgi eqpmavitkr fsmlktkldl tmegfpdvei
      121 hgdfwdwnls itsedrllad vsnewtgmgn ffmgkntyrl ritpglneqh haailgavms
      181 mdmlrtkqkn sd
//
LOCUS       WP_284768004             387 aa            linear   BCT 25-DEC-2024
DEFINITION  NRAMP family divalent metal transporter [Corynebacterium sp.
            MSK158].
ACCESSION   WP_284768004
VERSION     WP_284768004.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK158
  ORGANISM  Corynebacterium sp. MSK158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Corynebacterium sp. MSK158"
                     /db_xref="taxon:3050212"
     Protein         1..387
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=40331
     Region          3..379
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 magamflmat saigpgfltq tsvftvqmga sfafaimlsi lvdiaiqlnv wrvlcvtgmr
       61 antlgntvlp glgwvlavfv figgavfnig niagsglgin amlgidsrig gviaaaiaif
      121 iflskkagma ldrlvavlga vmillmlyva vvsqppvgea lkntvapgei dffvittiig
      181 gtvggyitfa gahrlidsgh tgvenvknit ytsvsgivvt gimrmllfla vlgvvatgva
      241 lsddntaada fynaagefgl rafgvvlfaa glssvigaay tsvsfvtsqd astrtrnilt
      301 iifiavctvv fvainsapqk llifagaing lilpigfalv mwvawfrrdl lqgykypkwl
      361 liigvlawvl tiiigfnafs gitelwa
//
LOCUS       WP_284771424             182 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: YceD family protein [unclassified Corynebacterium].
ACCESSION   WP_284771424
VERSION     WP_284771424.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..182
                     /product="YceD family protein"
                     /calculated_mol_wt=19130
     Region          1..182
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mtsplkfdvg ellnaqgada mpeqrtqtgp aperigvemi aipkgedltv aatltplgsg
       61 vlvdadisgv ltgecarclk elhpqldlhv tqvfaadesf vsgdeaesdd agsgdeipei
      121 qddeldllqa videaglnlp fapvcedgcd iqtpegvttg isgeeeeeek idprwaglek
      181 fl
//
LOCUS       WP_284771447             268 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Corynebacterium sp. MSK204].
ACCESSION   WP_284771447
VERSION     WP_284771447.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK204
  ORGANISM  Corynebacterium sp. MSK204
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Corynebacterium sp. MSK204"
                     /db_xref="taxon:3050217"
     Protein         1..268
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30647
     Region          3..237
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mptlwavadl hgairenfar iaelappdpa dwlivagdva erselivril rdlaarydtv
       61 iwapgnhelf srsqdqykgr ekydhlvaac reigvitped pypvfngiti vplftlydys
      121 frppgtsvee avqqarakkl vmtdevaiap fvdvrawcwd rlaysikrls rvqgptilin
      181 hwplvqeptm vlrfpeialw scsrhtrswp rrykaeaviy ghlhtpskmn vdgvdhievs
      241 lgyprewrnq phripwpypv tstfgevd
//
LOCUS       WP_284771593             610 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Corynebacterium sp. MSK204].
ACCESSION   WP_284771593
VERSION     WP_284771593.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK204
  ORGANISM  Corynebacterium sp. MSK204
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Corynebacterium sp. MSK204"
                     /db_xref="taxon:3050217"
     Protein         1..610
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66369
     Region          13..610
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mtlqqvhtpa eftiepgetc ltalmdtakk rphgvmftrp anyewvnvtg kefidevfev
       61 aqglialgvk qgdrialisa tryewslldy aiwaagaasv pvypsssasq vrwiiedsga
      121 vlaitetreh selvenlvlq ddgepnlkgs psqlrrvlei nssaidtlkf egrsvgtdev
      181 sariaatntd dlaslvytsg ttgrpkgcil thrnwlsear alttnpigvf avpgshtltf
      241 lplahvfsra vsiavairga sqnhwsdfst isiefarsrp nvilgvprvf ekvrnsaask
      301 aadsgiksfl feqsekiaie yskaldtpeg pdrllkikhk lfdklvysti rqgvggnvry
      361 citggsamgh dllhwfrgig vpvfegyglt etaaaaavdy vdqsigtvgp plggvtlrin
      421 ddgevcikgg mvfegywnnp eateeafedg wyntgdlgei dddgkltitg rkkdlivtag
      481 gknvspgpme dilrghplis qamvvgdgkp fvgalitldp dilkrwkldh nipenrsmdd
      541 iatdatlrae vqdavnkvns tvshaegikk fyilesdlte deneltptmk vkrnvvaqry
      601 asaiehiykr
//
LOCUS       WP_284771704             506 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Corynebacterium sp. MSK204].
ACCESSION   WP_284771704
VERSION     WP_284771704.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK204
  ORGANISM  Corynebacterium sp. MSK204
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Corynebacterium sp. MSK204"
                     /db_xref="taxon:3050217"
     Protein         1..506
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=57428
     Region          225..437
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mssrsphmkd eaaeddsgee gehlaspsrv lwqesfdeid tpawfthrap dgwktnvagv
       61 dsgearwkgw tfgdmrhwtw asgtdmrhyf tqahdkfaii dnkqqrlaes dsmnaeltsp
      121 eiavagqdrv nvefdhhyrq gkdrqnatvq vsfdggkpqe ialfdkdvfs khesigvdvp
      181 agtkkmqvsf kynhgnddww wavdnvgvvk plgqeigspq avvdvlsdiq gdpedykdav
      241 rqlngmedka galvlngdlv ddgsqeqwdt flaaheeeph dsgkelwtig nhemygkegs
      301 kaymdrflkh sgqdkpwkee ivdgvpmisi ntefysdllr hgkepfqris neqlnwlder
      361 laywdakgip alvfshpllp qtvsmshsaw yqndfedlea lsnvvnkynn ivwfsshshs
      421 slrqnnwwgt rrydgtgepg rtgfpvvntg ailneympdg dndekivkek eeastglrvk
      481 vfadrvrvea wdfkagelik yqdfar
//
LOCUS       WP_284771874             373 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium sp. MSK204].
ACCESSION   WP_284771874
VERSION     WP_284771874.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK204
  ORGANISM  Corynebacterium sp. MSK204
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Corynebacterium sp. MSK204"
                     /db_xref="taxon:3050217"
     Protein         1..373
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39961
     Region          26..372
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mttqafspev ysrrlaaaqe aaaqqgidll ligtgpdfay ltgswvsshe rltvlavpqs
       61 gtpwivspnt ditdiksapv gkldvelrgw ndgdnpyela lkgaapikkv algqsltadh
      121 ilqfqalvpe adyvlatyal aelftrkdea eiaelrkagq aidavhaqvp ellqpgrtea
      181 evahelekli leehsiidfv ivgsgpngan phhsfsdrkl sagepvvvdl ggtlpsgyhs
      241 dctrtyvvgg dlsqapqdfq dayavlydaq aaaraaakpg staeeidava rkaiadagwg
      301 dkfvhrtghg iglstheepf imegndlale egmafsiepg iylegqwgmr ledivvltkd
      361 gyeslnvver evr
//
LOCUS       WP_284771905             245 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium sp.
            MSK204].
ACCESSION   WP_284771905
VERSION     WP_284771905.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK204
  ORGANISM  Corynebacterium sp. MSK204
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Corynebacterium sp. MSK204"
                     /db_xref="taxon:3050217"
     Protein         1..245
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26492
     Region          16..235
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mgnsqrtaaa hvavkesrst dgdtrrqvll lllkdgpvta sylgerlgls tagirrhldi
       61 lveeeltevv errpvsrsrm hsgagrgrpa khfrltdrgr aqfghaydel asealtalrs
      121 aggseavknf akarferiia dvrpfvdaee sveevarkla etldkhgyaa tvdragqgvq
      181 icqhhcpvah vaaehpelce aeqevfsall gkhvqplasi adghgicttn ipltpvktnt
      241 erses
//
LOCUS       WP_284772012             157 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Corynebacterium sp. MSK204].
ACCESSION   WP_284772012
VERSION     WP_284772012.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK204
  ORGANISM  Corynebacterium sp. MSK204
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Corynebacterium sp. MSK204"
                     /db_xref="taxon:3050217"
     Protein         1..157
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17443
     Region          66..156
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 meiratqesd rtyiarlnfl tdtfgderge lssdftddfs fyvenwepnq ggfiawedlv
       61 paggvwlnwg tednhgygfv epaipefaia verrfagqgi atalidaais laqtlkapgi
      121 slavhpdnpr aqglyerlgf ehvgvyaehy imvkrfl
//
LOCUS       WP_284772089             351 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease [unclassified
            Corynebacterium].
ACCESSION   WP_284772089
VERSION     WP_284772089.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..351
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=36727
     Region          7..348
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mrttdlnatr aattsvrtia aryrrretiv lfvgvaavll aavvaltypg agldrvsawq
       61 alihpdsgfg ttviyewrlp rvtaaivvga glaiagtlfq tvtrnplgsp diigfntgay
      121 tgvivvsylg fssfinvalg avvgggital iivvlalrrq vsgmrlilvg igvsltlsav
      181 nrylilsadl dtamaaatwa agslngiewi fvgpaaivla liivltftlr srcealelad
      241 dtayslglnv trtrlvlvfl salltalcta lagpisfval aaphltrflt ggqrvslpag
      301 aligatlllv cdiigqqlfh ptmlpvgvvt vtlggtylii lmlfahrtyr r
//
LOCUS       WP_284772055             622 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Corynebacterium sp. MSK204].
ACCESSION   WP_284772055
VERSION     WP_284772055.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK204
  ORGANISM  Corynebacterium sp. MSK204
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 622)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 622)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 622)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 622)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Corynebacterium sp. MSK204"
                     /db_xref="taxon:3050217"
     Protein         1..622
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=67005
     Region          1..609
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mrqrlriilt cvvvatvalg grlawvqlvw gpdlaakavt qrervyidpa rrgeildrdg
       61 qrlaytmksr sltvsptrlr delkeqakme atsegkledm ddskkdeylt nqmedklkem
      121 aegipkmied sgasaskvda gdiknklkad tqyevlvrnv dpdvaveisn kyhgvaadrq
      181 dirqypngai aenvvgkvsm dghgqfgfea ardteltgid gqstedvsad gqvipgtlrd
      241 vvdavdgrdv tltldldlqt yvqqklekak ansqaegaea vvldaatgqv lamantdtvd
      301 pnkniedqlk egkdfenrsi shpyepgsva kivtaaaalq egittpdevh qvpgsidmag
      361 vtvndawnhg tepytttgif gkssnvgtlm iadklgpeky aeylkkfglg antgvelpne
      421 sagtvpdqeq wsggtfanlp igqgqawttl qmasvyqala nggeriepri ideikdpdge
      481 teklpepkkt qvvdketakt avdmfravfq dddagvqngt aanaqldgyq lsgktgtaqk
      541 vdpnsgaysn saywitfagi apaddprfvv avmldepksg vednggggqs aapifrdiss
      601 wllnrdnipt stpaprmtlr eq
//
LOCUS       WP_284772137             337 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Corynebacterium sp. MSK204].
ACCESSION   WP_284772137
VERSION     WP_284772137.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK204
  ORGANISM  Corynebacterium sp. MSK204
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Corynebacterium sp. MSK204"
                     /db_xref="taxon:3050217"
     Protein         1..337
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36613
     Region          103..209
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 maveslaelk siiseqllkf grvneedape ekdsprlgia spaaasslqd dvaneivdrl
       61 kaekdksspg dsaldadaar tlplgartkp rgvfeddwga rpsderpwpv ilvhgtcdtk
      121 gawqimgnil rqdgwavfap dyghratqti pessqqlgay idtvlavtga ekvilvghsq
      181 ggllarywmr mdggaekvih lmsisapnhg tthggiasrl irtqrqeavi rsiidgwfgp
      241 agmdqvvgse vlrdvnrdgd lesgvsytci atrsdavvvp petcfldpeg apegavrniy
      301 iqdfdrhavv mhedmpmdkr vhaivrtllr mvehtpr
//
LOCUS       WP_284772202             752 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium sp. MSK204].
ACCESSION   WP_284772202
VERSION     WP_284772202.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK204
  ORGANISM  Corynebacterium sp. MSK204
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Corynebacterium sp. MSK204"
                     /db_xref="taxon:3050217"
     Protein         1..752
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=82444
     Region          29..745
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mnsapknspa tnspadassy rradnagisa ieaeqnyvdg lfdrlddeva aanarlnevq
       61 aevdpatpda dalvrretey hglqakldrl nvaqmglvfg rididapgdn ptedgldrry
      121 igrmgldare enyrtllldw rapmarpfyl attaqpegvh trrqirmsgr tvtnvndeal
      181 ngpgvreeea gvasesalyf amqrartghm tsivetiqre qdeiirdntr gvmvveggpg
      241 tgktavalhr vayllythre llsstgvliv gpntnfldyi srvlpelget gvvlstiggl
      301 fpgitpthte glvgreikgs eamaeilsaa vkdyqqvpse pwditldgls ltitpsmvkr
      361 artrarrsrk phnqareafi ehfvedlaqd matkvgtdpl ggenllsrad vdqfhddlai
      421 desvvscidd fwpeldpsev laallssrel iasaargyde etqaalyrad gyawtdsdaa
      481 lldeltvlig lpnpeekkaa kdaewreqia daedaldils ssestdnddd mfeaeilsah
      541 dvidaetlaq rqevrdtrtt aqraredhtw afghiivdea qeltpmewrm lfrrcpsrwm
      601 tlvgdtsqtg spagvddwge alepfiaqrf rhhlltvnyr tpepitelan gllasinpda
      661 tpaiairdgv pvrrladadf tpgvtteddg rltavidatn aesvkglefd hvivlnprei
      721 vdaspqglqn lyvcitratq tltlvgdtgd vi
//
LOCUS       WP_284772255             370 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium sp. MSK204].
ACCESSION   WP_284772255
VERSION     WP_284772255.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK204
  ORGANISM  Corynebacterium sp. MSK204
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Corynebacterium sp. MSK204"
                     /db_xref="taxon:3050217"
     Protein         1..370
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=38236
     Region          25..368
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mrrnkaaqav qdkqstswqm pggvpfragp isflwrprvv lvciiaaali vflgalsigl
       61 gdypisvprv levifqgqgs rveklvvlew rmprvataia vgcalglsga ltqtvtrnal
      121 aspdilgitt gasamavtvi vlgsgggfag wlagigipla allgailsat viwalawrrq
      181 adsyrlvlvg iiitallssy inflmvrael rdasqaqfwl tgslarsews ttipiavlvi
      241 vcapllawia yqalattlgp dlaralgqrv navqvamlal avalaavavs aagpigfiaf
      301 vapqvalrlc gvpspplaas altgavlllg adivtqavlp velpvgivts alggifliyl
      361 lvqrtrstda
//
LOCUS       WP_284772305             103 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: histone-like nucleoid-structuring protein Lsr2
            [Corynebacterium].
ACCESSION   WP_284772305
VERSION     WP_284772305.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Gordon,B.R., Li,Y., Wang,L., Sintsova,A., van Bakel,H., Tian,S.,
            Navarre,W.W., Xia,B. and Liu,J.
  TITLE     Lsr2 is a nucleoid-associated protein that targets AT-rich
            sequences and virulence genes in Mycobacterium tuberculosis
  JOURNAL   Proc Natl Acad Sci U S A 107 (11), 5154-5159 (2010)
   PUBMED   20133735
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18741]
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Gordon,B.R., Imperial,R., Wang,L., Navarre,W.W. and Liu,J.
  TITLE     Lsr2 of Mycobacterium represents a novel class of H-NS-like
            proteins
  JOURNAL   J Bacteriol 190 (21), 7052-7059 (2008)
   PUBMED   18776007
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Oshima,T., Ishikawa,S., Kurokawa,K., Aiba,H. and Ogasawara,N.
  TITLE     Escherichia coli histone-like protein H-NS preferentially binds to
            horizontally acquired DNA in association with RNA polymerase
  JOURNAL   DNA Res 13 (4), 141-153 (2006)
   PUBMED   17046956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10570331
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..103
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11638
     Region          1..102
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 marreitqfy ddldnklige delevvrfsv nghsyimdls rdnarrfhea iapfveaaha
       61 apdaespqad prkvrewaqk qghdvarrgk ipqniidayn aah
//
LOCUS       WP_284772373             698 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Corynebacterium striatum].
ACCESSION   WP_284772373
VERSION     WP_284772373.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..698
                     /product="PhoX family protein"
                     /calculated_mol_wt=75560
     Region          46..692
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mallgknllp srftssrssl tctykcgnac lgecentsdn eyfgdqisrr talraggltv
       61 vavggsaala acspsstdsa agsstaaggg ktsdakvelt saqgmlfdav qpntkdevvi
      121 pagyeqsvli awgdpviega pkfdvnkqta adaekqfgfn ndfagliehp sddsrmvymc
      181 sheyttepmm lpnydadnpt eeqvkigwag hghtilevsk vegtgelkre fgplnrrita
      241 ttpfklvgpa kgsslvktta dpkgetvlgt lnncsggvtp wntmlsgeen fdqyfaagdi
      301 kdekakksle rfgikdketd rkwerfddrf dcskepnepn rfgwvveinp ldpkstpikh
      361 talgrfkhea gnihiaedgt vvcysgddsr feyiykfiss kkfeegnleh nlsildhgtl
      421 yvavlegnsp aeeidgsgvl pedgkfdgkg kwvklltsdt ennkftshvd gfsaeevavf
      481 treaadkvga tkmdrpedvq vhpdshkvyv altnnsyrga tgenakknke dvkewapvke
      541 nkngmvmeie ddhageeftw nlflvcgdpk vantyfggfd kskvspiscp dnlafdnhgn
      601 lwistdgnal dsndglyavt tegetrgelk cfltvpagae tcgpivdddr vmvnvqhpge
      661 addatfeaat shwpdggkst prpavvvvwk kdgkigvn
//
LOCUS       WP_284772417             447 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium
            striatum].
ACCESSION   WP_284772417
VERSION     WP_284772417.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..447
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=47749
     Region          1..444
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrmtvigtgy lgathaacma elghevlgid vdeskiealk ngrvpfyepg lpevlernie
       61 agrldfstsy ddaaefanvh flgvgtpqah gsyaadltyv ksvitelvpr lkgehiifgk
      121 stvpvgtaae lqemanelaq egshveiawn peflregyav kdtitpdriv lgvgeaglad
      181 gkshaeevar evyakplaqd tpfivtdlqt aelvkvsans flatkisfin avseiceiag
      241 advvkladai gyddrigrkf lgaglgfggg clpkdirafm aragelgadq altflrevda
      301 inmrrrdrmv dmaknafegs llghrvtvlg cafkpnsddv rdspalsvag slslagaavt
      361 vydpegmdna rkvfptlnya anceealres elvilatewq efrdldpaav aglvsskhii
      421 dgrnvldvaa wraagwtiea lgraleg
//
LOCUS       WP_284772508             847 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium striatum].
ACCESSION   WP_284772508
VERSION     WP_284772508.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 847)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..847
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=94787
     Region          19..841
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mnlsqmlpdl aevpeslvde aiwdtflswt nqrgislypa qeeaslgila gdnvilatpt
       61 gsgksmvana ahfialargq rsfytapika lvsekffalc eifgaenvgm mtgdatvngn
      121 apiiaataei vanialrdga eanidqvvmd efhyysepdr gwawqvplle lpkaqfllms
      181 atlgdtswle kdltertgre ttlvagstrp vpldfsyvft avhetieeil ksgkapvyvv
      241 hfsqreaser aqaltslsgi itpeekeaia aelssfrftt tfgrdlskll rrgigvhhag
      301 mlpkyrrlve rlaqkgllki icgtdtlgvg invpirtvlm tglakydgqr qrilksrefh
      361 qiagragrag ydtegtvive apeheienak arrrlsndpa rlkklkkksa regdvtwsek
      421 tfarlteaep eqltsqfrvs nsmllnvlar hgngyehmkh llrtnhdtrt kqnqdiltal
      481 dlfrgllnsg vvqkstkgld iygrpyhlvr elprdfalnq plgpfalaal slldpesdty
      541 tfdvisvyea ilddprqvli aqqkqrrgee iaalkaegvd ytermaivee itwpkpleel
      601 leqaydtfae tnawvkefel rpksvvrdml enamtfsdlv atyglarseg vilryltdaw
      661 rtlkqsvpde yfteelsdvv vwlgelirqv dsslvdewae magedspisq edlerelafg
      721 vedptaltsn rrafsimvrn ymfrlvqlfa lekeerlael ldyleeipdf gaalddyfde
      781 yddidsgpaa rgpeffrlsg qdtrswqvrq iikdpegdhg yqfvavvdld asdeagevrl
      841 ssliier
//
LOCUS       WP_284772582             326 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            striatum].
ACCESSION   WP_284772582
VERSION     WP_284772582.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..326
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35212
     Region          11..318
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 maernpakrd eaverltnls falqgaahgg gspdrsaawi rknvegyqnr sdeaflkqls
       61 rdvvtlqrag vpvvhssged gsmyrlnqde yqlppvdftp eeamvlgvag gigkpgglsd
      121 ftlsawtkia asgasrdlsg apvyvavndi trispeltta vitavrahlr itfdyyatps
      181 spavrrtmdp wglvnhnsrv ylvgwdvdre aarvfratri dnvkrsrqda thltvpgplq
      241 dlvvealqrg etvdalvsip qgsalelaaa gkqredglya mngvekdwlv rtaasyapgv
      301 evlepaevra aiielltaer pqegek
//
LOCUS       WP_284772731             630 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium striatum].
ACCESSION   WP_284772731
VERSION     WP_284772731.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 630)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..630
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=65062
     Region          32..629
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtsacgcehe pateiedldr pwwkdpelll pifsgialvi glaldwsgle tpatvlfwvg
       61 lllgaytfap gairnlatkr klgigllmti savgavilgf vgeaaalafl ysiaealedk
      121 amdraqgglr allklvpqta tvlrdgttae vaakdlevge lmlvrpgeri atdgiirsgr
      181 ssldtsaitg esipeevapg devpagains agvlevetta agtdnslttl vdlvekaqae
      241 kgdrariadr iarplvpgvm ilavlvgvig sllgdpetwi tralvvlvaa spcalaisvp
      301 ltvvaaigaa sqfgvviksg aaferlggir hlavdktgtl trnqpevtgv vpadgfdraq
      361 vlsfaaaveq qsthplaaai vaaepeapta ldiseeaghg iggtvegrrv lvgsprwida
      421 gplkadverm esegqtcvlv tvdnalagai gvrdelrpev pdavqslhdn dvevsmltgd
      481 ntrtaralae iagiddvrae lrpedkasiv aelssktpta migdgindap aladatvgia
      541 mgatgsdaai esadvaftgh dlrlipqalq harrgsriin qnivlslaii ivlmplaisg
      601 vlglaavvlv hevaevivil nglraarakr
//
LOCUS       WP_284773083             283 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: lysophospholipid acyltransferase family protein
            [Corynebacterium].
ACCESSION   WP_284773083
VERSION     WP_284773083.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..283
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31083
     Region          1..223
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mhnkwywtfk hilmgpflrv wnrpvlengq nipeegsail asshqavmds fyfpllcdrq
       61 lthpakkeyf tgkgikgaik rwffttvgqv pvdrqakgag etmaaaaqkv fdrgdlfciy
      121 pegtrspdgr iykghtgmar ialstgetii pvgmvdtrka npigttfprp hkvraivgag
      181 idplawarnr rmdpadheta raltdyvmht lskitgyeyv dayasevras leagkgypas
      241 tepkgdpaar rpghypknge havkdaekaa ekaaekssek gad
//
LOCUS       WP_284773294             379 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Corynebacterium frankenforstense].
ACCESSION   WP_284773294
VERSION     WP_284773294.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium frankenforstense
  ORGANISM  Corynebacterium frankenforstense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Corynebacterium frankenforstense"
                     /db_xref="taxon:1230998"
     Protein         1..379
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39632
     Region          3..373
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 mvayiagval falgiavtia lheaghlvaa rsfgmrvrry migfgpevfs rkigqtrygv
       61 calplggfce iagmtaldev tedeepyamr nqarwkrvvv llggilmnll igftilygva
      121 vtsgipnpya drtavvgevl pdgtaaaadi evgdrilavd geeipdfltl rdtvrgmpgg
      181 daeltverdg aertvtvdva daggvgavgl vgapvpeavk rfgpaeavpa tgaytgellq
      241 gtltalgklp aqipgvvasi fgaersqesp msvvgasrvg gelverslwd vfwmmlasln
      301 fflalfnlip lppfdgghva vvvweavrdr iralrglppa gpadytrllp ltytvgaall
      361 algavvivad vvnpvrlfg
//
LOCUS       WP_284773369             204 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium frankenforstense].
ACCESSION   WP_284773369
VERSION     WP_284773369.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium frankenforstense
  ORGANISM  Corynebacterium frankenforstense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Corynebacterium frankenforstense"
                     /db_xref="taxon:1230998"
     Protein         1..204
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21203
     Region          6..>186
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(164..171,177,180..181,184)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mpravplgvh vpgdtvihra dadlklivvt lfillatifg rsplgvalca vivavgylva
       61 ripwaaawsq iaaplplllv lgafqwwqnd lvtgavtvgl lgcsimgagl lpltttieel
      121 ldavehglrp lkrfgvpaen ialalsltlr liplqlatvg dvldarrarg agfsltavat
      181 pvivrslrra ralaealaar gagd
//
LOCUS       WP_284773406             341 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Corynebacterium].
ACCESSION   WP_284773406
VERSION     WP_284773406.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..341
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37907
     Region          5..>48
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          186..278
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 msttatnlkh vrillgytqk afaarlgvaq stlsgverqn ralsdklltt tqfvtgmtrd
       61 ffdedidyyg qndllfrtar lgrpdaekia tafsitehyl nhrypdlvsd vpaldvpdgp
      121 ldapvleaaa ararehfele pdtaignita vlhlhnilvt elpesvisgt nfdgvstpsa
      181 aplrvialnr qrsgdryrfs lahelahlil hastsrsdlt ameteanmfa asflmprrlm
      241 tpaitpestl adyaalksqw gysiqaivrr ahelelidyq ryrslrmqis grgwrvhepv
      301 dvllensyid pvtvtrpdrq dtdtandela svtplatprh e
//
LOCUS       WP_284773439             517 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Corynebacterium striatum].
ACCESSION   WP_284773439
VERSION     WP_284773439.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..517
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=55117
     Region          5..325
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(7..8,11..12,45,48,102..103,155)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(100,103,183..189,218,243..247,278,304..308,310)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mrvaalwfpd wpvqalrvld gaggqlssqq gtaivaqhkv vvcdaparra gvrrgmrlrq
       61 aqavspelrv eefnadrdda vfaeiaagld avassievlr pglvivdaaa agrfhggegv
      121 amhmlvdaas ragldatigv adeiatalia arhqgvgtvv pvggsrefla qqpvavlaae
      181 tslacpeelv sqlaklgvrs lgelaqlplr qvttrfgeag rrchavasaa pdrrvapela
      241 rpdlavemvf eeplervdaa afaarqlaar lhgvlkeagq vclrlrvvae fvggerleri
      301 wrtqealsen atadrvrwql dgwlssaras ngggvsklal epvevaapas aglwghaksd
      361 eqakrviarv qsqlgvdrvl qpreaggrgv aeriayvpyg eqrdpapegs wpgripsplp
      421 aslahpaari rlidasshdv yvtaeallss apvalgwgqk ryrvigwagp wpvdtlwwge
      481 keqriarlqv vgqgdkgqra wllvwaagrw sveasyc
//
LOCUS       WP_284773573             307 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family oxidoreductase [Corynebacterium frankenforstense].
ACCESSION   WP_284773573
VERSION     WP_284773573.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium frankenforstense
  ORGANISM  Corynebacterium frankenforstense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 307)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Corynebacterium frankenforstense"
                     /db_xref="taxon:1230998"
     Protein         1..307
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=31869
     Region          1..251
                     /region_name="fabG"
                     /note="3-oxoacyl-ACP reductase FabG; PRK05653"
                     /db_xref="CDD:235546"
     Site            order(12,14..15,17,36..37,89..91,140..142,155,159,
                     185..188)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187535"
     Site            order(113,142,155,159)
                     /site_type="active"
                     /db_xref="CDD:187535"
ORIGIN      
        1 mslsgssviv tgagaglgra yalelarqga kvvvndvsed aagavvdeis saggeavaav
       61 vpvgdsaaad qlvqtavdsf grldalvtna gilrdksllk mtdedfdavi hvhlrgtftc
      121 vraaykyfke ngvaghivci gsptgqrgnf gqtnyaaaka givgmvrtwa lemkkagvtv
      181 navipvaata mtktvpyfra aveadergep mpdffrkdlg fgpaddvagv vaflassead
      241 gitgqvlgag gdrlqvwshp qpvaeeyhdg gwdfsttsdr gnaivkenlq dvgekfpelp
      301 delkpkd
//
LOCUS       WP_284773603             592 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: AMP-dependent synthetase/ligase [Corynebacterium].
ACCESSION   WP_284773603
VERSION     WP_284773603.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..592
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65185
     Region          4..592
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mtafidqvrd rpygisflrp hnyewvnvts eefleeifev akgliangve pgdrvillaa
       61 tryewslmdf aisaagavlv piypsssaaq iqwivedsga vfavtetgeh tdmmrnlvld
      121 segnprlvgs ptqlrrivei nssgvdtlkf egrglddavv werientrss dvasivytsg
      181 ttgrpkgcvq thynwlsqvr alltnpiaan avapgksvlt ylplahvlar avslacvvvg
      241 clqshwpdtr tlqvqlarfr pnlllgvprv fekvrnaaas qaaekgpvgr aifaraeqaa
      301 ieyskamdtp ggpnryqeaq hrlyhklvyk kiheavggrv eycitggspm gsellhfyrg
      361 iglgvfegyg ltetcaaasv dfedqkigsv grplgggsvk indigeilfk gpwvfkeywk
      421 npeateksfe dgwyntgdlg eidedgyifi tgrkkdlivt aggknvspgp ledmlrshpl
      481 isqalvvgdg kpfigvlltl ddeelgrwkm dhnipehrsv revatdpglr aeiqdainqa
      541 nltvshaegi kkfhildrdl teeqneltpt lkvkrnvvte ryadaidkiy rr
//
LOCUS       WP_284773647             289 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: lysophospholipid acyltransferase family protein
            [Corynebacterium].
ACCESSION   WP_284773647
VERSION     WP_284773647.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..289
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31551
     Region          35..237
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 msarregfen rgpflvpvgt ekvpahpesr elvynriiir iiktvlraqg lqisvtgsen
       61 vpaeggalla snhtnyydfi lgqvpahlrg krltrfmakk eifdvpvvga lmramhhvsv
      121 drsaghgsie aavehlkage lvgiypeati srsfelkefk tgavriaaaa gvpvvpmvtw
      181 ggqriwtkdl pknlgrsrip vvirvgepmd ptgdpeeata rlrqkmsell daaradyead
      241 ygpfedgapw lpvslggsap tpeqaleidr reraerkark eakakkkgn
//
LOCUS       WP_284773695             108 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium
            frankenforstense].
ACCESSION   WP_284773695
VERSION     WP_284773695.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium frankenforstense
  ORGANISM  Corynebacterium frankenforstense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Corynebacterium frankenforstense"
                     /db_xref="taxon:1230998"
     Protein         1..108
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11669
     Region          1..93
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msgreelldl adrwaglfkl lgdptrlrll avmhhrapgt atvtdlaeat gvrvatasaa
       61 lrameaagvv sgervgrevr ytldnsrihd vlhhvgfshd syshekld
//
LOCUS       WP_284773873             527 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: SLC13 family permease [Corynebacterium].
ACCESSION   WP_284773873
VERSION     WP_284773873.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12045581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..527
                     /product="SLC13 family permease"
                     /calculated_mol_wt=55798
     Region          <30..193
                     /region_name="CitMHS"
                     /note="Citrate transporter; pfam03600"
                     /db_xref="CDD:460985"
     Region          127..518
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mttpkvqess shavgedsrt pdfkdirrrv tglivgllla vviylifpdg aaerindaya
       61 edgvdytgsa mritaavavl mgawwmteai plaatalvpl vafpllqvie fgeisssyae
      121 ptiflfmggf ilalgmqrwn lhrrlaltvv navgtqpkrl vlgfmlatgf lsmwvsntat
      181 avvmlpigms vlqltaetvg gmrnqrnfat almlaiaysa sigsvgtiig tppnallvay
      241 msnnhgieig fgqwmlvgvp iavvfliiaw lvlvtafkpe mkeipggkel ireeikklgk
      301 mhqpeavtai vfagaalcwi fvpilidnfg wsvtiadaai glaaslllfi lpsgykpgvk
      361 lmdwktandl pwdvlllfgg glalskmfse sglslwigdl aqglqvlpvi llvaavaalv
      421 lilteftsnt ataatflpil agvavgiglt eggneqnvll ltipvalaat cafmlpvatp
      481 pnaiafgsgy vsidnmikgg iwlnliavvl ttitvyfiai pvfgivl
//
LOCUS       WP_284773974             198 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium frankenforstense].
ACCESSION   WP_284773974
VERSION     WP_284773974.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium frankenforstense
  ORGANISM  Corynebacterium frankenforstense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Corynebacterium frankenforstense"
                     /db_xref="taxon:1230998"
     Protein         1..198
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21258
     Region          5..196
                     /region_name="HAD_sEH-N_like"
                     /note="N-terminal lipase phosphatase domain of human
                     soluble epoxide hydrolase, Escherichia coli YihX/HAD4
                     alpha-D-glucose 1-phosphate phosphatase, and related
                     domains, may be inactive; cd02603"
                     /db_xref="CDD:319790"
     Site            order(9..13,108..109,142,166..167,170..171)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            137
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mshptllfdm ygvlmrlpgp sfrrgvlaaa ggnediwpvy aelrpaldaa qvtevnywrq
       61 valragvedl diqeaiaady gdcleadhev vdnvlalrdk gykvgilsni ptglaarvrr
      121 rhsgwldefd avtfscdigv akpdtqafav avdalgaspr dtvffddred yiagaeaagl
      181 cavlftgwds vagelglk
//
LOCUS       WP_284774002             404 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [Corynebacterium].
ACCESSION   WP_284774002
VERSION     WP_284774002.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..404
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42084
     Region          15..388
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mtrppqdtra eddeaapsgp lagvvvadfs rvlagpyatm lladlgatvv kvespggddt
       61 rewrppvrdg vstyylsvnr nkrsialnlk dpedlatahr lvgaadvfie nfkpgglakf
      121 gldpesvaer wprlvhasit gfgtagganl pgydmlvqat sglmtitgaa dgppqkagva
      181 ifdvitglha avgilaalre reasgkgqhi alnlqssals glvnaagavv aggveprrlg
      241 nihpslfpyg pfaaadrevv iacgndaqfg rlvaalgapg laaderfatm eqrnahrgdl
      301 qelleerlaa gtadewtqrl revgvpaapi msigegvafa eelglnpvvd acgvptvadp
      361 mgfsrtpvdy rlappavdeh raeilawlae resstaadtp etgr
//
LOCUS       WP_284773223             193 aa            linear   BCT 25-DEC-2024
DEFINITION  CAP domain-containing protein [Corynebacterium striatum].
ACCESSION   WP_284773223
VERSION     WP_284773223.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Gibbs,G.M., Roelants,K. and O'Bryan,M.K.
  TITLE     The CAP superfamily: cysteine-rich secretory proteins, antigen 5,
            and pathogenesis-related 1 proteins--roles in reproduction, cancer,
            and immune defense
  JOURNAL   Endocr Rev 29 (7), 865-897 (2008)
   PUBMED   18824526
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..193
                     /product="CAP domain-containing protein"
                     /calculated_mol_wt=20465
     Region          81..188
                     /region_name="YkwD"
                     /note="Spore germination protein YkwD and related proteins
                     with CAP (CSP/antigen 5/PR1) domain [Cell cycle control,
                     cell division, chromosome partitioning, General function
                     prediction only]; COG2340"
                     /db_xref="CDD:441910"
ORIGIN      
        1 mnlssippaf tairegrmps yeeivrlaqg vitivallgt iimagiglgt ssapgggdps
       61 gssqdspenh yevpspeiql qldaiaidin ealnqwrida gsaplapwid rqsaarkkae
      121 ynaatgtesf tsenvsmvqh hlplskasgy afieawrqsp ehvavlrdph atfaavgtay
      181 angqvyvviq lek
//
LOCUS       WP_284774042             575 aa            linear   BCT 25-DEC-2024
DEFINITION  IucA/IucC family protein [Agrobacterium sp. lyk4-40-TYG-31].
ACCESSION   WP_284774042
VERSION     WP_284774042.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..575
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65524
     Region          3..566
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mplpleiqse pqdrvirqlv aamlfeglvs frieppdylt wtsdgryyrc ratlgtfgrp
       61 riqphsietk gddgnwvpas laaivvgmpg sdttrdkllr elqhtvtlcq wnednippre
      121 rrnmafahld galheghpyh pcfkarygft tadnqlygpe aakpfqlfwa lharetirqa
      181 ldhdetsfwk selgeevwsq iddaraaknl gwekftlvpm hpwqwqrlkd gagsdliasg
      241 klhglgqfgd nylasqslrs lhnsdrplaa siklpldvvn tssrrildph svctapvlsr
      301 wiagmvdeda afrdhyplti lqeyagvlae hegelsgqig tiwresalkd lqpgedvipf
      361 nalmmleadq kpfvhpwieq fglmpwlnrl leisvlpvwh llvhhglave ahgqnmllvh
      421 rngwpvrlvl rdfhesiefc ppflrdpaka pdfqsvdary rhaapnqyyw mdnldsvrel
      481 vadtlyvynl aeiahlldha yqlpeasfwq rveviietya ashdasqrma algydaptiq
      541 teslltrkll arepeyhhdv pnffakatae rrtmr
//
LOCUS       WP_284774043             244 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            frankenforstense].
ACCESSION   WP_284774043
VERSION     WP_284774043.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium frankenforstense
  ORGANISM  Corynebacterium frankenforstense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Corynebacterium frankenforstense"
                     /db_xref="taxon:1230998"
     Protein         1..244
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26467
     Region          16..244
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mrtgaparrr aprpatelfs etlplspkqr evlaalrehp agvsvaqlse ilgmhantvr
       61 ghldellahg avhtatapih grgrptilfs arlpdnraia reylslieim addltartpd
      121 peerfatahr igrrwarkmt ladeggrvga daafdqlvqr lrqlgfdpad epesrgdlte
      181 dpeegarvvs lracpfvage tapspvvcai hegfieeyfg atstaettml pltekgrctl
      241 cvrp
//
LOCUS       WP_284774204             420 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium frankenforstense].
ACCESSION   WP_284774204
VERSION     WP_284774204.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium frankenforstense
  ORGANISM  Corynebacterium frankenforstense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Corynebacterium frankenforstense"
                     /db_xref="taxon:1230998"
     Protein         1..420
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44407
     Region          <167..406
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mekilnwpll ggaaevtvwt clalgallal valatarnrr ggqgrrprra rrpatalgaa
       61 agvtvavwlv levvwrpfge ptswivyavw glvllglisl asaagrrlla aaalvalvlg
      121 algatnevfg qhptlrslhp vpaakemdwa efkattrppq edghdigalv hvdlpsgtdf
      181 tarqalayvp paywrspqhr lpvlmlmagn pgspeqwfds gaagetaday qathdgvspv
      241 vvsvdatgsl tgnpgctgas reyvtdtapd liarrfrvdq drshwtiggl syggtcalqv
      301 vtnspeafgs fldfsgqaep slgdhtrtvd elfggdeaaf haenpadllr dndytgiagr
      361 fvagrsdhea iaalkdlsqa adtagmdvey tevpgghdfg vwrtalranf dfvaerggle
//
LOCUS       WP_284774259             743 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Agrobacterium sp. lyk4-40-TYG-31].
ACCESSION   WP_284774259
VERSION     WP_284774259.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 743)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 743)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 743)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 743)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 743)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..743
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80052
     Region          164..718
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mrrgnrrldi vlalgaaali llpwyrierg ffgfgwlsdf lpsetsapaf lqiashgklw
       61 ligviiifla aflartiqdp mrrgrlmsii gavgllflsl qglaigftgw twtvsetifg
      121 qlangqpsmg agavtmavvf vllfafglae rgvmkgdafi vasisllifl vaifvfypig
      181 smftasvqdf dgsfnpdgfi rnlqdpgiws lgcvlgeerc gvawrtlala lmtasastll
      241 glgfalvatr trfpfkkglr lltvlpiitp pfviglaltl lfgragvvte glsnlfgiep
      301 grwlygltgi wiaqvlsftp isflvligvv egvspsmeea sqtlradrwr tfwrvslplm
      361 kpglanafli gfiesmadfg nplvlggshg vlsteiffav vgsqndpsra avlamvllcf
      421 tlsaflaqrf wlsgknfatv tgkgdsgahi alprglsigv havvvpwmlf tivvygmili
      481 ggfvktwgld nsltldhyir afsvgfnngs iswtgvawns fwttmkiali sapltaavgl
      541 ltayiivrqk fagknvfefa lmmsfaipgt vigvsyimaf nlppiemtgs aliliacfvf
      601 rnmpvgvrgg iaamsqldks ldeasltlra dsfrtirkvi lpllrpaita alvysfvrai
      661 tsisaviflv saeynmatsy ivglvengey gvaiayssml ivvmitvitg fqlivgerrl
      721 rrenrvagvt ttptvplaqe kaa
//
LOCUS       WP_284774264             702 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Agrobacterium sp. lyk4-40-TYG-31].
ACCESSION   WP_284774264
VERSION     WP_284774264.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..702
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76033
     Region          276..702
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 misrsflssi afrlpfaivf icclvfslsa talyglqrar nemaayglqa fsslakasli
       61 srqvsdlvss apflmnaasp yrmssesrav vaqvdgllsm igrdgedpvi rgfasgqive
      121 llnlihtqtr elardadaaq dhkakaaaal geiatgegve dvalrrqlng ivqaaatsds
      181 lfqlgelrrr yvsetdarqn rsapdvrvss erllpyervf eaqtnyllgm fairasvskl
      241 hdvsrdlsha tesqsdavaq glnddlists nalyqlliii alasmlvlvl avfsihsvmr
      301 vsrgivslsk gmnalatgdk nvgppsysgn etelirllda fkafndsver vtrlrrtaea
      361 aartirstfr nmnegialfd aagnpitmnr rvidligksa asrksplrkf ahaipeidpe
      421 llpchthsgt lqeravvrhr aenqqvieis lsrqpdrgiv llardvtamd rqeaeaskaq
      481 rldgimrmth qvshevgnmi giitgslgll ereagfnhrq krhlarirka adrgrslass
      541 mlsvgsqhpi hpssidiasl lrtmadilei avgakchvrl dleegmpkip ldpalfeqsi
      601 lnlclnsaaa mpdggvivir arrtdnlllv qvdddgagmt seavdkafep yfttrgdqgg
      661 aglglamvyg fvrqsggeaq ifsrqgegtt vqlsfplksd ae
//
LOCUS       WP_284774349             298 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Corynebacterium
            frankenforstense].
ACCESSION   WP_284774349
VERSION     WP_284774349.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium frankenforstense
  ORGANISM  Corynebacterium frankenforstense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Corynebacterium frankenforstense"
                     /db_xref="taxon:1230998"
     Protein         1..298
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31255
     Region          1..284
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(33,233,236)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(180,204,231,234..235,238)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mitvygeglv dlvpsqnnpl splvpalggg pfnvavvlar qgakvafqsr vsednygdal
       61 mrrleeegvd tsgvqrgpep ttlavttidq egsasynfyc egtadrlvep aavdcdiacf
      121 gtcslawepg asryievlhr haaagrlval dpnirpdfat dahrerllgl lddvnllkls
      181 eeeveffggi drlrvssvea ivttrggagl sldcgelhld vpahhtevsd tigagdtimg
      241 sllaaierag lnagqlgqat esqwheiltl aaaaaaitcs rtgaqpptld evaaelgr
//
LOCUS       WP_284774426             392 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Corynebacterium frankenforstense].
ACCESSION   WP_284774426
VERSION     WP_284774426.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium frankenforstense
  ORGANISM  Corynebacterium frankenforstense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Corynebacterium frankenforstense"
                     /db_xref="taxon:1230998"
     Protein         1..392
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41756
     Region          28..223
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 makerlntld rlrtvdksla srmgrvckrs waitqqavaa gtsywaaqev fghrfpffap
       61 iaaiiilgmt ggdrlrrave mslgcivgvg lgdllvpllg sgpwqiavav acalvfgsfi
      121 sksplvnnqi aigailiati mppggitpag tggpdrmida vigstvgilv iailpdnpln
      181 agrqeiskvm aiassvlddv aealrsrdar slanalqavr dtqgdinsml dsakvgreas
      241 tlsplmwgsr rrvrsleril gpvdnavrnv rvlarrsrvl tedgdtvsde qieiiselsg
      301 illsfselye rgaevseave ipnivnqlrr lgaranmslv kgrvlsahvv laqtrsiivd
      361 lleicgmsrp sslavlapts rtpayppevw de
//
LOCUS       WP_284774441             419 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284774441
VERSION     WP_284774441.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..419
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44488
     Region          1..418
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtkhvvviga givgaasaie llrdghkvti vepgppggrq aasygnsgwl spasivpmsm
       61 pglwkkvpgm vtdpsgplai rwrhilrlap wllrfvkaga tvakvertag ilsgllhdap
      121 erheklaaei grsdfivrqg liyaypdraa felealawsl rrqngvafre lsaaelhqle
      181 phldarysfg vivekgghcv dpggyvaaiv ehairlganm vtakatgfem tggkltavrt
      241 etgaiacdrt viaagihski latvagdkvp lesergyhiv ipndiakgam pvmpgdgkmg
      301 nnptraglri agqvelantt vdpdwtradi llrhakrtyt alsspfdesr idrwmghrps
      361 tpdgvpvigh snlttdiiya fghghvglat gpvtgclvan lvadrpsfvd lgpfsaarf
//
LOCUS       WP_284774569             504 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Corynebacterium
            frankenforstense].
ACCESSION   WP_284774569
VERSION     WP_284774569.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium frankenforstense
  ORGANISM  Corynebacterium frankenforstense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Corynebacterium frankenforstense"
                     /db_xref="taxon:1230998"
     Protein         1..504
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=55931
     Region          40..502
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mdqdpqagqa sqedqarqpg qadharqpgq agrtdaeplt lvwlhddlrl adnpaltwaa
       61 argavivvhv depesatgvr epgeaavwwl dqslgklerr laahrvplir argdaatllp
      121 rlarvtgaga ttwqhrhhtp laehdatvad alrtagltvt ehpghlltep advttrqgga
      181 yrvftpfshr agelidtpga lgaplpepal qgpgtdiada arrdvgnrgd varprdvsle
      241 rhnapgeqaa rarldeflrk lvegpgyeeg hdfpavdats glsahlrfge vsprevwvta
      301 aeladrepka agdahaflrq llwrdfawhr lhhhpdiawa nmrsrfddfg weyfpadgpa
      361 ehredlerwq tgrtgiplvd agmrelaetg rmhnrvrmvv gslltknlgi hwrhgeewfw
      421 erlvdadhaa npfnwqwvag cgddaapyfr ifnpvtqaer fdpdgeyvar wvpelgtday
      481 pepmldlkas rrralaayer ikdr
//
LOCUS       WP_284774662             265 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284774662
VERSION     WP_284774662.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..265
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29454
     Region          41..130
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 msgfdknwlt lreaadrdar skvlldtvnt ylgphplphi imdigcgtgs tyrtlspalp
       61 gavwklldye talldeakrq igdseniefh cqdlnqldet lfngvalvta salfdlcsee
      121 fcnrfvdhla rrkiglyaal nydgimewsl khpldkqivk dfnrhqqsdk gfgpalgpda
      181 sdrltalcea rgfivetaks pwrlgpetae lqkefllgfr qpiqeignis sadfkewldf
      241 rlsnigkkgs vcivghtdfl alpda
//
LOCUS       WP_284774618             332 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            frankenforstense].
ACCESSION   WP_284774618
VERSION     WP_284774618.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium frankenforstense
  ORGANISM  Corynebacterium frankenforstense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Corynebacterium frankenforstense"
                     /db_xref="taxon:1230998"
     Protein         1..332
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35801
     Region          65..332
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mssrapkrdv glerrlnlvf alidadnhgg ayldsgwlra hvagygdpan espreantgr
       61 krlardidel rrvgvpvevs rdgdgegyrl vreryelppi sftpdeaavl glagdlggts
      121 elgvfarsgw tklaaagldr dlsdaagtvf taandlarvp nstvgavlka vgtgtsvtfd
      181 yrrdrataaq rrrmdpwglv nhadriylag hdldrdeprt frllrvsave ltgapiahpd
      241 egrdlqqlva ealargrttv datvrlaegr cqelrrtaaq vdadgtahfa gvdrdwlvrt
      301 vagfgadavl laptdarrdv vnllrnggee hr
//
LOCUS       WP_284774666             218 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Corynebacterium frankenforstense].
ACCESSION   WP_284774666
VERSION     WP_284774666.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium frankenforstense
  ORGANISM  Corynebacterium frankenforstense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Corynebacterium frankenforstense"
                     /db_xref="taxon:1230998"
     Protein         1..218
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23841
     Region          129..202
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtvsvrsyra tdhddaikil vdafeddpsf rrvtplargl ghretlarml saqirrhyip
       61 hgridvavdg etddatplgv alwstpddgp gpvekisalk dwvslfgrha atavlrdrqe
      121 ssfeprfahw ylytlavspt aqrrgvgtal lnhgleragn davyleastp haanlyerlg
      181 fvpmgrlpkh gegvhemgmw rppvikapkp grgpaaeg
//
LOCUS       WP_284774706             324 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: quinone oxidoreductase family protein
            [Corynebacterium].
ACCESSION   WP_284774706
VERSION     WP_284774706.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..324
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34012
     Region          2..317
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(40..41,45,118,122,125,143,146..148,167..168,172,187,
                     210..211,232..236,257..260,307,309)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(130,225..226,239..244,252..259,262..263)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mkaiqvtrhg gpevmeytdv pdpvpepgqv lvgvdvagin yidtyyregl yhsappfvpg
       61 segtgrvied pagqiapgtv vawcsapgsy aekvvvdadr lvavpqdipq hvaatmllqg
      121 mtahylvngv yplaagdscl itagaggvgl latqlaahrg vrvfsvvstk ekeelayeag
      181 atevftysen laetvrrrng grgvdvvydg vgrdtfgesl eavrprgtvc lfgaasgpve
      241 pfdpqllnth gsifltrpsl gaytadadef rmraqaitqa ivdgtlnvrv ggvhplsdaa
      301 qahrdlqerr ttgslaldvt gdge
//
LOCUS       WP_284774494             253 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284774494
VERSION     WP_284774494.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..253
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27659
     Region          13..251
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mtlkitrrli pdwgttygpl gdgpfpaimi lhgsegawsg wshrnavila shgflafpfg
       61 ysnggnawna gdiinvsldr tvealtalra fhfasekvgv ygvsrgaeha lllaslmard
      121 gvdglpdaia ahsppdvicg afnarswrda gdpgwqawdp gnrawswrgs seellpttpi
      181 eierfdaplf lshgtadrvw svdmtrrlad rlhkygrkpe vhfyegqdhi pgsaaendhh
      241 ehlvaffers lat
//
LOCUS       WP_284774716             300 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Agrobacterium
            sp. lyk4-40-TYG-31].
ACCESSION   WP_284774716
VERSION     WP_284774716.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..300
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33523
     Region          8..290
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 msnpaksiri gtmvsatkgn aaeriaqiad kgfesfepff wqttsgqdva elgkrcldsi
       61 gdrditistl gmfgnpleet didlqtlqgw kdcidnahhf gatcvagftg rlrgkplpes
      121 lpryrqiwse lakraadkgv kiafencamd gnwasgdwni ahnpdawelm fnetpddnig
      181 iewepchqmv ylidplpqir kwapkifhvh gkdatirwdv ikehgifgke kfvfmrtpgf
      241 gdsnwtdiis elrlagwsgs idiegwhdpv yrdalemtgq vhglnylkac rggdfivvpv
//
LOCUS       WP_284774747             784 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284774747
VERSION     WP_284774747.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 784)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 784)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 784)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 784)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..784
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=87365
     Region          598..783
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          723..778
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mpnslprpqi vrritteasa iiflrapaga gksvvlhlca ndigiqvcsa hqprmddvkd
       61 gvliwdvpvt arsarlsaqv ldnarrivia crpeqrisgl arrimhegav tisaddltfr
      121 eeelaglpaa qrhtlleaya gwpafliisg qpdddtctny lretfltsls paqtanlsiw
      181 letpsagsag dwktllppal tsmparhthl lrllqaavqe rvsvlienga vidfasamer
      241 agrpllamdl lldngyeeha aqilerahgr eliyrgsvka fqniimrfsq pimatnetvl
      301 favarsllkq gelsrvrhlv srhlghdyld plkvltsnsr fsfaartfrl nlmisedltp
      361 ndamitrlge fmadyplgdy gkwsgyynai lefeirrrnf reaeaaaara lvylrkrggq
      421 plleffihlh qivlrlmsgd allarcaakd ardrletvph daiqefrmlr laeaclayea
      481 grprdlldfv qtdfeafaaa eiwpslmqfa lhyasqvlgd hfamtirpgf ldglwihlse
      541 glqfhammei rtaiayqnan rwtdaaatlt avrmpigrnw vdsatdeltr lgrrdeiaya
      601 mawlrdavhi atprtylrrq idalivnpkv tnrekvalql wqsyvshqrr dnasaraqll
      661 saletatrlg chgvlseerl flspllndqr isayietssd vrmalsifaa svnsphakal
      721 hgglsqrqaq mlqliaagma nkkiastlni sevtvkfhvg nlfrklgcsr raeairaaka
      781 lgwt
//
LOCUS       WP_284774752             458 aa            linear   BCT 25-DEC-2024
DEFINITION  Mur ligase family protein [Corynebacterium frankenforstense].
ACCESSION   WP_284774752
VERSION     WP_284774752.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium frankenforstense
  ORGANISM  Corynebacterium frankenforstense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13558984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Corynebacterium frankenforstense"
                     /db_xref="taxon:1230998"
     Protein         1..458
                     /product="Mur ligase family protein"
                     /calculated_mol_wt=48583
     Region          <47..>82
                     /region_name="PRK14016"
                     /note="cyanophycin synthetase; Provisional"
                     /db_xref="CDD:237586"
     Region          68..277
                     /region_name="Mur_ligase_M"
                     /note="Mur ligase middle domain; pfam08245"
                     /db_xref="CDD:462409"
     Region          316..414
                     /region_name="MurT_C"
                     /note="MurT ligase C-terminal; pfam08353"
                     /db_xref="CDD:462442"
ORIGIN      
        1 msdenqpsrr plwrrlrtra attsarlatt asrmtgrgag gmigglvaqa idptimaqlg
       61 ggrpcalvtg tngkstttrm laaatrtvhd vatndggdnm dagiisalla ggdashivle
      121 vdelhvprva erlhpevlvl lnlsrdqldr vgeintierr lrecvnahpd mlvvancddv
      181 lmtsvafdhe ktvwvaaggg wlgdsvscpr tgghivrega dwyavkplad grvfrrpepd
      241 wtvddaglha pegerglalk lpgranrgna aqavcaavrg fdvpferavr aaeqvddvag
      301 rystvqlger svhlllaknp agwqealsmv drtadglvia vngqvadged lswlwdvkfe
      361 dfenlsvkaa gergtdlavr lmyagidhdl vpdpldaira cpagrvevla nytafrdlkk
      421 alnravaghe dedaaeagaa dengaagaaa tkdeevgk
//
LOCUS       WP_284774820             338 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284774820
VERSION     WP_284774820.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..338
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34495
     Region          35..336
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtspsktass avwlwipcav vtvlllgvvh lgvgarpvsa rlvidalmar dhanfeqqil
       61 lklrlprlla amlcgaalgi sgrllqsilr nplgephilg lnagaslaiv ltialpsafi
      121 pfaltrplia algggllfsa vlalscagrt gltmtkltfc gialsalasa cvsailildq
      181 etleqmrfwl agdlsgisvs diqavipivi aaatttafiv trldimalgd tlaaglgvpv
      241 rqtrmlgmva aalfcgasvs lcgpigfvgl ivggmshrla ggrhslsvpl sallgacllv
      301 aadiaartia aprelatgil tafigapvfi lvvarrlk
//
LOCUS       WP_284774834             347 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284774834
VERSION     WP_284774834.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..347
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35500
     Region          40..343
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtfryarqpa rsavikrsng vrslwlmill gvlallcils vaigtrdvaw vdivaalggr
       61 aenigqaava vriprtvlal aagaalglag avmqgvtrnp ladpgilgvn mgaslavvig
      121 vawfniasan afiwaailga scsavfvyti gslgrggatp lklalagaat svafsslvia
      181 vvlprndiag girswqiggv ggatfdrish vlpflavgfv isllsarkln slalgdelaa
      241 glgervaiar afsalgaill cgattavcgp igflglvvph icrllvgvdh rwllpfsalc
      301 gaslllaadi igrivsrpae ldvgivtali gapffiwivr rqrvrdl
//
LOCUS       WP_284774837             346 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284774837
VERSION     WP_284774837.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..346
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35464
     Region          1..343
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mtihstitts ltrnrtqqar krmrviaalv vliivifslt lvlgqsftpp mdvirvllgq
       61 dvpgagftvg qlrlpravlc vlaglsfgls gvafqimlrn plaspdiigi ssgasaaavf
      121 aivvlslkgp ivsvfavaag lgvalsvyal ssrngvagtr lilvgigvsa mlesviayil
      181 stapawslqe amrwltgsvn gaqlsqvlpl liglavfgtl llsrqrdlea lrmgddtaaa
      241 lgvrvgetri lviiaavgmi aiataitgpi afvaflsgpi aarivgangs lllpaaliga
      301 llvlagdyag qfllpsrypv gvitgalgap ylifliirvn rtggsl
//
LOCUS       WP_284774952             274 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Agrobacterium
            sp. lyk4-40-TYG-31].
ACCESSION   WP_284774952
VERSION     WP_284774952.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..274
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29766
     Region          6..253
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 msldglsinf atikqggsfa tlvdaclahg ittispwrdq vhgvglseaa riveqngirl
       61 sghcrggffp asdeqgrrna iednkravde aaamradclv lvvgglpags kdiagarqmv
      121 edgmaellpy arqmgvplai eplhpfyaad racfntlkqs ldlcdrlgag tgvaidvyhv
      181 wwdpdleeqv aragrngqil ahhicdwlvp tkdplndrgm mgdgvidlkg frrmiekagf
      241 fgpqeveifs hdwngrpide vlstvveryk mlna
//
LOCUS       WP_284774977             289 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: TrmH family RNA methyltransferase [Corynebacterium].
ACCESSION   WP_284774977
VERSION     WP_284774977.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 289)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..289
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30821
     Region          9..279
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mtgptpvrid dpadprlddv rdlnhsdsrp dlpggkglvi aegplvcerl lesrfparcl
       61 vgfpdrlagf ltdhpdlped lpvyevtret lrevagfdmh rgllaaadra pepgleetla
      121 gartvvvleg vgdhenigai frnaagmgvd avifgngcad plyrrsvrvs mghvlrtsfv
      181 hlggthttwq rrleelraag frlvsltpdp gavvlpeala daagdayerv allvgaegpg
      241 ltehamratd vraripmapg tdslnvatsa avafyerdrs lgfpgvrrs
//
LOCUS       WP_284775149             401 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284775149
VERSION     WP_284775149.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..401
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41672
     Region          13..394
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mvehhacglt gammidclii gggllgsata fnlateglsv llvekgqing vassqnagsl
       61 hfqleyrmie ngadaarkaa eamplhldam arwgsveael gapvgvkrtg glmvaetaeq
      121 vavleqkaal erasgldvel ldrsaldgla pylgpavmaa ahckgegkad pkqttlafar
      181 aaikagaqie tgcevlelsr hgnvwharlq dgrlihaktv aitaggwsgr vaamagmqmp
      241 vspvgltmtv tmrtqpliph lvqhagrrls lkqtpegqvl igggwpaqlr hvggvidlda
      301 rpalqltsla gnmaaaasvv pkleqlqvmr vwtgmtslia dqlpllgeip kapglfiatg
      361 gsaftlglty arlladaicg kppildvrrf spgrfgsltl v
//
LOCUS       WP_284775184             251 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284775184
VERSION     WP_284775184.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..251
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25587
     Region          2..234
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 msdfrkaclg qkrligtfaa iphpvaievv aaagpdfici daehsqigre lienlirasd
       61 vhhvpalvrv pghapesiag vldagaagvl vprvstaaha kaavaatryp pvgergvgpg
      121 raagygyrip dylksanesl vlaiqietae glanveeiva vegidvifig pgdlsvsina
      181 lgpegaakle aailtitqaa ikagktvgif rpsaddvtkw sqagisfyll asdtmflgas
      241 vaagvtaard a
//
LOCUS       WP_284775229             337 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium frankenforstense].
ACCESSION   WP_284775229
VERSION     WP_284775229.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium frankenforstense
  ORGANISM  Corynebacterium frankenforstense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 337)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18950610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Corynebacterium frankenforstense"
                     /db_xref="taxon:1230998"
     Protein         1..337
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=37105
     Region          36..168
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
     Region          181..324
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 malheedkds aaellvdgry qriprdpakh fkratlaaga vlyrrradaa edatgadawe
       61 tavvhrphyd dwslpkgkvd pgeampttah reileetgle prleklvgtv typvgdrtkv
      121 vyywtasvvs geftannevd elrwlpfdea aellsyavdr rvlekalkri aagvdtrvly
      181 vrharahqrr nwagddfkrp ldkkgrrqse mlipallpfh ptavysaepd rcrqtaapla
      241 delgvdvivd rafgdegwle nmtgaqkaft dvvarggvpv ivgqgliipd miawlsangt
      301 lpldsdaesk kascwvlsfa dgrlvgadyl asplpak
//
LOCUS       WP_284775276             471 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [Corynebacterium].
ACCESSION   WP_284775276
VERSION     WP_284775276.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..471
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=51081
     Region          4..381
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtwqillafv agaalagllp pllaflrrhl rryrsaatle enqvttvsqv lhlaiqgspt
       61 givvldrgge vvlsngwahe mslvhersvl pevwelalra yedkethtld lnlperrtgs
      121 rvtsvrvvvk pltlvddrft ivygtdesen vrmenarrdf vanvshelkt pvggmallae
      181 altesaedpe qvqyfgkrlh tealrmsdli telislsklq gaealpemep vsvdavidea
      241 iarnqlaaen hkmtltrgkr sgvyvngdks llvtavsnlv snaihysses mpvsltqkiv
      301 dsdviqirvt drgigidaed qkrvferffr vdkarsrstg gtglglaivk hvvanhggni
      361 rlwskpgtgs tftvelpiyr pedsadpadp dhpaaedvvg gpdrpgrqar qaaagrvgka
      421 ghpgkagstg gadrdgrggr dgrddhgeqq adgplrkavs rvtarrkdkt q
//
LOCUS       WP_284775345             760 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Corynebacterium frankenforstense].
ACCESSION   WP_284775345
VERSION     WP_284775345.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium frankenforstense
  ORGANISM  Corynebacterium frankenforstense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 760)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 760)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 760)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 760)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 760)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..760
                     /organism="Corynebacterium frankenforstense"
                     /db_xref="taxon:1230998"
     Protein         1..760
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=84232
     Region          28..760
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mtqengrgrs igvrgmsarl arsltgnrpk inpvlaplls ihrqfhpkad gavldrayat
       61 aerlhdgvyr ksgdpyithp lavatiaaei gmdtttlvaa llhdtvedtd ytleqltedf
      121 geevarlvdg vtkldkvalg aaaeaetirk mivamahdpr vlvikvadrl hnmrtmrflp
      181 pekqakkarq tleviaplah rlgmanvkwe ledlsfaily pkkydeivrl vadrapqrdr
      241 aleeimaqlk valkenniea evmgrpkhyw siyqkmivrg hefdeifdlv girvlvdnvn
      301 ncyaaigvvh alyaampgrf kdyisaprfg vyqslhttvm tdsgrplevq vrthemhyna
      361 efgiaahwry ketkgshkgd qaeidqmawm rqlldwqkea adpnefldal rydltakqif
      421 vftpkgdvvn lpvdstpvdf aysvhtevgh rcigakingk lvaletklks gdrveiftsk
      481 dqhagpsadw kdfvvsprak akirqwfske rreehleagr dalaaevqrg glplhrlfts
      541 qsmkmvatel hypdvdalyt aigsgsvsaq hvahrlmaif gdedsaedel msrmplaela
      601 dkaehrpqav sgpgvlvegs pdvlaklakc cqpvpgdeif gfvtrgggvs vhrtdctnap
      661 klreeperli dvswagsdqg naftatlqve aldrggllme itrcvseqnl svlamnskag
      721 ddhiatirft favsdtkqlg alitalrnte gvfdvyrvta
//
LOCUS       WP_284775457             194 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase
            [Corynebacterium].
ACCESSION   WP_284775457
VERSION     WP_284775457.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..194
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=20984
     Region          13..146
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 matwkqitea npmhsenyaa rwrnfvaegr didgearlvd avadrgaril dagcgtgrva
       61 gylaarghhv vgtdvdpvli gyarkdfpdv rfevgdletd eipegnfdva vsagnvmgfl
      121 seegrepala niarslrpgg rflvgfglnr gwaapdfldt aaragfelqn ayeswqldpy
      181 tpmsgflvai larr
//
LOCUS       WP_284775508             435 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284775508
VERSION     WP_284775508.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..435
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=46519
     Region          1..434
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrivmigsgy vglvsgacfa dfghdvicvd kmpekiealk ngqipifepg ldaivasnak
       61 agrlsfttel ksavadadvv fiavgtpsrr gdghadlgyv yaaakeiaaa vtgftvivtk
      121 stvpvgtgde veriireenp sadiavvsnp eflregaaid dfkrpdrivv glsderarpv
      181 mtevyrplyl nqspllfttr rtselikyaa naflamkitf inemadlcek vggdiqdvsr
      241 gigldgriga kflhagpgyg gscfpkdtla laktaqdyds pvrliettia vndtrkramg
      301 rkviaavggd irgkkvavlg ltfkpntddm rdspaiavvq tlqdagakvt gydpegmana
      361 rplmegieya agpyeaaqda davvivtewn qfraldldrl ksimtspvlv dlrniyrpde
      421 vtahgftyag igrps
//
LOCUS       WP_284775560             328 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: SDR family oxidoreductase [Corynebacterium].
ACCESSION   WP_284775560
VERSION     WP_284775560.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Blankenfeldt,W., Kerr,I.D., Giraud,M.F., McMiken,H.J., Leonard,G.,
            Whitfield,C., Messner,P., Graninger,M. and Naismith,J.H.
  TITLE     Variation on a theme of SDR. dTDP-6-deoxy-L- lyxo-4-hexulose
            reductase (RmlD) shows a new Mg2+-dependent dimerization mode
  JOURNAL   Structure 10 (6), 773-786 (2002)
   PUBMED   12057193
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437758
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..328
                     /product="SDR family oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009226 - nucleotide-sugar biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0019305 - dTDP-rhamnose biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=33770
     Region          2..326
                     /region_name="RfbD"
                     /note="dTDP-4-dehydrorhamnose reductase [Cell
                     wall/membrane/envelope biogenesis]; COG1091"
                     /db_xref="CDD:440708"
ORIGIN      
        1 mrvvvtgarg qlgrslaltc ppgldgdvvw adrslldvtd taavaaspvl eaadvvlnca
       61 aftdvdgaee epgrtlaeaa natapgliar rcadvgarlv hvstdyvfgd avlddaahad
      121 vvvsrpvldd aapggvagpg aavpagarpl lpgdptspet iygrtklage raalaacpat
      181 tvvrtawvys gdtlpehrdf vstmlrlarr gvdpkvvddq fgsptyapdl aralwrlvld
      241 gdgaasgtag vrpaagrvlh gvgagwtswh llarevfaaa gfdpervspv dtagyptkak
      301 rprwsvlaad lelpewrtgv aravaarl
//
LOCUS       WP_284775629             730 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Agrobacterium sp. lyk4-40-TYG-31].
ACCESSION   WP_284775629
VERSION     WP_284775629.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 730)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 730)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 730)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..730
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=79449
     Region          49..722
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mphkhaktls igrstavagv lsalavvvvi vtvlilsalg dvakntnald eqrsqettsg
       61 alstflnqlt atlndyaawd daarfayapd glewlisnyg dmtvnselfd tavlidmddq
      121 ilmsyrqgap tdwslsdyfg dglagliqkv rsaplgqape isgflptkdg iaavgvalvr
      181 nksglldvpe akrrylifar hltaqkveql ahtyvingls lqpadarpay fvsiadpqgn
      241 vlgnltwrsq mpgdismrev spriiaaiai tmlfflalia igctalrklk sdeasarrel
      301 lrdrlsglyn rpglfwglkr lllrskedns yvkliyldld gfkeindsfg hgagdllikg
      361 vsaalqvlva eqallarlgg defaiavqgs darnqgrqlc ddllalfsep fmigdrvasi
      421 gcsigtavsk ggdidgeell rradmamyea kengrgryma yepymdtrre eknqleadlk
      481 yaiehdeikv vfqpvvntls rritgveala rwnragygpv spdifiaaae nsglidqlgl
      541 avlrkackaa mdwpqvklav nispvqfrnp lfssqvqail sehgiepsrv mlemtegyfi
      601 hhperaatai eklkqtgvsi alddfgsgfa sigylrqfgf nrmkidkslv ealdeggrsl
      661 emltatvala kslgipvtae gietedqaai lqlcgcdelq gylfskpvqp eqiftllseq
      721 dapvrqlkvs
//
LOCUS       WP_284775677             242 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium frankenforstense].
ACCESSION   WP_284775677
VERSION     WP_284775677.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium frankenforstense
  ORGANISM  Corynebacterium frankenforstense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Corynebacterium frankenforstense"
                     /db_xref="taxon:1230998"
     Protein         1..242
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25211
     Region          82..241
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mnafrrpvrs laallavgaf alagcagdeg dtsgsaeesa asltasssge edasaaades
       61 plvalardta ddpralgead apvqvllftd pscphcsnfh envlpklqsd yidtgkvrle
      121 vhdlgvlged svkmsaasra aadqgryfey idqlypatln getrgvdedk lvawaeaagv
      181 pdidafreai sgddlaanvq fdseaatnag lkvvptvivn gkeaenveel daflpqideq
      241 ld
//
LOCUS       WP_284775721             410 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Agrobacterium sp. lyk4-40-TYG-31].
ACCESSION   WP_284775721
VERSION     WP_284775721.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Tomich,M., Planet,P.J. and Figurski,D.H.
  TITLE     The tad locus: postcards from the widespread colonization island
  JOURNAL   Nat Rev Microbiol 5 (5), 363-375 (2007)
   PUBMED   17435791
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18792929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..410
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=43701
     Region          1..>60
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
     Region          <164..398
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mtkrmralls drqgnfammt altlpllmgf agagleltka lqvksdlqna adsgtlaaat
       61 kfretegkls ddqlkaevkl flgsadfake lnpaqkqeld envnsvasrf ktskgdgfri
      121 attvsyrmpl npllsfigak tltlsatsts essfnngspl smylvldrsg smsfktdtid
      181 ksksscqnft venwtskpst vkasspcyva kstslktavn ylvatlntsd isykasgspe
      241 stfirtgaia yndksfagqd idwgtqkana yvqaiplvpe ggtnadaali tafnalkstn
      301 tkegdehkkk gnlsfkryiv lmtdgemtgs snswnaavda svratcakak addidiftva
      361 fmappkgksl lqacatsadn yyapenmeei vaafgdiark asgnvsrltn
//
LOCUS       WP_284776030             288 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Corynebacterium frankenforstense].
ACCESSION   WP_284776030
VERSION     WP_284776030.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium frankenforstense
  ORGANISM  Corynebacterium frankenforstense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Corynebacterium frankenforstense"
                     /db_xref="taxon:1230998"
     Protein         1..288
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29112
     Region          14..264
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mnrspvpagt apdrsratgv llvlgscasl qfgasaatqv fpaagpwgvt vlrlafagiv
       61 ltalarprvg awsrgtwvkv vlfgvslglm ngffyasiar iplgvavtve flgplllaat
      121 tgrrardfaw iavalagill igfdsldplg ivfalvagaf waayilssar vgaavdgqgg
      181 lavaflvgal vqvpagfhga gviladptli gwmaltalfg slvpyalglg alrrlpvgvf
      241 gillslepvf aaaigwwllg qtpsaavwaa vvcvvaasvg ttrnkpga
//
LOCUS       WP_284775891             487 aa            linear   BCT 25-DEC-2024
DEFINITION  PAS domain-containing sensor histidine kinase [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284775891
VERSION     WP_284775891.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13566951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..487
                     /product="PAS domain-containing sensor histidine kinase"
                     /calculated_mol_wt=53227
     Region          41..150
                     /region_name="PAS_4"
                     /note="PAS fold; pfam08448"
                     /db_xref="CDD:312075"
     Region          <153..485
                     /region_name="COG3920"
                     /note="Two-component sensor histidine kinase, HisKA and
                     HATPase domains [Signal transduction mechanisms]"
                     /db_xref="CDD:443125"
ORIGIN      
        1 mnfvgggecg dlfrgfawen splgvpdswp velqtlvnvm lgslqpmliv wgpkqtclyn
       61 dgyavmcgnr hpaafghsfq elwfdiwdav dpiisaayag qgtsmndief imhrkgypee
      121 thfsfsytpv rdqsgivlgm fcacseitne iimrreqesm hekllqifqm spsgiatlsg
      181 pnhifefane eyysmigvgr diigrpvaea vsevvkqgfi dllddvyktg kpfaaravpv
      241 elnrgpdgek qsrmidlvyq amrsgsgeit gilvqaqdvt erlaeqkhre lishelghrl
      301 knqlamvqai asqtlrsaes ldsarktlsa rigvlsaahd tviqgglgts hvhklvnqml
      361 evhndpmasr ftvsgvnlrv gsrpslslsl ilhelatnai kygalsvpeg qvdirwhvtg
      421 eakdrfellw tetggpvvam pervgsgsrl ikaglagaad srvdiaydag glrciisadl
      481 ssfqqeh
//
LOCUS       WP_284776040            1415 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284776040
VERSION     WP_284776040.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1415
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..1415
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=140635
     Region          13..1378
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mtsiisslsv kqianlsttt maslktsdva alsatqtaal sskqiaalda gtissfktda
       61 iaaisakaiv gltvdqlqav atsqvsvlsa nqivamyssq laalttggie altstqvgsl
      121 taaqlgtlda gelnsfttne iaalnvksla glttdaisgl ttnkvavlst pqvaaltdkq
      181 lasissaqla afgtgqiaal takqivsist daivgltsnq tavlsatqla aittaqleaf
      241 ttaniaalts tqvgsltagq lgtldgseln sfttdeiaal svkslagvtt dtmaalatnk
      301 iaaltnpqia tltdkqlasi ssaqlaafgt sqiaaltakq ivsvstdaiv gltsnqtaal
      361 saaqlaaitt aqleafttan iaaltstqvg sltaaqigtl dggelnsftt deiaalsvks
      421 lagvttdtma alatdkiaal tnpqiatltd kqlasissaq laafgtgqia altakqivsv
      481 stdaivglts nqtaalsaaq laaittaqle afttaniaal tstqvgslta gqlgtldage
      541 lnsfttdeia alnvkslvgl ttdtmaalat nkiaaltapq vatlttkqis sitsgqlaal
      601 tttqitaltd kqvaalnsem lsglkseqvq alsnkqlval ttaqlaaftt gsiealtstq
      661 vgsltaaqig tldagelnsf ttdeiaalnv kslaglttda isglttnkia alsapqvatl
      721 tdkqlasiss aqlaafgtgq iaaltakqiv svstdaivgl tsnqtaalsa aqlaaittaq
      781 leafttania altstqvgsl tagqlgtlda gelnsfttde iaalnvkslv glttdtmaal
      841 atnkivalta pqvatlttnq vasitsgqla alttaqital tdkqvaalns emlsglksdq
      901 vqalsnkqlv alttaqlaaf ttgsiealts tqvgsltaaq igtldageln sfttdeiaal
      961 nvkslagltt etlaalatnk iaalsapqia tltdkqlasi ssaqlaafgt gqlaaltakq
     1021 ivsvstdaiv gltsnqtaal satqlaaitt aqleafttan iaaltstqvg sltaaqigtl
     1081 dagelnsftt deiaalnvks laglttetla alatnkival tnpqiatltd kqlasissaq
     1141 laafgtsqva altakqivsv stdaivglts nqtaalsatq laaittaqle afttaniaal
     1201 tstqvgslta aqigtldgge lnsfttdeia alnvkslagl ttdtmaalat nkivaltspq
     1261 iatltdkqla sissaqlaaf gtgqvaalta kqivslstda ivgltttqaa sisatqlaal
     1321 ttaqlqaftt aniaaltstq vavltsaqva tldagelnsf ttdeiaalnv kslaglttea
     1381 imgmedtrid amsdtqkqsl ndaqvaaiia aygni
//
LOCUS       WP_284776222             690 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Agrobacterium sp. lyk4-40-TYG-31].
ACCESSION   WP_284776222
VERSION     WP_284776222.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 690)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 690)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..690
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=74575
     Region          15..673
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 myqiltclti dhdprytlaa vvicilgsfl tmrlfararq yasiqrvnwl flagmiggtt
       61 iwtthfvaml gyqapgnvgf lpgftglsfi isvlattagf aiatyggnta laegggliig
      121 lgiacmhytg maaytvqgsl vwepvyvvas mvlggifgil atnrvvrpvn wfckysgmtf
      181 lvlaiasthf tamaafsvsy dpalaiepsl vspsvmggsa iiitfvllaf gfstyvidse
      241 nsqqavaryr hlslhdaltg ipnraafqeh lqalstrsnd ptariallaf dlnrfkeind
      301 vhghgagdav lraladrmss vlrpgefiar vggdefaavl prfyartdgl efahrllgav
      361 vrpiewneti lsvgasigia vggagtkdpd aliaqadvam yraktdvsgt icfydksmde
      421 aararnalav smrsglgkga felyfqqqnd tatgvivgfe vllrwnhper gmispaefip
      481 iaeqtgfiie mgewvlreac lhavrwknpl svavnvaplq lsdsdfvrkv qrillesgle
      541 pkrleleite sgiiadhrha lltirrlkal gvriamddyg tgysslstlq sfpfdkikid
      601 rgfveglgsn vqsqaivrst lilanslnip vlaegvetqa hleflrqegc qhvqgyyygr
      661 pgpattidai vnrvlpadet alietlplas
//
LOCUS       WP_284776223             221 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: YczE/YyaS/YitT family protein [Corynebacterium].
ACCESSION   WP_284776223
VERSION     WP_284776223.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..221
                     /product="YczE/YyaS/YitT family protein"
                     /calculated_mol_wt=24148
     Region          24..218
                     /region_name="YczE"
                     /note="Uncharacterized membrane protein YczE [Function
                     unknown]; COG2364"
                     /db_xref="CDD:441931"
ORIGIN      
        1 mknftprled rfpllvrwll fllgvavmsl vialtihadl gttpistppa alaawnltvg
       61 qwtiifnall vviqivllrr gftfmgylqv gvavvfgllc ilslrmtdfl apeaywqkwv
      121 laligslvva vgvfievlpg llyvpgegvi saivtgwnfg tvkqcfdwsl vilavvlsli
      181 lnghivgvre gtvfaafavg aivrvlqrld aerlrkkqfg y
//
LOCUS       WP_284776233             383 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Agrobacterium sp. lyk4-40-TYG-31].
ACCESSION   WP_284776233
VERSION     WP_284776233.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..383
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42314
     Region          15..383
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 malhfdaaef earrarltek maeekldail lfaqesmywl tgydtfgycf fqtlivkadg
       61 tvtlltrsad lrqarqtsni ediviwvdrl nadptldlkn llsemdllgc rigveydthg
      121 mtgrvarlld hqlasfgqii dasglvgqlr liksqaeivh akrageladd aldaalkiva
      181 pgadeanila amqgavfagg gdypanefii gsgpdallcr ykagrrklde kdqltlewag
      241 vsahyhaamm rtivigepef rqkelynaca eniraieevl rpgntfgdvf dvharimder
      301 gltrhrlnac gyslgarfsp swmeqqmfya gntqeilpnm tlfvhmiimd sdsgiamtlg
      361 qtylttegap eslsrhsldl ltv
//
LOCUS       WP_284776505             327 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284776505
VERSION     WP_284776505.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..327
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35771
     Region          <157..282
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mfdtfrnlqk tllimamvaf stsiataqsk sddemfdpar viagirtdpa sckemearht
       61 avwvnvegng yclryyaagl dlvgenavva awmpgdvmgg pksvghqqgi gvasmisqsk
      121 slserygipw iflarpgsyg sagkhydirh kpleaklvaa qidslkaryh igrwafgghs
      181 gggtlaaefl srrndiqcav lssaaaayre rlkqrgftgr lktevffdpy daldripiqa
      241 drrifvladp retnipfstq klyfdglksr ghaawmlalk kapapkyhsl vdfgeaatgm
      301 cakgmmktsv iletlqampp qseritn
//
LOCUS       WP_284776541             190 aa            linear   BCT 25-DEC-2024
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284776541
VERSION     WP_284776541.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..190
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20630
     Region          9..178
                     /region_name="YdeN"
                     /note="Predicted esterase of the alpha/beta hydrolase fold
                     [General function prediction only]; COG3545"
                     /db_xref="CDD:442766"
ORIGIN      
        1 mkaseadili vpgytnsgpe hwqsrwqekl starrveqae wtkpvkddwv aklieevnac
       61 tkpvvlvahs lgvptvmhal pqikdkiaga mfvappdvan pdirpkhlmt fgpyprdplp
      121 fptitiasqn dpfgtyehag dianawgstl idagmsghin tesghgpwpe gtmvfaqfis
      181 klkppagfsk
//
LOCUS       WP_284776705             629 aa            linear   BCT 25-DEC-2024
DEFINITION  ABCB family ABC transporter ATP-binding protein/permease
            [Agrobacterium sp. lyk4-40-TYG-31].
ACCESSION   WP_284776705
VERSION     WP_284776705.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 629)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..629
                     /product="ABCB family ABC transporter ATP-binding
                     protein/permease"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69734
     Region          10..612
                     /region_name="ATM1"
                     /note="ABC-type transport system involved in Fe-S cluster
                     assembly, permease and ATPase components
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5265"
                     /db_xref="CDD:444078"
ORIGIN      
        1 mtdpnkktia adasnplqti vnlwpymwpq grpdlkmrvv watffllvak lvlisvpyff
       61 kwatdalngk ldlaglvptf llgavvlvva ynltrliqig fnqlrdalfa svgqhavrql
      121 ayktfvhmhr lslrfhlerk tgglsrvier gtkgietivr ftilntaptf ieflltavif
      181 wltygfwyvf vtvitvwayi wftvkasnwr igirrsmnds dtdantkaid sllnfetvky
      241 fgneqmeasr fdasmaryek sataiwtslg wlnfgqgvif glgsaimmvm salavqrgeq
      301 tigdfvfina lllqlsvpln figfvyreir qgltdieemf dllevqaevv dapdakelqi
      361 gtgalcfrdv hfaydaerpi lkgisfdvpa gktvaivgps gagkstlsrl lyrfydiqgg
      421 aitidgqdir dvtqkslrsg igmvpqdtvl fndtlaynir ygrpdateae vmaaanaaqi
      481 sgfisklphg ydtmvgergl klsggekqrv aiartilkap pilildeats aldthteqei
      541 qsaldvvskn rttlviahrl stvigadeii vlkdgmiaer gthtsliasg glyasmwsrq
      601 reaiqaeerl revrekddlg vvdrgepah
//
LOCUS       WP_284776849             231 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284776849
VERSION     WP_284776849.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 231)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..231
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25624
     Region          18..>223
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msrsqrlldl lqllrthrrp vsgaelaret gislrtlyrd iatlqaqgan iegeagvgyv
       61 lrpgfllppl mfteaeieal vlgsrwvagr adgtmataar aalakiaavl peelgeelen
      121 stlligpgkv lemahvelgm lratirsqlk aqidygdeng qgtqrtvwpf alaffdqvrv
      181 vlawcelrqd frsfradrit afqplstryp rsrhsllkew rarqaitadk n
//
LOCUS       WP_284776862             242 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF899 domain-containing protein [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284776862
VERSION     WP_284776862.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..242
                     /product="DUF899 domain-containing protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=27149
     Region          1..234
                     /region_name="COG4312"
                     /note="Predicted dithiol-disulfide oxidoreductase, DUF899
                     family [General function prediction only]"
                     /db_xref="CDD:443453"
ORIGIN      
        1 mphavvskee wlearkalla qekeltrard rlnearralp wepvtkdyif dtpsgpkslg
       61 elfgtcsqli vyhfmlapdw eegcvgcsff adhvdgamah lkagdaafva asrapldkie
      121 aykarmgwkf pwvssqdsdf nydyqasfre edvasgtity nytdmpamgd lkdlhgtsvf
      181 akdedgkvfh tystyargae qtlttlmlld lvpkgrneeg tmdwvrrhdq yedapkaasc
      241 ch
//
LOCUS       WP_284777022             428 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284777022
VERSION     WP_284777022.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..428
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46540
     Region          31..394
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtwqspiapg mswyqdslse rpeyaamdgs rtvdvavigg gftglqaayn lakagvsval
       61 vegyrfgdga sgrnggqfgt gqrawpddle kdigferska lfdiaesakh yvldfareha
      121 idmeflpgql nvlhkasyer dyrksveamr trygyshvsf mekaetaqrl gsdhyhfgvr
      181 dtgtghihpl klviglakaa kaagaqifem tpaksiaqsg gktlietpsg titanrvlia
      241 tnahignlep vtaahvmpir sfigatvpld dfpdiipgke avadsrfvvr yfrktpdnrl
      301 lfggreayta dsprdiskhi rkqiaeiypa lnaiemthaw ggsvgitltr qpfvrevmpg
      361 vmsiggysgh gvmlanycgk lyadmvvakd kaldqfasld vpsfpggttl rapllflals
      421 wyalrdrf
//
LOCUS       WP_284777124              92 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284777124
VERSION     WP_284777124.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..92
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10049
     Region          31..87
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
ORIGIN      
        1 mknehitlpa dssdaedfev taealdrgqr arlirktrta lglsqlefas kfrvpvgtlr
       61 dweqaratap dfavayvrvi gqhpdmvaqa va
//
LOCUS       WP_284777181             529 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Agrobacterium sp. lyk4-40-TYG-31].
ACCESSION   WP_284777181
VERSION     WP_284777181.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 529)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 529)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 529)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..529
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56650
     Region          1..518
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mpliaifsia atggtdgwrh llvnvlprag gqtlmllamt gfaaavfgii tawlvstfqf
       61 plrralsval vlplaipsyl aayafgefld ftgpvqsalr tlfgyhsird ywfpdirslg
      121 gsvlvlssvl ypyvylsvra afglqgryat eaartlgasp lriflsvqlp marpaiiigl
      181 alvmmetlnd igaveylgvr tltfaiyetw lnrgnlagat qiasvliliv aaliiterra
      241 rsrqrfsaak stamtqrfal kplpaargwa atvfcllpif sgfaipvlvl ggyalkrlga
      301 lsnpkllkal ahslevslsa alitlicgfi fayvqrvnas plarsasrig slgygipgtv
      361 laigvllpls aldnamdgfl rlhlnystgl llsgtafaii yahsvrfmtl aegtidagfq
      421 klsphidmaa rtlgrtraqt litvllpnir paaitaallv fieslkelpa timlrpfnfn
      481 tlatlvyeda srskvqdasi paliiiaagl ipvllvsrsl dyrgeagrq
//
LOCUS       WP_284777211             774 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Cutibacterium acnes].
ACCESSION   WP_284777211
VERSION     WP_284777211.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 774)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 774)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 774)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 774)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..774
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=86209
     Region          54..774
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mtddsvygpy gsgkgtlgkp kpgqqrpqpr mrmrerivrw gtpkppaptq svtdplisvv
       61 lanhpkadta iierayrtae hyhrgqsrks gdpyithpla vtmilaelgm dertlcagll
      121 hdtvedtsyt neqltadfge eiallvdgvt kldkvqygds akaetirkmv iamsrdirvl
      181 vikladrlhn mrtlgflrpd kqnriaketl eifaplahrl gmnaikwele dlcfstlnpk
      241 lydeivhmva erapqreaql kdvitivrqd ldeagikaiv ygrpkhyysi yqkmvvrgrd
      301 fsdiydltgl rilvdtprdc yaalgvmhvr wnplpgrfkd yiampkynmy qslhttvlgp
      361 ggqpvelqir themhrraey gvaahwkyke npnavgrgiq pdgtdlswvq slnqwskees
      421 dpsefldslr feinsrevyv ftpkgdvmsl pqgatpvdfa yavhtevghr cigarvngkl
      481 vtldtklnng dvidiltsna pdagpsrdwl gfiasprars kiksyftker reesieagkd
      541 aiakqlrqag vplqslltve yltavaddlr vpginalyaa vgehnasaqs vveklialgg
      601 gpeeatadve eelavgvkap rrrrssetgv mvdgdpdmlv klarcctplp gdpimgfvtr
      661 ydgvsvhrtd csnaknlleh perivsvsws ddrqesyqvt iqvegldrag llvgtfrvfa
      721 eqgvsvisan mstskshlar lrltfeapdp thlkhltesi rrisgvydvf rvks
//
LOCUS       WP_284777226             641 aa            linear   BCT 25-DEC-2024
DEFINITION  autotransporter assembly complex protein TamA [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284777226
VERSION     WP_284777226.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..641
                     /product="autotransporter assembly complex protein TamA"
                     /GO_component="GO:0097347 - TAM protein secretion complex
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=67868
     Region          <17..>107
                     /region_name="nuc_hydro"
                     /note="Nucleoside hydrolases. Nucleoside hydrolases cleave
                     the N-glycosidic bond in nucleosides generating ribose and
                     the respective base. These enzymes vary in their substrate
                     specificity. This group contains eukaryotic, bacterial and
                     archeal proteins similar...; cl00226"
                     /db_xref="CDD:469670"
     Region          65..641
                     /region_name="TamA"
                     /note="Outer membrane translocation and assembly module
                     TamA [Cell wall/membrane/envelope biogenesis]; COG0729"
                     /db_xref="CDD:440493"
ORIGIN      
        1 mpkrrtdpkk siaywkagta mavaatialy pgfasnayaf klfginffgs dkdeqqvldp
       61 vtfsitlnap gadtkltesl tnssllasep ekpasgdlgl lirarddrer liaalyenar
      121 yggtvkvtva gqdidsippn psfnrsgpvp vvidvapgps ftlgnvrleg dvagrdleky
      181 glvtggdags laiiragnkl iddlkaegrp laeltkreav anhatntvdl tlsaaggpia
      241 plgavavkgq rtvdqdfirr ysrlnggepy speklrkasd rlrklgvfss itikeasala
      301 pngtipltie vsegkhrylg vgaqystteg iglqgywghr nlfgkaeslr iegavsrlge
      361 asnvqdmdys agiiftkpgv fnpattftas lkaktehpdt ydarsvtgyg gfsyefndyd
      421 tasaglevef tdtddafgnn qylttsiple fvrdmrddkl nptegfrasv sakpsyealn
      481 gtffssfegs ttgykglgad dqvvlagkia ggvlvgassl qdvpatrrfy aggggsvrgy
      541 syqeispynd egnatggrsy vvsslearfk vtetiglvpf vdagvvssdl apdfsdirag
      601 agiglryatp fgplrldvam plkkyeggss fgiyagigqs f
//
LOCUS       WP_284777231             461 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284777231
VERSION     WP_284777231.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..461
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51691
     Region          23..459
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mqhdlisktr havqetdfgp wlakasilii ddepgmrnfl mrtletrcaf vdeaadtvea
       61 srklderhfd vvildnimpk ktglewlaeq raigfyadai lmtayadldt aiqairagaa
      121 dfvlkpfrsn qilnaisral drsnlqqens alryqlktas ehiflrdrlv gssttiqqtr
      181 dmisrvaplp tsvlltgesg tgkevlahsi helsdradkp fvpincaaip admletelfg
      241 hvkgaftgad srreglflha qggtvfldei gempmalqsk llrviedrkv rpvgaerevp
      301 idirfifatn adlaadvekg rfradlfyri nvmqiylapl rdrerdvvel tdlfmhklsq
      361 qlgmppvain dtvramllay hwpgnvrelr nfierslilg rfpldlrgsn avtpatgtle
      421 eierrhilav lnemagnrde aakrlgisrk tidrkmsswh g
//
LOCUS       WP_284777354              90 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284777354
VERSION     WP_284777354.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 90)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 90)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..90
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=10038
     Region          7..68
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 maerrntemp prmlrtqeaa rflgislrtl ekhrtygtgp tyrkiggrvl ytvedlqswa
       61 digarkstsd egagtvfpar pltseerskl
//
LOCUS       WP_284777481             168 aa            linear   BCT 25-DEC-2024
DEFINITION  SixA phosphatase family protein [Agrobacterium sp. lyk4-40-TYG-31].
ACCESSION   WP_284777481
VERSION     WP_284777481.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..168
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18118
     Region          11..168
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mhepssrpsr iyllrhahaa wagpgqrdfd rpldaagfae aeviadraad kgylpdavis
       61 stalrcreta qavrrafnds ldvayidemy naeadiylal iaaqtasrav mlvghnptie
      121 avaealigrk qmedllpsgf ptaglavfda dptssgealw hlidffhp
//
LOCUS       WP_284777509             238 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284777509
VERSION     WP_284777509.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..238
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26821
     Region          64..236
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mqryeisqdl lirlqkadtm ddvallltei qnmfgfryyc vfetarveee episflfpsn
       61 mpvdlfykid ervaafaerl fkhlpgtlgp tpwdlsedea cgeidpdhaa fyrsvgftvg
      121 isfsalgvss lprligfagd rphpdvdeve rmsmlmfhmh mrltaigrar tekrqplsgl
      181 ekqilflaae gesfeiiaae valssitigy lmesicrkme vstfehavav tlrrglsr
//
LOCUS       WP_284777637             308 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284777637
VERSION     WP_284777637.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..308
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32883
     Region          1..265
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(34,246,249)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(186,217,244,247..248,251)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 milccgeali dmlprettkg epgfapyagg avfntaialg rlgvpsaffs giaddmmgei
       61 lkdtlrdsnv dyslcafshr pstiafvklv dghatyafyd egtalrmlse sdlpnigadc
      121 eamhfgaisl ipepcggtye allmrehekr visldpnirp gfikdkqkhl erinrmaaks
      181 divkfsdedl awfglegded tlarhwlhhg aklvvvtrga egavgytsnl rvevpserve
      241 vvdtvgagdt fdagilaslk lqglltkpqv aalteeqiak alalgakaaa vtvsraganp
      301 pwaneigl
//
LOCUS       WP_284777681             131 aa            linear   BCT 25-DEC-2024
DEFINITION  tautomerase family protein [Agrobacterium sp. lyk4-40-TYG-31].
ACCESSION   WP_284777681
VERSION     WP_284777681.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..131
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=14391
     Region          2..59
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
     Region          67..124
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mpilnvkvsv ekseemttki sallselthr ilgknpalta itiqyidprd wivggktlaa
       61 qgkssvyldi kitdetntka ekatyiaevf kgfsallgnl heesyiyved vratayghgg
      121 ltqerryhha a
//
LOCUS       WP_284777691             352 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284777691
VERSION     WP_284777691.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..352
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=38592
     Region          106..337
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mifipmpfvv alllalills iirsngegra nrpflamill savqstivgl rwgyqieelk
       61 yalpvmasvl pplayasfrs lmhswrlksa anivsiaapp ivvavllvty pvaidgilil
      121 lfvgyalaiv llgrrgpdgl eeaqfasvts vhralfiaaf alclsaafdv lvlldfewaq
      181 gqnagaiisn gnllglllig ltswvagdsr pekhrdvdpa padpapatpg dqeimgrlee
      241 mmsrqkvyrd enlnlsrlar kmvlpsrqis qainratggn vsqyinqlrv kdacrlleet
      301 nqsvtsimle sgfqtksnfn refrritgms piawrdrevw tlvsrhkkgh pa
//
LOCUS       WP_284777848             524 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Agrobacterium sp. lyk4-40-TYG-31].
ACCESSION   WP_284777848
VERSION     WP_284777848.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 524)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 524)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 524)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..524
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55664
     Region          2..523
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mlpvlallse aikgssglwe hlrntvlata lpetlilllg vgivagvigt asawlvsayd
       61 frgrkllewa lllplampty ivayayldil hplgpvqgav rwllgysspr efrlpdirsm
      121 tgciillgfv lypyvyipvr amfltqagnl ldaarmlgts rravflrvav plarpaiavg
      181 islalmealn digaseflgv rtltvsiytt wvtksdlpga sqialcmlll vvaliaverw
      241 arrrqrysts aqkstvlapa rvsglsglla fllgglpili gfvapaiylm veawkryqfs
      301 glssrfasea mntvafagta tlvtvgaglv vayamriipg kaslwsfrla tvgyaapgtv
      361 iaigvlialg sfdrfldqtl qqwfgvssgl lligsgaali fayaarflti agggidagls
      421 ripmsfdhas rtlgrtstat fsavhlplsk aamaaaallv fvdcvkelpa tlllrplnfe
      481 tfathlygea argtyeeasi aalaivvigi lpvillarig rvrg
//
LOCUS       WP_284777884             425 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Agrobacterium sp. lyk4-40-TYG-31].
ACCESSION   WP_284777884
VERSION     WP_284777884.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..425
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46413
     Region          1..406
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mpvenvdtlv vgagqagval sehlsksgvp hlvlerhria erwrserwds lvangpawhd
       61 rfpglefsda dpdafigkdk vadyfvayae kfaapircgv evkevrrnad grpgfrvets
      121 qgviearnvv aatgpfqrpi iprvvpddsg ilqihsnsyr npeqlpegav lvvgagssgv
      181 qiadelqrag krvylsvgph drpprayrgr dfcwwlgvlg kwdaetpgpg tehvtiavsg
      241 arggetvdfr rlaaqgitlm gmtqsyengt ltfakdlann iargdanyls lldeadayvq
      301 rngldlpeep aahiigpdpe cvanpilkld laeagitsii watgyavdys wlkidafdek
      361 grpkhqrgvs vepgiyflgl pwqsrrgssf iwgvwhdakh ladriatqhk ylsyhasakg
      421 etena
//
LOCUS       WP_284777891             390 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284777891
VERSION     WP_284777891.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..390
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43314
     Region          139..381
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mfkyfptnyv wnlsvnlsie mgarmgeiee mcaplqdaak apdaagtqaf rdtwirmaek
       61 lvslaeddea lrrtfsagdk llraanymlt aerllahgse grvalyqrfl avfekglkls
      121 gsscrrveip yegshlsaly vpaqgvegpa pllvqvngld stkemkflvg mpawlarrgv
      181 aslvvdqpgt gealrleglt arfdsehwas rvvdwletkd nvdasrigme gvslggyycp
      241 ravafeprfa cgviwganhd wrdvqkkrla regnfpvphy wshvmwvwga sdmddfmkia
      301 envhldgild rirvpflvth gekdsqiplk wahatydqlv nspkrelkif dertggvqhs
      361 sfdnsanaga yivdwvaeal gghngvrtae
//
LOCUS       WP_284777917             459 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Agrobacterium sp. lyk4-40-TYG-31].
ACCESSION   WP_284777917
VERSION     WP_284777917.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 459)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 459)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 459)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..459
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50496
     Region          133..456
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mknstlarkl flriapvvav aivvigvfaf nsatreidni ydaqmindan vmwgllrhrl
       61 edparqgshk igdidfnmdn qlalnedadd yadahmvraw vgdriavyss taflsdvppr
      121 pvgfsdfsyk geawriyslr ipdtaivlev gqkdtlratl vanillnlff pllvilpiia
      181 aliwlginss lstihdlvrq irtrspddls aiptgalsrd llplgrsinq llvklgnslt
      241 lerrfsdlaa hqlrtpqasv klllqmlqna ddeaergqli salvesndra shlieqllrl
      301 arvshhplrv envplyhmta svlaefgtli nsrnldvsle geedvevqtd gaavrtiivn
      361 lidnavkysv vggrvavvva reddacrlsi sdsgpgippe erfsvfqrfy rvetlqtegs
      421 glglaivadi aerlsikidm gtpdwgtglk vdlhipqnv
//
LOCUS       WP_284778073             360 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Agrobacterium sp. lyk4-40-TYG-31].
ACCESSION   WP_284778073
VERSION     WP_284778073.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..360
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=38398
     Region          1..315
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mkhfriftka lalgalfacq sigakaqetf epsqvtitvp faegggsdtl vrmiapylgk
       61 tlsgtpsiiv qnqpgggglp gtnqffrsae hdgsellams ssvfmanllr drqvrfeids
      121 fipvylsplg gviyvsektg akpgkgiegi saplvygaas ptsadvlvil aldllglevk
      181 pvfgtqrgaa riafergefn vdhqspaafn snvkplvasg qavplmsfgf adasgeivrd
      241 pafpemqtff elyretkgkd ldgpakrawi alfnasvstg kalvlpaktp esvrtayvaa
      301 fekifadpef varakteigd ypqstgdiam kqfsnaakld aeaftwlaqw yqtklgvkln
//
LOCUS       WP_284778080             250 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284778080
VERSION     WP_284778080.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..250
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27831
     Region          <85..241
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mlgvqlneyq gdlwvdgkrv efegfhkgnf svydynrqwq anmrsafdcv nfhipraalt
       61 aleedlgtkr ietlnvlpga dindptihgl vealmpafhn palasrlfmd hvglalathl
      121 atvygearsa paihpgalat wqlkratamm dagldgdlpi tdiayacgls tsyftrafka
      181 ttgmppyqwm mrrrvdkamd llkrgrlpls hvadicgfvd qshmtrvfkk mtgippgtwr
      241 rtetdpnqdh
//
LOCUS       WP_284778092             323 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Agrobacterium
            sp. lyk4-40-TYG-31].
ACCESSION   WP_284778092
VERSION     WP_284778092.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..323
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35657
     Region          1..261
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mkfatrlnsf askpsaewpe lsgkpsmlqm atraakvegl tdldlnypdh vnddpavlar
       61 qigdlglain gfamryytnp afkigaftnp daavrreaid ltkkgidaar aagsnlmtlw
      121 lgqdgfdyaf qadyhtlwqh eidgirevca hdpdclvsie ykpneprsys lmpdcattll
      181 aikdvdmsnl gvtldfahvl yadeqpafaa aliarysrvl gvhlndgyak rddglmvgav
      241 htqqtiellr qirkdgydga iyfdtfpdmt gldpvhecev niqtvkrmlk ivdrieqdnr
      301 lsgaverqda vsaqaviqel mlg
//
LOCUS       WP_284778141             505 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Agrobacterium sp. lyk4-40-TYG-31].
ACCESSION   WP_284778141
VERSION     WP_284778141.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..505
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=55634
     Region          5..341
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(8..9,12..13,48,51,107..108,160)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(105,108,185..186,187..189,218,247..252,278,304..308,
                     310)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mqrvvslylp twstdryrrt lgkqappldr pvvmigrqgs rrviaaqdva aaamglrlgm
       61 pvskaqaiip glivedlqaa ddakalrdla fwflriyapi vapdapdglv ldttgadhlh
      121 gnelmmltgm vnrlhglgft araaiadswg aahalarfgk epvtivpqng staalaalpl
      181 aalrletril adlkvlgfrq iadlmatara pltlrfgpqv grrldqahgl lsepiepirv
      241 pelvevfrff aepisaaeti aryteklvsq lclrlekrgl garrvdlvlh rvdsgvqair
      301 agtskpvrdv kqltrllsdr idtinpgfgi ekmtltatha ealvvgqvrs tllddakadi
      361 getvdviinr ghkvyryaav asdvpersvq ivaaqsaddp lgwpdhwprp vrllarpepi
      421 qtmallpdhp pksftwrgvr rlvkradgpe rvfgewwkrd reqaavrdyf tvedevgerf
      481 wifrsgdgeh vntgsqgwfl hgffg
//
LOCUS       WP_284778348             297 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Agrobacterium
            sp. lyk4-40-TYG-31].
ACCESSION   WP_284778348
VERSION     WP_284778348.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 297)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..297
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=33352
     Region          4..297
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 makrilftgg sgkagkhvvp wliakgyevh nldlvplhcp gvtnlivdvt dsgqvfnals
       61 mhrdfpdlet grgvqpydav vhfaaipril ikpdnetfrv ntmgtynvie aavklgvrki
      121 ivassettyg icfaeghrdf hqfpleedyd vdpmdsygls kvvnektara faerygadiy
      181 alrignviep heydkfpaff adpetrkrna wnyidardlg qichlciekd glgfqvfnaa
      241 ndtatanvps kelasrffpn vpftrdigeh eglysnrkir evlgfkeehd wrkyvka
//
LOCUS       WP_284778405             126 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Agrobacterium sp. lyk4-40-TYG-31].
ACCESSION   WP_284778405
VERSION     WP_284778405.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 126)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 126)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 126)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007442
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..126
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13533
     Region          21..121
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
ORIGIN      
        1 mriwisatfl llgvssafad gdvangeraf skcsachsie nprtrmgphl mgvvgrpags
       61 vadykysqam tdagaggmaw tednlrefls spkkkvpgts mrffglwses eindliaylk
      121 tvqapq
//
LOCUS       WP_284778453             304 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284778453
VERSION     WP_284778453.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..304
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32495
     Region          73..277
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mthktklasp lgavtsiala lclfssepas grsttqpegp vtgevgdlra qswrvgvpad
       61 rqgdrllldv dtyrptgsgp fplvvinhga aldaptdgpw dyrpdaairw fvsrgyavav
      121 pvrrgyglse gkrvvlgdcd apdyliggnt vaqdilavvd yfrqqpfida dqvilvghsl
      181 ggagslvaag rhpegvlgvv afapgagrvr pglicrldll ekafedfgag dsipalwiyt
      241 endgyfspei aqrlfkaygk gahafqrlei lpstdhndhd lflrddgast wglvvehfld
      301 qivh
//
LOCUS       WP_284778483             665 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Agrobacterium sp. lyk4-40-TYG-31].
ACCESSION   WP_284778483
VERSION     WP_284778483.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 665)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 665)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 665)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..665
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=74883
     Region          24..649
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mthtlvdvve ldligdetqk qssdalrkif leeadvkrrk airqglwiav piyllfsitd
       61 lllvpdvaph tmfarfvvgi aalltlemqi ranaktnhmd iacatalicg yigwvmpamm
      121 ttytvnmsyy mvfgaifmmg anlfftfnfs lslfasslvl miyfaalryi hediyyqian
      181 gtfyfscfif tsyvnlrlnr eryrvflnai eakvqqkqae ergqallhls ntdpltglen
      241 rraidtrlre lwdgwvnenr nfavflidvd ffkkyndfyg hqegdrcliq vaqtlqesms
      301 rfdavigryg geefialarf rnardieeia etlrqtvedm slvherrrdg tsvitvsvga
      361 sftrpqpdpk lerlineadr alylakangr ntvklfdpkd plnsddtenv aallniaiek
      421 dlvslvyqpi knlsscqidg aeslmrlrll dgtmvppcif ipiaertgvi mdlglwairt
      481 acqqvlrsdc vpivsvnvsp iqlkspgfat svaailgdvg vaggrlafei teglemdmns
      541 dvlhcisdlk tlgiriwldd fgtgfaglsw lrlidfdtvk idksflhdah tqrgkamlkd
      601 iiglirnrgh kilvegveta eqlallkelg idqvqgyfvg rptpvdkfrv dkpcylprtg
      661 lmrpv
//
LOCUS       WP_284778507             818 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-mannosidase [Agrobacterium sp. lyk4-40-TYG-31].
ACCESSION   WP_284778507
VERSION     WP_284778507.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 818)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 818)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 818)
  AUTHORS   Nascimento,A.S., Muniz,J.R., Aparicio,R., Golubev,A.M. and
            Polikarpov,I.
  TITLE     Insights into the structure and function of fungal
            beta-mannosidases from glycoside hydrolase family 2 based on
            multiple crystal structures of the Trichoderma harzianum enzyme
  JOURNAL   FEBS J 281 (18), 4165-4178 (2014)
   PUBMED   24975648
REFERENCE   4  (residues 1 to 818)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 818)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14312040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..818
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..818
                     /product="beta-mannosidase"
                     /EC_number="3.2.1.25"
                     /GO_function="GO:0004567 - beta-mannosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005537 - D-mannose binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=92118
     Region          15..>641
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          749..813
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; pfam17753"
                     /db_xref="CDD:465483"
ORIGIN      
        1 mtssyasdvv idlsgewtla mddgehstti tipgdvhtal rkaeiipdpy fgrnendvqw
       61 vahrdwvier rfyvdhadad wyldidyldt vavvfvndtp vlsadncfrr yrpdvsnalv
      121 qgenvirihf hssikagaer qaaqpfyvpy hpgnspiphg nmlrkpqchf gwdwnialap
      181 lglygtialr rldtariehl tttqhhvdgg velhveltlh akaaaslpih lslgderlrl
      241 dcgvgagetv vrhvffvenp klwwpagsge qslytltvel pdetvtrqig frtvelltdk
      301 deagsrfafr ingreifcrg anwipadalh slssrekted llcsaveanm nmirvwgggf
      361 yeqdwfydlc drmglmvwqd fmfacnlypc tddfldnveq evtyqvkrlf shpsialwcg
      421 dnelvgaltw fdqsrdnrdr ylvaydrlnr tiekalkkaa psslwwpssp asgymdygda
      481 whsdgsgdmh ywsvwhenks fdnyravkpr fcsefgfqsy tsmpvigtya dekdmnissp
      541 vielhqknag gneriagtmf ryfrfpkdfp nfvyisqvqq alaiktavey wrslkphcmg
      601 tlywqlndtw pvaswssldy ggswkalhya arrffqpvtv saipsengkt vrfstvndta
      661 etvdidmnif alstdgmrtp lksasgscgp daavvmaevd lgqlpvgall swnfiasngm
      721 tgeghhvldt ykaldlqpsg ldhsvgaldd gqfeievtts glalfvmiea dmegrysdnl
      781 fdlaagetrr ivfspkdtat msrpnfrifd lfssqsqg
//
LOCUS       WP_284778522              75 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284778522
VERSION     WP_284778522.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 75)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 75)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 75)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..75
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=8433
     Region          12..65
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 msdkhtnlva ldsyltlkev mtnikvasst lyrwvdagnf prpvrlgenc vrwrvadvka
       61 wqesrqsgep ikkta
//
LOCUS       WP_284778548             170 aa            linear   BCT 25-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Agrobacterium sp.
            lyk4-40-TYG-31].
ACCESSION   WP_284778548
VERSION     WP_284778548.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. lyk4-40-TYG-31
  ORGANISM  Agrobacterium sp. lyk4-40-TYG-31
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Schwartz,C.J., Giel,J.L., Patschkowski,T., Luther,C., Ruzicka,F.J.,
            Beinert,H. and Kiley,P.J.
  TITLE     IscR, an Fe-S cluster-containing transcription factor, represses
            expression of Escherichia coli genes encoding Fe-S cluster assembly
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 98 (26), 14895-14900 (2001)
   PUBMED   11742080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Agrobacterium sp. lyk4-40-TYG-31"
                     /db_xref="taxon:3040276"
     Protein         1..170
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=17749
     Region          2..140
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mklsdgveqa ihctaflagl sedgvlsaaa laelhgvsts yllkhlqals gagivattpg
       61 pkggyrlakt pkeislldiv lavegpapaf rcaeirqrgp nplpkryftk pcqinaamlk
      121 aerayraela kvsvaellad lgadddggia argcaflerh erktgnrass
//
LOCUS       WP_284778588             216 aa            linear   BCT 25-DEC-2024
DEFINITION  IMPACT family protein [Cutibacterium acnes].
ACCESSION   WP_284778588
VERSION     WP_284778588.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Park,F., Gajiwala,K., Eroshkina,G., Furlong,E., He,D.,
            Batiyenko,Y., Romero,R., Christopher,J., Badger,J., Hendle,J.,
            Lin,J., Peat,T. and Buchanan,S.
  TITLE     Crystal structure of YIGZ, a conserved hypothetical protein from
            Escherichia coli k12 with a novel fold
  JOURNAL   Proteins 55 (3), 775-777 (2004)
   PUBMED   15103642
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Okamura,K., Hagiwara-Takeuchi,Y., Li,T., Vu,T.H., Hirai,M.,
            Hattori,M., Sakaki,Y., Hoffman,A.R. and Ito,T.
  TITLE     Comparative genome analysis of the mouse imprinted gene impact and
            its nonimprinted human homolog IMPACT: toward the structural basis
            for species-specific imprinting
  JOURNAL   Genome Res 10 (12), 1878-1889 (2000)
   PUBMED   11116084
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..216
                     /product="IMPACT family protein"
                     /calculated_mol_wt=23019
     Region          1..205
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 mieysvlagp veteleikrs vfltrlvrvt cedearevia qarhdghnar hhvsafvlga
       61 drgvqrcndd gepagtagmp tlaaltaadp rgnpdlsdvv avtsrwfggi klgtgdltra
      121 ygnavsnalt vaafhrrvmm dtftttiglr ragheegvir aaghdvtnve ytakgsivtl
      181 acradrgsqm aidlakllgr evrltpagqc wvdiea
//
LOCUS       WP_284778659            1027 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-mannosidase [Cutibacterium acnes].
ACCESSION   WP_284778659
VERSION     WP_284778659.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..1027
                     /product="alpha-mannosidase"
                     /calculated_mol_wt=113630
     Region          261..1023
                     /region_name="MngB"
                     /note="Alpha-mannosidase [Carbohydrate transport and
                     metabolism]; COG0383"
                     /db_xref="CDD:440152"
ORIGIN      
        1 mhdhapildd rvhrhlaeki rpaetttvch lnvewapvtd tveglnsrpg vvgqgepisi
       61 saglalayep frigdtwgpp wgttwfhlta tvppehrddh lemivdlggv wdspgfqseg
      121 lvvrpdgsii kalnprntwi pvetdteghi dvyveaasnp illaqppfqp tedgdkltas
      181 tdtyyslkra dlvvvndevr eliadivtls glaaqlpeds errwdvrral dramdrldlf
      241 dvvssasaar selapaltrp ahdsaqtmta ighahidsaw lwplretrrk vartisnqln
      301 lidtdpahif afpaaqhsaw leedhpdlfa rlqkavkdgr iipvggmwve sdanlpgges
      361 mcrqllygqr yfmakfghhc pevwlpdsfg ysgalpqlak lagahwfltq kiswnqvdkf
      421 phhsfwwegi dgtrifthfp padtygsdls ahdleharan fqdkgrsnss lvpfgygdgg
      481 ggptremlaq arrvadldgs pklaieppat ffsraesehe dpgtwvgely lelhrgtfts
      541 qyevkkgnrr nehllrdael wcataavrel mdypgerlae iwrticlyqf hdilpgsaia
      601 wvyrevvadh rrisdeltel ihhaqellag egdeeivfds apmarpwast vamggskaps
      661 itegvhaeen eedfivdngl lrmtvdahgl ithlvdtasg rdaipagqrg nllqihpdfp
      721 nmwdawdidp fyantvtdld dgqatmsrkd gsvtisvtrt fghssatqsl tvnpgdprvk
      781 vhthvdwheq dsllklawpv dvhtdhadye iemghitrpt htntswdafr fevnahrwvy
      841 vsepgfgvai ansdtygwnv srhpkdnggt wsvarasllk garfpdprad egehdffhtl
      901 hvgadladai rdgyaanlcv rrrqgspvep lvsvegvave avklaedgsg dvivrlyepy
      961 grhvhttmtl gfeatsavev glledpldgn phaqvapsvv tadladgtig lsmrpfqvat
     1021 lrlgrnr
//
LOCUS       WP_284778760             596 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator, partial [Aerococcus
            urinae].
ACCESSION   WP_284778760
VERSION     WP_284778760.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         <1..596
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
     Region          5..>402
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 trqglaedyg vspatiqtdl kavgeallny dlhlvrddrk sylvrgweae rrqmlsslls
       61 qnvdeytffh pnrqggqnsq afmallered lelvqqifnr lnpttfakvt dnqlklimlq
      121 vtvtifrlks gqhledggqe kskhlalsrp gkteqqlaqq imtwisdala lpiginernf
      181 laqqlegvny kplehllien ydgtflyqvs eliqavsekt andfrtdsal yynlvthiqa
      241 tfnrpevsef qesphtlldr itdqyfdlyq avrtsfsqaf pgqkigrdel ayivihfats
      301 lerhpqgpqk islllvcasg mgttkilenr lkkyikqnll idvvklsaln qvaltsydiv
      361 lstlflpgls rhyhlvspll lddelkalei eieqiaqnkd rvgannrtre vgslarnnqe
      421 lslenyyhki keayqvyqsf qvikvnntgk akldlkalld qqigqlrgrq vgnsqqvsea
      481 vmrrfkesai giphssiglf htshvevlep yfviydlaeg ypilgmdhqm mtlrrlllll
      541 apnpltpwiq evmgaisssv iendanlsly drgdegrlkq llnnillati knmdsl
//
LOCUS       WP_284779046             476 aa            linear   BCT 25-DEC-2024
DEFINITION  protoporphyrinogen/coproporphyrinogen oxidase [Cutibacterium
            acnes].
ACCESSION   WP_284779046
VERSION     WP_284779046.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Pawelek,P.D., Cheah,J., Coulombe,R., Macheroux,P., Ghisla,S. and
            Vrielink,A.
  TITLE     The structure of L-amino acid oxidase reveals the substrate
            trajectory into an enantiomerically conserved active site
  JOURNAL   EMBO J 19 (16), 4204-4215 (2000)
   PUBMED   10944103
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440906
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..476
                     /product="protoporphyrinogen/coproporphyrinogen oxidase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006779 - porphyrin-containing compound
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=49312
     Region          8..476
                     /region_name="HemY"
                     /note="Protoporphyrinogen oxidase HemY/PPOX [Coenzyme
                     transport and metabolism]; COG1232"
                     /db_xref="CDD:440845"
ORIGIN      
        1 mnisdpqhvd avvigggmag lvaawqftqe glhpvlvesr gytggliars tlagvsydig
       61 aegwavrlpd taelatelgl tvekptiaps wvyfddacfa mpdnailgip anlsdpavvi
      121 algaekaara aeldrapmpe dlprdlgtlv asrmgpevlr rlvtpiaggi haadphllsa
      181 dvvspglraa aqatgslaag valcrsrmpa gpavasvagg mfimpaelrr qaeqagattm
      241 trvgargltr hedqwlveta gtsrnpdpsl ppvtngesrf fltprvvvac sagpatklis
      301 nvietvgpem apgapighvn lalqapelds sprgngmlva pgtttvtaka lthmsakwps
      361 lrescpeglh llrvsygrsg etnvslsidq aladasvllg vdlsaeqvvd sqiihwtgsl
      421 apttpqtraw rdglhrqlea lnqsgrgrig lvgawasgsg iaalvaqarr tvrqlv
//
LOCUS       WP_284779085             456 aa            linear   BCT 25-DEC-2024
DEFINITION  nitrate/nitrite transporter [Cutibacterium acnes].
ACCESSION   WP_284779085
VERSION     WP_284779085.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Yan,H., Huang,W., Yan,C., Gong,X., Jiang,S., Zhao,Y., Wang,J. and
            Shi,Y.
  TITLE     Structure and mechanism of a nitrate transporter
  JOURNAL   Cell Rep 3 (3), 716-723 (2013)
   PUBMED   23523348
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..456
                     /product="nitrate/nitrite transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49442
     Region          46..444
                     /region_name="MFS_NRT2_like"
                     /note="Plant Nitrate transporter NRT2 family and Bacterial
                     Nitrate/Nitrite transporters of the Major Facilitator
                     Superfamily; cd17341"
                     /db_xref="CDD:340899"
     Site            order(56..57,60..61,64,97,152..153,155..157,160,179,
                     182..183,186,269,272..273,276..278,281,318,322,377..378,
                     382,386,402,405..406,409..410,413)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340899"
ORIGIN      
        1 mifsgnirvn ytiprgdivs tspshhlien wdpeenwdsg iawrtltist fsmiiafcvw
       61 flvsaiapkl naigfhltks qlywltampg lsggfirlvy mflppvigtr rlvgysslly
      121 lvpmlgwffa vqntstgygt llllaflcgv gggsfsgymp stgyffpksk qgtalgvqag
      181 ignlgmsivq llgpwlmgfg llgltwiapq htagsplwvh niaivfvpwt ilatilafti
      241 lkdvpvkanf rrqidiftnp dtwimtlmyv mtfglfsgfs aqfgllient ygnssnlahg
      301 fsnlptgasy aflgpligsl vrviwgplcd rfggaiwtlv sgigmaltfg fcafflnpts
      361 psqfgyflwg mltmfffsgi gnagtfkqmp mimparqagg aigftaaigc fgpfvvgval
      421 ssmsavawfw ictvfcivcs iicwiryarp gapcpg
//
LOCUS       WP_284779230             358 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide)
            pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
            [Corynebacterium coyleae].
ACCESSION   WP_284779230
VERSION     WP_284779230.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Davies,G.J., Gloster,T.M. and Henrissat,B.
  TITLE     Recent structural insights into the expanding world of
            carbohydrate-active enzymes
  JOURNAL   Curr Opin Struct Biol 15 (6), 637-645 (2005)
   PUBMED   16263268
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   4  (residues 1 to 358)
  AUTHORS   van Heijenoort,J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit
  JOURNAL   Nat Prod Rep 18 (5), 503-519 (2001)
   PUBMED   11699883
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Ha,S., Gross,B. and Walker,S.
  TITLE     E. Coli MurG: a paradigm for a superfamily of glycosyltransferases
  JOURNAL   Curr Drug Targets Infect Disord 1 (2), 201-213 (2001)
   PUBMED   12455415
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..358
                     /product="UDP-N-acetylglucosamine--N-acetylmuramyl-
                     (pentapeptide) pyrophosphoryl-undecaprenol
                     N-acetylglucosamine transferase"
                     /EC_number="2.4.1.227"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0050511 -
                     undecaprenyldiphospho-muramoylpentapeptide
                     beta-N-acetylglucosaminyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051991 -
                     UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-
                     glutamyl-meso-2,
                     6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol
                     4-beta-N-acetylglucosaminlytransferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0030259 - lipid glycosylation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=36549
     Region          5..356
                     /region_name="MurG"
                     /note="UDP-N-acetylglucosamine:LPS N-acetylglucosamine
                     transferase [Cell wall/membrane/envelope biogenesis];
                     COG0707"
                     /db_xref="CDD:440471"
ORIGIN      
        1 mselnvvlag ggtaghiepa lavgevlrdr fganvvalgt erglettivp argfelalid
       61 pvpiprkkpw klaavpakll rsvnqakqam kssgaqvvlg tggyvsapay laakslrlpf
      121 fvletnalag manklgvklg gvglnavans gmagdvvgip vrpgvgvdpd gakrerglrt
      181 wgldpekttv lvtggsqgav sintalagav eritaaghqv lhaygrknda paphegytav
      241 pyiddmeaay avadvvvcrs gamtvaensa agvpaiyipl phgngeqgln sahlvatgaa
      301 lriddaelng dvlvekllpl lnnddaraem rraiaqsgag nvaedlarri adaagken
//
LOCUS       WP_284779369             325 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Corynebacterium coyleae].
ACCESSION   WP_284779369
VERSION     WP_284779369.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..325
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34836
     Region          2..322
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(40..41,45,118,122,125,143,146..148,167..168,172,187,
                     213..214,235..239,260..263,310,312)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(130,228..229,242..247,255..262,265..266)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mkailvtkhg gpevleytei adpvpgegql lvdvdyagvn yidtyfrsgt yaseppyipg
       61 tegcgrvvdd plgeiapgtl vawhdapgsy aekvavdrnr lvavpegvqp evaasmllqg
      121 mtshylihgv rdtrpgdtmv itagaggvgl iltqmaaale ttvysivssd ekedlaykag
      181 atkvfrygdk gsalaeeike vnggkgvnvv ydgvgrdtfq falevtgprg lvcsfgsasg
      241 dvepfkiqel nqhgalfltr pslkhyvatd eeflmraqav vraiedgtvr mrvhppyelk
      301 narkahedlq arkttgsvvl kierd
//
LOCUS       WP_284779644             378 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Corynebacterium coyleae].
ACCESSION   WP_284779644
VERSION     WP_284779644.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..378
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41043
     Region          1..375
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mnaplsgirv ldlsrvlagp fcsmiladlg aevikvespw gddsrqfgpf vdgtsayyrl
       61 fnrskmgitl dfkndddkev lrdlvrradv vvenfrpgvl eklglapkdl leinprlvvt
      121 sisgfgqtgs lakepaydlv aqamsglmsi tgwpnskptr vgislgdlip glyaaigtvs
      181 alyqressgt gqhldlamyd slisvmesvg mralyddtpp trigndhgls apfstyatkd
      241 gdvviaittn rlferlanal gipematdhr faepvarsdn rvalreliee alstktrset
      301 ialfeehgvp tarvydldea lrspfaqerg vvveetdgfr tlasplklag mgkptpapel
      361 gqdneriqsw lsedprtt
//
LOCUS       WP_284779625             340 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium coyleae].
ACCESSION   WP_284779625
VERSION     WP_284779625.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..340
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34102
     Region          22..337
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtkrvglval lvistvcaal vslligarem gfeatvsavr dglmlafsga deqseassde
       61 akiiaqlrvp rtllgllvga algtagallq ghtrnpladt nllgvgpgaa lavaaaisfy
      121 gsmtvlgtvg vgflgailav alvfvlsmrs lgstpitvvl ggsalgavcs altsgivlth
      181 trslnemrfw tagaiagrdm qvvtvlapvi vlglvgafas anqlnllnlg ddvanalgvr
      241 vsiartlgiv lvalltgaav agagpigfvg lvvphlvrsl tgpdyrwvlp csalagatll
      301 lladvigrvi arpgelqvgi tlafvgapfa lhilrkgtkl
//
LOCUS       WP_284779697             448 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Aerococcus urinae].
ACCESSION   WP_284779697
VERSION     WP_284779697.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..448
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48367
     Region          1..447
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 madydllvig sgpggyiaae eaaksglkta vvdkgpvggt clnsgcipiq syvqngrwdl
       61 qskqlakygl aqaseeidfk vlkarkdqvv qqnqqgilqi fksngidfie geavfvkdkt
      121 fkvndqtlsa knvllatgsr vleptipgie gvdylthesf fhmedlperl vivgasehgv
      181 efafamaalg vkvslieeka tiipnqvkev qdyvkklfkk lsveviegia idrvspgqvh
      241 lsdgqeigfd qlllmlsrrp dltmvkamgl dldkkgtyla vdenyqsssp giygvgdlig
      301 gwpfahaash egikavkail gqaeypldfn avprkmavdv dvesfgmhed qaqeagydvi
      361 shqipfmmng aaaaldeteg fvniiserqy gqilgglvvg hgaseimhil lavyqcegti
      421 delaqivfah ptlsetigdv akalvrky
//
LOCUS       WP_284779701             232 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium coyleae].
ACCESSION   WP_284779701
VERSION     WP_284779701.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..232
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25334
     Region          45..200
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mvavrperap vwlwglvdkl ragegdarvk amlgprvpqt pgedqaavli vfagdpdaee
       61 lpedarvlit hrtpsmrshs gqmafpgghi datdtgpvaa alreayeetg lapervvpla
      121 vmgqvktggs rrlvrpvvay apdpgevypa seletddvff vpvrdlvdpa nraklgwkhw
      181 tgptfwardy liwgftgill avvldlagwv rawderpgdl yealarsrnr el
//
LOCUS       WP_284779919             343 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium coyleae].
ACCESSION   WP_284779919
VERSION     WP_284779919.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 343)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..343
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=35889
     Region          61..343
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrlslrarit vmfvatvlgm glaliglvya ylkltpvpvt atfptvedgv iidgavpits
       61 eilrrvllas lsvlalltll agvigwfvag lvikplrdia ddaaivtrgd lsarithhgp
      121 ddevgelada lnvmldelag averqrrfas nashelktpi atiqtmadva ltgddaglrp
      181 tlsrvrevna rsadtvaall qlanvdvrdr qrldlaelcr evctdrdvpa dtvpvtvnas
      241 ptltrqavdn lvrnalthgh npvltlrkvg nvaevtvesg getysaaevs twtepfarae
      301 rtsgaghglg lalvdaiana hggslvlapr aggglvakls lpa
//
LOCUS       WP_284780124             794 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium sp. UMB4614].
ACCESSION   WP_284780124
VERSION     WP_284780124.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB4614
  ORGANISM  Corynebacterium sp. UMB4614
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 794)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 794)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 794)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Corynebacterium sp. UMB4614"
                     /db_xref="taxon:3046334"
     Protein         1..794
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=86178
     Region          16..790
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mtspasrgtt nnadrslaea iaseqdhldd llaevdatta tlkkrlasvr atadiddpqg
       61 lmrrdreiqd isqrldnlsi aeiglmfgri dvadeepenp vpgspdldrr yigrlglhtr
      121 ddemrtllmd wrapmarpfy lattlhpdgv hlrrhiktrg rrvthvader lttrgedras
      181 ltekttsaag gvaqeaalld avnaarstrm gdivetiaae qdaiirsehr svtvvqgapg
      241 tgktavalhr aayllytwre qlaktgvliv gpnarfldyi sqvlpslget gvvlatpgtl
      301 lpgvktrpep sllarevkgs aemlhilkla vqswqqvpeq prdfmvdgva velspkmvra
      361 artrarrsrk phnqarplfv dhaisslada laqtigrdpl ggenlltaed rtslrddlre
      421 epavvaalde fwpeltpeqv ladlyehaee iaseydedti rglqatppve ldggqilwta
      481 adaplldela dmlgiiddea aekaereewl akiaeaqdal diltgsatqd lddgfapeil
      541 maydvidaeq lagrqrvrda rstaqraaqd lrwafghviv deaqelsemd wrmifrrspn
      601 rwmtvvgdpa qtgnpagvas wgetlapyvs drwelkelsv nyrtpqdiad vanqllpeia
      661 adqepaialr gtgtgvayaa raelagalpe iarrageglv giiasdadle wargkvtaal
      721 gdalgsdlvg idaevlvvst aeakglefde vvliepaaiv aaspqglqdl yvaitratqg
      781 lsvfadqplp wdqg
//
LOCUS       WP_284780205             618 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Aerococcus urinae].
ACCESSION   WP_284780205
VERSION     WP_284780205.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 618)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..618
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=71386
     Region          10..613
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 malvdrwyei lnnlymhpki pqaefeaglk tsrqtlkkni qllnqelggi asitledkvy
       61 hltikdfaaf kkilagkfrq dtdfnssnkr qayilkqlie dqeaviiddl aevttvsrgt
      121 vnndishlrq eltdyhltiv gtpnkgltle gdeldirtay vnivlsyfke dqftiedkth
      181 llnlapnfnm tnftkdlllk vvyvtllrvr qghgltseil hyqnflqgqe dyevfiaeie
      241 dyfnltlshy eyqylaypfn iynkedivpe sfnsafvdhv yqevlqaiqr dlaiefdqek
      301 lyqamrnhli flirrllfrv nsedlffhev qqqyplsftl aeitgqvlee vldrevpgie
      361 lsylslyfel visrqvslks qkiaivchtg kgtarlikmq iqrilgtsle lstfsegefn
      421 qedpsqyfai fttipldktr ikrpiiqldn lfdesyirsq wnsvqrhnpl fsqlvyldfi
      481 tldqgesyed llqvmtdkvi eetgissdfq qaifereais dtvfdqgiam phtvvedfdq
      541 iilfigqvea dikekgrpid lvfllgipsq tnqvmdelli niyeaifava nnqdlkvllk
      601 tthsleeiqd ilqgddal
//
LOCUS       WP_284780324             357 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Corynebacterium sp. UMB4614].
ACCESSION   WP_284780324
VERSION     WP_284780324.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB4614
  ORGANISM  Corynebacterium sp. UMB4614
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Corynebacterium sp. UMB4614"
                     /db_xref="taxon:3046334"
     Protein         1..357
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=38205
     Region          50..337
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mdpisqqaaq tnnplsraml klyaaiyrad rkvglprevd adgnkvvkvp rlktqwvltl
       61 illicqtgit ftgslvrvtg sglgcetwpq chpgsfvpva gsapwihqii efgnrlltfv
      121 laaaalaafi allraarras ilhlafiqgl giiaqavigg isvrldlaww ivaahflpsm
      181 llvflaavll vkvtedddap akpqmpaalr vlttmsaval aftlftgvlv tsagphagde
      241 aikpehrlqv slesiahiha hamylylglt igliaaliav vaaprvrkaa awmcagilfq
      301 gvvgiiqfwl gvprwtvpih vigsglvtla tgylwalryq ktheeqsetv shavqgd
//
LOCUS       WP_284780473             368 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium sp.
            UMB4614].
ACCESSION   WP_284780473
VERSION     WP_284780473.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB4614
  ORGANISM  Corynebacterium sp. UMB4614
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Corynebacterium sp. UMB4614"
                     /db_xref="taxon:3046334"
     Protein         1..368
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38417
     Region          51..366
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 masstdtrre pgkgakaspl egtklaparr vptwvawvvg lillalvcym alfmgaatlt
       61 rdevwgsith klgifasdsr papslirqsi lfdlripriv mgifvgagla vagaslqait
      121 rndlaepyll gvsygastga vvalllmpvs falgltggaa igallsfgll mlllrgtgfv
      181 strvvltgvl vgqffsaits lilvargdae svrgitfwll gamgasrant mwivlitvvi
      241 tslliwmmsr yldamsfgde taksmgvpvv gvraavlilv almtaatvsa vgaigfigll
      301 vphavrmivg ssharlipls alvgaillvf tdalarsvfq pqevpvgvft allgvplfff
      361 ilnrgqrv
//
LOCUS       WP_284780494             372 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium sp.
            UMB4614].
ACCESSION   WP_284780494
VERSION     WP_284780494.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB4614
  ORGANISM  Corynebacterium sp. UMB4614
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 372)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Corynebacterium sp. UMB4614"
                     /db_xref="taxon:3046334"
     Protein         1..372
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38209
     Region          56..368
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 maistphaqs psqshlgsra datadasasa psgkiprrlv glgvlfllll asivasivfg
       61 srqipfgevs avfrdlgtaf dhaeglnvdq rvivelripr tllglvagaa lgasgaliqg
      121 htrnpladtg ilginygasl avvasfsllg vtsvwatsmw afggaiaata lvfslasigg
      181 gqanpmtlvl ggaalsavls aiisgfiltd danldrmrfw tvgsiagrdl tvfygvlpfi
      241 lvglllafit apqlnllnlg ddiasglgin tqrarligma liallagaat aavgpitfig
      301 lvvphlvrai tgpdyrwilp ysaltgavmm lfadvvgrli arpgelqvgi ilafvgapff
      361 ialiyrrrvv ai
//
LOCUS       WP_284780505             242 aa            linear   BCT 25-DEC-2024
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Aerococcus
            urinae].
ACCESSION   WP_284780505
VERSION     WP_284780505.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10061503
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..242
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27030
     Region          197..240
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
ORIGIN      
        1 mafkdnwnqf knkwkkeepa veeenanlee eveagpetss adeyenlknr qysrssrnkk
       61 ekgvsptvkv lialgllfil ipyaayiiyg nqqkqpesmn vdqvmvskse ndsqkqaeee
      121 skkaeeskqa eeskkqeesq qaaqasqqaa qearqaaeqs lavqqsqqqa aaqeqsrqqa
      181 srnqnqqntn qnqnvgsyqv sagdnlyria vnhgmtlnql lelnglhans piapgtvlrv
      241 yq
//
LOCUS       WP_284780581             226 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Corynebacterium sp.
            UMB4614].
ACCESSION   WP_284780581
VERSION     WP_284780581.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB4614
  ORGANISM  Corynebacterium sp. UMB4614
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Corynebacterium sp. UMB4614"
                     /db_xref="taxon:3046334"
     Protein         1..226
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24226
     Region          72..216
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 msrrgahlrs trpnlrsrsr aalaallaaa islggltacg egatgddava vggtfefvsp
       61 ggqtsisypq eerkevanlt geslmeegeq inledyagka vvlntwgqwc gpcrseaddl
      121 ervheklvkr gdgtvlginv rdpsrekpkn fvrtygityp siydppfksa lrlggipasv
      181 ipttivldkq hrpahiflke vtddelwnvl epildeedga gdgega
//
LOCUS       WP_284780720             115 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium coyleae].
ACCESSION   WP_284780720
VERSION     WP_284780720.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..115
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12672
     Region          25..112
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mkdyvatten tdldccslgs gllseddatr yadlfkvlad pgrlqllsri aeegcepmsv
       61 neltqrsgls qptvshhlkm lteaglleks rqgrtvihrl rpelfaelra vlqmd
//
LOCUS       WP_284780665             841 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium coyleae].
ACCESSION   WP_284780665
VERSION     WP_284780665.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 841)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 841)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 841)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 841)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..841
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..841
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=90691
     Region          59..840
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msnhehldnc ieearhaarq agidpgtatw dldgelvrpn asyafelegi edgpqltdia
       61 ealealpgvs arlvyptkma wvtapastpl veltdtiesf gvtatvtdst lqrrahgryw
      121 qehpmprrak hrrneeanli araqgfvrpv srrsrregdv lftardlvtp trlvvavllt
      181 ipvllltyip sldfpgwqwv cfalatpval wcaspfhram aggvrrgisa ldgassiail
      241 asyvwsfaml lftevgrigy tttgswmplr msdspelyfe vsctvttlll fgryfsmqvr
      301 tdlreelesr rpgtedvynv dhrdkrgtps peelpateir rgddvtltag hiipvdgevv
      361 ggsgriggel vdthrdqilk vgsivtagsv lasgeikvra arvghttlla avqrwlddas
      421 rhqnaatmvs trsagllipt ayviavlnfg lwllfngnin taaatslail vvvapvslai
      481 spalamrqgl dsavrhgmlv rdgnalrtla dtdmvvfnrv gtlvkpemhv etvtavrges
      541 telvlriagv lsadsdhpas kaivkaarga rdarsgdpri pdwieangdt fspdgefggp
      601 itatwgtgen arsetfaasl wrptnlsqlh gklsvaattg gtpvvvrwgg rdrgvitlyd
      661 pakddaiqai drlesmgvet vmltrdtypv arrfadflgi sqvlagihgl dkphavralh
      721 tqgsnvamvg dasvlptlrv adsgilfaed dlagtkeprw sddaevvlir edvmsvpqli
      781 ehaqrvkria nsnlafavay natavvlaaa galppvgatl lmlgsslfie aksrrarrfk
      841 i
//
LOCUS       WP_284780752             500 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Corynebacterium coyleae].
ACCESSION   WP_284780752
VERSION     WP_284780752.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..500
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52235
     Region          127..496
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mttavapads peqqtsnkln tgktiaffla fvalaavilt piaglampak ialgmlafav
       61 imwvseavsy pvsavmivgl iaimltfavd petgeaigas kglsiamsgf sssavalvaa
      121 alalatamqa tglhrrlaly vlkfagekvs nivigaivis iilaffvpsa taragavvpi
      181 lmgmvaafgl akesklaall vitatqavsi wnvgiktaaa qnlvavgfie dqmgqtvswg
      241 qwfiwaapws ilmsialyfi mraaikpeve sidggrelve kqlaemgpmt gaekrlttia
      301 vlllffwate gvlhpissat itivavgfml mpvigvmdwk yaqeqinwgt lvvfaagisl
      361 gkflldtgaa twlseatfga iglssmpila aialvslfni lihlgfasat slasalipvf
      421 ialaatldvp nggigfviiq qfvicfgfll pvsapqnmla ygtgaftskq flrtgiplti
      481 vayllillls atywnwiglv
//
LOCUS       WP_284780792             197 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Corynebacterium coyleae].
ACCESSION   WP_284780792
VERSION     WP_284780792.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..197
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=21161
     Region          1..190
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mrlvlasqsp srrmlleqgg vtpvlrpahi dedaviavlg dvppattvat larakaetai
       61 aqfpddvvvg cdsmlllddt llgkphtvde tirrwkaqrg keahlltgha vwfggewvvd
      121 tvttairfgd vsdadieaya rsgqplecag aftlealgsw fidsidgdpt sviglsmpll
      181 rrclyrfgld asdfwta
//
LOCUS       WP_284780884             257 aa            linear   BCT 25-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Corynebacterium sp.
            UMB4614].
ACCESSION   WP_284780884
VERSION     WP_284780884.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB4614
  ORGANISM  Corynebacterium sp. UMB4614
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Corynebacterium sp. UMB4614"
                     /db_xref="taxon:3046334"
     Protein         1..257
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28145
     Region          5..247
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mqhevkiiah rgaskhrpeh tigayelaaa qgadgyecdi rltrdghavc ihdrtvdrvs
       61 dgtgavsrmt laelkalnfg tstrpagvle lrelleflqd mrhsaeagqp elfietkhph
      121 vrslqveaem hrqlaaagla ggegiylisf dswslwrsrq inpqveriql rrkyhpparp
      181 llrgsgiarh agwsieqama slrgeggsap adyiwtvdqa eqlrwiaqrg arwvatnypg
      241 eaagwlqnsa gggagqp
//
LOCUS       WP_284781033             611 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Corynebacterium sp. UMB4614].
ACCESSION   WP_284781033
VERSION     WP_284781033.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB4614
  ORGANISM  Corynebacterium sp. UMB4614
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 611)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Corynebacterium sp. UMB4614"
                     /db_xref="taxon:3046334"
     Protein         1..611
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66722
     Region          1..611
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mrteytsepl ytigenetil talrdlqkdh psvvvfsrpk nfdwedvttt qfldevyava
       61 rgliangvka kdrvvimset ryewslldla iqaagaisvp iypssstsqc awivqdsgas
      121 favgetqehc erlenfiped gtvtekeplt rvlginrgav dilindgrdk kisqdevear
      181 iadvrtsdvc sivytsgttg rpkgckvlhs nwlseargla thpigrlgmp gksavtflpl
      241 ahvlsravsy lllttgctqt hwsdfgtlvt efqrsnpnmv lgvprvfekv hagvrakasd
      301 gskigeklfe raekiaveys kaldtpqgpn lalktshaif dkliyskvre amggeleyai
      361 sggsalntel mhffrgvgvy iyegygltes taaitvnfep dniigtvgrp vggntvriae
      421 dgeillkgdv ifggywnnee atkeafdedg fyatgdlgal lptghlritg rkkeilvtag
      481 gknvspgple dilrsaplis qamvvgddqk figalislde aaveswkarn gisagtsird
      541 laknpnlrge iqdaineanq svshaegikk frivhrdfee ergevtpsmk lkrfmveknf
      601 addiawiyse k
//
LOCUS       WP_284781059             868 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Corynebacterium sp. UMB4614].
ACCESSION   WP_284781059
VERSION     WP_284781059.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB4614
  ORGANISM  Corynebacterium sp. UMB4614
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15309921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..868
                     /organism="Corynebacterium sp. UMB4614"
                     /db_xref="taxon:3046334"
     Protein         1..868
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=94527
     Region          218..463
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(218,243..244,271,276,281..284,298)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(225..226,228..231,233,247,249,279,297..300,304,306,
                     345,347,349..350,352,361..362,365,377..380)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(225..226,228..231,233,247,249,279,297..300,304,347,
                     349..350,352,361..362)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(229,304,306,345,347,349,365,377..380)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(361..369,373..380)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          482..866
                     /region_name="PknG_TPR"
                     /note="Protein kinase G tetratricopeptide repeat;
                     pfam16918"
                     /db_xref="CDD:435652"
ORIGIN      
        1 msekdaaeqn iqeqgrtpep dagppteavn rtepdaatgp daatgpdvvt ggtaehpepd
       61 attgpatepg agkqdeddge ngteavvfdp faddddeeef dladlgdlsd liepgstaqg
      121 rsqadvptsa tevgsstsga ttdpvkvdsg ersrrealst frelrgaare gknvadgmvh
      181 lpfitptvpe eaiidpsdai akgidpptlk agdliagqye ilgpiahggl gwiyiatdhn
      241 vanryvvlkg lmateneher avadserafl adithpgivk ifnfiddprs pggfivmefv
      301 ggpslrerrr espdntlpvd iaigymlevl paldylhsrg vvyndlkpdn iiitedqvkl
      361 idlgavsgig ayghifgtkg fqapeiastg ptvasdiytv grtlaslvvn lpitngaydp
      421 elptpeeepl fqrymslyrl llratdpdpn krfssavtla nqmvgvlrev lairdrvqya
      481 hldtrftaqr stygtkhmlf rtdqlidgip rsvqiaasev iaalplpltd psdpgaslls
      541 aarytepgev ldtlesaakq pqmsssveip ltmvrarldm gqaqeaqdkl devqdwlggd
      601 wrfrwlsgva allrsdfvta qyhfnevlhl lpgepapkla laatnellmq qqgvnttkll
      661 ddetaqlgam lsyayrtpmt edvkvpparh lsqdpatlrm qtmrlyglvw atnpttvssa
      721 fglarqlaae glvdaavgvl drvpvasrhh rlarltsilm lisdrsrlse srirraarrl
      781 eimptneprm qqvrlavmla glnwiyinkk kgndvssesp lfdvpfterg lrlgleqglr
      841 mlarqahfdl hrfrlvdman mirprtwf
//
LOCUS       WP_284781216             293 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfurtransferase [Corynebacterium sp. UMB4614].
ACCESSION   WP_284781216
VERSION     WP_284781216.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB4614
  ORGANISM  Corynebacterium sp. UMB4614
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Corynebacterium sp. UMB4614"
                     /db_xref="taxon:3046334"
     Protein         1..293
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=32224
     Region          38..291
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 msqatsrrvh dtfskipgpf isgeqlyeay rlgermtiid shwaktensa weayvgqhlp
       61 gamfcnplqh lagtpsrarg rnpmpglaal qrsfynwgit egrpvviyda grniyaaraw
      121 wilrwagven vkilnggtsq weeaggdvag gigalrgrgd fkirprsmpe lyideidvwc
      181 rdrmlvdcrd perfrgvrep fdhqaghips avnipvasll deegkvlgga qlreifashg
      241 identeltvh sgsgldsalf laameeaglp vgrhfvggws qwsasssrki arg
//
LOCUS       WP_284781233             191 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Corynebacterium sp. UMB4614].
ACCESSION   WP_284781233
VERSION     WP_284781233.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB4614
  ORGANISM  Corynebacterium sp. UMB4614
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Corynebacterium sp. UMB4614"
                     /db_xref="taxon:3046334"
     Protein         1..191
                     /product="YceD family protein"
                     /calculated_mol_wt=20188
     Region          1..182
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 msnpfildvq dilgqqggpe hvhttgetph nlggemfgia pgtsvdidli ltnlgeaima
       61 qgtvsgqanv ecgrclrrft tdlsikvdqv fgtsadfitt ededsdeegd elpplveddr
      121 idltqtvlne aglnapfnpv cadyglecet nvpepdgise eeaeeekvdp rwaglsaiks
      181 qlaggddgsq a
//
LOCUS       WP_284781306             245 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium sp. UMB4614].
ACCESSION   WP_284781306
VERSION     WP_284781306.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB4614
  ORGANISM  Corynebacterium sp. UMB4614
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Corynebacterium sp. UMB4614"
                     /db_xref="taxon:3046334"
     Protein         1..245
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26683
     Region          80..226
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 msqkikapdq kggsgfmwti vavlviaavv igivvtrggs kediaanmpq edvnftitak
       61 dnvvelaskn idkdapvadi yedfscpycs hlleadhqdv keavsdgklk vrfnflnfld
      121 dgrrgpstrg aavayaiaet gnvkafwnfh nhimleqqtv artwdyedla eaasaydlde
      181 sliekiknge ledkgvevge anakalkkkv gkvsspvvli dgqqfdiktg eddkpkswvp
      241 dvvkk
//
LOCUS       WP_284781346             413 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Corynebacterium sp. UMB4614].
ACCESSION   WP_284781346
VERSION     WP_284781346.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB4614
  ORGANISM  Corynebacterium sp. UMB4614
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Corynebacterium sp. UMB4614"
                     /db_xref="taxon:3046334"
     Protein         1..413
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=42715
     Region          135..412
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 marhasgenn fkvagwvwav liavvlvtal iigwsavskn nqtsvaaeec aegdyelsvw
       61 aapqakaaae elakayndad rivadhcvta sisevadrdg lskldsevpa awvpedaaav
      121 lpaakdhgvr aagndvpnvg eparpvlrle agdrvpelgq raasdftsfa veeqklpstk
      181 vaeltgdkak dtedgkdkkd qkdaqakdak kdkdaakkpa largtdvtfl ldtsdamgvv
      241 egdarrldvv rgalhsafqr vgdnegavsl wnyssqlspg artpyrvnvd lsardggaaa
      301 gavldqlnvg ggnhanvsis aahkaavdsa aagsgkpagr mvvvlagknq delsveqlka
      361 qlaaanpqvr vdivgiggdv aadelariae atggrfyhar dakavdgvlk giv
//
LOCUS       WP_284781410             220 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA polymerase sigma factor [Corynebacterium sp. UMB4614].
ACCESSION   WP_284781410
VERSION     WP_284781410.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB4614
  ORGANISM  Corynebacterium sp. UMB4614
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Corynebacterium sp. UMB4614"
                     /db_xref="taxon:3046334"
     Protein         1..220
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=24301
     Region          39..211
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtapvtdtqh ttapdraktt twgsapsntg daphtsahrt dqellaehia gdplalhtll
       61 arhevrmhwa eraagvpese ladvhqeavl kihrraatfr nrssvvtwmv tiahrtalnf
      121 vtaqhrrghr hredisdcer dlpsshatpn qelsvdlhna lasipvlfrq tvvlrgmlgy
      181 siseisamld vapgtvksry srgrrllqdh lvladyadhp
//
LOCUS       WP_284781491             766 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional copper resistance protein CopD/cytochrome c oxidase
            assembly protein [Corynebacterium sp. UMB4614].
ACCESSION   WP_284781491
VERSION     WP_284781491.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB4614
  ORGANISM  Corynebacterium sp. UMB4614
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Corynebacterium sp. UMB4614"
                     /db_xref="taxon:3046334"
     Protein         1..766
                     /product="bifunctional copper resistance protein
                     CopD/cytochrome c oxidase assembly protein"
                     /calculated_mol_wt=83766
     Region          145..434
                     /region_name="PcoD"
                     /note="Putative copper export protein [Inorganic ion
                     transport and metabolism]; COG1276"
                     /db_xref="CDD:440887"
     Region          404..649
                     /region_name="Caa3_CtaG"
                     /note="Cytochrome c oxidase caa3 assembly factor
                     (Caa3_CtaG); pfam09678"
                     /db_xref="CDD:430748"
ORIGIN      
        1 msapvknaaa parsgsgaqk lgppilvyia aalvagivga visveflges laalgvpdpg
       61 tattfglpfl rsaatligcm gvggflmsaf gapprgdgyl dydgyaaart gqwgmflwav
      121 calfliplym sdvsgsplke tlkpdlwsva iqqvstakaf lavaiiaglt wffslltrkw
      181 iwqpvflala lctmiplald ghsasggnhd fgvnsllwhv matavwvggl malvahakrr
      241 gphlalitkr ysfvafwafv avvlsglvna airvrfsewl ttdyglvita kavlgivllv
      301 cgylhrksvi pkleaaegeg gsstaearka fsrlaigevl vmagaigvai slsrippplp
      361 qqieittmdi llgfritepp nylhmfgmfr ldliygvgai ilqvlymwaw ftlrkkgqdw
      421 plnrllwwta gnvfllyats sglgmyamam fsphmlqhmi lamvvpicwa lggpmtlflr
      481 alpaagrdgv pgprewlvvf innpisrfwt hpivagiqfv vgfywlylst lfdwmgsnhs
      541 ghlfmighfl isgyiyfwvi igvdaaprhi safnkmlvlf gsvvfhawfg ialmqmrspm
      601 nadfyqrldf pfaldilhdq wvggaiawgl gelpllivsi ahgvqwyrse dreakrydrh
      661 qdrtggqdlq aynamlasma gkggdfgeke yytadyetes vqsqlhtekq rrrkqvrrrk
      721 gqkftdlpsp eyganipgay gqaprsqrpa pdsgtrsdda saedad
//
LOCUS       WP_284781506             924 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Corynebacterium sp. UMB4614].
ACCESSION   WP_284781506
VERSION     WP_284781506.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB4614
  ORGANISM  Corynebacterium sp. UMB4614
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 924)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 924)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 924)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 924)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 924)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 924)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 924)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Corynebacterium sp. UMB4614"
                     /db_xref="taxon:3046334"
     Protein         1..924
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=93939
     Region          135..924
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mpqsangsci sgaaavgrls frsiaahkvr llltvlavil gtafiagslm ftaglsrtfd
       61 slvdgemknv davvsaspsp hegssggagg qstgsqsrns gdtaetvagg qatsagedat
      121 rapadraagq pqapsnrris eddlrriqqm pgvsqvniad qvqavaatas getlksapap
      181 tmlqpfynge esvkgethii dgaaptaage vainasaaet hgvkvgdrlk vvtsrnqdev
      241 tvtgiydsdi etggfiglsv aaetfkekfl qsgeprtlyv gsapgttade lvdrlaaefp
      301 ysvqtgeevs eelsaeiska lsfvsyflia fglvgllvgt fiiantfsmi vaqrmrefal
      361 lralgvsrgq ltasvvfeaa vvgvlgsalg vlagmglvka iyavlestga glpaggivlt
      421 plavalpmiv gvlvtilsaw aparsagatr pveamrsgda ssssslvgrt iagglafavg
      481 vaialagalg dgwstktrai lvgvaavlvi lgtflaspav arravpaigr vvglpfgtvg
      541 alarknsarn prrtattafa ltlglalvga vgmlgasmka svaevtetav kadfvatgps
      601 nsgfpvpnga vravqdtpgv gtvgvmgssl vniegigafa gqpfanyygg nphdgivlet
      661 vegktelade gfiadtktaa shgwkvgesy pahlgkvsag kklpllgtye pnqalgpyvl
      721 sragvesvqp saqgqwpgqi malmvtaapg egggeqsvpt elqeelreat rdyivvqvlt
      781 paeasgeaav mvdqmlnily allalaivva ilgivntlal nvierrqeig mlraigtmrg
      841 qirrmitlea vqiavygaiv gvliglglgw afvtvlageg leelavpwlq lvlmllgsal
      901 vgvvaaawpa ikagrtpple aiad
//
LOCUS       WP_284781509             553 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Corynebacterium sp. UMB4614].
ACCESSION   WP_284781509
VERSION     WP_284781509.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB4614
  ORGANISM  Corynebacterium sp. UMB4614
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12045581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Corynebacterium sp. UMB4614"
                     /db_xref="taxon:3046334"
     Protein         1..553
                     /product="SLC13 family permease"
                     /calculated_mol_wt=58481
     Region          <56..220
                     /region_name="CitMHS"
                     /note="Citrate transporter; pfam03600"
                     /db_xref="CDD:460985"
     Region          155..544
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 msapknrdse ntvverdaqd tgttatatta papeqkvdad literaeqeq karrravvgl
       61 fvgvllailv yaifpadaad vvnrahpdae kgpfdadalr itaaiavlmg awwmtealpl
      121 aatalvplva fpilgvvpfk evspsyanpt iflfmggfil algmqrwnlh rrlalrvvtl
      181 vgtkpkqmvl gfmiatgfms mwvsntatav vmlpigmsvl gltadmvggf skqkkfstal
      241 mlgiaysasi gslgtiigtp pntlmvaylq eshdihigfg qwmlvgvpma avfmvlawlv
      301 litvfkpemd qipggreliq eelekmgams raektagtif llaalawvfv pvisdwagwe
      361 hniddatiai taailmymlp adgsgsrvmd wehtkevpwg vlllfgggla lssmfdksgl
      421 slwigevarg lgglpivmli aataivilvl teftsntata aaflpimggv avgtgltagn
      481 dmnvllltvp valaatsafm lpvatppnai aygsgyvrig dmvrgglwln llgivlitiv
      541 tfalavpvfg ltl
//
LOCUS       WP_284781574             347 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium sp.
            UMB4614].
ACCESSION   WP_284781574
VERSION     WP_284781574.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB4614
  ORGANISM  Corynebacterium sp. UMB4614
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Corynebacterium sp. UMB4614"
                     /db_xref="taxon:3046334"
     Protein         1..347
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35319
     Region          6..340
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mtalhavkra rtrriflatl gfaaatvlgy flilgqgavk lspaevldvl tgggtrqain
       61 vvwdlrlpva iatvvvgaal glagswtqam arnplaspdi lgvsggaavl vvagtvlarp
      121 awsegiptfw wraglaligs lvivallmll ggfgtsqrvv liglalsflt qalvqylllk
      181 aeltraadaq twlagstgfv rteallpmvl gmlpfvvlgl vvavdlplfa hddatastlg
      241 vnvtrvrsil liaatgivav vvsfvgpigf iallapqlak lvagtptphp lcsavagsal
      301 mavcavvaga lpftapvglv taiiggpali wlvwsaarrg tvkgmtq
//
LOCUS       WP_284781975              70 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Alloscardovia
            omnicolens].
ACCESSION   WP_284781975
VERSION     WP_284781975.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 70)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 70)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 70)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..70
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7559
     Region          2..57
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(4,8,33)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(7,32)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(14..15,26,29,33..34)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mnlkillmvr slkqedlaea lgisrpavsq kitgkhpwsl gdiekaseff nvepealvag
       61 hgfepwtsgl
//
LOCUS       WP_284782351             307 aa            linear   BCT 25-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Alloscardovia omnicolens].
ACCESSION   WP_284782351
VERSION     WP_284782351.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Bagautdinov,B. and Kunishima,N.
  TITLE     Crystal structures of shikimate dehydrogenase AroE from Thermus
            thermophilus HB8 and its cofactor and substrate complexes: insights
            into the enzymatic mechanism
  JOURNAL   J Mol Biol 373 (2), 424-438 (2007)
   PUBMED   17825835
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..307
                     /product="shikimate dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=33360
     Region          14..288
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 mnadntssst gnqaavlgsp iahslspvlh naayealqlt dwqygrhdit aetledffls
       61 indswagvsm tmplkqkale fgevsderva flgvsntavf dwqrsnpqhe nmphislynt
      121 dvdgvkltfa defnignasd arvciigsgs tamsamaali eigardfvic aadaeqasam
      181 rtkmssyqks qahidvqpwg savkhiqqsd iiistvpahv tdglaqeinn laanisltnk
      241 hlldviydpr ptqlmqslsa reaivrggeh mllrqalaqv aymthlpvrh vidtafahmk
      301 talfeql
//
LOCUS       WP_284782967             192 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Alloscardovia omnicolens].
ACCESSION   WP_284782967
VERSION     WP_284782967.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..192
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=22202
     Region          90..>168
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mpsslgkeys lsdvarfsry ylddypvhiy alknshllvv gsaknsiwky qleynifamk
       61 hlitflpvll tadviimiav plwiqrrwmk srehertewi agvshdirtp ltlilgqada
      121 larhydnnpe vqhkaqiieq qslrlrdlis nlnlsnklty ghceiskekn ksattsaahc
      181 frsdephryr kv
//
LOCUS       WP_284783190             264 aa            linear   BCT 25-DEC-2024
DEFINITION  amidohydrolase family protein [Corynebacterium imitans].
ACCESSION   WP_284783190
VERSION     WP_284783190.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium imitans
  ORGANISM  Corynebacterium imitans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Corynebacterium imitans"
                     /db_xref="taxon:156978"
     Protein         1..264
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29328
     Region          5..263
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mstldiidsh fhqwnlekqt lpwlesepaa lkrsfsvhel mrqyeqiddv rlvglvhiea
       61 dcedpheehq lvrrlktcvp afgivsrakl saemdilads ngvrevlhtp sakpgrclee
      121 sflaglells nhglpfdavv rpqeiphiak asrlvpdasi ilnhvgniat lssenmqnlr
      181 efantpntfc klsgipvdqp dlaqeilqfv kntfgtdrll fasnwpvggv reaitqqvql
      241 vrnvfgddpa vfknnasaiy rlgv
//
LOCUS       WP_284783273             294 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Corynebacterium imitans].
ACCESSION   WP_284783273
VERSION     WP_284783273.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium imitans
  ORGANISM  Corynebacterium imitans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Corynebacterium imitans"
                     /db_xref="taxon:156978"
     Protein         1..294
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30519
     Region          1..279
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(33,228,231)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(180,199,226,229..230,233)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mitvygealv dlvptstdpl aplqpalggg pfnvaralgr lgadvefqsr lsndafgtal
       61 qsslidagvh lsncpagqep ttlavtalaa dgsatytfyv dgtadrlatp tpvsggyavf
      121 gtlslalepa slryaeaasa sakagavvcl dpnirpafas ekhrlflrgm lddvtvlkls
      181 deevdflgdt sqvpvvvttl ggegisvrap fgtctvpapk vkvadtigag dtimaaltyq
      241 fqhrgldrag llelneqqwe eilsfavhaa altvsrtgae tprleevlsf qrge
//
LOCUS       WP_284783365             452 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium imitans].
ACCESSION   WP_284783365
VERSION     WP_284783365.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium imitans
  ORGANISM  Corynebacterium imitans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Corynebacterium imitans"
                     /db_xref="taxon:156978"
     Protein         1..452
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=48631
     Region          29..397
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mtaptkaamr kpaealsthr sprsglpafv rrihfyaglf vapfilvaai sgglyalapt
       61 menmfyrdvl tvetqetstp ladqvaaaqa shpemevaqv wpsstptest rvllidesia
      121 dndelrsvfv nphtgavigd epsysgvgel pmrhwisalh knlhlgtpge lyselaaswl
      181 wvialgglyl wwrtagkkvf tglsntsgkr rrvlnlhgvv gawllvgmla lsatgitwsl
      241 fagqnvdktv ewlggdaepi ettvsstpgn pltdqqvaeq savvldaara egltgqlrlf
      301 ipedtsqawq aserwipgri tsdavsvnga tgevvdklpf selplfsklt swgiylhmgm
      361 mfglplqlal falavgicam ivmgymlwwc rrptkgalag vpgradltgt dwavlalftv
      421 avgaflplfg vsfvamlvad rllarrrgay aa
//
LOCUS       WP_284783608             178 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Corynebacterium imitans].
ACCESSION   WP_284783608
VERSION     WP_284783608.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium imitans
  ORGANISM  Corynebacterium imitans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Corynebacterium imitans"
                     /db_xref="taxon:156978"
     Protein         1..178
                     /product="YceD family protein"
                     /calculated_mol_wt=18866
     Region          1..178
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 matnpfiinv aealhgdgmp vtihrtgesp srvgpemiai pqgqpvelea titplgagvl
       61 vdasvtaqle gqcvrclktl tpthtlsisq vfeaedgfiv gdeeteedkg sgdeirrien
      121 etvdveqafv deagltlpfn pvcepecagd tdvpapdgvs geennlvdpr wadlekfl
//
LOCUS       WP_284783816             440 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium imitans].
ACCESSION   WP_284783816
VERSION     WP_284783816.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium imitans
  ORGANISM  Corynebacterium imitans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 440)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 440)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Corynebacterium imitans"
                     /db_xref="taxon:156978"
     Protein         1..440
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46907
     Region          16..429
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mkkttvsyhp reqvtrtala vwwgavavyi vaifgrtsfg vasmdamarf evsasqiavf
       61 tavqvgvyaa aqvptglaid rfgprfmlvs gavvmaagqi alglttsygl alaaraligl
      121 gdataflsvm rilpywfppk ktplytqltg algqlgqfls avpflallga rgwtvafvsl
      181 galglifalv aalvvsdspe wsamtreqrr evhaqkraqr vplaftlrtv vrspiaweaf
      241 fihgwvifwm fsfsllwgvp lmtqgmglse aqagtalilf svgnviaapi mgvvsarlgv
      301 rrdlaslwig aivpiafavl faspeprgfg aalvvtsllg lcmpagnfgf dtlreylpae
      361 mvatgtglan mggfiacmig sqlvgvlldw saggaeftwh dfriawlaff gtaavcligl
      421 lvsrrkakrl trhvpivsrt
//
LOCUS       WP_284783818             444 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium imitans].
ACCESSION   WP_284783818
VERSION     WP_284783818.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium imitans
  ORGANISM  Corynebacterium imitans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 444)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 444)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Corynebacterium imitans"
                     /db_xref="taxon:156978"
     Protein         1..444
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46653
     Region          12..427
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 manvhpreql tskalfvwlg avtvyavail grtsfgvasv aaidrfevda sriavftavq
       61 vgvyaaaqip tgllidklgp rfmlvagavi mavgqialgl ttsygvalaa rvligagdat
      121 aflsamrilp ywfpprktpl ftqltaalgq lgqflsavpf lallgargwt vafvslgvlg
      181 llvailaaia vadtpewaem tpgqrreikq qkqesspamp lsrilgtvlr spvaweaffi
      241 hgwvifwmfs fsllwglplm tlgmglseaq agtvlivfta vnivaapvig alsarmgsqc
      301 dlaalvlgav tpvvwlvffa setprgfgai lavavlmgvc mptanfgfda vreqlpasiv
      361 atgtglgnmg gfvscmiaaq avgvlldhsa hgqtyqwadf qhawlafyvt aavllvgllv
      421 srrkakrids psvkivsaea pdar
//
LOCUS       WP_284783851             598 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Corynebacterium imitans].
ACCESSION   WP_284783851
VERSION     WP_284783851.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium imitans
  ORGANISM  Corynebacterium imitans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Corynebacterium imitans"
                     /db_xref="taxon:156978"
     Protein         1..598
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=66922
     Region          181..>514
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mtettaqqwl ndleaataqt dptvageaaa alfepegfwr dltamtwnly taegreeiar
       61 mvtathpdst itnteltevv degdgvtriq ftcetgnffc rgiarlrdgk awtllisgre
      121 lkdfpekrgr nrelgaqhgp qqdpenwadr rekrratlgi seqpyvliig ggqggialga
      181 rlkrqgvpal ivdkadrpgd qwrgryhslc lhdpvwydhm pylpfpddwp vftpkdkmgd
      241 wlehyvgimd ldywtnaevt naefdeeqkr wnvtlkrage eltlhptqlv fatgmsgvpn
      301 rpqlkgqedf ageirhsseh pggegdkdkd vvilgannsa hdiaadlvhn garpvmiqrs
      361 sthvsqsdsl mkhvfgplys edaveagidt dtadllfasw pykvlpdaqr pafdqireed
      421 aefyqaledr gfmvdfgddd sglflkylrr gsgyyinvga selvadgsip vhsptsiaev
      481 kersvvlddg telpadvivl atgygsmngw vehlidketa dkvgrvwglg sdttkdpgpw
      541 erelrnmwkp tqvdqlwfhg gnlhqsrhys rylslqlkar yegmdtpvye laevhhts
//
LOCUS       WP_284783878             253 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium imitans].
ACCESSION   WP_284783878
VERSION     WP_284783878.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium imitans
  ORGANISM  Corynebacterium imitans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Corynebacterium imitans"
                     /db_xref="taxon:156978"
     Protein         1..253
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27068
     Region          2..229
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(16..17,19..20,23..24,62,66..67,70..71,101,105,112,
                     115..116,121,137,141..142,144..146,148..149,152..153,
                     156..157,177..178,180..182,184..186,188..189,191..192,196,
                     199..200,206,208)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(140,144,147..148,150..151,191,194..195,197..202,
                     205..207,211,213)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(161..168,179,182..183,186)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mnlldginpv trilglallt tpllvsidwv satvaivatl vaaplcgvsf rrlarrgwpl
       61 lllapiagip malygqsgge vyfdygliqv selsvslawa itlrvlaval pvvvlsadvd
      121 ptdlgdglaq vlrlparfvl gsvaalrmlt llredveamr rarrsrgiad vnrvryafsl
      181 afgllvmslr ragklatame arafgrager twareskmha rdwvvlavcv llaavalgaa
      241 watgefrpvw avs
//
LOCUS       WP_284783911             346 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium imitans].
ACCESSION   WP_284783911
VERSION     WP_284783911.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium imitans
  ORGANISM  Corynebacterium imitans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 346)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 346)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Corynebacterium imitans"
                     /db_xref="taxon:156978"
     Protein         1..346
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=35554
     Region          59..346
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mtlrlrltlv lvatvfgaga vltalvcayl altpvplhvs lpgpegvlid aampiptsii
       61 tivlatmlva lalltalagl vgwfvagyal spvrriaava revsdgdvak rmhyegpadd
      121 vgdlahafdt mldslaasld aqrrfaanas helktpiati qtvadvalmq agdsdaqlvd
      181 alrrirevna ragqtverll afaraeaaqp gsltgqpvdl valckevcaq ygvslrapgs
      241 pvvvngdevl lrqavgnlvg navehgapgt aevvvgegrv gvenqgpald leeverlkep
      301 fvrgagrvag shglglslad aiarahggtl dlapregggl rvelsl
//
LOCUS       WP_284783989             338 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium
            imitans].
ACCESSION   WP_284783989
VERSION     WP_284783989.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium imitans
  ORGANISM  Corynebacterium imitans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Corynebacterium imitans"
                     /db_xref="taxon:156978"
     Protein         1..338
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36377
     Region          56..311
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrnsiygalg vgtlaalvta almlgfgprq itlaeehtgn aqlaaalerl araepghhtl
       61 salvydqgev tfgglgadeh tefeigsitk tfnaelvrql idedvitldt tagdildasg
      121 apidtvtike llnhtsglep mgplgigdil wanlteggna yrndspddil aaapemelkd
      181 rgkeaysnyg hallgqllar ttdtpyeelv rtrifepagm entyvagpeg vdkqqlgrgl
      241 asngraaepw dmngwapaga irstaadmar yikwvdehgr pdygwatlde ytfhnggtgg
      301 frtmlvwdpd kphravyvag dteawideig iellkeee
//
LOCUS       WP_284783987             166 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium imitans].
ACCESSION   WP_284783987
VERSION     WP_284783987.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium imitans
  ORGANISM  Corynebacterium imitans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 166)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 166)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Corynebacterium imitans"
                     /db_xref="taxon:156978"
     Protein         1..166
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17453
     Region          87..162
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtsdasrlda learvaales alagssdtps rdmdlpdlpt amralegcdn gavafggsvt
       61 tdsgtydyqw trptewvsah dwseqierla alahpvrgei lrhllaapat aadlvaaevv
      121 tstgtayhhl nalqaagwvd kehgafvlrp arviplmaii taaeah
//
LOCUS       WP_284784136             342 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Aerococcus urinae].
ACCESSION   WP_284784136
VERSION     WP_284784136.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..342
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39782
     Region          9..220
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mevnitlnrp kfsivipayn aekfissaie svlnqtyedw eliliengst dnttkicknf
       61 ltdkriklfh sekgvskarn vginqakgfw lifldaddql lsdalesylk idklyspeli
      121 igeytdnaad cslwmtkeyv geslrnilll clenpnqkcn vtavafrtsv irnnniwfdy
      181 kinyaedsvf flnvlnyakk vvtfcypvyh yvyssqstir sgkkkldrey ipaikkikni
      241 idvsdpmikn gwyifilnql liifvndifs rkkifirqmk dakkvmeieq fkiaiyksni
      301 skiqglkkiv fkmmklncvf glmiaskirq rqnkkkenqf yv
//
LOCUS       WP_284784148             612 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Corynebacterium imitans].
ACCESSION   WP_284784148
VERSION     WP_284784148.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium imitans
  ORGANISM  Corynebacterium imitans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Corynebacterium imitans"
                     /db_xref="taxon:156978"
     Protein         1..612
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67069
     Region          13..612
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 msqnayttel gftvppeenc lsqlielctt qphivlfsrp rnydwvnvta gefleevyea
       61 akglvasgve agdrvailsa tryewalmdf aiwaagaisv piypsssmsq iqwiledsga
      121 klaltetreh tqlissfllq ddgtprlags tsklqkiyef nasgvetlkf egrdveqsli
      181 darvaaithd higslvytsg ttgrpkgvel thgnwvhqtr alifndigev avpgkrvvtf
      241 lplahvlqra valalamaga tqshwsdtst ltvelqrarp nmvlgvprvf ekvrnaaynk
      301 aadgsavgkr vfleaeraai eyskaletpe gptrvqkakr kvfeklvysk lkeamggavs
      361 ygitggsams pelshfyrgm gipvyegygl tetcaaacvn nkvrqkigtv gppvngysvr
      421 inddgeiefa gpgvikqywn npeataeafd gewfntgdlg evddegfvri tgrkkdlivt
      481 aggknvspgp meeiirqdpl isnalivgdg kpfigvlvtl dedelarwka nrnipehrkl
      541 tdlaqdaslr aevqdainma natvshaeai kkfrildrdl seqenemtpt mkvkrnvvfe
      601 rfsedidkly er
//
LOCUS       WP_284784276             748 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Aerococcus urinae].
ACCESSION   WP_284784276
VERSION     WP_284784276.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 748)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 748)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 748)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 748)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 748)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..748
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..748
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=85557
     Region          10..748
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mseiknkske eviasceqym pedkvamikk acafaerahe gqkrksgepf fihptqvasi
       61 ladlqmdpdt vatgflhdvv edtgitlddi eyffsktiat lvdgvtklgk vkyrskeeql
      121 aenhqkllla mandlrvivv kladrlhnmr tlkwhrpekq vsiseetldi yapladrlgm
      181 sqikweledt clryinpeay yqivhlmnsk reereayida tidvlnkyvk piidgeydiy
      241 grpkhiysiy kkmhqqkktf deiydllair vlvpsvkdcy avlgivhtsw kplpgrfkdy
      301 iampkangyq slhttvlgeh gqpveiqirt fdmhevaeyg vaahwaykkg vtdkvetddl
      361 dkqlewfhri edlqddsdna tqfvesvked ifkdkvyvft pkgdvselps gaspldfayq
      421 ihtevghstv gakvngkivp lnyglhtgdi veiltsknsa gpsrdwvnfv vtnraknkik
      481 rhfklldrde niergreavi ktvkemdfsf nelfnkdmqa kclerfnfss iddlfaavgf
      541 gelsasavan kitenerkrr dkeehqskle dflqeeeerk nngqssrggk sermavrhnd
      601 givvegednv lfrlahccnp ipgdeiigfi tmgrgvtihr qdcqniqnmn evqsqrliev
      661 ywedaathnn sytveimidg fdrngflndi lqvitplvtn isnvngnvdh ktnnlkvrir
      721 iviqsldqle kiidriknvp dvydverv
//
LOCUS       WP_284784477             244 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            imitans].
ACCESSION   WP_284784477
VERSION     WP_284784477.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium imitans
  ORGANISM  Corynebacterium imitans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Corynebacterium imitans"
                     /db_xref="taxon:156978"
     Protein         1..244
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25414
     Region          6..224
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 maeqhravgv dtrgdvmral ltlgpvtatd iaeqlglsaa gvrrhldkll gddlaetcdp
       61 rvvageeatr grpakyfrlt esgrrsfgth ydglavdave mikqlggera vrdfararie
      121 kvlaeanaae cddsdaasgk eatkatveai aevldrhgya atvtsagngi qlcqhhcpvs
      181 dvasahpeic eaeheaisal vgthvqplal iadgdgictt niplaatata agthtersgd
      241 ndes
//
LOCUS       WP_284784579             315 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            imitans].
ACCESSION   WP_284784579
VERSION     WP_284784579.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium imitans
  ORGANISM  Corynebacterium imitans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 315)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Corynebacterium imitans"
                     /db_xref="taxon:156978"
     Protein         1..315
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34537
     Region          41..308
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 maelepevrq anlafallgs prrrdtawvg shvdgyqhrs realnvqvrr dvealrlagv
       61 pvryrdgqls ldreryelap vdlteeeasv vglavdlsqr gslgafarsg wtklaasgat
      121 rtfdsaplas aahdatqldp dafhqllgai rhnlrahfdf hvpgsgrvqr rtvdpwtivs
      181 lntraylvgw dvdrdaervf ratrisdvtl vrdttdfhsp tgdageivre llrgpvtdar
      241 itvdsgsaee laakgtrepg pmpetdtlvl rqverdwvvr ttaahaldvr avepedirrd
      301 vlallrqagg gdhgn
//
LOCUS       WP_284784808             256 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Aerococcus urinae].
ACCESSION   WP_284784808
VERSION     WP_284784808.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..256
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=29115
     Region          14..255
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 mnktkqente tsndelhidl aafegpldll lhlikqmevd ifdipivdit nqyletihrh
       61 qkrdlelasd ylimaaslie iktklllpkk amekeeeddp radlvqqllt ykqykavsai
      121 leekqadrsl syskeasdls dlqavvplpe nevssedlls afkkmflrlk qeqplertvk
      181 getftideai tsieealdqe sdhlsffsll ssnqpnrekv vtyflallql vkqgkiliqq
      241 dqiaadisiq kkddgd
//
LOCUS       WP_284785428             506 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Alloscardovia omnicolens].
ACCESSION   WP_284785428
VERSION     WP_284785428.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..506
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=56022
     Region          14..506
                     /region_name="COG3920"
                     /note="Two-component sensor histidine kinase, HisKA and
                     HATPase domains [Signal transduction mechanisms]"
                     /db_xref="CDD:443125"
ORIGIN      
        1 mndfnslisk tpgydvqdkk qlhsliadwq iiadltfsdl lliippdmdd sddvskfiva
       61 aqcrpstail riesdwvgen peteliplle ntwrtnnmsr mdhyrvvdgv tvcdvatpvi
      121 rnnrviamvv retnmdtrgd ngyyemssig vgkqlfymit ngdfpyenrl slargkyrrh
      181 dprvadgfvv ldadgmvmya apnaiscfrr igvtgnmvgg yfsefvldhv dqqeklpeal
      241 pmvlmgkaaa aavleargav vsmrslplda dgkrtgalvl crditelrwr erqletkdat
      301 isevhhrvkn nlqavssllr lqarrtksee vrkeleeaqr rietiavvhe glsqtadeiv
      361 dfdavisnll rmsvdlasak dqhidisyvg kfgmlpaqda tplsliltel vtncvehgye
      421 nlqsghinis igragnsldi vieddgegid aeadadmmsa kssgsglgtq ivntfvkndf
      481 ngsirwlpgr dggtriemkm vlrate
//
LOCUS       WP_284785736             217 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium imitans].
ACCESSION   WP_284785736
VERSION     WP_284785736.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium imitans
  ORGANISM  Corynebacterium imitans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 217)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13031065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Corynebacterium imitans"
                     /db_xref="taxon:156978"
     Protein         1..217
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24130
     Region          68..206
                     /region_name="SpoU-like"
                     /note="SAM-dependent rRNA or tRNA methylase related to
                     SpoU; cd18096"
                     /db_xref="CDD:349969"
     Site            order(141,143,163..166,169,183..184,186,192..193,195,198)
                     /site_type="other"
                     /note="putative SAM binding site [chemical binding]"
                     /db_xref="CDD:349969"
ORIGIN      
        1 mpeqpakgpt ewnegrhgvg pwegplpdda rldpelltng drrnvvdayr ywsmdaivae
       61 ldarrhpfhv aienfendmn igtvvrtana flakevhiig rkrwnrrgam vtdryqhirh
      121 hesvedfaaw areedipvva idntpgcvpl etaelpercv lvfgqegpgi teetqyaasm
      181 tcsiaqfgst rsinagvaag iamhawvrqh adlgqaw
//
LOCUS       WP_284785960             266 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Corynebacterium imitans].
ACCESSION   WP_284785960
VERSION     WP_284785960.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium imitans
  ORGANISM  Corynebacterium imitans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Corynebacterium imitans"
                     /db_xref="taxon:156978"
     Protein         1..266
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30488
     Region          3..238
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 msttlwavsd lhaavkrngp kidaiqprdp sdwlivagdv aerldlivrv meqlaqrfdt
       61 viwapgnhel fsrsadryrg rdkytalvqa mreigvitpe dpypqfggvt iaplftlydy
      121 sfrganmtve eaieaahekn ivmtdqfaia sfvdvrawcw drlayttkrl srisgptili
      181 nhwplvqept lrmqwseial wcgtrhtrsw pqrynaqavi yghlhmpgvm eidgiehiev
      241 slgyprewer fprrhpfpyp vmevga
//
LOCUS       WP_284781508             386 aa            linear   BCT 25-DEC-2024
DEFINITION  NRAMP family divalent metal transporter [Corynebacterium sp.
            UMB4614].
ACCESSION   WP_284781508
VERSION     WP_284781508.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB4614
  ORGANISM  Corynebacterium sp. UMB4614
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Corynebacterium sp. UMB4614"
                     /db_xref="taxon:3046334"
     Protein         1..386
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=40258
     Region          1..378
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 mgamflmats aigpgfitqt svftvqlgaa fafailvsil vdiaiqlnvw rvlgvsgmra
       61 nelgnavvpg lgwvmgafvf vgglifnign iggaglgtna mlgvdpiigg aisalvaalv
      121 flskwagaal drivvilgal millmiyvai vsappvgeal kqtvvpdqid fviittligg
      181 tvggyitfsg ahrlidsglt gpehakditr vsvtgilvtg vmrtllflai fgvvasgval
      241 sgdniaadaf raaageigvr ffgivlwaag ltsvigasft svsfvttqki aprtrnlltl
      301 afilvcavay vilnqapqkl lifagafngl ilpigfgvvl wvawrrrdll kgykypvwlw
      361 sigaitwllt lwlgwrslsg ivamwa
//
LOCUS       WP_284786345             116 aa            linear   BCT 25-DEC-2024
DEFINITION  FluC/FEX family fluoride channel [Corynebacterium imitans].
ACCESSION   WP_284786345
VERSION     WP_284786345.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium imitans
  ORGANISM  Corynebacterium imitans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   McIlwain,B.C., Gundepudi,R., Koff,B.B. and Stockbridge,R.B.
  TITLE     The fluoride permeation pathway and anion recognition in Fluc
            family fluoride channels
  JOURNAL   Elife 10, e69482 (2021)
   PUBMED   34250906
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Li,S., Smith,K.D., Davis,J.H., Gordon,P.B., Breaker,R.R. and
            Strobel,S.A.
  TITLE     Eukaryotic resistance to fluoride toxicity mediated by a widespread
            family of fluoride export proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (47), 19018-19023 (2013)
   PUBMED   24173035
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Stockbridge,R.B., Robertson,J.L., Kolmakova-Partensky,L. and
            Miller,C.
  TITLE     A family of fluoride-specific ion channels with dual-topology
            architecture
  JOURNAL   Elife 2, e01084 (2013)
   PUBMED   23991286
  REMARK    Erratum:[Elife. 2013;2:e01700]
            Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Corynebacterium imitans"
                     /db_xref="taxon:156978"
     Protein         1..116
                     /product="FluC/FEX family fluoride channel"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:1903425 - fluoride transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:1903424 - fluoride transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11897
     Region          19..103
                     /region_name="CRCB"
                     /note="CrcB-like protein, Camphor Resistance (CrcB);
                     pfam02537"
                     /db_xref="CDD:460582"
ORIGIN      
        1 mdllvvagif iggflggiar walaripapr vdtwaanmva csvlgfvygq gmlvamavgt
       61 gfagalstws tlakelgqli kdkdysealr yalasallgl vaagfgmrwg arafga
//
LOCUS       WP_284786466             401 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Aerococcus urinae].
ACCESSION   WP_284786466
VERSION     WP_284786466.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..401
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=45626
     Region          160..384
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mtylledgka flpgaiqsil mtillvslff pfyitivvfg vvftlllatg mlsakhwpdd
       61 plitslfsfp fyaflisivh enwvgglisv gllialiysi yytkqvrpdy lteivnitli
      121 asiiififtl lehfdiisew dytfispamn kvhpdrveat ffnpnyfamm leffiviamy
      181 rmkttkhlak kltclfliac nllaivytgc rtsaiviiga syvffyvigy kktaiysllg
      241 lsilgliawg mglmprfddl ayafsdrfdi wqtgwqafkd nvwfgqgplt ymhvyseytt
      301 kytqhahnif ldtllsygii essllvyply rlgrmlnemr ryasirpela licsllsvvl
      361 ihgltdvtif wiqtagllma ivlvgpnllk takekanhle e
//
LOCUS       WP_284786692             165 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium marquesiae].
ACCESSION   WP_284786692
VERSION     WP_284786692.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 165)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..165
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17698
     Region          86..161
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mesiesrvla leervakleh atptpieasa destmwlada lepseelpkg svifggnlti
       61 gensyiyqwq qpteavthgd wsenldrlaa lahpirsail rrlltapasa telveeeivt
      121 stgtayhhls altsagwttk aggkyairaa rvvplltiit aseah
//
LOCUS       WP_284786868             260 aa            linear   BCT 25-DEC-2024
DEFINITION  inositol monophosphatase family protein [Corynebacterium
            marquesiae].
ACCESSION   WP_284786868
VERSION     WP_284786868.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..260
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=27057
     Region          5..253
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mmeprelvaf aeaavdqvep ifrsglgaap arfkgqgdfa tevdlvieqq lrdiltqmtg
       61 ipvygeesgg svldtvwvvd pidgtanysa gnpmagilva lihegspvaa vsdfpllgrr
      121 lvtcdgaplr svggpttgfg ggddamgfde arghvgcssh lpteifhelr etglrprmtg
      181 svgldnafva qgvfdgainf sphpwdnaag alqiqaaggv vtdpegnswt aqsrgmvagt
      241 pqvhatildi lsrhtgsfhr
//
LOCUS       WP_284786913             402 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Corynebacterium marquesiae].
ACCESSION   WP_284786913
VERSION     WP_284786913.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..402
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43443
     Region          1..396
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 manllgivff algigltval heaghmltar afgmrvrryf igfgprlfsf rkghteygla
       61 afpvggfcdi agmtaqdefl teeeephamy kkpwwqriiv maggiavnli lgfvilyfva
      121 mtaglpnpda dvrprvgevt csanqkpnqe letctgkgpa gkagvqegdi ivaldgqkld
      181 sftqlrdevm qrpgetitlt verggedrdf tvhldtvkrl nqdgelvdag siglsnqlid
      241 vvekhdavda lpatwrfsty slgatvdglk qfpgkipgvv asifgherea dgpmsvvgas
      301 rvggelaers lwsmffmmla tlnfflalfn liplppfdgg hiaviiyekl rdgirklagk
      361 palgpadytk lmpvtyvmag llmgvgvivi vadvvnpiql fd
//
LOCUS       WP_284786986             847 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium marquesiae].
ACCESSION   WP_284786986
VERSION     WP_284786986.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 847)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..847
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=94729
     Region          19..841
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mnlsqllpdl tevpeslvde aiwdtftswt tgrginlypa qeeaslgila gdnvilatpt
       61 gsgksmvana ahfialargq rsfytapika lvsekffalc difgaenvgm mtgdatvngn
      121 apiiaataei vanialrdga eanidqvvmd efhyysepdr gwawqvplle lskaqfllms
      181 atlgdtqwle edltrrtgra tnlvagstrp vpldfsyvfs avhetieell adkkapiyvv
      241 hfsqreaaer aqaltslsgi itkdekeaia qeiggfrftt afgkdlskll rkgigihhag
      301 mlpkyrrlve rlaqkgllkv icgtdtlgvg invpirtvlm tglakfdgqr qrilksrefh
      361 qiagragrag ydtegtvvve apeheienak errrigddpk rlkklkkksa regevswsek
      421 tfarlteaep eqltsqfrvs nsmllnvlar hgngydhmrh llrdnhdnrs kqnkdiltal
      481 dlfrglvdsg vvqkstkgld iygrpyhlvr elprdfalnq plgpfalaal slldpeaety
      541 nldvisvfea ilddprqvli aqqkqrrgee iaalkadgvd ytdrmnived itwpkpleel
      601 leqaydtfaa tnawvkefel rpksvvrdml enamtfsdlv atyglarseg vilryltdaw
      661 rtlkqsipde yntpelediv vwlgelirqv dsslvdewaq magedspidq dtvdrelafg
      721 vedptaltan rraftimvrn ymfrlvqlfa lekeerlael ldyldevpdf gailddyfde
      781 yddidsgpea rgpeyfrlsd tdsrawsvrq iikdpdgdha yqfvatvdld asdeagevrl
      841 adlrvey
//
LOCUS       WP_284787164             407 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Alloscardovia omnicolens].
ACCESSION   WP_284787164
VERSION     WP_284787164.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 407)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..407
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=45256
     Region          94..407
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mlkklrlrft litalvvlii tiapisvlnf vshwesgret svllrlinfh kgmlpaesvd
       61 gesehyqyfs vyrsssgevs vtskrnldnv sdtqissaae tlldslstag tviiadqsfs
      121 yqvvsesdgl rlsavninaq lanrsrlfhi siamflvalf ffisvaaiis kwavqpfven
      181 ykkqkrfitn aghelktpla iisantelqe mmegesewsa stkaqvermt alinqmvsla
      241 rleeqpdmtl gdvnfsetvq naassfkssi mrdgktfhmd vaeginikae aksafelvni
      301 lvdnankycd dggnvsvllr ksrdprysah levantyvdg kgknyshffe rfyrddesht
      361 ragssesekt tsgfgiglnm aqsmvklfkg ridvrysedt iifvvrl
//
LOCUS       WP_284787276             344 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Alloscardovia omnicolens].
ACCESSION   WP_284787276
VERSION     WP_284787276.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..344
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39161
     Region          5..194
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 madktisfvv psynvedyla rcvnslldts dtsdveiiiv ddgsrdgtai ladtfaeryp
       61 dvvrvihqtn aghggacnag iaaatgqyik ivdaddwids vayvtyitfl rsqamasqpv
      121 dlvvsnysye niakrhtrti ryknifeant rltwddmnpc riqqyllmht ltfrtevvra
      181 sgmvlpehtf yvdfiyafqp lpwvktltyl nidlyryfig regqsvqkdi miqrvdqlik
      241 vnkimveamp argevsdgly rymlhylssq fmvtsvfltl akdpkrleqk dqiwanlreh
      301 seelyndlra qeitarimti pgkfgrglvr tgyaltnfav gfns
//
LOCUS       WP_284787476             433 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Alloscardovia omnicolens].
ACCESSION   WP_284787476
VERSION     WP_284787476.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..433
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48651
     Region          6..>146
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mtstaqptvs iiipaynkek yigacldsav qqtlntieii vvddgstdnt saiisdyahs
       61 dsriihlahg vnkglhttrl tgvaqasgly tmfldaddtl altacetlyn fassrpdadi
      121 irygahveva dtedsslgtr veslfnatlg dcshaqilqa sfsppfaawv pwniitaffk
      181 tsliqeafkn lsvtrlnkie dgyeylaics lshklysyve yrglnyhfgr gissrtttsl
      241 difdrdqhsa wevdqevqaf sthysstein saarnfhara lkivgddfve rlasndyseg
      301 lrilqitwgk nnaylalhrh inshlydelt kdafpptanf alwsdlfsea iaethlelse
      361 eeqathastl yileqirtrt aqreaerqrv iyeeslrifk tgtkaryyfd kfiplgthrr
      421 glarrlakli lhr
//
LOCUS       WP_284787556             207 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Alloscardovia omnicolens].
ACCESSION   WP_284787556
VERSION     WP_284787556.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..207
                     /product="YceD family protein"
                     /calculated_mol_wt=22102
     Region          8..202
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 marehatpws vsisqlslkp gnsqdisdlv vpapsgigds lvgiaegsdv tvnarlesla
       61 dgilltgtis adfdsecmrc lepihetitv npvvfytyek dlsaasssga sgssseeevd
      121 iiasqdesnd typlspdsiy lnleslirdq laqalplqpl dredclglcs qcglnlnenp
      181 dhkhdvvniq waalegfkaq leaqeee
//
LOCUS       WP_284787691             394 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Alloscardovia omnicolens].
ACCESSION   WP_284787691
VERSION     WP_284787691.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..394
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42475
     Region          3..394
                     /region_name="FucP"
                     /note="Fucose permease [Carbohydrate transport and
                     metabolism]; COG0738"
                     /db_xref="CDD:440501"
ORIGIN      
        1 manlllgviy lafislglpd slmgsawpsm ypafhvpvsy agivtfiitl gtiisallsd
       61 rltyklgagk vtafsvaata iallgfslap sfwivclwai pyglgagaid aalnnyvalh
      121 ysnrhmswlh amwgvgtvis pyimayaiaq qhqwqlgyry isfiqigitc ivfaslpwwa
      181 krgaqsehss eteqsdkads aplgliatlr lpmakeilfm flaycgiegt aglwvstfam
      241 qargitaeda atwasyffig itvgrlacgf iaerftdsqm irlgcivlga givvtmiptp
      301 wnpltmigli vigvgcapiy psiihstpai fgeqhsqami gvemasaytg nlvlpplfgi
      361 iarnisavyl pvyllilfii lcgmhelivr kmsk
//
LOCUS       WP_284787697             785 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Alloscardovia omnicolens].
ACCESSION   WP_284787697
VERSION     WP_284787697.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 785)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 785)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 785)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 785)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 785)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..785
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..785
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=87957
     Region          33..771
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 madtnftqhd anaptsrilg aeissdplnp llpiiqvctf hhpdadtdll qrayeravvq
       61 hapqrrrsge pyiihpiava qiladlgmsp kviaagllhd tvedtdftld qcreefgdti
      121 aglvdgvtkl tkmdvgdsaq aetirkmiva msrdvrvlvi klsdrvhnar twryvkpksa
      181 ykkaqetidv yaplanrlgm naikteleel sfktlqpkiy deivelvrhr agqrelylqq
      241 iiadiredld eqnvhasing rpkdyysiyq kmivrghdfg diydlmgvri ivdsirdcya
      301 algavharwn pvpgrfkdyi atpkmnmyqs lhttvvgsgg kpveiqirtw dmhrraeygi
      361 aahwkykeng ragralsapd kqdaergkki daessdffeh dnlqwikqla dwqsevpdsd
      421 eflgflkddl gasqvyvftp kgkivsvpqe gtpvdfayav htevghhtmg aringrlmpl
      481 dtklqngdtv eiitsrgena gpshdwlnfv kspkarnkir qwftkerrte nmeegrdelt
      541 ralrkrnlft qnytrlevfv avaddlgypd vdslyiaige gqvstqnvit hilkfvddda
      601 despeqnivp lrrrsgsgpr rtksvgvsvk gvddvwvkla kcctpvpgdq ivgfvtrgag
      661 vsvhredcvn vaslkknqpe rlvdvswtsa qgvflvkiqv ealdrgrlls diarvlsdag
      721 vnivagtist gddrvaisqy sfemadmshl nqllasirki dgvfdvyrlt gtkddsklri
      781 rhidk
//
LOCUS       WP_284787763             307 aa            linear   BCT 25-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Alloscardovia omnicolens].
ACCESSION   WP_284787763
VERSION     WP_284787763.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Bagautdinov,B. and Kunishima,N.
  TITLE     Crystal structures of shikimate dehydrogenase AroE from Thermus
            thermophilus HB8 and its cofactor and substrate complexes: insights
            into the enzymatic mechanism
  JOURNAL   J Mol Biol 373 (2), 424-438 (2007)
   PUBMED   17825835
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..307
                     /product="shikimate dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=33402
     Region          14..288
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 mnadntssst gnqaavlgsp iahslspvlh naayealqlt dwqygrhdit aetledffls
       61 indswagvsm tmplkqkale fgevsderva flgvsntavf dwqrsnpqhe nmphislynt
      121 dvdgvkltfa defnivnasd vrvciigsgs tamsamaali eigardfvic aadaeqasam
      181 rtkmssyqks qahidvqpwg savkhiqqsd iiistvpaha tdglaqeinn laanisltnk
      241 hlldviydpr ptqlmqslsa reaivrggeh mllrqalaqv aymthlpvrh vidtafahmk
      301 talfeql
//
LOCUS       WP_284787781             440 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium
            marquesiae].
ACCESSION   WP_284787781
VERSION     WP_284787781.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..440
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=47346
     Region          1..438
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrmtvigtgy lgathaacma elghevlgvd vdenkisalk sgkvpfyepg lpevlernie
       61 agrldfstdy eeaaefgnlh flgvgtpqrr gsyaadmtyv kavitdlvpk lkgdhiifgk
      121 stvpvgtaae lqelanelap egttveiawn peflregyav kdtitpdriv lgvregesra
      181 eevarevyaq plsqdtpfiv tdwqtaelvk vsanaflatk isfinavsei ceiagadvta
      241 ladaiglder igrkflgagl gfgggclpkd irafmarage lgadqaltfl revdainmrr
      301 rdrvvdlake afngsllghr vtvlgcafkp nsddvrdspa lsvagslsla gaavtvydpe
      361 gmdnakkvfp tldyaantdd alreaelvil atewkqfkel dpqqagqlvd nkhiidgrnv
      421 lpvadwqqag wkvealgrtl
//
LOCUS       WP_284787924             317 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Alloscardovia omnicolens].
ACCESSION   WP_284787924
VERSION     WP_284787924.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 317)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..317
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35314
     Region          11..317
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mtralrsgge stayqkkkls plasfkrhte lywqlwllva palifvlvfa yipmwgiqla
       61 frefdpdkgl tggqwvgfsy fekffnsplf geimgntiri slwtlvmgfi apiilallin
      121 qisspkikgf vqtitymphf isvvvivsmi nifltpktgi lgqffgdtsi lgdthvitav
      181 ywiseiwqhv gwnsiiylaa lssvdtslye aakidgagrf qliryvdipa imptmtvlli
      241 msmgsilgvg fdkiflmqns lnlpatevis tytykigiln sqfsystaig lfnavvnflf
      301 livanfiskk atkssif
//
LOCUS       WP_284787925             121 aa            linear   BCT 25-DEC-2024
DEFINITION  Rieske (2Fe-2S) protein [Corynebacterium marquesiae].
ACCESSION   WP_284787925
VERSION     WP_284787925.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..121
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=12621
     Region          34..118
                     /region_name="NirD"
                     /note="Ferredoxin subunit of nitrite reductase or a
                     ring-hydroxylating dioxygenase [Inorganic ion transport
                     and metabolism, Secondary metabolites biosynthesis,
                     transport and catabolism]; COG2146"
                     /db_xref="CDD:441749"
ORIGIN      
        1 mikcsrrmfl lgtattfaga yaaacgssps aeiaateipi gsakivdgvi ftqpkegefk
       61 aysqtcphqr npiteidgmt atctahntsy nlsdgsvisg pgrdpleeye vkqdgsnvtt
      121 v
//
LOCUS       WP_284788067             195 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Corynebacterium marquesiae].
ACCESSION   WP_284788067
VERSION     WP_284788067.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..195
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=20834
     Region          1..191
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mrlilasqsp srasilrgag vepvlepadi dersleasla ghppadivaa lasakaekva
       61 eryptepvig gdsmlllddq lqgkphteea tierwhqqag rtaelltghc lifgnkrhve
      121 tstttvhfaq aseadiaaya hsgeplhcag aftleamggw fidriegdps sviglslpvv
      181 rralyafdln vsdfw
//
LOCUS       WP_284788104             225 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsB family cell division protein [Alloscardovia omnicolens].
ACCESSION   WP_284788104
VERSION     WP_284788104.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..225
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=24957
     Region          97..182
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 masrhrtsss rstssnrsss sartarsrss vsrsatrdel rdimnsrnsr ksqnesqgrt
       61 arressgkkr seqklsarss saknlavart prgglsfflg iiifllaaln iglvfksyaq
      121 nlgqlnalrn qeaeliqkka dlendisrws ddayvtarar krlgfvfpge rsvlvknapq
      181 daqhdsteek srtedkklpw yneilyames tdraenpnga tsqaq
//
LOCUS       WP_284788170             328 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            marquesiae].
ACCESSION   WP_284788170
VERSION     WP_284788170.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..328
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35336
     Region          13..323
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 maahnpapkr hdeaverltn lsfalqgaan sggspdrtaa wirshvagyg dksdeafaks
       61 lardiatlqr agvpivhsgg edgaryrlda ssyqlppvef speeamvlgi aggvgttggl
      121 sdfslsgwtk iaasgasrnl agapvytavn ditrlapeii tsvlaavrnq vritfsyran
      181 patepvrrvm dpwgvvnrds riylvgfdvd rneprvfral rvsdikrshd paehpnpten
      241 lqvlvervlq rgekvdarlv ipdgqarelm dageqqsdgt vllhkvdkdw lvrtaagyap
      301 evqvlepagi rqevisllhk asqsqeeg
//
LOCUS       WP_284788217             230 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium marquesiae].
ACCESSION   WP_284788217
VERSION     WP_284788217.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..230
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24077
     Region          1..227
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(13..14,16..17,20..21,58,62..63,66..67,91,95,102,
                     105..106,111,126,130..131,133..135,137..138,141..142,
                     145..146,165..166,168..170,172..174,176..177,179..180,184,
                     187..188,194,196)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(129,133,136..137,139..140,179,182..183,185..190,
                     193..195,199,201)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(150..157,167,170..171,174)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mqglhpatvi tiaacgwilt lalntpmasa svalialacg taatrnasvi lttvalsapa
       61 alsmlvihap ygddpvlplv tsdglvlaat ltlrfcalma cfiaamavlr iadiakwlqv
      121 sraghkvayi vgaslqtlpq gahawrcvre anqlagitvt wrntisrvii pviarlltqg
      181 tqrgqalaav gfdqegqrtl lrpvadsmvs rvirlviplv sfavvittwi
//
LOCUS       WP_284788240             325 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Corynebacterium marquesiae].
ACCESSION   WP_284788240
VERSION     WP_284788240.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..325
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34468
     Region          2..319
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(40..41,45,118,122,125,143,146..148,167..168,172,187,
                     210..211,232..236,257..260,307,309)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(130,225..226,239..244,252..259,262..263)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mhaiqvtetg gpevlrytev paptpnddev lvdvimagvn yidtyyregi ynaatpfipg
       61 fegtgrvvhd pqgeiaegtm vawnqafgsy aeqvcvpreg lvavpddfqp evaasmllqg
      121 itahylahgv yqlgegascl itagaggvgq iltqmasslg atvytvvstd ekeelsyaag
      181 adkvfrysdg laeqvrryng drgvdvvydg vgkatfhesl eavrprgtva lfgaasgpve
      241 pidpqllnkh gsifltrpsi gawtaqegef qmraqavvqa vidgdlsfnv tasypledaa
      301 aahrdlqerk ttgsivlrvq agdka
//
LOCUS       WP_284788560             253 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Alloscardovia omnicolens].
ACCESSION   WP_284788560
VERSION     WP_284788560.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 253)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 253)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..253
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=27978
     Region          1..240
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mvkialvedt dvdaahtqqa ierfahsenv gievqryksa edfladerac sadmifldie
       61 mpgedgtgmd gmtaasvyre tleehgskpi ifttkvtqla vkgyevsaig ylvkpfdyat
      121 faltmkrala rvemnsrdvm vtlpssdgth fissrnityi evrdhmvyvh dangavyvvw
      181 gtlkeyaall epvdfvqchr yclvnlhfva gftdkeliie adktytvgms rgkkvavfda
      241 llavksaath msk
//
LOCUS       WP_284788668             681 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Alloscardovia omnicolens].
ACCESSION   WP_284788668
VERSION     WP_284788668.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 681)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..681
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=74314
     Region          197..628
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mgkstdktap msskkrsfls niqwklscip laarlmtlvl aflivassvl vlasrqlvss
       61 almqktdtql mrqatlvinn idllqsenas dqkssseqsp slgnqlkeqf fknsdtasqk
      121 rpspysttgn qnlgptdyfv qirdndnnvl stplipiahd gvesiptlpq egksatflyg
      181 epttvaasvh vsknvslter qaimahspwr viaaqyvnra tgmeyvvyig lslfdvndti
      241 qaltvyfvws avgivitagf lallavrrsl rplkkmeqta ekiaagdlsq rveraplnte
      301 igslsnslnt mlsqiersfk kqeditlqmk rfvsdashel rtplavihgs telykmqrks
      361 pqadpvesad mvidhidkss trmsalvedl lslarldegr gidlaqtvhm tdilsdsved
      421 lhaldperti tlgrlsldmg simqsvqpvq gqndthsdeq vtdntlafip gqlphidagg
      481 dpvrmrqvmt niignihryt psdspvevga tvvrasalvr dleneastae tldkflkdvk
      541 esgtasntle yviiqirdhg pgvkdeaytk iferfytadp srardkggtg lgmsivqsiv
      601 kahhglicam ktpggglttt vvvpisqtvl fsstnptqer mrekntapai fgrrkksada
      661 dmatteikis igsnkdtstk k
//
LOCUS       WP_284788688             486 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Alloscardovia
            omnicolens].
ACCESSION   WP_284788688
VERSION     WP_284788688.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..486
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51365
     Region          2..481
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mtydydvlii gsgpggyata lrtselglst aviektdvvg gtclnrgcip tkayltaaht
       61 lhdvhragsw gldisvnsid mpalktakde tvagvvkglt qhmkarsidi ihgegslsga
      121 hnvsvtdges trelsahhiv latgsyatpl pgfdffhets aavseaiadk kvpvlssdea
      181 ldldiplnni vvvgagaial elaqfwnalg thvtvllrkd tplsrwdshv sstlmrtlkr
      241 dgvrfeshst ltgagdgevt ysiadpkkdt vtektipadf vlaaigrspr ttaswfkqag
      301 ialtstnrvi tdeygrtnle nvwavgditd gymlaheafe qalvvsesia glptqpvdpl
      361 tipqvvygmi davsigytss qaqnagfeqv eetvvpqlsn prvamlgsng ttvivsalns
      421 ektervvlgv hmagpqasei agaareiiqn riplsqaart lfahptises lgesllkadg
      481 rplnvr
//
LOCUS       WP_284788721             212 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Alloscardovia omnicolens].
ACCESSION   WP_284788721
VERSION     WP_284788721.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..212
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23829
     Region          6..195
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mlkryvvwdm dgtlidsmem wtnlvgeyle sqdispvdha qlvkqldmlt vsegtallsq
       61 hfprlgspra ieqqidalle chyredlvlk pgveqalrcl srkdvhmcva sataepliqa
      121 clarlgvlhh fdfllscetl qtskrepriy leaakrwavk psdiavceda yhaletahka
      181 gfytvavfdq snanqwadcl kiadesiink ee
//
LOCUS       WP_284788763             301 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Corynebacterium marquesiae].
ACCESSION   WP_284788763
VERSION     WP_284788763.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..301
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30994
     Region          51..164
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 msqrivaalt aaalglsapv ahaaepqwes sapeslgind pscvpsgdit epvvllhgts
       61 nnasvwgnlv hllqdqgacv wafdygaddv tlqnmipsvk aiadlddsaa eiadqvdyvr
      121 evtgsdkvnl vghsqggmhi ktytqmydga ghvshavvlg gnfhgttlng qgetlskfia
      181 faphlaafla stagiqqvvg sefmkrlnal pdtapgvlyt siyspgdttv tpnsssqlal
      241 gdgadvvnld lgevcgvapr hdklptnwtv lsqvifgltr apgegpnpst cvsegvpisg
      301 a
//
LOCUS       WP_284788913             473 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Corynebacterium
            marquesiae].
ACCESSION   WP_284788913
VERSION     WP_284788913.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..473
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49514
     Region          1..449
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mdslnsilsa istvvwgpfi liplllgtgl wltirlgglq fralgramrh ifatdsddes
       61 tegdisnyqa lttalaatvg vgnivgvata lsiggpgalv wiwitglvgm askyteaylg
      121 vrfrttdskg emsggpqqyl krgipgplgs vlavffaifa icasfgignl aqanavatnm
      181 estfgiapaa tgailfvlvg svllggiqai gritaafvpl miivyvlggl yvifshatei
      241 paafamifsd aftgtaadgg fvgstimmai qygvargifs nesgmgsaai aaaaaktphp
      301 arqglvsmtq tfidtiivvt itglvivvgg twdmgrdeag imtaeafsrv lpgdwggtiv
      361 slsiiffafs timawayyge rsleslcgrk asipyrmffa cllfvgsvse lelawtfsdl
      421 angliaipnl igllllsglv aretkaylaf dpklnkpvde vrafvesqgm nwk
//
LOCUS       WP_284788965             486 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Corynebacterium striatum].
ACCESSION   WP_284788965
VERSION     WP_284788965.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..486
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=54768
     Region          32..444
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 msdkhiydci ilgtgygglg mgaqlakdsi enflileaad evggvwrdnt ypgaacdtqa
       61 liycysyfln lgvsrmfagq demlgylkel atefglyehi kfnnrivrse wneerkawei
      121 atstgdiyyg rvfvgawgql skpkvpdfag retfegtqfh saewdhtvdl kgknvavvgn
      181 aasavqlvpe vakeaghlav fqrsanyilp rnqviftdee lrefqenpes yrairqeihd
      241 tredgfertr kgtdaaqegv eqamehltsq vndpelvkkl tptfafgckr ilrsddfypt
      301 fnrdnvslvt egieeitpqg irtadgvehe fdviiyatgf ysqefqgdlp vigrggldlr
      361 erwgnapeay lgmtvdgfpn ffmlygpntn lnhhsvvaml eeqdkyirqa veylrdnpdk
      421 vldvdpqvlr efndriqadl nesafsadcs swyknedgkv innwsgnvae yqdltrtlel
      481 adygva
//
LOCUS       WP_284789055             402 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Corynebacterium striatum].
ACCESSION   WP_284789055
VERSION     WP_284789055.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..402
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42993
     Region          30..224
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 maddkntstt qrvklstreq lrsvdrsmks rfarvksrfm filqstlgag laffvahvvf
       61 ghsqpffapm sviiilglsg sdrlkravdl siggivgviv gtllvdgvgt gpvhmtiiig
      121 cslliasfvt ssqlvsnqia igailiatim ppaemgglsr aidaiigavi gismvalipt
      181 splrgvrkei skvlrvassv lfdvaeglra ndprtilear davrgtqgdi nsmlnaakgg
      241 aetvkvspfl wsrqrnvksl eriltpvdna vrgvrvlsrr alvlaedgdh vtdeqielid
      301 elsdvtmels elyaqessne sraneavvip eivrklrilg arstmevige dgvlsaysll
      361 aqtrsiivdl lmvcgmsres avaqlaptsd hpayppevwd ge
//
LOCUS       WP_284789160             227 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Corynebacterium striatum].
ACCESSION   WP_284789160
VERSION     WP_284789160.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..227
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=25142
     Region          1..223
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mlfdvsrpat riapgvahvp gwvdvakqra lveetrevar ryagtpmamy qpqlksgkms
       61 vhqlhlgryw hyetyryvdn iegtrvppml vslqeiarpa lraaaevspe lepwvetfyp
      121 emalvnyypp gsgmgmhvdd feeslapvis lsigdealfr igntenrnkp rddvtlssgd
      181 livfggpkrl ayhgivrvnd atlpegcglk egrinitirq vgaratl
//
LOCUS       WP_284789171            1103 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Corynebacterium propinquum].
ACCESSION   WP_284789171
VERSION     WP_284789171.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1103
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..1103
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=116194
     Region          198..344
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          550..1049
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 msvkstsprn trggserkka rsnstrpapr srtsrtetkp sgsaastrag gkptrdsvtk
       61 vepthpetav fgsshraant shertgsafr avgsgigavf sktaealtkf gnigqsdedy
      121 deyaeydddv vanrgshgkl dedlysadtp dssvkqkkpa kktessvrsn petsdtdelg
      181 devstaqkat sgpssrsdai alvligiaiv lgasvwldia gfigrgiata thavlgagaf
      241 vipvalvvaa aalfsgkrva lenrvrvsag tglivvsmlg lihlfsgapd swaerfvagg
      301 algawtggal aagfssyvav pllilviiyg alkvtgitvk efaeylreai sgnagdteas
      361 aevsteldda yghvdkdida ivsgsprtpr rraplratpv vpparsagrg tapvnaagav
      421 apaaeqlnna ghkapsesal dngreeqtev lrntavhars eqssastagt rrapsmsdtd
      481 eiqavpdssr agsdnsstsa gsehtevlsa esrdavaqah dslqqqkkpv sqapqakash
      541 tahtaqtmpe vidaepadgt elnteaviep veysipspgl lepgrapktr tetndrtiea
      601 idacfaefkv daevtgftrg ptvtryivel gpgvkvskit nlqsnlayav atgnvrilap
      661 ipgksavgie vpnsdreivr lrdvlesevi agdedptlvg lgkdiegefi sssiqkmphl
      721 lvagstgsgk safvnsmlvs lltratpddv rlilvdpkmv eltpyegiph litpiitqpk
      781 kaaaalqwlv eemeqryqdm rsarvrhikd fnhkvrtgqv qapagservm epypfivcvv
      841 deladlmmta pkeieesivr itqkaraagi hlvlatqrps vdvvtglikt nvpsrlafat
      901 ssstdsrvil dqtgaeqlig mgdglfipqg grpvrmqgaf vsddevyavv eaakaqgepd
      961 ytegvtedkq aeakkaiddd igkdmddlle avelvvtsgl gstsmlqrkl rigfakagrl
     1021 mdlmetrgiv gpsegskare vltkpeeldt tiwmikgadp aeapkevqeq eahfgeaaed
     1081 dssdgtgapq vskasynpts saf
//
LOCUS       WP_284789189             326 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            striatum].
ACCESSION   WP_284789189
VERSION     WP_284789189.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..326
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35127
     Region          11..318
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 maegnpakrd eaverltnls falqgaahgg gspdrsaawi rknvegyqnr sdeaflkqls
       61 rdvvtlqrag vpvvhssged gsmyrlnqde yqlppvdftp eeamvlgvag gigkpgglsd
      121 ftlsawtkia asgasrdlsg apvyvavndi trispeltta vitavrahlr itfdyyatps
      181 spavrrtmdp wglvnhnsrv ylvgwdvdre aarvfratri dnvkrsrqda thltvpgplq
      241 dlvvealqrg etvdalvsip qgsalelaaa gkqredelya mngvekdwlv rtaasyapgv
      301 evlepaavra aiielltaer pqegek
//
LOCUS       WP_284789227             181 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Corynebacterium propinquum].
ACCESSION   WP_284789227
VERSION     WP_284789227.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..181
                     /product="YceD family protein"
                     /calculated_mol_wt=19294
     Region          <38..181
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mtspfvfdvk alltqqqspe qtthtgpapr rigaemlaie egaevtidav lhslgagima
       61 dadvsavlrg ecsrclsple rpmtvrisqv fsadddfitg daeddedegs gdeipqvshe
      121 dtidllqtlt delvvalpfn pvceggcpdd sltpapdgvs geddaqerid prwaglekfr
      181 d
//
LOCUS       WP_284789443             342 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Corynebacterium
            striatum].
ACCESSION   WP_284789443
VERSION     WP_284789443.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..342
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=37512
     Region          2..320
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 misnpnstsq sdalfrqvip llrdvegahm rmqfthyagh aeeivrgmtr tdfdaivvfg
       61 gdgtvnevvn gllgpadrkd rprpeelpvl gvvptgsanv fvralgipnt pveaahvlar
      121 lmerdtrrki hlgtwndrwf avnagfglda dvlarvdrar emgfsatplr ylavsaqayl
      181 rarvippeis vhavsrageq ftahkvplmf tsntnpwtfl gplpvvtnpr nsfdaglglf
      241 gvsdlggihg lvgmlhlmgv grrrmlskit qaralqfdda qsvdletptp krfqadgesv
      301 gkftevhles vadaievfap lqprpphers vreilrdlir ik
//
LOCUS       WP_284789390             106 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Corynebacterium
            striatum].
ACCESSION   WP_284789390
VERSION     WP_284789390.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..106
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11996
     Region          2..101
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mpacpvettl tllsnrwram ilrdlldgtm rfnelrrsvt gisqkvltsn lremedtglv
       61 hrevfaevpp rveysltplg qsmrpildam gewgkhyqqq vakeia
//
LOCUS       WP_284789454             344 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium striatum].
ACCESSION   WP_284789454
VERSION     WP_284789454.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..344
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35831
     Region          5..344
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mpnqtssapt satlqqqrha rarsfawrls vlaviivvlw atslmvgetf ygpgkvirvv
       61 fgetvpgasf tvgdlrlpra tvavaagiaf giagvtfqtm lrnqlaspdi igiasgasaa
      121 gitaivfynv sqttvslvsl vcsltiaali yllslksgft gtrliligig msailqawtn
      181 fvlskapsyd lptatrwitg slntmswerg lpllltvlvi apvmiflghq lnvlrlgddl
      241 avglglrlnv vrvsaivgsv iliavatast gpiafvafma gpiatrlfka gpsmiapaga
      301 vgailvlvad magqyffgtr ypvgvitgvl gapfliyllt rsnr
//
LOCUS       WP_284789527             630 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium striatum].
ACCESSION   WP_284789527
VERSION     WP_284789527.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 630)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..630
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=65065
     Region          32..629
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mssacgcehe pateieeldr pwwkdpelll pifsgvalit glaldwsdle tpatvlywlg
       61 lllgaytfap gairnlvtkr klgigllmti savgavilgf vgeaaalafl ysiaealedk
      121 amdraqgglr allklvpqta tvlrdgttae vaakdlvvge lmvvrpgeri atdgiirsgr
      181 ssldtsaitg esipeevapg devpagains agvlevetta agtdnslttl vdlveqaqae
      241 kgdrariadr iarplvpgvm ilavlvgvig sllgdpetwi tralvvlvaa spcalaisvp
      301 ltvvaaigaa sqfgvviksg aaferlggir hlavdktgtl trnqpevtgv vpadgfdraq
      361 vlsfaaaveq qsthplaaai vaaepeapta ldiseeaghg iggtvegrrv lvgsprwida
      421 gplkadverm esegqtcvlv tvddalagai gvrdelrpev pdavqslhdn dvevsmltgd
      481 ntrtaralae iagiddvrae lrpedkasiv aelssktpta migdgindap alagatvgia
      541 mgatgsdaai esadvaftgh dlrlipqalq harrgsriin qnivlslaii ivlmplaisg
      601 vlglaavvlv hevaevivil nglraarakr
//
LOCUS       WP_284789614             505 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Corynebacterium
            propinquum].
ACCESSION   WP_284789614
VERSION     WP_284789614.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..505
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=58015
     Region          5..504
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mstpqpalmw frddlrlrdn saldwiaqqg pviavvieed pettrtrelg aaarwwwqrs
       61 vhqlknslaa hgvpllyhsg dpreiipaiv eefgvsavgw srryheplre ldaeikqmlh
      121 ergvtarsfa ghlltepwev ltqqgkqykv ytrfaktart iaevnvasyl nnvndqapsp
      181 tghdelspig lagpgtdfpa ssplpdwnep dwthtlaqhw lpgenaawki aeefldqlaa
      241 aarkqaphya adrdrldkqa tsrlspylrf geisihrlwa lvteasdtgr iagedasafl
      301 nellwrdfaw hrlyhlpelh rrnvrqqfdh fdwhwdetea qrlsttrrdp rcaeatedlp
      361 tddfrrvfsa wragqtgiav vdagmrelwe tgtmhnrvrm vvasfltknl gihwrhgeaw
      421 fwdtlvdadp asnpfnwqwa agcgddaapy frifnpdsqa krfdphyryi rhwvpefgtp
      481 mypqplvdlk esrrqalaay devkn
//
LOCUS       WP_284789625             405 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Corynebacterium propinquum].
ACCESSION   WP_284789625
VERSION     WP_284789625.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..405
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42872
     Region          3..392
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mklndlatqr leswkqqgll rtpvefagpq drrarlhghs dkrillsssn ylglathpev
       61 iaaarsalet fgagsggsrl ttgsttwhrr veedlaafvd fddavlfatg yqanisvlqt
      121 latpdlqifs dslnhaslid girlagasga qksiyphldy aaleqqltks tsphklvvsd
      181 gvfsmdgdia dlavlreicd rhgawlmidd ahgigtvgkh gigaievhat rpdilivtas
      241 kalgaeggfa acsapvarml rnqargyvys tacsapncaa isaalgiiqq pltdhhpvvr
      301 lqqrvaalrt iagtrsngsd svsgdspiip lpvgaesaam elaaalaqrg fhvpairypt
      361 vargqailra tamatleldd iaefsttlkn lgwrrrdaag tkpkn
//
LOCUS       WP_284789670             353 aa            linear   BCT 25-DEC-2024
DEFINITION  HesA/MoeB/ThiF family protein [Corynebacterium striatum].
ACCESSION   WP_284789670
VERSION     WP_284789670.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..353
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38534
     Region          93..340
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mslisfrtah earplgdgrs vvgsntagig hyvqdpdhhl qklnkilngt lnqqeateqi
       61 akqtgispfn ahtllekliq lghieaisqp nltpeqqtrf srstalyswl ggfgkfdrwa
      121 pqeiicsssi cilgaggigs sialqmtasg igkitlvdfd tvelsnlnrq iayseksigk
      181 lktdelknri relnsdcsvr tierkiegve elipifkevd lviraidnpp esaywvseaa
      241 iatktpwidc syagpmavca tfvpgttgcy rclresekqr lqqnnisgly eetplginaa
      301 iapivsiasa laslealrfl vsrtnlsmgk vlhqnladys nqysidfpss cqh
//
LOCUS       WP_284789929             340 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium propinquum].
ACCESSION   WP_284789929
VERSION     WP_284789929.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..340
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34377
     Region          28..336
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mqapalfarr tlgmllilia vaatvcisla lganplpvre vwdgllahdn seaaiivwtl
       61 riprtvvavi tgaafgvaga liqaltrnpl adpgilgvna gagfavtigv gffgltsisg
      121 yiwfaflgaa vttavvyfig sgaalgangk anpatlvlag valaavlsgv tqfltlldpn
      181 tfqairswgl gsvaraelad talvapflaa glvvalaisp slnsialgdd lasalgtkiv
      241 rtrvlgiiai tllaggatal tgglafvglm vphvvrwivg pdqrwillys alaapvlvla
      301 adiigriiar pseievgivt avlgapvlim lvrrrkasgl
//
LOCUS       WP_284789965             433 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium striatum].
ACCESSION   WP_284789965
VERSION     WP_284789965.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 433)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 433)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 433)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..433
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46301
     Region          12..419
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 msapnprevv ttkalsiwva amlvyivait grtsfgvagl eamerfdvda sriavftsvq
       61 lgiyafaqip tgvlidkygp rkllvigavi mgvgqvalgl ttnywmaiaa rlligagdat
      121 aflsvmrilp ywfplhrtpm ftqvtsslgq lgqfvsaipf aallgwagwt tafvalgaag
      181 ilialaaava vadtpeslgi ietpaeqpns qahslstrla mvlrspvawq gffihfcgll
      241 gatvfvmlwg ipfmteglgi skvqagtvlt fyticmitlg pihgkissra qgfrdwmalf
      301 fttlnimswt afflwgnsff slfilmvais lcspcsnygf divrenmers vvatatglan
      361 mggfissmva aqifgmvlds rghaphyelg dfhaaavtsl iiwlagmlgi vvthflrkrg
      421 ggyrpkvtvv svs
//
LOCUS       WP_284790123             359 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium striatum].
ACCESSION   WP_284790123
VERSION     WP_284790123.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..359
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38531
     Region          63..358
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mkristiiaa aaiaagalta paagaatltp qqvagettls evsdlqvtpe veatkwfqky
       61 kddarvlklq atspamngrv vplavirakd anrptiylln gagsaeqdsd wlnlsqavdf
      121 ysqknvnvvv pqagafsyyt dweqepngsy lsgpqkwetf ltkelptale grlqasnkra
      181 vagmsmsats sllfaqhnqg fydvvgsfag caatstpleh qflrltvnrg gaepeqmwgq
      241 mgsennrhnd allnseklrg talyvssatg lagetdtssy ytaqgmnpav almgsaqlqv
      301 eggiieaavn hcthnlkakl dkqqipatfn frnvgthswp gwredieksw pvfeaalns
//
LOCUS       WP_284790039             604 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium
            striatum].
ACCESSION   WP_284790039
VERSION     WP_284790039.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Geistlich,M., Losick,R., Turner,J.R. and Rao,R.N.
  TITLE     Characterization of a novel regulatory gene governing the
            expression of a polyketide synthase gene in Streptomyces
            ambofaciens
  JOURNAL   Mol Microbiol 6 (14), 2019-2029 (1992)
   PUBMED   1508047
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18715624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..604
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=65134
     Region          55..230
                     /region_name="PtsP"
                     /note="Signal transduction protein containing GAF and PtsI
                     domains [Signal transduction mechanisms]; COG3605"
                     /db_xref="CDD:442824"
     Region          311..596
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msalseilrr lnssvtipdh llaplqedel salrmlenti dsnrtwrvms tkilevsqml
       61 nagrasndvl dtivrharsi igahigyisl nddesgftni latagvvteg frnirmpigt
      121 gilgivaatn rpawtydhae dpevshvdyv deaveaegir gilgapiris gktvgallvg
      181 drhprhysrd eimaiellga mtavaldtar vieaqgesva klsrsqlelr thveelhkla
      241 dadsrllavl igdarfeela evlseflgvq velwleesst fvgdgtrdew adaiaaarkh
      301 nntrsvdnrs vlpvefhgrf lgaicvpkgi ndvelrvvgh asaafaaial fnealvdata
      361 rkvddlvysv avgtagneea lrlkrltgid laqpeslyfl gvncadpals rmrldglldg
      421 asavtrheqh ycvlfqpdrd vatsvrrlva essapvfvaa apvagvteah eahdsamayl
      481 daaitlgmsg elvtedtlga vglilgadps alatlvrrsv galveydaah dteleatayq
      541 fflsghsipg tarelylhvn tvrqrleris rvlgedwatg ersldtqlal riralargrs
      601 htgv
//
LOCUS       WP_284790179             429 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium striatum].
ACCESSION   WP_284790179
VERSION     WP_284790179.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..429
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=46836
     Region          8..379
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msisnhgams rlhktagvli apflivaals gffyalapsi esvvykkeiv asgsgeahsl
       61 deqiaaaqkv ypdlqvskvq afeegkttrv lfaddalkss syahavfvdp atleikgdlv
      121 qygssralpl rswlseghrr lwlddagriy selaaswlga laimgiylwf krrrkagkml
      181 tlhskigvwl lpgfvfltit gltwslvage nistlrekmd wmqpkpaata aadphaehhh
      241 hmdmtgdmnv mgaadalaaa rsagltgild mtppsaekpa wtitearqdy klsydaiavd
      301 phtgevvdrv dfkdwplmak vvpwliqlhm gtlfgiynqv alallalgll avsvmglwmw
      361 fsrpkralqh lklspalvvg avlysiiapl fgaslvlffl vdwavqrakk akqtgpretq
      421 egesikqpv
//
LOCUS       WP_284790257             584 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Corynebacterium striatum].
ACCESSION   WP_284790257
VERSION     WP_284790257.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..584
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=61461
     Region          1..454
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          518..583
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(541,550..552,559)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            551
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 misavlianr geiavriara ardlgirsia iyseadagal htrvadeaya lpgntaadty
       61 mnvpalldia vragadaihp gygflsenad faravagagl twigptpesi ellgdkiaar
      121 rvaeevgapl apgtsdpidd wqearafaek hglpiaikaa yggggrglkv venledieaa
      181 fnsagreake afgraecyve kflthprhve aqiladthgn vavlgtrdcs tqrrfqklie
      241 eapapalsda qrtgihegar aicakvgytg agtveyivse dgtisflevn trvqvehpvt
      301 evvtgvdiia eqfriasgep lsfvdesldp ephghafefr inaedilngf apcpgtivrf
      361 epptgpgirv dagvrsgsiv ppyydsliak llvwgptrev alarakqala efdiegvrtv
      421 lpfhrdmvss qvladhgdak aaagiytdwl dhnyrpsaes tsniapveai yakrtqvaie
      481 idgklvsvgl penlfaaapa aaggvkvasp sagsqegevt apydanlvaw nvadgdtvee
      541 geaiatieam kmessvkapr ggtikllake gdrlstgsvi atid
//
LOCUS       WP_284790480             481 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Corynebacterium
            propinquum].
ACCESSION   WP_284790480
VERSION     WP_284790480.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..481
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=50642
     Region          8..454
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 maddsfadsl qnildgidkf iwsqwflipl llftglwlti rlrgvqfrkl gvalrhglvd
       61 rndadgagdi tqyqalttal aatvgvgniv gvataisigg pgalfwmwit gllgmaskys
      121 eaflgvrfrv adahgkvsgg pqrylsqgip grlgkflawf ftisaiiasf gignltqgna
      181 vaaglentfd vsptvtgvim fvligavllg gigsigkvts afvplmiiiy ltggiivlvm
      241 haseipaafa milndaftgt satggflgag iilamqmgva rgifsnesgm gsaaiaaaaa
      301 ktthpvrqgl vsmtqtfidt ivvvtmtglv ivttgvwkag qsnaanmtaa afsegigsdw
      361 ggiivslsvv ffafstilgw syygersver afgtwasipy rmvftcviyi gatteiglaw
      421 tfadianglm aipnliglli lsglvaretk ayldfdptlr aqprdiekfl iaskspwrsk
      481 f
//
LOCUS       WP_284790528             326 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            striatum].
ACCESSION   WP_284790528
VERSION     WP_284790528.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..326
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35142
     Region          11..318
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 maegnpakrd eaverltnls falqgaahgg gspdrsaawi rknvegyqnr sdeaflkqls
       61 rdvvtlqrag vpvvhssged gsmyrlnqde yqlppvdftp eeamvlgvag gigkpgslsd
      121 ftlsawtkia asgasrdlsg apvyvavndi trispeltta vitavrahlr itfdyyatps
      181 spavrrtmdp wglvnhnsrv ylvgwdvdre aprvfratri dnvkrsrqda thltvpgplq
      241 dlvvealqrg etvdalvsip qgsalelaaa gtqredglya mngvekdwlv rtaasyapgv
      301 evlepaevra aiielltaer pqegek
//
LOCUS       WP_284790648             744 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium striatum].
ACCESSION   WP_284790648
VERSION     WP_284790648.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 744)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 744)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 744)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 744)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..744
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77628
     Region          6..742
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtnlvhldlg vsgmtctscs srverklnkv dgveatvnfa tesasieydp ststpdslie
       61 vvrgagydaf tlmeeqeads eetanpvdea raqeakdllr rtivsaaist pimvvsmlpa
      121 lqftnwqwaa ailativyif ggapfheatw anlkhgsftm dtlitmgtta ayfwslyamf
      181 fghaghpgmk mhmelvsnna emdhiylesv gmvitflllg rwfevkakgq ssealrtllg
      241 mgakdatllv dgaekrvpik dlkvgdvfvv rpgekiatdg vvnagasavd esmltgesvp
      301 vevkegdhvt gatinssgrl evratkvgad ttlaqmaklv teaqaskapv qrlvdkiaqv
      361 fvpiviaisv ltliahliig gaaatapafv aavavliiac pcamglatpt ailvgtgrga
      421 qlgllikgpe ilestkqvdt ivmdktgtit egkmsvadvh aaqtsdqdat qvlklaaave
      481 agsehpiaka ivhaasdvtp asdfvsvtgr gvegtvegqr irvgrvegel gslseafraa
      541 eaeggtpvav yaadaligii dvrdtvkess aaavaqlkel glvphlltgd nesaaqavaq
      601 avgidpenvt agvlpeekvd vvkqlqssgc nvamvgdgvn daaalaqadl glamgagtdv
      661 aieasditlm nddlrsaada irlsrrtlri ikgnlfwafa ynvilipvaa igllnplfag
      721 iamafssvfv vsnslrlrtf qpta
//
LOCUS       WP_284790650             323 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Corynebacterium striatum].
ACCESSION   WP_284790650
VERSION     WP_284790650.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..323
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34594
     Region          72..297
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mskgilrsct paiaaaltll agfcvscadn sagsgesgme hsasqapatq ktkkpevsak
       61 klvyaheher qhgflvtpkk pqpgkklplv vflhgggwqe kstaqsaapa vndlvehgaa
      121 vwnveyrgvs idgedapggw pmtyqdvaaa idfipqltnh sdvpldlnnv vvagysaggn
      181 latwtcsrpe lapdapgahp afhvdkcvgi agvydmelay qqhdkfvrtl lggtpqevpa
      241 hyfdaspayn vnkkarvlvl hgendemvnv devtrfadya kqrglnidai ifddakhlsw
      301 anpaglqwqq arrtileqvg iks
//
LOCUS       WP_284790893             384 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Corynebacterium striatum].
ACCESSION   WP_284790893
VERSION     WP_284790893.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..384
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42106
     Region          70..354
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 masikkyeta kghawrvqyr spdgrnrnkr gfrtkdeark waeknaasit dgdwvnpaeg
       61 kvrveelgar wlamqthlkp sttelyrqvw nsgvkprwgg vragsilpsq vqewvaemtl
      121 ddvsgswvrh chmvlaqvld mavgdrllkk npargvklpr kgkarkvflt mpqleafaae
      181 cgdredlill lgtsglrwge aialrpcdld plrgrinitr naakvgndvv lgtpkthear
      241 tvavaprvme mlmeraaglg kddllwtgkr ggwlrapghn twfdgalkrv qrkdlsfprv
      301 tphglrhvaa glliqaganp kivqrqlgha saavtldvya alwedgldqv aqalaglsnp
      361 qpgpgvptsq sqgrsfphav datq
//
LOCUS       WP_284790986             342 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Corynebacterium marquesiae].
ACCESSION   WP_284790986
VERSION     WP_284790986.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..342
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=37182
     Region          16..305
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mlcvnywtki krffkeaapt lqqqrliali lllcqggitv sgsivrvtgs glgcptwpec
       61 qpgslvpmeg aapalhqaie fgnrlltfvv taaaiaavva mrmarrrael kvyawlnvag
      121 ivlqaviggi svhldlrwws valhflpsml lvwlaamlys rilepddgtp rvrfpqairl
      181 laavatvals ivlitgtmvt gsgvhsgdsg vgmegrlqvd teamavtham cmyvylaltv
      241 itvfllyknr apqdakkagw vlivciliqw avgvyqfyms iprwtvpfhi glssfvtayt
      301 allwahgvrr tdgtadlitg sprgdekyaa rqtsleqera ta
//
LOCUS       WP_284791271             345 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Corynebacterium
            marquesiae].
ACCESSION   WP_284791271
VERSION     WP_284791271.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..345
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=38127
     Region          1..325
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mhalmisnpn stsqtnalfr qivpclqave glhlkvqfth ypghaeemvk gmtrddydvi
       61 iavggdgtvn evvngllgpa dgqrpdpqsi palaviptgs anvfvralgf pstpveathv
      121 larmldrdlr rtiylgtwne rwfavnagfg ldadvlarvd rareqgfsat plrylnvair
      181 awsrarknpp hiavtaesss geqlrkddvp llftsntnpw tflgplpvvt nprnsfdegl
      241 alfgleefsg lggvvgllhl fgadkrgwln rltkektvaf ddamrvelvc repqrfqadg
      301 elegrfdavt lasvkdaiev fapqdrreah qrtmkevfrd firlr
//
LOCUS       WP_284791283             741 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium marquesiae].
ACCESSION   WP_284791283
VERSION     WP_284791283.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 741)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 741)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..741
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=81448
     Region          14..734
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mnsasnkhaa aagssereai ateqdyvdgl fsrlddevaa anerlnevqa dvdpstpdad
       61 alvrreteyh glqakldrln vaqmglvfgr ididapgdnp tsegldrryi grmgldared
      121 dyrtllldwr apmarpfyla ttaqpegvht rrqirtkgrt vtgiheevls gpgvreeetg
      181 vasesalyha mqrartghma sivetiqreq deiirdntrg vmvveggpgt gktavalhrv
      241 ayllythrel lsatgvlivg pnssfldyis rvlpelgetg vvlstigglf pgiepsheed
      301 lvareikgsd amveilstav kdyqllpdap relaidgltl svtpnmvksa rtrarrsrkp
      361 hneardafie hlvedlaqqm adtvgadplg gknllsradv dqfhddlaed aavtalidef
      421 wpelhptdvl aalvssreri asaahgydee tqealyraeg rawtdsdaal ldelavligl
      481 pnpeekkaad daawreqvad aedaldilss sestdndddm feaeilsahd vidaetlahr
      541 qevrdkrtta qraredhtwa yghiivdeaq eltpmewrml frrcpsrwmt lvgdtsqtgs
      601 pagvddwgea lepfvaqrfr hhfltvnyrt pqpitdlang lleminpdai patairdgvq
      661 vrrlehgtyt pgvhseedgr ltavidaata ehykglefdh vvvldpqriv daspqglqnl
      721 yvcitratqs ltlvgdcgev l
//
LOCUS       WP_284791444             671 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Alloscardovia omnicolens].
ACCESSION   WP_284791444
VERSION     WP_284791444.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..671
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=73327
     Region          187..618
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 msskkrsfls niqwklscip laarlmtlvl aflivassvl vlasrqlvss almqktdtql
       61 mrqatlvinn idllqsenas dqkssseqsp slgnqlkeqf fknsdtasqk rpspysttgn
      121 qnlgptdyfv qirdndnnvl stplipiahd gvesiptlpq egksatflyg epttvaasvh
      181 vsknvslter qaimahspwr viaaqyvnra tgmeyvvyig lslfdvndti qaltvyfvws
      241 avgivitagf lallavrrsl rplkkmeqta ekiaagdlsq rveraplnte igslsnslnt
      301 mlsqiersfk kqeditlqmk rfvsdashel rtplavihgs telykmqrks pqadpvesad
      361 mvidhidkss trmsalvedl lslarldegr gidlaqtvhm tdilsdsved lhaldperti
      421 tlgrlsldmg simqsvqpvq gqndthsdeq vtdntlafip sqlphidagg dpvrmrqvmt
      481 niignihryt psdspvevga tvvrasalvr dleneastae tldkflkdvk esgtasntle
      541 yviiqirdhg pgvkdeaytk iferfytadp srardkggtg lgmsivqsiv kahhglicam
      601 ktpggglttt vvvpisqtvl fsstnptqer mrekntapai fgrrkksada dmatteikis
      661 lgsnkdtstk k
//
LOCUS       WP_284791491             473 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Corynebacterium
            marquesiae].
ACCESSION   WP_284791491
VERSION     WP_284791491.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..473
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49426
     Region          1..449
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mdslnsilsa istvvwgpfi liplllgtgl wltirlgglq fralgramrh ifatdsddes
       61 tegdisnyqa lttalaatvg vgnivgvata lsiggpgalv wiwitglvgm askyteaylg
      121 vrfrttdskg emsggpqqyl krgipgplgs vlavffaifa icasfgignl aqanavatnm
      181 estfgiapaa tgailfvlvg svllggiqai gritaafvpl miivyvlggl yvifshaaei
      241 paafamifsd aftgtaaggg fvgstimmai qygvargifs nesgmgsaai aaaaaktphp
      301 arqglvsmtq tfidtiivvt itglvivvgg twdmgrdeag imtaeafsrv lpgdwggtiv
      361 slsiiffafs timawayyge rsleslcgrk asipyrmffa cllfvgsvse lelawtfsdl
      421 angliaipnl igllllsglv aretkaylaf dpklnkpvde vrafvesqgm nwk
//
LOCUS       WP_284791504             559 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Corynebacterium marquesiae].
ACCESSION   WP_284791504
VERSION     WP_284791504.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..559
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62480
     Region          12..534
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 msndskntgs avnrrrflqt tgtagaaial staaantana qsslsprvkq hmvepklgkr
       61 pflhgvasgd pipdsvilwt rvtpeddamp gsglgeatrv eweiakdegf gdvvkrgevt
      121 tdvnqdhtvh vdphglepet vyffrfkaqd kyspigrtkt apalsaspee ltfgvascan
      181 wesgffnayg diaqrgradq ldymiflgdy iyeypqreys gygpvrlhhp aheiisledy
      241 rirfgryrtd enlqaahgal pwvvvwddhe vandnwrega enhtegeega fldrrkaamq
      301 ayfewmpvra tnpseqghly rsltfgdlve ltmmdlrtyr deqvrfgprk maaegrtmlg
      361 seqynwllnk ietssakwnm lgnsvmfspm nlatlqkddr tapvssslss nitgipvngd
      421 qwdgysaerr llidalskhd shtlfvtgdi hsewahnisk ddrifgaemv casvsapnvn
      481 eqlklpegne lsklaeryll ganphtrhvd ldhhgysyvt vrpdsaemhw lrvdnlltak
      541 spvreavtmt wrpgegytt
//
LOCUS       WP_284791517             435 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium marquesiae].
ACCESSION   WP_284791517
VERSION     WP_284791517.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46082
     Region          17..383
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mshpnprevi ttqalgiwva amavylvait grtsfgvagl daierfdvda griavftsvq
       61 lgvyalaqip tgilidkfgp rlllvvgavi mgigqvvlgf ttsygvaiaa rvligagdat
      121 aflsvmrilp ywfplhrtpm ftqvtsslgq mgqfisavpf lwllgaagwt aafvtlgavg
      181 ilvaiaaiva vadspeklgi iptekeppns qatsiparlk tvfrspvawq ayfihyigml
      241 plivfvmlwg mpmmtqgmem skaksslvlt llavflvlvg plhgkissra qhvrpwlslg
      301 fvaihvltwl vfftfgtdsg vvailvvsfv talctptany gfdivrermd rsvvatatgl
      361 gnmggftsgm lgaqlfgmvl dhssdapdys mpdftaaaaa vlavwvvgmi gviithflrh
      421 ragedgpsvt ivevs
//
LOCUS       WP_284791636             293 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium marquesiae].
ACCESSION   WP_284791636
VERSION     WP_284791636.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..293
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31250
     Region          22..244
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mttsreprhp rrtattragg dpartaaffd ldktiiatss ayafgreflh nglispaeal
       61 qlslakasym fsgltsegmd strdqltamv tgwsvdevra iaretmhhvv tpsiyaeare
      121 lirahraagh hvvivsasaa vlvniiaeel gvehviatel aeengrftge vlfyckgpnk
      181 aaaleqtaaa enldlnasya ysdsatdipm lekvghpvav npdkqlkrha lthewnirsf
      241 kdpvpllaap takeigigas vlagtaavig aglwltqhpg rpgppkrgpr rap
//
LOCUS       WP_284791678             717 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium
            marquesiae].
ACCESSION   WP_284791678
VERSION     WP_284791678.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 717)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 717)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 717)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..717
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=74488
     Region          2..713
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mshldlgvtg mtctscssrv erklnkldgv nasvnfatea aaieydsqtv spqelisvve
       61 gagygafdma aakteepqae knsdggllrr tvisgalslp lmvvsmwpal qfpnwqwaca
      121 ivativfvfg gapfhtatwt nlkhgsftmd tlitmgtsaa yfwslwalff gnagepgmkm
      181 hmtldsnaaq mdhiyfesvg mvitflllgr wfearakgqs sealrellsl gakeasvlre
      241 ggeqripiaq lqvgdvfvvr pgekiatdgi vvagssavda smitgepvpv evgsgdavtg
      301 atinasgkle vratkvgedt vlaqmaqlvt daqtskapvq rlvdriaqvf vpaviavavl
      361 tllahlflgg vapafiaavs vlivacpcam glatptailv gtgrgaqlgl vikgpeiles
      421 tqqidtivmd ktgtvtagem svtavhgdvl dlaaavehns ehpiaraiak erdvkpatdf
      481 avvpggvegt vegvrvgvgk pqgplgdlea pfreaqdsga tpvvvsvdgq pagiievrdt
      541 ikpssaaava qmkelgltpy lltgdnagaa ravaaevgie hvsaevlped kvnhikklqs
      601 aghtvamvgd gindaaalaq adlglamgag tdvaieasdi tlmngdlrca adairlsrrt
      661 laiikgnlfw afaynvvlip vaalgwlnpl laglamalss vfvvtnslrl ksfsvqr
//
LOCUS       WP_284791759             454 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Corynebacterium
            marquesiae].
ACCESSION   WP_284791759
VERSION     WP_284791759.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..454
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=48477
     Region          5..242
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mtlklnffak sdrglirdnn edsgyagphl liladgmggh aagevaselm vnhleildqd
       61 pgqedtaall eaaaeqanea isdhvkahpe tegmgttlst mlfngrdfgv chvgdsrgyl
      121 lrdgklkqvt kddtyvqslv dkgeldpddv sshpqkslil kaytgrpvea tlftldakpg
      181 drillcsdgl sdpvtastie talgqgsieq agstlvdlai rsggpdnvtv vigevteesp
      241 qehepfrvga lagpteepth pdssasraaq lsrkpqvipp avmadgkdeh pepnddeaee
      301 etsgrkigwk vllallivla lvigaglwak nflsnnyyva tneaqeitiq qgadysvfgk
      361 elhsthqnvc indsnsllfs sqpcegdftp lkvtdlpese rsavdhlstg dlgevqqqvn
      421 dlgdkalkpc itapsqkdkk dakknkpgvt crev
//
LOCUS       WP_284791777             329 aa            linear   BCT 25-DEC-2024
DEFINITION  lipase family alpha/beta hydrolase [Corynebacterium marquesiae].
ACCESSION   WP_284791777
VERSION     WP_284791777.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18498059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..329
                     /product="lipase family alpha/beta hydrolase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36080
     Region          95..201
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
     Region          101..307
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 maelkstise qlrkfwrand keltdsprrg vaspaeatal reevateiad likaqkskts
       61 pgdtaldada aatlplgari kprgvfeddw sarptaqrpw pvilihgtcd tkgvwqilgn
      121 elrqdgwavf apdygrratq plaesaqqld ayihtvrmat gadkviligh sqggllaryw
      181 mrmiggaehv lhlmcisapn hgttyggivs rlirtprqea vmrsvidgwf gpagmdqivg
      241 sealreanrd gdlesgvsyt ciatrsdavv vppetcfldp rgvaegtvrn iyvqdfdrla
      301 mvmhedmpmd krvraivrti lelvetipr
//
LOCUS       WP_284791842             382 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Corynebacterium
            marquesiae].
ACCESSION   WP_284791842
VERSION     WP_284791842.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..382
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41376
     Region          10..378
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mvttghphsl eglrvldmsr vlagpfcsmi ladlgaevik ietpwgddsr nfgpdfngds
       61 ayyrlfnrsk kgitlnlked sdlatlrelv kradvlvenf rpgvmeklgi speslmelnp
      121 qlivtsisgf gqtgsmskap aydlvaqams gimsitgwpg grptrvgisl gdlipglyga
      181 igtlgalqer hrtgcgqhvd vamfdslvsi lesvamrdly edevptavgs dhamtvpfst
      241 yrvddgevvi ailneklfgc ltralgleym vddprynsna arkerreeir siiedalrgk
      301 tveqalalfq ehgvptapvh svdealhgev gterdvlfte sdgfttlssp lrltgsrspe
      361 papqlgehns lipewlaepa rg
//
LOCUS       WP_284791897             328 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            marquesiae].
ACCESSION   WP_284791897
VERSION     WP_284791897.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..328
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35363
     Region          13..323
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 maahnpapkr hdeaverltn lsfalqgaan sggspdrtaa wirshvagyg dksdeafaks
       61 lardiatlqr agvpivhsgg edgaryrlda ssyqlppvef speeamvlgi aggvgttggl
      121 sdfslsgwtk iaasgasrnl agapvytavn ditrlapeii tsvlaavrnq lritfsyran
      181 patepvrrvm dpwgvvnrds riylvgfdvd rneprvfral rvsdikrshd paehpnpted
      241 lqvlvervlq rgekvdarlv ipdgqarell dsgeqqtdgt vllhkvdkdw lvrtaagyap
      301 evqvlepagi rqevisllhk asqsqeeg
//
LOCUS       WP_284791899             938 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium marquesiae].
ACCESSION   WP_284791899
VERSION     WP_284791899.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..938
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103515
     Region          4..936
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtethldsft aalpypldef qvkgcqaved ghgvlvcapt gagktivgef avslalsrgt
       61 kcfyttpika lsnqkyhdlv eehgeeavgl ltgdvsinsd aeivvmttev lrnmiyaesa
      121 aldrlthvvm deihfladas rgavweevil nladhvsiig lsatvsnsee fgdwlstvrg
      181 dttvivsehr pvpldqwmml grkiyplfep esggqvnael errihrleag dtddgradyk
      241 sgkgfrarar hkgggrsefh gkgrgrsgaa rkqdryrplg rpevlkvlqs qdmlpaitfi
      301 fsragcdgal yqclrsrmvl tsqeeaqeik divdagvegi peedlqvldf krwrealsrg
      361 faahhagmlp afrhivedlf vrglvravfa tetlalginm partvvlekl ikfngeahvd
      421 ltagqytqlt gragrrgidt lgnavvqwap amdprqvagl astrtyplis tfapgynmai
      481 nllgmlgfee slrlleksfa qfqadgsvve etreieraeh rvrelrnqld davaslappa
      541 kdgedpaevl mdyvrlrrel tveekqskid sanqrnqevi avlgrlqlgd viampgkkrp
      601 ilaavvtpan qtadprpwit tesgwsgrid aaginnppiq vgsikipkpv rknprrntry
      661 vqdvlhrehf drpkrmksqt rarpnkrvgq lrdalrahpa hdwpatdreq laglaqklar
      721 rerdrdklqs kvnkatdtlg rtferivdll aemnyveftg vgagrtpvit eegerlakih
      781 sesdllvaqc lkrgiwddld paelagvasl ccfenrkats gqpeaaterm adamnatwrv
      841 yteltadeqr hrlpptrepe agfalavhqw aagaplgycm aaaneagael tpgdfvrwcr
      901 qvidllqqva ktgydgeiqr narraidaiq rgvvaiga
//
LOCUS       WP_284791900             375 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium marquesiae].
ACCESSION   WP_284791900
VERSION     WP_284791900.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..375
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=40126
     Region          18..374
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mtdtqtfsad vyaqrlhaaq kaaadkgidl lligtgpdfa yltgswvssh erltvlvvpq
       61 qgnawiaapn tditdikaap vgeldvelrg wndgedpykl alhgagdglg kvalgqslta
      121 dhvlrfqdll prasyelaty alaelftrkd eaeiaelrka graidavhaq vpqllqagrt
      181 evevahelek lilrehsvid fvivgsgpng anphhsfsdr vlaegepvvv diggtlpsgy
      241 hsdctrtyvv ggdmskapqd fqdayavlad aqaagraaah pcstaadida ivrqaisaag
      301 wgdyfvhrtg hgiglsthee pfimegndla leegmafsie pgiylegewg mrledivvlt
      361 ndgyeslnqa prdvr
//
LOCUS       WP_284791963             229 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Corynebacterium marquesiae].
ACCESSION   WP_284791963
VERSION     WP_284791963.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..229
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=24969
     Region          1..223
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mlfdslprps vrvapgvghv pgwvgvdkqk alveemrgia reyaatpmam vrprlksggq
       61 msvfqlhlgr ywhypsyryv dnmdgtrvpp vpeslrqiap galraaaeva pelepwvetf
      121 vpemalvnyy ppgsamgmhv dafeespapv islsigdeal frmghtesrt rpwdditlcs
      181 gdlvvfggpk rfayhgvvrv ndgtlpegcg lsegriniti rqvsaravg
//
LOCUS       WP_284791991             195 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Corynebacterium marquesiae].
ACCESSION   WP_284791991
VERSION     WP_284791991.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..195
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=20806
     Region          1..191
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mrlilasqsp srasilrgag vepvlepadi dersleasla ghppadivaa latakaekva
       61 eryptepvig gdsmllldge lqgkphteea tierwhqqag rtaelltghc lifgekrhve
      121 tstttvhfaq aseadiaaya hsgeplhcag aftleamggw fidriegdps sviglslpvv
      181 rralyafdln vsdfw
//
LOCUS       WP_284792011             103 aa            linear   BCT 25-DEC-2024
DEFINITION  histone-like nucleoid-structuring protein Lsr2 [Corynebacterium
            marquesiae].
ACCESSION   WP_284792011
VERSION     WP_284792011.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Gordon,B.R., Li,Y., Wang,L., Sintsova,A., van Bakel,H., Tian,S.,
            Navarre,W.W., Xia,B. and Liu,J.
  TITLE     Lsr2 is a nucleoid-associated protein that targets AT-rich
            sequences and virulence genes in Mycobacterium tuberculosis
  JOURNAL   Proc Natl Acad Sci U S A 107 (11), 5154-5159 (2010)
   PUBMED   20133735
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18741]
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Gordon,B.R., Imperial,R., Wang,L., Navarre,W.W. and Liu,J.
  TITLE     Lsr2 of Mycobacterium represents a novel class of H-NS-like
            proteins
  JOURNAL   J Bacteriol 190 (21), 7052-7059 (2008)
   PUBMED   18776007
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Oshima,T., Ishikawa,S., Kurokawa,K., Aiba,H. and Ogasawara,N.
  TITLE     Escherichia coli histone-like protein H-NS preferentially binds to
            horizontally acquired DNA in association with RNA polymerase
  JOURNAL   DNA Res 13 (4), 141-153 (2006)
   PUBMED   17046956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10570331
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..103
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11561
     Region          1..102
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 msrrevtqfy ddldhalipe dqlevvrfsv ngqnylidls vdnarhfhnl lapyvdaari
       61 apdinaqran psqirewara qglpvahrgk ipqdvieayn aan
//
LOCUS       WP_284792040             337 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium marquesiae].
ACCESSION   WP_284792040
VERSION     WP_284792040.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..337
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36372
     Region          55..328
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mtasikgrvl saimavaval glavvagsqp aeaanrdwlr rdatgtcewd kvawwvqrcd
       61 vwsqamgrni pvqiqpakrg gnaalylldg lratnltnaw vndvnaakty ephnitlamp
      121 vggaasfyad wqgpatydls hpvnykwetf ltselpgyle rnfgvarnnn siaglsmgag
      181 aaltlaakhp nqfrqalsfs gfltttvpga rtfmrlamld aggfninamy gslfspkrfq
      241 ndplllipql rntnlyissa sgipgpgdsh ylpehqaaga alevgsnitt hawegaarlq
      301 glnptvsypa qglhnweqfg yqlnrskpqv lnvmnaw
//
LOCUS       WP_284792047             361 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium marquesiae].
ACCESSION   WP_284792047
VERSION     WP_284792047.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..361
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36078
     Region          54..354
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msattkvgqk iqtdntadsp tatgaaapvm traqshklll valilaslvl avasltlgsr
       61 sippgeviaa lhgageqdih divwnlrmpr tflayfagaa lavagvlaqs wtrnpladpg
      121 figvtagasf fvalgtaigi atstsmrtal alvgagittl lvlavsrrfe dpltlilvga
      181 gvsaalgsga tiiglystdv ldsmrrwtig stfgrgpedv aiagiglvig vacaamvarp
      241 ldllamgees slalggsptt arvgaalsvv vlagsataat gpiafvgfai phivrrvvgp
      301 svatlllpsa llggcavlaa ditgrliagn selemsivla ivgapfliwg ahrgvgrawg
      361 q
//
LOCUS       WP_284792159              75 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Aerococcus urinae].
ACCESSION   WP_284792159
VERSION     WP_284792159.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 75)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 75)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 75)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..75
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8347
     Region          2..58
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(4,8,33)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(7,32)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(14..15,26,29,33..34)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mkfreivnks gltglelshi vgipsaniya ymsgrrnnps letafklada lkidinelrn
       61 afkkddeekv heskn
//
LOCUS       WP_284792257             268 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: TrmH family RNA methyltransferase [Corynebacterium].
ACCESSION   WP_284792257
VERSION     WP_284792257.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..268
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28568
     Region          3..262
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mlitdpadpr lddirnlnks dksgeglvia egplvvsrla esrfpmrclv gfpkkveayi
       61 seygepecpi yevsretlae vagfdmhrgl vaaadrasep evseivesaq tiavlegvgd
      121 henigaifrh aagmgvdavl lgsgaadply rrsvrvsmgh vlrlpfahle ggfttwqrsl
      181 qaladasftl isltpnpqav hlaeamhgld kvamlvgaeg pgltehamka tdiraripma
      241 pgtdslnvat aaaisfyerq rslsdlnv
//
LOCUS       WP_284792304             923 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Aerococcus urinae].
ACCESSION   WP_284792304
VERSION     WP_284792304.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 923)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 923)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 923)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 923)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 923)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 923)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 923)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18767243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..923
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..923
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=106469
     Region          1..922
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          1..204
                     /region_name="AAA_27"
                     /note="AAA domain; pfam13514"
                     /db_xref="CDD:433272"
ORIGIN      
        1 mklqaidifg ygkfvhrqfq ltddfnvflg pngsgkstlm sfvlsimfgf pnqrrkgsrd
       61 fdtndqvrfg grlyfkdtqw gdcaiertra ngkqvlkmsv agqeaqevdn fkqlfgdltr
      121 dtylayfgft epdlmqfiwe seedfarslv nlgvtgklsl sqevdqlqad adslyrpqgq
      181 npklnqemva lerqdqdlaa arqeedayfd ldqelsekka alaevqsaeq sarqslmdle
      241 kadqqsasde ervalgfela qydgprfsdq dvdqwqnivs tkdrlveeyq elnpegfvim
      301 dsveakaepe eelnaggqwi sdhlgiseqm laearayreq irqnenlhdq ivekryqesr
      361 llsalgaeni delprdftde ereewqkrqk aidsrrvfyk ntkaglenlm edreslgqer
      421 qeissnyddf katvykytqs wirpigmtll avglicyais lfhtspfwrg agmpalilgl
      481 ifvliawfqe rkgkhyvnee ekayqldlrd idsetaeiqr qidnqnqqia eleeeskqft
      541 kdleaflqak ggsayimplv wlqtdyvkqi edlegeinql ihqsgagafg qahqaewsdy
      601 rqasnnqals ldslfqqfed dyhnyrlyaa nldyedqeqk akqarlsqla dhidqlekte
      661 enflkqynlt dradlekalt aygqfkdkea ryqllnqyld kkasalnede aevseqikat
      721 kdqinsyegq rqvlladiar ienqlkqmkn sqalqameqd kqeqvdqsyd tavawasdtl
      781 aaktmeeatl gqgqdtvqrv laqanrylfd ltntkfekmr ytdesvevyq pmrdqwtsvn
      841 qlsrgekall fvamrfafld aqlghqdlpi lidegfahld qeyrqniyrf lkekslsrqi
      901 nvftfdqeit qglhsdqvhh lea
//
LOCUS       WP_284792339             634 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Corynebacterium
            marquesiae].
ACCESSION   WP_284792339
VERSION     WP_284792339.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..634
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=68057
     Region          1..613
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtspvlsvkd lrvnfpseag svsavrgvdf dlypgrtlgi vgesgsgksv tsmsimgllp
       61 dyakitgsvk fdgrellgls dkqmseirgn gigmifqdpl saltpvfdig sqlveaiqah
      121 rdvgkkqalk eatelldlvg ipdphlrlks fphefsggmr qrvviaiaia nnprvliade
      181 pttaldvtiq aqildvikla qretgaatim ithdmgvvae taddvmvmya grpvergdvd
      241 tifsqpsmpy tvgllgstpr pdvsaeeplt pivgsppvlv dlkqrcqfap rcpvaqpacs
      301 dgeppliald dapshqsacl rapdihdrki ggelmftppq laedvmagip rderpttlkv
      361 tdlrkefplt kgalvkrrvg tvkavdgltf dirkgecmai vgesgcgktt tlleimdlkp
      421 engavvlngk daagmsnser rearkdiqiv fqdpmsslnp rltvreviae plnslgydgd
      481 vdarvnelmg lvgldssqld rfpshfsggq rqriglaral atnpsvlvld epvsaldvsi
      541 qagvinlled lkrklglsyl fvahdlsvvr hlsdrvavmy kgqfvesgpt ddifespqad
      601 ytkklldaip ipdpaaarrr rspgpaqasp isqk
//
LOCUS       WP_284792550             296 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium
            coyleae].
ACCESSION   WP_284792550
VERSION     WP_284792550.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..296
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32075
     Region          1..276
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrasadtypl rnvaacvvee gkanfaglga dehtefeias itktfnaell eqaitkglvd
       61 tdttvgdvlg qrvrgnalad vklaelanht sglprtgkqr lrniarallg lnpdvgvtse
      121 dvieqalsat lrergveeys nlghdllgfl larvstttyp tlikewvldp lgmtetyval
      181 pgtvgpdrpr gvsalglpvq awemdgtaps gglrsttsdm akyamhiler rstrftwani
      241 kgtelywhng atrgfssmll ldlstqrasf vttdsyadie wiafeliglh dparek
//
LOCUS       WP_284792618             499 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Alloscardovia omnicolens].
ACCESSION   WP_284792618
VERSION     WP_284792618.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..499
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53492
     Region          <300..354
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 msspiytfah ifggttvldn pdelhtyacq minyaeqlem ntsamqqths yihqrsmtia
       61 tcaahsgash pssahcanlc tvlaqhvqsa lsviaqlrhi adcmmrsynl ysqteaqtsr
      121 iisaltmaaa yhypvptafa lgawstirem tsphasliga ltnsrsaqed ylsgvsrifs
      181 pcegipgvad alahpvspls sthtsyamni kavsvsaplp aahnlhdtiv nleklsigqp
      241 gnsygtvaiq rythtdgshs wivtipgtdg kkdspfgwsq nlslmssreq treqahslla
      301 vrtamhragi kagepvalvg hsqggivaaa lasdaqqpyt iahvvtagsp iahhpiatkt
      361 twvtsietdr eivshldgrs npkhphwltv rgvisdsasg lannatapnp apahstfpsp
      421 tpvahaaekh elthgmnyhr atledaqnct tkismntisi sahsrrelwi ktcisdaeyr
      481 atkrsaricl avgwgyeln
//
LOCUS       WP_284792702             106 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Corynebacterium coyleae].
ACCESSION   WP_284792702
VERSION     WP_284792702.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..106
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11723
     Region          13..>73
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mtrfnstdhl npeaiaayvd gelskaatlr aerhlqlcge cceevqaqrg tsqrlqvcns
       61 sdmhapaslv erlamlcded vtdtpetpkr irsrvesair slthre
//
LOCUS       WP_284792850             729 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium coyleae].
ACCESSION   WP_284792850
VERSION     WP_284792850.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 729)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..729
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=80292
     Region          14..727
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mqdlqhnlsp dpvadeqsha dtlfahldae varararlee vqrdvdpdnp dsdalvrret
       61 eyhglnakld tlgvaeaglv fgridvadde penpvpgred ldrryigrlg iddrednyrt
      121 llldwrapla rpfylattah pegvetrrni rmrgrkvtav ddevlsgdna dtsvagvgse
      181 aalrramnea rtghmrsive tiqreqdeii rdpthgvmvv qggpgtgkta valhriaylm
      241 ytwreqlsrt gvlivgpnpa fleyisrvlp elgetgvvls tadqlvpgft ptgsdsiaar
      301 evkgseemvt ilkravqaye tvpdkpvvlt idsvaieatp amikaartra rrsrrphnqa
      361 rpffaehltq slaealaqki gedplgganl lsaadidqlh ddladepqvl alidehfpel
      421 dptdllgefl tdedaiahaa ydyddytraa llrspeedfs padtalvdel avligtvdpe
      481 earckeeaew relveeaeda ldilassest dndddqfeae ilsaadvida etlaarqrvt
      541 dnrstaqras adqtwayghi ivdeaqelsp mewrmvfrrc parwmtlvgd taqtsspagv
      601 ddwtaalerf vgqrfrlhel tvnyrtpkei sdyaaevltq idpeatapta irstgipvdf
      661 lpagaevvdk rdglhavidv hnvdemkgle fdhvtvvepq kiveaspqgw qdlyvavtra
      721 tqtltvign
//
LOCUS       WP_284792960             487 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium coyleae].
ACCESSION   WP_284792960
VERSION     WP_284792960.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..487
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52795
     Region          225..462
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mlrvasgday etrlgaghsl rlklavlsgf ivaaavgltt mlgmwlstkt hegvldtelr
       61 sktlgmarql dgasedqirs eiaafrrsnp ltsiavsgad snlflgdpvs isgpylrtes
      121 gdavsvrsvn gkrvvvrqtp dgmvvaasrt edpygrisgs raaaalvvig vgslvawisg
      181 afisavgltp vrrlhreldn anessgprel pvegddefae vtssinalvr sleeskkrqa
      241 qlvadaghel ktpltsmrtn iellmmlhns grqdqisaed radlerdvla qmeemsilig
      301 dlvdlsrdes hetepegfrl devleealdr vrrrrpdvtf lfhadpwvir gdrfamgrap
      361 inlidnaakw speggavrvs lkaakrnavl ivddsgpgip peerekvfer fyrspesram
      421 pgsglglaiv kqvmdrhgat ivaeesddgg arfrvvfpgr ppedetvadl avedenetrv
      481 ipkksys
//
LOCUS       WP_284793047             526 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Corynebacterium coyleae].
ACCESSION   WP_284793047
VERSION     WP_284793047.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..526
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55819
     Region          128..517
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mstpvmhesa slsegdlaka pepgewrrql iglitgvvla vlvyflfptn aaetvmqssg
       61 akegveysad tmrivaattv lmgawwmtea iplaatalip iavfpiagva pfkevsspya
      121 satiflfmgg flmalglqrw nlhrrlalvv vkivgtspkr iilgfmlatg fmsmwvsnta
      181 tavvmlpigt svlmltadtv ggmknqrkfa talmlaiays asigslatli gtppnallkg
      241 ymeeahgivi gfgqwmlvgl pvavvftfia wwllitvfkp evdtipggke liddeikklg
      301 awtfpqvavg vifliaalaw ifiplgrnhf gwdfpyddai vgiiagmlmf iipgtsdgkr
      361 lldwktanem pwdvlmlfgg glslsamfta tglslwigek akglsslpmf llifaiaalv
      421 lllteltsnt ataatflpim ggvavgiglt eatemnvlll aipvalsatc afmlpvatpp
      481 naiayssgyv tmgemikggv wlnaialvli slatyfiavp vfglvl
//
LOCUS       WP_284793048             484 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium coyleae].
ACCESSION   WP_284793048
VERSION     WP_284793048.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..484
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=52227
     Region          16..400
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msstvqrrsg lpaltrrihf yaglfiapfv fvaalsgaly avapslenvv ykdvltvpas
       61 dtnaplasqi raaqdthpdm dvaqvwpsst pdeatrvlli desltetnql rsifvnphtg
      121 dvigdeptys glgelplryw isslhkslhl gevgelyaev vaswlwvval gglylwwrma
      181 rkralvglen atgrrrkvln lhgvagtwll vamlglsatg itwsvfagen vdrtitwlgg
      241 kaepietslv adaeaapade hadhhpasah gaegltkdev adqaatvlet araegltgsv
      301 rlfvpkntde awqaserwvp wrttsdavsv ngqngdlvdk lpfselplfs kltswgiylh
      361 mgimfglplq illaicalai camvvmgyil wwrrrptkna iagvpgqadl tgrdwailav
      421 vaipvglflp llgltfaaml vadrllarrr tafttpekep vplaadervg vsgdeaelgl
      481 vevg
//
LOCUS       WP_284793247             378 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Corynebacterium coyleae].
ACCESSION   WP_284793247
VERSION     WP_284793247.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..378
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41145
     Region          1..375
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mnaplsgirv ldlsrvlagp fcsmiladlg aevikvespw gddsrqfgpf vdgtsayyrl
       61 fnrskmgitl dfkndddkev lrdlvrradv vvenfrpgvl eklglapkdl leinprlvvt
      121 sisgfgqtgs lakepaydlv aqamsglmsi tgwpnskptr vgislgdlip glyaaigtvs
      181 alyqrestgt gqhldlamyd slisvmesvg mralyddtpp trigndhgls apfstyatkd
      241 gdvviaittn rlferlsnal gmpelatdhr faepvarsdn rvalreliee alstktrset
      301 ialfeehgvp tarvydldea lrspfaqerg vvveetdgfr tlasplklag mekptpapel
      361 gqdneriqsw lsedprtt
//
LOCUS       WP_284793256             283 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Corynebacterium
            coyleae].
ACCESSION   WP_284793256
VERSION     WP_284793256.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..283
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30706
     Region          37..230
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mklrayrgfn vpqrftgspa hrteaverfy qglvgtlrra mralnidatv igaehipteg
       61 galiagnhtg yadfilmgtg pylrgerlvr fmakqevfdv pvlgrllrkm hhvpvnrahg
      121 staiapaver lrsgnlvgif peatisrsfe lasfktgaar iahqagvpli pcviwgsqri
      181 wtkdlpkhfr nvpvivryga pveltgdaea dtaelkrqmq llldesrtey talagpgtge
      241 pwlpaalggt aptieeadri haeeraakaa areakaakkg rkp
//
LOCUS       WP_284793282             442 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium coyleae].
ACCESSION   WP_284793282
VERSION     WP_284793282.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..442
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=47887
     Region          1..440
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrltvigtgy lgathaacma elghevlgvd vdehkiealk nskvpfyepg lpevlernid
       61 agrlsfttny deaanfanvh figvgtpqqr gsyaadtrfv eaviddlvpk lhghhvilgk
      121 stvpvgtaaa lqeraddltr ragrgatvei awnpeflreg yavkdtiepd rivlghrsen
      181 shaeeiarev yatplangtp fivtdlqtae lvkvsanafl atkisfinav sevceivgad
      241 vtqladaigy ddrigrkflg aglgfgggcl pkdirafmar agevgadqal tflrevdain
      301 mrrrqrvvdm areelgslig rnitvlgaaf kpnsddvrds palavagqls laganvtvfd
      361 pqamdnarkv fptldyadtl eealrgaelt ilatewgqfr emdpewvagv vekqllidar
      421 nvldvqqwrn agwemralgr tl
//
LOCUS       WP_284793329             541 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Corynebacterium coyleae].
ACCESSION   WP_284793329
VERSION     WP_284793329.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..541
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57809
     Region          86..536
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 madksfdpea raayealraq lgddalegid iadlesgrdt dfghlemtdh gitlnladms
       61 aesgadgsda dtdepaptla pegdhpdfdk vvaqldaraa andpnpsldr iamlmdllgt
      121 tqqsfnvihv agtngktsta rmaesilral nrrtglftsp elervtecil idgeeisqtr
      181 fvdvwrdiep yvdmvdahfr ergeaemsrf ellvgiayaa fadapvdvai vevgmggtwd
      241 atnvveadvs vitpigidhq rflgetieei aahkagiika rerdgygpae niaivaeqep
      301 eamqvilera vetgaavarq grdftiddss vavggqqlsl qglggvyddi flplsgahqa
      361 enasvalaav esffgvsreh pldmdsvrqg faevkvparv ervlgdpvvl idaahnphga
      421 atlaeamqrd fnyqsvigvv sifadkdara mlaalepvla dvvitqntdp ramdayelae
      481 iayevfgder vrvddnlpsa ielaielaee egpegvgvli tgsvatagqa rtylrssrgv
      541 q
//
LOCUS       WP_284793341             315 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Corynebacterium coyleae].
ACCESSION   WP_284793341
VERSION     WP_284793341.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..315
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=34236
     Region          1..298
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 meqraeagki segtlaaykt pyervkaerg hllirectap rlgawveeaa egkpsvhrsl
       61 rrvlsqafdf gesqgivtfn pgraiptmet atketnalta qeavrlrsvi rawedehvgk
      121 skpgtggrpl qpylgdvvdv mlgtgfrige vlglrwedvn fqanpvevtv sgavkqrkat
      181 pdspslvwep rpktkkglrt vsvptftada lhrlfiekap davfvfatsk gtprspanvr
      241 trlrrvcgst fegltphtlr rtvltivaeq tdvltasrla ghastkitee kylkfgpkap
      301 daswalesig agets
//
LOCUS       WP_284793503             385 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Corynebacterium coyleae].
ACCESSION   WP_284793503
VERSION     WP_284793503.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..385
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40981
     Region          3..380
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 maetfdvvvv gagiigaata yycaeaglrv avvekhtaas qtsshcegnl lvsdkengpe
       61 lelakyslgl wrgelsqfae eiefepkggl vvatndqtme slqralaaqr eygidveels
      121 pqelrdkepf itddavgaaw ypqdsqlmpm atvncflana vrlgarlyeh npvqelitng
      181 ttvvgvrcpa gdfhaktvvn ctgpfaagvs eqwgamplpv eprrgyvlvt qradmtvnhk
      241 vysasyldnv vssdgglqts pvvestqagt iligssrerv gfsnevsqda lkgiaqnaia
      301 lfpglskvnv lrfyhgfrpy cadhvpiigp dtrldglwha tghegagigl sagtgklisq
      361 altggigstd vplddflpsr fetar
//
LOCUS       WP_284793555             841 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium coyleae].
ACCESSION   WP_284793555
VERSION     WP_284793555.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 841)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 841)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 841)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 841)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..841
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..841
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=90682
     Region          59..840
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msnnehldnc ieearhaarq agidpgtatw dldgelvrpn asyafelegi edgpqltdia
       61 ealealpgvs arlvyptkma wvtapastpl veltdtierf gvtatvtdst lqrrahgryw
      121 qehpmprrak hrrneeanli araqgfvrpv srrsrregdv lftardlvtp trlvvavllt
      181 ipvllltyip sldfpdwqwv cfalatpval wcaspfhram aggvrrgisa ldgassiail
      241 asyvwsfaml lftsvgdigy tttgswmplr msdspelyfe vsctvttlll fgryfsmqvr
      301 tdlreelesr rpgaedvynv dhrdkrgtps peelpateir rgddvtltag hiipvdgevv
      361 ggsgriggel vdthrdqilk vgsivtagsv lasgeikvra arvghttlla avqrwlddas
      421 rhqnaatmvs trsagllipt ayviavlnfg lwllfngnin taaatslail vvvapvslai
      481 spalamrqgl dsavrhgmlv rdgnalrtla dtdmvvfnrv gtlvkpemhv etvtavrges
      541 telvlriagv lsadsdhpas kaivkaarga rdarsgdpri pdwieangdt fspdgefggp
      601 itatwgtgen arsetfaasl wrptnlsqlh gklsvaattg gtpvvvrwgg rdrgvitlyd
      661 pakddaiqai drlesmgvet vmltrdtypv arrfadflgi sqvlagihgl dkphavralh
      721 tqgsnvamvg dasvlptlrv adsgilfaed dlagtkeprw sddaevvlir edvmsvpqli
      781 ehaqrvkria nsnlafavay natavvlaaa galppvgatl lmlgsslfie aksrrarrfk
      841 i
//
LOCUS       WP_284793606             731 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium coyleae].
ACCESSION   WP_284793606
VERSION     WP_284793606.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 731)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 731)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..731
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76108
     Region          9..729
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtqppvalqq ielgvtgmtc sscssriqrk lnkldgvdas vnystetasv sfdpsststq
       61 llidevraag ydafemgdet ggmtggdggs stsnaldear dneaeqlkrt tiwsalvslp
      121 vmlvsmihgl qfpnwefaal aattlvffsa gsvfhratwv nlkhgamtmd tlitlgtsaa
      181 ylwsiwalfv ggpgepvyle tacvvitfll lgrwfetrak gqssealrel lsmgakdaav
      241 irgdkevrvp isqvvvgdrf vvrpgekvat dgrvisghsa idesmltges vpvevsegsm
      301 vtgatlntsg rlvveatrvg settlaqmgq lvkdaqagkv pverlvdris qvfvptvvvi
      361 slitlvghll vghavedaft aavavliiac pcalglatpt ailvgtgrga qmgllikgpd
      421 vlestrqvdt vvmdktgtvt tgqmgvadvl pgpgyeadev lslaagveag sehpiaqaiv
      481 eaaddvpeat gfenlpgqga sariddrlvr vgrptgdlga ladafteaeq rgatavavev
      541 dgvvagviav rdtvkedsrd avarlrdlgm tphlltgdnq gaaeavaaev gidpanvtsg
      601 vlpedkvnvv krlqesghrv amigdgvnda aalaqadlgm amgagtdvai easditlmhs
      661 slrsavdair lsrktlktik gnlfwafayn vllipvaalg fldpmlagia mafssvfvvs
      721 nslrlrafks a
//
LOCUS       WP_284794128             232 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284794128
VERSION     WP_284794128.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..232
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=25367
     Region          1..223
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mlfdslprps eriapgvahl pgwlgvdkqa klvhevreia rtyadtsmam lrptlksggq
       61 msvyqlhlgr ywhypsyryv dkiagttvpp vpeslvalap valraaaeva eelapwvetf
      121 vpemvlvnyy ppgsgmgmhv defeesrapv islsigdeal frmghtesrt qpwddvtlcs
      181 gdlvvfggpk rfayhgvvrv ndatlpdgcg laegriniti rqvsaapkgr er
//
LOCUS       WP_284794323             763 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284794323
VERSION     WP_284794323.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 763)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 763)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 763)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 763)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 763)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..763
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..763
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=84489
     Region          32..763
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mtdnkaakrp spsvrsmsar larsltsgkv kikpvleplm sihrefhpka dadvinraye
       61 taerlhegvt rnsgdpyith plavatiaae igmdtttvva allhdtvedt dysledltrd
      121 fgtevtrlvd gvtkldklaf gsgaeaetir kmivamskdp rvlvikvsdr lhnmrtmrfl
      181 ppekqakkar etleiiapla hrlgmasvkw eledlafail ypkkydeivr miadrapqrd
      241 rvlkeitsev sstlkangie aevrgrpkhy wsvyqkmivr grefaeifdl vgirilvhdv
      301 nscyaaigvv hglysalpgr fkdyiaqprf gvyqslhttv isgagkplev qirthemhhn
      361 aeygvaahwr ykelkgknsg kdaevdqmaw mrqlldwqke aadpneflds lrydltssqi
      421 faftpkgdvi tlpagstpvd faytvhtevg hrcigakvng klvalesalk sgdrveifts
      481 kdpnagpsrd wqnfvvspra ranirqwfak emrevhleag rdalaaeiqr gglpmhrlft
      541 tssmkqvatq lhypdidaly taigaghvsa qhvanqlmam fgdqedavda ladrtplsel
      601 lqskqqaahq dhnrsgilve gnpdvlakia kccqpvpgde ifgfitrggg vsvhradctn
      661 atklrdeper vlkvswannv dtegafsatl qlealdrqgl lydltgifqk sslsvlsmns
      721 qssedhvatv rftftvsgsk qlgalmntlr ntegvfdvyr vta
//
LOCUS       WP_284794374             936 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284794374
VERSION     WP_284794374.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 936)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 936)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..936
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..936
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103548
     Region          2..934
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtsthfetfr sqltyeldpf qvqgcraven grgvlvcapt gagktivgef avslalsrgt
       61 kcfyttpika lsnqkfhdlv aihgedavgl ltgdvsfqpd adivvmttev lrnmiyaksp
      121 aldrlthvvm deihfladqa rgavweevil nleehisiig lsatvsnsee fgrwlstvrg
      181 dtevivsehr pvpleqwmli gqkvyplfap gtpaiegptt sepagvnpel qrrvarleag
      241 daadgrddfr pgqgfrsrtt agtgnsrsgn vrpqdryrpl grpevlrilq gqnmlpaiif
      301 ifsragcdga lhqclrskmv ltdedeqrii tevidagveg iphedlevlr fsqwrkalir
      361 gfaahhagml pafrhivekl fvrglvravf atetlalgin mparsvvlek lvkfngeahv
      421 dltpgqytql tgragrrgid tlgnaivqwa pamdpqrvag lastrtypli stfepgynma
      481 inllnnlgmd dslrlleksf aqyqadgsvv eetreierav hrveklreql neaiaafapp
      541 sfddqdpaql lseyvelrkr lsveekslks rakdergdet railaklqpg dvialpskkr
      601 pvlavvntpa nqtadprpwi ttekgwsari dvsgfdnppa lvgkmklpgk alknprrhnh
      661 ivvdkfared yprpkkmklr arirdterik dlrtqmkkhp ahawpamere qltqlaqkyl
      721 rrkgeldklr atvdkatetl gdmlrrivdl lteldyvdiv dgepvvsieg eklaqvhnas
      781 dlliaqclkr giwqeldpae lagvvslctf enrratggql fdgvtdamts amentmrlwe
      841 elisdesrhg lphtrepepg fsiaihqwca gaplgyclaa aaesgaeltp gdfvrwcrqv
      901 idllqqvakt gysseikrta gqaiasinrg vvaigs
//
LOCUS       WP_284794447             773 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284794447
VERSION     WP_284794447.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 773)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 773)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..773
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=85713
     Region          23..768
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 msprrttgqq stgsqrtkrv hhsnysaela aeqsyvdalf gildsdvsqa rqrladaqlt
       61 idpanadsda llrreteyhr lqekldqlnl aqiglvfgri dvdakgenpt segldrryig
      121 riglmdrddd yrsllidwra pmarpfylat tahpegvrvr rhirttdrvv kdiddellsg
      181 tapadadrad vageaallha mnsargehme sivetiqreq daiirdstrg vlvveggpgt
      241 gktavalhrv ayllytwreq lsrtgvliig pnptflnyis qvlpelgetg vvlstigrly
      301 pglrptlhdt adtrrvkgsl qmvdvlkaav kayqhvpkhs revvlegtrv eltptmvkta
      361 rtkarrsrkp hneareifse qlqellaqgl aeiighdpld ggnllnsadi salhedisde
      421 aivdelvdef wpqlgprqvl rellsdhetl haacrgngge efasalwrse qgwsdsdaal
      481 ldelaqllgs gddeqqaaad eqewrealee aegaldilat sestdnddvf dseilsahhv
      541 idaetlarrq qardyrttae raegdrtwaf ghvvvdeaqe lsamewrmvf rrspnrwmtv
      601 vgdpaqtssp agcdswseal epfvgkryrq hqltinyrtp veiaelaesi vhkyspdtav
      661 aqairnrkga vrwlpsgtsa eevrdqlrad etaasaeddt adqnqrsyai isahnaatyk
      721 glefdhviiv epeeiiaass rgwqdlyvac tratqtlnii gtldlaglkl drh
//
LOCUS       WP_284794529             337 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284794529
VERSION     WP_284794529.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..337
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35646
     Region          24..332
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkkslatali agvavlfgai algpqriala dqatgnkrla aelaelavpg hnqltaltid
       61 dgvteyagwg adseteveig svtkmmtael lrheiknkev eldttlgeli delhepvasv
      121 tleeavnhtg glprmagvnf asnlgfsvlg tnpyqgigrd dvfaaandie elenrgeeqy
      181 snlgfallgw alaenagtty eemlndvlfr plgmhntyva sqplpddqpa gllnngrhaq
      241 pwvtegyapa gmvrstaadm akfaeylleq glpdygwapt vstddkdsga gwhngqtggy
      301 samlvvapet aravfvagnt prgveqiglq lageevr
//
LOCUS       WP_284794702             549 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284794702
VERSION     WP_284794702.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..549
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=59912
     Region          145..534
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 msesepqkap eptagwgapg erkrrsyray rthrplrlrt wlvvltvlvs afglfassfa
       61 vysvmrevfy qrvdddltqs magwaqnsel fsgnlsaspp tdyavihifp dgssrvyndr
      121 dtlpqinnlv igggprsvas vdgpqqpewr alanqqngvv tivaknlere ngllrglaml
      181 qalislvmlg flallafavi rqtlkplqiv ertasdiaeg dldlrvpkwp lntevgqlaa
      241 alnimlerlq dsvetaqske eqmrrfvgda shelrtplts lrgyvelyrs gatndvdhvf
      301 atiddesgrm kllvedllal traegsrldk rtvdvlelsl avvgtaraay pertirvenk
      361 ttdipvvsgd pdrlhqvlln litnglnhgg peasvtltlr kesqddcmrv aaeqqeagdn
      421 yeaeektsgw sqedgkngka gkdgnkgtdg esakgyvcid itddgrgmsk evtgliferf
      481 yredpsrarg agggsglgla ivkslvdqhd geitvdsepg vgstftvrip aldepsasee
      541 tfddygeny
//
LOCUS       WP_284794724             135 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: thioredoxin family protein [Lactobacillales].
ACCESSION   WP_284794724
VERSION     WP_284794724.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillales
  ORGANISM  Lactobacillales
            Bacteria; Bacillati; Bacillota; Bacilli.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 135)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Lactobacillales"
                     /db_xref="taxon:186826"
     Protein         1..135
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14857
     Region          <52..127
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 mkhpfrhfli ntvigvviat aslsalyvya pkaminvatp itinaqkkdq yilyysptcp
       61 vcqqvyctyf wrsvtgqlkf asvaneqnre aaaalgitkv ptlvhykkgk vvtqytghre
      121 qqidkvlagg kageh
//
LOCUS       WP_284794779             196 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284794779
VERSION     WP_284794779.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..196
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21642
     Region          4..134
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 madnpaihqy rvplrwsdfd ryghvmnany veiaqearla ykeayfdpag medfaafvrk
       61 ldldfrkpie pegnsvllve sqvvevgnss fvtrqeikdk hgriacvvet vsvavdmdtq
      121 mprplteqer evmrlestla kaadkaeaes gsapsaggvq adslgdeisy dddisygdev
      181 gygdevdygd eigydd
//
LOCUS       WP_284794902             413 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284794902
VERSION     WP_284794902.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..413
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45541
     Region          122..398
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mpsslfqraa alaltaafsl pavaavssav atpqahaqqf ssetssriaf dgssapmaew
       61 skdpavqghv lnvlqffqnh tpwhqlpmwn lwgeqtpyti dkeqdfaqpr lihreaderf
      121 averlyvesp amrrvvqvqv qypkdrnaaa pmlylldgvs aprqsgwlrk gdvqgtmane
      181 hvttimpvea ggtnytdwna tdpylgrakw etfltqelpg vmeqqtgipf ngeryiggls
      241 mggsaavrla nlypqlysgt fsvsgcyssi stagrayfdl aalvmggnpe lmwgpgntpe
      301 rlrndvvsdp kgiasmpvyi ysangyateh dielarpegi ptffgnitle kltnqctael
      361 ehslqekglm heriefdhaa tgihdwpyyk qqlpvawasv tqgkytypnq aen
//
LOCUS       WP_284794911             313 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284794911
VERSION     WP_284794911.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..313
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33967
     Region          137..295
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 msssrnafqr kpallwtlva lvvalavliv vavvrsgdde smsaggqdam hgpqapssaq
       61 sgnsdsqstp mpggeyspeq arelakqvep gtdfsrpnsp dptiigpgae itsnddilnv
      121 hrrnaedpfa mgaldapvvl sefsdfecpf ctrfavetap klkekfvdtg llriewndlp
      181 vngphaetga qagraagnqg kfyefhdvly nntydnqtgg hpgydvadyv rfakeagied
      241 lekfrteien eqyrdvvrqa lhyassigmr gtpafilgdr fisgaqpyev fedevyrqla
      301 kvadgtvphp ksk
//
LOCUS       WP_284795088             246 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284795088
VERSION     WP_284795088.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..246
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25900
     Region          11..243
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(29..30,32..33,36..37,74,78..79,82..83,107,111,118,
                     121..122,127,142,146..147,149..151,153..154,157..158,
                     161..162,181..182,184..186,188..190,192..193,195..196,200,
                     203..204,210,212)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(145,149,152..153,155..156,195,198..199,201..206,
                     209..211,215,217)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mkqstastaq vpvgkpvhfl hpltviiigv sawvaalsis wpllhaalia lgwlagiags
       61 rslavpatsi alsipaglsm llvhaphgeh qiaplltsdg lvtagelalr fcalmtslla
      121 amanvhipdl lkalqhlglh hsvvyvlgas lqllpqasal isevatanrl arrkvtlttv
      181 iprmiipvit rlltrgadrg ialqgmgyda pgrrtvlypv rahrweillr ltfpaaaigl
      241 vvlawi
//
LOCUS       WP_284795102             345 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284795102
VERSION     WP_284795102.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..345
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35567
     Region          16..340
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mhtsapsryv hlagirfyra slctsavlvl viiaaaivgl llgdypmtlg qtvaglfglg
       61 ddpliryfvq dqrlprvfga lmvgaalgla gnifqrlsnn plgspdiigf stgsasgalf
      121 aiiilqagpa aigvgamlgg vasatlvyll siknrkvsgt qlvlvgigva ailqalnsil
      181 ivraelgpaq taaqwlagsl nattwpeigv lvailavvvp lalllarplq imlsgddlaa
      241 glgvrvhrrr remiavgvvl talsvaiagp iafvalaapq larrfdpgva mvnsglmgav
      301 lvllsdiiaq rllapvqlpv gvvtgslggv yliwlllrkw htndk
//
LOCUS       WP_284795113             378 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284795113
VERSION     WP_284795113.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..378
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40592
     Region          7..367
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mvatsvsasv pqridclegi ralaavgvli thvhfqtasg pvvlerfdyf vavffalsaf
       61 llwrrpigpg flrkraarvl paylvcvavv alalpaastm gwqqllanlt atqiyipdgl
      121 apglthlwsl cvefafyftl pliawvllrw qartrvlvlc avgiaslgwa flpfvagfdg
      181 sdgaswaasv nrqiwppayt lwfvvgmlaa eaesagiakr pgvvrrilgm kplfwalata
      241 clflasweai sprglthpsp lefairislg tvfaacivvp yalrptqsgl llsqpvqavg
      301 rwsyslflwh vavlsiafpl agiemfsggf viilaltlgl svavaaisyt lveeparlwl
      361 rqatapaakh vasklspa
//
LOCUS       WP_284795146             391 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284795146
VERSION     WP_284795146.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..391
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42751
     Region          29..148
                     /region_name="Creatinase_N"
                     /note="Creatinase/Prolidase N-terminal domain; cl46291"
                     /db_xref="CDD:480631"
     Region          31..390
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 msshnnstaa dsaahstyip vtadhfrarl akaekivaeq nlagflvspg pefqyltgst
       61 fssheratfl vlragkdpva vcpetdvltl qqenldelgf rfeawrdgqs pyeitrklle
      121 ensehkavav anamtadhvl rldaalpnhs ielgsdamsq lllakgeeei sqlaaaaaai
      181 drvheqvpal lrdgaterev adklhdlilq ehhsidfiiv gcgenganph hsfsdrvlrt
      241 gepvvvdlgg afgdgyrsds trtyvvdgav dkapqefrda yevvtrafha areaakpgat
      301 aesidraare iiteagygen fshrlghgig lsthedpfyl dgnkqrvqeg ftfsiepgiy
      361 vegkwgmrle divvleedgp rhlnqqprel r
//
LOCUS       WP_284795467             482 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Alloscardovia omnicolens].
ACCESSION   WP_284795467
VERSION     WP_284795467.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..482
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51848
     Region          <300..354
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 msspiytfah ifggttvldn pdelhtyacq minyaeqlem ntsamqqmhs yihqrsmtia
       61 tcaahsgash pssahcanlc tvlaqhvqsa lsviaqlrhi ancmmrsynl ysqteaqtsr
      121 iisaltmaaa yhypvptafa lgawstirem tsphasliga ltnsrsaqed ylsgvsrifs
      181 pcegipgvad alahpvspls sthtsyamni kavsvsaplp aahnlhdtiv nleklsigqp
      241 gnsygtvaiq rythtdgshs wivtipgtdg kkdspfgwsq nlslmssreq treqahslla
      301 vrtamhragi kagepvalvg hsqggivaaa lasdaqqpyt iahvvtagsp iahhpiatkt
      361 twvtsietdr eivshldgrs npkhphwltv rgvisdsasg lannatapnp apahstfpsp
      421 tpvahaaekh elthgmnyhr atledaqklh nenlnehdqh irtltegtmd knmyfrcris
      481 sn
//
LOCUS       WP_284795809              98 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase, partial [Alloscardovia omnicolens].
ACCESSION   WP_284795809
VERSION     WP_284795809.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 98)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         <1..>98
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
     Region          <1..>98
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 tesevadeis aaileeghva idfvivgsae nganphhdfs drvieegdvv vvdiggtlpl
       61 gyhsdctrty vvgkpgekea aawaalrkaq eaavaavr
//
LOCUS       WP_284795906             530 aa            linear   BCT 25-DEC-2024
DEFINITION  N5-glutamine methyltransferase family protein [Corynebacterium
            propinquum].
ACCESSION   WP_284795906
VERSION     WP_284795906.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Schubert,H.L., Phillips,J.D. and Hill,C.P.
  TITLE     Structures along the catalytic pathway of PrmC/HemK, an
            N5-glutamine AdoMet-dependent methyltransferase
  JOURNAL   Biochemistry 42 (19), 5592-5599 (2003)
   PUBMED   12741815
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..530
                     /product="N5-glutamine methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=57536
     Region          <158..318
                     /region_name="RF_mod_PrmC"
                     /note="protein-(glutamine-N5) methyltransferase, release
                     factor-specific; TIGR03534"
                     /db_xref="CDD:274634"
ORIGIN      
        1 mtthansttp hpaerfgeaa kelieyfaai gfdsaglaah lgpdylsalh rgdpgalrfr
       61 tqqatefdql iqafilrdpv ekehfsqllg adladkvida niavcngpai vrvvidvrph
      121 vingkprwvf sdpdaamvcq dpaedhvpgv gaaslsllqf cptepvasvl dlgtgsgvqi
      181 lgqadaaqkv tatdvstral aladatirga niaekvelra gswfepvvgk qfdrivanpp
      241 fvvgsteith tyrdsgldld gaselvvsev adylapggsa yllaswahsg eipwqhrvas
      301 wlpshgvaaw vlqrdfadpa lyvstwlrde aidprsheas ersaewlqhf adhdvhaigf
      361 gyiaiqdigd qpseiiaedi pqafddrlad evseyfvraa wlreqssedi anaryqlrpq
      421 vareiievpd taagmgfqpq vyrltrmdgp rwshevdehv aaivaglnpe glplrevvsm
      481 yaaahnisnv damrtedfnn nddellrqav gviadlvrhg lvipadlvdd
//
LOCUS       WP_284795924             936 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium propinquum].
ACCESSION   WP_284795924
VERSION     WP_284795924.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 936)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 936)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..936
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..936
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103400
     Region          3..934
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mmsthfetfr sqldyeldpf qiqgcvaven gqgvlvcapt gagktvvgef avslalsrgt
       61 kcfyttpika lsnqkfhdli dvhgpdavgl ltgdvsirpd aeivvmttev lrnmiyaksp
      121 aldrlthvvm deihfladqa rgavweevil nleehisiig lsatvsnsee fgrwlsavrg
      181 dtevivsdtr pvpleqwmll gqkvyplfap gtdiagddva eratkvnpel qrrvarleag
      241 daddgradfq agqgfrsrsv kgtnssrsgv vrpqdkyrpl grpevlrilq gqnmlpaiif
      301 ifsragcdga lhqclrskmv ltdndeqrti aeiidagveg ipqedleilr fsqwrkalir
      361 gfaahhagml pafrhiveel fvrglvravf atetlalgin mparsvvlek lvkfngeahv
      421 dltpgqytql tgragrrgid tignaivqwa pamdpqrvag lastrtypli stfepgynma
      481 inllnnlgmd dalrlleksf aqyqadgsvv eetreierav hrvdklreql ndaiaafapp
      541 stddedpaql lseyvelrkr lsveeksakt rakeerndet railaklqig dvialpskkr
      601 pvlavvntpa nqtadprpwi ttekgwsari dssgfenppa iigrmklppk avknprrhnh
      661 vvvdkfakek yprpkkmklr arvrdtqrit kirtamkehp ahawpalere qltqlaqkyv
      721 rrknelarlq dtvdkatdtl gdmlrrivdl lteldyvdvi dgeptvsaeg eklaqvhnas
      781 dllvaqclkr giwqnldpae lagvvsmctf enrratggqv fegvtdemtt amehtmrlwe
      841 eliadearhg lpntrepepg fsiaihqwca gaplgyclaa aaesgaeltp gdfvrwcrqv
      901 idllqqvakt gysgdikrma gqaigainrg vvaigs
//
LOCUS       WP_284795959             441 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium
            propinquum].
ACCESSION   WP_284795959
VERSION     WP_284795959.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..441
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=46336
     Region          1..440
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrltvfglgy lglthaacma eaghevlgid itparvaqlq agqvpffepe laelvargld
       61 sgrlrfscdy qqaadfaqlh fiavgtpesa aspaadtsav eavvdklapl lrgehvvvgk
      121 stvpvgtaar lqeracsnsp atvdvvwnpe flreghavad tlqpdrivvg tgtaasvave
      181 tlrevyrlpl ergtpflvmp wasaelvksa anaflatkis finaiaevce aagadvtava
      241 ealgyderig pqflraglgf gggclpkdvr afraradelg agdalaflgq velinarrrh
      301 rvvelactll aqkglsvsga vitvlgaafk pnsddvrdsp alavagelal rgarvrvcdp
      361 qalvnaravy pgleypesla dgmagadlvi latewreyre ldpvwaaglv aepvlidarn
      421 aldlarwrga gwqvhalgrg g
//
LOCUS       WP_284796786             433 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Aerococcus urinae].
ACCESSION   WP_284796786
VERSION     WP_284796786.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..433
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48652
     Region          1..424
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mdyeefekdl pvlergkwtl gldhirdlma vfdnpqdklp tvhiagtngk gstasmiart
       61 lqlagykvgl ytspslvsfn eriringeni adeklramkd ymkeklagtk iqcsefelft
      121 amawlifyhe gcdiivlevg lggrldatnl vksplvsvit kialdhenil ghtiseiake
      181 kagiikyytp vvvypypkea ievlsetaer qgaplktidt esienihpdn rqqvftykge
      241 dyqlnllgkh qvlnaclaie alaeikragf nvelkqikeg lqtvswpgrf ewvhqdpeii
      301 idgshnldgv ramrhavedy fpniprlait gmlkdkdvyr mlgevvhlfd eivtitpdsd
      361 ramtaneltk aahmvtglqk vktytaknne damayarrwa dqqegdclic ifgslylvge
      421 lrelvfesfe adq
//
LOCUS       WP_284797043             645 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Corynebacterium propinquum].
ACCESSION   WP_284797043
VERSION     WP_284797043.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 645)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 645)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 645)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 645)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..645
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72365
     Region          1..485
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mrfttlrisn fqsfgltptt lnltdmtyvl gangtgktaa lealsrlfsp vttqrkiris
       61 dfhvpvgssl adlqdkeavl wievdiefpe sdsdsyhasi pphfhhmmie sadgvpkvrv
      121 rltarlaldg vveerieyvr qvnesgaptn ctemsrydrg yievhylpar rdpsehiayt
      181 atsligrtlr aadwsqertt lsglseqlnn altsngavss mgihlkkqwd glhhgkfftd
      241 ptigfgqgel egvfrhltin fspshdgasl pfnllsdgqk sllyislvla wqslsrrvlr
      301 neeasldptr lrppvhtiia leepenslsp hylgriirql hnackeedvq vliathastl
      361 lrrvepesic flrlnekret tvhrillped ndetakyvre avraypelyf srlvilgegd
      421 seqvvlpril aaagiaedda svsvvplggr hvnhfwrlln elriphvtll dldsgrrgag
      481 wgriryalnq inqirpktya ketidglpkw dspvdfpqfv dpqfpegngl vqrlerhgvf
      541 fsnpvdldll mlesfpdayc vtatppdeka ivavlgkshv nekhlpqevl slfddyhanf
      601 dlkskpdthl halskladsd llegmpkvfq rlidhvkknl selpe
//
LOCUS       WP_284797225             186 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Cutibacterium acnes].
ACCESSION   WP_284797225
VERSION     WP_284797225.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..186
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20646
     Region          <102..169
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 miqeswefsl swhrseitei maghlrsall ipiaagveaa iiwalrdwii cgnwpgqgel
       61 amigaatlvv vavimvalea hhwrtatwrs wqttpdwhgg ayvapparrh gpmlmcvhav
      121 prtqghgsqi ltqvcqwade hgltlelkps gpaaerfykr fgfvktsqrv mrreclsgra
      181 dphkgv
//
LOCUS       WP_284797321             290 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Cutibacterium
            acnes].
ACCESSION   WP_284797321
VERSION     WP_284797321.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..290
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30906
     Region          3..289
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mdsalrprrs vlfmpganar alekarsidc dgiiidleda vapdlkvear ertagvvrgh
       61 pygyrevair vngmdtqwyh ddlvaavaag pdaiavpkvs saeqvraiva dmeaagadks
      121 vklwamietp ravldcldia easdrltvli mgtndltkel rashvagrap vvtalqicml
      181 aaraagtail dgvyndvrdv egftaqcrea qlmgfdgktl ihpgqvgpan evfapdaeqv
      241 aeargiidaw esgnglgvvt yhgrmienlh vdtarralam teaieargqe
//
LOCUS       WP_284797623             503 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Cutibacterium acnes].
ACCESSION   WP_284797623
VERSION     WP_284797623.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..503
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=56118
     Region          19..>480
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mirfsqrqal llqllsevdh pikgtdlagl lgvstrtlry diaringisr dniiesttng
       61 ysveqsvytg vvvrnsefst qlehherill ylldtpdtti ydvmrdcyls esvikaslkr
      121 lkpqfedhsl hlslrgssih ldgneiyfrn flgslvntam davvgqndkv nrylpdvrlg
      181 dienlvvesl rdyyleiddi rlsnmvvnia icvqrysfpi gdnaatdlmm snqsemlcdq
      241 llvglrklyp erplssadda ylrsivgatl gfghgeldhh sdscdiystv srclddtveh
      301 fglviakeel ygsvskhvgr lmahapsmpy frntlreslr srspflydaa vyltdklsrl
      361 lgifftddei gllavyigly sepapnpnlv tavvvcpryq alrdvllagl vdhfanrmri
      421 vdivssvaev dmcdgdivis tteepshhht cvpisalmsd ldlsaidsal lrasekksri
      481 atasamkrfl dptlfftgrs fds
//
LOCUS       WP_284797660             495 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Cutibacterium acnes].
ACCESSION   WP_284797660
VERSION     WP_284797660.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..495
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52564
     Region          17..472
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mvstpnsaqd eirhgntapt asgagrgvek rtidmvpdge rhgtpksqft lwfgvnmqit
       61 avvngalaiv fgadvvwaii glfigqvigg avmalhsaqg palglpqmis sraqfgvyga
      121 alplflvlll yfgfaatgtv lagpainnaf gvqsrwigil vfaaltaiia vfgydlihkl
      181 gkvsstigll gllyvavrlf qvssfgpqlt dvhfsvvpfl lsialaagwq ltyapyasdy
      241 srylprdtkf gsawfgpfag svlgatismt lgvfiaaagg qafigdqvgf mgnlaqnrvl
      301 ailvfisivi gkltintlna yggvmalsta lsgftgkssv spktrfgfvi gfnvvvvlta
      361 laassdflqv fksfiltllm fflpwsainl ltyylicrrc idipalytpr grygklhwpt
      421 ivvyllgvvv qipfisqafy vgpvaaamgg adiswlvglv vtalvyfplg rrafdyplei
      481 vypkdveldp sigsr
//
LOCUS       WP_284797796             503 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Cutibacterium acnes].
ACCESSION   WP_284797796
VERSION     WP_284797796.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..503
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=56280
     Region          21..>480
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mirfsqrqal llqllsevdh pikgtdlagl lgvstrtlry diaringisr dniiesttng
       61 ysveqsvytg vvarnsefst qlehherill ylldtpdtti ydvmrdcyls esvikaslkr
      121 lkpqfedhsl hlslkgssih ldgneiyfrn flrslvntam davvgqndki nrylpdvrls
      181 dienlvvetl rdyyleiddi rlsnmvvnia icvqrysfpi ednaatdlmm snqsemlcdq
      241 llvglrklyp erplssadda ylrsivsatl gfghgeldhh sdscdiystv srclddtveh
      301 fglviakeel ygsvskhvgr lmahapsmpy frntlreslr srspflydaa vyltdklsrl
      361 lgifftddei gllviyigly sepapnpnlv tavvvcpryq alrdvllagl vdhfadrmri
      421 vdivssvaea dtcdgdivis tteepshhht cvpisasmsd ldlsaidsal lrasekksri
      481 atasamkrfl dptlfftgrs fds
//
LOCUS       WP_284797803             344 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Cutibacterium acnes].
ACCESSION   WP_284797803
VERSION     WP_284797803.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..344
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35424
     Region          30..341
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 maflvrslhr rtpvrfillv allvltpvls iafgaapvpi gqvlgvladh cglpvhlswd
       61 sitdaivwqn rmprivtglg vgailgadgv tlqavvrnpl aepyvlgvsa gassgvatai
      121 ilvgisstfg vagmaflgal astaivlfmg ggrnsstlrl ilaglavgfv fqaltnfiif
      181 ssdspetara vmfwtlgdls raswaqgwts ivvavvlsil lwicapwlda lasgdstata
      241 vgidpamirv lllvpvsagv aiavaisggi gfvglviphl mrsfighghr rlvvssaita
      301 aiflvwadtf srtvfspael pigvitgllg apfllvlvkr gtla
//
LOCUS       WP_284797918             111 aa            linear   BCT 25-DEC-2024
DEFINITION  peptide chain release factor family protein, partial [Aerococcus
            urinae].
ACCESSION   WP_284797918
VERSION     WP_284797918.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Pel,H.J., Rep,M. and Grivell,L.A.
  TITLE     Sequence comparison of new prokaryotic and mitochondrial members of
            the polypeptide chain release factor family predicts a five-domain
            model for release factor structure
  JOURNAL   Nucleic Acids Res 20 (17), 4423-4428 (1992)
   PUBMED   1408743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10452619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         <1..>111
                     /product="peptide chain release factor family protein"
                     /GO_function="GO:0003747 - translation release factor
                     activity [Evidence IEA]"
     Region          7..111
                     /region_name="RF-1"
                     /note="RF-1 domain; pfam00472"
                     /db_xref="CDD:459823"
ORIGIN      
        1 iestdhieip enelkidvfr ssgpggqsvn ttdsavrmth iptgivvsmq deksqiqnra
       61 aalrvlqsrl lvlrheeeqa kkkelagdvk aswgdqmrsy vlqpytmvkd l
//
LOCUS       WP_284798008             267 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Cutibacterium acnes].
ACCESSION   WP_284798008
VERSION     WP_284798008.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..267
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28830
     Region          7..253
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 matfididdp adprladyvn lrdvnlrksl eaelfiaega kvirraceag ypprsfllap
       61 rwidglrdlf dgldvevfvv setlaeqvtg fhvhrgalas mcrqtrwsaa dlmaarrlvv
      121 cedivdhtnv gaiircaagi gwdgvllapr aadplyrrai ktsmgtvfql pwarledwag
      181 glgelrdhgf tvaamelsgd svtldefsad lrqnprkval lmgtegagls ahwisqadvv
      241 vripmaggvd slnvaaaaav acyelrg
//
LOCUS       WP_284798069             345 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: diacylglycerol/lipid kinase family protein
            [Corynebacterium].
ACCESSION   WP_284798069
VERSION     WP_284798069.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..345
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=38180
     Region          1..325
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mhalmisnpn stsqtnalfr qivpclqave glrlkvqfth hpghaeemvk gmtrddydvi
       61 iavggdgtvn evvngllgpa dgqrpdphsi palaviptgs anvfvralgf pntpveathv
      121 larmlernlr rtiylgtwnd rwfavnagfg ldadvlarvd rareqgfsat plrylnvair
      181 awsrarknpp hiavkaessi geqlrkddvp lmftsntnpw tflgplpvvt nprnsfdegl
      241 alfgleefsg lggvvgllhl fgadkrgwln kltkektvaf ddamrvelvc repqrfqadg
      301 esegrfdavt lasvkeaiev fapqdrrevh krtmkevlrd firlr
//
LOCUS       WP_284798123             146 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase, partial [Cutibacterium acnes].
ACCESSION   WP_284798123
VERSION     WP_284798123.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         <1..146
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
     Region          <62..129
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 iiwalggwii cgnwpgqgel amigaatlvv vavimvalea hhwrtatwrs wqttpdwhgg
       61 ayvapparrh gpmlmcvhav phtqghgsqi ltqvcqwadq hgltlelkps gpaaerfykr
      121 fgfvktsrrv mrreclsgra dphkgv
//
LOCUS       WP_284798397             635 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Cutibacterium acnes].
ACCESSION   WP_284798397
VERSION     WP_284798397.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 635)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..635
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=71386
     Region          29..598
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 msdfnntnrn nlavealflg prsenraffr eslrsvvdeh chwrrnfhpd daplvnrvsm
       61 enesfrktea rsvdildelt arlkktstpw fstrylghmn sdtlmisnla ematilynpn
      121 nvayessvat semeaevgad lcklfgydtn kawghitadg tianyeglwl arnlkslpra
      181 ikatcpdlvs gksnwelcnl rreealdllg qlrndrdtyk qvltasargk gmadgvgrvf
      241 vpgtrhyswd kacdllgigi dnlvhvplad nfrmdlgelr kqletcleqe ipviavvgvv
      301 gtteegqvdd vqglldlree frtrgldfyl hvdaayggyg rslfldedgr ymefeelrar
      361 lqkdglavdg ewpsehtwrs yracseadsv tidphkmgyv pyaaggvifr drrilglisy
      421 taayvfedad agdlvsslgs vtlegskpga svagvwaahk llplnysgyg qviarswgga
      481 rkfshiletl dgievagati qcqpllldpd fnmicmafnv lgnhdldamn elnqeiyync
      541 syqykplyen dwitshtmld revygdspqg fiekfgisga ewekaegvtv lrasvmhpwl
      601 leskeypqvv dnfrcimqrk letvvpkwle rhsqk
//
LOCUS       WP_284798550             646 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Cutibacterium acnes].
ACCESSION   WP_284798550
VERSION     WP_284798550.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..646
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=71069
     Region          35..630
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mvmaasthqp graeldpage llgkpvpgen fieshlahmf ratvanhgfr patrvrqggq
       61 wiirtyaetg rrvaglaraf vtpglltedg lqrgdrislf agncpewiea dlagmtigvi
      121 pvpiyptstp dqivhivtda gvrviitagp keldrilear dqmpgletvi linpadqvgd
      181 hdgltvlsle qvrqagvsee iqtvveermg qscpddvaal iytsgttgep kgvmishraa
      241 laelqaldaf fdvtpadhsl sflplshale wgwsmavirh gclntfvpnp ktisamlaev
      301 rptlfvsvpk lyeqvmsvar ekvsdspakl kifewsirig rewwqaeqeg rrpsvslrar
      361 hgvadrlvlk airdaiggpk tvlaaggapl rkeveeffaa cgllvcqgyg lteasplvsf
      421 nspdgykfgt agrplvgsqm tttedgeily rgpnvmkgyw kapeataaai edgwlhtgdi
      481 ghidedgflv itdrlkdiiv tlngknispq pienslmkdp lfehavllgd nrpcltllvk
      541 pslpqveela erlhitsmtg pemlrseela eeirrrvaei teklphqeqi rdlrvlwdef
      601 ttdnglltpt lkvrrrevek rfteiveemy arlaarrrag krdskh
//
LOCUS       WP_284798763             426 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acid phosphatase [Corynebacterium].
ACCESSION   WP_284798763
VERSION     WP_284798763.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130290
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..426
                     /product="acid phosphatase"
                     /EC_number="3.1.3.2"
                     /GO_function="GO:0003993 - acid phosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=46409
     Region          99..302
                     /region_name="PAP2_acid_phosphatase"
                     /note="PAP2, bacterial acid phosphatase or class A
                     non-specific acid phosphatases. These enzymes catalyze
                     phosphomonoester hydrolysis, with optimal activity in low
                     pH conditions. They are secreted into the periplasmic
                     space, and their physiological role remains...; cd03397"
                     /db_xref="CDD:239491"
     Site            order(189,196,224..226,259,265,269)
                     /site_type="active"
                     /db_xref="CDD:239491"
ORIGIN      
        1 mnyrnklrpa vralalcaat gltitlapaa saalpvavpq lrepvtqqtt gappvqhpga
       61 pvpepfstdy iagfesdvss yqfgnywqvv qlfdhikaqp eirqenmdka vainnaaagd
      121 palirraqad akasstsvln avsdsmgknl gdafraalae hrlpkteyll gngyaaragg
      181 lanstmseky yfnyqrpyqr apqaikrydd gskdlyptsp afpsghtnqa twittlmsfm
      241 lpevgpqlml rgaeagnhrv vlgvhypldv iggrmtgqaa aadrlndkrm rnalwqasme
      301 vrkeikwrtg ktveelvaqd reegtdyrst adaveqystf mdydfapryr tdapmvvpqa
      361 apvllaashp eltwyqraev lrqtarpagn pldwqaeggs wqrldlaram aarvtiapdg
      421 gvsvsg
//
LOCUS       WP_284798816             393 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Cutibacterium acnes].
ACCESSION   WP_284798816
VERSION     WP_284798816.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..393
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42455
     Region          1..378
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrtvgmilsa iigavvgagl mvlmsrvves srhpvdtlat dieaievnsa faraldltte
       61 aavivgphde vlhttlgars melvrgsria netllklvrt arregrdivd tmemkrastg
      121 adliltvrag plddhgnaii aasdssrhvr laetrrdfva nvshelktpi gavsilaeai
      181 egaaddpeai rhfsqrltae ssrlsalvtq iidlsrlqad epllraepva vadvideavs
      241 rhreqaanre vslvvrcddd lwvlgdqsql teavanlvhn aivysepkvr vavsarrvrd
      301 vdtdviaiav adngigisea dqkriferfy rvdysrsren ggtglglslv khtcqahggs
      361 vdvwsklgqg stftlrlptl dvdhhnesdq ees
//
LOCUS       WP_284799121             351 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease [unclassified
            Corynebacterium].
ACCESSION   WP_284799121
VERSION     WP_284799121.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..351
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36778
     Region          40..346
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mqgaevaala rqhkkltwqr igivagltli aavafiisnf vgaidispae vmkgivnpag
       61 lddqtrtvlw qlrlpmavma vligmalsla gaemqtilnn plaepftlgi saaaafggas
      121 sivlkwqlia qpqfnlalma wlaaavatai iviaavirga kaetmvllgi glvfffqaml
      181 aliqyqssae alqqivfwsm gsltranwaa ngvlaavlii alpilwalgw rltalrlgda
      241 ratamgints rlrvvvlivv slvaattvaf agiigfiglv gphiarmlvg edqryflpas
      301 maagaavmca ahavslmikp glaipigivt sllgvpffia ivmtrrralw t
//
LOCUS       WP_284799158             917 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Cutibacterium acnes].
ACCESSION   WP_284799158
VERSION     WP_284799158.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 917)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 917)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..917
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..917
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=100850
     Region          2..913
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 msetldrfia glsfepddyq vkacqdlddg agvlvaaptg agktvvgeya tdlalasglk
       61 cfyttpikal snqkfhdlva rhgedqvgll tgdvtinsea pvivmttevl rnmiyrnsht
      121 ldtlgwvvld evhyladrfr gpvweevilg ldprvkivgl satvsnaeef gewldevrgd
      181 vrvvvserrp vplvqhvava rrlyelfdsr rptevnpelt siakeearfq rddsrrprgr
      241 sgkgkrsvsy gtgrfggasa qrrgrggrpr gprnqpsriq vvrslhkvnf lpaiifvfsr
      301 sgcdaavsql lntdlvltsq qearqlrria qrrgegltde erravgwnhf maafergiaa
      361 hhagllpvik aiveegfvag llkvvvatet lalginmpar tvvleklvky ngqthaditp
      421 geytqltgra grrgidtqgh avvcwqpgmd pravaglasr rtyplnstfv ptynmavnlv
      481 gsmgrekard llehsfaqfq idrrlggsav rnrqtqadie aylkaahcer gnftvyarlr
      541 enireleheq arlrkgelps qvadslssld pgdiiavpsg rhagwvvvvd pgthgtrgqr
      601 prplvmtpdr tvirlghqdi dapvtrvagv kvprhfhpen qadrrclgka fdrvleglgr
      661 pvvkprraav daelsdqite lrsqmkahpc hscpdresha rfaeramrlr rrsereltka
      721 rakatsiatq ferivlvlea lgylgtggdt vtdagrmlsg iyseldlvta eairrgvfdg
      781 ldcpqlaavl stivhesrpg drghlhrmpd gkseaaesql ravragigll erdhrierpr
      841 dldigfaeas yawaagagle tvlddmsagd fvrrvrqvcd lagqiahagv genlahtcrq
      901 vvgamqrgvv tmdreed
//
LOCUS       WP_284799351             491 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Alloscardovia omnicolens].
ACCESSION   WP_284799351
VERSION     WP_284799351.1
KEYWORDS    RefSeq.
SOURCE      Alloscardovia omnicolens
  ORGANISM  Alloscardovia omnicolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Alloscardovia.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Alloscardovia omnicolens"
                     /db_xref="taxon:419015"
     Protein         1..491
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53869
     Region          123..452
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mnnwflniyi drgwvmwtav aittalvlll lpvghkqvvl ahqheqanna qeaharqsgw
       61 wqshwytiia aqvfwtvlmg vlgwiivyll snvfvvfgvg lgdkvfmrva cgfagvgyai
      121 ssavmyrgwr rtiafclipa aivlsalqvn aaygqystvr dvlgmphfte ahsfprattg
      181 vddylekvka gsievpkygr ihsvaipate shfkarhatv yippaaltkd vpflpvlmll
      241 pgqpgnpstf ftaghmgeia dayaskhhgl apviispdql gnrfhntlca dtikygkaqt
      301 ylmkdvvnwm ekklpvttnh kqwgiggfsq ggtcsvelgp ayphlfhyvi dvagedgpha
      361 gsaqnmieny fggnkaaykr hlpkntfssh pyqgqriifg agqldtlgqa ncrnvsqyar
      421 qngwsiqsvm sygsahdwtt vravtayala dfgymnglgd kldfssfkgi thiagiepta
      481 hhahtsrntq h
//
LOCUS       WP_284799356             196 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [unclassified
            Corynebacterium].
ACCESSION   WP_284799356
VERSION     WP_284799356.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..196
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21729
     Region          116..187
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 msakirhalp sdipaaartl alafesypwt rrsiprdnyq qrlyrlqyiy lthavtngfv
       61 lisgksdgva aalppkcpgl ekaqqsevad lmesrfttis qiklpkqpad awtsatlgvh
      121 ptraghglgt alieeclshv srsstprigl etstkrnvdl yrrqgfklvh kthvekeliv
      181 ysmfldmqan tlgenr
//
LOCUS       WP_284799666             157 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Curtobacterium citreum].
ACCESSION   WP_284799666
VERSION     WP_284799666.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..157
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16730
     Region          16..148
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtntltapat adrtastddl drvlrafrtl qtqharvlah qsalrglhat dlrflvfvag
       61 adagvtpkha gehlelttga mtslidrler rghierrpnp gdrrsilvhl tpsgaaiage
      121 vaavyreafr sgvdpadlar vaaaledvgs aldprdr
//
LOCUS       WP_284800014             526 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Curtobacterium
            citreum].
ACCESSION   WP_284800014
VERSION     WP_284800014.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18527136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..526
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=56213
     Region          23..>78
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          91..522
                     /region_name="MurA"
                     /note="UDP-N-acetylglucosamine enolpyruvyl transferase
                     [Cell wall/membrane/envelope biogenesis]; COG0766"
                     /db_xref="CDD:440529"
ORIGIN      
        1 msdtttvvtp adpaapaaat aplrevgali rgarkgrsmt qsqlaervgt sqsainrieq
       61 ggqnlsleml trisealdqq ivsiggapqr shlrvqggrk lsgsiavnss knaavallca
      121 sllnrgvtrl hrvarivevd riidvlrslg atvtwssdge vleivapsdl hldaidadaa
      181 rrtrsvlmfl gplsgrygsf rlpyaggcdl gtrtvephli alrpfgvdve atsgwyevgv
      241 anqdvpahsv vltergdtvt enailaaaar dgvttirnas pnymvqdlcf flellgvqve
      301 gigtttlrit gksridevvd ywpsedpvea mslltagivt sstltvtrap iefleielat
      361 laemglrfdv seeysaangr trlvditvhp selhapidki hampfpglni dnlpffvvia
      421 amaegttlvh dwvyegraih lldltrlgas vtlrdphrld vtgpthfsga evscppalrp
      481 avvillamla akgesvlrnv giiargyeql qerlnslgas ietfhd
//
LOCUS       WP_284800016             227 aa            linear   BCT 25-DEC-2024
DEFINITION  DedA family protein [Curtobacterium citreum].
ACCESSION   WP_284800016
VERSION     WP_284800016.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..227
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23983
     Region          15..209
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mlstlplavs lfdaasvlha fgpyvlagia llifiesgvl fpflpgdsll vtaaiisstl
       61 gvapwqvavv asvaaiagdq vgywigkryg rrlfkddari lttarldeae afftrwggls
      121 lvlgrfvpiv rtyvplaagt aqmhyrrfll fnligaiswa cgltvvgvll ggiplvahni
      181 dalmivivlv silpivigal rkrhvagkrr eaaaeasepa grtagdr
//
LOCUS       WP_284800030             262 aa            linear   BCT 25-DEC-2024
DEFINITION  inositol monophosphatase family protein [Corynebacterium coyleae].
ACCESSION   WP_284800030
VERSION     WP_284800030.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..262
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=26965
     Region          5..258
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mhnpaellda alcavdeare vfvdkvgaap alrkgagdfa teadliieml lrkrltdttg
       61 iavygeeqgg sfdpeacwvv dpidgtsnys sgnpncailc tlllggkpva aitdapllnm
      121 rltavdgepv hlngnalppv galtsaaeqv gigslasadr qrypasfrld lagaltdshl
      181 rprisgsvgv dlafvaqgiy qaavsfsphi wdnaagvlla rsaganasaf dgsewtptta
      241 gvvigtphah rtvldaiqmv ak
//
LOCUS       WP_284800116             332 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Curtobacterium
            citreum].
ACCESSION   WP_284800116
VERSION     WP_284800116.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..332
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35562
     Region          26..306
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtasrgmivd madpssrrla llsllqvhre wpgdelatrl avsprtlrrd vdrlrdlgyr
       61 veavrgpagg yrlgagsdlp pllfddeqav avalalavap asgadiaeaa aralttvrqv
      121 mpehlrnrvd lvdavtapgt tradpevlva vsaavhrhev lrfgygerdt lhrvephavv
      181 arggrwylla wapehddwrt yrvdriaprm ptrlpftprp vpggdaatfv sarlrgsdrd
      241 dvwpctgsvl vraedaarit pflpedavve algdgrsrvt rgswswdgla gafaastvpf
      301 avegpdalra avaalagrlq davgstppsa rp
//
LOCUS       WP_284800142             521 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase 2 family protein [Curtobacterium
            citreum].
ACCESSION   WP_284800142
VERSION     WP_284800142.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450613
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..521
                     /product="DNA-3-methyladenine glycosylase 2 family
                     protein"
                     /calculated_mol_wt=55358
     Region          4..387
                     /region_name="AdaA"
                     /note="Methylphosphotriester-DNA--protein-cysteine
                     methyltransferase (N-terminal fragment of Ada), contains
                     Zn-binding and two AraC-type DNA-binding domains
                     [Replication, recombination and repair]; COG2169"
                     /db_xref="CDD:441772"
     Region          285..497
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mtstadntlh aeryrvvasr darfdgqfvt avhstgiycr pscpartpra sgvtffrtsa
       61 aahlagyrac krclpeatpg spewdlredv agramrlvld gvveregvpg laarvgyser
      121 qlgrimttel gagpkalsra hraqtarall tssdlsvadv afaagfasvr qfndtirevf
      181 avtpsqlrar rvlrpvedgw lhvhlparap fdaqglldwh alhalagleq verddtgrvt
      241 sygrlvdlpg gparftasas atrpagpaag rtgidlrvrl ttlsdlptlv arvrslfdld
      301 adpeavdavl aavpelapav arvpgirlpg hadadevlfr tligqqvsva aartaqtrlv
      361 aalgapvpdd lvpgsrlfpt aaviaehgre vlrgpaarvd tiirvaeala vgtlvvdagq
      421 sldelrdgll avkgigpwta dyvalrvrhh pdvflhsdla vrngaqelgl pgaarelsvr
      481 seqvapwrsy ltmhcwrpiv draaavaets araaaaaaer s
//
LOCUS       WP_284800197             649 aa            linear   BCT 25-DEC-2024
DEFINITION  amylo-alpha-1,6-glucosidase [Curtobacterium citreum].
ACCESSION   WP_284800197
VERSION     WP_284800197.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..649
                     /product="amylo-alpha-1,6-glucosidase"
                     /calculated_mol_wt=68798
     Region          257..645
                     /region_name="GDB1"
                     /note="Glycogen debranching enzyme (alpha-1,6-glucosidase)
                     [Carbohydrate transport and metabolism]; COG3408"
                     /db_xref="CDD:442634"
ORIGIN      
        1 mtttttppda aeqaahavpr qpllhdevvv laaptqawsd rhgdvgtnpv hgywtgdqrv
       61 vsavtlavag ssvepvetvp agarevvftg llrgldgpga dpdvrldrir tvrvdgvher
      121 lritdrlapg qppaersght grtvtvrivp dasgmdavka gappvpvpav lvtdgggtda
      181 graswtagsv svtlradgat vttdgdavvl nwtlphartv evawdchvta pdavaigatt
      241 prtfhapqgv eddrlrrwld ravedldalr lrrpegefla agapwfftlf grdslwaarf
      301 llpvdttvag stlrvlaalq gtrddpatae qpgkiphelr qaslpvdnde islpplyygt
      361 vdatplwict lhdawragmp edqvrallpa leralawmrd sgdadgdgll eyvdesgrgl
      421 anqgwkdsgd svqwrdgrla dgpialcevq gyaheaavhg adlldafglp ggpewrawaa
      481 rladrfratf wvtdavgphp aialdarkha vdsatsnigh llgtgllder eeavvaarvv
      541 apdmasgfgl rtlsttasgy wslsyhggsv wahdtavvva gltrsgfrde aralaeqlla
      601 aavafdfrmp elhagdaaae asrpapypaa crpqawsaaa vfpvwvalr
//
LOCUS       WP_284800149             489 aa            linear   BCT 25-DEC-2024
DEFINITION  APC family permease [Curtobacterium citreum].
ACCESSION   WP_284800149
VERSION     WP_284800149.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..489
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51713
     Region          15..484
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 malrtksiea sladseeqgr slkrslktfd iaamgiavav gagifsvgan aaanfagpsv
       61 iisfllaavt cglaimcyae fastipvags aytftyatmg ellawivgwd liletltasa
      121 viakywgiyl stafgvfgid lpdtiqlgpi gftwgpvliv glftvllafg trlssrvsav
      181 itvikvaivv fvivagaffv kaanfapfvp paeptkgaeg gvltqslvsf vtgsapaqyg
      241 vfgllaaasl vffafigfdv vatsaeeten pqktlprgif iglgivtlly vgvsivitgm
      301 vsyrrlaeed apslasafdi vglpwaagii aigsligltt vvmvlllgls rivfsmsrdg
      361 llprwfsktn pktqtpvrvq vvagvvvafi agftaverle gminigtlsa fvlvsigivv
      421 lrktrpdapr afrvpwspvl piisavlcfw lmlnlevetw lrfivwlaig faiyfgysrr
      481 hsrvckglq
//
LOCUS       WP_284800171             132 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Curtobacterium citreum].
ACCESSION   WP_284800171
VERSION     WP_284800171.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..132
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14767
     Region          10..115
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mheqaeqwpl grllsaaara verdwderlr aiglthaali aidilirtgp tgadtlarta
       61 hvrpqtmslt leraerdglv ertphpddrr rrvvsvtdag raawdtarhi erevlpddda
      121 lrerltkilt sd
//
LOCUS       WP_284800200             272 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium coyleae].
ACCESSION   WP_284800200
VERSION     WP_284800200.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..272
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28598
     Region          12..266
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 maldfeqplt ertprvvnaa klkraagrrk akaflaegen aveaavatga atdlfvteaa
       61 aerfeeivra agymdvytha indkaaqhla davtntgifa vcrpvlwtvp silkgrprli
      121 avcvetndpg nagtiirlvd algadavifa gdtvdpespk vvrstagslf hvpvardrdv
      181 hrvigqlhsa glatvatsas getslaqade vlarptawlf gneahglsde lltnadhris
      241 ipikgsaesl nlataasmcl wesskaldad er
//
LOCUS       WP_284800206             729 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium coyleae].
ACCESSION   WP_284800206
VERSION     WP_284800206.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 729)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..729
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=80366
     Region          1..727
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mqdlqhdlsp dpvadeqsha dtlfahldae varararlee vqrdvdpdnp dsdalvrret
       61 eyhglnakld tlgvaeaglv fgridvadde penpvpgren ldrryigrlg iddrednyrt
      121 llldwrapla rpfylattah pegvetrrni rmrgrkvtav ddevlsgdna dtsvagvgse
      181 aalrramnea rtghmrsive tiqreqdeii rdptrgvmvv qggpgtgkta valhriaylm
      241 ytwreqlsrt gvlivgpnpa fleyisrvlp elgetgvvls tadqlvpgft ptgsdsiaar
      301 evkgseemvt ilkravqaye tvpdkpvvlt idsvaieatp amikaartra rrsrrphnqa
      361 rpffaehltq slaealaqki gedplgganl lsaadvdqlh ddladepqvl alidehfpel
      421 dptdvlgefl tdedaiahaa ydyddytraa llrspeedfs padtalvdel avligtvdpe
      481 earrkeeaew relveeaeda ldilassest dndddqfeae ilsaadvida etlaarqrvt
      541 dnrstaqras adqtwayghi ivdeaqelsp mewrmvfrrc parwmtlvgd taqtsspagv
      601 ddwtaalerf vgqrfrlhel tvnyrtpkei sdyaaevltq idpeattpta irstgipvdf
      661 lpagaevvdk rdglhavidv hnvdemkgle fdhvtvvepq kiveaspqgw qdlyvavtra
      721 tqtltvign
//
LOCUS       WP_284800386             291 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium coyleae].
ACCESSION   WP_284800386
VERSION     WP_284800386.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 291)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19108954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..291
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32456
     Region          33..242
                     /region_name="NUDIX_AcylCoAdiphos_Nudt19"
                     /note="Nucleoside diphosphate-linked moiety X)) motif 19;
                     cd18870"
                     /db_xref="CDD:467582"
ORIGIN      
        1 mptekkrnea vlshdeadsi dpseksgffg arlsatvill rnsaegievw vqervlsmpn
       61 ypgltvfpgg gvdsrdfppr awddgelwlg rsaislarql gvtkykahav lfaavrelfe
      121 etgtllavdd dgtllddarp fhnhrlrles helsltdvlq esnlnvcadl lkpvarwvgv
      181 sesgnwfdtf tfvaanpegq epdsdtwead danwfppqli ldgwrhglvr lapstwaqln
      241 elrrfntvdd vlhaaegasl apvigdpvdd eryeefftfr pvdrigkryd i
//
LOCUS       WP_284800415             275 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Aerococcus urinae].
ACCESSION   WP_284800415
VERSION     WP_284800415.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..275
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31546
     Region          12..271
                     /region_name="YbbA"
                     /note="Predicted hydrolase of the alpha/beta superfamily
                     [General function prediction only]; COG2819"
                     /db_xref="CDD:442067"
ORIGIN      
        1 mfnadyyylk mkthylslpy sgkkrrvrvl lpknyqqesa sypvvymhdg qnvfyskesf
       61 lgyswkvipt lkrnpdlakm ivvgidndsq traddynaws fenpsdpkar plgglgndfs
      121 dfimkvvkpf idqtyrtktd kkhtamigss fganitaymg ikyadqigrl gifslaqwia
      181 qepfdrylks qsldpeqkiy lqvgtkegdd tdrlflpgnm dqayidaslh yqalliaggi
      241 pvenidfniy vdeehnefyw akhlpdslrf lssgw
//
LOCUS       WP_284800515             441 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Curtobacterium citreum].
ACCESSION   WP_284800515
VERSION     WP_284800515.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..441
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45516
     Region          104..426
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 msptewllat plqapnklvp idtafvvlal vvllpavrrw rdraawrrva wragialaga
       61 glvlvacwft tsvvdlfgva lspvtqmwsa fagaalalav tgivhgggwr ralaivlvpa
      121 alvvpalgin vefakyptlg tvvqsdpypt yhagarptaq ptpggptata satpampasg
      181 qivsadipgt rsgfhprpav mylppaalvp dpqplpvvia fsgqpgapsd lftagqlatp
      241 ldeyarahgg rapivvsvdq lsspglntmc vdsrlgnvdt yvtrdvpawi lantpattdr
      301 kawgltgfsq gatctmqfls ghpgdfgaal avsselqpid qgprhsadqa fggsiarwqa
      361 aapialmrkn glgghsvwlv agsvdgefta narelgaaat aagarvsvss apgsghdwnt
      421 vqwafrtdvt pfcdalfaah s
//
LOCUS       WP_284800604             370 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium coyleae].
ACCESSION   WP_284800604
VERSION     WP_284800604.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..370
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=39308
     Region          139..368
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrykpgdlvl avavailaav ytasaftqpt haaswgqavl swgfvavcvv ltskpkfssv
       61 alialnvaws tmwlaapvnl gfspwvlavp vatfiagrft gkrfalvvla aacgwallsp
      121 fmwtwddnfv lfyrhgvdlg itlalhwgas vvgyllganv aaedevrrre ahakeqrlaa
      181 areeerraia rdihdllghs ltlikaqana glavgqerea lqqineaagq slseirllvr
      241 glresdhafs paagipdlps lvqryrdagl evsleapavd vspvtslaty rivaealana
      301 arhqvdptvt vrvapgetvv vevvstgqir pqpgtgvgle glreraasag gtlktwqsge
      361 tftvraelaa
//
LOCUS       WP_284800653             282 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Curtobacterium
            citreum].
ACCESSION   WP_284800653
VERSION     WP_284800653.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..282
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30600
     Region          37..263
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 maadaagrgp adgagdglea rptsatdvtt glptpgrrwr rgelntafri tasvvipvfr
       61 fsaryhwhgs krlpeggafv lapnhftnid plvvgtavwl srraprflak aslfkvpvfg
      121 klmsgmgqip versgrtrls dplgggrsvi eqggaiivyp egtltrdpdl wpmrgktgav
      181 rialendvpl ipmahwgtqg imarygkklk lfpptrvdvi vgdevdlsay rgrpidqqml
      241 leataivmqr itelleelrg etapatrwdp sannqketgk fe
//
LOCUS       WP_284800706             224 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium coyleae].
ACCESSION   WP_284800706
VERSION     WP_284800706.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..224
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24190
     Region          5..197
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 msrqrpaavf wdmdgtlidt eplwgqatye lgellgrplt pevrertigg sfpntlriva
       61 qwaghtltdg deqrykdwmf grmaellsag iecnpgilev lqslkedhmp mfvttnterv
      121 ladpcidaig rafftgtitg devihpkpap dmyleaarrv gaapqdclvv edsfsgmsaa
      181 aaagcavlgl adhvpagvyr fdphlfvgas addvyrwfaa acga
//
LOCUS       WP_284800741             187 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Curtobacterium citreum].
ACCESSION   WP_284800741
VERSION     WP_284800741.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..187
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19240
     Region          2..137
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mepiraqtie tllvsvnrli raaaqatgnp tsaavwrtlg iletdqplrl gelaalsrva
       61 qptmtrlvtg mladglvtrt vdpddsrgql iaitpaghdr lvtwratite tvgpvfadld
      121 ddewdvlhda aeviasrvav plavpppggp gagpsstals srasgaapss tspsptspss
      181 trseiha
//
LOCUS       WP_284800752             325 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Corynebacterium coyleae].
ACCESSION   WP_284800752
VERSION     WP_284800752.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..325
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34807
     Region          2..322
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(40..41,45,118,122,125,143,146..148,167..168,172,187,
                     213..214,235..239,260..263,310,312)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(130,228..229,242..247,255..262,265..266)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mkailvtkhg gpevleytei adpvpgegql lvdvdyagvn yidtyfrsgt yaseppyipg
       61 tegcgrvvdd plgeiapgtl vawhdapgsy aekvavdrnr lvavpegvqp evaasmllqg
      121 mtshylihgv rdtrpgdtmv itagaggvgl iltqmaaale ttvysivssd ekedlaykag
      181 atkvfrygdk gsalaeeike anggkgvnvv ydgvgrdtfq falevtgprg lvcsfgsasg
      241 dvepfkiqel nqhgalfltr pslkhyvatd eeflmraqav vraiedgtvr mrvhppyelk
      301 narkahedlq arkttgsvvl kierd
//
LOCUS       WP_284800799             208 aa            linear   BCT 25-DEC-2024
DEFINITION  HIT family protein [Curtobacterium citreum].
ACCESSION   WP_284800799
VERSION     WP_284800799.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..208
                     /product="HIT family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22490
     Region          69..195
                     /region_name="FHIT"
                     /note="FHIT (fragile histidine family): FHIT proteins,
                     related to the HIT family carry a motif HxHxH/Qxx (x, is a
                     hydrophobic amino acid), On the basis of sequence,
                     substrate specificity, structure, evolution and mechanism,
                     HIT proteins are classified into...; cd01275"
                     /db_xref="CDD:238606"
     Site            order(94,96..97,104,106,152,160,162,166,168)
                     /site_type="active"
                     /note="nucleotide binding site/active site [active]"
                     /db_xref="CDD:238606"
     Site            order(164,166,168..170)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238606"
     Site            166
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238606"
ORIGIN      
        1 mvaeqpggtp svpgtghvdg vvgpdplvir daatgaavpd afqrlwnphr mayidagreg
       61 kgrgheddcp fceaprksde dalivargeh ayvllnlfpy nnghllvcpy rhvplydeat
      121 pdetremael tqtamrvlra vshcdgfnig mnqgeiagag vaghlhqhvv prwasdsnff
      181 piiartksms qllgdtrrlv aegwptah
//
LOCUS       WP_284800811             476 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Curtobacterium citreum].
ACCESSION   WP_284800811
VERSION     WP_284800811.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..476
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=50785
     Region          21..456
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 msvpvtpfpt rdlppvaqqp rltvigtgyl gathavsmav lgyevlgvdv npakvdalva
       61 grvpfhepgl peklaealas grlrfsssmq eaaefgdvhf vcvgtpqqrg snaaeltyvd
      121 gafrelashi trralvvgks tvpvgtaarl aalvrevapa gadvevawnp eflregyavq
      181 dtlhpdrlvf gvespwaeaq lraafrpvld egtplvvadl ptselvkvaa nsflatkisf
      241 inamaeicea tgadvsllas alshdsrigg rflkpglgfg ggclpkdira fsaradelgv
      301 gqavrfldev dainlrrrqr tvdlvaelvd gdlagkkvaa lgaafkpnsd dirdapaldv
      361 armlrdagai vtvydpeama naarvrpelr yaqsltaavv dadvvvllte wqqfrdadpe
      421 dlgalvhtrr ivdgrhalda dryraagwey ralgrpvapr tveisvdeqd elqrsa
//
LOCUS       WP_284799647             381 aa            linear   BCT 25-DEC-2024
DEFINITION  inorganic phosphate transporter [Curtobacterium citreum].
ACCESSION   WP_284799647
VERSION     WP_284799647.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..381
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38634
     Region          17..332
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 mdvlvtvvlv ivvalvfdft ngfhdtanam atsvatgalk prtavlisav lnvvgaflst
       61 evaktvsqgi iregqdgiqi sptmifaglv gavlwnlatw yfglpsssth alfggligas
      121 ligaglhsvd watvvskvvl pallspviag aialvatyla ytltrnatth gaatgfrhgq
      181 tisaslvsla hgtndaqktm gvitltliaa nyqpsgtgpa lwvilacgla iglgtytggw
      241 rimrtvgkki sdvqspqgfa aetssaatil vsshlgfals tthvtsgsvi gsglgkklad
      301 vhwsvvgriv vawvitlpaa avvgalatlv aststiglvv vavlalvggl gffflarrkp
      361 itkdtvndeq ptepasasvs a
//
LOCUS       WP_284800887             213 aa            linear   BCT 25-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Aerococcus urinae].
ACCESSION   WP_284800887
VERSION     WP_284800887.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..213
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24732
     Region          21..178
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdayiknfvg kfsrqetltp rqhailqasi dlfadygysn tstkeiagra gvgeetlfkh
       61 fgskqnllfa cilpiiaems kekyaqefdl erikddkwif qdfvhhilan cfqedsdhyk
      121 vmkifaqeml yrenflkrla eliplhlkmg ffnileyfkd kgelnnwpna livrlmispi
      181 lsfqwvqfes gsqedfaqal syieafivrg lcc
//
LOCUS       WP_284800618             455 aa            linear   BCT 25-DEC-2024
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Curtobacterium citreum].
ACCESSION   WP_284800618
VERSION     WP_284800618.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..455
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=48231
     Region          1..430
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 mshdghgftt eqvhggfrld adhgarvpav hmtsgflfed fdqardrfag tddgytytrl
       61 gnptnadver riallergae ailvasgqaa atvaflgllq agdhvvsaqs iyegtrglll
      121 qnlgrlgiev dfvadardld ewaaavrpnt kaffaetipn pkndvldiag vaatahragv
      181 plvvdntlat pylvrpvehg advvvhsask flsghgsglg gvvvdagtfd wsaaperwth
      241 lttpeptlgn rsyvdvhgpr awvvyardvi asrigptpsp fnafllrqgi etlslrverh
      301 canalavatw ldqqpevtsv dhaglasspy hdlaqrylpr gagsvfaftl aggepaaraf
      361 idavelfsrm thlgdvrslv lhpattthag rtpaeraaqg iddglvrlsv giedvadllr
      421 dlergfaavr revgstagre argasatgra atqva
//
LOCUS       WP_284800888             479 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Curtobacterium citreum].
ACCESSION   WP_284800888
VERSION     WP_284800888.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..479
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50351
     Region          68..474
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mlslrariti gstaiaavvi lllvlvmrfq vvsvvasatr tlldadvdpy vatlevdsdp
       61 dlsapgnlql vavvapsgdi rlstmpesve ralgsltarp agaslvdvag seyrvviehp
      121 vnqagrwtvv aarnsqaeai vvddltttls ltglailiaf giaswvlatt alrpvnrmrr
      181 eaerlsvape raelpvgpaq delaslattl naflartrqa tererqmvsd ashelrtpla
      241 ilttqldlas ldaddatala ahidrakrsv arlsrlandl ltlsrieese rreqdggppp
      301 laawtdlgde vmaavdrvrl iastkdvtvd feleppstag gtdepryrld tggiaqlvtn
      361 tasnavaalp rgggvfvswr tegtegvlqv tddgpgvpes fipvafdrft rpdeartsrp
      421 dpdpatgavp mpggsglgla ivraiaerag gtaalrnvrs gglevtirip avhepasrg
//
LOCUS       WP_284800949             228 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            coyleae].
ACCESSION   WP_284800949
VERSION     WP_284800949.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..228
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24545
     Region          35..228
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 merryaprpa gelitavhrl sakqvevfqe vqshaegiqv aeigealgmh pntvrghlde
       61 llnagvisrr vatgsgrgrp shiytarvap tsrasgaivs lvevlasqls addtdaakal
      121 grewadrvne grdngademd lataerqiae llrelgfdpl qrpdattrkv relslnacpf
      181 vtennkrpap vicalhegfl dgtlggvkvq lrphdrpgec garltkra
//
LOCUS       WP_284800966             919 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Aerococcus urinae].
ACCESSION   WP_284800966
VERSION     WP_284800966.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 919)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 919)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..919
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..919
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=106510
     Region          <471..879
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mknkikinka takellkdid kltlndhnim nnselesllk ecskeynhlm qsklsdisfs
       61 elkqvdslnk qgniflfppl mlpgislaye tnrrkiahll fnfqtrlkve kehsdfiesl
      121 rknlefvinn drnsfalffm nkknrsqlke nkewilenye hiellksklk eaidkssdnk
      181 dyliiiqdnk aeidkvivnk ttylenrkdn llleieeylg qvqaainlid vqslegeiks
      241 qinqikekkg ltqalnqplr vlnifsdekl hlnrlkdrgi tnladlqtkl wdvrprsglt
      301 taacwkiete lnkyleyakk dyyprmdlqk ldldeitllk liyryihlae neeknldllk
      361 vtlkraqnnl diiwdrqlns yqmtqlevtk qeetvklyyl lfdcfnqlta ipkklwqvpk
      421 lsnseaindf esniakyyav idkvngggrk dtndlpslvv dkvnkfqldn rsfkgilrpy
      481 qefgvkyalt fkkvllgdem glgktiqala ianhlsqkgy khhvvlgpls ilmnwqreik
      541 kwttmesfvy rnanreeafe nwqdqggvll lnyeqathlv enqfsmlpsl vivdeahyik
      601 npwtkrskna yrlaqladyn lfmtgtplen rlkemkqlls vlqpdldyfk dndqgffndy
      661 ndnpqafrdg iatvylrrkr edvlrdlpei emvemwssfs eeeqdyynea vmrgisglqm
      721 mrraafsgrd rkhsekiana cdicqeamen gdkiiifsff klvlnklkdf lgdnvigmis
      781 gdvstaerqe lidqlensgk gsillaqida ggvglniqaa nivilcepqw kpsteqqaig
      841 rvyrmgqakn vivyrllted sidesmlell gektdlfndy andsvvsday drteadpine
      901 kelqtkvlei ererlkasv
//
LOCUS       WP_284800968             436 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Curtobacterium
            citreum].
ACCESSION   WP_284800968
VERSION     WP_284800968.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..436
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=45698
     Region          6..430
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mtqtpvrtst ratdtgpivl sglrrgwepl akqalvtalv agaaaasaal ptwllisnat
       61 smwagvglgv lllavtalmt rwtalariei ivpladfvav gllrfgtgds rsvflaivil
      121 pliwiaagpg rwrvlaplla tcvtlllpli lqpghglpvs eivrlvitlt vfgaaaavin
      181 elsrtslqql rrsqrsrrva eaevtqaalv qqslqpadgk glsptvrvag vcvpartvgg
      241 dfydwyptpd ggtalilgdv mgkgvgagmi aaavrtvirs nlgnpdpasa fqltsiglst
      301 gtttmtsaqf ttcfhgrvsa dgnlrwadag hgltllrhht ggseflrsqh lplgvgtewa
      361 sasiellpgd svisvsdgvl dlfggdlrsi dryqafiddr ndidhivtdi taladagdrl
      421 ddvtvlamtw gttrnd
//
LOCUS       WP_284800998             257 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA primase family protein, partial [Aerococcus urinae].
ACCESSION   WP_284800998
VERSION     WP_284800998.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13928233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..>257
                     /product="DNA primase family protein"
     Region          61..191
                     /region_name="D5_N"
                     /note="D5 N terminal like; smart00885"
                     /db_xref="CDD:197953"
     Region          136..>246
                     /region_name="primase_Cterm"
                     /note="phage/plasmid primase, P4 family, C-terminal
                     domain; TIGR01613"
                     /db_xref="CDD:273716"
ORIGIN      
        1 mtnefdevlr rarnltnppk ekaprtmeei rsaleaagak whaehqkenk sapflhegtg
       61 aelfmqhvhc iligndrdra mlayydpeqg lyissqnems glincleeyk ykhwievirq
      121 lrirvplkep fssrdlipvn ngiyslkehk llpfspkyai tskiatnynp latkpiingf
      181 dfdkwlkaia cgdeevvtll wqvinealnp nhtrnkigfl igngnsgkgt fqqllinlig
      241 kknvsalkpp dfgsqfg
//
LOCUS       WP_284801125             847 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Corynebacterium coyleae].
ACCESSION   WP_284801125
VERSION     WP_284801125.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 847)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 847)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 847)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 847)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 847)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 847)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..847
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88409
     Region          3..847
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mnkvslrnla ahklrlaltv lavvlgtsfl sgalmftnml sstfdsavdt vlddvdavvr
       61 pakgesaldk etvdgirang dvdrvnlmad epvvlatdde vavqtrlgss rlgvfyepqd
      121 tvgrtvevve ghapkeigda vinangaeey glhvgqeliv vdrdgrntvr itgliddplv
      181 qatslrlgvt eetyldyysy derfpaitvg akegvgaaev vdnlrsefpg lkieagekva
      241 qetteqirda lsfvtyflva fglvgllvgt fliantfsmi vaqrtkefal lralgasrgq
      301 itrsvaleaa lvgllgsvlg vvagaglvlv iragmntfgm plpqsgigls vdavvvplvv
      361 gtvvtvlsal aparkagkvr pveamrasea atpqplmwrt iagavlvvva vvaagyamaw
      421 ddgatrhrai lvgvaalsvi sglflagpal slpvvpplgr vigapfgevg rlastntrrn
      481 prrtattafa lmlgislvtm igmlgasmkq svddvaasev nadyvlmgpe mgsfpvpgdl
      541 pdrlaevdgv gniasytqap itvdgefghq fgpvgmtdvl rgdpsdlidl nvvdgdvslt
      601 gdsliapehi aqergwkvgd tvqvaapsap gktvdvtvag lftgsnvlqm fvvsdsaaak
      661 vssisntrll mvgvdsdgst dletlrarle devrgdivvq vrsaeemsge vtalidqmlf
      721 ilyallslav vvavlgivnt ltlsvierrq eigmlravgs qrrqirtmil lesvqmtvyg
      781 aalgvllglg lgwafltvle sqglttiavp tgliatvlaa svvvgllaav wpgqraaktp
      841 pldaiae
//
LOCUS       WP_284801144             284 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Curtobacterium
            citreum].
ACCESSION   WP_284801144
VERSION     WP_284801144.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14302731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..284
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31140
     Region          33..101
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          106..264
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mndpdenrlg rylaarralv tpeqvglpag pnrrvpglrr eevallagis adyylrlerg
       61 rdrnpsaqvl dslarvltld dverayladl tasrprtrsr pslvripprl rhllaavevp
      121 afiesrtldv laanslatal sprlaagqnr lrsllvdpee rafqqdwera vvemvaafrh
      181 algsdvddpr avelvgqlsl asarfrdlwa rqdvrplagt tvtvqhpelg slrlnrdklp
      241 vggvilvlyy adegsadaqk lrllaslart srtetgpqea sama
//
LOCUS       WP_284801176              80 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            coyleae].
ACCESSION   WP_284801176
VERSION     WP_284801176.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 80)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..80
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=9026
     Region          1..64
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mnrnpdqllk aeelgdylgl tkqqlalmrv ngtgprffra sanniryrwg dvtawieans
       61 hestdeytnq pgtyhrkata
//
LOCUS       WP_284801224             541 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Corynebacterium coyleae].
ACCESSION   WP_284801224
VERSION     WP_284801224.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..541
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57787
     Region          86..536
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 madksfdpea raayealraq lgddalegid iadlesgrdt dfghlemtdh gitlnladms
       61 aesgadaada dsdepapsla pegdhpdfdt vvakldaraa andpnpsldr iamlmdllgt
      121 pqqsfnvihv agtngktsta rmaesilral nrrtglftsp elervtecil idgeeisqtr
      181 fvdvwrdiep yvdmvdahfr ergeaemsrf ellvgiayaa fadapvdvai vevgmggtwd
      241 atnvveadvs vitpigidhq rflgetieei athkagiika rerdgygpae niaivaeqep
      301 eamhvilera vetgaavarq grdftiddss vavggqqlsl qglggvyddi flplsgahqa
      361 enasvalaav esffgvsreh pldmdsvrqg faevkvparv ervlgdpvvl idaahnphga
      421 atlaeamqrd fnyqsvigvv sifadkdara mlaalepvla dvvitqntdp ramdayelae
      481 iayevfgder vrvddnlpsa ielaielaee egpegvgvli tgsvatagqa rtylrssrgv
      541 q
//
LOCUS       WP_284801271              95 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase, partial [Aerococcus urinae].
ACCESSION   WP_284801271
VERSION     WP_284801271.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 95)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         <1..>95
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          <16..78
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 lveavakdap dktivatvag devqsckpdp epyltaakkl gidikkcivv edsnsglqag
       61 iasgakvvav kgvakiddye gityldslss ldlda
//
LOCUS       WP_284801316             307 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Curtobacterium
            citreum].
ACCESSION   WP_284801316
VERSION     WP_284801316.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..307
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30982
     Region          53..294
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mkrspcsggp gletlasspv dpastdvasg gwrafraqea amrlhnhtss paaplndrvv
       61 iitggskglg aaisarcaaa garvvlvgrd gqalrehaat lgqaaswiqa dlndpaapte
      121 vlaqtlerhg rvdglvnnag tahfapieri sasdidltms ldvrapllls gaaalvmreg
      181 gsivnvsstl savgspatal yaaakgalda atralaaelg prnirvngvr pgltrteate
      241 lahsdgvlfe tyratvplgr tgtgaevgda vvfllssaaa fitgqtlavd gghttsnlav
      301 rpsadrh
//
LOCUS       WP_284801343             280 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Curtobacterium citreum].
ACCESSION   WP_284801343
VERSION     WP_284801343.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 280)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..280
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30342
     Region          1..252
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 miglavifva vftlipilas lglsftswdv isspkwvgfd nytrlftdgp vlasfgvtva
       61 laiaivvlqi slglllavla nnrkrnatrv ffrtsfylpl lastaavsif mgyifdtkfg
      121 linyylneig lpgahwlndp fwakvtvvmv vvwqqvgftf vlfvaallav pvdvqeaaai
      181 dgagpwrtlf rikiplispt ilfatviami namqlfdqpf imtkggpgta tttatismyq
      241 agfqnlqfgf asaiailllv iigiitgiqf iaarklvfyq
//
LOCUS       WP_284801346             468 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Curtobacterium citreum].
ACCESSION   WP_284801346
VERSION     WP_284801346.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 468)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..468
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49562
     Region          46..460
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(164,166,318,321,351..353,394)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mangfstpid rrtlfkfgga glalagigsl aacsttgggg stsgtvkmly fgeqsaatal
       61 qkaiepkika ldkkaslqvt aingtdwndf lakvltqias gdvpdivsva tegqqllask
      121 nlltplddyv tknlsdlhky ftgahpalle stmyqghlyt lpdsfnagsm fystdlfdka
      181 glsrptskws mddfhssaes iakvgggtya fdwvvrlwgs wtsflyandg nlleegkysg
      241 gdwlwkskaf sdnpigvsgr kggwkwgdpt ansdaaveal qyvidlqksg aspspdvggg
      301 atlqglmasg rigmtigggf wagglhnagm kngsfdvvef ptwksnkslf gaggygifns
      361 sknkdlafev ikvmvqpesf dalwpgnvtt paqkslmtae rykttgpehw svfydqldns
      421 vpisappyyn alatalnqrt tqaissgnak kaldglqadi ekaasqas
//
LOCUS       WP_284801432             277 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Curtobacterium
            citreum].
ACCESSION   WP_284801432
VERSION     WP_284801432.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..277
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29179
     Region          5..264
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 miptvslqly tvnaalepdl dagvarlaai gfdtveafaf vdrapqlkqa fdahgisakt
       61 ghaflveesv plpdgsvmta pshmdtfaaa avlgieivid pfvgpdawtt regvervaar
      121 lnaaaeeaaa qgmrvgyhnh dhelrpridg kpalqvlael ldprvvleld lywasaagid
      181 vpafvaelgd rvvavhvkdg pmregistas vptdqtpagq gdvrlaeala aataleyavi
      241 efdgfdgeif dgvaqshrwl tdtlsaadtp skdevha
//
LOCUS       WP_284801448             697 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Curtobacterium citreum].
ACCESSION   WP_284801448
VERSION     WP_284801448.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 697)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 697)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..697
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=71227
     Region          24..>226
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mdpnhpapts gdpaaarpar wwhqtvpqrt tlaaivvlga vltswnlarg gdmsfyaaaa
       61 rsmseslpaf lsgsfdpgat vtldklagfa vpqaisihlf gmstaslalp qvvegavttl
      121 avavvalrwl garaglvaaa laastpifvs mfghpmedgl ltmslavalv wwqraaltrt
      181 wwplllaglf vgvgfqakml qawmvlpalv latviatagp garwrratgh vaallgaavv
      241 aslawsvvlg llptgdhpyf dgstddsvfa mvfgyngvdr flpglwpgav galgaavgha
      301 gthvadawrt atagrggggh sllqlfspry asqvgwswpa altgigtgaa rwwrrttgre
      361 arvpaatlva lvvwlvtava vlsvlrlpht ayvagigvql aalgalgwwg aaslvdatdr
      421 rlrlvpvgll vvqgawwawl arassepall gtvavgvtvv alvllvvrwr rsdptvastr
      481 grrtaagllv aavvlgpacf slqvldaard gsggdasvgv gqgafarggt perafalgrg
      541 gsggssaggr sagtaaftvs apdvvgghtr lpsdeaalva aaqragggqd gaplfltdsw
      601 riaadvigdt gdevltdggf sgrvpvftaa qvesivrsgr thllvvassa aatdpvrraa
      661 ddlgcrvvqh wgstfadaap grsfggrgts falercs
//
LOCUS       WP_284801461             294 aa            linear   BCT 25-DEC-2024
DEFINITION  inositol monophosphatase family protein [Curtobacterium citreum].
ACCESSION   WP_284801461
VERSION     WP_284801461.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..294
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=30583
     Region          40..285
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mteptptvpp raglprtdpp apavlrraae daaravapsl lgafrsdvvv htkrdahdvv
       61 tehdraaera ltgllttavp gstvlgeegt agpapdgarv rwivdpidgt anfarglayw
      121 cvsiaaevdg tvvagvvldp vadhefgadd tgafldgrpm rsvsapprda tvltsfpvqq
      181 dfellgetaa fgllrdltld frhhhstgsg alnlvhvaag wsdvtlgfat hpwdvaagal
      241 vleraggrfr gfrhgvptdr avdaedyvav gagdpherlv trvaalsatv trag
//
LOCUS       WP_284801522             723 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Curtobacterium citreum].
ACCESSION   WP_284801522
VERSION     WP_284801522.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 723)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 723)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 723)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..723
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..723
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73119
     Region          42..>273
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mttyptpvtd rpgharpgrt taardrrrpp lvrlfagere darwlrpafw allvltavvy
       61 cwdlsvsaya nsfyaaavqa gtksweafff gsldssnfit vdkppaslwv mvlsarlfgf
      121 sstslllpqa lmavasvalv wgtvrrtlar lgtttanvga llagfvvaat paaalmfrfd
      181 npdallvllm tagayctvra lprgswrwia lagvalgfaf ltkmlqgllv lpafglvylv
      241 aartswgkra vglgiaavsl vvsagwwvva valwpaesrp yiggstnntv ldlvfgyngl
      301 grifggsgng gggggmgggt agssfggstg ldrlfssemg leiswllpaa lvalvlglvv
      361 vgrrhladpa raglvlwggw llvtglvfsf msgtihpyyt valapaiagl vgtggallwh
      421 arervtgrlg laamvggtaf wswcllnedp twlpwlrwvv lfggllaaaa ivvgsvptlr
      481 rlvavgvlag tlfgltgtta yalvtttvah sgsipsvgpa gsssggfggg pggggmpggt
      541 agpggsaags etdgsdgtdg sqqgpggqpp tgsmptmpgg ttgegasgeg ttgegttgvd
      601 grtgggagve gattsaaltk llaatdttws aavngsqsaa qleldsdtav maiggwssdp
      661 tptlaefkal vaegkigyyi ssgsgrgmgg gsstasaiqe wvaanydstt vggstvydlt
      721 tak
//
LOCUS       WP_284801536             377 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Curtobacterium citreum].
ACCESSION   WP_284801536
VERSION     WP_284801536.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..377
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40154
     Region          137..373
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mtvvvwalva lvvlvvvggl lavravvgki vlpgrhrwtp vldadadsvq lpltsdtlrp
       61 geyglwhegd ghttvgpvle vdeaagtvrr avvrttgavs arirwsghvh pdpaamevdw
      121 sevsiptplg aapawvvrpa rpdddaaatw avhvhgirtt rvtalrtvpa aleagwtsiv
      181 psfrgdgeap wegrashlga rewvdveaal dhavangarr ivlvgwsmga tithelllrs
      241 ahrdlvtgvl lvapaldwea avrfqaartp vpgfvvsaal aamrtpllhr vvglrapvdv
      301 ralswlrvpp plpptllvhs dgdrtvpfav sqefaagepd rvtlvvsgsa ehawernlda
      361 awfdaqvagw iarlpar
//
LOCUS       WP_284801624             205 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium coyleae].
ACCESSION   WP_284801624
VERSION     WP_284801624.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13031065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..205
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22789
     Region          56..194
                     /region_name="SpoU-like"
                     /note="SAM-dependent rRNA or tRNA methylase related to
                     SpoU; cd18096"
                     /db_xref="CDD:349969"
     Site            order(129,131,151..154,157,171..172,174,180..181,183,186)
                     /site_type="other"
                     /note="putative SAM binding site [chemical binding]"
                     /db_xref="CDD:349969"
ORIGIN      
        1 megrhgvgpw egewpddpry dpeylehgdt rnvvdayryw sldavvtdld trrhpfhvai
       61 enfendmnig tvvrtanafl akevhivgrk rwnrrgamvt dryqhirhhe tvadliewan
      121 gegiavvaid ntpgcvplet aelprecvll fgqegpgvte aaqeaavmtc siaqfgstrs
      181 inagvaagia mhawirqhad lshaw
//
LOCUS       WP_284801697             487 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium coyleae].
ACCESSION   WP_284801697
VERSION     WP_284801697.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..487
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52844
     Region          225..462
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mlrvasgday etrlgaghsl rlklavlsgf ivaaavgltt mlgmwlstkt hegvldtelr
       61 sktlgmarql dgasedqirs eiaafrrsnp ltsiavsgad snlflgdpvs isgpylrtes
      121 gdavsvrsvn gkrvvvrqtp dgmvvaasrt edpygrisgs raaaalvvig vgslvawisg
      181 afisavgltp vrrlhceldn anessgprel pvegddefae vtssinalvr sleeskkrqa
      241 qlvadaghel ktpltsmrtn iellmmlhns grqdqisaed radlerdvla qmeemsilig
      301 dlvdlsrdes hetepedfrl devleealdr vrrrrpdvtf lfhadpwvir gdrfamgrap
      361 inlidnaakw speggavrvs lkaakrnavl ivddsgpgip peerekvfer fyrspesram
      421 pgsglglaiv kqvmdrhgat ivaeesddgg arfrvvfpgr ppedetaedl iaedenetrv
      481 ipkksys
//
LOCUS       WP_284801769             549 aa            linear   BCT 25-DEC-2024
DEFINITION  chitinase [Curtobacterium citreum].
ACCESSION   WP_284801769
VERSION     WP_284801769.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10158442
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..549
                     /product="chitinase"
                     /calculated_mol_wt=57869
     Region          43..352
                     /region_name="GH18_PF-ChiA-like"
                     /note="PF-ChiA is an uncharacterized chitinase found in
                     the hyperthermophilic archaeon Pyrococcus furiosus with a
                     glycosyl hydrolase family 18 (GH18) catalytic domain as
                     well as a cellulose-binding domain. Members of this domain
                     family are found not only in...; cd06543"
                     /db_xref="CDD:119360"
     Site            order(48,74,119,155,157,159,229..230,281,315)
                     /site_type="active"
                     /db_xref="CDD:119360"
     Region          387..422
                     /region_name="ChiC_BD"
                     /note="Chitin-binding domain of chitinase C; cd12215"
                     /db_xref="CDD:213178"
     Region          455..492
                     /region_name="ChiC_BD"
                     /note="Chitin-binding domain of chitinase C; cd12215"
                     /db_xref="CDD:213178"
ORIGIN      
        1 maarrlsplr vavavlavva vgaggyvgfd rwqsahaaes ekpwfaaytd vtvtptfafe
       61 dvksargrdv mlsfvvadhd aactptwgsa ytldgaadtl dldrriarle qqdgevgvsf
      121 gglandelat tctdpkdlva ayasvvqryd vstvdfdveg ddltnraage rraaavaelq
      181 karraaghpl avwltlpaap sglttdgtta vsqflaagvd lagvnamtmd fgegkgssqs
      241 mysasvqtlq evhrqlgvly dragtplgda tlwrkvgatp migqndvrde vfgladarkl
      301 nawardqglg rmsmwslnrd ttcgtnyvnl stvsnscsgv dqggqlfadv lgkgfggrit
      361 aaagdvttae psateqptdd pstspypvws adaaylegtk ivwhhnvyea kwwtsgdlpd
      421 dpvlsayetp wrlvgpvlpg erpvqpltlp vgtfpawsge avhdtgdrvl fhgvpyqakw
      481 wntgdspeas tsdpdgspwv rlkdveieri ladqragkpi pssaasgaps apasaaptgs
      541 ptaspsvgr
//
LOCUS       WP_284801823             411 aa            linear   BCT 25-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Curtobacterium citreum].
ACCESSION   WP_284801823
VERSION     WP_284801823.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..411
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44551
     Region          1..269
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mmisigmvga gqfapqfakl fkvhpdvdrv lvtdvvadra delvaaqhld gtladfdavl
       61 asdvdavaif tqrwthgplv vralragkhv ysavpmaite eeiaaiidav retgltymmg
      121 etshynpatv farqkvaega fgrvfyaegd yvhdmdlgfy aayqysggeq wkrtasyppm
      181 lypthsvggv lgaipghavs vscigvkddr ddgvfdkavs qfdndfsnas alfeldnggv
      241 vrinemrrvg ypshlresrf ryfgteasfe qlatvsvwqd keavhdvsdq idtrptmeld
      301 dprladvdpa lrdafvsgya pvhdtsrlpa eydgvptghe gshhflvddf vravvdgtlp
      361 pvnawvaary tlpgivahrs alqggvrlpv pdhgdapepa tstvssrias e
//
LOCUS       WP_284801843             378 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Corynebacterium coyleae].
ACCESSION   WP_284801843
VERSION     WP_284801843.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..378
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41145
     Region          1..375
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mnaplsgirv ldlsrvlagp fcsmiladlg aevikvespw gddsrqfgpf vdgtsayyrl
       61 fnrskmgitl dfkndddkev lrdlvrradv vvenfrpgvl eklglapkdl leinprlvvt
      121 sisgfgqtgs lakepaydlv aqamsglmsi tgwpnskptr vgislgdlip glyaaigtvs
      181 alyqressgt gqhldlamyd slisvmesvg mralyddtpp trigndhgls apfstyatkd
      241 gdvviaittn rlferlsnal gmpelatdhr faepvarsen rvalreliee alstktrset
      301 ialfeehgvp tarvydldea lrspfaqerg vvveetdgfr tlasplklag mekptpapel
      361 gqdneriqsw lsedprtt
//
LOCUS       WP_284802013             425 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF445 domain-containing protein [Corynebacterium coyleae].
ACCESSION   WP_284802013
VERSION     WP_284802013.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..425
                     /product="DUF445 domain-containing protein"
                     /calculated_mol_wt=46804
     Region          17..424
                     /region_name="YjiN"
                     /note="Uncharacterized membrane-anchored protein YjiN,
                     DUF445 family [Function unknown]; COG2733"
                     /db_xref="CDD:442039"
ORIGIN      
        1 mtdqlmpspt neaerrrvlr nhkiavtsll gvaaviflac swaqsrgvdg fwigffraga
       61 eagmvgglad wfavtalfkh pmgipiphta iipnkkdqva galsdfvsen flnartitqk
      121 vmdagiperv gtwmaqpana ervseevgtf vvrmvegidp keaerfidsq vidrfaepvw
      181 applgraleg liadgkvepv vddmvvwgrr kvhgmedtvv slidermprw apqfakdlvg
      241 qrvydelvsf madvdedpqh earralrrqi ndfaqdlqfd gemisrveal kgdimasnav
      301 rsasagmwaq lstalmeaas dpsstlrrki adasmewgtk lrddptvrad aearlekith
      361 yaaengaeqi vgiiaetier wdgeeaaeki elmvgrdlqf irlngtvvga laglviytvt
      421 qllff
//
LOCUS       WP_284801926             385 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Corynebacterium coyleae].
ACCESSION   WP_284801926
VERSION     WP_284801926.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..385
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40999
     Region          3..380
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 maetfdvvvv gagiigaata yycaeaglrv avvekhtaas qtsshcegnl lvsdkengpe
       61 lelakyslgl wrgelsqfae eiefepkggl vvatndqtme slqralaaqr eygidveels
      121 pqelrdkepf itddavgaaw ypqdsqlmpm atvncflana vrlgarmyeh npvqelitng
      181 ttvvgvrcpa gdfhaktvvn ctgpfaagvs eqwgamplpv eprrgyvlvt qradmtvnhk
      241 vysasyldnv vssdgglqts pvvestqagt iligssrerv gfsnevsqda lkgiaqnaia
      301 lfpglskvnv lrfyhgfrpy cadhvpiigp dtrldglwha tghegagigl sagtgklisq
      361 altggigstd vplddflpsr fetar
//
LOCUS       WP_284801972             272 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium coyleae].
ACCESSION   WP_284801972
VERSION     WP_284801972.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..272
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29618
     Region          4..225
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 msptrpvaaf fdldktiiat ssafafgkef rnngmitrqe awdlyltkaq ymlvghssek
       61 mdatrdslaq liegwsiedv qritqetmrt vvtpaiyaea reliddhraq ghdviiisas
      121 asilvepiar elgvdtvvat elaekdgklt geitrylkgg akaeavrqfv adhdydlers
      181 yaysdsatdi pmlelvgnpv avnpdrplrk halahdwqvr tfknpepliq mpnarevgig
      241 asviagvtal avagiliara vsgksgdkrr sa
//
LOCUS       WP_284802034             507 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA carboxylase subunit beta [Corynebacterium coyleae].
ACCESSION   WP_284802034
VERSION     WP_284802034.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..507
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52680
     Region          10..505
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mssskpdmtt tagriqdlrn rldeaqapvg qdaidavhea ggttarervl sllddgtfve
       61 tdalakhrve aykmdkskps tdgvitgygl idgrrvcvfs qdptifdgqv gevycekilk
      121 iydlatktgv pligiydstg prwkegivta hmqaqilraa trasglipqi avvagdvasl
      181 aattvpmadi tvmaegaslh vttadivskv sgaettsdel ggtavhaaet glaqlvaatd
      241 teavdlartv vsylplnnka asplgadnae apateadldt fmpdddnqpy dvtdilasvt
      301 dgdvlglsag fagsvvtgfa hvggravgvv atqpsvlagc ltrdaarkaa rfirtcdafn
      361 lpivqfvdsp gflpsveeer sgsaaaaaal ayafaeaqvg titvvtrkaf gpsyallgsk
      421 glgadlvfaw ptaqialada ttaaeaigtd eeqyaadnln pyvatergmv daviepsttr
      481 arvleglrll erkvtypaqk khgnipl
//
LOCUS       WP_284802021             394 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium coyleae].
ACCESSION   WP_284802021
VERSION     WP_284802021.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..394
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42762
     Region          <81..376
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mspvlafilg alvavpaahl grralrwyar nsaddhdedt gvstvsdmlh lvtqgsptgi
       61 vvvgrngkvq lsnarahdms lvhdgtvnpr vfdvaeqvmd daeqrvidme mpqrttgnri
      121 rnvravvapl tltdnssvii ygsdesenvr meharrdfva nvshelktpv ggmsllaeal
      181 lqdptdpemv eyfggklhke ahrmgemitd lialsklqga ealpdmapvr vddiideavi
      241 rnhvtaenrk ieinrgaptg lfvlgdksml tvavanlisn ainyspdgqp vsitqktvrd
      301 kavlirvtdr gigiapedqk rvferfyrvd karsrstggt glglaivkhv vanhggnitv
      361 wsrpgtgstf tielpifdpe svhasagrke leqq
//
LOCUS       WP_284802142             258 aa            linear   BCT 25-DEC-2024
DEFINITION  spermidine synthase [Corynebacterium coyleae].
ACCESSION   WP_284802142
VERSION     WP_284802142.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..258
                     /product="spermidine synthase"
                     /EC_number="2.5.1.16"
                     /GO_function="GO:0004766 - spermidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27417
     Region          35..230
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mnsprrkpra pkrritgtyp iasghaaiia dperdggytl evnnvpssyv vpgapevley
       61 dymrwiagfi qgfvedrpla pfaavhlgaa gcalpsyvqh rwpssnvave ldgqlarlvr
      121 dafdppvaik vaearaftha llegsvdviv rdvfagpdtp rplttvefyr avhralcpgg
      181 lfvanigdaa glartraela glsevfrhtm vvasapvlag gaygnvvvaa sdqplrccad
      241 vpsklgqlli ddtpphhd
//
LOCUS       WP_284802152             506 aa            linear   BCT 25-DEC-2024
DEFINITION  HNH endonuclease signature motif containing protein
            [Corynebacterium coyleae].
ACCESSION   WP_284802152
VERSION     WP_284802152.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..506
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55972
     Region          <178..376
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          369..421
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(394,396..398,400,411..412,416..417,420)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 mtseitqcvn disaalrtls tlfddpstlv fddirrdmer leeqfkkkat idaafafiae
       61 rddagrivga nypnaylqqy ldlskgeayn rlergrllfg pppepaappv eedqdddlfg
      121 aadedrqeqq eqqdrqkqqq ddarknssqv saekqdiirr eldkllkaaa gertriyada
      181 maeallrspe dlrqfvrrav aeanrkhaph snpnagyenr glsfgrrkad gtvdilinat
      241 agaaalikah adkglapnsn lpadqhnevd srtpqqrrfd qffaifqqye qdcqkkngga
      301 asvvismtld dladgdasml ydtntgievd cfdlirlgmd gttdfllqvd gvtsvplwmg
      361 rttrlasveq riamfaiqgv cswlgcttpm teceahhila wikggntdie nltglcrehh
      421 rcnndnrdgs lnkgymdydp qtgkagyrkh pfdplkynqs vpakhsavsr iyaakgrcdc
      481 artgtldpaf yppgpppgsp pmpkga
//
LOCUS       WP_284802157             328 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Curtobacterium citreum].
ACCESSION   WP_284802157
VERSION     WP_284802157.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 328)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..328
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35716
     Region          1..291
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtqvrphgkt plykrerplw mllpggvlml vvivvpllvg vyiamldldq ytlrewfsap
       61 fvglanfvea ftdspllhsv wisvslsvlv taitvpigva aavstqnrfp grglvrsiyl
      121 ipyvlpafvv gtffrtmlqp qgvvntvlgt dvlwlngsas ywalagvmiw tswpfvylls
      181 laglqavdne vheaaaldgv twwaklryiv fpylrgplsl aviisilhni nnftlpfvlf
      241 giplpssvev mpvltyiasf qsfrfglsaa maicslviva iplfvylrav kldtgddagp
      301 srkqrrsdrl tlaaatpaaa adldgara
//
LOCUS       WP_284802164             442 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium coyleae].
ACCESSION   WP_284802164
VERSION     WP_284802164.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..442
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=47918
     Region          1..440
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrltvigtgy lgathaacma elghevlgvd vdehkiealk nstvpfyepg lpevlernid
       61 agrlsfttny deaanfanvh figvgtpqqr gsyaadtrfv eaviddlvpk lhghhvilgk
      121 stvpvgtaaa lqeraddltr ragrgatvei awnpeflreg yavkdtiepd rivlghrsen
      181 shaeeiarev yatplangtp fivtdlqtae lvkvsanafl atkisfinav sevceivgad
      241 vtqladaigy ddrigrkflg aglgfgggcl pkdirafmar agevgadqal tflrevdain
      301 mrrrqrvvdm areelgslig rnitvlgaaf kpnsddvrds palavagqls laganvtvfd
      361 pqamdnarkv fptldyadtl eealrdaelt ilatewgqfr emdpewvagv vekqllidar
      421 nvldvqqwrn agwemralgr tl
//
LOCUS       WP_284802280              62 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            coyleae].
ACCESSION   WP_284802280
VERSION     WP_284802280.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 62)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 62)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 62)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..62
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..62
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=6370
     Region          6..>44
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mypatvsipe aasllgisrs saynavqngt fpskviking ryvvptkpll dvvglnelpa
       61 ta
//
LOCUS       WP_284802444             302 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Curtobacterium citreum].
ACCESSION   WP_284802444
VERSION     WP_284802444.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..302
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33512
     Region          16..244
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 msqgtvrrha apyrgrpria vvvltqgtrp adlrrgidsv laqrdvdldv vcvgngwept
       61 dlpegvhala lpenlgipag rnagaevvdg dhvfflddda wvpsdtflrd avemldrdps
      121 lglvqprvvd ptgaanprrw vprirkgdaa dsspvfsvwe gavvlpmdvy ravggwgaey
      181 fyahegiela wrvwdagrra wyagdlvanh paidparhte yyrlnarnrv wlarrnlpap
      241 lrplyvgswa aiqvarwwrh parlrtwfag aregwtsdcg ptrtmgwltv armtlagrpp
      301 vv
//
LOCUS       WP_284802517             443 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase 5 family protein [Curtobacterium citreum].
ACCESSION   WP_284802517
VERSION     WP_284802517.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Sharma,K., Dhillon,A. and Goyal,A.
  TITLE     Insights into Structure and Reaction Mechanism of &#946;-Mannanases
  JOURNAL   Curr Protein Pept Sci 19 (1), 34-47 (2018)
   PUBMED   27739373
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Ketudat Cairns,J.R. and Esen,A.
  TITLE     beta-Glucosidases
  JOURNAL   Cell Mol Life Sci 67 (20), 3389-3405 (2010)
   PUBMED   20490603
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467628
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..443
                     /product="glycoside hydrolase 5 family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47135
     Region          1..344
                     /region_name="COG3934"
                     /note="Endo-1,4-beta-mannosidase [Carbohydrate transport
                     and metabolism]"
                     /db_xref="CDD:443135"
ORIGIN      
        1 mrfgvnhtps vgwfhswldf spsdtardle qiaslgadhv rifplwpvvq pnrtmirqra
       61 lddvatvvdi agsfgldvnv dalqghlssf dfvpawldtw hrrnlftdpd vvastaayve
      121 alartvadrp nllgitigne vnqfahaphp apfgvtaeqg hawaatmvaa arrglgtdge
      181 tglearrgsa plvtvaqyda awyddaqpfg pqhaadhgda tvthswvfng vaqlhgalgp
      241 gsvrhgeyll qlaaawnrdp hrpnwlqevg aptnvvptad aasfteqtir hvlgaqdvlg
      301 vtwwcshdva rsladfpele ydlglftndg rrkpageafa alarsatasp aappatgivl
      361 ddvgpdgtpr pgvradcapg grfaagwlal aeaapdgrgp qvllrsrlhd dvlraargit
      421 tiehvpdgld rtvlavahpa tga
//
LOCUS       WP_284802555             336 aa            linear   BCT 25-DEC-2024
DEFINITION  1-phosphofructokinase family hexose kinase [Curtobacterium
            citreum].
ACCESSION   WP_284802555
VERSION     WP_284802555.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..336
                     /product="1-phosphofructokinase family hexose kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008443 - phosphofructokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33507
     Region          9..292
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 mngtpstriv tvtpnpsldr tielagelqr gavqravhtt aepggkgvnv srvvvasggd
       61 tlavlpgdel dpvllglatr giptvalpig aplrsnvtvt eptgtttkln epgpslagrl
      121 ddlaalvada agptatgpaa rwvvfagslp pglpddalav lvravrerhg dtvriavdss
      181 glpftallqs geridlvkpn aeelaevvgg dpdayeqdpd aaavaaqrlr dkhvdavllt
      241 lgsagavlvs degafaaaap rivarstvga gdsslagyll aevagatpae rlaqavatga
      301 aaaalpgsdv paldhtdpgs vtvrtlhpar vpapia
//
LOCUS       WP_284802562             379 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Curtobacterium citreum].
ACCESSION   WP_284802562
VERSION     WP_284802562.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 379)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 379)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..379
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=39794
     Region          112..375
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mtrvwsigar talafaaaam altvaalvfv nlasqwsigg qvqldadats tpwpsaprps
       61 iqpdpdstpd agssvsivsv vaqqqwqwsa vavvgvgvla gavgsvvsrr mlrpvdrmra
      121 tadrisastl herialggpd delrrlsrti drlldrlets fegqrrfvaq aahelrtpla
      181 vqraalqigl pddagprnva aaraelleqn rrtehlvesl lvlaeadrgl dgvealdlaa
      241 llddvatqlg atadtagial rptvdavsvg tvvgeptlvr qlllnlvdna veynvpggtv
      301 wvrltadgiv ventgapvdp etvtgllepf rrggeqgsrr hsglglsiva avvhahgwtl
      361 dvaaregggl rvrirvssv
//
LOCUS       WP_284802570             340 aa            linear   BCT 25-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Curtobacterium citreum].
ACCESSION   WP_284802570
VERSION     WP_284802570.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..340
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35948
     Region          1..327
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mgavrtavig lgmmgrhhtr vlrslpgvel vavadalgdr hgvadgapvm psasdvlrlg
       61 idaavvavpt saheavalel aeagvhclve kpvasdvaga trmvsrfdea glvgavghie
      121 rynsalqelr rrldagelge vyqvvtrrqg pfpariadvg vvkdlathdi dltswllgsp
      181 fvrlfaqaah ksgrehedlv afsgtladgt vtnhlvnwls pfkervtivt geggsfvadt
      241 ltgdlwfhen gtvatewdav safrgvsegp vtrfafakre plvaeheafr davlgdrsri
      301 vplcdglqtl rvaeaaiesa rtlsivhpla psehpegtpa
//
LOCUS       WP_284802584             424 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Curtobacterium citreum].
ACCESSION   WP_284802584
VERSION     WP_284802584.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..424
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=44306
     Region          171..404
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mavvgdtttl rkdprpvlgi pthlaprvna wstvrafhaa avgsvvaaav vlllyrladp
       61 dvrivgavla lvpmalmigv hvqfgtwrsa vafllvggvs awwfalvvqr evpagwvtsy
      121 llslviiplv lvggagavag rvvlwsvggf lvgrlatsia vaqvdgpprp lllawvtlgf
      181 vvalvlftsr ntarservqp ellrsareeh vsayragvea eaaailhdtv lnhlgaiala
      241 pdgpmdpqla rtvesdvaml tgkewlapsg stadrpsava vdafeamvde hraeglqvdv
      301 tgdtavlgal dhtastalfr avgqclanvr khagtdraev svfddgasct vmvvddgrgf
      361 deqetspdrm glrgsvreri arvggdvqvw sspgsgtsvm mtvphaatav pvaatlddew
      421 gtgr
//
LOCUS       WP_284802649             301 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Curtobacterium citreum].
ACCESSION   WP_284802649
VERSION     WP_284802649.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..301
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30111
     Region          4..284
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(31,235,238)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(175,206,233,236..237,240)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mssvivigea lvdvvdrpeg rsehpggspm nvavglarlg rparlvcalg dddrgaavra
       61 hveasgvrvd atavprtsta vatiaadgga syefdldwri dpvdvpegtp lvhvgsigav
      121 lqpgaatvld avrarpagtl lsldpnvrps itpdrdavla tlepllaead vvkcsdedaa
      181 wlwpdrdvda vldgllaaga tlaavtlggs gcaiasrgar rriaapavtv adtigagdsf
      241 magllaavla tgtaptalde ddlgrlagla lacaavtvsr pgadppttee lpadvradat
      301 p
//
LOCUS       WP_284802651             186 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Curtobacterium citreum].
ACCESSION   WP_284802651
VERSION     WP_284802651.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..186
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20151
     Region          31..169
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mtapsvallp vdladpigrs wlvaflttnr fpfhvtpdpt rngvkrriad gdfsgpahal
       61 frveadgaav gmitlddldd gaplidvrla erargqglgv pvvrvlagtv fagypdvdrl
      121 eaqtrddnva mrkvlvrcgw vqeaqyrraw pveggaprds vaygllredh rsgrvtpfyg
      181 rfdage
//
LOCUS       WP_284802667            1219 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Curtobacterium citreum].
ACCESSION   WP_284802667
VERSION     WP_284802667.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 1219)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 1219)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165397
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1219
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..1219
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=124805
     Region          227..716
                     /region_name="Peptidases_S8_subtilisin_Vpr-like"
                     /note="Peptidase S8 family domain in Vpr-like proteins;
                     cd07474"
                     /db_xref="CDD:173800"
     Site            order(236,313,399..401,431,657)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:173800"
     Site            order(236,313,657)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173800"
     Region          <460..>596
                     /region_name="myxo_dep_M36"
                     /note="myxosortase-dependent M36 family metallopeptidase;
                     NF038112"
                     /db_xref="CDD:468355"
ORIGIN      
        1 mtratpnrat pdqtdpttpt rhrrltrvlt agvaavaltc gglavggaan aapsglssad
       61 lklaqplrda kpsktiaafv rttgegalav dakakggdlt ksktqstqak qrvqaiastv
      121 davsaavkqs dakatelyst eytvpgvavv advdalrsia ersdvesiip ltpkkivdpa
      181 pgdasqapsg vdpdlvkpga dgvspknaas dvytraldaw qqtgktgkgv niavldtgld
      241 ytqadfggpg ttaayqtala stnapdpswy dgskylggyd fagptynadt ssaaydptpk
      301 pdanpidgkg gdhgthvagt aagfgltadk ktfrgdyskl tnqtvqdmwv gpgtapqagl
      361 yalkvfgddg gstdltgaal dwvgkalteg kdinvlnlsl gsdygapddp dnakidalta
      421 rgvlpviasg naddftdigg spgnaegalt vaasatgqsl fdgvqatapa dvantyraqy
      481 sqnyqgtlpv egdvvvpstn idgcqafsad eaakvkgkvv wlkwtdgale cgsgvrfnnv
      541 qaaggvgvll agtvtsfesg iagnatipga eltsdsvasl qaaaqagtlh vrfaqelkgf
      601 qlatdqanvn tlapftsrgv hgsfddivkp dvagpgvnvi saangtgdgr msmsgtsmat
      661 phvagivalt fqshpswtap qvkaavmnta thdvrqgdrt atllrqgtgr vdalqavtag
      721 ttvrsiendq lvtasygvve vsgattesrt lqientdgrp htydvayqpq vdqpgvaftl
      781 stkrvtapah gtatvkltft iadptrlrrv idptqesvqs gyqrefvaaa sgvvaftptd
      841 kslnplrlga yvapkpvsav hgkdiafsga qttadlaltg ravdqgdavt gyhsvvapfv
      901 lggtdpqesf pagsakqslq aadirsygan ydkasdtlaf gvqtagadan pgavtnvevm
      961 idtnrdgkpd ylvydaksat vdatfattvd latgktvdsq plnggtagqd vntfdsavkv
     1021 ltvsastiga tgpfdysvlt esayapalat sgsyvvdetd satydpskpa ltfaqgtttg
     1081 vlfadqgslq vtrpadvtna rilllhlgna vgdqadtlaa aqtaptlalr kgsavtisgd
     1141 pkvgktlraq hgswdgkkvt ysyqwlrdgv avkgatgery slgttdqghr fqvqvtakak
     1201 gyqdgsatsk stakvaprr
//
LOCUS       WP_284802675             295 aa            linear   BCT 25-DEC-2024
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Curtobacterium
            citreum].
ACCESSION   WP_284802675
VERSION     WP_284802675.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..295
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=31718
     Region          122..223
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mtptepvrrr rprwpipssl llgllplvaf aavsawrsrp sddyatlgqt vdsvvhalvl
       61 pesiavlvlc vyvtalgwwp gaavdhdrtp lrwtsvtivl iavvcaarlp lvdwsalpvr
      121 yfvlltlgvl fvgvfeellt rgvllvglrr rlpefgvwia scvlfgllhl lnilagaavg
      181 atllqvgfaa sfgstlylar rltgnlllpv llhafwdfgs iavsatvdtt dlgrllpvgi
      241 vglvsfgvla lglvagglva wrddrprrlr rrwrdvppag vdagrgaepr lpsav
//
LOCUS       WP_284802682             154 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Curtobacterium citreum].
ACCESSION   WP_284802682
VERSION     WP_284802682.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..154
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16301
     Region          1..140
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtehavqgid evlaasrgll gvvarslapa ledvtvpqfr livlvvslgp trsgdladrl
       61 avgpstltrn vdrlvaggwv errpgadnrr evriaatdrg ralvdevter rrreleaiva
      121 gmpeqdrava vagmaafrra mgepapeevs afgg
//
LOCUS       WP_284802698             917 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Curtobacterium citreum].
ACCESSION   WP_284802698
VERSION     WP_284802698.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 917)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 917)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 917)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 917)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..917
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..917
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=100300
     Region          10..>664
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mtlereelrd dwtvaiagdq vpsgapadlv gralpatvpg qvhtdlereg viadptfdrn
       61 edatawvgra dwayrrpvdv dprgfervdl vcdgldtvae laldgvvlgt trnmhrryrf
      121 dlndvpgpag qrelellfes pyreagrvaa ragampgpyd epfpyvrkqa snfgwdwglt
      181 avtsgpwrpi aierwstarl aevqplvdve agegvldahi rversgmndl dqdgedddlv
      241 lvvtvagptv dggttrqrsr aqltpkddet vvtvrvpdal rwwprgygaq prydvtvelq
      301 tvdgevldrr taktgfrsar idttddavgk pfdvvvngav vdvrgvnwip ddvivsrvdr
      361 arvldrlrva adlgvnlvrv wgggvyesde fydvcdelgl lvwqdfafac aaypeiepir
      421 sevvaeardn varlsghpsl vlwngnneni wlhevdgwge vlgdrgwgld yyldllptiv
      481 davdpsrfyt vaspwsgses lfandvdhet hhswdvwnrl sdehyrdsvp rfvsefgwqa
      541 ppawrtlrda vtdeplrvda pgvvhhqkad dgmvklargi aprfgsvdps efdrwhyltq
      601 lqqaraiatg vehwrthwpr ntgvvlwqln dlwpvsswsa vdsagrlkpl ahelrrlydd
      661 vlltirpvtr asgpagaaaa dgsgtvdgsg pddgsapada slpaaddqpg gtahdvpsas
      721 aggtaelvtl sdtlslgvsp gafgqspvev avrsaragrd svvrvrrvtv agtilaevtl
      781 pvrlseagva vvalpesvgv lddptrelvv admdwrravw taapdkdvrw eparyrttvt
      841 paadgdghdl vveadslvrd llvqpdrlap tgtvdrgfmt llpgervdfr lrgltdadvr
      901 rlgepfvlst lddhlgh
//
LOCUS       WP_284802543             365 aa            linear   BCT 25-DEC-2024
DEFINITION  N-acetyl-gamma-glutamyl-phosphate reductase [Curtobacterium
            citreum].
ACCESSION   WP_284802543
VERSION     WP_284802543.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Cherney,L.T., Cherney,M.M., Garen,C.R., Niu,C., Moradian,F. and
            James,M.N.
  TITLE     Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase
            from Mycobacterium tuberculosis in complex with NADP(+)
  JOURNAL   J Mol Biol 367 (5), 1357-1369 (2007)
   PUBMED   17316682
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414156
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..365
                     /product="N-acetyl-gamma-glutamyl-phosphate reductase"
                     /EC_number="1.2.1.38"
                     /GO_function="GO:0003942 -
                     N-acetyl-gamma-glutamyl-phosphate reductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016620 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, NAD or NADP as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37422
     Region          3..365
                     /region_name="ArgC"
                     /note="N-acetyl-gamma-glutamylphosphate reductase [Amino
                     acid transport and metabolism]; COG0002"
                     /db_xref="CDD:439773"
ORIGIN      
        1 msvsvavaga sgyaggellr vlaahpefdv rtvtaysnag qpliatqphl rslahltlve
       61 ttaehlrghd vvflalphgq sgeitaelde dtlvvdcgad hrltdpaawd afyggdyhga
      121 wtyglpellh aaptpgsaee wrdvddiagt grqrtelaat kriavpgcnv tavtlgiqpg
      181 iqaglvesdd ivavlsvgps gagkklatty laseimgsas ayavggthrh ipeiqqnlva
      241 agagdvtisf tpvlvpmsrg ilatttarla pgvsardvrl aweqayadep fvhllpqgef
      301 prtadtvgan tclvglavde aagrvvavsa ldnlakgtag aavqsanial gfpetlglnv
      361 dgvap
//
LOCUS       WP_284802999             482 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Curtobacterium citreum].
ACCESSION   WP_284802999
VERSION     WP_284802999.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..482
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50360
     Region          128..471
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtlrrrlvls ivalvvavsa vigagsilal asiqrsaidq qlqyatsraq rsveqqgggs
       61 pgidigrpsg qaagtltvyf lngdvavgtv ldndgavdri gtdvvrplgg vtvdglphtv
      121 dlggdlgryr vtavslgtav lvvglpmapv yesvwkllgv vlvvtvvall vasfvaavvv
      181 rrslrplerv aetasavarm plersdaldg vrvpdtdprt evgrvgtafn rmlghignam
      241 qarerseqkv rqfvadashe lrtplasvrg yaeltrrmgg dlppdvvyam grieseslrm
      301 tsmvedllll arldegrevq faevdltglv fdavndahaa spaheiavev pdepvvvpgd
      361 aarlhqvivn lvtnarthtp dgtritvgls paaggvdltv rddgqgidpe flpklferfa
      421 radssrsrsa gstglglaiv davvqahggt vsvasvpgdt vftvhlpstr pvapadvvva
      481 ta
//
LOCUS       WP_284803001             314 aa            linear   BCT 25-DEC-2024
DEFINITION  TolB family protein [Curtobacterium citreum].
ACCESSION   WP_284803001
VERSION     WP_284803001.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..314
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=33500
     Region          <18..>249
                     /region_name="COG4946"
                     /note="Uncharacterized N-terminal domain of tricorn
                     protease, contains WD40 repeats [Function unknown]"
                     /db_xref="CDD:443973"
     Region          164..311
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 mtdttrgrql lpgqtsrvhv ydlatrtsrp vfasravlve apnvldertl vlngdgdlwl
       61 lrlpepgsdv vldesalvrv pmpgvteinn dhvldpsgts vvvsardgel yrvplpdggs
      121 aerltdtaav lpvvrkyylh giapdgsvla aivgertadg vwttdvalvd pasgattflt
      181 rdehpddgca itpdgrtvlf nterftpgta qlaalrldgg dpvrltader vdwfphlspd
      241 gqhllylsyg pgvqghpadh pvelrllpga lvrgarmavv petlvaldgg qgtvnvppws
      301 pdstwfaycd ypva
//
LOCUS       WP_284803004             383 aa            linear   BCT 25-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Curtobacterium citreum].
ACCESSION   WP_284803004
VERSION     WP_284803004.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..383
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39729
     Region          32..363
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtdttttaae stdsarrtgp vgvgvigagv isdqylsnlt afpdlqvrfi adidepraaa
       61 qaekwgvpgs gsvaelladd dveivvnlti paahvevalq alaagkhvwg ekpyaldres
      121 aaqlrdaaaa agrtvsvapd tflgaglqta lrtiregrig tplngltlfq spgpeswhps
      181 peflfaygag plfdigpyyi ttlvqafgpv arvtatasks ratrtigsgp kagtdfpvev
      241 ptnhsaliqf edggsaqsvf sfesdrgrtg fveiagetgt vvfpdpnnfd gdtelyahga
      301 dgpetipavg stysrgtgvv dlarslrage gnripgalaf hvldvmvsia eaaergetvl
      361 vestvepspt lpegwdpaeq tls
//
LOCUS       WP_284803011             373 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Curtobacterium citreum].
ACCESSION   WP_284803011
VERSION     WP_284803011.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 373)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..373
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=36899
     Region          25..369
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 msaaaprnaa aprsaaaprs aaapvrrgvr vgpvglawrp rvlgytvaal alavvlvvlg
       61 vavgstwiap gtvvralvga edgpdgfivt tlrlprvltg alvglvlgva galtqtvtrn
      121 plgtpdiigv tsgasvgava aivlgggsys vssvvtsggi pvaatigalv aaaavcgfgw
      181 rggvqsyrlv lvgigvsatl damtsyllvr akitvataas qwlvgslsst swssvwpllv
      241 vaavavplal atsaalgigq lgdevatgvg lgvqrhrllv ialavvltaa avaaagpvgf
      301 vafvvpqval rlagtnrppl llagalgavl vlgadllars afpwqvpvgi vttvvgapyl
      361 iwllvrhrke msr
//
LOCUS       WP_284803047             324 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Curtobacterium citreum].
ACCESSION   WP_284803047
VERSION     WP_284803047.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..324
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32447
     Region          68..324
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mssssepvvv pprpaatrag revtgrrrgv gkrflvvgdv ldgvlvqtsa eavgthdpaa
       61 viqhrslgaa gntatwlgwl gaevdlvtrv gvddvlrher sladagvrah vrydaraatg
      121 aivsvrdgrg rtamtdpaas gdldaadvpg dlvaradivh ltgaamlggg gaeriaglva
      181 ragsagarvs ldpsaeavvr svgpeaflaa ldgvdvlfpd eaeacaltga ataaeavrrl
      241 tavvplvvvt tgsdgallgr pgrspqrvpa tpatvvdtlg agdafaagfl rawatdpvrv
      301 gaaaregtrv asralgfvgg rppv
//
LOCUS       WP_284803076             373 aa            linear   BCT 25-DEC-2024
DEFINITION  lactonase family protein [Curtobacterium citreum].
ACCESSION   WP_284803076
VERSION     WP_284803076.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..373
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=37488
     Region          17..367
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 msesgalddl avlddlhvlv gsytatgggs atgisivhgt tahtaavmdd psflaadgdr
       61 vyavsetadg svsafryadg alehrwdata ggdapchvrv dpsgalvvtn yvsgtvtaig
      121 laaaeahasa vfdgssvapg saephglgdr vvvpdsaivt gvlpdvegpv edrqegphah
      181 qsigtpdgtv lvadlggdal hefrvtdepa idlvrvhhlg pgvgprhmvw lgddlivage
      241 ldgrvyrlrr ddsgslvpig saatfegpvg esllshievd dagrvlvavr grdlivvldt
      301 dgdglavvgs assggvwprh faqvpgfllv anqmsdavav lpvgedgvpg gpvaqiavgs
      361 pacvlpiaps aqg
//
LOCUS       WP_284803257             446 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Curtobacterium citreum].
ACCESSION   WP_284803257
VERSION     WP_284803257.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..446
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46263
     Region          111..>335
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mtpsrtspia ssvltlrpal pradeptwag aawvgavdrp talaattval agadgfrrar
       61 llvrdgleia gsvdvsvtpd gdldpaelgr alralpatsl padtgaalvg rvsvvigtrd
      121 rpedlrtclr svlastwpdl evvvadsapt tsatrdvvas iadprvtyvl earpgvarar
      181 naglavatge vvaftdddvv vdpdwvtava gafardadva cvtglvpsae lrtptqrwfd
      241 ervtwarntr rrvfraaepp vdlplfpfsv gafgtganvs lrhsaavalg gfddalgvgt
      301 ptkggedldv fvrvlssgaa lavepsavvw hrhrsepaal raqavgygtg lgawvtklvl
      361 hprtalavvr ravpalrrlg slgqddggrs agapgavgad apgtarsgaw vadeelraat
      421 vglrrielta alggpwrylv srrarr
//
LOCUS       WP_284803259             385 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Curtobacterium citreum].
ACCESSION   WP_284803259
VERSION     WP_284803259.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..385
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40138
     Region          <18..59
                     /region_name="PHA03231"
                     /note="glycoprotein BALF4; Provisional"
                     /db_xref="CDD:223014"
     Region          144..385
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mdfiaqerdr llrsttrvvg vtcalvsvvg ivssasvpim pllgalacia vliaaflafg
       61 angspwwsal asvsglgala llllgttpdq rpvvaaavvp laagslsapl maqrgsrlgl
      121 altissgaaa lvavvwasgs vlsaaavgta lgwiliavit vwiarsiprv arriqsigta
      181 hraerqaset eaqrrqgarl lhdtvlatlt llahsgrgvs eqamreqaae darllrhlrl
      241 gatpqpqqsg dysltrqees plgqtlesvk qrfgrmglev swhgtgqvll pshvldafll
      301 algeclenvr rhagvgeahv tivhdqetvr amvtdsgvgf dldavgaerl gfkesvvnrl
      361 revggdaklf sapgsgttvv leapr
//
LOCUS       WP_284803269             422 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Curtobacterium citreum].
ACCESSION   WP_284803269
VERSION     WP_284803269.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium citreum
  ORGANISM  Curtobacterium citreum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Curtobacterium citreum"
                     /db_xref="taxon:2036"
     Protein         1..422
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=44258
     Region          47..332
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mgatagtlvr qaiaqrdlvv dlvrtacvvl vvvvhitmvg vavgpdgiav tsplqeapwy
       61 vaatwvgqvm plffvvggfa savgwrstva rgggardfva trlvrlfrpa iplflvlava
      121 lgtatalgtp pellgevafg igsplwflaa ygitqccvpf marlharapw rtlgallvla
      181 aavdavrfat gvaevgllnl gpvwlfaqql gflwadgwft rrsrlvlvgg avagyaalvp
      241 ltsvglwapd mlqdlnppml plaflavaqa clvqlvhgpl srlmrtrgaq aavfvvgrdg
      301 mvvylwhlpl fialngiall lgapfpepgs avwwatrpva lvvvlavaig iarglrwfdr
      361 plprlvpgtd rpgwpvlava alctigpafa vmqlhlslgt avvgavlvpl gvvllgrivr
      421 ln
//
LOCUS       WP_284803367             471 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium macclintockiae].
ACCESSION   WP_284803367
VERSION     WP_284803367.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..471
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51283
     Region          3..405
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msrriirrvh tlaglfiapl ilvatlsgff yalaptiesw vydgeltats sspaqpvakq
       61 ieaakrihpd levakvqipd eegkttrvlf adpslpsesy sravfvdpgd lhitgeltqy
      121 gsaaslpfra wlseghrnlw ldtpgriyse taatwlgpma vtgvamwwfm rkqknqrapk
      181 kksrrqamkr htligliaap gliflcisgl twshfagdni alvreelnwi apkpntning
      241 eqstqdsgsg hgehaghagh gehaghggaa asevdfgqad tvlqvgrdeg ltgtlqlvpp
      301 skpgqawtvs eprqaykmyn daitvngeng dvvdrlpfks wpiaaqltsw iiqlhmgtlf
      361 gltsqialal lalgigaliv ygyimwwrrr ggkntgarvd lsaltwkhwl alavllggys
      421 vlaplfavsg ailfviawal dfrskntqks pkvilkepnd eekepvtvds h
//
LOCUS       WP_284803625             264 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Corynebacterium
            macclintockiae].
ACCESSION   WP_284803625
VERSION     WP_284803625.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..264
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28464
     Region          6..262
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mstldlsqet vlitgassgl gkefalqlaa kganlvlvar rqdrlnriaa eikrrhkvkv
       61 eviakdlseh gvageiswel strgitvtsl innagfanye sfsdvptdsl raeiavnvha
      121 lvelthmflp rfeergngfi lnvssiagfq pspgmvvyga tkafvlsfte glyaerkgsg
      181 vrimalcpgp teteffrvag sdradgglkr mnshdvvaag ieallrkspp psvvagarnk
      241 lltsvsqrmp rrvmtevmgr lmkr
//
LOCUS       WP_284803635             311 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            macclintockiae].
ACCESSION   WP_284803635
VERSION     WP_284803635.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..311
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34032
     Region          12..311
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mnrnrpveth wmpgatrlfn lviallnsdg prsvewvlan vdgyqhdndd sarrqlsrdr
       61 rdlaalgvhi ggtdelsldp aqtflpdief tdaeaaviaa ashwaqssgm hhaaqsayak
      121 laaagmqhri stgevaipai pdhtdldgds fdaifraldn glvlsfnyyp slvdtpqerr
      181 lepwafgaqd gltyvtgfdp draaqrtfrl aridsvvalp efsqhprpes tpqqliaqgl
      241 ahsrqmvtat vefpddgawe lrrltddngq igpvertwfv rtaaayaphv ivtsppdlva
      301 dvvavlreav k
//
LOCUS       WP_284803738             208 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium macclintockiae].
ACCESSION   WP_284803738
VERSION     WP_284803738.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..208
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22124
     Region          10..205
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(33..34,36..37,40..41,78,82..83,86..87,101,105,112,
                     115..116,121,144,148..149,151..153,155..156,159..160,
                     163..164,179..180,182..184,186..188,190..191,193..194,198,
                     201..202,208)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(147,151,154..155,157..158,193,196..197,199..204,
                     207..208)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(168..175,181,184..185,188)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mkqplhvhvp lsvfhpgtsv fhrapaglki flllvflvgt alwakvpwqa gvvvgftaic
       61 ylaaripvrl alrqllaptv llaafagllw wqrdlptalt yfgvilsava maslltlttt
      121 vvalmdavea glrplgtigl pvetisllia ltirliplta ltvnevqdar kargasrsvl
      181 afgvpvivrs llrarylgea lksrgvgn
//
LOCUS       WP_284803762             321 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA cytosine methyltransferase [Aerococcus urinae].
ACCESSION   WP_284803762
VERSION     WP_284803762.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..321
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=36971
     Region          1..314
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mnkvkilelf ggigairkaf inlkipyevv dyveidkacv ksynalyged ykaksvvgyk
       61 apnekidlvm hgspcqdfsr irkkqggvkn sgtrssllfe tiriikemkd kpkwiiwenv
      121 kgvldrnmrd sffiylkele slgyeskyei lnamdfgipq krerifvvsc lgknnfsfdk
      181 lerketrpls ellekdvsel ytmtqpymlk flnkgidnsf kgrlkvikdf sytistkqmr
      241 vpnsgiidig ngkyrylter eclrlmgfdd sdidkleevh prrknctssk lykqagnsiv
      301 vdvlmaiike ihrmevgnas k
//
LOCUS       WP_284803831             431 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium macclintockiae].
ACCESSION   WP_284803831
VERSION     WP_284803831.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..431
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46712
     Region          131..426
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 miefirkipl tgtwpevvtw avilavlsal ffalpsdppg rrwrailwsl avtvvltgag
       61 laflmlgttt pwseigfrll lgagalilaa nmagwcvgas ikkswtillv allavgtvaa
      121 anqsyelyqd vgevdpvelr tfhsvdelpk apavplkqwr gtkhpdlpae gsmlnvsapk
      181 kesgfhardl rvylppawfs sprpqlpvlv llagipgdpd qwfdsgqate iarryqqqhg
      241 gvapiiisad atggtwenpv ctdsnkgkvq tfltvdlprw aqqhlspnpd qhtwtiggls
      301 yggtcafqvi tnhpdsygsf vnisgertpd dgtshestvq nffggsedkf kaqnpedllk
      361 krtyprtagm fiagrddssa kaalkhlqpl avaakmqasy heisgahnfk twrgglnlaf
      421 pfivrrggle s
//
LOCUS       WP_284803864             168 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein, partial [Aerococcus urinae].
ACCESSION   WP_284803864
VERSION     WP_284803864.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         <1..>168
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
     Region          <1..>168
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 tahintqetg avesrghkil tisndqgklt aerlaaylea feanpnrahm vapgmvyity
       61 ptelgtlysk eeltqiyqic qdndlplyid garlgyglms peadltlael ahlcdafyig
      121 ankigalcge aivfsqrpap ayfpalvkqh ggliakgrll giqfdelf
//
LOCUS       WP_284803903             576 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Corynebacterium
            macclintockiae].
ACCESSION   WP_284803903
VERSION     WP_284803903.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..576
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62208
     Region          68..566
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mtnrsvnpht ssnpnnssss aspsiatgar sralgtsrrt flagagatga allgtgvana
       61 lgsqagsvag sagstgsagv agssgaigsl glqrarpvit hgvatgdvrp dgglvwarvd
      121 rparmvveas tdptfprhkt ktfrgamltp dsdgtgrlrl vgmqpgqkih yrvimedqht
      181 avrsqpvtgs fttapstnqa rksirlhwsg dvagqgygin pdiggmfcwk tmadrnpdlf
      241 ihsgdtvyad gpieanhkmd dgrifknlts pfknkvaetl eefrgqhayn lmdenykrfn
      301 sqvaqlvqwd dhettnnwyp geileddkyq vkdvnllaqr gfqafhewqp ldrkmavdgr
      361 vyrkisygsl ldifvldmrs ykdrnpdsga satkpghilg akqekwlvdg vknstatwki
      421 iandlplgiv vpdgddqegv sngtggkavg reaeigrvls gikdvrnvvw ltadvhytaa
      481 hhyspdradf qdfapfwefv sgplnaggfg pnkmdgtfgp evvyvhappk dkqnsspldd
      541 fqhfgevdid ggskdltvrl fttrgkelws ktlraq
//
LOCUS       WP_284803934             669 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Corynebacterium macclintockiae].
ACCESSION   WP_284803934
VERSION     WP_284803934.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 669)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..669
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=70982
     Region          4..246
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mlsaesaqhi sqrqkpqaiq pqsppattwr lttallaflt ilallptlav nanaednntg
       61 gdgkvaivld asdsmaekdt ndggtrmdaa kkaatdtint ladktetaii aygskesnap
      121 dnrakgcqdi ttlaplgnnk aedlnnkind lqpkgytpig naikkaaeel gdsgkrniil
      181 vsdgidtcap ppvcdvakdi agdgidlaih tvgfkvdnka qeelqcisev sggtyssadd
      241 tealskalad aaqraagdye sagtpvqlad natdgfylge glyqsslpsp rdssngdegd
      301 ekwfsisvpe gkkaqvsanl vpvgfeggdh iyynvdvefk netcdhsgsg yytgsnwpgp
      361 peaetvtidp eedcdptkyr vklnhsgtei dhdlpveivi gfepqldgse agpkndrevp
      421 egedrdkvkv psskpkptpg gtsynkatei tpgtvsdtlv pgetkfyrmn vdwgqrplae
      481 vefdkkhsnd srdgdiyvas prrtitsket insldkdvpv taravstpyv fyrnkegnvs
      541 qdkasdagqw yimvtlegyg dngkqdkdie frlstalegn kvdgpewrqt lepgpapsqd
      601 ppgsgnddgs gnsdgaesgd gnngdeaaaq akdidnasqs ntilyiglgi lavilaaava
      661 vyftavrrk
//
LOCUS       WP_284803936             268 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium sp. UMB10321].
ACCESSION   WP_284803936
VERSION     WP_284803936.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB10321
  ORGANISM  Corynebacterium sp. UMB10321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Corynebacterium sp. UMB10321"
                     /db_xref="taxon:3046312"
     Protein         1..268
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28709
     Region          6..226
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 masnsapvaa ffdldktiia tssvfafgke flnngmitrq ealdlyltka aymligqsse
       61 kmdttrdnla nmitgwsved vtavttetmh nvitpaiyse arelieahrk lghdviiisa
      121 sanilvapia kelgidmiva sevevvdgtl tgritrylkg dakaeairef vaehgydldr
      181 syaysdsatd ipmlelvgnp vavnpdralr khaqaegwdv qtfknpepli qmpnakevgi
      241 gasviagvta lavagtllak aikkdksa
//
LOCUS       WP_284803962             424 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium sp. UMB10321].
ACCESSION   WP_284803962
VERSION     WP_284803962.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB10321
  ORGANISM  Corynebacterium sp. UMB10321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Corynebacterium sp. UMB10321"
                     /db_xref="taxon:3046312"
     Protein         1..424
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45176
     Region          131..414
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mniarpaiag aaavaiaagg wyavapseqa ttisaaqsve etsineattt sssktttttt
       61 kveettvvev veedsteptl ddadiptaeg aettndaiar vkkletapqk psggdqywft
      121 nidgikgsek lsvyspamer dipvgvirag vpnaptvyll ngaggseqdt dwiaqagtvv
      181 kkvfedepvn vvipmagafs yyidwlyepn srylqgkqlw stflgselpd aiepylnand
      241 kravvgfsms atsalllaeh npgryaavgs fsgcaatstg ipngwvnltv nrggakpeem
      301 wgragseynr hndalvnaek lkgtklyiss atglfaesdt vgflrktrdm dfvqasanaq
      361 tliveggvie aamnacthdl lvklkandip ynanlratgt hswriwkedl elswkqtikp
      421 algl
//
LOCUS       WP_284803158              65 aa            linear   BCT 25-DEC-2024
DEFINITION  superoxide dismutase, partial [Aerococcus urinae].
ACCESSION   WP_284803158
VERSION     WP_284803158.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         <1..65
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
     Region          <2..60
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 egelkivstp nqdspvmngq apvlgldvwe hayylkyrnv radyidafwh lvnwdyvnel
       61 yaaak
//
LOCUS       WP_284803964             315 aa            linear   BCT 25-DEC-2024
DEFINITION  N5-glutamine methyltransferase family protein [Corynebacterium
            macclintockiae].
ACCESSION   WP_284803964
VERSION     WP_284803964.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Schubert,H.L., Phillips,J.D. and Hill,C.P.
  TITLE     Structures along the catalytic pathway of PrmC/HemK, an
            N5-glutamine AdoMet-dependent methyltransferase
  JOURNAL   Biochemistry 42 (19), 5592-5599 (2003)
   PUBMED   12741815
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..315
                     /product="N5-glutamine methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32750
     Region          1..314
                     /region_name="HemK"
                     /note="Methylase of polypeptide chain release factors
                     [Translation, ribosomal structure and biogenesis];
                     COG2890"
                     /db_xref="CDD:442135"
ORIGIN      
        1 mtinqavrea taqlaaagid saavearllm ryllaepgaa evagageate ateaaasapr
       61 aavdpgtlfl raddpapaey gdwvarrvar eplqhivgsa pfcgmdlfve pgcfvprpet
      121 ellaewaarf lagrptprvv dlccgpgtlg lgvsflfdap isligidisr aalqlaekna
      181 glvpqakarf iqadlsadgp aelsaipgav tanlepadvv vcnppyvpes tdispevaad
      241 phaavfsgad glelmprvlq waealgrrga gvgiehddsn gaqvaammqe rgwteviqhr
      301 dlagrprfvt allpq
//
LOCUS       WP_284804084             338 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            macclintockiae].
ACCESSION   WP_284804084
VERSION     WP_284804084.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..338
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34118
     Region          17..326
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mqilaalvgl alllvaslyl gsknlsvgev tsilmhgpqp saqsginaeq sgiiwdlrvp
       61 rtllavvtga alamagaiaq swtrnpladp giigvnagas favaaaltlg wattvgertl
      121 vglvgaaiaa lvvllisrvs rnpltlvlvg vgvtfalqaa tnmlslyssd tleglrrwtv
      181 gstagrgmed valaalglal galcgalaar pldllamged sarslgsspt rtrllaaaav
      241 iilagsatat vglvtfvgfa vphllrpftg paltrlllpt givggaavll adivgrfvlq
      301 pnelemsivl aivgapvmil avrrkkslpn sndselai
//
LOCUS       WP_284804085             350 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            macclintockiae].
ACCESSION   WP_284804085
VERSION     WP_284804085.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 350)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..350
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35752
     Region          19..343
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 msdttsirsi krsrkrrila atsgfaliaa lcyclilgqg avklspmevi evltgggtqq
       61 ainvvwdlrl pvaiatvlvg aalglagawt qtmarnplas pdilgvsgga avlvvagtvv
      121 trpawseqlp tfwwraalal vgalvivgll vllggfgtsq rvvviglals fltqslvqyl
      181 llradltrat daqtwlagst gfvrteallp malgllpfvv lglcvtrdvp llshddatas
      241 tlgvnvtrvr ailliaatgi vavvvsfvgp igfvallapq laklvaatpt phplcstfag
      301 aallaacavv agalpftspv glvtaiiggp alvllvrlaa rrgtlkgmvq
//
LOCUS       WP_284804133             514 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Corynebacterium sp. UMB10321].
ACCESSION   WP_284804133
VERSION     WP_284804133.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB10321
  ORGANISM  Corynebacterium sp. UMB10321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Corynebacterium sp. UMB10321"
                     /db_xref="taxon:3046312"
     Protein         1..514
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=55076
     Region          5..331
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(7..8,11..12,41,44,98..99,151)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(96,99,176..182,211,235..240,271,294..298,302)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mrvaalwfpd wpvqaaklea edtleepiai avqhrikvcs qearragvrr gmrvrnaqav
       61 apeltvvedn perdgrtfsa lagslddvaa svevlrpglv vadlaaaakf hgdedtalem
      121 lldaaarhgi dvmagaadei ataviatrss hvvaagesaq flavqplrvl taeaalgadp
      181 etvrtlgqlg iqtlgqlaql pssavmtrfg vagihlhris saapdrrvap elpvedfave
      241 mtpeepierv daaafaaral aatlhqrlkg agvhclrlki saelvdatrv ervwrtreal
      301 teagtadrvr wqldgwltng gagpiaslml eplelaqpdm vgelwsdgas degarrvier
      361 vqsqlgmeav lqpvavggrg vaeriqlvpy gevppqgrga fvgavpsplp arlgggiehp
      421 ssrvqlldsa dqpillnaev llsgqpttlv wgkrcydita wagpwpvdee wwgahptrla
      481 rlqvlghdqa vgtgqrgwll vwhrqrwsve alyh
//
LOCUS       WP_284804203             274 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family oxidoreductase [Corynebacterium macclintockiae].
ACCESSION   WP_284804203
VERSION     WP_284804203.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Blankenfeldt,W., Kerr,I.D., Giraud,M.F., McMiken,H.J., Leonard,G.,
            Whitfield,C., Messner,P., Graninger,M. and Naismith,J.H.
  TITLE     Variation on a theme of SDR. dTDP-6-deoxy-L- lyxo-4-hexulose
            reductase (RmlD) shows a new Mg2+-dependent dimerization mode
  JOURNAL   Structure 10 (6), 773-786 (2002)
   PUBMED   12057193
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437758
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..274
                     /product="SDR family oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009226 - nucleotide-sugar biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0019305 - dTDP-rhamnose biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28914
     Region          3..273
                     /region_name="RfbD"
                     /note="dTDP-4-dehydrorhamnose reductase [Cell
                     wall/membrane/envelope biogenesis]; COG1091"
                     /db_xref="CDD:440708"
ORIGIN      
        1 msvlvfgasg qvgrallrlr pdfvpvgraq adlavagsvd sflltppspv eaivnlaaft
       61 avddaekpen asavhqvnav apgrmaswaw ahgvpmlhvs tdyvfpgnlp vgwenpvdgq
      121 papvnaygrs klegerqvln fggrvvrtgw vydaesrnfa ttmvrlarsg vnptvvddqy
      181 grpthasvla aelaamvdgk raaaishvtg sgpvttwcgf areifatigh dprrvkavps
      241 seyptpahrp rnstlqipas glpawrdslr aalg
//
LOCUS       WP_284804248             187 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Corynebacterium sp.
            UMB10321].
ACCESSION   WP_284804248
VERSION     WP_284804248.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB10321
  ORGANISM  Corynebacterium sp. UMB10321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Corynebacterium sp. UMB10321"
                     /db_xref="taxon:3046312"
     Protein         1..187
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19163
     Region          16..>77
                     /region_name="SCO0930_lipo"
                     /note="SCO0930 family lipoprotein; NF040526"
                     /db_xref="CDD:468525"
     Region          55..187
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mtyprsrrsl svprprhlas alflaavmal ttacasspsg psaapggssp daagavavtv
       61 sdidgttrti pdgkpaalff fsvgcgecvk gadslnkast algssadyll vdvdprepke
      121 tingfrdyik apelpavidt gatlttrynv tsistlvvvd akgdvtfrat dpsaekiqee
      181 ltkasaq
//
LOCUS       WP_284804261             409 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium macclintockiae].
ACCESSION   WP_284804261
VERSION     WP_284804261.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..409
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43908
     Region          77..382
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mkrsivrtla avtaaiapfa tvsaiapaaq aasisaaqka dgiapakisl ntqtqglsee
       61 tttwrsiiks wndkgfdniq evsayspsmk rhiplvviqp kdkekrdnap tlymlngadg
      121 gqgianwirq tdivtyyggn sdpskgtvsp giganivipm tgaysyytdw vtepdtseik
      181 gpqkwetflt relpqaiepa lkandkraia gmsmtgttsl lyaqhhpgfy dsvgsfsgca
      241 atttgltpkf idlvlnrggt dftkmwgpvn gevarnndal inaeklrgqk niyvstssgf
      301 pgehdmpwse rvngqlssaa pvifegavie gatnactrdl arktnalgip vnynfrpagt
      361 hqwgywqddl rgywndlvng lgtgaerpkl qptkpisped ywagstsgs
//
LOCUS       WP_284804296             275 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium macclintockiae].
ACCESSION   WP_284804296
VERSION     WP_284804296.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..275
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30227
     Region          18..237
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mtnvnqhqep arasgngril aifdldktii dtsaslayrr pmaergllnt gevlkmmaml
       61 gnymlsthse dnlestkdal tsiikdrese plrqvaqdal qevitpfiyt eareliewhr
      121 kmghriaivt asasimvqpi akelgvdhlf ateleekdgr ftgavthfnk ghakverilq
      181 lvaehgydld esyaysdaat dipmlelvgn piavnpdrpl kkratesdwp irqfsrpepl
      241 fpqaavlaga gatlallgia atglamwlrg rdegv
//
LOCUS       WP_284804473             233 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II [Corynebacterium
            macclintockiae].
ACCESSION   WP_284804473
VERSION     WP_284804473.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..233
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /note="Members of this family of hydrolases with an active
                     site Cys residue belong to MEROPS family C26.; Members of
                     this family of hydrolases with an active site Cys residue
                     belong to MEROPS family C26.; Members of this family of
                     hydrolases with an active site Cys residue belong to
                     MEROPS family C26.; Members of this family of hydrolases
                     with an active site Cys residue belong to MEROPS family
                     C26."
                     /calculated_mol_wt=24905
     Region          3..199
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 mrilvidnyd sfvynlvqyi gqlgfsgddc vvlrndapel qgnglattlq dfdailvspg
       61 pgepsaagrt ldvlkiavdq qipllgvclg hqaiamhfga qvvradelfh gktspvthdg
      121 tgvlvgvpsp frvtryhslt vdpasvpeel lvtatsdsgm imamrhrslp ihsvqfhpes
      181 vmtqyghlml anwlneagqr aglgevvpae lvdrlvqeql evtgaisaea sml
//
LOCUS       WP_284804476             482 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Corynebacterium macclintockiae].
ACCESSION   WP_284804476
VERSION     WP_284804476.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..482
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=50785
     Region          1..477
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mnrsiravai fsfilvmali anltyiqafq qkslahnpln srqfleaksq ergritaggq
       61 vlaqsvkdse dfydreypym sakygsvigy lsdqygasgi essqnsiltg eddslfatrt
      121 wdmltgkevg ganveltlnp kvqevaydql ankgysgsvv alrpstgevl amastpsadp
      181 grivgppaee akanfdnyak desspllnrs tqqiqppgst fkvittaaal kdgdnpntsv
      241 taasqitlpg tnttlenygg aacggggttt lreafkrscn tafvemanrh gtdkfkdvah
      301 afgvgekddy lglpvepsrv gdipddaalg qssigqrdva ltplqnavia atianggvrm
      361 kpylvskitg rdlstlrttk pqkvgraipe ktadtlkelm vdaekwaggd asiasktgta
      421 ehgedsrnsk phawyiafst sadvavavlv enggdrgqaa tggsvagpig ravihaaeke
      481 qq
//
LOCUS       WP_284804482             214 aa            linear   BCT 25-DEC-2024
DEFINITION  IMPACT family protein [Corynebacterium sp. UMB10321].
ACCESSION   WP_284804482
VERSION     WP_284804482.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB10321
  ORGANISM  Corynebacterium sp. UMB10321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Park,F., Gajiwala,K., Eroshkina,G., Furlong,E., He,D.,
            Batiyenko,Y., Romero,R., Christopher,J., Badger,J., Hendle,J.,
            Lin,J., Peat,T. and Buchanan,S.
  TITLE     Crystal structure of YIGZ, a conserved hypothetical protein from
            Escherichia coli k12 with a novel fold
  JOURNAL   Proteins 55 (3), 775-777 (2004)
   PUBMED   15103642
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Okamura,K., Hagiwara-Takeuchi,Y., Li,T., Vu,T.H., Hirai,M.,
            Hattori,M., Sakaki,Y., Hoffman,A.R. and Ito,T.
  TITLE     Comparative genome analysis of the mouse imprinted gene impact and
            its nonimprinted human homolog IMPACT: toward the structural basis
            for species-specific imprinting
  JOURNAL   Genome Res 10 (12), 1878-1889 (2000)
   PUBMED   11116084
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Corynebacterium sp. UMB10321"
                     /db_xref="taxon:3046312"
     Protein         1..214
                     /product="IMPACT family protein"
                     /calculated_mol_wt=23137
     Region          15..203
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 mrtsyelpaa gdittheiei krsrfitwig rtqseaeara liqraretyp darhhcsayi
       61 lnvddalpve rssddgepsg tagkpmldml hgsemldlta vviryfggik lgagglvhay
      121 sdsvgqtlpl vprvlrstke lvrvdlphae agrieaelrn agfdivnvey gaaatytlah
      181 dpgqrealda qlaastqgra eaeeagsqwi esar
//
LOCUS       WP_284804403             549 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Corynebacterium macclintockiae].
ACCESSION   WP_284804403
VERSION     WP_284804403.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..549
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=59973
     Region          24..491
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mnatpdtsta ptnatsplpq ladataerpl dilivgagls gidlahhvak nfpdwnwaav
       61 dsnynlggtw atfqypgirs dsdmatfslp fkkwphkgtl gsgkqirdyc reaaeeigml
      121 drlqlstwvq avnfhtdqgl wevtmrlgrp ghansegtdg atypaspeqp tlttwtrrlh
      181 fatgyyrhse gftadiegvn tfegtalhpq qwprdldvrg kkvtvigsga taitlvpalh
      241 emgaevtmlq rtptyiaplp etdtissfvg lalstepgtf ghrlarslhi grdmaqyhlc
      301 qtfpsiaklv frgwnrlylp adevrrnftp pydpwdqrvc kspggdffka vrggarvatd
      361 hisrvdaggv qlrsggyies dvlviatglq llafgdahfs vdgtpvptes lvayramman
      421 rlpnfsytig ylnqswtlra dmtsrylvql wkdmdargeq wacpvlpage aadlpllems
      481 sgyiqrsvat lprqgagdpw rmeqdyiker rtytgadnrh dmafgtdale aaaplaageg
      541 gggaaelrv
//
LOCUS       WP_284804668             251 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsB family cell division protein [Corynebacterium macclintockiae].
ACCESSION   WP_284804668
VERSION     WP_284804668.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..251
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=27936
     Region          77..159
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 msestkgepg kepedlahad vaserkgqes drpesarlpr arsierrerr reraqtapkr
       61 martfvavpk nmspatwlva lmlaiflals ianplrnyfe qraelaqina kiegqekeka
      121 eltdelnryr dqdyikeqar trlgliepge sayriispki hadklgteqg edatgdeasr
      181 dwyarlwdsi stpeeakdeg sdpakenhkl ptvpeqnpqq dpaqnseqap eqnpgapega
      241 pqpapeqapa n
//
LOCUS       WP_284804728             924 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium sp. UMB10321].
ACCESSION   WP_284804728
VERSION     WP_284804728.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB10321
  ORGANISM  Corynebacterium sp. UMB10321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 924)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 924)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Corynebacterium sp. UMB10321"
                     /db_xref="taxon:3046312"
     Protein         1..924
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=102868
     Region          9..922
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 msassdsfla qfqaskdfpl dpfqieacqa leddrgvlvc aptgsgktvv gefavalals
       61 rgtkcfyttp ikalsnqkyh dfvaaygees vglltgdvsi ngsadivvmt tevlrnmvya
      121 eaprldrlth vvmdeihfla dpergpvwee iilnlddsvq ivglsatvsn seefgewlnt
      181 vrgdttvivs edrpvplsqy mmvgkkvlpl fepanpssep elnralahqi ariesrttee
      241 gaddfhegrg frarssgrrh grtrqqdryr pvgrpeivev ldglemlpai vfifsragcd
      301 galyqclrsr keltteeera raaeiidagv egipeedlkv lnyrqlrsaw lrgfashhag
      361 llpafkhive qlfveglvrv vfatetlalg inmpartvvl eklvkfngeg hvdltpgqyt
      421 qltgragrrg idvlgnavvq wapamdpqyv aglastrtyp lispfapgyn mainmlamng
      481 fddsirlieq sfaqfqtdrs vvgevrdler legkvarlra qlsrdissya ppsdhaiedl
      541 leyldirhal sveekkarrd aldnrhteva rvlarlevge iialpgkrqp elavvvqpag
      601 rhddprpwvt tergwssrin adffkntplv vgrmkvprht rdqprrfakk iasqlrhapv
      661 hapkrlreka ryrtpksvtk lreqlhahpv hswpatdrem larvgeklar eqraldrlsr
      721 qvdnatdtlg rtferligll qeldyvelve gefqvtdege rlaklhnvsd llvaqclkrg
      781 iwdeldpael agvvsmvvfe nrrttggspe aatepmaham netmrvygel vsdeqrhklp
      841 ltrmpdphfs lalhqwtaga plgyalaaaa esgaeltagd fvrwcrqvid lleqvkkvgy
      901 sdeirnnanr aieairrgvv aign
//
LOCUS       WP_284804733             442 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: SAM-dependent methyltransferase [unclassified
            Corynebacterium].
ACCESSION   WP_284804733
VERSION     WP_284804733.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..442
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=48626
     Region          47..>88
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
     Region          183..319
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mpipepvpth lhtvdatkwp rlvqpldgfa lktrarlaea efaracdaag vtlsgddadi
       61 lvnherlfer iaaagwtgla egymagewsv tssdvlvevi akllgqgyvp rrtswkprpe
      121 tvgamlpssl vqhfsgdrvs afqghfatgv atterkltks ypeqrakqrg akrryidvtt
      181 yeapldadra dlgdiqarsa qqlldlvgag rgtrmleypn sggavalaai grgvvvdtla
      241 ishdsaahlr eylilngaan dvrvavgklg daqwaqqhgp ydaivsfsql escpkrdkvq
      301 ylramdrmll pggrigvqsv marrvqsksv nracrsalqv lgayvwpgme yqyevdflkl
      361 veqqthlqai sisrapehlr lsirlqrqmf egrlreaaad gydevfrrlw lwqfavreav
      421 asvggldlaq avlvrkhrgg rr
//
LOCUS       WP_284804758             419 aa            linear   BCT 25-DEC-2024
DEFINITION  acid phosphatase [Corynebacterium macclintockiae].
ACCESSION   WP_284804758
VERSION     WP_284804758.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130290
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..419
                     /product="acid phosphatase"
                     /EC_number="3.1.3.2"
                     /GO_function="GO:0003993 - acid phosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=45402
     Region          18..299
                     /region_name="PAP2_acid_phosphatase"
                     /note="PAP2, bacterial acid phosphatase or class A
                     non-specific acid phosphatases. These enzymes catalyze
                     phosphomonoester hydrolysis, with optimal activity in low
                     pH conditions. They are secreted into the periplasmic
                     space, and their physiological role remains...; cd03397"
                     /db_xref="CDD:239491"
     Site            order(186,193,221..223,256,262,266)
                     /site_type="active"
                     /db_xref="CDD:239491"
ORIGIN      
        1 mtknkslkit matvmattms lsavnvepav aapsmpavag segvpgfphp vqhkgaptpq
       61 pfgpeylggy isdisshgyg vyldvvdgfn dvranhpgim kqnldkvvni nnavqdnpaa
      121 iqraqkdara dkagvldafs dslgtelgrh frdalrenrl pktqfllgng ylaraggvas
      181 stfvekmvfg ydrpfvvape rinkyedgqn kyygtsksyp sghtnqavws ttllaltlpe
      241 lapqilargs eagnnrivmg vhypldvmgg rmsgtaaaad rwndpkmrda iqqagkelra
      301 elewragrpi aqvvksdkay rstdqavrey tdrmtygfpk iyrkdapmiv pqaapdllla
      361 kfpklnykqr asilrqtaip sgsplddqgp rgswqrlnma aafaakikvn gdgsvtvlr
//
LOCUS       WP_284804930             338 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            macclintockiae].
ACCESSION   WP_284804930
VERSION     WP_284804930.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..338
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34391
     Region          29..334
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mpnkhkpsah sgvwllaigv iviallpvsi ivgavdispr eawhaffafd pgntkhllvr
       61 eirmprtala iivgvglgaa gvvmqaitrn plaepgllgv nsgvtltvtv aiaffgyssl
      121 aasmafgflg agltgalvya lggvwqgagp vrlvlagaav nvallasari ilvnsdtdvf
      181 drfrtwtvgs legrgtelll ptgaavlagf viaytisgal dasvlghdls rslgikpavv
      241 lsfataaiif mcgavtaaag pisfvgltap figralvglr hrrlipatal iasavvlvad
      301 iagrlvvpsg eigvgimasv igapvfiaiv rrrkipql
//
LOCUS       WP_284805013             717 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Corynebacterium macclintockiae].
ACCESSION   WP_284805013
VERSION     WP_284805013.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 717)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 717)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 717)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17597966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..717
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=76184
     Region          45..312
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
     Region          <601..715
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mtferrlpal akadvqsvfe pmqlqtlprs safswravqe grlprnenev aispnqaesg
       61 avntlkvndt ievrlqasek gtlvagenka kvkivgvlep dattqffgir siystpalad
      121 gletqgqpad geirmkfpdv steeaikhlr dlnletleiy sgqtygdtla dkyvgdrkyy
      181 filldgfmav iiivaalvif ssyqlitaqr vreygllral gasndgirrs giyeaallat
      241 gasavavpig lwftgqaaqk atslgiklsl esdrvptwav alvvvgaiav tvaacvpsis
      301 ktlkndtlan lrqsrnasmq rptvlvgtfl sivligasif gldyladaaq egttstkrla
      361 asialgsvla lgaaflagvl ipvlyrvtgn lvsvsglkip fryagvqslr saalviiala
      421 ssalvvavgv gqsrvsdhln dkadtiftpd vtvtpvdgsd vaalakqiqk ngsfgsvvsa
      481 wsvavtaedq sgdsepadam ssahfetfnh gganpdlkqr flvgtqsrlr etlkdgemsk
      541 fsvngkdvnl tvkftnaqgn yidadalsen ginfkigpes laltlrqgek srglnfvsan
      601 kelteilskd grqfvikqgf eakqtvknta armssisval iivslvittt acansmalai
      661 rersndrkll laigvnrlal frfaslelmi llipsvivga wigsfaahei vqtlgag
//
LOCUS       WP_284805044             700 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Corynebacterium macclintockiae].
ACCESSION   WP_284805044
VERSION     WP_284805044.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..700
                     /product="PhoX family protein"
                     /calculated_mol_wt=76735
     Region          46..694
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mglkgrnllk kmdftssrsh rtcvykcgda cskpvnnksd nnyfmdliqg tfsrrsalra
       61 ggaavvtvgg asflaacsdd ngeggakggn genkggngsg nadatdglkf emvepntkde
      121 vvvpagykse vvirwgdpvv egakefdvdn qtaeqaakqy gfncdfaall piegennrfl
      181 lvsnheystp qqmipdydle npskehvdie lashgmsive vegndkdgkl kpvmgkynrr
      241 ltgttefelr gpivghklvk tsddkegkiv kgtfnncsgg vtpwgtilsg eenvdqyfag
      301 genvkdekvr erlsrygied aktarqwekh ydrfdvtkep nephrfnyvv evnpwdpkst
      361 pvkhtalgrf khegsnihvt ndgtvvaysg ddsrfeyiyk fvssrkirsg ntdkdreenm
      421 kildegtlyv atfegnnkdf dennppkgek fdgtgkwikl vtvkedgsae shvdgmsaee
      481 vivftreagd kvgatkmdrp edvephpttg kvyaaltnnk yrgtqeegkn kegvreyapv
      541 kenkngmvie ieddftgeel kwnlllvcgd pdeaetyfgg fdkskvspis cpdnvtfdsf
      601 gnlwvstdgn alesndglfa vslegetrgl tkqfltvpag aetcgplvfd krvlvnvqhp
      661 gedeeatvkt skshwpdggd siarpatvva wkedfgtiga
//
LOCUS       WP_284805091             765 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium macclintockiae].
ACCESSION   WP_284805091
VERSION     WP_284805091.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 765)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 765)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 765)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..765
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=83544
     Region          1..763
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 msptddiaae qrylddllar vdharekleq rlkavrlead iddpqglmvr dreardiaqr
       61 ldsysaaevg lmfgridved eeaenpvagn ekldrryigr iglhdddeqm rtllmdwrap
      121 larpfylatt lhpdgvhtrr hittrgrtvr svadeqlsta adpsesvgag arggvakeea
      181 lldavnrart aymqdiveti aaeqdtiira ehrgvtvvqg apgtgktava lhraayllyt
      241 wreqldntgv liigpndrfl syisqvlpsl getgvvlatp gtllpnlhtv petnllarev
      301 kgseemltil adaiksyqtv pedsidisid glnvqltptm vraarararr srkphnhara
      361 afldyglnal adalgkniga dplgganlls kgdiatlree lgadptvvdv lgqfwpelrp
      421 tqvlerlyad paaiavdyde dtwhglathp sgewtdadap lidelidmlg yvsdeetaae
      481 ereqwlekit eaqealdilt gsasqdlddg fapevlmayd vidaetlaar qqvrdertta
      541 eraaadsrwa fghvivdeaq elspmawrmv frrspnrwmt lvgdpaqtgn pggvdswaea
      601 lspfvadrwq lhqltvnyrt pkdiadlaap llqeidptqs vplalresgt gvrylpvega
      661 elgskvqaav eqareltgee gligvittrp eplqvalses tdasgaevvf vdtaaakgle
      721 fdevvlvepa diveaspqgl ndlyvamtra tqgltvvhar elpwn
//
LOCUS       WP_284805324             375 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium sp. UMB10321].
ACCESSION   WP_284805324
VERSION     WP_284805324.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB10321
  ORGANISM  Corynebacterium sp. UMB10321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Corynebacterium sp. UMB10321"
                     /db_xref="taxon:3046312"
     Protein         1..375
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=39940
     Region          7..368
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mnhgpgltfr flaaqvlvvv isllvaaava ttvgpplfhd hmlmagredp slelfhaeqa
       61 yrdanlitla valptalisa llaslwlsrr lrtplqdltr aatslaagns rtrvpageag
      121 pevatlahaf ntmadrleht eqvrrqmlsd lahemgtpls vltvyldglq dgvvdwdnan
      181 htimadqltr ltrlmedidd vsraqehrid ldlveeglgd llhtaaaaag eayadkgvdl
      241 qvetitdaar vlvdrqrfgq vmsnllsnal rhtpaggqvr isvqrqgast alihvaddge
      301 gippsqlghi ferfyrgdaa rsrdnggsgi gltiskalie ahggtltats pgpgrgavft
      361 lrlplsppds eeaar
//
LOCUS       WP_284805389             612 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Corynebacterium sp. UMB10321].
ACCESSION   WP_284805389
VERSION     WP_284805389.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB10321
  ORGANISM  Corynebacterium sp. UMB10321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Corynebacterium sp. UMB10321"
                     /db_xref="taxon:3046312"
     Protein         1..612
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67273
     Region          14..612
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 masetyttpl gfklsptdtc lsalvdictk kphivlfsrp rnydwvnvta gefleevyet
       61 akgliangve pgdriavlss tryewslvdf aiwaagavsv piypsssmhq iqwiledsga
      121 eiaftesrdh tqlmsafllq edgkprlkds ssklrkiyef naagvetvkf egrdveqslv
      181 darsaslthd dlgsivytsg ttgrpkgval thgnwahqtw alikndigev arpgkrvvtf
      241 lplahvlqra vslaltmaga tqshwadtht ltvelqraqp nmvlgvprvf ekvrnaaynk
      301 aadgsaigka afleaektai eyskamdtpe gpsrilkakr rvfdrvvysk ikeaiggsvk
      361 ygitggsams adllhffrgi gipiyegygl tetcaascvn nknankigtv grpvngyqvr
      421 tnddgeiefk gpgvfdrywn nkaateeaft egwfntgdlg evddegyvri tgrkkdlivt
      481 aggknispgp mediirqdpl isnalvvgdg kpfvgvlvtl deeelqrwks thnipenrkl
      541 sdlagdpvlr aevqdainva ngtvshaeai kkfrildrdl seqenemtpt lkvkrnvvfe
      601 rfredidkly er
//
LOCUS       WP_284805520             242 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium sp. UMB10321].
ACCESSION   WP_284805520
VERSION     WP_284805520.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB10321
  ORGANISM  Corynebacterium sp. UMB10321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Corynebacterium sp. UMB10321"
                     /db_xref="taxon:3046312"
     Protein         1..242
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26264
     Region          84..230
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mttrkvknpn ekngagfiwa ivaviaiaal viglifvngk kgreaamaen midttgitvs
       61 wneddhfirl aaegvddapm aelyedfscp hcadlavatd eqmfeklreg kievelrpmv
      121 tldgltnghs tmglaaelal vandepaamm nlrdhlmvnq kdvyskvtdd dladlardyg
      181 asdkavqdir dktyydaara msngnlklqq erggeagtpr vmvdgkdveg einnwvdtva
      241 ns
//
LOCUS       WP_284805716             396 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator, partial [Aerococcus
            urinae].
ACCESSION   WP_284805716
VERSION     WP_284805716.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..>396
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
     Region          17..>394
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 msstvvehwt dlyfdsseqe iiysklerql mitllsfsni scnsifelql ffdvskntiv
       61 ndiaalrsel ekedldltys rakgyqlkgd eltvrsfafd kmgdllklqn gerllykglt
      121 qisndyyakv rlsfdtiiqn nhlkivetrf nkslyfvayl lqrskynnch ftqadkklis
      181 svrlyhsski lldnveniks ydeekyyfti llliicekip kpngfdflyq cskeiinefq
      241 risaveieny dylleslyqh lvpaffrikf nfyisnplle evlnqyndlf nilkvalepf
      301 rqvlnkripd neigfftvlf ggqtqskysk qslkavilcp ngisssvimr aelqsmfpei
      361 eminsesind fegflkdndn hsevdlvfst vpikld
//
LOCUS       WP_284805729             523 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator, partial [Aerococcus
            urinae].
ACCESSION   WP_284805729
VERSION     WP_284805729.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         <1..523
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
     Region          <1..508
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 aeydisvvnt kkgleirgse lkqrqflidy ffsrkfnssf minlqntvfd ssinlgeitv
       61 ivldeirnad lyvsdfvien sivhialmvq rlrngntlmr hllddldkqg knyqvakniy
      121 drlvrsfpdi ripeveaeyi sihlisrnnk klsikntevd keiktainnf selvngriqn
      181 dsilykglvd hfnqllirlq nqieisnpvl rdvekyysee laitkksfqs iadildypin
      241 dnewsyvtlh miaamerysn sqkirvlimc atgvgsaqvm knrlerefgn alsiskvisy
      301 yeldkkvlne vdlvissinv dglylpvpvi nvsviindsd irnikkfvni ktdnkrklsn
      361 sdhkyeniqn eyvfyncfse drfivthken inkekmlshm iallednpqt nfnemflrei
      421 kiretygpii fnnilaiphp tkpltkdeki vvaiikkgly wdsenpnirf ifllspsitn
      481 nknmrqvsns lakiienksl edellninny ndfknimlki lsl
//
LOCUS       WP_284806025             331 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium amycolatum].
ACCESSION   WP_284806025
VERSION     WP_284806025.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..331
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=35286
     Region          159..320
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mseenkdnia tdhsgdsqqp sadearqetl qepqqasqpv pteqdlesws adsdgktksw
       61 ysipnaawal avvalivvga agffagsrsa sfngvstvnm agvapgkgei apvpgpngdf
      121 dasiygpkag aqlkspedmd nvhrrnendp falgavdapv visiysdfec pfcakfanet
      181 esalvekyvn eglvrlewnd maingekaik daeagraaaa qgkfwefsra lfkkagekgq
      241 ghpeftekel iavareagvp dmkrfekelk dgkwteaven atqfgsmlgi sgtpgflvgt
      301 qfvsgaqpld vfedsielal ihakraeeag k
//
LOCUS       WP_284806079             224 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Corynebacterium amycolatum].
ACCESSION   WP_284806079
VERSION     WP_284806079.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..224
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=24739
     Region          1..222
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mlfdqlprdd aritpgvvhl pgwlplerqa giitqlrdia rdvagtplam trpqlksgqm
       61 qvfmlhlgrm watnpyryvt hvggvrvppv pdnllqlate alraaalyde slsqwpatfr
      121 pdmalvnyyp pgatmgmhqd rnenspapiv slsigdealf riggtenrnk pwddvtlasg
      181 dvivfggpkr lafhgvpktr pgtlpercgl kegrinitfr qver
//
LOCUS       WP_284806153             377 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Corynebacterium striatum].
ACCESSION   WP_284806153
VERSION     WP_284806153.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..377
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41640
     Region          70..355
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 masikkyeta kghawrvqyr spdgrnrnkr gfrtkdeark waeknaasit dgdwvnpveg
       61 kvrveelgar wlamqthlkp staelykqvw nsgvkprwgg vrvgsilpsq vqewvaemtl
      121 ddvsgswvrh chmvfaqvld mavgdrllkk npargvklpr kgkarkvflt mpqleafaae
      181 cgdredlill lgtsglrwge aialrpcdld plrgrinitr naakvgndvv lgtpkthear
      241 tvavaprvme mlmrraaglg kdellwtgkr ggwlrapghn twfdgalkrv qrkdssfprv
      301 tphglrhvaa glliqaganp kivqrqlgha saamtldqya elwddgldei asvldgsfsd
      361 avklqsnggf raveqgv
//
LOCUS       WP_284806248             584 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Corynebacterium striatum].
ACCESSION   WP_284806248
VERSION     WP_284806248.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..584
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=61629
     Region          1..454
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          <456..572
                     /region_name="PRK12999"
                     /note="pyruvate carboxylase; Reviewed; cl39082"
                     /db_xref="CDD:476865"
     Region          518..583
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(541,550..552,559)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            551
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 misavlianr geiavriara ardlgirsia iyseadagal htrvadeaya lpgntaadty
       61 mnvpalldia vragadaihp gygflsenad faravasagl twigptpesi ellgdkiaar
      121 rvaeevgapl apgtsdpidd wqearafaek hglpiaikaa yggggrglkv venledieaa
      181 fnsagreake afgraecyve kflthprhve aqiladthgn vavlgtrdcs tqrrfqklie
      241 eapapalsde qrtgihegar aicakvgytg agtveyivse dgtisflevn trvqvehpvt
      301 evvtgvdiia eqfriasgep lsfvdesldp ephghafefr inaedilngf apcpgtivrf
      361 epptgpgirv dagvrsgsiv ppyydsliak llvwgptrev alarakqala efdiegvrtv
      421 lpfhrdmvss qvladhgdak aaagiytdwl dhnyrpsaes tsniapveai yakrtqvaie
      481 idgklvsvgl penlfaaapa aaggvkvasp sagaqegevt apydanlvaw nvadgdtvee
      541 geaiatieam kmessvkapr ggtikllake gdrldpskvi atid
//
LOCUS       WP_284806256             630 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium
            amycolatum].
ACCESSION   WP_284806256
VERSION     WP_284806256.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 630)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..630
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64819
     Region          32..629
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mssacgcehe pateiedldr pwwkdpelll pifsgvalgi glaldwsgle tpatvlfwig
       61 lllgaytfap gairnlvtkr klgigllmti savgavilgy vgeaaalafl ysiaealedk
      121 amdraqgglr allklvpqta tvlrdgttve vtakdlvvge lmlvrpgeri atdgiirsgr
      181 ssldtsaitg esipeevapg devpagains agvleietta agtdnslttl vdlveqaqae
      241 kgdrariadr iaqplvpgvm ilavlvgvig sllgdpetwi tralvvlvaa spcalaisvp
      301 ltvvaaigaa sqfgvviksg aaferlggir hlavdktgtl trnqpevtdv vpadgfdraq
      361 vlafaaaveq qsthplaaai aaagteapaa ldiseeaghg iggtvegrrv lvgsprwida
      421 gplkadverm esegqtcvlv tvddalagai gvrdelrpev peavqtlhan gvevsmltgd
      481 nartaralae iagiddvrae lrpedkasiv aelssktpta migdgindap alagatvgia
      541 mgatgsdaai esadvaftgh dlrlipqalq harrgsriin qnivlslaii ivlmplaisg
      601 vlglaavvlv hevaevivil nglraarakr
//
LOCUS       WP_284806273             507 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Corynebacterium
            striatum].
ACCESSION   WP_284806273
VERSION     WP_284806273.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..507
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=53735
     Region          43..483
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 metktvlaqg avdqtiqnvf gpfvdvlekv vffaipigea elplvviwll mgglfctfyl
       61 rvrpfkdakq tfrvvrgmla rksdpgevts fqafatelag tiglgniagv avaislggpg
      121 aslwiiiagl lgmalklaea tlsqmfrrvn sdgsisggpm yylkdgltsv gkpklgsflg
      181 mfyaigfals afgagnifqa nqvalhvidi tggtnsffan kawligvfla ipaalvilgg
      241 isaiaqwtsr mvplmsviya vgvlavlgan ftdiphaasl ivsgafnpds isggvigvmi
      301 igiqralfsn vagvgtagla hsvtknrrpa eegftaawep ffdsvvvctl talsiivtgq
      361 ylnqgeegvt lasnafatvn gvfpwllslc iilfafstvl sycfygekaa gyvfkenkia
      421 elgykvvyll miivgaavsl dtvvrfsdat fflvsipnll giyllakplr keiteyrasv
      481 dngtidvvpe heqvkmfpkl ektvads
//
LOCUS       WP_284806408             301 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Corynebacterium striatum].
ACCESSION   WP_284806408
VERSION     WP_284806408.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..301
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31267
     Region          5..283
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mtnplailcv igscislqlg aalavqlfdd ggtwgtaalr llmaaavlll isrpkvrtwg
       61 reqwlaaaal glslgmmngf fyaaiaripi gpavtiefig plllaaflsr slrdavcval
      121 avfglgllgw dsltgepldp igvglvlvag acwvayilas kkagslfsgq dglavalaig
      181 giallpmggq gavvlvsdsh llllafgtgl laslipysle italrslnpn vfsilvalep
      241 vfaaffgwll lsqnlsplkl laialvimas vlqtmvparg tkpklrrvpw kahrrsrakv
      301 g
//
LOCUS       WP_284806594             659 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Corynebacterium amycolatum].
ACCESSION   WP_284806594
VERSION     WP_284806594.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..659
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=69494
     Region          <5..230
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mirtrqlsav vltismllvl vgsfagitag raqaqeaast isptmvilda sgsmladdag
       61 gqtrmeaakd atskfaesvs edseigfmvy gtevgnspee reagcqditt llpvqagnsa
      121 kipaevgkiq asghtpmgpa lrqaadelpk egqrsivlvs dgedtcappp vcevakelkq
      181 qgidlvintv gflvdagara eleciaeatg geyldaqdsd slaesmktla trtartaqss
      241 aqeiqggdap tsatqvpadv etfstklrek tpesersisn qegdgaeyfs vpvaegerla
      301 isaatvpgas sgatlmdldv rnfaltmhld dsscflandf gngiidsngp ffasittkqp
      361 ggaegdcksg nmvfsvarkg gpfegqdipa evtikrfane nltdvpeafp sdkeslnppp
      421 atpeadqakk vtpgswfdda teltadniss vtadivpget hvykikseyg qqlrgavkli
      481 dapeadklaq isgldiktln sarqlagsee nrpvnehqig eettfgnsar inyrnriged
      541 geksgdyeae rawldgdqyi vvffnnswga gkshdvadvq nvpvtyqltt elvgekipgp
      601 afeqvahksp sseaqtssqq npkgteened egssnmmwfs igavllavvv gavialtrr
//
LOCUS       WP_284806750             452 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium striatum].
ACCESSION   WP_284806750
VERSION     WP_284806750.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..452
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48985
     Region          116..449
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mplrtwllvl mvlvsglgla gsslavssim tdvmyanvde qlkeatngwv rnlsndsyag
       61 dysrrpptey vvlsylpdgt ilytgpnasm pdakklyidd epatiksvgd setkwravai
      121 kqngtvtiva kdltretiml rglaivqiii tavvmgiiav vgmwfirral rplrvvekta
      181 sqiaagdldk rvpdwplhte vgqlsaalni mlgqlqrsvv qaqekeeqmr rfvgdashel
      241 rtpltslrgy telyrsgatq dvdmvfskid deskrmsllv edllaltrae gsrldmgtvd
      301 mlelvlsags saraafpgrq idvvneaadi plvtgdpdrl hqvllnlvsn alrhggeeak
      361 vkltireeag ekgtdvlidv addgkgmape dashiferfy radtsrtrdt ggsglglaiv
      421 kslveqhggr isvesalgeg stftlrlpal aa
//
LOCUS       WP_284806759             402 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Corynebacterium striatum].
ACCESSION   WP_284806759
VERSION     WP_284806759.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..402
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43197
     Region          1..396
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 mvnilgiflf algigitval heaghmfsar afgmrvrrfy igfgpkiaaf trghteygla
       61 afpvggfcdi agmtaqddfl teeeepyamy kkpawqrviv mvggiavnll lgfiilllia
      121 mttglpnpda dvrprvgevv csadqnlqge lekcqgkgpa geagvevgdi vlaidgkple
      181 nftqlreevm arpgetvqlr verdgavqnf dvtldkvkrl ngegklvdag siglsnqvid
      241 ivekhdfiga fpatarytty vldatvggii qfpakipgvv asifgherdv ngpmsvvgas
      301 rvggelvars lwstffmmla tlnfflalfn liplppfdgg hiavifyeki rdgirrllgk
      361 epkgpadyta lmpvtyviaa llmtvgalvi vadvvnpirl fg
//
LOCUS       WP_284806771             398 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium amycolatum].
ACCESSION   WP_284806771
VERSION     WP_284806771.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..398
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=43698
     Region          3..359
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mnsakssyvp eltsiraiga fgvllthaaf wtghytddww grlngrfeig vtiffvlsaf
       61 lltgrwlgsp ddvpanrpdl rkyftsrakr vlpaywivvt aaflihaadd pppsggglqg
      121 wlrsmsftqt lqfgwihpgl pqmwsmvvev gfylvlplvg lgiwtitkgr lrpgptlaii
      181 igfgligpvw tvlshqeell pvvarlwpma yfdwfaigml laygrkvgwr vnlaaswlia
      241 lvlfflsttt hvgpatlvpd dvdqalwktt lyglsagafv apialgtevr wlrhpamiwl
      301 gevsyefffv hvlvmdwvmt lmgyqtfqgs mlavaivtaa falplswllr ritdvltrrp
      361 gpaspwatyr sssssgpssa tstscatfia dsaagapq
//
LOCUS       WP_284806821             935 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Corynebacterium
            striatum].
ACCESSION   WP_284806821
VERSION     WP_284806821.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..935
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..935
                     /product="class I SAM-dependent DNA methyltransferase"
                     /calculated_mol_wt=104873
     Region          98..933
                     /region_name="YeeA"
                     /note="Type II restriction/modification system,
                     endonuclease and methylase domains [Defense mechanisms];
                     COG1002"
                     /db_xref="CDD:440626"
ORIGIN      
        1 maemthaqrv saardfaerw kdrgaeksdt qqfwidlcsn vlgmedqtta lhfesrttga
       61 gwidvvvpda ktfieqkslg idmdkpeprq gsmvtpyqqa kryadqqrns krpdyivicn
      121 fdefrihnld ddfpeteyes fkleelpeql hlldflvdpq aqrarreqka slqageligk
      181 lykllreqyv dpdsaasqha lnvlcvrlvf clfaedagif pknavlnyla pvnapamrla
      241 lkrlfkqldt pmdlrdpyde qalavipyvn gglftdadie ipnftdeire lliselsadt
      301 dwsqisptif ggvfestlnp etrhaggmhy tspenihkvi dplflnaltd elasiinepg
      361 vgavkrrnnl kryhdklagl tffdpacgsg nfltetyisl rrlenkvlse landqtaldf
      421 ggessqlqvh isqfygiein dfavsvaqta lwiaklqada eteiltsani dnlplrdsan
      481 imlgnalqld wadilepdqc sfvignppfl garnqskeqk adlqaafksi gatknlgnid
      541 yvggwyakaa eylgdndira afvstnsicq geqvanvwsp lwdmgiridf ahdtfkwtng
      601 aadqaavfcv ivgfsklggp ktlfhyptvt gepeishpkq lnaylkdape vfvwnrskpl
      661 sdvpimgigs qpiddgnylf taeekaefla aepkaapffh rwygsrefiq gverwvmwvg
      721 datpaqlqsl prvrerveav rgyrlksrrs qtlkaaetpq rfgtqiiats nsllipevss
      781 qrrnyipigf itpenfcsnk vklvseatry hfavlhsrlh nawmrvvgvr lksdysysag
      841 vvynnfiwpd vtpeqeaeia qlgqavlear aqypdstiaq mydpdndwmy peltkahaal
      901 daaveraygl epgceektiv ehlfelysqa ikkas
//
LOCUS       WP_284806834             117 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter, partial [Corynebacterium amycolatum].
ACCESSION   WP_284806834
VERSION     WP_284806834.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..>117
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          4..106
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mkqwfllaga ittevaatls lkaalnhpsw yivvaagyig afvfltfclr egmqigvayg
       61 iwgasgvvla avlsaaifge pltavmglgm vliisgvltv elgsqkaqqt aaqeagv
//
LOCUS       WP_284806946             123 aa            linear   BCT 25-DEC-2024
DEFINITION  Rieske (2Fe-2S) protein [Corynebacterium striatum].
ACCESSION   WP_284806946
VERSION     WP_284806946.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..123
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=12706
     Region          34..118
                     /region_name="NirD"
                     /note="Ferredoxin subunit of nitrite reductase or a
                     ring-hydroxylating dioxygenase [Inorganic ion transport
                     and metabolism, Secondary metabolites biosynthesis,
                     transport and catabolism]; COG2146"
                     /db_xref="CDD:441749"
ORIGIN      
        1 mntcsrrmfl lgtattfaga ylaacgkeps aeiaateipv gsavmvdkvi faqptegefk
       61 aysqtcphqg slitkidgmt atctshftsy nltdgsvidg pgtkplteyg vesdgttvkn
      121 vsa
//
LOCUS       WP_284806950             259 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Corynebacterium striatum].
ACCESSION   WP_284806950
VERSION     WP_284806950.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..259
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27241
     Region          8..241
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mpipvelppt ftraldhapl igawicsgsq vaaeivasag fdwllidgeh spysletiae
       61 llratdvygp trmvrvpvnd talikqyldv gaqnlmvpmv dtaaeaekav aamyypprgv
      121 rgvgsalars srwngvegyl qkaaetvslt vqiesftave naaeiaavdg vdqvfvgpsd
      181 laasmgllgq qthpdvldav qrtfdavraa dkpvgvnafn leqaqrylda gasfalvgad
      241 vqllsgaart ladkfskkg
//
LOCUS       WP_284807199             343 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            amycolatum].
ACCESSION   WP_284807199
VERSION     WP_284807199.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..343
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37616
     Region          18..338
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtvhaareld anvsvdella vvpyfsqhrs mteaatelai pfariraive qiadidqpgl
       61 lgvrafevdy rnsfdvrirp qatvlsqpra ltaeetatll liletiedsa attsseaaqt
      121 aatklrsalg invpiidsta aengkafsfs eqiysalhqr kvlkvryrna sgqitvreld
      181 cvnvytvest tylravdraq edrrqksfrv drleaaevld tpsgfhrpep vdirdphafg
      241 aetgtsewas vlidadatwi adyepvffte degeeedtel vsdqglgqse fvadvpmsdl
      301 aatvsfvlrr spsvtvaepl klknavvara realaeygrn dka
//
LOCUS       WP_284807238             289 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium sp. MSK218].
ACCESSION   WP_284807238
VERSION     WP_284807238.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 289)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..289
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=30467
     Region          123..283
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mpssssrpts dskksalsti spvawgllvi vvvlaiiigf llaertsssn estsaaqkta
       61 tsaapaedla kdadkatpgt kfsdgkgdpm tfgpggdtks gditvvhrkk eddpfaigav
      121 dapvvisefs dfecpfcsrh anvtepdilt kyvekglvri ewndfpvngp aaieaakagr
      181 aaaaqgkfae fkhelytask disghpefdi ddfmtfakqa gvadldkfrq qatddtytev
      241 ietatryasq igitgtpafv vgdqfvggaq ppevfeqiiq eqlgkaang
//
LOCUS       WP_284807373             392 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Corynebacterium
            amycolatum].
ACCESSION   WP_284807373
VERSION     WP_284807373.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..392
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41519
     Region          12..391
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mtnadankpn eriflslatv teaeeqavvr alhsgwvapl gpevdafeae iakrcgveha
       61 lalssgtagl hlallalgig egdyipvstm tfaattnaia yvgatpvfvd aaedgnidpe
      121 lllrtvdell tegksvpavm ivdlfgrcad ypafaprlee lgialiedaa ealgasvdgq
      181 pagsfgraaa lsfngnkimt tsgggmllsd dadliarary lstqarqpva wyehteigyn
      241 yrlsnllaal graqhsrldg miarrrqird ayidllasld ddapgkgtrl lsdsderfte
      301 ncwltsivlp qeavdkgvlt pdsviaalge asiearhlwk pmhlqpvyeg arasingtae
      361 nlfsrgitlp sgpalddddv arvigvlkev lg
//
LOCUS       WP_284807412             302 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Corynebacterium sp. MSK218].
ACCESSION   WP_284807412
VERSION     WP_284807412.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..302
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31804
     Region          5..279
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mtnplailcv igscislqlg aslaiqlfph agtwgtasmr llmasailll iarpkvhtwd
       61 rekwisaalf gvslglmngf fyagievvpl gpavtiefvg plllaavlsr slrdatcvtl
      121 aligmallgv dsltgeplsp rgvvflvlag acwaayilas kkagalfsgq dglavalfig
      181 gltllplggr galvlvsdpw llfvalgtgv laslipytle fialkrlapn vfsilialep
      241 vfaaffgwll lsqgvtalkl taialvvlas vvqtmvparg riifrtialr prapwrfrrp
      301 rn
//
LOCUS       WP_284807420             518 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium amycolatum].
ACCESSION   WP_284807420
VERSION     WP_284807420.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..518
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55361
     Region          156..500
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mlrrrrstgg gvqsnqrsat evnpgqgtvg kqeksantet mageslpglp rssripslrw
       61 rltiltaliv amsvglmtla afftvqaaly revdsnlrsq aekllmspya sefaigpsfe
      121 adsnrilnpd ldavyfahgs vagkgggsis iggpelavlr gnrqesirtd eyngrrvyav
      181 rsedgatlil sqdlsstqsv lkalsavlls isaigilfai gsgitvattg lrpvtrlria
      241 aervtetdel rpipvegdde larftrsfne mlaalqasri kqaelvadag helktpltsl
      301 rtniellmma srsgaaisde dcadleadvi aqleelstlv gdlvdlared gpqqviehvd
      361 vdeiistsla rverrrpdit fdvqtapwyv ygdsaglgra vlnlmdnaak wspengtvrv
      421 rltplsevva eftvadsgpg ipkedrdkvf erfyrsiqsr smpgsglgla ivksvivrhg
      481 gtitadesdd ggalmrvtlp gsphsgkgdd sdsaqeps
//
LOCUS       WP_284807493             196 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Corynebacterium sp. MSK218].
ACCESSION   WP_284807493
VERSION     WP_284807493.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..196
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=20718
     Region          1..191
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mrlvlasqsp srlsilrgag vepviapadv deraieerla gaepaeivca latakaeais
       61 pnypedvvvg gdsmllldgs lqgkphtpea tverwhaqag rtaelitghc vlhgekrfve
      121 asrttvhfae assadieaya rtgeplecag aftlealggw fidriegdps sviglslpvl
      181 rralysfgln vsdfwa
//
LOCUS       WP_284807878             187 aa            linear   BCT 25-DEC-2024
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Corynebacterium sp.
            MSK218].
ACCESSION   WP_284807878
VERSION     WP_284807878.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..187
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20761
     Region          4..182
                     /region_name="YdeN"
                     /note="Predicted esterase of the alpha/beta hydrolase fold
                     [General function prediction only]; COG3545"
                     /db_xref="CDD:442766"
ORIGIN      
        1 mhfyivhgyq aspdshwfpw lerqltaegh tvhtlalpdp napkldewve tirkdigrpd
       61 adtciithsl ggiallhylt alegecelag lfivsgfvek lrviseldef igqahvdvpa
      121 ikphiahtev fvstndilvd pvltqqlada lsatpitihd aghflesdgy tefpqleerl
      181 tqwlrgl
//
LOCUS       WP_284807964             332 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium sp.
            MSK218].
ACCESSION   WP_284807964
VERSION     WP_284807964.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..332
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35857
     Region          67..327
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mpssadraat rapardmaie rltnltfalh gaahqggvpd rsaswirshv egyqdksdda
       61 fskllsrdir tlqragvpvv hssgaegply rlnpedyqlp pvdftpeeam vlgvaggigt
      121 pgglsdfsls awtkiaasga srdlsgapvy tavndmtkls pelvkavlta vragvrisfd
      181 yyatpasepv rrvmdpwglv nhrdrvylvg wdadreaprt fratriddvr rsrqeathle
      241 qsaplqdlvv aalqrgetvt avlevpqgqa aelvdagtrr sdgrvelcdv drdwlirtaa
      301 gyapdvvvle pedvrsdila llrsaseeea hg
//
LOCUS       WP_284807965             321 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium sp.
            MSK218].
ACCESSION   WP_284807965
VERSION     WP_284807965.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..321
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35694
     Region          9..316
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 madqsrklqa lvrslnlipy lrnhpglspm eaaedlgmtp velkdaidrl fcsgvgrnte
       61 dlidlsfsyr dgieiyndqg ltqalrltpt eagallltle sleampglvd vsavhsaask
      121 lraimddkta aiydslattd peesevqaal agavdkrqqv rftywsmssn rttertvhpa
      181 rifivdgepy laawdetage hrtfrldrmh nvevldvaat phlreldfnp dspfgldhtl
      241 taqieihqef twlaehydit lgeelgngli aatmpvgsed wfsrfalgqg drlrvvgpek
      301 lvetisqhrk raverytqhp d
//
LOCUS       WP_284807969             360 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium sp. MSK218].
ACCESSION   WP_284807969
VERSION     WP_284807969.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..360
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=38550
     Region          10..359
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mtdyasrlsr areavaahgi dvallgtgae fayltgswvs sherltclvi rpdsepviva
       61 pstdieslqg vdaalrgwkd gedpyalale glsarhvalg stltadhvlr fqaalndasy
      121 vlatnalsel ftrkdadeid elrtaaraid avhievprll qpgrteaeva edlrqlilre
      181 hsavdfiivg sganganphy dygdrvlsag dpivvdiggt lpsgyhsdct rtyvvggdva
      241 aapaefreay avlekaqaag raaarpgvsa qdidrvtrqv ieeagwgehf thrtghgigl
      301 stheepfime gneltlaesm afsiepgiyv pgqwgmrled ivvttadgye slnqaprelr
//
LOCUS       WP_284807988             200 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Corynebacterium sp.
            MSK218].
ACCESSION   WP_284807988
VERSION     WP_284807988.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..200
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21760
     Region          36..146
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mptwkevtaa npahshnfar kwktlraqgk didgearlid amverssrvl dagcgsgrlg
       61 gelakrghtv vgvdvdpili ehaehdypea rwevgdlsed eipegdfdia vaagnvmtfi
      121 apegreatlr nvfdalrpgg rfvvgfgegr gwgfeeflal aravgyrvdf tfsswdmkvf
      181 kdnstflvav ltrpgadllg
//
LOCUS       WP_284808032             300 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Corynebacterium sp. MSK218].
ACCESSION   WP_284808032
VERSION     WP_284808032.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..300
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=32078
     Region          1..287
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mqrilalill lcqggitvsg sivrvtgsgl gcvtwpnchp gslvplkgaa plvhqviefg
       61 nrlltfvvaa aavativamy kakrrkelkv yawlglfgiv vqaligalsv ilklswwsva
      121 ihflpsmvlv wiaallysri aepdegiptr lfpaairtla vvaaialslv lltgtfvtgs
      181 gthsgdagvg megrlgvdty gmavihaicm yvylaltlvv vfllhrsdap taakkagwvl
      241 ivcilvqwai gvlqfylhip rwtvpfhvgm ssvvtaftal lwahgqrril keeqpsasvq
//
LOCUS       WP_284808060             267 aa            linear   BCT 25-DEC-2024
DEFINITION  inositol monophosphatase family protein [Corynebacterium sp.
            MSK218].
ACCESSION   WP_284808060
VERSION     WP_284808060.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..267
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=27779
     Region          13..261
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mapmrglsss dprelvafae asvdqvtdlf raglgaepar fkgesdfate idlrieehlr
       61 vtlsqltgip vygeesggal edtvwvvdpv dgtanysagn pccgvlvsll heakpvvava
      121 dfpllerrvv aaegmplrts ggpstgfggg egaqgfdear ghvgcsshlp idlfndlret
      181 glrprmtgsv gldnafvaqg vfdgavnfsp hpwdnaagal mikaaggrvs dpdgnewtat
      241 skgfvggtpq vhatildaia rnprgqr
//
LOCUS       WP_284808087             553 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Corynebacterium sp. MSK218].
ACCESSION   WP_284808087
VERSION     WP_284808087.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 553)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 553)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 553)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 553)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..553
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58981
     Region          72..550
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mstttrspqr tfgiyavllv llvlvaaplv svlisavvgy rdepsslhki vepgmgevll
       61 ntvvlsllvv vfstlfaapl aflrawtpfs kanwieiaim ipfmtppfaa amawmdftrr
      121 ggvsellfgh tvgklahdai ysvpgmafim acelfpflyl ilrncltsip asslemaqva
      181 gasrwqqisr iilptvvgpy slgaliifik aagefgtpvt lgnaigftvl vssiyqdvti
      241 dplsfsdaaa sssvlfalgv gawafqqwvs rrdltsggrv srqvslriga vgkalggavt
      301 fliiacsvli pyisitlaam tilrsapptp qnltfdyfai vlqmpsaqea llrsialgav
      361 gattavilgi avtlltqrtk qvsarvtdfl avapdtvpgi vlaigfillw napwlpwtpy
      421 gsmiilvmaf tvlflpmavq niktsagavs psvyeaaavs gasaphklrs itlpllapgi
      481 fagwllaffv gfrelvmssl irpsqlnlla pwimnqfdqg hraeamamtl igvgtstvvl
      541 vlitwwqgrr arg
//
LOCUS       WP_284808263             392 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Corynebacterium sp. MSK218].
ACCESSION   WP_284808263
VERSION     WP_284808263.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..392
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41275
     Region          16..386
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 msledwafss naswcergle rtervisgsq sprtvvdgre tllagssdyl glganralad
       61 aaheatlrag vgsggsrltt gtsdyhvale relagfvgap valvfgsgyh anmgvipala
      121 aaardcgerl sifsdadnha siidgirlak ssyqgvrssv yphldvktle eqlaadaser
      181 rlivsdgvfs msgelanlha lqelardyna wlmiddahgi gtlgrngrgv cehfdlplpd
      241 iyigtaskal gaagafvags eplielfrqr crsyifstsm ppsqaatisa alalvpshvs
      301 rlahvvhnlr qrlrangwkv vdspapiivl pvgaedaame caaqaaergv ivspirypsv
      361 slgqallrlt ahadyseedi alivdavgpa pq
//
LOCUS       WP_284808327             204 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium sp. MSK218].
ACCESSION   WP_284808327
VERSION     WP_284808327.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..204
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21689
     Region          6..201
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(143,147,150..151,153..154,189,192..193,195..200,203)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(164..171,181,184)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mpkniplgfy vdadttihri paavkfltli afilvtslav ktvawaalsl aiplvlfpva
       61 hiplrvavgq lapplyllva laafqwwqkd ltsaaimflt vyaaviaavl ltlttkvsem
      121 mdsfdralap lgklgvpven itlamsltir llplmlgtvl evldarkarg atasltafgt
      181 pviirslrra ramgealhar gvgd
//
LOCUS       WP_284808342             266 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium sp. MSK218].
ACCESSION   WP_284808342
VERSION     WP_284808342.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..266
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27933
     Region          12..266
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mdldfssaft ertprvvnaa klhraanrrk adrfiiegen avdaavstga atdvfvteka
       61 aerfahivtt csymdvyvhp itdkaakhls dtatstglfa vcrpvlwtag kilagkpklv
      121 svpvltsepg nagtlirtsd amgadgvifa gdtvdplgck varasagslf hipvardpni
      181 kdvlgklrss gmqvlataad gevdladadl sqptawlfgn eahglgdlkd eadmrvripi
      241 lgraeslnla taasiclyes akqqsn
//
LOCUS       WP_284808569             402 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Corynebacterium accolens].
ACCESSION   WP_284808569
VERSION     WP_284808569.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..402
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43723
     Region          1..396
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 manllgivff algigltval heaghmftar afgmrvrryf igfgprvfsf rkghteygla
       61 afpvggfcdi agmtaqdefl teeekpyamy kkpwwqriiv laggigvnli lgfvilyfva
      121 mtaglpnpda dvrprvgevt ctadqkenqe lesctgngpa gkagvqegdi ilaldgehld
      181 sftqlrdevm qrpgetvtlt verggeekdf sieletvkrl nqqgelvdag siglsnevld
      241 ivekysatqa lpatwhftsy sleatvegik qfpakvpgvv asifgherdv ngpmsvvgas
      301 rvggelvers lwasffmmla tlnfflalfn liplppfdgg hiavilyeki rdgirklmgk
      361 qplgpadytr lmpityvmaa llmglgvvii iadvvnpirl fg
//
LOCUS       WP_284808605             482 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium sp. MSK218].
ACCESSION   WP_284808605
VERSION     WP_284808605.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..482
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52325
     Region          175..480
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 msdtttnnqa pvsgatrvse ktqrrriqrp kalplrtwll vlmvlvsgig lamsslavss
       61 imrnvlytrv dtelndalhs wasnldetfy tqdrsrrppt dyvaiayypn gsvvstgpms
      121 aipdvrdvyv ggepmsvast egdtewrava avkpdgsvvv vakdmttens ilkglaivqv
      181 iiaavvmlii aivgmwfihr alrplrvvek tasqiaagnl dkrvpewplh tevgqlaaal
      241 nvmlgqlqns vvdaqekeqq mrrfvgdash elrtpltslr gytelyrsga tqdaefvfsk
      301 idaeskrmsl lvedllsltr aegnrldlrq vdmlelvlsv gssaraafag rtinvnneat
      361 dipivdgdpd rlhqvllnlv sngirhgged aavtltlrdd eehvlidvsd dgkgispeda
      421 shiferfyra dtsrtrdtgg sglglaivks lveqhggsis veselgrgsv ftvclpkakq
      481 ad
//
LOCUS       WP_284808650             847 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium accolens].
ACCESSION   WP_284808650
VERSION     WP_284808650.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 847)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..847
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=94796
     Region          19..841
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mnlsqqlpdl tevpeslide aiwdtfnswt tskgidlyra qeeaslgila gdnvilatpt
       61 gsgksmvana ahfialargq rsfytapika lvsekffalc eifgaenvgm mtgdatvngn
      121 apiiaataei vanialrdga eanidqvvmd efhyysdpdr gwawqvplle lpkaqfllms
      181 atlgdtdwlq edltrrtgre tnlvagstrp vpldfsyvfs avhetieell adnkapiyvv
      241 hfsqreaaer aqaltslsgi inkeekkdia eeiggfrftt afgkdlskll rkgigihhag
      301 mlpkyrrlve rlaqrgllkv icgtdtlgvg invpirtvlm tglakfdgqr qrilksrefh
      361 qiagragrag ydtegtvvve apeheienak arrrigddpk rlkklkkksa regevswsek
      421 tfarlteaep eqltsqfrvs nsmllnvlar hgdgyahmrh llrdnhdprs kqnkdiltal
      481 dlfrglvdsg vvqkstkgld iygrpyhlvr elprdfalnq plgpfalaal slldpeadsy
      541 hldvisvfea ilddprqvlq aqqkkrrgee iaalkadgvd ytdrmnived itwpkpledl
      601 leqaydtfae tnawvkefel rpksvvrdmv enamtfsdlv atyglarseg vilryltdaw
      661 rtlkqsipde yttpqiedii vwlgelirqv dsslvdewaq magedspidq dtldrelafg
      721 vedptaltan rrafgimvrn ymfrlaqlfa leeedrlaev ldyldevpdf gavlddyfge
      781 yddidtgpea rgpeyfrlee sssrswpvrq iikdpagdra yqfvatvdld asdeagevrl
      841 selrvey
//
LOCUS       WP_284808664             699 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Corynebacterium sp. MSK218].
ACCESSION   WP_284808664
VERSION     WP_284808664.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..699
                     /product="PhoX family protein"
                     /calculated_mol_wt=76143
     Region          46..693
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 malhgrnllt nmftssrssl tctykcgnac fgecentsdn pyfgdqfsrr talragglav
       61 vavggssala acaapgeeds aagssaagkt sevkeseiel tsaegmhfek vepntkdevv
      121 ipkgyeqsvl iawgdpvieg apefdvnnqt aeaaekqfgf nndfaglieh pddknrliym
      181 csheyttepm mfpdydpenp teeqvkigwa ghghtilevs kvgdtgelkr efgplnrrit
      241 attpftlvgp akgsdfvkts adqkgekvlg tlnncsggvt pwntmlsgee nfdqyfaggd
      301 vkdekaaesl krfgikegps drkwekyddr fdvtkepnep nrfgwlvein pldpestpvk
      361 htavgrykhe agnihitkdg tvvcysgdds rfeyiykfvs skkykegdlk hnmsildhgt
      421 lyvakmegns pekeidgsgv lpedgafdgs gewvklltsd tendkyeshv dgmsaeevai
      481 ftreaadkvg atkmdrpedv eispandkvy valtnnkyrg atgenakknq edpmeyapvk
      541 enknglvmei eddhagekft wnlllvcgdp keantyfggf dkekvspisc pdnlafdshg
      601 nlwistdgna ldsndglyav tvdgetrgel kcfltvpaga etcgpivddd rvmvnvqhpg
      661 eaddatfena tshwpdggns tprpavvvvw kkdgkigsk
//
LOCUS       WP_284808788             391 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium sp. MSK218].
ACCESSION   WP_284808788
VERSION     WP_284808788.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..391
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=42195
     Region          1..350
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mrflpelegv ralaamavvv thvsfqtstg wawaerldyg vavffvlsgf llwrrrhaht
       61 trqyvlsrva rlaplylvcv vavlallpda spltlpqllt nltgtqlyia dglvpgltql
      121 wslsvefafy avlpllawml dkfsarprva liagagvlsl fwgflpfvag yesgdvntqi
      181 wppayfswfa vgmlaaeaes agvrvragri vravcwavaa gcvwlasrew fgpqglvhpa
      241 pdefarriav gavcgacivv pvalapresw lssewmralg rwsygvfmwh vavlaiafpl
      301 lgvsafsgsa wdfavvlvft vvvscvlsaa tytlvevpgr dlirslasgr iavprslprq
      361 adspansars aepyaagwvp saccgvggrr r
//
LOCUS       WP_284808831             586 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Corynebacterium
            sp. MSK218].
ACCESSION   WP_284808831
VERSION     WP_284808831.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..586
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=63358
     Region          6..215
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 msavtnfvyr qithvgravt vaqglkmrls gvenipdegg avivcnhtgy mdflfgayla
       61 yqkkrlvryl akasvfkapv vgrlfemmgh vpvdridgga sivkgtelak sgelvgvfae
      121 gtisrsfeir smrngaaria haagvpiipq ivfgsqrlwt kgqkkhlgrt ntpilitale
      181 pyyttgdpda diaevrrrmq ealeelwkqy esefgpmpag eywvparkgg gaptleeaea
      241 qdavvedery rvrrlrddlt hlkdhvsaat ielvrdrmtl kktaapedda vladvpsdat
      301 pdnttdsnad sttesttadq akerprtape tlewikenln svveeatrgl eegrdkvtev
      361 maqlksdvae aqasmtasgk eifagsvveq glltaatqsr livsrlphri kaeysavpri
      421 vvadqsamsm eggevskrlq ealaqlhpqv eelviisqqg tvldaaaved ipqnvwriac
      481 aegaedvqfn dapggpvata sspaeglaav vkkigaepkd lllfanepgd etfaegdedv
      541 avhmvaleta pievvkaaqa vtysaerfgm aevleamarl qkskkk
//
LOCUS       WP_284808916             622 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Corynebacterium accolens].
ACCESSION   WP_284808916
VERSION     WP_284808916.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 622)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 622)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 622)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 622)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..622
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=67131
     Region          1..609
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mrqrlriilt cvvvatvalg grlawvqlvw gpdlaakavt qrervyidpa rrgeildrdg
       61 qrlaytmksr sltvsptrlr delkeqakme atsegklegm deskkdeylt kqmedklkem
      121 aeripkmied sgasaskvda sdiknklkad tqyevlvrnv dpdvaveisn kyhgvaadrq
      181 dirqypngai aenvvgkvsm dghgqfgfea ardteltgid gqstedvstd gqvipgtlrd
      241 vvdavdgrdv tltldldlqt yvqqklekak ansqaegaea vvldaatgqv lamantdtvd
      301 pnkniedqlk egkdfenrsi shpyepgsva kivtaaaalq egittpdevh qvpgsidmag
      361 vtvndawphg tepytttgif gkssnvgtlm iadklgpeky aeylkkfglg attgvelpne
      421 sagtvpdqeq wsggtfanlp igqgqawttl qmasvyqala nggeriepri ideikdpdge
      481 teklpepkkt qvvdketakt avdmfravfq dddagvqngt aanaqldgyq lsgktgtaqk
      541 vdpnsgaysn saywitfagi apaddprfvv avmldepksg vednggggqs aapifrdiss
      601 wllnrdnipt skpaprmtlr eq
//
LOCUS       WP_284808992             149 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Corynebacterium sp. MSK218].
ACCESSION   WP_284808992
VERSION     WP_284808992.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..149
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16340
     Region          46..>107
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 meslngkshe rsrslpgift eaqakvrdka karaqradti ghlgpeaiva fvdgempaky
       61 ahrvrvhlvh caecraeihh qrnasewvre csveshvkap eslmaklagi ahqgagpgpd
      121 aeepacqprq dfldkvemvm raikhnqrg
//
LOCUS       WP_284809214             270 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium sp. MSK218].
ACCESSION   WP_284809214
VERSION     WP_284809214.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..270
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29094
     Region          12..233
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mtehfstpsg narvaaffdl dktiiatssa yafgrefmhn glithtealq lslakasyml
       61 aghssehmda trdqlaamvv gwsvqkvhdi avetmhtvvt ptiyaeardl iaahrekghe
      121 vviisasasv lvrpiaeelg iehvvatela eedgrftgei lfyckgaaka ealkrmaqkl
      181 gvdkdtsyay sdsatdipml kqvghpvavn pdrllkkhaa dngwetrtfk dpvplftpps
      241 arefgigtav lagiaalivg gvlfarqrnk
//
LOCUS       WP_284809231             189 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Corynebacterium sp.
            MSK218].
ACCESSION   WP_284809231
VERSION     WP_284809231.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..189
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20119
     Region          <82..189
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 msqysrwpgy vkasivavim laalalvgvv nllendepev avpqsqeadv aprpkcpegp
       61 iagvdlpclg asstaaakni qivtvwawwc epcrtelpff qdiarshstw nvvgvhadpn
      121 aangaalldd lgvdipsyqd ekgtfagels lpgvipitlv vrdgqvvekf vkpftsaeel
      181 eeaidevlk
//
LOCUS       WP_284809229             225 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium sp. MSK218].
ACCESSION   WP_284809229
VERSION     WP_284809229.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..225
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=24937
     Region          39..193
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 msrlhparap ewlrpalgvd travqerlir hvrpakrrre savlvllkge sfedgevllt
       61 hrspslrshs gqiafpggrk degdaslvda alreaeeetg ldrstvtple qwgkldirat
      121 gntvspvlay whtpgtvwpa spaetddvft vplreladpa nrimvghsrw kgpafrsrgy
      181 lvwgftagvl sglmdhagws vewdknkvhd lresltrsln nekmg
//
LOCUS       WP_284809263             428 aa            linear   BCT 25-DEC-2024
DEFINITION  Mur ligase family protein [Corynebacterium sp. MSK218].
ACCESSION   WP_284809263
VERSION     WP_284809263.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13558984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..428
                     /product="Mur ligase family protein"
                     /calculated_mol_wt=45278
     Region          64..262
                     /region_name="Mur_ligase_M"
                     /note="Mur ligase middle domain; pfam08245"
                     /db_xref="CDD:462409"
     Region          312..410
                     /region_name="MurT_C"
                     /note="MurT ligase C-terminal; pfam08353"
                     /db_xref="CDD:462442"
ORIGIN      
        1 mnfnfrnals sartavatta aslattasra tgrgaggmig gliagaidpt imqnlakkrp
       61 avlvtgtngk stttrmlaaa vraehsvatn dggdnmdagi isallagkea shlvlevdel
      121 hvphvadnld ptalvllnls rdqldrvgei nkieralrga veahpdmlvi ancddvlmts
      181 vaydaknviw vsagagwmge svtcprtggh ivrdgedwha vkqladgref rrptptwavt
      241 eeglvspegv dklrlslpgr anrgnaaqav aaaveafgvd rhkaiaaaeg vddvagryst
      301 itlgkrtirl llaknpagwq ealsmvdrda dglviatngh vadgidmswl wdvrfedfed
      361 ipvkasgerg tdlavrlvya disheliddp ltaiqscpeg hievlanyta frdlkkalta
      421 avkehsnd
//
LOCUS       WP_284809420             165 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium accolens].
ACCESSION   WP_284809420
VERSION     WP_284809420.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 165)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..165
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17707
     Region          86..161
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdslesriah learvtklen papdpvessa gestmwlada lepsdqlpeg svifggnitt
       61 glgsyvyqwq rptntvtagd wsdnldrlaa lahpvrgeil rrllsapata telveeeivt
      121 stgtayhhls altsggwttk thgqysiraa rviplltiit aseyh
//
LOCUS       WP_284809468             402 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Corynebacterium sp. MSK218].
ACCESSION   WP_284809468
VERSION     WP_284809468.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..402
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43026
     Region          1..396
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 manvlgiilf algigitval heaghmltar afgmrvrrff igfgptvasf srghteygla
       61 afpvggfcdi agmtaqdefl teeeephamy kkpwwqriiv laggitvnll lgfiilliia
      121 mttglpnpda dvrprvgevs ctsdqkadge lepcqglgpa geagvepgdi vlalngeavd
      181 sfaqlrdtvl qhpgetvtle verdgsprsf dialdtvtrl naegelvsvg aigmtnqlid
      241 ivetysfvea fpatarytgf vldatvqgia qfpakipgvv asifgqerdv ngpmsvvgas
      301 rvggelvers lwssffmmla slnfflalfn liplppfdgg hiavilyekl rdgirrlmgk
      361 epkgpadytr lmpityvlaf llmavgalii vadvvnpvrl fg
//
LOCUS       WP_284809607             280 aa            linear   BCT 25-DEC-2024
DEFINITION  trypsin-like serine peptidase [Corynebacterium sp. MSK218].
ACCESSION   WP_284809607
VERSION     WP_284809607.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..280
                     /product="trypsin-like serine peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=29726
     Region          70..216
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mnivklfsfs lacvftvlgf cpvvavaadn dfaslrasst vpvndnriaa vwsvapsldd
       61 sqqqrvrrdc tasyagdnfw ltahhcvsds pfmdgflrqs dgevagiaam ytksstedia
      121 likvgdgina dsftlateal kigdqailtg ygqphdyass astvisekvd slnfgnvtyt
      181 dllkgksstp srscggdsga pvykdntlya ihtaggfnpe ctdgqdrpmw htnlppranw
      241 vhetinsnag lspqekvkae nglkyapaaa pppvapyirp
//
LOCUS       WP_284809663             471 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Corynebacterium accolens].
ACCESSION   WP_284809663
VERSION     WP_284809663.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..471
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50138
     Region          3..465
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mdkqphaviv gagpngltaa arlatagwrv dvyerashpg gaaassteif pgtivdlgaa
       61 ghpfgiaspa frslnleshg lrwrharypm ahplegapag ilhnsleeta aglgtdaraw
      121 trlhghvvrn idahltnalt plvhwpehpv rlaqfgvpgl lpasalaraa ftspqaralf
      181 agsavhaits ptraftsafg llfdalgmtr gwpvveggtq aladalvsll rshnariytg
      241 aditdvrslp radalilnlt prqilrlggl dlpartrrnl rrwrygsavy kvdfhlsepv
      301 pwadprvgqa gtvhvggsve eiggaerdig krrmpvnplv mvcqqyvadp srglvlwtya
      361 hvphgyeery prevtgliar qierfapgfr dtilvtrats padlerwnpn lvggdiagga
      421 mtglqtvlrp rlsahphrla pgifmasgst apgagvhgmp gwwaagdvat p
//
LOCUS       WP_284809709             417 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium sp. MSK218].
ACCESSION   WP_284809709
VERSION     WP_284809709.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..417
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44458
     Region          158..397
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mnsfiqsvlg lpltdsvngg iyiailvisa lliawrlrkr dfvsfllaav iavvayfalk
       61 hwevpfylfv aglvpiaali slihhsgrrm lmtviaafst lavaglvnme yqsypdigsl
      121 nptpvaqemd yaqfkglkss dsaaivhldl pgttsgftar qatayippay wssperslpv
      181 lvllhgnpgg peqwfgsgea aetadafqrv nggvspivva vdatgsetan picadssvak
      241 vmtylttdvp tgiksafrvd enqqhwtvag lsyggtcslq iltnhpdafg navdisgqae
      301 ptigkhadtv akfyggdeaa yqaanpahll atkkypdlqv ifiagnrdta avkalsqlsd
      361 aargagmrtf yttrpgghsf dvwrpalret fawiarqggm kdvndpfdgv qdadlqh
//
LOCUS       WP_284809867             448 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Corynebacterium sp.
            MSK218].
ACCESSION   WP_284809867
VERSION     WP_284809867.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..448
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49916
     Region          2..443
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mmesskvivi gagfsglvaa relqtagvnc evfeardrig grawtddrmg lplemgatwv
       61 hwfqpymwge itrynqgiht spadndaywv tqgkvrkake geadekmmpa ldviyegsdr
      121 ffpnphdpla ilrdeygadp ndveafkqfd hksvmdivne agvdqelqdm vegfwsaayi
      181 gdprtgsslm akqwaalsdh shklvdeinl rfkldngmrg lyenirddlr cpvhlsspvt
      241 kveqtdsgvr vtletgevke ankvistvpl galtniefdp plsgdqqrvi gdkwnstgak
      301 iwikikghhk iiayagadyp mslirseyfm ddgttvlvgf gadhskvdln siedaqrimd
      361 twdlgvevid stghdwvkdk wtqqvwatlr kgqfidgwsh fidsesdihf agadfapgwr
      421 gvivdgaiqs giitarrvis qlreigkl
//
LOCUS       WP_284810002             514 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Corynebacterium
            accolens].
ACCESSION   WP_284810002
VERSION     WP_284810002.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..514
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=54794
     Region          1..472
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 masfldalns iiwspalvfl clgagvyftv vtrglqvrcl pdmlrqiskg eksddgvssf
       61 qslmvslsgr vgvgniagvs taiafggpga vfwmwavall gsstsfiect laqiykekdq
      121 dtgeyrggpa yyiekaykht kaapfmmvyg ilfaiamila tsyflpgiqa navaaaadta
      181 wginstwaav vlagilaiii iggvkrianf atlvvpfmav iyigisivvm linysqipev
      241 fglifksafn leagfsgmlg vaimwgvkrg iysneagqgt gpqsaaaaev shpakqgfvq
      301 sfavyidtlf vcsatafmii stdmytvfrg esedgevvyq gslpddvavg pgfvqsglds
      361 vfagwgptfi avsiaffaft tvlayyymse vnltyfnrwv ksrpirrglv walriliivs
      421 vivgatttpg sawalgdigv gttawlniia ilflqvpalk vlkdyekqkk agkdpefdpe
      481 avgiknadfw vdrknaraaa qaaskqaage naes
//
LOCUS       WP_284809881             120 aa            linear   BCT 25-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Corynebacterium sp. MSK218].
ACCESSION   WP_284809881
VERSION     WP_284809881.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK218
  ORGANISM  Corynebacterium sp. MSK218
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Corynebacterium sp. MSK218"
                     /db_xref="taxon:3050218"
     Protein         1..120
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12538
     Region          3..120
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 miiisalavl vggflggcgr faltrilpsp tctfaanitg aalagvaygy aththapeff
       61 lpllaaglag glstwstmak elgemikakr wwrlarylfw tvglgialaw rgawvgslla
//
LOCUS       WP_284810004             399 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Corynebacterium accolens].
ACCESSION   WP_284810004
VERSION     WP_284810004.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..399
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44218
     Region          61..367
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mavqkrvtks gttrwvarir ddsrkersks fntrreakaw eervqseirq gewiapeiga
       61 vtvgrlarew adqpardntk anrealarnl gplkdmpink vrssdvsawh aelihgrswk
      121 sgktlsanta anlagmlsgl faravddkml rsapkftmrk sarsslqrad ilttkevetl
      181 ilragedhfn sparpwlatm iavaagsglr vselgglkve nvdflrgqih vrqqsnndgt
      241 elvalksdsa rrsvpvpdsv fevlerylhd fprepgqtvf yrvtdgverl hsknsagtal
      301 rrvqslhglr kksfhdfrhy yatvliagga pvnvvqsalg hanptttmet yvhfwpgsee
      361 ltreaasvgv dflrdhcgig arvrpdeaid qgvkvqfvg
//
LOCUS       WP_284810109             218 aa            linear   BCT 25-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Corynebacterium accolens].
ACCESSION   WP_284810109
VERSION     WP_284810109.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..218
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=24583
     Region          3..200
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mlicqemfll ltkdngkkev lsnnetalra glfsdlllhe avyiapknkv hatdkkpehp
       61 vlawawdslh ehrtssvktl lqarwfspre kiaqdfqdrg qleiedsaww qlggdryimt
      121 dtaledevre rlaavldgtq npstkdmiil dilrevngay pllkedapem krremrnrik
      181 elkqqveydd aaasavktil qettaiiaai avstagtt
//
LOCUS       WP_284810197             698 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Corynebacterium striatum].
ACCESSION   WP_284810197
VERSION     WP_284810197.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..698
                     /product="PhoX family protein"
                     /calculated_mol_wt=75716
     Region          46..692
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mallgknllp srftssrssl tctykcgnac lgecentsdn eyfgdqisrr talraggltv
       61 vavggsaala acspsstdsa assstaaggg ktsdtkvelt saqgmlfdav qpntkdevvi
      121 pagyeqsvli awgdpviega pkfdvnkqta adaekqfgfn ndfagliehp sddsrmvymc
      181 sheyttepmm fpnydadnpt eeqvkigwag hghtilevsk vegtgelkre fgplnrrita
      241 ttpfklvgpa kgsslvktka dpkgetvlgt lnncsggvtp wntmlsgeen fdqyfaagdi
      301 kdekakksle rfgikdketd rkwerfddrf dcskepnepn rfgwvveinp ldpkstpikh
      361 talgrfkhea gnihiaedgt vvcysgddsr feyiykfist kkfeegnleh nlsildhgtl
      421 yvavlegnsp aeeidgsgvl pedgkfdgkg kwvklltsdt ennkftshvd gfsaeevavf
      481 treaadkvga tkmdrpedvq vhpdshkvyv altnnsyrga tgenakkske dvkewapvke
      541 nkngmvmeie ddhageeftw nlflfcgdpk vantyfggfd kskvspiscp dnlafdnhgn
      601 lwistdgnal dsndglyavt tegetrgelk cfltvpagae tcgpivdddr vmvnvqhpge
      661 addatfeaat shwpdggkst prpavvvvwk kdgkigvn
//
LOCUS       WP_284810295             939 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium striatum].
ACCESSION   WP_284810295
VERSION     WP_284810295.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 939)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 939)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..939
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..939
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103903
     Region          2..937
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtsthldtfr drlshplddf qvegcravee ghgvlvcapt gagktivgef avslalsrgt
       61 rcfyttpika lsnqkyhdlv aahgadavgl ltgdvsinsq aeilvmttev lrnmiyaesg
      121 aldrlshvvm devhfladas rgavweevil nldesvsiig lsatvsnsee fgewlsavrg
      181 dttvivsdhr pvpldqwmmi grkiyplfep esggqvnael arrirrleag dsddgrndah
      241 sgqgfrarar hkggdrdsrn srggrgrsga srpqdryrpl grpetlqvlq gmdmlpaitf
      301 ifsragcdga lhqclrsrmv lttqeeseri kaiidagveg ipeedlqvld fkrwrealsr
      361 gfaahhagml pafrhivedl fvqglvravf atetlalgin mpartvilek lvkfngeahv
      421 dltpgqytql tgragrrgid tignavvqwa pamdphavag lastrtypli stfapgynma
      481 inllgmlgfe eslrlleksf aqfqadgsvv eetreiekae hrvrelrnql ddaidalapp
      541 srdgedpaev lmdyirlrrk ltdeeksara nnnaqrnqev avvlsrlqlg dviaiagkrh
      601 pilavvvtpa nqvadprpwv ttetgwsgri dvsginnppi vvgrmklprp vqknprrntk
      661 fiqdsfkrnr ydrpkkmrma prnrtnkkvg elrdairnhp ahswpatdre qlagiaqkla
      721 rrerdlekvs kkveratdtl gktfgrivdl lsemdyvefe gfgedrrpvi tdegerlsqi
      781 hsesdllvaq clkrgiwnel dpaelagvas lclfenrket rgepeaatda madameatyr
      841 iyteliadea rhnlprtrep eagfalaihq waagaplgyc maaaneagae ltpgdfvrwc
      901 rqvvdmlqqi aktgyeedir rnarraidai qrgvvaiga
//
LOCUS       WP_284810413             204 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium striatum].
ACCESSION   WP_284810413
VERSION     WP_284810413.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..204
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22089
     Region          6..201
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(55,59..60,66..67,97,101,108,111..112,117,140,
                     144..145,147..149,151..152,155..156,159..160,175..176,
                     178..180,182..184,186..187,189..190,194,197..198)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(143,147,150..151,153..154,189,192..193,195..200,203)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(164..171,177,180..181,184)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mpkniplgyy vdadtiihrc ptrvkfvvli tfivvttlwa ksiptaigaa aiavayypia
       61 ripisvawgq llpplyllla laafqwwqkd fvtavvmffs vyasiiaavl ltlttkvsdm
      121 mesferalqp faklglpven lslamsltir llplmlgtin evldarkarg agtsllafgt
      181 pvvirsirra qamgealqar gvgd
//
LOCUS       WP_284810428             473 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Corynebacterium
            striatum].
ACCESSION   WP_284810428
VERSION     WP_284810428.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..473
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49567
     Region          1..449
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mdsvqntldt vggvvwgpfv liplllgtgl wltirlggiq frtlgralrh afvdhpddks
       61 aegdisnyqa lttalaatvg vgnivgvata lsiggpgslv wiwvtglmgm askyaeaylg
      121 vrfrttdskg eqaggpqyyl krgikgplgt tlatafaifa vfasfgignl tqansvatnm
      181 esafgvtpva sgalmfvlvg avllggiqai gritsafvpl miiiyvvggl vvlivnagqi
      241 pealgliftd aftgtsaagg fvgssiimvi qygvargifs nesgmgsaai aaaaaktphp
      301 arqalvsmtq tfidtlivvt itglvivvtg vwdmgrdeag imtakafeag lpghwggtiv
      361 slsiiffafs tivgwsyyge ralsslfgrv atipyrmfft vvvfigavte ldvvwsfsdl
      421 anglmaipnl igllilsgli aretkaylef dpklnkpikd veefvrsqqm dwk
//
LOCUS       WP_284810507             330 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium
            marquesiae].
ACCESSION   WP_284810507
VERSION     WP_284810507.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..330
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35079
     Region          66..330
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrklalaava avvsatflli vgpqrismad tatgdpelst hlrehpeagf nnltaftldq
       61 gkatfaglga dehteveigs vtkmftaeia hqlveegkir ldttmgevle vgdspvsdvt
      121 vrelldhtsg lprqakamtf ssavfsitgs npyagvsted ivdsatesel adrgtesysn
      181 lgyallghtl etaadtpyeq llherilkpa gmketylmtp gsvpddaprg ltaagreaep
      241 wemegcpaaa gavrstaqdm aaftawfmeh gdtsygwqkn ddgksfwhng gtsgystmlv
      301 idpkenraaf anndspagte gltealferi
//
LOCUS       WP_284810575             744 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium striatum].
ACCESSION   WP_284810575
VERSION     WP_284810575.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 744)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 744)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 744)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 744)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..744
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77612
     Region          6..742
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtnlvhldlg vsgmtctscs srverklnkv dgveatvnfa tesasieydp ststpdslie
       61 vvrgagydaf alteeqeads eetanpvdea raqeakdllr rtiisaaist pimvvsmlpa
      121 lqftnwqwaa ailativyif ggapfheatw anlkhgsftm dtlitmgtta ayfwslyamf
      181 fghaghpgmk mhmelvsnna emdhiylesv gmvitflllg rwfevkakgq ssealrtllg
      241 mgakdatllv dgaekrvpik dlkvgdvfvv rpgekiatdg vvnagasavd esmltgesvp
      301 vevkegdhvt gatinssgrl evratkvgad ttlaqmaklv teaqaskapv qrlvdkiaqv
      361 fvpiviaisv ltliahliig gtaatapafv aavavliiac pcamglatpt ailvgtgrga
      421 qlgllikgpe ilestkqvdt ivmdktgtit egkmsvadvh aaqtsdqdat qvlklaaave
      481 agsehpiaka ivhaasdvtp asdfvsvagr gvegtvegqr irvgrvegel sslseafraa
      541 eaeggtpvav yaadaligii dvrdtvkess aaavaqlkel glvphlltgd nesaaqavaq
      601 avgidpenvt agvlpeekvd vvkqlqssgc nvamvgdgvn daaalaqadl glamgagtdv
      661 aieasditlm nddlrsaada irlsrrtlri ikgnlfwafa ynvilipvaa igllnplfag
      721 iamafssvfv vsnslrlrtf qpta
//
LOCUS       WP_284810586             238 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium
            striatum].
ACCESSION   WP_284810586
VERSION     WP_284810586.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..238
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=24826
     Region          5..55
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(7,32)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(14..15,26,29,33..34)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mdpvqllkks plslseisrr sgvsrntlnl wmrgaaqpsl tglakvmrvl gyevsvqvhr
       61 msdaaaataa rvllgdlase epdvkawidr fvqwgdtpac ggscqalier aawasnpygr
      121 hgalhflpan pitlasavda sgqpwamsga faaqqvsghi agegeprstl iwctnpadiv
      181 pslptriras aepvsggitl vpvageeltg atneagihyv sphqlaidvc aenyigga
//
LOCUS       WP_284810605             157 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter, partial [Corynebacterium striatum].
ACCESSION   WP_284810605
VERSION     WP_284810605.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         <1..157
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          <27..139
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 hvqkviglla qkatglrvqk ahghnkdgla valaiggial lpmggqgavv lvsdshllll
       61 afgtgllasl ipysleital rslnpnvfsi lvalepvfaa ffgwlllsqn lsplkllaia
      121 lvimasvlqt mvpdrgtkpk lrrvpwkahr rsrakvg
//
LOCUS       WP_284810673             546 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Corynebacterium
            striatum].
ACCESSION   WP_284810673
VERSION     WP_284810673.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..546
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=58705
     Region          4..533
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtdnhtpllk vrdlnvsytt aagevpavqg vslevypgei taivgesgsg kstsamaaig
       61 llasnaqvda gtiefqgrdi tdldnkrwre lrgrsiglip qdpnnslnpl ktigasveeg
      121 laihgvgtaa erkqraiell drvgiddper rygqyphels ggmkqrvlia aavalepeli
      181 iadeptsald vtvqkvildl ldemrretgv gilfithdla vagdradriv vmekgqvres
      241 gqaarvltdp qhaysrrlla dapslsvadv anakrrpars tetvlrvrdl tqrygdflal
      301 dgvsfdvakg tthalvgesg sgktttgrsi alfnaptfgs ielaganggs teltklkgka
      361 lrearknvql vyqnpyssld prqsigdaia eplrnlagas kakakiraqe flelvaldpq
      421 hydrhprels ggqrqrvaia ramivepelv vldeavsald vtvqaqilrl ladlqdelql
      481 tyvfishdla vvnqisdtvs vlshgqqvel grtadvfanp qseftrtlid aipgqryrag
      541 dlnlgl
//
LOCUS       WP_284810722             230 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium marquesiae].
ACCESSION   WP_284810722
VERSION     WP_284810722.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..230
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24043
     Region          1..227
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(13..14,16..17,20..21,58,62..63,66..67,91,95,102,
                     105..106,111,126,130..131,133..135,137..138,141..142,
                     145..146,165..166,168..170,172..174,176..177,179..180,184,
                     187..188,194,196)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(129,133,136..137,139..140,179,182..183,185..190,
                     193..195,199,201)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(150..157,167,170..171,174)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mqglhpatvv tiaacgwilt lalntpvasa svvlialacg taatrnasvi lttvalsapa
       61 alsmlvihap ygddpvlplv tsdglvlaat ltlrfcalma cfiaamavlr iadiakwlqv
      121 sraghkvayi vgaslqtlpq gahawrcvre anqlagitvt wrntisrvii pviarlltqg
      181 tqrgqalaav gfdqegqrtl lrpvsdsmvs rvvrlfiplv slvvviaawi
//
LOCUS       WP_284810896             116 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium marquesiae].
ACCESSION   WP_284810896
VERSION     WP_284810896.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 116)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 116)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 116)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..116
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12469
     Region          16..113
                     /region_name="ArsR_Rv2640c_fam"
                     /note="Rv2640c family ArsR-like transcriptional regulator;
                     NF041413"
                     /db_xref="CDD:469304"
ORIGIN      
        1 mdsspsnadn tpdaqccsls sgplsqgdsl rfsqqfkvla dptrlrllsi lcdegcgpms
       61 vteltalsgl sqptvshhlg klrksgllik qqsgrtvthr vqkeafrtlr qllsfd
//
LOCUS       WP_284810954             559 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Corynebacterium marquesiae].
ACCESSION   WP_284810954
VERSION     WP_284810954.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..559
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62481
     Region          12..542
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 msndskntgs avnrrrflqt tgtagaaial staaantana qsslsprvkq hmvepklger
       61 pflhgvasgd pipdsvilwt rvtpeddamp gsglgeatrv eweiakdegf gdvvkrgevt
      121 tdvsqdhtvh vdphglepet vyffrfkaqd kyspigrtkt apalsaspee ltfgvascan
      181 wesgffnayg diaqrgradq ldymiflgdy iyeypqreya gygpvrlhhp aheiisledy
      241 rirfgryrtd enlqaahgal pwvvvwddhe vandnwrega enhtegkegt fldrrkaamq
      301 ayfewmpvra tnpseqghly rsltfgdlve ltmmdlrtyr deqvrfgprk maaegrtmlg
      361 seqynwllnk ietssakwnm lgnsvmfspm nlanlqkddr tapvssslss nitgipvngd
      421 qwdgysaerr llidalskhd shtlfvtgdi hsewahnisk dgrifgaemv casvsapnvn
      481 eqlklpegne lsklaqrylm ganphtrhvd ldhhgysyvt vrpdsaemhw lrvdnlltvk
      541 spvrealtmt wrpgegytt
//
LOCUS       WP_284811001             378 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Corynebacterium marquesiae].
ACCESSION   WP_284811001
VERSION     WP_284811001.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..378
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42549
     Region          72..371
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 masiepyylk ykegdekakk ralrymvqyr tpdrkltkkr gfkrkgdaqd faqevertkk
       61 tgtfihpqag kaevskvyel wlpsqeslap rtkrtnlsay nvhvkprwgs wpvdsitaph
      121 vrkwvadmqs egkkrdtilr avyvlralce tavesrmiaa npvqkitvkr estarrgylt
      181 pkqvevlaav qgtdneraii ytmaycgpri seiaalnved ldesthrlhi dkavkdygvi
      241 gptktyenrr vpvprflleq lteltdgreq naplflskdg qrldvgnyra rifkpsvdka
      301 kkkwkedght gefptvlphg lrhtcaslai svganvkavq allghesaav tlniyadlfp
      361 ddlnqvgdal nalhddve
//
LOCUS       WP_284810696             328 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            marquesiae].
ACCESSION   WP_284810696
VERSION     WP_284810696.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..328
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35346
     Region          13..323
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 maahnpapkr hdeaverltn lsfalqgaan sggspdrtaa wirshvagyg dksdeafaks
       61 lardiatlqr agvpivhsgg edgaryrlda ssyqlppvef speeamvlgi aggvgttggl
      121 sdfslsgwtk iaasgasrnl agapvytavn ditrlapeii tavlaavrnq lritfsyran
      181 patepvrrvm dpwgvvnrds riylvgfdvd rneprvfral rvsdikrshd paehpnpten
      241 lqvlvervlq rgekvdarlv ipdgqarell dsgeqqtdgt vllhkvdkdw lvrtaagyap
      301 evqvlepagi rqevisllhk asqsqeeg
//
LOCUS       WP_284811121             361 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium marquesiae].
ACCESSION   WP_284811121
VERSION     WP_284811121.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..361
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36058
     Region          54..354
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mpattmdgqq iqsdsaadsp tttgtptpvv araqshkmll vafilaslvl avaslavgsr
       61 sippgevlaa lhgageqdih divwnlrmpr tflayfagaa lavagvlaqs wtrnpladpg
      121 figvtagasf fvaigtaigi atstgmrttl alagagittl lvlavsrrfq dpltlvlvga
      181 gvsaalgsga miiglystdv ldsmrrwtig stfgrgpedv aiagiglvig lacaamaarp
      241 ldllamgees slalggsptt arvgaalsvv vlagsataat gpiafvgfai phivrrlvgp
      301 svatlllpsa llggcavlaa ditgrliags selemsivla ivgapfliwg ahrgvgrawg
      361 q
//
LOCUS       WP_284811177             270 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Corynebacterium marquesiae].
ACCESSION   WP_284811177
VERSION     WP_284811177.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..270
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31238
     Region          3..237
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mptvwavsdl hgavktnser idqlsppdpa dwlivagdva ertdliiril rqlndryarv
       61 iwvpgnhelf srsqdryqgr ekyahlverc reigvitped pypvfhgtti vplftlydys
      121 frphgltvde aidaarakql mmtdefaiap fvdvrawcwd rlaysikrls rvhgptvlvn
      181 hwplvqeptm llrfpeialw cgtrhtrswp rrynaqsviy ghlhmpsrmn vdgvdhiets
      241 lgyprewqgr enaqawpypv lrsfveegtr
//
LOCUS       WP_284811179             320 aa            linear   BCT 25-DEC-2024
DEFINITION  DHH family phosphoesterase [Corynebacterium marquesiae].
ACCESSION   WP_284811179
VERSION     WP_284811179.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..320
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=34412
     Region          7..319
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mtkkqyepav aalhdahsic ivthlrpdad aigsaaalll alrqrgkdvc avvgqereis
       61 hnlytipaad dvttslklpe gydlyvtvdc gsldrtgffa drieqlaqqg rvlcidhhss
      121 npgfgavnvv dtecesttvv llrildslei qidrhiahcl yaglmtdtgs frwgrpamhd
      181 iatrlmhydl dtkqiaadll dsttpddlqm igrvlaglrl eeagehtlgi lvarlediqg
      241 hsdsaveslv efvralegtt vgvvfkeqap evwavslrss ridcssvalt fgggghvpaa
      301 gytahgapee iikelvaaiq
//
LOCUS       WP_284811225             440 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium
            marquesiae].
ACCESSION   WP_284811225
VERSION     WP_284811225.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..440
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=47330
     Region          1..438
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrmtvigtgy lgathaacma elghevlgvd vdenkisalk sgkvpfyepg lpevlernie
       61 agrldfstdy eeaaefgnlh flgvgtpqrr gsyaadmtyv kavitdlvpk lkgdhiifgk
      121 stvpvgtaae lqelanelap egttveiawn peflregyav kdtitpdriv lgvregesra
      181 eevarevyaq plsqdtpfiv tdwqtaelvk vsanaflatk isfinavsei ceiagadvta
      241 ladaiglder igrkflgagl gfgggclpkd irafmarage lgadqaltfl revdainmrr
      301 rdrvvdlake afngsllghr vtvlgcafkp nsddvrdspa lavagslsla gaavtvydpe
      361 gmdnakkvfp tldyaadtdd alreaelvil atewkqfkel npqqagqlvd nkhiidgrnv
      421 lpvadwqqag wkvealgrtl
//
LOCUS       WP_284811448             700 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Corynebacterium marquesiae].
ACCESSION   WP_284811448
VERSION     WP_284811448.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..700
                     /product="PhoX family protein"
                     /calculated_mol_wt=76809
     Region          46..692
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 malkgrnlls slfassrssl tctykcgnac fgecenksdn pyfadqfsrr talragslsv
       61 vtvgggaala acsnpddasn easssegkgg ktseanvelt saegmkfdpv qpnekdevvi
      121 pdgyeqsvli awgdplfeda pefddknqta eaaekqfgfn ndfagliehp dddnrliyvc
      181 sheyttepqm fpnydadnpt eeqakigwag hghsivevsk vgktgelkre fgplnrrita
      241 tteftlvgpa agsdyvktsa dktgkkvkgt lnncsggitp wntmlsgeen fdqyfahakl
      301 ddkkaqesle rfgmedgesq rkwerfdkrf dvskepnepn rfgwiveinp ldpkstpvkh
      361 talgrfkhea gnihiasdgt vvcycgddsr feyiykfist kkykegdieh nltildhgtl
      421 yvakvegnsp edeidgsgvl pedgafdgkg ewiklltsdt ennkfeshvd gmsaeevavy
      481 treaadkvga tkmdrpedme vhpdsekvyv altnnkyrga tgenakknke epmewapike
      541 nknglvmeie ddhagekftw nlflvcgdpk eantyfggfd kekvspiscp dnlafdshgn
      601 mwistdgnal esndglyavt tegdtrgelk cfltvpagae tcgpivtder vmvnvqhpge
      661 tddatfekqt shwpeggkst prpavvvvwk kdgnigvdkk
//
LOCUS       WP_284811253             259 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium sp.
            MSK297].
ACCESSION   WP_284811253
VERSION     WP_284811253.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..259
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27498
     Region          24..245
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mtqsnkhteg gsgssaaagv sgketrtteg etrrqvmhll ltlgpvtasm lgdhlglsaa
       61 gvrrhldilv edgltetvqr rpqgqsrgrp akhfrltdrg rayfghsyds lasdaldalr
      121 eaggsdavra farqrvrkll dtitpassla ddneevdeqa vehtaqqlae vlnahgyvst
      181 vrpsesgiqv cqhhcpiahv aaehpelcea ehevvtslls qhvqplatia eghgicttni
      241 pltqahtitk gaghdsgti
//
LOCUS       WP_284811497             298 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Corynebacterium sp. MSK297].
ACCESSION   WP_284811497
VERSION     WP_284811497.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..298
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33776
     Region          16..250
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mthldeasep vefpptvwav adlhaavran rkrlaeitpr hpddwlivag dvaerfdlia
       61 svlnelrsrf aqviwvpgnh elfcrstdah vgrakydslv qlcreinvlt pedsfpvfgd
      121 ttivplftly dysfrpagmg veealdaagq knvvladeia iapftdiraw cwdrlaysit
      181 rlsrvhgptv linhwplvqe ptlrlglpev alwcgtrhtr hwprrynaka vvyghlhmpd
      241 esefdgvlhh evslgyprew trydedrvwp cpileladdg agtmtahtay rqrgrgmq
//
LOCUS       WP_284811533             664 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            marquesiae].
ACCESSION   WP_284811533
VERSION     WP_284811533.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..664
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=72244
     Region          1..66
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mtatltladv arltgvtrpa vnewiqrfns esitpfpspy gehdghpyya iteiqdwlra
       61 tklgrrdtav edalfyssly rmllhnpera algllncnta lspqdfspsa avidsltaay
      121 qraadnipsd dpeadiaqaa eqvaeaafgp aaalarladd lsaqrqvtls srftsramqa
      181 vsealtlenp tppiiptdey slgfvtgltr eleetlvlsi gyrkdcapds lywaelacrn
      241 vefidaseei pansllvhav psppktapey fehlqdlldn ldergamfci stadmlieds
      301 laqvvrrrfl aptetgaiap lrysarlprg ifpdrgqqqg alwilkrpnr eaignpadaa
      361 vviadvpdlk rpglvsdwat mlttpdeark hafvrgrilr aadawrsrth sldvsvfsst
      421 stssaadlmh tahqagldis sagledaqpk igmraesgat rleylpwkaa tnartgvlqk
      481 lsgsriaehd lapeavakle ligepeilgs ipqgarcidr lrlediaprg tltepgdvvf
      541 iknprprali deeggklvta paqalrcrtf rgrshtpleq vclpylveka ineavssela
      601 svyfpvlprk naedlstveq qlgarrrqlv eqlrsidvlr hnltisigtg avtiaesraq
      661 sppg
//
LOCUS       WP_284811590             493 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Corynebacterium
            sp. MSK297].
ACCESSION   WP_284811590
VERSION     WP_284811590.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..493
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=52164
     Region          4..458
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mnflesveav ivkfndgiwa iipwlliasg vyfavrtsgv qvtklgdmfr slgegpkgkg
       61 knldpeyggi safkaftisa asrvgtgnia gvavaitigg pgavfwmwvi aivggatafi
      121 eatlaqlwkt ressgnyrgg payymtrglg fkplaavfsv alaftfgfvy nafqsnaivd
      181 tmstslgleg wvfnliigii laaissvvif ggvqrianft qiivpfmagl yviiglvvii
      241 ininevpgmi ghivghafgv tevvgatvga afshgmrrgl fsneagqgsa pnaaatatvs
      301 hpvkqglvqt lgvyfdtllv csitafiill ggdhkygldn iegaaltqta lanevgnwgi
      361 hivtfiifcl afssvlgnyy laqtnlqylt espkilngfr vgvlafiiig svtsipvvfa
      421 ladtfaatmv vlnliaivpl ggvalkllkn ynqqkrrgqd pvfhrdmlpg lknveawdgs
      481 dpvtrrneed alk
//
LOCUS       WP_284811595             181 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Corynebacterium sp. MSK297].
ACCESSION   WP_284811595
VERSION     WP_284811595.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..181
                     /product="YceD family protein"
                     /calculated_mol_wt=19285
     Region          <38..181
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mtspfvfdvk alltqqqspe qtthtgpapr rigaemlaie egaevtvdav lhslgsgima
       61 dadvsavlrg ecsrclsple rpmtvrisqv fsadddfitg daeddedegs gdeipqvshe
      121 dtidllqtlt delvvslpfs pvceggcpdd sltpapdgvs gdedaqerid prwaglekfr
      181 d
//
LOCUS       WP_284811646             503 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium marquesiae].
ACCESSION   WP_284811646
VERSION     WP_284811646.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..503
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=54630
     Region          157..498
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 medsqetqgq apapatatar pqsmwheglg qgegekessk rrmfsqipqa mplrtwlvil
       61 lvvvsglgit gssfavnsim rnvlfnnvdd elrsasttwa rdisndffig dhtkrpptey
      121 vvlnylpdgt irysgpsstt pnaeniplgg ypttvgsien ntkwralafa dsngvitvia
      181 kdmtheneil hglamvqvti aaialaaiaa vgfwfirral rplrvvekta seiaagdldk
      241 rvpkwplhte vgqlaaalni mlgqlqrsvv raqekeeqmr rfvgdashel rtpltslrgy
      301 telyrsgatk dvdlvfskid deskrmsllv edllaltrae gtrldmhpvd llelalsvgs
      361 saraafpgre ikvandaksi pvvngdasrl hqvllnlvtn girhggedat vtlrlrrean
      421 dvlvdviddg kgmsqddaah iferfyradt srtrdtggsg lglaivhslv eqhdgsisvd
      481 sqlgrgttft vrlpaladap sep
//
LOCUS       WP_284811768             247 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Corynebacterium
            marquesiae].
ACCESSION   WP_284811768
VERSION     WP_284811768.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..247
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27324
     Region          55..149
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mrhtrematl rrsiqllrsf rfeqtrpeif ygglaedtaa lvdnlgrdlg vqlfgarvld
       61 vgggpgyfad afarrgaryv glepdagems aagihlsnsv rgdgtnlpfa dnsfdvvyss
      121 nvaehipnpw dmgeemlrvt rpgglailsy tvwlgpfggh etglwehyig gefarnrytr
      181 rhghppknvf gtslfdvpcs aglawaqrtg alqfafpryh pswawwltrv pgvrefavsn
      241 ltlvlqk
//
LOCUS       WP_284811776             386 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium marquesiae].
ACCESSION   WP_284811776
VERSION     WP_284811776.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..386
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=42458
     Region          23..344
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 msnqfqvdpg lgasvqpqas vksvpqhlpe ldglravasl giivthvsfq tgtgwgfagr
       61 fdffvavffa lsafllwrrr glhtlsryar srvarllpay yacvvavmll lpdahslspt
      121 qllsnltstq iyvvdglapg lthlwslcve fffylalpll awlfgalprr wrvaaialga
      181 vvswawgfvp fvadyakdqv nsqiwppaya swfavgmlaa eceeagvsrr vqrvlrprwa
      241 wwlaaavvlw lasrewfgpq glvhpepgef srriiagaaf aavvvvpval aprdkswlts
      301 plmqalgaws ysiflwhvai lglafpltgv plfsgkpldf wvilavtvvv tvvvsaasyt
      361 liecpgrdll lgrrrkdrpr prhtss
//
LOCUS       WP_284811797             462 aa            linear   BCT 25-DEC-2024
DEFINITION  acid phosphatase [Corynebacterium sp. MSK297].
ACCESSION   WP_284811797
VERSION     WP_284811797.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130290
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..462
                     /product="acid phosphatase"
                     /EC_number="3.1.3.2"
                     /GO_function="GO:0003993 - acid phosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=50475
     Region          <139..341
                     /region_name="PAP2_acid_phosphatase"
                     /note="PAP2, bacterial acid phosphatase or class A
                     non-specific acid phosphatases. These enzymes catalyze
                     phosphomonoester hydrolysis, with optimal activity in low
                     pH conditions. They are secreted into the periplasmic
                     space, and their physiological role remains...; cd03397"
                     /db_xref="CDD:239491"
     Site            order(228,235,264..266,299,305,309)
                     /site_type="active"
                     /db_xref="CDD:239491"
ORIGIN      
        1 mktflisrrr atslltaaaa lavvagapdl vqqhggtaha taaeaslqsp lhastthlal
       61 pfeipqlqlp apklssehde gaehsplssi gatpkhhdga pvpkpfdaty ltgyssdiss
      121 yqygiyyevv refkdlrsnh pdvmrknldi vadynnnaqp ervdkairda ladkdgvlft
      181 aaealgdefg qhflqalqek rlpktefllg ngyaaraggi aswghaekll fnndrpfvqa
      241 perikrhesp erelydgssk sfpsghtnqa twittllamm lpevgtqlle rgseagesrl
      301 vmgvhfpldv iggrmtgqaa aadrwndpkm rdallqaree ivaemewrag kpfaemiaed
      361 shalsdqqae adytrrmtyg fapifatdep vnvpaaapal letrfpelsy eqraevlrht
      421 alpsgypldd rdpakgdwqr inlarawnaq vsigaggevv vk
//
LOCUS       WP_284811842             285 aa            linear   BCT 25-DEC-2024
DEFINITION  indole-3-glycerol phosphate synthase TrpC [Corynebacterium sp.
            MSK297].
ACCESSION   WP_284811842
VERSION     WP_284811842.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..285
                     /product="indole-3-glycerol phosphate synthase TrpC"
                     /EC_number="4.1.1.48"
                     /GO_function="GO:0004425 - indole-3-glycerol-phosphate
                     synthase activity [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29641
     Region          2..264
                     /region_name="TrpC"
                     /note="Indole-3-glycerol phosphate synthase [Amino acid
                     transport and metabolism]; COG0134"
                     /db_xref="CDD:439904"
ORIGIN      
        1 mvagiladva arearlpfad ikalsravpa prpvlpllsq sgcsviaeik rakpaarydd
       61 afgtcatgas qtdslidfga vdtladvasl ahdfesagva viacqteqlr frgsledmat
      121 araassvpml crdiivdpyq ihearffgad mvplqvelle qarlealvdr ieslgmtvla
      181 evrspgqacr avsagvsvvg inarglesrt lspdrfaaiv phlpesviri glggvlgare
      241 lwryagwgad avlvgealms apnpaatara lvaagrhpac pavrg
//
LOCUS       WP_284811855             246 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Corynebacterium
            sp. MSK297].
ACCESSION   WP_284811855
VERSION     WP_284811855.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..246
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27306
     Region          6..223
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mnngwyrffk yvligpwlrv wnrpfteglg nvpnqgsamf vsnhqavmds fylplicprq
       61 ltfpakkeyf tgtgfvgaiq rffftsagqv pidrtakdag dalidtaetv farddifgiy
      121 pegtrspdgr iyrgrtgmar iamttnvdvi pvamintaka npigswiprp akvgvrfgka
      181 isphqwadeq glnpedhqti rkftdfvmre lalltgteyv dryasevkds lqagngypeg
      241 tepnpa
//
LOCUS       WP_284811973             248 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Corynebacterium sp.
            MSK297].
ACCESSION   WP_284811973
VERSION     WP_284811973.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..248
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25876
     Region          <139..>220
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mnkqtalali svialvllsa avgfgaytll sgnsngsgad aadagdggqa nqsenetavp
       61 gsdsdyasga ldlagierpa cpsptipgvg lelpclsere pataagvgks peqgsaeqgs
      121 adqhsanqer advvhddavt ivnmwawwcq pcreeipyle qvhkqhpewq ivgvhadqna
      181 kngagmldem gvdfvsyqds hnkfatelgl pgvipitivy vgetqkkvla qpfrsadeii
      241 esiegvvq
//
LOCUS       WP_284812017             512 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Corynebacterium sp. MSK297].
ACCESSION   WP_284812017
VERSION     WP_284812017.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 512)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..512
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=55874
     Region          42..497
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mdapfdkfap qarsglqflg dgyshkhals saeqtldial aptftpspdt lhpsqdldvd
       61 slstafgtve idtplgsldk alkelntlwi shairydspr ylahlncpit aagfagatis
      121 aglntavesw dqgrgaaiie dqlikwfaat agmnphkatg tftsggtqsn lqalytsrek
      181 alqsgsslds lrilcsseah ysiarsahil glpkeaviti dsdsngvlki aslrrtidsl
      241 lesdkkftia clvltagttd lgaidplaqa tqiaqqhgiy vhvdcaygga lllsnkdqkl
      301 lsglhqansf sldfhksffq pvacsaliyr dltelenvtw hsdylnpetd trmnlanrsl
      361 qttrrfdalk lwlslraegp kalgqafdrc ceiatdtavm vrdfpelell tdptlstvlf
      421 rylpplsgkp ssntclqdte vvnrindeir rqlfnanelv iastrrndki ylkltilnph
      481 ltmddmhyal ekicaagtte carlqskeev dd
//
LOCUS       WP_284812057             517 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Corynebacterium sp. MSK297].
ACCESSION   WP_284812057
VERSION     WP_284812057.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..517
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54814
     Region          17..513
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mssgfarssf ahngearvav igagpnglta aavlaqagcr vevfesaahi ggsarthsaf
       61 gpesvvdfga aahpfgvvsp vfrqlglekf glkwkhpeyp mahplvdapa ailyrdlrtt
      121 aaqfsdhdgr vwnhlhkplv dgvdklvnsv lpvrprypla larlglrgvw parsltsrll
      181 vdesarallv gsavhairpp sqpgtaafgl lfntlgmttg wpmvsggtgq lamalarvik
      241 hyggtiqtga eivelsafat ydavvttqtp rqlltlqgle lsrlrsrslr rwkygtavyk
      301 mdylingpvr wndprvagag tvhvggtvse mqsaesqaaa gilperpfvm vcqqqaadst
      361 rfsgsrrsvg agrapsaqpg sgripeeatq philwayahv phgyqekfpg evaglieaqi
      421 sryasglsaq iierhqsspe qlqeananli ggdiaggamn vaqmprqrqy vgtltrnpev
      481 pvvqaggasl pgagvhgmag wraaqtilrr fgavafr
//
LOCUS       WP_284812154             348 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium sp. MSK297].
ACCESSION   WP_284812154
VERSION     WP_284812154.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..348
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37606
     Region          46..268
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mhdphstadq sqqqqplpqp qpassafpqq spqasshpnp hpqpqrgrva affdldktii
       61 atssafaygr eflhnglitp qdalslslak asymfagqss aqmdstrdql tsmitgwsek
      121 qvrdivhetm htvltpaiys eareliqahq eagheviiis asarqlvepi akelgitevi
      181 steleivdga ftgtvefyck ggakadaita lvdergydlk hsyaysdsat dapmlelvgy
      241 pvavnpdral kkialerswe irsfkdpapl fqlpgakeig igagvlagiv alvtagtllt
      301 kfyahdkpak pdkpaktase sstrapaipm pkgldwrfld cwfkkssa
//
LOCUS       WP_284812170             256 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium sp. MSK297].
ACCESSION   WP_284812170
VERSION     WP_284812170.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..256
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27614
     Region          7..244
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(17..18,20..21,24..25,63,67..68,71..72,102,106,113,
                     116..117,122,138,142..143,145..147,149..150,153..154,
                     157..158,178..179,181..183,185..187,189..190,192..193,197,
                     200..201,207,213)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(141,145,148..149,151..152,192,195..196,198..203,
                     206..207,212,216,218)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(162..169,180,183..184,187)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mpsgaprinp ltriiimllv ttpllfsldw vsasislait ivvalvggvg lktlaatlwp
       61 llliaplsgi smllygaegg evyfefwlmt isdnsielai aimirilava spvillarni
      121 dptrlgdsla qilhfpdrfv igsvagvrmt glfkddwvam nrarrarglg drgkiahfft
      181 mafgllvlal rrggklatam eargfgrqpl ygerrtwarp atlraadwra lgialvcaai
      241 pvvvavlvgs wrwfgl
//
LOCUS       WP_284812208             378 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium sp. MSK297].
ACCESSION   WP_284812208
VERSION     WP_284812208.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..378
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40654
     Region          7..361
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mvatsvsasv pqridclegi ralaavgvli thvhfqtasg pvvlerfdyf vavffalsaf
       61 llwrrpigpg flrkraarvl paylvcvavv alalpaastm swqqllanlt atqiyipdgl
      121 apglthlwsl cvefafyftl pliawvllrw qartrvlllc avgiaslgwa flpfvagfdg
      181 sdgaswsasv nrqiwppayt lwfvvgmlaa eaesagiakr pglvrrilgm kplfwllata
      241 clflasweai sprglthpsp lefairislg tvfaacivvp yalrptqsgl llsqpvqavg
      301 rwsyslflwh vavlsiafpl agiemfsggf vsilaltlgl svavaaisyt lveeparlwl
      361 rqatapaakh aasklspa
//
LOCUS       WP_284812337             603 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Corynebacterium sp. MSK297].
ACCESSION   WP_284812337
VERSION     WP_284812337.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..603
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=66958
     Region          17..571
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 matppingtn dsqstpsrrq ilksmtamss amvlnhiapk ahagiapeal aaesevtdqa
       61 revfrhsvas gdplphglii wtritptpea lpgsdlgpdt avhweiatdp efsriiqhgt
      121 eiaaatsdht vkvdvgglap attyfyrfsa kingqtvtsr vgrtrtapaa easldslrfg
      181 vcscanyeag yfqvyrdmar rddlefvlhl gdytyeyeqg gypglyqtsv rqvapqhktt
      241 tladfrirqg lyhedadlae lhaskpmici wddhefadnr wregatggsf denqdfdslk
      301 aaatqayfew mpvrrdhdls sdglyrtlry gnlvdliipd lrtyrdeqli qtgdhllktn
      361 pdfaraagrd grtmlgesql nwfkdsvtgs ttqwqiians vlfspmtipp glspqlqhwl
      421 idtidlppdg iglnmdqwdg ymaerqeiid vvgdapgrni ifltgdihss wasdiprdvr
      481 ayrngqdmts iatefvtpav tsngpfatla ahealegtaq aiveqganll rafnhwfkwi
      541 dfrfngymsv dinqegaqcd whfvdnvlsp dtelwtarsy svrpgnprpm paekpldqtq
      601 tsf
//
LOCUS       WP_284812342             534 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium sp. MSK297].
ACCESSION   WP_284812342
VERSION     WP_284812342.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..534
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=58781
     Region          166..519
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 msesepqkap eastgwaatg errrrsyray rthrplrlrt wlvvltvlvs afgllassft
       61 vysvmrevfy qrvdddltqs mdgwaqrsel fsrnlsaspp tdyavihifp dgssrvyndr
      121 dtlpqinnlv igdsprsvss lggtqqpewr alaskhngvv tivaknlere ngllrglaml
      181 qalislvmlg flallafavi rqtlkplqiv ertasdiaeg dldlrvpewp lntevgqlaa
      241 alnimlerlq esvetaqske eqmrrfvgda shelrtplts lrgyvelyrs gatndvehvf
      301 atiddesgrm kllvedllal traegsrldk rtvdvlelsl avvgsaraay pertirlenk
      361 tndipvvsgd pdrlhqvlln lvtnglnhgg peaavtltlr kenhadhdrl tgeqhnasdt
      421 hevdehttgk gkhdgkkgkd yvcidvtddg rgmskevagl iferfyredp srargagggs
      481 glglaivksl vdqhegditv dsepgvgstf tvripalnep saseetfdgy dedy
//
LOCUS       WP_284812355             344 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Corynebacterium sp.
            MSK297].
ACCESSION   WP_284812355
VERSION     WP_284812355.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..344
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=37896
     Region          1..325
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mrillianpn stsqtnelfr riiplvrsid dshvltkfth yvghaedmtr glsredvdvv
       61 iavggdgtvn evvngllgkv gdgrrkasev palaviptgs anvfvralgy prdavhttel
      121 vvghikqnlr rrirlgtwnd rwfainagig idadvlhsid klreqgfaat plrylrisyq
      181 awhrilnapp kisahaesae gqtqhideap lvfasntnpw tflgplpvvt nprnsfdkgl
      241 gtfgltdlkg fggfvgllhl fgadgkgrln kftdartlrf ddatritlec dkelrfqadg
      301 etqgklktve lnsipdaiev fspeeiipvq qrgvwavvrd lfri
//
LOCUS       WP_284812377             239 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium sp. MSK297].
ACCESSION   WP_284812377
VERSION     WP_284812377.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..239
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25756
     Region          76..221
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mskkvtnpnq kssagfigai vavlvivvav iayiviagqg akaekfanwe ikqvsaetsf
       61 ddntltfgda dkaphvdlye dfscphcgel aeatdaeale einagnlavs ihpmtfldhq
      121 sdghstqava allalaehdd vnalwnlrea mfenlqdivr swgpddfada aaqmeasdea
      181 vedirngkfl ekareagean gkdleskvdr vstprvlmdg kdlevedind wvkvavesk
//
LOCUS       WP_284812401             203 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Corynebacterium sp.
            MSK297].
ACCESSION   WP_284812401
VERSION     WP_284812401.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..203
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21972
     Region          36..154
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mptwndltrn npshsenyaa rwkrfvaegk didgearfid alsprgakil dagcgtgrag
       61 gpliarghtv agidldpvli nhaqhdfpkg ewhvgdlgsa slydqpelgh mrgsfdvvfs
      121 vgnvlgfidp vdrehaienl yaplrpggra vlafgagrgw gfsefldsct eagfaqelll
      181 ssfniepfnt dsdfliavlr rpr
//
LOCUS       WP_284812647             331 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium sp. MSK297].
ACCESSION   WP_284812647
VERSION     WP_284812647.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 331)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18950610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..331
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=36230
     Region          40..164
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
     Region          177..318
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mvkksqmsea dkdnqsgfsl saryhqiakn pgadypkptl aagavlwrrg dngtaevavi
       61 hrpryddwsl akgkvdpges lasccvreia eetgyqvqlg sllgsvnypv qgrtkvvfyw
      121 naevtggkfr kndevnklrw lsvneacdkl tydtdrrvle qaatrhddav dtrvlyvrha
      181 kahdrktwsg ddnlrplhkk grrqaeflvp mlsaykptal ysaeparcqs tiaplsdals
      241 lpvtteqivg daglddlaaa tarfreiatg ggvpvivsqg gmmpeiietl aaetdfdiep
      301 refkkagtwv lalregtlvg adylasplpv r
//
LOCUS       WP_284812725             464 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium
            propinquum].
ACCESSION   WP_284812725
VERSION     WP_284812725.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..464
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=48578
     Region          1..463
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mhltvfglgy lgathaacma eaghevlgvd iaparvaqlq agrvpfyepg laelvargve
       61 sgrlrfscdy rqaaefaqlh fiavgtpera dspaadtsav eavvgklapl lrgehvlvgk
      121 stvpvgtaar lqerassisp atvdvvwnpe flreghavad tlrpdrivvg agaestpkga
      181 dapngvgsap alqklrevyr aplergtpfl vmpwasaelv ksaanaflat kisfinaiae
      241 vceavggdva avaealgyde righqylgag lgfgggclpk dvrafrarad ecgagdalaf
      301 lgqvelinar rrqrvvqlas elvaqspkaa epagsarpgl sgavitvlga afkpnsddvr
      361 dspalhvaae lalrgarvrv cdpqavenar rvypgleypa sladgvaead lvilatewse
      421 yreldpvwaa elvaepvlld arnaldlarw rdagwqvhal grgd
//
LOCUS       WP_284812740             333 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium propinquum].
ACCESSION   WP_284812740
VERSION     WP_284812740.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..333
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33903
     Region          24..326
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtrisflpat vlavavlgva ivaslffgsn nispgqvwas lsnngdtatd tlvlqqrlpr
       61 tivvvlvgaa lgvagalmqa ltrnpladpg ilginagasi avvagvafag vtginnyifl
      121 aivgallasi mvyvlggagr nsvpsparlt lagvaismai sslvqaiils nanafnefry
      181 waagsvegrg wpvlehiwvf illglvfafa sapslnalsl geemgtalgv kvwrtrvltf
      241 saitilagta taavgplmfv glavpyaarg lfghdnrail agsvvigpvf llaadvlarl
      301 vimpqevqtg llsavlggpi fiavvrmkki gav
//
LOCUS       WP_284812987             381 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium sp. MSK297].
ACCESSION   WP_284812987
VERSION     WP_284812987.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 381)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..381
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39790
     Region          70..376
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mminakksaa kndtsatsds aqdsaaprtv atdhavvelg rqhkkltwqr igivsalcfi
       61 alaafvtsnf vgainispge vitgiinpss ldeqthtvlw rlrlpmavma lligvslsla
      121 gaemqtilnn plaepftlgi saaaafggas aivlqwqiia qpqlnlalva wlssviatgi
      181 iviaavlrgv raetmvllgi glvfffqaml aliqyrssae alqqivfwsm gsltraswtg
      241 navlagvlvv alpilwalsw qltalrlgda raaamgvnts alrvivlvvv slvaattvaf
      301 agiigfiglv gphiarmlvg edqryflpas maagaavmct ahalslivkp glaipigivt
      361 sllgvpffia ivmakrralw s
//
LOCUS       WP_284813045             328 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium sp. MSK297].
ACCESSION   WP_284813045
VERSION     WP_284813045.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..328
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32993
     Region          27..322
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 matqtttrfi vafaianavl llmivlalgi gavavppsev vrrlmeadnl iwkfrvpral
       61 vgvfagagma isgcllqlgl rnplaapdtv gitaggglaa vvallgagal paqaltpval
      121 vgacvgaglv lvasgkgmnn pirlaltgva vsvglgavtq lllvrtapea gaamawlkgs
      181 lyarslsdav vvgpivvvvf clsliiakhf dvlllddatm kgigamplrw rllavgcaiv
      241 sgaaavaaag vlafaglivp hlarllvgpq llrqlpmatv igsalvvgsd algrwmfspt
      301 eipvgaliai igapyfvfll mritskgt
//
LOCUS       WP_284813110             530 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium sp. MSK297].
ACCESSION   WP_284813110
VERSION     WP_284813110.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..530
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=56901
     Region          35..468
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mtlrqdrpaq asatmpagav detsarnsrg arkpnalval lrrlhfyagm figpflliaa
       61 isgalyavap taeklayqdv ltvtpppgae gvtntitlee qvnnaheafp dldiaqvwps
      121 sepgettrvl lidetideae lrsvfvnpyt gsvvgdepsy sglgelplrr wishlhesmh
      181 lgpvgelyse laaswlwffa fgglvlwasr nkkvqqlfgf gnartgketk nggaknakda
      241 kdaknkgtgr rrlvslhgvt gtwmligmla lsvtgitwst yaganvnrtv ealqwradpi
      301 ttelsgesaa eaglhaehag hggsaaseae arawtpeeia eqadqvlata reegltgslr
      361 mypgesvehg wqaserwtew rttsdaisvd getgevidrl pfselplfsk ltswgiylhm
      421 gimfglplqi lllvtalaia glvvlgyliw wkrrptpgat agipgprtkl sstqwiivai
      481 flvavggflp lfgislaaml ladvllskra gqtghtghet rraavdgarv
//
LOCUS       WP_284813219             648 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Corynebacterium propinquum].
ACCESSION   WP_284813219
VERSION     WP_284813219.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..648
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=69606
     Region          14..635
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mhkrlrliaa lllvfavvla grlawvqvvw gpdlsaraed qrariyvdpa rrgavldreg
       61 kqiaytmqar sltvspttlr kelreqaqle sderlddkqk deyvrttlre msreipkiie
      121 easddeqdlk skdlldklna dtqyevlvrn vdpdvaaeis erfhgvaadh qdirqypnga
      181 igenvvgrvs mdgtgqfgle asrdsklsgi ngrstedvst ngqvipgtlr detpavdgkd
      241 ieltldldlq tyvqqqleqa krnslaesae avvldattge vlamantdti dpngdigkql
      301 eegkhfdnrs isfpyepgsv akiitaaaai eeglttpdev htvrgsiqva dvtvndawph
      361 gplpyttagi fgkssnvgtl qlaerlgqdk fdeylnkfgi gettgielpn essglrpprs
      421 qwsgstfanl pigqgmswtt lqmasvfqtl anggervepr iiksdrddkn andkdnsdda
      481 agsagtaadg ndgndgngan dkktdastsd dkpektrvvs ketaeavvdm fratvqadpa
      541 gvnngtapda niegynisak tgtaqkvdpn tgaysnsayw itfagiapvd dprfvvaiml
      601 depergvldg ggggasagpl fhqiaswlld rdnvppspaa pdltlqap
//
LOCUS       WP_284813272             332 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium sp. MSK297].
ACCESSION   WP_284813272
VERSION     WP_284813272.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..332
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34178
     Region          27..328
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mlsrfrtagl vvlvivtlas lllslaigar siapddvlry lfhpelgdpi sqvvwqsrvp
       61 rtilvvlaga slgvagglmq avtrnpltdp gilgvnagas lavvaglafv gltdlrnymw
      121 falagafits ivvfivgntg knrgnavrmt lsgvaigavl sgfssaillt nsdvlrqmrg
      181 waagttasqs ledalsvvpl iaiglviafl straldvlal geasavamga rpnrirlval
      241 vaitllagga taatgpigfv gllaphlarm mvgphqgwit aysmflgtlv vavsdvlgri
      301 lssgevpvgv vtafigapvl iwmarrfrln el
//
LOCUS       WP_284813326             327 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium propinquum].
ACCESSION   WP_284813326
VERSION     WP_284813326.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..327
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35369
     Region          28..250
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mhdphstadq sqqeqasshp hphphpqrgr vaaffdldkt iiatssafay greflhngli
       61 tpqdalslsl akasymfagq ssaqmdstrd qltsmitgws ekhvrdivhe tmhtvlipai
      121 yseareliqa hqdaghevii isasarqlve piaeelgite visteleiid gaftgtvefy
      181 ckggakadai talvdergyd lehsyaysds atdapmlelv gypvavnpdr alkkialers
      241 weirsfkdpa plfqlpgake igigagllag ivalvtagtl ltkfyaqdkp aktakpaavs
      301 strtpaismp kgldwkflds wfkkssa
//
LOCUS       WP_284813422             460 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Corynebacterium sp.
            MSK297].
ACCESSION   WP_284813422
VERSION     WP_284813422.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..460
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48559
     Region          4..460
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 msenmkvdvl vigfgkagkt iamnraaagd rvalveqssa myggtcinig cvptkalltd
       61 aerhhakpta ddstafteai qrrgtltskm nqanldlaeg ngvivvdgha sfisekavev
      121 tggderleit getviintga epvvlplpga dlervidsta aqqlderpds llivgggpig
      181 mefatyfakf gtkvtvvdtv dkpfanfdrd iadhvgtimd dlgitwvtgv qvtefrenga
      241 davttvwkdd dgneqtaets hvlvavgrkp atkdlgldka gieltergav avdkhlrtnv
      301 egvyaagdvn ggpqftyvsf ddhrvilsdr wgdgsrtten rvvptttfid pplatvglge
      361 eaarkevegr gntldvkaad ikdipimprp kilgkpegra kilveretdh ivgatllcvd
      421 aqelintlal amsagisast vgsgiythps ssevfnallg
//
LOCUS       WP_284813415              95 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium sp. MSK297].
ACCESSION   WP_284813415
VERSION     WP_284813415.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 95)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 95)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 95)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..95
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=10264
     Region          12..78
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(17..18,22..24,37..39,48..51,53..54,57..58,60..61,
                     67..69,74..76)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(37,40,83)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mptdviantt aaatiiraln splrlqilhc lsqrdccvye lvrelgrsqp lvsqhlrilk
       61 esglvsshsc grevtyqltr realniaaia asiap
//
LOCUS       WP_284813432             276 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium sp.
            MSK297].
ACCESSION   WP_284813432
VERSION     WP_284813432.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..276
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29868
     Region          13..274
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtnqepltsf ekiadwpadn vaaalirdge vahtlgddeh vfavasvtkp vaaygfamav
       61 eegvfawdtp vgpegvtvrh llahasgigk daehpdrape drriyssagf evlqeklede
      121 tgmdcaeylk lglfeplgmn ntvlkgssgy alettaadla rfaqevleps lldpstvkem
      181 ltpqfadlrg ivpgygmqkp clwglgfeih gaknphwmgt elpdnavghf gmngsflwlv
      241 pttktallal tdkdfgewak plwaetndai wkelta
//
LOCUS       WP_284813435             394 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Corynebacterium
            propinquum].
ACCESSION   WP_284813435
VERSION     WP_284813435.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium propinquum
  ORGANISM  Corynebacterium propinquum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Corynebacterium propinquum"
                     /db_xref="taxon:43769"
     Protein         1..394
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42413
     Region          13..382
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 matdasttkq hdpaplagvr vldcsrvlag pfcamiladl gaevikvesp wgddtrqfgp
       61 yyegestyyr lfnrskksit ldfksengkq tlrelakrsd vvvenfrpgv lsklglsake
      121 lmaanpgliv tsisgfgqtg slakepaydl vaqamsglms itgwpegkpt rvgislgdiv
      181 pglyaaigtv salyqrvntg kgqhidlamy dslisvmesv gmralhgdtp psrigndhgl
      241 sapfstyatk dgdiviaitt nrlfdrlcea lglqhlaedq rfataenrsd yrddlreele
      301 krlaeltmge aialfeeygv ptarvyeldd alkspfaqer gvvaeesdgf atlasplkls
      361 gmtgpvpasg lgqfnddiqt wlsepvkneg hand
//
LOCUS       WP_284813457             155 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Corynebacterium sp.
            MSK297].
ACCESSION   WP_284813457
VERSION     WP_284813457.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK297
  ORGANISM  Corynebacterium sp. MSK297
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Corynebacterium sp. MSK297"
                     /db_xref="taxon:3050221"
     Protein         1..155
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=17086
     Region          90..>137
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mtgtstgaap pttarepehl trnrrvdaah tprrqnqmks iaqivqnnrr llaayedkvq
       61 prflsryare pmdaaavyrk lraldpgpda pardldlgcg tgwlahmlaa epryrraniv
      121 gydlspnair iareragmvy fctltkksai geagk
//
LOCUS       WP_284813627             335 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284813627
VERSION     WP_284813627.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..335
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36653
     Region          65..335
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 maaaatpaqr pktgprydaa verltnltfa lqgaaqsggn psrsaewiha nvagyhenkh
       61 nfrmqlqrdv atlaragvhi dssvgengas yrlnpesyrl pevsftpeea tvlgiasevg
      121 rnsglgalsa agwtklaasg arreitpgag ylainditsl dpevlrailt gvahklrisf
      181 nyqhhsgaei qrrtmdlwgi vphhnrlyvv gwdvdrqaer sfrstrisdi rrsrevatht
      241 epsgslreii ektlavrdva datirsrrqa appleeaade iqevdasdei rlfikgadre
      301 wlirtcaaya aeavveqpkd ireqvsrllq kagar
//
LOCUS       WP_284813716             305 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284813716
VERSION     WP_284813716.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..305
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34406
     Region          7..238
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mnhprptlwa vadlhaavra nrlrldeita rhpddwllva gdvaehldli stvlselrsr
       61 faqviwvpgn helfsrstda hrgrakydal vqicrsidvl tpedtfpvfg dttvvplftl
      121 ydysfrpagt gveealelaa qknvvmtdei aiapfadira wcwdrlaysi trlsrvngpt
      181 vlvnhwplvq eptlrmalpe lalwcgsrht rtwpqrynak avvyghlhmp aifeldgveh
      241 hevslgypre wgrsdqnriw pcpvlelaad pnggqiaqrv gleqcreshp elrmprrrgk
      301 gsdgv
//
LOCUS       WP_284813891             219 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium sp.
            UMB0012].
ACCESSION   WP_284813891
VERSION     WP_284813891.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB0012
  ORGANISM  Corynebacterium sp. UMB0012
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Corynebacterium sp. UMB0012"
                     /db_xref="taxon:3046344"
     Protein         1..219
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23366
     Region          10..219
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mpdslprptt elfpealnls pkqrevltav qrhpegakag tvaeelgmhv ntarghidel
       61 vnagavnvvs apskgrgrps lifqaripdn kavaeeyitl vevlttmlad keelddaasa
      121 kaleigrrwa raagadasdg aldtlfatlr dmgfdpatkp dstdielhac pfvssgieps
      181 pflcavhagf lqetshddts itlvprqrpn vcrlkikpa
//
LOCUS       WP_284813918             462 aa            linear   BCT 25-DEC-2024
DEFINITION  acid phosphatase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284813918
VERSION     WP_284813918.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130290
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..462
                     /product="acid phosphatase"
                     /EC_number="3.1.3.2"
                     /GO_function="GO:0003993 - acid phosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=50512
     Region          <139..341
                     /region_name="PAP2_acid_phosphatase"
                     /note="PAP2, bacterial acid phosphatase or class A
                     non-specific acid phosphatases. These enzymes catalyze
                     phosphomonoester hydrolysis, with optimal activity in low
                     pH conditions. They are secreted into the periplasmic
                     space, and their physiological role remains...; cd03397"
                     /db_xref="CDD:239491"
     Site            order(228,235,264..266,299,305,309)
                     /site_type="active"
                     /db_xref="CDD:239491"
ORIGIN      
        1 mktflisrrr atslltaaaa lavvagtpgl vqqhggtaha taaeaslqsl lhastthlal
       61 pfeipqlqlp apklssehde gaehsplssi gatpkhhdga pvpkpfdaty ltgyssdiss
      121 yqygiyyevv refkdlrsnh pdvmrknldi vadynnnaqp ervdkairda ladkdgvlft
      181 aaealgdefg qhflqalhek rlpktefllg ngyaaraggi aswgraekll fnndrpfvqa
      241 periqrhesp erelydgssk sfpsghtnqa twittllamm lpevgtqlla rgseagesrl
      301 vmgvhfpldv iggrmtgqaa aadrwndpkm rdallqaree ivaemewrag kpfaemiaed
      361 shalsdqqae adytrrmtyg ftpifvtdep vnvptaapal letrfpelsy eqraevlrqt
      421 alpsgypldd rdpakgdwqr inlarawnaq vsigaggevv vk
//
LOCUS       WP_284813925             232 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284813925
VERSION     WP_284813925.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..232
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=25367
     Region          1..223
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mlfdslprps eriapgvahl pgwlgvdkqs elvrevreia rryadtpmam lrptlksggq
       61 msvyqlhlgr ywhypsyryv dkiagttvpp vpdnlaalap valrtaagva eelapwvetf
      121 vpemvlvnyy ppgsgmgmhv defeesrapv islsigdeal frmghtesrt qpwddvtlcs
      181 gdlvvfggpk rfayhgvvrv ndatlpdgcg laegriniti rqvsaapklq gr
//
LOCUS       WP_284813939             394 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284813939
VERSION     WP_284813939.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..394
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42364
     Region          13..378
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 matdaslnkq hdpaplagvr vldcsrvlag pfcamiladl gaevikvesp wgddtrqfgp
       61 yyegestyyr lfnrskksit ldfksedgkq tlkelakrsd vvvenfrpgv lsklglsaeq
      121 lmavnpgliv tsisgfgqtg slakepaydl vaqamsglms itgwpegkpt rvgislgdiv
      181 pglyaaigtv salyqrvntg kgqhidlamy dslisvmesv gmralhgdtp psrigndhgl
      241 sapfstyatk dgdiviaitt nrlfdrlcea ldlqhlaedq rfataenrsd yrddlreele
      301 trlsdltmge aialfeehgv ptarvyeldd alksplaqer gvvatesdgf atlasplkls
      361 gmtgpvpasg lgqfnddies wlsepvkdeg qadd
//
LOCUS       WP_284813989             191 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase [unclassified
            Corynebacterium].
ACCESSION   WP_284813989
VERSION     WP_284813989.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..191
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=20913
     Region          35..135
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mhnpshqehr acvptseeme eryqsservw sgnpnetlvd yaakltpgta ldigcgegad
       61 alwlknhgwd vlgidfapta vartrargva aqvatfsdfs hepfdlvsvh yggvratpee
      121 veklerlvap ggtllyvhhd mesaeaampe wlaenlrele tveltrrerh ltegagahhq
      181 sdvvlvakra a
//
LOCUS       WP_284814098            1137 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Corynebacterium sp. UMB0012].
ACCESSION   WP_284814098
VERSION     WP_284814098.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB0012
  ORGANISM  Corynebacterium sp. UMB0012
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1137
                     /organism="Corynebacterium sp. UMB0012"
                     /db_xref="taxon:3046344"
     Protein         1..1137
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=118843
     Region          151..301
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <349..>456
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          567..1072
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 msvknassrg trrksnrsrp sgrsrsgagm petlamtssh rraaatsqer tgsafravgk
       61 glgvafsata rgmgnmargv shgvaglkps edvydteeye ttrepeeisa rgekkkkskv
      121 trardvaaee elstmeasee esrgiqvknp davalvligi aivlaatvwf gvagqvgawv
      181 gnivryviga gawvlpvalv alaislmmdi sgpaghfkpr ivggisiivl amlslihifa
      241 gtpelgftpd saggaggvig yaigglleta ftsfvavpll flviiygall vtgitireay
      301 elvadaiaaa fsrfggtded yydeegddly ghvtgdiddi aegrerserp arpvakrrss
      361 erggslrafr rpsedpaprg ssypvdspaa aeeeqatraf saptrggfqs vsnaaekpvs
      421 rdigdtdeip vvddaaasst aqpdsgdpep trvlgttrqr stspsarsat aagadagtaa
      481 gnaigsaaga aagaagaaga asgaaktaaa gaagaagaaa agaaagaags aveggadavs
      541 sahekarqlf rersgrdatt gaqvdstepa teaagetgts aapapsaqfg nenyavpttd
      601 lltpgtpake rteindriie aitdvfeefk vdaqvtgfsr gptvtryeie lgpgvkvski
      661 tnlqsnlaya vatdnlrllt pipgksavgi evpnpdremv hlrevldaps mtsspdpmli
      721 glgkdiegey tsfsvqkmph llvagatgsg ksafvnsmlv slltratpeq vrlilvdpkm
      781 veltpyegip hlitpiitqp kkaaaalqwl veemeqrymd mkaarvrkie dynrkvisge
      841 yqapagsere vrpypyivcv vdeladlmmt apkeiedsiv ritqkaraag ihlvlatqrp
      901 svdvvtglik tnvpsrlafa tssltdsrvi ldqggaekli gmgdglfipq gkrpvrmqga
      961 fvsddevmav vdaaksqaap nytegvteek qseakqeide eigkdmddll eavelvvtaq
     1021 lgstsmlqrk lrigfakagr lmdlmesrgv vgpsegskar evlvkpeeld tiiwmikgad
     1081 paeapkeiqe emqqqeqeea aatsdadssp ssdsspqgdd gdtrtvqaty npsagaf
//
LOCUS       WP_284814373             364 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284814373
VERSION     WP_284814373.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 364)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..364
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=37997
     Region          21..359
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mssqsqdtqa pasvdpgyrk lvvrtrwvsl hfptrlllta lglfalavig aiaaitlgey
       61 pldlgevita lfsggdgfdt tivrewrlpi avaavafgal lgiggaifqs ltrnplgspd
      121 iigfdagayt avvitmlvig tssfwsiaaa siiggiital avyvlawrkg vqgfrliivg
      181 igisamltsl nsylitradv eegmqvgfwa agsitkvtwq gllptlvlgv iviigaails
      241 rplrhlelgd daattqgfev nrarlllivv gvattalvta aagpisfial vapqiarrlm
      301 htagvsllga aamgavlltg ahvlsliiat fyrqipvgli tvviggmyml wllireskrh
      361 ygtg
//
LOCUS       WP_284814450             374 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284814450
VERSION     WP_284814450.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..374
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39594
     Region          74..371
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mklrnvavaa aaistlaltp vsgiaqpapq agiaqgavqq paaentipag tvseeilpae
       61 fddeswrqvi aekgnrvqev tvyspsmdrk ipvvtikade sagprptlyl lngagggeqs
      121 anwivqtdav dfylekninv vipmrgafsy ytdwneaptg skylqgpqkw etflinelpg
      181 pienylgang krgiagmsms atsslllaah npgmfdatgs fsgcaetnsp mgraavgltv
      241 nrggahpdqi wgpmgsqral endallqaef lrgtaiyvsn atgligeret aeglraqgip
      301 eqalsanqan laiagggiea vtnacthrfv aklnhlgipv hhhkpavgth twsywqddlr
      361 tswptfahaf gieq
//
LOCUS       WP_284814472             546 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Corynebacterium sp.
            UMB0012].
ACCESSION   WP_284814472
VERSION     WP_284814472.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB0012
  ORGANISM  Corynebacterium sp. UMB0012
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Corynebacterium sp. UMB0012"
                     /db_xref="taxon:3046344"
     Protein         1..546
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60435
     Region          265..477
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mknklcafss vlaltgvlga pmaaaqsslp gssfgsslgs slgssygssl gssegeaaqp
       61 kegegvgsrv lwkesfdevd tpawfthrap egwktdvqgv dsgearwkgw tfgdirhwtw
      121 aagtdmrhyf tqahdtfaii dnnqqrlaeg dsmtaglksp aisvagqdrv nvefdqhyrq
      181 gkegqnatvk vafdggeaqe iaafekdvfs khesigvdvp agaknmqvsf synngnddww
      241 wavdnvgvvk plgelkgspq aivdvlsdvq gdpqdykdav rqlngmedka galvlngdlv
      301 ddgsqeqwdd flaahseeph dsgkelwtig nhemygkegs etylerflky sgqdkpwkee
      361 vvdgvplisv ntefysdilr hgkepfqris keqldwlder laywdakgtp alvfshpllp
      421 qtvsmshsaw yqndfedlea lsnvvnkynn ivwfsshshs slrqnnwwgt rrydgtgeag
      481 rtgfpvvntg ailneylpdg dndekivkek eeastglrvk vfadrvrvea wdfksgemik
      541 yqdfar
//
LOCUS       WP_284814498             501 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium sp. UMB0012].
ACCESSION   WP_284814498
VERSION     WP_284814498.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB0012
  ORGANISM  Corynebacterium sp. UMB0012
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Corynebacterium sp. UMB0012"
                     /db_xref="taxon:3046344"
     Protein         1..501
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=54334
     Region          155..496
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 medsqetqgq apapaaarpq smwleglgqg egeeksskrr mfsqipqamp lrtwlvillv
       61 vvsglgitgs sfavnsimrn vlfnnvddel raasttward isndffigdh tkrppteyvv
      121 lnylpdgtir ysgpssttpn aeniplggyp ttvgsiennt kwralafads ngvitviakd
      181 mthekeilhg lamvqvtiaa ialaaiaavg fwfirralrp lrvvektasq iaagdldkrv
      241 pkwplhtevg qlaaalniml gqlqrsvvra qekeeqmrrf vgdashelrt pltslrgyte
      301 lyrsgatkdv dlvfskidde skrmsllved llaltraegt rldlrpvdll elalsvgssa
      361 raafpgreie vandaksipv vngdasrlhq vllnlvtngi rhggedatvt lrlrreandv
      421 lvdvsddgkg msqedaahif erfyradtsr trdtggsglg laivhslveq hggsisvdse
      481 lgrgttftvr lpaladapse p
//
LOCUS       WP_284814522             535 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Corynebacterium sp. UMB0012].
ACCESSION   WP_284814522
VERSION     WP_284814522.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB0012
  ORGANISM  Corynebacterium sp. UMB0012
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 535)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 535)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 535)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Corynebacterium sp. UMB0012"
                     /db_xref="taxon:3046344"
     Protein         1..535
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55934
     Region          8..534
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mlknpsvsal rvgiwliaig lfiaplalvv slalggnqip illeqglgia twnslfttvl
       61 salaaviigt viaialdrtd iygssllrlf llspllvppf igaiawiqlf gpnqglnrlf
      121 efeiwniyga dgvialmtih sfptayviis sslrsispdf elaarvsgas vmtvlrtvtl
      181 pllrpallsa ftltaianla dfgipaiigs parfetlatm iyrfidsgtv snplqvvsti
      241 gvvllflgig avimdyltsl knsssthdsg sparfalhsa rwpvtiimwv cglaisigpi
      301 lglayrallp apgvpftlet islanfssal snprvidglg nsaflsltaa licgilgwvi
      361 gilvtriqar gntlltlsal lpsalpglii gvawliagry tglyntiwii liayvcafta
      421 lvvqavrapl lstpvtveea arisgatplk alftttgamt ipaaisgavl vavtairelt
      481 isvllvapgt ttlgvqvfnl qqagnynqas alallfallg iiavaltira pkvrt
//
LOCUS       WP_284814529             636 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284814529
VERSION     WP_284814529.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 636)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 636)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..636
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=68146
     Region          14..623
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mhkrlrliaa lllvfsvvla grlawvqvvw gpdlsaraed qrariyvdpa rrggvvdreg
       61 kqiaytmqar sltvspttlr kelreqaqle sderlddeqk deyvnatllk msreipkmie
      121 easedkqdlk skdlldklra dtqyevlvrn vdpdiaaeis erfhgvaadh qdirqypnga
      181 igenvvgrvs mdgtgqfgle asrdstlsgi ngrstedvst ngqvipgtlr detpavdgkd
      241 iqltldldlq tfvqqqleqa knnsraesae avvldattge vlamantdti dpngdiakql
      301 edgkhfdnrs isfpyepgsv akiitaaaai eegittadev htvpgsiqia dvtvndawph
      361 gplpyttagi fgkssnvgtl qlaeklgqdk fdeylnkfgi gattgielpn essglrpars
      421 qwsgstfanl pigqgmswtt lqmasvfqtl anggervepr iiktsaedda kknagegnga
      481 ndnkvkdsdd angagasdde pektrvvske taktvvdmfr atvqadpagv nngtapdani
      541 egynisgktg taqkvdpntg aysnsaywit fagiapvddp rfvvaimlde pergvldggg
      601 gggsagplfh qiaswlldrd nvppsppgpe ltlqap
//
LOCUS       WP_284814602             769 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284814602
VERSION     WP_284814602.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 769)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 769)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 769)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..769
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=85119
     Region          23..765
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 msprrttgqq stgsqrtkrv hhsnysaela aeqsyvdalf gildsdvsqa rqrladaqlt
       61 idpanadsda llrreteyhr lqekldqlnl aqiglvfgri dvdakgenpt segldrryig
      121 riglmdrddd yrsllidwra pmarpfylat tanpegvrvr rhirtadrvv kdiddellsg
      181 tapgdadrad vageaallha mnsargehme sivetiqreq daiirdstrg vlvveggpgt
      241 gktavalhrv ayllytwreq lsrtgvliig pnptflnyis qvlpelgetg vvlstigrly
      301 pglhptlhdt adtrrvkgsl qmvdvlkaav kayqhvpkhs revvlegtrv eltptmvkta
      361 rtkarrsrkp hneareifsd qlqellaqgl aeiighdpld ggnllnsadi salhedisde
      421 aivdelvdef wpqlgprqvl rellsdhetl haacrgngge efasalwrse qgwsdsdaal
      481 ldelaqllgs gddeqqaaad eqewrealee aegaldilat sestdnddvf dseilsahhv
      541 idaetlarrq qardyrttae raegdrtwaf ghvvvdeaqe lsamewrmvf rrspnrwmtv
      601 vgdpaqtgsp agcdswseal epfvgkryrq hqltinyrtp veiaelaesi vhkyspdtav
      661 aqairnrkga vrwlpsgtsp eevrdqlrad etaasaeddt adqnqrsyai isahnaatyk
      721 glefdhviiv epeeiiaass rgwqdlyvac tratqtlsii gtldlagwn
//
LOCUS       WP_284814531             446 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284814531
VERSION     WP_284814531.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..446
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46586
     Region          17..427
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 msraggpaph prevvtrral vvwvagvacy ivaitgrtsf gvagveaiar fdvdasriav
       61 faavqlgvya laqiptglgi drfgpravvm fgavvmglgq fllalttsyp laivarvlig
      121 agdasaflav mrllpywfpl rktplftqlt gaigqtgqfi savpflallg sagwtgafvt
      181 lgatsillag laglaikdlp dvdrhaahas essmpvsgrd slrtrmrtll rtpvawqgff
      241 mhysclmfql vflmmwgfpl mtlgmglsaq qagavlaint vvtvfsgplh glfsarigav
      301 rhwavvgfsv tivltwavff asatprglaa ivvvnvival cassanygfd nvregvprev
      361 vatatglanm ggflagmaas qgigvvldis saggeyawgd fqvaalaagv vwavgvigll
      421 vasawrkypg pahrilphrl ralrsh
//
LOCUS       WP_284814685             478 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 32 protein [Corynebacterium sp.
            UMB0012].
ACCESSION   WP_284814685
VERSION     WP_284814685.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB0012
  ORGANISM  Corynebacterium sp. UMB0012
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Corynebacterium sp. UMB0012"
                     /db_xref="taxon:3046344"
     Protein         1..478
                     /product="glycoside hydrolase family 32 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52741
     Region          9..467
                     /region_name="SacC"
                     /note="Sucrose-6-phosphate hydrolase SacC, GH32 family
                     [Carbohydrate transport and metabolism]; COG1621"
                     /db_xref="CDD:441228"
ORIGIN      
        1 msepiqlsnd rwypqfhita psgwindpng lsffngryha ffqhhpysat wgpmhwghvs
       61 stdliswqhe pialapgepn eddadgiwsg savvhddtly afytgnrwvn svddsegkyq
      121 tqmlatstdg ihftkhgavv ppvaadardp kvfwvkdrwy mtigasiddr ghvrlysspd
      181 llnwtgegsl fedpdstvfm iecpdffplg dkwvllygpm vnkpvrsgya lrnghnagyv
      241 vgswtpgekf vpetsyrpld wghhfyatqs meapdgrria fgwmgefanp lgtqadgwsg
      301 qlaipreltl dddltlvstp arelsalfas ptthnhslga nkgfevsdip aaklsvkvdl
      361 dkdvplqvpt ceqvvlsfkr gsssatklvf dtlarrvhlv hgddndagrg yrsapwtpge
      421 dltvyldkgs ieafigegre tlssldfkge gnrtlsvetv ngpadvtvdi aaltherd
//
LOCUS       WP_284814737             325 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Corynebacterium sp.
            UMB0012].
ACCESSION   WP_284814737
VERSION     WP_284814737.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB0012
  ORGANISM  Corynebacterium sp. UMB0012
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Corynebacterium sp. UMB0012"
                     /db_xref="taxon:3046344"
     Protein         1..325
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34429
     Region          2..319
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(40..41,45,118,122,125,143,146..148,167..168,172,187,
                     210..211,232..236,257..260,307,309)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(130,225..226,239..244,252..259,262..263)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mhaiqvtetg gpevlrytev paptpnddev lvdvimagvn yidtyyregi ynaatpfipg
       61 fegtgrvvhd pkgeiaegtm vawnqafgsy aeqvcvprea lvavpddfqp evaasmllqg
      121 itahylahgv yqlaegascl itagaggvgq iltqmasslg atvytvvstd ekeelsyaag
      181 adkvfrygdg laeqvrryng dkgvdvvydg vgkatfqesl eavrprgtva lfgaasgpve
      241 pidpqllnkh gsifltrpsi gawtaqegef qmraqavvqa vidgdlsfnv tasypledaa
      301 aahrdlqerk ttgsivlrvq agdka
//
LOCUS       WP_284814811             668 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD/NAD(P)-binding protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284814811
VERSION     WP_284814811.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 668)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11816065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..668
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72139
     Region          6..632
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
     Region          7..228
                     /region_name="NAD_binding_9"
                     /note="FAD-NAD(P)-binding; pfam13454"
                     /db_xref="CDD:433222"
ORIGIN      
        1 mtatqialig agprgisvle rlaaylrdss ssgqaqtktq avrpqitihi vddsqigagr
       61 vwdttqtrtl cmntladavt lftepgstvg asvlsgptly ewirlvrgdd llaaftagnl
      121 nydtnaqvvq ekealfrahp prkglandyh eelvgtveqs npsralygey lrwvyqvvla
      181 hlpdsvevie hnsravdmyt vpdsantdvi tladgtsfsa hatvlatgwv lnadndeqhq
      241 lraasqaehl twispnnpve qpvdniaaek pvlvrglgmg ffdllalctl grggsfdvdp
      301 ttrsglryra ngkephfvvs srrgypflpk sdygslppka hmprlhnalq avqkqeridf
      361 sidlapaiir daieafyatl srlapesilt stedintvld stpvyvlldp hglsgvlarh
      421 tteicnlqpy lhprvestqq vaeamardid ealkgsnspi kaalwvfasc rkhvgiagsq
      481 gkfmtdsatp tlsqimalgq mvgsgpplfr sqqllalvda glveflgaqp rltigsaeft
      541 ltcgsgvsar qasattlvda wlpkpdvrfp adplsqalfa sgrirpfsid gveqgspeta
      601 yttrrtirpd gsedsrlhii gipthaqmpd ttispmpgtd pimlqetdkt arsvhaiiqg
      661 lrdeapqp
//
LOCUS       WP_284815238             327 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284815238
VERSION     WP_284815238.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..327
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33835
     Region          22..326
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mrktwtiagi saatllvalv gsltvgsssm sfseliglvv psqpspsplr tsiltelrip
       61 rilmaafvga ilavcgvamq avthndlaep yllgvssgas tgavvailfs twqygiifga
      121 tigslasfal lmlllrntgg datkvvltgv ligflfqslt slvvtasgda estrsimfwl
      181 lgvlgaarwp tlfavmivgs igmlvlwals rhldalslgg dtastmgvpv valryivlic
      241 vslmtattva svgaigfvgl iiphairmln vpkhaslipl salvgavtlv iadafarsif
      301 apqelpvgvi taligvpmff lilrrkh
//
LOCUS       WP_284815306             435 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: MFS transporter [unclassified Corynebacterium].
ACCESSION   WP_284815306
VERSION     WP_284815306.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46115
     Region          17..383
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mshpnprevi ttqalgiwva amavylvait grtsfgvagl daierfdvda griavftsvq
       61 lgvyalaqip tgilidkfgp rlllvvgavi mgigqvvlgf ttsygvaiaa rvligagdat
      121 aflsvmrilp ywfplhrtpm ftqvtsslgq mgqfisavpf lwllgaagwt aafvtlgavg
      181 ilvaiaaiva vadspeklgi iptekeppns qatsiparlk tvfrspvawq ayfihyigml
      241 plivfvmlwg mpmmtqgmem skaksslvlt llavflvlvg plhgkissra qhvrpwlslg
      301 fvaihvltwl ifftfgtdsg vvailvvsfv talctptany gfdivrermd rsvvatatgl
      361 gnmggftsgm lgaqlfgmvl dhssdapdys mpdftaaaaa vlavwvvgmi gviithflrr
      421 ragedgpsvt ivevs
//
LOCUS       WP_284815385             376 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284815385
VERSION     WP_284815385.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..376
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39251
     Region          63..370
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtqnsnkttt apsaaraatt arhrrenpra pqqhhdvfaq rhrlrvgtfv alivllvgsv
       61 llstalgqyy lslpdllsil tsgpraetdi aasvvwdirl priflgflvg aalgvagclm
      121 qavfanplae psivgvtsga gvgaalvivf evsflgtftv paaafltsli vtaiiyrlah
      181 nrgkvavvnl iltgiavnav cgalisfmvy lapttsreqi ifwqmgslng sqwkhvwvvl
      241 piviigfaia srlgaqldvl algekaaght ginvavlrmv aivasavlta aavsfaglig
      301 fvglivphvl rtivgpenki llpasalaga llialadvaa rtlipfadlp igiftalvgg
      361 ptffillrrm mrkgsv
//
LOCUS       WP_284815795             461 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium sp. UMB0012].
ACCESSION   WP_284815795
VERSION     WP_284815795.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB0012
  ORGANISM  Corynebacterium sp. UMB0012
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Corynebacterium sp. UMB0012"
                     /db_xref="taxon:3046344"
     Protein         1..461
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=49376
     Region          8..402
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mtisthgals rlhkfagvii apflivaals gflyalaptf epwiyhdevt ataqgsprsl
       61 deqiaaaqrq hpdgtvvrve psedpqettr vlfddptapn ssythavfvd pvdlhitgel
      121 qqyggsralp frtwasdghr tlwlgepgrl yaelaaswlg alsilglylw lkrkqknrkr
      181 lskpltlhar vgawllpgfl fltvtgltws lvagtaigkv reelnwkeps vatsvaevga
      241 stetgersgh aghkghggha ghagheggak pvgaqtalsa arsqgltgvl emtppekpgd
      301 awgvrearaa fklrsdavav tpngevidri nsadwplaaq ltswliqlhm gtlfgiysqi
      361 alaalalgll vvsiaglrmw wikprrglpe lkitpavlag vmaysiiapl fgaslviffl
      421 gdwivrrlra pqrgrgaaag ettprprges ssrslstdrs g
//
LOCUS       WP_284815918             332 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium sp. UMB0012].
ACCESSION   WP_284815918
VERSION     WP_284815918.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB0012
  ORGANISM  Corynebacterium sp. UMB0012
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 332)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18950610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Corynebacterium sp. UMB0012"
                     /db_xref="taxon:3046344"
     Protein         1..332
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=36853
     Region          40..163
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
     Region          176..319
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mpnikkmhet dkdqqheefi sgrhqeipvd pakefhrttl aagaviwrgs pqdpeialih
       61 rphyddwslp kgkvdpgesl pttaareile etgfsvrlgk ligkvtypvq grtkvvyywv
      121 akylggtysa nsetdelrwl pideaqdlls ydvdtavvak aakrlriapa trvlyvrhar
      181 ahkssswqgd dnlrpldkkg rrqaemlvpm lsafqptaiy salpqrcqqt aapladelgk
      241 disinknfgd eawendpeaa kkafrrvvnd ggvpvivsqg atipgiiedl apkflkkpvd
      301 klkfkkasvw vlsfndgelt gadylasplp vr
//
LOCUS       WP_284815973             364 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Corynebacterium sp. UMB0012].
ACCESSION   WP_284815973
VERSION     WP_284815973.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB0012
  ORGANISM  Corynebacterium sp. UMB0012
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 364)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Corynebacterium sp. UMB0012"
                     /db_xref="taxon:3046344"
     Protein         1..364
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39404
     Region          62..345
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mksrfrsrfl pqvelssqpd halidvitvp rdensspwrq lgkrvlwafg ivvfvtivvy
       61 vdgggysedm slldsayyaa vslttvgygd ivpvspqarl inlvlitpar liflvllvga
      121 tlsvltdkar rtfqiqnwrk qlrnhtvvig ygtkgagava alladdvpss qivvidtnra
      181 slahaehhgl vtifgsgtkq dvlkvagveh assivvtpst ddtavlccls vrelapkaki
      241 vasvresenr hlllqsgads vvtsaetagr llglatvtpt vvemmedlls pnegfsvaer
      301 avrefevgsn prhladivla vlrnnelhrv dtadasalkp gdrllyikhe meqpievmdd
      361 dded
//
LOCUS       WP_284815994             375 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [Corynebacterium].
ACCESSION   WP_284815994
VERSION     WP_284815994.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..375
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40025
     Region          7..368
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mnhgpglafr flaaqvlvvv isllvaaava tmvgptlfhd hmlmtgredp slelfhaeqa
       61 yrganlitla vslptalisa llaslwlsrr lrtplqdltr aatsltagns rirvpagkag
      121 pevttlahaf ntmadrleht eqvrrqmlsd lahemgtpls vltvyldglq dgvvdwnnat
      181 htimadqltr ltrlmedidd vsraqehrid ldlaeeglgd llhtaavaag eayadkgvdl
      241 qvesitdtar vlvdrqrfgq vmsnllsnal rhtpaggqvr isvhrqgast vlihvaddge
      301 gippdqlghi ferfyrgdaa rsrdnggagi gltiskalie ahggtltats pgpgrgavfa
      361 lrlplsppds eeaar
//
LOCUS       WP_284816245              82 aa            linear   BCT 25-DEC-2024
DEFINITION  pyrroline-5-carboxylate reductase family protein, partial
            [Corynebacterium sp. UMB0012].
ACCESSION   WP_284816245
VERSION     WP_284816245.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB0012
  ORGANISM  Corynebacterium sp. UMB0012
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Corynebacterium sp. UMB0012"
                     /db_xref="taxon:3046344"
     Protein         <1..>82
                     /product="pyrroline-5-carboxylate reductase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004735 - pyrroline-5-carboxylate
                     reductase activity [Evidence IEA]"
                     /GO_process="GO:0055129 - L-proline biosynthetic process
                     [Evidence IEA]"
     Region          <1..>71
                     /region_name="ProC"
                     /note="Pyrroline-5-carboxylate reductase [Amino acid
                     transport and metabolism]; COG0345"
                     /db_xref="CDD:440114"
ORIGIN      
        1 vtygrfvdde qrqtvdella aagevvtvte pqidavtavs gsgpayfflv teamvdagvs
       61 lglprdlaer lakataagag am
//
LOCUS       WP_284816387             232 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284816387
VERSION     WP_284816387.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..232
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=25339
     Region          1..223
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mlfdslprps eriapgvahl pgwlgvdkqa elvrevreia rtyadtpmam lrptlksggq
       61 msvyqlhlgr ywhypsyryv dkisgvtvpp vpeslaalap valraaaeva eelapwvetf
      121 vpemvlvnyy ppgsgmgmhv defeesrapv islsigdeal frmghtesrt qpwddvtlcs
      181 gdlvvfggpk rfayhgvvrv ndatlpdgcg laegriniti rqvsaapklq gr
//
LOCUS       WP_284816411             276 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284816411
VERSION     WP_284816411.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..276
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29872
     Region          13..276
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtnqepltsf ekiadwpvdn vaaalirgge lahtlgddeh vfavasvtkp vaaygfamav
       61 eegvfeletp vgpegstvrh llahasgigk daanpdrape drriyssagf evlqekleee
      121 tgmdfaeylk lglfeplgmn ntvlkgssgy alettaadla rfaqevlaps lldpstvkem
      181 ltpqfadlrg ivpgygmqkp clwglgfeih gtkdphwmgs elpdnavghf gmngsyiwll
      241 pdekiallal tdkdfgewak plwaetndai wqelqg
//
LOCUS       WP_284816456             446 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284816456
VERSION     WP_284816456.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..446
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46561
     Region          17..427
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 msraggsaph prevvtrral vvwvagvacy ivaitgrtsf gvagveaiar fdvdasriav
       61 faavqlgvya laqiptglgi drfgpravvm fgavvmglgq fllalttsyp laivarvlig
      121 agdasaflav mrllpywfpl rktplftqlt gaigqtgqfi savpflallg sagwtgafvt
      181 lgatsillag laglaikdlp dvdrhaahas esgtaasrrd slrtrmrtll rtpvawqgff
      241 mhysclmfql vflmmwgfpl mtlgmglsaq qagavlaint vvtvfsgplh glfsarigav
      301 rhwavvgfsv tivltwavff asatprglaa ivvvnvival cassanygfd nvregvprev
      361 vatatglanm ggflagmaas qgigvvldis saggeyawgd fqvaalaagv vwavgvigll
      421 vasawrkypg pahrilphrl ralrsh
//
LOCUS       WP_284816544             364 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284816544
VERSION     WP_284816544.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 364)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..364
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=37996
     Region          21..359
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mssqsqdtqa pasvdpgyrk lvvrtrwvsl hfptrlllta lglfalavig aiaaitlgey
       61 pldlgevita lfsggdgfdt tivrewrlpi avaavafgal lgiggaifqs ltrnplgspd
      121 iigfdagayt avvitmlvig tsnfwsiaaa siiggiital avyvlawrkg vqgfrliivg
      181 igisamltsl nsylitradv eegmqvgfwa agsitkvtwq gllptlvlgv iviigaails
      241 rplqhlelgd daattqgfev nrarlllivv gvattalvta aagpisfial vapqiarrlm
      301 htagvsllga aamgavlltg ahvlsliiat fyrqipvgli tvviggmyml wllireskrh
      361 ygtg
//
LOCUS       WP_284816556             324 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284816556
VERSION     WP_284816556.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..324
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33782
     Region          1..289
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 massanpisv lciigscisl qlgsalavkl fddggtwgts avrllvaavv llaitrprvh
       61 ewnrqqwagv lglglslglm ngffyagidl vplgpavtie flgplllaaf lsrsvrdgic
      121 vvlamtgmal lgldafngnp lnplgvafll gaalfwaiyi lanknagalv pgqgglavaf
      181 vvggvamlpm gadgawnlvt stdtlwfaig tgilgslvpy slelialrgl apnvfsilis
      241 lepvfaaffg wlllaqnist lklvaigvvi aasvvqtvgp krsgedgepr aklkklqdig
      301 kkvatkrtek rlrtearsrk knld
//
LOCUS       WP_284816654             668 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD/NAD(P)-binding protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284816654
VERSION     WP_284816654.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 668)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11816065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..668
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72115
     Region          6..632
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
     Region          7..228
                     /region_name="NAD_binding_9"
                     /note="FAD-NAD(P)-binding; pfam13454"
                     /db_xref="CDD:433222"
ORIGIN      
        1 mtatqialig agprgisvle rlaaylrdss scgqaqtktq avrpqitihi vddsqigagr
       61 vwdttqtrtl cmntladavt lftepgstvg asvlsgptly ewirlvrgdd llaaftagnl
      121 nydtnaqvvq ekealfrahp trkglandyh eelvgtveqs npsralygey lrwvyqvvla
      181 hlpdsvevie hnsraidmht apgntntdvi tladgtsfsa hatvlatgwv lnadndeqhq
      241 lraasqaehl twispnnpve qpvdniaaek pvlvrglgmg ffdllalctl grggsfdvdp
      301 ttrsglryra ngkephfvvs srrgypflpk sdygslppka hmprlhnalq avqeqeridf
      361 sidlapaiir daiqafyatl srlapesilt stedintvld stpvyvlldp halsgvlarh
      421 tteicnlqpy lhprvestqq vaeamardid ealkgsnspi kaalwvfasc rkhvgiagsq
      481 gkfmadsatp tlsqimalgq mvgsgpplfr sqqllalvda glveflgaqp rltigsaeft
      541 ltcgsgvsar qasattlvda wlpkpdirfp adplsqalfa sgrirpfsid gveqgspeta
      601 yttrrtirpd gsqdsrlhii gipthaqmpd ttispmpgtd pimlqetdkt arsvhaiiqg
      661 lrdeapqp
//
LOCUS       WP_284816704             337 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284816704
VERSION     WP_284816704.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..337
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35618
     Region          24..332
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkkslatali agvavlfgai algpqriala dqatgnkrla aelaelavpg hnqltaltin
       61 dgvteyagwg adseteveig svtkmmtael lrheienkev eldttlgeli delhepvasv
      121 tleeavnhtg glprmagvnf asnlgfsvlg tnpyqgigrd dvfaaandie elenrgeeqy
      181 snlgfallgw alaenagtty eemlndvlfr plgmhntyva sqplpddqpa gllnngrhaq
      241 pwvtegyapa gmvrstaadm akfaeylleq glpdygwapt vstddkdsga gwhngqtggy
      301 samlvvapet araafvagnt prgveqiglq lageevr
//
LOCUS       WP_284817352             239 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284817352
VERSION     WP_284817352.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..239
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25495
     Region          76..221
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mskkvtnpnq kssagfigai vavlvivvav ivyiviagqg akaekfanwe ikqvsaetsf
       61 dgntltfgaa dkaphvdlye dfscphcahl aeatdaeale einagnlavs ihpmtfldnq
      121 gdghstqava allalaehdd vnalwnlrea mfenqqdiar swgpddfada aaqmeasdea
      181 vedirsgkfl ekareagean gkdleskvgr vstprvlmdg kdlevedind wvkvavask
//
LOCUS       WP_284817188             531 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284817188
VERSION     WP_284817188.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..531
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=55293
     Region          10..247
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mspsqnslkl nytaasdrgl vrtnnedsaf agrnllvlad gmgghaagev asqllvttmq
       61 rldrdpgend mlallgtaad daniaiadtv rqrpetqgmg ttctalmfng ttfgmchvgd
      121 srgyrlrggk leqitiddty vqslvdsgsl kpedvsthpq kslilkaytg rpvdptlrmi
      181 daqpgdrlll csdglsdpvt adtieqtlke gtpeqaaskl idlalrsggp dnvtvvvadv
      241 lagddestti ptapvsagal alpeaerahp ntaagraaal nrrpqvvepk aqaagahnhg
      301 tganagngsg pgngagtgaa sgawaggsag aaennahdna skrgrnwtlt ivvlvllggl
      361 igggwwvyas sqdkyyiatn dsdeliierg vdyslfgkdl hepyqrvclt kddevrttdl
      421 gekpsndchp fsltdlpgsv rgsithldsg sysevtdqlq rlsdkalpvc vnraetdnng
      481 knnegknsdg nsnnsgankd tnkdtnkdaa naesaddggl stpgvncrev s
//
LOCUS       WP_284817497             313 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium sp.
            UMB10119B.1].
ACCESSION   WP_284817497
VERSION     WP_284817497.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB10119B.1
  ORGANISM  Corynebacterium sp. UMB10119B.1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Corynebacterium sp. UMB10119B.1"
                     /db_xref="taxon:3050601"
     Protein         1..313
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34307
     Region          12..313
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mkqntaverq vrlarllnll sylsqhpdrs pmeiardigt daeqvksdla mlhltgvgng
       61 pgemidlkhs wtevtviddq glsrplrltp teantlllll dsfetmpgll dqaalssaae
      121 klravvgsts vldadgeqsd qesilgilqs glqqgvqvqv tyfspssdtl rerqltgirf
      181 fhqgghtyft aldegeeksf rtdrireaql tevpadrsav gktfdgsdpf gfdseniatl
      241 lvssdatwla dyweieigda yddgrieatm vygsadwlir fclsqgdrie lvgppelaae
      301 arrrafsgle ale
//
LOCUS       WP_284817530             212 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Corynebacterium sp. UMB10119B.1].
ACCESSION   WP_284817530
VERSION     WP_284817530.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB10119B.1
  ORGANISM  Corynebacterium sp. UMB10119B.1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Corynebacterium sp. UMB10119B.1"
                     /db_xref="taxon:3050601"
     Protein         1..212
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22066
     Region          19..121
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mallsyvpri lpspstansq ttgrivvalh gtgsspfvfr rlahalekhg igliapgygh
       61 ratagidass keiaafldsl aaqqvdvvgh sygaliglra vqlseiaarc gtivglgasw
      121 rgthgiarlf ppglvravag dafvelehfr eepvapsgte ivsivsdtdr ivpawssrwg
      181 dvievpgvph aalplrtnei laalrvapsd hs
//
LOCUS       WP_284817649             590 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Corynebacterium sp. UMB10119B.1].
ACCESSION   WP_284817649
VERSION     WP_284817649.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB10119B.1
  ORGANISM  Corynebacterium sp. UMB10119B.1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Corynebacterium sp. UMB10119B.1"
                     /db_xref="taxon:3050601"
     Protein         1..590
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62648
     Region          9..465
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          523..589
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(546,555..557,564)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            556
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mpihnqqvtk vlvanrgeia vriiraaqde giasvavyad sdaatpyvsl adeafalgge
       61 taaetyldma kllkvaadsg adavhpgygf laenaefaqk vidagltwig pspeaiatlg
      121 dkvaaraiae avdapmapgt khpvadeqev lafadehglp iaikaayggg grgmkvahtr
      181 eeipelfesa treavaafgr gecfveryld karhveaqvl adqhgnvvvv gtrdcslqrr
      241 fqklieeapa pfltdeqrer iersaeaick eagysgagtv eylvgadglv sflevntrlq
      301 vehpvteltt dldlvreqfr iargeqlsit etptprghaf efringedpt infmpspgpi
      361 nvyrepagpg vrvdsgvreg saingqfdsm laklivygat reealnrarr alaeyvvegi
      421 ptvipfhram vehdafigdg tsfdvytrwi eetwdgempa vtaadgegve geagvdkqvf
      481 avevdgrrie valpsalvpg agparkpkkr rasaaktaas gdavtapmqg tlikvnvaeg
      541 dtvaegdvlv vleamkmenp vkahkdgvvt glaaeqgaqa akgatlmelk
//
LOCUS       WP_284817668             631 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD/NAD(P)-binding protein [Corynebacterium sp. UMB10119B.1].
ACCESSION   WP_284817668
VERSION     WP_284817668.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB10119B.1
  ORGANISM  Corynebacterium sp. UMB10119B.1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11816065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Corynebacterium sp. UMB10119B.1"
                     /db_xref="taxon:3050601"
     Protein         1..631
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=67060
     Region          1..603
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
     Region          6..198
                     /region_name="NAD_binding_9"
                     /note="FAD-NAD(P)-binding; pfam13454"
                     /db_xref="CDD:433222"
ORIGIN      
        1 mqpaiaivga gprgisiier vaatlnesns tqsltihlid daqhgagrvw dttqthtlcm
       61 ntlagavtlf tepgatvtap vlegptmyew iqllrgerda vsatkqslfd ahptpdhvta
      121 dfgaelaatr pesnpsraly geylhwgltv alaqlpehvt vtnhrsraqr itaenghdai
      181 tledgttvha datvlatgwv vpehpvafrg hwiqpgnpve qdvdtlvage taivrglgmg
      241 ffdlmalsti nrggrfvpad trsglryeps gaephlvvts grgypylpks eyhslppkad
      301 lsrlraaieq hsgtttvsfg eqlwpalird syaayyttla rvrpdalrip ladiisrida
      361 aplagaatrt sllpcaraln daladattep fdvsywidpl agcdgldaes lncviadala
      421 rdiaeavaah nspiksalwv isagrkptai avengrgtpe dqrgalsdym afgqmvgsgp
      481 plfrsrella lidaglvtll gptptvtqsg ttftatster tvtadtlada flpspnitra
      541 adpltaslle serirpfapf gtptgspetd adtrrtvhpd gtldprlhia giptgkqwad
      601 ttispmpgtd prmlqetdlt aqsllpqagv r
//
LOCUS       WP_284817795             394 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284817795
VERSION     WP_284817795.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..394
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42517
     Region          13..378
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 matdaslnkq hdpaplagvr vldcsrvlag pfcamiladl gaevikvesp wgddtrqfgp
       61 yyegestyyr lfnrskksit ldfksedgkr tlkelakrsd vvvenfrpgv lsklgisaeq
      121 lmavnpgliv tsisgfgqtg slakepaydl vaqamsglms itgwpegkpt rvgislgdiv
      181 pglyaaigtv salyqrvntg kgqhidlamy dslisvmesv gmralhgdtp psrigndhgl
      241 sapfstyatk dgdiviaitt nrlfdrlcea lelqhlaedq rfataenrsd yrddlreele
      301 krlteltmae aialfeehgv ptarvyeldd alkspfaqer gvvatesdgf atlasplkls
      361 gmtgpvpasg lgqfnddies wlsepvkdeg hand
//
LOCUS       WP_284817859             422 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium sp.
            UMB10119B.1].
ACCESSION   WP_284817859
VERSION     WP_284817859.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB10119B.1
  ORGANISM  Corynebacterium sp. UMB10119B.1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Corynebacterium sp. UMB10119B.1"
                     /db_xref="taxon:3050601"
     Protein         1..422
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=44690
     Region          1..419
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrlsvvgagy lgathaacma elghevlavd tdarkvaalq sgsapffepg ldtllqrhta
       61 sgrlrfttdl revagfarvh flavgtpqvs gglaadtsfl ddatsrlaai legehlvvgk
      121 stvpvgtahr lqerlpgave vawnpeflre ghavkdtlap drivvgqrpg graeqvlrev
      181 yatpieqgsp vvvtdlptae lvkvaanafl atkisfinav aevcdaagad vtqladaigm
      241 dgrigrqfln aglgfgggcl pkdvrafiar aeelgagdsl rflrevdain qgrrarvvdl
      301 arrelgtleg rtiavlgaaf kpnsddirds paldvaqrlh dtgahvrvyd pkaldnaraa
      361 ypdldfpgtl tlatagadlc ilatewdafl eplvgvdkrv iidarnaldv ptwqlagwrv
      421 ir
//
LOCUS       WP_284818043             517 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284818043
VERSION     WP_284818043.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..517
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54930
     Region          17..514
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mssgfarssf ahnggarvav igagpnglta aavlaqagcr vevfesaddi ggsartypaf
       61 gagsavdfga aahpfgavsp vfrqlgleny glewkhpqyp mahplvdapa vllhrdlkst
      121 aaqfsdhder vwnhlhkplv ddvgklvnsv lpvrprypla larlglrgvw parsltsrll
      181 vdeparallv gsavhairpp sqpgtaafgl lfnslgmttg wpvvsggtgq lvmalarvik
      241 hyggtiktga eiqdlsvfat ydavvttqtp rqllalqgle lsrlrsrslr rwkygtavyk
      301 vdylvngpvr wndprvagag tvhvggtvse mqlaesqaaa gtlperpfvm vcqqqaadpt
      361 rfsgnrrsvg agrvlsaqld agrmpedarl philwayahv phgyqekfpg evaglietqi
      421 sryasgfsaq iierhqaspg qlqeananli ggdiangamn laqmlrqrqy vgtltmnpev
      481 pvvqasgasl pgagvhgmag wraaqtilrr fgatelr
//
LOCUS       WP_284818065             729 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium sp.
            UMB10119B.1].
ACCESSION   WP_284818065
VERSION     WP_284818065.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB10119B.1
  ORGANISM  Corynebacterium sp. UMB10119B.1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 729)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 729)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Corynebacterium sp. UMB10119B.1"
                     /db_xref="taxon:3050601"
     Protein         1..729
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76576
     Region          4..727
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msnaqielgv sgmtctscss rvqrklnkme gveasvnfst etasveydpa ladpdalikt
       61 irnagydaft vtdadepldd apseperdtl lwtivwsaav slpvmlvsmi palqfpywqw
      121 aafaattlvy fsagslfhra tlvnlrhgsm tmdtlismgt taaygwsiya lffgnagepg
      181 mrmrmslvpn sagmdevyle tvcvvitfll lgrwfenrak grssealrnl lhmgakdatv
      241 lrdgvetrvp iadvkvgdtf vvrpgekvat dgtvvegrsa idasmltges vpvdvkegdd
      301 vtgatlnthg rllvqatrvg sdttlaqmgq lvkdaqagka pverlvdria qifvptviai
      361 savslvvhll ldysvaaaft aavavliiac pcalglatpt ailvgtgrga elgllirgpe
      421 ilestrqvdt ivmdktgtvt tgemtvvdan gssdalalaa aveahsehpi araitayvqd
      481 artesvtdfr nepgigasat vdgkhvrvgr psgdlgeyrg afdameatga tvvavevdga
      541 legviavrda vkedsrvgve klkelgleph lltgdnrata lavakevgid aanvtagvlp
      601 adkvelvrsl qdagkrvami gdgvndaaal aqadlgmamg agtdvaieas ditlmnnslv
      661 saadgirlsr atlrtikgnl fwafaynvvl ipvaaiglln pllagiamaf ssvfvvtnsl
      721 rlrrfratr
//
LOCUS       WP_284818136             161 aa            linear   BCT 25-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284818136
VERSION     WP_284818136.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Schwartz,C.J., Giel,J.L., Patschkowski,T., Luther,C., Ruzicka,F.J.,
            Beinert,H. and Kiley,P.J.
  TITLE     IscR, an Fe-S cluster-containing transcription factor, represses
            expression of Escherichia coli genes encoding Fe-S cluster assembly
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 98 (26), 14895-14900 (2001)
   PUBMED   11742080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..161
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=16852
     Region          2..137
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mhlttfadlg lrtlmvlgdl qpgqrvtisd latringstn hvakvnarlv elgwvaavrg
       61 rnggvyladd trqasvgkil rqlegpgevv dceggqscpl tsrdcalrsr laaareaffa
      121 eldgdtigdl iantapapfg enptrqalgl prtqqssgvt a
//
LOCUS       WP_284818372             526 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Corynebacterium sp. UMB10119B.1].
ACCESSION   WP_284818372
VERSION     WP_284818372.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB10119B.1
  ORGANISM  Corynebacterium sp. UMB10119B.1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Corynebacterium sp. UMB10119B.1"
                     /db_xref="taxon:3050601"
     Protein         1..526
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55816
     Region          128..517
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mstpvmhess alsdgelaks pepgewrrqr iglilgvlla vlvyyifpds aadtvlqssg
       61 adpettydad vmrvvaattv lmaawwmtea iplaatallp iaifpvmgva kfsavsgpya
      121 satiflfmgg flmalglqrw nlhrrlalvv vrivgtspkr iilgfmlatg fmsmwvsnta
      181 tavvmlpigv svltltadsv ggmqnqkkfa tslmlaiays astgslgtli gtppnallag
      241 ymkeahditi gfgqwmlvgm pmailltvia wfvlinvfkp eidripggke lideeyrklg
      301 awtfpqvavg iifliaalaw ifiplgikqf gwefpyndai vgiiagllmf ivpgtkqgkr
      361 lmdwetanem pwdvlllfgg glslsamfts tglslwigea akglavlpti llimavaalv
      421 lglteltsnt ataatflpim ggvavgiglt eatemnilll aipvalsatc afmlpvatpp
      481 naiayssgyv tmgemlkggl wlniislgli tvvtyflavp vfglvl
//
LOCUS       WP_284818413             333 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium sp.
            UMB10119B.1].
ACCESSION   WP_284818413
VERSION     WP_284818413.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. UMB10119B.1
  ORGANISM  Corynebacterium sp. UMB10119B.1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Corynebacterium sp. UMB10119B.1"
                     /db_xref="taxon:3050601"
     Protein         1..333
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35031
     Region          30..306
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mskaptkslp kgllvafail avvvlfvvdl cvgpadikls nfsavldpds vehiaffrmr
       61 mpaalmavgv gmslglagav mqtilnnpla spftlgvssa aslgaaivfv mavpmvfvtg
      121 galllallsv lvifavgkyi emsnsslvla gialnflfda flsliqyras eeslsyivfw
      181 tmggltrasy pqawillstf vvvfavllrn awnltalkfg earaealgvk vgrvkilslv
      241 lasiltalav sfcgkigfig laaphlarrl vsedqrfylt ssailgamil lvssilskli
      301 vpgvvvpigi issiigipfl vyaltsqrrq rav
//
LOCUS       WP_284818464             180 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284818464
VERSION     WP_284818464.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..180
                     /product="YceD family protein"
                     /calculated_mol_wt=19150
     Region          1..180
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mtspfvfdvk alltqqqgpe qithtgpapr rigaemlaie egaevtvdav lhslgsgvma
       61 dadvsavlrg ecsrclsple rptefrvsqv faaddefisg daeddedags gdeipqvshe
      121 dtidllqtvt delvvalpfn pvcedgcpdd aptpapdgvs geeteervdp rwaglekfrd
//
LOCUS       WP_284818479             292 aa            linear   BCT 25-DEC-2024
DEFINITION  indole-3-glycerol phosphate synthase TrpC [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284818479
VERSION     WP_284818479.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..292
                     /product="indole-3-glycerol phosphate synthase TrpC"
                     /EC_number="4.1.1.48"
                     /GO_function="GO:0004425 - indole-3-glycerol-phosphate
                     synthase activity [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30674
     Region          3..279
                     /region_name="TrpC"
                     /note="Indole-3-glycerol phosphate synthase [Amino acid
                     transport and metabolism]; COG0134"
                     /db_xref="CDD:439904"
ORIGIN      
        1 mttvlaadai vaeiladvaa reahvsfadi kalsrsvpsp rpvvaelirp gcsiiaeikr
       61 anpvphvhgg ddfgvradap slfdfdavss ladvaglaqg faqagvaava cqteqlrfrg
      121 sledmatara assvpmlcrd iivdpyqvhe arffgadmvp lqvellaqar lvalvdries
      181 lgmtvlaevr speqaqrava agvkvvgina rglhsrhlnp hrfsaivpcl psdvvriglg
      241 gvmsarevwr yagwgadavl vgealmaaph ptmlardlva aglhpacpvw rs
//
LOCUS       WP_284818579             232 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284818579
VERSION     WP_284818579.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..232
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=25351
     Region          1..223
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mlfdslprps eriapgvahl pgwlgvdkqs elvrevreia rryadtpmtm lrpklksggq
       61 msvyqlhlgr ywhypsyryv dkiagttvpp vpdnlaalap vallaaagva eelapwvetf
      121 vpemvlvnyy ppgsgmgmhv defeesrapv islsigdeal frmghtesrt qpwddvtlcs
      181 gdlvvfggpk rfayhgvvrv ndatlpdgcg laegriniti rqvsaapklq gr
//
LOCUS       WP_284818627             562 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284818627
VERSION     WP_284818627.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..562
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=61043
     Region          4..553
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msdnskplle lkdlnitfss sggdvhavrg anlevypget vaivgesgsg ksttamsiig
       61 llpkngkigg gsilfngedl tkasekrfqq irgaeiglvp qdpmsnlnpv wkigtqvtes
      121 lkannaldga dkdekvaqll teaglpdaak kakqyphefs ggmrqralig iglaarpqll
      181 iadeptsald vtvqrkildh laslteelgt avllvthdlg laaeraehlv vmhrgrvves
      241 gpsqeilqdp qhpytqrlvq aapsintary sdnvtvnens daadsqstsg epinadndfv
      301 ievanltkef aqrgrgkdvf kavddvsfnv rrgttlamvg esgsgkstia nmvlqllept
      361 sgtikfnged vskfskkqlf nlrekmqvvf qnpygsldpm ysiyksieep lilhkrgnrk
      421 erqrrvaell dmvampasam qrfpnelsgg qrqriaiara malnpevlvl deavsaldvl
      481 vqdqilkllq nlqdehnlsy lfithdlavv rqsaddvvvl qngnlveknt tenlfrnaeq
      541 eytrnlinsv pgmniklgng qa
//
LOCUS       WP_284818665             331 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284818665
VERSION     WP_284818665.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 331)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18950610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..331
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=36395
     Region          40..163
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
     Region          177..318
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mvkksqmsea dkdnqsgfnl saryhqigkn pgadypkptl aagavlwrrg engawevavi
       61 hrpryddwsl akgkvdpges lasccvreia eetgyqvqlg sllgsvnypv qgrtkvvfyw
      121 nanitggkfq kneevnklrw lnvneahekl tydtdrrvlq qaairhddav dtrvlyvrha
      181 kahdrktwsg ddnlrplhkk grrqaeflvp mlgaykptal ysaeparcqs tiaplsdals
      241 lpvtteqvvg dagldnltaa tarfreiatg ggvpvivsqg gmmpeiietl aaeadfdiep
      301 refkkagtwv lalregklvg adylasplpv r
//
LOCUS       WP_284818785             668 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD/NAD(P)-binding protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284818785
VERSION     WP_284818785.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 668)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11816065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..668
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72139
     Region          6..632
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
     Region          7..228
                     /region_name="NAD_binding_9"
                     /note="FAD-NAD(P)-binding; pfam13454"
                     /db_xref="CDD:433222"
ORIGIN      
        1 mtatqialig agprgisvle rlaaylrdss ssgqaqtktq avrpqltihi vddsqigagr
       61 vwdttqtrtl cmntladavt lftepgstvg asvlsgptly ewirlvrgdd llaaftagnl
      121 nydtnaqvvq ekealfrahp prkglandyh eeligtveqs npsralygey lrwvyqvvla
      181 hlpdsvevie hnsravdmyt vpdsantdvi tladgtsfsa hatvlatgwv lnadnneqhq
      241 lraasqaehl twispnnpve qpvdniaaek pvlvrglgmg ffdllalctl grggsfdvdp
      301 ttrsglryra sgkephfvvs srrgypflpk sdygslppka hmprlhnalq avqeqeridf
      361 sidlapaiir daieafyatl srlapesilt stedintvld stpvyvlldp hglsgvlarh
      421 tteicnlqpy lhprvestqq vaeamardid ealkgsnspi kaalwvfasc rkhvgiagsq
      481 gkfmtdsatp tlsqimalgq mvgsgpplfr sqqllalvda glveflgaqp rltigsaeft
      541 ltcgsgvsar qasattlvda wlpkpdirfp adplsqalfa sgrirpfsid gveqgspeta
      601 yttrrtirpd gsqdsrlhii gipthaqmpd ttispmpgtd pimlqetdkt arsvhaiiqg
      661 lrdeapqp
//
LOCUS       WP_284818943             349 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284818943
VERSION     WP_284818943.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 349)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..349
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=36091
     Region          20..344
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mrhrmhtsap sryvhlagir fyraslctsa vlvlviiaaa ivglllgdyp mtlgqtvagl
       61 fgigddplir yfvqdqrlpr vfgalmvgaa lglagnifqr lsnnplgspd iigfstgsas
      121 galfaiiilq agpaaigvga mlggvasatl vyllsiknrk vsgtqlvlvg igaaailqal
      181 nsilivrael gpaqtaaqwl agslnattwp eigvlvaila vvvplallla rplqimlsgd
      241 dlaaglgvrv hqrrremiav gvvltalsva iagpiafval aapqlarrfd pgiamvnsgl
      301 mgavlvllsd iiaqrllapv qlpvgvvtgs lggvyliwll lrkwhtndn
//
LOCUS       WP_284818957             246 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284818957
VERSION     WP_284818957.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..246
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25930
     Region          11..243
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(29..30,32..33,36..37,74,78..79,82..83,107,111,118,
                     121..122,127,142,146..147,149..151,153..154,160..161,
                     164..165,181..182,184..186,188..190,192..193,195..196,200,
                     203..204,210,212)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(145,149,152..153,155,159,195,198..199,201..206,
                     209..211,215,217)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mkqstastaq vpvgkpvhfl hpltviiigv sawvaalsis wpllhaaiia lgwlagiags
       61 rslavpatsi alsipaglsm llvhaphgeh qiaplltsdg lvtagelalr fcalmtslla
      121 amanvhipdl lkalqhlglh hsvvyvlgas lqllpqastl isevatanrl arrkvtlttv
      181 iprmiipvit rlltrgadrg ialqgmgyda pgrrtvlypv rahrweillr ltfpaaaigl
      241 vvlawi
//
LOCUS       WP_284819156             649 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase, partial
            [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284819156
VERSION     WP_284819156.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         <1..649
                     /product="class I SAM-dependent DNA methyltransferase"
     Region          <25..646
                     /region_name="YeeA"
                     /note="Type II restriction/modification system,
                     endonuclease and methylase domains [Defense mechanisms];
                     COG1002"
                     /db_xref="CDD:440626"
ORIGIN      
        1 cnieikplkp kpprikpvql sgassifgsl fqlvkskear rhsgehytse knilktiepl
       61 fldelraear rlinskstsv kklrefrdsl anniycdpac gsgnflivay relrkietem
      121 ivaireregs agsmtfdisw eqklsidqfy gfeinwwpak iaetamflvd hqanrelada
      181 iglaperlpi nitahihhgn alqldwaeil petsgqtyif gnppfigqyt ktkeqtadmk
      241 rawgkdydgy ldyvtgwhaq alnvlqtrhg efayvttnsi tqgqpvpalf gpifrdhwri
      301 kfahrtfswd seapgkaavh cvivgfsrnt svkprlwdyp elrgeavpvp veksinaylv
      361 dgpnilvkkr stpladippa rfgskpadgg nlvvevddyp efandtvaak ylrpycgsre
      421 lirgldrwcl wmddenfdps dlqkskllye rvtgcrefre ssspsgdayk lrtiphlfrp
      481 nskrptvdyl ciprvvsenr rfftaaqfsa dtitsdgaft vedptglsfa lisssmfitw
      541 qqtvggrlks dlrfsntltw ntfpvpqlds askeriiaag kkvlearelh persladhyn
      601 plamdpallk ahdsldkevd kafgaprklt terqrqellf enysklrdk
//
LOCUS       WP_284819220             481 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284819220
VERSION     WP_284819220.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..481
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=50656
     Region          8..454
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 maddsfadsl qnildgidkf iwsqwflipl llftglwlti rlrgvqfrkl gvalrhgfid
       61 rndadgagdi tqyqalttal aatvgvgniv gvataisigg pgalfwmwit gllgmaskys
      121 eaflgvrfrv adahgkvsgg pqrylsqgip grlgkflawf ftisaiiasf gignltqgna
      181 vaaglestfa vsptvtgvim fvligavllg gigsigkvts afvplmiiiy ltggivvlam
      241 haseipaafa mifndaftgt satggflgag iilamqmgva rgifsnesgm gsaaiaaaaa
      301 ktthpvrqgl vsmtqtfidt ivvvtmtglv ivttgvweag qnnaanmtaa afsegigsdw
      361 ggtivslsvv ffafstilgw syygersaer afgawasipy rmvftcviyi gatteislaw
      421 tfadianglm aipnliglli lsglvaretk ayldfdptlr aqprdiekfl itsknpwrsk
      481 f
//
LOCUS       WP_284819750             361 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium macclintockiae].
ACCESSION   WP_284819750
VERSION     WP_284819750.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..361
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=38554
     Region          14..361
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mskkyfdayr trrakatglv kdsdhagvli sdlknvrylt gfsgsngllv iredgqhlll
       61 tdgrydtqvr ietgepedvr ieigrklfdr aaefakevge sfavepsldy gqaqalgnpp
      121 vlgsvveglr lvkdelevaa laeagelads vwrsfiedgg iregiteiqa aaelefqlrt
      181 agadglsfdt ilasgvnaak phagvsreki vpglvtvdfg vyldgyasdq trtvcvgepd
      241 elarelydvv yrsqkageai lapgvelrnv daacrdviae agygeffvhs tghgvgldvh
      301 eapraaagvn peeklvegmt vtvepgiyip gktglrient yvitadgaks fnaspteliv
      361 v
//
LOCUS       WP_284819826             490 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Corynebacterium
            macclintockiae].
ACCESSION   WP_284819826
VERSION     WP_284819826.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..490
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51649
     Region          1..454
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 memienfvan tlneniwkii pvfllsagay fgirtllvql rmvpdmfrsv kepavgksge
       61 sisafqafsi saasrvgtgn vvgvaiaitl ggpgavfwmw vvalvggata fveatlaqlw
      121 ksrdkdgyvg gpayymtkgl gakplalifg iaititygfv ynavqtnsia eaagsslhal
      181 nsniapdaaw lkvgvgllva lltalvifgg vkrianatqv ivplmatayi llgvlvlain
      241 isevpamfgt ivehalgike iagatlgaaf mngmrrglfs neagqgsapn aaataavshp
      301 vkqglvqtlg vyfdtlvvcs itafvillsd paygegvqta nltqhalsaq vgewgthfit
      361 iilfflafss vlgnyylaqa nveyftkskt klnifrvlvv lcvfggaigt vplvwsladt
      421 faatmvlinl caivplggva ikllrdfsqq kaagmdpifh rdnlpelknv dcwdgtdpec
      481 qrrelhngaa
//
LOCUS       WP_284819935             356 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Corynebacterium macclintockiae].
ACCESSION   WP_284819935
VERSION     WP_284819935.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..356
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=38219
     Region          37..326
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mkqraaeesn pfakallkly afvyaadrky gfprpvtapt ihrqrlfaii llacqtgitf
       61 tgalvrvtgs glgcstwpqc qpgslfpvag sapwvhqiie fgnrtltfvl siaalvcfis
      121 vvraarrtpi lhlafiqgig iivqavlggi tvrmdlmwwt valhflpsml lvflaaklvv
      181 rigepddgem qplmpralrl ltdgssvsla ivlitgtmvt gagphagdea ilpehrlqvp
      241 lidmahvhag fmylylglti gllagvfaln lehriktaay wvigaiilqa aigimqfwlg
      301 vprwsvplhv igsglttaat gflwalksry sggnashtgt ttgdsqrhea vnakdg
//
LOCUS       WP_284820044             308 aa            linear   BCT 25-DEC-2024
DEFINITION  lipase family alpha/beta hydrolase [Corynebacterium
            macclintockiae].
ACCESSION   WP_284820044
VERSION     WP_284820044.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18498059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..308
                     /product="lipase family alpha/beta hydrolase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33257
     Region          45..162
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
     Region          49..278
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mlpfsfltpr paarkqreld advpatlqgr fmlggpvnds rkelseehpy plvfihgttd
       61 nslrwqkaat yfsargysvw alnygkpeag rpvipgvfav ndidesavei aktidhilav
      121 tgaskvdlvg hsqgglhikk yvaehggqdt vrravgiaat yhgttitgms silqnlvdrn
      181 pdfadlvagk aavqqlnsse lirrlnelpd thpnvmytni ytskdltatp nstsqlesig
      241 gadvaeaevg avcgllippg haslpendhv iglvewgltr kqgdctpvhn gcnggqrwkl
      301 gyrffhen
//
LOCUS       WP_284820279             394 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium tuberculostearicum].
ACCESSION   WP_284820279
VERSION     WP_284820279.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..394
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=43198
     Region          152..392
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mkklwpdalr awvgppwril iplffwvssv syaadvvdgd slfhrgvlvl ycvvlplalw
       61 lhpklkekai gaiaivftlc lftplaalsn vhafplaycv fligahspkr mrrvwiawig
      121 vgtlfsvwaq hfgnlifsdi dfglegaqid plvslasvvi iawpvmgfff llgtndrkkr
      181 edqqlliera emagavernr iaremhdiva hnlagviala dgarfaaakn paaatealet
      241 iastsrdslk qmrgllsvlr dgdsradtka pgasdiagli searrsgfdi tvhgledlpt
      301 esdelyqftv yrvvqeiltn mlkhsrdkrg vlrfrstgng lvlsadnpaa rtpdnhkpgy
      361 gligmservk ayggsvatrt edghffitve vpnd
//
LOCUS       WP_284820293             320 aa            linear   BCT 25-DEC-2024
DEFINITION  DHH family phosphoesterase [Corynebacterium tuberculostearicum].
ACCESSION   WP_284820293
VERSION     WP_284820293.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..320
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=34392
     Region          7..319
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mtkkqyepav aalhdahsic ivthlrpdad aigsaaalll alrqrgkdvc avvgqereis
       61 rnlytipaad dvttslklpe sydlyvtvdc gsldrtgffa dridqlakqg rvlcidhhss
      121 npgfgainvv dtecesttvv llsildslei qidrhiahcl yaglmtdtgs frwgrpamhd
      181 iatrlmhydl dtkqiaadll dsttpddlqm igrvlaglrl eeagehtlgi lvarlediqg
      241 hsdsaveslv efvralegtt vgvvfkeqap evwavslrss ridcssvalt fgggghvpaa
      301 gytahgapee iikelvaaiq
//
LOCUS       WP_284820322             230 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: energy-coupling factor ABC transporter ATP-binding
            protein [Corynebacterium].
ACCESSION   WP_284820322
VERSION     WP_284820322.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..230
                     /product="energy-coupling factor ABC transporter
                     ATP-binding protein"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25589
     Region          4..226
                     /region_name="EcfA2"
                     /note="Energy-coupling factor transporter ATP-binding
                     protein EcfA2 [Inorganic ion transport and metabolism,
                     General function prediction only]; COG1122"
                     /db_xref="CDD:440739"
ORIGIN      
        1 mptiefssvs vafddtvvle dinltlteqr igiigqnggg kstltrling lgepsegtvt
       61 vdqmdvakqg kkvrekvgfv fsdaenqivm pnvrddvafs lrrfklpkhe rlarvdatlk
      121 rfglaefaer sphtlsggqk qllalaavmv idpiliiade pttlldlrnr drikrefarl
      181 eqqlivvthd ldflsdfdrv iciddhhiaa dgrpaevidf yqdlmaqrpl
//
LOCUS       WP_284820342             549 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Corynebacterium macclintockiae].
ACCESSION   WP_284820342
VERSION     WP_284820342.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..549
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=59824
     Region          24..491
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mnatpdtsta ptnatsplpq ladataerpl dilivgagls gidlahhvak nfpdwnwaav
       61 dsnydlggtw atfqypgirs dsdmatfslp fkkwphkgtl gsgkqirdyc reaaeeigml
      121 drlqlstwvq avnfhtdqgl wevtmrlgrp ghansegtdg asapaspeqp tlttwtrrlh
      181 fatgyyrhse gftadiegvn tfegtalhpq qwprdldvrg kkvtvigsga taitlvpalh
      241 emgaevtmlq rtptyiaplp etdtissfvg lglstepgtf ghrlarslhi grdmaqyhlc
      301 qtfpsiaklv frgwnrlylp adevrrnftp pygpwdqrvc kspggdffka vrggarvvtd
      361 hisrvdasgv qlrsggyies dvlviatglq llafgdahfs vdgtpvptes lvayramman
      421 rlpnfsytig ylnqswtlra dmtsrylvql wkdmdargeq wacpvlpage aadlpllems
      481 sgyiqrsvat lprqgagdpw rmeqdyiker raytgadnrh dmafgtdale aaaplaageg
      541 gggaaelrv
//
LOCUS       WP_284820488             323 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Corynebacterium
            macclintockiae].
ACCESSION   WP_284820488
VERSION     WP_284820488.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..323
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=33357
     Region          14..315
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mvdridtrlt elwgidkpii gapmagrsdg elaaavsrag glgmfgagag tapewilena
       61 riaaeagpyg iglmvwaled npaqfdavle arptvvslgf gdpapyvdra heagisvvap
      121 intmaqlrqa laagvdavcv qgtdagghtg rigtlpllqi vteymqlhap gvpiavaggi
      181 atgrgvasvl vagadaawvg tallaspeaa gaeelrhaav kataskavlt diydraekqk
      241 wdteqwptrt vrnafvdtyg plsdagevsd eeliaaraag gdfadelklh agqgvellra
      301 evpagdvvqk mydealcclr rfa
//
LOCUS       WP_284820513             332 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium tuberculostearicum].
ACCESSION   WP_284820513
VERSION     WP_284820513.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 332)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18950610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..332
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=36853
     Region          40..163
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
     Region          176..319
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mpnikkmhet dkdqqheefi sgrhqeipvd pakefhrttl aagaviwrgs pqdpeialih
       61 rphyddwslp kgkvdpgesl pttasreile etgfsvrlgk ligkvtypvq grtkvvyywv
      121 akylggtysa nsetdelrwl pideaqdlls ydvdtavvak aakrlriapa trvlyvrhar
      181 ahesgswqgd dnlrpldkkg rrqaemlvpm lsafqptaiy salpqrcqqt aapladelgk
      241 disinknfgd eawendpeaa kkafrrvvne ggvpvvisqg atipgiiedl apkflkkpvd
      301 klkfkkasvw vlsfnngelt gadylasplp vr
//
LOCUS       WP_284820543             227 aa            linear   BCT 25-DEC-2024
DEFINITION  IMPACT family protein [Corynebacterium macclintockiae].
ACCESSION   WP_284820543
VERSION     WP_284820543.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Park,F., Gajiwala,K., Eroshkina,G., Furlong,E., He,D.,
            Batiyenko,Y., Romero,R., Christopher,J., Badger,J., Hendle,J.,
            Lin,J., Peat,T. and Buchanan,S.
  TITLE     Crystal structure of YIGZ, a conserved hypothetical protein from
            Escherichia coli k12 with a novel fold
  JOURNAL   Proteins 55 (3), 775-777 (2004)
   PUBMED   15103642
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Okamura,K., Hagiwara-Takeuchi,Y., Li,T., Vu,T.H., Hirai,M.,
            Hattori,M., Sakaki,Y., Hoffman,A.R. and Ito,T.
  TITLE     Comparative genome analysis of the mouse imprinted gene impact and
            its nonimprinted human homolog IMPACT: toward the structural basis
            for species-specific imprinting
  JOURNAL   Genome Res 10 (12), 1878-1889 (2000)
   PUBMED   11116084
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..227
                     /product="IMPACT family protein"
                     /calculated_mol_wt=24872
     Region          23..214
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 mpddtvplna nrpepsyvrp qqgrftaeve ikrsrfiala erctsedear efinsirrey
       61 pdarhhcsaf vvhvdsaqpi erssddgepa gtagqpmlev lkgwhtpepl qdvavvvvry
      121 fggvklgtgg lvrayqeatr evlqqvplvl rrqldlytcd vphadagrve aevraagytv
      181 vgveykavae lsiacepgap lpdflasits gtaephlegq rwiedtl
//
LOCUS       WP_284820576             220 aa            linear   BCT 25-DEC-2024
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Corynebacterium
            tuberculostearicum].
ACCESSION   WP_284820576
VERSION     WP_284820576.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..220
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=23103
     Region          122..215
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mavdnirlkd aligiaavva mdvllvatvf avmkvglttg glgtimpial alsvvvptva
       61 lvlylkrrgi glgflplgrr gwhlvwqvpl tifmagaaaa ivgpllgisp sestysadgr
      121 gamviislac ylilapliee ivfrrllmgy ldrsfpafvs vilssllfga ahiappvivy
      181 atflgmgcal vtrfhnslra glilhfvnnl tvqliaisal
//
LOCUS       WP_284820624             654 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase C [Corynebacterium tuberculostearicum].
ACCESSION   WP_284820624
VERSION     WP_284820624.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..654
                     /product="phospholipase C"
                     /calculated_mol_wt=70110
     Region          25..523
                     /region_name="PlcC"
                     /note="Phospholipase C [Cell wall/membrane/envelope
                     biogenesis]; COG3511"
                     /db_xref="CDD:442734"
ORIGIN      
        1 mklrsravav caaaaattsl vpgiaqaatt tpiehvvviy senisfdhyf gtypnalnkd
       61 geklqgsgkn apkftakegt pkaknlendd vmgeknpnsv kpfrigpdha vttdqnhhyg
      121 deqaaynggk mdkfpetvst didkssngyy aapgmtmgyy dgntvtgmwn yaqnfalndn
      181 systifgpst pgalnlisgt vaggtmhdpa tgeqkkieag knhalagvse dgktatvvgd
      241 pdplyddcsn nssagtnqvt amhsknigdq lndkdvtwgw fqggfrptde atdnararcg
      301 ashttltgqn qtdynphhqp fqyyastanp hhlapssdem igktdranhq ydlkdfdtai
      361 eqgnlpavsf lkaanyqdgh agysnpldeq afithyinel qnspewdsta vviayddsdg
      421 wydhkapeir ngsndphqdk eictaaaakv gvagdkhgqc gpgtrqpllv ispyaktnhi
      481 dstyteqtsv tkfiqdnwgl grlggiafde ragelnnmfd fnttkkapkl flnetdgtva
      541 kdyasiekvd nssragtnlk dvvegmddpk vtekdvpsit klhqeskpqp gtnkpadsss
      601 sssagsskag tiaailtalg vgagivawym nghpgldlkk lqdfklpplp nlpf
//
LOCUS       WP_284820684             700 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: PhoX family protein [Corynebacterium].
ACCESSION   WP_284820684
VERSION     WP_284820684.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..700
                     /product="PhoX family protein"
                     /calculated_mol_wt=76788
     Region          46..694
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mglkgrnllk kmdftssrsh rtcvykcgda cskpvnnksd nnyfmdliqg tfsrrsalra
       61 ggaavvtvgg asflaacsdd ngeggakggn genkggngsg nadapdglkf emvepntkde
      121 vvvpagykse vvirwgdpvv egakefdvdn qtaeqaakqy gfncdfaall piegennrfl
      181 lvsnheystp qqmipdydle npskehvdie lashgmsive vegndkdgkl kpvmgkynrr
      241 ltgttefelr gpivghklvk tsddkegkiv kgtfnncsgg vtpwgtilsg eenvdqyfag
      301 genvkdekvr erlsrygied aktarqwekh ydrfdvtkep nephrfnyvv evnpwdpkst
      361 pvkhtalgrf khegsnihvt ndgtvvaysg ddsrfeyiyk fvssrkirsg ntdkdreenm
      421 kildegtlyv atfegnnkdf dennppkgek fdgtgkwikl vtvkedgsae shvdgmsaee
      481 vivftreagd kvgatkmdrp edvephpttg kiyaaltnnk yrgtqeegkn kenvreyapv
      541 kenkngmvie ieddftgedl kwnlllvcgd pdeaetyfgg fdkskvspis cpdnvtfdsf
      601 gnlwvstdgn alesndglfa vslegetrgl tkqfltvpag aetcgplvfd krvlvnvqhp
      661 gedeeatvkt skshwpdggd siarpatvva wkedfgtiga
//
LOCUS       WP_284820702             138 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Corynebacterium tuberculostearicum].
ACCESSION   WP_284820702
VERSION     WP_284820702.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..138
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15671
     Region          4..132
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mmatpsvhty riqtrwsdfd myghmmnany ielaqearla fakehiyskg ldfiafvrhl
       61 dvdfqrpmef kdtttvevet tisqigttsf tttqqvknaq gevaatvecv qvvidrqqqt
      121 prpltdqekd ilhntaan
//
LOCUS       WP_284820768             769 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional lysylphosphatidylglycerol flippase/synthetase MprF
            [Corynebacterium tuberculostearicum].
ACCESSION   WP_284820768
VERSION     WP_284820768.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458459
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..769
                     /product="bifunctional lysylphosphatidylglycerol
                     flippase/synthetase MprF"
                     /calculated_mol_wt=84162
     Region          235..755
                     /region_name="MprF2"
                     /note="Lysylphosphatidylglycerol synthetase MprF,
                     lysyl-tRNA-binding C-terminal domain [Lipid transport and
                     metabolism]; COG2898"
                     /db_xref="CDD:442143"
ORIGIN      
        1 msvlktiltr fpvslavlvi mwalhlvdfp tshwlaltta hpggaiilsi lillwlvpae
       61 wrlgslrtla vgitsqlitv plsivlargi etvglnrwgn dllsdtfltp igfiagaagf
      121 asallprlwr rrlrislivl tatfvlysgt msdvlgivaa alsitagqll fkpesappsi
      181 rerrvllavg vacvaigpaf valdpmaegp fsqitqllwt phlsaleatq scadsvtsas
      241 ctaavdlara qgigavvani mpfiiqlvvc fgltrgrvla wwvavitqvl aitlltsqlw
      301 ddarlsyllp nlvlvllpwl lalfmllinr slfhtpenra fftrtvtlai laaaigaglw
      361 iltaslhntv ppanlaaila etplrfvpav valilphhva patmiswfvy ewvgnafwll
      421 vavrlylgfs rpvdpaqesd rdnarrllea gtgdhlsfmt lwksnryffh gdsyvayrvs
      481 ngialtlgap ighdissefe qfaaeqgwtv awysvntqfa dahpqlkrlq vaeeavlsce
      541 svefkgkkfq nvrtarnkae kegittrwtt wkeldiasia rvtalsedwv seralpemsf
      601 tlggieemmv dgtrlllaes adgtlhgvts wmpvyengai agyildvmrr nehgfkgvie
      661 lliseamlia hsegrawisl sgaplagqpd epswldvald rlgeeveply gfrtlaaskr
      721 kfqpkeqpwf lcyhdelklp sialatmhay lpdvktkdav safrawmaa
//
LOCUS       WP_284820761             473 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Corynebacterium
            tuberculostearicum].
ACCESSION   WP_284820761
VERSION     WP_284820761.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..473
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49403
     Region          1..449
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mdslnsilsa istvvwgpfi liplllgtgl wltirlgglq fralgratrh vfatdsdeqs
       61 tegdisnyqa lttalaatvg vgnivgvata lsiggpgalv wiwitglvgm askyteaylg
      121 vrfrttdskg emsggpqqyl krgipgplgs vlavffaifa icasfgignl aqanavatnm
      181 estfgiapaa tgailfvlvg svllggihai gritaafvpl miivyvlggl yvifshaaei
      241 paafamifsd aftgtaaggg fvgstimmai qygvargifs nesgmgsaai aaaaaktphp
      301 arqglvsmtq tfidtiivvt itglvivvgg twdmgrdeag imtaeafsrv lpgdwggtiv
      361 slsiiffafs timawayyge rsleslcgrk asipyrmffa cllfvgsvse lelawtfsdl
      421 angliaipnl igllllsglv aretkaylaf dpklnkpvne vrafvesqgm nwk
//
LOCUS       WP_284820775             468 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium macclintockiae].
ACCESSION   WP_284820775
VERSION     WP_284820775.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445464
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..468
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48574
     Region          145..>273
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
     Region          195..410
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mrsfvgekyf arrrviaata aaslslaals gvadvtdgag magvaaaqss apslqssaps
       61 vqssapsvqs sapsvvnrgv pmrtpapyag kpvdsglkig atpatagvlm nsvpldpsag
      121 lsaagqqfrf systtnqhgt vspstgavff pkgklpvggw pvlawahgtv gladqctpsm
      181 nprsprdady lnhwlkqgya ivasdyagmg teglmsylng kstaanvvds viavqelpav
      241 kqggqalskk wavigqsqgg gaalhvalra tqrskqagln flgtvatgap ayveeivlag
      301 spsfppaplp aglntyalyi lagfreanpn vdvdsaltpe gkrmvkaaee sclpelsesl
      361 kgtnvarafs kplrtvpgle palraymqtp atgynkpvfl ghglldkdvp tpigiilnsd
      421 mwihqfigdm qkrnkrvevh wyptdhggtv pasqrdstpf lanlfrqg
//
LOCUS       WP_284820866             420 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium tuberculostearicum].
ACCESSION   WP_284820866
VERSION     WP_284820866.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..420
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=45548
     Region          16..379
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 melilsfaag vvacglalpv iswlrgriar yrqatdaean qvttvsqvlh lavqgsptal
       61 avldrsqeiv msnpaahems lvhdravnpd vwqtaqevfe dketrtvdla ipkrrtghrv
      121 tqfkavikpl tlndgrfvii ygtdesenvr mesarrdfva nvshelktpv ggiallaeal
      181 lqdpgdpetv eyfgnkvyke anrmadmvse lislsklqga ealpemepla vddlieeals
      241 rnqlaaears ielnrgasvg vqvkgdrsll vtalsnlisn ainyspekmp vsvsqkvvdg
      301 gvvlirvtdr gigiapddqk rvferffrvd qarsrqtggt glglaivkhv vanhggnikl
      361 wsrpgtgstf tielpiyree kpaqdagmkd nekkdavtaa apglpravar vaarrkdkaq
//
LOCUS       WP_284821080             227 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium macclintockiae].
ACCESSION   WP_284821080
VERSION     WP_284821080.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13031065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..227
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25090
     Region          78..216
                     /region_name="SpoU-like"
                     /note="SAM-dependent rRNA or tRNA methylase related to
                     SpoU; cd18096"
                     /db_xref="CDD:349969"
     Site            order(151,153,173..176,179,193..194,196,202..203,205,208)
                     /site_type="other"
                     /note="putative SAM binding site [chemical binding]"
                     /db_xref="CDD:349969"
ORIGIN      
        1 mtptspeshd kpgptewleh prgvrswede hpgqprptdp rfdpelldag dtrnvvdayr
       61 ywkqsaiiad idtrrhalhi aienfendsn igtvvrtana favdtvhivg rrrwnrrgam
      121 vtdryqhlqh hatvgevlef aaqeglvvva vdntpgcvpl etaelpercl llfgqegpgv
      181 tqeaqeaarm tvsiaqfgst rsinagvaag iamhawirqh adlsqaw
//
LOCUS       WP_284821122             271 aa            linear   BCT 25-DEC-2024
DEFINITION  Fpg/Nei family DNA glycosylase [Corynebacterium
            tuberculostearicum].
ACCESSION   WP_284821122
VERSION     WP_284821122.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Le Bihan,Y.V., Angeles Izquierdo,M., Coste,F., Aller,P., Culard,F.,
            Gehrke,T.H., Essalhi,K., Carell,T. and Castaing,B.
  TITLE     5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA
            glycosylases
  JOURNAL   Nucleic Acids Res 39 (14), 6277-6290 (2011)
   PUBMED   21486746
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Zaika,E.I., Perlow,R.A., Matz,E., Broyde,S., Gilboa,R.,
            Grollman,A.P. and Zharkov,D.O.
  TITLE     Substrate discrimination by formamidopyrimidine-DNA glycosylase: a
            mutational analysis
  JOURNAL   J Biol Chem 279 (6), 4849-4861 (2004)
   PUBMED   14607836
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..271
                     /product="Fpg/Nei family DNA glycosylase"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.-"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003906 - DNA-(apurinic or apyrimidinic
                     site) endonuclease activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008534 - oxidized purine nucleobase
                     lesion DNA N-glycosylase activity [Evidence IEA]"
                     /GO_function="GO:0140078 - class I DNA-(apurinic or
                     apyrimidinic site) endonuclease activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=30614
     Region          2..269
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpeghvihrl ankfnadyrg mplrvtspqg rfaaeaelld gerielaety gkhlfvhfsa
       61 enprhilyih lgligklrfe preevggqir vridngaeaa nlrgpqfcrl lteeeyraql
      121 akvgqdplrt dadvealwak vhksrrsigs lmmdqhlyag vgniyraetl frhglspflp
      181 grdvsretfd atwtdlvdlm eygvehgrid tvrpehspka mgreprkddh ggevyvyrra
      241 glpcyicgtp vaekvmegrn lfwcptcqpa p
//
LOCUS       WP_284821126             586 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Corynebacterium macclintockiae].
ACCESSION   WP_284821126
VERSION     WP_284821126.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..586
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=62957
     Region          17..337
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(18..19,22..23,52,55,109..110,162)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(107,110,187..193,222,247..251,282,308..312,314)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mglsgaevng tarvavlwfp dwpvyvqaqs rgwdvlapaa viadyrvlac naaaraqgik
       61 igmkqrhala aypqlnvaed dpnkqasvhe dvlaalqdvs avvetlrpgl lafpvdalar
      121 yygdedtave klldaavrvh adcmvgvadd lvsavwaarq gksippggsa afiaglpinv
      181 lgiepelrap ahlsstlqql glrtmrdfaa lpradvaarf gqeavewhri asghverava
      241 parrreelev ryeaeepiar tetaafiarh vatalhntlf aageaclrla vrayleppan
      301 ytgptvierl wrcreplseq dtaqrvrwql dgwltrlrae tadggnvhgg ntyggdvhdg
      361 dahggeadwa dntagvtcie lvpvetvpag slatplwggp degiraaraa agraqaligm
      421 nrvlrpihrg gravarriat vpygeddpea italptrqwe gqllhplpgl igaptsgvvp
      481 asgvadthnp saahpaarlm lldrhsdpvh vtgrglmsap pdtlrwgarq lritgwagpw
      541 pvdehwwaeg kryarlqvsa regtsesvha fllvckgkqw rieaty
//
LOCUS       WP_284821201             630 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium
            macclintockiae].
ACCESSION   WP_284821201
VERSION     WP_284821201.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 630)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..630
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64793
     Region          28..624
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mssacgcehe tateieeldq pwwkdpelll pifsgvalgi glaldwsgve tpatvlfwvg
       61 lllgaytfap gairnlvtkr klgigllmti savgavilgf vgeaaalafl ysiaealedk
      121 amdraqgglr allklvpqta tvlrggttae vaakdlevge lmvvrpgeri atdgiirsgr
      181 ssldtsaitg esipeevapg devpagains agvlevetta agtdnslttl vdlveqaqae
      241 kgdrariadr iaqplvpgvm ilavlvgvig sllgnpetwi tralvvlvaa spcalaisvp
      301 ltvvaaigaa sqfgvviksg aaferlggir hlavdktgtl trnqpevtsv vpavefdraq
      361 vlafaaaveq qsthplaaai aaarpeapaa ldiseeaghg isgtvegrrv lvgsprwida
      421 gplkadverm esegqtcvlv tvddalsgai gvrdelrpev peavqtlhan gvevsmltgd
      481 ntrtaralaa iagiddvrae lrpedkasiv aelssktptt migdgindap alagatvgia
      541 mgatgsdaai esadvaftgh dlrlipqalq harrgsriin qnivlslaii ivlmplaisg
      601 vlglaavvlv hevaevivil nglraaqakr
//
LOCUS       WP_284821230             318 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            tuberculostearicum].
ACCESSION   WP_284821230
VERSION     WP_284821230.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..318
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35007
     Region          9..316
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 madgslklqa lvrslnlipy fknhpdktpm eaakdlgmdp gelkdaldrl fcsgtgrnte
       61 dlidltfsyr dgvtihndqg lsqalrltpt eagallltle slqampglid ahavesaaak
      121 lrgimdektv aiyeslstpa peetdiqall tqavnerkrv rlrywsassn aeservvdpa
      181 rifivdsepy vaaweeakqa hrtfridris kariveeesq phlkdldfda sspfnlgdgd
      241 tvqlainqef twlaeyydmr lgedlgngev aatmpmgsvd wlirfalgqa drlrvvapqs
      301 vvnliaergn talsgytq
//
LOCUS       WP_284821266             551 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Corynebacterium macclintockiae].
ACCESSION   WP_284821266
VERSION     WP_284821266.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20358183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..551
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=59915
     Region          61..297
                     /region_name="SBP_bac_11"
                     /note="Bacterial extracellular solute-binding protein;
                     pfam13531"
                     /db_xref="CDD:463911"
     Region          <359..548
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mtspypssln anngkksssk fflvvvllli aavayvvgsg nfpgsltgsg gksydtskpl
       61 kivaatelsd mepfiqqass dlgfeiemey dsgtlvntrn lvdgdygdky datwfatnaf
      121 araegssqqs edhsiarspv alglkqdavn rlgwrnkdvk wsdiaeavkr gdltfgmtdp
      181 qesnsgfltl lsvaaalsns pqgqkfdlst afldkprmkd ffsgqtitsg ssgwlrdtfv
      241 knpgkadgif nyqsvlqsmk endgvdievi vpgdaagaad yplsaltkpg etgpeadtva
      301 kvealadwfk ehseevgert hlivsgkdae nkgtqnyyey ptskdhirsl vslyrddlrr
      361 padsnflldt sgsmrgnrla dlkgilnrli dgtageagnp kgfgrretit lmpfsskvad
      421 gytqehydpd saeqsrglrd yvnglqprge taiydavlra ydrvgegdgs lnsivlmtdg
      481 esnsgtnrqe fitkmkrkma etdrkipvfv ilygeaseee mnfladftgg kvfnarsgdl
      541 skafeeirsy q
//
LOCUS       WP_284821334             664 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            tuberculostearicum].
ACCESSION   WP_284821334
VERSION     WP_284821334.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..664
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=71977
     Region          1..66
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mtatltladv arltgvtrpa vnewiqrfns esiapfpspy gehdghpyya itevqdwlra
       61 tklgrrdtav edalfyssly rmllhnpara alglldcnta lspqdfspsa avidsltaay
      121 qraadnipsd dpeadiaqaa eqvaeaafgp aaalarladd lsaqrqvtls srftsramqa
      181 vsealtlenp tppiiptdey slgfvtglar eleetlavni gyrkdcapgs lywaelacrn
      241 vefidaseei panslivhaa pfplknapey fehlqnlldn ldergamfci stadmlieds
      301 vaqvvrrrfl aptetgaiap lrysarlprg ifpyrgqqqg alwilkrpnl kakgnsadaa
      361 aviadvpdlk tpglvsdwat mlttpdeark htfirgrilr aadawrsrth slddsvfsst
      421 stssaanlmh tahqagldis sagledaqpk igmraesgat rleylpwkaa tnartgvlqk
      481 lsgsriaerd lapeavakle ligepeilgs ipqgarcidr lrlediaprg tltepgdvvf
      541 iksprprali deeggklvta paqalrcrtf rgrsktplek vcvpylvaka ineatssels
      601 slyfpvfprg nakhlgsveh qlrarrqqll eqlhsldele hglvmsigtg avtiaesrgq
      661 sppg
//
LOCUS       WP_284821373             386 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium
            tuberculostearicum].
ACCESSION   WP_284821373
VERSION     WP_284821373.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..386
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=42456
     Region          23..344
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 msnqfqvdpg lgasvqpqas vksvpqhlpe ldglravasl giivthvsfq tgtgwgfagr
       61 fdyfvavffa lsafllwrrr dlhtlsgyar srvarllpay yacvvavmll lpdahsltlt
      121 qllsnltstq iyvvdglapg lthlwslcve fffylalpal vwllgalprr wrvaaialga
      181 vvswawgfvp fvadyakdqv nsqiwppaya swfavgmlaa eceeagvsrr vqralrprwa
      241 wwlvaavvlw issrewfgpq glvhpepgef srriiagaaf aavvvvpval aprdkswlts
      301 plmqalgaws ysiflwhvai lglafpltgv plfsgkpldf wvilavtvva tvvvsaasyt
      361 lierpgrdll lgrrrkdrpr prhtss
//
LOCUS       WP_284821383              98 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Corynebacterium].
ACCESSION   WP_284821383
VERSION     WP_284821383.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 98)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..98
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10686
     Region          16..94
                     /region_name="HTH_34"
                     /note="Winged helix DNA-binding domain; pfam13601"
                     /db_xref="CDD:463932"
ORIGIN      
        1 mshprhdldp vlanplrfsl laslsnvvdm tfkelrdhla ttdstmskhs taleeagyih
       61 ikkgfvgktp qtrlsitktg eqalthhldt lnriaqgg
//
LOCUS       WP_284821385             440 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium
            tuberculostearicum].
ACCESSION   WP_284821385
VERSION     WP_284821385.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..440
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=47215
     Region          1..438
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrmtvigtgy lgathaacma elghevlgvd vddnkvsalk sgkvpffepg lpevlernie
       61 agrldfstdy eeaaafgnlh flgvgtpqrr gsyaadmtyv kavitdlvpk lkgdhiifgk
      121 stvpvgtaae lqelanelap egttveiawn peflregyav kdtitpdriv lgvregesra
      181 eevarevyaq plsqdtpfiv tdwqtaelvk vsanaflatk isfinavsei ceiagadvta
      241 ladaiglder igrkflgagl gfgggclpkd irafmarage lgadqaltfl revdainmrr
      301 rdrvvdlake afngsllghr vtvlgcafkp nsddvrdspa lavagslsla gaavtvydpe
      361 gmdnakkvfp tldyaadtdd alreaelvil atewkqfkel dpqqagqlvd nkhiidgrnv
      421 lpvadwqqag wkvdalgrtl
//
LOCUS       WP_284821393             441 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF445 domain-containing protein [Corynebacterium macclintockiae].
ACCESSION   WP_284821393
VERSION     WP_284821393.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macclintockiae
  ORGANISM  Corynebacterium macclintockiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Corynebacterium macclintockiae"
                     /db_xref="taxon:2913501"
     Protein         1..441
                     /product="DUF445 domain-containing protein"
                     /calculated_mol_wt=48958
     Region          31..439
                     /region_name="YjiN"
                     /note="Uncharacterized membrane-anchored protein YjiN,
                     DUF445 family [Function unknown]; COG2733"
                     /db_xref="CDD:442039"
ORIGIN      
        1 mtasdaplsq apaslaqvpg pdpateaarr aelrkhktia tgllviatli yvtmrwleyq
       61 gnpgawigyv raaseagmvg aladwfavta lfrhplhipi phtaiikrkk dqvghalsef
      121 vgenflnaal isdklrkari perasdwvvd ggganrvsqe vgkvidltvn ginpeeaehv
      181 lralvidkls eptwgpplgr gleqliqegr tepaveaivi wmddkartse dfvvrlider
      241 tpswaprfvr dlvgsrvyhe lveftgdvrr dpdhdarrql rsfiyqlsqd lqhddkmiar
      301 vegfkndimt sgpvtampgr lwesvratlt twsrdpdsll rrriaqwvea ygrrvqeepe
      361 lreelerriv gaasyladny agevtgiige tverwdaqea sdkielmvgk dlqfirvngt
      421 ivgalaglai ysltelifal g
//
LOCUS       WP_284821469             152 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Corynebacterium tuberculostearicum].
ACCESSION   WP_284821469
VERSION     WP_284821469.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..152
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16918
     Region          19..147
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mastnnsvip tallespsfq lerlrrrtrd gveaalqtkq ttlreywvlt clvdadaasq
       61 sylsetlaid asdmvrlida ledrgwakre rdpkdrrrqi vastkkgakv hkdlaelvat
      121 aedealdest nkqlkhlrkl aksiiaadee ea
//
LOCUS       WP_284821530             407 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent RNA methyltransferase [Corynebacterium
            tuberculostearicum].
ACCESSION   WP_284821530
VERSION     WP_284821530.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..407
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=43133
     Region          10..405
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 mtestmsrgd slevtidrma hggegigqap dgrvvfvpra fpgdvvkata grvkksfika
       61 elesilspgp lrvpsscpaa aqgagccdfa eldpaaetgi kaeilseqlr rtgvvtseel
      121 nieqhtlepv rgwrtrvrwg vdkqgragtr qrrsnelitg aactqlapgl aeglvgegar
      181 rftpgaevia vldgegnrhv vetrkaprgr rvetirevve gsgkvhehvd grtfsfpata
      241 fwqahshapa aytdliaewl ggreyqehta wdlyggvglf vpslahavqg kvisvdyspa
      301 atageqaala dcevevksak veqvaaqlpk pgavvldppr tgagedvirs vaaaapqavv
      361 hvgcdpatfa rdlgywnqhg ygiekmalin afpgthhfet ialitpa
//
LOCUS       WP_284821594             179 aa            linear   BCT 25-DEC-2024
DEFINITION  HIT family protein [Corynebacterium tuberculostearicum].
ACCESSION   WP_284821594
VERSION     WP_284821594.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..179
                     /product="HIT family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19998
     Region          35..160
                     /region_name="FHIT"
                     /note="FHIT (fragile histidine family): FHIT proteins,
                     related to the HIT family carry a motif HxHxH/Qxx (x, is a
                     hydrophobic amino acid), On the basis of sequence,
                     substrate specificity, structure, evolution and mechanism,
                     HIT proteins are classified into...; cd01275"
                     /db_xref="CDD:238606"
     Site            order(59,61..62,69,71,117,124,126,131,133)
                     /site_type="active"
                     /note="nucleotide binding site/active site [active]"
                     /db_xref="CDD:238606"
     Site            order(129,131,133..135)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238606"
     Site            131
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238606"
ORIGIN      
        1 maetfvdsga gepdrlerlw apyrmayiak rskdpfveap kssdedglii argktvyall
       61 nlfpynaghl mvvpyrkesq lenltqeesh elmafaqkav rvlkrvsrpe ainvglnlgr
      121 asggsvgdhl hlhvvprwpg dsnfmtvldg tkvlpqllqd trrvlaegwr emeeedsra
//
LOCUS       WP_284821758             376 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium marquesiae].
ACCESSION   WP_284821758
VERSION     WP_284821758.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..376
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40593
     Region          114..369
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtlqrtaalt avicvaltll gafftptehq lsaaifglil tvittlafrh plvmsvlfvt
       61 vwmsstfaag tpylcyiflt pifiaviayh gknwqtfavg avfwaaglid pssarisvnp
      121 aaafawamfi svgavigatf ahsaqrykta mvewnadvqr rqsdlaetlh nsvvssltvn
      181 tmqlealsle yskdpelakr ldelsdsmrs smsevraltk vlrnniegin dgmsfgsttk
      241 pdsfaqllsq eesrlsklnr kpimdvgaed faphfppetl dsiaaittea clnavkyspp
      301 gaeimisvrp hlgwtvitis npvskptstn adissgigma smsriaatid arvdtklern
      361 qweltlslpp saqkas
//
LOCUS       WP_284821771             526 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Corynebacterium tuberculostearicum].
ACCESSION   WP_284821771
VERSION     WP_284821771.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 526)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 526)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..526
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56749
     Region          1..502
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mevllvligl mlltvfvvai gdkiglpwpa lltiitacav fvpglpqfep ptelilpifl
       61 ppllwalarr tswgvireqw vtilslsvll vvattlavgf tayaflpgis laaailigaa
      121 iappdpvavd avaepagipr riittlqteg lfndaasiva fnlaltavtq gdelsfgggv
      181 lnffysafva gglgwgvgrl valfithvhd vtarnaltwv tpfavylise elgasgviav
      241 viaavelnsr adiqaedrls gqsfwetiel lftgvafgli gltvntaige vgsdlwhsvv
      301 vgvilslvaf vvrlvwmyiy yrinvsrgrp rvaplrlqev llmtwsgmrg lvtlalvlsi
      361 pagvfsfhhe lavialtvll vtmvvpglll pwlmerldlt easqiasdkm raavvsrara
      421 asidalshfr pdghiapdae kvdpeisanv ikwfedrlgd gedvsddsri hrawqarhva
      481 learrtalaa aqeellrmrg draynpaivd evleeidrmv lgtkrh
//
LOCUS       WP_284821811             119 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Corynebacterium tuberculostearicum].
ACCESSION   WP_284821811
VERSION     WP_284821811.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..119
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12403
     Region          3..106
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mrawvilfla iasevvgtva lkyavdhfwi ygvaalcfil afallhrvmq egvnvgvayg
       61 lwasggvist allsaalfge plgavklagi alimagvfcv emgakpdedq dhtvevapq
//
LOCUS       WP_284821888             268 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium
            tuberculostearicum].
ACCESSION   WP_284821888
VERSION     WP_284821888.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..268
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28578
     Region          3..262
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mlitdpadpr lddirnlnks dksgeglvia egplvvsrla esrfpmrclv gfpkkveayi
       61 seygepecpi yevsretlae vagfdmhrgl vaaadrapep evseivesak tiavlegvgd
      121 henigaifrh aagmgvdavl lgsgaadply rrsvrvsmgh vlrlpfahle ggfttwqrsl
      181 qaladasftl isltpnpqav hlaeamhgld kvamlvgaeg pgltehamka tdiraripma
      241 pgtdslnvat aaaisfyerq rslsdlnv
//
LOCUS       WP_284821951             147 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF1990 family protein [Corynebacterium tuberculostearicum].
ACCESSION   WP_284821951
VERSION     WP_284821951.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..147
                     /product="DUF1990 family protein"
                     /calculated_mol_wt=16760
     Region          2..145
                     /region_name="COG4762"
                     /note="Uncharacterized conserved protein, UPF0548 family
                     [Function unknown]"
                     /db_xref="CDD:443794"
ORIGIN      
        1 mptplsysdv sdfpqlhmsr vidadfdaaa hrlfrwsvqr sglfrvrpth evvelgaevt
       61 mglgpwdfrc rvvdvfyedg rcgftygtlp ghlergeetf tlerlrdgrt vllidaasep
      121 flpflrplvd vprrllisrl ylhalde
//
LOCUS       WP_284822202             208 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium freneyi].
ACCESSION   WP_284822202
VERSION     WP_284822202.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium freneyi
  ORGANISM  Corynebacterium freneyi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Corynebacterium freneyi"
                     /db_xref="taxon:134034"
     Protein         1..208
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21632
     Region          10..205
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(34..35,37..38,41..42,77,81..82,85..86,101,105,112,
                     115..116,121,144,148..149,151..153,155..156,159..160,
                     163..164,184,186..188,190..191,193..194,198,201..202)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(147,151,154..155,157..158,193,196..197,199..204,207)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(168..175,184..185,188)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 magrgalvvp lsvyvkrdsp vhrmpalpkl glvvafivva tifartipta avalavalcg
       61 yavaripfkv avaqllgavp llaliaviqg ltgnwelgam lflqilacvi aatlltlttr
      121 vsdlmnafdr llaplgrigl pvatislams ltlrlvplqv qavrevldar rargasasat
      181 afgvpviirt irrsramsda llargvgd
//
LOCUS       WP_284822295             486 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Corynebacterium striatum].
ACCESSION   WP_284822295
VERSION     WP_284822295.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..486
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=54724
     Region          32..444
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 msdnhiydci ilgtgygglg mgaqlakdnl enflileaad evggvwrdnt ypgaacdtqa
       61 liycysyfln lgvsrmfagq demlgylkal atefglyehi kfnnrivrse wneelkawei
      121 atstgdiyyg rvfvgawgql skpkvpdfag retfegtqfh saewdhavdl kgknvavvgn
      181 aasavqlvpe vakeaghlav fqrsanyilp rnqviftdee lrefqenpes yrairqeihd
      241 tredgfertr kgtdatqegv eqamehltsq vndpelvkkl tptfafgckr ilrsddfypt
      301 fnrdnvslvt esieeitpqg irtadgvehe fdviiyatgf ysqefqgdlp vigrggldlr
      361 erwgnapeay lgmtvdgfpn ffmlygpntn lnhhsvvaml eeqdkyirqa veylrdnpdk
      421 vldvdpqvlr efndriqael nesafsadcs swyknedgkv innwsgnvae yqdltrtlel
      481 adygva
//
LOCUS       WP_284822232             300 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Corynebacterium freneyi].
ACCESSION   WP_284822232
VERSION     WP_284822232.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium freneyi
  ORGANISM  Corynebacterium freneyi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Corynebacterium freneyi"
                     /db_xref="taxon:134034"
     Protein         1..300
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30402
     Region          54..176
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mrrtkrmrma giaavtaala masagpagaa slaggddvgf pdfdwanddt cmpsadhprp
       61 vllvhgttsn agemenigra ladqghcvfa vnygaddssi vgqfpgalgl gdldasaeev
      121 hrairhvage tnagraagai dvlgysqgaa lvklamnehg daevvdtavy lagshrgttm
      181 ggidalniha vpeavaigda vlgrsslqqv vgseqvarlr alpdtqpgvr yavivsdddt
      241 tvtpprsgfl eagpgatvdn vavqdvcpga pridhvgird heigadlvad afagrtiacg
//
LOCUS       WP_284822447             468 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium freneyi].
ACCESSION   WP_284822447
VERSION     WP_284822447.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium freneyi
  ORGANISM  Corynebacterium freneyi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Corynebacterium freneyi"
                     /db_xref="taxon:134034"
     Protein         1..468
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=50198
     Region          17..404
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mpetsaarra irdrparflr rlhfyaglmv gpfllvaais galyalaptv ekvvyadllt
       61 vdaaphsvsv geqveaaaat spgssvaqiw pahdpgdttr vlfddpsstd ktlpaafvdp
      121 ataavvgeer tysglgelpl rrwlsglhqh lhlgepgely aelaaswvwv lalgglylww
      181 rrvsaarrrd pgtrtrlwrt apapkgdvgr rrrslnlhav lgvwlivaml glaatgitws
      241 qkaganvdav vsaldwkapk vdaslppesp gagrpaspaq adrviaaart egltgplvlr
      301 pptetgegwr vserwvewrt asdsivvdga dgsvvsrqpf aelpffskls swgiylhmgv
      361 mfglplqlal favglgiaai ivlgyrmwwl rrptvrgtsv pglpdvpswr ivagvvvfaa
      421 tvgaflpllg isligfllld lvligrsrar rrtvekqrep ailsggvp
//
LOCUS       WP_284822515             205 aa            linear   BCT 25-DEC-2024
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Corynebacterium freneyi].
ACCESSION   WP_284822515
VERSION     WP_284822515.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium freneyi
  ORGANISM  Corynebacterium freneyi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Corynebacterium freneyi"
                     /db_xref="taxon:134034"
     Protein         1..205
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21706
     Region          26..201
                     /region_name="YdeN"
                     /note="Predicted esterase of the alpha/beta hydrolase fold
                     [General function prediction only]; COG3545"
                     /db_xref="CDD:442766"
ORIGIN      
        1 msekhhdpvt dlpdgvdads grprvvivhg yngypakhwy pwlatelvga sfpvtrvalp
       61 eptrpdpaew aaalaeqagt ldgavvvahs lgcitvlshl erhpeqrphg lvfvagfdar
      121 vaalpelddy igdgvgteel lprlgevavv msdgdhivpn adtaamagrl gvepivvpga
      181 khflysdgvt evpevrdavl rilst
//
LOCUS       WP_284822528             402 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Corynebacterium striatum].
ACCESSION   WP_284822528
VERSION     WP_284822528.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..402
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42890
     Region          30..224
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 maddkntstt qrvklstreq lrsvdrsmks rfarvksrfm filqstlgag laffvahvvf
       61 ghsqpffapm sviiilglsg sdrlkravdl siggivgviv gtllvdgvgt gpvhmtiiig
      121 cslliasfvt ssqlvsnqia igailiatim ppeemgglsr aidaiigavi gismvalipt
      181 splravrkei skvlgvassv lsdvaeglra ndprtilear davrgtqgdi nsmlnaakgg
      241 aetvkvspfl wsrqrnvksl eriltpvdna vrgvrvlsrr alvlaedgdh vtdeqielid
      301 elsdvtmels elyaqessne sraneavvip eivrklrilg arstmevige dgvlsaysll
      361 aqtrsiivdl lmvsgmsres avaqlaptsd hpayppevwd ge
//
LOCUS       WP_284822743             447 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium freneyi].
ACCESSION   WP_284822743
VERSION     WP_284822743.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium freneyi
  ORGANISM  Corynebacterium freneyi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Corynebacterium freneyi"
                     /db_xref="taxon:134034"
     Protein         1..447
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=47444
     Region          1..446
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrmtvigtgy lgathaacma elghevlgvd vdpakieals qgrvpfyepg lpellrkhvd
       61 sgalrfttdy deaaefaelh fvgvgtpqvk gsnaadvryv davidelakr itgdhvilgk
      121 stvpvgtaqr lqeradalia arsgdgepva tvdlawnpef lreghavkdt lepdrmvlgl
      181 ganstraeaa trecfapild rgtpmivtdl atselvkvsa naflatkisf inavseicet
      241 tgadvtvlad aigmdprigr rflnaglgfg ggclpkdira fmaragelga dqamtflrev
      301 dainmrrrek avglvkqafg gnvlgrqvav lgaafkpdsd dvrdspalsi agslslagaa
      361 vrvydpqamd narkvfptld yresvadald gaeivavate wdefrnldpv aagewvaakk
      421 lidgrnclpv dewraagwdv tclgrgn
//
LOCUS       WP_284822918             534 aa            linear   BCT 25-DEC-2024
DEFINITION  aspartate:alanine exchanger family transporter [Corynebacterium
            striatum].
ACCESSION   WP_284822918
VERSION     WP_284822918.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..534
                     /product="aspartate:alanine exchanger family transporter"
                     /calculated_mol_wt=54893
     Region          3..533
                     /region_name="YbjL"
                     /note="Uncharacterized membrane protein YbjL, putative
                     transporter [General function prediction only]; COG2985"
                     /db_xref="CDD:442224"
ORIGIN      
        1 mtqllaflad qpillvfali gvgmalgnik lkgvslgaaa vlflgiafaa asastgsavs
       61 vppvigtfgl vifafgignn sgivffqslr tatapvlsmi avfiiaaiaa htvgtyvfgl
      121 disviagtfa gaitntpsla aaaeatgdga aatvgyavsy lfgvigmmiv atlllrdapn
      181 dtdkaapvtr vhmqitrkeg isiadllaag nneiqvirlr rvgsnliiip gyldelnpgd
      241 vvtvvgtpkd ldavllaggr espqildddr hdldfrriti sqhqlagkti aqvnnalndr
      301 wgarisrirr gdedqvanpe flvelgdrvr vvgpaghlka iskylgdssh gltdinpval
      361 glglalgill ghidiplpre atlnlgaaag vllvalvmgr igrigkmita lphsantvla
      421 dlglllflaq agtnaggqia gafssgawwk illlgmlvtt ivavgialvm hrmlgngatk
      481 tagilagaqt qpailafvnn rtaadtrval gytlvypaam iskilithgl allg
//
LOCUS       WP_284823120             953 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium freneyi].
ACCESSION   WP_284823120
VERSION     WP_284823120.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium freneyi
  ORGANISM  Corynebacterium freneyi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 953)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 953)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..953
                     /organism="Corynebacterium freneyi"
                     /db_xref="taxon:134034"
     Protein         1..953
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103459
     Region          2..951
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtvlddfiae lgfapddfql racrsiaagr gvlvcaptga gktvvgefai raalddggkc
       61 fyttpikals nqkyndlvav ygedrvgllt gdvsrngdad vvvmttevlr nmlyaqsptl
      121 nrlshvvmde ihyladrerg pvweevilnl desvtlvgls atvsnseefg dwlstvrgrt
      181 dvvvtdrrpv plsqhmlvgr rlyplfeagg tevnrdllda aaraesgydd grggggrggh
      241 ggdrgfrggg grrgrgshsg shsdsgsggg nylgggkfar hqwtrrqetq kwrpprrsdv
      301 vkllgsrsml paivfifsra gcegalqqlg asrmeltsia eqeeiaaiid agvadipaed
      361 levlgfrrwr rtvvrgfaah hagmlpafrh iveklfnrgl vkvvfatetl alginmpart
      421 vvleklvkyn geahvdltpg qytqmtgrag rrgidtqgna vvqwapamdp kwvaglastr
      481 typlvstftp gynmsinllr tlghadarkm mersfaqfqa dgdivgdvae lerararvkq
      541 ltaelgaadd gpggdvegll aylelrstis aeekaakrrn iedrhtetvt vlrrlrrgdv
      601 iaipvgkkaq laavvredsa rhrprptvvg vggftgriep dafpsapevl grvkvpsdaa
      661 rhprravniv rseidrhgir gpkrlrrrts vtspelkrlr relrdhplhg dpavesvard
      721 adalrraqnt vatlerrvaa asdtlartfd rvldllgeld yvewpgggdg egggegggrg
      781 epfvseeger larihngsdl laaqclrrgi wddldpaela gavstlvfen rkatqgsdev
      841 pteplaaais dtfriwqela sdeqrhrlpm trmpdlafat aihqwtagap lgyclaaakd
      901 agaeltpgdf vrwcrqvvdl laqvrqtgys erirdnasqa vqairrgvva lgn
//
LOCUS       WP_284823256             257 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Corynebacterium freneyi].
ACCESSION   WP_284823256
VERSION     WP_284823256.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium freneyi
  ORGANISM  Corynebacterium freneyi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Corynebacterium freneyi"
                     /db_xref="taxon:134034"
     Protein         1..257
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26224
     Region          115..257
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mnddmnrgdg arddvrphev hrddvhrddt vragepgaav eatgpvsvpr gsartstmia
       61 vilavvgtva vlwfavsqtm ggddgtvtga agedelveep vaprpdcpep apgaagsgpl
      121 agvtlpclga ehqgeidvaa alagtpavvn vwswncapcr eelpvleewa aanpdvrvvg
      181 vqaatsearg aalledlgle tfvsyqdgfd avgpalelpr vvpitvvlra dgtvaavlpq
      241 afdsvdefda avrgala
//
LOCUS       WP_284823300             481 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium freneyi].
ACCESSION   WP_284823300
VERSION     WP_284823300.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium freneyi
  ORGANISM  Corynebacterium freneyi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 481)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Corynebacterium freneyi"
                     /db_xref="taxon:134034"
     Protein         1..481
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48784
     Region          31..456
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(41..42,45..46,49,85,135..136,138..140,143,163,
                     166..167,170,286,289..290,293..295,298,325,329,378..379,
                     383,387,403,406..407,410..411,414)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mtptttgtta artapgpwas pthrrsvllv laivaiailf dgydlviyga vlptlladps
       61 qigaltpeta gtlgawalig vlvgaltaga vgdrfgrkrv mlaasvwfsa gmaataltts
      121 attfgffrfl tgvgvgmiva tggaiiaefa prgrknlfna ivysgvpagg vlasvlaill
      181 ldaigwrglf ligatpllfl vpmivvalpe sprwlvsvgr teealavcer hglpqadfip
      241 aasantasah datnatpapa paekvgyaal fsrtyamgai ligfmsftgl lltyglntwl
      301 pkimenaggq akgsllflvv lnggaiaggl aaswladrig akrvvaatfl iaalclvalp
      361 mnlplgvlya avaiagfgti gtqvlvyglt anyfgteara agvawcagfg riggilgpvi
      421 ggviigagls sgsalyifag lalvgsvlta lvprspaqeq riellpeter atestpvaat
      481 k
//
LOCUS       WP_284821640             450 aa            linear   BCT 25-DEC-2024
DEFINITION  TrkH family potassium uptake protein [Corynebacterium
            tuberculostearicum].
ACCESSION   WP_284821640
VERSION     WP_284821640.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..450
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47069
     Region          12..445
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mkhllsirqw gparltaagf lvlilvgtvl lmlpfaeagt arasflsalf tatsavsltg
       61 livvdtgsfw spagqviilv liqlgglgim slaslsgllf tgrisfkark tgayegrpia
      121 pggirktlif tfaftavaet iiavivaarl migyghsfpr avwegifhav safnnagfst
      181 nsdnlvpfvs dawillplaa aliggglgfp vwaelvrlvr rdrhvvhris itarmtlaat
      241 tvlllaggvf facmewtgll ssmslgdkll nsffasaspr tagfnaidyg qahpitlmgt
      301 dilmfigggs agtaggikvt tacvllaama aefsgrettt ighrslprsv trqalalsfa
      361 gvmvvtlgva alrffdpefs gdqvsfevls afatvglstg itaslsapsq ivlclimylg
      421 rvgpttlvaa laaksvsrry sypeerpflg
//
LOCUS       WP_284823313              61 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            freneyi].
ACCESSION   WP_284823313
VERSION     WP_284823313.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium freneyi
  ORGANISM  Corynebacterium freneyi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 61)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 61)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 61)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..61
                     /organism="Corynebacterium freneyi"
                     /db_xref="taxon:134034"
     Protein         1..61
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=6468
     Region          2..51
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mklypipavm eetglgrtti fglissgelr svkvgrrrlv paaaldeyia nltgdnthev
       61 a
//
LOCUS       WP_284823388             469 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Corynebacterium
            freneyi].
ACCESSION   WP_284823388
VERSION     WP_284823388.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium freneyi
  ORGANISM  Corynebacterium freneyi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Corynebacterium freneyi"
                     /db_xref="taxon:134034"
     Protein         1..469
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48798
     Region          1..445
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mneffnalds fvwspfllip vllgtglwlt irlgavqlrm lgpalrlgli dredeggegd
       61 isqyqalata laatvgvgni vgvataigig gpgalfwmwv tglvgmasky geaflgvkyr
      121 tvdaageqsg gpqyylkkai pntfgkvlay vfavfaaiaa fgignltqgn avatnlntaf
      181 glpleatgal mfvlvgavli ggiksigrft aafvpmmiil yigaaiwvlv anisgvpgal
      241 alvftdaftg tsavggfaga giilviqmgv arglfsnesg mgsgaiaaaa attthpvrqg
      301 lvsmtqtfid tlivvsftgl viittgtwee gaddagamta hafsaglpgd fggdlvamsi
      361 vffafstmlg wsyygerafe sivgrrgtip yrfvftcvvy lgavteletv wafasalngl
      421 malpnliglv ilsgliaret kayldfdpql rasarevaew ernraisgr
//
LOCUS       WP_284823408             361 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Corynebacterium freneyi].
ACCESSION   WP_284823408
VERSION     WP_284823408.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium freneyi
  ORGANISM  Corynebacterium freneyi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 361)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Corynebacterium freneyi"
                     /db_xref="taxon:134034"
     Protein         1..361
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39344
     Region          49..345
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mrdrirerlg sdielddlpd hallgvirmp qtarrgpwrl iarrlgyala mmliatfvvy
       61 ldkggytepl tfvdalyysa vslsttgygd itpvterarm mniliitplr vvflallvgt
      121 tltvlteesr ralqiqrwrk qmrnhtvvig ygtkgrsaia alladgvdps qivvvdqdqq
      181 aldqasvrgl vtvhgsatka dvlklagvpr arsvvvapnk ddtavlvtls vreiapgati
      241 vasvresenr hlltqsgadq vvissetagr mlglatvtps vvemmedlls pdegfsvaer
      301 lvteeeigan prhladivlg vvrsgelyri dspecesvep gdrllyvrrv lkedsdpdvv
      361 k
//
LOCUS       WP_284823494             266 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Corynebacterium breve].
ACCESSION   WP_284823494
VERSION     WP_284823494.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..266
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30597
     Region          3..238
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mtttlwavsd lhaavkanha hiatltppnp ndwlivagdv aertdvvvrv lgeftqryak
       61 viwvpgnhel fcratdrarg rhkydelvla lrrigvvtpe deypvfdgvt ivplftlydy
      121 sfrgpgmtve eavkaaeekh immtdelaia pfvdvrawcw drltystkrl sriegetili
      181 nhwplvqept mrmrwseial wcgtrhtrgw aqrynakavv yghlhipdvt tydgiehiev
      241 slgypkewsk yereepwpyp vleved
//
LOCUS       WP_284821596             528 aa            linear   BCT 25-DEC-2024
DEFINITION  inorganic phosphate transporter [Corynebacterium
            tuberculostearicum].
ACCESSION   WP_284821596
VERSION     WP_284821596.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10475700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..528
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006817 - phosphate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56103
     Region          62..511
                     /region_name="PHO4"
                     /note="Phosphate transporter family; pfam01384"
                     /db_xref="CDD:460184"
ORIGIN      
        1 mtdietvngk gndwiwhaif ggltavtlig fmiwghdyvd gskpillgta iifalfmafn
       61 iggndvansf gtsvgagtls mkqalvvaai fevsgailag gevtdtvrsg ivdldaidgl
      121 dpmefvyimm ssllgaaiwl lvatrmgwpv stthsivggi vgaaltvgfv tgkggldmvq
      181 wggigtiais wvlspvlggl aafilfkwik tsilvyneea dqklreiktr raelrqehks
      241 rfarlneiqq isytnamard aalvaeedfd pdqleseyyr dlynlnkdmd dvkahrales
      301 wvpvlaaiga iiisamvmfk glkhtgldfs vlqnllvmgm vgavvwmavf ifarslkkks
      361 lakstfllfs wmqvftasaf afshgsndia naigpfaavi dvlktdqvsd eaavpvavmi
      421 amgvalisgl wfigrfviqt vgsgltqmhp ssgfaaelaa aavvmgssil glpvssthil
      481 igavlgvgiv nkaanwnlmk pialawvitl paaaviaait vsvlrvvf
//
LOCUS       WP_284823623             173 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium breve].
ACCESSION   WP_284823623
VERSION     WP_284823623.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 173)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..173
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19619
     Region          4..160
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04693"
                     /db_xref="CDD:467575"
ORIGIN      
        1 msiekwdvyd vhrnrtgkiv drgtphgpge fhlvvtlclf dergrmliqr rsdekelwpg
       61 lwdvtvggsa vagensqeam qretfeelgi aldfsrlrpa ftanyrngfd dvyvlrhpva
      121 latlaipnre vvaatwatrs evaeliragq flnyrasfid fawdfidrtd vfa
//
LOCUS       WP_284823637             488 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Corynebacterium
            breve].
ACCESSION   WP_284823637
VERSION     WP_284823637.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..488
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=52070
     Region          1..453
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 metaeqfita tindnlwmvv pwvlilagvy fgvrtivvql rmlpdmfryv aekpatddrd
       61 shddgisafk aftisaasrv gtgnvagvav aismggpgav fwmwliaiig gatafiestl
      121 aqlwktkded gnyhggpayy mtrglgwkpl avffaialsi tygfvynaiq tnsivesmgq
      181 sfhadsttfk liigaavall tgaiifggvt riasatqiiv pfmagayiiv gvivlalnit
      241 eiprmfsdiv thalglreia gatlgaafmn gvrrglfsne agmgsapnaa atatvshpvk
      301 qglvqtlgvy fdtlvvcsit afiillgptp kygeeiqgas ltqaalsdsv gawgthfltf
      361 ilfflafssi ignyylaqan iqyltesktv lnlfravvlg fvffgavgsi plvwalgdtf
      421 aalmvfinlv aivplggvai kllknfteqr aqgkdpvfhr dmlpelknve fwdgtdaatr
      481 ggqqnliv
//
LOCUS       WP_284823642             178 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Corynebacterium breve].
ACCESSION   WP_284823642
VERSION     WP_284823642.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..178
                     /product="YceD family protein"
                     /calculated_mol_wt=18760
     Region          1..178
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 matnpfvfnv vevlhgdgmp qvvtqtgpsp srigpemiai paggdvtvva tltnlgsgvl
       61 vdatataqlk gecvrclkel tpthdvtisq vfsthdefit gdpeddedmg sgdevkrved
      121 dcvdleqafi deaglslpfn ptcqpscdse stdvpapdgv sgeeervdpr waglekfl
//
LOCUS       WP_284823811             176 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium breve].
ACCESSION   WP_284823811
VERSION     WP_284823811.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 176)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..176
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19140
     Region          4..156
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18879"
                     /db_xref="CDD:467590"
ORIGIN      
        1 mpipefivet rkkighdpmw lpavtavvlr dstddspwav pevllvkrsd ngqwtpitgi
       61 cdpgeeahvt avreteeett iktkpaallg vgavgpvvha ngdqasymsi alrlevdgdp
      121 fqepavgdde svevgwfsia hmpvtnpkwr lviadaaaqr khpkaftprm gfekrn
//
LOCUS       WP_284823860             276 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium breve].
ACCESSION   WP_284823860
VERSION     WP_284823860.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..276
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30426
     Region          15..259
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mnlskyfenw pvndvaaavv gsteaehgdv drifhlmsvt klfsayaflm aveegvfeld
       61 qpagpegstv rhllahasgv gfasreqerp lgerriyssa gfewladile eetgiamrhy
      121 ardgvfrplg mddtaiygsp ghdgrstvad mekfarellq ptllhestvr eaftpqfpel
      181 rglvpgygmq kpcpwglgfe irgrkaphwm gtgvpeetvg hfgmagtylw avpswsdhel
      241 agtaaicltn rqfgnwakpl wedtntslad elltlk
//
LOCUS       WP_284823933             255 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Corynebacterium freneyi].
ACCESSION   WP_284823933
VERSION     WP_284823933.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium freneyi
  ORGANISM  Corynebacterium freneyi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Corynebacterium freneyi"
                     /db_xref="taxon:134034"
     Protein         1..255
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27306
     Region          7..252
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mpsknvtfig stghtlaati dlpdgepraw alfahcftcn rkvpgaartc ralakqgiac
       61 lrfdftglge sggdfadttf ltnvddlvaa yefmeaeyra psllvghslg gaaailagqr
      121 mpkvkavati gapfdpahsi yhfadaigdi dahgtqmlsi agrdipisre fletladinp
      181 etyihklrtp llllhsptdq tvgidsaqki flvarypksl isldkadhll ikpgapqraa
      241 dlirtwaepy lpesa
//
LOCUS       WP_284824160             478 aa            linear   BCT 25-DEC-2024
DEFINITION  acid phosphatase [Corynebacterium freneyi].
ACCESSION   WP_284824160
VERSION     WP_284824160.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium freneyi
  ORGANISM  Corynebacterium freneyi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130290
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Corynebacterium freneyi"
                     /db_xref="taxon:134034"
     Protein         1..478
                     /product="acid phosphatase"
                     /EC_number="3.1.3.2"
                     /GO_function="GO:0003993 - acid phosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=50648
     Region          151..344
                     /region_name="PAP2_acid_phosphatase"
                     /note="PAP2, bacterial acid phosphatase or class A
                     non-specific acid phosphatases. These enzymes catalyze
                     phosphomonoester hydrolysis, with optimal activity in low
                     pH conditions. They are secreted into the periplasmic
                     space, and their physiological role remains...; cd03397"
                     /db_xref="CDD:239491"
     Site            order(239,246,277..279,312,318,322)
                     /site_type="active"
                     /db_xref="CDD:239491"
ORIGIN      
        1 mktgsrrfsr aglrsaaavt alaltlplap taaaqaipel ptrdaipglg dvipgrtgda
       61 aapegrgdav pgeagdivpg atgdalpgvt gfppmgapsf ipsqdqgtga dgapvpqpfp
      121 adslarpfts dtsnegwfyh yvvhpfrdle qnhpevmden leivvrinna akddreaqll
      181 alqddhddpm vnlsagfgqn lgahfraave egrlpkttal lsgnlaragg iasstfveky
      241 tynydrpfvv aperieryyr dnpgdddpys etpsypsght nkaawtatlm ammlpevapq
      301 iqarsseagq srlvmgvhyp ldvmggrmmg nqaaadrwad pefrplieaa aaelraelew
      361 rcgttlaeci aadtpymsde aavaqyterm tygfkrvgea gvgvtvpagy agllatthpq
      421 ltdeqrvkvl eataidsgyp ldrtdgrash vrmnmaaama anvtvnadgs ltvngvrv
//
LOCUS       WP_284824177             610 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Corynebacterium freneyi].
ACCESSION   WP_284824177
VERSION     WP_284824177.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium freneyi
  ORGANISM  Corynebacterium freneyi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Corynebacterium freneyi"
                     /db_xref="taxon:134034"
     Protein         1..610
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66383
     Region          1..610
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mreysaeaky vvgeketivt amqelvakrp klvmftrpkn fewvnvtaqe fhdeamavak
       61 gliangvqkg drvallsetr yewnliniai wmagativpi ygsssagqir wiiedsgavf
      121 aitesrqhte rmknliidds ghaplsespt qlrrvleina savdtlmyeg rdiddsevqs
      181 ridsttcddl asviytsgtt grpkgcmlvh snwlaearai ltndigviar pgnriltflp
      241 lahvlanavs lasiiggatq shwadtstvt lefqrsrphl ilgvprvfek vrdsaqagak
      301 ekgafgtalf eraeaaaiey skaldtpsgp ttaqklrlkl ydkllfgkik aamgeavqyt
      361 isggsalssd lghffrglgv tvyegyglte staaitvnnp ndqvigtvgr pvggcavkig
      421 ddgeillkgp vvfkgywqne eatkaafdge wfktgdlgel detghlritg rkkdlivtag
      481 gknvspgpme drmrshplvs qavvigdgrp fvsvlvslde eavekwkaeh nvpehtpvre
      541 laanavlrae iqdavnsane lvshaeaikk fhilprdlse eageltptmk vkrnvvvdky
      601 sreiedmytr
//
LOCUS       WP_284824212             542 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Corynebacterium freneyi].
ACCESSION   WP_284824212
VERSION     WP_284824212.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium freneyi
  ORGANISM  Corynebacterium freneyi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Corynebacterium freneyi"
                     /db_xref="taxon:134034"
     Protein         1..542
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=60125
     Region          2..490
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mndsvrktev livgagfsgi tagvrllreg iedfqiidrg hevggtwrdn typgaacdvp
       61 shlyslsfaq nfdwsrsfgt qpeiadyqrs vavqqglyph irfrtemvda rwddaagrwl
      121 vttrefphvl ddvdgrtava msgeladkvf gggaggdard gegtaaepet ttwsarelvl
      181 gvgalceprl pdiegiggfe gtifhssrwd hdadlrgkrv avigtgasai qiipkiapvv
      241 ghldvyqrta pyviprldra yagweraalr nvpglrrvvr aqdwffrelq ipgltkndal
      301 mapikglsla mlraqvrdrk lrekltpkft igckrmlisn tyypaiardn velvtdpiqr
      361 vnahsittad gterpidvli vctgfhvtds ptfelvhgrg geslaeawrr egmsahkgtt
      421 ihgypnlsvl mgpatglghs smiymiesqa nyfmdmlrtk rrhgadvaev seraqgewnd
      481 wirkrlpdtv wvsgcgswyl ddhgnapavw pswtwkfrlk trkfdassyd lrvarpalep
      541 sr
//
LOCUS       WP_284824268             118 aa            linear   BCT 25-DEC-2024
DEFINITION  FluC/FEX family fluoride channel [Corynebacterium breve].
ACCESSION   WP_284824268
VERSION     WP_284824268.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   McIlwain,B.C., Gundepudi,R., Koff,B.B. and Stockbridge,R.B.
  TITLE     The fluoride permeation pathway and anion recognition in Fluc
            family fluoride channels
  JOURNAL   Elife 10, e69482 (2021)
   PUBMED   34250906
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Li,S., Smith,K.D., Davis,J.H., Gordon,P.B., Breaker,R.R. and
            Strobel,S.A.
  TITLE     Eukaryotic resistance to fluoride toxicity mediated by a widespread
            family of fluoride export proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (47), 19018-19023 (2013)
   PUBMED   24173035
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Stockbridge,R.B., Robertson,J.L., Kolmakova-Partensky,L. and
            Miller,C.
  TITLE     A family of fluoride-specific ion channels with dual-topology
            architecture
  JOURNAL   Elife 2, e01084 (2013)
   PUBMED   23991286
  REMARK    Erratum:[Elife. 2013;2:e01700]
            Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..118
                     /product="FluC/FEX family fluoride channel"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:1903425 - fluoride transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:1903424 - fluoride transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12100
     Region          13..105
                     /region_name="CRCB"
                     /note="CrcB-like protein, Camphor Resistance (CrcB);
                     pfam02537"
                     /db_xref="CDD:460582"
ORIGIN      
        1 mtavlavvtv vaggflgglg rwalakipge fvgtwtanmv acvilgvait gpgivplalg
       61 tgcagalstw stlakqfgel vlarrwtmla tyfvatmavg mvaawrgtiw gariwgyl
//
LOCUS       WP_284824405             702 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Corynebacterium breve].
ACCESSION   WP_284824405
VERSION     WP_284824405.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..702
                     /product="PhoX family protein"
                     /calculated_mol_wt=76574
     Region          108..695
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 malkglnlfs nkftssrssl tctykcgnnc fgecrnttdn eyfgdmtrrs alkagslsvv
       61 avggaaalaa cspseeeaas sgsssadgsa aptkdvkvdt vsvdgmkfep vepnnnddvt
      121 vpegyeysvl vawgdpiieg apefdienqt akaqeeqfgf nndflglfdh pedenkmvyv
      181 csheyttepq mhpnydaenp teeqvnigla ahgqsiievs kvegsgelkm efgplnrrit
      241 amtpmtfsgp aagtdllktn edpsgmevlg tlnncaggvt pwgtylsgee nidqywtnsk
      301 aldgrnkeya drigveeegq sergwelfhd rfdmekepne inrfgyivei dpmdpeskpv
      361 khtllgrfkh eagnthiadd gravvymgdd erfeyiykfv tadkykegdk ehnmklmtag
      421 tlyvaslegn skedeidgsg elpedgqfdg kgtwhplvtv didgnaeshi egfspeevcv
      481 ytrlaadtvg atkmdrpedf eqnpvtgkay valtnnsyrg atgenakkne eepmewapik
      541 enkngfvmei ddaekgtgee ftwnlfivcg dpeeaytyfg gfdkekvspi scpdnvafdk
      601 hgllwistdg nalgthdgly aastegdtrg elkcfmtvpa daetcgpyid dehvlvnvqh
      661 pgegdestve npssnwpegg dakprpaavv vwktdggkig ma
//
LOCUS       WP_284824464             714 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Corynebacterium freneyi].
ACCESSION   WP_284824464
VERSION     WP_284824464.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium freneyi
  ORGANISM  Corynebacterium freneyi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 714)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Corynebacterium freneyi"
                     /db_xref="taxon:134034"
     Protein         1..714
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=78971
     Region          50..661
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mnapqkdlsp ppistiglpk pqtgdgygwk idgyaspade pidrevlenp apsvgamvlr
       61 ratatpdrpa wrfrdadenw veltwdqfrg vveehsagll daglrkgdaa alisgtsmqw
      121 vnsdmalmsi gvnsvaiypt svpgdiefii ndsgsrmvia edgdqvakll eirdaipgve
      181 hvyviddaws aqvqavtspa gtsaeeiadw vsplaaltar grallatdph vvrraidevt
      241 petiatfqyt sgttgkpkga iiphsawmnn vasvtstpsl ydkdvhflwl pmahlmgrfl
      301 lylsintgil taidgridki venlqdikpt lmggaprife kaysaihaqf egngikaklg
      361 kvsmalamea telrlagkev pkwlefrlri adkvvlskir dalggnvrmf vsgsapinqd
      421 itkwylsvgm pivegfglte gcithltrln ayrigsvgwp fpeveqkiae dgelllksaw
      481 nmtgyynred ataeslpgdg ylrtgdiari dddgfvyitd rkkslykssn gkyiapapie
      541 sefkglcpla melvtygegk kfmvgmvvle ekatrewcer ngceaetfad mtrdpkvvaf
      601 vqaslgrlns elnsweqvkr frildreltv dadeltpslk lrrkhvhekl kdkfeelyad
      661 pmapgchesa gvkwvsfeqp alhehpvlae dedihlrpsr hrrehrehre hrah
//
LOCUS       WP_284824506             389 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Corynebacterium breve].
ACCESSION   WP_284824506
VERSION     WP_284824506.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..389
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41404
     Region          21..216
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 makqrmgtla rleivdrslq srlsrvkkrl fsifqaalaa glaywvasrf vghelpffap
       61 iavviilgls gggrinrafe mslgcvlgvl lgdllfvrlg sgawqiaiav agsllvasff
      121 sksqlvsnqv aigsiliati mppgaettgi drtvdaiigs vialsviavl pasplvsgry
      181 eisnvlglss svlddvakgl rtkdsvlide aihaiqgsds qvdamlaatr sgaestkisp
      241 llwgarryvr slervvgpvd savrnvrvla rramvlvrdn dtvseqqvei iddlakisle
      301 lseiydvkte lnqaqeipil vnelrvlgak asldvldeds vlsayailaq srsiivdlle
      361 icgmsresan avlaptsetp afppelhee
//
LOCUS       WP_284824628             370 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium breve].
ACCESSION   WP_284824628
VERSION     WP_284824628.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..370
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40085
     Region          8..357
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mtggykvnrs tylgeleglr avaalgivvt hvafqtatds alfarfdyfv avffalsafl
       61 largghrkly pyiikrtari apaylacvgi vlvalpeags vslgqaaanl amlqiyvpdg
      121 liagltqlws lcvevafylv lplylalgrk grlvalvagi ivgfawpwlp fvrdsieifn
      181 vnlqiwpmsy aswfavglvc aelegrvspl vqrvlrarwv ywiaaltvaw lagqeyvgpl
      241 glehpsplef nirillgavf calivvpyal apsqgvlgge vmrtlgtwsy siflwhvavl
      301 tvvfpllgip mfsgyffavl aatvvlsiav syisyelver pgarwiqrvg garhtsaaqp
      361 attiatefpa
//
LOCUS       WP_284824662             815 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium freneyi].
ACCESSION   WP_284824662
VERSION     WP_284824662.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium freneyi
  ORGANISM  Corynebacterium freneyi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 815)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 815)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 815)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 815)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..815
                     /organism="Corynebacterium freneyi"
                     /db_xref="taxon:134034"
     Protein         1..815
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=83851
     Region          14..777
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mstptdtagr qfdldvggmt cascanrver klnkldgvta tvnyatekah vtvpdgfdpq
       61 qlidtidaag ysatlppppq peddggrpgd gasssnagqt aadrelealr nrligsavlt
      121 vpvilismfp vlqftnwqwl altltapvvv wagwpfhrat wknlrlgeat mdtlitvgtv
      181 safawslyal flgtagtpgl kheftlsvap tdgaanvyle vaagvimfvl ggryfekrak
      241 hragdalram ldlgakdvrl lddagerlvp astlkvgdrf vvrpgekiat dgrvveggsa
      301 vdesmltges vpvevrvgdd vtgatvnasg rlvveatrvg adtqlaqmak lveaaqsgka
      361 evqrladris gvfvpvviai atatlgawlg agfppsaaft aavavliiac pcalglatpt
      421 allvgtgrga qmgvllkgpe vlestrrvdt ivldktgtvt sgdmalvetw agegvdrael
      481 lrragavesa sehpiaraia dgaraelagg stvvgrnllv gsgddrpslp pvadfvnlpg
      541 rgvrasvrta dgpvevtvgr nlgempadla arfdaavsag rtavtvawdg girgvlvvsd
      601 qvkptsakai aelrglglep vlltgdnavv akhvadevgi ddvraevmpa dkvdvvkelq
      661 aegrivamvg dgvndaaala qadlglamgt gtdaaiqasd vtlvrgdlma avdavrlarr
      721 tlatikgnlf wafaynvaai plaalgllnp mlagaamafs svfvvsnslr lkgfrskaeh
      781 vggtvehags kaghvgdgsa eragdgtaar vkegv
//
LOCUS       WP_284824723             616 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Corynebacterium breve].
ACCESSION   WP_284824723
VERSION     WP_284824723.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12021846
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..616
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=67649
     Region          10..372
                     /region_name="FAD_binding_3"
                     /note="FAD binding domain; pfam01494"
                     /db_xref="CDD:396193"
ORIGIN      
        1 mtttsadltt dvlvvgsgpa gssaalflat ygieclvvsk ysntahtpra hitnqrtvei
       61 mrdigiedqi kaaevphhmi getvfctain geefgrvhsw gtgpdregey iaaspslncd
      121 lpqthfepil vrnamergav frwkteyvsh tqdaqgvytv vrdrltgqty tvhskyliga
      181 dggrsqiaad lelpmdgqmg vdgsmnihcd mdlteycqdr qsslywvlqp gaavggiglg
      241 lvrmvrpwne wlvtwgydin qpppemddak aadivrnlvg ipdleinirh wslwtvndty
      301 atenmkgrvl cvgdavhrhp psnglgsnts iqdsynlawk lamilkgqag eelinsyqde
      361 rvpvakqivr ranksisefs hvldalgidp adddeamqaa mdvrkqptee gerrrqalhk
      421 alkikdyefn algvemgqry essavvsdgt pwptqdtdpe lhyqptthpg arlphawlsp
      481 knpfapkvst ldlaggghft iltgtnghaw veaaaelaae lgidipayri gpdqdytdty
      541 gdwarlreia ddgcllvrpd nhvayrearl vddptaalrd altavlhlkg dektaqqakg
      601 eenphpnhrq letaga
//
LOCUS       WP_284824738             104 aa            linear   BCT 25-DEC-2024
DEFINITION  histone-like nucleoid-structuring protein Lsr2 [Corynebacterium
            breve].
ACCESSION   WP_284824738
VERSION     WP_284824738.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Gordon,B.R., Li,Y., Wang,L., Sintsova,A., van Bakel,H., Tian,S.,
            Navarre,W.W., Xia,B. and Liu,J.
  TITLE     Lsr2 is a nucleoid-associated protein that targets AT-rich
            sequences and virulence genes in Mycobacterium tuberculosis
  JOURNAL   Proc Natl Acad Sci U S A 107 (11), 5154-5159 (2010)
   PUBMED   20133735
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18741]
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Gordon,B.R., Imperial,R., Wang,L., Navarre,W.W. and Liu,J.
  TITLE     Lsr2 of Mycobacterium represents a novel class of H-NS-like
            proteins
  JOURNAL   J Bacteriol 190 (21), 7052-7059 (2008)
   PUBMED   18776007
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Oshima,T., Ishikawa,S., Kurokawa,K., Aiba,H. and Ogasawara,N.
  TITLE     Escherichia coli histone-like protein H-NS preferentially binds to
            horizontally acquired DNA in association with RNA polymerase
  JOURNAL   DNA Res 13 (4), 141-153 (2006)
   PUBMED   17046956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10570331
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..104
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11810
     Region          1..102
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 marreitqyy ddldntpiea eelhvirfsm dgndyvldls kenaqefhet lapfikaarq
       61 apsdvarrvn prevrkwaqs qgmaiahrgk ipfaiidayn eaha
//
LOCUS       WP_284824909             262 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Corynebacterium breve].
ACCESSION   WP_284824909
VERSION     WP_284824909.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..262
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29722
     Region          4..249
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mtrtlwatsd lhvtfpenqa ivdklmpqdp gdwlivagdv aeripdvtra lepltrrfak
       61 viwvpgnhel fnrrsering karyralvga lraigvvtpe dpfpvfgntt icplftlydy
      121 sfrplgltak qavaqatvvl ddefaiapyv dierwcaerv eysvdrlnav kgetvlvnhw
      181 plvvepthrl wepdialwcg teltrdwavk yharmvihgh lhipletrvd gvshvdvslg
      241 ypfekhppgp krpwpfpvmr vd
//
LOCUS       WP_284825006             103 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium breve].
ACCESSION   WP_284825006
VERSION     WP_284825006.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 103)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 103)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 103)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..103
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11232
     Region          1..95
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtnlernlnl aeewsgtfki mgdptrlkll naihfagqfk lsvseladat gvrvattsaa
       61 lramelngtv tstrdgrsil ygiaddhvhq llhwigsshl hqh
//
LOCUS       WP_284825031             119 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium freneyi].
ACCESSION   WP_284825031
VERSION     WP_284825031.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium freneyi
  ORGANISM  Corynebacterium freneyi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 119)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 119)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Corynebacterium freneyi"
                     /db_xref="taxon:134034"
     Protein         1..119
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12528
     Region          28..116
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 magtpttqri lpladptacc slgsgpltpd eaeryaalfr vladparlri lsklaaegcg
       61 pitvgeltgr lglsqptvsh hlkklsdagl leksrsgrtv thavrpelfa elrtvlqmd
//
LOCUS       WP_284825096             476 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium breve].
ACCESSION   WP_284825096
VERSION     WP_284825096.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..476
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48637
     Region          26..447
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(36..37,40..41,44,80,130..131,133..135,138,158,
                     161..162,165,277,280..281,284..286,289,316,320,369..370,
                     374,378,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mstaleqtpn qtwasgahrr tiylvlaivg isilfdgydl vvygavlstl lddpshigel
       61 spavagtlgs wamigvmiga lgagavgdrl grrkvmivai iwfslgmaat amstsifafg
      121 alrfvtglgv gvivatggav iaefapanrk nlfnaivysg vpaggvmasl lalvledaig
      181 wrglfmigas pllfllplal valpesprwl msrgradeaa stcerfglpk aqfmsepvaa
      241 lkeetnskqa adlnksgfag ifsrsylpgt iligtmsfig llstyglntw lpkimqanga
      301 sahdslysll alnggavlgg lfaswiadki gakavitstf glaalslail pqfntvapmy
      361 lpialagigv lgtqvltygl tsnyfgtasr aagvawcagf grlggivgpl vgglilgagl
      421 gptyafyifa gaaligaict aiiprspaaa tivsssealt qeeraqalae akavag
//
LOCUS       WP_284825122             710 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-glucosidase family protein [Corynebacterium breve].
ACCESSION   WP_284825122
VERSION     WP_284825122.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Varghese,J.N., Hrmova,M. and Fincher,G.B.
  TITLE     Three-dimensional structure of a barley beta-D-glucan exohydrolase,
            a family 3 glycosyl hydrolase
  JOURNAL   Structure 7 (2), 179-190 (1999)
   PUBMED   10368285
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444920
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..710
                     /product="beta-glucosidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0015926 - glucosidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=77208
     Region          26..459
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          354..594
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
     Region          628..699
                     /region_name="Fn3-like"
                     /note="Fibronectin type III-like domain; pfam14310"
                     /db_xref="CDD:433860"
ORIGIN      
        1 mtesqrpwmd dnlsdrerae klvenmtleq kiaqlhggme tiniyaasne idpededame
       61 qlamqiqier hvpeipelgi prfritngpv gvgmgdgtps ppatalpmti gvaasfdpel
      121 afkygdiigr etddlgqhvl egpgvclhrt vtagrnfeyf sedpylsgvm gievtkaiqa
      181 hdiiamakhy avndqeferf rtnvevdeqt lremyllpfe mvvkdgqvaa imsaynrvrg
      241 dyatenryll ndvlrgdwgf egyvqsdfws trsaaaslna gldhempdak wlnednvkaa
      301 ledtsleiel vdralvrryt qmfrfnqfdr eyapreidaa gngaisreig admavllknd
      361 knilpldpns agkilivgqe kfakyacqgg ggsskvdply tvdpepglrd viadlggsat
      421 vesfiverdl snlegaveaa kgadtvlima gliategadm ptmlmpqkqs dmiaellkan
      481 dnsvvvlkss aplvmpwidd aatvlevwnq gaedghvvgd lvfgsvnpsg kvpttypkte
      541 adwighdhpe rypgvnlgeg yntitysegl emgyrwfqan dvtpafpfgy glsytsfels
      601 dvsvagsaag vkvsatvknt gdvagaevvq vylgipsegq ppkrlvgfak vqvepgssaa
      661 veinidadat hhplsvwdva ardfvvpsge ftvyvgtssd ddshvekftv
//
LOCUS       WP_284825130             448 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium breve].
ACCESSION   WP_284825130
VERSION     WP_284825130.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..448
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47315
     Region          32..447
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(42..43,46..47,50,84,134..135,137..139,142,162,
                     165..166,169,276,279..280,283..285,288,315,319,369..370,
                     374,378,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mtsstanqsa esrrastspa tskprrsagf viflcfltiv fdgydlvvyg tivpallaye
       61 ewgltpvqtg aygsyalagm figaiivgyl tdvigrrkvl iasiiafsll mvatafapsp
      121 fwfgafrfla glglggvipt aiaitvefsr rerrnfnnal mfsgyafggi maailamlll
      181 phigfrgmla igalplvtil plvfflmpes paylrskgdv aeanavleqh glnpypptaa
      241 tddakrfdhe pkrksamael frsrfivatl lfclagiagq tlvyglntwm pqllvmadys
      301 insslsfllt tnvgavfgvl vssrladrvg pramvmfsfi asgtalvlmg tgifplwamy
      361 llvavvgfgs igaqilvngf vatfypddvr asalgltlgi grigaviaia gggvlvsmal
      421 stfanfsvwa iaagigliaa llvprapr
//
LOCUS       WP_284825225             832 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium breve].
ACCESSION   WP_284825225
VERSION     WP_284825225.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 832)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 832)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 832)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 832)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..832
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..832
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=92019
     Region          650..831
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          769..825
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mrnwegpgmg wisepslake fdldpevlna vidrvaqklh aklatgqlff trlpkeylaa
       61 qilvramstl dpqneprcfn fdtrrdaesl riefagplvi dvtgplnrcs sdsreenanr
      121 lrsrksktvl alqtndlsia esyvvradnv ftdsdlllsl tdleelsgeg vvveklldet
      181 ggvpgfvvaa ltdhargkar afpamarswa reivplvtnn laldamvwlp piaeyslrti
      241 vnqvapdglg emqlvsalas pavvaagtfp paypwqlkaa lqelslydda fcplhdyvsl
      301 ansdlvpfpd ricalaaeqw weeldalirt rpcwlilvpv svrrrlvalf paaiptsltg
      361 ldtakrffag eltqehvsgk npmwaelidl vpgtervrrq afaspgfepv sdvarelnef
      421 imrftvtgpr vetplhdpds avefldlcrt litehirkvt earepeildd tamlivllnt
      481 qadlaidlgl isiaddcsfq aqlllgrlgg asdayaplya nvlavrafvs gmvgnnqaaa
      541 gfieryrdls gptipeldsm vdlaellrld eecirktipl hveiesihaa teafcqgvrv
      601 asgygqdaai sywrsihdrv ewsaaatwrm wpvraalvsl ygvngqpkea rawldagwlp
      661 qplqrlaeii idlqvqpeqs leelekilge fnlptrwrmi algykiecli lmgtgegeia
      721 vavrgenwae higlssilpe narqrivehy gfdvsefpgl qphtgqsvee lserqlqile
      781 llatgklqre aadelgiste tvkatskkiy rklhvgnlqe avrvaraqgw lq
//
LOCUS       WP_284825292             279 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium breve].
ACCESSION   WP_284825292
VERSION     WP_284825292.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..279
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=29558
     Region          113..272
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 maettqttki palmwaftiv lalaaavggy figfsegkaq apanslatqe spaadtaeat
       61 eipdvepgke ftepqpnddg tfnaqlhgpg iegeqvarrd pndpfakgav dapivlsefs
      121 dfgcpfcarf atdteaelvq eyvdtglvrv ewndftingp nseaaaraar aaaeqgkffe
      181 fkdalfgdfd vnggqpytid ilagyaeeag vkdiekfkkd aesdkyddai ggakefaasl
      241 gmngtpsfvi gtqtmsgalp leefqkvint elaksqdka
//
LOCUS       WP_284825303             658 aa            linear   BCT 25-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Corynebacterium
            breve].
ACCESSION   WP_284825303
VERSION     WP_284825303.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Shan,L., Mathews,I.I. and Khosla,C.
  TITLE     Structural and mechanistic analysis of two prolyl endopeptidases:
            role of interdomain dynamics in catalysis and specificity
  JOURNAL   Proc Natl Acad Sci U S A 102 (10), 3599-3604 (2005)
   PUBMED   15738423
REFERENCE   2  (residues 1 to 658)
  AUTHORS   Polgar,L.
  TITLE     The prolyl oligopeptidase family
  JOURNAL   Cell Mol Life Sci 59 (2), 349-362 (2002)
   PUBMED   11915948
REFERENCE   3  (residues 1 to 658)
  AUTHORS   Polgar,L.
  TITLE     A potential processing enzyme in prokaryotes: oligopeptidase B, a
            new type of serine peptidase
  JOURNAL   Proteins 28 (3), 375-379 (1997)
   PUBMED   9223183
REFERENCE   4  (residues 1 to 658)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 658)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..658
                     /product="prolyl oligopeptidase family serine peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=72155
     Region          10..652
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mdtsispell dditapeala wagswsaktl agrdftalqs rirevldtea ripyvtrrge
       61 flynfwrdas hprglwrrtt ldsylsespt wqvlidvdal aategedwvw kgahvrtpdy
      121 dralirlsrg gadatviref ditsceflrn gftlpeaksd vswvdldtvl vgtdtgeesl
      181 tssgypvevr twrrgesied sevfargnyd dvllgawhdp tpgfertvva raidfyntit
      241 svsterglqt lelptdcepv lhqqwlfilp rtdfgavpag alavieldsf ldgsreftll
      301 lvpdahtsia slaftastll vtslvdvath isafelgtwq rselaipeas tasvvatspl
      361 dgdeywinas sfstpstllr ngetakqaps lfddtgletr qhwaesadgt kipyfitgdf
      421 slgkrptlvg gyggfevslt pgysavrgis wlekgyyfvq pnlrgggefg pqwhsqvvkt
      481 nrhkvwedhh avlldlvarg yceaqhigir ggsnggllts galvqypeaf gaaviqvplt
      541 dmlryhtlsa gaswmaeygn pddpeeraai ekwsplhnvs stsvyppalv ttstrddrvh
      601 pahartfala lakagqpvdy yentagghag aadneqtsrv ealiyswlee klatrvsk
//
LOCUS       WP_284825344             865 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium breve].
ACCESSION   WP_284825344
VERSION     WP_284825344.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 865)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 865)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 865)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 865)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..865
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..865
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=93841
     Region          191..863
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mnasrtplqg dvtqaideai raakaagidv ddgpkhvfda dqrpktsyaf elenlpdapd
       61 vgeiedalee ipgvwarivy ptntvwitap dvidptqlvk vmarfnvrat mtdsslrrrv
      121 selrspepat trrgnrgtkg msgrmrrqhe leaktiesar vsgflndpan tarhtppdnd
      181 llytardlit lkrlaiaivf gapvfltsyf qelqfpgwqw vvlalsipvv fyaawpfhra
      241 laggvrrglt aldgasslai llafgwsivl lvatpagdig wqaepkwlaf nhsrladgel
      301 fldvacgmti lllagriwtm rarpslleem ekrrpepsse vrvsvrnrat gavteemmpl
      361 aevnpgddii lvpgdiipvd gqvmggscvl epglvdared lnikvgskvy sgativsgki
      421 kvrvvhtghl trmaaihrwv qeashrqnra tllstktaay lipaafmlav adfvlwvliy
      481 qnynaamata lavlasvapt alalspamai rlgiessarn giiirdgatl rslenvdtvi
      541 fnrvgtlvqp fmtvetvtaa rgenadmvlr vagalamesn hpssqalvra areardhdeg
      601 gvdiphwidv akneitrngd lkarieivsr dddgeehtqq veamlwrptn lsslhgrlaa
      661 aatnggtpiv vrwkgkdrgv itlydpvkdd aaesitrled mgietvmlsr dtypvarrfa
      721 dllgisnvla gightdkpga vravhtqgat vamvgdrsvv ntlrvadvgi lvgsgdslet
      781 gnelredisv ivvrddvsai pqlieqarrv criidrnivy swvynisamv lavagllhpm
      841 aatvlmlgss lfvearslsv kkfps
//
LOCUS       WP_284825350             105 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Corynebacterium breve].
ACCESSION   WP_284825350
VERSION     WP_284825350.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..105
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=10768
     Region          2..105
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mnwfiligsg lfegvwanal aktegftklw pslvflvalv ismgglawam rsisagtaya
       61 vwagvgaaaa viiaiamgee svsvlkilfl vmivagivgl qvvsn
//
LOCUS       WP_284825481             463 aa            linear   BCT 25-DEC-2024
DEFINITION  MBL fold metallo-hydrolase [Corynebacterium breve].
ACCESSION   WP_284825481
VERSION     WP_284825481.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..463
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50941
     Region          2..194
                     /region_name="POD-like_MBL-fold"
                     /note="ETHE1 (PDO type I), persulfide dioxygenase A (PDOA,
                     PDO type II) and related proteins; MBL-fold
                     metallo-hydrolase domain; cd07724"
                     /db_xref="CDD:293810"
     Site            order(56,60,116,141,144,148..150,194)
                     /site_type="active"
                     /db_xref="CDD:293810"
     Region          383..457
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mlleriyeed lsqasyfigc qargeaivid prrdiqvyld lakkngmkis avtethihad
       61 ylsgsrelas atgaelylsd eggpdwsygf egnrlkdgds itignltlqa vftpghtpeh
      121 msylltdgaf tdrpgymftg dfvfagdlgr pdlldeaagg hdtrfegakq lfaslrdkfl
      181 tlpdyvqvhp ahgagspcgk algsvpsstv gyertfawwa kyletndeqg fidelldgqp
      241 dahayfgrmk renrdgpavm geraplkryt saeaiagqrd nevifldpra lddvrqgtva
      301 gainvawnak psmyvgwaid perdkrdivi ltdeeefaed mrnrfvrvgv dnvtgftsls
      361 delpaylpel vqpedldgfe hdllldvrnn sefrdgsipg aqhisagkvm wslnelpkdg
      421 tivafcqsgv rssviasslr eagfhvveld gsyaawslrq qha
//
LOCUS       WP_284825652             284 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium
            amycolatum].
ACCESSION   WP_284825652
VERSION     WP_284825652.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..284
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30583
     Region          10..280
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtswkpsvla qidqwpadtv aaavrandgs whthgdsgrv felasvtkll tavgmlvave
       61 egaveldqel tppghgatvr hllahaggvg fasrelekep gerriyssag fdiiadaiaa
      121 eaempfneyl rqavfeplgm edsvldgsag hgarssvanl mafvdeiftp tllhpdtvte
      181 altvqfpgln gvvpgygmqr padwglgfei fghpdskqgl wfgasmpkdv aghfgqagtf
      241 lwlhrptgra aialtnrafg ewakplwadf ndelwrelee haed
//
LOCUS       WP_284825599             625 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Corynebacterium amycolatum].
ACCESSION   WP_284825599
VERSION     WP_284825599.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..625
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=67170
     Region          <1..176
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mdlsgsmlad daggtrldaa krastelids lpddallgml vygqressde snrergcqdi
       61 evlspvqkvd keglksriag leaqgytpig nalrkaadel gpdgersiil vsdgidtcap
      121 ppvcevakel agqgvgltih tvgfkvdeea raelecvaqa tggqsmtadd atqladhmkf
      181 ltqrsvqgye ttgtpfefse tkedakwlge gkyqttlvpe vaqhdrtply yriavpkghn
      241 aivtskvlan idaegkgqqd vrtevdeiin etggkcqddg rmgsltgaea sadswtptsa
      301 dasilewdsd riesscdqtk wlvannvwvy dsesvadyrd epvkvevsvq fepvlkkqea
      361 dklnegrsss tgdkaykkat fgeakpvsgg nnaaqalevk sgdtisdtiv pgeqkyykip
      421 vewgqrpvva artgnserdn adsmgvalln pfevsvadgt mhfyrdseal nlatdrpiey
      481 nnrsanvggr pvanagyyya tvrmanyrpd eevsgidqpf qlaflldnks tkgpdwrptd
      541 kngptpsdkp ilakgeseqe sskdssedas kesdspdtds qasasssdme degmsplvig
      601 tvvavvavfi giagaivyqn kkrke
//
LOCUS       WP_284825900             368 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Corynebacterium
            amycolatum].
ACCESSION   WP_284825900
VERSION     WP_284825900.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..368
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=39921
     Region          1..321
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mrallisnpn stsnsarrmp sivralrsvd girltsmfta ypghaeemva gitvrdydvi
       61 islggdgtin eivnglmdsn pfsalsatel paiatiptgs anvlagalgi prdpvdaawy
      121 iasllrsrtr saisvghaae rcfvvnagig idaevistme qlrhngtrak avrylpaift
      181 awnelrkspp qitatidgke fgrdlamavv snsnpwtflg dlpivtnptv slrrglgfyg
      241 ftslkgvtgl vaaanlagff trlrspfhie arerrvdnaq hiqltatapl rlqldgeyin
      301 qrdslnirvk qgainfvara ddytedqftk kvatrpvder llvvvtkkam drtrrlfsts
      361 qkteanpa
//
LOCUS       WP_284825846             274 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium breve].
ACCESSION   WP_284825846
VERSION     WP_284825846.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 274)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..274
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29556
     Region          11..273
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mssnnpapqh itdpldprld dirdlktaek tlvvaegpli vgrlvesryp lrcligfqar
       61 leqflathkv qapvyavtre vlaqvvgydm hrgllavadr agessisqiv eesrtvvvle
      121 gvgdheniga ifrnaagmdv davllgsgta dplyrrsvrv smghvlrtpf ahldggfttw
      181 qrsldqlres gyrlvaltpd pqaehladal vddtgapyek vallvgaegp gltehamrat
      241 dvraripmaa gtdslnvats aaiafyersr slrd
//
LOCUS       WP_284825902             276 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Corynebacterium
            breve].
ACCESSION   WP_284825902
VERSION     WP_284825902.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..276
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30070
     Region          13..275
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mmtnqwnpvg pgllfapadr perfakaaer sdmvildled gcrpenreea raniqdseld
       61 pdkvivrvnp tttdefvldc ralattryrt vmlakaesen nvdtlakalp evqiialvet
      121 plgvlnaqqi aahdavvamf wgaedlvagl ggtssrtadg tyrmlpkyar ahvqvaaaay
      181 gkaaldsvyv nipdteglra evadaaalgy agtccihpsq veiireefrp seekidwasr
      241 llreaqsnrg afsfegrmvd eplfrqaqai vrragi
//
LOCUS       WP_284825925             243 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium amycolatum].
ACCESSION   WP_284825925
VERSION     WP_284825925.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..243
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26430
     Region          75..222
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 msqkiknpne kgsgfvvgli allavvavvi ggviyigrsq pieglpdedv dfsvaldgdv
       61 irlskdgaee aktatifedf schycaqmse eghddelkal ndgklvaeyr tlnfldgeek
      121 eqrdghstrv yatarkiaet gdaraywnfr tmmmadqqds vtwsndelad rleqlgvade
      181 ivsevrsgid tteakasana nfddlekrlg kvssphvfvd gkdilenisg dgglgqwvkv
      241 alr
//
LOCUS       WP_284826033             452 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium breve].
ACCESSION   WP_284826033
VERSION     WP_284826033.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..452
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47173
     Region          41..413
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(51..52,55..56,59,91,141..142,144..146,149,169,
                     172..173,176,261,264..265,268..270,273,300,304,353..354,
                     358,362,378,381..382,385..386,389)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 masisdpqrl adgasnnlrd yesenhgftv lgisgrrlaa vligwffvvf dgydlivygt
       61 vqgalmeewg isaaqagtvg saaflgmvig avligrisdr igrkfavlgs vvvlsiftia
      121 cafapgpvvf aifrllagig lgglvpsvna mtadlvppnk msswstvmms gvplggsiaa
      181 ilaqwivpsd phwgwrimfl iafvplvvgl piawfviptd rwiqadheah qgaddpaqkv
      241 gfgallgpqy rtvsiwfala tfvtllawyg lgtwlpklmt tagydfgaal nftlalnlga
      301 iigsvvtawa gdkfgpvlsg svaafvagva llllltgpsi gavylilvla gvgthgtqil
      361 iiaavthfyp hklrgtalgw algvgrlgav aapqlaglll swglgvnsny lmfaiaalls
      421 slslfilagi qrrqvgavdq etstvvshsd ph
//
LOCUS       WP_284826185             353 aa            linear   BCT 25-DEC-2024
DEFINITION  DHH family phosphoesterase [Corynebacterium amycolatum].
ACCESSION   WP_284826185
VERSION     WP_284826185.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..353
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=37911
     Region          28..338
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mttspqaqeq aahqlsqain rrmskpiqqm qdmladakkv gviahvhpda daigaasamv
       61 malvqrgisa vasygesdlp akslltipgw erfveytdld edidtwvtvd caspgrlgal
      121 edrvmasdrv invdhhatnt rfgavnmide haesstmvll dffgvwgikl ttpmahalya
      181 glltdtasfq fgrsrmhtaa arlldkgldp rtigaqllee hpfaylpflg tvlstatlvp
      241 ewgdgaglih vvieydqtae vghdeiesvv divrttnaad vcavlkeyep gqwavslrsr
      301 klvdvsqval eigggghera agltrecske ellqaildts daaaqarrga sea
//
LOCUS       WP_284826260             397 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium amycolatum].
ACCESSION   WP_284826260
VERSION     WP_284826260.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..397
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=43569
     Region          3..359
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mnsakstyvp eltsiraiga fgvllthaaf wtghytddww grlngrfeig vtiffvlsaf
       61 lltgrwlgsp ddvpakppsl rkyfisrakr vlpaywivvt aaflihaadd pppaggglqg
      121 wlrsmsftqt lqfgwihpgl pqmwsmvvev gfylvlplvg lgiwtitkgr lrpgptlaii
      181 igfgligpiw tvlshqeell pvvsrlwpma yfdwfaigml laygrkvgwr vnlavswlia
      241 lalfflsttt hvgpatlvpd dvdqalwktt lyglaagafv apialgtevr wlrhpamiwl
      301 gevsyefflv hvlvmdwvmk tmgyqtfqgs mlavaivttv itlplswllr ritdvltrrp
      361 gpaspwatyq ssssgpssat stscatfiad saagapq
//
LOCUS       WP_284826297             659 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Corynebacterium amycolatum].
ACCESSION   WP_284826297
VERSION     WP_284826297.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..659
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=69347
     Region          <5..230
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mirtkqlsav vltismllvl vgsfagitag raqaqeaast isptmvilda sgsmladdag
       61 gqtrmeaakd atskfagsvs edseigfmvy gtevgnspee reagcqditt llpvqagnsa
      121 kipaevgkiq asghtpmgpa lrqaadelpk egqrsivlvs dgedtcappp vcevakelkq
      181 qgidlvintv gflvdagara eleciaeatg geyldaqdsd slaesmktla trtartaqss
      241 aqeiqggdap tsatqvpadv etfstklrek tpesersisn qegdgaeyfs vpvaegerla
      301 isaatvpgas sgatlmdldv rnfsltmhld dsscflandf gngiidsngp ffasittkqs
      361 ggaegdcksg nmvfsvarkg gpfegqdipa evtikrfane nltdvpeafp sdkesltppp
      421 atpeadqakk vtpgswfdda teltadntss vtadivpget hvykikseyg qqlrgavkli
      481 dapeadklaq isgldiktln sarqlagsee nrpvnehqig eettfgnsar inyrnriged
      541 geksgdyeae rawldgdqyi vvffnnswga gkshdvadvq nvpvtyqltt elvgekipgp
      601 afeqvahksp sseaqtssqq npkgteened egssnmmwfs igavllavvv gaaialtrr
//
LOCUS       WP_284826556             273 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Corynebacterium breve].
ACCESSION   WP_284826556
VERSION     WP_284826556.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..273
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=30139
     Region          16..259
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 mstpsatdah qpeitgftlv lnnfegpfdl llnlisakkl dvtevalaev tdefiayvka
       61 lgetaeldev teflviaatl ldlkaarlvp rgdveseddl ellesrdllf arllqyrayq
      121 qvadmfaewq kdaqhrypra vaiepqfvdl lppvrlghtp atfaelaasv frpkapdevr
      181 tdhlhqvevs vpeqagrild tlrlagadsw lsfasltrdc trsmevvgrf lallelykar
      241 avethqeval gdldvswtgl dvdpavvaas nwe
//
LOCUS       WP_284826606             209 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Corynebacterium breve].
ACCESSION   WP_284826606
VERSION     WP_284826606.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..209
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23035
     Region          36..146
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mptwkevtaa npshsesyar rwkrmeeqgh dingearlid aiaprdaril dagcgqgrvg
       61 gylaeqghtv vgtdideili dyaqklypds awyvgdlskd pipegnfdia vsagnvmgfl
      121 dpngrrealq hvydalrgdg rfvvgfgagr gwdfpdfial tkdvgfnvei lfeswdlapf
      181 deestflvaf lrkpalsvde qtllgnmrn
//
LOCUS       WP_284826724             327 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Corynebacterium breve].
ACCESSION   WP_284826724
VERSION     WP_284826724.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..327
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=34690
     Region          18..313
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mstttstdss atsgeqtssq gptlrtqril amvlliaqgg itvtgslvrv tgsglgcdtw
       61 plchegslvp vagaapwihq aiefgnrlla fvvaaialal fiavykakrr reimtlafvs
      121 glgiilqavi ggisvlldlk wwavaihflp smilvwiaai lymriaepds gvptrffstg
      181 irtltvisai alsavlmtgt mvtgsgphsg ddgvgmdgrl qidtellafv haacmymyla
      241 ativvvwmlw rqhaskaakn talvligmii iqwaiglsqf ylgvprwtvp lhiamsgvvv
      301 afsaflfahg vrrqapsaea sresisa
//
LOCUS       WP_284826796             405 aa            linear   BCT 25-DEC-2024
DEFINITION  saccharopine dehydrogenase family protein [Corynebacterium
            amycolatum].
ACCESSION   WP_284826796
VERSION     WP_284826796.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..405
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43358
     Region          13..404
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 mttfsaqpqg rnhdreydiv vygatgfvgr livdylakha gqtkvalagr naqkladvae
       61 nagvsdwpvi vadaadqqav aqlaastkvv ltvvgpyaky grtlvaecak agthyvdlcg
      121 evlfvhdsia nnhevaqqtg akivhscgfd sipsdvavre lheaahtklg ettllfkhvk
      181 ggvsggtids vrvqieqakk dpklrriiad qyalaepgpd qgkfgvdlrp arfrrhwrap
      241 ffmspfntri vqrsamlady gdsfryrell nvgrgpkafv ranafaavcr lalaamafgp
      301 taklidkklp kpgegpsaea qaegrftiea ytvdtsgihw rskvsleedp gyagtaimis
      361 saalalvhdd lpdttgvltp tvalgdalsr rlraggmtie avqar
//
LOCUS       WP_284826830             757 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Corynebacterium breve].
ACCESSION   WP_284826830
VERSION     WP_284826830.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 757)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 757)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 757)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 757)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 757)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..757
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=84072
     Region          27..757
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mtqektqris gmrsvsarla rsltggrsrt npvldpllsi hrqfhpkada eiltraydta
       61 eelhegvyrk sgdpyithpl avaticaeig mdtttlvaal lhdtvedtdy slddltvdyg
      121 pevarlvdgv tkldkvalga aaeaetirkm ivamahdprv lvikvadrlh nmrtmrflpp
      181 ekqakkarqt leviaplahr lgmasvkwel edlsfailyp kkyeeivrlv adrapsrdqa
      241 lqeisnkvss elkanninae vmgrpkhyws iyqkmivrgr efdeifdlvg irilvdnisd
      301 cyaaigvvhs iysalpgrfk dyisnprfgv yqslhttvmt dggrpleiqv rthemhynae
      361 fgvaahwryk etkgshkgdq aevdqmswmr qlldwqkeaa dpnefldslr ydltaqqifv
      421 ftpkgdvinl pagstpvdfa yavhtevghr cigakvngkl valesklqsg drvevftskd
      481 inagpsqdwq dfvvspraka kirqwfaker reehlelgrd alatevqrgg lpmhrlftae
      541 smrtvatqlh ypdvdalyta igaghvsaqh vshqlmalfg deddavdalt artpmsklvt
      601 penkpttegg vlvdgtpdvm akmakccqpv pgdeilgfvt rgggvsvhrt dctnapklle
      661 eperiievqw atdgsdgngf natmqleald rhgllaeltk alseqklsvv elssqigddr
      721 iatvrftlmv sdtkqlgslm nqirniegvf diyrvta
//
LOCUS       WP_284826844             293 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Corynebacterium breve].
ACCESSION   WP_284826844
VERSION     WP_284826844.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium breve
  ORGANISM  Corynebacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Corynebacterium breve"
                     /db_xref="taxon:3049799"
     Protein         1..293
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33005
     Region          4..273
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 msptpqsiin ildlepieqd iyrskakesv lsrtfggqva aqalvaatrt vgddkfvhsl
       61 hgyfirpgia dqdtvyivnr mrdgnsfatr hveaiqngei ifsmqasfhr agdegpehsd
      121 lmrtvphpde ipeardtlpa ssrallaewe dwdirvvpsd lyehnkytps qqvvwfrskr
      181 rlpdddtfhv ctlaymsdmt llysamvphp ghkvqmasld hamwflrpfr adewlmydqv
      241 spsahggral thgrifdaqg rlvamvtqeg ltrtlregaq pvpsklprne sqd
//
LOCUS       WP_284826648             371 aa            linear   BCT 25-DEC-2024
DEFINITION  lipase family alpha/beta hydrolase [Corynebacterium amycolatum].
ACCESSION   WP_284826648
VERSION     WP_284826648.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18498059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..371
                     /product="lipase family alpha/beta hydrolase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37964
     Region          84..>176
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
     Region          89..303
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mgthrafakl arsatallaa agvalaaapi aaaapasatd ndqvlswtem gewgpkandf
       61 ptvmvnqgmt enispegtnv qcvpapgenp vvmihgmnsn syqtyarmap elkamgkcly
      121 afnvgklgpd efsvlgsipt mrnmtpldta laeltakidt vkaetgatav divghsagga
      181 laaayakqeq grgigtvvsl agvlhgttll gasygleqln qfdnagdkaa gyvvspslvd
      241 lmqhgqfmak ineggleqpg vnyvaistqv deavtpmaas qwnaptsnni llqdgcsadl
      301 sghigltfsp raialvanal grnvevpcvp vtavfeggin dnanvrpehv navsggitei
      361 dgriaqaaga r
//
LOCUS       WP_284826865             257 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium amycolatum].
ACCESSION   WP_284826865
VERSION     WP_284826865.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..257
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26747
     Region          24..256
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mtnsttdsat klakakeflh sagailfdld gvitptadvh eqawadmfsd yfehkgvtay
       61 teedyftyld grrrdegiaa ilesrgislp hgndedtaed etivglgkrk nddflarvar
      121 gieaypgsva lldelqgagd ssasdkpqla vvsssknavp vltaaglrer fveivdgvva
      181 hennlpgkpa adtfvyaaek lgvaprdavv vedaisgvqa gaagafglvi gvdrgagaea
      241 lsragadivv sdlaelv
//
LOCUS       WP_284827183             293 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium amycolatum].
ACCESSION   WP_284827183
VERSION     WP_284827183.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..293
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32228
     Region          32..253
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mntgenrast tpqphastnt givddapata nsrvaaffdl dktiiakssa yafnkqfler
       61 giisptdmlq malshalyms qghdevqmea treqfsslia ghsarelrqv aietleqnit
      121 pyiyaealel irehraqghq vfiisasarq ivepiaqalg vynvvatele vrdglftget
      181 effcrgenka vqmrriaekr qfdlaecfay sdsitdepml savghpvvvn pdralrkiat
      241 erewpvrqfr npvplfraps krnaailagv tlalgagatl lalrknddes kad
//
LOCUS       WP_284827187             251 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Corynebacterium
            amycolatum].
ACCESSION   WP_284827187
VERSION     WP_284827187.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..251
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25382
     Region          139..251
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mneqggrshn gghigdrqad vnrsaslitl liagisivgl vvfaivnttg gndeaddggt
       61 gagvsagvdg agsdgtgsde vdgasaapam skdeiaavag sgslagvrlp llaesgdsad
      121 qsneagrtel vdmgqvvegk ptvlnvwawn cgpcrqelpl iaqwgkdnpd vqvvtvhaar
      181 eagrgqaflq eigvnlptys dtvdvvgpal nlprvvpitv vfkadgtvat ihpgeftdaq
      241 qitdlvrgvl k
//
LOCUS       WP_284827271             178 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsB family cell division protein [Corynebacterium amycolatum].
ACCESSION   WP_284827271
VERSION     WP_284827271.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..178
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=19479
     Region          <55..119
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
     Region          <92..150
                     /region_name="PRK06782"
                     /note="flagellar motor switch protein; Reviewed"
                     /db_xref="CDD:235861"
ORIGIN      
        1 msasdrsrrg tqsrpagagq rsaaaiasgm rslstaqkig igllvlflvs vlaiplrtfa
       61 qqqadvaatq dniarmeqri eqledekely snpayikeqa rlrlglvepg etpfrildpa
      121 vgeqpvtqpe eipqhqakkw yetlwdsisi ppepeetrpn pgrdqatkpe slptvpes
//
LOCUS       WP_284827280             358 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Corynebacterium amycolatum].
ACCESSION   WP_284827280
VERSION     WP_284827280.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..358
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=39226
     Region          68..350
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 masikrykks kgygwrvqyr apdgtsrtkq gfrtkdeaqa wadknattir dgqwisptve
       61 saavsslwag weksqhhlaa ssmkaldasw rvhvkprwgh tpvskvhpad vqewvdelag
      121 krsptivhra ygvlrslmgd avryrmvran pcdgvrlpak rgkkmyvlte kqlrtladev
      181 skyrslvlfm gwtgarwgea valtvgdldl dtgratisks astiggkvsv getktghtrt
      241 igiprhvcee lkadvrgklp galvwtnarg ghlttpskrs wfhsavarcr aadedfpgvt
      301 phdlrhtaas mliasgapvt lvarqlghqs akltldtyah lfddqlsdvv gmswsaan
//
LOCUS       WP_284827382             534 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Corynebacterium
            coyleae].
ACCESSION   WP_284827382
VERSION     WP_284827382.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..534
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=57593
     Region          1..520
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mstpllevdg ltvaygdaep tveniafavd agkmtaivge sgsgkttsam aaldllgptg
       61 nvragsirfk gqdlaslsaa ewrqlrgaki glvpqdpnns lnplktigas vedgleihgv
      121 gdaasrrrqa iallervgid dpekrynqyp helsggmkqr vliaaavale pevliadept
      181 saldvtvqkt ildlldemra elglgvifit hdlavagdra ddvvimergr vvehgpvsqv
      241 ltnptqdysk rllanvpsls vanayrrppv ttdtllrvdn lavrygdfta vsdisfevar
      301 gsthalvggs gsgktttgrt iamfnqpaeg sitldgeelt tlspkqkrqf rnriqmvyqn
      361 pfssldpkmr vgeivaeplr nlagaskres laraneyler valdperfat rtpaqlsggq
      421 rqrvaiaral ivepelvvld eavsaldvtv qaqilellen lqrelgltyv fishdlavvr
      481 qisdtvsvfs rgqqveygpt devfshprhd vtrelidaip gtvfrarqlg efvv
//
LOCUS       WP_284827388             295 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Corynebacterium coyleae].
ACCESSION   WP_284827388
VERSION     WP_284827388.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..295
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30676
     Region          16..290
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mtlrapspve pnadrtavlc ilgsclflql gaalatqlfp hagtwatssf rlliasvill
       61 aisrpafwrw tpeqwgaaiv lgvslgcmng fyyagiatvp lasavtiqfl gplllaavls
      121 rsvrdgisvg laltgmallg vdslsgepld rlgvfyilia gaawavyila nkrtgrliag
      181 qgglavalav gglvtlpfgf egalvivsdt nllllaigta ilasllptsl eliamrrlrp
      241 qvfsilisfe pafaalvgwl vlsqdpsplk laaialviga svnqtlagkr lrrqv
//
LOCUS       WP_284827453             316 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Corynebacterium coyleae].
ACCESSION   WP_284827453
VERSION     WP_284827453.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..316
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=34209
     Region          27..310
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mstttaqpks qsrfkeawqd pslhlqrvlg mvllicqggi tvtgslvrvt gsglgcdtwp
       61 lchegslvpv agaapwihqt iefgnrllaf vvaaaavlvl iavykakrsd aiktmawvsf
      121 lgvvvqavig gisvrldlqw wsvavhflps mllvwvaavl ymriaetdaa dptrrfpaha
      181 qtwtfiaava lcfvlvtgtm vtgsgphsgd sgvgmegrln ldtrmlayvh aicmyvylia
      241 tfvvafilrr sdapdakrtv wvlialilvq waigviqfrm gvprwtipah igmsstvvaf
      301 saflfahgkr rlptlv
//
LOCUS       WP_284827533             998 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Corynebacterium coyleae].
ACCESSION   WP_284827533
VERSION     WP_284827533.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..998
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=107489
     Region          121..261
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          428..944
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 msvkntaprn srsssrrsad gtryggpvsm thpptsstva adtadervgs aykvvgsslg
       61 aaargvgsfl rreprhheqe eenlstsrrr prrdqyddhd eleqrdddpt prsstfehha
      121 dawglvligl aaviggsvwf dvagpvgdli stgthwliga galilpvvlv gvaialmlnv
      181 rasdevrara algfsiiava mlglihvfag tpsawedrri aggaigaftg gllaagfssf
      241 vavpllgliv lygalkatgi tvreaydyvk glvtgmlnae ddedddpysh vdadlddiae
      301 grdrprpras rpaprlmprp rrprtpmesy ptnededddl fdfaddlndt ddtddtsepe
      361 pepeattvvp rpkrrpapts apapaqttra dnnpnetkvl erpeetsdrr qavapdavet
      421 sreqmakaia arsgidaski pattpksetq ppapkqvrki pqgdytlpst dllipgnppk
      481 trteandrmi eaitdvfeef nvnaqvtgfs rgptvtryev elgpgvkvsk itnlqsnlay
      541 avatdnvrll tpipgksavg ievpnadrem vrlrdvldap nvasqddpml iglgkdiegd
      601 fiassvqkmp hllvagstgs gksafvnsml islltratpe evrlilvdpk mveltpyegi
      661 phlitpiitq pkkaaaalqw lveemeqrym dmksarvrhi kdfnrkvrsg eltappgser
      721 emrpypfivc vvdeladlmm tapkeiedsi vritqkaraa gihlvlatqr psvdvvtgli
      781 ktnvpsrlaf atssltdsrv ildqggaerl igmgdglfip qgagkpqrmq gafvsdeeiq
      841 avvdaaksqq depdyvegvt edkqaeakvi dddigkdmdd lleavelvvt sqlgstsmlq
      901 rklrigfaka grlmdlmesr gvvgpsegsk arevlvkpee letiiwmikg adpaeapkdv
      961 mldddtttdg pdsgsdtggt dgdtrtvtat ynptggaf
//
LOCUS       WP_284827696             265 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium
            coyleae].
ACCESSION   WP_284827696
VERSION     WP_284827696.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..265
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28612
     Region          29..264
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mqlekffqdw pvdnvagalv gkqeasfgdt arvfelasvt kllsayavll aveegafsld
       61 ddarpenati rhllshaagv gfdsrepqka pgerriyssa gyeiladive ettgitfady
      121 aregvfeplg mtateiygsa ghggrstvad lsrfaaelle prlldpstvr eaftnqfgdl
      181 rgvvpgygmq kpcpwglgfe ikgeksphwt gdgmpadtvg hfgmagtylw vagdqacvvl
      241 tdrdfgdwak plwqetntal weals
//
LOCUS       WP_284827817             351 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium coyleae].
ACCESSION   WP_284827817
VERSION     WP_284827817.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..351
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=37965
     Region          8..343
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mnprpavlpe ldglravaay givathvafq tgtgsavler fdyfvavffa lsafllargg
       61 mrpgyysrrv arlvpayvvc vavvllalpp lagvsatqvv anvllvqvyv phalidgltq
      121 mwslcievaf yivlplylrl gargryvals vavavgfvwp wavsgiadpa vlnlqiwpps
      181 yalwfavglv laeveragvr yagprwpfvl lalpvawvag vigprglehp splefnvriv
      241 lgavfaallv apfalgqrfe gtvlssksmr tlghwsysvf lwhmavlyfv fpilgvpmfs
      301 ghfllvfatt tllstavayi syelvevpga rlvrqatakq aarmrkvdep a
//
LOCUS       WP_284827796             564 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Corynebacterium coyleae].
ACCESSION   WP_284827796
VERSION     WP_284827796.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..564
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62691
     Region          7..546
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 msskprvnrr iflqtvaasv aavalgtgga vaarrstvst pevptpadqw dlpflhgvas
       61 gdplpdrvvl wtrvtpsrea lpgsglgddv elewqidtte dfthpktgsa iaraesdhtv
      121 hvdpdgldpd teyfyrfivk sgehagsfsp vgrtltapav dadldtldla iascanwesg
      181 ffsayadmaq rarageidhv vflgdyiyey ptgeyvgksg varmhhpewe ittledyrqr
      241 ygryrtdlnl qaahaacpwi vvwddhesan nswregaenh sdglvegkwa qreaaamqay
      301 fewlpvrrsa lieapgiyrs fqfgnlaqlt mmdlrtfrde ettsdyfand ertmlgdeqf
      361 awvaeqlqqs tarwdvlgns vmvspmrfvt ikdnekania tgymreratg iavnsdqwdg
      421 yvaerdrllt mldeqesnal fltgdihsew ansiaspsgf geigcemvtt sisapnvdei
      481 lttafgtyhk ednstsllve qtirdanpwv shidfdahgy gvasihydyv dmlyyrvsdv
      541 edpdasvslg ekrqwrigeg fvea
//
LOCUS       WP_284828050             686 aa            linear   BCT 25-DEC-2024
DEFINITION  RecQ family ATP-dependent DNA helicase [Corynebacterium coyleae].
ACCESSION   WP_284828050
VERSION     WP_284828050.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Larsen,N.B. and Hickson,I.D.
  TITLE     RecQ Helicases: Conserved Guardians of Genomic Integrity
  JOURNAL   Adv Exp Med Biol 767, 161-184 (2013)
   PUBMED   23161011
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Rezazadeh,S.
  TITLE     RecQ helicases; at the crossroad of genome replication, repair, and
            recombination
  JOURNAL   Mol Biol Rep 39 (4), 4527-4543 (2012)
   PUBMED   21947842
REFERENCE   3  (residues 1 to 686)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 686)
  AUTHORS   Bernstein,K.A., Gangloff,S. and Rothstein,R.
  TITLE     The RecQ DNA helicases in DNA repair
  JOURNAL   Annu Rev Genet 44, 393-417 (2010)
   PUBMED   21047263
REFERENCE   5  (residues 1 to 686)
  AUTHORS   Chu,W.K. and Hickson,I.D.
  TITLE     RecQ helicases: multifunctional genome caretakers
  JOURNAL   Nat Rev Cancer 9 (9), 644-654 (2009)
   PUBMED   19657341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..686
                     /product="RecQ family ATP-dependent DNA helicase"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0043138 - 3'-5' DNA helicase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=75140
     Region          4..499
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
ORIGIN      
        1 mtatrtqade llkgiagpea mlrddqwtai dalvnqrkrm lvvqrtgwgk savyfiaakl
       61 lreagagpsi ivspllalmr nqvesaarag iraatinsan mtewdeiqah lndydlllis
      121 perlnapdfr eqvlpqlars agmlvvdeah cisdwghdfr pdyrriavli ddlpeatpvl
      181 attatandrv vadvvaqlge ntgvlrggld reslalnvvq lpdptqraaw iaqylayvng
      241 sgiiycltva aahdlaeale nagwnvaayt grteaeerer leralidnel kalvatsalg
      301 mgfdkpdlgf vvhlgapssp vsyyqqigra gratdhaevv llpgpederv wdyfasvsmp
      361 eehvvhqllg alseepfstp rlenfvdlsr tridqalkvl dvdgavrrvk ggwvstgaaw
      421 kydheryggl aearkreqdl mlayeatdgc rmaflrreld dptlapderc grcdnctgnh
      481 lpvdvdaala qrmdeqlrtp gvqltqrkmw ptgsarrgki kgvlqgkalg rlndvargpa
      541 laellranty rplsnwreda wlgrfvavla dwaweerptt vvalgdadpa rnemivatae
      601 alarvgqmrf ggvvdtpsre vearnsafrv ngldryydyt glevetgpvl lltgemdsgw
      661 svtvaaadia erygvevlpl afasra
//
LOCUS       WP_284828226             487 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium coyleae].
ACCESSION   WP_284828226
VERSION     WP_284828226.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..487
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52934
     Region          225..462
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mlrvasgday etrlgaghsl rlklavlsgf ivaaavgltt mlgmwlstkt hegvldtelr
       61 sktlgmarql dgasedqirs eiaafrrsnp ltsiavsgad snlflgdpvs isgpylrtes
      121 gdavsvrsvn gkrvvvrqtp dgmvvaasrt edpynrisgs raaaglvvig vgslvawisg
      181 alisavgltp vrrlhreldn anessgprel pvegddefae vtssinalvr sleeskkrqa
      241 qlvadaghel ktpltsmrtn iellmmlhns grqdqisaed radlerdvla qmeemsilig
      301 dlvdlsrdes hetepedfrl devleealdr vrrrrpdvtf lfhadpwvir gdrfamgrap
      361 inlidnaakw speggavrvs lkaakrnavl ivddsgpgip peerekvfer fyrspesram
      421 pgsglglaiv kqvmdrhgat ivaeesddgg arfrvvfpgr ppedetaedl ivedenetrv
      481 ipkksys
//
LOCUS       WP_284828289             444 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium coyleae].
ACCESSION   WP_284828289
VERSION     WP_284828289.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..444
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=47782
     Region          1..442
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrltvigtgy lgathaacma elghevlgvd vdehkiealk nskvpfyepg lpevlernid
       61 agrlsfttny deaaafgnvh figvgtpqqr gsyaadtryv eaviddlvpk lhghhvilgk
      121 stvpvgtaaa lqeradnltq dgasveiawn peflregyav kdtiepdriv lgvrgasath
      181 gdskaeavar evyatplann tpfivtdlqt aelvkvsana flatkisfin avsevceivg
      241 advtqladai gyddrigrkf lgaglgfggg clpkdirafm aragevgadq altflrevda
      301 inmrrrqrvv dmareelgsl igrnitvlga afkpnsddvr dspalavagq lslaganvtv
      361 fdpqamdnar kvfptldyad tleealrgae ltilatewgq fremdpewva gvvekqllid
      421 arnvldvqqw rnagwemral grtl
//
LOCUS       WP_284828477             308 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Corynebacterium coyleae].
ACCESSION   WP_284828477
VERSION     WP_284828477.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..308
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33131
     Region          23..306
                     /region_name="COG4132"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443307"
ORIGIN      
        1 mttsvskanp vsgdetrtnv kethsrlntv rhhvpwgvlp yfifvgiflv lpvlanvwks
       61 fqdpsgafsl qtmieamgps yrpafvltfn lsfvtavigg ffgvllawal sheerpkrfs
      121 gllnsfaala aqsggvglay afiallgtqg iltvaisnaw pgfrdsfsit gfwgvaivyl
      181 yfqiplmatl mlpamggvkk twydaaaslg atrmqyvkdv vipvlwpsil gallllfana
      241 faayatayal aggslnlvpi vigffisgnv llnpglaaal vtwmmliiia amllrmgltr
      301 ksdqwlnq
//
LOCUS       WP_284828726             396 aa            linear   BCT 25-DEC-2024
DEFINITION  trypsin-like serine peptidase [Corynebacterium mastitidis].
ACCESSION   WP_284828726
VERSION     WP_284828726.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium mastitidis
  ORGANISM  Corynebacterium mastitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Corynebacterium mastitidis"
                     /db_xref="taxon:161890"
     Protein         1..396
                     /product="trypsin-like serine peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=41757
     Region          68..284
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mkksvvlals aafaaashla pmaaaddgsr lpqpnpagsv ldghlseind kgayfaetpy
       61 aeqaasravg qivnagslct gsvidsasrt lvvtaahclg kwqdgkwqis qgtrdsiaag
      121 ksfftpafdg vaqepaqrvp fgswkiadah vsetsgvdva vleiapddqg rkiqdvtgaf
      181 gihpelqqge vvqasligyp gpapfngksq svcvgnytky qgggnsqirr vegerecwvg
      241 ggssggpfat tssnpnlage iitvlhsggg gniapvmgel vnaaegdipa eekaevapss
      301 rpllrsplrp rsprnppprp ssprtprssp rrrprrrrsp aprapssprp rslarplpps
      361 rgfrrrgstp prsrrsrrpr rraltplpfm gprakr
//
LOCUS       WP_284828776             463 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Corynebacterium
            mastitidis].
ACCESSION   WP_284828776
VERSION     WP_284828776.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium mastitidis
  ORGANISM  Corynebacterium mastitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Corynebacterium mastitidis"
                     /db_xref="taxon:161890"
     Protein         1..463
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48452
     Region          7..463
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mrnieldviv lgfgkagkti amkrgragdr vaiveqspqm yggtcinvgc vptktlltaa
       61 hrhriggged hagafaaarr hrdefvarln aankemavds gvrvidgrgr ftgpntvevt
      121 ggaealtlta ptivintgav pvlpgvpgvd ldrvvdstav qrlpelpdrl avvgggpigl
      181 efatmfaqfg srvtvldgse aflgrfdrdi agvaradlea qgieivggar vtgfastagg
      241 gvsvrygggd gedsaetvea dyallaigrr pnteglnlqa agvevterga vrvddhlrts
      301 vpgiyaagdv tggpqftyis yddhriiled rwgtgaasrs aagrlfpttt flnpplsqig
      361 mgeqeareea arrghtlavr aqdiadiaim prpkilgqpq grakflvdee edrilgatly
      421 cvdsqelint vavamrhgvp aselgagiyt hpsssevfna llg
//
LOCUS       WP_284828898             268 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Corynebacterium mastitidis].
ACCESSION   WP_284828898
VERSION     WP_284828898.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium mastitidis
  ORGANISM  Corynebacterium mastitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Corynebacterium mastitidis"
                     /db_xref="taxon:161890"
     Protein         1..268
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29755
     Region          5..251
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 msaptlwavs dlhaavpanr rwvaglrprh pgdwlivagd vaenmevvvs tlerlrgrfa
       61 rvvwapgnhe llsrateryr greryaelir rcrevgvdtp edaypsffgt vvaplltlyd
      121 htlappgvtl ararraghtl iddlalapfa dvpawcrerl fygarrlael ggaptvlvnh
      181 wplvrepvdr lglpelalwc gtahtrqwar ryraravvhg hlhlpgayev dgvrhieasl
      241 gyprewrarp ggpaaqpwpy pvlggeaa
//
LOCUS       WP_284828964             273 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Corynebacterium mastitidis].
ACCESSION   WP_284828964
VERSION     WP_284828964.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium mastitidis
  ORGANISM  Corynebacterium mastitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Corynebacterium mastitidis"
                     /db_xref="taxon:161890"
     Protein         1..273
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29780
     Region          1..268
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mesvekilsv ahlggqtweg iaagtrqrrt fggqvvgqsl aaavaaaadl gegkvvdslh
       61 gyfvsggdaa rgmtvdaipv rrgrsysnfs vraaqgeatl fvgnvsfrrp gdpgpehsvp
      121 mpqvpppegl sdgreylpqk nlllfsewed wefrmvenha eggyghqrlw frasrrlpdd
      181 pvfhtlalay msdmtilyga maphrghpvq masldhavwf hrparvdqwl lydqvspsas
      241 egralctgri yaqdgtlvat vaqegltrtl req
//
LOCUS       WP_284829181             367 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium mastitidis].
ACCESSION   WP_284829181
VERSION     WP_284829181.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium mastitidis
  ORGANISM  Corynebacterium mastitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 367)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Corynebacterium mastitidis"
                     /db_xref="taxon:161890"
     Protein         1..367
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=37296
     Region          13..363
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 msatatpapa rasarvlrlg pvswrinarl lacmaataal lalgvcwavt qgeyrmtlgq
       61 vvevfagggt aiqravvfdm rlgravvacl vgaalaysga ltqsvarnpl aspdilgitq
      121 gaslaavtti vfagaghggv ieagattvmg tvglpgaaia gallaalliw llagpahnsm
      181 lqvvligagm siflsagvtw llayaqldra asarmwltgs lngrdwnhaw aplavlvvav
      241 alggwlafql salvlgetta hvlghrvrva qlvqlltavv laavgvaaag pigfvafvvp
      301 hlaralagtp tppllfsall gaalllgadl larvvlpwel pvgvvtaflg apfllfmifr
      361 trreeti
//
LOCUS       WP_284829307             393 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Corynebacterium mastitidis].
ACCESSION   WP_284829307
VERSION     WP_284829307.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium mastitidis
  ORGANISM  Corynebacterium mastitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Corynebacterium mastitidis"
                     /db_xref="taxon:161890"
     Protein         1..393
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42069
     Region          21..221
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mpkqkmstla rlravdqslh sralrvrkra wpivqsavaa glafwvaqri fghpvpffap
       61 iaaviilgle ggdrmrrave msigcivgva lgdllffylg pghwqiavav alslllasfi
      121 sksplvnnqa aigsiliati mppgtvsait gtgstgrvvd amvgsavgll vvafipsdpl
      181 nagrqevsnv lgiassvlqd vsqalrtgdv elmkntldav rgtqgkinam laaaktgres
      241 ttlsplmwgn wrrvrslerl lipvdnsirn vrvlarraqv liededavsr eqvaiidels
      301 dvalqlsemy erdaeinear eipvlvnqlr rlggrasmev vggrvlsahv vlaqsrsliv
      361 dflqicgmsr esalavlapt satpayppev wee
//
LOCUS       WP_284829370             260 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Corynebacterium
            mastitidis].
ACCESSION   WP_284829370
VERSION     WP_284829370.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium mastitidis
  ORGANISM  Corynebacterium mastitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Corynebacterium mastitidis"
                     /db_xref="taxon:161890"
     Protein         1..260
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28756
     Region          60..156
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mptarrlprt rrratlrrsl gllgdfryeq pdparfyghl ardtaelles lnrdagrgtl
       61 rhqsildvgg gpgyfaaefe rrgaryvsve pdvgemaaag ievaasvrgs gldlpfrtga
      121 fdlvyssnva ehvpdpwrmg eemlrvtapg glmvlsytvw lgpfgghetg lwehyvggey
      181 ardrytrrhg hppknvfgst lfdvscaagl gwarslersg rarvlgafpr yhpgwawwlt
      241 rvpgvrelav snlvivarrv
//
LOCUS       WP_284829426             112 aa            linear   BCT 25-DEC-2024
DEFINITION  histone-like nucleoid-structuring protein Lsr2 [Corynebacterium
            mastitidis].
ACCESSION   WP_284829426
VERSION     WP_284829426.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium mastitidis
  ORGANISM  Corynebacterium mastitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Gordon,B.R., Li,Y., Wang,L., Sintsova,A., van Bakel,H., Tian,S.,
            Navarre,W.W., Xia,B. and Liu,J.
  TITLE     Lsr2 is a nucleoid-associated protein that targets AT-rich
            sequences and virulence genes in Mycobacterium tuberculosis
  JOURNAL   Proc Natl Acad Sci U S A 107 (11), 5154-5159 (2010)
   PUBMED   20133735
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18741]
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Gordon,B.R., Imperial,R., Wang,L., Navarre,W.W. and Liu,J.
  TITLE     Lsr2 of Mycobacterium represents a novel class of H-NS-like
            proteins
  JOURNAL   J Bacteriol 190 (21), 7052-7059 (2008)
   PUBMED   18776007
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Oshima,T., Ishikawa,S., Kurokawa,K., Aiba,H. and Ogasawara,N.
  TITLE     Escherichia coli histone-like protein H-NS preferentially binds to
            horizontally acquired DNA in association with RNA polymerase
  JOURNAL   DNA Res 13 (4), 141-153 (2006)
   PUBMED   17046956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10570331
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Corynebacterium mastitidis"
                     /db_xref="taxon:161890"
     Protein         1..112
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12580
     Region          1..110
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 markeitqyf ddlsgtples hevnvvrfal dgtdyiidls aenaekfrem frpylavark
       61 haapvsgrrn sgaarnskar eirqwaldhg kdialrgkip sevieaynqa hr
//
LOCUS       WP_284829430             340 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Corynebacterium
            mastitidis].
ACCESSION   WP_284829430
VERSION     WP_284829430.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium mastitidis
  ORGANISM  Corynebacterium mastitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Corynebacterium mastitidis"
                     /db_xref="taxon:161890"
     Protein         1..340
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=37028
     Region          2..320
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 misnpnattq sglmlrrvma alreveglrv rsvlthhagh aaemcrglrr edydvviavg
       61 gdgtvnevin gllgevegap aagevpalav vptgsanvfa ralgyqpfpd lvarqlaqal
      121 redqrrsicl gtwnegwfav nagfgidatv ierveqvrsr gfaatplryl vvsteawlrs
      181 qikppsievr atsaaggdlr lsrmpllfas ntnpwtflgp lpvvtnpgns fdqglglfgl
      241 tdirglggva smlhligvgh qrrlegwikr rtvrfddata vemvcptpeh fqvdgeyegd
      301 ytrvrlgsvp aalevfapre eplsvrrtvw rtlrdfvrvr
//
LOCUS       WP_284829629             483 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Corynebacterium
            mastitidis].
ACCESSION   WP_284829629
VERSION     WP_284829629.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium mastitidis
  ORGANISM  Corynebacterium mastitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Corynebacterium mastitidis"
                     /db_xref="taxon:161890"
     Protein         1..483
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=51120
     Region          4..228
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mlrlnytvas drglvrgnne dsayagpyll aladgmggha agevasqimi thlehldkdt
       61 gdndmlalla agadeanrai adevgahpet qgmgttltal afngrefglc hvgdsrgyrl
      121 rggaleqltv ddtyvqslvn egrllpedvs thpqrslilk aytgrdvept lktldakagd
      181 rlllcsdgls dpvthstiee tlaqgtpaea anrlvelalr sggpdnvtvv vadvvdadam
      241 degalaelpt epatggalcg epsedshpdt aagraaalrt kvttispdgq vsaqplsgvp
      301 dppeaaedee adadqgserg sawrwgtliv allvlialiv ggwwvyhtak eryflatdda
      361 gailvergld ytvlgrdlhe eyqhaclgad asvrltdpqe gsekdchrfs lndlpasars
      421 sveampsgty eeinqqlrrl adqalpacvt vrkesdpart eessrpgelt dlakpgvdcr
      481 evk
//
LOCUS       WP_284829873             341 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Corynebacterium mastitidis].
ACCESSION   WP_284829873
VERSION     WP_284829873.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium mastitidis
  ORGANISM  Corynebacterium mastitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Corynebacterium mastitidis"
                     /db_xref="taxon:161890"
     Protein         1..341
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=36301
     Region          32..328
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mpvhallgvi sipgkprssp wvligtrvgy almllvlvav ivyadgdgys epltfidaly
       61 ysavslsttg ygditpvtqg arvvnilvit pmriafliil vgttlsvlte esrkslqiqr
      121 wrnrvrnhti vvgygtkgrs avaalladgv pahqivvidt drvalsraen qglvtvhgsa
      181 tkadvlkiag vsrarsvvva pnlddtavlv tlsvrelaps amivasvres enqhlleqsg
      241 adsvvisset agrmlglatv tpsvvemmed llspdegfsv aerpvaedev ganprhladi
      301 vlgvvrsgel yridspeaea vepgdrllyv rrvteqdveg r
//
LOCUS       WP_284829694              35 aa            linear   BCT 25-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Corynebacterium
            mastitidis].
ACCESSION   WP_284829694
VERSION     WP_284829694.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium mastitidis
  ORGANISM  Corynebacterium mastitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 35)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 35)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..35
                     /organism="Corynebacterium mastitidis"
                     /db_xref="taxon:161890"
     Protein         1..35
                     /product="type II toxin-antitoxin system RelE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0017148 - negative regulation of
                     translation [Evidence IEA]"
                     /calculated_mol_wt=4196
     Region          <1..35
                     /region_name="RelE"
                     /note="mRNA-degrading endonuclease RelE, toxin component
                     of the RelBE toxin-antitoxin system [Defense mechanisms];
                     COG2026"
                     /db_xref="CDD:441629"
ORIGIN      
        1 mwryrvgdyr vvvafqreev vilavdvghr kemyr
//
LOCUS       WP_284829889             447 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium mastitidis].
ACCESSION   WP_284829889
VERSION     WP_284829889.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium mastitidis
  ORGANISM  Corynebacterium mastitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Corynebacterium mastitidis"
                     /db_xref="taxon:161890"
     Protein         1..447
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=47883
     Region          23..357
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mstpmdspeh psppaarrar ggtlrptlyr mhswagvlva pflvvaaltg llyalspsle
       61 qivyrdaltt satgeripvs raiaaarevh pdldlagvqv deradatvrv lfadpslpns
      121 aykqavfvdp vtakvvgdmp qyasfgslpl rtlidqghsn lwlgepgrfy semaaswlga
      181 maltglflla qrwrrsvsqk nrprrwhslv glacvpgflf ltltgltwsa taggtigdlr
      241 thldwrpptp evtvasvdsg dpapaagdag adaalagare sgltgvldmv vpeegnvwsv
      301 tesaaqpwvf rydavsvdga tgavvdsvpf sswplpaqlt ewlirshvgs lfgllnqval
      361 aalalgllaa vvlgyamwwr rgkgssfgrl paprswetvp rpalvcfllv mavygvlapy
      421 fglsvlafla adalyrafrr rrtrplh
//
LOCUS       WP_284829918             254 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium mastitidis].
ACCESSION   WP_284829918
VERSION     WP_284829918.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium mastitidis
  ORGANISM  Corynebacterium mastitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Corynebacterium mastitidis"
                     /db_xref="taxon:161890"
     Protein         1..254
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=27871
     Region          91..249
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mktrfdtyvn phrpwyrtap fyialaviai flvvvliaql vnkdsagdna aagasgtqsa
       61 eaasdpdaqi kslierreen dpravgdvda pvvlvewtdl rcpfcalfsr eilptlkkey
      121 vdtgkvrief rdvvyfgers atasaaaraa grqdkyvdyl ravyarapes ghpdlpdeel
      181 ieiaeevgvp dmerfkadmt dpqleaeaqa eteearqwgv qgvpffavgg nviagaqsld
      241 nfrefldqai eeas
//
LOCUS       WP_284829973             530 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Corynebacterium
            mastitidis].
ACCESSION   WP_284829973
VERSION     WP_284829973.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium mastitidis
  ORGANISM  Corynebacterium mastitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Corynebacterium mastitidis"
                     /db_xref="taxon:161890"
     Protein         1..530
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=56966
     Region          1..517
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msallsirdl svsyhagrgr epvravrgvs levqpggltc vvgesgsgks ttalasmgll
       61 ppnaridags ielagrevta yserqwrglr grrvglipqd phnslnplkt igaavaepla
      121 mhgrdtssvv dllaavgidd prrradqyph elsgglkqra lvaaalalep eliiadepts
      181 aldvtvqkvi ldlldsvrre rgigvlfith dlavagdrad rvvvmqrgrv resglaarvl
      241 teprdrytqr lladapslsa ppapragreg dalvevrgvt qsfggvtavd dvsfrvargs
      301 thaivgesgs gktttgrmia gfrrpdsgtv rvgdtrvdtl darglralrs rvqmvyqnpy
      361 ssldprrsvr ysvgeplrnl gggppreirr rvgrhlelvs ldsalasrrp aelsggqrqr
      421 valaralivn pevvvldeav saldvsvqaq ivallrrlqe dlgltyvfis hdlavvrqva
      481 dtvsvmrrgr qeeyapagei fenpqsdytr alldavpgrr yrhgglnlvl
//
LOCUS       WP_284830239             225 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            mastitidis].
ACCESSION   WP_284830239
VERSION     WP_284830239.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium mastitidis
  ORGANISM  Corynebacterium mastitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Corynebacterium mastitidis"
                     /db_xref="taxon:161890"
     Protein         1..225
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24606
     Region          15..190
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mpatqapqra pravtdlfpe slalspkqna vlgilrefph gasatqlser lgmhantvrg
       61 hleeliaqqa vsqraapaqg rgrptliyqa rvpdtqavae eyidlithla kvidveqake
      121 vgrlwarskg tgtvdelmek lrtlgfdprl redrtaidlr acpfihnrnp phpsvcglhe
      181 gffqeyldap egirflplrs nctctivlst gddaatspee fsepa
//
LOCUS       WP_284830438             115 aa            linear   BCT 25-DEC-2024
DEFINITION  histone-like nucleoid-structuring protein Lsr2 [Corynebacterium
            mastitidis].
ACCESSION   WP_284830438
VERSION     WP_284830438.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium mastitidis
  ORGANISM  Corynebacterium mastitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Gordon,B.R., Li,Y., Wang,L., Sintsova,A., van Bakel,H., Tian,S.,
            Navarre,W.W., Xia,B. and Liu,J.
  TITLE     Lsr2 is a nucleoid-associated protein that targets AT-rich
            sequences and virulence genes in Mycobacterium tuberculosis
  JOURNAL   Proc Natl Acad Sci U S A 107 (11), 5154-5159 (2010)
   PUBMED   20133735
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18741]
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Gordon,B.R., Imperial,R., Wang,L., Navarre,W.W. and Liu,J.
  TITLE     Lsr2 of Mycobacterium represents a novel class of H-NS-like
            proteins
  JOURNAL   J Bacteriol 190 (21), 7052-7059 (2008)
   PUBMED   18776007
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Oshima,T., Ishikawa,S., Kurokawa,K., Aiba,H. and Ogasawara,N.
  TITLE     Escherichia coli histone-like protein H-NS preferentially binds to
            horizontally acquired DNA in association with RNA polymerase
  JOURNAL   DNA Res 13 (4), 141-153 (2006)
   PUBMED   17046956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10570331
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Corynebacterium mastitidis"
                     /db_xref="taxon:161890"
     Protein         1..115
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12925
     Region          1..110
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 marketvqyf ddlngtplge ddvqvvyfsl geksyvmdls aenaekfqdv lrpyldvarp
       61 hvpmakkrrs ngatrkskar eirqwaldng kdialrgqip seiveaynea hsane
//
LOCUS       WP_284830459             626 aa            linear   BCT 25-DEC-2024
DEFINITION  C-terminal helicase domain-containing protein [Corynebacterium
            mastitidis].
ACCESSION   WP_284830459
VERSION     WP_284830459.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium mastitidis
  ORGANISM  Corynebacterium mastitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13039667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Corynebacterium mastitidis"
                     /db_xref="taxon:161890"
     Protein         1..626
                     /product="C-terminal helicase domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=70707
     Region          <14..59
                     /region_name="SF1_C_RecD"
                     /note="C-terminal helicase domain of RecD family
                     helicases; cd18809"
                     /db_xref="CDD:350196"
     Site            25
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350196"
ORIGIN      
        1 melpadyvkt nvelgyastv hrsqgmtvee sfflpspkmd rqglyvgltr gktlnriyia
       61 ddeipdlddh spqqqppsar evvesildrd grsltarail aqadqpadle tlslvydeln
      121 dhliydhvth takhagldqa aellrqdwqt prlgaalsai eqqhpgdttl lseaierawh
      181 rfeednadst hddwivareh hdddspassl aflvrmeltn aigdtpspal sgedlwavsg
      241 lakplthhns mdpevhqamv yaaeqisqrl dtaadqavat hpewvhaige yrpkdedyhe
      301 kwthavrlia agreigdtda lsiaeknppe qsvyhhamha vryeqqrssh tryasmgrse
      361 lerflrhcdd kasladqear twemrassld qlraheekvr aervacvkka eqgvpilqar
      421 kmlsdrekqv yaaqaqlhaa hregfftrgk kvkdatshle aviaardket efyhslress
      481 pvaieeleka talasnegqw arrfqqayak dqelvdtaar narrlrmdeg lwqqrsrkia
      541 dkleesrplt hkeaqvyiqh ikdtlnrklp kgaatdidga npysldaadd lktqlaqqha
      601 qprsttphtp thhhtyehrt hndmel
//
LOCUS       WP_284830496              54 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium
            mastitidis].
ACCESSION   WP_284830496
VERSION     WP_284830496.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium mastitidis
  ORGANISM  Corynebacterium mastitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 54)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 54)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 54)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..54
                     /organism="Corynebacterium mastitidis"
                     /db_xref="taxon:161890"
     Protein         1..54
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=5418
     Region          <5..43
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mpqvaaglss ssiaklskga nlqtdtllri cealncdiad icevaltspn getn
//
LOCUS       WP_284830511             119 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein
            [Corynebacterium mastitidis].
ACCESSION   WP_284830511
VERSION     WP_284830511.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium mastitidis
  ORGANISM  Corynebacterium mastitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Corynebacterium mastitidis"
                     /db_xref="taxon:161890"
     Protein         1..119
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12895
     Region          3..103
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 msivkinalt vpaeaaatle erfaarkhsv dsapgfegfq llrptageer yfvvtwwkde
       61 asyadwrdnr aaaahgegee gqekrrpaat naellefevv ldsraedagn sedagntad
//
LOCUS       WP_284830581             435 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium sp. MSK194].
ACCESSION   WP_284830581
VERSION     WP_284830581.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK194
  ORGANISM  Corynebacterium sp. MSK194
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Corynebacterium sp. MSK194"
                     /db_xref="taxon:3377093"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46010
     Region          17..422
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 msqpnprevi ttqalgiwva amavylvait grtsfgvagl daierfdvda griavftsvq
       61 lgvyalaqip tgilidkfgp rlllvvgavi mgigqvvlgf ttsygvaiaa rvligagdat
      121 aflsvmrilp ywfplhrtpm ftqvtsslgq mgqfisavpf lwllgaagwt aafvtlgavg
      181 ilvaiaaiva vadspeklgi iptekeppns qatsiparlk kvfrspvawq ayfihyigml
      241 plivfvmlwg mpmmtqgmel skaksslvlt llavflvlvg plhgkissra qhirpwlslg
      301 fvavhvltwl ifftfgtdsg laailvvsfv talctptany gfdivrermd rsvvatatgl
      361 gnmggftsgm lgaqllgmvl dhssaapnys mpdftaasaa vlavwvvgmi gvvvthflrr
      421 ragedgpsvt ivevs
//
LOCUS       WP_284830618             634 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Corynebacterium sp.
            MSK194].
ACCESSION   WP_284830618
VERSION     WP_284830618.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK194
  ORGANISM  Corynebacterium sp. MSK194
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Corynebacterium sp. MSK194"
                     /db_xref="taxon:3377093"
     Protein         1..634
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=68388
     Region          1..613
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtspvlsvkd lrvnfpseag svsavrgvdf dlypgrtlgi vgesgsgksv tsmsimgllp
       61 dyakitgsvk fdgrellgls dkqmseirgn gigmifqdpl saltpvfdig sqlveaiqah
      121 rdvgkkqalk eatellalvg ipdphlrlks fphefsggmr qrvviaiaia nnprvliade
      181 pttaldvtiq aqilevikla qretgaatim ithdmgvvae taddvmvmya grpvergdvd
      241 tifsqprmpy tvgllgstpr pdvsaeeplt pivgsppvlv dlkqrcqfap rcpvaqpacs
      301 dgeppliald dapshqsacl rapeihdrki ggelmfkppq laedvmagis reerattlev
      361 tdlrkefplt kgalvkrrvg tvkavdgltf dirkgecmai vgesgcgktt tlleimdlkp
      421 engavvlngk daagmsnser rearkdiqiv fqdpmsslnp rltvreviae plnslgydgd
      481 vdarvnelmg lvgldssqld rfpshfsggq rqriglaral atnpsvlvld epvsaldvsi
      541 qagvinlled lkrrlglsyl fvahdlsvvr hlsdrlavmy kgqfvesgpt devfenpqad
      601 ytkklleaip ipdpeaarrr rnpdpadtsp isrk
//
LOCUS       WP_284830854             256 aa            linear   BCT 25-DEC-2024
DEFINITION  inositol monophosphatase family protein [Corynebacterium accolens].
ACCESSION   WP_284830854
VERSION     WP_284830854.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..256
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=26665
     Region          5..252
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mmdprelvaf aeaavdqvep ifrsgigapp ahfksrgdfa tevdlaiekq lrdilqqmtg
       61 ipvygeesgg sihdtvwvvd pidgtanysa gnpmagilva lvhegqpvaa isdfpllgrr
      121 lvasdgsplr saggpsggfg ggeespefdd arghvgcfsn lptaafhelr esglrpritg
      181 svgldnafva qgvfdgavnf sphpwdnaag allikaaggi itdpegnpwt vqsrgmvsgt
      241 pqvhetilei lshhsn
//
LOCUS       WP_284830791             435 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium accolens].
ACCESSION   WP_284830791
VERSION     WP_284830791.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45929
     Region          12..421
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 msqpnprevi ttqalmiwva amavylvait grssfgvagl daierfdvda griavftsvq
       61 lgvyaiaqip tgmlidkfgp rillvvgavi mgvgqvmlgf tssygvaifa rvligagdat
      121 gflsvmrilp ywfplhrtpm ftqvtssigq mgqfisavpf lwllgtagwt aafvtlgavg
      181 ilvaiaaava vadspeklgv iplekeppns qgssigarlk avftspiawq ayfihysgml
      241 plivfvmlwg mpmmtqgmel skgkaslvlt llavflvlvg plhgrissra qnirpwvalg
      301 fvclhvltwv lffafgtggg laaitvvsfi lalctptsny gfdiirenmd rsvvatatgl
      361 gnmggftsgm lgaqlfgmvl dhsadapnys mpnftsasla vlavwlcgma gvvithilrr
      421 rggyagpsvr ivevt
//
LOCUS       WP_284830862             182 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Corynebacterium accolens].
ACCESSION   WP_284830862
VERSION     WP_284830862.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..182
                     /product="YceD family protein"
                     /calculated_mol_wt=19117
     Region          1..182
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mtsplkfdvg ellnaqgada mpeqrtqtgp vperigvemi aipkgedltv aatltplgsg
       61 vlvdadisgv ltgecarclk elhpqldlhv tqvfaadesf vsgddadsdd agsgdeipei
      121 eddeldllqa videaglnlp fapvcedgcd iqtpegvttg isgeeeeeek vdprwaglek
      181 fl
//
LOCUS       WP_284830890             451 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Corynebacterium accolens].
ACCESSION   WP_284830890
VERSION     WP_284830890.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..451
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48966
     Region          1..451
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mhlhhdyakh lpdlvsathg eeqpdpqlvv lneelaqqlg ldtdwlrsae gldfllgrdg
       61 ghamaysgfq fgsfnpqmgd gramllgeve kdgklwdlha kgtgltpysr lgadgrgtls
      121 smlreylise amhalgvptt rslavistgr piqrghvqpa gvlvrvaash irvgtfhyaa
      181 qsghlqalad yaiarhypga dyreffqgvm drqiatvssw mrlgfihgvm ntdnttisge
      241 tidygpcafm esyspdtvfs sidqqgryaf gnqpailgwn larlteslvp lfdadinagv
      301 dfaqetingf qekfatqrrs diaaaldttt evasayltam qlprpditla hraladaarg
      361 htlpaqelfp dsdfldsyla thpapaavda amprviprnm aveaalraae agdmqpftel
      421 lhavthpwep hpsyeqpdpn glagfltycg t
//
LOCUS       WP_284830903             322 aa            linear   BCT 25-DEC-2024
DEFINITION  DHH family phosphoesterase [Corynebacterium accolens].
ACCESSION   WP_284830903
VERSION     WP_284830903.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..322
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33822
     Region          7..319
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mtrkeyqdav daisgaqsic iithlrpdad aigsatalll amqqsgkdac avigqdkdfa
       61 pnlysipgad qvkvmrelpq gydlyvtvdc gsidrtglfs adiaelaaag rvlcidhhss
      121 npgfgsvnlv dsecesttva iltildmlsv qientiahcl yaglltdtgs frwgrpamhd
      181 vatrlmhygl dtkqiatdll dattpddlqm vgrvlaglri ehagelgvgi liagladieg
      241 hsdsaveslv dfvralegtq lgvvfkeqsp giwavslrst aincaelaaq fgggghipaa
      301 gymtqgseea ivaelvsaid eh
//
LOCUS       WP_284830914             207 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium accolens].
ACCESSION   WP_284830914
VERSION     WP_284830914.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..207
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22925
     Region          9..204
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(32..33,35..36,39,41,69..70,100,104,111,114..115,120,
                     143,147..148,150..152,154..155,158..159,162..163,182..183,
                     185..187,189..190,192..193,197,200..201)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(146,150,153..154,156..157,192,195..196,198..203,206)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(167..174,183..184,187)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mtrrrtnipl svyvpgttvi hrmkpswkil illvfilvts iffnslpwas gaviaaalty
       61 fiarippria wsqlwpplvi liplagfqww akdfdyaavm flnilaamil aflltltstv
      121 daimeslees lqplnrfgvp venislamsl tirliplmfe tvyevldark argagfspsa
      181 fvtpviirsi rraraigeal qargvgd
//
LOCUS       WP_284830933             847 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium accolens].
ACCESSION   WP_284830933
VERSION     WP_284830933.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 847)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..847
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=94791
     Region          19..841
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mnlsqqlpdl tevpeslide aiwdtfnswt tskgidlypa qeeaslgila gdnvilatpt
       61 gsgksmvana ahfialargq rsfytapika lvsekffalc eifgaenvgm mtgdatvngn
      121 apiiaataei vanialrdga eanidqvvmd efhyysdpdr gwawqvplle lpkaqfllms
      181 atlgdtdwlq edltrrtgre tnlvagstrp vpldfsyvfs avhetieell adnkapiyvv
      241 hfsqreaaer aqaltslsgi inkeekedia eeiggfrftt afgkdlskll rkgigihhag
      301 mlpkyrrlve rlaqrgllkv icgtdtlgvg invpirtvlm tglakfdgqr qrilksrefh
      361 qiagragrag ydtegtvvve apdheienak arrrigddpk rlkklkkksa regevswsek
      421 tfarlteaep eqltsqfrvs nsmllnvlar hgdgyahmhh llrdnhdprs kqnkdiltal
      481 dlfrglldsg vvqkstkgld iygrpyhlvr elprdfalnq plgpfalaal slldpeadsy
      541 hldvisvfea ilddprqvlq aqqkkrrgee iaalkadgvd ytdrmnived itwpkpleel
      601 leqaydtfae tnawvkefel rpksvvrdmv enamtfsdlv atyglarseg vilryltdaw
      661 rtlkqsipde yttpqiedii vwlgelirqv dsslvdewaq magedspidq dtldrelafg
      721 vedptaltan rrafgimvrn ymfrlaqlfa leeedrlaev ldyldevpdf gavlddyfde
      781 yddidtgpea rgpeyfrlee sssrswpvrq iikdpagdra yqfvatvdld asdeagevrl
      841 selrvey
//
LOCUS       WP_284830970             368 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium accolens].
ACCESSION   WP_284830970
VERSION     WP_284830970.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..368
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39122
     Region          13..366
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 maladtrfsd rrrklaaela gqridavlvt hlihvrylsg fsgsngglll rkdlsalmat
       61 dgryttqiaq evpdleaveg ravgkvllqq fdkdetpvrv gfeadymsvs eledlkdsap
      121 dgvtlvpisg iiediritkd avelekleei aalanqaled llaagelrag rterevaadl
      181 efrmrilgse rvsfdtivas gpnsamphhg addrviedgd lvtidfgahl rgfnsdctrt
      241 yvvgtandfa keiydlvlra qqagveaava gtslsdvdaa crnviadagy gdyfvhstgh
      301 gvgldvheap faattgkgel apgmtltiep gvyvpgkggv riedtliitd gapkiitaas
      361 kdftelpa
//
LOCUS       WP_284831002             622 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Corynebacterium accolens].
ACCESSION   WP_284831002
VERSION     WP_284831002.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 622)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 622)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 622)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 622)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..622
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=67062
     Region          1..609
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mrqrlriilt cvvvatvalg grlawvqlvw gpdlaakavt qrervyidpa rrgeildrdg
       61 qrlaytmksr sltvsptrlr delkeqakme atsegklegm deskkdeylt kqmedklkem
      121 aegipkmied sgasaskvda sdiknklkad tqyevlvrnv dpdvaveisn kyhgvaadrq
      181 dirqypngai aenvvgkvsm dghgqfgfea ardteltgid gqstedvstd gqvipgtlrd
      241 vvdavdgrdv tltldldlqt yvqqklekak ansqaegaea vvldtatgqv lamantdtvd
      301 pnkniedqlk egkdfenrsi shpyepgsva kivtaaaalq egittpdevh qvpgsidmag
      361 vtvndawphg tepytttgif gkssnvgtlm iadklgpeky aeylkkfglg attgvelpne
      421 sagtvpdqeq wsggtfanlp igqgqawttl qmasvyqala nggeriepri ideikdpdge
      481 teklpepkkt qvvdketakt avdmfravfq dddagvqngt aanaqldgyq lsgktgtaqk
      541 vdpnsgaysn saywitfagi apaddprfvv avmldepksg vednggggqs aapifrdiss
      601 wllnrdnipt skpaprmtlr eq
//
LOCUS       WP_284831095             470 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium accolens].
ACCESSION   WP_284831095
VERSION     WP_284831095.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..470
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51487
     Region          5..401
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msrttlrsfi qrihfyggmf vgpfiliaal tgclyalapt lekfayrdvm tveevnnpvs
       61 ledqisaaqk ehpdmpvsqv wpaesatdst rvlvadpgid eslqrtvfin padgevigdy
      121 ptysglgemp lrrwisslhe sfhlgqpgel yselaaswlw vlacgglymw wirrrpkkaa
      181 aplkkqpqrs krwkatrlhs tmgawifigl iglsatgitw sqlagenvns vvekmnwkat
      241 pvetalttds sadaahdaha gheghgahgg daeaageape peviaeqaer vyatgraegl
      301 tgplrlyape dtdsgwkvse rwvewrytsd evsvdgstge vidrlpfsel plfsklsswg
      361 iylhmgimfg lplqialfal glaiaamvvl gyymwwkrrp qfapgskrhf swattglgal
      421 faatvgvfmp llgitlaafl vldiilmntg krkatapkkk dedaelvpvg
//
LOCUS       WP_284831176             341 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium accolens].
ACCESSION   WP_284831176
VERSION     WP_284831176.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..341
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34439
     Region          25..337
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msvrttrllg lgallllvlv gticsllyga rsipaedvwt alrdlpaasg pqdevptnqr
       61 vvaelrlprt ilaiivgaal gvagaliqgh trnpladpgi lgvssgaals vvvsfalfgi
      121 tapwatavva flgaiaatal vfglasagka avdpltlvlg gaalsavlsa itsafvltne
      181 nnldrmrfwt vgslagrdmn ialgilpfiv vglilafatg pqlnilnlgd dvaaglgint
      241 aaarlagmgi iallagaata aagplgfigl vvphivralt gpdykwilpy salagaalll
      301 cadvvgrlia rpgelqvgiv lafvgapffi aliyrkkvmt l
//
LOCUS       WP_284831218             440 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium
            accolens].
ACCESSION   WP_284831218
VERSION     WP_284831218.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..440
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=46994
     Region          1..438
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrmtvigtgy lgathaacma elghevlgvd idedkiailq sgkvpffepg lpevlernia
       61 agrlgfstny naaaqfanvh flgvgtpqrr gsyaadmtyv kavitglvpk lrgehvifgk
      121 stvpvgtaae lqeladglap egtrveiawn peflregyav hdtitpdriv igtresdsra
      181 edlareiyaq plaqdtpfiv adlqtaelvk vsanaflatk isfinavsei ceiagadvva
      241 ladaigidkr igrkflgagl gfgggclpkd irafmarage lgadqaltfl revdainmrr
      301 rdrmvdlske afngsllghr vtvlgcafkp nsddvrdspa lsvagslsla gaavtvydpe
      361 gmdnakkvfp tldyaadtes alreaelvil atewqqfkdl dpneagelvd nkhiidgrnv
      421 ldvaawsnag wkiqalgrtl
//
LOCUS       WP_284831358             425 aa            linear   BCT 25-DEC-2024
DEFINITION  Mur ligase family protein [Corynebacterium accolens].
ACCESSION   WP_284831358
VERSION     WP_284831358.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13558984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..425
                     /product="Mur ligase family protein"
                     /calculated_mol_wt=44795
     Region          64..>187
                     /region_name="Mur_ligase_M"
                     /note="Mur ligase middle domain; pfam08245"
                     /db_xref="CDD:462409"
     Region          312..410
                     /region_name="MurT_C"
                     /note="MurT ligase C-terminal; pfam08353"
                     /db_xref="CDD:462442"
ORIGIN      
        1 msfsvpgalk klrttaatsa aklattasra tgrgaggmig glianaidps imtnlgggrp
       61 avlvtgtngk stttrmlaaa vraehqvatn dggdnmdagi isalmagkda shlvlevdel
      121 hvphvadnln pqalvllnlt rdqldrvgei nkieralrga veahpdmlvi ancddvlmts
      181 vaydarnviw vsagagwlgd svtcprtggh vvrteddwya vkpladgref rrpqptwgid
      241 khgvitptak rplnlalpgr anrgnaaqai aaavegfgvd ldraiaaaes iddvagryst
      301 ihwkgreirl llaknpagwq ealsmvdrsa dglviatngq vadgidmswl wdvkfegfng
      361 lsvkaagerg tdlavrlvya dithqlipdp mdaltacpeg rievlanyta frdlkkalsk
      421 eanna
//
LOCUS       WP_284831436             441 aa            linear   BCT 25-DEC-2024
DEFINITION  nitrate/nitrite transporter [Corynebacterium accolens].
ACCESSION   WP_284831436
VERSION     WP_284831436.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Yan,H., Huang,W., Yan,C., Gong,X., Jiang,S., Zhao,Y., Wang,J. and
            Shi,Y.
  TITLE     Structure and mechanism of a nitrate transporter
  JOURNAL   Cell Rep 3 (3), 716-723 (2013)
   PUBMED   23523348
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   7  (residues 1 to 441)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..441
                     /product="nitrate/nitrite transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48311
     Region          31..429
                     /region_name="MFS_NRT2_like"
                     /note="Plant Nitrate transporter NRT2 family and Bacterial
                     Nitrate/Nitrite transporters of the Major Facilitator
                     Superfamily; cd17341"
                     /db_xref="CDD:340899"
     Site            order(41..42,45..46,49,82,137..138,140..142,145,164,
                     167..168,171,254,257..258,261..263,266,303,307,362..363,
                     367,371,387,390..391,394..395,398)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340899"
ORIGIN      
        1 mttldtsgkv iqgwdpedsd hwdskiawrt lwistfvlii gfatwylvsa iapqlnqigf
       61 dlsrsqlywl taipglacgi frlifmflpp ilgtrklvfs ssllfiipml gwffavqdss
      121 tpywwlmtla flsgigggvf sgfmpstgyf fpkrlsgtal giqagignfg isfiqlvapw
      181 lmgftllgvg fvapqrtddg eifvhnpaif lvpwaivgaf lawtllkdvp vkanfrqqmd
      241 ifgnkntwil tvvyfmtfga fsgfaaqtal linqifgegs dfagtydnlp agasyaflgp
      301 ligalvralw gplcdkfgga iwtfigclgm tiftvvatff ltpdepdevw wflgtmliff
      361 fftglgnagt fkqmpmilpk rqaggvigwt gaigafgpfv agvllsmmsa ptffwgcavy
      421 faittvlvwi yyarpnapfp g
//
LOCUS       WP_284831455             332 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium
            accolens].
ACCESSION   WP_284831455
VERSION     WP_284831455.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..332
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35168
     Region          25..332
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrkrnmalai tatfmsaall lvigpqriav attetgdael satlrkhtea gfnnltaftl
       61 hdgkatfagl gadehtevei gsvtkmftae lahqlveegk isldttvgev ldvgqapise
      121 vtvqellnht sglprlaqgn ifadaitavt ganpyagett qdildaatea dlkdrgtesy
      181 snmgygllgh lletaadtsy eellherilq pagmtetylm tpgsvpddap rgltatgrea
      241 dpwemggsna aagalrstah dmaafaewim dngdmafgwq ksednqsfwh dggtggystm
      301 liidpknkra afanndtpaw tsdlaqalfd gi
//
LOCUS       WP_284831601             411 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Corynebacterium accolens].
ACCESSION   WP_284831601
VERSION     WP_284831601.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..411
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=45728
     Region          68..398
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mkpvkklqlg siyktkrgdw raaitigydg qgrqirrtts gktkaecirr rnelylqlqq
       61 etmtptkvtv eafihqwidt aalekyspns lrnvkgycrn yiiptlgkyq ikdvgadevr
      121 eldhavrnag csdrmvqivh safsaamrda vrrglievnp vsrvdrprav skprtaltvd
      181 qarhlimhss nagdplaslw asylflgprk gellgltrdr vsltegaaqi dlswamsnip
      241 wrhgrgckcg idtradncam rehavppgye wqplngalil crpktltsrr ivpvpaplde
      301 vlrrhvestp dnewnlvwls atgrplrper alkrwkmalr daglpvvdlh tarhtaasll
      361 recgvgpevi atilghskvd mtfnyvhvna gqtqralady saflglpggd a
//
LOCUS       WP_284831751             475 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium accolens].
ACCESSION   WP_284831751
VERSION     WP_284831751.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..475
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=50757
     Region          8..404
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mkttthgals rlhkfagviv apflivaals gffyalaptl eqwvyhdeit ataqgsprsl
       61 ddqiaaaqrq hpgaavaave asedpeettr vlftdpdaks psythavfvd pvdlritgee
      121 qqyggsralp lrtwlsnghr tlwlgepgri yaelaaswlg altiagvylw lkrrkktqkk
      181 nnkalrvhar lgswllpgfl fltitgltws mvagsnigkv reelnwkeps vatsvaeaga
      241 gagghaghag hagheghegh aghsggeavd ndvlegaqta lstarseglt gvlrmtppeq
      301 agdawtvreg raayklrsda vavtadgrvi drinsadwpl aarltswliq lhmgtlfgiy
      361 sqvalaalal gllvisiagl wmwwnkprrr lpelkitpav vagvviysii aplfgaslll
      421 ffagdwlvrr lrpqsrsrsr sgsqsgpgrg ngasgptarp rgesssrips tvqng
//
LOCUS       WP_284831771             240 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium accolens].
ACCESSION   WP_284831771
VERSION     WP_284831771.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..240
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26128
     Region          12..198
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mttvsnpqls prpaaifwdm dgtltnsepl wgeatyylse vlgkrltpsq rmdtvgatft
       61 ttlricadna gvvlgegdve ayrhkmfdym ktlfagrlei fpgipellts lhhdgmpmmv
      121 ttntdrdvad aaiavigsey fvdticgdev ptgkpapdmy leaarrlqln paqclvfeds
      181 pagmraavaa gctviglpkd egvevpdgvv eisrlrdsrh lagalhtdvy ewfraiqemn
//
LOCUS       WP_284831777             938 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium accolens].
ACCESSION   WP_284831777
VERSION     WP_284831777.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..938
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103674
     Region          4..936
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtethldtfa aglpypldef qvqgceaven gqgvlvcapt gagktvvgef avslalsrgt
       61 kcfyttpika lsnqkyhdlv aehgedavgl ltgdvsinad aeivvmttev lrnmiyadsp
      121 aldrlthvvm deihfladas rgavweevil nladhvsiig lsatvsnsee fgewlatvrg
      181 dtsvivtehr pvpldqwmml grkiyplfep esggqvnsel ehriqrleag dsddgradyk
      241 sgkgfrarar hkgggrsefh gkaggrsgss rpqdryrplg rpevlkvlqs qdmlpaitfi
      301 fsragcdgal yqclrsrmvl ttqeeaeeik aivdagvegi peedlqvldf rrwrealsrg
      361 faahhagmlp afrhivedlf vrglvravfa tetlalginm ptrtvvlekl ikfngeahvd
      421 ltpgqytqlt gragrrgidt lgnavvqwap amdprfvagl astrtyplvs tfapgynmai
      481 nllgmlgfed slrlleksfa qfqadgsvve etreleraeh rvrelreqld davdalappa
      541 kdgedpaevl mdyirlrrel taeekqskvd kehqrtqevi avlarlqlgd viaiagkkrp
      601 tlaavvtpan qtedprpwvt tesgwsgrid atgisnppiq lgrikipkpv rknprrntky
      661 iqdvfhrekf drpkrmkskp rlrpnkrvge lrdairehpa hewpatdreq lagvaqklar
      721 rerdleklqa kvdkatdtlg rtferivdll aemdyvefsg agsdrtpvit eegerlakih
      781 sesdllvtqc lkrgiwdeld paelagvasl ccfenrkatg gqpeaatdrm adamnatwri
      841 ytelgaderr hrlpptrepe agfalaihqw sagaplgycm aaaneagael tpgdfvrwcr
      901 qvvdllqqia ktgydgqiqr narramdaiq rgvvaiga
//
LOCUS       WP_284831981             524 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Corynebacterium accolens].
ACCESSION   WP_284831981
VERSION     WP_284831981.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..524
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55568
     Region          128..515
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mttphthest aqsegaedpg aprnewrrqf iglfiglala ilvffifpsn aidtvqqstg
       61 vdeeadytls airtvaavti lmgvwwmtea iplaatalip lvifplasvg tikevgapya
      121 satiflfmgg flialslqrw nlhrrlalyv vkligtsprr lilgfmlatg flsmwvsnta
      181 tavvmlpigt svlaltaetv ggwdkqkkfa talmlgiays asigslgtli gtppnaflna
      241 ymtdtwdvtl gfgrwmavgv plaltfllia wvllitifkp emteipggre lindeikalg
      301 pwtrpqimtg iifilaalaw vslpivlgdf dnyddaivgi aagillfilp adserrirll
      361 dwktanempw dvlllfgggl slssafnssg lslwigemak glsslpivli vaavaalvlf
      421 lteitsntat aatfipimgg vavgvgltte gdinvlllti pvalaatcaf mlpvatppna
      481 iaygsgyvki gemikggvgl nvigiflitl tvfllavpif glav
//
LOCUS       WP_284832067             402 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Corynebacterium accolens].
ACCESSION   WP_284832067
VERSION     WP_284832067.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..402
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43711
     Region          1..396
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 manllgivff algigltval heaghmftar afgmrvrryf igfgprvfsf rkghteygla
       61 afpvggfcdi agmtaqdefl teeekpyamy kkpwwqriiv laggigvnli lgfvilyfva
      121 mtaglpnpda dvrprvgevt ctadqkenqe lesctgngpa gkagvqegdi ilaldgehld
      181 sftqlrdevm qrpgetvtlt verggeekdf sieletvkrl nqqgelvdag siglsnevld
      241 ivekhsatea lpatwhftty sleatvegik qfpakvpgvv asifghqrdv ngpmsvvgas
      301 rvggelvers lwasffmmla tlnfflalfn liplppfdgg hiavilyeki rdgirklmgk
      361 qplgpadytr lmpityvmaa llmglgvvii iadvvnpirl fg
//
LOCUS       WP_284832102             435 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium accolens].
ACCESSION   WP_284832102
VERSION     WP_284832102.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45930
     Region          12..421
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 msqpnprevi ttqalmiwva amavylvait grssfgvagl daierfdvda griavftsvq
       61 lgvyaiaqip tgmlidkfgp rillvvgavi mgvgqvmlgf tssygvaifa rvligagdat
      121 gflsvmrilp ywfplhrtpm ftqvtssigq mgqfisavpf lwllgtagwt aafvtlgavg
      181 ilvaiaaava vadspeklgv iplekeppns qgssigarlk avftspiawq ayfihysgml
      241 plivfvmlwg mpmmtqgmel skgkaslvlt llavflvlvg plhgrissra qnirpwvalg
      301 fvclhvltwv lffafgtggg laaitvvsfi lalctptsny gfdiirenmd rsvvatatgl
      361 gnmggftsgm lgaqlfgmvl dhsadapnys mpdftsasla vlavwlcgma gvvithilrr
      421 rggyagpsvr ivevt
//
LOCUS       WP_284832238             377 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium accolens].
ACCESSION   WP_284832238
VERSION     WP_284832238.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..377
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41332
     Region          11..356
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mrtqasvkrl pqhlpeldgl ravaalgiiv thvsfqtgtg wgfagrfdff vavffalsaf
       61 llwrrrglht vrgyahsria rlapayyacv vsvvlllpda hsitptqila nltstqiyva
      121 dglapglthl wslcvefffy lvlpllvwai gglpqrwrma viagaavvsw gwgfipfvad
      181 ysedqvnsqi wppayaswfa vgmlaaevee rgigkrtarl lqvrwiwvvl aglvlwvasr
      241 dwfgpaglvh pepaefarri iagavfaacv vvpvalvprg tswltsplmq algawsysif
      301 lwhvavlava fpltgvalfs gkpldfwvil avtvigtvvv saasytlier pgrdllmgrg
      361 rgrrrrkgrp tprhist
//
LOCUS       WP_284832312             186 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsB family cell division protein [Corynebacterium accolens].
ACCESSION   WP_284832312
VERSION     WP_284832312.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..186
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=21362
     Region          44..129
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 marekkterr rsrtrvpvas raadirksqw aqekknrkpd rmsivgmtvi vvfvllmlvi
       61 iavplrnyyh grseiarlne siaakqdekd alleeidkyk sedyikqear rrfgvveqge
      121 tayrildpni qpdnqvttns keqedsrpwf evlwdsvaqp peeeapages hhlpiepape
      181 esgdvr
//
LOCUS       WP_284832380             524 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Corynebacterium accolens].
ACCESSION   WP_284832380
VERSION     WP_284832380.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..524
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55524
     Region          128..515
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mttphthest aqsegaedpg aprnewrrqf iglfiglala ilvffifpsn aidtvqqstg
       61 vdeeadytls airtvaavti lmgvwwmtea iplaatalip lvifplasvg tikevgapya
      121 satiflfmgg flialslqrw nlhrrlalyv vkligtsprr lilgfmlatg flsmwvsnta
      181 tavvmlpigt svlaltaetv ggwdkqkkfa talmlgiays asigslgtli gtppnaflna
      241 ymadtwdvtl gfgrwmavgv plaltfllia wvllitifkp emteipggre lindeikalg
      301 pwtrpqimtg iifvlaalaw vslpivlgdf dnyddaivgi aagillfilp adserrirll
      361 dwktanempw dvlllfgggl slssafnssg lslwigemak glsslpivli vaavaalvlf
      421 lteitsntat aatfipimgg vavgvgltte gdinvlllti pvalaatcaf mlpvatppna
      481 iaygsgyvki gemikggvgl nvigiflitl tvfllavpif glav
//
LOCUS       WP_284832482             445 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Corynebacterium accolens].
ACCESSION   WP_284832482
VERSION     WP_284832482.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..445
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=49959
     Region          1..442
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mtslmwfrdd lrlsdnqalt raaeaatdkn gskpelvavv ldepaypstr plggathwwr
       61 erslhalaqe lasrgvkllr atgdartvip riahevgadt vtwnrryhgp lrevdatvka
      121 tladaginai scpgftlvep wevtnaqgnp ykvftpfaaa arsqfaddep lpvpellagr
      181 emgasasssw pnpsadepqw aaslaqywtp geagarerla qldlahyaee rdiparnats
      241 llsphlrfge vsprevwvaa aeepnaekyq sellwrdfaw hrlyhlpdla trnvrqkfnr
      301 fdwswddprl kdwqegttgi plvdagmrel whtgymhnrv rmvvgsfltk nlgihwrlge
      361 ewfwdtlvda daasnpfnwq wvagcgddaa pffrifnpet qaqrfdpdga yirrwaptls
      421 appivdlrqs rqaaleayae ikdad
//
LOCUS       WP_284832490             256 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium accolens].
ACCESSION   WP_284832490
VERSION     WP_284832490.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..256
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27908
     Region          1..244
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(17..18,20..21,24..25,63,67..68,71..72,102,106,113,
                     116..117,122,138,142..143,145..147,149..150,153..154,
                     157..158,178..179,181..183,185..187,189..190,192..193,197,
                     200..201,211,213)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(141,145,148..149,151..152,192,195..196,198..203,206,
                     211..212,216,218)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(162..169,180,183..184,187)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mpnllrnvnp ltriflmfvw vtpllasidw vsaalslslt filaplcgvs wlrlwkagwf
       61 lfliaplsgi smllygapgg eeyfswwlit vtensvtlai aitlrvlava lptvvlardi
      121 dptelgdals qilrlpsrfv igavagvrmm tllksdwqsl gmarrarglt degrfkhllt
      181 msfgllvial rrggklatam eargfgrtpp gggertware srlhardgwv macglalacv
      241 pvvtsvltga wrffgl
//
LOCUS       WP_284832573             392 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Corynebacterium accolens].
ACCESSION   WP_284832573
VERSION     WP_284832573.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..392
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42541
     Region          125..387
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mkiiarllsv plalvaflal wlavapftph ipywgagali gpqyigpvil fslillvlaa
       61 igrlgsrsfy vpgafaaval iagislfgtq ihaakeqgtd vdiraalswa gvestdegpd
      121 htvaydsfhg edldmdiytp ndggthpvmm yvhgggwdqm nkhsqafnmr qmaqrgylvl
      181 sidytlsswd qptwkvaagh vgwpmnwvna haadydgdpg rfftygesag gqlvlnatad
      241 aaahpnhlps adcpgtpavp ravyadspal dvrhiydsdd pyaaqgsrdt vqkylggtpe
      301 eypdradfvt sathlttdmp pikivrsdnd rlvppesydd frriaqekni dlseyvrpha
      361 dhasalsahg vwnqhllqam pqffaehdpq gs
//
LOCUS       WP_284832644             924 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium bovis].
ACCESSION   WP_284832644
VERSION     WP_284832644.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium bovis
  ORGANISM  Corynebacterium bovis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 924)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 924)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Corynebacterium bovis"
                     /db_xref="taxon:36808"
     Protein         1..924
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=100435
     Region          40..922
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mssetphasg ppdpdpdapa tpstspspda aataptvatf rehygfplds fqveaveavd
       61 agrsvlvcap tgagktvvge favftalrhg gtcfyttpik alsnqkyhdl varygeadvg
      121 lltgdvsvng dapvvvmtte vlrnmiysgs prldslthvv mdevhfladr srgpvweeai
      181 ltldprvllv slsatvsnag efggwlrtvr gdtdivvtth rpvplhqhlm vgtrvlplft
      241 gdtddlgavn raavaaaata ekqgrrrgtk rsdavmrlrg dgmlpaiyfi fsragcdgav
      301 rqllvdridl vtpeqreeil rtvdagvdgi gredlgilgf rqwrralshg faahhagmlp
      361 afrhivedlf srglvkvcfa tetlalginm parsvvlekl vkyngeahvd ltpaqytqlt
      421 gragrrgtdt vghavvlwsp gmdpyavadl astrsyplds tfrpgynmav nliatkgydd
      481 ahrilersfa qyqidgtvve raeqverrrr dldearrtle tavgrvappa vdgtdaveel
      541 ldyaelrrll sheerrakrt agderraett alladrgfgd iivlptgrdp dvavvvrpdg
      601 nrrdprpwiv tedgwcgpvs advfrnvpla vghmalprga qksprrlars vaatlrrqhv
      661 dkprslkvta rgstraasdl rdrvhthpvh awpdreqlva patqllkarr rldhelgeag
      721 pdadtlgrtf drildllrel dyvdgrgpdt avtvegqrla rvhhesdllv aqclrrgvwd
      781 hldpaelaaa vstcvfeirr evpvagagpg lptepltaav edvirihrel tsdeerhrlp
      841 vtrppepafa aalhqwtaga pldyclraae aagapmtpgd fvrwcrrvtd llsqitqtgy
      901 sdevragara aaralnrgvv avga
//
LOCUS       WP_284832645             377 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium bovis].
ACCESSION   WP_284832645
VERSION     WP_284832645.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium bovis
  ORGANISM  Corynebacterium bovis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Corynebacterium bovis"
                     /db_xref="taxon:36808"
     Protein         1..377
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=40345
     Region          18..365
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mserssifpp etfrsrldrv adlvesrgld galitpgpdl eylldsriat herfaglvva
       61 pgrrvmvvpa vdaadmrssv agaigvdvvg wsdgedpyal vpagdvavsa sttadhltil
      121 mdrglrpvna ttvlrdvfmr keeaeigelr raahaidevh rqvpailrag vtenevaael
      181 ealilaehrs vdfiivgsgp hgadphhdhs drvirdgdvv vvdiggtldt gyhsdctrty
      241 vvgepddrqr emyavlqaaq qrgldvarpg vtaqevdrav rqvideagyg eyvihrtghg
      301 iglsgheepf iiegndlvle esmafsvepg lyvpgswgar iediivltad gheqlnvtth
      361 dlvhvpaegg aatgagr
//
LOCUS       WP_284832685             514 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Corynebacterium
            bovis].
ACCESSION   WP_284832685
VERSION     WP_284832685.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium bovis
  ORGANISM  Corynebacterium bovis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Corynebacterium bovis"
                     /db_xref="taxon:36808"
     Protein         1..514
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=55515
     Region          1..509
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtpllsvrnl diafgsrptv sdvsfdvhpg etvavvgesg sgksttamsl lgllpgrghv
       61 tggtitldgq dvthlsparw talrgsvvgl vpqdpmsnfn pvwtigrqvg ealranglpv
      121 srvpelleea glpdarrrms qyphqfsggm rqraliaagl aarpklliad eptsaldvtv
      181 qrqildhlag ltaqlgtavl lithdlglaa eraerivvms rgrvvetgpa levlrnpqhe
      241 ytrrlvaaap svraasparp etppvveven ltktfggfta akdvsfqlrr gqtlalvges
      301 gsgkstvaqm vlgllpptsg rvlvdgadvt rlrrkeelaf rrrvqpvfqn pygsidpmys
      361 vfstiveplr ihrvgsraer earvrelldm valpqemmhr fpgelsggqr qrvaiarala
      421 ldpevlilde avsaldvlvq aqildlladl qarmgltylf ithdlavvkq iadetlvmrr
      481 geivergltd elfadpqddy trrlldsvpg atll
//
LOCUS       WP_284832862             397 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium bovis].
ACCESSION   WP_284832862
VERSION     WP_284832862.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium bovis
  ORGANISM  Corynebacterium bovis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 397)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18950610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Corynebacterium bovis"
                     /db_xref="taxon:36808"
     Protein         1..397
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=41238
     Region          40..190
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
     Region          203..>278
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mithtgtgdl stslslsvhd rghvarigsr paqefarptf aagavlwrrp sgagvtagqd
       61 gaarpaagar agdavpesad vlvamvhrpr yddwslpkgk vdpgenlpat avreiveetg
      121 ltpslgwllg yvhypvgsrt kvvyywtaev pdgsfvpnde vdelrwvtpa earelatyea
      181 drtvidaaer vlslgcarrv lyvrhakahd rqgwggnddl rpltkkgrrq aemlvseleg
      241 yrpttvstaq pdrcvhtatp laqdlgvtlr tdralgdavl gdaapgdpta agrthatgga
      301 gadgsdaasg aagagdatga tggdaaaaaf arattapvsv vvsqgavipe lisrfaagtg
      361 vetddmrvkk sstwvlhfdr dggllgadyl asplpvk
//
LOCUS       WP_284832890             432 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Corynebacterium bovis].
ACCESSION   WP_284832890
VERSION     WP_284832890.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium bovis
  ORGANISM  Corynebacterium bovis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Corynebacterium bovis"
                     /db_xref="taxon:36808"
     Protein         1..432
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=44471
     Region          1..426
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 mafalgvvlf vigiavtigl heaghmqvar wcgmrvrrff igfgptvwsf rrggteyglk
       61 avpvggfcdi agmttldpvt adelpdamyg rpwwqrvcvl vagvvvnvll glvivyavtv
      121 vwglpnpspd irpvvgrttc vpvtladata assaaasggt agctgagpaa esgvragdrf
      181 vridgrdtpq fgdvsaavaa aaeghtdvgs tvrvpatver dgrrtditls vlvveraass
      241 gassstsgap gpggtvttga igvvratpen ltlhynpvta vggtasftgt mvsqtvsgii
      301 slparfpgvv esifggqrat dspmsvvgas raggelvqhd qwqafaltla slnfflagln
      361 lvplppldgg havvvlwerl rdavrrrrgl ppggpadyrr lmpvtyvaag lllvfgvtvi
      421 vadvvnpvrl fp
//
LOCUS       WP_284832972             773 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium bovis].
ACCESSION   WP_284832972
VERSION     WP_284832972.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium bovis
  ORGANISM  Corynebacterium bovis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 773)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 773)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Corynebacterium bovis"
                     /db_xref="taxon:36808"
     Protein         1..773
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=83570
     Region          4..767
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mllahvdaar drltrrlgev qrrtadidhp qallerdhey heisrrldey saaeiglffg
       61 ridvddedpe npvpghpdrd rryigriglh tdddemrtll mdwrapmarp fylattlrpd
      121 gvhtrrhirt rgrtvtgvfd erlrggdgsp tgpadpadaa rhrgavaree alldavtrar
      181 tlhmtdivdt iaaeqdliir edhrgvtvvq ggpgtgktav alhrtaylly twrrqletqg
      241 vliigpsprf lsyisqvlps lgetgvvlat pgtllpgltt rplsdeslta qevkgsgemv
      301 hilgravaar qtvpdapvel svdgvavtlt pamvrtartr arrsrrphnl arprftetvl
      361 dqlaealaet lganplggpn lltphdreel radladdpgv aaeldalwpa ltpeglladl
      421 ysdpvlldaa aaeyddltrd alrrpeapdd wteadaplld elavllgvpd reeedagaea
      481 awreriaeaq ealdilagsa sqdvdesgrd mahdstdaei lmaydvidae tlaarqqvrd
      541 trttaqraaa drdwayghvi vdeaqelsvm awrmifrrsp nrwmtvvgdp aqtgnpagve
      601 twaetlgpfv ddrwrlhelt vnyrtpgdia aiagdllarv spgqtapsal rrtgtgvrsa
      661 pradaaaava rarelagdgl vgvigtprtv aalraegvga gagpadgtas evvvtdvaga
      721 kglefdevvl vepaeiveds pqglndvyva vtratqgltv lhdrdlpwsv ttg
//
LOCUS       WP_284832982             215 aa            linear   BCT 25-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Corynebacterium bovis].
ACCESSION   WP_284832982
VERSION     WP_284832982.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium bovis
  ORGANISM  Corynebacterium bovis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Schwartz,C.J., Giel,J.L., Patschkowski,T., Luther,C., Ruzicka,F.J.,
            Beinert,H. and Kiley,P.J.
  TITLE     IscR, an Fe-S cluster-containing transcription factor, represses
            expression of Escherichia coli genes encoding Fe-S cluster assembly
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 98 (26), 14895-14900 (2001)
   PUBMED   11742080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Corynebacterium bovis"
                     /db_xref="taxon:36808"
     Protein         1..215
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=22300
     Region          2..>105
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mqltrftdlg lrviiylaad qltddgtrpr rrhtsssvak aidasathva kvvsrlaeig
       61 virstrgrtg gvrlaeggld frigtlirql egdsrlldsf rtpdhddaaa pttadgtgap
      121 tttparttda eppvhtvvtg pdgtpadagg espaawrehc dklstalvea qsaffaaldt
      181 irvrdiagvr ppgtsastps pvrgpgptvp ldagh
//
LOCUS       WP_284833044             329 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium bovis].
ACCESSION   WP_284833044
VERSION     WP_284833044.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium bovis
  ORGANISM  Corynebacterium bovis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Corynebacterium bovis"
                     /db_xref="taxon:36808"
     Protein         1..329
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33291
     Region          30..325
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtrpavrrtv glaglgvalv lllalsvavg snplpldtvw rmltapdgsf eaiivrdqri
       61 prtvlvvvvg aalgvagalm qsltrnplad pgilgvnaga slavavtgit svwfylwfaf
      121 agaaaaaavy llggggrrap dpaqlalagv avsmavsavv qgvvlsntna fnefrfwvag
      181 saegrgypvt lavlgfivag lilaalvapa lnalalgdes grslgvhvar trvlvvvait
      241 llagaataav gplmflglvv pfvaraicgp dqrwitptci laapvvalva dvaartvvap
      301 qevqlgimta llggpvfiav vrrrrieal
//
LOCUS       WP_284833204             896 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium bovis].
ACCESSION   WP_284833204
VERSION     WP_284833204.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium bovis
  ORGANISM  Corynebacterium bovis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 896)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 896)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 896)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 896)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..896
                     /organism="Corynebacterium bovis"
                     /db_xref="taxon:36808"
     Protein         1..896
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=96287
     Region          60..860
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 masappptpp gggpnrvddv ireakeaara agvdshadgd fsyhdrlarr egaalttfaf
       61 hldgltsavh agqleralrs mpgvdatvvy ssrmawvtap dtmtpddvra titdagvesw
      121 ltdtslrrra drltisdrrr rmrrhrathe rarmlmerrk rehaplgpqr rggvagtdvl
      181 ytarelitka rlivavllgl pvialqvvea wqfpywqwvs lalatpvvtw cawpfhrati
      241 aglrrgmsal daassvailg gyaysvwvll ndgwhngtga pgwtsrpvlm amdyadvvag
      301 slfldvacga tvlllfgrll srrsqlrsrg llsslrvpst vqvtvvrndr agkpvkseia
      361 taeirvgddi ivhsgglvps dgvvvggktt vdmgpvgglt rttevtvddr iyagarvlgg
      421 avkirvsrtg srtrlaamgr wignadreen rlaqlatrta silvpwafvv agvdllmwil
      481 vtgniqaafa sslsvlacva pvalalsttl glrlglaraa angtllrdts tihklavvds
      541 iifnrvgtlt sgpmrvvnlt aaagenpelv lrvagalsle sdhavsraiv radreardag
      601 tggdsvphwl dvdtvtvtdr gsftgvvdip vtdprtgeve trhteaslwr prdvselrdf
      661 rmvsaavsgg tplvvswkgr vrgvinvadf pkpdaadavd rledmdietf mltrdtypva
      721 rkvadslgis tvlagiapnr kqatvrgvha qganvamvgd kdvldcltva dvgilmgsad
      781 ridnaeadvv lireditaip eavnltrhvr atvdwniwla wlynlgaivl avsgvlhpll
      841 atvlmlgsss liewrssril srdysrsqmg eaaglrrigi rvrewagrnl tvreea
//
LOCUS       WP_284833244             272 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium bovis].
ACCESSION   WP_284833244
VERSION     WP_284833244.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium bovis
  ORGANISM  Corynebacterium bovis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Corynebacterium bovis"
                     /db_xref="taxon:36808"
     Protein         1..272
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28674
     Region          60..218
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mtytfddwyr arsrqpdpvp dvppwlagvt grarsstldr llpgpgravp etdddgvppr
       61 ysavlvllgg dpdatetpgd atlllthrtp tmrthsgqva fpggrrepgd agpvatalre
      121 aveetgldpa gvdplavcre iyipgsnsav vpvlaywrrp vpvrpattet dwvapvplat
      181 ladparrsrv glagwsgpaf dlgpyllwgf tggvvsavld lggwarpwdd gtvrdlvtal
      241 gesgngeplg tldrrrhgad aapapdtetp ed
//
LOCUS       WP_284833706             536 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium bovis].
ACCESSION   WP_284833706
VERSION     WP_284833706.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium bovis
  ORGANISM  Corynebacterium bovis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Corynebacterium bovis"
                     /db_xref="taxon:36808"
     Protein         1..536
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54884
     Region          177..477
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkrwvryagg vgaavvvvgl vtgtavavni aptattgmay iakaacerry vqgqgnftpd
       61 vppnsidgfv stgfeaqees atasvmglyp stawripgsg cvvadsrpav tdpvppvaer
      121 ttpgvpqpvr pftgpadaav qravaaaldr egsrgvvvvq dgavvgegys ggfdeftpqr
      181 gwsmtksvtn alagrvaaga vpgatlspdd hdlwagwgeg derrsisvdn lmrmtpglew
      241 desygltgdv aellyhepdq aafvadkplt srpgttrtys tgttallcsv lqdrtrmgad
      301 mayrllyrpl gmasaelefd rsgglacgsg mmatprdwak fgqfilndgv vdpdapdvvd
      361 patgeaspap aarrllprdw lresftthpa ggegatessg gtgtapygag wwvnraadgr
      421 ahfpdlpvdm vwadghdgqy lavvpsrrlv vvrqgftpga sfansgmrel vrdavaatdt
      481 asggrrwpgt vgagtdadat agagsgsgag agsasgsggg wsgagadata gaglmq
//
LOCUS       WP_284833853             468 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Corynebacterium bovis].
ACCESSION   WP_284833853
VERSION     WP_284833853.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium bovis
  ORGANISM  Corynebacterium bovis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 468)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 468)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 468)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 468)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Corynebacterium bovis"
                     /db_xref="taxon:36808"
     Protein         1..468
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51654
     Region          3..456
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 millsltvrn hrsirdeitl dlttpslrtl kprddrtwae stypllgilg anatgksail
       61 daltymfaai hrsatvwqea pamlrrpfal dpesrdssst yeidfvlddr rhrygfevda
      121 dgivaewlyd lprsrwrtrl erdrdsgrlv iggrpaplst vtdrelvlsr alllrtsplh
      181 tlarslvdrv dvvrindsyr rsrlqslads laegattfad irgllqiadi gvkdvslred
      241 aipdalldlt rklkevfspd tstdddttdd dsstarendg apstgtpdps peapdgparp
      301 edpdavlrhv vrsltfthhg dtgeapefsi ddesagtvaw lvlavpalea lrrggllivd
      361 eidsslhphl ldillttfad paintrhaql iftahdanil splstvplae eqiwftdktr
      421 egvteltcla dfpkhpdanr qkrylsgvyg gvphlspsif arlidtds
//
LOCUS       WP_284833787             343 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase, partial
            [Corynebacterium bovis].
ACCESSION   WP_284833787
VERSION     WP_284833787.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium bovis
  ORGANISM  Corynebacterium bovis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Corynebacterium bovis"
                     /db_xref="taxon:36808"
     Protein         1..>343
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
     Region          5..227
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mtltlnyaaa sdvglvrtnn edsafagqrl laladgmggh aagevasqll isalahleed
       61 apgsrlltrl aeatdegnra iaayveehps qegmgctlta llfdgdrlgl chvgdsrayl
      121 lrdgeltqit kddtfvqslv ddgkldpedv sshpqrslil kaltgravep tlsvreareg
      181 dryllcsdgl sdpvsrdtik eildqgtpae vsrrlieial rgggpdnvtv vvadvvdaat
      241 pglpadpvls gavnldapei prpdtaasra vgfrvltraa nashgtsahs tsgagptltp
      301 gaaagsapap gggttpssag tpgpasapga gdatpggaaa aga
//
LOCUS       WP_284833902             298 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Corynebacterium appendicis].
ACCESSION   WP_284833902
VERSION     WP_284833902.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..298
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31005
     Region          10..285
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mtrtddavdl rpvllvligs lgiqssaivs stlfaelgtv avstfrlvia avmllvafrp
       61 avrtfsrgrw inaciygiam aamnqfyfaa vdrlplgvvv tldflgpclv sflglkhwre
      121 rgwalmafig vvliagpssg mdpvgliygf laggffaayt vfaervgkae ggglsdlais
      181 vavaalvtlp iaapklidvs pnawlvltla aligvvipyi adtlaarits aqvvgtlfal
      241 dpvvgsilgw llkgdeltar mligiplval agaiitwrsk prgeaggsaa rpqvqdgd
//
LOCUS       WP_284833914             284 aa            linear   BCT 25-DEC-2024
DEFINITION  N5-glutamine methyltransferase family protein [Corynebacterium
            appendicis].
ACCESSION   WP_284833914
VERSION     WP_284833914.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Schubert,H.L., Phillips,J.D. and Hill,C.P.
  TITLE     Structures along the catalytic pathway of PrmC/HemK, an
            N5-glutamine AdoMet-dependent methyltransferase
  JOURNAL   Biochemistry 42 (19), 5592-5599 (2003)
   PUBMED   12741815
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..284
                     /product="N5-glutamine methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29634
     Region          5..280
                     /region_name="HemK"
                     /note="Methylase of polypeptide chain release factors
                     [Translation, ribosomal structure and biogenesis];
                     COG2890"
                     /db_xref="CDD:442135"
ORIGIN      
        1 mkqsslraai adatqslida gvasphvdsr liaahllgvp ptqlvlaepg vgffddyaal
       61 iarraqrepl qhiigtapfg ahdlkvgpgv fiprpetevl aewavgqkpt gtvvdlgtgs
      121 galavyiaer aklelvigve kshvaaaaar dnaaafpnvr iiegdmtdpd lladlsgavd
      181 livanppyvp fvpeesgele pevyrdplda vfsgddgmda irglipvaar llapdgklgi
      241 ehddstavlt relveangsf tdvgnmpdlt grdrfvtask issn
//
LOCUS       WP_284833935             157 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium appendicis].
ACCESSION   WP_284833935
VERSION     WP_284833935.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 157)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 157)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..157
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17004
     Region          71..153
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 medlearvaa lesthatsts gdfwvvdhik sansfqpgtd qgsvafggav tlggreyayq
       61 wersteflag rewdeyidri aaiahpvraa ilrrllstpt tvaelveesv vsstgtgyhh
      121 igalhdagwi skldgryeir psrvipllti iasgedh
//
LOCUS       WP_284834002             740 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium appendicis].
ACCESSION   WP_284834002
VERSION     WP_284834002.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..740
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=80723
     Region          6..739
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 maksvdtrdt raeeqrhvdt lfahldreva aasarleevq ravdpdnpda dalvrretey
       61 hglnakldal niaetglvfg riditdndpe npvpgrgdld rryigrmgmd dradnyrtll
      121 ldwrapmarp yylattahpe gvekrrnirm rgrtvaavdd evlsgdnada aaqttdvgse
      181 aallramnsp rtghmqsive tiqreqdeii rdptrgvlvv gggpgtgkta valhrvayll
      241 ytwrdqlart gvlvvgpnrt fldyisrvlp elgetgvvls tvadlvpgit phgtdslvar
      301 evkgsedmal ilkravqylq tvpdddialr idgidlavtp amvaaartra rrsrkphnea
      361 rayfadhltq liaealaeki gadplggtnl lseadvdqlh ddlaedgqva givdkyfpel
      421 dapavlagfv sdadaiaaaa hdyddvtrda lfradgwaft padtalidel ytltgiptps
      481 geaekadrkw relvadaeda ldilassant dtdddefeae vlsahdiida etlasrqret
      541 dirstaerar adlswayghv ivdeaqeltp mewrmvfrrc psrwmtlvgd paqtsspagv
      601 eswseslapf igerfrfhel tvnyrtpkei mefadellae idtaaepavt vrstgepvrr
      661 ldagtdldyd aaaekirael darggltavv tadnvgevkg lefdhvvvvd pdaivnaspq
      721 gwqdlyvavt ratqtltlig
//
LOCUS       WP_284834070             336 aa            linear   BCT 25-DEC-2024
DEFINITION  YncE family protein [Corynebacterium appendicis].
ACCESSION   WP_284834070
VERSION     WP_284834070.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..336
                     /product="YncE family protein"
                     /calculated_mol_wt=35016
     Region          101..288
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mklrrvltkk sagpaavlag salllaacsq ppgvpqeapd mgnaepaqsp pasdiegekv
       61 dypavedlei tdgmigvrad gvlrtgtlde vkdgagtahe ladscgdvta nagafvtvcd
      121 gevrvftgad ertftpdepv tvaaplpdgr viagsaeeak vwvfdtdgnq tgritvarps
      181 dfvlagqdrv vrlnrfdtti qdiqldkdrq ggtlrvglgv gqakfgddgl vlasdatgsq
      241 llvyttdevv rlhqtvptdp hpwavawdpa nklawitste antatgfdis kgvpreqrkv
      301 gtvadaqhmi slddgtilia sssgdglqii ppdsnn
//
LOCUS       WP_284834081             179 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF421 domain-containing protein [Corynebacterium appendicis].
ACCESSION   WP_284834081
VERSION     WP_284834081.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..179
                     /product="DUF421 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=19340
     Region          7..155
                     /region_name="YcaP"
                     /note="Uncharacterized membrane protein YcaP, DUF421
                     family [Function unknown]; COG2323"
                     /db_xref="CDD:441897"
ORIGIN      
        1 menifyndws tigvtaakgv liyialiaml risgkrslsk fnifdfviti aigsifastl
       61 tsndvklaqa vtaivvllgg qylisklalr sesfeklvks dpallfysge fndetmkner
      121 vtrrevlqav rgsgsasmnd vtaviletdg tisvigaaed tappkrnelf dsvkrnpea
//
LOCUS       WP_284833983             495 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Corynebacterium
            appendicis].
ACCESSION   WP_284833983
VERSION     WP_284833983.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..495
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=55122
     Region          11..494
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mttapsppdh spitlvwfrd dlriqdnpal adaaahgavv alfveeentg irpigaaarw
       61 wrnrslealr adlaahgvem lyahgdprtl vpdiaqqiaa gttgtvrvsw nrryhepmrd
      121 tdasvktala eqsieahsfp gylltepwrv qtgsgtpyrv ftpfaksaqq sllddppqpr
      181 evpelrgakl alahpslida aqlgcgttqp awtaqlaehn apgetaaher lqafldglar
      241 gesykadhdi psadatsgls phlrfgeisp gyvwaetarf aeahpaaapd awaflrqllw
      301 rdfawhrlyh lprlttnnvr eqfddfpwew sgkvapgasi safvraeddp daqhlaqlaa
      361 wqcgrtgipl idagmrqlwt tgtmhnrvrm vvgswltknl gihwrhgeew fwdtlvdady
      421 asnpfnwqwv agcgddaapy frvfnpltqe kkfdphglyv aqwvperhtp gypepmvdvk
      481 esrkvalaay ddirr
//
LOCUS       WP_284834146             282 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Corynebacterium appendicis].
ACCESSION   WP_284834146
VERSION     WP_284834146.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..282
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31791
     Region          7..272
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mpfdipsidd ilnleqlddh ifrgtsvysg lqrtyggqva aqalsaatkt vedgklvhsl
       61 hsyfirpgqa drdivfvvnr vrdgrsfatr ivdavqgget ifsleasfhi tddkgiehsd
      121 emrpvpepes vvpleetdgp lkffsmwakd wdvrvvpdde fehnpytpsq qvvwfkskrq
      181 lpddqtfhic tlaymsdltl lhsalvphrd hkvqmasldh amwfmrqfra dewmlydqvs
      241 psahgaralt qgrifdrqgn lvamtvqegl trtlkeggaa fs
//
LOCUS       WP_284834196             241 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Corynebacterium appendicis].
ACCESSION   WP_284834196
VERSION     WP_284834196.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..241
                     /product="energy-coupling factor ABC transporter
                     ATP-binding protein"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26606
     Region          4..226
                     /region_name="EcfA2"
                     /note="Energy-coupling factor transporter ATP-binding
                     protein EcfA2 [Inorganic ion transport and metabolism,
                     General function prediction only]; COG1122"
                     /db_xref="CDD:440739"
ORIGIN      
        1 mptisfdras vaydsdvilh pqtfeltekr igvigsngsg kstlvrling liepssgtvs
       61 yngldvaehg kdvrkkvgfi fsdaeaqivm prvrddiafs lrrfklpkae vnarvddmle
      121 rfqladraen sphtlsggek qmlalaavmv iepetiiade pttlldmrnr rrivreltsl
      181 dqqvivvthd idmltdfdrv lcvnngdiaf dgparkaiaf ytdlmdqldr deagesgnve
      241 t
//
LOCUS       WP_284834299             280 aa            linear   BCT 25-DEC-2024
DEFINITION  cell division protein FtsQ/DivIB [Corynebacterium appendicis].
ACCESSION   WP_284834299
VERSION     WP_284834299.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..280
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=30445
     Region          86..280
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mstsvtpphg eddrtgdgde rgrelreens ldrarskyte rsnrsgnrsk qkttnargrr
       61 evpwrriagi agvglvvlav lwavvyftpl fsvknvevdg nahldnadvv aaadvaegtp
      121 laqvnmrqta snvvslpwvk satasrkwps tisvevvenv avayrdsseg thlidregke
      181 favdtppeda veltgeadad dtvrkdavdi aaalsdtgrg avksieaksk yefvlnlkde
      241 rtvvwgased nenkslalet vlqregrefn vtnpqlitvk
//
LOCUS       WP_284834390             594 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Corynebacterium appendicis].
ACCESSION   WP_284834390
VERSION     WP_284834390.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..594
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64382
     Region          1..594
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mttytvpagf evapdencys alvataeknp divlfsrpge fdwvdvtaad fvehvrkvak
       61 gligigvekg driallsgar yewavidfai maagattvai yptssldqiq wivedsgatl
      121 aigetkdhgv kfehladtel eqillfneda igyletaget vsdeileeri qsishddias
      181 lvytsgttgr skgcivthln wifqvrglqq hpigkiagpg tkmvtylpla hvmarsvhll
      241 atisgtlqth wsdvktiaae fqraqpdvvl gvprvyekvr naaavkasdg saigarifke
      301 aektaieysk aleedgpsis lklkrkifdk lvyskireal ggnvqygisg gsalgvplgh
      361 ffrgaglpvy egygltetas aaavnfgeda kigsvgkpms gysakttdeg eicfsgdgif
      421 vgywqnekas kealidgwfh tgdlgeiden gfititgrkk dilvtsggkn vapqpleeml
      481 rqdplisqav vvgdgkpfig vlialdedal vrwkeqrglg mptyklaklp elrgemqdai
      541 nrvnqsvska eqikkfrilp rdlteedgel tatlkvkrpv vldhfahqmr klyg
//
LOCUS       WP_284834499             272 aa            linear   BCT 25-DEC-2024
DEFINITION  inositol monophosphatase family protein [Corynebacterium
            appendicis].
ACCESSION   WP_284834499
VERSION     WP_284834499.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..272
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=28008
     Region          16..270
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 maavstaafi dshrsssdak laralvetag glalsmrdeg letgqktsvs dvvtnadtaa
       61 edfvagalea lrpddgivge egatkastsg rtwvidpvdg tynfasgsdy fcsalalveg
      121 nvhdpartla savhrpalat twvadngtat rndrtleqli daplphlala tylhptsmkd
      181 eairgawlda tnsaatvrmf gagsidlatv asggiggwlq hsvadwdwlp gkalveaagg
      241 kavkadaggv twciagnrql vnevlakleq hg
//
LOCUS       WP_284834568             103 aa            linear   BCT 25-DEC-2024
DEFINITION  antitoxin [Corynebacterium appendicis].
ACCESSION   WP_284834568
VERSION     WP_284834568.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..103
                     /product="antitoxin"
                     /calculated_mol_wt=11237
     Region          12..84
                     /region_name="VagC"
                     /note="Virulence-associated protein VagC (function
                     unknown) [Function unknown]; COG4456"
                     /db_xref="CDD:443554"
ORIGIN      
        1 mtkamrgkrl rttvfrsgns qavripaafr vesgsavieq vpeglllrpv eenfgdviar
       61 lrefqkehga deslidelad lpvdpvpeid rpaaknedgd rng
//
LOCUS       WP_284834588             376 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Corynebacterium appendicis].
ACCESSION   WP_284834588
VERSION     WP_284834588.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 376)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..376
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40287
     Region          24..326
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mstvvkrrgt aenaepakkn agprsdagka wglvtpaliv laivigypil raiwlsfqan
       61 rhldpstgvf vdggfagldn ylywiqnrcm tptgtvgecp pgvlatdfwp algitlfftv
      121 vtvsleavlg mvmalimnhp srvraliraa vlipwaipta vtaklwqfmf apngivnsll
      181 gqsiawttdp waarvaviia dvwkttpfva llilaglqmi pkdvyeaarv dgasawqtft
      241 ritlplvrpt lmvailfrtl dalrmydlpv imisgssnsp tatisqlvve dmrqnnfnsa
      301 salstlifll iftvafllvr fggadvggee trsrrekraa kkqakqqrgr ngsadgassa
      361 asdaaaaatt steaar
//
LOCUS       WP_284834623             361 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium appendicis].
ACCESSION   WP_284834623
VERSION     WP_284834623.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..361
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37807
     Region          48..355
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mttrvapetd yekdspdrai esyrrrgrrk aiaiallvlg aiasflvavv vgpielslsd
       61 vfravfspds vdqqtetvvr tlrlpaavma vlvgaslgls gaqmqtildn plaepftlgi
      121 saaaalgaav sivmgwtiil naqlnlalta alsalfavli iasaaiwrga saesmillgi
      181 alsfffqavl sllqyvasne alqqivfwtm gsmqraswta niviaivlal aipfcvvnsw
      241 rltalrlgdd raaalginvq rlrvttliva sllaaasvaf tgiigfiglv gphiarmivg
      301 edqkfflpga aaagamlmsl ayavslsiip gvaiplgiit slvgvpffvf liftrsrgrs
      361 a
//
LOCUS       WP_284834681             181 aa            linear   BCT 25-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Corynebacterium appendicis].
ACCESSION   WP_284834681
VERSION     WP_284834681.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..181
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20227
     Region          1..145
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mkigvivgsi rksrtaekva gwmkeniger egaeyefidl adfelplydg aglpmlmnkq
       61 ydndevtrws kaidacdafi fitpeynhsv paalknavdt lgpewvgkpi afvgyggvga
      121 iraiehwrqi aanfhmhdir eqlgfiqame mrdgfnpmph raqelaamcd rleeltsklr
      181 g
//
LOCUS       WP_284834696             228 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Corynebacterium appendicis].
ACCESSION   WP_284834696
VERSION     WP_284834696.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 228)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 228)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 228)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 228)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..228
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23337
     Region          20..222
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mqplidafay ltapshwtgs tgfgirileh lgyaglavla aamiavpagv avghsrrgak
       61 avvavagalr alpelgvltw laislprgis wpivpsvivl vllavaplla givagfdsve
      121 rdvvlsaraa gysesqilrd velplaapvm lgglrscvvq vlatatvvay iglgglgryl
      181 idglavqdya rmvagaivvt llalvvdlll agvqrwvtpk glnvkena
//
LOCUS       WP_284834989             523 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Corynebacterium appendicis].
ACCESSION   WP_284834989
VERSION     WP_284834989.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..523
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=54902
     Region          5..331
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(7..8,11..12,41,44,98..99,151)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(96,99,176..182,211,235..240,271,297..301,303)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mrvaavwfpd wpvqaarlda ddelqeplai gaqhrikvvs hraralgirr gmkvrhaqsv
       61 cpeltvvddn pdrdgrmfta laasfddvaa svevlrpglv vvdiavagtf hgseetaaem
      121 lidaaarrgi dafagvadei ataliaarss avvqpggsaa flasqplnvl laetslgadv
      181 etvkaldqlg vgtlgdlacl pstavstrfg ragmachria raapdrrvap elpaadlsva
      241 vtpedpidrv daaafaaral aaslherlae agqnclrlkv kaeladgtvv eriwrtreal
      301 teeatadrvr wqldgwltsg gagtitslvl eplelaqpes vghlwgrgag gsgagearra
      361 aervqsalgi davlqprfvg grgvaerial vpfgehdpes pdgadpasas wpgaippplp
      421 arigggvdhp aakitmidda arpvgvtaea llsttpyals wggshylitg wagpwpvdqg
      481 wwgehpqkva rlqvvgereg gggpvawlll wskrkwrvea mys
//
LOCUS       WP_284834850             268 aa            linear   BCT 25-DEC-2024
DEFINITION  trimeric intracellular cation channel family protein
            [Corynebacterium appendicis].
ACCESSION   WP_284834850
VERSION     WP_284834850.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..268
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=28520
     Region          6..196
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mndfgtfyyi leytgvllaa mvggsvaknm nfdvvgfgfi alisslaggl irdcllsngp
       61 aaalqtpwyl iiavigaaia ffieiegalw dqvrfyldvv tvgvwsvvga thaivndlpw
      121 isalllavit stggalvrdv vlgkvpalft sqkmhvfpsl lagamtlvfa hfevkawvgm
      181 lvssvaasvl smtvywvsts rahqptlter sldrriaael nmspddsvtn iadaiagakd
      241 kdvlnlirvy lhdevlerag tsptaasr
//
LOCUS       WP_284835220              79 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium
            appendicis].
ACCESSION   WP_284835220
VERSION     WP_284835220.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 79)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 79)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..79
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8164
     Region          10..70
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 msspstepqv ichldelmaa rgitgtalae kvgitpvnls vlknnrakav rfttlaaice
       61 aldcqpgdvf svrrpgada
//
LOCUS       WP_284835280             102 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium
            appendicis].
ACCESSION   WP_284835280
VERSION     WP_284835280.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10578545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..102
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11218
     Region          14..64
                     /region_name="HTH_17"
                     /note="Helix-turn-helix domain; pfam12728"
                     /db_xref="CDD:463684"
     Region          <58..98
                     /region_name="PRK13428"
                     /note="F0F1 ATP synthase subunit delta; Provisional"
                     /db_xref="CDD:184048"
ORIGIN      
        1 msekdtttav aprfytlqel tdlgvgsest lrkaikegrl sfhrfgtayr irqddldayl
       61 aaarrhapql fdgfvdavvd aapqltdeqr qqlvtvlggv kh
//
LOCUS       WP_284835129             247 aa            linear   BCT 25-DEC-2024
DEFINITION  O-methyltransferase [Corynebacterium appendicis].
ACCESSION   WP_284835129
VERSION     WP_284835129.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..247
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24436
     Region          89..247
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 msnsafssln eyiegkqqqg plidarsdas eyslptpsva vgellgtlaa tagsagapgs
       61 aaaasasgag asgaatagpa tgavaitpaa gvvglhilag lpakasltci dpeadhqara
      121 kaafrdagfg asrarflpsr pldvlgrlat gayhlvyadv dpvdlpavik aawpllspgg
      181 tlvlsgslld atitdptrkd rgtlaaread elveklaage aegfegesav atrlpldsgi
      241 tlvtrra
//
LOCUS       WP_284835298             304 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Corynebacterium appendicis].
ACCESSION   WP_284835298
VERSION     WP_284835298.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium appendicis
  ORGANISM  Corynebacterium appendicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426811
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Corynebacterium appendicis"
                     /db_xref="taxon:163202"
     Protein         1..304
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32953
     Region          26..304
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 msskprtqqp vspktialdg pfehvwlhtr girlhaavag dpsnplvvlv hgtfgawvdf
       61 qhviaplaah gfhvaavdmr gygmsdkppa ragdptriav gdiagsvtal ghdrahivgh
      121 dtggalawvf agaypertas lvsvsaahpg dmrahmrarp welmfmlvrv avgrlpiwlh
      181 qacaplvprv wrrelvlnta pgfagtpefd ealrlriraa ridnalrgiv rntrmltasr
      241 qtrtlidapt lllhprqsvw dridaravkr laipptvdtv pgsknvpqve npqgfvdkla
      301 affa
//
LOCUS       WP_284835378             690 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Corynebacterium
            sp. MSK185].
ACCESSION   WP_284835378
VERSION     WP_284835378.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK185
  ORGANISM  Corynebacterium sp. MSK185
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Corynebacterium sp. MSK185"
                     /db_xref="taxon:3377092"
     Protein         1..690
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73093
     Region          32..514
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mqfrrigqlv atttisaval sgvqavaqen kttisvtnit dihghledki gdpakagdei
       61 gvarlqslik qvnegqefnl tssgdnvggs afvsaisddk ytlealnqmg mkvsavgnhe
      121 fdkgtedlte riqpnstypi lganvlkdgk pllkpshved vdgvkvgyvg tvtentkykv
      181 saakipgvtf tdpvkatnee aarlkesgea dvvvalfhed aqeyaegfnk dvdvlfggdt
      241 hqrtkgevpr dgalplqwaq gheygkllnd vditfdksak kvtdiklsqy datdaaavep
      301 dagiaavvek aqkeaevegs ktagtvkqdl frgsdegaea gsnrgvestl nnfiadgqry
      361 amskqvgkdi eigvmnaggv radlkggdvt ykdifevqpf gnsvitakis geefinalen
      421 qwqegsrprl amglsnnvqv vydqkankge rvksvtinge qidpkkdysi alssflassd
      481 eeaggdgyfn agsikdkndv gymdtqamid yiksgesevr tgqgqigahv egevkpgkei
      541 tvnlsslnys tegepmakka tvklgdaeqt vdidnaaqeg daqfgergra tvkltvpenl
      601 sgkqnleitt dagtkatlpi evsgegsqep gakpepkgss lssngssmgs avfaivaalv
      661 agvavvgmnp qilpaparkm iedlrkqfhl
//
LOCUS       WP_284835511             372 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase family protein [Corynebacterium].
ACCESSION   WP_284835511
VERSION     WP_284835511.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..372
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41262
     Region          9..356
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mqpqasvksv pqhlpeldgl ravaslgiiv thvsfqtgtg wgfagrfdff vavffalsaf
       61 llwrrrglhs lagyarsrva rllpayyacv vavmlllpda hsltltqlls nltstqiyvv
      121 dglapglthl wslcvefffy lflpvlvwll gtlprrwria aiavagvlsw awgfvpfvad
      181 yakdqvnsqi wppayaswfa vgmlaaefee agisrrvqrv lrprwawwiv aavvlwvasr
      241 ewfgpqglih pepaefsrri magaafaavv vvpvalapre kswltsplmq algtwsysif
      301 lwhvailgla fpltgvplfs gkpldfwvil tvtvvgtvvv saasytlier pgrdlllgrr
      361 rkdrprprht ss
//
LOCUS       WP_284835528             232 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: CPBP family intramembrane glutamic endopeptidase
            [Corynebacterium].
ACCESSION   WP_284835528
VERSION     WP_284835528.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..232
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=25321
     Region          135..224
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mtkslraell ivltltfgis gvravlnlin sfaspqrlne qsvtlnssqs slawvdmglq
       61 lcsaavlcsy galalfllak dhifprayra rdwlegagla aligipglal yftavhfgws
      121 kevipgdfan awvhipvslf kaaanafaee tvvvmwfmtr lrqarwslpt ilaassilrg
      181 syhlyqgvsa gcgniimglv ygyyyhrtgr vwplviahfl idavafvgys fl
//
LOCUS       WP_284835604              76 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium sp.
            MSK185].
ACCESSION   WP_284835604
VERSION     WP_284835604.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK185
  ORGANISM  Corynebacterium sp. MSK185
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Corynebacterium sp. MSK185"
                     /db_xref="taxon:3377092"
     Protein         1..76
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8386
     Region          9..73
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mttnrtfsyk plwkllidrd mnktqlqera gispatlskl grggnvttdv lsricealdc
       61 diidicevvk deesaq
//
LOCUS       WP_284835612             458 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Corynebacterium].
ACCESSION   WP_284835612
VERSION     WP_284835612.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..458
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48371
     Region          97..397
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mhtlrsigss vagiaiaagv lsapiasave pakiqgdatp stirevnltd sadpeninya
       61 ittegenrvv diaglkdkdk wkgyafghks aqgnhygnhv kvmtatsaam ggrevplavi
      121 spdgnfekkr ptlyllngag gaeqgmdwit atakrdvnpe qegvqdmvdf ytskdvnvvi
      181 pqagafsyyt dwvstpdagy lkgpqkwetf ltkelpgale dhiggngkrg iagmsmaats
      241 slllaehnpg fynavgsfsg caatsrplpr lytqltvnrg ggsadqmwga mgseynvynd
      301 alvnatpknl gpsetyvsvn sglggandwg akgsstlive ggvieaamss cthdlkakmd
      361 sqgmkadwnf rntgthswpg wrddifsswk tfergfnkda aeapaepevk pnelsidapq
      421 aqenaqikdv psaadqspdk dfvegkeaea peaagaae
//
LOCUS       WP_284835637             187 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Corynebacterium sp.
            MSK185].
ACCESSION   WP_284835637
VERSION     WP_284835637.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK185
  ORGANISM  Corynebacterium sp. MSK185
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Corynebacterium sp. MSK185"
                     /db_xref="taxon:3377092"
     Protein         1..187
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19524
     Region          55..187
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mknyvlgtvi aailiaviav vgvsqlrggd eveeavptea apqevpqrpd cpagtvagve
       61 ldclggkatg kradegvsvi nvwawwcepc raelpylqkv aethpdwqvv gvhadknagn
      121 gaaflndvgv dlpsfqdadn kfagqlslpg vvpvtvvlkd gevrkqfaqp fssaaeiera
      181 vkeaiaa
//
LOCUS       WP_284835643             256 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: energy-coupling factor transporter transmembrane
            component T family protein [Corynebacterium].
ACCESSION   WP_284835643
VERSION     WP_284835643.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..256
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27717
     Region          1..244
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(17..18,20..21,24..25,62,67..68,71..72,102,106,113,
                     116..117,122,138,142..143,145..147,149..150,153..154,
                     157..158,178..179,181..183,185..187,189..190,192..193,197,
                     200..201,211,213)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(141,145,148..149,151..152,192,195..196,198..203,206,
                     211..212,216,218)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(162..169,180,183..184,187)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mpnllrganp ltrvfmmfiw vtpilasidw vsaavslvlt lifaplcgvs warvfkagwf
       61 lflvapisgi smllygepsg teyfhwglih vtenslslai aitlrvfava lpmvvlardi
      121 dptelgdals qilklpsrfv igavagvrmm tlfqsdwqsl gmarrarglt dvgklkhllt
      181 msfgllvial rrggklatam eargfgrtpp gggartwarp srlhardgwi malgtvlafv
      241 pvvvsvltga wrffgl
//
LOCUS       WP_284835660             189 aa            linear   BCT 25-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Corynebacterium sp.
            MSK185].
ACCESSION   WP_284835660
VERSION     WP_284835660.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK185
  ORGANISM  Corynebacterium sp. MSK185
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Corynebacterium sp. MSK185"
                     /db_xref="taxon:3377092"
     Protein         1..189
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20321
     Region          2..122
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mqrhravdia evarasgrll degglkaltm ravaqqvgva paslysrves vddlfdlald
       61 vvladdplms esinnadlpa lmqaffthlt thrwagqvig mraprgpayl alsermcvll
      121 eregvpdplg tayrlsnlvi gaaltapmap dekrvainpe qaptyarlha ahhispqeil
      181 segikklls
//
LOCUS       WP_284835683             392 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [Corynebacterium].
ACCESSION   WP_284835683
VERSION     WP_284835683.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..392
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42739
     Region          156..389
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mstdtvaear lgdkiltava vlialfyvis aaknpsiiei iqaglsllfl pfmwvwrsrp
       61 vlsatgfivl laawamawms qlptnlgitp waltapmavy atsryvtrra iprtvlalti
      121 lgsfispfmw ridpesfflh yqldrrylam lvvhwavlgs tyfiaaryfd larqrerlah
      181 erfrqaqeee rlliarelhd vlahsltlik vqanagiiaa ranteaahda lasirdgads
      241 aleevrgivt alrstgptsl epttqlehie giidgfraag ldinahipea yeapaltqla
      301 lvriiseglt nalrhqgpgt qvdvelalad varltlisst psptpsevpg sgvgligvee
      361 ranalggkle swgdatkftl laelplqren rv
//
LOCUS       WP_284835878             406 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium sp. MSK185].
ACCESSION   WP_284835878
VERSION     WP_284835878.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK185
  ORGANISM  Corynebacterium sp. MSK185
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Corynebacterium sp. MSK185"
                     /db_xref="taxon:3377092"
     Protein         1..406
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=43970
     Region          172..401
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mirtkwstag ivaacavanw ligvvlmsmd ieeyspsfee ygpyictgfa vgvvtiialp
       61 falehqprel sdvdysdstr sfiagcivll gsssyfgaas gvvafismvs rrstsrsvaa
      121 vacfvaafai daffnpymaw ddigwvgaif vvvvivagll vgqkranlre krwrveqqar
      181 mnreemrakv erarreeren iardmhdtls hrlslvaiha galsypregv paeftdaart
      241 iraeaqnave dlrtvlsalr edlsqdprtt leelvasaqe agtqvtvtya dgaspdvftg
      301 lstmaqhavh ravqegltna rkhaagqpvs itvrevagev gvemrnplpv akaeeragsg
      361 vggyglvglr ervelsggrm nvhvgeegee fgwsirlpla rqeatq
//
LOCUS       WP_284835978             327 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium sp. MSK185].
ACCESSION   WP_284835978
VERSION     WP_284835978.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK185
  ORGANISM  Corynebacterium sp. MSK185
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Corynebacterium sp. MSK185"
                     /db_xref="taxon:3377092"
     Protein         1..327
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32895
     Region          24..319
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mrhkrivgvl vglilalils avigmgvgav mkspgevttg fftgdpliwk yraprilvgi
       61 cagsamavsg cilqsalrnp laapdtvgit sggglaavav lmgagalpah lltfiafiga
      121 lagtglvlll agrgasdpvr lpltgvavsf glgaitelll vraapeagaa mtwlkgslya
      181 rslgdativa pfillaltaa mvvakhldml alddstmagi gvnakmwrli aialavilga
      241 agvaaagvlg faglivphaa rlmvgsnlrr qmpvaalgga tlvtvcdtfg rwafapteip
      301 vgalialiga pyfiflltrl trvrngg
//
LOCUS       WP_284836081             847 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Corynebacterium sp. MSK185].
ACCESSION   WP_284836081
VERSION     WP_284836081.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK185
  ORGANISM  Corynebacterium sp. MSK185
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 847)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 847)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 847)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 847)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 847)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 847)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Corynebacterium sp. MSK185"
                     /db_xref="taxon:3377092"
     Protein         1..847
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88858
     Region          9..847
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 margnamrrv slrnivahkl rlgltilavv lgtafiagsf mftnslkstf dsavdnefrg
       61 vdavvsqkdd ngakldeklr qkladdedvk niniadsetv vaanenseay qtqggtasvv
      121 pfypedkvvg gadklkegee psgkdevlvn ssaadkygis vgqklivvhp deqdtvtvsg
      181 isepavdqgd sivlsmaekd ylerygdpsq lkvsaaegvd analvdhlnd kydvkaesge
      241 rlaeetsemm ssalkfinyf liafgliall vgtfiiantf smivaqrtke fallralgas
      301 rrqitnsvvv esaivgllgs ivgvvagmgl vaiikavmsa kgmpfdgglg lsvsaivvpi
      361 ilgtivtvvs awaparragr vqpveamrtt esasatslkv rtifgaiill vgivaalagv
      421 lsdgetnvra vlvgvgafgi ivgfflagpa lslplvptvg kvigapfgai gslaatnsrr
      481 nprrtaataf altlgvalvt aigmlgatmk ssvadtveqn itsdyllsgp ssgefptpkd
      541 tgkraaeaeg vdkaitigma pvtvdgqasm dygpqfqqtt tadgdpssmi aldmvegdan
      601 ldkgfiated fakehgwkvg etykvasaek dkkaeaklvg ifkstdvvqn mvlsqevaek
      661 vapeksftvq mvgvlgqegy dkeelrhnle davkdlvvvq vnsgeeyagq aagfidqmls
      721 ilygllalav iiavlgivnt ltlgvierrq eigmlravgt qrrqirtmit lesvqialfg
      781 avmgiliglg lgwsfikilg degldsaqip wamvlimlvg salvgiiaav wpshraaktp
      841 pleaiad
//
LOCUS       WP_284836092             454 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: PP2C family protein-serine/threonine phosphatase
            [Corynebacterium].
ACCESSION   WP_284836092
VERSION     WP_284836092.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..454
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=48410
     Region          5..242
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mtlklnffak sdrglirdnn edsgyagphl liladgmggh aagevaselm vnhleildqd
       61 pgqedtkall eaaadqanea isdhvkahpe tegmgttltt mlfngtdfgv chvgdsrgyl
      121 lrdgkleqit kddtyvqslv dkgeldpgdv sshpqkslil kaytgrpvea tlftldakpg
      181 drillcsdgl sdpvtastie talgqgsieq agstlvdlai rsggpdnvtv vigevteesp
      241 qehkpfrvga lagptedpth pdssasraaq lsrkpqvipp avmadaeder peptedeaee
      301 etsgrktgwk vllallivla lvigaglwak nflsnnyyva tneaqeitiq qgadysvfgk
      361 elhstnqyvc indsnsllfs gepckgdfap lkvtdlpese rsavdhlstg dlgevqqqvn
      421 dlgdkalkpc itapsqkdkk dakknkpgvt crev
//
LOCUS       WP_284836161             375 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium marquesiae].
ACCESSION   WP_284836161
VERSION     WP_284836161.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..375
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=40105
     Region          18..374
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mtdtqtfsad vyaqrlhaaq kaaadkgidl lligtgpdfa yltgswvssh erltvlvvpq
       61 rgtawiaapn tditdikaap vgeldvelrg wndgedpykl alhgagdglg kvalgqslta
      121 dhvlrfqdll prasyelaty alaelftrkd eaeiaelrka graidavhaq vpqllqagrt
      181 evevahelek lilrehsvid fvivgsgpng anphhsfsdr vlaegepvvv diggtlpsgy
      241 hsdctrtyvv ggdiskapqd fqdayavlad aqaagrtaah pgstaadida ivrqaisaag
      301 wgdyfvhrtg hgiglsthee pfimegnala leegmafsie pgiyledkwg mrledivvlt
      361 ndgyeslnla prdvr
//
LOCUS       WP_284836163             328 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            marquesiae].
ACCESSION   WP_284836163
VERSION     WP_284836163.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..328
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35340
     Region          13..323
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 maahnpapkr hdeaverltn lsfalqgaan sggspdrtaa wirshvagyg dksdeafaks
       61 lardiatlqr agvpivhsgg edgaryrlda ssyqlppvef steeamvlgi aggvgttggl
      121 sdfslsgwtk iaasgasrnl agapvytavn ditrlapeii tsvlaavrnq vritfsyran
      181 patepvrrvm dpwgvvnrds riylvgfdvd rneprvfral rvsdikrshd paehpnpten
      241 lqvlvervlq rgekvdarlv ipdgqarelm dageqqsdgt vllhkvdkdw lvrtaagyap
      301 evqvlepagi rqevisllhk asqsqeeg
//
LOCUS       WP_284836219             690 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Corynebacterium
            marquesiae].
ACCESSION   WP_284836219
VERSION     WP_284836219.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..690
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=72813
     Region          32..514
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mqfrrigqlv aattvsaval sgaqavaqen kttisvtnit dihghledki gdpakagdei
       61 gvarlqtlik qvnegqefnl tssgdnvggs afvsaisddk ytlealnemg mkvtavgnhe
      121 fdkgtedltg riadssdypi lganvfkdgk plleashvee idgvkvgyvg tvtentkykv
      181 saakipgitf tnpaeatnke atrlkesgea dvvvalmhed aqgfaedfnk dvdvafggdt
      241 hvatkgeier egalplqwaq gheygkllnd vditfdktak kitdislkqy dataaakvep
      301 daeiaaivkk aqqeadiega ktagtveral frgsdenads gsnrgvestl nnfiadgqry
      361 amskqvgedi eigvmnaggv radlkggdvt ykdifevqpf gnsvitakis geefiqalen
      421 qwqegsrprl amglsnnvqv vydqkadkge rvqsvtinge qidpkkdysi alssflassd
      481 eeaggdgyfn agsikdkndv gymdtqamid yiksgesevr tgqgqigani egdvksgeei
      541 tvnlsslnys tdgepmakka tvklgdaeqt vdidnaaqeg daqfgergra tvkltvpenl
      601 sgtqnleitt dagtkatlpl evsgegseep gakpapkgss lssngssvgg avfaivaalv
      661 agvavvgmnp qilpaparkm iedlrkqfhi
//
LOCUS       WP_284836317             466 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Corynebacterium
            marquesiae].
ACCESSION   WP_284836317
VERSION     WP_284836317.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..466
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=51166
     Region          21..397
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mtatsqqrpr sksfgdrvre lrerarqeag ldyqllrfii fflvgigvlm vfsssmatsl
       61 tedggvwnqa lrqcvmvflg lvafwfglkv sphtlrkcvp wivglsiill iavlipgvgt
      121 greevgsqsw iylgpfslqp selarvavgm fgatvladke hksmkvtdpf mmysliagvm
      181 fllivfqgdl gmalsfalvv vftlifagvd wrvpatigva avcgllfifl sggfrsnrfh
      241 tyfdalvgni sdtqgtgfqs yqgflsladg gfwgvgigqs rakwfylpea kndfifaivg
      301 eelgwwggal vivlfaalgy vglrtamraq nqfqsllaat ltigvvtqaf vnigyvigll
      361 pvtgiqlpmi saggtaaiit igsmgilcnv arhepmqisa mqnfgrplfd rllfigepqp
      421 vpqpkkkqqg rharpqeprf rvreerfgrp vtgsgrrypr aerryr
//
LOCUS       WP_284836532             516 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Corynebacterium marquesiae].
ACCESSION   WP_284836532
VERSION     WP_284836532.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..516
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56896
     Region          10..487
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mpysnsrpsf nrrnflqiag vsaaavaagi sapakagaqs slsswgssqg gelpqdself
       61 glgvaagtpr hdsmilwtrl apeplaedgh ggmtggdvrv gwevakderf gdvvkqgeal
      121 aqrelahsvh pqvtglepat eyfyrfrvdg kvspvgrfkt lpapgakvdn ftftvascqa
      181 wyhgyftpwk hiaqepdldm tifvgdyiye ygivegdnlw rqgasvpnvf katvetleqy
      241 rlryslfksd khlqaahara amaivwddhe vennyagsws eigttaehfl yqraaayraf
      301 yenlpvappa lpegpnnriy dsfdvgtlmr fnlvdtrqyr eesaedasil gaeqeqwlnd
      361 klatspaqwn vvvnsvvvvp iadstdqwdg fpaarrrlie slskvsdpiv ftgdihqhca
      421 aeiqsesgqp vgvelvatsi asdgdgfags kstewlekpy vkamdkrrgy ikvrasrehl
      481 dsefvvvpwi erddtapret afsfrtnage htlrsl
//
LOCUS       WP_284836553             486 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA carboxylase subunit beta [Corynebacterium marquesiae].
ACCESSION   WP_284836553
VERSION     WP_284836553.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..486
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51178
     Region          6..484
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mtdlkttagk iedldaklae sraplgegep aartrvtqll degsfvetda larhrstdfg
       61 rehdrpytdg vvtgygsidg rrvcvfsqdg eifdgtmgev yaekltkvyd laiktgvpii
      121 giyestgprv qegivtmagy arlmarvsqa sglipqisvv agntsgiaaf aptfadvlvv
      181 tqgtalhqaa shvagaepet fggaaahaes gtahlvasdd kqalslvrdv laylpannra
      241 eaprveagsv adfdlnavip dtaaqaydms dviqavvdeg sffelsaeaa qniltgfayi
      301 dgravgivan qplalagald saaaekaarf vrtcdafnap ivefvdspgf vptpeeekag
      361 llrraskfay aqaeasvgkl tvitrkaigp ayvfmgakdl gadlvyawpt aeiavtqasq
      421 aslaiygsed keeemdelfl hpyaaaergl adnvieptat rhylveglrl lerkavaqvp
      481 kkhgtv
//
LOCUS       WP_284836613             296 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [Corynebacterium].
ACCESSION   WP_284836613
VERSION     WP_284836613.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 296)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..296
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31713
     Region          1..275
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
ORIGIN      
        1 mddnfiprip igdwtndgid wltdnatwlf dafsavmefl vegfsealts vpvlvmlgif
       61 vliawffrsw slaigsllgf vlvigmrqwe tmletmslvl vstltavvia iplgiwaaks
      121 htvsaivrpi mdfmqtmpaf vylipavtff sigvvpgvfs tiifalppgv rmtelgirqv
      181 deetveagrs ygassgqilr giqlplaipt imaginqvim lslsmaviag mvgadglgke
      241 vtsaistldv aqgveaglav vilavfldrl taalgnpshy pssllsllrk kkqhqa
//
LOCUS       WP_284836619             294 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Corynebacterium marquesiae].
ACCESSION   WP_284836619
VERSION     WP_284836619.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..294
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30652
     Region          5..282
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(34,231,234)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(181,202,229,232..233,236)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mtihvcgegl vdlvpvapgs lndhtpalgg gpfnvaiaaa rlgadvefqs ristdgfgqe
       61 lvarlkaegv ttthlqrgde pttlavttih edgsasynfy iegtadrlve prlvpadiac
      121 fgtvslalep gasryaqllk dfaaqgtlva ldpnirpfya tpehraflan llphvtllkl
      181 sdeevdflgp dlisqvpvvi vtrggeglsv qagetklnvp aaqvpvtdti gagdtimaal
      241 ltqidergld ssalaqlgaa ewkellsfaa aaagitvsrk ganpprreev essl
//
LOCUS       WP_284836630             256 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium marquesiae].
ACCESSION   WP_284836630
VERSION     WP_284836630.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..256
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27622
     Region          1..244
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(17..18,20..21,24..25,63,67..68,71..72,102,106,113,
                     116..117,122,138,142..143,145..147,149..150,153..154,
                     157..158,178..179,181..183,185..187,189..190,192..193,197,
                     200..201,211,213)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(141,145,148..149,151..152,192,195..196,198..203,206,
                     211..212,216,218)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(162..169,180,183..184,187)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mpnllrganp lsriflmfiw vtpllasidw vsaavsltlt lilaplcgvs wgqllkggwf
       61 lfliapisgi smllygepgg teyfswwlia vtqnsltlai aitlrvfava lpmvvlardi
      121 dptelgdals qilklpsrfv igavagvrmm tlfqsdwqsl gmarrarglt dvgklkhllt
      181 msfgllvial rrggklatam eargfgrtpp gggartware srlrardgwi malgavlafv
      241 pvvvsvltga wrffgl
//
LOCUS       WP_284836671             444 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF445 domain-containing protein [Corynebacterium marquesiae].
ACCESSION   WP_284836671
VERSION     WP_284836671.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..444
                     /product="DUF445 domain-containing protein"
                     /calculated_mol_wt=48979
     Region          34..443
                     /region_name="YjiN"
                     /note="Uncharacterized membrane-anchored protein YjiN,
                     DUF445 family [Function unknown]; COG2733"
                     /db_xref="CDD:442039"
ORIGIN      
        1 mthraeegle tatvtassga apvpqagnqe arradlrrwk aialsfliga aviflgcsww
       61 qasesgaplw vgyvraaaea gmvggladwf avtalfrrpm glpiphtali pnnkdrvgda
      121 lkdfveenfl tadalsakvr eaelplwlar qgvepgkaee vsawigeraa svvadldpee
      181 aehfirtqvm drlaepewgp plgrllegyi adgkarpled dliewvhgki lnmeptvvta
      241 idermpgwap rfaremvgek vytelvefad evrrngnhea rlairrnlsk lasdlqwded
      301 mrgriegikq emlasdqaqq apaamwrtvs ttlidqlndp esflrqkita kvkelahrll
      361 edseflaqan alvdkaarya vekfapeiia iipetikrwd aeeasqniel mvgkdlqfir
      421 lngtivgsla glvifainhl ifga
//
LOCUS       WP_284836702             526 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Corynebacterium marquesiae].
ACCESSION   WP_284836702
VERSION     WP_284836702.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 526)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 526)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..526
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56903
     Region          15..502
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mdvllvligl mlltvfvvai gdkiglpwpa lltiitacav fvpglpqfep ptelilpifl
       61 ppllwalarr tswgvireqw vtilslsvll vvattlavgf tayaflpgis laaailigaa
      121 iappdpvavd avaepagipr riittlqteg lfndaasiva fnlaltavtq gdelsfgggv
      181 lnffysafva gglgwvvgrl valfithvhd vtarnaltwv tpfavylise elgasgviav
      241 viaavelnsr adiqaedrls gqafwetiel lftgvafgli gltvntaige vgsdlwhsvv
      301 vgvilslvaf vvrlvwmyiy yrinvsrgrp rvaplrlqev llmtwsgmrg lvtlalvlsi
      361 pagvfsfhhe lavialtvll vtmvvpglll pwlmerldlt easqiasdkm raavvarara
      421 asiealshfr pdghitadae kvdpeisanv iqwfedrlgd gedvsddsrw qrawqarhvv
      481 learrtalaa aqeellrmrg yraynpaivd evleeidrmv lgtkrh
//
LOCUS       WP_284836712             120 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: YidH family protein [Corynebacterium].
ACCESSION   WP_284836712
VERSION     WP_284836712.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..120
                     /product="YidH family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=12929
     Region          3..100
                     /region_name="YidH"
                     /note="Uncharacterized membrane protein YidH, DUF202
                     family [Function unknown]; COG2149"
                     /db_xref="CDD:441752"
ORIGIN      
        1 msdsrfprsv favgtdpdpr ftlanertfl awirtslali aggvaleafd vplptalrsa
       61 vsvfmlvvai ilpvvawvhw krseramree rplpfsfaip vlvvaivvva galvvgeflg
//
LOCUS       WP_284836713             127 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium marquesiae].
ACCESSION   WP_284836713
VERSION     WP_284836713.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 127)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..127
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=13470
     Region          2..124
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 mievaavvfr nslghvltvr kdsstkfqlp ggkleagetp aqaaarevae eigvdvrlpe
       61 lsllgifdap aanepgetvr ghiftyprpi lahaaaeiae aawvaptnpd relahllrde
      121 vfpales
//
LOCUS       WP_284836727             386 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium marquesiae].
ACCESSION   WP_284836727
VERSION     WP_284836727.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..386
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=42459
     Region          23..370
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 msnqfqvdpg lgasvqpqas vksvpqhlpe ldglravasl giivthvsfq tgtgwgfagr
       61 fdffvavffa lsafllwrrr dlhtlsgyar srvarllpay yacvvtvmll lpdahslslt
      121 qllsnltstq iyvvdglapg lthlwslcve fffylalpll awllgalprr wrvaaivlgg
      181 mlswawgfvp fvadyakdqv nsqiwppaya swfavgmlaa eceeigvspr vqrvlrarwa
      241 wwlvaavvlw issrewfgpq glvhpepgef srriiagaaf aavvvtpval apwdkswltg
      301 plmqalgaws ysiflwhvai lalafpltgv plfsgkpldf wvilavtvvg tvvvsaasyt
      361 lierpgrdll lgrrrkgrpr prhtss
//
LOCUS       WP_284836771             380 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium marquesiae].
ACCESSION   WP_284836771
VERSION     WP_284836771.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..380
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40862
     Region          82..363
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
ORIGIN      
        1 mmkkhltacl taaavmaapv avsgtltvga gaqeapapaa dqkpdvlgrp tvsdkqvsde
       61 egyfdsahge gvkiyyrkqk vanprgavvl ahgvsehsgr ydyvakrlld agynvyrvdh
      121 rghgksaggs vplghidnfq yilddfdhvv dmakednqgv ktfllghsmg sltveaygir
      181 epgkvdgiit ngggaplnls gknvagknit pedisetqkk ldptiferlp laqltsfnah
      241 yaqnliphrt eigaqspews kdikfsnpft dgistnqavk deyassplia qktsagtalq
      301 laaianydav nadlftaptl imhgtkdgiv ppyfsqdwyn sissedveyv twegqkhevf
      361 nepaadqald tvvdwldrha
//
LOCUS       WP_284836832             120 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium
            marquesiae].
ACCESSION   WP_284836832
VERSION     WP_284836832.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..120
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13210
     Region          1..83
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mnkfgkvtar llnderlhkg vtqaelaeat gisqsqiskq mrgtrdinid elgaiadald
       61 islvelirka eqeinpdtrn eleerrrkar mstpsdsmpe gavaysgpde daerndvddd
//
LOCUS       WP_284836862             610 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Corynebacterium marquesiae].
ACCESSION   WP_284836862
VERSION     WP_284836862.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..610
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66531
     Region          13..610
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mtlqevhtpa qftiepgetc ltalmdtakk rpngvmftrp anyewvnvtg kefidevfev
       61 aqglialgvq qgdrvalisa tryewslldf aiwaagaasv pvypsssasq vrwiiedsga
      121 vlaitetreh selvenlvlq edgepnlkgs psqlrrvlei nssaidtlkf egrgvaaeev
      181 yarikatstd dlaslvytsg ttgrpkgcil thrnwlaqtr glctnpigif avpgshtltf
      241 lplahvfara vsiavamrga sqnhwsdfst isiefarsrp nvilgvprvf ekvrnsaaak
      301 aadsgiktll feqsekiaie yskaldkpeg pdrllkakhk vfdklvysti rngvggnvsy
      361 citggsamgh dllhwyrgig ipvyegyglt evaaaaavdf vdqsigtvgp pmggvtfrin
      421 degeicikgd ivfhgywnnp eataealedg wyntgdlgei dedgklvitg rkkdlivtag
      481 gknvspgpme dilrghplis qamvvgdgkp fvgalltldp dilkrwkldh nipenrsmre
      541 latdptlrae lqdainqvna tvshaegikk fyilesdlte eeneltptmk vkrnvvsqry
      601 aesiehlykr
//
LOCUS       WP_284836875             405 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium marquesiae].
ACCESSION   WP_284836875
VERSION     WP_284836875.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..405
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=44361
     Region          169..403
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mklfrksdam lqrplwqklv iaavavigdf mvvaarfset dgssgrlfil fgvmigtwil
       61 lpfalrhaar erdprstqpg prsalvaati isatvtiaef rpsvfiaafs aasrrsrlwm
      121 alvctamvls elvdfdisrs eglsapgklg ffsgiilpav vvlvvglvrs nqkertialq
      181 aqaeltheem ttrenfarqe erdriardmh dtlshrlsmi avyagglayr kdldpeetrq
      241 sartirdeae aavgdlreal hslrsegrid pregveslve rsrragmdve vryqegagpq
      301 sleelstmag halnravqeg ltnarkhapg epvtititia tladalsitm snpvtraekk
      361 ssmhsggygi vgmrerasvv ggslqvnnee grfswtlrlp rkevq
//
LOCUS       WP_284836906             432 aa            linear   BCT 25-DEC-2024
DEFINITION  inorganic phosphate transporter [Corynebacterium marquesiae].
ACCESSION   WP_284836906
VERSION     WP_284836906.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..432
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=43878
     Region          3..344
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 mtatliilgi vvvtalafdf tngfhdtana matsiatgal kpftavaisa alnlvgafls
       61 vnvaatvakg ivnldsydls gaaadtdgqa llmvvftgli ggiiwnlftw llgmpssssh
      121 alfggligaa faamgsagve wssivgkiii pavaspiiaa lvsacatfli ywvtntipnk
      181 aknehfrhgq ivtaclvsla hgagdaqktm gviflalvas ghavadarip twvivscava
      241 iaagtlsggw rvirtlgkgl veiespqgma aeatsaaiil tsatggmals tthvstgsil
      301 gtglgrrgae vrwgvamrmv sawlitlpca afvgfatwwl ahgvssftnv atgaivdfvl
      361 llamaalivi rsrmnpvdas nvnndwepns esvdssmgag sdrkepvaag aapvsatnae
      421 dasapstvqe er
//
LOCUS       WP_284836949             664 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            marquesiae].
ACCESSION   WP_284836949
VERSION     WP_284836949.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..664
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=72016
     Region          1..60
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mtatltladv arltgvtrpa vnewiqrfns esitpfpspy gehdghpyya iteiqdwlra
       61 tklghrdtav edalfyssly rmllrnpara alglldcnta lspqdfspsa tvidsltaay
      121 qraadnipsd dpeadiaqaa dqvaeaafgp aaalarladd lsaqrqitls srftsramqa
      181 vsealtlenp tppiiptdey slgfvtglar eleetlalni gyrkdcapgs lywaelacrn
      241 vefidaseki panslivhaa psplknapey fehlqdlldn ldergamfci stadmlieds
      301 laqvvrrsfl aptetgaiap lrysarlprg ifpyrgqkqg alwilkrpnr kaignpadaa
      361 aviadvpdlk tpglvsdwat mlttpdeark htfirgrilr aadawrsrth slddsvfsst
      421 stssaanlmh tahqagldis sagledaqpk igmraesgat rleylpwkaa tnartgvlqk
      481 lsgsriaerd lapeavakle ligepeilgs ipqgarcidr lrlediaprg tltepgdvvf
      541 iksprprali deeggklvta paqalrcrtf rgrsktplek vcipylvaka ineatssels
      601 slyfpvfprg nakhlgsveh qlrarrqqll eqlhsldele hglvmsigtg avtiaesraq
      661 sppg
//
LOCUS       WP_284836878             415 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium marquesiae].
ACCESSION   WP_284836878
VERSION     WP_284836878.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..415
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=44612
     Region          143..411
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mvrtkwstag ivaacavanw ligmvlmnld ieeyspsfae ygpyictgfa vgvlgiialp
       61 falehqprel sdvdyagstr sfiagcivll gsssyfgaas glvafismvs rrstsrsvaa
      121 vacfvaafai dtifnpymsw deigwvgaif vvvvmvagll vgqkranlre krwrveqqar
      181 mnreemrakv erarqeeres iardmhdtls hrlslvaiha galsypregv pveftdaart
      241 irteaqnave dlrtvlsalr edlsqdprsg leelvaaare agtevtvtya dgagpdvftg
      301 lstmaqhavh ravqegltna rkhalgqpvs itvretsgav diemrnpvpr etpgaatgng
      361 adtsggyglv glrervelsg grmsiaanqe spegkegeef gwsiqlplah keaaq
//
LOCUS       WP_284836953             337 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium marquesiae].
ACCESSION   WP_284836953
VERSION     WP_284836953.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..337
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36509
     Region          55..328
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mtasikgrvl svimavaval glavvagsqp aeaanrdwlr rdatgtcewd kvgwwvqrcd
       61 vwsqamgrti pvqvqpakrg gnaalylldg lratertnaw vndvnaakty ephnitlamp
      121 vggaasfyad wqgpatydle npvnykwetf ltselpgyle rnfgvarnnn siaglsmgag
      181 aaltlaakhp nqfrqalsys gfltttvpga qtmmrfamld aggfninamy gslfnpkrfq
      241 ndplllipkl rntnlyisaa sgvpgagdsh ylpehqaaga alefgsnitt rvwegaarlq
      301 glnptvsypa qglhnweqfg yqlnrskpqv lnvmnaw
//
LOCUS       WP_284836986             400 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium marquesiae].
ACCESSION   WP_284836986
VERSION     WP_284836986.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..400
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43135
     Region          141..380
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 msfllnlpla dpingvifya ilaiagiiil lqrkvwplvi aallcviawy flrhwqvpwy
       61 iflaafipaa avvrkpkivt vtagifslla mvgivnmeyq typdiasldp rpvakemnye
      121 efshtksgaa ivhvdlpgtt shfsarqata yippaywtdh tlpvivllhg npggpeqwfg
      181 sgeaaetadq fqaanggrsp ivvavdatgs etanpicads sqarvmtyls qdvpqaikqk
      241 fkvnpdqrtw tvgglsyggt cslqiatnrp eaygsiidis geaeptignh aatvkkffag
      301 desafndqdp shllahkrys aqaifiagdk dtasvnalrs lsdaarnagm ktyfgtrpgg
      361 hsfqvwrpal resfawaarr ggmtaikdpf dgigandvrs
//
LOCUS       WP_284836987             769 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional lysylphosphatidylglycerol flippase/synthetase MprF
            [Corynebacterium marquesiae].
ACCESSION   WP_284836987
VERSION     WP_284836987.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458459
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..769
                     /product="bifunctional lysylphosphatidylglycerol
                     flippase/synthetase MprF"
                     /calculated_mol_wt=84557
     Region          242..755
                     /region_name="MprF2"
                     /note="Lysylphosphatidylglycerol synthetase MprF,
                     lysyl-tRNA-binding C-terminal domain [Lipid transport and
                     metabolism]; COG2898"
                     /db_xref="CDD:442143"
ORIGIN      
        1 msvlktiltr fpvslsilvi mwalhlvdfp tshwlaltta hpggaiilsa livlwlvpae
       61 wrlgslrtla vgvvsqlisv plsivlargi etvglnrwgn dllsdtfltp igfiagaagf
      121 asallprlwr rrlrvslivl tttfvfysgt msdvlgivaa tlsitagqll fkpesappsi
      181 rehrvllavg vacvaigpaf valdpmaegp fsqitqllwa phlsaleatq vctdsltsts
      241 ctaavdlara qgigalvani mpfiiqlvvc fglmrgrvla wwmavitqil aialltyqlw
      301 ddsrlsyllp nlvlvilpwl lalfmllinr slfrirenrt fftrtiafai laaalgaglw
      361 iltaslhntv ppanladila etplrfvpav vafilphhva patmfswfiy lwvgnafwml
      421 lavrlylgfs rpvnpalesd rgtarrllea gtgdhlsfmt lwksnryffh gdsyvayrvs
      481 ngialtlgap vgrdisaefe rfateqgwav awysvnaqfa dahpqfkrlq vaeeavlnce
      541 svefkgkkfq nvrtarnkae kegistrwtt weelditsia risalsedwv sdkalpemgf
      601 tlggleemmv ngtrlllaes adgtlhgvts wmpvyedgai agyvldvmrr nehgfkgvie
      661 lliseamlia hsegrawisl sgaplagqpd epswldvald rlgeeveply gfrtlaaskr
      721 kfqpeehpwy lcyhdelklp sialatmhay lpdmktkdav savrawmaa
//
LOCUS       WP_284837150             268 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: TrmH family RNA methyltransferase [Corynebacterium].
ACCESSION   WP_284837150
VERSION     WP_284837150.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..268
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28678
     Region          3..262
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mlitdptdpr lddirnlnks dksgeglvia egplvvdrla esrfpmrclv gfpkkieayi
       61 seygepecpi yevsretlae vagfdmhrgl vaaadrapep evselletaq tiavlegvgd
      121 henigaifrh aagmgvdavl lgsgaadply rrsvrvsmgh vlrlpfahle ggfttwqrsl
      181 qaladasftl isltpnpqav hlaeamhgld kvamlvgaeg pgltehamka tdiraripma
      241 pgtdslnvat aaaisfyerq rslsdlnv
//
LOCUS       WP_284837201             326 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease
            [Corynebacterium].
ACCESSION   WP_284837201
VERSION     WP_284837201.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 326)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..326
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36035
     Region          60..304
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtfqedslga ggagtttasp araespgdsa alvrkakrnr hkewllaaal lapnlillav
       61 ftyrplldni rlsffnwnis sptstfvgld nyvewfsrdd tktivlntlv ftffavigsm
      121 viglalalll nqnikgrnfa rsvvfapyai sgaaigiafq fvfdpnfgli qellgwfgvd
      181 spnfyavpgw amfmvtftfv wknlgytfvi ylaalqgldk eldeaaaidg tgrwrkfwrv
      241 tmpqlrnttf flsitvllns vqvfdiinvm trggpqgngt qtlvfqiyne tfvnfragyg
      301 ataatilfli lliitliqvr imdkrg
//
LOCUS       WP_284837471             833 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium amycolatum].
ACCESSION   WP_284837471
VERSION     WP_284837471.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 833)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..833
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=91047
     Region          35..829
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 masrasepgq dqtgrightg qaglpdqass apqreeesil aaeqayvdra fsfldrarer
       61 dqeylrqvml iddpdpqarv ereveyhrlq anldryrsae iglvfgridi ddtdpdnpls
      121 eegpgatvdk ryigriglsd enddyrtvim dwradgarpf ylattahpeg vslrrhlrth
      181 grkvrsidde wlsgeeadsa heteveagvg gesvlrevmn qartghmrgi vetiqreqdl
      241 iirdstrgtl vvqggpgtgk tavalhrvaw llytyrdqla ktgvliigpn ttfldyisrv
      301 lpslgetgvv lttiadlypg vrgsnalidg hnpeplvaqe vkgsiemlti lreavrayqe
      361 lpaeplevrn dnitltitpd mvkaartrar rtrkphnlar pifrdhvvel laaqmaevig
      421 adplggenll svtdiadlrd eidesgavad ildelwpalt pervlsells sreaidyaat
      481 dydeltreal yrpegtdwmp sdaplldela ellgpvgdae adeedwqarv eeaqgaldtl
      541 sssasqdldd gfeaeilsay dvidaealae rhrerdlrst aeraaadrlw ayghvivdea
      601 qelsamawrm lrrrspngwm tlvgdvaqtg spagaatwdd vlepiigsrw hlheltvnyr
      661 tpaevmevaa svlaeidpel eapqsiratg rkpvqartvt ealahveqva qpdrlvavia
      721 paelleatra evrdflggga dgdgdpdgag gasaaddapa trpskltnca vydittskgl
      781 efdevivvap dqivaqspqg lqdlyvaltr atqglivvap qqsgvlpelq wle
//
LOCUS       WP_284837511             724 aa            linear   BCT 25-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Corynebacterium
            amycolatum].
ACCESSION   WP_284837511
VERSION     WP_284837511.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Shan,L., Mathews,I.I. and Khosla,C.
  TITLE     Structural and mechanistic analysis of two prolyl endopeptidases:
            role of interdomain dynamics in catalysis and specificity
  JOURNAL   Proc Natl Acad Sci U S A 102 (10), 3599-3604 (2005)
   PUBMED   15738423
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Polgar,L.
  TITLE     The prolyl oligopeptidase family
  JOURNAL   Cell Mol Life Sci 59 (2), 349-362 (2002)
   PUBMED   11915948
REFERENCE   3  (residues 1 to 724)
  AUTHORS   Polgar,L.
  TITLE     A potential processing enzyme in prokaryotes: oligopeptidase B, a
            new type of serine peptidase
  JOURNAL   Proteins 28 (3), 375-379 (1997)
   PUBMED   9223183
REFERENCE   4  (residues 1 to 724)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 724)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..724
                     /product="prolyl oligopeptidase family serine peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=80032
     Region          21..724
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mgtdtdtdlg ndfsflstdl vpdwlddidg sqalawaraq skatvagvds laddtsdrtn
       61 leqrilaaln tdariaypvr rgeylynfwr daehprglwr rtslqsylag qedpqatewe
      121 tlidldalak aegenwvwkg tvyrypeydr alillsrgga datmvrefdl vnctfvedep
      181 fylpeaksdv cwlgrdeilv gsdfgpgslt dsgyprqvrr wrrgmpsssa dvifsghsdd
      241 vavggwfdat egferlfver ahdfynsqrf vaaerpgkla aqqngdfslq ilevpqdcrt
      301 svhrqwlvlm prtefngipa ggvavvelek wlagsrevev iftpdahtsf qqlawtknfl
      361 vltlledvat klvvlregsw epveafgelp aqatvsvidt aserddeiwl vstsatqpat
      421 lwygqvgspl tevrrapelf dsegmetrqh watsadgtri pyritgrfsa gagasadtga
      481 saetttatpt pnpaptlvha yggfevslvp qysairgltw lerggyfvea nlrgggefgp
      541 twhssvvkte rmrvyedhqa vlrdlvergy ctreqlgvrg gsngglltav cltsypelvg
      601 avvsqvplad mmryhklsag aswmaeygnp ddpteraaia qyspvqrvvk reqrayppal
      661 ittstrddrv hpaharslaw lleeagqpvd yhenteggha gaadnsqvaf vealistwlw
      721 nklk
//
LOCUS       WP_284837541             649 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Corynebacterium amycolatum].
ACCESSION   WP_284837541
VERSION     WP_284837541.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 649)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 649)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 649)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..649
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=68394
     Region          <35..220
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mltismllvl vgsfagittg raqaqeaast isptmvilda sgsmladdag gqtrmeaakt
       61 atskfagsvs edseigfmvy gtevgnspee reagcqditt llpvqagnsa kipaevgkvq
      121 asghtpmgpa lrqaadelpk egqrsivlvs dgedtcappp vcevakelkq qgidlvintv
      181 gflvdagara eleciaeatg geyldaqdsd slaesmktla trtartaqss aqeiqggdap
      241 tsatkvpadv etfstklrek tpesersisn qegdgaeyfs vpvaegerla isaatvpgas
      301 sgatlmdldv rnfsltmhld dsscflandf gngiidsngp lfasittkqs ggaegdcksg
      361 nmvfsvarkg gpfegqdipa evtikrfane nltdvpeafp sdkeslnppp atpeadqakk
      421 vtpgswfdda teltvdniss vtadivpget hvykikseyg qqlrgavkli dapeadklaq
      481 isgldiktln sarqlagsee trpvnehqig eettfgnsar inyrnriged seksgdyeae
      541 rawldgdqyi vvffnnswga gkshdvadvq nvpvtyqltt elvgekipgp afeqvahksp
      601 ssetptssqq npktteened dgsskmmwfs mgavllvlvv gatialtrk
//
LOCUS       WP_284837721             399 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium coyleae].
ACCESSION   WP_284837721
VERSION     WP_284837721.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..399
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42285
     Region          82..360
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 midalsvpma asslfstipl lavpalfltt lgggvfgssm yegssvggss ggsssyqlsd
       61 tfpdpdarpa elkslthien dvyevvvysh amgkevknev ilpggpdndt prptfyllmg
      121 adgaangwsw rnssdyqeff qdklvnvvtp igsvssmqad wyredkatgr nkwltyltke
      181 lpplidehfh gtghdaiagi smsggpalni asiaperfaa aasysgcpat tgmlgdtyvr
      241 ealkmngadp kkmwgmssdp awrahspvln ldalrdtalf iaaaqgvpga idasktsser
      301 igppvtieaa syacsayfad kakragldve wypqvegths wglfeksmre swrvigpaln
      361 vepferetpv tksplpseap qplgqrgssg ssessgsss
//
LOCUS       WP_284837746             488 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium coyleae].
ACCESSION   WP_284837746
VERSION     WP_284837746.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..488
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52064
     Region          172..477
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mkltrpaiav aavalvtaga vpvvhyassl dddtpavlsa aqstvnttlp etttsettep
       61 teksttsets atstsneptp ttselvpegs skdttnedlt skdgkddsat dadadatvls
      121 edaaklnpmg edmqqhpaik elgevpktms gadqrwvkrl adnqhvwkne alrvysesmg
      181 ryipvavfya tndkgetven aptvyllnga ggseqdtdwv sqaleevhev ygrsganvvi
      241 pmegafsyyv dwaaepptek nvfykgkqmw stflakelpq aiepyikadp nrrgvigmsm
      301 satsslllae hnpnmfkavg sfsgcpatsr plpsffinlt vdraapgvmt peyifgpmgs
      361 dynrrydalv napalagtdt kvyistgtgl aaetdmpgtl rkrledagld ssdafvkgsa
      421 naatllvegg aieaamnact hdflvkaran gaevahaelr pvgthswpvw rddlkrsyet
      481 vfksalgl
//
LOCUS       WP_284837983             451 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Corynebacterium coyleae].
ACCESSION   WP_284837983
VERSION     WP_284837983.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 451)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 451)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..451
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50765
     Region          1..421
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 milafevkny rsfaesaslh ftkrflktnh psdgdwvaat nrvaglfgpn asgkttllea
       61 lwelctypvv smrsdkllrs mykphrlqed reveffldfe yqgkrfrwel lldnegitye
      121 haevnetgqw kkifernena vtfgggslvs raarnfirqg atswvsvvap wgksqnpgey
      181 veafvnlces aefisphsrl lgglspklqk mlddrswgql atpvmhfadv gvsalkkeek
      241 etpelqrklf ksifaliess elapsaddvd eipipdkenv wtfvhsgapg dtfelnvvde
      301 slgtvswlet alpaleiisr gglmivdeld sslhpmlvrq lislfedeei nwrgaqlafs
      361 shdltllgnf pkpaltmdsa wlcekingas kirsideykl pstanaekry mqgvfgavpl
      421 vpqrkvasgf yelfrdlhsk sfetdenred k
//
LOCUS       WP_284838090             537 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Corynebacterium
            coyleae].
ACCESSION   WP_284838090
VERSION     WP_284838090.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..537
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=57891
     Region          4..523
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mstattplle vdsltvaygd aeptveniaf aveagkmtai vgesgsgktt samaaldllg
       61 ptgnvragsi rfkgqdlasl saaewrelrg akiglvpqdp nnslnplkti gasvedglei
      121 hgvgdaasrr rqaiallerv giddpekryn qyphelsggm kqrvliaaav alepevliad
      181 eptsaldvtv qktildllde mrtelglgvi fithdlavag draddvvime rgrvvehgpv
      241 stvltnptqd yskrllanvp slsvanayrr ppvttdtllr vdnlavrygd ftavsdisfe
      301 vargsthalv ggsgsgkttt grtiamfnqp aegsitldge elttlnpkqk rnfrnriqmv
      361 yqnpfssldp kmrvgeivae plrnlagask reslaraney lervaldper fasrtpaqls
      421 ggqrqrvaia ralivepelv vldeavsald vtvqaqilel lenlqrelgl tyvfishdla
      481 vvrqisdtvs vfsrgqqvey gptdevfsrp hddvtrelid aipgtvfrar qlgefvv
//
LOCUS       WP_284838165             500 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Corynebacterium coyleae].
ACCESSION   WP_284838165
VERSION     WP_284838165.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..500
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52215
     Region          127..496
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mttavapads peqqashkln tgktiaffla fvalaavilt piaglampak ialgmlafav
       61 imwvseavsy pvsavmivgl iaimltfavd petgeaigas kglsiamsgf sssavalvaa
      121 alalatamqa tglhrrlaly vlkfagekvs nivigaivis iilaffvpsa taragavvpi
      181 lmgmvaafgl akesklaall vitatqavsi wnvgiktaaa qnlvavgfie dqmgqtvswg
      241 qwfiwaapws ilmsialyfi mraaikpeve sidggrelve kqlaemgpmt gaekrltaia
      301 mlllffwate gvlhpissat itivavgfml mpvigvmdwk yaqqqinwgt lvvfaagisl
      361 gkflldtgaa twlseatfga iglssmpila aialvslfni lihlgfasat slasalipvf
      421 ialaatldvp nggigfviiq qfvicfgfll pvsapqnmla ygtgaftskq flrsgiplti
      481 vayllillls atywnwiglv
//
LOCUS       WP_284838270             378 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Corynebacterium coyleae].
ACCESSION   WP_284838270
VERSION     WP_284838270.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..378
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41117
     Region          1..375
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mnaplsgirv ldlsrvlagp fcsmiladlg aevikvespw gddsrqfgpf vdgtsayyrl
       61 fnrskmgitl dfkndddkev lrdlvrradv vvenfrpgvl eklglapkdl leinprlvvt
      121 sisgfgqsgs lakepaydlv aqamsglmsi tgwpnskptr vgislgdlip glyaaigtvs
      181 alyqressgt gqhldlamyd slisvmesvg mralyddtpp trigndhgls apfstyatkd
      241 gdvviaittn rlferlsnal gmpelatdhr faepvarsdn rvalreliee alstktrset
      301 ialfeehgvp tarvydldea lrspfaqerg vvveetdgfr tlasplklag mekptpapel
      361 gqdneriqsw lsedprtt
//
LOCUS       WP_284838406             197 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Corynebacterium coyleae].
ACCESSION   WP_284838406
VERSION     WP_284838406.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium coyleae
  ORGANISM  Corynebacterium coyleae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Corynebacterium coyleae"
                     /db_xref="taxon:53374"
     Protein         1..197
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=21133
     Region          1..190
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mrlvlasqsp srrmlleqgg vtpvlrpahi dedaviaalg nvppattvat larakaetai
       61 aefpddvvvg cdsmlllddt llgkphtvde tirrwkaqrg keahlltgha vwfggewvvd
      121 tvttairfgd vsdadieaya rsgqplecag aftlealgsw fidsidgdpt sviglsmpll
      181 rrclyrfgld asdfwat
//
LOCUS       WP_284838525             659 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD/NAD(P)-binding protein [Corynebacterium accolens].
ACCESSION   WP_284838525
VERSION     WP_284838525.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11816065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..659
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72236
     Region          1..627
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
     Region          9..202
                     /region_name="NAD_binding_9"
                     /note="FAD-NAD(P)-binding; pfam13454"
                     /db_xref="CDD:433222"
ORIGIN      
        1 mtdntssial iglgprgisv lerlvaqlnt vshppekltl hliddaqhgg gkiwdinqpk
       61 ylcmntfahg mtlfsepgst veapvvegpt iyewirltlg danvpagard yaathpldpq
      121 aleefgrvel eklrpesylp ralyghyilw vfhsvlqdvp ewvevkqhha rvvdiesrdg
      181 adilhlnndt tveagstlav tgwqnqgyte nerwilktle enpslrwira dnpidqgvds
      241 ikdnekvlvr glgmgffdil ilstvgrggk fvedsskpwg mryeatgtep tfaaasrrgy
      301 pflpqsdegs lppaaeiprl kkvvaelshr tgarsinydt evwpavarda yqayidtlar
      361 vepeslrtsr eeiitdldat pvdagvayng laqldevihr httkdfsllr wmhlltedfs
      421 sqqeltehia qslcedlaea qkgpdspvra alwsvgfsrk ptqvlgaegr ytlesrhhmf
      481 dkaislgqtt csgpppfrtq qllalvdagi vsfvggnpvl gtnadtgewt isssasggkr
      541 ipgttlldaw vhkpdirrtp hdsfmhslve sgrvraftet ardgievptg spaedpdtrq
      601 vhnadgtvde rlhlvgipah aeypdttlap pipgtdswfi qeadkaavha aqvafagqa
//
LOCUS       WP_284838542             182 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Corynebacterium accolens].
ACCESSION   WP_284838542
VERSION     WP_284838542.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..182
                     /product="YceD family protein"
                     /calculated_mol_wt=19087
     Region          1..182
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mtsplkfdvg ellnaqgada mpeqrtqtgp aperigvemi aipkgedltv aailtplgsg
       61 vlvdadisgv ltgecarclk elhpqldlhv tqvfaadesf vsgddadsdd agsgdeipei
      121 eddeldllqa videaglnlp fapvcedgcd iqtpegvttg isgdeeeeek vdprwaglek
      181 fl
//
LOCUS       WP_284838730             562 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Corynebacterium imitans].
ACCESSION   WP_284838730
VERSION     WP_284838730.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium imitans
  ORGANISM  Corynebacterium imitans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Corynebacterium imitans"
                     /db_xref="taxon:156978"
     Protein         1..562
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62437
     Region          51..544
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 msseirvnrr vvlqaaaasa aavavgagga yaartstvst peiptqaeqw dlpflhgvas
       61 gdplpdrvil wtrvtpsrda lpgsglgedv elewqldtse dfknpqtgtv vaiasadhtv
      121 hvdptglspd teyfyrfivk dgahagatsp vgrtltapae dgeidqlnla iascanwesg
      181 ffcaygdmaq rarnreidhv vflgdyiyey ptgeyagksg varmhhpewe ittledyrqr
      241 ygryrtdlhl qaahgacpwi vvwddheian nnwregaenh tdgrvegewa qrreaamqay
      301 fewlpvraes lsgerrlyrr fnfgtlaqlt vmdlrtyrda ettgsqfndp drtmlgseqf
      361 nwlteqlkns tarwdvlgns vmispmrfat iagndkanea igyirerstg iavnsdqwdg
      421 yaaerdrllt vldeqnsnal fltgdihsew ansisatyge igcemvttsi sapnvdeilt
      481 safgtyhped nstsllvekv irdnnpwvnh idfdahgygi asihldfvdm cyyrvsdved
      541 pdatvalger rqwrigegfv da
//
LOCUS       WP_284838853             290 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Corynebacterium marquesiae].
ACCESSION   WP_284838853
VERSION     WP_284838853.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..290
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32023
     Region          1..272
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 masirevlav eetkvadvfk gpavesrier tfggqiaaqa vaaaqrtvsg kdihslhgyf
       61 vgpgdasqpi eirverireg rsfanrqvrv yqgdvllftl masfhrdgdy gpqhqdaapk
      121 vlgpeeaarm gggapystri ilkeweewdi rlvpeedrdp vaaertgagy ryiwfrntgh
      181 lpadsafhca altymsdmtl irsaliphqg ekvqlasldh aiwflrpfrv dewllyeqvs
      241 paasnatava rgkifteqge lvalvnqegl tryldenlgs gsahgnwhnv
//
LOCUS       WP_284838647             400 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Corynebacterium imitans].
ACCESSION   WP_284838647
VERSION     WP_284838647.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium imitans
  ORGANISM  Corynebacterium imitans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Corynebacterium imitans"
                     /db_xref="taxon:156978"
     Protein         1..400
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43716
     Region          59..381
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 maiqrretat gkvrwivrwr dkggkehsks fsrradakqh aaevehrrar ggsttpqtls
       61 vlelynrwld srplrdtsrt lyehtrdknl tplhhypaae ldntdvqqwa hqlaggrgwv
      121 srddtglspa gvqnalrhlr saykwgvete lvarnpvrvr vadravepte lptvdeiaav
      181 iagvrtggap yieksrskdp akrgtaytah qrprpdiadm letaaatglr vselaglnvg
      241 evdlaagvir vraqlgktpp rkrvalktdn srrdvpipdg lvpvlqrhte drdpaallfv
      301 tktgrpints haavvvkraa ehagaprvhf halrhyyasa litagvpiqd vaavmghtva
      361 vtmktyahvl egyqdrvraa vtgsgiyagr palrvvegga
//
LOCUS       WP_284838899             221 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium marquesiae].
ACCESSION   WP_284838899
VERSION     WP_284838899.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..221
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23707
     Region          1..185
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mdgtltnsep lwaeatfyls ellgkrltpt qrlatvgatf dttlaicadn agvtlqpgds
       61 ecyrarmfdy vkglfarqle ifpgipallq elkadgvpmm vttnternva daaidslgrh
      121 yfvdticgde vpagkpapdm yreaarriga dpadclvfed satgmraavd agcaviglpe
      181 gdqvevptev teisslrdsr hlagakaadv yewfakisvr q
//
LOCUS       WP_284838913             382 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Corynebacterium
            marquesiae].
ACCESSION   WP_284838913
VERSION     WP_284838913.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..382
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41582
     Region          10..378
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mvdtghphsl eglrvldmsr vlagpfcsmi ladlgaevik ietpwgddsr nfgpdfkgds
       61 ayyrlfnrsk kgitlnlkee adlntlrelv qradvlvenf rpgvmeklgi speslmelnp
      121 qlivtsisgf gqtgsmskap aydlvaqams gimsitgwpg grptrvgisl gdlipglyga
      181 igtlgalqer hrtghgqhvd vamfdslvsi lesvamrdly eeevptavgs dhamtvpfst
      241 yrvddgevvi ailneklfgc ltralgleym vddprynsnp arkerreevr siiedalrgk
      301 tveqalalfq ehgvptapvh svdealhgdv gterevlfte sdgfttlssp lrltgsrqpe
      361 papqlgehna hipewlaepv rg
//
LOCUS       WP_284838930             219 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            marquesiae].
ACCESSION   WP_284838930
VERSION     WP_284838930.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..219
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23305
     Region          10..219
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mpdslprptt elfpealnls pkqrevltav qrhpegakag tvaeelgmhv ntarghidel
       61 vnagavnvvs apskgrgrps lifqarvpdn kavaeeyitl vevlttmlad keelddaasa
      121 kaleigrrwa raagadasdg aldtlfatlr dmgfdpatkp dstdielhac pfvssglaps
      181 pflcavhagf lqetsdedti inlvprqphn vcrlkikpa
//
LOCUS       WP_284838971             332 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium marquesiae].
ACCESSION   WP_284838971
VERSION     WP_284838971.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 332)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18950610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..332
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=36886
     Region          40..163
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
     Region          176..319
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mpnikkmhet dkdqqheefi sgrhqeipvd pakefhrttl aagaviwrgs pqdpeialih
       61 rphyddwslp kgkvdpgesl pttaareile etgfsvrlgk ligkvtypvq grtkvvyywv
      121 akylggtysa nsetdelrwl pideaqdlls ydvdtavvak aakrlriapa trvlyvrhar
      181 ahesgswegd dnlrpldkkg rrqaemlvpm lsayqptaiy salpqrcqqt aapladelgk
      241 disinknfgd eawendpeta kkafrrvvnd ggvpvivsqg atipgiiedl apkflkkpvd
      301 klkfkkssvw vlsfnngelt gadylasplp vr
//
LOCUS       WP_284838761             733 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium imitans].
ACCESSION   WP_284838761
VERSION     WP_284838761.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium imitans
  ORGANISM  Corynebacterium imitans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 733)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 733)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 733)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..733
                     /organism="Corynebacterium imitans"
                     /db_xref="taxon:156978"
     Protein         1..733
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=80429
     Region          7..730
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mgtpekiaae qayvdtlfah ldaevtaaqe klaavqrdvd pdnpdsdalv rreteyhgln
       61 akldalniae vglvfgridv addevenpvp greglerryi grmgmddred nyrtllldwr
      121 aplarpfyla ttahpegveq rrnirmrgrt vtavddevla gegldaever gnvgseaalr
      181 hamnaartgh mrsivetiqr eqdeiirdpt rgvmvvqggp gtgktavalh rvayllytwr
      241 eqlsrtgvli igpnpafldy isrvlpelge tgvvlstied lvpgfrptas gesaaarevk
      301 gseemvtilk ravqayetvp aapvplkigs vdiaatptiv kaartrarrs rkphnqaref
      361 faehltqsla ealadrigrd plggenllst advdqlhddl aeeqqvidlv deyfpeldpa
      421 evldatltdr arietvagdy daytqdalyr apgtgfypsd talydelsil igvtdpteqk
      481 akeeaqwrql veeaedaldv lassestdnd ddqfeaeils aadvidaetl asrqrvtdir
      541 staqraredh twayghvivd eaqeltpmew rmvfrrcpsk wmtlvgdtaq tsspagsddw
      601 attlapfvge rfrthqltvn yrtpaevmey adellaeidp easssvaire tgvpvrhlpa
      661 gtdpaevvgs lqadgrmvai idadnvaqmk glefdhvilv dprriidasp qglqdlyvaa
      721 tratqsltvi gel
//
LOCUS       WP_284839044             268 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium marquesiae].
ACCESSION   WP_284839044
VERSION     WP_284839044.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..268
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28515
     Region          3..262
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mlitdpadpc lddirnlnks dksgeglvia egplvvsrla esrfpmrclv gfpkkveayi
       61 seygepecpi yevsretlae vagfdmhrgl vaaadrasep evseivesaq tiavlegvgd
      121 henigaifrh aagmgvdavl lgsgaadply rrsvrvsmgh vlrlpfahle ggfttwqrsl
      181 qaladasftl isltpnpqav hlaeamhgld kvamlvgaeg pgltehamka tdiraripma
      241 pgtdslnvat aaaisfyerq rslsdlnv
//
LOCUS       WP_284839193             294 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Corynebacterium marquesiae].
ACCESSION   WP_284839193
VERSION     WP_284839193.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..294
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30653
     Region          5..282
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(34,231,234)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(181,202,229,232..233,236)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mtihvcgegl vdlvpvapgs lndhtpalgg gpfnvaiaaa rlgadvefqs ristdgfgqe
       61 lvarleaegv ttthlqrgde pttlavttih edgsasynfy iegtadrlve prlvpadiac
      121 fgtvslalep gasryaqllk dfaaqgtlva ldpnirpfya tpehraflan llphvtllkl
      181 sdeevdflgp dlisqvpvvi vtrggeglsv qagetklnvp aaqvpvtdti gagdtimaal
      241 ltqidergld ssalaqlgaa ewkellsfaa aaagitvsrk ganpprreev essl
//
LOCUS       WP_284839296             328 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            marquesiae].
ACCESSION   WP_284839296
VERSION     WP_284839296.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..328
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35362
     Region          13..323
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 maahnpapkr hdeaverltn lsfalqgaan sggspdrtaa wirshvagyg dksdeafaks
       61 lardiatlqr agvpivhsgg edgaryrlda ssyqlppvef speeamvlgi aggvgttggl
      121 sdfslsgwtk iaasgasrnl agapvytavn ditrlapeii tsvlaavrnq vritfsyran
      181 patepvrrvm dpwgvvnrds riylvgfdvd rneprvfral rvsdikrshd paehpnpten
      241 lqvlvervlq rgekvdarlv ipegqarell dsgeqqtdgt vllhkvdkdw lvrtaagyap
      301 evqvlepagi rqevisllhk asqsqeeg
//
LOCUS       WP_284839297             375 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium marquesiae].
ACCESSION   WP_284839297
VERSION     WP_284839297.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..375
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=40142
     Region          18..374
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mtdtqtfsad vyaqrlhaaq kaaadkgidl lligtgpdfa yltgswvssh erltvlvvpq
       61 qgnawiaapn tditdikaap vgeldvelrg wndgenpyel alrgagdglg kvalgqslta
      121 dhvlrfqdll phasyelaty alaelftrkd eaeiaelrka graidavhaq vpqllqagrt
      181 evevahelek lilrehsvid fvivgsgpng anphhsfsdr vlaegepvvv diggtfpsgy
      241 hsdctrtyvv ggdmskapqd fqdayavlad aqaagraaah pgstaadida ivrqaisaag
      301 wgdyfvhrtg hgiglsthee pfimegndld leegmafsie pgiylegkwg mrledivvlt
      361 ndgyeslnla prdvr
//
LOCUS       WP_284839359             293 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium marquesiae].
ACCESSION   WP_284839359
VERSION     WP_284839359.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..293
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31179
     Region          22..244
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mttsreprhp rraattragg dparaaaffd ldktiiatss ayafgreflh nglispaeal
       61 qlslakasym fsgltsegmd strdqltamv tgwsvdevra iaretmhhvv tpsiyaeare
      121 lirahraagh hvvivsasaa vlvniiaeel gvehviatel aeengrftge vlfyckgpnk
      181 aaaleqtaaa enldlnasya ysdsatdipm lekvghpvav npdkqlkrha lthewnirsf
      241 kdpvpllaap takeigigas vlagtaavig aglwltqhpg rpgppkrgpr ras
//
LOCUS       WP_284839378             511 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Corynebacterium
            marquesiae].
ACCESSION   WP_284839378
VERSION     WP_284839378.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..511
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=55546
     Region          1..189
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mrlsgeenip dkggavlvcn htgymdflfg aflayckkrl vrflakagif kapvagpllr
       61 amhhvpvdri dgsasfrqav qlakdgelvg vfsegtisrs feirsmksga sriayeagvp
      121 vipqvifgsq rlwtkghkkn lgrtktpvfi talepyyptg daeadtaeir rrmqealegl
      181 weqyeaefgp mpageywvpa rkgggaptld eaeardaeve terhrvrrlr ddlvglkerv
      241 svttvdlvrn hmaaakgtdg eepknkarta petlewikhn lnavveeatr gldegrdkva
      301 dvmaqlksdv aqtqvsitas skeiwagsva eqgllaaatq srlivsrlph rmkaqfssip
      361 rvvvahssal nwedgaltpr lhkalaeiyp aaevlivisp agevdvpqav wsvvldedav
      421 qprldtnals vtaatavqgv eriledlqak seealvfane pgdedfldwm pvvaletapi
      481 evvkgaqavt ysaekagmse vlevmarlaq k
//
LOCUS       WP_284839409             630 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium
            marquesiae].
ACCESSION   WP_284839409
VERSION     WP_284839409.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 630)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..630
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64802
     Region          32..624
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mssacgcehe pvteideidr pwwkdpelll pifsgvalit glaldwsdle tpatvlywvg
       61 lllgaytfap gairnlvtkr klgigllmti savgavilgf vgeaaalafl ysiaealedk
      121 amdraqgglr allklvpqta tvlrdgtaae vaakdlevge lmlvrpgeri atdgiirsgr
      181 ssldtsaitg esipeevapg devpagains agvlevetta agtdnslttl vdlveqaqae
      241 kgdrariadr iaqplvpgvm ilavlvgvig sllgdpetwi tralvvlvaa spcalaisvp
      301 ltvvaaigaa sqfgvviksg aaferlggir hlavdktgtl trnqpevtgv vpadgfdraq
      361 vlsfaaaveq qsthplaaai aaagseapta sdiseeaghg iagtvegrrv lvgsprwida
      421 gplkadverm esegqtcvlv tvddalagai gvrdelrpev peavqalhan dvevsmltgd
      481 ntrtaralag iagindvrae lrpedkasiv adfssktpta migdgindap alagatvgia
      541 mgatgsdaai esadvaftgh dlrlipkalq harrgsriin qnivlslaii ivlmplaisg
      601 vlglaavvlv hevaevivil nglraaqakr
//
LOCUS       WP_284839417             119 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Corynebacterium marquesiae].
ACCESSION   WP_284839417
VERSION     WP_284839417.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium marquesiae
  ORGANISM  Corynebacterium marquesiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Corynebacterium marquesiae"
                     /db_xref="taxon:2913503"
     Protein         1..119
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12481
     Region          3..106
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mrawvilfla iasevvgtva lkyavdhfwi ysvaafcfil afvllhrvmq egvnvgvayg
       61 lwasggvist allsaalfge plgavklagi alimggvfcv emgakpdedq dhtvevapq
//
LOCUS       WP_284839602             256 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium sp. MSK163].
ACCESSION   WP_284839602
VERSION     WP_284839602.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK163
  ORGANISM  Corynebacterium sp. MSK163
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Corynebacterium sp. MSK163"
                     /db_xref="taxon:3377091"
     Protein         1..256
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27593
     Region          1..233
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(17..18,20..21,24..25,63,67..68,71..72,102,106,113,
                     116..117,122,138,142..143,145..147,149..150,153..154,
                     157..158,178..179,181..183,185..187,189..190,192..193,197,
                     200..201,211,213)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(141,145,148..149,151..152,192,195..196,198..203,206,
                     211..212,216,218)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(162..169,180,183..184,187)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mpnllrganp lsriflmfiw vspllasidr vsaavsltlt lilaplcgvs wgqllkggwf
       61 lfliapisgi smllygepgg teyfswwlia vtqnsltlav aitlrvfava lpmvvlardi
      121 dptelgdals qilklpsrfv igavagvrmm tlfqsdwqsl gmarrarglt dvgklqhllt
      181 msfgllvial rrggklatam eargfgrtpp gggkrsware srlrardgwi mtcgavlalv
      241 pvvvsvltga wrffgl
//
LOCUS       WP_284839662             200 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Corynebacterium amycolatum].
ACCESSION   WP_284839662
VERSION     WP_284839662.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..200
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=21280
     Region          4..194
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mssprivlas tspsrlhilr sagiepitva pnvdedavva alpdaspvri veelaqakah
       61 aaspaypndi viggdsmlll dgklqgkpht eektierwhq qsgrtaelit ghcvvtpkge
      121 hlevaitsld faevpeedir ayaatgeplk cagaftleal ggwfvdging dsssviglsl
      181 pvvrralyry gysvsqfwnk
//
LOCUS       WP_284839783             444 aa            linear   BCT 25-DEC-2024
DEFINITION  nitrate/nitrite transporter [Corynebacterium amycolatum].
ACCESSION   WP_284839783
VERSION     WP_284839783.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Yan,H., Huang,W., Yan,C., Gong,X., Jiang,S., Zhao,Y., Wang,J. and
            Shi,Y.
  TITLE     Structure and mechanism of a nitrate transporter
  JOURNAL   Cell Rep 3 (3), 716-723 (2013)
   PUBMED   23523348
REFERENCE   6  (residues 1 to 444)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   7  (residues 1 to 444)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..444
                     /product="nitrate/nitrite transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48195
     Region          31..432
                     /region_name="MFS_NRT2_like"
                     /note="Plant Nitrate transporter NRT2 family and Bacterial
                     Nitrate/Nitrite transporters of the Major Facilitator
                     Superfamily; cd17341"
                     /db_xref="CDD:340899"
     Site            order(41..42,45..46,49,82,137..138,140..142,145,164,
                     167..168,171,255,258..259,262..264,267,306,310,365..366,
                     370,374,390,393..394,397..398,401)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340899"
ORIGIN      
        1 mepldtsgkv ikgwdpedpa hwdskiawkt ltistialii gfatwylvsa iapmlnrigf
       61 dltagqlywl tsiaglscgl frlvfmflpp iigtrklvtl ssflfvipml gwyfavqntd
      121 tpywwlltls flsgigggvf sgfmpstgyf fpkhmsgtal giqagignfg isliqlvgpw
      181 lmgfsllglg fvapmrtdeg hdvfvynpai vlvpwtiimg ivawtmlkdv piranfreqi
      241 difgnkntwi ltivylvtfg afsgfaaqla lltndvfgan skfaeayala nlpqgakyaf
      301 lgpligalvr alwgplcdkf ggaiwtfigc agmtiftgva aifltpdspd eygwflgsml
      361 imffftglgn agtfkqmpmi lpkrqaggvi gwtgaigafg pfivgvllsv mapvaffwgc
      421 vaffafttvl vwiyyarpna pfpg
//
LOCUS       WP_284839801             287 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Corynebacterium
            amycolatum].
ACCESSION   WP_284839801
VERSION     WP_284839801.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..287
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30845
     Region          21..286
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mtgfssldge qtfpwlpsgp allfapadrp erfqkaaers dmviidledg aavdnheqar
       61 aniinnpldp ettilritgp gtptfaedva faracdydiv mvpkirdsip aeleglkiia
      121 mietpqamin iqqiamhpdv vglfwgaedl taelggvssr qsvdenprrh yrdpqrlara
      181 lvqvhaaaag iaaidavhtd frdergqyle aldavgcgfl atacihpamv pplrkaykps
      241 eatlararki vdhagthtga fqldgemida pvvkqavaal aragite
//
LOCUS       WP_284839804             554 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Corynebacterium amycolatum].
ACCESSION   WP_284839804
VERSION     WP_284839804.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 554)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..554
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=59383
     Region          10..329
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(13..14,17..18,50,53,107..108,160)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(105,108,187..193,222,251..256,283,309..312,314)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 maaaesnrvv alwlpdwpvq aahlasvtsq anplslvaiv gdsgvaacsp sarragvrrg
       61 qsrrhaealc pelevveesa vrdaaefesv lqrleavaag vealrpglav vaargvmryy
      121 ggqdvalekl ldaaavpgvd cslgladdiv tailaarrgv lvapgedegk rfrqgislve
      181 lraesalemp aelakswqel glrtlgdvaa lpkrdianrf gvqgarwhdl acrgevrlva
      241 prslppglaa syqswesplr rvdeasfvar flagqlheql fnhgyscyrl avvaqfsdgs
      301 evrrvwrcte plaeqttadr vrwqldgwln nrnrqqprgn sdtgagvvgc aeendgddsr
      361 givelqlepl dvvaagtvkq dlwhgsddar akarraaerv qgllgpeavq qpimqggrgp
      421 gervgfvafg enpkntktae inqpwpgavl apnpaiipat anaevevlda dghtvgvtgr
      481 atmtaepslv rhgvttyrvs swagpwpide rwwvpdearr aariqirava ndgtiaawll
      541 ighagawrie gaya
//
LOCUS       WP_284839929             371 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium amycolatum].
ACCESSION   WP_284839929
VERSION     WP_284839929.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..371
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39247
     Region          16..371
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 msngifsfdi yqqrldrtae llrtrdadaa vfgtgadlqy ligsavtshe rltalvvtaa
       61 gtttlvlpav ergdlplcai ndlnadvvlw edgqdphriv adlvghvgtl aigasltadh
      121 lipiqdltga ktvlagellk elfmrkdaae idqlreagaa idrvharvpg mlragrtere
      181 vadeisaail eeghvaidfv ivgsaengan phhdfsnrvi edgnvvvidi ggtlplgyhs
      241 dctrtyvvgk pgeketaawa alrkaqeaav aavrpgvtaa eidaiarnsl taagygeyfi
      301 hrtghgigls theepfimag nelalepgma fsvepgvylp gdfgmrledi iivtedgges
      361 vnnsphdlit v
//
LOCUS       WP_284840013             230 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium amycolatum].
ACCESSION   WP_284840013
VERSION     WP_284840013.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 230)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 230)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..230
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24627
     Region          1..91
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mkqrtyfeqa aaiaaecssp vrlaileyll kngptrvrsl aestniaest lsnnlrrlre
       61 aeivdverqg ksatysianp sirqvianlf qaagadtaap ipehqpavtf arscydhlag
      121 slgvqltral fakealitda ddiafgpnae kcfaylgtgl ssldasrkta flcndwthad
      181 shlagslgaa llrgliskgw lkpipdsrgl eltaegkvnl edfigtrlep
//
LOCUS       WP_284840019             346 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Corynebacterium amycolatum].
ACCESSION   WP_284840019
VERSION     WP_284840019.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..346
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=38956
     Region          37..335
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 meqarawrsk eltlihddvw tppaeregrk krtgltvaey fetlptkrnw epttergyrs
       61 mftndiaptf gemhlaaitr aevrkwydsm vkankdrkkr nrdvysllkt iysqavedel
      121 iqvspvnipg astrpsakke qeiptsqefa klvaavpery qvptmvaavc alrigewael
      181 rrkdvrrdsa tgvmkvhvcr qvreakgksg kvvvpftktk qdrwvtvpaa ivpaleqhid
      241 tyagagrdgl lfpnkegdwv drrrfnrmlk aachealghd nihshilrhy ggtqfamagg
      301 tmaetmarlg htttsaalry qhaaevrdve vanrmvmplv avpdva
//
LOCUS       WP_284840450             404 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Corynebacterium
            pyruviciproducens].
ACCESSION   WP_284840450
VERSION     WP_284840450.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pyruviciproducens
  ORGANISM  Corynebacterium pyruviciproducens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Corynebacterium pyruviciproducens"
                     /db_xref="taxon:598660"
     Protein         1..404
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44791
     Region          68..399
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mkhskigtgs iyresatgrw raaftvgydg agrqirktvt akdknscikk rnelmlklmq
       61 qtetpekism etwcekwlre iareklhplv yqdnkgkvrk yiipclgayp vreigaeevr
      121 elhafvraag vtdrtvqivh sllstilhda vregictsna carvdrprav lrerpalsvy
      181 hakrvlfaaa eagdpltsfw aaalmlgark geliglersr vdlasgvidl swqvqtlpwr
      241 hgahcscanr qkfaaqcpqr ehdvpshfel rechgsrvft rpktaaglrv vpipapliav
      301 lheqmstqpv aennlvwvtr eglplaqkki telwhtalar agapeldfhs arhttvslll
      361 eagvspevia qivghssvls trnymhvpas mardamsklg ella
//
LOCUS       WP_284840584             223 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium pyruviciproducens].
ACCESSION   WP_284840584
VERSION     WP_284840584.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pyruviciproducens
  ORGANISM  Corynebacterium pyruviciproducens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Corynebacterium pyruviciproducens"
                     /db_xref="taxon:598660"
     Protein         1..223
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=25439
ORIGIN      
        1 mfalhslvfl qvypfhksal fatihrfipm qlgstggtff filsgfliyw snshirtgte
       61 vrhyllrrvt kiypthllal vlfvvpsatf tahgvklvld fsrlalwlln alllhtwrpa
      121 watlggmntp swslvsemlf ylslplfvpl frrirgrgnw vgrtefpigy gatkviaegc
      181 vaptdhirgr gghlwwyqpn taeeiwaflr vqhrqtcrlg tkt
//
LOCUS       WP_284840651             833 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium pyruviciproducens].
ACCESSION   WP_284840651
VERSION     WP_284840651.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pyruviciproducens
  ORGANISM  Corynebacterium pyruviciproducens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Corynebacterium pyruviciproducens"
                     /db_xref="taxon:598660"
     Protein         1..833
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=93102
     Region          14..826
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mlpdlkevpe slvdeatfds fihyvrsqgi elypaqeeaa lgilagdnvi lstptgsgks
       61 mvanaahfia lsrgqrsfyt apikalvsek ffalcsmfgp envgmmtgda tvngkapiic
      121 ataeivania lrdgaeadid qvimdefhyy adpqrgwawq vpllelpkaq fllmsatlgd
      181 ttalredlak rtgrptnevs gsvrpvplef hyvytpvqet venllesgtv pvyivyftqr
      241 ealeraqals sinvankeek akiakeigsf rfttkfgktl srllrkgigv hhagmlpkyr
      301 rlverlsqag llkvicgtdt lgvginvpir tvlftglvky dgfrsrvlks refhqiagra
      361 gragfdtkgt viveapehei enyklrkrag qdekklkklr kakvkkgevt wsddtfekli
      421 tsspeqltsq frvstsmlin vlardgdtle hfrhllrtsh ntrkqqnhdi ltaielyrgl
      481 veagvvseen gteltedlpr dfalnqplgq falaalelld pesptltldv isvfesilen
      541 prnllraqqr aeraeenaal kdegvdyner rvlldevtwp qplgelltga cemyakghpw
      601 vreyeltpks virymiehgl tfsdivaefg vsrsegellr yltdawrtlk qsvpeayytd
      661 elddvvvwlg eiiqqvdssl idewaqmadp dapvsadtie qqlafgvtdp nalsankraf
      721 timvrnyffh lvelfaleke dklgelteyl ddqpdfssal dayfddyadl dlspaargkd
      781 yfrltedgrs whvrqivkdp eddrsfafvg tvdleasdae gevrlsalti eqn
//
LOCUS       WP_284840686             722 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-glucosidase family protein [Corynebacterium
            pyruviciproducens].
ACCESSION   WP_284840686
VERSION     WP_284840686.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pyruviciproducens
  ORGANISM  Corynebacterium pyruviciproducens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Varghese,J.N., Hrmova,M. and Fincher,G.B.
  TITLE     Three-dimensional structure of a barley beta-D-glucan exohydrolase,
            a family 3 glycosyl hydrolase
  JOURNAL   Structure 7 (2), 179-190 (1999)
   PUBMED   10368285
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444920
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Corynebacterium pyruviciproducens"
                     /db_xref="taxon:598660"
     Protein         1..722
                     /product="beta-glucosidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0015926 - glucosidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=78893
     Region          40..472
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          368..606
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
     Region          640..710
                     /region_name="Fn3-like"
                     /note="Fibronectin type III-like domain; pfam14310"
                     /db_xref="CDD:433860"
ORIGIN      
        1 mttvteatng nkkpstskkf rvgnmtktpr eraeelvsrm tleqkiaqlh ggmetiniyg
       61 ysneidpdde dameqlaaqi rierhvpeie elgiprfrit ngpvgvgmgd gtpsppatal
      121 pmtigvaasf dpelayqygd iigqetddlg qhvlegpglc lhrtvtagrn feyfsedpyl
      181 tgvmgvevtk aiqdhdiiam akhfvvndqe yerfrtniei deqtlremyl lpfemvvkdg
      241 kvaaimsayn rvrgdyaten ryllndvlrg dwgfegyvqs dfwstrscaa slnagldhem
      301 pdakwfnenn lkaaledtst eielidrali rrytqmyrfn qfdrpyapre idaqghgaiv
      361 rrigadmavl lknsegllpl spdagkiliv gqskfaefac qggggsskvd plytvdpepg
      421 mkdvveelgg satvesfive rdltnlseai aaakdadvvv imagliateg admptmimph
      481 qqnemiakll tanpktavvl kssapmvmpw tddapailev wnqgvedghv vgdllfgkvn
      541 psgrvpttyp kteddwighg hgheerypgv nlgegyntmt yterlhmgyr seaitpafpf
      601 gyglsyttfe ladvsvdgsa skvtvtatvt ntgdvagkdv vqvylgvpae gqpakrlvgf
      661 akvyvepgas ekveividad asnhplsvwd vaahdfvvps geftvyvghd vtddshvstf
      721 tv
//
LOCUS       WP_284840824             220 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium pyruviciproducens].
ACCESSION   WP_284840824
VERSION     WP_284840824.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pyruviciproducens
  ORGANISM  Corynebacterium pyruviciproducens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Corynebacterium pyruviciproducens"
                     /db_xref="taxon:598660"
     Protein         1..220
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=24250
     Region          30..189
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mippwmahva hsapainnll ghqpatnrdr eaavlmlfsg dseaetlprd agvllthrnp
       61 tmrthsgqia fpggrtdptd dspvhtalre aweetgldpd tvqpvvklde vhirrsgypi
      121 hpiigywvep eevypaslde tddvfeaplf hlldpanrmm vghggwkgpa fsingyvvwg
      181 ftagllsavf rgagwerpwd qtvtdlttai hrsrngerlr
//
LOCUS       WP_284840916             237 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium pyruviciproducens].
ACCESSION   WP_284840916
VERSION     WP_284840916.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pyruviciproducens
  ORGANISM  Corynebacterium pyruviciproducens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Corynebacterium pyruviciproducens"
                     /db_xref="taxon:598660"
     Protein         1..237
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25752
     Region          21..236
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(25..26,28..29,32..33,57,61..62,67..68,98,102,109,
                     112..113,118,133,137..138,140..142,144..145,148..149,
                     152..153,175..176,178..180,182..184,186..187,189..190,194,
                     197..198,203,205)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(136,140,143..144,146..147,189,192..193,195..200,
                     202..204,208,210)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(157..163,177,180..181,184)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mfeleaaaas srissvptae killlvgltf cavavnptvv avpliiaffw akpplklylp
       61 iigfnavfvg vgmiplvwnl tssgivavpg gfsnaafvww rcvvaasgtl lfacttplsd
      121 iiswarrvhi ptsltyvvqi myrmvgalwq tfvgmreaaa qrlsertfrt rmhstgliga
      181 slfvvafmra rlmqealelr adplevktfh syvparparl vaialflvat fcvgyvl
//
LOCUS       WP_284841074             355 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium simulans].
ACCESSION   WP_284841074
VERSION     WP_284841074.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium simulans
  ORGANISM  Corynebacterium simulans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Corynebacterium simulans"
                     /db_xref="taxon:146827"
     Protein         1..355
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35945
     Region          55..351
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mlalprkada ihgaagarhg geaaaldsrg rsrallttal vvstlllllc slvvgsrtip
       61 fpdlfaallh ggeadieniv wdlriprtfv ayfagaaiav sgviaqswtr npladpgfig
      121 itagasflva lgttlgiats tgmrtalall gaglatalvl gvsrrfqdpl tlvlvgagva
      181 aalsssamli glystdvlds mrrwtigstf grgpedvaia gaglfigfii aarvarpldl
      241 lamgeessva lggspalarr gaalsivvla gcataatgpi afvgfaiphl lrrftgpevt
      301 amiapaallg gcsvlaadil grliagpsel emsivlafvg apfliwavhr gertl
//
LOCUS       WP_284841240             348 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium simulans].
ACCESSION   WP_284841240
VERSION     WP_284841240.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium simulans
  ORGANISM  Corynebacterium simulans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Corynebacterium simulans"
                     /db_xref="taxon:146827"
     Protein         1..348
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35917
     Region          14..344
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mshliqrggl pkgqwrvgtg kysvivhfrs wgvclacsil llalslvalr vgttsygfad
       61 lwevlsggge krarlvivew rlprilagiv vgallgmsgv vfqtitrnpl gspdiigfsm
      121 gaqtgilvsv lvfggsiigs sfaamvggtl agavifalss kggfggvrli lagialsaml
      181 gslnrwlllq adsdaaygaa raitgtltav ewkevtvala aggvvmllll caqrqlhlla
      241 lgeqrastlg mrvnterawl vilatlmvai atttagpiaf iallaphisk qltgcntpvv
      301 paaaagttll lgadvmgqvw aselpvgvit aavggfyffg lllrketr
//
LOCUS       WP_284841283             336 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium
            simulans].
ACCESSION   WP_284841283
VERSION     WP_284841283.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium simulans
  ORGANISM  Corynebacterium simulans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Corynebacterium simulans"
                     /db_xref="taxon:146827"
     Protein         1..336
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36076
     Region          29..335
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mnfsigklai gflvtalmas slvlvgphri alateatgst dlaqklrdna qrghhnltaf
       61 tlangetsfa glgadehtev eigsvtkmft aelirqevse gnlkydarvg qfldtgdspi
      121 sdvrieelme htsglprlaa tnpftgistm ltggnpyane tktqlidaat ssdlagrgee
      181 nysnlgygll glileeasgk pfeqllqeki fapigmhety lmtpgsvpfd aprgytsrgq
      241 raqpwefpas gaaggirstp kdmslfanwl iehgdfqhgw qdneapvpag ywhnggtygy
      301 stmliidpqs skvafvsndt ekgteelart ifgeld
//
LOCUS       WP_284841330             334 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Corynebacterium simulans].
ACCESSION   WP_284841330
VERSION     WP_284841330.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium simulans
  ORGANISM  Corynebacterium simulans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Corynebacterium simulans"
                     /db_xref="taxon:146827"
     Protein         1..334
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=35891
     Region          12..302
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mnsgnkvstf freatpaika qrliamillv cqggitvsga ivrvtgsglg citwpechpg
       61 slvplsgaap wihqliefgn rlltfvvtaa avaaimamhm arrrtelkvy awlnlagivv
      121 qaiigaisvf lklnwwaval hflpsmilvw laamlysril epddgvrtqi fsqairvlaa
      181 masialavvl ttgtmvtgsg vhsgddgvgm egrlnvdtem mavahamcmy ayliltvivi
      241 fmlyrvhapa fvkkaawvli aciliqwgig vaqfymhipr wtvpihigms svvtaftall
      301 wahgvrring teglntgspa aeekfaarqa alak
//
LOCUS       WP_284841284             173 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium simulans].
ACCESSION   WP_284841284
VERSION     WP_284841284.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium simulans
  ORGANISM  Corynebacterium simulans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 173)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 173)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 173)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Corynebacterium simulans"
                     /db_xref="taxon:146827"
     Protein         1..173
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19013
     Region          89..169
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdsktsarql earltalear vealeeqnsa apppaptsds rywlvealee gpdipdgsvi
       61 fggditignr eykyqwqrpt qfvtdeswee nikrltaiah ptraeilrrl lcapasandl
      121 vqeglvsstg ttyhhlnels sagwiaksks gtfeirptrv iplmtiitat eah
//
LOCUS       WP_284841525             447 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Corynebacterium
            simulans].
ACCESSION   WP_284841525
VERSION     WP_284841525.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium simulans
  ORGANISM  Corynebacterium simulans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Corynebacterium simulans"
                     /db_xref="taxon:146827"
     Protein         1..447
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=47438
     Region          5..242
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
     Region          <257..>330
                     /region_name="PknB_PASTA_kin"
                     /note="Stk1 family PASTA domain-containing Ser/Thr kinase;
                     NF033483"
                     /db_xref="CDD:468045"
ORIGIN      
        1 mtlslkftai tdrglvrqnn edsahagphl llladgmggh aagevasqlm vehlehldqd
       61 pedndmlall gaaaedanas isahveqhpe tegmgttlta mmfngtefgv chvgdsrgyr
      121 lrdgkltqvt rddtyvqslv degrldpedv sshpqkslil kaytgrpvdp tlfmldakvg
      181 drlllcsdgl sdpvtaatie lalsqgtldd aavtlrdlal rsggpdnvti vlaevvegkg
      241 dsspvkvgai agvvpepthp dssasraaal trpreaspap qeeeddteep hspkkkvgwk
      301 vigalvvvla lvigggfwtk neisnnfyva tdeegalsie qgvdfsvfgr slhhkyqnac
      361 vdkantlrlg stpcegdfap fkvtdlpdse raavdnlpsg syaevqtqls nlsskalkpc
      421 istpskktde klekktakpg itcrevs
//
LOCUS       WP_284841560             229 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Corynebacterium simulans].
ACCESSION   WP_284841560
VERSION     WP_284841560.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium simulans
  ORGANISM  Corynebacterium simulans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Corynebacterium simulans"
                     /db_xref="taxon:146827"
     Protein         1..229
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=25021
     Region          1..221
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mlfdvsrpav qvapgvahlp gwlsvssqea lvsavrevar ayagtpmamy rprlksgqms
       61 vhqlhlgrfw ryetyryvdn iegtrvppml eslrelaspa lraaaevape lapwaesfvp
      121 emalvnyypp gsgmgmhvdd feeslapvis lsigdealfr mgntenrnkp wddvllgsgd
      181 livfggpkrl ayhgvvrvnd atlpegcglr egrinitirq vdaraslcc
//
LOCUS       WP_284841717             937 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium simulans].
ACCESSION   WP_284841717
VERSION     WP_284841717.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium simulans
  ORGANISM  Corynebacterium simulans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 937)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Corynebacterium simulans"
                     /db_xref="taxon:146827"
     Protein         1..937
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103360
     Region          5..935
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtsmhldtfr aelshplddf qvegcraved ghgvlvcapt gagktivgef avslalsrgt
       61 rcfyttpika lsnqkyhdlv aahgedavgl ltgdvsinsg aeilvmttev lrnmiyaesg
      121 alerlshvvm deihfladas rgavweevil nldesvsiig lsatvsnsee fgewlstvrg
      181 dttvivsehr pvpldqwmmi grkvyplfep etggqvnael arrirrleag dsddgktagn
      241 dragfrsrar hkggghgggr dkrgrsgnar sqdryrplgr petlqvlqgm dmlpaitfif
      301 sragcdgaly qclrsrmvlt tqeeseeika iidagvegip eedlqvldfk rwrealsrgf
      361 aahhagmlpa frhiveelfv kglvravfat etlalginmp artvvlekli kfngeahvdl
      421 tpgqytqltg ragrrgidti gnavvqwapa mdphavagla strtyplist ftpgynmain
      481 llgmlgfees lrlleksfaq fqadgsvvee trevekaehr vrelrnqldd aidalappar
      541 dgedpaevlm dyirlrrklt eeekaahann taqrnqevav vlarlqvgev iaiagkkrpi
      601 lavvvtpanq aadprpwvtt etgwsgrida sginnppivv grmklprpvq knprrntkfv
      661 qdsfkrnhyd rpkkmrlepr nrpnkkvgql rdairqhpah awpatdreql aglaqklarr
      721 erdlekvnar ieratdtlgk tfsrivdlls emdyvefegl gaertpvitd egerlaqihs
      781 esdllvaqcl krgiwneldp aelagvaslc vfenrketrg epeaatkama dameatyriy
      841 teliadearh nlprtrepea gfalaihqwa agaplgycma aaneagaelt pgdfvrwcrq
      901 vvdmlqqiak tgyeedirrn arramdaiqr gvvaiga
//
LOCUS       WP_284841936             108 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium simulans].
ACCESSION   WP_284841936
VERSION     WP_284841936.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium simulans
  ORGANISM  Corynebacterium simulans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Corynebacterium simulans"
                     /db_xref="taxon:146827"
     Protein         1..108
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11972
     Region          10..95
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msprdyhhpe tdeitlarvl aalsdptrle mirrladgle hdsleladdl prstltyhtr
       61 mlreagvtwt rgegraclir lrgedldrlf pgvlaavvan adpregqa
//
LOCUS       WP_284841949             267 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium
            simulans].
ACCESSION   WP_284841949
VERSION     WP_284841949.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium simulans
  ORGANISM  Corynebacterium simulans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Corynebacterium simulans"
                     /db_xref="taxon:146827"
     Protein         1..267
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28813
     Region          7..262
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msefskisew padniagall yrgeivesvg aldrafsvas vtkpvvaygi amaveegavd
       61 ldmpagpegs tlrhllahas gvkfdsreqq kpvgerriys svgyewvaev vekatempfp
      121 eylregvfap lgmgstrleg saghglvttv sdlaaftaev dspqllhpgt vaemrrvqfp
      181 glrgivpgyg sfkdctwglg feihgekqqw mgalpcsavg hfgmsgtylw lagdwamval
      241 tdrdfgdwak plwaeantai wkecqvr
//
LOCUS       WP_284841950             568 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Corynebacterium simulans].
ACCESSION   WP_284841950
VERSION     WP_284841950.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium simulans
  ORGANISM  Corynebacterium simulans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Corynebacterium simulans"
                     /db_xref="taxon:146827"
     Protein         1..568
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62700
     Region          19..550
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mnifprnnsq kdapasrgfn rrrflqtssv asaaaltagg lspanaqssl pgnkrqliep
       61 pkgelpflhg vasgdpipds vilwtrvtas peampgsgvg pdvtleweva tdeemrdvvk
      121 rgsvvataer dhtvnvdphg lnpettyffr frvtdgehag kaspvgrtkt apaanaspeq
      181 ltfgvgscan wesgffsayt diakraragq ldymiflgdy iyeygvgkys gfgpvrhhhp
      241 aheivslqdy rvrfgryrtd pelqaahgal pwivvwddhe tannswagga enhdpategd
      301 wnsrragamq ayfewmpvrm tnpsqdghiy rsltfgdlve ltmmdlrtyr dkelswdpag
      361 fakedrtmlg seqyewllgk letsqtawnm lsnsvmfspl nlitlqqdpq tekvssalss
      421 nitgipvngd qwdgysaerr rviealaakg sqalfvtgdi htewahnith qgniigaelv
      481 casvtapnin eqlklpqnna lsdaaehilr sanphckhvd ldnhgysfvt vrreeaemhw
      541 lrvddiltpg spvrdsltmt wrkgqgfk
//
LOCUS       WP_284841991             270 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium simulans].
ACCESSION   WP_284841991
VERSION     WP_284841991.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium simulans
  ORGANISM  Corynebacterium simulans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Corynebacterium simulans"
                     /db_xref="taxon:146827"
     Protein         1..270
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28906
     Region          5..265
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mreviadpld prlddvrdln ksdkkgeglv iaeghlvvsr ladsrfplrc vvgfgaklda
       61 yveeygdpgc pmyevsretl aavagfdmhr glvaaadrap epsldeilkt astvvvlegv
      121 gdhenigaif rnaagmdvda vllgsgaadp lyrrsvrvsm ghvlrlpfvh ldggyttwqr
      181 slqalrdadf rlvsltphpe avhladalrg askaallvga egpglteham katdvrarip
      241 mapgtdslnv atsaaiafye rqrsridfev
//
LOCUS       WP_284842048             462 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Corynebacterium pyruviciproducens].
ACCESSION   WP_284842048
VERSION     WP_284842048.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pyruviciproducens
  ORGANISM  Corynebacterium pyruviciproducens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 462)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Corynebacterium pyruviciproducens"
                     /db_xref="taxon:598660"
     Protein         1..462
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=50343
     Region          40..459
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mtsnpvtfnp rvpelatqfi gtifndydpr syapgadflt rqedrqqvsp taipavgrpl
       61 aeatkelvdv lehdsnlrhp rffgfipgpa qsvswlgdvi ataynphasn waqspgasal
      121 ekqvidwace aagisspnrg gilvsggsma nltglmaare srvpldqipr avvytteqth
      181 ssvnkalhil gishirtlpv dselrmqpav lreaiekdke egllpfavvg tcgttntgai
      241 dpldaiadlc defdlwfhvd gayggsvvls srkadargve rcdsmawdgh kwlfqtygla
      301 mvlvknradl vrsfsaggey lqdveggshn pdwwdmgpel trparaprlw ltlqtvgter
      361 lsqmidssis vaelfekeiq svegisivtp achaivtftt gdeaknvala eylrrhniag
      421 iwtttlngkn vlrlctispd eteedmealv kdiekalkki ql
//
LOCUS       WP_284842049             515 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Corynebacterium pyruviciproducens].
ACCESSION   WP_284842049
VERSION     WP_284842049.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pyruviciproducens
  ORGANISM  Corynebacterium pyruviciproducens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Corynebacterium pyruviciproducens"
                     /db_xref="taxon:598660"
     Protein         1..515
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=55347
     Region          43..316
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(91,94,171..177,206,230..235,266,292..296,298)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mrvmalwfpd wpihaadlag apaavtdnge vwvanaaara rgvrrgmrlr aaqalvpglr
       61 svprdvdrda rvfesivagl ddvvstievy rpglvvvdmr aaakfhgsee aaaeklldaa
      121 acrgvdcygg iadevttafi aaraeaivpp gasrkflaaq pvsmlaaeea lhcdpevvqk
      181 fadlgvrtlg elaalpstai ttrfgiagar chaiaradpg rkvssavpmp elavtmvped
      241 pisrvdaaaf aarhlaarlh erlaragltc vrlkvtavmv ggetvervwh treelnedtt
      301 adrvrwqldg wltarttqae vggiieftlt plechppdsa glwnsgnakk qqarraamrl
      361 qstlgtdkvl vpvasggrsp vecvelvpfg eqraparpve gpwlgqipap yparrgggen
      421 hpasrlqivd kqgtgveidg eaqltgepfa lawgekryev tawagpwpvd grwwegdgag
      481 rarmqvvgre vrtnrqhawl ivwshgrwsi eavyg
//
LOCUS       WP_284842298             288 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Corynebacterium
            pyruviciproducens].
ACCESSION   WP_284842298
VERSION     WP_284842298.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pyruviciproducens
  ORGANISM  Corynebacterium pyruviciproducens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Corynebacterium pyruviciproducens"
                     /db_xref="taxon:598660"
     Protein         1..288
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30362
     Region          1..265
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(33,228,231)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(180,199,226,229..230,233)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mitvygegli dlvprspapl aplvpalggg pfnvaracgr lgcttrfvsr lssdgfgqkl
       61 vdaleeagvd tsqvlrghqp ttlavtsiae dgsasyqfyv dgtadrfaep epategfasf
      121 gtvslalepa asryaeacat sdkngvvccl dpnirtiynt pehreflgim lphitvlkms
      181 ddevdfmgdv tevpvvittr ggeglsirap fgeltvtapk vevadtigag dtvmaallae
      241 ferldldrdk llalgeaewr eilgfaaraa avtvtrtgad tptrdevr
//
LOCUS       WP_284842253             126 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium
            pyruviciproducens].
ACCESSION   WP_284842253
VERSION     WP_284842253.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pyruviciproducens
  ORGANISM  Corynebacterium pyruviciproducens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 126)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 126)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 126)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Corynebacterium pyruviciproducens"
                     /db_xref="taxon:598660"
     Protein         1..126
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13585
     Region          48..113
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msndhsaprv hnvmpdssgr felvdattvl shtpiteaqq ssvlstvral dsplrltivl
       61 lltqgekrvh elvketgasq plvsqhlkvl kesglvtshr vgrekvysls sdkpsiiila
      121 clqqgl
//
LOCUS       WP_284842435             160 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Corynebacterium pyruviciproducens].
ACCESSION   WP_284842435
VERSION     WP_284842435.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pyruviciproducens
  ORGANISM  Corynebacterium pyruviciproducens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Corynebacterium pyruviciproducens"
                     /db_xref="taxon:598660"
     Protein         1..160
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16772
     Region          <1..47
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mlahtgaekv tivghsqcgg ilpiyyitel ggdkkvdhlv gfapsnngtt vggmfdasaa
       61 asgivgfvag tasqqqivgs elvnevyksg pvprpgvkyt fiasetdktv tpytnsfvde
      121 pgvvnvtaqd hhpglvtdhn nmtyyeqvid lakkalnhkl
//
LOCUS       WP_284842453             214 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium pyruviciproducens].
ACCESSION   WP_284842453
VERSION     WP_284842453.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pyruviciproducens
  ORGANISM  Corynebacterium pyruviciproducens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Corynebacterium pyruviciproducens"
                     /db_xref="taxon:598660"
     Protein         1..214
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=24597
     Region          4..>161
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; cl21495"
                     /db_xref="CDD:473885"
     Region          39..>157
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; cl46765"
                     /db_xref="CDD:481105"
ORIGIN      
        1 mftlhslvfl qvypfhksal fatihrfipm qlgstrgtff filsgfliyw snshirtgte
       61 vrhyllrrvt kiypthllal vlfvvpsatf tahgvklvld fsrlalwlpn alllhtwrpa
      121 watlggmntp swslvsemlf ylsfplfvpl frrirgrgnw vgrtefpigy gatkviaegc
      181 vaptdhirgr gghlwwyqpn taeeiwaflr vqhr
//
LOCUS       WP_284842518             331 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pyruviciproducens].
ACCESSION   WP_284842518
VERSION     WP_284842518.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pyruviciproducens
  ORGANISM  Corynebacterium pyruviciproducens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Corynebacterium pyruviciproducens"
                     /db_xref="taxon:598660"
     Protein         1..331
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33205
     Region          23..324
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mrkrnvlivv vtavalliga vaatssgalg isfgalvdhv vgraplgard lavvtqirlp
       61 rvvlaiivga tlavsgavfq tlfhnpladp yflgvssgas lgvtvamvag assagvipaa
      121 fvgglaavgi aylvgtragg qptvvilagv avsalanaiq sytqvrgink lenvyvwllg
      181 nlgrsdwgki avimcvvvpc wavilaaakt ldvlmlgese arsigvnvvv aqavliavat
      241 lataaavsvs gligfvgivv phvlrllvgp ghklllpltl ivgggfllaa dtlarslvap
      301 qelpvgvvta fvgapfflfl lvrstrsgar s
//
LOCUS       WP_284842568             215 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium
            pyruviciproducens].
ACCESSION   WP_284842568
VERSION     WP_284842568.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pyruviciproducens
  ORGANISM  Corynebacterium pyruviciproducens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13031065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Corynebacterium pyruviciproducens"
                     /db_xref="taxon:598660"
     Protein         1..215
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23928
     Region          66..204
                     /region_name="SpoU-like"
                     /note="SAM-dependent rRNA or tRNA methylase related to
                     SpoU; cd18096"
                     /db_xref="CDD:349969"
     Site            order(139,141,161..164,167,181..182,184,190..191,193,196)
                     /site_type="other"
                     /note="putative SAM binding site [chemical binding]"
                     /db_xref="CDD:349969"
ORIGIN      
        1 mdslkgptew gegrhgvgpw egpyptdpry dpellregdh rnvvdayryw kreaivadid
       61 trrhplhiai enfendanig tvvrtanafa vdtvhvvgrr rwnrrgamvt dryqhlmhhd
      121 tvedlvewtr gqelslvaid nipgsvplet atlperclll fgqegpgvta eaqhaatmtl
      181 siaqfgstrs inagvaagia mhawirqhad lskaw
//
LOCUS       WP_284842596             446 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium
            pyruviciproducens].
ACCESSION   WP_284842596
VERSION     WP_284842596.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pyruviciproducens
  ORGANISM  Corynebacterium pyruviciproducens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Corynebacterium pyruviciproducens"
                     /db_xref="taxon:598660"
     Protein         1..446
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=47401
     Region          1..445
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mkmtvigtgy lgathaacma elghevlgvd vdeskisala agrvpfyepg lpeilsrgid
       61 sgrlnfttsy eeaanfahvh flgvgtpqth gsyaadlryv havidtlvpl lrgehiifgk
      121 stvpvgtaae lqkrvdslvh dgpdgdggtr veivwnpefl regfavkdtl spdrivlgta
      181 tpdspaidva reiyarplae gtplvltnlp taelvkvsan sflatkisfi navseicelt
      241 gadvtklaea igyddrigkk flraglgfgg gclpkdiraf maragelgas ealsflrevd
      301 tinmgrrehv vtlskklldg sllgknvtvl gaafkpnsdd vrdspalsva gslslkgasv
      361 tvydpqamgn aakvfptldy apdvltaltg adlvilatew defrnmdpek agelvkqcli
      421 ldarnvlpid dwtqkgwrvq alghge
//
LOCUS       WP_284842604             215 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Corynebacterium
            pyruviciproducens].
ACCESSION   WP_284842604
VERSION     WP_284842604.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pyruviciproducens
  ORGANISM  Corynebacterium pyruviciproducens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Corynebacterium pyruviciproducens"
                     /db_xref="taxon:598660"
     Protein         1..215
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23126
     Region          17..167
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mptwkeitdr npqhsanyaq rwdriaaegk gifgearlvd alvdrksril dagcgqgrig
       61 gylaqrghtv tgvdidpyli giarsrhpea rwqvgdlvge glprgpfdai vsagnvltfl
      121 epgtqvtaws nlaavlapgg riaagfgldr gysleqcqad ieeaglttsl llsswdirpf
      181 trgestfavv iaqraghdrp raktatidlg rlrkl
//
LOCUS       WP_284842740             336 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium pyruviciproducens].
ACCESSION   WP_284842740
VERSION     WP_284842740.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pyruviciproducens
  ORGANISM  Corynebacterium pyruviciproducens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Corynebacterium pyruviciproducens"
                     /db_xref="taxon:598660"
     Protein         1..336
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=37772
     Region          1..325
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mnrsyipald alravsalgi mtthvafqtg tpgfdrfdyf vavffalsgf llwwrypsfs
       61 tpwgryarnr fgrivpayla vvvisfvafn sagvnallan lffvqlyvpg almtglthlw
      121 tmcvevafyi ifpflreilg rvprpwriai iilialaslg waylplnfea nsqifppayc
      181 swyavgilla elhsaervrs trfpwwiwpp iaiaalvagt clgpaglthp tptefairif
      241 fgavfalall ypvvdwqprv pdwlaflgri sysiflwhlp vltalyaltt itlfsghfll
      301 vwlltfafti pvsyvsyewt ekpfhtgaat hsrdal
//
LOCUS       WP_284842791             983 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Corynebacterium
            pyruviciproducens].
ACCESSION   WP_284842791
VERSION     WP_284842791.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pyruviciproducens
  ORGANISM  Corynebacterium pyruviciproducens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..983
                     /organism="Corynebacterium pyruviciproducens"
                     /db_xref="taxon:598660"
     Protein         1..983
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=105214
     Region          152..296
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <335..474
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <455..930
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 mtvrnssanr rkkaetgpst rrpagdsrth prssafraad tagertgsat ratakgvstl
       61 lsavahgsan ivrsiaspkp npeefeeddf wneeddfald eeepqrpprr lrrrknspep
      121 veeadttptp ergdpapras ardseptpss dgialtllgl avvlaaavwf nlagpvgewi
      181 svgvgsviga arwllpialv alawilfsgk qvtferrkei alggtiivac vlgilhifag
      241 lpgdwpgrie aggavglivg qplalgfsry iampllilav iygavvatgt tvkdfatelw
      301 nylgfgsagg gdlsaedddl ygdasdeida laenrplprr serardvrpp lpqrgsrght
      361 tpsprrlfta spepepetta petaampavp tgetaaaaap epqpepeprr apkpqpaper
      421 rqatpkaasv seedtdeede sapamdmvss hanyvlpsts llipgkppka rsaandriid
      481 aidevfrefk vgaqvtgfsr gptvtryeve lapgvkvski tnlqadlaya vatdnvrlla
      541 pipgksavgi evpnsdremv rlsdvlnapa vqqnddplvi glgkdiegnf vshsiqkmph
      601 llvagstgsg ksafvnsmlv slltratpdq vrlilvdpkm veltpyegip hlitpiitqp
      661 kkasaalqwl veemeqryld mkaarvrhik dynkkvlsge iqapvgsere yrpypsivcv
      721 vdeladlmmt apkeiedsiv ritqkaraag ihlvlatqrp svdvvtglik tnvpsrlafa
      781 tssltdsrvi ldqggaekli gmgdglfipq gagrprriqg afvtdeeiqa vvdaakqqae
      841 peyaegvtee kepekkaide eigkdmddll eainlvvtsq lgstsmlqrk mrigfakagr
      901 lmdlmesrei vgpsvgskar dvlvkpeeld tviwlvkgad patapkevae edtvdgevvs
      961 eevataapqt ttvevarptn gvf
//
LOCUS       WP_284842855             305 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284842855
VERSION     WP_284842855.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..305
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34479
     Region          7..238
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mnhprptlwa vadlhaavra nrlrldeitp rhpddwllva gdvaerldli stvlselrsr
       61 faqviwvpgn helfsrstda hrgrakydal vqicrsidvl tpedtfpvfg dttvvplftl
      121 ydysfrpagt gveealelaa qknvvmtdei aiapfadira wcwdrlaysi trlsrvngpt
      181 vlvnhwplvq eptlrmalpe lalwcgsrht rtwpqrynak avvyghlhmp aifeldgveh
      241 hevslgypre wgrsdqnriw pcpvlelvad pnggqiaqrv gleqcreshp elrmprrrgk
      301 gsdgv
//
LOCUS       WP_284842863             233 aa            linear   BCT 25-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284842863
VERSION     WP_284842863.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..233
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25571
     Region          3..232
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 msqrtnaatl aangiteyik rnqlhpgdpl pteanlceal nlsrssvrea vrtlssldiv
       61 evrhghgtfv gslslspliq glvlrttids ensfqhlrdv vevrigldls madelcaaft
      121 addathllel vqamhekhsa gqsfaeedha yhrrlhslia nnlirelsda fwqihmdvlp
      181 lmevqmpgdi ektieahaai vhaleagdaq lyrekvlahy splqraiaav qap
//
LOCUS       WP_284842925             153 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284842925
VERSION     WP_284842925.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..153
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16821
     Region          15..85
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mveyhrwywt syghalannl rslremrgls qarlaqlsgl srnlisnler nesgakaadp
       61 vlstvyklaq ilyvppgvll pgvdeviagp cvattphlqg rwpvaehdta pfspvylara
      121 vtdelpefaa peplgtaeim ppkrspgerr rkr
//
LOCUS       WP_284843052             232 aa            linear   BCT 25-DEC-2024
DEFINITION  phosphate signaling complex PhoU family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284843052
VERSION     WP_284843052.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Baek,S. and Lee,E.J.
  TITLE     PhoU: a multifaceted regulator in microbial signaling and
            homeostasis
  JOURNAL   Curr Opin Microbiol 77, 102401 (2024)
   PUBMED   37988810
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Gardner,S.G., Johns,K.D., Tanner,R. and McCleary,W.R.
  TITLE     The PhoU protein from Escherichia coli interacts with PhoR, PstB,
            and metals to form a phosphate-signaling complex at the membrane
  JOURNAL   J Bacteriol 196 (9), 1741-1752 (2014)
   PUBMED   24563032
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Lamarche,M.G., Wanner,B.L., Crepin,S. and Harel,J.
  TITLE     The phosphate regulon and bacterial virulence: a regulatory network
            connecting phosphate homeostasis and pathogenesis
  JOURNAL   FEMS Microbiol Rev 32 (3), 461-473 (2008)
   PUBMED   18248418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431170
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..232
                     /product="phosphate signaling complex PhoU family protein"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_process="GO:0006793 - phosphorus metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006817 - phosphate ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0030643 - intracellular phosphate ion
                     homeostasis [Evidence IEA]"
                     /GO_process="GO:2000185 - regulation of phosphate
                     transmembrane transport [Evidence IEA]"
                     /calculated_mol_wt=25356
     Region          9..217
                     /region_name="PhoU"
                     /note="Phosphate uptake regulator PhoU [Inorganic ion
                     transport and metabolism]; COG0704"
                     /db_xref="CDD:440468"
ORIGIN      
        1 mrtayrntld nfandivels ntvhqvmdla sqallaepea aqepatqava rteeldaire
       61 rsearafell alegpvasel rqvvssiyiv edftrmaala thiakavlrr fpervlpesv
      121 tadfaqlsel vddmaqqtta ilkdpaggia tamnddddav dklnaallal staddwahgs
      181 raavdvamla ryyeryadhc vnvyarivfl atgklpegfl ssqfhrsqfv id
//
LOCUS       WP_284843139             962 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284843139
VERSION     WP_284843139.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 962)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 962)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..962
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..962
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=109236
     Region          <40..588
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
     Region          <829..>957
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
ORIGIN      
        1 mdkgrsnltd hqakyfahql ersysndhvg klagllfdaq vepkphqida alfalqtpya
       61 kgiiladevg lgktieagiv atqywaerkr riliiapasl rqqwkqelwe kfmlpaelle
      121 rknlgellsp kaannpcili csyefagany drlsrrwdlv iadeahrlrn fwngkaktae
      181 avahifqasa kvvlltatpl qnrleelygl vstfdpsyfh sldafreryi khtsldsgdd
      241 ladrvalisk rtlrkdaeky ipftqriplt iefdsspeeq klyelvddyl srdklwafts
      301 sqrflsamil rkrlgsstya iastleniad rlqaqltgrn ftytdthsgl fdaelddlts
      361 eevqiaadal pynrdeltea ekrtaiaqel eelrgfaala rsikvnqkav hlkealdqgf
      421 aklrevgape kaiiftdsti tqqylaehlt sigyggglvl fngsnkseas teiyrqwlea
      481 nngsdlitrn aaadrrkalv dyfrdhgsim iateaasegv nlqfasmlin ydlpwnpqrv
      541 eqrigrihrf gqkynvvian fsnrsntaeq rilellsekf klfssvfgas deilgsiedg
      601 ldverkindi ladyktaeei saafdqlase yateistems kakskvfdnl dphvqdrlkn
      661 ydaqsevvln qferlllelt kyelkefadf ddaghnfhlh hapvpsalvg dyyfkstpip
      721 nahqyryasp lsqfvinral ttetpdasfi fslnkservp kaiqklsgqs gelvvkkitf
      781 rinageqdls esyllaaatt dsgeildaef vddilnltav eshdcddidq arfddvlqeq
      841 aatydkevkn rnsryyneqd dvlqssledr raehekqire wkakvdeyrk qarhaddame
      901 slslkkkanr leekiddadd efrtlrrkmr qqsndyldsv aqalkgseeq epvlalrwei
      961 qn
//
LOCUS       WP_284843167             535 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284843167
VERSION     WP_284843167.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..535
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=57467
     Region          35..473
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mtlrqdrpaq asatmpagav detsarnkrd arkpnalval lrrlhfyagm figpflliaa
       61 isgalyavap taeklvyqdv ltvtpppgae gvtntislek qvnnaheafp dldiaqvwps
      121 sepgettrvl lidetideae lrsvfvnpyt gavvgdepsy sglgelplrr wishlhesmh
      181 lgpvgelyse laaswlwffa lgglvlwasr nkkvqqlfgf akaragketk nggaqegkdv
      241 kdakegkkkg sgrrrlvnlh gvtgtwmlig mlalsvtgit wstyaggnvn rtvealqwra
      301 dpittelsge saaeadphae haghggggga eaeaearawt peeiaeqadq vlatareegl
      361 tgslrmypge svehgwqase rwtewrttsd aisvdgetge vidrlpfsel plfskltswg
      421 iylhmgimfg lplqilllvt alaiaglvvl gyliwwkrrp tpgatagipg prtklsttqw
      481 iivavflvav ggflplfgis laamlladvl lskraghtgh tghetrraav dgara
//
LOCUS       WP_284843172             259 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284843172
VERSION     WP_284843172.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..259
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26955
     Region          8..243
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mpipvklprt fsqqlqeesg pqvgawissg spvaaeivas agfdwllvdg ehspysletv
       61 tdllratday gatrvvrvpv gdtalikqyl dlgaqnlmvp mvdtaeqard avaamhyppr
      121 gvrgvgaala rssrwnaved ylqnasdlvs ltiqlesata vdnaaeiaav dgvdqlfigp
      181 sdlaasmgvl gqqthpdvld avsramkacq dagkpvgvna fnleqaqayl dagaafvlvg
      241 advqllagaa rgladkfar
//
LOCUS       WP_284843195             517 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284843195
VERSION     WP_284843195.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..517
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54632
     Region          17..514
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mssgfarssf ahnggarvav igagpnglta aavlaqagcr vevfesaddi ggsartspaf
       61 gagsavdfga aahpfgavsp vfrqlgleny glewkhpqyp mahplvdapa vilhrdlgtt
      121 aaqfsdhder vwnhlhkplv ddvgklvnsv lpvrprypla larlglrgvw parsltsrll
      181 vdesarallv gsavhairpp sqpgtaafgl lfnslgmttg wpvvsggtgq lvmalarvik
      241 hnggiiktga evqdlsafat ydavvttqtp rqllalqgle lsrlrsrslr rwkygtavyk
      301 vdylvngpvr wndprvagag tvhvggtvse mqlaesqaaa gtlperpfvm vcqqqaadpt
      361 rfsgnrrsvg agrvlsaqld agripedarl philwayahv phgyqekfpg evaglietqi
      421 sryasgfsaq iierhqaspg qlqeananli ggdiaggamn laqmlrqrqy vgtltmnpev
      481 pvvqasgasl pgagvhgmag wraaqtilrr fgatelr
//
LOCUS       WP_284843296             311 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284843296
VERSION     WP_284843296.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..311
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32985
     Region          18..310
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mlepqvpqvi tladaqvddp rladirqlnh prlrpdrqpr leldssgdyi pasrpsvila
       61 dgalpiarmc gtdsavapaa ifgrteklqk fatdypeqws riaqlgipvy elpaallrdv
      121 vgfelhrgll avalrpdsve lgtksaeevl apartivvle gvgdpeniga iyrsaaslga
      181 dalvfgagcg dlwdrrvirv smgqalrvps mripggftnw hhgladlrnq gfyvtalspg
      241 aqavqlrdal vgpsgnrrek valllgaegp gltphamnaa dacavipmaa gadslnvavt
      301 aacclyerwr g
//
LOCUS       WP_284843439             481 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284843439
VERSION     WP_284843439.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..481
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=50656
     Region          8..454
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 maddsfadsl qnildgidkf iwsqwflipl llftglwlti rlrgvqfrkl gvalrhgfid
       61 rndaagagdi tqyqalttal aatvgvgniv gvataisigg pgalfwmwit gllgmaskys
      121 eaflgvrfrv adahgkvsgg pqrylsqgip srlgkflawf ftisaiiasf gignltqgna
      181 vaaglestfa vsptvtgvim fvligavllg gigsigkvts afvplmiiiy ltggiivlam
      241 haseipaafa mifndaftgt satggflgag iilamqmgva rgifsnesgm gsaaiaaaaa
      301 ktthpvrqgl vsmtqtfidt ivvvtmtglv ivttgvweag qnnaanmtaa afsegigsdw
      361 ggtivslsvv ffafstilgw syygersaer afgawasipy rmvftcviyi gatteislaw
      421 tfadianglm aipnliglli lsglvaretk ayldfdptlr aqprdiekfl itsknpwrsk
      481 f
//
LOCUS       WP_284843495             189 aa            linear   BCT 25-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284843495
VERSION     WP_284843495.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..189
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21476
     Region          11..159
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpvvseneln rrrqeilvga rkcfaeygye gatvrrleqa tgksrgaifh hfsdkenlfl
       61 alaredaarq aevvareglv evmrdtirnp ekydwlatrl eiskmlrtda sfrarweehq
      121 avldqavhdr laknaaegrm rvdvpidtlq yflemvmdgl itrnamgmat deavldiaeq
      181 airrdgndv
//
LOCUS       WP_284843588             309 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284843588
VERSION     WP_284843588.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..309
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31767
     Region          2..289
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 massanpisv lciigscisl qlgsalavkl fddggtwgts avrllvaavv llaitrprvh
       61 ewnrqqwagv lglglslglm ngffyagidl vplgpavtie flgplllaaf lsrslrdgic
      121 vilamtgmal lgldafngnp lnplgvafll gaalfwaiyi lanknagalv pgqgglavaf
      181 ivggvamlpm gaggawnlvt stdtlwfaig tgilgslvpy slelialrgl apnvfsilis
      241 lepvfaaffg wlllaqnist lklvaigvvi aasvvqtvgt ggsgadgapr sklkklqdvg
      301 rkvvprrrq
//
LOCUS       WP_284843573             254 aa            linear   BCT 25-DEC-2024
DEFINITION  phage antirepressor [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284843573
VERSION     WP_284843573.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..254
                     /product="phage antirepressor"
                     /calculated_mol_wt=28691
     Region          1..107
                     /region_name="COG3617"
                     /note="Prophage antirepressor [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442835"
     Region          146..238
                     /region_name="ANT"
                     /note="Phage antirepressor protein KilAC domain;
                     pfam03374"
                     /db_xref="CDD:460903"
ORIGIN      
        1 mattlqaftn hefgtirtit sagqilfcgr dvatalgyan tkdalarhck gvvnhyplet
       61 aggiqqvrfi segdlyrliv ssklpaaeqf eawvfddvlp sirrhgmyai dellnddefl
      121 eranatlrae rskrlaaeqa lleaapkvsy ydvvlaspsl ittteiakgy glsakklnqi
      181 lreeqvqfrq sgrwflyarf teqgytqskt heydkgktrt hmywtqtgrl fiydllkntr
      241 gllpviereg edar
//
LOCUS       WP_284843682             327 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284843682
VERSION     WP_284843682.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..327
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33867
     Region          22..326
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mrktwtiagi saatllialv gsltvgsssm sfseliglvv psqpspsalr tsiltelrip
       61 rilmaafvga ilavcgvamq tvthndlaep yllgvssgas tgaviailfs twqygiifga
      121 tvgslasfal lmlllrntgg datkvvltgv ligflfqslt slvvtasgda estrsimfwl
      181 lgvlgaarwp tlfaviivgs igmlmlwals rhldalslgg dtastmgvpv valryivlic
      241 vslmtattva svgaigfvgl iiphavrmln vpkhaslipl saligavtlv iadafarsif
      301 apqelpvgvi taligvpmff lilrrkh
//
LOCUS       WP_284843623             804 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284843623
VERSION     WP_284843623.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 804)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 804)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 804)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..804
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..804
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=86991
     Region          205..436
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 matprtafdi gpaagtdsaa gsasaadtas iehdahsahd arflptllrr irramgddsv
       61 elttlricca amavallvyl glqyvtygsn yigdwygyli siglalsgif mlasaivgkl
      121 vwlryslytn aivllvatla fpvayytmpd lgpavlrftd ftgvlaisvv llsptrravl
      181 vailiqvfps alhslvygrt sipellaitg favlmnlipf vlgavtlmrv artideteqk
      241 vqdslaeses khaaiaerkr lnglvhdhil gslsaiargq nmqadavrsl psrpatgedi
      301 tlqqlladvt csvqdltpnc sitingqdah ngssdlgfst ikdsaaeair lsvteaarns
      361 rkhagdscqr scainitdge lvfefsddgr gfdmatrnpq raginvsilh rmrsidggda
      421 qivsspdngt tvtvrwclrt aesqfnerma aqandfsedq ltaakleqql lqpaqvsrsw
      481 awpylilavi sivsavwvns geflmaipaa avaiatlall vldssphidg tkrfvftvgf
      541 lmlgplsmlq rvdyaagren lwalsiisll ccililrgqi lwgagcfvas aalmkactll
      601 tagaiasppl adilvqvnlv maatvvflat ntllknlprl rmekrtayae aarvrqiqlv
      661 hrhwheriel haapvfeavq hfqtpppllr erarltelai rdmlraplld rpeiktaawd
      721 arkagatvll lddrserdss tvgrksdgrd vgaalerlvp lvlerlnfag tdkvtirilp
      781 pgrkyfatit tdstgitrvp fpev
//
LOCUS       WP_284843832             320 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: DHH family phosphoesterase [unclassified
            Corynebacterium].
ACCESSION   WP_284843832
VERSION     WP_284843832.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..320
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=34432
     Region          7..319
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mtkkqyqpav aalhdahsic ivthlrpdad aigsaaalll alrqrgkdvc avvgqereis
       61 rnlytipaad dvttsrelpe gydlyvtvdc gsldrtgffa drieqlaqqg rvlcidhhss
      121 npgfgainvv dtecesttvv llsildslei qidrhiahcl yaglmtdtgs frwgrpamhd
      181 iatrlmhyel dtkqiaadll dsttpddlqm igrvlaglrl eeagehtlgi lvarlediqg
      241 hsdsaveslv efvralegtt vgvvfkeqap evwavslrss ridcssvalt fgggghvpaa
      301 gytahgapek iikelvaaiq
//
LOCUS       WP_284843833             270 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: metallophosphoesterase family protein [unclassified
            Corynebacterium].
ACCESSION   WP_284843833
VERSION     WP_284843833.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..270
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31184
     Region          3..237
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mptvwavsdl hgavnanser idqltppdpa dwlivagdva ertdliiril rqlndryarv
       61 iwvpgnhelf srsqdryqgr ekyahlverc reigvitped pypvfhgtti vplftlydys
      121 frphglsvde aidaarakql mmtdefaiap fvdvrawcwd rlaysikrls rvhgptvlvn
      181 hwplvqeptm llrfpeialw cgtrhtrswp rrynaesviy ghlhmpsrmn vdgvdhiets
      241 lgyprewqgr dstqawpypv lrsfegeear
//
LOCUS       WP_284843851             230 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: energy-coupling factor ABC transporter ATP-binding
            protein [unclassified Corynebacterium].
ACCESSION   WP_284843851
VERSION     WP_284843851.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..230
                     /product="energy-coupling factor ABC transporter
                     ATP-binding protein"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25647
     Region          4..226
                     /region_name="EcfA2"
                     /note="Energy-coupling factor transporter ATP-binding
                     protein EcfA2 [Inorganic ion transport and metabolism,
                     General function prediction only]; COG1122"
                     /db_xref="CDD:440739"
ORIGIN      
        1 mptidfssvs vafddtvvle dinltlteqr igiigqnggg kstltrling lgepsegtvt
       61 vdqmdvakqg kkvrekvgfv fsdaenqivm pnvrddvafs lrrfklpkhe rlarvdaale
      121 rfglaefaer sphtlsggqk qllalaavmv idpiliiade pttlldlrnr drikrefarl
      181 eqqlivvthd leflrdfdrv icidnhriaa dgrpaevidf yqdlmaqrpl
//
LOCUS       WP_284844040             382 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [unclassified Corynebacterium].
ACCESSION   WP_284844040
VERSION     WP_284844040.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..382
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41385
     Region          10..378
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mvttghphsl eglrvldmsr vlagpfcsmi ladlgaevik ietpwgddsr nfgpdfngds
       61 ayyrlfnrsk kgitlnlked sdlatlrelv kradvlvenf rpgvmeklgi speslmelnp
      121 qlivtsisgf gqtgsmskap aydlvaqams gimsitgwpg grptrvgisl gdlipglyga
      181 igtlgalqer hrtgcgqhvd vamfdslvsi lesvamrdly edevptavgs dhamtvpfst
      241 yrvddgevvi ailneklfgc ltralgleym vddpryhsna arkerreevr siiedalrgk
      301 tveqalalfq ehgvptapvh svdealhgev gterdvlfte sdgfttlssp lrltgsrspe
      361 papqlgehns lipewlaepa rg
//
LOCUS       WP_284844052             149 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: anti-sigma factor family protein [unclassified
            Corynebacterium].
ACCESSION   WP_284844052
VERSION     WP_284844052.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..149
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16276
     Region          46..>107
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mdslrgrrpv stlsvhggfd aaqakardka kakarrsdti ghlgpeavva fvdgemepkf
       61 mhrvrihlvh caecradvhq qrhasewvrh cadsakvkap qsllaklagi ateevapgpd
      121 aatpvhrpqq dfldkvemmv raikhnqrg
//
LOCUS       WP_284844225             415 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified
            Corynebacterium].
ACCESSION   WP_284844225
VERSION     WP_284844225.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..415
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=44384
     Region          143..411
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mvrtkwstag ivaacavanw lvgvvlmnld ieeysptfee ygpyictgfa vgvlgiialp
       61 falehqprel sdvdysgstr sfiagcivll gsssyfgavs gvvafismvs rrsttrsvaa
      121 vacfvvafai dasfnpylsw deigwvgaif vvvvmvagll vgqkrgnqre krwrveqqar
      181 mnreemrakv eharreeres iardmhdsls hrlslvaiha galsypregv peeftdaart
      241 iraeaqnave dlrtvlsalr edlsqdprtg leelvasare agaevtvaya dgaspdvfdg
      301 lstmaqhavh ravqegltna rkhapsqpvs itvreaagav diemgnpvpr gkagadtdgv
      361 eggaggyglv glrervelsg grmsiaanqe spggkggeef gwsiqlplah keatr
//
LOCUS       WP_284844248             610 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: AMP-dependent synthetase/ligase [unclassified
            Corynebacterium].
ACCESSION   WP_284844248
VERSION     WP_284844248.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..610
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66565
     Region          13..610
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mtlqevhtpa qftiepgetc ltalmdtakk rphgvmftrp anyewvnvtg kefidevfev
       61 aqglialgvq qgdrvalisa tryewslldf aiwaagaasv pvypsssasq vrwiiedsga
      121 vlaitetreh selvenlvlq edgepnlkgs psqlrrvlei nssaidtlkf egrgvaadev
      181 yarikatstd dlaslvytsg ttgrpkgcil thrnwlaqtr glctnpigif avpgshtltf
      241 lplahvfara vsiavamrga sqnhwsdfst isiefarsrp nvilgvprvf ekvrnsaaak
      301 aadsdiksll feqsekvaie yskaldkpeg pdrllkakhk vfdklvysti rngvggnvny
      361 citggsamgh dllhwyrgig ipvyegyglt evaaaaavdf vdqsigtvgp pmggvtfrin
      421 eegeicikgd ivfhgywnnp eataealedg wyntgdlgei dedgklvitg rkkdlivtag
      481 gknvspgpme dilrghplis qamvvgdgkp fvgvlltldp dilkrwkldh nipenrsmre
      541 latdptlrae lqdainqvna tvshaegikk fyilesdlte eeneltptmk vkrnvvsqry
      601 aaaiehlykr
//
LOCUS       WP_284844293             233 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NUDIX hydrolase [unclassified Corynebacterium].
ACCESSION   WP_284844293
VERSION     WP_284844293.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..233
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25751
     Region          47..201
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 msqllpertp dwlkpalgvd psqvqelign rqasslngtn vqvpvkreaa vlmllsgesa
       61 eeasillthr spsmrshsgq iafpggrrdp adtslvdtal reaweetdlq rnsvtpleqw
      121 dqlhiratgn pvspilahwt qpgevypasp detddvflvp irelvdprnr fmvgfrkwqg
      181 pafhangyvi wgftagvlsa llqhagwsvp wdnnsvmdlr dsltnsrnne kms
//
LOCUS       WP_284844466             548 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: metallophosphoesterase family protein [unclassified
            Corynebacterium].
ACCESSION   WP_284844466
VERSION     WP_284844466.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..548
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60604
     Region          267..>451
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mknklcafss vlaltgmvga pvaaaqsslp gssfgsslgs slgsswgssq gssegssagd
       61 dvqpgegtes rvlwqesfde vdtpawfthr apegwktdvq gvdsgearwk gwtfgdmrhw
      121 twaagtdmrh yftqahdtfa iidnkqqrla egdsmtaglk spaipvagqe rvnvefdhhy
      181 rqgkdgqnat vtvsfdgget qeiaafdkdv fskhesigvd vpagaknmqv sfsynngndd
      241 wwwavdnvgv vkplgelqgs pqatvdvlsd vqgdpqdykd avrqlngmed kagalvlngd
      301 lvddgsqqqw ddflaahsev phdsgkelwt ignhemygke gsetylerfl kysgqdkpwk
      361 eevvdgvpli svntefysdi lrhgkepfqr iskeqldwld erlaywdakg tpalvfshpl
      421 lpqtvsmshs awyqndfedl ealsdvvnky nnivwfsshs hsslhqnnww gtrrydgtge
      481 agrtgfpvvn tgailneylp dgdndetivk ekeeastglr vkvfadrvrv eawdfksgem
      541 ikyqdfar
//
LOCUS       WP_284844551             516 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alkaline phosphatase D family protein [unclassified
            Corynebacterium].
ACCESSION   WP_284844551
VERSION     WP_284844551.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..516
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56954
     Region          54..487
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 msdsnsrpsf nrrnflqiag vsaaavaagi naptkasaqs slsswgssqg gdhpqdsdlf
       61 glgvaagtpr hdsmilwtrl apeplaedgh ggmtggdvrv gwevakdegf gdvvkhgeal
      121 aqrelahsvh pqvtglepat eyfyrfradg kvspvgrfkt lptpdakvdn ftftvascqa
      181 wyhgyftpwk hiaqepdldm tifvgdyiye ygilegdnlw rqgasvpdvf kakvetleqy
      241 rlryslfksd ehlqaahara amaivwddhe vennyagnws eigtkaehfl yqraaayraf
      301 yenlpvappa lpdgpnnriy dsfdvgtllr fnlvdtrqyr eesakdasil gaeqeqwlnd
      361 klatspaqwn vvvnsvvvvp iadstdqwdg fpaarrrlie slskvsdpiv ftgdihqhca
      421 aeiqsesgqp vgvelvatsi asdgdgfags kstewlekpy vkamdkrrgy ikvrasrehl
      481 dsefvvvpwi erddtapret afsfrtnage htlrsl
//
LOCUS       WP_284844569              88 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: type II toxin-antitoxin system RelE family toxin
            [unclassified Corynebacterium].
ACCESSION   WP_284844569
VERSION     WP_284844569.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..88
                     /product="type II toxin-antitoxin system RelE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0017148 - negative regulation of
                     translation [Evidence IEA]"
                     /calculated_mol_wt=9979
     Region          3..88
                     /region_name="RelE"
                     /note="mRNA-degrading endonuclease RelE, toxin component
                     of the RelBE toxin-antitoxin system [Defense mechanisms];
                     COG2026"
                     /db_xref="CDD:441629"
ORIGIN      
        1 meyniaftrq akrelqkihq gnrkqyqrik raigglakdp yppgsialsg rsgrrirvgn
       61 yrvlysveeq evlvevftvg argsvykr
//
LOCUS       WP_284844599             181 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NADPH-dependent FMN reductase [unclassified
            Corynebacterium].
ACCESSION   WP_284844599
VERSION     WP_284844599.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..181
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19712
     Region          3..166
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 msrigiiigs trdksagkev gewlydlaqg rkdgveytll dlkefdvpll ttevipatan
       61 kqyadkkvqa wsdavdacdg fvfvtpeynh svpgpfknaf dclaaewagk pvafagygpa
      121 gairgveawr sivvnfsmpq lrnqldfgff tdwadgefrp adakvertns llaeledals
      181 a
//
LOCUS       WP_284844628             524 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: SLC13 family permease [unclassified Corynebacterium].
ACCESSION   WP_284844628
VERSION     WP_284844628.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..524
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55381
     Region          128..515
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mttphthest ahtegdeapg aprsewrrqf iglfiglgla vlvffifpsn aietvqgsag
       61 adpeaeytls airtvaavti lmgvwwmtea iplaatallp lvifplagvg tikevgapya
      121 satiflfmgg flialalqrw nlhrrlalyv vkiigtspkr lilgfmlatg flsmwvsnta
      181 tavvmlpigt svlaltaetv ggwekqkkfa talmlgiays asigslgtli gtppnaflna
      241 ymadtwgvtl gfgrwmavgv plavtfllia wallitifkp emkdipggre lindeikalg
      301 pwtrpqimtg iifvlaaaaw vtlplvlkef enyddaivgi aagillfilp adnqrrirll
      361 dwktanempw dvlllfgggl slssvfnssg lslwigemak glsvlpvvli vsavaalvlf
      421 lteitsntat aatfipimgg vavgvgltad gdinvlllti pvalaatcaf mlpvatppna
      481 iaygsgyvki gemikgglgl niigiflitl tvyllavpif glsi
//
LOCUS       WP_284844634             526 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: cation:proton antiporter [unclassified
            Corynebacterium].
ACCESSION   WP_284844634
VERSION     WP_284844634.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 526)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 526)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..526
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56889
     Region          15..502
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mdvllvligl mlltvfvvai gdkvglpwpa lltiitacav fvpglpqfep ptelilpifl
       61 ppllwalarr tswgvireqw vtilslsvll vvattlavgf tayaflpgis laaailigaa
      121 iappdpvavd avaepagipr riittlqteg lfndaasiva fnlaltavtq gdelsfgggv
      181 lnffysafva gglgwvvgrl valfithvhd vtarnaltwv tpfavylise elgasgviav
      241 viaavelnsr adiqaedrls gqafwetiel lftgvafgli gltvntaige vgsdlwhsvv
      301 vgvilslvaf vvrlvwmyiy yrinvsrgrp rvaplrlqev llmtwsgmrg lvtlalvlsi
      361 pagvfsfhhe lavialtvll vtmvvpglll pwlmerldlt easqiasdkm raavvarara
      421 asiealshfr pdghitadae kvdpeisanv iqwfedrlgd gedvsddsrw qrawqarhvv
      481 learrtalaa aqeellrmrg yraynpaivd evleeidrmv lgtkrh
//
LOCUS       WP_284844660             442 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: UDP-glucose dehydrogenase family protein
            [unclassified Corynebacterium].
ACCESSION   WP_284844660
VERSION     WP_284844660.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..442
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=47459
     Region          1..440
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrmtvigtgy lgathaacma elghevlgvd vddnkisalr sgkvpfyepg lpevlernie
       61 agrldfstdy eeaaafgnlh flgvgtpqrr gsyaadmtyv kavitdlvpk lkgdhiifgk
      121 stvpvgtaae lqelanelap egttveiawn peflregyav kdtitpdriv lgvgetnnes
      181 raeevarevy aqplsqdtpf ivtdwqtael vkvsanafla tkisfinavs eiceiagadv
      241 taladaigld erigrkflga glgfgggclp kdirafmara gelgadqalt flrevdainm
      301 rrrdrvvdla keafngsllg hrvtvlgcaf kpnsddvrds palavagsls lagaavtvyd
      361 pegmdnakkv fptldyaadt ddalreaelv ilatewkqfk elnpqqagql vdnkhiidgr
      421 nvlpvadwqq agwkvealgr tl
//
LOCUS       WP_284844945             181 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NUDIX hydrolase [Corynebacterium].
ACCESSION   WP_284844945
VERSION     WP_284844945.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 181)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..181
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19534
     Region          4..156
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18879"
                     /db_xref="CDD:467590"
ORIGIN      
        1 mptpdfivql rekighdqif vpacsaiivr dvpadaalwe vpsvllvkrs dngtwtpveg
       61 icepgeeitt talrevkeev gldakveall gvgqsgpvty pngdectfmg talrvsvadg
      121 aepvisdeen teagwfsvak lpdsvsrrhr lmiadavaqm khprgfaprm gwmkrseqpg
      181 l
//
LOCUS       WP_284845142             609 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284845142
VERSION     WP_284845142.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..609
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65469
     Region          11..609
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mqeafspaky tiepgqtllt ltidavkaqp kaeifsrpkn htwvsvsrqe fldevyavak
       61 glidagveqg drvalmsntr yewmlinyai waaggvvvpv ypssslsqvq wiiensgavl
      121 gigetqehte ilrmlqladd geprvkdsts qmrsffeind gavdvlqaag ktidddvvdk
      181 riaatatddv aslvytsgtt grpkgcmlth rnwnaqilgl lsnpiggiar pgkhvltflp
      241 lahvlafsvs aaamisgatq nfwadfatla tefqrskpnl ilgvprvfek vrngarakah
      301 dsgaiqgalf draeataiay sraldtekgp slalrsahka ldklvlskir agmggevdyc
      361 isggsamspe lmhffrgigv pvyegyglte taaaatvdfe eqkigtvgpp lggtrvriap
      421 dgelqlagdl vfagywrnae atdeafdgqw yctgdlgeil psghvkivgr kkdlivtagg
      481 knvapggmed glrshplisq alvvgdgkpf vavlvtldee algrwksqhn vdasrsvadv
      541 ahdaslraei qdainavnat vshaeaikkf yildddftee sgeltptmkv krnvvvqrys
      601 evldklysr
//
LOCUS       WP_284845157             215 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284845157
VERSION     WP_284845157.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..215
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=22571
     Region          19..209
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mtkhnaqhaq haphtqpapr ivlasqspsr agilrsagve pviepahvde daiqaelsna
       61 spseivtala sakaqaiari ypndvviggd smllldgvlq gkphtepati arwraqagrn
      121 aqlltghcli fggktyteaa ttdiafaqas eadiaayaat gepwqcagaf tlealggwfi
      181 dridgdpssv iglslpvvrr alyhfgfsvs dfwna
//
LOCUS       WP_284845274             375 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284845274
VERSION     WP_284845274.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..375
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40040
     Region          7..368
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mnhgpgltfr flaaqvlvvv isllvaaava tmvgptlfhd hmlmtgredp slelfhaeqa
       61 yrganlitla valptalisa llaslwlsrr lrtplqdltr aatsltagns rirvpagkag
      121 pevttlahaf ntmadrleht eqvrrqmlsd lahemgtpls vltvyldglq dgvvdwnnat
      181 htimadqltr ltrlmedidd vsraqehrid ldlveeglgd llhtaaaaag eayadkgvdl
      241 qvetitdtar vlvdrqrfgq vmsnllsnal rhtpaggqvr isvhrqgast alihvaddge
      301 gippdqlghi ferfyrgdaa rsrddagagi gltiskalie ahggtltats pgpgrgavfa
      361 lrlplsppds eeaar
//
LOCUS       WP_284845254             636 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284845254
VERSION     WP_284845254.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 636)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 636)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..636
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=68375
     Region          14..623
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mhkrlrliaa lllvfsvvla grlawvqvvw gpdlsaraed qrariyvdpa rrggvvdreg
       61 kqiaytmqar sltvspttlr kelreqaqle sderlddeqk deyvnatllk msreipkmie
      121 easedkqdlk skdlldklra dtqyevlvrn vdpdiaaeis erfhgvaadh qdirqypnga
      181 igenvvgrvs mdgtgqfgle asrdstlsgi ngrstedvst ngqvipgtlr detpavdgkd
      241 iqltldldlq tfvqqqleqa knnsraesae avvldattge vlamantdti dpngdiakql
      301 edgkhfdnrs isfpyepgsv akiitaaaai eegittadev htvpgsiqia dvtvndawph
      361 gplpyttagi fgkssnvgtl qlaeklgqdk fdeylnkfgi gattgielpn essglrpars
      421 qwsgstfanl pigqgmswtt lqmasvfqtl anggervepr iiksraedda kknlgeghea
      481 nhdkvkdsdd angagasdde pektrvvske taktvvdmfr atvqadpagv nngtapdani
      541 egynisgktg taqkvdpntg aysnsaywit fagiapvddp rfvvaimlde pergvldggg
      601 gggsagplfh qiaswlldrd nvppsppape ltlqap
//
LOCUS       WP_284845360             403 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284845360
VERSION     WP_284845360.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..403
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43758
     Region          41..160
                     /region_name="Creatinase_N"
                     /note="Creatinase/Prolidase N-terminal domain; cl46291"
                     /db_xref="CDD:480631"
     Region          43..402
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 msshnnstaa dsaadsaasa aansaansty ipvtadhfra rlakaekiva eqnlagflvs
       61 pgpefqyltg stfssherat flvlragkep vavcpetdvl tlqqenldel gfrfeawrdg
      121 qspyeitrkl leensehkav avanamtadh vlrldaalpn hsielgsdam sqlllakgee
      181 eisqlaaaaa aidrvheqvp allrdgiter evadklhdli lqehhsidfi ivgcgengan
      241 phhsfsdrvl rtgepvvvdl ggafgdgyrs dstrtyvvdg avdkapqefr dayevvtraf
      301 haareaakpe ataesidraa reiiteagyg enfshrlghg iglsthedpf ylegnkqqvq
      361 egftfsiepg iyvdgkwgmr ledivvlead gprhlnqqpr elr
//
LOCUS       WP_284845379             378 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284845379
VERSION     WP_284845379.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..378
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40646
     Region          7..361
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mvatsvsasv pqridclegi ralaavgvli thvhfqtasg pvvlerfdyf vavffalsaf
       61 llwrrpigpg flrkraarvv paylvcvavv alalpaastm swqqilanlt atqiyipdgl
      121 apglthlwsl cvefafyftl pliawvllrw qartrvfalc avgiaslgwa flpfvagfdg
      181 sdgaswaatv nrqiwppayt lwfvvgmlaa eaesagiakr pgvvrrilgm kplfwalata
      241 clflaswesi sprglthpsp lefairislg tvfaacivvp yalrptqsgl llsqpvqavg
      301 rwsyslflwh vavlsiafpl agiemfsggf viilaltlgl svtvaaisyt lveeparlwl
      361 rqatapaakh aasklspa
//
LOCUS       WP_284845399             246 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284845399
VERSION     WP_284845399.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..246
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25942
     Region          11..243
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(29..30,32..33,36..37,74,78..79,82..83,107,111,118,
                     121..122,127,142,146..147,149..151,153..154,157..158,
                     161..162,181..182,184..186,188..190,192..193,195..196,200,
                     203..204,210,212)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(145,149,152..153,155..156,195,198..199,201..206,
                     209..211,215,217)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mkqstastaq vpvgkpvhfl hpltviiigv sawvaalsis wpllhaaiia lgwlagitgs
       61 rslavpatsi alsipaglsm llvhaphgeh qiaplltsdg lvtagelalr fcalmtslla
      121 amanvhipdl lkalqhlglh hsvvyvlgas lqllpqasal isevatanrl arrkvtlttv
      181 iprmiipvit rlltrgadrg ialqgmgyda pgrrtvlypv rahrweillr lifpaaaigl
      241 vvlawi
//
LOCUS       WP_284845526             208 aa            linear   BCT 25-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284845526
VERSION     WP_284845526.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Niehaus,T.D., Elbadawi-Sidhu,M., de Crecy-Lagard,V., Fiehn,O. and
            Hanson,A.D.
  TITLE     Discovery of a widespread prokaryotic 5-oxoprolinase that was
            hiding in plain sight
  JOURNAL   J Biol Chem 292 (39), 16360-16367 (2017)
   PUBMED   28830929
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Fan,C., Li,Z., Yin,H. and Xiang,S.
  TITLE     Structure and function of allophanate hydrolase
  JOURNAL   J Biol Chem 288 (29), 21422-21432 (2013)
   PUBMED   23754281
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Wang,L., Grau,R., Perego,M. and Hoch,J.A.
  TITLE     A novel histidine kinase inhibitor regulating development in
            Bacillus subtilis
  JOURNAL   Genes Dev 11 (19), 2569-2579 (1997)
   PUBMED   9334321
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005226
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..208
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=22393
     Region          4..205
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 mlipygdrgl lidfsdhkdp lgqvlayqsq lqraglesii dlvpaaqtll itfdrnpsqi
       61 tlpeldaqaa ahssgnahii evsyngddld eladelgvst eelvtahtet twtaafagfa
      121 pgflylrpdl tnprakvfan isrrsqprts ipagsvglag gfsavypqss pggwqligtt
      181 earmwdidrd qpallqpgdt vrfqektc
//
LOCUS       WP_284845562             417 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284845562
VERSION     WP_284845562.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..417
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=44755
     Region          3..403
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mnltelvtqr lekwqqqglm rtpiefsgpq tpraqlndqp serillsssn ylglathpev
       61 idaarsalek fgtgsggsrl ttgsttwhrr ierelanfvg fedavlfatg yqanlsvlqt
      121 lahpdlhifs dslnhaslid girlattsgt kktiyphcdy taleqqlaec taryklvvsd
      181 gvfsmdgdig dlarlreict hhdawllvdd ahgigtvgkh gigstevhnt rpdilivtas
      241 kalgaeggfv acstpvanll rnqargyvys tacsaancaa isaaleviqq pltqqhpvvr
      301 lqqraaalre itgirvfdgv dsdsvnsdsa nsdsayspiv plpvgaessa vrlaseladr
      361 gfhipairyp tvargqailr atamatlela dikqfaqtlr dlgwrpptpa katspgr
//
LOCUS       WP_284845567             519 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284845567
VERSION     WP_284845567.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..519
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=59287
     Region          9..512
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mpsekdtpqp almwfrddlr lhdnaalvwa akqgpviavv idedatvtga ralgaatrww
       61 wqrsvhqlhk rlaahgvpll yyqgdpraii pavvqkfgvs avgwsrryhk plreldaelk
      121 hllqekgvaa ksfpghllte pwevqtqqgk qykvytpfak tarevaednv asylntgndq
      181 apsptshdel gpigftgpga dlasahplpd wdepdwthsl aqhwrpgena awkvaegfld
      241 qltaaarkqe phyaadrdrl dkqatsrlsp ylrfgeisih rlwamvtean dtgriageda
      301 saflsellwr dfawhrlyhl pdlhrrnvre qfdhfdwhwd ekearriant rrdprcpete
      361 kdipeiatad dfrsvfsawr agktgiavvd agmrelwatg tmhnrvrmvv asfltknlgi
      421 hwrhgeawfw dtlvdadpas npfnwqwaag cgddaapyfr ifnpdtqakr fdpdyryiqh
      481 wvpeyatpmy pqpvvdlkas rrqalaayee mknfhprpe
//
LOCUS       WP_284845681             773 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284845681
VERSION     WP_284845681.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 773)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 773)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 773)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..773
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=80365
     Region          19..757
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mptprstssp ipapstasst ielnisgmtc ascaarvekk lnkhdgvhae vnyatekati
       61 tgdtdaldad aliatvektg ygaeltpest tagtqapqda maeaeldslr rrlivsavla
      121 vpvialamvp awqfdywgwv slaltlpvvv wagwpfhrat wqnlrhgsvt mdtlislgts
      181 salvwsmval lfgsagdpgm rhgfdftvsr gdglshiyle vaagvitfil lgryfekrsk
      241 rtagsalral ldlgasevtv lrngaettin ineltvgdef vvrdgekiat dgvivsghst
      301 idtsmlsges vpveagpdda vagatinvgg gklvvratkv gkdtqlaqma qmvedaqsgk
      361 asaqrladki sgvfvpivia vslltliawl lidgdwaaaf taavavliia cpcalglatp
      421 tallvgtgrg aqmgvlikgp evlehsrgid rvildktgtv ttgvmeladv vtaegfdrde
      481 vvhlagsleh esehpigrai araatnqrtd grlsevsdfk sirsagvrgv vegrrvavgk
      541 psladnedlg alqqpflsaq tqghtalmvl vdgtpaavll vadqvkptsa aaiqqfhalg
      601 ietmlltgdn qavaetvaae vgiehvraev mpedkvavia dyqdrgykva mvgdgindap
      661 alaqadlgma mgtgtdvame saditlvrgd lraatdairl srrtlgtikg nlfwafaynt
      721 aaiplaalgl lnpmlagaam alssvfvvsn slrlrrftst agasvgatag atv
//
LOCUS       WP_284845751             519 aa            linear   BCT 25-DEC-2024
DEFINITION  FGGY family carbohydrate kinase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284845751
VERSION     WP_284845751.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Yeh,J.I., Kettering,R., Saxl,R., Bourand,A., Darbon,E., Joly,N.,
            Briozzo,P. and Deutscher,J.
  TITLE     Structural characterizations of glycerol kinase: unraveling
            phosphorylation-induced long-range activation
  JOURNAL   Biochemistry 48 (2), 346-356 (2009)
   PUBMED   19102629
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426119
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..519
                     /product="FGGY family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=56263
     Region          2..512
                     /region_name="GlpK"
                     /note="Glycerol kinase [Energy production and conversion];
                     COG0554"
                     /db_xref="CDD:440320"
ORIGIN      
        1 mfiaaldqgt tstrclifdr dgnvvsqaql ehqqimprkg wvehdpneiw antrrvissa
       61 mvelditard vqalgvtnqr etavvwekat gepiynaivw qdtrtggefd daaawqaktg
      121 llansypagp kiawildhvd gareraerge llagtidswl vwnlsggaeq genageadga
      181 daestpgnss datnqaqhit dvtnasrtll ldlhtldwdd elcealrvpk kilptivpsi
      241 galgevrhrg sltgvqitgi lgdqqaamfg qrcfrpgdak ntygtglfll lntgtepkfs
      301 ehgllttiay qqqgekpvya legsvavggs liqwlrdqlg iipdaasses iaaddnggvy
      361 ivpafsglfa prwrpdaagv ivgltryadr shitraalea tcfqtrevve amqkdagrel
      421 sglcvdggmv andllmqmqa dilgssvqrp emiettvwga alaagigigw wdfsdddyaa
      481 drvwepkmpe aqreqlyrmw nqavertlgw edagrgead
//
LOCUS       WP_284845864             911 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium sp. MSK039].
ACCESSION   WP_284845864
VERSION     WP_284845864.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..911
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=101093
     Region          14..910
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mansatcnak nyptlveefr keydfeldef qldaaaaiae grgvlvgapt gagktivgef
       61 avymafhggg acfyttpika lsnqkyhdlc asygeenvgl ltgdvtlnpd apivvmttev
      121 lrnmiyadsn rlaslthvvm devhfladrw rgpvweetil nldqrvtlvs lsatvsnvee
      181 fggwlrtlrg etdiivtdkr pvpltqymmv gskimrlfsk naehlagenh pgainrslls
      241 avgkaeaygn qrgprredvv rhleqakmlp aiyfifsrig cdkavqqlli rkvelttpee
      301 areigeiidd gvaglepadl hmlgfrqwrr almrgfgahh agmlpafrhi veklfsrgll
      361 kvcfatetla lginmpartv vlekmtkfng eahaeltpgq ytqltgragr rgidtvgnav
      421 vlwspqvdpy avaalasart ypldstfrpg ynmavnliat kgwaeahril ersfaqyqan
      481 dtiverahav elrrqdfdre raelqalvgr teaaqradaa elteqvldya elrrtlshee
      541 rqakrdaale rqqevehllr sinvgdvlal ptgknpvtav vvrsdsgrnp rptlvlddgw
      601 vervaadmfr ntpviighmr ihrgverapk rharavasql rrmhldkpkk irpharggsk
      661 kaaelrnqlh vhpvhawaer eelakkaqsv lkagrrweyq kqeseqpgds ltatfdriia
      721 lleelgyvet wtaeggtpaa kvteegekla rihhesdllv aqclrrglwd dldpaelaaa
      781 vsacvfenrr estvrtqlpt daleeavaht lrvykelvsd eerhrltatr epqlgfatav
      841 hqwvagaple yclqaaeasg avltpgdfvr acgrvkdlld qikmtgysnd vrksarkavd
      901 amqrgvvaid v
//
LOCUS       WP_284845901             361 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium sp. MSK039].
ACCESSION   WP_284845901
VERSION     WP_284845901.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..361
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=38410
     Region          12..361
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mtqtqryaer rnklaarlqe rdlpgllvtd lknvryltgf sgsnavylqr pdgrgvlgtd
       61 gryatqveie tgqpedvell idnkllekvp eraqvtgfav esslsigeak klaadgplpe
      121 vaagiveelr lvkdsaeiaa leaagelads vwqefldegg iregrteiea aadleyrlrk
      181 agaealsfdt ilasgvnatk phagvsrdpi vpglvtvdfg iyldgyasdq trtvcvgepd
      241 elsatlydvv lrsqragaaa vapgtalfdi dktcrdiitd agygeyfvhs tghgvgldvh
      301 eapsansrvd rsvtlaegmt ltvepgiyip gktglrient yvvtadgaks cnasstdlri
      361 v
//
LOCUS       WP_284845952             208 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium sp. MSK039].
ACCESSION   WP_284845952
VERSION     WP_284845952.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..208
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21985
     Region          13..205
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(147,151,154..155,157..158,193,196..197,199..204,207)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(168..175,181,184..185,188)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mrlprintaa pvlyiptgsv ihrlpagakl tgliaflvla aifaktlvag agcvvaavva
       61 yalakipwrt alrqlipili illafgaltw wrsglnealv rflvlwasvs vailltmttk
      121 vsdlqraver alapaaaigl pvdkislais ltihmiplql rtinevveaq qarggkfsar
      181 algiplvirt llrgrevgea lqargvgd
//
LOCUS       WP_284845992             501 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Corynebacterium
            sp. MSK039].
ACCESSION   WP_284845992
VERSION     WP_284845992.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..501
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=53001
     Region          1..461
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mekltelvdg singviwnii pwlligagiy fglrtlfvqv rllpamlkav aekppvarde
       61 qgnevkdger vgisafkaft isaasrvgtg niagvalais iggpgavfwm wmiaivggat
      121 afvestlaql wksrdadghy hggpafymtr glgwkplavi favalsftyg fvynaiqtns
      181 ivdavgvsln sdsmtlkliv avvvasltal vifggvtria svtqivvplm avayiivgli
      241 vvlmnlgevp gmiglivgha lgikqvagag igmafgigmr rglfsneagq gsapnaaata
      301 tvshpvkqgl vqtlgvyfdt lvvctitafv vllgpavayg rddiqgvslt qaaladsvga
      361 wgahfitfil fflafssvig nvylaqanie ylseskkvmt ifrlgviafv ffgafgslpl
      421 vwalgdtmag tmaiiniiai vplggivfkl lknfndqrkq gldpvfhrdm lpeaknvevw
      481 dgsdsatrrg wlerrslref t
//
LOCUS       WP_284846015             479 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase, partial [Corynebacterium
            sp. MSK039].
ACCESSION   WP_284846015
VERSION     WP_284846015.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         <1..479
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          <25..476
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 lksvivpsvq sppsmlklhd fcnraitges ipaekkdgdq vfagtwlrsg alrveavdig
       61 sdttlakiih rvenaqddra ktqtflekfs rwytpavmig ailvglitrn telaltllvi
      121 gcpgalvisi pvsivagigr aardgilikg geyleqaakv davvvdktgt ltlgrpaltd
      181 vrtlpgsrws ekeilqiaad vesasehpla aaivegavdr svreagfvad iqdadpvvaq
      241 gitatvpgvg rvsvgtaell ddaasgvnaa laavaelneq gktamivgvd gapagvvava
      301 devrpearpa vealhkagvk vvmatgdaep varnvaaelg idefhagmlp etkvdvvrgl
      361 qseghtvaml gdgvndmpal ataeigvamg aagspatiet adialmadrl trlpqslila
      421 krtartmrvn ifialatvlv lllgvflggv tmavgmlvhe asvllvivia mtllrpvrt
//
LOCUS       WP_284846023             555 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Corynebacterium sp. MSK039].
ACCESSION   WP_284846023
VERSION     WP_284846023.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12045581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..555
                     /product="SLC13 family permease"
                     /calculated_mol_wt=58682
     Region          <58..222
                     /region_name="CitMHS"
                     /note="Citrate transporter; pfam03600"
                     /db_xref="CDD:460985"
     Region          157..546
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 msapknrdse ntvverdaqd tgttatatta eapapeqkvd adliteraeq eqkarrravv
       61 glfvgvllai lvyaifpada advvnkahpd aekgpfdada lritaaiavl mgawwmteal
      121 plaatalvpl vafpilgvvp fkevspsyan ptiflfmggf ilalgmqrwn lhrrlalrvv
      181 tlvgtkpkqm vlgfmiatgf msmwvsntat avvmlpigms vlgltadmvg gfskqkkfst
      241 almlgiaysa sigslgtiig tppntlmvay lqeshdihig fgqwmlvgvp maaifmvlaw
      301 lvlitvfkpe mdqipggrel iqeelekmgs msraektags ifllaalawv fvpvisdwag
      361 wehniddati aitaailmym lpadgsgsrv mdwehtkevp wgvlllfggg lalssmfdks
      421 glslwigeva rslgglpivl liaataivil vlteftsnta taaaflpimg gvavgtglta
      481 gndmnvlllt ipvalaatsa fmlpvatppn aiaygsgyvr igdmvrgglw lnlvgivlit
      541 ivtfalavpv fgltl
//
LOCUS       WP_284846034             354 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family oxidoreductase [Corynebacterium sp. MSK039].
ACCESSION   WP_284846034
VERSION     WP_284846034.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Blankenfeldt,W., Kerr,I.D., Giraud,M.F., McMiken,H.J., Leonard,G.,
            Whitfield,C., Messner,P., Graninger,M. and Naismith,J.H.
  TITLE     Variation on a theme of SDR. dTDP-6-deoxy-L- lyxo-4-hexulose
            reductase (RmlD) shows a new Mg2+-dependent dimerization mode
  JOURNAL   Structure 10 (6), 773-786 (2002)
   PUBMED   12057193
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437758
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..354
                     /product="SDR family oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009226 - nucleotide-sugar biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0019305 - dTDP-rhamnose biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=36076
     Region          52..353
                     /region_name="RfbD"
                     /note="dTDP-4-dehydrorhamnose reductase [Cell
                     wall/membrane/envelope biogenesis]; COG1091"
                     /db_xref="CDD:440708"
ORIGIN      
        1 mpqsqdsptn perplgahgd aarstgagre adrmyeslaa gtgttggvvp givvlgaggq
       61 lgtalvagla dhaapvvavg raeldltasd eecatalraa ieqaggrdvv vinaaawtav
      121 daaedaantt tvervngtap gvlaqvaaaq nagfvhistd yvfsgeagrp ravtsedppa
      181 pvneygrtkl vgeravldag gtvvrtawvf sgatgpgrdf ldtmagladr gvdpkvvddq
      241 wgrptftghl aaglvelait lwrqrpvdae artpelprll hatgsgeatt wagfaaaifd
      301 atghdparvs riptaeyptp arrpvgvyld tgcweaagls plpawqdglr aalg
//
LOCUS       WP_284846073             529 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium sp. MSK039].
ACCESSION   WP_284846073
VERSION     WP_284846073.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 529)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 529)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 529)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..529
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=57537
     Region          3..522
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          277..523
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mslrrlspep rgrasrsatg ertagenvdh gmlleperaa eltkrprwrr fldgtlgsik
       61 qrltilaslv iifsiatvtf aayatvsqil wrtsdsllrs qaqsiiempp ektpggvqee
      121 nyepaferis ntlsfivvpe tytgiaapva kfepvledae isvirgehph syrsdgddry
      181 favaapdgrv vvlvsdasst qraldslali ltmigicgal gaivlvtavv stglrpidrl
      241 rratdrvtet delrqlvvfs ndevgtltqs fnnmmlalqt srekqkelva dashelktpl
      301 tslrtniell llatredspg iseadrreie rdvlsqldem salikdlvdl aredgpvlsd
      361 qevdlndcir vgvakvqrrr pdvifeihae pwvaqgdpls lkrallnlld naakwspqgg
      421 tvrvwmqpip paasglpaga qggegyeeav eirvadsgpg iptndrakvf drfyrsissr
      481 smqgsglgls ivkqavvnhg gaiiadesdd ggalmrvvlp arrgtpsek
//
LOCUS       WP_284846126             344 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium sp. MSK039].
ACCESSION   WP_284846126
VERSION     WP_284846126.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 344)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..344
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=35955
     Region          58..344
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mklslrarit vlflgtvlgv glaliglvya ylkltpvpfm aqiptpdegl lidgavpiad
       61 evlrrvlvas ltvlalltav agvigwfvag lvikplrdfa ddaatvtrgd lsarishqgp
      121 ddevgelada lnamldelad alerqrrfas nashelktpi atiqtmadva lasgdeqvlr
      181 dtlgrvrevn araadtvaal lqlanvdvrd rqeldlaalc rdigrgqgva vtaeavtvaa
      241 sptlvrqave nmvrngithg edpsmtvaqv grnaeitves dgpqldaaev rtwvepfara
      301 qrtsgagqgl glaivdaiak ahggsveltp raegglavtl rlpa
//
LOCUS       WP_284846170             604 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Corynebacterium sp. MSK039].
ACCESSION   WP_284846170
VERSION     WP_284846170.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..604
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=64455
     Region          <2..226
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mwarrsvgai lafvvgaila vavpvgvana didkpkkqrv hlvmdssgsm aekidggktr
       61 idaakdalns lvdstpeete lglrvygand knkgseescr dselvvpiat gnredlskai
      121 egyspagwtp isyalkeagk digkpgedee ntivlvsdge etcvpdpcdv vdelqkqgin
      181 vtinvvgmnv dgkarnqlqc iakkgngkyy sadnadeikt aieeaamrtg qafqldgdpi
      241 tggdsrseap dmrpgtyldk fgfnetrwyr vpkqakdsvv wagaamslae tdkehgsitv
      301 elvdptseek caresgyghs sgpegllats lssrecedad nlllkvttev kgegelpvri
      361 hleergavqn ldelpeaaka peweemeaek apegtsyggd sfgnakviep gahniavtmg
      421 esqvfavdld wgqhvqvqtd letvqkrfma wntrvlspfg sdalvndtds sdfgsgksvs
      481 lkartypiry knsgeiypne nslpgryfii vsggeredta dkhgeakgtm tvevldkage
      541 gapefasfdk dlgeeqddga adaknvaaeq eddgmswpmi gaagvgiial laaivlavtg
      601 rkks
//
LOCUS       WP_284846177             351 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium sp. MSK039].
ACCESSION   WP_284846177
VERSION     WP_284846177.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..351
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35272
     Region          31..344
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mqkrrlsspa vaiaiaaila ailfiaalai gpvtiavpdv lasvwaqitg rgeiarqdpa
       61 lgsaynvvat irlpraiiaa lvgaalavag tvmqavfrnp ladpgiigvs agaataavla
      121 ivtgfsavaa walpasaflg algavaivql aaamrgggpa tlvlvgials aflgavtaaa
      181 ianapsdsdi rgvafwlngd lvartwehva iaslpivlgi vllllfsrdl nillmgdqaa
      241 rttgvnvrrv rvvtltvaal itasavavsg vigfvglvvp hlirliigpn hksllptaal
      301 agaafllaad tiarmlfapv tlqtgtvvaf igspiflwll lrgrrpagws a
//
LOCUS       WP_284846349             663 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD/NAD(P)-binding protein [Corynebacterium sp. MSK039].
ACCESSION   WP_284846349
VERSION     WP_284846349.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 663)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11816065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..663
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72241
     Region          1..636
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
     Region          9..208
                     /region_name="NAD_binding_9"
                     /note="FAD-NAD(P)-binding; pfam13454"
                     /db_xref="CDD:433222"
ORIGIN      
        1 mssierriai igagprgisv lerivatyre laeqgtdper lavavvddvq pgagriwrtd
       61 qnfdlcmntl adavtlfpep gssvhapvle gptmyewiml vrgeelgeqr dprgakaalf
      121 srhpvqplgh raqdiqqaep nthpprglyg eylrwafsav lgmvpeaiev tvhrskavgi
      181 eaaadgtdai eladgtrlra hatvlalgwl dtdlapeeqe laaaaakheq lewvapnnpa
      241 dqdfsaipsw eesgqeilir glgmgffdam smltlgrgga fipdatapag lryqpsgrep
      301 rilamagrgy phqprpefsg mppraelrrl deaisqldtp lpansldfge tlwpallrda
      361 qeayyrvlla aepdvlkkvt eviddpatdp lnmhedtrld glvdpekrfn ipwennpvar
      421 ledkaeaage elsidsftrs lfehllgdwr eaqrgeespv kmglfsfgaa mkrialvdep
      481 grftqasree eyalfgsiaq mvsvgppafr taellalida glvrflgakp eltvdeetpa
      541 frvssattge evcataliea lihdpdvrht dcplstqlla qsrmrawawg dgspsgapev
      601 dretglliga sgqrdtrvhm lgvplrevra dmtnspkvge dpvifqetda aarsalriam
      661 srp
//
LOCUS       WP_284846354             226 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Corynebacterium sp.
            MSK039].
ACCESSION   WP_284846354
VERSION     WP_284846354.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..226
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24242
     Region          72..216
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 msrrgahlrs trpnlrsrsr aalaalltaa vslggltacg egatgddava vggtfefvsp
       61 ggqtsisypq eerkevanlt geslmeegeq inledyagka vvlntwgqwc gpcrseaddl
      121 ervheklvkr gdgtvlginv rdpsrekpkn fvrtygityp siydppfksa lrlggipasv
      181 ipttivldkq hrpahiflke vtddelwnvl epildeedga gdgega
//
LOCUS       WP_284846421             257 aa            linear   BCT 25-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Corynebacterium sp.
            MSK039].
ACCESSION   WP_284846421
VERSION     WP_284846421.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..257
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28031
     Region          5..247
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mqhevkiiah rgaskhrpeh tigayelaaa qgadgyecdi rltrdghavc ihdrtvdrvs
       61 dgtgavsrmt laelkalnfg tstqpagvle lrelleflqd mrhsaeagkp elfietkhph
      121 vrslqveaem hrqlaaagla ggegiylisf dswslwrsrq inpqveriql rrkyhpparp
      181 llrgsgiarh agwsieqama slrgeggsap adyiwtvdqa eqlrwiaqrg arwvatncpg
      241 eaagwlqnsa gggagqa
//
LOCUS       WP_284846465             290 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Corynebacterium sp.
            MSK039].
ACCESSION   WP_284846465
VERSION     WP_284846465.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..290
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29975
     Region          143..288
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mattppgshp naaapgdaaa sghggpeevt atredvdvar gsgeeagasr prvlllvlai
       61 vigllvaaip lvagvmsggd dqpgaqsqqq qqaepgmvgg agsapghpge sdrgadgdad
      121 pgpeqpvsit nprscpapeg atqpapdsel agielpclts gknetadlga alagkptiin
      181 iwawwcepcr relphfdkla kqhpewnvag ihldkksqag adfldelnvt tmpvysdrsh
      241 rfdtatslpk vvpitvvyra dgtraqmypq vfrdyeelea avhaalsgqn
//
LOCUS       WP_284846588             424 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium sp. MSK039].
ACCESSION   WP_284846588
VERSION     WP_284846588.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..424
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44248
     Region          15..424
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mtsasnspip ttvtpravgi wvtgvlvyvm avlgrtslgv vsvdaldqfq inagqlavft
       61 tvqlatyafa qipagllvdr lgprkmmlyg avlmavgqvl lafttsfpva vaarvlvgag
      121 dataflsvmr iipawfplrt aplfgqatga vgqlgqflsa vpflalvgsa gwsigfvslg
      181 avgllvgiva fvvvwdtpge ltsgrrggvd nqedgpgpsp mvavkyalgn rtawhgffih
      241 wsglsllvvf tllwgmpimt lgmgmdkata gwaisastla mavcgvlvgf lsarlgrsrw
      301 kaivvgtslg aaawllffis peprtaaaaf vmnvvmgvvs planigfdsv reecrrefva
      361 tatglanmgg wlagmaanqa mgiyltlaap ngdytwaefr fgwfvvlgvw alglvgvvat
      421 rprr
//
LOCUS       WP_284846604             813 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium sp.
            MSK039].
ACCESSION   WP_284846604
VERSION     WP_284846604.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 813)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 813)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 813)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 813)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..813
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..813
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=84397
     Region          27..804
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 menlsqhqds satevgaiga aqpvldldyq itgmtcasca nrierklnkl dgvtasvnya
       61 tekahveqdg aaeavtdeqi reiiadmgye aqlsqplasr paagdpqgga geqgaadaaq
      121 pgaeptsqts aeqaaerele glrnrligsl wlaipvivla mipnlqftnw qwlsltlaap
      181 vivwagypfh ratwlnikhg avtmdtlitv gtgaaflwsl valffgtage pgmshtwnlf
      241 nvhsdpmgdi ylevaagvim fvlagryyek rakhrageal ralselgakd vavvddaqgg
      301 nerripigql aegmyfvvrp gekiatdgrv vagssavdes mltgesvpve vapgdmvtga
      361 tvnasgrliv eatrvgsdtq laqmaklveq aqsgkadvqr ladrvsavfv pvvialavit
      421 lvawllitgd vgaamassva vliiacpcal glatptallv gtgrgasmgv lirgpetleq
      481 trgvdaiild ktgtittgem tateawlapa adsiadgsgk agfseadlwr iagavenhse
      541 hpiaqaiaer arkeiggelp eaedfesvpg rgvtatvdgv tvqvgrgfet sdgttvgaei
      601 versglggtv vpvlvagqla gavavedavk pdsaeaiaql kelglepmlv tgdneqvare
      661 vagvvginpe nvragvmpad kvtavkdlqa dgkrvamvgd gvndaaalaq adlgiamgtg
      721 tdvaieaadi tlvraemsav vdsirlsrkt lrtikmnlfw afaynvaaip laafgllnpm
      781 lagaamalss vfvvsnslrl rgfksiqpev eek
//
LOCUS       WP_284846745             245 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium sp. MSK039].
ACCESSION   WP_284846745
VERSION     WP_284846745.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..245
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26559
     Region          76..226
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 msqkvkapdq kggsgfmwti iavlviaavv igivvtrgga kediaanmpq edvnftitak
       61 dnvvelaskn idkdapvvdi yedfscpycs hlvkadhqdv kqavsdgklk vrfnflnfld
      121 dgrrgpstrg aavayaiaet gnvkafwnfh nytmleqetv artwdyedla qaasaydlda
      181 sliekiknge ledkgvevge anakvlkkkv gqvsspivlv dgqkldiktg kdgmpqswvp
      241 dvvkn
//
LOCUS       WP_284846792             580 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Corynebacterium sp. MSK039].
ACCESSION   WP_284846792
VERSION     WP_284846792.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..580
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62552
     Region          2..458
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          511..577
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(534,543..545,552)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            544
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mianrgeiai riiraaqdeg iasvavyaep dadapyvrma deafalggqt saesylnidk
       61 liaaaresga daihpgygfl aenadfarav idaglnwigp ppeaidrlgd kvtarqiaam
      121 vdapmtpgtk hpvssaaeve efakehglpv avkasfgggg rgmkvaytme eipdlfdsat
      181 reaiaafgrg ecfveryldr arhveaqvma dkhgnvlvas trdcstqrrf qklieeapap
      241 fltaeqnrri yesaeeicra agyqgagtve ylvgsdglvs flevntrlqv ehpvteeitg
      301 wdlvreqfri aegrplsrts rptlrghaie fringedaan nfmpnpgmit ayrepsgpgv
      361 rmdsgieega viggqfdsml aklivwgenr eqaiarskra lrefqvaglp tvipffqqml
      421 nnpdftaedg fkvytrwiee ewdgslpest kdasaaagge eklprqrvtv evegrrveit
      481 vpgelmaagg rtkraprrra aageaaitgd tvaapmqgti vkievsegqr vaegdtllvl
      541 eamkmenalq ahksgvvtgl aiapgdsvtk nqalfeildd
//
LOCUS       WP_284846824             687 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Corynebacterium sp. MSK039].
ACCESSION   WP_284846824
VERSION     WP_284846824.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..687
                     /product="PhoX family protein"
                     /calculated_mol_wt=75078
     Region          42..679
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 maikgmnllf qsrrssrtct ykcgnacfge csntssnpyf gdisrrsvlr gaglaaltvg
       61 ggsalaacad gstaqsvsss eggkapgplk gmqfepvaan ekdelvvpag yasgvliawg
      121 dpifpdapkf dpykqtakaa erqfgfnndf agllehpkdp nrllyvcshe yttephmfpr
      181 ydaenptdeq iniglanhgh tilevskvgk tgelkrefgp lnrritgeti femrgvaagh
      241 elvktkadps gkkvrgtlnn csggitpwgt flsgeenfeq ywanadkaqv egkakedikr
      301 fdppegaser kwerlhdrfd lskepnefhr fgwmvevdpt dpystpvkht smgrfkheag
      361 niyvtddgtv vcysgddarf eyiykfvssk kikegdmkhn mtildegtly vatlkgnspd
      421 keitgdgelp edgkfdgtgq wkklltvtad gaeshvegft peevavytrm aadkvgatkm
      481 drpedfeanp htgllyvslt nnkyrgatge naeknqedpk eyapikenkn glvmeiddeh
      541 agekftwnll lvcgdpeeae tyfggfdksk vspiscpdnl afdshgnlwi stdgnaldsn
      601 dglyavglkg enrgetrcfl tvpvaaetcg pivtdervmv nvqhpgeddd atfekpashw
      661 peggnsvprp avavvwrrdg kkigiea
//
LOCUS       WP_284846800             115 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium sp.
            MSK039].
ACCESSION   WP_284846800
VERSION     WP_284846800.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..115
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12162
     Region          14..68
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(15,19,44)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(18,43)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(25..26,37,40,44..45)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mihgsgvsem isaienalss aglsqrdlaa rtglsqstvh rilkgernvk mpeliriada
       61 tgctvaqltg egvakrvvsa arstngakmd amrqrllhfm eldaylddqa iakvl
//
LOCUS       WP_284846838             446 aa            linear   BCT 25-DEC-2024
DEFINITION  saccharopine dehydrogenase family protein [Corynebacterium sp.
            MSK039].
ACCESSION   WP_284846838
VERSION     WP_284846838.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..446
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48211
     Region          22..437
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 madapkdatp qgkktptggk qrpvditlfg atgfvgkila gwlaehapkd vtialagrnr
       61 eklvflkqql ltihqgvmdw qiveadafde damtelaknt rvvistvgpf vrygedlvra
      121 caeagthyvd stgevlfmrk midkyddvak angariihac gfdsvpsdig mllineaaak
      181 dgkklaevtn lvsmrgamsg gtvesareqf qaaqrdpeqr rvladpysls pdreaepelg
      241 eqpdygvlqt etvgapegwa gpflmasvnt rvvrrsnals gfkygkslry refqstgpgl
      301 kgraqayamg gvqqtmltam kapklrdfis qwapepgegp tskaqengyf rcvfhgfvkp
      361 npapnvepdy iatlysqgdp gyrstsrmlg taaltllkde aelpgteggv ltpatglgmv
      421 yvrrlresgm rldvarggly rtstpq
//
LOCUS       WP_284846847             552 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Corynebacterium sp. MSK039].
ACCESSION   WP_284846847
VERSION     WP_284846847.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..552
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=59166
     Region          22..338
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(23..24,27..28,57,60,114..115,167)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(112,115,192..198,227,251..256,287,313..317,319)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mtgqgknsae agaaaaervt vlwfpdfpvy avglargwdm lrpaatiady rvqacnaaar
       61 aqgvrqgmkq rhalatcpel rhapadpvqe atihedivaa lmdvaagvet lrpglvalpt
      121 rplanyygge aaavelllds aarlgvecla gtaddlmpav waarrgvhvp pgrnssfvpt
      181 lpigflavea vlsapaelvs tlqelgvrsl rdfaalgrkh vagrfgaeav ywhrvacgep
      241 grevspqrpt qpvevlhqve epirstetaa fvarqaaarl hgelfrrgea clrltvrvhl
      301 nppaeytgpt vverawrcre plteedtaqr vrwqldgwit rlrakvgepe qegfedsaag
      361 vvaiellpve tvpagtiaep lwggadeglr aaraaagraq aligmaavqq vvhrggraig
      421 grvltlpyge eapeeiaalp ttqwrgelpa plpatvgeia npsaghpaaa iavlgeraqp
      481 vhvtgrglms dspqrlrwgn rtlsirgwag pwpvdeqwwa egkryarlqi atdegayllv
      541 ckgqkwriea ty
//
LOCUS       WP_284847063             584 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Corynebacterium sp. MSK012].
ACCESSION   WP_284847063
VERSION     WP_284847063.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK012
  ORGANISM  Corynebacterium sp. MSK012
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Corynebacterium sp. MSK012"
                     /db_xref="taxon:3050189"
     Protein         1..584
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=63256
     Region          32..560
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mpssdksqta asdlngavsn sdataqkpft psrravlrag atgaagaigl atatsaganp
       61 esqspanagg sggfqvfqhg vasgdplpds vliwtrvtsh pgdtaganqg rpvalkweva
      121 sdegfgniva sgalntdpda dntvkidvkg lsadsyyfyr ftvtaghhag qvspigqtrt
      181 appvnsspdh lgialtscan wesgffsayr dmaendridi imcvgdyiye yeaggysgkg
      241 pvrdhkpahe iisladyrlr yatyrtdadl qeahrakpwi vtwddhevan ddwhsgaenh
      301 dpetegdyva rrdaaiqayl ewlpvravpf sqggklyrsf rfgdladltm ldlrtyrdqq
      361 lkfiragetd desrsmlgse qfnyllgqwr sssakwrvvg nsvmftpvlv ppldpeatha
      421 vtellslpqd glpynldqwd gyaaerrkli dimgkegydn vvfltgdihs swncnvpkvp
      481 gqypsagiaa ieivctsvsa pniddivklp qdnpislaat aglkaanpyv nylefdrhgy
      541 tavyfgredv tseyrlvevk eepnqplfva atyrgkpgeg mtqa
//
LOCUS       WP_284847146             724 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: prolyl oligopeptidase family serine peptidase
            [Corynebacterium].
ACCESSION   WP_284847146
VERSION     WP_284847146.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Shan,L., Mathews,I.I. and Khosla,C.
  TITLE     Structural and mechanistic analysis of two prolyl endopeptidases:
            role of interdomain dynamics in catalysis and specificity
  JOURNAL   Proc Natl Acad Sci U S A 102 (10), 3599-3604 (2005)
   PUBMED   15738423
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Polgar,L.
  TITLE     The prolyl oligopeptidase family
  JOURNAL   Cell Mol Life Sci 59 (2), 349-362 (2002)
   PUBMED   11915948
REFERENCE   3  (residues 1 to 724)
  AUTHORS   Polgar,L.
  TITLE     A potential processing enzyme in prokaryotes: oligopeptidase B, a
            new type of serine peptidase
  JOURNAL   Proteins 28 (3), 375-379 (1997)
   PUBMED   9223183
REFERENCE   4  (residues 1 to 724)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 724)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..724
                     /product="prolyl oligopeptidase family serine peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=79701
     Region          21..724
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mgtdtdtdlg nnlsflstdl vpdwlddidg sqalawaraq skatvagvds laddtsdrtn
       61 leqrilaaln tdariaypvr rgeylynfwr daehprglwr rtslqsylag qedpqatewe
      121 tlidldalak aegenwvwkg tvcrypeydr alillsrgga datvvrefdl vncifvedes
      181 fylpeaksdv cwlgrdeilv gsdfgpgslt dsgyprqvrr wrrgtpsssa dvvfsghsdd
      241 vavggwfdat egferlfver ahdfynsqrf vaaerpgkla aqqngdfslq ilevpqdcrt
      301 svhrqwlvlm prtefngipa ggvavveldk wlagsrevev iftpdahtsf qqlawtknfl
      361 vltlledvat klvvlregsw epveafgelp aqatvsvidt aserddeiwl vstsatqpat
      421 lwygqvgspl tevrrapalf dsegmetrqh watsadgtri pyritgrfga gagasadaga
      481 saetttatpa pnpaptlvha yggfevslvp qysairgltw lerggyfvea nlrgggefgp
      541 twhssvvkte rmrvyedhqa vlrdlvergy ctreqlgvrg gsngglltav cltsypelvg
      601 avvsqvplad mmryhklsag aswmaeygnp ddpteraaia qyspvqrvvk reqrayppal
      661 ittstrddrv hpaharslaw lleeagqpvd yhenteggha gaadnsqvaf vealistwlw
      721 nklk
//
LOCUS       WP_284846569             284 aa            linear   BCT 25-DEC-2024
DEFINITION  CAP domain-containing protein [Corynebacterium sp. MSK039].
ACCESSION   WP_284846569
VERSION     WP_284846569.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK039
  ORGANISM  Corynebacterium sp. MSK039
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Gibbs,G.M., Roelants,K. and O'Bryan,M.K.
  TITLE     The CAP superfamily: cysteine-rich secretory proteins, antigen 5,
            and pathogenesis-related 1 proteins--roles in reproduction, cancer,
            and immune defense
  JOURNAL   Endocr Rev 29 (7), 865-897 (2008)
   PUBMED   18824526
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Corynebacterium sp. MSK039"
                     /db_xref="taxon:3050193"
     Protein         1..284
                     /product="CAP domain-containing protein"
                     /calculated_mol_wt=30374
     Region          13..219
                     /region_name="YkwD"
                     /note="Spore germination protein YkwD and related proteins
                     with CAP (CSP/antigen 5/PR1) domain [Cell cycle control,
                     cell division, chromosome partitioning, General function
                     prediction only]; COG2340"
                     /db_xref="CDD:441910"
ORIGIN      
        1 mkrklavata tvlslafpta ianaapsptt gvelvngkdq fgntrakfni negntvglpa
       61 lkelrswawd qnplfrgydh egfgkgtrlq dvarangitt kdeylniath sdlhwiavqr
      121 ametstkfdh vrpdgssprt atrngvtpai eslsagtplr daiingwgks evkklnnngg
      181 vwaggtghai hilhprhkvw gfgqvtvpgs kyrvystavh admalqdadg fgknytntgn
      241 nnpnnppamd sssgsdigki igiilgvvsi lgsiwmaiqq flpr
//
LOCUS       WP_284847292             814 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium sp. MSK012].
ACCESSION   WP_284847292
VERSION     WP_284847292.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK012
  ORGANISM  Corynebacterium sp. MSK012
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 814)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 814)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 814)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..814
                     /organism="Corynebacterium sp. MSK012"
                     /db_xref="taxon:3050189"
     Protein         1..814
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=89321
     Region          35..800
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 masrasepgq dqtgrigrtg qaglpdqass apqreeestl aaeqayvdra fsfldrarer
       61 dqeylrqvml iddpdpqarv ereveyhrlq anldryrsae iglvfgridi ddtdpdnpla
      121 eegpgatvdk ryigriglsd enddyrtvim dwradgarpf ylattahpeg vslrrhlrth
      181 grkvrsidde wlsgeeadsa heteveagvg gesvlrevmn qartghmrgi vetiqreqdl
      241 iirdstrgtl vvqggpgtgk tavalhrvaw llytyrdqla ktgvliigpn ttfldyisrv
      301 lpslgetgvv lttiadlypg vrgsnalidg hnpeplvaqe vkgsiemlti lreavrayqe
      361 lpaeplevrn dnitltitpd mvktartrar rtrkphnlar pifrdhvvel laaqmaevig
      421 adplggenll svtdvadlrd eidesgavad ildelwpalt pervlsells sreaidyaat
      481 dydeltreal yrpegtdwmp sdaplldela ellgpvgese adeedwqarv eeaqgaldtl
      541 sssasqdldd gfeaeilsay dvidaealae rhrerdlrst aeraaadrlw ayghvivdea
      601 qelsamawrm lrrrspngwm tlvgdvaqtg spagaatwdd vlepiigsrw hlheltvnyr
      661 tpaevmevaa svlaeidpel eapqsiratg rkpvqahtva ealthveqva qpdrlvavia
      721 paelleatra evrdflggga ggagdskltn cavydittsk glefdevivv apdqivaqsp
      781 qglqdlyval tratqglvvv dkqrpehlpe lgra
//
LOCUS       WP_284847357             570 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Corynebacterium
            sp. MSK004].
ACCESSION   WP_284847357
VERSION     WP_284847357.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK004
  ORGANISM  Corynebacterium sp. MSK004
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Corynebacterium sp. MSK004"
                     /db_xref="taxon:3050186"
     Protein         1..570
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=61143
     Region          53..483
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mrnrhtilaw tallslnasn avaaesdpgq aavatgdvvy fqdmkefepr awddgshqgg
       61 iaylatalek trqeegdpiv afggelaags lfgsvfrgep fveafnelgv dvgnfgnhdf
      121 dygvdhtrsl iekaefpwis snlttqngep isddgttfta ksgdltvgfv sltadldrtv
      181 aakdvvvgdf idsaragvnk lqeegvdaiv llsqiskedt trvmeenpel aaalreenea
      241 qspeevtyta dgrpivapra dygtlvhldi tvdrstqent vkvvnhpvnp slnaneewkt
      301 rseklygeld rqlgeqlgta tqtlskaelg plvadayreh fdtqlgwqng ggqraamkeg
      361 tltrrdaqsv lpfgnspiai qatgaqikda lekgiesnpd ggngfprtag ftfdyeinap
      421 fgervtaikl ddgtsmdmna tyslaisnyv vnggdkidsf vdapvtsegt aidvdvfsey
      481 ikrhgellpl ktpdkpnspa ndgkreessi gssrgaavai gviaalagaf vaftpkpvle
      541 givrylktfl pgswqlnlps drfplqglhq
//
LOCUS       WP_284847618             358 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Corynebacterium sp. MSK004].
ACCESSION   WP_284847618
VERSION     WP_284847618.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK004
  ORGANISM  Corynebacterium sp. MSK004
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Corynebacterium sp. MSK004"
                     /db_xref="taxon:3050186"
     Protein         1..358
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=39487
     Region          67..347
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msiasyelkn gakryrvryt ladgtrtdkr gftskaqark weaeiisgtr ptpggreqpl
       61 stykdlylkt lkgksantid vftialnkhv lprwgrttps nvtpqavqmw isesansnsq
      121 atrnlavlss llrlsgmakk dlptqdvikp skavqrnvyl typqlcafak eaktyegiil
      181 tlgmvgmrwg elaglrvrdw dserqvlyls qsativrgkl vlgptkggkp rtvivpqkvv
      241 pfidqatrgr gkdtpiwprs nggymlrpkg sswfdgaltr vrakdetfpl lrlhdlrhta
      301 aslmvqsgah vkliqhqlgh asaamtldty adlypedlsg lraamnrsfg gqdvgtes
//
LOCUS       WP_284847680             335 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium sp. MSK004].
ACCESSION   WP_284847680
VERSION     WP_284847680.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK004
  ORGANISM  Corynebacterium sp. MSK004
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Corynebacterium sp. MSK004"
                     /db_xref="taxon:3050186"
     Protein         1..335
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=33789
     Region          3..329
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mivsvrsvls fagivivala iaayslfspg agqdsaalws vatnpnstdf aatvvwqwra
       61 prvvaaivvg mclgiagaif qilthnplgs pdiigfntga ytgviavsla sfssafnial
      121 galvggtita llimglsfag rltgarlvvv gigvtfflsa inkwlilsge leqslgaatw
      181 aagtlnavsw arviplgvlg gaacvaglll rgwcdalalg dstasalgln vsrarvvmvl
      241 vgtvlvavst aiagpisfia laaphmarll srpdrtpvll sgvlgalfll aadlagqrlf
      301 fpialpagli tvcaggiyla glllwqsrsa gmkgq
//
LOCUS       WP_284847770             261 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Corynebacterium sp. MSK004].
ACCESSION   WP_284847770
VERSION     WP_284847770.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK004
  ORGANISM  Corynebacterium sp. MSK004
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Corynebacterium sp. MSK004"
                     /db_xref="taxon:3050186"
     Protein         1..261
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27339
     Region          17..243
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mpipvklppt fadvlekaeq plvgawicsg seaaaeiias agfswtlidg ehspygletv
       61 lsllratday gltrvvrvpv nntalikqyl dlgaqnlmvp midtaeeaea avaamhyppr
      121 gvrgvgsala rssrwngven yltnasdtvs ltvqiesata venvedivav egvdnifvgp
      181 sdlaasmgll gqqthpdvle avnhtfeavr asgkkvgvna fnleqaqkyl esgasfalvg
      241 advqllsgaa rqladkfhlg g
//
LOCUS       WP_284847954             187 aa            linear   BCT 25-DEC-2024
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Corynebacterium sp.
            MSK004].
ACCESSION   WP_284847954
VERSION     WP_284847954.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK004
  ORGANISM  Corynebacterium sp. MSK004
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Corynebacterium sp. MSK004"
                     /db_xref="taxon:3050186"
     Protein         1..187
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20832
     Region          4..182
                     /region_name="YdeN"
                     /note="Predicted esterase of the alpha/beta hydrolase fold
                     [General function prediction only]; COG3545"
                     /db_xref="CDD:442766"
ORIGIN      
        1 mhfyivhgyq aspdshwfpw lerlltadgh tvhtialpep napkldewve sirndierpn
       61 antciithsl ggtallhylt alegewelpg lfivsgfvek lrvipeldef igqarvdvaa
      121 vkhhiahtev fvstndvlvd paltqqlada lsavsitihd aghfleddgy tefpqlgdri
      181 tqwlrsl
//
LOCUS       WP_284847805             249 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Corynebacterium sp. MSK004].
ACCESSION   WP_284847805
VERSION     WP_284847805.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK004
  ORGANISM  Corynebacterium sp. MSK004
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Corynebacterium sp. MSK004"
                     /db_xref="taxon:3050186"
     Protein         1..249
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27365
     Region          25..131
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mttlplgarr rtrgvceddw sarptaerpw pvilihgtcd skgvwqvlad mlraagwatf
       61 apdygtrata plqesarqld ayinavlavt gaekvilvgh sqggllaryw mrmhdgaefv
      121 rhvvcisapn hgttqggias plfrgerqee vvrtlidgwf gpagmqqvvg sevveatnrd
      181 sevepgvsyt ciatrsdavv vppntcflng pqvrniyiqd ierraiirhe dmpldkrvch
      241 vvleeleql
//
LOCUS       WP_284848013             149 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Corynebacterium sp. MSK004].
ACCESSION   WP_284848013
VERSION     WP_284848013.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK004
  ORGANISM  Corynebacterium sp. MSK004
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Corynebacterium sp. MSK004"
                     /db_xref="taxon:3050186"
     Protein         1..149
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16130
     Region          46..>107
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mkaeghsgdg hslslsgfft eaqakvrdka karaqradti ghlgpeavva fvdgemaaky
       61 ahrvrihlvh cpecraeihh qrnaaewvre csveshvkap dslmaklagi ahqgaspgpd
      121 aeapahqprq dfldkvemvv rairhnqrg
//
LOCUS       WP_284848270             402 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Corynebacterium sp. MSK004].
ACCESSION   WP_284848270
VERSION     WP_284848270.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK004
  ORGANISM  Corynebacterium sp. MSK004
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Corynebacterium sp. MSK004"
                     /db_xref="taxon:3050186"
     Protein         1..402
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43115
     Region          1..396
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 manvlgivlf algigitval heaghmftar afgmrvrryf igfgprvasf trghteygla
       61 afpvggfcdi agmtaqdefl teeekpyamy tkpawqriiv laggitvnll lgfiilllia
      121 mttglpnpda dvrprvgevs caanqkadge lepcqgvgpa geagvepgdi vlalngetmd
      181 sfaqlrdtvm sypgdtvtlk verdgeprdf ditlatvtrl ngeghlvevg aigmsnqiid
      241 iretysfvda fpatarysgy alnatvqgia qfpakipgvv asifgqerdv ngpmsvvgas
      301 rvggelvers lwssffmmla tlnfflalfn liplppfdgg hiaviiyeki rdalrrlmgk
      361 dpkgpadytk lmpvtyvlaf llmavgalim iadvvnpirl fg
//
LOCUS       WP_284848075             937 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium sp. MSK004].
ACCESSION   WP_284848075
VERSION     WP_284848075.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK004
  ORGANISM  Corynebacterium sp. MSK004
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 937)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Corynebacterium sp. MSK004"
                     /db_xref="taxon:3050186"
     Protein         1..937
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=104128
     Region          2..935
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtlthldeft qalpyslddf qiegcqavea ghgvlvcapt gagktvvgef avslalrqgt
       61 rcfyttpika lsnqkyhdlv eahgedavgl ltgdvsinss adilvmttev lrnmiyagsg
      121 aldrlthvvm deihfladas rgavweevil nleehvsiig lsatvsnsee fgrwlttvrg
      181 dtevivtdkr pvpldqwmmv grkiyplfep dsggqvnael arriqrleag dsdngradya
      241 qnrasfrvra rhkgggrndr nkdrrsgapr aqdryrplgr pevlkelqam emlpaitfif
      301 sragcdgaly qclrsrmvlt sqeeaaeika ivdkgvegip dedlkvldfk rwrealsrgf
      361 aahhagmlpa frhiveelfv kglvravfat etlalginmp artvvleklv kfngeahvdl
      421 tpgqytqltg ragrrgidtl gnavvqwapa mdptavagla strtyplist fepgynmain
      481 llgmlgfdds lrlleksfaq fqadgsvvee treieraehr vrelqaqldq avdnlappti
      541 dgedpaeilm dymrlrralt eeeksarask reernkevaa vlarlqvgev iaiatkkrpt
      601 lavvitpanq tadprpwvtt etgwsgrida agidnppivv ghmklpraaq knprrhtkyv
      661 qdafkrdyyk rpkkmrtepr nrpnkkiaql rdalrehpvh nwpatdreql agvaqklarr
      721 erelhkleak veratdtlgr tferivdlla emdyvefegy gedrepvitd egerlakihs
      781 esdllvaqcl krgiwndldp aelagvaslc vfenrkatrg epsaasddma damnatwriy
      841 telvsdekrh nlpqtrepep afalaihqwt agaplaycma aanesgaelt pgdfvrwcrq
      901 vidllqqvak tgyeeeirrn arraidaiqr gvvaiga
//
LOCUS       WP_284848331             248 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Corynebacterium
            sp. MSK004].
ACCESSION   WP_284848331
VERSION     WP_284848331.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK004
  ORGANISM  Corynebacterium sp. MSK004
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Corynebacterium sp. MSK004"
                     /db_xref="taxon:3050186"
     Protein         1..248
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27626
     Region          3..223
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mrnkwywafk hiffgpalrv wnrpwsegme ripesgpail asshqavmds fyfpllcprq
       61 itflakseyf ttpgfvgrlq kwffssvgqv pidrvnkdas damlasaeri igrgdlfgiy
      121 pegtrspdgr iykgrtgmar ialttgekvi piamintrka npigswiprp vrvgmrvgep
      181 idprawaaer nldpqdhata raftdyvmkq lsemtgepyv dvyasdvkas lqaghgypeg
      241 aepgsear
//
LOCUS       WP_284848364             765 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Corynebacterium sp. MSK004].
ACCESSION   WP_284848364
VERSION     WP_284848364.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK004
  ORGANISM  Corynebacterium sp. MSK004
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 765)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 765)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 765)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 765)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 765)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Corynebacterium sp. MSK004"
                     /db_xref="taxon:3050186"
     Protein         1..765
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=84569
     Region          34..765
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mttekqdkta wrpgsvrgms arlarsltgg rvkinpaldp lmsihrefhp kadaellnka
       61 yamaerlheg vfrksgepyi thplavatia aeigmdtttv aaallhdtve dtdysledlt
      121 rdfgpevarl vdgvtkldkv algaaaeaet irkmivamat dprvlvikvc drlhnmrtmr
      181 flppekqakk arqtldviap lahrlgmasv kweledlafa ilypkkydei vrmvadraps
      241 rdkalkeika qvsqalkang iqaevmgrpk hywsiyqkmi vrgrdfaeif dlvgirilvd
      301 dinscyaaig vvhslyqalp grfkdyissp rfgvyqslht tviadggstl evqvrthemh
      361 ynaefgvaah wryketkgrn sghqeevdqm awmrqlldwq keaadpnefl dslrydltak
      421 qifaftpkgd vinlpagstp vdfayavhte vghrcigakv ngklvalese lksgdkveif
      481 tskdpnagps rdwqeflvsp raktkvrqwf akerreehle agrdalaaev qrgglpmhrl
      541 ftassmkqva eqlhypdvda lytaigaghv saqhvanqlm alfgdrddav dalasrtpls
      601 elensraqht kdsasgtgil vegspdvmak lakccqpvpg daifgfvtrg ggvsvhradc
      661 tnaeklksep ermmqvewag gpkssgafsa tlqleaidrq gllfeltrif sdqslnvlsm
      721 tsnrgddhia tvrftfsvsd tkqlgqlmtt lrntegvfdv yrvta
//
LOCUS       WP_284848365             702 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Corynebacterium
            sp. MSK004].
ACCESSION   WP_284848365
VERSION     WP_284848365.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK004
  ORGANISM  Corynebacterium sp. MSK004
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Corynebacterium sp. MSK004"
                     /db_xref="taxon:3050186"
     Protein         1..702
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=74290
     Region          31..527
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mnfrrfgqll aattvtavav sgapafaaea dqvtisvtnf tdfhghlela enfdkeseel
       61 vgysemgaar maalikavnk dqeyaltssg dnvggsafvs aisedkytne alnamnldvt
      121 avgnhefdkg tddlmgrikd qsnfpilgan vtkdgkplld asfvkevdgv kvgfvgtvte
      181 ntkykvsaas ipgvefsdpv eatnkeasrl ketgeadvvv almhedaqqy aegfskdvdi
      241 lfggdthvkt qgevaregam plywaqgyey gkvlndvdit fdkaekkitk idlkqydvad
      301 aevfaqlqgl eddpevakvv eeakkvaeie gaktagttek amyrgsdegk dtgsnrgves
      361 tlnnfiadgq ryalskqtdk dieigvmnag gvradlkqgd vtyqdifavq pfgnsvitae
      421 vsgaafital enqwkpgqsr prlalglsnn vtvvydqkae qgkrvksvti ngepidpekn
      481 ysialssfla sseteaggdg ffepgsiknr ndvgymdtna midyiasges kvrtgqgqig
      541 ahvsgdlkpg keitvdlssl nysnaeepqa kkvtvalgda kaeadidnaa qpgdeqfger
      601 gratvkltip eglkgeqkll ittdagteaa lpisldgddd akdpkdtgsa kdaassiglg
      661 vgitaaiaaa iaavigainm pvaalpapvq qlieqlrkqf ni
//
LOCUS       WP_284848485             327 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284848485
VERSION     WP_284848485.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..327
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35247
     Region          20..238
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mdnsrstaas dteaqpgqva affdldktii atssafaydr eflhnglitp qdalslslak
       61 asymlagqss tqmdstrdql tsmitgwsek qvreivretm hnvltpaiys eareliqahk
      121 kagheviiis asarqlvepi aeelgitevi steleivdga ftgvvefyck gtakaeaitt
      181 lvgkhgyelq qsfaysdsvt dapmlelvgn pvavnpdrpl kklalergwe irsfkdpapl
      241 fqmpgakeig igagllagvi alitagtlls kfyapnkhea saletaqalt entgrylnst
      301 arairrtiin qhtisanilr karegia
//
LOCUS       WP_284848502             609 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284848502
VERSION     WP_284848502.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..609
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65496
     Region          11..609
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mqeafspaky tiepgqtllt ltidavkaqp kaeifsrpkn htwvsvsrqe fldevyavak
       61 glidagveqg drvalmsntr yewmlinyai waaggvvvpv ypssslsqvq wiiensgavl
      121 gigetqehte ilrmlqladd geprvkdsts qmrsffeind gavdvlqaag ktidddvvdk
      181 riaatatddv aslvytsgtt grpkgcmlth rnwnaqilgl lsnpiggiar pgkhvltflp
      241 lahvlafsvs aaamisgatq nfwpdfatla tefqrskpnl ilgvprvfek vrngarakah
      301 dsgaiqgalf draeataiay sraldtekgp slalrsahka ldklvlskir agmggevdyc
      361 isggsamspe lmhffrgigv pvyegyglte taaaatvdfe eqkigtvgpp lggtrvriap
      421 dgelqlagdl vfagywrnae atdeafdgqw yctgdlgeil psghvkivgr kkdlivtagg
      481 knvapggmed glrshplisq alvvgdgkpf vavlvtldee algrwksqhn vdasrsvadv
      541 ahdaslraei qdainavnat vshaeaikkf yildddftee sgeltptmkv krnvvverys
      601 evldklysr
//
LOCUS       WP_284848492             460 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284848492
VERSION     WP_284848492.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..460
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48521
     Region          4..460
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 msenmkvdvl vigfgkagkt iamnraaagd rlalveqssa myggtcinig cvptkalltd
       61 aeshhakpta ddstafaeai qrrgtltskm nqvnldlaeg kgvivvdgha sfisektvev
      121 tggddrmeia getviintga vpvvlplpga dlervidstq aqqlderpes llivgggpig
      181 mefatyfakf gtkvtvvdtv dkpfanfdrd iaehvgtimd nlgitwitga qvtefrenga
      241 davttvwkdg dgneqtadta qvlvavgrkp atkdlgldka gieltergav avdkhlrtnv
      301 egvyaagdvn ggpqftyvsf ddhrvilsdr wgdgsrttdn rvvptttfid pplatvglge
      361 daareevear gntldvkaad ikdipimprp kilgkpegra kilveretdr ivgatllcvd
      421 aqelintlal amsaeipast vgggiythps ssevfnallg
//
LOCUS       WP_284848603             413 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284848603
VERSION     WP_284848603.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..413
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45451
     Region          122..398
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mpsslfqraa alaltaafsl pavaavssav atpqahaqpg ssetssriaf dgssapmaew
       61 skdpavqghv lnvlqffqnh tpwhqlpmwn lwgeqtpyti dkeqdfaqpr lihreaderf
      121 averlyvesp amrrvvqvqv qypkdrdtaa pmlylldgvs aprqsgwlrk gdvqgtmane
      181 hvttimpvea ggtnytdwna tdpylgrakw etfltqelpg vmeqqtgipf ngeryiggls
      241 mggsaavrla nlypqlysgt fsvsgcyssi stagrayfdl aalvmggnpe lmwgpgntpe
      301 rlrndvvsdp kgiasmpvyi ysangyateh dielarpegi ptffgnitle kltnqctael
      361 ehslqekglm heriefdhaa tgihdwpyyk qqlpvawasv tqgkytypnq aen
//
LOCUS       WP_284848615             227 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284848615
VERSION     WP_284848615.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..227
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24003
     Region          <119..227
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mmnkqialis viglvlsvav gfgayamlhs stghvageta vsnkaespag eamegsvaqd
       61 egaglrrpac psleipgaqv qlpclseqav tdadkndels tgekneaigg dagaagdeit
      121 vvnvwawwcq pcreeipylq evqdkhpewq vvgvhadkna kngagmldem gvdfvsyqda
      181 hntfaselgl pgvipitivy vgneqrkvfv qpfrsteeii esiegvl
//
LOCUS       WP_284848650            1175 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284848650
VERSION     WP_284848650.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1175
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..1175
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=124899
     Region          244..390
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <646..1119
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 msvkstsprn prgggernka ranstrpapr tgpgraagkk lsfgmpgktg gdqaksreek
       61 sdsanletvv fgsaqraant shertgsafr avgsgiataf sktsdalkrf gnigqadddy
      121 dayadyddli ddadtdadaa emdrqatdkn kklknspagl dedlystdmt skkaktkkrq
      181 rssgamaqsr grkrstdthv sdddldqhgd daqaeqtegd evavsesalp aakpevgvps
      241 srsdaialtl igvaivlgas vwldiagfig raiatathav lgagafiipv alviaasalf
      301 sgrrvavehr arvsmgtali vismlglihl fsgaptewpe rfvaggalga wtggalaagf
      361 spyvavpllf lviiygalkv tgitvkefte ylrnvisgng sknldadpdr esvgghneyg
      421 daygrandei aaiasgaqrt prrraplrtn pvasqsnrpg fttsqssnag thdvvangkk
      481 stglfprteq psqvehtevl ysngsrehqe qvsktaagle saptasdtde fpavldsptr
      541 srsartepev ekteklplap edavdqaqag lqqkqaaenp rtvdtkhpdt arqtrvpgvk
      601 pqsdarqpva qqatqvglas qindgpreda gatqqaskla teytipsagl lepgrapktr
      661 teindrtiea idacfaefkv daqvtgftrg ptvtryivel gpgvkvskit nlqsnlayav
      721 atgsvrilap ipgksavgie vpnsdreivr lrdvlesevi agdedptlvg lgkdiegefi
      781 sssiqkmphl lvagstgsgk safvnamlvs lltratpddv rlilvdpkmv eltpyegiph
      841 litpiitqpk kaaaalqwlv eemeqryqdm rsarvrhikd fnhkvrtgev qapagserkm
      901 epypfivcvv deladlmmta pkeieesivr itqkaraagi hlvlatqrps vdvvtglikt
      961 nvpsrlafat ssstdsrvil dqtgaealig mgdglfipqg grpvrmqgaf vsddevyavv
     1021 eaakeqgepd ytegvtedkq aeakkaiddd igkdmddlle avelvvtsgl gstsmlqrkl
     1081 rigfakagrl mdlmetrgiv gpsegskare vltkpeeldt tiwmikgadp adaprevqeq
     1141 qnqgqpdnvv edsagdtags ahitkatynp tsqaf
//
LOCUS       WP_284848657             488 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284848657
VERSION     WP_284848657.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..488
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53736
     Region          3..488
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mqhlhhdfad hfpdlcldwr aaeapapqiv clneplahel gldpswlrsp egigflcgth
       61 lpegaqpvam gyaghqfgqf sprlgdgral llgelrdgag klrdihlkgs gptafsrggd
      121 gwgalgpmlr eylvseamha lgvpttrsla vistgraiar ervvpgallv rvahshirig
      181 sfqyaqltgg eelvcklaey trnrhypdaa dtrevfhhal dtqlatvaqw mrlgfihgvl
      241 ntdnttlsge tidygpcafi defdehavfs sidhsgryry rnqpqiigwn farlaeamlp
      301 tfaadpdeav gfaqetmntf qerwrkahna ercraigvey sednaklade fyelvgktsp
      361 dltsahralv daadrnghti pasgvdttrt pvsmlarhlg dttparewia rwlnhapsph
      421 alarlhpmii prnhlvenal ssatdgdlep fhqllhaith pfgrnhppef lkpaprefsa
      481 tyqtfcgt
//
LOCUS       WP_284848761             219 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284848761
VERSION     WP_284848761.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 219)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..219
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=23275
     Region          <13..205
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 maklpfhhak qpvviiglgr fgmalgkelv qsgvevlgid vdeavvtkaa sllthavvae
       61 ttdqealrql gvhdahrvvi gigsdmgasl ltasavmdlg vpnvwakadn qqqakiltqi
      121 gvhhvvrper dtgrrvahli aghvqeyief dsdfamakla pplwmhgrkv eqtpqgiaiv
      181 avrsadahfs tppagyvlrs gdlviaagri ndldkfads
//
LOCUS       WP_284848850             313 aa            linear   BCT 25-DEC-2024
DEFINITION  S1 family peptidase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284848850
VERSION     WP_284848850.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Perona,J.J. and Craik,C.S.
  TITLE     Evolutionary divergence of substrate specificity within the
            chymotrypsin-like serine protease fold
  JOURNAL   J Biol Chem 272 (48), 29987-29990 (1997)
   PUBMED   9374470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475742
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..313
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32880
     Region          1..224
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mstkkialsl aaaatmavss iatpfahavq ggtpvsgdda naknvvivsg ctgtaisphw
       61 vlaarhcfgd gttaklvrtg iektgtkgse evyhapsgdi slvrmsthss fdfdsypela
      121 teepkpgqvg tfygwdntsh krlphsqaev qgvyqdgsyd ngkmytvhhk dgaysqpgds
      181 ggpffingkl sgvasaisgd gvplnladis aqldwikqtm akngdepnlg ngavngmdki
      241 lqekelkkpg aekdkengqq tqeqapnpeq pqpqpaqpek qepkpaqtkp gkqqpvkpar
      301 pnqgspllss ssl
//
LOCUS       WP_284848941             519 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284848941
VERSION     WP_284848941.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..519
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=59098
     Region          9..512
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mpsekdapqp almwfrddlr lhdnaalawv akqgpviavv idenatvtga ralgaamrww
       61 wqrsvhqlqh klhahgvpll yyqgdpraii pavvkefavs avgwsrryhk plreldaqlk
      121 hllqekgvaa ksfpghllte pwevqtqqgk qykvytpfak targvaednv asylntgndq
      181 apsptshdel apiglagpga dlasarplpd wdeadwthsl aqhwspgens awkvaegfld
      241 qltaaarkqa phyaadrdrl dkqatsrlsp ylrfgeisih rlwamvtean dtgriageda
      301 saflsellwr dfawhrlyhl pdlhrrnvre qfdhfdwhwd ekearriant rrdprcpete
      361 kdipeiatad dfrsvfsawr agktgiavvd agmrelwatg tmhnrvrmvv asfltknlgi
      421 hwrhgeawfw dtlvdadpas npfnwqwaag cgddaapyfr ifnpdtqakr fdpdyryiqh
      481 wvpeyatpmy pqpvvdlkas rrqalaayee mknfhprpe
//
LOCUS       WP_284848967             273 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284848967
VERSION     WP_284848967.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..273
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28678
     Region          12..272
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mtldfsapft ertprvsraa klhraavrkk eqrfliegen svdaavstga atdlfvtqsa
       61 aerfehivst agfmdvyihp itegaaklls ettttpgifa vclpvmfsag kiikssprll
      121 tipvetsepg nagtlirvsd algadgvvfa gntvdphsnk varasagslf htpvaretgv
      181 ndvlgqlraa nlqilatsad geitleeaee sgmlhkptaw llgneahgls agvaaradhr
      241 vsipirgnae slnlataaai clyesakaqn rrr
//
LOCUS       WP_284849057             773 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284849057
VERSION     WP_284849057.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 773)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 773)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 773)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..773
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=80168
     Region          19..757
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mptprstssp ipapstasst ielnisgmtc ascaarvekk lnkhdgvhae vnyatekati
       61 tgdtdaldad aliatvektg ygaeltpeat aagtqapqda maeaeldslr rrlivsavla
      121 vpvialamvp awqfdywgwv slaltlpvvv wagwpfhrat wqnlrhgsvt mdtlislgts
      181 salvwsmval ffgsagdpgm rhgfdftvsr gdglshiyle vaagvitfil lgryfekrsk
      241 rtagsalral ldlgasevtv lrdgaeatin ineltvgdef vvrdgekiat dgvivsghst
      301 idtsmlsges vpveagpdda vagatinvgg gklvvratkv gkdtqlaqma qmvedaqsgk
      361 asaqrladki sgvfvpivia vslltliawl lidgdwaaaf taavavliia cpcalglatp
      421 tallvgtgrg aqmgvlikgp evlehsrgid rvildktgtv ttgvmeladv vtaegfdrde
      481 vvhlagsleh esehpigrai araatnqrad gtlsevsdfk sirsagvrgv vegrrvavgk
      541 psladnedlg alqqpflsaq tqghtalmvl vdgtpaavll vadqvkptsa aaiqqfhalg
      601 ietmlltgdn qavaetvaae vgiehvraev mpedkvavia dyqdrgykva mvgdgindap
      661 alaqadlgma mgtgtdvame saditlvrgd lraatdairl srrtlgtikg nlfwafaynt
      721 aaiplaalgl lnpmlagaam alssvfvvsn slrlrgftst agagvdatag atv
//
LOCUS       WP_284849061             344 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284849061
VERSION     WP_284849061.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..344
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=37836
     Region          1..325
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mrlllianpn stsqtnelfr riiplvrsid dshlitkfth yaghaedmtr glsrddydvv
       61 iavggdgtvn evvngllgkv gdgrrkasev palaviptgs anvfvralgy pldpvhttel
      121 lvghikknlr rrirlgtwnd rwfavnagig idadvlhsid klreqgfsat plrylrisyq
      181 awrrilhapp kisahaesad gqtqhidqap lvfasntnpw tflgplpvvt nprnsfdkgl
      241 gtfgltdlkg vggfvgllhl fgadekgrln kftdartlrf ddatritlec dealrfqadg
      301 eaqgklktve lnsipdaiev fspeeiipvq qrgilavvrd lfri
//
LOCUS       WP_284849137             335 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284849137
VERSION     WP_284849137.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..335
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36593
     Region          65..335
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 maaaaipapr pktgprydaa verltnltfa lqgaaqsggn psrsaewiha nvagyhenkh
       61 sfrmqlqrdv atlaragvhi dssvgengas yrlnpesyrl pevsftpeea tvlgiasevg
      121 rnsglgalsa agwtklaasg arreitpgag ylainditsl dpevlrailt gvahklrisf
      181 nyqhhsgaei qrrtmdlwgi vphhnrlyvv gwdvdrqaer sfrstrisdi rrsrevatht
      241 epsgslreiv ektlavrdva datirsrrqa appleeaade iqevdasdei rlfikgadre
      301 wlirtcaaya aeavveqpkd ireqvsrllq kagar
//
LOCUS       WP_284849573             344 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease
            [Corynebacterium].
ACCESSION   WP_284849573
VERSION     WP_284849573.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..344
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35261
     Region          13..344
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mttisstlqa qqrrrhvrvl aatlvfalia laaylvllgq gpldlsprqv fdvltgggse
       61 shirvvwdlr lpvaiatviv gaalgvagsw tqtmarnpla spdilgvtgg asvlvvlgtv
      121 hsrpgfadgi pdfwwracla migaflvvil lavlggigts nrivivgial slmfqavvay
      181 lmrsaqiqra aeaqtwlags tgfvrmeviv pllvalapfl aigiwcarel pllahddssa
      241 itlgvnisrq rallliaatg icavvvsvvg pigfiallap hlarmaartp tpspvasaaa
      301 gaalltvcav iagaipvnap vgavssvigg calvvlvwna arrs
//
LOCUS       WP_284849574             359 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease [unclassified
            Corynebacterium].
ACCESSION   WP_284849574
VERSION     WP_284849574.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..359
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36144
     Region          54..350
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msattkdgqt iqtgstaqnp tatpvmergk grttflvali laslalavas lalgsrsipp
       61 deviaalrra geqdirdivw nlrmprtfla yfagaalava gvlaqswtrn pladpgfigi
      121 tagasffval gtaigiattt gmrttlalvg agittllvla vsrrfqdplt lilvgagvsa
      181 algsgaaiig lystdvldsm rrwtigstfg rgpedvaiag iglliglaca tmaarpldll
      241 amgeesslal ggspttarvg aalsvvvlag sataatgpia fvgfaiphiv rrvvgpsvat
      301 milpsallgg cavlaadiig rlivgnsele msivlaivga pfliwgahrg vgrawgdna
//
LOCUS       WP_284849605             328 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium sp.
            MSK078].
ACCESSION   WP_284849605
VERSION     WP_284849605.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK078
  ORGANISM  Corynebacterium sp. MSK078
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Corynebacterium sp. MSK078"
                     /db_xref="taxon:3050200"
     Protein         1..328
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35280
     Region          13..324
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mvasrstpsr qdaaverlin lsfalqgaan sggspdrsaa wirshvagyn dksdeaftka
       61 lardiatlqr agvpivhtgr edgasyrldq snyqlppvef tpeeamvlgi aggvgtpggl
      121 sdfslsgwtk iaasgasrnl egapiytavn ditrlapevi tfvlaavrnk vritfsyrph
      181 paaetvrrtm dpwgvvnhqs riyivgfdvd raaprvfral rlsdikrshq paehievtvd
      241 idklvkealq rgekvdatly ipegqaqele svgtrtadgt vvltgvqkdw lvrtaagyap
      301 evkvlgppev rteiinllra aanhngae
//
LOCUS       WP_284849616             240 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [Corynebacterium].
ACCESSION   WP_284849616
VERSION     WP_284849616.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..240
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26251
     Region          12..204
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mttvsnfqll srpaaifwdm dgtltnsepl wgeatyylse vlgkrltpsq rletvgatft
       61 ttlricadna gvvlgqgdve ayrhkmfdym ktlfagrlei fpgipellts lhqdgmpmmv
      121 ttntdrdvad aaiavigsey fvdticgdev ptgkpapdmy leaarrlqld paqclvfeds
      181 pagmraavaa gctviglped egvevpegvv eisrlrdsrh lagarhvdvy ewfraiqemk
//
LOCUS       WP_284849659             694 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Corynebacterium
            sp. MSK078].
ACCESSION   WP_284849659
VERSION     WP_284849659.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK078
  ORGANISM  Corynebacterium sp. MSK078
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Corynebacterium sp. MSK078"
                     /db_xref="taxon:3050200"
     Protein         1..694
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73210
     Region          41..515
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mqfrrigqlv aattataval sgthalaqed tttisvtsit dlhghledgl sdpakagdei
       61 gvarlqslik qvnegqefnl tssgdnvggs afvsaisddk ytlealnamg mkvtavgnhe
      121 fdkgtedltd riqpasdypi lganvlkdgk plldashvee idgvkvgyvg tvtqntkfkv
      181 saakipgvtf tdpveatnke atrlkesgea dvvvslfhed aeeyaegfnk dvdilfggdt
      241 hqttqgtqer dgalplqwaq gyeygkllnd aditfdkaag evkkielkqy datdaaqvep
      301 daeiagivkk aqdeaevkgs ktagtvetdl frgsdegqkp gsnrgvestl nnfiadgqry
      361 amskqvgedi dlgvmnaggv radlqggdvt ykdifevqpf gnsvitakvs gkdfitalen
      421 qwqdgssrpr lamglsnnvq vvydhtashg ervksvting epldadkdys ialssflass
      481 dsekggdgyf eagsikdknd vgymdaqami dyiasgesev rkgqgqigah idgdiapgke
      541 itvdlsslny tsegepmakt vtvklgdeea tanidnskqe gddqfgergr aqvtlnvpeg
      601 ltgsqnleit tdagtqailp vkvdeaggde agsqedgsed edspklpqgs siggaalaiv
      661 aalaagiafi glnpqvlpap lrsifddlrk tfhi
//
LOCUS       WP_284849752             752 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium sp. MSK078].
ACCESSION   WP_284849752
VERSION     WP_284849752.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK078
  ORGANISM  Corynebacterium sp. MSK078
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Corynebacterium sp. MSK078"
                     /db_xref="taxon:3050200"
     Protein         1..752
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=82141
     Region          29..745
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mnsapknspa thspadasss sradnagisa ieaeqnyvdg lfdrlddeva aanarlnevq
       61 aevdpatpda dalvrretey hglqakldrl nvaqmglvfg rididapgdn pteegldrry
      121 igrmgldare enyrtllldw rapmarpfyl attaqpegvh trrqirmsgr tvtdvndeal
      181 dgpgvreeea gvasesalyf amqgartghm tsivetiqre qdeiirdntr gvmvveggpg
      241 tgktavalhr vayllythre llsstgvliv gpntnfldyi srvlpelget gvvlstiggl
      301 fpgitpthte glvgreikgs aamaeilsaa vkdyqqvpne prditvdglt ltitpsmvkr
      361 artrarrsrk phnqareafi ehfvedlaqe matkvgtdpl ggenllsrad vdqfhddlai
      421 desvvgcidd fwpeldpsev laallssrer iasaargyde etqaalyrad gyawtdsdaa
      481 lldelavlig lpnpeekkaa kdaewreqia daegaldils ssestdnddd mfeaeilsah
      541 dvidaetlaq rqevrdtrtt aqraredhtw afghiivdea qeltpmewrm lfrrcpsrwm
      601 tlvgdtsqtg spagvddwge alepfiaqrf rhhlltvnyr tpepitelan gllasidpda
      661 tpaiairdge pvrrladadf tpgitteddg rltavidstn aeavkglefd hvivlhprei
      721 vdaspqglqn lyvcitratq tltlvgdtag vl
//
LOCUS       WP_284849758             731 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: heavy metal translocating P-type ATPase
            [Corynebacterium].
ACCESSION   WP_284849758
VERSION     WP_284849758.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 731)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 731)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..731
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76485
     Region          2..725
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mshvdlgvsg mtctscssrv erklnkvdgv easvnfates asiefdpets taadlikvve
       61 gagysafdms gsddadqggd adaegtpvdd araeeqqsll rrtiisavls apimvvsmvp
      121 alqfqnwqwa camlatvvfi fggapfhsat wtnlkhgsft mdtlismgts aaylwslyal
      181 ffgnagepgm tmsmswssss aemdhiyfes vgmvitflll grwfevkakg qssealrtll
      241 smgakeasvl rdgkekripi sqlqvgdvfv vrpgekvatd gevvsgnsav dasmitgesv
      301 peevgvgdtv tgatinasgk levkatqvge dtvlsqmatl vtnaqaskap vqrlvdriaq
      361 vfvpvvigis vltllvhlif ggvapafiaa vsvliiacpc alglatptai lvgtgrgaql
      421 gllikgpeil estkqvdtiv mdktgtvtag emsvtavhgn vleyaaaver nsehpiaqai
      481 arerdvepgt dfststagve atvdgvrvgv gkprgdlgqy adafreaeaa gatpvavyld
      541 delaglievr dtvkptsaea vqqmkklglt phlltgdneg aakrvaeevg itevtagvvp
      601 eekvdvikkl qseghnvamv gdgvndaaal aqadlglamg agtdvaieas ditlmngdlr
      661 saadairlsr rtlqiikgnl fwafayniil ipvaafglln plfagiamal ssvfvvsnsl
      721 rlrkfssqry d
//
LOCUS       WP_284849761             389 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Corynebacterium sp. MSK078].
ACCESSION   WP_284849761
VERSION     WP_284849761.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK078
  ORGANISM  Corynebacterium sp. MSK078
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Corynebacterium sp. MSK078"
                     /db_xref="taxon:3050200"
     Protein         1..389
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40787
     Region          11..388
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mnesleqvas arldkwredg lwrspsvfgs gqvpesslrt atgktakdav lfsssnylgl
       61 aehpeiknav kdsvdhygag sggsrlttgt selhvaveaa aaqltgypds vffatgyqan
      121 lstlqalasp eltivsdarn hasiidgcrl akasgaslvv tahrdtrave nalvtrttky
      181 alvitdglfs mdgvlaplpe lsrlarehga wlmvddahsf gtvgnrglgl peyfgvqpdi
      241 qlitaskalg aegglvatsk pvaqllrqqa rsfvfstspt patsaavlaa lkliesdssl
      301 vsqlqgniay whstrgttpq qgpiipvhvg deaaamdasa alldhgfivp airwptvarg
      361 aailrvtlma thtraqidal cteleqlgl
//
LOCUS       WP_284849785             349 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium sp. MSK078].
ACCESSION   WP_284849785
VERSION     WP_284849785.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK078
  ORGANISM  Corynebacterium sp. MSK078
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 349)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Corynebacterium sp. MSK078"
                     /db_xref="taxon:3050200"
     Protein         1..349
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36654
     Region          37..342
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtqtmsketd tfarrrtqra wvfvllgilt vlaalisvvl gqyyvplsdl fpilaaghaq
       61 dsltasvvwd irlprlvlgl vvgaalgvag tlmqavfanp laepsiigvt sgagvgaavv
      121 ivfnieffgt ftvpaaaflt allvtfiiyq laryngrvav vhliltgiai navcnaiisf
      181 mvylaptanr eaivfwqmgs lngsqwkhvw avlpivvvgl avalrlgkql dvlalgeraa
      241 ahtgvnvprl rivaivasav ltaaavsfag ligfvglivp hllrsivgpe nrillpasal
      301 ggavligfad vaartmipfa dlpigiftal vggptffill rrimrkgvh
//
LOCUS       WP_284850648             464 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284850648
VERSION     WP_284850648.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..464
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=48642
     Region          1..463
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrltvfglgy lgathaacma eaghevlgvd iaparvaqlq agrvpfyepg laelvargve
       61 sgrlrfscdy rqaaefaqlh fiavgtpera dspaadtsav eavvgklapl lrgehvlvgk
      121 stvpvgtaar lqeratsiss atvdvvwnpe flreghavad tlrpdrivvg tgaestpkga
      181 dapngvgsap alqklrevyr aplergtpfl vmpwasaelv ksaanaflat kisfinaiae
      241 vceavggdva avaealgyde righqylgag lgfgggclpk dvrafrarad ecgagdalaf
      301 lgevelinar rrqrvvqlas elvaqspkaa epagsarpgl sgavitvlga afkpnsddvr
      361 dspalhvaae lalrgarvrv cdpqavenar rvypgleypa sladgvaead lvilatewpe
      421 yreldpvwaa elvaepvlld arnaldlarw rdagwqvhal grgd
//
LOCUS       WP_284850727             477 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Enterococcus faecalis].
ACCESSION   WP_284850727
VERSION     WP_284850727.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..477
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=56392
     Region          1..465
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mkrvmwfrrd lrlqdnkala halqnsaade lillfqmnpq qfiqesanhn affaslasfk
       61 eridqeahlq imvgepldlf srlkrklpdw qaiyfnedtc gfgakrdqqa mrffeenniq
      121 sfsfqdaylh gseeikkndg skyqvftpyy nkwkeapket pipvsytaek ifsaclfpee
      181 eaayreqiar iplkhysvge ktarrclntf idqklrsyen krdfpyqdqt shlstflrtg
      241 elsirtiwqe lasapsslsk etfkkelawr dfynmiystf pqqkeeaiqe kfryiqwtnd
      301 pemfakwqkg etgypiidaa mrqlnqtgwm hnrirmitas flvknlhidw rwgekyfqkm
      361 lidydaanni ggwqwaastg tdavpyfrif npiiqskkfd ndgqfikkyv pelkqvpqky
      421 ihqpnlmnea lqtqyhvhlg enypkpivdy asskkqtlfl yeaskeihqe mnnprfq
//
LOCUS       WP_284850743             773 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284850743
VERSION     WP_284850743.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 773)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 773)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 773)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..773
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=80150
     Region          19..757
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mptprstssp ipasstasst ielnisgmtc ascaarvekk lnkhdgvhae vnyatekati
       61 tgdtdaldad aliatvektg ygaeltpest tagtqapqda maeaeldslr rrlivsavla
      121 vpvialamvp awqfdywgwv slaltlpvvv wagwpfhrat wqnlrhgsvt mdtlislgts
      181 salvwsvval lfgsagdpgm rhgfdftvsr gdglshiyle vaagvitfil lgryfekrsk
      241 rtagsalral ldlgasevtv lrdgaeatin ineltvgdef vvrdgekiat dgvivsghst
      301 idtsmlsges vpveagpdda vagatinvgg gklvvratkv gkdtqlaqma qmvedaqsgk
      361 asaqrladki sgvfvpivia vslltliawl lidgdwaaaf taavavliia cpcalglatp
      421 tallvgtgrg aqmgvlikgp evlehsrgid rvildktgtv ttgvmeladv vtaegfdrde
      481 vvhlagsleh esehpigrai araatnqrtd gtlsevsdfk sirsagvrgv vegrrvavgk
      541 psladnedlg alqqpflsaq tqghtalvvl vdgtpaavll vadqvkptsa aaiqqfhelg
      601 ietmlltgdn qavaetvaae vgiehvraev mpedkvavia dyqdrgykva mvgdgindap
      661 alaqadlgma mgtgtdvame saditlvrgd lraatdairl srrtlgtikg nlfwafaynt
      721 aaiplaalgl lnpmlagaam alssvfvvsn slrlrgftst agaavgatag atv
//
LOCUS       WP_284850886             215 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284850886
VERSION     WP_284850886.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..215
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=22571
     Region          19..209
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mrilikhnaq haphtqpapr ivlasqspsr agilrsagve pviepahvde daiqaelgna
       61 spseivtala sakaqaiari ypndvviggd smllldgvlq gkphtepati arwraqagrn
      121 aqlltghcli fggetyaeaa ttdiafaqas eadiaayaat gepwqcagaf tlealggwfi
      181 dridgdpssv iglslpvvrr alyhfgfsvs dfwna
//
LOCUS       WP_284851099             218 aa            linear   BCT 25-DEC-2024
DEFINITION  cell division protein FtsQ/DivIB [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284851099
VERSION     WP_284851099.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..218
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=23470
     Region          8..218
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 makkpititt aaivvvlalt aavfwfipvl rvssveisgt ervaeasild dsaiqegdnl
       61 lridasgaaa riakqpwvrg vtvsrhlpst veieiterev vgfiehddgp hlidhqghaf
      121 fidtppdeav eisgaiedeg avnaavsaia tipaeirrdi asvevkasha melhlhdgrt
      181 iywgvdeine qkaaalehvl hrdgqhwdis npglvtvr
//
LOCUS       WP_284851176             127 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284851176
VERSION     WP_284851176.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..127
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13861
     Region          13..92
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mthpnlpdqw etgkiiettr ekigmsrrsa arlagisesw wrkletgyvi rdgkittvnp
       61 tpealakvad viriptskll ssagfnpdev lvgsrqiahd midgidakhl paviaflkgl
      121 syglnnr
//
LOCUS       WP_284851807             223 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium sp. KPL2734].
ACCESSION   WP_284851807
VERSION     WP_284851807.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. KPL2734
  ORGANISM  Corynebacterium sp. KPL2734
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Corynebacterium sp. KPL2734"
                     /db_xref="taxon:3158312"
     Protein         1..223
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23294
     Region          2..217
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(5..6,8..9,12..13,50,54..55,58..59,79,86,89..90,95,
                     110,114..115,117..119,121..122,125..126,129..130,156..157,
                     159..161,163..165,167..168,170..171,175,178..179,185,187)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(113,117,120..121,123..124,170,173..174,176..181,
                     184..186,190,192)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(134..141,158,161..162,165)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mllsvlvina valshghlpt llisiafssi alatvkphyg liclcafals ylgywgllql
       61 pgstffafsa aifswlsrfv ismsigafgl ltltpstlts alrdlrlpgw atippavflr
      121 vlpiivaeak airdamvlrg lqpgakswft qptqssamli ipllgavvra gdelaasalv
      181 rglggptrpt ttadlsfklv dataiaglgl vvasvwlpte aql
//
LOCUS       WP_284852756             313 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284852756
VERSION     WP_284852756.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..313
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33981
     Region          137..295
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 msssrnafqr kpallwtlva lvvalavliv vavvrsgdde smsaggqdam hgpqapssaq
       61 sgnsdsqstp mpggeyspeq arelakqvep gtdfsrpnsp dptiigpgae itsnddilnv
      121 hrrnaedpfa mgaldapvvl sefsdfecpf ctrfavetap klkekfvdtg llriewndlp
      181 vngphaetga qagraagnqg kfyefhdvly nntyenqtgg hpgydvadyv rfakeagied
      241 lekfrteien eqyrdvvrqa lhyassigmr gtpafilgdr fisgaqpyev fedevyrqla
      301 kvadgtvphp ksk
//
LOCUS       WP_284852889             280 aa            linear   BCT 25-DEC-2024
DEFINITION  PaaI family thioesterase [Corynebacterium sp. MSK032].
ACCESSION   WP_284852889
VERSION     WP_284852889.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK032
  ORGANISM  Corynebacterium sp. MSK032
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Corynebacterium sp. MSK032"
                     /db_xref="taxon:3050191"
     Protein         1..280
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=30828
     Region          31..167
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 msigpslrrt lyklaekems pakakfllni wpplfgtgir iteiaddwsa grlelrlnal
       61 tanmhgaafg galfsmtdvl fgtlvmqrld vkkyeawtrt gsfefirpgk ngaylevevp
      121 demveklkae teggystvvp ytsvirnrdg slvgigqqel yvrrrgrkkp panpnqqdrv
      181 agenlisaar tlarlgmrgv enrdvlvrqe rtarrcispe sravawlhgv leygdvtvdd
      241 yraaglpdvv iealtsdnps paaqqlladv vtaresltkl
//
LOCUS       WP_284852909             758 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium sp. MSK032].
ACCESSION   WP_284852909
VERSION     WP_284852909.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK032
  ORGANISM  Corynebacterium sp. MSK032
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 758)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 758)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 758)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..758
                     /organism="Corynebacterium sp. MSK032"
                     /db_xref="taxon:3050191"
     Protein         1..758
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=83010
     Region          <259..388
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 merwnpdsal agqspsiems vlrsgaiiia vtgflwqves avrsvpfenf lshwfpfasl
       61 lifilsdmll iwavinntrr glitalrvpm yimlvflmlv stywdlphnv vgnalwyspf
      121 sglalaafal tvplhislsv mvfvpgliav inswllghtf wldmlsdvgf nlintfpfvi
      181 iagsaqpvar lidftyensr kvneraermr vrgeamssfn ayvhdyvlaa lsaigkgski
      241 dfsldeqtgl ffsprqtvsg rtfaesvraq lmsvspdigv tldtseeggp vrlpgevant
      301 fllaatevan nakrhagaaa ekkchirvas gevsigfrdd gtgfdpegid phragirlsv
      361 kgrmealrgg dalvnskpgk gtqvilkwhg ntspveeedv vdssahttsl ydlmgmsivf
      421 swqfygaivg vlfmvlvsng qlftaagqis lalaigllgl imygrhsqlp laraivtgva
      481 ivvlavvgly qpipnnlews yfwhfslisf asallairgr pwvalnsvlg gaimvellkf
      541 fpfapsdtth isisgvdllv rsvmlvagil tsimvrffmr tvpqsiqdyn ralyaagaak
      601 eyeissqsny ewlqrrvgpi fsaaavleep tprlqlrarl teqllrdvlr sphlnvgslh
      661 qavwdararg vhvrllddrn htqavsdstd vrriplvddd savaklmpnf leaidnaeeg
      721 svtirllppg rrafasisdd ngvqrfdeag erivmsrd
//
LOCUS       WP_284852980             368 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: diacylglycerol/lipid kinase family protein
            [Corynebacterium].
ACCESSION   WP_284852980
VERSION     WP_284852980.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..368
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=39882
     Region          1..321
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mrallisnpn stsntarrmp gvvralrsve girltsmfta ypghaaemva gktvrdydvi
       61 islggdgtin eivnglmnsn pfsalpatdl paiatiptgs anvlagalgi prdpvdaawy
      121 iasllrsrtr stisvghaae rcfvvnagig idaevistme qlrqngtrak avrylpaift
      181 awnqlrkspp qitatidgte fgrdlamavv snsnpwtflg dlpivtnptv slrrglgfyg
      241 ftslrgvtgl vaaanlagff trlrspfhve arerrvdnvq hieltatapl rlqldgeyin
      301 qceslnirvk qgainfvara ddytedqftk kvatrpvder llvvvtkkvm drtrrlfsts
      361 qkaeanpt
//
LOCUS       WP_284853021             353 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: esterase/lipase family protein [Corynebacterium].
ACCESSION   WP_284853021
VERSION     WP_284853021.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..353
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39259
     Region          56..193
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mddyspstrv fgpllrafpq aylrslhhpe wiphgvqdvr eildgkvtpe ldryngrtpi
       61 vlvhgtwmns fnsfamlgpf larnrpvfsl dygsdpaalv srlrsvkatt dlsdalaevt
      121 dlldrfrahl slpridligh sqgglhcrsy anasidslyd ealnrglnee aaeqyasdns
      181 pvravislag nhrgttawgm rrrlsalerc glpihklvdr lvgraciqql ldsdyiatln
      241 raargitrrg phylnigtpf dtvvrpwtga flpeqeghhi tnvnnatggg dwsdhlally
      301 spntlerihe fleeldgaea gdvphhprqr vlplygalpr rlgrrgsgrr dri
//
LOCUS       WP_284853035             630 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium sp.
            MSK032].
ACCESSION   WP_284853035
VERSION     WP_284853035.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK032
  ORGANISM  Corynebacterium sp. MSK032
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 630)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Corynebacterium sp. MSK032"
                     /db_xref="taxon:3050191"
     Protein         1..630
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=65073
     Region          28..629
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mssacgcehe pateiedldr pwwkdpelll pifsgvalci glaldwsgle tpatvlfwig
       61 lllgaytftp gairnlvtkr klgigllmti savgavilgy vgeaaalafl ysiaealedk
      121 amdraqsglr allklvpqta tvlrdgtave vaakelmage lmlvrpgeri atdgiirsgr
      181 ssldtsaitg esipeevapg devpagains agvlevqtta agtdnslttl vdlveqaqae
      241 kgdrariadr iarplvpgvm ilavlvgvig sllgdpetwi tralvvlvaa spcalaisvp
      301 ltvvaaigaa sqfgvviksg aaferlggir hlavdktgtl trnqpevtgv vpadgfdraq
      361 vltfaaaveq qsthplaaai aaaepeapaa ldiseeaghg iggtvegrrl lvgsprwida
      421 gplkgdverm esegqtcvlv tvddtlagai gvrdelrpev peavqtlran dvevsmltgd
      481 ntrtaralae iagiddvrae lrpedkasiv aelssktpta migdgindap alagatvgia
      541 mgatgsdaai esadvaftgh dlrlipqalq harrgsriin qnivlslaii ivlmplaisg
      601 vlglaavvlv hevaevivil nglraarakr
//
LOCUS       WP_284853105             226 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Corynebacterium sp. MSK032].
ACCESSION   WP_284853105
VERSION     WP_284853105.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK032
  ORGANISM  Corynebacterium sp. MSK032
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Corynebacterium sp. MSK032"
                     /db_xref="taxon:3050191"
     Protein         1..226
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=24815
     Region          1..222
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mlldqlprdd aritpgvvhl pgwlplerqa giitqlrdia rdlagtplam trpqlksgqm
       61 qvfmlhlgrm watnpyryvt hvggvrvppv pdnllqlate alraaalyde slnqwpsafr
      121 pdmalvnyyp pgatmgmhqd rnenspapiv slsigdealf riggtenrnk pwddvtlasg
      181 dvivfggpkr lafhgvpktr pgtlpegcgl kegrinitfr qvensh
//
LOCUS       WP_284853113             176 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium sp.
            MSK032].
ACCESSION   WP_284853113
VERSION     WP_284853113.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK032
  ORGANISM  Corynebacterium sp. MSK032
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Corynebacterium sp. MSK032"
                     /db_xref="taxon:3050191"
     Protein         1..176
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20416
     Region          12..71
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(15,19,49)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(18,48)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(25..26,42,45,49..50)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 msfadeesrl irrmtekrle kgwsqnefar klqevglnwk qptvdrvekg trplrfteal
       61 aiakffgetv esmsapeeft rwqllvreaa vamlaerlvh yqwenesmee rvieiygrsv
      121 yedlpksvak wvdwishksp ttqaslalyd hdfdlyeaaa qesgrifvss mhsvpk
//
LOCUS       WP_284853139             331 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease
            [Corynebacterium].
ACCESSION   WP_284853139
VERSION     WP_284853139.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..331
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33428
     Region          24..319
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mltsaalvgl allllaslyl gskdlsigev tsilmhgphp stqsgiiwdl rvprtllavi
       61 tgaalamaga iaqswtrnpl adpgiigvna gasfavaaal tlgwattvgq rtlvglvgaa
      121 vaasivllis rvsrnpltlv lvgvgvtfal qaatnmlsly ssdtleglrr wtvgstagrg
      181 medvalaalg lalgalcgal aarpldllam gedsarslgs sptrtrllaa aaviilagsa
      241 tatvglvtfv gfavphllrp ftgpsltrll lptgivggaa vlladivgrf vlqpnelems
      301 ivlaivgapv milavrrkks sptsndselt i
//
LOCUS       WP_284853218             679 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Corynebacterium
            rhinophilum].
ACCESSION   WP_284853218
VERSION     WP_284853218.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium rhinophilum
  ORGANISM  Corynebacterium rhinophilum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 679)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Corynebacterium rhinophilum"
                     /db_xref="taxon:3050197"
     Protein         1..679
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=71695
     Region          32..514
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mqfrrigqlv aattvtaval sgtqalaqen mttisvtnit dlhghledgl sdpakagdei
       61 gvarlqslik qvnegqefnl tssgdnvggs afvsaisddk ytlealnamg mkvtavgnhe
      121 fdkgtedltd riepasdypi lganvlkdgk plldashvee idgvkvgyvg tvtqntkfkv
      181 saakipgvtf tdpveatnke atrlkesgea dvvvslfhed aeeyakgfnk dvdilfggdt
      241 hqttqgtver dgalplqwaq gyeygkllnd aditfdkaag kvksidlkqy dataaaqvep
      301 dadiagivkk aqdeaevegs ksagtvetdl frgsdegqkp gsnrgvestl nnfiaegqry
      361 amskqvgedi dlgvmnaggv radlqggdvt ykdifevqpf gnsvitakvs gkdfitalen
      421 qwqegsrprl amglsnnvqv vydqkashgq rvkavtvnge pldpnkdysi alssflassd
      481 sekggdgyfe agsikdkndv gymdaqamid yiasgesevr kgqgqigahi dgdivpgkei
      541 tvelsslnyt segepmaktv tvklgdeevs adidnskqeg ddqfgergra qvtltvpegl
      601 tgsqnleitt dagtqailpv elgeadgspk ipqgssfgga alaivaalaa giafiglnpq
      661 vlpaplraif ddlrktfhi
//
LOCUS       WP_284853270             268 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Corynebacterium
            rhinophilum].
ACCESSION   WP_284853270
VERSION     WP_284853270.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium rhinophilum
  ORGANISM  Corynebacterium rhinophilum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Corynebacterium rhinophilum"
                     /db_xref="taxon:3050197"
     Protein         1..268
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30642
     Region          3..237
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mptlwavadl hgairenfar iaelnppdpa dwlivagdva erselilril rdlaarydtv
       61 iwapgnhelf srsqdqykgr ekydylvaac reigvitped pypafngiti vplftlydys
      121 frpagtsvee avqqahskkl vmtdevaiap fvdvrawcwd rlaysikrls rvqgptilvn
      181 hwplvqeptm vlrfpeialw sgsrhtrswp rrykaeaviy ghlhmpskmn vdgvdhievs
      241 lgyprewrnq phripwpypv tstfgevn
//
LOCUS       WP_284853280             451 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Corynebacterium rhinophilum].
ACCESSION   WP_284853280
VERSION     WP_284853280.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium rhinophilum
  ORGANISM  Corynebacterium rhinophilum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Corynebacterium rhinophilum"
                     /db_xref="taxon:3050197"
     Protein         1..451
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49076
     Region          1..451
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mhlhhdyadh lpefvaathg eeqpdpklvv lneelavqlg ldtdwlrsad gldfllgrdg
       61 ghamaysgfq fgsfnpqmgd gramllgevd kdgklwdlha kgtgltpysr lgadgrgtls
      121 smlreylvse amhalgvptt rslavistgr piqrghvqpa gvlvrvaesh irvgtfhyaa
      181 qsghlqdlad yaiarhypga dyreffqgvm drqiatvssw mrlgfihgvm ntdnttisge
      241 tidygpcafm esyspdtvfs sidqqgryaf gnqpailgwn larlaeslvp lfdadinvgv
      301 dfaqetingl qekfasqrrs dlasaldtst evassyftam qlyqpditla hraladaarg
      361 rtlpaqelfa dtdfmdsyla thpspdavda amprviprnm aveaalraae agdmqpftdl
      421 lhaathpwqp npsyeqpdpd glagfltycg t
//
LOCUS       WP_284853659             659 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD/NAD(P)-binding protein [Corynebacterium rhinophilum].
ACCESSION   WP_284853659
VERSION     WP_284853659.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium rhinophilum
  ORGANISM  Corynebacterium rhinophilum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11816065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Corynebacterium rhinophilum"
                     /db_xref="taxon:3050197"
     Protein         1..659
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72245
     Region          1..627
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
     Region          9..202
                     /region_name="NAD_binding_9"
                     /note="FAD-NAD(P)-binding; pfam13454"
                     /db_xref="CDD:433222"
ORIGIN      
        1 mtdntssial iglgprgisv lerlmaqlnt vshppekltl hliddaqhgg gkiwdinqpk
       61 ylcmntfahg mtlfsepgst veapvvegpt iyewirltlg danvpagard yvaahpldpq
      121 vleefgrael eklrpesylp ralyghyilw vfrsvlqdvp ewvevkqhha rvvdiesrdg
      181 adilhlnndt tveagstlav tgwqnqgyte nerwilktle enpslrwira dnpidqgvds
      241 ikdnekvlvr glgmgffdil ilstvgrggk fvedsskpwg mryeatgtep tfaaasrrgy
      301 pflpqseegs lppaaeiprl kkvvaelshr tgarsinydt evwpavarda yqayidslar
      361 vepeslrtsr eeiiaaldat pvdagvvyng laqldeviar httkdfsllr wmhlltenfs
      421 sqqeltehiv qslcedlaea qkgpdspvra alwsvgfsrk ptqvlgaegr ytlesrhhmf
      481 dkaitlgqtt csgpppfrtq qllalvdagi vrfvggnpvl gtnadadewt msssasggkr
      541 ipgttlldaw vhkpdirrtp hdsfmrslve sgrvraftet asdgievptg spaedpdtrq
      601 vhnadgtvdk rlhlvgipah aeypdttlap pipgtdswfi qeadkaavha aqvalagqa
//
LOCUS       WP_284853534             165 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium
            rhinophilum].
ACCESSION   WP_284853534
VERSION     WP_284853534.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium rhinophilum
  ORGANISM  Corynebacterium rhinophilum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 165)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Corynebacterium rhinophilum"
                     /db_xref="taxon:3050197"
     Protein         1..165
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17929
     Region          86..161
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mnivesrlhd leervarleg kssippqaps eestywlvda ltpstqlpdg svifggnial
       61 gkrtyayqwq rpttaitdee wsenlerlaa lahpvrgeil rrllaapata aelvdeeivs
      121 stgtayhhls altsagwttk tsgeysirpa rvipllaiit asedh
//
LOCUS       WP_284853939             509 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Corynebacterium rhinophilum].
ACCESSION   WP_284853939
VERSION     WP_284853939.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium rhinophilum
  ORGANISM  Corynebacterium rhinophilum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Corynebacterium rhinophilum"
                     /db_xref="taxon:3050197"
     Protein         1..509
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53377
     Region          137..505
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 maqaqastas ssshsspqes teptkkekfh ldavwfalaf lalaavllip ipgldwpakv
       61 algmlafavi mwvteavsyp vsallivgli slllglgpdp esdgiygtsn alkvamagfs
      121 ssavalvaaa lilagamqat glhkrialyv lkiagektsh ivigaiaiai ilaffvpsat
      181 aragavvpil lgmvaafgls yesklgallv itaaqavsiw nvgiktaaaq nlvavgfied
      241 qmgqsvswgq wfiwaapwsi lmsialyfim ravikpeter ieggkeliak qledlgptsp
      301 eekrligfsl lllffwateg llhpissavi tavavalmll pkigvftwpe aqksvswgtl
      361 ivfaigislg sflldtgaat wlsektfglm gldslpilat ialvslfnil ihlgfasats
      421 lasalipvfi alaatldvpn ggigfvviqq fvicfgfllp vsapqnmlay gtgafstkqf
      481 lrsgipltiv gyllilllsa tywawlglv
//
LOCUS       WP_284854503             250 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Corynebacterium
            sp. MSK041].
ACCESSION   WP_284854503
VERSION     WP_284854503.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK041
  ORGANISM  Corynebacterium sp. MSK041
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Corynebacterium sp. MSK041"
                     /db_xref="taxon:3050194"
     Protein         1..250
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27771
     Region          6..224
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mnnkwykffk yiligpwlrl wnrpetqgld nippegtpal mvsnhqavmd sfyfplvcpr
       61 qlvhpakkey ftspgfsgav qkffmtavgq vpidreskda gsallkvtke vfgngdlfci
      121 ypegtrspdg riykgktgma rvamesgvpc ipvamigtrn anpigswipr ptkvrvkige
      181 pvdphqward ngfepddpav wrpftdffme qlvelsgysy vdayaadvkk sleagkgypk
      241 gteptgntld
//
LOCUS       WP_284854372             503 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Corynebacterium sp. MSK041].
ACCESSION   WP_284854372
VERSION     WP_284854372.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK041
  ORGANISM  Corynebacterium sp. MSK041
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Corynebacterium sp. MSK041"
                     /db_xref="taxon:3050194"
     Protein         1..503
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=55996
     Region          17..445
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 msrldtssre npldlfivga glsgidlahh vnenfpdwnw qivdsnkavg gtwvtftypg
       61 irsdsdmatf sfpfkrwphk gslgsgeriq qyiedvaree gvfdrltlht wvksanfdss
      121 aglwevtmlt rndgqpipeg napedaplte htvwakrlhf ssgyykhnrg ftadipgmer
      181 ftgtlihpqh wpsnldmagk kaiiigsgat avtllpalhe agadvtmlqr tptyvaplpn
      241 rdnitavttk lmpetralat aralhigrdm mqywlcqgfp rlargyfmll nrmyipfkdi
      301 lahfnppygp wdqrvckspd gdffkamqdg atvvtgkiat vtadgielqd gsflpadiii
      361 tatgldiqvf ggatisvdge ekpvpsavay rglmvdglpn fsftvgylnq swtlradlvs
      421 rymcrlwklm sadgyttatp rfpahlsadv plmnmdsgyl vrarkdlptq aeadpwaftq
      481 dyiheyrtwg rkstdlrkdm vfs
//
LOCUS       WP_284854244             258 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Enterococcus faecalis].
ACCESSION   WP_284854244
VERSION     WP_284854244.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..258
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28810
     Region          4..252
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mkeitstknn qlkewkklhk kkyreelnqy iiegfhlvee avkanadvqw ilfnqrgqqe
       61 wgtwlaeqet eklifvsdev lnylselpts qgilaivtle tqqeqslsfk ggwllldniq
      121 dpgnvgtmir tadaaglagv ilgkgtadiy ntkvlrsmqg shyhlpvlqr eltevvqafk
      181 kqglpvfgte lneaaiayye qeavenyali lgnegsgvsp ellaettknl yipmkgqaes
      241 lnvaiaagvl mfyfennq
//
LOCUS       WP_284854531             340 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium sp. MSK041].
ACCESSION   WP_284854531
VERSION     WP_284854531.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK041
  ORGANISM  Corynebacterium sp. MSK041
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 340)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 340)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Corynebacterium sp. MSK041"
                     /db_xref="taxon:3050194"
     Protein         1..340
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=35180
     Region          56..326
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mslrsritam fvattasvgl alialvygyl kltpvpfrae fpdsavidga vpvtseilra
       61 mltaslvsll vltvlagvig wfvagwvitp lssiastark vtagdmkert gysgasdelg
      121 dvskaldtml dtladsitaq krfsanashe lktpistiqt iadvalsgnd dselrealir
      181 irevnagsak tvtalldlar aemptvdaid fgaicrdcgi daesvtvtgd pvllqhavsn
      241 lvrnahthge yvagalnvcd gmatvtvess gsvltaedva tfvepftgsg hglgltltds
      301 iatshggkle laprndggli arfsvptsrp tptnqsgrpa
//
LOCUS       WP_284854741             935 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Corynebacterium sp. MSK041].
ACCESSION   WP_284854741
VERSION     WP_284854741.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK041
  ORGANISM  Corynebacterium sp. MSK041
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..935
                     /organism="Corynebacterium sp. MSK041"
                     /db_xref="taxon:3050194"
     Protein         1..935
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=99506
     Region          109..258
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          376..885
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 msatstsrrn kgrsqtgpkg rakrstgsyg yrsssgaada sdervgsavg avgrgvgnaa
       61 rditgafkvv ggrgrrrree iqddydatea apyeemdedv nsrrapsada igliliglaa
      121 vlgasvwmdv agpvgalias gtswvigaga lvlpvvlvgi aialmlnlgd saserahsgv
      181 gltiiavcml glihifagsp gdwesrriag gavgafiggp lsagftpfva vpllglvivy
      241 aallatgitv resfdyirgl fssiassaht pdpededlya dadddidaia eerprarrrt
      301 pmdnypvdep tlfdgdstap apeepkkkrs trkkvgvaps ivdepdnetk ilerpapaae
      361 tttdavsasr eemrkaiiar sgidaagkag gdaekpsprv petttdykip stslliagkt
      421 pktrteandr mieaitevfe efnvdaqvtg fsrgptvtry evelgpgvkv skitnlqsnl
      481 ayavatdnvr lltpipgksa vgievpnadr emvrlrdvld aptvrgdhdp mliglgknie
      541 gdfvsasvqk mphllvagst gsgksafvns mlvslltrat peevrlilvd pkmveltpye
      601 giphlitpii tqpkkaaaal qwlveemeqr ymdmksarvr hikdynakvr ageytaplgs
      661 erevrpypli icvvdeladl mmtapkeied sivritqkar aagihlvlat qrpsvdvvtg
      721 liktnvpsrl afatssltds rvildqagae kligmgdalf ipqgagkpqr lqgafvsdee
      781 iqavveavke qgephytegv teekapekkd ideeigkdmd dlleavelvv tsqlgstsml
      841 qrklrigfak agrlmdlmes rgvvgpsegs karevlvkpe eldtiiwmik gadpaeapke
      901 vleeqeldde tsdapdapdt pntvtatynp tggaf
//
LOCUS       WP_284854825             647 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Corynebacterium sp. MSK041].
ACCESSION   WP_284854825
VERSION     WP_284854825.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK041
  ORGANISM  Corynebacterium sp. MSK041
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 647)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Corynebacterium sp. MSK041"
                     /db_xref="taxon:3050194"
     Protein         1..647
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=69981
     Region          40..633
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mdpqrrqqrg epqkvitakr mqlltvvflv valvlvgrla wvqlkwgpql qtvaadqrtr
       61 tfvdparrge ivdrqgnvls ytmqarsltv spvilrrelg eqarndmvne gatraeveaq
      121 egarvedmlr qmaneiprmi gqgdddkdes edsdnrvktq kvnskdilek lhastdyevl
      181 vrnvdpdvaa evakkfhgva adhqdireyp ngavaeniig rvsmdgqgqf gleassdsil
      241 tgingrstld vsdkgqvipg tlrdvvpavn gakieltidl dlqayvqqll eqakensrak
      301 gaeavvldaa tgevlamant dtidpngdle kqlkngrsfd npsishpfep gsvakiitat
      361 aaieerltnp devhqvpgqi emagvtvada wehgvvpytt tgifgkssnv gtlmlaqrvg
      421 eerfddylkr fglgqatgve lpnesaglvp treqwsggtf anlpigqgms mttlqlasvy
      481 qslanggeri epriiknvta stgeeipqee prrtrvasee tartvvnmfr apfqedpagf
      541 nsgtaqgnni pgyqlsgktg taqqvnpdtg aysnsdywit fagiapaddp rfvvavmldd
      601 pergplegga ggqssapvft qianwliare nippsrdpge pmvlqaq
//
LOCUS       WP_284854829             261 aa            linear   BCT 25-DEC-2024
DEFINITION  inositol monophosphatase family protein [Corynebacterium sp.
            MSK041].
ACCESSION   WP_284854829
VERSION     WP_284854829.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK041
  ORGANISM  Corynebacterium sp. MSK041
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Corynebacterium sp. MSK041"
                     /db_xref="taxon:3050194"
     Protein         1..261
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=27581
     Region          8..259
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mdemreylri aeeaadearr mfvdglgsvp alykdsgdfa temdlrieem lrdqltpatg
       61 ipvlgeeegg vlrndaswvv dpidgtanya sgnpscavli slvvdkqpvv avtdipllnm
      121 rltarqgsgv hlngellppv nmaahvsnqv gvgavgsdeg srippdsrlr likaleyenm
      181 rprisgsvgi dlafvaqgvy eaavsfsphp wdnaagvlla rsagavvtdi egnewelgsl
      241 gviagspdvh eavlrtiksv a
//
LOCUS       WP_284854839             229 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: potassium channel family protein [unclassified
            Corynebacterium].
ACCESSION   WP_284854839
VERSION     WP_284854839.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 229)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..229
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=24435
     Region          <3..216
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 makqirafhr shgrinippv mviglgrfgi slaseltang vevlgvdads rvvkehapyl
       61 tdavvadttd pealeqlgld diecvvvsvg sqleasiltv shlldagvpd iwakasseph
      121 grilsqlgvh hvvhperdtg rrvahllggk frefaevtpg ycvtsmsaph aftgfaldle
      181 eiwrkhrvqi iamkhdngdv mpmvngtvla psdiiiaggs paaleslnr
//
LOCUS       WP_284854842             313 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium sp.
            MSK041].
ACCESSION   WP_284854842
VERSION     WP_284854842.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK041
  ORGANISM  Corynebacterium sp. MSK041
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Corynebacterium sp. MSK041"
                     /db_xref="taxon:3050194"
     Protein         1..313
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34262
     Region          13..313
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtkkdspeki shlvrtlnli pylhkhpnat pmeiardlgy shtdvmddlq rlmlsgvgkr
       61 peelidlape wtgvtviddq gmnaplrltp teanallltl esletmpgli dhsavtsaaq
      121 kirevmsnvg vsdaehpdtp galgtiseal aqrrmlrlny ysatsdttre rtvapvgifh
      181 rdgntylsav eegaaktfrv drikdallid apvpasstpg gpvydatdpf gfgdakvatl
      241 rihpeatwla dfwqielhde rdrgwvvasm pygsddwlvr fclsqadrva vtepthiaee
      301 laargkagle rya
//
LOCUS       WP_284854903             270 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: TrmH family RNA methyltransferase [unclassified
            Corynebacterium].
ACCESSION   WP_284854903
VERSION     WP_284854903.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..270
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28004
     Region          12..270
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 msldfsqpft ertprvvnaa klnraagrkk akaflaegen sveaavatga atdlfvteaa
       61 adrfadivtt agymdvytha itekaaqslt dtvhttgifa vckpvtwtlg silkgrpklv
      121 avcvetndpg nagtiirlvd algadavvfa gdtvdpespk vvrssagslf hvpvarerdi
      181 kgvlgqlraa glstlattmn gnldltnagd alnkptawlf gneahglpdd vlaaaddtas
      241 ipikgsaesl nlstaasicl wesakalrer
//
LOCUS       WP_284854911             740 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium sp. MSK041].
ACCESSION   WP_284854911
VERSION     WP_284854911.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK041
  ORGANISM  Corynebacterium sp. MSK041
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Corynebacterium sp. MSK041"
                     /db_xref="taxon:3050194"
     Protein         1..740
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=80932
     Region          15..737
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 manqsgdlsl nspeavqheq ayvdvlfahl drevsnaqqr leevqrdvdp dnpdadalvr
       61 reteyhglna kldalniaet glvfgridve dgspenpvpg spnqdrryig rmgmddrddn
      121 yrtllldwra pmarpyylat tahpegvvsr rnirmrgrtv tavdddvlsg pgadgagads
      181 gvaseaalvr alnaprtghm qsivetiqre qdqiirdktr gvlvvaggpg tgktavalhr
      241 iayllytwrn qlartgvliv gpnrtfleyi srvlpelget gvvlstvedl vpvftpglqd
      301 dlltrevkgs aemvtilsra vrnyqvvpss pipltidgie iattpkmfma artrarhsrk
      361 phneaqsvfa evltqrlaea maerigadpl gganllshad vdqlhddlad epqvadliae
      421 hfpilnpvev laeflssrea isaaahdyde etqdalyrad gdaftasdta lidelytlig
      481 iptptdeaek aerqwrelva daedaldila ssantdtdde feaevlsahd iidaetlasr
      541 qretdarsta eraiadmtwa yghvivdeaq eltpmewrmv frrcpskwmt lvgdtaqtss
      601 pagvddwata lepfvgqrfv shelsvnyrt peevmevane vltaidpdaq pavtirssgh
      661 pvrilpegtd tttvraevee lgglvvvink dnvnavkgle fdhvivdkph eiieaspqgq
      721 qdlyvaltra tqtltvigel
//
LOCUS       WP_284854978             174 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [unclassified
            Corynebacterium].
ACCESSION   WP_284854978
VERSION     WP_284854978.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 174)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 174)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..174
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18986
     Region          98..170
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mqqeisishe tdttilerlk alesrvaale ssptssssgd fwvvdqiqcs nssdhdhhgs
       61 vvfggaitld greyayqwer sadyltgrew neyihriaai ahpvrgailr rllvapatva
      121 elvdealvss tgtayhhiaa lqsagwiakl dgryevrpsr viplltiiaa gedh
//
LOCUS       WP_284854979             340 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [unclassified Corynebacterium].
ACCESSION   WP_284854979
VERSION     WP_284854979.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..340
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36529
     Region          45..330
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrqqyirria vgvpaalatl slllyfgprp idsatdhtgd dtitsvlvah apkgyyqlag
       61 fiydggevrf gglgadehte feigsltktf ngelarqqie ngslrldtqv qdiidaagtp
      121 iadvtieell nhtsglsrle gvgfanlvls llrnggnpyk datpndilea akqaelknrg
      181 eenysnygha llgqllavna dtpyeellrt qifepagmas tflampgtvd ghpqgltfsg
      241 reaerwdmng wapagairst ahdiakyvdw vvahggpelg wadfeedgtt yifhnggtgg
      301 ystmlvwdpe sphpraafva nsseadvddl gielvkgtrp
//
LOCUS       WP_284855507             498 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Corynebacterium sp.
            MSK041].
ACCESSION   WP_284855507
VERSION     WP_284855507.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK041
  ORGANISM  Corynebacterium sp. MSK041
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Corynebacterium sp. MSK041"
                     /db_xref="taxon:3050194"
     Protein         1..498
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54408
     Region          11..496
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mnssapkhei erdvvivgag paglmaartl tkagksvavl earervggrt wngrvrdang
       61 vdhfvelggq wispdqtrli dlvdelglst fqryregksi yvspdgerhe yegpvfpase
      121 stqaemdkli kilddlaaei gakepwahpk aaeldsisfr hwleqlsdde eaidnvsiyv
      181 asgmltkpsf tfsalqavlm aasagsfsnl vdedfildrr veggmmsvse tmakelgedv
      241 flgtpvreiq waqpdpsted slnnvkpdvr ngvpnngkps dvtvvsdkvi ahaknvviav
      301 ppnlynrisy vpamprdlhi ahqhismglv ikvhaiyetp fwrekglsgt gfgggrlvqe
      361 iydntnrgan iaggtageed tygtlvgfvs dvyaeemwhl peeerkhril samadylgpe
      421 tmepiafyls dmaaeewtrg ayatsydlgg lsrwghlqnq pvgpihfacs diadegyqhv
      481 dgavrqgera anailany
//
LOCUS       WP_284855565             234 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium sp.
            MSK041].
ACCESSION   WP_284855565
VERSION     WP_284855565.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK041
  ORGANISM  Corynebacterium sp. MSK041
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Corynebacterium sp. MSK041"
                     /db_xref="taxon:3050194"
     Protein         1..234
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24395
     Region          5..214
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mnqvarstdg vtrgrimsai ltsapvtasq lakdigispa gvrrhidkll eeglvehssq
       61 psrstgkagr grpaqhyqlt esgrdsfgsg ydelaleafa aveeiggrea vkklarkrae
      121 kllgalrnkp qgeiadvand vadtmaaqgy aaeanhvgsg mqlcqhhcpv havaaeypei
      181 ceaehelise lvgsavapla liangdgvct ahismiesst faggttmers ggrd
//
LOCUS       WP_284855946             287 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: DsbA family protein [unclassified Corynebacterium].
ACCESSION   WP_284855946
VERSION     WP_284855946.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..287
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=30143
     Region          124..284
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mtnntpktki pplmwaftiv falasavggy vigerdgqqn alnqmaeqvg gvgpdgavve
       61 gtsagipdga tpgtdfspvk ansngffdat ihgpsapits qdeidnaarr dpkdpmavga
      121 ldapvviaef sdwecpfcir hattvepeli keyvdegyvr iewndlavqg pasiaaakag
      181 raaaeqgrfa aykdaymaaa aekgghpgfe ledfigfark aevpdidkfi adaqsdkydd
      241 aidearnyaq glgitgtpgf iigkkflaga mpiddfrsai ntqlaan
//
LOCUS       WP_284855988             905 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium sp.
            MSK041].
ACCESSION   WP_284855988
VERSION     WP_284855988.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK041
  ORGANISM  Corynebacterium sp. MSK041
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 905)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 905)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 905)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 905)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..905
                     /organism="Corynebacterium sp. MSK041"
                     /db_xref="taxon:3050194"
     Protein         1..905
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=98625
     Region          241..884
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtnpenngeh pdpvtesheq lgrsiqdamd aareagigve ekpgeasvwf aadvedrphv
       61 sysfvlknlp papdidmvea aveeldgvec rvvhprktaw vtatvdtrpg vivdkfaelg
      121 ieasltdtsm fryaaavesa ehyvrrkatk dvpiqlrrrr rsaqrsldra rqagfgprar
      181 reeaqrknqs kdpvkrdrkd dvlytardli tparmwvalv ltlpvlvlay vqaaqfdgwq
      241 wielalatpv vtwcafpfhr alaggvrrgi taldgassva iiiaylwsaa villaptgqr
      301 gghsgftwfa ttlgtdhgpe lfldvacgit lllligrrys irarrllide madqslnpev
      361 eyirinkmrg raeidkelip vaeinrgddi vvhvgevipa dgkviggkar lkqglidvhe
      421 pndvkvgstv yagsviesge ikvraqrtgh atrwlvvmqw lrdvevrqry asvqyaqsaa
      481 rllpvsmtva ffsfilwgli sgdynaalrt slavlagvap valalspala lrlgiesaar
      541 ngvllrdgnt lrsletvdtv vfnrvgtlak sqmcvetvtp aegeseemil riagavsmes
      601 dtpagralvq gareaktqtd nnpdlptrye lvnvatepsg dvsarvnlvf vdeegretst
      661 qvdallwrpv nlshlrgrla vaatsggtpv vvrwkgkdrg vitlydpfkd dadeavsrle
      721 qmgvetvmlt rdtypvarrf adflgisnvl agitnnrkag airnlqaaga evalvgdasv
      781 rdalraatvs imyadseele fsrrrgrtvs avllrhdvma vpqlvshark vcevidrnla
      841 lawiynglml vcavagvipp iaatvlmlgs sllieglsmr arsfpnedrv epetiselvn
      901 genng
//
LOCUS       WP_284856127              75 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Corynebacterium].
ACCESSION   WP_284856127
VERSION     WP_284856127.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 75)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 75)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 75)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..75
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7733
     Region          12..72
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 malsnptdap rvvchldelm aargitgaal aeqvgitpvn lsvlknnrak avrfttlaai
       61 cqaldcqpgd vfsvk
//
LOCUS       WP_284856122             136 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [unclassified Corynebacterium].
ACCESSION   WP_284856122
VERSION     WP_284856122.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..136
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15239
     Region          1..132
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 msnllsdtqv iplrwndydr yghlnnckfv disqeariaf mqqnfadreq efgvfvrrve
       61 vdylrpvmpd ttqvtvettv teigntsfkt tqdlkdrhgn vcgvvktvlv avdlstaspr
      121 eitqqergil tagsge
//
LOCUS       WP_284856183             336 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium sp. MSK041].
ACCESSION   WP_284856183
VERSION     WP_284856183.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK041
  ORGANISM  Corynebacterium sp. MSK041
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Corynebacterium sp. MSK041"
                     /db_xref="taxon:3050194"
     Protein         1..336
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36513
     Region          56..315
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mnatlsvrra lialvtavva amsmmlvapn eahanprgwl rpdatghchw dpvgywvqrc
       61 dvwspsmnrn ipvqivpaar ggnaglylld glratektna wfedvnaaai yensnitlva
      121 pvggegsfya dwtadpqygn gktyrwetfl trelpgylqq hfgvapnnns iiglsmggta
      181 amnlaakhpn qfrqvlsfsg yltttlpgmq tmlrlsllda ggyninamyg sllsptrfen
      241 dpflnmhglr ntdvyisaas gipgpadasy lpqhqvagsl leigamastr iwegkarltg
      301 invtsdypsl glhnwkefgg qmvktkarvl nhmnaw
//
LOCUS       WP_284856190             301 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Corynebacterium sp. MSK041].
ACCESSION   WP_284856190
VERSION     WP_284856190.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK041
  ORGANISM  Corynebacterium sp. MSK041
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Corynebacterium sp. MSK041"
                     /db_xref="taxon:3050194"
     Protein         1..301
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30931
     Region          20..297
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mprernqtrl twqginafla lpaapvlmvl igslgtqaaa vivtdmlaav gapgvsglrm
       61 aaaavimvvl frpkltgmtr arainivvyg vamgmmsmmv yaaiarlpqg vavtidflgp
      121 cvvsflgltm wrsrlwavva figvaliaqp sndldivgig faalgavffg aytlfaarmg
      181 gtdgggmpdl alsvvvaali lmpfsvpavp lldapmwiti iisgfigavi pyvmdtiaag
      241 ivsaavvgtl faldpvigai lgwafsgdel twsmvagivl iavagaiitw rgaqespdig
      301 e
//
LOCUS       WP_284856299             391 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Corynebacterium sp.
            MSK041].
ACCESSION   WP_284856299
VERSION     WP_284856299.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK041
  ORGANISM  Corynebacterium sp. MSK041
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Corynebacterium sp. MSK041"
                     /db_xref="taxon:3050194"
     Protein         1..391
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42139
     Region          6..385
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 malqqpqggp lqgivvadfs rvlagpyatm lladlgatvi kvegptgddt rhwvppkrgd
       61 vgtyylsinr nknsikldlk npddletaya iidradvlid nfrvgsldkf gldpesvekr
      121 wpdlihakit gfgsragsql pgydmliqas sgfmsmtgsp dgppqkagya fidvltglht
      181 tvgilasllr rerfgggget irtnllsaal ssmvnmssaa vasdaemtrt gndhpsifpy
      241 gpfpakdrel viavgnnkqf gvfaeglgap elasdprfat neqrntnree lrpilhella
      301 akdaqewidl frakglpiap iltvreavhf adelelepvv tiptkdgsde ipfvsnpldm
      361 ssgaiqytka apgldedrdd vldwisntpt k
//
LOCUS       WP_284856316             454 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Corynebacterium
            sp. MSK041].
ACCESSION   WP_284856316
VERSION     WP_284856316.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK041
  ORGANISM  Corynebacterium sp. MSK041
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Corynebacterium sp. MSK041"
                     /db_xref="taxon:3050194"
     Protein         1..454
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=48057
     Region          6..243
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mstlklnfaa vsdrglvrgn nedsayagph lllladgmgg haagevasql mvehmehldr
       61 dpedadvlal lgaaaddana aiqssiaenp eqdgmgttlt almfngtqfg lihvgdsrgy
      121 rlrdgeltqi tvddtfvqsl veqgklqaed vsshpqksli lkaytgrpve pylelldaqp
      181 gdryllcsdg lsdpvtheti astvgtgtpa eaaqrliela lrsggpdnvt vviadvvdte
      241 addcpelpak salagalalv desshpdtaa graaklvrtq nrsqssggak qtdtpaadde
      301 edhprrfpwt alilvlalva agvvgvwwfd rassntysit vndadefvie qgftssilgk
      361 qlhkpvqqic indenqitvv dtdevpkdcq rfgvadvpes taarvhtlgt gsyseisdqv
      421 nrladealpa cvdktdtsae teqagssqkc revs
//
LOCUS       WP_284856714             731 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Corynebacterium sp. MSK035].
ACCESSION   WP_284856714
VERSION     WP_284856714.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK035
  ORGANISM  Corynebacterium sp. MSK035
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Corynebacterium sp. MSK035"
                     /db_xref="taxon:3050192"
     Protein         1..731
                     /product="PhoX family protein"
                     /calculated_mol_wt=79270
     Region          54..725
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mvrigknllt npfatsrssl tctykcgnac addapnefsd nqyfgdvakq afsqrafsrr
       61 aalkvtgasa lavgggavla acssddsgsa aggsdasgtt aagdgskges pegmrfdavk
      121 pntedavvip dgyeqnvlir wgdpiheggp efdfdkqtpe nqlkqfgfnn dfaglikaed
      181 gtllyvcshe yttepmmfra ykkedatkeq vdiglaahgq tilaveeddk gflkpilsdk
      241 rnrritgfte ftvdgpaagh dllktkadps gmkvegtlnn csggvtpwgt ylsgeenvdq
      301 yfgnvgklkd edtvkklkry svkneelsdr awekyydrfd vskepnepnr ffwlveidps
      361 dpnsipvkht algrfkheag qiyvtddgtv vcysgdderf eyiykfvssr kvkegdlkhn
      421 mgilsegtly vgkfngnses eidgsgelpk dgrfdgdiew lplmtakadg kheshvdgmt
      481 aeevciytri agdkvgatrm drpediepsp ktgkvyaalt nnkyrgkasp dssgktqdnk
      541 aakktdgagr pyegatevap itenknglvl emeddhagtk gkwnlllvcg dpneaytyfg
      601 gfdkesvspi scpdnvtfde ygnlwvstdg naldsndglf avavegerrg etkcfltvpv
      661 aaetcgpqvf snrvmvnvqh pgeietdqgh pvgdnpdptt nptshwpdgg keqprpavvq
      721 vvrtdgkkig v
//
LOCUS       WP_284856736             426 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium sp. MSK035].
ACCESSION   WP_284856736
VERSION     WP_284856736.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK035
  ORGANISM  Corynebacterium sp. MSK035
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Corynebacterium sp. MSK035"
                     /db_xref="taxon:3050192"
     Protein         1..426
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=46702
     Region          45..423
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mtskayaaap nagqdtvsss vpnstpntvs ssgsstasns attfrpgflp sleglravas
       61 mgiigthvaf qtghdvgalw ervlgrfdff vavffvlsgf llwrshrsgy ggiprrkala
      121 dadggrkksw akyykkrvar impaywvlvl ivlialpvgr gadfkiwltn ltltqvyfsg
      181 slhgglthlw slsvevafyi alplfaigls rldphrqqgr rivtisllai lsfgwpylpl
      241 pypegvnphi qpiayfswfa agmilaeles lqgvdtdaar arvetmqrwa rrrplwlaia
      301 vgalvlasyl gpeglvelts weftrrllcg lvfgaaiigp wtmapesrfl ehpimqalgr
      361 wsygiflwhv amlsiafpll gvklftghll svtivtvals ipvaaasyal veeparrffa
      421 rvwvnr
//
LOCUS       WP_284856739             255 aa            linear   BCT 25-DEC-2024
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Corynebacterium
            sp. MSK035].
ACCESSION   WP_284856739
VERSION     WP_284856739.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK035
  ORGANISM  Corynebacterium sp. MSK035
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439579
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Corynebacterium sp. MSK035"
                     /db_xref="taxon:3050192"
     Protein         1..255
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27529
     Region          20..222
                     /region_name="PssA"
                     /note="Phosphatidylserine synthase [Lipid transport and
                     metabolism]; COG1183"
                     /db_xref="CDD:440796"
ORIGIN      
        1 mnastssdia ssaapqtftr rqhaiawavh gftltglvwa tlavvalldg kpewmwlwlg
       61 ialvvdgvdg nmarkhhike vvpwfngavv dnivdyltwt aipaafmvmy lplgprplai
      121 flaivvlvss mfcyaneaak sgdyyfvgfp aawnivavll wvwnapmavc isaififsam
      181 tlvplhythp frvergrian iaatfiwivs tgmliasetm aaslskasih glvavnvaag
      241 awliiggvrr slsgr
//
LOCUS       WP_284856747             306 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Corynebacterium sp. MSK035].
ACCESSION   WP_284856747
VERSION     WP_284856747.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK035
  ORGANISM  Corynebacterium sp. MSK035
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Corynebacterium sp. MSK035"
                     /db_xref="taxon:3050192"
     Protein         1..306
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31623
     Region          25..305
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 msreenqtev pqqgpllqrv nkfltlpvap vilvligslg tqaaavlvtg mlstvgapgi
       61 sglrmtaaai imvvqfrpkl sgmtrarain ivvygiamgm msmmiyaaia rlpqgvavti
      121 dflgpcvvsf lglkmwrsrl waivafigva liaqpsndld ligigyaaig aiffgaytlf
      181 sarmgssegg gmpdlalsvv vaaivlapfs vsaaplvdgs mwativisgf igavipyvmd
      241 tiaagivsaa vvgtlfaldp vigailgwaf sgdrvtwsma lgivliavag aiitwrgare
      301 srelaq
//
LOCUS       WP_284856777             292 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Corynebacterium
            sp. MSK035].
ACCESSION   WP_284856777
VERSION     WP_284856777.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK035
  ORGANISM  Corynebacterium sp. MSK035
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Corynebacterium sp. MSK035"
                     /db_xref="taxon:3050192"
     Protein         1..292
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30877
     Region          10..292
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 msthkswqpl gpailfapad rperfakaad radmvildle dgcraenrea areaiascdl
       61 dpartivrvn ppevedyaad idmlrgtafr qvmlpkassa qqvdelvaal gektqviali
      121 etplgvmrae elaqadgvva lfwgaedlva glagtssrfs eaeaalapgr ihagsyrsva
      181 vhtrshvhla aaahgkasld siyvnisdan glaaeaadaa algfaatvci hpgqvptirq
      241 ayrpsdeeid warrllaeae entgafsfdg qmvdaplfrq aeaiarraav tg
//
LOCUS       WP_284856792             358 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Corynebacterium sp. MSK035].
ACCESSION   WP_284856792
VERSION     WP_284856792.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK035
  ORGANISM  Corynebacterium sp. MSK035
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Corynebacterium sp. MSK035"
                     /db_xref="taxon:3050192"
     Protein         1..358
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39759
     Region          56..193
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mddyspstrv fgpllrafpq aylrslhhpe wiphgvqdvr eildgkvtpe ldryngrtpi
       61 vlvhgtwmns fnsfamlgpf larnrpvfsl dygsdpaalv srlrsvkatt dlsdalaevt
      121 dlldrfrahl slpridligh sqgglhcrsy anasidslyd ealnrglnee aaeqyasdns
      181 pvravislag nhrgttawgm rrrlsalerc glpmhklvdr lvgraciqql ldsdyiatln
      241 raargitrrg phylnigtpf dtvvrpwtga flpeqeghhi tnvnnatggg dwsdhlally
      301 spntlerihe fleeldgaea gdvphhprqr vlplygalpr glgrrrlgrr gsgrrgri
//
LOCUS       WP_284857080             253 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Corynebacterium sp.
            MSK035].
ACCESSION   WP_284857080
VERSION     WP_284857080.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK035
  ORGANISM  Corynebacterium sp. MSK035
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Corynebacterium sp. MSK035"
                     /db_xref="taxon:3050192"
     Protein         1..253
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25695
     Region          141..253
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mneqgghshn gghyedrqvd vnrsaslitl liagvsivgl vifaivnttd gndeadgggt
       61 gsgvsvgadg agngdgagsd gevdgapaap amskdeiaav agsgsltgvr lpllaesgds
      121 agqdneagrt elvdmgqvve gkptvlnvwa wncapcrqel plieqwakdn pdvqvatvha
      181 areagrgqaf lqeigvklpt ysdtvdvvgp alnlprvvpi tvvfkadgtv atihpgeftd
      241 aqqitdlvrg alk
//
LOCUS       WP_284857021             343 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium sp.
            MSK035].
ACCESSION   WP_284857021
VERSION     WP_284857021.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK035
  ORGANISM  Corynebacterium sp. MSK035
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Corynebacterium sp. MSK035"
                     /db_xref="taxon:3050192"
     Protein         1..343
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37559
     Region          18..338
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtvhaareld agvsvdella vvpyfsqhrs mteaatelai pfariraive qiadidqpgl
       61 lgvrafevdy rnsfdvrirp qatvlsqpra ltaeetatll liletiedsa attsseaaqt
      121 aatklrsalg invpiidsta aengkafsfs eqiysalhqr kvlkvryrna sgqitvreld
      181 cvnvytvest tylravdraq edrrqksfrv drleaaevld tpagfhrpep vdirdphafg
      241 aetgtsewas vlidadatwi adyepvffte degeeedtel vsdqglgqse yvadvpmsdl
      301 aatvsfvlrr spsvtvaepl klknavvara realaeygrn dka
//
LOCUS       WP_284856759             368 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Corynebacterium sp.
            MSK035].
ACCESSION   WP_284856759
VERSION     WP_284856759.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK035
  ORGANISM  Corynebacterium sp. MSK035
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Corynebacterium sp. MSK035"
                     /db_xref="taxon:3050192"
     Protein         1..368
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=39904
     Region          1..321
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mrallisnpn stsntarrmp gvvralrsve girltsmfta ypghaaemva gktvrdydvi
       61 islggdgtin eivnglmnsn pfsalpatdl paiatiptgs anvlagalgi prdpvdaawy
      121 iasllrsrtr stisvghaae rcfvvnagig idaevistme qlrqngtrak avrylpaift
      181 awnqlrkspp qitattdgte fgrdfamavv snsnpwtflg dlpivtnptv slrrglgfyg
      241 ftslrgvtgl vaaanlagff trlrspfhve arerrvdnvq hieltatapl rlqldgeyin
      301 qceslnirvk qgainfvara ddytedqftk kvatrpvder llvvvtkkvm drtrrlfsts
      361 qkteanpa
//
LOCUS       WP_284857096             233 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Corynebacterium sp. MSK035].
ACCESSION   WP_284857096
VERSION     WP_284857096.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK035
  ORGANISM  Corynebacterium sp. MSK035
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 233)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Corynebacterium sp. MSK035"
                     /db_xref="taxon:3050192"
     Protein         1..233
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=24891
     Region          <25..219
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 manskfnpfa gfaehfanqv ssspvvilgm grfgqalgee lvaggievlc vdhrekvvqe
       61 lsstfdhvvt adttmpevlk qlgvdeaerv viaigsdiea slltasalvd mdvpliwaka
      121 dnqahakilg qigvhhvirp eadtgrriah liggkvqdfl efdrdyavgk vappihcldk
      181 tvaeinqsap itvvavqkrg qrfrpaladd ritagdlliv sgairqletf age
//
LOCUS       WP_284857124             844 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium sp. MSK035].
ACCESSION   WP_284857124
VERSION     WP_284857124.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK035
  ORGANISM  Corynebacterium sp. MSK035
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 844)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 844)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 844)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..844
                     /organism="Corynebacterium sp. MSK035"
                     /db_xref="taxon:3050192"
     Protein         1..844
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=92107
     Region          35..830
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 masrasepgq dqtgrigrtg qaglpdqass apqreeestl aaeqayvdra fsfldrarer
       61 dqeylrqvml iddpdpqarv ereveyhrlq anldryrsae iglvfgridi ddtdpdnpla
      121 eegpgatvdk ryigriglsd enddyrtvim dwradgarpf ylattahpeg vslrrhlrth
      181 grkvrsidde wlsgeeadsa heteveagvg gesvlrevmn qartghmrgi vetiqreqdl
      241 iirdstrgtl vvqggpgtgk tavalhrvaw llytyrdqla ktgvliigpn ttfldyisrv
      301 lpslgetgvv lttiadlypg vrgsnalidg hnpeplvaqe vkgsiemlti lreavrayqe
      361 lpaealevrn dnitltitpd mvkaartrar rtrkphnlar pifrnhvvel laaqmaevig
      421 adplggenll svtdvadlrd eidesgavad ildelwpalt pervlsells sreaidyaas
      481 dydeltreal yrpegtdwmp sdaplldels ellgpvgese adeedwqarv eeaqgaldtl
      541 sssasqdldd gfeaeilsay dvidaealae rhrerdlrst aeraaadrlw ayghvivdea
      601 qelsamawrm lrrrspngwm tlvgdvaqtg spagaatwhd vlepiigsrw hlheltvnyr
      661 tpaevmevaa svlaeidpel eapqsiratg rkpvqahtvt ealthveqva qpdrlvavia
      721 paelleatra evreflggga gdaggaggag dartstdiag avgatsadat pttraskltn
      781 cavydittsk glefdevivv apdqivaqsp qglqdlyval tratqglviv dkqrpehlpe
      841 ldwa
//
LOCUS       WP_284857233             284 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase [unclassified
            Corynebacterium].
ACCESSION   WP_284857233
VERSION     WP_284857233.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..284
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31088
     Region          84..181
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mtsfrfpafi vppalkelrs fatlsrsfgl lndfkyeqtd pdifyghlae dtigllegia
       61 agadgaagst dtggtsssvt tntalsgkri ldvgggpgyf grafaqrgve yytcepdvge
      121 maaagikles svrgsglelp frddafdlty ssnvaehvpe pwtmgeemlr vtkpgglvvy
      181 sytiwygpfg ghemgmthyl ggerarrmye kkhgkrpkny fgeslfkvgc geglkwaraa
      241 aeagdcella afpryhpwwa wwmvhvpglr efavsnlvlv lrkr
//
LOCUS       WP_284857417             469 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: metallophosphoesterase family protein [unclassified
            Corynebacterium].
ACCESSION   WP_284857417
VERSION     WP_284857417.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..469
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50528
     Region          153..430
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mavnsvgtra vasaapnqap fpftgltsgl vvtdlevvtv tdtsvtfswa tyagphpawg
       61 klaplapadt evalvpvdad eggelpvvhk detqvgyhfv tvdklrpgtt yrfecrsngl
      121 vaepglitrn lpntpeqtgq fttlvapege ylttiailnd thigenghgi itgnfpapif
      181 sepgagpype vmltaalael rgmgiekvfv ngdatsearp aevrrfaeim ntfgaqerqw
      241 fvtrgnhdrp hkpdadpsag ydefpvlegt enhrdpfgvl lgrprqelwv tqqgpirvig
      301 ldsskldesg geispeqfda lerelqraps kptvvlahhp itaeagwtha agptfilnsa
      361 darrlqqmln dapgvffaga ghthrakrtr gdvgagvdyl etgackaypg gytllhvysg
      421 gyqvnfhrls sedalawtar arwamygfep eallgelsdr nyvvnrvia
//
LOCUS       WP_284857460             839 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [unclassified
            Corynebacterium].
ACCESSION   WP_284857460
VERSION     WP_284857460.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 839)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 839)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..839
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..839
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=93446
     Region          14..832
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mlpdlaevpe slfddairds fiawtrdqgi tlypaqeeaa iglaggdhvi latptgsgks
       61 mvaiaahfca largqrsfyt apikalvsek ffalcevfga envgmmtgda tvnggapiic
      121 ataeivania lrdgadadid qvvmdefhfy adpdrgwawq vpllelsrsq fllmsatlgd
      181 tskfetdlke rtgldvnlvt gttrpvpldf hyvytpvhdt laellesgka piyivffsqr
      241 qaaeqaqalt glklltkeek erireeigdf rfttafgrvl sklvrqgigv hhagmlpkyr
      301 rlverlsqtg llkvicgtdt lgvginvpir tvlitglakf dgrrsrilks refhqiagra
      361 gragydtegt vvveapehei enaklrrrag qdeaklkklr lksvpkgevt wsektfdkiv
      421 sqppepltsr favtngmlln viarggdtye hmrhllrtnh dtrhqqneai ltaielyrgl
      481 vnagivvthg egddcrselt melqrdfaln qplspfaiaa lelldkdspn yaldvisvfe
      541 siledprpll iaqqkkarge eiaalkaegv dytermnive ditwpmplad elegafdtya
      601 qghpwvrefl lspksvvrem vekamtfsdv vseygiarse giflryltda wrtlrhtlpp
      661 eaaneelrdi vewlgelvvq vdnslvdewa qmadpdkpld eetlkeaafg tdesrpltgn
      721 eraftrmvrn lmfrhvqlfa fekeeeladl dnylddapdw paamddyfde yddlgidaka
      781 rggdmisidr qageglwhvi qilddpegdh gwrfeadidl aasdeygevr laslriiqg
//
LOCUS       WP_284857621             700 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: vWA domain-containing protein [unclassified
            Corynebacterium].
ACCESSION   WP_284857621
VERSION     WP_284857621.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 700)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 700)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..700
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=74718
     Region          <38..251
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mvvvqdffkd sfssssskrl rvtivvtlll aawtigfsai papvaaaqds pspsgveqpa
       61 ptgeggtgea kaelimdlsg smladdaggt rldaakrast elidslpdda llgmlvygqr
      121 essdesnrer gcqdievlsp vqkvdkeglk sriaglqakg ytpignalrk aadelgpdge
      181 rsiilvsdgi dtcapppvce vakelagqgv gltihtvgfk vdeearaele cvaqatggqs
      241 mtaddatqla dhmkfltqrs vqgyettgtp fefsetkega kwlgegkyqt tlvpevaqhd
      301 rtplyyriav pkghnaivts kvlanidaeg kgqqdvrtev deiinetggk cqddgrmgsl
      361 tgaeasadsw tptsadasil awdsdriess cdqtkwlvan nvwvydgdsv adyrdepvkv
      421 evsvqfepvl kkqdadklhe grssstgdka ykkatfgeak pvnggnnaaq apevksgdti
      481 sdtivpgeqk fykipvewgq rpviaartgn serdnadsmg vallnpfevs vadgtmhfyq
      541 dsedlnlstd rpveynnres nvggrpvana gyyyatvrma nyrpdeevsg idqpfqlafl
      601 ldnkptkgpd wrptdkngpt psdkpilakg eseqetskds sedaskesds sdtdsqasas
      661 ssdmedggms plvigtvvav vavfigiaga ivyqnkkrke
//
LOCUS       WP_284857677             292 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: HpcH/HpaI aldolase/citrate lyase family protein
            [unclassified Corynebacterium].
ACCESSION   WP_284857677
VERSION     WP_284857677.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..292
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30951
     Region          10..292
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 msthnswqpl gpailfapad rperfakaad radmvildle dgcraenrea areaivscdl
       61 dpartivrvn ppevedyaad idmlrgtafr qvmlpkassa qqvdelvaal gektqiiali
      121 etplgvmrae elaqadgvva lfwgaedlva glagtssrfs eaeaalapgr ihagsyrsva
      181 vhtrshvhla aaahgkasld siyvnisdtd glaaeaadaa algyaatvci hpgqvptirq
      241 ayrpsdeeid warrllaeae kntgafsfdg qmvdaplfrq aeaiarraav tg
//
LOCUS       WP_284857698             585 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alkaline phosphatase D family protein [unclassified
            Corynebacterium].
ACCESSION   WP_284857698
VERSION     WP_284857698.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..585
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=63467
     Region          32..561
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mpssdksqta asnlngavsy sdataqkpft psrravlrag atgaaagaig lapatsagan
       61 pesqspanag gsggfqvfqh gvasgdplpd svliwtrvts hpgdtaganq grpvalkwev
      121 asdegfgniv asgalntdpd adntvkidvk glsadsyyfy rftvtagdha gqvspigqtr
      181 tappvnsspd hlgialtsca nwesgffsay rdmaendrid iimcvgdyiy eyeaggysgk
      241 gpvrdhkpah eiisladyrl ryatyrtdad lqeahrakpw ivtwddheva nddwhsgaen
      301 hdpetegdyi arrdaaiqay lewlpvravp fsqggklyrs frfgdladlt mldlrtyrdq
      361 qlkfiraget ddenrsmlgs eqfnyllgqw rsssakwrvv gnsvmftpvl vppldpeatr
      421 avtellslpq dglpynldqw dgyaaerrkl inimdkegyd nvvfltgdih sswncnvpkv
      481 pgeypsagia aieivctsvs apniddivkl pqdnpislaa taglkaanpy vnylefdrhg
      541 ytavyfgred vtseyrlvev keepnqplfv aatyrgkpgq gmtqa
//
LOCUS       WP_284857707             309 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: EamA family transporter [unclassified
            Corynebacterium].
ACCESSION   WP_284857707
VERSION     WP_284857707.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..309
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31950
     Region          25..303
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 msreenqtev pqqgpllqrv nkfltlpvap vilvligslg tqaaavlvtg mlstvgapgi
       61 sglrmtaaai imvvlfrpkl sgmtrarain ivvygiamgm msmmiyaaia rlpqgvavti
      121 dflgpcvvsf lglkmwrsrl waivafigva liaqpsndld iigigyaaig aiffgaytlf
      181 sarmgstegs gmpdlalsvv vaaivlapfs vsaaplvdgs mwativisgf igavipyvmd
      241 tiaagivsaa vvgtlfaldp vigailgwaf sgdrvtwsma lgivliavag aiitwrgare
      301 srelqglaq
//
LOCUS       WP_284857830             486 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alanine/glycine:cation symporter family protein
            [unclassified Corynebacterium].
ACCESSION   WP_284857830
VERSION     WP_284857830.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..486
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51815
     Region          1..450
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 meqatdwvna wndkywllmi vlligtglyf cwrtimvqir yipemfrait ekpsdisegv
       61 kgisafkaft isaasrvgtg nvagvavait tggpgavfwm wllaaiggat sfvestlaql
      121 ykvrdkdsyr ggpayyitkg lgenwrwmas lfviaitvty gfvfnavqsn sitaavaqst
      181 gqetpifkfc vgivlailag viifggvqri savtqivvpi mavayiilgl ivlalnitev
      241 pgmiklifeh afgireiaga avgtammqgi rrglfsneag mgstpnaaat asvshpvkqg
      301 liqtmgvyfd twvvctitav iillsdptfg gdvegtaltq aalsaqvgtw aihavtviif
      361 flafsslvgn yyyaeanipf lskskavlnt vrvlvilcvi ggavgsvplv wsladtfsal
      421 matiniiail plggvavall knyseqkskg lnpvfhrddl pnlrghdkie cwdgsdpmtv
      481 resdva
//
LOCUS       WP_284857869             630 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: heavy metal translocating P-type ATPase [unclassified
            Corynebacterium].
ACCESSION   WP_284857869
VERSION     WP_284857869.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 630)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..630
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64960
     Region          28..624
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mssacgcehe pakeieeldr pwwkdpelll pifsgvtlgi glaldwtgve tpatvlfwvg
       61 lllgaytfap gairnlvtkr klgigllmti savgavilgy vgeaaalafl ysiaealedk
      121 amdraqgglr allklvpqta tvlrdgtavd iaakdlvage lmlvrpgeri atdgiirsgr
      181 snldtsaitg esipeevapg devpagains agvlevetta agtdnslttl vdlveqaqae
      241 kgdrariadr iarplvpgvm ilavlvgvig sllgdpetwi tralvvlvaa spcalaisvp
      301 ltvvaaigaa sqfgviiksg aaferlggir hlavdktgtl trnqpevtsv vpavefdraq
      361 vlafaaaveq qsthplagai aaarpeapaa ldiseeaghg isgtvegrrv lvgsprwida
      421 gplkadverm esegqtcvlv tvddalagai gvrdelrpev peavqtlhan gvevsmltgd
      481 ntrtaralaa iagiddvrae lrpedkasiv aefssktpta migdgindap alagatvgia
      541 mgatgsdaai esadvaftgh dlrlipqalq harrgsriin qnivlslaii ivlmplaisg
      601 vlglaavvlv hevaevlvil nglraaqakr
//
LOCUS       WP_284857919             219 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase [unclassified
            Corynebacterium].
ACCESSION   WP_284857919
VERSION     WP_284857919.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..219
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24119
     Region          46..170
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mdamsngthn hrtwkeiiaa dpqhsrryan rwrgfvregr didgearlvd amaprharil
       61 dagcgqgrvg gylakaghqi vgvdvdpyli deakrqfpea twlvgdlaql phvlddglen
      121 tphddtasaf dviicpgnvl tfvapedrak vlqgfaevln pengraiigf gagrgwdfad
      181 fettaqeagl iviqrystwd lrpfddesqf lvavlerak
//
LOCUS       WP_284857948             368 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: diacylglycerol/lipid kinase family protein
            [unclassified Corynebacterium].
ACCESSION   WP_284857948
VERSION     WP_284857948.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..368
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=39868
     Region          1..321
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mrallisnpn stsntarrmp gvvralrsve girltsmfta ypghaaemva gktvrdydvi
       61 islggdgtin eivnglmnsn pfsalpasdl paiatiptgs anvlagalgi prdpvdaawy
      121 iasllrsrtr stisvghaae rcfvvnagig idaevistme qlrqngtrak avrylpaift
      181 awnqlrkspp qitatidgte fgrdlamavv snsnpwtflg dlpivtnptv slrrglgfyg
      241 ftslrgvtgl vaaanlagff trlrspfhve arerrvdnvq hieltattpl rlqldgeyin
      301 qceslnirvk qgainfvara ddytedqftk kvatrpvder llvvvtkkvm drtrrlfsas
      361 qkteanpa
//
LOCUS       WP_284858033             395 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Corynebacterium riegelii].
ACCESSION   WP_284858033
VERSION     WP_284858033.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..395
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42688
     Region          17..381
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mgvktdlrst yqhlqptsad vviigggimg vstafhlasr gvknivller hrlgrgssak
       61 pmggvranfs dpnnvmlgqr slesfrtfye dfgtnieltq vgylflarte qevadlelat
      121 kvqnelgvrs rmvdpkelvq inpfvdeqav lagsfspddg facpaaavng yaraciqlgv
      181 tildmtevln ietgpdgmrs vetnlgvist dkvvcaagaw saaigemagq vlpvepvrrm
      241 igitpqqplk hpsvpftldl gtkmywhnyy ngllvgishd tapgfdrdft fewldefnaa
      301 asvvapslmn prldegwagl yentpdrnai igasskvpgf fyitgfsghg flqgpaagef
      361 madiiqgkes flpadafsvd rfgdedrelv etnii
//
LOCUS       WP_284858056             364 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide)
            pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
            [Corynebacterium riegelii].
ACCESSION   WP_284858056
VERSION     WP_284858056.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Davies,G.J., Gloster,T.M. and Henrissat,B.
  TITLE     Recent structural insights into the expanding world of
            carbohydrate-active enzymes
  JOURNAL   Curr Opin Struct Biol 15 (6), 637-645 (2005)
   PUBMED   16263268
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   4  (residues 1 to 364)
  AUTHORS   van Heijenoort,J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit
  JOURNAL   Nat Prod Rep 18 (5), 503-519 (2001)
   PUBMED   11699883
REFERENCE   5  (residues 1 to 364)
  AUTHORS   Ha,S., Gross,B. and Walker,S.
  TITLE     E. Coli MurG: a paradigm for a superfamily of glycosyltransferases
  JOURNAL   Curr Drug Targets Infect Disord 1 (2), 201-213 (2001)
   PUBMED   12455415
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..364
                     /product="UDP-N-acetylglucosamine--N-acetylmuramyl-
                     (pentapeptide) pyrophosphoryl-undecaprenol
                     N-acetylglucosamine transferase"
                     /EC_number="2.4.1.227"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0050511 -
                     undecaprenyldiphospho-muramoylpentapeptide
                     beta-N-acetylglucosaminyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051991 -
                     UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-
                     glutamyl-meso-2,
                     6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol
                     4-beta-N-acetylglucosaminlytransferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0030259 - lipid glycosylation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=37186
     Region          5..352
                     /region_name="MurG"
                     /note="UDP-N-acetylglucosamine:LPS N-acetylglucosamine
                     transferase [Cell wall/membrane/envelope biogenesis];
                     COG0707"
                     /db_xref="CDD:440471"
ORIGIN      
        1 msfsslsvvv agggtaghie palavaevlr dtygaevral gtekgletti vpargfelcl
       61 idpvpiprgk pwklfgvpak laksvnqtrr alkdagaqvv fgtggyvaas aylaakslgl
      121 pffvletnal agmanklgvr lggvglnava nsgmrgdvvg ipvrpgvgvd pdgakaergy
      181 rmwdldparp tllvtggsqg avsintalag aierltnegf qvlhaygrkn dapaphpgyt
      241 avpyiddmea ayavadavlc rsgamtvaen saaglpaiyv plphgngeqg lnsahlvsag
      301 aalriddsal tpdtlyeavk dvlgsperve emrralaetg agevaediar riagaaesaa
      361 esak
//
LOCUS       WP_284858184             403 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent RNA methyltransferase [Corynebacterium
            riegelii].
ACCESSION   WP_284858184
VERSION     WP_284858184.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..403
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=42622
     Region          6..401
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 mvtevqhvtv tvarmahgge giaqlddgrv vfiagtipgd tvdaritksk krwaraelve
       61 vrtpsemrva htcpaaaaga gccdfshiap eaqlglktei lrgqlralaq tanaeelpie
      121 avslppsthw rtrvrlgvdd hgragvrkar stevvtsatc tqpvvglmds lpsfspgsev
      181 vavmdstgar hivqttramr gkrvehidtv vegsgevtqr ieagygsstf qfpatafwqa
      241 htaapnayar vieqwgkgty ksdvawdlyg gvgafvpaih aatggasvis vdyspaatsr
      301 tqpaldgidv rvvaerverg vdkleapglv vldpprtgag aqvvaaiaak apervihigc
      361 dpatfardva awreggytvk rlglidafpn thhfetiavl epr
//
LOCUS       WP_284858192             286 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Corynebacterium riegelii].
ACCESSION   WP_284858192
VERSION     WP_284858192.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..286
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31699
     Region          6..272
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mesirelerv ltlkqvgptt fegpamnalv fvrmfgghla aqalaaasat iedgkyvhsl
       61 hsyflrpaea dlpvryevlp lrdgrsyalr tvqayqgekl cfvlsasfhh nldegpehae
      121 qmpdvprpea itpggkipsg vpdaekefhe wdirdvpies naqdattvsg rslwfryrhq
      181 lpdtdvfhaq altyltdmtl lytslqahpe akvqlasldh nmwflrpvrv ddwllyrqss
      241 psagsgralt qgkifdaagn lvavivqegl arnlregatq vpmrgk
//
LOCUS       WP_284857959             441 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: AAA family ATPase [unclassified Corynebacterium].
ACCESSION   WP_284857959
VERSION     WP_284857959.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 441)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 441)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..441
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50337
     Region          5..435
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 mdktmllefg vtnyksfsee tiltmaasre qrhkqriprv kskynirvlp vaglyganas
       61 gksnlvsala tlrrilsnpi tddsglpyep ykldeqystw ptifrilfiq deqiyeytis
      121 ynrdmivdes lvkirsrdev lvferqgenl rlgevfgsre irdflssvdh kipaatalaq
      181 fkkvntqgir dvlalrkwin rlvtiyagfl tenryvplpk tgidfmknig agiedikrvp
      241 velddislpd ekrrvivndl dssgkiitfe qdgvryeavn ldgeikiqkv lllhsgqgas
      301 mpfnwseesd gtkavgaiyp liwalaqren ppivvideid rsfhtlltln ilesflsrcn
      361 eetraqllft thdlllmdld vfrkdeiwim eksrlgssrl vslvdfkgir kdrdlrksyl
      421 egrfggipni rnlrvsdegr a
//
LOCUS       WP_284858275             428 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Corynebacterium riegelii].
ACCESSION   WP_284858275
VERSION     WP_284858275.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..428
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=45343
     Region          188..310
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mtvnsaadhl vgvdasawpg vaapphirga alrskraeaa fakaasqagl aldgdepalv
       61 vahadvfari aasgwiglae gylageweta dsdalvavlr gliaakycpk tprispsraa
      121 delpadlish fsgdgvspfq ghfstgvptt qrelvksfvr gagrqhepak hfvdvtefat
      181 pldagrgdls daqarsaaml ldavhagtgi hlqirpaags alavvasrrg atvdcvansd
      241 qaaaelreql tfagvadavr vetlgeaahg aydaivsveh letlpekakg eflrlldnsl
      301 vpsgmvciqt vvcverlpsa avaaleslra yiwpglsflt shdiakttdr ntglriiaet
      361 rapehlaesl alqrrtfegn lrdaaadgfd vvyrrlwiwq lalrealare gmlsltqltm
      421 vrrrrrgr
//
LOCUS       WP_284858373             260 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium riegelii].
ACCESSION   WP_284858373
VERSION     WP_284858373.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..260
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28144
     Region          1..260
                     /region_name="Cof"
                     /note="Hydroxymethylpyrimidine pyrophosphatase and other
                     HAD family phosphatases [Coenzyme transport and
                     metabolism, General function prediction only]; COG0561"
                     /db_xref="CDD:440327"
ORIGIN      
        1 mkiavfdfdg tlyhrrpdgt ysfnpqdlea isawrdngnl aiaatgrsrs altfampped
       61 alvfdyrvls ngasattgng adliyaypid tdilraavek fgdtegvaif gttvgsvdga
      121 fsvntktgdl ftdhfahmtl seipdhtfav vpirvtdpal rrrvvswaeq fpqvtvaqnl
      181 dyvdimangr nkgtgvlell ehlginredv giytfgdswn dldmhaiadq sfsfthspad
      241 vkeatdhvie avadvlngla
//
LOCUS       WP_284858407            1231 aa            linear   BCT 25-DEC-2024
DEFINITION  UvrD-helicase domain-containing protein [Corynebacterium riegelii].
ACCESSION   WP_284858407
VERSION     WP_284858407.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 1231)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437585
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1231
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..1231
                     /product="UvrD-helicase domain-containing protein"
                     /EC_number="3.1.11.5"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=133153
     Region          35..1223
                     /region_name="RecB"
                     /note="3#-5# helicase subunit RecB of the DNA repair
                     enzyme RecBCD (exonuclease V) [Replication, recombination
                     and repair]; COG1074"
                     /db_xref="CDD:440692"
ORIGIN      
        1 mstqytylsp adivvegdam atdlngrnfi qwstdsnvfv qagagsgktt tliqrlltli
       61 iddginvdqi aaitfteaaa gklvsdlrqa ltqvaatgth apfaksaptv frkvdqqeaq
      121 aradralesl pgavigtlhs fclrllkqfp leaglppkvd kvdelrqqvd lslrsdaive
      181 mltrlieadd talaeleeik rtyglrhtda aqvaadvqll vtegaslegl advacwmdqr
      241 wgelgetlka prfevegdae hvrrmfdavd gtydevknfv pendellaal ttyrdaiqpy
      301 vadaaaaklw qpilpraggl sakdweklai pdataeylsd vdknvksdka gahvkgmlvh
      361 mhnafekrgr pgltaaltgv lpvlaalvlq qkdsrlrkgt leyhdmvfla delvcgedng
      421 nirtalheqf kvifvdefqd tdpvqydivr aiasgevngt pvpghlfvvg dpkqsiyrfr
      481 nadidsfdrv kasygldgsg hgvllnlyqn frsstavvsa inqvfphild gtrgeglptq
      541 asyeameaqp tqsynlpdgd trdlpgkvif lheedtaagt aaeikqaeee divaliraat
      601 snvggeyyrh npefetdaeg nliegtatpk alqfsdiavl tptngesrri vralsnanip
      661 svsegstllf rvpevsdllt vlraisdpad aftqvaalrt allgcsdaql aaaakaeaga
      721 agfeqaqekv qqerdwlrak aleaqaldvg tlvrhvvsec elrnayvasq rtdnlgsleq
      781 vialadkfgr vtglglrefv rwadeqtdna ssahdpvldn nangvrvmti hrskglefpm
      841 viaagfsnpp ppnktnkgfs rgeakvaevq lggvstpgye rwkkfdtaas adelkrlayv
      901 altraesvla vplhigltka nkrkavrgtp liqaldaiap liqlqdrasl naprdplppl
      961 glrasvseqa lsnanpdrrq allhaaaalt qrlgvtsiah aadsasateq disraqahde
     1021 apyatrmtgs avrmqleheg viptdvfrav nanvrrgdsg aafgsavhev merlpdsdgd
     1081 vnrlsaiaaa lyglpdtaia qvaatarafs askpymrald sdvvyrelpi aghvtgvkfd
     1141 rpnpsdsqet vtkeetiavn gyidllyrdg dtwviadykt deyatperva syflqlelya
     1201 rilsrtlgte vgrlelifqd gdecqvvdfs r
//
LOCUS       WP_284858538             471 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium riegelii].
ACCESSION   WP_284858538
VERSION     WP_284858538.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..471
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48742
     Region          25..447
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(35..36,39..40,43,79,129..130,132..134,137,157,
                     160..161,164,277,280..281,284..286,289,316,320,369..370,
                     374,378,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mpatpkiqre gwasakhras vylilavvgi ailfdgydlv iygavlsnll edptqigals
       61 pqvagtlgsw amvgvmvgal aagavgdrlg rrnvflvaiv wfsigmavts maqsivmfgl
      121 lrfltglgig vivatggaii aefapanrkn lfnaivysgv paggvmaslm alwfqdawgw
      181 rglflfgasp llfllplayv alpesprwli trgrhakata vcekyglpkd sflfdpaass
      241 ntaasatqak sdiektgfag ifsrsyligt lligamsfig llstyglntw lpkimqanga
      301 sphdslysll alnggavigg lfaawvadki gakivitctf llaavmlail pqfntvapmy
      361 lpialagigv lgtqvlvygl tsnyfgtaqr aagvawtagf grlggifgpa iggliigsga
      421 tpstafyqfa avaavgalct aliprspvdr mldqgpvpaa apekepvpva r
//
LOCUS       WP_284858641             566 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Corynebacterium riegelii].
ACCESSION   WP_284858641
VERSION     WP_284858641.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..566
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62923
     Region          51..539
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 msakprvnrr vflqsvaaaa aatafgagga yaarrgtgst pefpviaqew dlpflhgvas
       61 gdplsdrvvl wtrvtpsrea lpgsglgedv elewqiatse sfrnprtgrv tasaeqdhtv
      121 hvdptglepa teyfyrfvvk sgafagatsp igrtltaptl daeldhlnla iascanwesg
      181 ffnaygdmar rartgeidhv vflgyyiyey ptgeyagksg vtrmhhpewe ittledyrqr
      241 ygryrtdlhl qaahaacpwi vvwddhetan nswregaenh tegrvegawd errqaaeqay
      301 yewlpvraql ldsgtpqlyr sfnfgtlaql tmmdlrsfrd aettgaefan pdrtmmgqeq
      361 fnwvaqrlqe snarwevlgn svmvspmrfa tipnndkanl atgymqerat giavnsdqwd
      421 gyaaerdrll tmldeqeana lfltgdihse wansiaspsg fgeigcemvt tsisapnvde
      481 ilttafgtyh pednstslvv eqairdanpw vkhidfdahg ygiasihhdy vemlyyrvsd
      541 vedlhatvsl gesrtwrige gfvese
//
LOCUS       WP_284858741             443 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium
            riegelii].
ACCESSION   WP_284858741
VERSION     WP_284858741.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..443
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=47530
     Region          1..442
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrmtvigtgy lgathaacma elghevlgvd vdqhkiealq nstvpfyepg lpevlernid
       61 agrlsfstdy ataasfanih figvgtpqqr gsyaadtryv eaviddlvpk lqghhiifgk
      121 stvpvgtaaa lqeradklvq ngasveiawn peflregyav kdtiepdriv lgvnatnsqa
      181 essavqvare vyatplahnt pfivtdlqta elvkvsanaf latkisfina vsevceivga
      241 dvtqladaig yddrigrkfl gaglgfgggc lpkdirafma ragelgadqa ltflrevdai
      301 nmrrrqrvvd laremlgsli gtritvlgaa fkpnsddvrd spalavagql slagasvrvy
      361 dpqamdnark vfptldyass ledalrnael vilatewqef kemepgwvag vvdkqklidg
      421 rnvlpaeawh aagweiqalg rsl
//
LOCUS       WP_284858910             333 aa            linear   BCT 25-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Corynebacterium
            riegelii].
ACCESSION   WP_284858910
VERSION     WP_284858910.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..333
                     /product="isopenicillin N synthase family dioxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37335
     Region          1..314
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 mseatlpiis yaklaagdve eidrlrqvth eigffyladh gvdealrdtv iskskeffal
       61 pleqkneisn lnnrhyrgys clgdertqnk vdwreqldys fdlpapdeae ykerpwrvve
      121 gpnpwpaqvp elkgavngyi ehltgvaqni irawsqalgq dpgvfdeqfa npfpllklvr
      181 ypavehneat qgvgahkdsg vitllyiepd ssglqvetdn gwidvqpipn tyvvnigell
      241 eratdgylva trhrvlptak gserysfpff ltpnldtvlp tlelpdsrgv gqdmqgqqiy
      301 ensglntlks rlrahpetta kfnqaiadqf qel
//
LOCUS       WP_284859138             483 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Corynebacterium riegelii].
ACCESSION   WP_284859138
VERSION     WP_284859138.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..483
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51176
     Region          1..480
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mthskssasg apvvetlgid ivpesertak psdlfwpwfa anisvfgisy gsfvlwfgls
       61 fwqgalvtal gvrfsfflcg liavagkrgs aptmvlsraa fgvqgqkvpg ivswltsigw
      121 etflaimavl atttvlrelg gnpgmatkvi atvivagliv aasvlgyhti mklqsvltwi
      181 tgavtllyma ltipridwsa vqeipagsag svvgalvmvm tgfglgwini aadwsryqrr
      241 dtpdrsiifw ntfggaiapa ilvifgllla asdeslaeai addpigalav vlptwvlvpf
      301 litavlalvs gavlgiyssg ltlltlgini prpaaaaidg viltigtiwv vfvsqsflgp
      361 fqsflitlgv plaswagili adiftrtkdy depalydsag rygavdwisi gilvissvig
      421 wglvanlfae eaawnnwqgy flplvgehwa danlgvlval vlsfvaawfa rrgrirrqee
      481 iaa
//
LOCUS       WP_284859143             628 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium riegelii].
ACCESSION   WP_284859143
VERSION     WP_284859143.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 628)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 628)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 628)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 628)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 628)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 628)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..628
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=68868
     Region          184..616
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mgksqatrdv qqvvnealga thdilaadnv ehlrsllngd plalvtvtvh edglapdhpl
       61 lelisepgfe ytrvmvltta pevagldalt dmgrldmlvf tpaikaeall hniqqqlnry
      121 wymrakhdps iagtfalpev teldvgltdq eiisriiqaa dmhlgyqprl vfppgvyltk
      181 eghyveevif alsgqvllqr ftdagdivmh hastghvigl lalasnrvgf ftartttevv
      241 avqlpteqvd ylirqepela rlfnilfvrs ydrrlrraed iqieqhelta qlederarlt
      301 talhnleaar relmsqarfa slgelaagva helnnpmaai ertaahlaed vegliasspn
      361 rrwrdatsha leaarsshav stkearalrr eltevtgdra laqrwvlagl hdvefakqvr
      421 anrrldyetv ehaasigtal rnlstastri tqlvaslray arpdgdpvtd vdlhqsiedt
      481 lqliahklrg veikrdfael phvtctpgqi aqvwtnlitn aaeaieesgk gttitirtsa
      541 pkpgwvrvev iddgpgiple ridklfeprf ttkngevrfg mgiglsicrg ivsahhgtie
      601 ltsstngtca tvglpidgph ahdegdtp
//
LOCUS       WP_284859160              96 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA polymerase sigma factor [Corynebacterium riegelii].
ACCESSION   WP_284859160
VERSION     WP_284859160.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..96
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=10020
     Region          <8..45
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mlalkisgls speiadelgi aagtvksrvs rarrqlsral dqvgepaksi skgvldcvqi
       61 ptyatnemar qrapgqqppm qqpsalthen gnelgg
//
LOCUS       WP_284859310             711 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium riegelii].
ACCESSION   WP_284859310
VERSION     WP_284859310.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 711)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 711)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 711)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..711
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=74204
     Region          2..708
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mthielgvtg mtctscssrv qrklnkldgv eaavnystet atvdydpskv dveqllstvr
       61 sagydafvvq dkepllddan sapttdpllt ttvwsaivsl pvmlvsmipa mqfanwqwaa
      121 faattlvyfs agsvfhratl tnlrhgsftm dtlitlgtta aygwsiwalf fdgsdhiyle
      181 tvcvvitfll lgrwfehrak grssealrnl ldmgakdaav lrdgvevrip igelrvgdhf
      241 vvrpgekvat dgrvvsgssa idaslltges vpveitegdt vtgatlntsg rlvveatrvg
      301 enttlaqmaq lvkdaqssqa pvqrlvdris qvfvptvivv allalvghli agqgvtqaft
      361 aavavliiac pcalglatpt ailvgtgrga elgllikgpe alestgnvdt ivldktgtvt
      421 sgqmqvtdvy pargwdkdev wglaggvekq sehpiaqaia agtqpaeatd fvaepgigas
      481 aridghrihv grptrdlgel aaafdaaeaq gatavaverd gkaigviavr dtvradsaaa
      541 vaelkrmglt phlvtgdnag aaeavarevg ieevtagvlp adkvdvvrsl qsagkrvsmv
      601 gdgvndaaal atadlgmamg agsdvaieas ditlmhdslg savdaihlar rtlrtikgnl
      661 fwafaynvll ipvaalgwld pmlagiamaf ssvfvvsnsl rlkgfkaqfg g
//
LOCUS       WP_284859332             850 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium riegelii].
ACCESSION   WP_284859332
VERSION     WP_284859332.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 850)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 850)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 850)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 850)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..850
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..850
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=91209
     Region          132..848
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msvsedlsrs ielardaarl agvetsgqsm ridggdddhq rrnisyafel vgvkdapqla
       61 dievaleeip gvttrmvypt smawitapsd vhpeqlenii rafgvdpvmt dttlqrqall
      121 kdaveprspr kstrgmsvri rrrrrdaqas lsaardagfv rrartrsssn dvlftardlv
      181 tparlitavv lslpvivlsy spavqfpgwq wlclalttpv afwcalpfhr amaggvrrgl
      241 saldgassva vlaaylwsvv allftpagei gwvsatgwtp trrgdamdlf ldvacgvtal
      301 llvgrfyakr agaslvdqma qftppsdtey kvirrghgde evlplseinr gddvevragq
      361 tipvdgevvg gsahldhvlv gvdaepnvkv gdevaagtvv drgkikvrar rtghatkwaw
      421 vsrwveeasr renaatmvst rsagmmipaa yalavidfgl wwlidgnina afstalaila
      481 vvapvalais palairhgve aaarhailvr dgatlrkcee vdtvvfnrvg tlvepemtve
      541 tvtaaegedt dvvllvaaal lvesnhpssr aivaaareak ghgapwrvdl eestihqdgt
      601 ttgrvtlrpv vdgraaddde vtyldaelwr ptnlsrlkgr lalaavsgga pivvrwknrd
      661 rgvitlhdpa kqdaadavdr leamgtttvm ltrdtyavgr rfanmlgiss vlagvtahdk
      721 agavrqlhsr ganvamvgsl svldvievgd lgvlyaeedf fesnmkknte leidalvmrd
      781 dvmavpqlle hgrrvsriid snmafaliyn avavalamsg vlppmgatlv mlgssliigq
      841 rssragrfps
//
LOCUS       WP_284859343             115 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium riegelii].
ACCESSION   WP_284859343
VERSION     WP_284859343.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..115
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12644
     Region          25..112
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mkdyvatten tdldccslgs gllseadatr yadlfkvlad pgrlqllsri aeegcepmsv
       61 geltqrsgls qptvshhlnm ltkaglleks rqgrtvihrl rpelfeelrt vlqmd
//
LOCUS       WP_284859404             464 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Corynebacterium riegelii].
ACCESSION   WP_284859404
VERSION     WP_284859404.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 464)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 464)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..464
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51242
     Region          5..448
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 msvnllsfsv gnfksireiq tlefadgpld skqprpvpvs vllganasgk snlleamvfa
       61 framklsata wldvdhyeyd stiptpfsld qdsqgepsff efdfvakgrr ylygftfgrs
      121 gvveewmsyv psvrwtsvfn rtaqpevewe wnssavsrtl qreieradvr elavshalrg
      181 klgliyesvs alldgvnylp lgdsqkdqrl sqlaramrkg qvklsevtqm mqaadtgivd
      241 vsideenlsp alaelakilt qrledvskde kgslkgfhma hepgayidis daelkaiayq
      301 lmfthrgdns nhtlkmaaqs dgtltwlsva piivdalrng hvviadelds slhvqllelv
      361 vkaftdesin vngaqlifss hdtnllehmr algldtdafw fveklqsgas evfplsgfek
      421 rkdanyerry ldgrygalpr vspalirglv leavgegpea adgs
//
LOCUS       WP_284859424             526 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Corynebacterium riegelii].
ACCESSION   WP_284859424
VERSION     WP_284859424.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..526
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55569
     Region          128..517
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mstpvvhest alsdgdraps peagewrrql iglltgivla ilvyiffpag aadtvaqssg
       61 akegveysaq smrvvaattv lmaawwmtea iplaatallp laifpvmgva pfkdvsspya
      121 satiflfmgg flmalglqrw nlhrrlalvv vkmvgtspkr iilgfmlatg fmsmwvsnta
      181 tavvmlpigt svlaltaesv ggmknqkrfa talmlaiays asigslgtli gtppnallkg
      241 ymeeahgiti gfgewmlvgm pvaivftfva wwmlitvfkp evdripggke lidaelkklg
      301 swtfpqvavg vifllaaltw ifiplgrnhf gwdfpyddav vgiiagllmf ivpankdgkr
      361 ildwktanem pwdvlllfgg glslsamfta tglslwigek akglsvlpvf lllaavaalv
      421 lflteltsnt ataatflpim ggvavgiglt estemnvlil aipvalaatc afmlpvatpp
      481 naiayssghv kmgemikggv glnliglvli slatyfiavp vfglvl
//
LOCUS       WP_284859428             425 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium riegelii].
ACCESSION   WP_284859428
VERSION     WP_284859428.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..425
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45317
     Region          8..411
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(18..19,22..23,26,60,110..111,113..115,118,138,
                     141..142,145,246,249..250,253..255,258,285,289,338..339,
                     343,347,363,366..367,370..371,374)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mrtkgavvfl lwlavlldgf dlvvlgaamp amlddpnwhl dpagatqist aglvgmtlga
       61 lfigaatdkl grrkvmifsv lafsvltlam gftynfwafl tlrflagfgl ggclptaism
      121 vtefrgraka gsstttvmtg yhvgavltaf lalflispfg whsmfivgai pglilapvmy
      181 fllpespdfl rvtgreeear rvasqyglsl eeasagvvpq veekagaaal lrppylrnsi
      241 avwvtsfmgl llvyglntwl pqimrqadyd mgnalgflmv lnigavvglv iagqvsdkhs
      301 prrsglvwfv lsalflamla irmpmpvlyt vvfltgvfvf ssqnlvyafv genhpsnlra
      361 tamgisagig rlgaisgpml ggllvhhnla npwgfysfai vglaaalffs ltkplvvidr
      421 egaka
//
LOCUS       WP_284859455             263 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium riegelii].
ACCESSION   WP_284859455
VERSION     WP_284859455.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..263
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28525
     Region          1..220
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mtaaffdldk tiiatssafa fgkefmhngm itraealely wakvsymlvg qssekmdstr
       61 dalaqlvegw kvedvqritq etmrtvvtpa iyaearelin qhkaaghdvi iisasasilv
      121 epiarelgid tvvatemgve dgrltgeitn ylkgdakada vrrfaeehgy nlaesyaysd
      181 satdipmlem vgnpvavnpe ralkkhaaan gweirvfknp epliqmpnar evtigasvva
      241 giaavalaat lltrqllkdk rsa
//
LOCUS       WP_284859604             573 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Corynebacterium riegelii].
ACCESSION   WP_284859604
VERSION     WP_284859604.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium riegelii
  ORGANISM  Corynebacterium riegelii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 573)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 573)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Corynebacterium riegelii"
                     /db_xref="taxon:156976"
     Protein         1..573
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=63714
     Region          24..432
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mdrdsemiql qprigviklk sgeqvrlegg silaivgpnn sgkshflkql raclygasie
       61 tvdrdaglie slgirwptad rktylqsvaa qkferrgavf daelpsrvyg saasvftetd
      121 iqaiasdgnc fgpfvetfvr fdeplsrise serqlmqdqs splirlraqk kayeavqkdf
      181 afvfdediyf hqhegklnff lgkpptpmpl iteayspeie rflegartid rqglgmrnvv
      241 glllrlytda rsiilldepe aflhppqanr lgqaiqsvce rrklqvicas hdrnlisgls
      301 kakenqlvvq rlssttgsgv syfsrtvssk afdnvralsr irftpvlesm fasvavlven
      361 endalffesa lefyakdldn rsartlrdsl lfiptngnsn fastaqllrn lcsptvivgd
      421 ldicsdpkrl rqtvdamnps lgeeaeqlak riigrfsqih eaklakiekg kqegklkkwv
      481 seevrvdhed qtvrglvgel llflkgagiv lipegeledf grevtsssdk niwvreaidq
      541 qiyaednvqg fcetivsaaf aaidaqarht ssn
//
LOCUS       WP_284859776             488 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284859776
VERSION     WP_284859776.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..488
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53621
     Region          3..488
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mqhlhhdfad hfpdlcldwr aakapapqiv clneplahel gldpswlrsp egigflcgth
       61 lpegaqpvam gyaghqfgqf sprlgdgral llgevrdgag nlrdihlkgs gptvfsrggd
      121 gwgafgpmlr eylvseamha lgvpttrsla vistgraiar ervvpgallv rvasshirig
      181 sfqyaqltgg eelvcklaey trnrhypdaa darevfhhal daqlatvaqw mrlgfihgvl
      241 ntdnttlsge tidygpcafm defnehavfs sidhsgryry hnqphiigwn farlaeamlp
      301 tfaadpdeav gfaqqtmntf qerwrkahns ercraigvey sednaklade fyeligkans
      361 dltsahralv daavrdrhti aapgvdtars pvnvlarqlg dtaparewia rwlnhapsph
      421 alarlhpmii prnhlvedal ssatdgdlep fhqllhavth pfgknhppef lkpaprefsa
      481 tyqtfcgt
//
LOCUS       WP_284859916             849 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284859916
VERSION     WP_284859916.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 849)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 849)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..849
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..849
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=95288
     Region          20..843
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mnlndvvpdl sevpssllee siwesflrwt kdkgislypa qeeaslaala gdnvilstpt
       61 gsgktmvata aqffclaegk rsfytapika lvsekffalc dvfgpenvgm mtgdatvngn
      121 apiiaataei vanialrdgk daridqvvmd efhfysepdr gwawqvplle lpqaqfvlms
      181 atlgdvswlr edltqrtgrt ttlvtgttrp vplafsyefi aveemidtlv dnhkapiyvv
      241 hfsqrkateq aqsltatsfl nseekqrmve eigdfrfstt fgkqlskmir rgiglhhagm
      301 lpkyrrlvek laqtgllkvi cgtdtlgvgi nvpirtvllt glakfdgrre rivksrefhq
      361 iagragragy dtegtvvvla pefeienakm rrkagddpkr lkklkkkapr dgevswsekt
      421 yerlinsepe slssqfqmsn smllnviarp gdvyahmkhl irsnhdtraq qnqsilaats
      481 lfrglrnagi vdkpanetgt dsqgrryhlt eelqrdfaln qplapfalaa vglwdpdspt
      541 ytldvistfe ailddprqll qaqqsfarge einalkaegv dytermkive einwpmpcre
      601 eldaafetyc qghpwarefd ispksvvrdm lensmtfsdl iatyglarse gvvlryltda
      661 wrtlnhsvpa eaktdelsdi ivwlgeliqq vdsslvdewa tmtdedapvs qervdrelaf
      721 gvedpsalsa npralkimvr nymfrlvqlf alerevrleq lldylenypd isdalddyfe
      781 qytdldtgpe argpeyfhld asarsrlwpv rqiirdpegn ndfqfvatvd ldasddagev
      841 rlrdlrier
//
LOCUS       WP_284859885             417 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284859885
VERSION     WP_284859885.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..417
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=44660
     Region          9..403
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mnltelatqr lekwqqqglm rtpiefagpq tpraqlkdqp serillsssn ylglathpev
       61 iaaarsalkk fgtgsggsrl ttgsttwhrr ierelanfvg fedavlfatg yqanlsvlqt
      121 lahpdlhifs dslnhaslid girlattsgt kksiyphcdy taleqqlaec taryklvvsd
      181 gvfsmdgdia dlarlreict hhdawllvdd ahgigtvgkh gigstqvhnt rpdilivtas
      241 kalgaeggfv acstpvanll rnqargyvys tacsaancaa isaaleviqk pltqqhpvvr
      301 lqqraaalre itgirvfdgv dsdsvlfdsa hsgsahspii plpvgaesaa vrlaseladr
      361 gfhipairyp tvargqailr atamatlela ditqfaqtlr dlgwrpptpa kaispgr
//
LOCUS       WP_284859865             527 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284859865
VERSION     WP_284859865.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..527
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56091
     Region          128..518
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mstphihest skaegqdsev rerrettrqy tgllvgials vlvylifpsn avetlsqsag
       61 adpevdynlq slrlvaavtv lmgswwmtea iplaatamvp lvvfplfqvg efsdvatpya
      121 satiflflgg flialglqrw nvhrrialmv vllvgtspkk lilgfmlatg flsmwvsnta
      181 tavvmlpigm svlqltadvv ggmrkqakfa tglmlaiays asigslgtli gtppnallag
      241 ymseahgyti gfaqwmmvgm piavvfvfia wavlvtvfkp emteipggre likkelhemg
      301 kwtgpqigvs iifvlaavsw ilvplildqw leietgyeda ivgiaagllm falpadkkgt
      361 rlmdwkttne lpwdvlllfg gglalssmft ktglslwige iakglgslpl fllifavagl
      421 vlilteftsn tataatflpi mggvavgigl tanaehnvlv laipvalaat cafmlpvatp
      481 pnaiafgsgy vrigdmikgg vwlnvvavil ttlvvyfvai pvfdivl
//
LOCUS       WP_284860013             488 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284860013
VERSION     WP_284860013.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..488
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53610
     Region          3..488
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mqhlhhdfad hfpdlcldwr aaeapapqiv clneplahel gldpswlrsp egigflcgth
       61 lpegaqpvam gyaghqfgqf sprlgdgral llgelrdgag klrdihlkgs gptafsrggd
      121 gwgalgpmlr eylvseamha lgvpttrsla vistgraiar ervvpgallv rvahshirig
      181 sfqyaqltgg eelvcklaey trnrhypdaa dtrevfhhal daqlatvaqw mrlgfihgvl
      241 ntdnttlsge tidygpcafi defdehavfs sidhsgryry rnqpqiigwn farlaeamlp
      301 tfaadpdeav gfaqetmntf qerwrkahna ercraigvey sednaklade fyelvgktsp
      361 dltsahralv daadrnghti pasgvdtars pvdvlarqlg dtaparewia rwlnhapsph
      421 alarlhpmii prnhlvenal ssatdgdmkp fhqllhavth pfgknhppef lkpalrefsa
      481 tyqtfcgt
//
LOCUS       WP_284860019             310 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284860019
VERSION     WP_284860019.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..310
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34963
     Region          12..243
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mghdgmnhpr ptlwavadlh aavranrlrl deitprhpdd wllvagdvae rldlistvls
       61 elrsrfaqvi wvpgnhelfs rstdahrgra kydalvqicr sidvltpedt fpvfgdttvv
      121 plftlydysf rpggtgveea lelaaqknvv mtdeiaiapf adirawcwdr laysitrlsr
      181 vngptvlvnh wplvqeptlr malpelalwc gsrhtrtwpq rynakavvyg hlhmpaifel
      241 dgvehhevsl gyprewgrsd qnriwpcpvl elvadpnggq iaqrvgleqc reshpelrmp
      301 rrrgkgsdgv
//
LOCUS       WP_284860022            1175 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284860022
VERSION     WP_284860022.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1175
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..1175
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=124839
     Region          244..390
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <646..1119
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 msvkstsprn prgggernka ranstrpapr tgpgraagkk lsfgmpgktg gdqaksreek
       61 sdsanletvv fgsaqraant shertgsafr avgsgiataf sktsdalkrf gnigqadddy
      121 dayadyddli ddadtdadaa emdrqatdkn kklknspagl dedlystdmt skkakakkrq
      181 rssgamaqsr grkrstdthv sdddldqhgd daqaeqtegd evavsesalp aakpevgvps
      241 srsdaialtl igvaivlgas vwldiagfig raiatathav lgagafiipv alviaasalf
      301 sgrrvavehr arvsmgtali vismlglihl fsgaptewpe rfvaggalga wtggalaagf
      361 spyvavpllf lviiygalkv tgitvkefte ylrnvisgng sknldadpdr esvgghneyg
      421 daygrandei aaiasgaqrt prrraplrtn pvasqsnrpg fttsqssnag thdvvangkk
      481 stglfprteq psqvehtevl ysngsrehqe qvsktaagle saptasdtde fpavldsptr
      541 srsartepev ekteklplap edavdqaqag lqqkqaaenp rtvdtkhpdt arqtrvpgvk
      601 pqsdarqpva qqatqvglas qindgpreda gatqqaskla teytipsagl lepgrapktr
      661 teindrtiea idacfaefkv daqvtgftrg ptvtryivel gpgvkvskit nlqsnlayav
      721 atgsvrilap ipgksavgie vpnsdreivr lrdvlesevi agdedptlvg lgkdiegefi
      781 sssiqkmphl lvagstgsgk safvnamlvs lltratpddv rlilvdpkmv eltpyegiph
      841 litpiitqpk kaaaalqwlv eemeqryqdm rsarvrhikd fnhkvrtgev qapagserkm
      901 epypfivcvv deladlmmta pkeieesivr itqkaraagi hlvlatqrps vdvvtglikt
      961 nvpsrlafat ssstdsrvil dqtgaealig mgdglfipqg grpvrmqgaf vsddevyavv
     1021 eaakeqgepd ytegvtedkq aeakkaiddd igkdmddlle avelvvtsgl gstsmlqrkl
     1081 rigfakagrl mdlmeargiv gpsegskare vltkpeeldt tiwmikgadp adaprevqeq
     1141 qnqgqpdnvv edsagdtags ahitkatynp tsqaf
//
LOCUS       WP_284860055             323 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284860055
VERSION     WP_284860055.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..323
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34405
     Region          2..319
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(40..41,45,118,122,125,143,146..148,167..168,172,187,
                     210..211,232..236,257..260,307,309)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(130,225..226,239..244,252..259,262..263)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mkaiqitrtg gpevlqitev esptpsddqv lvdvlvagvn yidtyyregi ysattpfipg
       61 fegvgrvrhd pigkiasgtm vawntafgsy aeqvcvardk lvavpndfdl staasmllqg
      121 itahylthgv yeladgdncv itagaggvgl latqfaaaag anvytvvssd ekeelsyqag
      181 athvlrygpe lanqvrelta gkgvdvvydg vgkdtfeqsl dmvrnrgtvc lfgaasgpvd
      241 pidpqilnek gsifltrpsv agwtsregef qmraqavvqa vvdgdlkfrv snsypleeaa
      301 qahrdlqdrk ttgsivlrvq evi
//
LOCUS       WP_284860075             936 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284860075
VERSION     WP_284860075.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 936)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 936)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..936
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..936
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103520
     Region          2..934
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtsthfetfr sqltyeldpf qvqgcraven grgvlvcapt gagktivgef avslalsrgt
       61 kcfyttpika lsnqkfhdlv aihgedavgl ltgdvsfqpd adivvmttev lrnmiyaksp
      121 aldrlthvvm deihfladqa rgavweevil nleehisiig lsatvsnsee fgrwlstvrg
      181 dtevivsehr pvpleqwmli gqkvyplfap gtpaiegptt sepagvnpel qrrvarleag
      241 daadgrddfr pgqgfrsrtt agtgnsrsgn vrpqdryrpl grpevlrilq gqnmlpaiif
      301 ifsragcdga lhqclrskmv ltdedeqrii tevidagveg iphedlevlr fsqwrkalir
      361 gfaahhagml pafrhivekl fvrglvravf atetlalgin mparsvvlek lvkfngeahv
      421 dltpgqytql tgragrrgid tlgnaivqwa pamdpqrvag lastrtypli stfepgynma
      481 inllnnlgmd dslrlleksf aqyqadgsvv eetreierav hrveklreqi neaiaafapp
      541 sfddqdpaql lseyvelrkr lsveekslks rakdergdet railaklqpg dvialpskkr
      601 pvlavvntpa nqtadprpwi ttekgwsari dasgfdnppa lvgkmklpgk alknprrhnh
      661 ivvdkfared yprpkkmklr arirdterik dlrtqmkkhp ahawpamere qltqlaqkyl
      721 rrkgeldklr atvdkatetl gdmlrrivdl lteldyvdiv dgepvvsieg eklaqvhnas
      781 dlliaqclkr giwqeldpae lagvvslctf enrratggql fdgvtdamts amentmrlwe
      841 elisdesrhg lphtrepepg fsiaihqwca gaplgyclaa aaesgaeltp gdfvrwcrqv
      901 idllqqvakt gysseikrta gqaiasinrg vvaigs
//
LOCUS       WP_284860097             335 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284860097
VERSION     WP_284860097.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..335
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=36163
     Region          17..305
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mstspetsqt ansphfspsl kwqrrlalil llsqagitvs gsivrvtgsg lgcdtwpncq
       61 egslvpvaga qpwvhqiief gnrlltfvvv aaaiavlval kqagrrrelk aysvasilgi
      121 vlqaviggis vhmelhwwtv alhflpsmvl vwiaallysr iaeddsqspq rifaahtrqf
      181 aalaagalsi vlitgtmvtg sgphsgdada gmkgrleldt evlavvhavc myayllltll
      241 vvwqlykqka pqrakhtawv lvtviiiqwg igvaqfylgv prwtvpfhia mssvvvafta
      301 alwargyarp rfqldysare tcsssglvsq rkgsn
//
LOCUS       WP_284860156             249 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284860156
VERSION     WP_284860156.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..249
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27337
     Region          55..215
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 miansdhpgc niavqpeqap qwlgklaglh egslqkylpn rsaeefnlpk pktikkaavl
       61 mlfggsqtpa gdggapddat vllthrhpgm rshsgqiafp ggridntdls pvdtalreaw
      121 eetglnrnnv tplkqfnela ipvtgnqvhp vlsywdkpse vavtspeead dvftvhvgel
      181 ltpenrfaig hgnwvspafr vrdyviwgft agllnaifhy sgwerdwnkt dvfdlresla
      241 ksrnnealr
//
LOCUS       WP_284860204             340 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284860204
VERSION     WP_284860204.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..340
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34428
     Region          28..336
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mqapalfarr tlgmlailaa ivvmicfsia lganplpwge vwngllardn seaaiivwtl
       61 riprtvvaia tgaafgvaga liqaltrnpl adpgilgvna gagfavtlgv gfcgltsisg
      121 yiwfaflgaa ittvvvyfig sgaslgasgk anpatlvlag valaavlsgi tqfltlidpd
      181 tfqairnwsl gsvaradlsd talvapflaa glvlalaiss slnsialgdd laaslgtkvv
      241 rtrvlgiiav tllaggatal tgglafvglm vphvvrwivg pdqrwiiiys alaapvlvla
      301 sdvigriiar pgeievgiit avvgapvlim lvrrrkasgl
//
LOCUS       WP_284860241             465 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284860241
VERSION     WP_284860241.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 465)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 465)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 465)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 465)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..465
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51731
     Region          3..444
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 mklvnlvven hrsfrdefhl eltrphftsn ipdsrdswae nvfpviaiyg anasgkttvi
       61 dalkylwsal sassgewlnr asiphapfll gkareqpsty sidftldady sqanptpget
      121 rfhyefdvtp qgfrhellqv yrssrattll srkqsedgvk lklaaglggk fevthrelal
      181 sragmtgrgq lgviaqkikd glliigvddd ernlrlhrit eeldkgnihl ddfsalaqvs
      241 dfgiekidvd iqelpndiak rlrtimdvfe ndapehaasa elpkrehsek eahefiqrsl
      301 qfthkpihad apqpkfgind qssgtlawla laipmvevlr hgtvlcvdel ssslhpklaa
      361 eivrvfqtpa lnphhaqlif sthdisllmp qaelnlqpgq iwftekeidg aselyslrdf
      421 pdirggtnia kqfmedryga tprvipelis kialrgaheg tgalv
//
LOCUS       WP_284860306             201 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284860306
VERSION     WP_284860306.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..201
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=21013
     Region          5..195
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mqpaprivla sqspsragil rsagvepvie pahvdedaiq aelsnaspse ivtalasaka
       61 qaiariypnd vviggdsmll ldgvlqgkph tepatiarwr aqagrnaqll tghclifgge
      121 tyteaattdi afaqaseadi aayaatgepw qcagaftlea lggwfidrid gdpssvigls
      181 lpvvrralyh fgfsvsdfwn a
//
LOCUS       WP_284860362             668 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD/NAD(P)-binding protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284860362
VERSION     WP_284860362.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 668)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11816065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..668
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72040
     Region          6..632
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
     Region          7..228
                     /region_name="NAD_binding_9"
                     /note="FAD-NAD(P)-binding; pfam13454"
                     /db_xref="CDD:433222"
ORIGIN      
        1 mtatqialig agprgisvle rlaaylrdss ssgqaqtktq pvgpqitihi vddsqigagr
       61 vwdttqtrtl cmntladavt lftepgstvg asvlsgptly ewirlvrgdd llaaftagnl
      121 hydtnaqvvq ekealfrahp prkglandyh eelvgtveqs npsralygey lrwvyqvvla
      181 hlpdsvevie hnsraidmht apgntntdvi tladgtsfsa hatvlatgwv lnadndeqqq
      241 lraasqaehl twispnnpve qpvdniaaek pvlvrglgmg ffdllalctl grggsfdvdp
      301 ttrsglryra ngkephfvvs srrgypflpk sdygslppka hmprlhnalq avqeqeridf
      361 sidlapaiir daiqafyatl srlapesilt stedistvld stpvyvlldp hglsgvlarh
      421 tteicnlqpy lhprvestqq vaeamardid ealkgsdspi kaalwvfasc rkhvgitgsq
      481 gkfmtdsatp tlsqimalgq mvgsgpplfr sqqllalvda glveflgaqp rltigsaeft
      541 ltcgsgvsar rasattlvda wlpkpdvrfp adplsqalfa sgrirpfsid gveqgspeta
      601 yatrrtirpd gsqdsrlhii gipthaqmpd ttispmpgtd pimlqetdkt arsvhaiiqg
      661 lrdeapqp
//
LOCUS       WP_284860448             417 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284860448
VERSION     WP_284860448.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..417
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=44771
     Region          9..403
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mnltelatqr lekwqqqglm rtpiefsgpq tpraqlndqp serillsssn ylglathpev
       61 idaarsalek fgtgsggsrl ttgsttwhrr ierelanfvg fedavlfatg yqanlsvlqt
      121 lahpdlhifs dslnhaslid girlattsgt kktiyphcdy taleqqlaec taryklvvsd
      181 gvfsmdgdig dlarlreict hhdtwllvdd ahgigtvgkh gigttevhnt rpdilivtas
      241 kalgaeggfv acstpvanll rnqargyvys tacsaancaa isaaleviqq pltqqhpvvr
      301 lqqraaalre itgirvfdgv dsdsvnsdsa nsdsayspiv plpvgaessa vrlaseladr
      361 gfhipairyp tvargqailr atamatlela dikqfaqtlr dlgwrpptpa katspgr
//
LOCUS       WP_284860492             769 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284860492
VERSION     WP_284860492.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 769)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 769)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 769)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..769
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=85192
     Region          23..765
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 msprrttgqq stgsqrtkrv hhsnysaela aeqsyvdalf gildsdvsqa rqrladaqlt
       61 idpanadsda llrreteyhr lqekldqlnl aqiglvfgri dvdakgenpt segldrryig
      121 riglmdrddd yrsllidwra pmarpfylat tahpegvrvr rhirtadrvv kdiddellsg
      181 tapadadrad vageaallha mnsargehme sivetiqreq daiirdstrg vlvveggpgt
      241 gktavalhrv ayllytwreq lsrtgvliig pnptflnyis qvlpelgetg vvlstigrly
      301 pglrptlhdt adtrrvkgsl qmvdvlkaav kayqhvpkhs revvlegtrv eltptmvkta
      361 rtkarrsrkp hneareifsd qlqellaqgl aeiighdpld ggnllnsadi salhedisde
      421 aivdelvdef wpqlgprqvl rellsdhetl haacrgngge efasalwrse qgwsdsdaal
      481 ldelaqllgs gddeqqaaad eqewrealee aegaldilat sestdnddvf dseilsahhv
      541 idaetlarrq qardyrttae raegdrtwaf ghvvvdeaqe lsamewrmvf rrspnrwmtv
      601 vgdpaqtssp agcdswseal epfvgkryrq hqltinyrtp veiaelaesi vhkyspdtav
      661 aqairnrkga vrwlpsgtsa eevrdqlrad etaasaeddt adqnqrsyai isahnaatyk
      721 glefdhvivv epeqiiaass rgwqdlyvac tratqtlnii gtldlagwd
//
LOCUS       WP_284860572             431 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284860572
VERSION     WP_284860572.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..431
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47170
     Region          165..271
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 madrkhgakr srkrgteqst krdaeqnteq stesftesvs ssltrlknsl rrhlsqqwte
       61 ltspsfsvpt sklpeplahh atevsastip esvvaeiaes lnlrgkhahh haatdqesgn
      121 apepedgsqt aeksdynfds srhlplgarf kprgvfeddw sarpsankpw pvilihgtvd
      181 tkgvwqelgt elradgwcvf apdygkrgta ameesavqlg ayieavrtit gaeqviligh
      241 sqggllaryw mrtsgqaryv khlvslgapn hgttmggils plvtnnlten imhslihrwf
      301 gpvgfqqitg seifavfndd garntdddga ssthgsgele dgvdytcias rqdtvvqppe
      361 tcflngpahq vrnvwvqdii pranvqhqdl pmnkhvraii rtglkkgase anpkhktqnt
      421 epktrslehg v
//
LOCUS       WP_284860594             338 aa            linear   BCT 25-DEC-2024
DEFINITION  S1 family peptidase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284860594
VERSION     WP_284860594.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Perona,J.J. and Craik,C.S.
  TITLE     Evolutionary divergence of substrate specificity within the
            chymotrypsin-like serine protease fold
  JOURNAL   J Biol Chem 272 (48), 29987-29990 (1997)
   PUBMED   9374470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475742
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..338
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36026
     Region          1..224
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mntkkialsl taaatmaasi itapvahavq ggtpvsddda naknvvivsg ctgtaisphw
       61 vlaarhcfgd gttaklvrtg iektgtkgse evyhapsgdi slvrmsthss fdfdsypela
      121 teepkpgqvg tfygwdntsh krlphsqaev qgiyqdgsyd ngkmytvhhk dgaysqpgds
      181 ggpffingkl sgvasaisgd gvplnladis aqldwikqtm akngdepnlg ngavngmdki
      241 lqekglqkpg aekikktgsk lrsrqqiqss pshsnhnrsq rarnqslrkq nlesssqrnl
      301 hgltraarcc rrpackflsg nfllghmetf pnevtcpa
//
LOCUS       WP_284860847             271 aa            linear   BCT 25-DEC-2024
DEFINITION  amidohydrolase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284860847
VERSION     WP_284860847.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..271
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30288
     Region          5..268
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mtnlkifdsh ihvwdlaaqq ldwlqvvdsm lhrsfsfsdl kqaynnlhdk gledvelvga
       61 lhveadvadp vdedaritsl mqqeplltgf vthanlrkdm hvtpdavgvr evlhndnvpr
      121 grclessfta gcrnlssqak vfdlcmrtpe ladfhaayen canvrvvidh cgnaqkldde
      181 fvsnmralae hpnvycklsg lnyestaday llleflgeif gpqrlmfasn wpvigiytel
      241 hthitairkv fgddpdvfsg tarsvynlkg k
//
LOCUS       WP_284860854             462 aa            linear   BCT 25-DEC-2024
DEFINITION  acid phosphatase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284860854
VERSION     WP_284860854.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130290
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..462
                     /product="acid phosphatase"
                     /EC_number="3.1.3.2"
                     /GO_function="GO:0003993 - acid phosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=50450
     Region          <139..341
                     /region_name="PAP2_acid_phosphatase"
                     /note="PAP2, bacterial acid phosphatase or class A
                     non-specific acid phosphatases. These enzymes catalyze
                     phosphomonoester hydrolysis, with optimal activity in low
                     pH conditions. They are secreted into the periplasmic
                     space, and their physiological role remains...; cd03397"
                     /db_xref="CDD:239491"
     Site            order(228,235,264..266,299,305,309)
                     /site_type="active"
                     /db_xref="CDD:239491"
ORIGIN      
        1 mktflisrrr atslltaaaa lavvagtpgl vqqhggtaha taaeaslqsp lhastthlal
       61 pfeipqlqlp apklssehde gaehsplssi gatpkhhdga pvpkpfdaty ltgyssdiss
      121 yqygiyyevv refkdlrsnh pdvmrknldi vadynnnaqp ervdkairda ladkdgvlft
      181 aaealgdefg qhflqalhek rlpktefllg ngyaaraggi aswgraekll fnndrpfvqa
      241 peritrhesp erelydgssk sfpsghtnqa twittllamm lpevgtqlla rgseagesrl
      301 vmgvhfpldv iggrmtgqaa aadrwndpkm rdallqaree ivaemewrag kpfaemiaed
      361 shalsdqqae adytrrmtyg ftpifatdep vnvptaapal letrfpelsy eqraevlrht
      421 alpsgypldd rdpakgdwqr inlarawnaq vsigaggevv vk
//
LOCUS       WP_284860888             257 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284860888
VERSION     WP_284860888.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..257
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27712
     Region          22..243
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mpdrsvdsdq dsgeatgltg ketrttdgdt rrqvmhlllk qgpitagmlg dhlglsaagv
       61 rrhldilved gltetvhrrl rgqtrgrpak hfrltdrgra yfghsydlla sdalealrea
      121 ggadavrafa rqrvrkildk itpatspdda eeqvdehave htakqlaetl sahgyistvr
      181 psesgiqmcq hhcpiahvaa ehpelceaeh evitsllsqh vqplatiaeg hgicttnipl
      241 tqsqtimkga ghdsgtt
//
LOCUS       WP_284860912             555 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284860912
VERSION     WP_284860912.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..555
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=60478
     Region          145..540
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
     Region          <401..>461
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
ORIGIN      
        1 msepepqkap epstgwgpqg erkrrsyray rthrplrlrt wlvvltvlvs afglfassfa
       61 vysvmrevfy qrvdddltqs magwaqnsel fsgnlsaspp tdyavihifp dgssrvyndr
      121 dtlpqinnlv igggprsvas vdgpqqpewr alanqqngvv tivaknlere ngllrglaml
      181 qalislvmlg flallafavi rqtlkplqiv ertasdiaeg dldlrvpkwp lntevgqlaa
      241 alnimlerlq dsvetaqske eqmrrfvgda shelrtplts lrgyvelyrs gatndvdhvf
      301 atiddesgrm kllvedllal traegsrldk rtvdvlelsl avvgtaraan pertirvenk
      361 ttdipvvsgd pdrlhqvlln litnglnhgg peasvtltlr kesqdgcmrl aaeqqetgdn
      421 hedgektsgw sqddgkngkv grdgkagkdg nkgtdgesak dyvciditdd grgmskevtg
      481 liferfyred psrargaggg sglglaivks lvdqhdgeit vdsepgvgst ftvripalde
      541 psaseetfdd ygegy
//
LOCUS       WP_284860933             246 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284860933
VERSION     WP_284860933.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..246
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25930
     Region          11..243
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(29..30,32..33,36..37,74,78..79,82..83,107,111,118,
                     121..122,127,142,146..147,149..151,153..154,157..158,
                     161..162,181..182,184..186,188..190,192..193,195..196,200,
                     203..204,210,212)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(145,149,152..153,155..156,195,198..199,201..206,
                     209..211,215,217)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mkqstastaq vpvgkpvhfl hpltviiigv sawvaalsis wpllhaalia lgwlagiags
       61 rslavpatsi alsipaglsm llvhaphgeh qiaplltsdg lvtagelalr fcalmtslla
      121 amtnvhipdl lkalqhlglh hsvvyvlgas lqllpqasal isevatanrl arrkvtlttv
      181 iprmiipvit rlltrgadrg ialqgmgyda pgrrtvlypv rahrweillr ltfpaaaigl
      241 vvlawi
//
LOCUS       WP_284860972             391 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284860972
VERSION     WP_284860972.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..391
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42721
     Region          29..148
                     /region_name="Creatinase_N"
                     /note="Creatinase/Prolidase N-terminal domain; cl46291"
                     /db_xref="CDD:480631"
     Region          31..390
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 msshnnstaa dsaahstyip vtadhfrarl akaekivaeq nlagflvspg pefqyltgst
       61 fssheratfl vlragkepva vcpetdvltl qqenldelgf rfeawrdgqs pyeitrklle
      121 ensehkavav anamtadhvl rldaalpnhs ielgsdamsq lllakgeeei sqlaaaaaai
      181 drvheqvpal lrdgvterev adklhdlilq ehhsidfiiv gcgenganph hsfsdrvlrt
      241 gepvvvdlgg afgdgyrsds trtyvvdgav dkapqefrda yevvtrafha areaakpgat
      301 aesidraare iiteagygen fshrlghgig lsthedpfyl egnkqqvqeg ftfsiepgiy
      361 vegkwgmrle divvleadgp rhlnqqprel r
//
LOCUS       WP_284861128             460 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284861128
VERSION     WP_284861128.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..460
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48785
     Region          4..460
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mtenmkvdvl vigfgkagkt iamkraasgd rvalveqsst myggtcinig cvptkalltd
       61 aerhhakptt ddstafseai qrrgtltskm nqvnldlaeg kgvivvdgha sfisektvev
      121 tggeermeit getviintga epvvlplpga dlervidstq aqrlderpds llivgggpig
      181 mefatyfakf gtkvtvvdtv dkpfanfdrd iaehvgtimd nlgitwitga qvtefresga
      241 davttvwkdg dgneqtadta qvlvavgrkp atkdlgldka gieltergav avdkhlrtnv
      301 egiyaagdvn ggpqftyvsf ddhrvilsdr wgdgsrttdn rvvptttfid pplatvglge
      361 daareevear gntldvkaad ikdipimprp kilgkpegra kilveretdr ivgatllcvd
      421 aqelintlal amsaeipast vgggiythps ssevfnallg
//
LOCUS       WP_284861217             381 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284861217
VERSION     WP_284861217.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 381)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..381
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39887
     Region          70..376
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mmmnetqriv trgisapksl akppavdkie vankavlelg rqhrkltwqr igivsglcav
       61 aiaafvtsnf vgaidispge vitgivnpss ldeqthtvlw rlrlpmavma lligvslsla
      121 gaemqtilnn plaepftlgi saaaafggas aivlhwqiva qpqlnlavva wlssvvatgi
      181 ivvaavlrgv raetmvllgi glvfffqaml aliqyrssae alqqivfwsm gsltraswtg
      241 navlagvlvi alpvlwalsw qltalrlgda raaamgvnts alrvivlvvv slvaattvaf
      301 agiigfiglv gphiarmlvg edqryfvpas maagaavmct ahalslivkp glaipigivt
      361 sllgvpffia ivmakrralw s
//
LOCUS       WP_284861221             636 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284861221
VERSION     WP_284861221.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 636)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 636)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..636
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=68103
     Region          14..623
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mhkrlrliaa lllvfsvvla grlawvqvvw gpdlsaraed qrariyvdpa rrggvvdreg
       61 kqiaytmqar sltvspttlr kelreqaqle sderlddeqk deyvdatllk msreipkmie
      121 easedkqdlk skdlldklra dtqyevlvrn vdpdiaaeis erfhgvaadh qdirqypnga
      181 igenvvgrvs mdgtgqfgle asrdstlsgi ngrstedvst ngqvipgtlr detpavdgkd
      241 iqltldldlq tfvqqqleqa knnsraesae avvldattge vlamantdti dpngdiakql
      301 edgkhfdnrs isfpyepgsv akiitaaaai eegittadev htvpgsiqia dvtvndawph
      361 gplpyttagi fgkssnvgtl qlaeklgqdk fdeylnkfgi gattgielpn essglrpars
      421 qwsgstfanl pigqgmswtt lqmasvfqtl anggervepr iikssaedda kknagegnga
      481 ndnkvkdsnd adgagasdde pgktrvvske taktvvdmfr atvqadpvgv nngtapdani
      541 egynisgktg taqkvdpntg aysnsaywit fagiapvddp rfvvaimlde pergvldggg
      601 gggsagplfh qiaswlldrd nvppsppape ltlqap
//
LOCUS       WP_284861224             338 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284861224
VERSION     WP_284861224.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..338
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34248
     Region          23..335
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 miwsillvll livvfasgii idptpislsd vrialahnif gaeapasass tnaviwdiri
       61 prlilgaavg aglavagail qavvrnalad pyilginsga stgaalailf gvsagfgeya
      121 lqgaafigal aasavmffia rsagrltsvr llmagiavgy alsaltsfli fasdsaegsr
      181 svmfwllgpl glgavgglll lgsaplvlav tivfwsmgrr idaltvgdda alalgvnpdr
      241 mrvilvvltc ilvgsvvama gligfvglvi phaarrlvgg shrqmipvaa llgaslliaa
      301 digartllap qeipigilts lvgapflill vrrmgvlk
//
LOCUS       WP_284861275              97 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein
            [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284861275
VERSION     WP_284861275.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..97
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=11028
     Region          3..>66
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mtyvnisals fpegaaeeie qrfaqrakgv dkaegfegfe llrpvsgedr yfvitrwdsq
       61 enyqkwsdar pegnhvedek rgmavdvlgf esiqler
//
LOCUS       WP_284861345             352 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284861345
VERSION     WP_284861345.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 352)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..352
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38512
     Region          2..310
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mparttwssq lrqagwlvap alivlaivig ypvvraifls fqgnrrldpe tglfteggfa
       61 glenylywvn srcmgsdgta itcppgslat dfwpavgitl fftvvtvsle iilgmamali
      121 mngkyrgrgl vraavlipwa iptavtaklw qfmfadhgiv nslldanihw ttdpwaarfa
      181 viiadvwkts pfmallilag lqmipdevyd aakvdgasrm qrfvritlpl vkpalmvail
      241 frtldalrmy dlpvimisgs snsptavisq lvvedmrqgn fnsasalstl ifllifavaf
      301 fmirffganv sgnprgrtsp drgrraraka arrqakqeqa kpertatpqe vs
//
LOCUS       WP_284861377             267 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284861377
VERSION     WP_284861377.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..267
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28911
     Region          18..255
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(28..29,31..32,35..36,74,78..79,82..83,113,117,124,
                     127..128,133,149,153..154,156..158,160..161,164..165,
                     168..169,189..190,192..194,196..198,200..201,203..204,208,
                     211..212,218,220)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(152,156,159..160,162..163,203,206..207,209..214,
                     217..219,227,229)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(173..180,191,194..195,198)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 maseqipsgt lipsgapkin pltrilimll vttplllsld wlsatvslvi tivaalvggv
       61 gwkklvatlw pllfvaplsg ismllygaeg gevyfefwlm tisdnsiela iaimirilav
      121 aspvillarn idptrlgdal aqivrvpdrf vigsvagvrm tglfkddwva mnrarrargl
      181 gdrgriahff tmafgllvla lrrggklata meargfgrrp lygehrswar psrwrtadwl
      241 alglalvcaa ipvvvavmvg swrwfgv
//
LOCUS       WP_284861395             215 aa            linear   BCT 25-DEC-2024
DEFINITION  ComF family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284861395
VERSION     WP_284861395.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..215
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=22825
     Region          6..215
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mskfrrragr agfielvlpr acagcgvpgq llcrqcrtll aqpprriapk advlapvyac
       61 ggyggphrev ilemkernnr airpyiaavl raavetlqar gefshrltlv paptrthsar
      121 lrggdpitql ctasgfptrq avrlassmpd qsglnrddrl hnvrgnvqlv rsvprgaevv
      181 ivddvittga tlaatvdtlt yagadvagcv vlaaa
//
LOCUS       WP_284861517             462 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF445 domain-containing protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284861517
VERSION     WP_284861517.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..462
                     /product="DUF445 domain-containing protein"
                     /calculated_mol_wt=50738
     Region          53..461
                     /region_name="YjiN"
                     /note="Uncharacterized membrane-anchored protein YjiN,
                     DUF445 family [Function unknown]; COG2733"
                     /db_xref="CDD:442039"
ORIGIN      
        1 mnppkhsiaa krtaakstta estagknaya nsssvshaaa nnaaptdqqr alelrkhkif
       61 vtsllvlaaa iflgcswwqs qpgdtpgwgg yvraaaeagm vggladwfav talfrhpmgl
      121 piphtalirk kkdqlgdsls qfvgdnflna elitskvraa klpewlgawl serenaekvs
      181 revgklttni vraidaqeae eliqrhlidk aaepiwgppl grtldalide gklepvvdev
      241 vtwakskidd seesivtlin drmptwaprf arqlvgekvf remasfirev eadpqhpark
      301 sirkglrqls ydlqfdatmi srveewkaei rgsravkalp emlwdkaatg llsaaedpes
      361 tlrqkivelc vrwgenirad aelrgsldrr insaveflan nyssevtgli setiarwdad
      421 easekielmv gkdlqfirln gtvvgalagl viytvnqllf ga
//
LOCUS       WP_284861543             661 aa            linear   BCT 25-DEC-2024
DEFINITION  M13 family metallopeptidase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284861543
VERSION     WP_284861543.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 661)
  AUTHORS   Bland,N.D., Pinney,J.W., Thomas,J.E., Turner,A.J. and Isaac,R.E.
  TITLE     Bioinformatic analysis of the neprilysin (M13) family of peptidases
            reveals complex evolutionary and functional relationships
  JOURNAL   BMC Evol Biol 8, 16 (2008)
   PUBMED   18215274
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 661)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..661
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..661
                     /product="M13 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73556
     Region          2..661
                     /region_name="PepO"
                     /note="Predicted metalloendopeptidase [Posttranslational
                     modification, protein turnover, chaperones]; COG3590"
                     /db_xref="CDD:442809"
ORIGIN      
        1 mndlysyvng pwlenhvipd dravdgtfhk lrdqaeedvr eivnedngra gnlfasfmdt
       61 egvnaaglep laddfaklsv adigefvenl galervgvgs pltfwvekds gsedsvaylv
      121 qsglglpdea yyrsethaet laayrehvak mlgfvdpakl fgldadvaae rivaleteia
      181 sghwdvvasr dalktynpad fdelpeliqr llrggnlpah rlvnmmpsyv ehlvglltdd
      241 rladwqlwat whillsragi lpeevteanf nfygrqltgs teqrdrwkra vgivesvvgq
      301 eigklfvdkh fpasskedml elvdyliray rqriselewm tqatrerale kleqfkakig
      361 ypdtwrdysg lefspkgadl vanvragaaf shdyelgkvg kparrdewva npqtvnafyn
      421 pvvnditfpa ailrapfynp eadaaenfga igsvigheig hgfddqgsny dgqgnlnqww
      481 sdedraafde lteklvqqfd glvpsvlqaa gsgtdgsadn aentdsvekp gvngeftlge
      541 nigdlgglgi avvayrlylq drgmsyddta veafavegaq pelyerkfng lqrlflawgr
      601 vwrtairpem akqylaidph spaefrcnqi aanidefyea feeidtdspm ylppeqrvsi
      661 w
//
LOCUS       WP_284861605             936 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284861605
VERSION     WP_284861605.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 936)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 936)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..936
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..936
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103413
     Region          2..934
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtsthfetfr sqltyeldpf qvqgcraven grgvlvcapt gagktivgef avslalsrgt
       61 kcfyttpika lsnqkfhdlv aihgedavgl ltgdvsfqpd adivvmttev lrnmiyaksp
      121 aldrlthvvm deihfladqa rgavweevil nleehisiig lsatvsnsee fgrwlstvrg
      181 dtevivsehr pvpleqwmli gqkvyplfap gtpaiegptt sepagvnpel qrrvarleag
      241 daadgrddfr pgqgfrsrst agtgnsrsgn vrpqdryrpl grpevlrilq gqnmlpaiif
      301 ifsragcdga lhqclrskmv ltdedeqrii aevidagveg iphedlevlr fsqwrkalir
      361 gfaahhagml pafrhivekl fvrglvravf atetlalgin mparsvvlek lvkfngeahv
      421 dltpgqytql tgragrrgid tlgnaivqwa pamdpqrvag lastrtypli stfepgynma
      481 inllnnlgmd dslrlleksf aqyqadgsvv eetreierav hrveklraql neaiaafapp
      541 stndqdpaql lseyvelrkr lsieekslks rakdergdet railaklqpg dvialpskkr
      601 pvlavvntpa nqtadprpwi ttekgwsari dvsgfdnppa lvgkmklpgk alknprrhnh
      661 ivvdkfared yprpkkmklr arirdterik dlrtqmkkhp ahawpamere qltqlaqkyl
      721 rrkgeldklr atvdkatetl gdmlrrivdl lteldyvdiv dgepvvsieg eklaqvhnas
      781 dlliaqclkr giwqeldpae lagvvslctf enrratggql fdgvtdamts amentmrlwe
      841 elisdesrhg lphtrepepg fsiaihqwca gaplgyclaa aaesgaeltp gdfvrwcrqv
      901 idllqqvakt gysseikrta gqaiasinrg vvaigs
//
LOCUS       WP_284861680             249 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284861680
VERSION     WP_284861680.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..249
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27381
     Region          55..217
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 miansdhpgc niavqpeqap qwlgklaglh edslqkylpn rsaeefnlpk pktikkaavl
       61 mlfggsqtpa gdggapddat vllthrhpgm rshsgqiafp ggridntdls pvdtalreaw
      121 eetglnrnnv tplkqfnela ipvtgnqvhp vlsywdkpse vavtspeead dvftvhvgel
      181 ltpenrfaig hgnwvspafr vrdyviwgft agllnavfhy sgwerdwnkt dvfdlresla
      241 ksrnnealr
//
LOCUS       WP_284861857             333 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284861857
VERSION     WP_284861857.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..333
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37326
     Region          16..326
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mntdspeklv alvqslnlvp yfkahpersi feaakdlgls pdelvraler lhcsgistqt
       61 qdlidlsyel tkgvvihddq gmdsswrltp teagallltv evletmpglv drsavasaae
      121 klrsimddrs raiydgiaeh ssatedvqyr iaqalhtkkr vqfdywsass nststrtvdp
      181 arifirgdva yltafveqyg ehrnfrvdrm rnveilpeta rprtrklqfs sedpfgfrds
      241 ttatlavspd alwmldeydm krqdetppcp aaddqktwvk atmpigstsw ftrfalshad
      301 rvrvlgpqdl vdavheraqv giqrysmvdt nks
//
LOCUS       WP_284861893            1175 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284861893
VERSION     WP_284861893.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1175
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..1175
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=124899
     Region          244..390
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <646..1119
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 msvkstsprn prgggernka ranstrpapr tgpgraagkk lsfgmpgktg gdqaksreek
       61 sdsanletvv fgsaqraant shertgsafr avgsgiataf sktsdalkrf gnigqadddy
      121 dayadyddli ddadtdadaa emdrqatdkn kklknspagl dedlystdmt skkakakkrq
      181 rssgamgqsr grkrstdthv sdddldqhgd daqaeqtegd evavsesalp aakpevgvps
      241 srsdaialtl igvaivlgas vwldiagfig raiatathav lgagafiipv alviaasalf
      301 sgrrvavehr arvsmgtali vismlglihl fsgaptewpe rfvaggalga wtggalaagf
      361 spyvavpllf lviiygalkv tgitvkefte ylrnvisgng sknldadpdr esvgghneyg
      421 daygrandei aaiasgaqrt prrraplrtn pvasqsnrpg fttsqssnag thdvvangkk
      481 stglfprteq psqvehaevl ysngsrehqe qvsktaagle saptasdtde fpavldsptr
      541 srsartepev ekteklplap edavdqaqag lqqkqaaekp rtvdtkhpdt arqtrvpgvk
      601 pqsdarqpva qqatqvglas qindgpreda gatqqaskla teytipsagl lepgrapktr
      661 teindrtiea idacfaefkv daqvtgftrg ptvtryivel gpgvkvskit nlqsnlayav
      721 atgsvrilap ipgksavgie vpnsdreivr lrdvlesevi agdedptlvg lgkdiegefi
      781 sssiqkmphl lvagstgsgk safvnamlvs lltratpddv rlilvdpkmv eltpyegiph
      841 litpiitqpk kaaaalqwlv eemeqryqdm rsarvrhikd fnhkvrtgev qapagserkm
      901 epypfivcvv deladlmmta pkeieesivr itqkaraagi hlvlatqrps vdvvtglikt
      961 nvpsrlafat ssstdsrvil dqtgaeslig mgdglfipqg grpvrmqgaf vsddevyavv
     1021 eaakeqgepd ytegvtedkq aeakkaiddd igkdmddlle avelvvtsgl gstsmlqrkl
     1081 rigfakagrl mdlmetrgiv gpsegskare vltkpeeldt tiwmikgadp adaprevqeq
     1141 qnqgqpdnvv edsagdtdgs ahitkatynp tsqaf
//
LOCUS       WP_284861970             232 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284861970
VERSION     WP_284861970.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..232
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=25315
     Region          1..223
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mlfdslprps eriapgvahl pgwlgvdkqa elvrevreia rtyadtpmam lrptlksggq
       61 msvyqlhlgr ywhypsyryv dkiagttvpp vpeslvalap valctaagva eelapwvetf
      121 vpemvlvnyy ppgsgmgmhv defeesrapv islsigdeal frmghtesrt qpwddvtlcs
      181 gdlvvfggpk rfayhgvvrv ndatlpdgcg leqgriniti rqvsaapklq gr
//
LOCUS       WP_284862015             609 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284862015
VERSION     WP_284862015.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..609
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65521
     Region          11..609
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mreafspaky tiepgqtllt ltidavkaqp kaeifsrpkn htwvsvsrqe fldevyavak
       61 glidagveqg drvalmantr yewmlinyai waaggvvvpv ypssslsqvq wiiensgavl
      121 gigetqehte ilrmlqladd geprvkdsts qmrsffeind gavdvlqaag ktidddvvdk
      181 riaatatddv aslvytsgtt grpkgcmlth rnwnaqilgl lsnpiggiar pgkhvltflp
      241 lahvlafsvs aaamisgatq nfwpdfatla tefqrskpnl ilgvprvfek vrngarakah
      301 dsgaiqgalf draeataiay sraldtekgp slalrsahka ldklvlskir agmggevdyc
      361 isggsamspe lmhffrgigv pvyegyglte taaaatvdfe eqkigtvgpp lggtrvriap
      421 dgelqlagdl vfagywrnae atdeafdgqw yctgdlgeil psghvkivgr kkdlivtagg
      481 knvapggmed glrshplisq alvvgdgkpf vavlvtldee algrwksqhn idasrsvadv
      541 ahdaslraei qdainavnat vshaeaikkf yildddftee sgeltptmkv krnvvvqrys
      601 evldklysr
//
LOCUS       WP_284862038             461 aa            linear   BCT 25-DEC-2024
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284862038
VERSION     WP_284862038.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..461
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47750
     Region          <28..>122
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          142..378
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mneskpgrra ivrygstcca nllvvgmatg aatlgigafg satphaaatp llhaqqeept
       61 plegpapaps eadeaaapep lsreeapdts scpnrvhppq arttseavap gqpsptplpp
      121 lekqncgvst apgfhvdeav lasawlvadi dsgeiiaqkd phgryrpasi ikallalvai
      181 aeldlektvt vsqesadqvg srvgigagge ytieqllhgl llasgndaah alaqelggde
      241 atlrkinkla gelgttdtya asysgldvag nsasaydlgl iyraayqnpt fdrivntefi
      301 afpgfdaheg fevwndnhlf mndpdgmggk tgytddanht fvgalnrdgr rlmaiildtt
      361 vdkaraweqa qkllhsgfsv apgtnigmlq pvadadtept ltqgaspapq nsddaspdsa
      421 dadnagmdag phemtivivv laviaagagi aaiagfflrr r
//
LOCUS       WP_284862109             313 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284862109
VERSION     WP_284862109.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..313
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33957
     Region          137..295
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 msssrnafqr kpallwtlva lvvalavliv vavvrsgdde smsaggqdam hgpqapssaq
       61 sgnsdsqstp mpggeyspeq arelakqvep gtdfsrpnsp dptiigpgae itsnddilnv
      121 hrrnaedpfa mgaldapvvl sefsdfecpf ctrfavetap klkekfvdtg llriewndlp
      181 vngphaetga qagraagnqg kfyefhdvly nntydnqtgg hpgydvadyv rfakeagied
      241 lekfrteien eeyrdvvrqa lhyassigmr gtpafilgdr fisgaqpyev fedevyrqls
      301 kvadgtvphp tsk
//
LOCUS       WP_284862166             769 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284862166
VERSION     WP_284862166.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 769)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 769)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 769)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..769
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=85197
     Region          23..765
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 msprrttgqq stgsqrtkrv hhsnysaela aeqsyvdalf gildsdvsqa rqrladaqlt
       61 idpanadsda llrreteyhr lqekldqlnl aqiglvfgri dvdakgenpt segldrryig
      121 riglmdrddd yrsllidwra pmarpfylat tahpegvrvr rhirtadrvv kdiddellsg
      181 tapadadrad vageaallha mnsargehme sivetiqreq daiirdstrg vlvveggpgt
      241 gktavalhrv ayllytwreq lsrtgvliig pnptflnyis qvlpelgetg mvlstigrly
      301 pglrptlhdt adtrrvkgsl qmvdvlkaav kayqhvpkhs revvlegtrv eltptmvkta
      361 rtkarrsrkp hneareifsd qlqellaqgl aeiighdplv ggnllnsadi salhedisde
      421 aivdelvdef wpqlgprqvl rellsdrekl haacrgngge efasalwrse qgwsdsdaal
      481 ldelaqllgs gddeqqaaad eqewrealee aegaldilat sestdnddvf dseilsahhv
      541 idaetlarrq qardyrttae raegdrtwaf ghvvvdeaqe lsamewrmvf rrspnrwmtv
      601 vgdpaqtgsp agcdswseal epfvgkryrq hqltinyrtp veiaelaesi vhkyspdtav
      661 aqairnrkga vrwlpsgtsp eevrdqsrad etaasaeddt adqnqrsyai isahnaatyk
      721 glefdhvivv epeeiiaass rgwqdlyvac tratqtlsii gtldlagwn
//
LOCUS       WP_284862209             208 aa            linear   BCT 25-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284862209
VERSION     WP_284862209.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Niehaus,T.D., Elbadawi-Sidhu,M., de Crecy-Lagard,V., Fiehn,O. and
            Hanson,A.D.
  TITLE     Discovery of a widespread prokaryotic 5-oxoprolinase that was
            hiding in plain sight
  JOURNAL   J Biol Chem 292 (39), 16360-16367 (2017)
   PUBMED   28830929
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Fan,C., Li,Z., Yin,H. and Xiang,S.
  TITLE     Structure and function of allophanate hydrolase
  JOURNAL   J Biol Chem 288 (29), 21422-21432 (2013)
   PUBMED   23754281
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Wang,L., Grau,R., Perego,M. and Hoch,J.A.
  TITLE     A novel histidine kinase inhibitor regulating development in
            Bacillus subtilis
  JOURNAL   Genes Dev 11 (19), 2569-2579 (1997)
   PUBMED   9334321
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005226
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..208
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=22373
     Region          4..205
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 mlipygdrgl lidfsdhkdp lgqvlayqsq lqraglesii dlvpaaqtll itfdrnpsqi
       61 tlpeldaqaa ahssgnahii evsyngddld elanelgvst eelvtahtet twtaafagfa
      121 pgflylrpdl tnphakvfan isrrsqprts ipagsvglag gfsavypqss pggwqligtt
      181 earmwdidrd qpallqpgdt vrfqektc
//
LOCUS       WP_284862261             317 aa            linear   BCT 25-DEC-2024
DEFINITION  DHH family phosphoesterase [Enterococcus faecalis].
ACCESSION   WP_284862261
VERSION     WP_284862261.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..317
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=34897
     Region          5..311
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mdvvkeimaa ikqyetiiih rhqrpdpdai gsqvglaell rasfpekniy qiggpvegle
       61 flaemdvitd dvyrgalviv tdtanapris darfslgdql ikidhhpnde pygnlvwvnt
      121 nasscseiiv dfwqqhlael tmtdnaarll yagivgdtgr flypstsaht lavaaqlrtf
      181 nfnaadlnre ldqmplkvak lagyiyqnle idangaarvi lpqsilnsyd ivdsetaaiv
      241 smpgkiedvl swaifveqpe gyyrvrlrsk gpiintiakk hhggghplas ganardtaei
      301 eviyqeiqat cqewaqk
//
LOCUS       WP_284862304             118 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284862304
VERSION     WP_284862304.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..118
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12643
     Region          6..73
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mgviqmsvvn ieigqrigda rkvvgvsqre laketglsqp tiqriekger aasrlelvli
       61 adgcgvlvdd llgtnsiade vrcagrtded gskeladyli yafgvsrrld qlgipefv
//
LOCUS       WP_284862358             376 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284862358
VERSION     WP_284862358.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..376
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39237
     Region          63..370
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtqnsnkttt apsaaraatt arhrrenpra pqqhhdvfaq rhrlrvgtfv alivllvgsv
       61 llstalgqyy lslpdllsil tsgpraetdi aasvvwdirl priflgflvg aalgvagclm
      121 qavfanplae psivgvtsga gvgaalvivf evsflgtftv paagfltsli vtaiiyrlah
      181 nrgkvavvnl iltgiavnav cgalisfmvy lapttsreqi ifwqmgslng sqwkhvwvvl
      241 piviigfaia srlgaqldvl algekaaght ginvavlrmv aivasavlta aavsfaglig
      301 fvglivphvl rtivgpenki llpasalaga llialadvaa rtlipfadlp igiftalvgg
      361 ptffillrrm mrkgsv
//
LOCUS       WP_284862361             348 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284862361
VERSION     WP_284862361.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..348
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35796
     Region          35..340
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mdrqrtqqvl rarnrnrvll fivlvfalvs gtiaslvigq ytipigelpr ilavgplgvs
       61 amdesviwqi rlprlvlgll vgaalgvgga lmqavfanpl aepsvigvta gagvgaslai
      121 vlgiswfgat tvpvfaflsg llttwlvyql arfggsirvi nlvlvgiavn avagalisff
      181 ifiaptssre qvvfwqmgsl sgakwahisv vavlvgagia lalllvdkld vlalgdraag
      241 hvgidvarlr vlalllatll tagavsyagl igfvglvvph iirtvagpsn vvllpasalg
      301 gaalivladt aarsiidfad lpigiftalv ggptffillr ammrrgav
//
LOCUS       WP_284862536             332 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284862536
VERSION     WP_284862536.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..332
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33719
     Region          24..325
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtrisflpat vlavavlgva iaaslffgsn nispgqvwas lsnngdtatd tlvlqqrlpr
       61 tivvvlvgaa lgvagalmqa ltrnpladpg ilginagasi avvagvafag vqginnyifl
      121 aivgallasi mvyllggags svpsparltl agvaismais slvqaiilsn anafnefryw
      181 aagsvegrgw pvlehiwvfi vlglvfafas apslnalslg eemgtalgvk vwrtrvltfs
      241 aitilagtat aavgplmfvg lavpyaargl fghdnraila gsvvigpvfl laadvlarlv
      301 impqevqtgl lsavlggpif iavvrmkkig av
//
LOCUS       WP_284862702             871 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284862702
VERSION     WP_284862702.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 871)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 871)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 871)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 871)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 871)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 871)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 871)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..871
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..871
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90427
     Region          21..871
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 makrtsmrti avrnivshkl rlaltvlsvm lgtafisgaf mftnslsstf eaavgsayed
       61 vdaavgpaeg hpiidgetvq aitddesvra vnltestnvv vanenleayq vgggtstlqm
      121 yyppenkvgd adeiidgaap hgegevivnd taaeeqdisv gekiilvtpe eryevtvsgi
      181 ytpaleqglg slsvlmeags yqnlfnpdgl asqmavaahd gttaeqlvnh lnetypqvea
      241 qtgqaladel teqisnalsf vnyflvafgl igllvgtfii antfsmivaq rikefallrs
      301 igasqrqitg svvvealvvg llgsalgvva giglvavira vfsargmsfd dgglglslta
      361 ivvpiilgvv vtiasawapa rragqvkpve amrstesaag apltartiig tviivagvla
      421 aglamlldds gttlraslvg igaflvvvgy fmagpafsmg ivpalgrvig apfgsmgrla
      481 stnarrsprr taatafaltl gmmlvtgigm lgatmknsig dmledtvtad flatgpqdgs
      541 fpvpqavpga laetdgvest vtmrmapvqi agqagynygp gytftnsidg npqdfvdmei
      601 legsadlvsq pgvlvsdela kaegwtvgqa lplttletae ssdesgepva vepghetevt
      661 itgiyssend ifenllvsqs avdevmegdt apiqmiavnt ddsvgedemr erlaesvkef
      721 lviqvktgae yadeasqlid qmlsilyall alaviiavlg iintltlgvi errqeigmlr
      781 avgayrgqir tmiiveavqi alfgaimgil aglglgwafi dvlageglgg avipwnqvli
      841 mlggaavvgv vsalwparka aktppleaia d
//
LOCUS       WP_284862791             186 aa            linear   BCT 25-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284862791
VERSION     WP_284862791.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..186
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20001
     Region          1..169
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mnigvfigsi ragrageaig ywvhehassr ndghiyeiid lqdhdlpfla aetvpamang
       61 eygdpktqqw akviaqydgf vfvtpeyngt vpgpmknafd qlgqewqgkp igfvgygysq
      121 agkgatdtwr tvvsgmlamq ladedvnidl ntaypedang efrasdaeka gldkildqvt
      181 kagans
//
LOCUS       WP_284862825             194 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284862825
VERSION     WP_284862825.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..194
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21630
     Region          16..60
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(19..20,31,34,38..39)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mektrwwryi epkisgmtlr daakkagfnq saftrwkaga kadpefvvkf araynlnvle
       61 alveaefite eeaaidsskn shlystlref eaetsmvraa sdilgetlak ikasyvrdvl
      121 getvpttgfr swekleerfk eacetkttph ltsvpdlhnd nddgvvrnlh ltperavsds
      181 speegggspd dyep
//
LOCUS       WP_284862926             324 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: DHH family phosphoesterase [Corynebacterium].
ACCESSION   WP_284862926
VERSION     WP_284862926.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..324
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33707
     Region          7..315
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 masatladva sairgartvt vvahlrpdad aigsvtasva alrrlgltar gqigqdapie
       61 ahlltipgad evtcsrellr aelylvldca sldrtgylag qleerehqvv cvdhhesnpg
      121 fgglnlivpe aestttilad lfaelgvddt epdiahglya glvtdtgsfr wggarmhelg
      181 grwlaagldp rriaaelmda vsvddltmig rvlatsrmhd vdglgvaalv adcaevqghp
      241 ksvlevvidm vtavrgatva avlkelrpgh wsvslrapra dvshlavhlg ggghrasagy
      301 tapgtaesvi aellegvrac rgel
//
LOCUS       WP_284862982             484 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Corynebacterium sp. MSK006].
ACCESSION   WP_284862982
VERSION     WP_284862982.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK006
  ORGANISM  Corynebacterium sp. MSK006
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Corynebacterium sp. MSK006"
                     /db_xref="taxon:3050187"
     Protein         1..484
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51414
     Region          1..481
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mtssavvvgs gpnglaaava ladagvrvtl lesaesvggg lrsgdflvdg vthdicsaah
       61 pmlqaspffh ryrdrlsglg lsfaspdydm vhvlddarsa tlfsdldqmh rgipdrgdae
      121 rwrsgcerla anadavagdf lrpvfgvpss prsfaefglk aalpaswtwr ryssdearal
      181 fagiaahaft plswpgssap gfliavvghr ygwpvavggs qsiadamlrl flslggefvp
      241 gtlvesyeei qdadvvmldt sveaarkilg prlpsrvera wsrfrrgpgv akvdyvidgd
      301 vpwisepars agtvhlggra eevaaaesec wkgrlpdspf tlvgqqylad psrsyvgggr
      361 rlnplwsysh vpagwggdek acfelvtsqi eryapgfrdt ivefkaspps rveeynpnni
      421 ggdisggand lvqlikrprv ssdpyftgvp gvflcsssta pgagvhfmcg anaargalkh
      481 lhla
//
LOCUS       WP_284863025             748 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: HelD family protein [Corynebacterium].
ACCESSION   WP_284863025
VERSION     WP_284863025.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 748)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 748)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 748)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..748
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..748
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=81584
     Region          10..747
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mtsrdsekdt dyaaevaaeq ayadglfarl ddeiaqarar ldevqanvdp anpkaealvq
       61 reteyhglne rldrlalaql glvfgridve dptgdgdnpv pgadgldrry igrmgldare
      121 dnyrtllldw rapaarpfyl attahpegvr trrhirmrgr evtgvdderl sgeaaaelpa
      181 eqaaslragv ggeaalyeam qaartgrmss ivetiqreqd qiirdptrgv lvveggpgtg
      241 ktavalhrva yllytwreql srsgvlivgp nrvfldyish vlpelgetgv vlstlgelyp
      301 gvspvaeepm lgreikgsee mvtvlreavr dlqvvpddpr elrvgsltlt vepamvktar
      361 trarrsrrph neargafaes lidqlaaqma qligadplgg enllgaadvd qlhddlaeep
      421 vvrdlveelw prltptgvla gllssraavd saaraydeet reallredge awtasdaall
      481 delaellgea gerdddpeek aerrrleaaq aaldvlegsa vtdndddqfd aeylgaydvl
      541 daealaarqe erdtrttaer aaadrgwayg hvvvdeaqel tpmewravfr rcparwmtlv
      601 gdiaqngspa gvdswadtle pfvgsrfrrh slsvnyrtps evmevadell sridpeerpa
      661 eairstgipv rrlpagtdpe evadglrrae persvavvrp gavgdlkgle fdhvivvdpd
      721 gveeasplgl qdlyvavtra trsltlig
//
LOCUS       WP_284863051             420 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium sp. MSK006].
ACCESSION   WP_284863051
VERSION     WP_284863051.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK006
  ORGANISM  Corynebacterium sp. MSK006
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Corynebacterium sp. MSK006"
                     /db_xref="taxon:3050187"
     Protein         1..420
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44264
     Region          91..406
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mekilnwpll ggaaevtvwt clalgallal aalatarnrr ggqgrrprra rrpatalgaa
       61 agvtvavwlv levvlrpfge ptswivyavc glvllglisl asaagrrlla aaalvalvlg
      121 algatntvfq qyptlrslhp vpaakemdwa efkattrppq edgrdigalv hvdlpsgtdf
      181 tarqalayvp paywrspqhr lpvlmlmagn pgspeqwfds gtagetadaw qaahdgvspv
      241 vvsvdatgsl tgnpgctgas reyvtdtapd liarrfrvdp drshwtiggl syggtcalqv
      301 vtnspqafgs fldfsgqaep slgdhtrtvd qlfggdevaf raenpadllr dndytgiagr
      361 fvagssdhea taalkdlsqa adkagmdvey tevpgghdfg vwraalranf dfvaerggle
//
LOCUS       WP_284863281             275 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Corynebacterium sp. MSK006].
ACCESSION   WP_284863281
VERSION     WP_284863281.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK006
  ORGANISM  Corynebacterium sp. MSK006
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Corynebacterium sp. MSK006"
                     /db_xref="taxon:3050187"
     Protein         1..275
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30816
     Region          1..269
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 marieeilal eriddlifrg pavestltrt fggqvagqal vaavntvdde rpvhslhgyf
       61 lrpgdssept vflvdrlrdg rsfsvrqvrg vqrgetifsm qasfhvagds gpdhsdemra
      121 vpdpeelgee gqlrppgsra lldewgdwdi rvvpperyep nkyaasqqvv wfrsqrrlpd
      181 dpkfhqctla ymsdmtllhs slvphpdtkv qmasldhaiw flrpfraddw llydqtspsa
      241 hggramtqgr ifnragdlva qvtqeglvrt ldear
//
LOCUS       WP_284863348             303 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Enterococcus faecalis].
ACCESSION   WP_284863348
VERSION     WP_284863348.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 303)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 303)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 303)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..303
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34139
     Region          2..297
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mkklkkfydq rqlhwmvlpg vafmivfnyi piygiiiafk nytivdtvss apwvglenfr
       61 iimedsffwe avrntlaisl mklflgfaip iilavmifem rdghlkkviq tisyiphffs
      121 wivsggmlis wlstngfinq vmmslglmnq gvnhlldpdk ywwiavlsdl wkevgwgtil
      181 ylagmsridp tfyeaaridg askltqirti tlpllapiis lnlilnvsgl lgsnldqtlv
      241 lmnaqnqnks evinsfvyrm gltqgdfsya tavglgisvi sivllvitdr itrkmnngrs
      301 vil
//
LOCUS       WP_284863576             159 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [Corynebacterium].
ACCESSION   WP_284863576
VERSION     WP_284863576.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..159
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17712
     Region          22..150
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msekraadpl pppaellssp sfqlerlrrr trdevesrla aedttlrefw vlaclvevgg
       61 dgenqsrlaa tllidpsdvv riidrleeks wagrtrdpqd rrrqlvtatk kgrkahgrla
      121 eliaegedaa ldestskqlk hlrklaraii vedtpaqqa
//
LOCUS       WP_284864037             215 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: IMPACT family protein [Corynebacterium].
ACCESSION   WP_284864037
VERSION     WP_284864037.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Park,F., Gajiwala,K., Eroshkina,G., Furlong,E., He,D.,
            Batiyenko,Y., Romero,R., Christopher,J., Badger,J., Hendle,J.,
            Lin,J., Peat,T. and Buchanan,S.
  TITLE     Crystal structure of YIGZ, a conserved hypothetical protein from
            Escherichia coli k12 with a novel fold
  JOURNAL   Proteins 55 (3), 775-777 (2004)
   PUBMED   15103642
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Okamura,K., Hagiwara-Takeuchi,Y., Li,T., Vu,T.H., Hirai,M.,
            Hattori,M., Sakaki,Y., Hoffman,A.R. and Ito,T.
  TITLE     Comparative genome analysis of the mouse imprinted gene impact and
            its nonimprinted human homolog IMPACT: toward the structural basis
            for species-specific imprinting
  JOURNAL   Genome Res 10 (12), 1878-1889 (2000)
   PUBMED   11116084
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..215
                     /product="IMPACT family protein"
                     /calculated_mol_wt=22980
     Region          1..195
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 mssyllpvag etfrgeheik rsrficlirr vrdedearaf idatraefpd arhhcsafih
       61 hvddanpver ssddgepsgt agrpmleqlk gsgmldvaav vvrhfggvkl gagglvhays
      121 navgdllpkv prvrrvrrrl ftfelphada grveadlrar gvtvtdvayg aavtltvacd
      181 ldgleglftt laavtagaae paeagtawve vpaer
//
LOCUS       WP_284864057             411 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase
            [Corynebacterium].
ACCESSION   WP_284864057
VERSION     WP_284864057.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..411
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43956
     Region          1..411
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mpeavvvgag mtglsvawfl qnhgfdvevi drvgvvggss wgnagwlapg ksktiplahp
       61 slwrygptal fdpnaalavp pridprlwaf carfmahatr sgwdetmaal tpadklalaa
      121 ydelvdggve arthtgdyva afrdekeagg figeiegavr hgqeisfeyi drdaalglap
      181 vlseaaravy riggqryiep gpfceaiaes vrarggrvtt gvavtevnst rkpvlelstg
      241 eyrtpdtvvl aagawlpela rrlgvrtmvq agrgysfsvp tetpvehpiy lpeqrvactp
      301 yqgrlriagt mefrgpdeaf qparidsvve avrpmftgvd lddrkdewvg scpvtpdglp
      361 ligatkapnv yttgghgmwg vvlgpvsgkl laeqiatgrv dpvlkpfdpl r
//
LOCUS       WP_284864113             374 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: M24 family metallopeptidase [Corynebacterium].
ACCESSION   WP_284864113
VERSION     WP_284864113.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..374
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39478
     Region          17..373
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mselfdasvy adrlgcaqgl lrerglagiv igpgpelayl tgswtssher ltaltvtptk
       61 srliapetdl hsladsavse ldvevlgwad gedahalaaa pvlegdadga vglgdslttr
      121 hvlalqelfa pretkvaala laelftrkda aeieqlraag raidavhakv pellragrte
      181 aevaadidkl ilerhgvvdf vivgsgpnga nphhdfsdrv ledgdmvvvd iggtygvgyh
      241 sdctrtyvvg gdpatlpeea rsmyavlaea qeaavaavrp gvtaasiddv arsriteagy
      301 geayfhrtgh giglstheep fimagndlvl epgmafsvep giylrgrfga riedivvvte
      361 dgcerlnegp relr
//
LOCUS       WP_284864126             235 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium sp. MSK006].
ACCESSION   WP_284864126
VERSION     WP_284864126.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK006
  ORGANISM  Corynebacterium sp. MSK006
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Corynebacterium sp. MSK006"
                     /db_xref="taxon:3050187"
     Protein         1..235
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24699
     Region          8..208
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 maassgrtpa avffdmdgtm vdseplwgia tfelseklgr rltpelrqat iggsfpntlr
       61 icaehagvtv deatadrlre emfarvadlf rerlepkpgv rdllgdlgsa gvpavvttnt
      121 vrpladiaid avgrdffada vtgdqvaryk papdmfleaa rrtgvspadc vvfedslagm
      181 sgaleagcvv iglpevpgqa pqpgaadlge lngersfvgv dahrvgvwfd rlsgv
//
LOCUS       WP_284864128             344 aa            linear   BCT 25-DEC-2024
DEFINITION  YncE family protein [Corynebacterium sp. MSK006].
ACCESSION   WP_284864128
VERSION     WP_284864128.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK006
  ORGANISM  Corynebacterium sp. MSK006
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Corynebacterium sp. MSK006"
                     /db_xref="taxon:3050187"
     Protein         1..344
                     /product="YncE family protein"
                     /calculated_mol_wt=35419
     Region          195..>338
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mrkraiglpl ltaalltlta cggtdgqdgt eenmgnarpa vsdsagdapd getfeapagl
       61 geisqavtdg evvglrgrda vafgtvaqlr dgkaevvetd pacgtltqga gtfvlacgse
      121 vllfdpadpa eperrdvegd atraalvasg elftanadep eivmtrpdrs terievedpa
      181 telvsvpgrd gerdavvrtf npdttiqdvd wtndpprqgg rlrvglgvgt vapgeddfll
      241 aadatggqla vyttddvirl hqtvpvdgep wavawdphak rawvsspgdr glrafdlssg
      301 speqttqlra vpdaqsivvl ddgtlvavsa tgsgvqvvad aaga
//
LOCUS       WP_284864143             115 aa            linear   BCT 25-DEC-2024
DEFINITION  YidH family protein [Corynebacterium sp. MSK006].
ACCESSION   WP_284864143
VERSION     WP_284864143.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK006
  ORGANISM  Corynebacterium sp. MSK006
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Corynebacterium sp. MSK006"
                     /db_xref="taxon:3050187"
     Protein         1..115
                     /product="YidH family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=12018
     Region          2..99
                     /region_name="YidH"
                     /note="Uncharacterized membrane protein YidH, DUF202
                     family [Function unknown]; COG2149"
                     /db_xref="CDD:441752"
ORIGIN      
        1 marvalphgd epdprftlan ertflawtrt slaflaggva lgafeleglp revrvalavf
       61 viavglvisl gaavrwlrve ramrehrplp vpaivpvlsa aaviacavaa gvfla
//
LOCUS       WP_284864201             458 aa            linear   BCT 25-DEC-2024
DEFINITION  Mur ligase family protein [Corynebacterium sp. MSK006].
ACCESSION   WP_284864201
VERSION     WP_284864201.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK006
  ORGANISM  Corynebacterium sp. MSK006
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13558984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Corynebacterium sp. MSK006"
                     /db_xref="taxon:3050187"
     Protein         1..458
                     /product="Mur ligase family protein"
                     /calculated_mol_wt=48564
     Region          <47..>82
                     /region_name="PRK14016"
                     /note="cyanophycin synthetase; Provisional"
                     /db_xref="CDD:237586"
     Region          68..277
                     /region_name="Mur_ligase_M"
                     /note="Mur ligase middle domain; pfam08245"
                     /db_xref="CDD:462409"
     Region          316..414
                     /region_name="MurT_C"
                     /note="MurT ligase C-terminal; pfam08353"
                     /db_xref="CDD:462442"
ORIGIN      
        1 msdenqpsrr plwrrlrtra attsarlatt asrmtgrgag gmigglvaqa idptimaqlg
       61 ggrpcalvtg tngkstttrm laaatrtvhd vatndggdnm dagiisalla ggdashivle
      121 vdelhvprva erlhpevlvl lnlsrdqldr vgeintierr lrecvnahpd mlvvancddv
      181 lmtsvafdhe ktvwvaaggg wlgdsvscpr tgghivrega dwyavkplad grvfrrpepd
      241 wtvddaglha pegerglalk lpghanrgna aqavcaavrg fdvpferavr aaeqvddvag
      301 rystvqlger svhlllaknp agwqealsmv drtadglvia vngqvadged lswlwdvkfe
      361 dfenlsvkaa gergtdlavr lmyagidhdl vpdpldaira cpagrvevla nytafrdlkk
      421 alnravaghe dedaaeagaa dengaagaaa tkdeevgk
//
LOCUS       WP_284864215             281 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sulfurtransferase [Corynebacterium].
ACCESSION   WP_284864215
VERSION     WP_284864215.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..281
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29616
     Region          33..265
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 maaiidvdql ssvrrravll fataggarpt eaipgsfvaa ldgdfsdpth plpntvpvdp
       61 arvfeaygis dktpvvvydd setplaprvw wlarvaglrn vavldgglaa wraadrplae
      121 pksaeeatpg qitaapswel ltdadgvrea lalghrhvvd vrsatrfcgt epeprenvrs
      181 ghmpgavnlp ytrfrtadgr yrdvdemrdl letvlgpaga atfvcgsgvt acvgalaatl
      241 agygdvevye gswtewghvd ndpaefpavt gdgaedldgr a
//
LOCUS       WP_284864227             465 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Corynebacterium sp. MSK006].
ACCESSION   WP_284864227
VERSION     WP_284864227.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK006
  ORGANISM  Corynebacterium sp. MSK006
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10646251
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Corynebacterium sp. MSK006"
                     /db_xref="taxon:3050187"
     Protein         1..465
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=46776
     Region          <90..>258
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     Region          288..451
                     /region_name="VWA"
                     /note="von Willebrand factor (vWF) type A domain;
                     smart00327"
                     /db_xref="CDD:214621"
ORIGIN      
        1 magrhrtdtd spkvagwliv avilvialia alvawfalrd serdarseae gdciegeltl
       61 pvaeafpgaa eelmnayrds apvvrdhciv petapvadaa vfvgvdspaa daalkvadrs
      121 rgtaspqpag tkavglaare aadpkdtaad qvvypagdqt diavtaaakl agdnaaellt
      181 rdrgeklada dgsrpvvate atapegttft pivgaelsla aipldaagae adeevtraaa
      241 dftefagkqe gaeaeterpd dalyaaagng avaggerase sadgaahdtl flvdtsaame
      301 pqadhlgaav gkpaaelasd ghavalwnys splnpgvtvp yrtnlgfgdg sqvegvvdal
      361 gtggvpmtrt svlaalgsvq sqaaqtgkpv glvvvttgta pgdmddesfr salkdalgen
      421 velavvhvgd getdkvlsen akatakadgg raldeavarl agves
//
LOCUS       WP_284864293             864 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Corynebacterium sp. MSK006].
ACCESSION   WP_284864293
VERSION     WP_284864293.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK006
  ORGANISM  Corynebacterium sp. MSK006
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 864)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 864)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 864)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 864)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 864)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 864)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 864)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..864
                     /organism="Corynebacterium sp. MSK006"
                     /db_xref="taxon:3050187"
     Protein         1..864
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89966
     Region          10..864
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 malsspamrr vslrniashk lrltltviav vlgtafisga fmftkalsnt fdnavatsfd
       61 gvdvvlspge getgiplael dtlradekig tvniqsgttv avgdaegnal qsggtsairv
      121 wypegesvsv dqpivegnap egpdqvlvnq yaaehyglsp gdrvivvdkq nraeleltgi
      181 ystdtdqasn npapalgmse asyierytdg eqvgqvvlsa agdqsaedll gyveqtypqf
      241 qadtgeklae emseqisqal qfvnyflvaf gligllvgtf liantfsmiv aqrtkefall
      301 ralgasrrqi tvsvvfealv vgllgsvvgv lagmglvali kavlaatgne ltgsglglsw
      361 qavvipivlg tvvtilsawa paqragqvqp veamrsteas tstpltarti lgvvltligi
      421 gaamwgalne dwssntrail vgvglvavii gfffagpals ipvvpsvgrv iglpfgavgr
      481 laatnsrrnp rrvattafal tlgialvtai gmlgqtmkts maefyednmr sdfvlagpts
      541 gqfplpaetv dearevdgva elgevylvpl vvdgepaqpg npygeaiegd ittalpldlk
      601 evapgadkde vahtdgeegf fatpglaaer gwtvgetyql ssgpggqtvd apllgtfdgt
      661 gpmvmpviat kttaeqfaap gtmqlyqvav sktedadadd lragledavk qllvvqvmds
      721 kdlaeemgga idamlnilyg mlalavviav lgivntltln vierrqeigm lravgtqrrq
      781 vrtmiileav aiaifgalag iaiglglgwa flrvlaeegl dtlsvpwali gwmlvgsavv
      841 gvlaalwpaa saartaplda iaed
//
LOCUS       WP_284864981             340 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium sp. MSK044].
ACCESSION   WP_284864981
VERSION     WP_284864981.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK044
  ORGANISM  Corynebacterium sp. MSK044
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 340)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 340)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Corynebacterium sp. MSK044"
                     /db_xref="taxon:3050195"
     Protein         1..340
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=35135
     Region          56..326
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mslrsritam fvattasvgl alialvygyl kltpvpfrae fpdsavidga vpvtseilra
       61 mltaslvsll vltvlagvig wfvagwvitp lssiastark vtagdmkert gysgvadelg
      121 dvskaldtml dtladsitaq krfsanashe lktpistiqt iadvalaged dsdlrealtr
      181 irevnagnak tvtalldlar aemptvdand fgaicrdcgi daesvtvtgd pvllqhavsn
      241 lvrnahthge yvagalnvcd gmatvtvess gsvltaedva tfvepftgsg hglgltltds
      301 iatshggkle laprngggli arfsvptsrp tptnqsgrpa
//
LOCUS       WP_284864995             185 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Corynebacterium sp. MSK044].
ACCESSION   WP_284864995
VERSION     WP_284864995.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK044
  ORGANISM  Corynebacterium sp. MSK044
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 185)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Corynebacterium sp. MSK044"
                     /db_xref="taxon:3050195"
     Protein         1..185
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20698
     Region          3..182
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
ORIGIN      
        1 mpmtvrhlta pqfiemvpel vdlyiaamky ppaireqria vwcrdatspg fvavaayegd
       61 slagiaygfk gtpdrwwdlq lrrglfqrqa mtpamitvir nyfevaeihv apdlqckgtg
      121 rklmhllleq ttepyallst pevpgennaa fglyrslgfl dvlrhftydg dsrpfailgr
      181 klpla
//
LOCUS       WP_284865041             202 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsB family cell division protein [Corynebacterium sp. MSK044].
ACCESSION   WP_284865041
VERSION     WP_284865041.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK044
  ORGANISM  Corynebacterium sp. MSK044
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Corynebacterium sp. MSK044"
                     /db_xref="taxon:3050195"
     Protein         1..202
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=22500
     Region          58..137
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 matsrtpgtr rprsskprik vpttvpvasr daaarrataa pkrkrvemlk gdilgvavli
       61 tvvlivliai avplrnyysg rteiarleas ienkkehkad lqeqldrynd peyakqearr
      121 rlgmmepget awriidprmd vdhlttgrmd didpdtpwtt ilwdslrevp evpvapeapq
      181 eppadapvdp pveehapepv eq
//
LOCUS       WP_284865117             261 aa            linear   BCT 25-DEC-2024
DEFINITION  inositol monophosphatase family protein [Corynebacterium sp.
            MSK044].
ACCESSION   WP_284865117
VERSION     WP_284865117.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK044
  ORGANISM  Corynebacterium sp. MSK044
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Corynebacterium sp. MSK044"
                     /db_xref="taxon:3050195"
     Protein         1..261
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=27523
     Region          8..259
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mdemreylri aeeaadearr mfvdglgsvp alykdsgdfa temdlrieem lrdqltpatg
       61 ipvlgeeegg vlrndaswvv dpidgtanya sgnpscavli slvvdkqpvv avtdipllnm
      121 rltarqgsgv hlngellppv nmaahvsnqv gvgavgsdeg srippdsrlr likaleyanm
      181 rprisgsvgi dlafvaqgvy eaavsfsphp wdnaagvlla rsagavvtdi egnewelgsl
      241 gviagspdvh eavlrtiksv a
//
LOCUS       WP_284865118             647 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Corynebacterium sp. MSK044].
ACCESSION   WP_284865118
VERSION     WP_284865118.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK044
  ORGANISM  Corynebacterium sp. MSK044
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 647)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Corynebacterium sp. MSK044"
                     /db_xref="taxon:3050195"
     Protein         1..647
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=69856
     Region          40..633
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mdpqrrqqrg epqkvitakr mqlltvvflv valvlvgrla wvqlkwgpql qtvaadqrtr
       61 tfvdparrge ivdrqgnvls ytmqarsltv spvilrrelg eqarndmvne gatraeaeaq
      121 egarvedmlr qmaneiprmi gqgdddkdes edsdnrvktq kvnskdilek lhastdyevl
      181 vrnvdpdvaa evakkfhgva adhqdireyp ngavaeniig rvsmdgqgqf gleassdsil
      241 tgingrstld vsdmgqvipg tlrdvvpavn gakieltidl dlqayvqqll eqakensrak
      301 gaeavvldaa tgevlamant dtidpngdle kqlkngrsfd npsishpfep gsvakiitat
      361 aaieegltnp devhqvpgqi emagvtvada wehgvvpytt tgifgkssnv gtlmlaqrvg
      421 eerfddylkr fglgqatgve lpnesaglvp treqwsggtf anlpigqgms mttlqlasvy
      481 qslanggeri epriiknvta stgeeipqee prrtrvasee tartvvnmfr apfqedpagf
      541 nsgtaqgnni pgyqlsgktg taqqvnpdtg aysnsdywit fagiapaddp rfvvavmldd
      601 pergplegga ggqssapvft qianwliare nippsrdpge pmvlqaq
//
LOCUS       WP_284865267             363 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Corynebacterium sp. MSK044].
ACCESSION   WP_284865267
VERSION     WP_284865267.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK044
  ORGANISM  Corynebacterium sp. MSK044
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Corynebacterium sp. MSK044"
                     /db_xref="taxon:3050195"
     Protein         1..363
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=38859
     Region          15..363
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 msfadsrflt rrrtlsaqla gkridsflvt hptnvrylsg ftgsagallv nkdlsaaiat
       61 dgryttqiad evkdieaviv rngaeallat vpegwrvgfd aarttvaele amkkacpdgv
      121 tlvpvdgaie qirlrkdrye larleeaaqi gtdaltglie agelragrte rdvaadleyr
      181 mrllgaerps fdtivasgpn salphhgage rviesgdivt idfgahyrgf nsdmtrtfii
      241 ghvsdfarei yetvleaqka gvraatagra lvevdkasrd iieqagygey fvhstghgig
      301 ldvhegpaas trakgsleen mtltiepgiy vpghggvrie dtvvitggap rvittfpkel
      361 tvl
//
LOCUS       WP_284865298             310 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Corynebacterium sp. MSK044].
ACCESSION   WP_284865298
VERSION     WP_284865298.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK044
  ORGANISM  Corynebacterium sp. MSK044
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Corynebacterium sp. MSK044"
                     /db_xref="taxon:3050195"
     Protein         1..310
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=33530
     Region          5..295
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mkqvptvktq rifafillvv qagitftgsl vrvtgsglgc newplchegs lfpvrgaapw
       61 vqqfiefgnr altfvvvaat ilvfyavkka drrkslvdla vasgigvivq aviggisvkl
      121 dlqwwavalh flpsmilvav aavlymrlae pddaepqrrf dstastlaii aaialclvli
      181 tgtmvtgsgp hsgdagvgme grleldtkml ayvhaacmyv ylaftlataf vlrkkkaped
      241 amktvwvlla mivvqwaigv iqfylgvprw tvpahiimss vvvaftaflw ahgqrrlpil
      301 spkqynttts
//
LOCUS       WP_284865341             357 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium sp. MSK044].
ACCESSION   WP_284865341
VERSION     WP_284865341.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK044
  ORGANISM  Corynebacterium sp. MSK044
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Corynebacterium sp. MSK044"
                     /db_xref="taxon:3050195"
     Protein         1..357
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36587
     Region          41..353
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mkiatqadlp phtvragfsl tgkssalavl fallavgfml slavgarsia lvdvwhalth
       61 irdlhrnmdt isqdeltvaa lrfprtllai lvgaalgvag aliqghtrnp ladpgilgvs
      121 agaalavvvs ftflgvtsvt gsavvafiga glatvtvfal aaagnghinp lnlvlggaal
      181 savmraatsa fvlidansld qmrfwnvgsv agrsldvfwg vlpfigfgvv aafasapgln
      241 lltlgedvas slgvnvqrhr vagmaiiall agsataaagp igflalvvph isrticgpdy
      301 rwilplssvi ganfllyadi agrliarpae vqvgivlafv gapffiwmmy rnkvmal
//
LOCUS       WP_284865490             520 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Corynebacterium sp. MSK044].
ACCESSION   WP_284865490
VERSION     WP_284865490.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK044
  ORGANISM  Corynebacterium sp. MSK044
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Corynebacterium sp. MSK044"
                     /db_xref="taxon:3050195"
     Protein         1..520
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=54728
     Region          5..331
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(7..8,11..12,41,44,98..99,151)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(96,99,176..182,211,235..240,271,297..301,303)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mrvaavwfpd wpiqaarlea gdelaeplai gahhrikvvs qearklgirr gmkvrhaqsv
       61 cpdltvvedn pdrdgrmfaa laasfddvaa svevlrpglv vvdiaaagtf hgseekatem
      121 lidaasspgi dpltgvadei ataviaaras avvppggsat flarvplrml vaetslgada
      181 dtvaalgqlg vgtlgelaal pstavstrfg raglhchria raapdrrvap eiptadlsvs
      241 vtpedpidrv daaafaaral aaslherlaa aglnclrlkv kadvdggevv ertwrtreal
      301 teeatadrvr wqldgwlthg gagaitslil eplevaqpdl agqlwgsesa agpaaggdqv
      361 rrvaervqsq lgidavvqpr liggrgvver valvpfgerg pegsnatwpg aipqplpari
      421 ggglnhpasr vkmidaqatp igvtaeallt sqpyalswgd nkylitgwag pwpvdggwwe
      481 dtphkvarlq vvgcsphdek pvgwllvwsq qqwrieamyt
//
LOCUS       WP_284865635             935 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Corynebacterium sp. MSK044].
ACCESSION   WP_284865635
VERSION     WP_284865635.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK044
  ORGANISM  Corynebacterium sp. MSK044
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..935
                     /organism="Corynebacterium sp. MSK044"
                     /db_xref="taxon:3050195"
     Protein         1..935
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=99598
     Region          109..258
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          376..885
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 msatstsrrn kgrsqtgpkg rakrstgsyg yrsssgaada sdervgsavg avgrgvgnaa
       61 rditgafkvv ggrgrrrree iqddydatea atyeemdedv nsrrapsada igliliglaa
      121 vlgasvwmdv agpvgalias gtswvigaga lvlpvvlvgi aialmlnlgd saserahsgv
      181 gltiiavcml glihifagsp gdwesrriag gavgafiggp lsagftpfva vpllglvivy
      241 aallatgitv resfdyirgl fssiassaht pdpededlya dadddidaia eerprarrrt
      301 pmdnypvdep tlfdgdstap apeepkkkrs trkkvgvaps ivdepdnetk ilerptpvte
      361 tttdavsasr eemrkaiiar sgidaagkag gdaekpsprv petttdykip stslliagkt
      421 pktrteandr mieaitevfe efnvdaqvtg fsrgptvtry evelgpgvkv skitnlqsnl
      481 ayavatdnvr lltpipgksa vgievpnadr emvrlrdvld aptvrgdhdp mliglgknie
      541 gdfvsasvqk mphllvagst gsgksafvns mlvslltrat peevrlilvd pkmveltpye
      601 giphlitpii tqpkkaaaal qwlveemeqr ymdmksarvr hikdynakvr ageytapigs
      661 erevrpypli icvvdeladl mmtapkeied sivritqkar aagihlvlat qrpsvdvvtg
      721 liktnvpsrl afatssltds rvildqagae kligmgdalf ipqgagkpqr lqgafvsdee
      781 iqavveavke qgephytegv teekapekkd ideeigkdmd dlleavelvv tsqlgstsml
      841 qrklrigfak agrlmdlmes rgvvgpsegs karevlvkpe eldtiiwmik gadpaeapke
      901 vleeqeldde tsdapdapdt pntvtatynp tggaf
//
LOCUS       WP_284865637             230 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Corynebacterium sp. MSK044].
ACCESSION   WP_284865637
VERSION     WP_284865637.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK044
  ORGANISM  Corynebacterium sp. MSK044
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Corynebacterium sp. MSK044"
                     /db_xref="taxon:3050195"
     Protein         1..230
                     /product="energy-coupling factor ABC transporter
                     ATP-binding protein"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25484
     Region          4..226
                     /region_name="EcfA2"
                     /note="Energy-coupling factor transporter ATP-binding
                     protein EcfA2 [Inorganic ion transport and metabolism,
                     General function prediction only]; COG1122"
                     /db_xref="CDD:440739"
ORIGIN      
        1 mptitfdgag vvyegttile pvsltlteqr igiigsngsg kstlvrling lieptrgrvl
       61 fdaspttthg khirrrvgfi fsdaeaqivm prvrediafs lrrfklpkve vnqrvdamme
      121 rfgltalaen sphtlsggek qmlalaavlv iepetiiade pttlldlrnr kriirelqel
      181 eqqvivvthd ldmlhnfdrv iclndgaiay dgtprdaisf ytdlmertss
//
LOCUS       WP_284865662             424 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent RNA methyltransferase [Corynebacterium sp.
            MSK044].
ACCESSION   WP_284865662
VERSION     WP_284865662.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK044
  ORGANISM  Corynebacterium sp. MSK044
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Corynebacterium sp. MSK044"
                     /db_xref="taxon:3050195"
     Protein         1..424
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=45347
     Region          13..422
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 msdpsgdltr gatltlrpha mahggeavay apdsrvvfig gaipgdtvsv tldrvkkrwa
       61 radvvevlep spdrvehacp aaaagagccd yshiapaaqq rfkrevligq lvhhtesslv
      121 lrgfdlaidl eeetleptlg wrtrtrlgvg qdgragvrka rsndivadva ctqvvpgald
      181 givgpgartf tpgaelvvvm dshgqrhvve takaqrgrri ewmetviegd mavtevvpve
      241 aggqvedfef vfpptafwqa hsaapatysr yitdwaaddy erpigwdlyg gvgvfvpsis
      301 kamgghphid svdysvaatq ekqqclsgfd vtvhshpvet gligfadpgl vvldpprtga
      361 gahvvediaq ynpqrvihig cdpatfardl aswgnngyvv ermalvdafp mthhfevvcs
      421 lvpa
//
LOCUS       WP_284865745             640 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Corynebacterium sp. MSK044].
ACCESSION   WP_284865745
VERSION     WP_284865745.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK044
  ORGANISM  Corynebacterium sp. MSK044
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 640)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 640)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Corynebacterium sp. MSK044"
                     /db_xref="taxon:3050195"
     Protein         1..640
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=68694
     Region          <42..223
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mktlsmparm raafalvvaa vltvawapvv fgqdeaadsk amlildasss mleedadgsr
       61 idaakqaand lvdslpatan mglmvygane sdapdnrdag ckdietlvpv gkvdkgkfts
      121 aingltpkgy tpmgnslraa akelgdegqr siilvsdgid scapppvcev akelaadgvd
      181 laihtvgfkv ddaareelqc iaeagngefh eaddagslae tlkflsqrdv gkyklkgtrf
      241 efadnpedak wlgegqyqtk vkpdtntkkd ryfrvsvpek hnalisitpv wqsngnvrha
      301 dlfldtsdit nevdsscgdv sktlgnssif gnamfgidpy eialrrdgqd dncdmstwli
      361 gmqvyqtgee itedvnlevn vfyepipeag qaekwknqki ssqskfsgdi sitnsqeitg
      421 gsgfndavei tegsysdkiv pgefrfykip vswgqrpvik lktpesetsd hdgigfgfhd
      481 plrseagsgs vsmtgqkade sdpvmpsdva wfapksppqg yyfawvgmgs kggsqitgve
      541 qpyefavald gepgdggpdw qptyedgpep sdtpiqfdsa nvpketsked saedaqvaed
      601 sssagwvvpa migagillvv llgvllflln rnkknqmprr
//
LOCUS       WP_284865724             377 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium sp. MSK044].
ACCESSION   WP_284865724
VERSION     WP_284865724.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK044
  ORGANISM  Corynebacterium sp. MSK044
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Corynebacterium sp. MSK044"
                     /db_xref="taxon:3050195"
     Protein         1..377
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40414
     Region          122..372
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtnhveveli rprdvllalv lvafclispf atgfglldaa lvvcagaapf trrrwpwvti
       61 ascvvvlaac sfteslptgv igvamitayi iarhlpapvr yvvattllag diaataliap
      121 alvtlplpvr apyiawsvtl lviafllgel rhraeeaaak elqiqlerqr dvfervaaeq
      181 rahlareihd ivthsltviv aqadgaryga scddalrtis tvgreslrqm rgvlsllrgg
      241 eqrpveplvp aldidglvat sraggldidy svegtlppld pgtmltihri vqealtnamk
      301 hgdgtarltv awhpteatic lengftpgak qqqghglrgm rerasliggs ltsspshnnt
      361 wltearlplq hadrvep
//
LOCUS       WP_284865897             230 aa            linear   BCT 25-DEC-2024
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Corynebacterium
            sp. MSK044].
ACCESSION   WP_284865897
VERSION     WP_284865897.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK044
  ORGANISM  Corynebacterium sp. MSK044
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Corynebacterium sp. MSK044"
                     /db_xref="taxon:3050195"
     Protein         1..230
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=24668
     Region          <159..215
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mkrlvaevai vlcvtfgmag vkallrlida aqsplnqhqv vlngatsalp wldislqvas
       61 altlfawgal alyllercle rpswrdlawg aglaaligip glalyvgayh lgfsaevvpa
      121 tdasrvplll lwsaanafse evvvvlwlvt rlrqlkvpvw gavagsavlr gsyhlyqgfs
      181 agvgnvvmgv vfawffartg kvwplilahf lidvvayvgy lmldlswlgl
//
LOCUS       WP_284865948             679 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Corynebacterium sp. MSK044].
ACCESSION   WP_284865948
VERSION     WP_284865948.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK044
  ORGANISM  Corynebacterium sp. MSK044
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 679)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 679)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 679)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Corynebacterium sp. MSK044"
                     /db_xref="taxon:3050195"
     Protein         1..679
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=75723
     Region          1..529
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mrikrlqien fraiknfdee igpytafigy ngsgkssilh avkwffedfp ltttdifcqd
       61 drenslepls kvkvtvtfdn itdrdrenfg pyargeemvl tringadevs klygdqmvyq
      121 pfqkirdans vsikrqliqk lmeadpavad ldipekapak eieaaleawe ndpinrghle
      181 pirnedanhf fgavgsdklk ihsgfvfipa apdltgqfdv sgkgsalqll lgdilkgavt
      241 dsinewtekn qkvlnelelt vkqaaqhslt dratrvnhhl knylpnvqid fevglqdwtp
      301 kaspsaqskl rdgerdfvie rqghgvqraa llallqatad irtelkqdti dnanpestki
      361 dppsdplivf ieepevyqhp vqarmmarsf vkaargsniq fvlathspyf ldptqidhtf
      421 rvesapngst vyrakfcdal spkqkmgeld kyfletvtec lfsraalvve gdteraifds
      481 mpcdangttl rdlgvavava ggsktlldma qlvhsfgvpv ivvrdgdsdc gialesakkr
      541 vehqirkefg capdfkveeh felarqrcdq klnswksdvm efikkaseig fgggldefew
      601 ggglqqgdci vvlphdlese lekwpsfmns adnfglhknt lrdnkkagil ariasqsrse
      661 dmpeslrkim ekvsnlath
//
LOCUS       WP_284866134             450 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium sp.
            MSK044].
ACCESSION   WP_284866134
VERSION     WP_284866134.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK044
  ORGANISM  Corynebacterium sp. MSK044
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Corynebacterium sp. MSK044"
                     /db_xref="taxon:3050195"
     Protein         1..450
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=48373
     Region          1..449
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrmtvigtgy lgathaacma elghevlgid vdqakidtlk agkvpffepg lpevlernla
       61 ngrlrfttdy keaaefanvh figvgtpqlr gsyaadtsyv eaavdslvph lqgehvifgk
      121 stvpvgtaqa lqeranklin apatieiawn peflregyav ndtitpdriv lgvrstsdte
      181 slteepaesr aeeiarevya tpladgtpfi vtdlqtaelv kvsanaflat kisfinavse
      241 vceivgadvt qladaighde rigrkflgag lgfgggclpk dirafmarag elgadqaltf
      301 lrevdainmr rrervvdlsr eilgsligrr itvlgaafkp nsddvrdspa lavagqlnla
      361 gasvrvydpe amdnarkvfp tldyadsldd altdaelvil atewdefknl dpehagqlva
      421 tktlidarnv lpvptwrtag wnlhalgrsl
//
LOCUS       WP_284866151             225 aa            linear   BCT 25-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Corynebacterium sp. MSK044].
ACCESSION   WP_284866151
VERSION     WP_284866151.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK044
  ORGANISM  Corynebacterium sp. MSK044
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Corynebacterium sp. MSK044"
                     /db_xref="taxon:3050195"
     Protein         1..225
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=24591
     Region          5..175
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mlvsealfll lsnksahpel gvshqrvaln gallcdlvat glvevhggks ptltavpgaa
       61 araqshpala hgververkg qptlysalns rkfaakeaia erlieegvld eeragflglk
      121 wsrfpekdet ieatmrqryr difrgkaepr peeamlivll rntgelrrqf leeiegipfd
      181 alrvrvyeid knvldaatye naeginlild gvarvaaiee eaass
//
LOCUS       WP_284866221             440 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF445 domain-containing protein [Corynebacterium sp. MSK044].
ACCESSION   WP_284866221
VERSION     WP_284866221.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK044
  ORGANISM  Corynebacterium sp. MSK044
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Corynebacterium sp. MSK044"
                     /db_xref="taxon:3050195"
     Protein         1..440
                     /product="DUF445 domain-containing protein"
                     /calculated_mol_wt=48376
     Region          31..439
                     /region_name="YjiN"
                     /note="Uncharacterized membrane-anchored protein YjiN,
                     DUF445 family [Function unknown]; COG2733"
                     /db_xref="CDD:442039"
ORIGIN      
        1 maeytldsaa adlnrlgvpg lsladqaekr rslrihktim tgllvvaaii fiictlwlkh
       61 ldgnaawwvg llragaeagm vggladwfav talfrhpmgl piphtalvpr kkdqiagdls
      121 kfvgdnflna dqiaqqisna nlseklgsfl aqpenaelvt dkacqftvha inaidcteae
      181 alinqqvisr ftepawgppl grildaliad gkvepvvqei iswgrvkvre meptvvtlid
      241 ermprwaprf akelvgervy relvvfmaev dtdpqhearg airrtlsqfa qdlqfdaemi
      301 trieelkqdi mgsraaanla gelwdaases lidaavdpns ylrrrgaasa qrlgerinnd
      361 allredldrr ieglarwsak yaadeitgmi akqiqswdgq eaaekievev gkdlqfirln
      421 gtivgalagi aiytvshfll
//
LOCUS       WP_284866524             391 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Corynebacterium sp.
            MSK044].
ACCESSION   WP_284866524
VERSION     WP_284866524.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK044
  ORGANISM  Corynebacterium sp. MSK044
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Corynebacterium sp. MSK044"
                     /db_xref="taxon:3050195"
     Protein         1..391
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42079
     Region          6..390
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 malqqpqggp lqgivvadfs rvlagpyatm lladlgatvi kvegptgddt rhwvppkrgd
       61 vgtyylsinr nknsikldlk npddletaya iidradvlid nfrvgsldkf gldpesvekr
      121 wpdlihakit gfgsragsql pgydmliqas sgfmsmtgsp dgppqkagya fidvltglht
      181 tvgilasllr rerfgggget irtnllsaal ssmvnmssaa vasdaemtrt gndhpsifpy
      241 gpfpakdrel viavgnnkqf gvfaeglgap elasdprfat neqrntnree lrpilhella
      301 akdaqewidl franglpiap iltvreavhf adelelepvv tiptkdgsde ipfvsnpldm
      361 ssgaiqytka apgldedrdd vldwiantpa k
//
LOCUS       WP_284866917             373 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Corynebacterium
            pseudokroppenstedtii].
ACCESSION   WP_284866917
VERSION     WP_284866917.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudokroppenstedtii
  ORGANISM  Corynebacterium pseudokroppenstedtii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Corynebacterium pseudokroppenstedtii"
                     /db_xref="taxon:2804917"
     Protein         1..373
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42262
     Region          50..355
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mrysagrtfn tkldaegwlf herqlidngt wmppklrreq aalerersst tvgqwcekwl
       61 ttrlhagdir estyraectr iaritevtge agrlkdrpls kltkadiyew adavssqydt
      121 nktnvgaakl lrraldnave rgliednpap knlikrrpar krenipdsem aavlyalper
      181 yrflgvltlf mglrisealg vrrrdvvgde ssgyvvqvrg qfrlfemenk tywtselkte
      241 sarrdvpvwp efsslvaehm rvfaprggdr nvnatpkgtp isdrrfrdvl rrasevvgvk
      301 tndgyvsphd grrwavtala eagllppeig rfmgdkdltt imeiymqvrp dhmeeglglv
      361 ngrigvslrg egk
//
LOCUS       WP_284866980             447 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Corynebacterium
            pseudokroppenstedtii].
ACCESSION   WP_284866980
VERSION     WP_284866980.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudokroppenstedtii
  ORGANISM  Corynebacterium pseudokroppenstedtii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Corynebacterium pseudokroppenstedtii"
                     /db_xref="taxon:2804917"
     Protein         1..447
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=49466
     Region          72..>139
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
     Region          202..331
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mknkghidpt twpnlvreps apmmgarasa vhdrleefld svdisvpdep igigdidpep
       61 piaynpeaif ssepmrmsvy dpnvmnrmvd sgflglgegy vagewdaipl advlatlldh
      121 dieagwgkml srwsrnkvtg vpragelple lielctgpsk twgsplfats srtsvtetln
      181 wknkttivdv tryespqsvs yddiesaqyr rvnqmldecr vgpgsrvlef passatlavt
      241 aarrgatvdv ltsdpvyaed irrivreekl agavhvetis gpipsprqws gvydaimsve
      301 rmetmgiggl rpflraigrm lspggraciq svintglsen slqalgimrg yvwpaleypt
      361 venvrdalmr ytdlveraev hcgdhlrvtl plwrrefain rdaaaaagfd rvyrrlwfyv
      421 lalqealfmr geldvaqfvl lkpkkse
//
LOCUS       WP_284867037             872 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Corynebacterium pseudokroppenstedtii].
ACCESSION   WP_284867037
VERSION     WP_284867037.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudokroppenstedtii
  ORGANISM  Corynebacterium pseudokroppenstedtii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 872)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 872)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 872)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 872)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 872)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 872)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 872)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..872
                     /organism="Corynebacterium pseudokroppenstedtii"
                     /db_xref="taxon:2804917"
     Protein         1..872
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=92309
     Region          17..872
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mnasatpnnq lrhhpmwtls frnlrahkvr laltvlavil gtafvsgsfi ftatlnkaft
       61 eivttmydgv diavkpgnat dfahqrdtin nipgvratne mtdmnvavah ddgtmidtgg
      121 ataqilpnyp ddeqantaws itqghaptks geatlnsnaa kknnislgdh livatptmrt
      181 dvtivgfytt stnfggwagv amnpdqfrel agtsissynv aiqpgadkqq vmaaisravp
      241 gskvqtgkea skemtssiss qltfinyfll afgaiglivg tfiiantfsm ivaqrirefs
      301 llrslgasrg qitrsvliea livgivgsvi giaagfglvh llvaglsktg ldmpdssipl
      361 twqsmvwplv igiivtlvsa wapawragst rpvesmnatt qsapllrrtl igliilggga
      421 alawwgsyad dfttrnrmii lgieavaiiv gtlavsaals lplvsgigrv lglpwrsvgk
      481 laatnssrnp rrtattafal tlglalvssv gmigasmkst vsdlvdnelt adlvatppga
      541 ttgsmfslpg gvnkeiasvd gvtgvapfyt lanatlrgdd knrgyviftp nnphgyidlk
      601 mkegtedlsr ggtvihasfa kkhglhvgdt vdidaltaas pgstgglisq ggapadahat
      661 stvigimdsk lfptalvsqq didkispdkh twrslmttvr tdhsvddvtm qkrikekvkh
      721 yviaqvqtrd efkgqqaqlv nqllsilygl lalsvviaiv giintlalsi verrqeigml
      781 ravgmvrgqv rrmitlesiq lsvygaiigv iiglyigwmf mnvmkaqgit qivipweqii
      841 amliasavvg iiaavwpgir asrispldai ad
//
LOCUS       WP_284867076             832 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Corynebacterium
            pseudokroppenstedtii].
ACCESSION   WP_284867076
VERSION     WP_284867076.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudokroppenstedtii
  ORGANISM  Corynebacterium pseudokroppenstedtii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 832)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 832)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 832)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..832
                     /organism="Corynebacterium pseudokroppenstedtii"
                     /db_xref="taxon:2804917"
     Protein         1..832
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=83866
     Region          55..>273
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 msmvkgaggs hsetkhhgqh htsvpqgsnt qenttksgfr aqvqgfprgk elagfialll
       61 gsaflfmwel dnnsygndfy aaasqagskn wtaflfgssd wgntitvdkt plslwpsala
      121 ikifglnsws vllpyallgv asvavlwatv rryagstaaf vsgivlaltp vavlmfrfnn
      181 pdamlvllmt calwaamrcv etgkwrwavl tgvfvglgfl akqgevllii palvvllavv
      241 sprswkvklg qslatvaamv vsagwyivav alwpsssrpy iggstnnsiw eltlgyngfs
      301 rlsgngsapg ggagggpgga gqggsasdaa qgaasaasng tgqagssgqm gnmpqggspg
      361 ggghggptfs gepsilrlfn eqlggqatwl fiaalialvm givlcgrapl kntkrglyig
      421 lgvwllmcag tfsfmegtmh qyytvamvpp maglvgmgaa dawqhrdrlw vravsaaail
      481 tsgvtgfgvl rrasdsfptw lpwvilvatv igaagwfalp wmsaagarrh adgsasskls
      541 arvlslragv vgvvtaamla gpsaysayti ahantgsvva agpksdsgmg gpggggpggq
      601 ggadgqggad gqgatdgqss adgqgangqd gasspgqmpg ngqnsgpggt apngggtppn
      661 ggngqgmpgg pngsgstsdn ssngmpggss dgksdgkggl sasagkqggt sspggpgqmt
      721 vsetlkkklk edsdkykwsa atigsqgaas yqlatdtdvm piggfsgsdd aptldqfkkl
      781 vsekkihffi adsgqggapg gnneitswvk ehftattvdg vtvydltqek ss
//
LOCUS       WP_284867105             283 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein, partial [Corynebacterium
            pseudokroppenstedtii].
ACCESSION   WP_284867105
VERSION     WP_284867105.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudokroppenstedtii
  ORGANISM  Corynebacterium pseudokroppenstedtii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12206295
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Corynebacterium pseudokroppenstedtii"
                     /db_xref="taxon:2804917"
     Protein         1..>283
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          197..>283
                     /region_name="AAA"
                     /note="ATPases associated with a variety of cellular
                     activities; smart00382"
                     /db_xref="CDD:214640"
ORIGIN      
        1 mmrhgeavsv depvpvnppp veppapspte ttkppfdipq phvsapsidv ghvvliglvi
       61 vgvvvavyva vslvqrwwfr gneaiilark qrkkivddfg ltigvpgrdg sfsiapketd
      121 kwsreglage ltsalrpksg kvlvefptpg rvrlrtavep sgvvhgecfs dakslcigvs
      181 avdssparit qsqtcgylvv gvpgsgktva lnalkkawkn gprpvkigsw dgkkdsqsrg
      241 lklleslkqa mdnrlardvd awngndavdv elkvlvvdea drl
//
LOCUS       WP_284867186             312 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284867186
VERSION     WP_284867186.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..312
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33478
     Region          3..277
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
ORIGIN      
        1 malseeiipr iplgswgdna lmwlrenaav ifdvfseitk flvealadgl kaipaillla
       61 ifacagwalr swrlalsaci sfllvmglrq weqmldtmam viiatlvavv ialpvgiwaa
      121 kndrvsatvr pildfmqtmp afvyllpavm ffsigvvpgt fstiifalap gvrmtelgir
      181 hvapevveag raygatdrqi lrgielpmam psimaginqi imlslsmavi agmvgadglg
      241 kevvaaistl nlgrgleagl avvilavfld rltaalgnpg dypssllarw rkarrqrqkg
      301 rveqglvena kp
//
LOCUS       WP_284867211             548 aa            linear   BCT 25-DEC-2024
DEFINITION  LGFP repeat-containing protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284867211
VERSION     WP_284867211.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..548
                     /product="LGFP repeat-containing protein"
                     /calculated_mol_wt=61048
     Region          137..346
                     /region_name="Psp3"
                     /note="LGFP repeat-containing protein, may be involved in
                     cell wall binding [Cell wall/membrane/envelope
                     biogenesis]; COG5479"
                     /db_xref="CDD:444230"
ORIGIN      
        1 mlkrhlfttl tallaligsa tttniayadp svpasqdpet vtlasdlppl svdgvggyse
       61 eevvemqeff rtveqnidet taqetltpge mwsdsielpd avdkedadqa elmiaeeqes
      121 gvasrwqsra prcrifwpsp hrvcgailqa yeqlggmtsw llfpieaesi npdlqgyrqr
      181 fangfiywhp ntgahpvsth asliwsnlgw etgmlgypts seilrtegla isqrfqhgaa
      241 lltlagasam fndafrtwel qgaergplgy plglpnetiy pegrtqvftg gitisdqhrd
      301 alpvygevfd qwitdfendk liglptqapq ktarnrvsqv fehqtlngks fgnlasdvms
      361 hvflpfktqe aadeffefay salnqveqlr deflprntrn drdqprrrql lgeianlmgg
      421 ylfggrctvr mdnihkrspq sgpdwkigwk pqttcttdra itvthtntlk ylgdseelwl
      481 qvpldsgrva sgaaikfqqk dieyrcireg kitykgitkv vikqaygdpl havaetakah
      541 ktkcigrk
//
LOCUS       WP_284867235             465 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284867235
VERSION     WP_284867235.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 465)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 465)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 465)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 465)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..465
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51896
     Region          3..444
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 mkllnlvven hrsfrdefhl eltrphftsn ipdsrdswae nvfpviaiyg anasgkttvi
       61 dalkylwsal sassgewlnr asiphapfll gkareqpsty sidftldady sqanptpget
      121 rfhyefdvtp qgfrhellqv yrssrattll srkqsedgvk lklaaglggk fevthrelal
      181 sragmtgrgq lgviaqkikd glliigvdde ernlrlhrit eeldkgnihl ddfsalaqvs
      241 dfgiqkidvd iqklpndiak rlrtimdvie ndapehaasa elpkrehsek ethefiqrsl
      301 qfthktihsd tpqpkfgind qssgtlawla laipmvevlr hgtvlcvdel ssslhpklaa
      361 eivrvfqtpe lnphhaqlif sthdvsllmp qaelnlqpgq iwftekeidg aselyslrdf
      421 pdirggtnia kqflearyga tprvipelis kialhgahed tealv
//
LOCUS       WP_284867273             519 aa            linear   BCT 25-DEC-2024
DEFINITION  FGGY family carbohydrate kinase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284867273
VERSION     WP_284867273.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Yeh,J.I., Kettering,R., Saxl,R., Bourand,A., Darbon,E., Joly,N.,
            Briozzo,P. and Deutscher,J.
  TITLE     Structural characterizations of glycerol kinase: unraveling
            phosphorylation-induced long-range activation
  JOURNAL   Biochemistry 48 (2), 346-356 (2009)
   PUBMED   19102629
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426119
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..519
                     /product="FGGY family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=56318
     Region          2..512
                     /region_name="GlpK"
                     /note="Glycerol kinase [Energy production and conversion];
                     COG0554"
                     /db_xref="CDD:440320"
ORIGIN      
        1 mfiaaldqgt tstrclifdr dgnvvsqaql ehqqimprkg wvehdpneiw antrrvissa
       61 mvelditard vqalgvtnqr etavvwekat gepiynaivw qdtrtggefd daaawqaktg
      121 llansypagp kiawildhvd gareraerge llagtidswl vwnlsggaeq genageadga
      181 daestpgnss datnqaqhit dvtnasrtll ldlhtldwdd elcealrvpk kilptivpsv
      241 galgevrhrg sltgvqitgi lgdqqaamfg qrcfrpgdak ntygtglfll lntgtepkfs
      301 ehgllttiay qqqgekpvya legsvavggs liqwlrdqlg iipdaasses iaaddnggvy
      361 ivpafsglfa prwrpdaagv ivgltryadr shitraalea tcfqtrevve amqkdagrel
      421 sglcvdggmv andllmqmqa dilgssvqrp emiettvwga alaagigigw wdfsdddyaa
      481 drvwepkmpe aqreqlyrmw nhavertlgw edacraead
//
LOCUS       WP_284867324              85 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284867324
VERSION     WP_284867324.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..85
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9451
     Region          20..>59
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mpklepahqv iedlaanvfr ryrnytlkef aadtgvsalt isdltrgnaw psaltvarle
       61 vavryplwpr khvhtpsqnh gmttp
//
LOCUS       WP_284867354             522 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284867354
VERSION     WP_284867354.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 522)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 522)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..522
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=54287
     Region          10..247
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mspsqnslkl nytaasdrgl vrtnnedsaf agrnllvlad gmgghaagev asqllvttmq
       61 rldrdpgend mlallgtaad dantaiadtv rqrpetqgmg ttctalmfng ttfgmchvgd
      121 srgyrlrggk leqitiddty vqslvdsgsl kpedvsthpq kslilkaytg rpvdptlrmi
      181 daqpgdrlll csdglsdpvt adtieqtlke gtpeqaaskl idlalrsggp dnvtvvvadv
      241 lagddestti paapvsagal alpeaerahp ntaagraaal nrrpqvvepk aqvagahnhg
      301 tggnagngsg pgngagtgaa sgawaggsag aaennahdna skrgrnwtla ivvlvllggl
      361 igggwwvyas sqdkyyiatn dsdeliierg vdyslfgkdl hepyqrvclt kddevrttdl
      421 gekpsndchp fsltdlpgsv rgsithldsg sysevtdqlq rlsdkalpvc vnraetdnng
      481 knnegknndg ntgankdkda anaesaddgg lstpgvncre vs
//
LOCUS       WP_284867439             464 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284867439
VERSION     WP_284867439.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..464
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=48585
     Region          1..463
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrltvfglgy lgathaacma eaghevlgvd iaparvaqlq agrvpfyepg laelvargva
       61 sgrlrfscdy rqaaefaqlh fiavgtpera dspaadtsav eevvgklapl lrgehvlvgk
      121 stvpvgtaar lqeratsiss atvdvvwnpe flreghavad tlrpdrivvg tgaestpkga
      181 dapngvgsap alqklrevyr aplergtpfl vmpwasaelv ksaanaflat kisfinaiae
      241 vceavggdva avaealgyde righqylgag lgfgggclpk dvrafrarad ecgagdalaf
      301 lgqvelinar rrqrvvqlas elvaqspkaa epagsarpgl sgavitvlga afkpnsddvr
      361 dspalhvaae lalrgarvrv cdpqavenar rvypgleypa sladgvagsd lvilatewpe
      421 yreldpvwaa elvaepvlld arnaldlarw rdagwqvhal grgd
//
LOCUS       WP_284867482             276 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284867482
VERSION     WP_284867482.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 276)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..276
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28825
     Region          1..248
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mtrfklvrfg fafiffisvl cgpwiaellg dvasvaprgv pfassdqlkp lgtdhlgrpv
       61 lgailhggqs llltaiiggt lttifaavlg sfgalyprlg vvidtladai ilvpsvilml
      121 lltvifpeag vwlliltvaf lgtpyaarvc aagahniaat gyvqaaqslg epawkiivkd
      181 ivpnmshilr svwglriiea lyllaiasfl gvgnslgqfa wstmvnenaq gillnpwavg
      241 apavllglss vvilsalgaa eatdissqkk vaeyvr
//
LOCUS       WP_284867534             519 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA repair protein RadA [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284867534
VERSION     WP_284867534.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..519
                     /product="DNA repair protein RadA"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140664 - ATP-dependent DNA damage sensor
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=53661
     Region          1..515
                     /region_name="Sms"
                     /note="DNA repair protein RadA/Sms, contains AAA+ ATPase
                     domain [Replication, recombination and repair]; COG1066"
                     /db_xref="CDD:440685"
ORIGIN      
        1 makkqraiht csecgysspk wlgrcpecgs wgtleeaapi fsagftaglg sgakasaarg
       61 gagglgagar asssgrrggl apssaavpit qisaqsaqsm htgigeldrv lgdgivagsv
      121 vlmagepgvg kstlllevaa rwsqvpepqt dsgessaaat eitadqqaqp atrtalyvta
      181 eesaaqvysr akrtgglspt lylaaesdld vvfqqvealr psliivdsvq tmqatgvegv
      241 aggvaqsrav taalttlakt tgipillvgh vtkdgnvagp rvlehlvdvv lnfegerqss
      301 lrmlrgiknr fgatdevgcf eqtadgirev adpsglflsh hgatpngsav tvamdgvrpi
      361 vaevqsltvd pvaknprrvv tgldqnripl vlavlqarag ertnekdayv atvggvrite
      421 tatdlavala twsslhetpl paktvfigei glagemrtvp nlrrrlqeaa rigyrcavap
      481 srndaedral akelaadgld lrsvstlrqa lavvrelrg
//
LOCUS       WP_284867536             327 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284867536
VERSION     WP_284867536.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..327
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33849
     Region          22..326
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mrktwtiagi saatllvalv gsltvgsssm sfseliglvv psqpspsplr tsiltelrip
       61 rilmaafvga ilavcgvamq avthndlaep yllgvssgas tgaviailfs twqygiifga
      121 tigslasfal lmlllrntgg datkvvltgv ligflfqslt slvvtasgda estrsimfwl
      181 lgvlgaarwp tlfavmivgs igmlvlwals rhldalslgg dtastmgvpv valryivlic
      241 vslmtattva svgaigfvgl iiphairmln vpkhaslipl salvgavtlv iadafarsif
      301 apqelpvgvi taligvpmff lilrrkh
//
LOCUS       WP_284867599             181 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium sp. MSK150].
ACCESSION   WP_284867599
VERSION     WP_284867599.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 181)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..181
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19620
     Region          4..156
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18879"
                     /db_xref="CDD:467590"
ORIGIN      
        1 mptpdfivql rekighdqif vpacsaiiir dvpadaalwe vpsvllvkrs dngtwtpveg
       61 icepgeeitt talrevkeev gldakveall gvgksgpvty pngdectfmg talrvsvaen
      121 aepvisdeen teagwfsvak lpdsvsrrhr lmiadavaqm khprgfaprm gwmkrseqpg
      181 l
//
LOCUS       WP_284867688             402 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Corynebacterium sp. MSK150].
ACCESSION   WP_284867688
VERSION     WP_284867688.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..402
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43324
     Region          1..396
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 manllgivff algigltval heaghmltar afgmrvrryf igfgprlfsf rkghteygla
       61 afpvggfcdi agmtaqdefl teeeephamy kkpwwqriiv maggigvnli lgfvilyfva
      121 mtaglpnpda dvrprvgevt csasqkpnqe leactgkgpa gkagvqegdi ivaldgqkld
      181 sftqlrdevm qrpgetitlt verggeekdf pvhldtvkrl nqdgelvdag siglsnqlid
      241 vvekhgavda lpatwrfsty sldatveglk qfpgkipgvv asifgherea dgpmsvvgas
      301 rvggelaers lwsmffmmla tlnfflalfn liplppfdgg hiaviiyekl rdgirklagk
      361 palgpadytk lmpvtyvmaa llmgvgaivi vadvvnpirl fg
//
LOCUS       WP_284867693             451 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Corynebacterium sp. MSK150].
ACCESSION   WP_284867693
VERSION     WP_284867693.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..451
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49350
     Region          1..451
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mqlhhdfaqk lphlvrpteg eeqpnpemvi lnedlatelg ldpdwlrsse gidfltgrag
       61 ghamaysgfq fgafnpqmgd gramllgeve kdgrlwdlha kgtgltpfsr lgsdgrgtls
      121 smlreylvse amhalgvptt ralavistgr piqrghvqpa givvrvaash irvgtfhlaa
      181 qtdytrqlad yaiarhypga dyqefftqvm daqirtvshw mrlgfihgvm ntdnttisge
      241 tidygpcafm eayspstvfs sidrqgryaf gnqpsilgwn larlaesllp lfdmdmnkam
      301 dfaqesikgf tdrfehqhra dlaqaldtsr evassyaaam qlngpditla hraladaaag
      361 hptharelfa kgdflegyla sspdpsrvdn amprviprnl avesaldaae rgelgpyqel
      421 lhavthpwep npafespdpn glegyltycg t
//
LOCUS       WP_284867739             382 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Corynebacterium sp.
            MSK150].
ACCESSION   WP_284867739
VERSION     WP_284867739.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..382
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41554
     Region          10..378
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mvdtghphsl eglrvldmsr vlagpfcsmi ladlgaevik ietpwgddsr nfgpafkgds
       61 ayyrlfnrsk kgitlnlked adlntlrelv qradvlvenf rpgvmeklgi speslmelnp
      121 qlivtsisgf gqsgsmskap aydlvaqams gimsvtgwpd grptrvgisl gdlipglyga
      181 igtlgalqer hrtghgqhvd vamfdslvsi lesvamrdly eeevptavgs dhamtvpfst
      241 yrvddgevvi ailneklfgc ltralgleym vddprynsnp arkerreevr siiedalrgk
      301 tveqalalfq ehgvptapvh svdealhgdv gterevlfte sdgfttlssp lrltgsrqpe
      361 papqlgehna hipewlaepv rg
//
LOCUS       WP_284867851             741 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium sp. MSK150].
ACCESSION   WP_284867851
VERSION     WP_284867851.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 741)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 741)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..741
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=81464
     Region          14..734
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mnsashkhat aagssereai ateqdyvdgl farlddevaa ankrlnevqa dvdpstpdad
       61 alvrreteyh glqakldrln vaqmglvfgr ididapgdnp tpegldrryi grmgldared
      121 dyrtllldwr apmarpfyla ttaqpegvht rrqirtkgrt vtgihdevla gpgvreeeag
      181 vasesalyha mqrartghma sivetiqreq deiirdntrg vmvveggpgt gktavalhrv
      241 ayllythrel lsatgvlivg pnssfldyis rvlpelgetg vvlstigglf pgiepsheed
      301 lvareikgsd amveilstav kdyqllpdap reltvdgltl svtphmvksa rtrarrsrkp
      361 hneargafie hlvedlaqqm aekvgadplg gknllsradi dqfhddlaed aavtalidef
      421 wpelhptdvl aalvssreri asaahgydee tqealyraeg rawtdsdaal ldelavligl
      481 pnpeekkaad daawreqvad aedaldilss sestdndddm feaeilsahd vidaetlahr
      541 qevrdkrtta qraredhtwa yghiivdeaq eltpmewrml frrcpsrwmt lvgdtsqtgs
      601 pagvddwgea lepfvaqrfr hhfltvnyrt pqpitelang lleminpdai patairdgvq
      661 vrrleqgayt pgvhseedgr ltavidaata erykglefdh vvvldpqriv daspqglqnl
      721 yvcitratqs ltlvgdcgev l
//
LOCUS       WP_284867868             290 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Corynebacterium sp. MSK150].
ACCESSION   WP_284867868
VERSION     WP_284867868.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..290
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31900
     Region          1..272
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 masirevlav eettmadvfk gpavesrier tfggqiaaqa vaaaqrtvsg kdihslhgyf
       61 vgpgnasqpi eirverireg ssfanrqvrv yqgdvllftl masfhrdgdy gpqhqdaapk
      121 vpgpeevarm gggapystri ilkeweewdi rlvpeegrdp vaaertgagy rhiwfrntgh
      181 lpadsafhca altymsdmtl irsaliphqg vkvqlasldh aiwflrpfrv dewllyeqis
      241 ptasnatava rgkifteqge lvalvnqegl tryldenlgs gsahgnwhnv
//
LOCUS       WP_284867879             690 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Corynebacterium
            sp. MSK150].
ACCESSION   WP_284867879
VERSION     WP_284867879.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..690
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=72672
     Region          32..514
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mqfrrigqlv aattvsaval sgaqavaqen kttisvtnit dihghledki gdpakagdei
       61 gvarlqslik qvnegqefnl tssgdnvggs afvsaisddk ytlealnemg mkvtavgnhe
      121 fdkgtedltg riadssdypi lganvfkdgk plleashvee idgvkvgyvg tvtentkykv
      181 saakipgitf tnpaeatnke atrlkesgea dvvvalmhed aqgfaedfnk dvdvafggdt
      241 hvatkgeier egalplqwaq gheygkllnd vditfdktak kitdislkqy dataaakvep
      301 daeiaaivkk aqqeadiaga ktagtveral frgsdenads gsnrgvestl nnfiadgqry
      361 amskqvgedi eigvmnaggv radlkggdvt ykdifevqpf gnsvitakis gedfikalen
      421 qwqegsrprl amgisnnvqv vydqeagkge rvksvtinge pidpkkdysi alssflassd
      481 eeaggdgyfn agsikdkndv gymdtqamid yiksgesevr tgqgqigahi egdvkpgeei
      541 tvnlsslnys tdgepmakka tvklgdaeqt vdidnaaqeg daqfgergra tvkltvpenl
      601 sgtqnleitt dagtkatlpl evsgegseep gakpapkgss lssngssvgg avfaivaalv
      661 agvavvgmnp qilpaparkm iedlrkqfhi
//
LOCUS       WP_284867961             938 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium sp. MSK150].
ACCESSION   WP_284867961
VERSION     WP_284867961.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..938
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103621
     Region          4..936
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtethldsft aalpypldef qvkgcqaved ghgvlvcapt gagktivgef avslalsrgt
       61 kcfyttpika lsnqkyhdlv eehgeeavgl ltgdvsinsd aeivvmttev lrnmiyaesp
      121 aldrlthvvm deihfladas rgavweevil nladhvsiig lsatvsnsee fgdwlstvrg
      181 dttvivsehr pvpldqwmml grkiyplfep esggqvnsel erriqrleag dtddgradyk
      241 sgkgfrarar hkgggrsefh gkgrgrsgaa rqqdryrplg rpevlkvlqs qdmlpaitfi
      301 fsragcdgal yqclrsrmvl tsqeeaqhik divdagvegi peedlqvldf krwrealsrg
      361 faahhagmlp afrhivedlf vrglvravfa tetlalginm partvvlekl ikfngeahvd
      421 ltpgqytqlt gragrrgidt lgnavvqwap amdprqvagl astrtyplis tfapgynmai
      481 nllgmlgfen slrlleksfa qfqadgsvve etreieraeh rvrelrnqld davaslappa
      541 kdgedpaevl mdyvrlrrel taeekqskid sanqrnqevi avlgrlqlgd viampgkkrp
      601 ilaavvtpan qtadprpwit tesgwsgrid aaginnppiq vgsikipkpv rknprrntry
      661 vqdvlhrehf drpkrmksht rarpnkrvgq lrdalrahpa hdwpatdreq laglaqklar
      721 rerdrdklqs kvnkatdtlg rtferivdll aemdyveftg vgadrtpvit eegerlakih
      781 sesdllvaqc lkrgiwdeld paelagvasl ccfenrkats gqpeaaterm adamnatwrv
      841 yteltadeqr hrlpptrepe agfalavhqw aagaplgycm aaaneagael tpgdfvrwcr
      901 qvidllqqva ktgydgeiqr narraidaiq rgvvaiga
//
LOCUS       WP_284867975             200 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Corynebacterium sp.
            MSK150].
ACCESSION   WP_284867975
VERSION     WP_284867975.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..200
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21886
     Region          36..143
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mptwkevtea npehshnfar kwkvlaaqgk dingearlid amvernstil dagcgtgrvg
       61 gellhrghsv vgvdvdpili ehaehdfpeg qwfvgdlcee evpegpfdia vsagnvmgfl
      121 akegrepalr niynslkpgg rlvtgfgegr gwefsdfldm aqkvgyrvdf tfsswdmklf
      181 sehstflvav lsrpgsdlla
//
LOCUS       WP_284867995             265 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Corynebacterium sp.
            MSK150].
ACCESSION   WP_284867995
VERSION     WP_284867995.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..265
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=29011
     Region          8..251
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 mtqpeitgfr ialrnfegpf dlllqliqsk kmdvtdvals evtdefvayt rqlgesadld
       61 ettdfllvaa tlldlkaarl lprgdvddie dlellesrdl lfarllqyka ykqaadqfav
      121 wqreaqrsyp ravsieetfa ellppvslgh tpasfaelaa gvfrpkppee vatghvhava
      181 vsvpeqagki leilkllgag qwtsfgaltr dctvsmqivg rflallelyk akavdaqqee
      241 algqldlswt gldvdpavva aanwd
//
LOCUS       WP_284868210             277 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Enterococcus faecalis].
ACCESSION   WP_284868210
VERSION     WP_284868210.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..277
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31890
     Region          4..264
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(28..29,31..32,35..36,71,75..76,79..80,121,125,132,
                     135..136,141,156,160..161,163..165,167..168,171..172,
                     175..176,202..203,205..207,209..211,213..214,216..217,221,
                     224..225,231,233)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(159,163,166..167,169..170,216,219..220,222..227,
                     230..232,236,238)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(180..187,204,207..208,211)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mserqmlgyh pdstwihrln gtsklvfliv vsvacmttyd tryllgmsvv slvllklsni
       61 kwhqisfvik fiaifslldi ltvylfapey gvdlyqsrtv iwegigrftl tqeelfyefn
      121 lvlkyfctip lalifllttn psefasslnr igvsyrisya valairyipd iqedffnisl
      181 aqqargyems kkgrlgqrik gvaqivlpli lssldrietv stamelrrfg qkknrtwyaq
      241 qpfhlrdfsv mllalcllgi sfwlfhvngg rfynpfq
//
LOCUS       WP_284868337             610 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Corynebacterium sp. MSK150].
ACCESSION   WP_284868337
VERSION     WP_284868337.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..610
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66535
     Region          13..610
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mtlqevhtpa qftiepgetc ltalmdtakk rphgvmftrp anyewvnvtg kefidevfev
       61 aqglialgvq qgdrvalisa tryewslldf aiwaagaasv pvypsssasq vrwiiedsga
      121 vlaitetreh selvenlvlq edgepnlkgs psqlrrvlei nssaidtlkf egrgvtadev
      181 yarikatstd dlaslvytsg ttgrpkgcil thrnwlaqtr glctnpigif avpgshtltf
      241 lplahvfara vsiavamrga sqnhwsdfst isiefarsrp nvilgvprvf ekvrnsaaak
      301 aadsgiktll feqsekvaie yskaldkpeg pdrllkakhk vfdklvysti rkgvggnvny
      361 citggsamgh dllhwyrgig ipvyegyglt evaaaaavdf vdqsigtvgp pmggvtfrin
      421 degeicikgd ivfhgywnnp eataealedg wyntgdlgei dedgklvitg rkkdlivtag
      481 gknvspgpme dilrghplis qamvvgdgkp fvgvlltldp dilkrwkldh nipenrsmre
      541 latdptlrae lqdainqvna tvshaegikk fyilesdlte eeneltptmk vkrnvvaqry
      601 aaaiehlykr
//
LOCUS       WP_284868358             415 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium sp. MSK150].
ACCESSION   WP_284868358
VERSION     WP_284868358.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13213516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..415
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=44465
     Region          <45..>162
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Region          143..411
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mvrtkwstag ivaacavanw ligvvlmnld ieeyspsfae ygpyictgfa vgvlgiialp
       61 falehqprel sdvdyagstr sfiagcivll gsssyfgavs gvvafismvs rrsttrsvva
      121 vacfvlafai dasfnpylsw deigwvgaif vvvvmvagll agqkrgnqre krwrveqqar
      181 mnreemrakv eharreeres iardmhdsls hrlslvaiha galsypregv peeftdaart
      241 iraeaqnave dlrtvlsalr edlsqdprtg leelvasare agaevtvtya dgaspdvfdg
      301 lstmaqhavh ravqegltna rkhapgqpvs itvreaagav diemrnpvpr gkagadtdgv
      361 eggaggyglv glrervelsg grmsiaanqe spggkggeef rwsiqlplah keaaq
//
LOCUS       WP_284868521             734 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Enterococcus faecalis].
ACCESSION   WP_284868521
VERSION     WP_284868521.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 734)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..734
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=85633
     Region          5..210
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
     Region          325..>439
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 menvkvsviv pvynvetyle ealmslknqt lkeiefliin dgstdnsqki ieeiaqddpr
       61 frvfnvkngg igkafnlgvs eakgeyiaef esddyvalhs yerlyntaks hhadvvrcnw
      121 vefsseeeve rdilwqypdk ynqlidlktt dlivqvypwn aiykksmiek envtwdeeik
      181 sygdtglfwk insasqnvif ikdclyfyrq dnpnstvnnv atkvpflfqq fklirsnlie
      241 qnkferykgy fykqmfekyf waieklthlr desvyeviqk vavdfkqaie idqlndidfe
      301 yikqfyqian dpaayyedyl knlykvsvvm pihnaskylr qtletvceqs lreieiilve
      361 ngstdntmdi inefavkdpr itgisigksn pgharnvgis margrylqfl daddhfeanl
      421 lqdayyrayd satdillfgm keklpngevh vvhnplltng grmsgeeisl devtpylydk
      481 lflleyiken nlvnleqfvg edayftytal lgtekivaln kylltrivrq dglmstygmn
      541 yrdefnlhdk mleylkqhap nrieayrlki intlnwfifd mnrvdqafke rfyqelkeky
      601 iqqlgldlvk kekysndpeq veritriqni lqynleiyqn iykdfgmkkt fiipnvhiqe
      661 rggkvifgqe ktqgngtaie mfsiiiadnd tsnasgvidf vymgdntkii hdsllvslli
      721 incqikldns slhm
//
LOCUS       WP_284868620             420 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium sp. MSK150].
ACCESSION   WP_284868620
VERSION     WP_284868620.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..420
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=45483
     Region          16..379
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 melilsfaag vvacglalpa iswlrgriah yrqasdaean qvttvshvlh lavqgsptal
       61 avldrsqeiv msnsaahems lvhdravnpd vwqtaqevfe dketrtvdla ipkrrtghrv
      121 tqvkavikpl tlndgrfvii ygtdesenvr mesarrdfva nvshelktpv ggiallaeal
      181 lqdpgdqetv eyfgnkvyke anrmadmvse lislsklqga ealpemepla vddlieeals
      241 rnqlaaears ielnrgasvg vqvkgdrsll vtalsnlisn ainyspekmp vsvsqkvvdg
      301 gvvlirvtdr gigiapddqk rvferffrvd qarsrqtggt glglaivkhv vanhggnikl
      361 wsrpgtgstf tielpiyree kpardagmkd nenqdavtaa apglpravar vaarrkdkaq
//
LOCUS       WP_284868691             371 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium sp. MSK150].
ACCESSION   WP_284868691
VERSION     WP_284868691.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 371)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..371
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=38256
     Region          25..369
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mrrnkaaqav qdkqsaswqm pggvpfragp isflwrprvv lvciiaaalt vflgalsigl
       61 gdypisvprv levifqgqgs lveklvvlew rmprvataia vgcalglsga ltqtvtrnal
      121 aspdilgitt gasamavtvi vlgaggsgfa gwlagigipl aallgailsa mviwalawrr
      181 qadsyrlvlv giiitallss yinflmvrae lrdasqaqfw ltgslaksew sttipmvvlv
      241 lvcapllawi ayqalattlg pdlaralgqr vnavqvamla lavalaavav saagpigfia
      301 fvapqvalrl cgvpspplaa saltgavlll gadivtqavl pvelpvgivt salggvfliy
      361 llvqrtrstd a
//
LOCUS       WP_284868760             425 aa            linear   BCT 25-DEC-2024
DEFINITION  Mur ligase family protein [Corynebacterium sp. MSK150].
ACCESSION   WP_284868760
VERSION     WP_284868760.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13558984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..425
                     /product="Mur ligase family protein"
                     /calculated_mol_wt=44817
     Region          64..>187
                     /region_name="Mur_ligase_M"
                     /note="Mur ligase middle domain; pfam08245"
                     /db_xref="CDD:462409"
     Region          312..410
                     /region_name="MurT_C"
                     /note="MurT ligase C-terminal; pfam08353"
                     /db_xref="CDD:462442"
ORIGIN      
        1 msfrvpgalk klrtttatta aklattasra tgrgaggmig glianaidps imtnlgggrp
       61 avlvtgtngk stttrmlaaa vrtehtvatn dggdnmdagi isalmagkda shlvlevdel
      121 hvphvadnln pqalvllnlt rdqldrvgei nkieralrga veahpdmlvi ancddvlmts
      181 vaydaknviw vsagagwlgd svtcprtggh vvrteddwya vkpladgref rrpqptwgvd
      241 krgiitptak rplnlalpgr anrgnaaqai aaavqgfgvd ldkaiaaaeg iddvagryst
      301 ihwkgreirl llaknpagwq ealsmvdrsa dglviatngq vadgidmswl wdvkfegfns
      361 lsvkaagerg tdlavrlvya dishelipdp mdalaacpeg rievlanyta frdlkkalsk
      421 eatna
//
LOCUS       WP_284868767             526 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Corynebacterium sp. MSK150].
ACCESSION   WP_284868767
VERSION     WP_284868767.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 526)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 526)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..526
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56804
     Region          15..502
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mdvllvligl mlltvfvvai gdkiglpwpa lltiitacav fvpglpqfep ptelilpifl
       61 ppllwalarr tswgvireqw vtilslsvll vvattlavgf tayaflpgis laaailigaa
      121 iappdpvavd avaepagipr riittlqteg lfndaasiva fnlaltavtq gdelsfgggv
      181 lnffysafva gglgwgvgrl valfithvhd vtarnaltwv tpfavylise elgasgviav
      241 viaavelnsr adiqaedrls gqafwetiel lftgvafgli gltvntaige vgsdlwhsvl
      301 vgvilslvaf vvrlvwmyiy yrinvsrgrp rvaplrlqev llmtwsgmrg lvtlalvlsi
      361 pagvfsfhhe lavialtvll vtmvvpglll pwlmerldlt easqiasdkm raavvsrara
      421 asiealshfr pdghitadae kvdpeisanv ikwfedrlgd gedvsddsrv qrawqarhva
      481 learrtalva aqeellrmrg yraynpaivd evleeidrmv lgtkrh
//
LOCUS       WP_284868796             336 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium sp.
            MSK150].
ACCESSION   WP_284868796
VERSION     WP_284868796.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..336
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35593
     Region          54..336
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkrparltnv sasngdtsla alllealpln rpvyaaclaa vgpqgariat igcdlndtfh
       61 igsiskalng liytemvhag lisphnrlad ylplagtaag eatlesclth tsglpatgga
      121 traaaralva vliggdpqpe svealinqlr ksrvsnpgrf sysnlaasal ghalaaangt
      181 dyfnlvrnrl aiplgcprlr aqqpgqrnlp ydvkaftvwg teqrpwtgqg ygpagairgs
      241 ardfatilsa llsnedpysd afrvrftddt esiaagwfva derdrhlvwh ngyasgfgah
      301 mvldrenrqg afisvvspwp dpeiepiamr alnaam
//
LOCUS       WP_284868826             195 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Corynebacterium sp. MSK150].
ACCESSION   WP_284868826
VERSION     WP_284868826.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..195
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=20742
     Region          1..191
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mrlilasqsp srasilrgag vepvlepadi dersleasla ghppadivaa latakaekva
       61 erypaepvig gdsmllldge lqgkphtaea tikrwhqqag rtaelltghc lifgdkrhve
      121 tstttvhfah asetdiaaya hsgeplhcag aftleamggw fidriegdps sviglslpvv
      181 rralyafdln vsdfw
//
LOCUS       WP_284868955             458 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium sp. MSK150].
ACCESSION   WP_284868955
VERSION     WP_284868955.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..458
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48592
     Region          97..396
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mhtlrsigss vagiaiaagv lsapiasave paenqgdatp stirevnftd padaeninya
       61 ittegenrvv diaklkdkdk wkgyafghks kagkhygnhv kaltatsaam dgrevplavi
      121 tpdgnfdkkr ptlyllngag gaeqgmdwlt atanhdvdpe tegvqdmvdf ytskdvnvvi
      181 pqagafsyyt dwvsspnngy lkgpqkwetf ltkelpdale khiggngkrg iagmsmsats
      241 slllaehnpg fynavgsfsg caatsrplpr lytqltvnrg ggsadqmwga mgseynvynd
      301 alvnanpnnl gksetyvsvn sglggandwg vpgsstlive ggvieaamns cthdlkakmd
      361 sqgmnadwnf rntgthswpg wrddifsswk tfergfakda aeapaepevk pnelsieapq
      421 aeedaqvkda psaadqspdk dyvedltada petagtae
//
LOCUS       WP_284868968             478 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Corynebacterium sp. MSK150].
ACCESSION   WP_284868968
VERSION     WP_284868968.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..478
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50669
     Region          4..469
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mdyqpraviv gagpngltaa arlamagwsv diyerarrag gaaassaeif pgtivdlgaa
       61 ghpfgvaspa fraldleahg vrwrnapypm ahplegasag ilhgsladta aelgtdaqaw
      121 rrlhghivrh idehvdnalt plvrwpnrpv rlaqfgaagv vpasslaraa frtpqaralf
      181 agsavhaits pttpftsafg llfgglgmtr gwpvveggtg alidallnll rshharlhtg
      241 cevtdlrelp padaiilnlt prqilrlggl elrdgtrrsl arwrygsavf kvdfhlsepv
      301 pwtdprvgra gtvhvggtme eicgaegdvg krrmpkrplv lacqqyvadp srgqtlwtya
      361 hvprgyvery pgevteliaa qierfapgfr dtilatrats padlerwnpn lvggdiagga
      421 mtglqtllrp rlsahphrlt pgvfmasssa apgagvhgmp gwwaaeeals awnggaak
//
LOCUS       WP_284868989             119 aa            linear   BCT 25-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Corynebacterium sp. MSK150].
ACCESSION   WP_284868989
VERSION     WP_284868989.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..119
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12956
     Region          2..115
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 mnllcvllgg figgslrygf trlvpapyct fvanilgsla lglaygfaql adaplihpfl
       61 alglagglst wstlakelge mikrkqwwrl skylfwtigl givlawrgti watriyhgi
//
LOCUS       WP_284868990             400 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium sp. MSK150].
ACCESSION   WP_284868990
VERSION     WP_284868990.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK150
  ORGANISM  Corynebacterium sp. MSK150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Corynebacterium sp. MSK150"
                     /db_xref="taxon:3050209"
     Protein         1..400
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43091
     Region          141..380
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 msfllnlpla dpingvifya ilaiagiiil lqrkvwplii aallcviawy flqhwqvpwy
       61 iflaafvpva aflrkpktvt iaagifslla tvgiinmeyq typdiasldp rpvakemsye
      121 efshtnsgaa ivhvdlpgtt shfsarqata yippaywtdh tlpvivllhg npggpeqwfg
      181 sgeaaetadq fqaanggrsp ivvavdatgs etanpicads tqakvmtyls qdvpqvikqk
      241 fkvnpdqrtw tvgglsyggt cslqiatnrp eaygsiidis geaeptignh aatvkkffag
      301 desafndqdp ahllahkhys aqaifiagdk daasvnalrs lsdaarnagm ktyfstrpgg
      361 hsfqvwrpal resfawaarr ggmtaikdpf dgigandvrs
//
LOCUS       WP_284869389             847 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium sp. MSK073].
ACCESSION   WP_284869389
VERSION     WP_284869389.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK073
  ORGANISM  Corynebacterium sp. MSK073
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 847)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Corynebacterium sp. MSK073"
                     /db_xref="taxon:3050198"
     Protein         1..847
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=95057
     Region          19..841
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mnlsqqlpdl tevpeslide aiwdtfnswt tskginlypa qeeallgila rdnvilatpt
       61 gsgksmvana ahfialarrq rsfytapika lvsekffalc eifgaenvgm mtgdatvngn
      121 apiiaataei vanialrdga eanidqvvmd efhyysdpdr gwawqvplle lpkaqfllms
      181 atlgdtdwlq edltrrtgre tnlvagstrp vpldfsyvfs avhetieell ahnkapiyvv
      241 hfsqreaaer aqaltslsgi iskeekenia eeiggfrftt afgkdlskll rkgigihhag
      301 mlpkyrrlve rlaqrgllkv icgtdtlgvg invpirtvlm tglakfdgqr qrilksrefh
      361 qiagragrag ydtegtvvve apeheienak arrrigddpk rlkklkkksa regevswsek
      421 tfarlteaep eqltsqfrvs ssmllnvlar hgdgyahmrh llrdnhdprs kqnkdiltal
      481 dlfrglvdsg vvqkstkgld iygrpyhlvr elprdfalnq plgpfalaal slldpeaesy
      541 hldvisvfea ilddprqvlq aqqkkrrgee iaalkadgvd ytdrmnived itwpkpleel
      601 leqaydtfae tnawvkefel rpksvvrdmv enamtfsdlv atyglarseg vilryltdaw
      661 rtlkqsipde yttpqiedii iwlgelirqv dsslvdewaq mvgedspidq dtldrelafg
      721 vedptaltan rrafgimvrn ymfrlaqlfa leeedrlaev ldyldevpdf gavlddyfde
      781 yddidtgpea rgpeyfrlee sssrswpvrq iikdpagdra yqfvatvdld asdeagevrl
      841 selrvey
//
LOCUS       WP_284869392             764 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: RelA/SpoT family protein [unclassified
            Corynebacterium].
ACCESSION   WP_284869392
VERSION     WP_284869392.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..764
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=84300
     Region          33..764
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 matdksakrq anngmrsmsa rlarsltggr vkinpaldpl msihrkfhpk adaellnaay
       61 ntaerlhegv frksgepyit hplavatiaa eigmdtttiv aallhdtved tdytledltr
      121 dfgpevarlv dgvtkldkva lgaaaeaeti rkmivamand prvlvikvsd rlhnmrtmrf
      181 lppekqakka rqtleviapl ahrlgmasvk weledlsfai lypkkydeiv rmvaerapsr
      241 dralkeiinq vsaalkengi eaevmgrpkh ywsiyqkmvv rgrefaeifd lvgirvlvdd
      301 inscyaaigv vhsiyqalpg rfkdyvsspr fgvyqslhtt vladggatle vqvrthemhy
      361 naefgvaahw ryketkgkns ghqeevdqma wmrqlldwqk eaadpnefld slrydltarq
      421 ifaftpkgdv vdlpagstpv dfayavhtev ghrcigakvn gklvalespl ksgdkveift
      481 skdpnagpsr dwqeflvspr akakvrqwfa kerreehlea grdalasevq rgglpmhrlf
      541 tassmkqvae qlhysdvdal ytaigaghvs aqhvanqlva mfgdrddavd alasrtplse
      601 leqsraqhtk dsasgtgilv egspdvmakl akccqpvpgd aifgfvtrgg gvsvhradca
      661 naeklksepe rmlkvewssg tsstgafsat lqlealdrqg llseltrvls dqninvltmn
      721 snrgedqiat mrftfsvsdt kqlgslmttl rntegvfdvy rvta
//
LOCUS       WP_284869493             263 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Enterococcus faecalis].
ACCESSION   WP_284869493
VERSION     WP_284869493.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..263
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29340
     Region          4..260
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 maflqaniys nvlemevnvn vilpqetvkk vgtstqaalt dipvlyllhg mggnhsvwar
       61 rtsieryvad lgiavimpst dlawytdtqy dmnywtfise elpkichqlf pqlstkrekt
      121 faaglsmggy galklvlakp esfaavasls gavslsstsf gellkvrkrs ywegifgpld
      181 qiegsihdpl yllqqlvesq tempqfylcc geqdmllsan qqmaqaleqa qasytfetgp
      241 gehdwvfwde wiqkalawlp ipk
//
LOCUS       WP_284869552             228 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Enterococcus faecalis].
ACCESSION   WP_284869552
VERSION     WP_284869552.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 228)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..228
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25524
     Region          7..210
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mtesktaiif dmdgvlvdse ayyyerrkaf laefdltieg ltlpelvcad mrslwqkieq
       61 vnkkeldiaf lneqyiaykk ahpidylavl denakrvlqf lkrqgykigl assstkdaie
      121 evltvgqlss yfdavvsged feeskpapdi ylhtlqelav apqeciaied sekgiasake
      181 aglevwamrd ehfgmdqsqa dafltqlsdi ckkisenrid essestps
//
LOCUS       WP_284869689             938 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium sp. MSK073].
ACCESSION   WP_284869689
VERSION     WP_284869689.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK073
  ORGANISM  Corynebacterium sp. MSK073
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Corynebacterium sp. MSK073"
                     /db_xref="taxon:3050198"
     Protein         1..938
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103599
     Region          4..936
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtethldtfa aglpypldef qvqgceaves gqgvlvcapt gagktvvgef avslalsrgt
       61 kcfyttpvka lsnqkyhdlv aehgedavgl ltgdvsinsd aeivvmttev lrnmiyadsp
      121 aldrlthvvm deihfladas rgavweevil nladhvsiig lsatvsnsee fgewlatvrg
      181 dtsvivtehr pvpldqwmml grkiyplfep esggqvnsel erriqrleag dsddaradyk
      241 sgkgfrarar hkgggrsdfh gkaggrsgss rpqdryrplg rpevlkvlqs qdmlpaitfi
      301 fsragcdgal yqclrsrmvl ttqeeaeeik aivdagvegi peedlqvldf rrwrealsrg
      361 faahhagmlp afrhiveelf vrglvravfa tetlalginm partvvlekl ikfngeahvd
      421 ltpgqytqlt gragrrgidt lgnavvqwap amdprfvagl astrtyplis tfapgynmai
      481 nllgmlgfed slrlleksfa qfqadgsvve etreleraeh rvcelreqld davdalappa
      541 kdgedpaevl mdyirlrrel taeekqskvd kehqrtqevv avlarlqlgd viaiagkkrp
      601 tlaavvtpan qtedprpwvt tesgwsgrid atgisnppiq lgrikipkpv rknprrntky
      661 iqdvfrrekf drpkrmkskp rlrpnkrvge lrdairehpa hewpatdreq lagvaqklar
      721 rerdleklqa kvnkatdtlg rtferivdll aemdyvefsg agsdrtpvit eegerlakih
      781 sesdllvaqc lkrgiwdeld paelagvasl ccfenrkatg gqpeaatdrm adamnatwri
      841 ytelsaderr hrlpptrepe agfalaihqw sagaplgycm aaaneagael tpgdfvrwcr
      901 qvvdllqqia ktgydgqiqr narraidaiq rgvvaiga
//
LOCUS       WP_284869758             344 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium sp. MSK073].
ACCESSION   WP_284869758
VERSION     WP_284869758.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK073
  ORGANISM  Corynebacterium sp. MSK073
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Corynebacterium sp. MSK073"
                     /db_xref="taxon:3050198"
     Protein         1..344
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35249
     Region          13..344
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mttinsilqa qqrrqhvrvl astlvfglia laaylvllgq gplelsprqv ldvltgggse
       61 shirvvwdlr lpvaiatviv gaalgvagsw tqtmarnpla spdilgvtgg asvlvvlgtv
      121 hsrpgfadgi pdfwwracla mcgallvvil lavlggigts nrivivgial slmfqaivay
      181 lmrsaqiqra aeaqtwlags tgfvrmeviv pllvalapfl aigiwcarel pllahddssa
      241 ttlgvnitrq rallliaatg icavvvsvvg pigfiallap hlarmvahtp tpspvasaaa
      301 gaalltvcav iagaipvnap vgavssvigg calvvlvwna arrt
//
LOCUS       WP_284869764             575 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Corynebacterium sp. MSK073].
ACCESSION   WP_284869764
VERSION     WP_284869764.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK073
  ORGANISM  Corynebacterium sp. MSK073
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 575)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 575)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 575)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 575)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Corynebacterium sp. MSK073"
                     /db_xref="taxon:3050198"
     Protein         1..575
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=62826
     Region          26..568
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mksllsirtm mksplniivv calmyfiitf liwpnitmll qvfrpdgewt ldvfdkllss
       61 eramkslrns fllaislait vnvigifivl atrffdikgs kilyvgfatt liyggvilvs
      121 gynliygpng fltnvmlkvf pgmdanwfrg mpavvllmtf sgtgshllfm gnsiskidqq
      181 tieaakqmga stwkilmtvv lpvikpmifa ttvlvflggl samtaplilg gddfqtissm
      241 iltfsrtkgs qdlaatlami lgvatllvlt vlnkverggt yfsvskvpvs lekqkienpv
      301 vnavvhvtaw slwvvyiipp ilivlfsftn asaiaqgtis fsdltlsnyv qiftskeain
      361 pfvvsivysa icsfivvfal lfvariiqry rnvatalley llhipwvlpg tlialgllit
      421 fsepqpliag kvlsgtvyil aigyivekip ftfrilkasf sgvpanveea asilgasdlr
      481 ifrkilfplv ipvataiaal nfnsllgnyd taiflahpfh qplgifiyna tstdtmndtt
      541 vltfvysvll miissvvlyl vygrssksvt knkti
//
LOCUS       WP_284869808             566 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alkaline phosphatase D family protein [unclassified
            Corynebacterium].
ACCESSION   WP_284869808
VERSION     WP_284869808.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..566
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62889
     Region          15..537
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mtsrnhsmqs emshvnrrkf lqtsgtvgaa laltttasta nastahaqss lssrpephmv
       61 eptlgerpfl hgvasgdpip dsvvlwtrvt pdadampgsg agapttvewe iardeefrdi
      121 vkrgevttdp aqdhtvhvdp hglepesvyy frfraqdkis pvgrtktapa vtaspeeltf
      181 gvascanwes gffqaygdia qrgragqldy mvflgdyiye ypqreyagfg pvrlhhpahe
      241 ittledyrtr lgryrtdenl qaahaalpwi avwddhetad nswrdgahnh tegkegawid
      301 rrnaamqayf ewmpvrasnp sdnghlyrcl tfgdlveltm mdlrtyrdkq ilfgparmaa
      361 egrsmlgseq ydwlvnkidt saaawnmlgn svmfspmnla tlqrddklap vssslssnit
      421 gipvngdqwd gysaerrmli dalakhdsha lfvtgdihse wahniskdgr ifgaemvcss
      481 isapnvneql hlpednglst laeryllean phtrhvnldh hgysyvtirp dsaemhwlrv
      541 edllnptaav neaitltwrp degfss
//
LOCUS       WP_284869902             725 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Corynebacterium sp. MSK073].
ACCESSION   WP_284869902
VERSION     WP_284869902.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK073
  ORGANISM  Corynebacterium sp. MSK073
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 725)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 725)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Corynebacterium sp. MSK073"
                     /db_xref="taxon:3050198"
     Protein         1..725
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=79691
     Region          2..718
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 msaieaeqny vdglfdrldd evaaanarln evqaevdpat pdadalvrre teyhglqakl
       61 drlnvaqmgl vfgrididap gdnpteegld rryigrmgld areenyrtll ldwrapmarp
      121 fylattaqpe gvhtrrqirm sgrtvtdvnd ealdgpgvre eeagvasesa lyfamqrart
      181 ghmtsiveti qreqdeiird ntrgvmvveg gpgtgktava lhrvayllyt hrellsstgv
      241 livgpntnfl dyisrvlpel getgvvlsti gglfpgitpt hteglvgrei kgsaamaeil
      301 saavkdyqqv pneprditvd gltltitpsm vkrartrarr srkphnqare afiehfvedl
      361 aqematkvgt dplggenlls radvdqfhdd laidesvvgc iddfwpeldp sevlaallss
      421 reriasaarg ydeetqaaly radgyawtds daalldelav liglpnpeek kaakdaewre
      481 qiadaegald ilsssestdn dddmfeaeil sahdvidaet laqrqevrdt rttaqrared
      541 htwafghiiv deaqeltpme wrmlfrrcps rwmtlvgdts qtgspagvdd wgedlepfia
      601 qrfrhhlltv nyrtpepite langllasid pdatpaiair dgepvrrlad adftpgitte
      661 ddgrltavid stnaeavkgl efdhvivlhp reivdaspqg lqnlyvcitr atqtltlvgd
      721 tagvl
//
LOCUS       WP_284869950             167 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium sp.
            MSK073].
ACCESSION   WP_284869950
VERSION     WP_284869950.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK073
  ORGANISM  Corynebacterium sp. MSK073
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Corynebacterium sp. MSK073"
                     /db_xref="taxon:3050198"
     Protein         1..167
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18889
     Region          1..>37
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mddhldqllt iaeaarltgv akstitrart rgefpraqqk qdtwyipigd linsgrldti
       61 thttpetpts atstqdhqtl vhalelekqr ahyaeqqlhq aqqliqakqd tidalkttih
      121 alentphkql tttphqenth pkpetepknp pierrsplqr lsqwikk
//
LOCUS       WP_284870018             209 aa            linear   BCT 25-DEC-2024
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Enterococcus
            faecalis].
ACCESSION   WP_284870018
VERSION     WP_284870018.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10061503
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..209
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23188
     Region          167..208
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
ORIGIN      
        1 mskkdkkknq arepweqsiy epdqngggsr lakrqqqrgn slfltvlvil llliiaipig
       61 tflwmmqdkk pnesasknsq pssslvqsss kekkkestsk svessepass qpaenttpss
      121 sdaaaqqqqd qqaqqqqqqq qqehqqqqea qnqqqqqaqn qqpvydtvqs gegarqvaer
      181 ngmtleqila lnpgidtsvf ypgqplrik
//
LOCUS       WP_284870029             497 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Corynebacterium sp. MSK019].
ACCESSION   WP_284870029
VERSION     WP_284870029.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK019
  ORGANISM  Corynebacterium sp. MSK019
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Corynebacterium sp. MSK019"
                     /db_xref="taxon:3050190"
     Protein         1..497
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53306
     Region          181..458
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mnsvngnkki drrsvlrlga vagagavava vnsvgtrava saapnqspfp ftgltsglvv
       61 tdlevvtvtd tsvtfswaty agphpawgkl aplapadtev alvpvdadeg gelpvvhkde
      121 tqvgyhfvtv dklrpgttyr fecrsnglva epglitrnlp napeqtgqft tlvapegeyl
      181 ttiailndah igenghgiit gdfpapvfse pgaapypevm ltaalaelrg mgiekvfvng
      241 datsearpae vrrfaeimnt fgaqerqwfv trgnhdrphk pdadpsagyd efpvlegten
      301 hrdpfgvllg rprqelwvtq qgpvrvigld sskldesgge ispeqfdale relqrdpskp
      361 tvvlahhpit seagwthaag ptfilnsada rrlqqmlnda pgvffagagh thrakrtrgd
      421 vgagvdylet gackaypggy tllhvysggy qvnfhrlsse dalawtarar wamygfepea
      481 llgelsdrny vvnrvia
//
LOCUS       WP_284870120             592 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 35 protein [Enterococcus faecalis].
ACCESSION   WP_284870120
VERSION     WP_284870120.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 592)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 592)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..592
                     /product="glycoside hydrolase family 35 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=67325
     Region          9..328
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
ORIGIN      
        1 mqtfeikedf llngqpikii sgaihyfrmt psqwedslyn lkalgantve tyipwnihep
       61 eegvyvfegm knieafvrla eklnllvilr psayicaewe fgglpawllk ekdvrlrstd
      121 pifmtkvrny fqvllpklap lqitqggpvi mmqveneygs ygmekaylrq tkqimeelgi
      181 evplftsdga weevldagtl ieedvfvtgn fgshskenaa vlkkfmtrhg kkwplmcmey
      241 wdgwfnrwge pviqregtdl akevkdmlav gslnlymfhg gtnfgfyngc sargakdlpq
      301 vtsydydall teagepteky yavqkaikev cpevwqaqpr tkklgnlgsf pvtasvslfa
      361 vkdqmmtpkt tayplsmeea gssygyllys fdlknyhhen klkvveasdr lhiyvdgdla
      421 atqyqetvge ellisgqtek dtlaldilve nlgrvnygfk lnnptqskgi rggvmqdihf
      481 hqgyqhyplt fsqeqlakid ytagknplqp sfyqvtfele qladtyidcr gygkgfvvvn
      541 ghhlgrywei gpihslycpk eflqqgqnev vifetegiei eylkftnqvi id
//
LOCUS       WP_284870127             323 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium sp. MSK019].
ACCESSION   WP_284870127
VERSION     WP_284870127.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK019
  ORGANISM  Corynebacterium sp. MSK019
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Corynebacterium sp. MSK019"
                     /db_xref="taxon:3050190"
     Protein         1..323
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=35729
     Region          3..323
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mnsakstyvp eltsiraiga fgvllthaaf wtgnytgdww grlngrfeig vtiffvlsav
       61 lltgrwlgsp ddvpanrpdl rkyftsrakr vlpaywivvt aaflihaadd pppsggglqg
      121 wlrtmsftqt lqfgwihpgl pqmwsmvvev gfylvlplvg lgiwtitkgr lrpgptlaii
      181 igfgligpvw tvlshqegll pvvarlwpma yfdwfaigml laygrkvgwr vnlaaswlia
      241 lvlfflsttt hvgpatlvpd dvdqalwktt lyglsagafv apialgtevr wlrhpamiwl
      301 gevsyefflv hvlvmdwvmt lmg
//
LOCUS       WP_284870174             475 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Corynebacterium
            sp. MSK019].
ACCESSION   WP_284870174
VERSION     WP_284870174.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK019
  ORGANISM  Corynebacterium sp. MSK019
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Corynebacterium sp. MSK019"
                     /db_xref="taxon:3050190"
     Protein         1..475
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49523
     Region          1..448
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mesfsdfasa adsfiwspyl lipaligtgi iltirlgaih lvklgpalrl glidrnddda
       61 egditnyqal atalaatvgv gnivgvatai glggpgalfw mwvtgllgma skyseaflgv
      121 kyrqtdaage qsggpqyylr kaipngfgkt lgilfavfaa laafgignlt qgnavasnle
      181 nsfdidptls gmimfilvga almggiksig ritagfvpmm ivlyigaavw vlvanvsalp
      241 etfkliftda ftgtaavggf agstlilalq mgvarglfsn esglgsgaia aaaastthpv
      301 rqglvsmtqt fidtiivvsf tglviistgv wqdgnvdtga ltaeafsrgl pghwggtivt
      361 lsvvffafst mlgwsyyger afeslvgrrg tglyravftc vvfvgavtql etvwsvasal
      421 nglmalpnli glivlsglia retkaylefd pqlrataaei dkwqsqqdfe afskn
//
LOCUS       WP_284870249             343 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium sp.
            MSK019].
ACCESSION   WP_284870249
VERSION     WP_284870249.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK019
  ORGANISM  Corynebacterium sp. MSK019
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Corynebacterium sp. MSK019"
                     /db_xref="taxon:3050190"
     Protein         1..343
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37558
     Region          18..338
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtvhaareld agvsvdella vvpyfsqhrs mteaatelai pfariraive qiadidqpgl
       61 lgvrafevdy rnsfdvrirp qatvlsqpra ltaeetatll liletiedsa attsskaaqt
      121 aatklrsalg invpiidsta aengkafsfs eqiysalhqr kvlkvryrna sgqitvreld
      181 cvnvytvest tylravdraq edrrqksfrv drleaaevld tpagfhrpep vdirdphafg
      241 aetgtsewas vlidadatwi adyepvffte degeeedtel vsdqglgqse yvadvpmsdl
      301 aatvsfvlrr spsvtvaepl klknavvara realaeygrn dka
//
LOCUS       WP_284870383             392 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Corynebacterium sp.
            MSK019].
ACCESSION   WP_284870383
VERSION     WP_284870383.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK019
  ORGANISM  Corynebacterium sp. MSK019
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Corynebacterium sp. MSK019"
                     /db_xref="taxon:3050190"
     Protein         1..392
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41575
     Region          12..391
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mtnadankpn eriflslatv teaeeqavvr alhsgwvapl gpevdafeae iakrcgvehs
       61 lalssgtagl hlallalgig egdyipvstm tfaattnaia yvgatpvfvd aaedgnidpe
      121 lllrtvddll aegksvpavm ivdlfgrcad ypafaprlee lgialiedaa ealgasvdgq
      181 pagsfgraaa lsfngnkimt tsgggmllsn dadliarary lstqarqpva wyehteigyn
      241 yrlsnllaal graqhsrldd miarrrqird ayldllasld ddapgkgtrl lsdsderfte
      301 ncwltsivlp qeavdkgvls pdsviaalge aniearhlwk pmhlqpvyeg aratingtae
      361 nlfsrgitlp sgpalddddv arvigvlkev lg
//
LOCUS       WP_284870412             863 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium sp.
            MSK019].
ACCESSION   WP_284870412
VERSION     WP_284870412.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK019
  ORGANISM  Corynebacterium sp. MSK019
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 863)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 863)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 863)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 863)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..863
                     /organism="Corynebacterium sp. MSK019"
                     /db_xref="taxon:3050190"
     Protein         1..863
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=94872
     Region          59..839
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msdtgefdfs ldnrveqaiv dakvaarkal prsrqdidee sahqrlahrr gqsntafali
       61 lenlenaesa eraehvlesf pdvtasvvyk pgrawitapd tidpnqfiea lreigvesyl
      121 trstlrrrat rldvsqhrrp avpvaaqqne eerirrreaa lrrsgggsev lftarelvtk
      181 qrfwgslfls ipvlvtslnv nwqfpgwqwm clvlttivvw wggwpfhram aaslrrrmsa
      241 ldgassiail lawlwslaql ifgpagqigy ttaptwfafn yresasaevf fdvacgltvl
      301 lltgrmftry nkvrtgqilr nlripaernv tvvrksaksa epkrvevtva elnigddivv
      361 pphsvipvdg sviggastmd aqllgigvep qkvkvnskvw againldsel kvrvertgfk
      421 trassiarwl rqavreetvm hqtavhsase lvpwtlslag vafcgwwlat gtmsgalava
      481 lamlsgiapv alamststvq rigilagasn gilirgnetf rnlaaadvvi fnrvgtlteg
      541 dthvlgvaae rnenpdlvlr vagalmmesn hpasaaivra crasrdagsg ggevphwiet
      601 vhvaiaedga fvgqveipvk dsddklemrf vegrvwrprd ltalsekmav aalsggtpmv
      661 vswrgkvrgv itigedikpd avesidqled mgvdtmmitr dpypvarrfa drlnisrvfa
      721 giiasrkaia vrsvhsdget vvmvgdkdir dslraadvgv lmdntegnqn ldvdyadvva
      781 lrnnvlsipe aieiaravvr mmdsniyfaw fynvavillg mtgmihplla sllmifsslw
      841 idwrsrrvss rrkhlfrvkl grw
//
LOCUS       WP_284870499             839 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [unclassified
            Corynebacterium].
ACCESSION   WP_284870499
VERSION     WP_284870499.1
KEYWORDS    RefSeq.
SOURCE      unclassified Corynebacterium
  ORGANISM  unclassified Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 839)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 839)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..839
                     /organism="unclassified Corynebacterium"
                     /db_xref="taxon:2624378"
     Protein         1..839
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=93390
     Region          14..832
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mlpdlaevpe slfddaimds fiawtrdqgi tlypaqeeaa iglaggdhvi latptgsgks
       61 mvaiaahfca largqrsfyt apikalvsek ffalcevfga envgmmtgda tvnggapiic
      121 ataeivania lrdgadadid qvvmdefhfy adpdrgwawq vpllelsrcq fllmsatlgd
      181 tqkfetdlke rtgldvnlvt gttrpvpldf hyvytpvhdt laellesgka piyivffsqr
      241 qaaeqaqalt glklltkeek erireeigdf rfttafgrvl sklvrqgigv hhagmlpkyr
      301 rlverlsqtg llkvicgtdt lgvginvpir tvlitglakf dgrrsrilks refhqiagra
      361 gragydtegt vvveapehei enaklrrrag qdeaklkklr lksvpkgevt wsektfdkiv
      421 sqppepltsr favtngmlln viarggdtye hmrhllrtnh dtrhqqneai ltaielyrgl
      481 vnagivvthg egddcrpelt melqrdfaln qplspfaiaa lelldkdspn yaldvisvfe
      541 siledprpll iaqqkkarge eiaalkaegv dytermnive ditwpmplad elegafdtya
      601 qghpwvrefs lspksvvrem vekamtfsdv vseygiarse giflryltda wrtlrhtlpp
      661 eaaneelrdi vewlgelvvq vdnslvdewa qmadpdkpld eetlkeaafg tdesrpltgn
      721 eraftrmvrn lmfrhvqlfa fekeeeladl dnylddapdw paamddyfde yddlgidaka
      781 rggdmisidr kageglwhvi qilddpegdh gwrfeagvdl aasdeygevr laslriiqg
//
LOCUS       WP_284870476             352 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Enterococcus
            faecalis].
ACCESSION   WP_284870476
VERSION     WP_284870476.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..352
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=38957
     Region          30..345
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mlftddnyls dvervlektp dwtkvtnksv fitgasgmig tflidvlmyq nktrnanisi
       61 wamgrtlsrl eerftsyled plfhivigdv teeiqvaeac dyvlhcasnt hpksyasdpi
      121 gtimtniagt qhildyavka nsekvlflst veiygenrgd vdkftedycg yidcntlrag
      181 ypegkrases lcqayiqkyg idvviprisr tfgptmllsd skassqfimn avhkenivlk
      241 sagsqlysya yvadiasall fllvkgqtge aynvsnehcd itlrtfaetl anvagtkvih
      301 geataqekqg fskatkalld nqkiyalgwr plfdsmeepl khtikilegs gn
//
LOCUS       WP_284870522             736 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium sp.
            MSK019].
ACCESSION   WP_284870522
VERSION     WP_284870522.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK019
  ORGANISM  Corynebacterium sp. MSK019
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 736)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Corynebacterium sp. MSK019"
                     /db_xref="taxon:3050190"
     Protein         1..736
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76925
     Region          8..725
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msdqqlltld ipvggmtcas canriqrkln kldgvnasvn yatekahvea padinpqqli
       61 dtivaagyta elpreetaee pgaapeekdr elqdlrnrvv gaviltvpvi amsmipalqf
      121 tnwqwlcltl sapvfvwagw pfhratlknl rhgevtmdtl itmgttasfl wsvgalffgr
      181 aglpglkhef hltvtpgdad mniyleamag iimfvllgry fekrskrnag qalrelmklg
      241 akevsvless gvekrlpveq lrpgvvfvvr pgekiatdgv vvegtsavda smltgepmpv
      301 evgpgdevtg atintsgrll vratrvgset qlaqmaamve aaqtgkapvq rladrvsgvf
      361 vpaviaiaav tlgawlltgh gaseavtaav avliiacpca lglatptall vgtsegakag
      421 vllrgpevle sarkvdtvvl dktgtvttgv meltevpptp enllplaasv eaashhpiaq
      481 aivraadpds llpvsdfrdi pgvgvegtvd ghrievgrsg ensgsggtvv avrrdgellg
      541 tlevsdsvkp tsaaavakfr ewgvrpillt gdaagpafrv adevgiared visgvmpedk
      601 vatieklqag gacvamvgdg indaaalaqa dlgmamgtgt dvameaadit lvrgdllaaa
      661 dalrlsrrtl rtirsnlfwa ffynvlaipv aalgllnpml agaamafssv fvvgnslrlr
      721 gfspsqpaiq kgvthe
//
LOCUS       WP_284870676             242 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Corynebacterium
            sp. MSK008].
ACCESSION   WP_284870676
VERSION     WP_284870676.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..242
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26540
     Region          6..222
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mnnkwyslfk vilgppllvw nrptidgaeh ipeegaailv snhqavldsf ylplmvrrqi
       61 tfpakkeyft spglsgriqk fffssvgqip vdraskdagd alqnaaesvl dkgdlfgiyp
      121 egtrspdgrv ykgrtgmarv amatgapvvl igmigsgkan pigtkiprpv kvrikvseqi
      181 hphawaaeng fdpasrevmr pftdycmrrl aemvgedyvd vyasdvkksl aetgeypeea
      241 rp
//
LOCUS       WP_284870719             480 aa            linear   BCT 25-DEC-2024
DEFINITION  RecQ family ATP-dependent DNA helicase [Enterococcus faecalis].
ACCESSION   WP_284870719
VERSION     WP_284870719.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Larsen,N.B. and Hickson,I.D.
  TITLE     RecQ Helicases: Conserved Guardians of Genomic Integrity
  JOURNAL   Adv Exp Med Biol 767, 161-184 (2013)
   PUBMED   23161011
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Rezazadeh,S.
  TITLE     RecQ helicases; at the crossroad of genome replication, repair, and
            recombination
  JOURNAL   Mol Biol Rep 39 (4), 4527-4543 (2012)
   PUBMED   21947842
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Bernstein,K.A., Gangloff,S. and Rothstein,R.
  TITLE     The RecQ DNA helicases in DNA repair
  JOURNAL   Annu Rev Genet 44, 393-417 (2010)
   PUBMED   21047263
REFERENCE   5  (residues 1 to 480)
  AUTHORS   Chu,W.K. and Hickson,I.D.
  TITLE     RecQ helicases: multifunctional genome caretakers
  JOURNAL   Nat Rev Cancer 9 (9), 644-654 (2009)
   PUBMED   19657341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..480
                     /product="RecQ family ATP-dependent DNA helicase"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0043138 - 3'-5' DNA helicase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=55017
     Region          1..443
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
ORIGIN      
        1 mlltleqelf trfgyaafkp gqkevitnll dgmntlavlp tgtgkslcyq fvgqkleglt
       61 vivspllslm edqvrqlqrq gikgavalns tlqysekryi lakmfqydyl flspemllqq
      121 evlsvlqrqk ialfvvdeah cvyqwgvdfr peyskldlvq kqldfpltla ltatatpvvq
      181 haiikqlfsh gsyqevlssv nrkniglfvk etlekeevll dylsktagki iiycamrnkt
      241 eqisqliqak tsfkvayyhg gleasersrl qeqfidnqid ilcatnafgm gidkpdvrgv
      301 ihfdlpdsle nylqeigrag rdgqkswall lykkgdefih rffleetran ratlkslieg
      361 eeqagllena telqqkwvqg ylakdysfee lehrleekek drqaqlrgml tyietttcrr
      421 tliqtyfqep ivkqspetcc dncalffdiy qdsivksnkt snqneggwrs kflklfkerd
//
LOCUS       WP_284870742             267 aa            linear   BCT 25-DEC-2024
DEFINITION  inositol monophosphatase family protein [Corynebacterium sp.
            MSK008].
ACCESSION   WP_284870742
VERSION     WP_284870742.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..267
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=27415
     Region          33..258
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mtdvtgnlea aeaavdaare ifvnelgaap alhkgsgdfa taadlaveel lrdkltgatg
       61 igvygeeqgg eldahacwvv dpidgtsnys tgnpncailv sllverqpvv avvdaplldm
      121 rmtavdgepa hlngtalppv seassaphvg vgslfsrdrr rmpsnqrldl ageltrahlr
      181 prisgsvgid lafaaqgiyq aavsfsphvw dnsagillar sagavatagd gtpwepgkvg
      241 avvgtakaha avmeairrvr vdageed
//
LOCUS       WP_284870859            1037 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Corynebacterium sp. MSK008].
ACCESSION   WP_284870859
VERSION     WP_284870859.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..1037
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=111478
     Region          139..279
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          464..980
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 msvkntaprs srsstrrptg gtryggpvsm thpttssnva aetadervgs aykvvghsls
       61 aaargvgsff rrdkdesdyd dtatrsprrs rgdwddewed dfempeerte ssakderrsr
      121 elrresrsvg hstfethada wglvliglaa viggsvwfdv agpvgevist gthwligaga
      181 lilpvilvgi aialmlnvrt sdavrarvtl gfsiiaigml glihvfagnp asweerklag
      241 galgaftggv laagfssfva ipllglvily galkatgitv reaydyikdl vtrmlsntdt
      301 pdnedqdpys hvaedlddia egrerrttra asrrsrgrta dterpdrpar ptrrpslrrp
      361 tpmesypadg ddeldlfdfa devedsfeqp aaepadsaet avvqrpaaat apapkpaapk
      421 paapkppqrd netkvlqrea pegerreata pdtvassreq makaiaarsg idaskipatt
      481 pkseteqpap kqvrkipqgd yhlpstdlll agnapktrte andrmieait dvfeefkvna
      541 qvtgfsrgpt vtryevelgp gvkvskitnl qsnlayavat dnvrlltpip gksavgievp
      601 nadremvrlr dvldspkvsa qddpmliglg kdiegdfias siqkmphllv agstgsgksa
      661 fvnsmlisll tratpeevrl ilvdpkmvel tpyegiphli tpiitqpkka saalqwlvee
      721 meqrymdmks arvrhikdfn rkvrsgelta ppgseremrp ypfivcvvde ladlmmtapk
      781 eieesivrit qkaraagihl vlatqrpsvd vvtgliktnv psrlafatss ltdsrvildq
      841 ggaekligmg dglfipqgag kpqrlqgafv sdeeiqavve aakaqqdepd yvegvtedkq
      901 aeakvidddi gkdmddllea velvvtsqlg stsmlqrklr igfakagrlm dlmesrgvvg
      961 psegskardv lvkpeeleti iwmikgadpa eapkdvsldd gaddadgsgs gadgsdaggd
     1021 sdtrtvtaty nptggaf
//
LOCUS       WP_284871205             253 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium sp. MSK008].
ACCESSION   WP_284871205
VERSION     WP_284871205.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..253
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27722
     Region          2..226
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(16..17,19..20,23..24,62,66..67,70..71,101,105,112,
                     115..116,121,137,141..142,144..146,148..149,152..153,
                     156..157,177..178,180..182,184..186,188..189,191..192,196,
                     199..200,206,208)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(140,144,147..148,150..151,191,194..195,197..202,
                     205..207,211,213)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(161..168,179,182..183,186)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mnllreinpv trilglvllt tplmftidwv satfvlaftl lmvpvcglgy grffkralpi
       61 lliaplagip malygqagge tylewglvhv telsvslawa vvlrvlaial pvvllsadvd
      121 ptdlgdglaq vlhlperfvi gtvaalrmlt llrddldamr rsrrargiad qgkikywfsl
      181 sfgllvmslr ragklatame argfdgprkr swaresklhs rdwtvmavcl avalaalala
      241 wstgylrpvw avr
//
LOCUS       WP_284871367             574 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Corynebacterium sp. MSK008].
ACCESSION   WP_284871367
VERSION     WP_284871367.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..574
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=61285
     Region          6..450
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          508..573
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(531,540..542,549)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            541
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mtlsavlian rgeiavriar tardlgirsi avysepdtga lhtqvadeay llpgntsaet
       61 ymnipaliei ahragadclh pgygflsena dfartveeag lkwigpspea iellgdklsa
      121 ralaveagap lapgtgepls tweeardfas ehgmpiaika afggggrglk vvfdeadiee
      181 gfasagreak eafgrgecyv ekflthprhv eaqvladahg nvavlgtrdc stqrrfqkli
      241 eeapapfltd eqrtaieega reiirkanyq sagtveyivs edgtvsflev ntrvqvehpv
      301 teaitgvdii aeqfriadgl plsfgdadpq ihghafefri naedvtngfa pspgtvtrfd
      361 vptgpgvrid tgvrtggqip pyydslmgkl vvwgpdrdta lkrakqalse fviegvrtvl
      421 pfhrdmvdap eitgdsldvy tdwvdhnysp sqkhsdvdie hiyderrdvv ieidgrlhti
      481 gfpvallggg aapaaadaaa psgdeagavt skyeativew lvadgdvvsk gdaiatveam
      541 kmesqlkapr dgqislaaqq gervkanati atis
//
LOCUS       WP_284871410             458 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium sp. MSK008].
ACCESSION   WP_284871410
VERSION     WP_284871410.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..458
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50055
     Region          152..457
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mpysvltaps kkplkrqlva vvmaastigi alssvliyfv mryflfdrad dqlregmatw
       61 aqqtpawqfn ilslpsefnq atlypgydql vprrgsvnpp dyskverldq pttipsvddk
      121 gqgvkwrama hqqsdgtvqy vaksleteak mlralawvea gvgvlalfgi gvaanymvar
      181 alaplkiven talaianget dsrvpawpre tevgslsyam ntmvsklqds ldnartqeeq
      241 mrrfvgdash elrtpltsvr gytelyrkgm andpdmvlgk ideesarmql lvedllaltr
      301 aegarlekkp mdvlewvlsa kstvdaafpd rsvevikdtp ditqvngdpd rlhqvlvnli
      361 tnaykhagpd aevtvtirkn ldrvvidvad ngcgmeakda ehiferfyra dssrnratgg
      421 sglglaitks lieahggtvk vttapgegst ftislpal
//
LOCUS       WP_284871487             489 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Corynebacterium sp.
            MSK008].
ACCESSION   WP_284871487
VERSION     WP_284871487.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..489
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=54759
     Region          105..488
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mnldlswwqf aamvvdyaik fvmigvvpgg rkpssanawl llilllpvvg lplyllfgst
       61 fvsrrrhriq vearrvldga wagpdstiah lppetaslvr lnreltgypa vrgdvralwa
      121 dyrktmlria klideasati sieiyavawd dttdvvfqal eravargvhv rllfdhigsa
      181 kypgfrklkk rltdigvdwh mmlplaplrg rwrrpdlrnh rkvvvidsev afvgsfnlid
      241 rgylmpghvr agrqwvdafv elegpivesv esmfavdwyt esgenldivv garnegeaep
      301 stgdvlqlvp sgpgyltepn lrmfnsivhn akeqltlcsp yfvpeeslle aitsacyrgv
      361 rvdlfvgeka dqfmvqhaqs syyeallkag vriwefpapy vlhtkfvlad pgsedavgvl
      421 gssnmdirsf slnyessllv asgallpale qlganyqavs reltlerwar rpwyrryvdn
      481 vmkltsalq
//
LOCUS       WP_284871543             220 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium sp. MSK008].
ACCESSION   WP_284871543
VERSION     WP_284871543.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 220)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13031065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..220
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24443
     Region          71..209
                     /region_name="SpoU-like"
                     /note="SAM-dependent rRNA or tRNA methylase related to
                     SpoU; cd18096"
                     /db_xref="CDD:349969"
     Site            order(144,146,166..169,172,186..187,189,195..196,198,201)
                     /site_type="other"
                     /note="putative SAM binding site [chemical binding]"
                     /db_xref="CDD:349969"
ORIGIN      
        1 msdssngelr gptewnegrh gvgpwegewp ddprldpefl rdgdrrnvvd ayrywsldav
       61 vadldqrrhp fhvaienfen dmnigtvvrt anaflarevh ivgrkrwnrr gamvtdryqh
      121 irhhetvagl mewaaaedip vvaidntpgs vpletaelpr ecvllfgqeg pgvteaaqka
      181 svmtcsiaqf gstrsinagv aagiamhawi rqhadlsqaw
//
LOCUS       WP_284871570             807 aa            linear   BCT 25-DEC-2024
DEFINITION  penicillin-binding protein [Corynebacterium sp. MSK008].
ACCESSION   WP_284871570
VERSION     WP_284871570.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..807
                     /product="penicillin-binding protein"
                     /calculated_mol_wt=83733
     Region          28..682
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
     Region          695..746
                     /region_name="PASTA_pknB"
                     /note="PASTA domain of bacterial serine/threonine kinase
                     pknB-like proteins. PknB is a member of a group of related
                     transmembrane sensor kinases present in many gram positive
                     bacteria, which has been shown to regulate cell shape in
                     Mycobacterium tubercolosis; cd06577"
                     /db_xref="CDD:119328"
ORIGIN      
        1 msalkslgsl laalvaaala ialclapiag lggaavartd etmqsnlsdl thgdvpgvtt
       61 indatgtpma wifkqrryev asdgisqhvk dalvatedrr fyqhegvdmq gfaramvtnv
      121 laggveqgas tinqqyvkny lwlidaenee eanaateqsi prklremrma sdldktlekd
      181 evltrylnlv sfgnhafgie aaaltyfdvp arelkpeqaa llvgilqsve alnpytnpeg
      241 atqrrnivln nmaaqgyldq aeadrlagap lgilerpktl pqgcitagdk gfmcdyalry
      301 ladkgldmeq ilngsytitt tldpavqeaa nnavrnnvsp yapgvaevmd virpgadsrd
      361 ilamassrfy gldldqsqti lpqptslvga gagsvfkift aaaaleqgyg lntmletpvr
      421 svlygmgdgg aancppgayc venagtyapr mtlqdalaqs pnttfveliq ktgvapvvdl
      481 avrlglrsya densfgdgrs iaqaakeenm gaftlgplav nalelsnvga tlasggrwce
      541 pnpikevlde hgkqvfidrp aceqavdpev agalshgmak diidgtaavs arnngwsapa
      601 aaktgttesh hstaflgftr smsaapyiyn dgtqstplct qpvrqcqygt lfggneaadt
      661 wfqaaagvpg aatgglppas pvhvrgtkrg aldavvgqys saaksqleaq gyvvtlntvh
      721 gagapagtvv savqdgpnat vtlnvsdgag aasaspsapp ssaaapsspt appppspapp
      781 pgiegleqsl ndardaiadv fgggnpn
//
LOCUS       WP_284871578             232 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium sp. MSK008].
ACCESSION   WP_284871578
VERSION     WP_284871578.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..232
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25084
     Region          45..200
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mdaplrpdra plwlkplvea iadggagipr rllsprvlqk dgadqaavli lfagdprate
       61 lpedarvlit hrtprmrshs gqmafpgghi dpgdggpvna alreaweetg ldpdrvipla
      121 mldaattggs nrrvrpvvaf tpepgevypa seeetdavff vpvrdlvdpr nramlgikew
      181 sgpafwagef lvwgftgvll avvlklggwv rpwdekpgdl raalarsanr er
//
LOCUS       WP_284871581             270 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium sp. MSK008].
ACCESSION   WP_284871581
VERSION     WP_284871581.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..270
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29082
     Region          5..225
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 msankpvaaf fdldktiiat ssafafgkef lnngmitrqe awelyltkaq ymlvgqssek
       61 mdstrdalaq mvagwdvedi qritrdtlre vvapaiyaea reliddhrqa ghhviiisas
      121 aailvepiae elgvdtvvat emavdngklt geitrylkgd akaeavrqfa aehdfdldss
      181 yaysdsatdi pmlelvgnpv avnpdralkk halangwqar tfknpeplfq mpnarevgig
      241 agviagvtal avagvfiara mggkddkrsa
//
LOCUS       WP_284871608             372 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium sp. MSK008].
ACCESSION   WP_284871608
VERSION     WP_284871608.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..372
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39701
     Region          65..362
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mkkiktaala altavslact sapvasaqpa gqegvvkawd artnpplitr tgqaqewvnq
       61 vdhktvlsyn vyspsmrrdi piavvpatda agnrvrnapt lyllngagga eqnqdwlkly
      121 pvkdyfagkg vnvvvpqaga fsyytdwvke dvssdyvngp qkwetfltke lpgpvermlg
      181 angrravtgv smsatsallf aqhnpgmyqa aaafsgcast ssphgynfar vtvnragnpn
      241 fqtvtpemmw gpmngpynry ndallgaekl rgtrlyvssg tglaghpdqv syllgkgapm
      301 paaqlgagvl qveggvieaa vnkcthdlka kldglgipah felrnvgths wpywtedmdr
      361 awhttikpal gv
//
LOCUS       WP_284871642             868 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium sp.
            MSK008].
ACCESSION   WP_284871642
VERSION     WP_284871642.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 868)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 868)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 868)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 868)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..868
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..868
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=93547
     Region          82..862
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mskyegedle klsatgrega kltqlsgeel ddyieaarda areagvdpat arrdldgelv
       61 rpnasyafel rgvedgpqlt eiedalesld gvsarlvypt rmawvtapat mplpqlikti
      121 edfgvtavvt dstlqrrahg rywtehpmpr rakhhrkeea ahllaraqgf iqnktraerr
      181 sgdvlftard lvtpgrlwla vmltipvlll tyvpalgfpg wqwvafaltt pvalwcaspf
      241 hramaggvrr glsaldgass iailasylws famllftdag rigyqssgtw vpldigsgpe
      301 lylevsctvt tllllgrffs mrvrtnllde learrpgads myevthrkkg ggreelpate
      361 imrgddvrvr agqvipvdge vvggsgaigw elvnthaspq lkvgkrvvag svlregdikv
      421 rasrvghttl ltavqrwlee asrhqnaatm vstrsasmli paayaiavld fglwllftgn
      481 intaastala ilvvvapfsl aispalairq gieaavrngv lmrdgnalrv lsqvdtvvfn
      541 rvgtlvlpem hvetvtaagg esselvlria galsadsdhp asraivkaar eardarsgdp
      601 rlpdwievgd diitpdgefg grvtatwgsg ehartqtfda slwrptnlsq lkgklsvaat
      661 tggtpvvvrw dgkdrgvitl fdpakedaiq avdtlesmgv etvmlsrdty pvarrfadfl
      721 gishvlagir sqekpsavra lhtqggivam vgdstvlpvl rvadsgilya gddlygtkap
      781 nwnsicdvvl vrndvmavpq aveharrvnr iadrnlrfag iynaaaiila aagvlppvga
      841 tllmlgssll veyssrrasr frvqglrr
//
LOCUS       WP_284871651             190 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Corynebacterium sp.
            MSK008].
ACCESSION   WP_284871651
VERSION     WP_284871651.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..190
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20466
     Region          44..186
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mrklfaaplc aaallltacs gadndgnfaf hspggqteif yeeadrkpla gfegesltee
       61 gqsislsdfe dqvvvlnawg qwcapcraev ddlqqvhehl qeqnsgtvlg invrdpnpqi
      121 ardfladngv typsiydppf ktaanlggvp ssvipttivl dkqhrpaavf lreitaddll
      181 evidrldgea
//
LOCUS       WP_284871665             115 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium sp. MSK008].
ACCESSION   WP_284871665
VERSION     WP_284871665.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..115
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12427
     Region          25..112
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mkdyvattad tgldccslgs gllstddatr yaalfkvlad pgrlqllsrl aeegcepmsv
       61 seltqrsgls qptvshhlkk lteaglleks rqgrsvihrl rpevfaelra vlqmd
//
LOCUS       WP_284871682             526 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Corynebacterium sp. MSK008].
ACCESSION   WP_284871682
VERSION     WP_284871682.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..526
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55488
     Region          128..517
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mstpvihdsa alsdgdlaka pepgewrrql iglitgvila alvyfffpsg aadtvaqssg
       61 akegveysad tmrivaattv lmgawwmtea iplaatallp iavfplagva pfkdvsspya
      121 satiflfmgg flmalglqrw nlhrrlalmv vkvvgtspkr iilgfmlatg fmsmwvsnta
      181 tavvmlpigt svlmltadtv ggmknqkkfa talmlaiays asigslatli gtppnallkg
      241 ymeeahgivi gfgewmlvgl pvavvftfia wwvlitvfkp evdtipggre lidaelkklg
      301 pwtfpqvavg viflvaalaw ifiplgrsqf gwdfpyddai vgiiagllmf ivpgtsngkr
      361 lldwetanem pwdvlllfgg glslsamfta tglslwigek akglaslpmi llifavaalv
      421 lilteltsnt ataatflpim ggvavgiglt datemnvmll aipvalaatc afmlpvatpp
      481 naiayssgyv tmgemikggv wlnviamvli tlatyfiavp vfglvl
//
LOCUS       WP_284871732             661 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Corynebacterium sp. MSK008].
ACCESSION   WP_284871732
VERSION     WP_284871732.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 661)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 661)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 661)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..661
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..661
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=70808
     Region          <68..245
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mswsvsqkga rvvlalmiav ccclawapva wgqssstavs tvtetssstt stntssaase
       61 gsedskamli ldasssmvea daegtrmesa kkaanelves lpetanmglm ayganesdap
      121 dnrergckdv etlakvgkid kakftsaidg lepkgytpmg nslrkaaeel gdegersiil
      181 vsdgidscap ppvcevakel aedgvdlaih tvgfqvddaa rkelqciaea gngqfleakd
      241 asslatslkf laqrdigkyk vegtpfefad spdsakwlge gqyqtkvtpd snaktdryfr
      301 vsvpegynal iamtpiwqpd ghfedaevvl essaqtnend pncgraktkl spasiagsak
      361 famepywisl aredqldncd msdwlittqi fkrgaelvdd vnvevnvfys pipdaeqake
      421 wsgrsissgk ydgevplgts qeitggtsfn daveisegty adkivpgeyr fykipvtwgq
      481 rpvmkmkvse svtndadsmk ikifdptrie tatrdfsfyd keeesgpvsp aqftmyggdn
      541 phqgyyflhv gmgaksegea tgveqpyefa vmldgepvdg gpdwtptyen gpepsdepik
      601 fdgasgsdee qtveettqaa esteaaedks gglslpllgg lavlllavig avvfllnrnr
      661 a
//
LOCUS       WP_284871770             337 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium sp.
            MSK008].
ACCESSION   WP_284871770
VERSION     WP_284871770.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..337
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36075
     Region          40..309
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mratdiavgv iaaavtaval lstgprdist atehtgdpei ssalehlaen ghrnlaafsy
       61 dggetrfggl gadehtefei gsitktfnae lvrqfieege lsldtqvrel idvpsapisd
      121 vtleellnht sglattesls fkelfmanlr dggnpyrrdt pqdiidaaga aqlkdrgekq
      181 ysnyghallg qllathagvp ydellrtrif epagmtstyv alpgtidgap tglsanghha
      241 gpwdmdgwap agairstaad makyvewvss hgvpnygwgd ldedgqeitf hnggtggfrt
      301 mlvwdperdd dsratfvagd tdawvdrlgv dlmketr
//
LOCUS       WP_284871869             270 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium sp. MSK008].
ACCESSION   WP_284871869
VERSION     WP_284871869.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..270
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28316
     Region          12..266
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mpldfqqpft ertprvvnag klkraqarrk akaflaegen aveaavatga atdlfvteaa
       61 aerfeeivra agymdvytha itdkaadsla davtstgifa vcrpvlwtvp kilkgrpklv
      121 avcvetndpg nagtiiriad avgadavifa gdtvdpeapk vvrstagslf hipvardrdv
      181 rrvigqleda glstfattmd gevnlaqpge tlaqptawlf gneahglsdd ilsaadyras
      241 ipiqggaesl nlataasicl wesskalaev
//
LOCUS       WP_284872003             243 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium sp.
            MSK008].
ACCESSION   WP_284872003
VERSION     WP_284872003.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..243
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25596
     Region          9..225
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 metvethnpa padasrvggd trsqvmsvll krgpvaandi aeeldlsaag vrrhvdklve
       61 eelaepcapr avageeqgrg rpakhfqlta agrerfgshy dglaldavel iqqiggeaav
      121 rdfararvee ilgdvepadd pevtarrvaa alekhgyaps vhrtdagiqi cqhhcpvsav
      181 aaahpefcea ereavarivd thvqplalis dgdgicttni plaaartrtr pagtatkgaa
      241 dhd
//
LOCUS       WP_284872062             442 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium sp.
            MSK008].
ACCESSION   WP_284872062
VERSION     WP_284872062.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..442
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=47820
     Region          1..441
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mrmtvigtgy lgathaacma elghevlgvd vdetkiealk nskvpfyepg lpevlernie
       61 agrlsfttsy aeaaafgnvh figvgtpqqr gsyaadtryv eaviddlvpq legehlilgk
      121 stvpvgtaaa lqqradklaa ehgnkaqvei awnpeflreg yavkdtiepd rivlghraen
      181 sraeeiarev yatplendtp fivtdlqtae lvkvsanafl atkisfinav sevcenvgad
      241 vtqladaigy ddrigrkflg aglgfgggcl pkdirafmar agevgadqal tflrevdain
      301 mrrrqrvidl areelgsvig rnitvlgaaf kpnsddvrds palavagqls lagasvrvyd
      361 pqgmdnarkv fptldyatsl edalrgaelv ilatewqefk emdpqwaael vdkqllidgr
      421 nvlnvtdwqn agwqiralgr sl
//
LOCUS       WP_284872067             273 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Corynebacterium sp. MSK008].
ACCESSION   WP_284872067
VERSION     WP_284872067.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..273
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29568
     Region          38..145
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mklssammtl aagygavrgl qnrppmpfnd rnfqpryptp vmyvhginsr taafesnaqr
       61 lkeqgfwvwg ydygdmiapg ffgagdlnsi vedveehvdr vlrktgaeqv divahsqgal
      121 mtklfisrgg aakvrrvvam ggnfhgtdfr glagrmgeia snhphftalf apgaaqqlag
      181 sawlrkfsrg pdtvpgivyt siyspadtvv tptstsmlea vpgadvanid sgqwydgyap
      241 yhalmprdpl yadltvwgll revgdhvppt sfd
//
LOCUS       WP_284872106             337 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium sp. MSK008].
ACCESSION   WP_284872106
VERSION     WP_284872106.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..337
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36724
     Region          53..335
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mnsknsvrrk ltallmalvt glaavigapq asaahrdwlr pdstghcewd rvgfwvqrct
       61 vwspamnrhi tvqiqpaqrg gnaglymldg lrateitnaw vndvnaartf kdnnitlvmp
      121 vggqssfytd wnapatydfn hpvtykwdtf ltkelppylq qhfgvsptnn silglsmggt
      181 aainlaalhp nqfrqvlsys gyltttvpgg qtalraalld gglynvnamw gsslnprrfe
      241 ndpflnmgnl rgrdvyvsag sgvpgpadek ylpqhraagi aleqvasvtt rawsakatvt
      301 gvkhtavftp tglhnwdqfg sqleatkpri lnvmnaw
//
LOCUS       WP_284872121             529 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Corynebacterium sp. MSK008].
ACCESSION   WP_284872121
VERSION     WP_284872121.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 529)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..529
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56558
     Region          1..510
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mgtfialigl llatvlvaav gertglpwpa lltvvvapvi fipgidtvsi dphlilpifl
       61 ppllwslarr tswgqigsql nvvltmsiil vfltiaalta tamwmlpgls laaamvlaaa
      121 iappdpvavd avagpagipk ritgtlqteg lfndaasivt fnvamaaava hgevdfgkga
      181 lqflyaaiaa vliglvvgrl aaafansvpd svirtaftwv lpfaiyagce aigasgviai
      241 viaavemssr stmtaedrlt ghsfwetvel lftgvafgli gmsvrdaidt agthiwqavq
      301 vgvvlsvvaf avrfiwmwvl ykinqkkhht nvsplrlqev llmawagmrg lvtlalvlai
      361 pasatnyhhe lsvialtvlt ctmvlpglll pwlvdkldlq ngpagdkale elnqrafdaa
      421 rkavrehgee yapeayammq erldsiaekr lqdpegseer kaafdrartg aaqlqevalr
      481 aasrelqqar rerkynpadv davladldrl ilardrkalt gpstlweqk
//
LOCUS       WP_284872158             517 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Corynebacterium
            sp. MSK008].
ACCESSION   WP_284872158
VERSION     WP_284872158.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..517
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=55516
     Region          1..472
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 megfidtlng viwsnalvyl clgagayftl vtlflqircl pdmirqlksg esseqgissf
       61 qslmislagr vgvgniagva taiafggpga vfwmwlvall gsatsfiecc laqiyketdr
      121 dtgeyrggpa yyiektykht aaapfmlvya iifsvcmlla tsyflpgiqa ngvaaavdna
      181 wgvnvwvsat imtvllafii iggvkrianf asmvvpfmag iyiiiaivvl fanasqipev
      241 fgtivrsafd keaafsgmlg aaimwgvkrg iysneagqgt gpqsaaaaev shpakqgfvq
      301 afavyidtlf vcsatafiii stdmykvfeg qsedgaliye gsladgipvg pgfvqeglns
      361 fsaglgpsfi alaimffaft tvlayyymae tnftylnrwv knegtrkaii wilralilva
      421 vfigatttpg tawalgdigv gatawlniva iiflqvpalk clwdyrrqkk agidphfdpe
      481 algiknadfw verknrmiea gtwpgvegkv vtttrnn
//
LOCUS       WP_284872168             376 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Corynebacterium sp.
            MSK008].
ACCESSION   WP_284872168
VERSION     WP_284872168.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..376
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40905
     Region          1..367
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mnaplsgirv ldlsrvlagp fcsmiladlg aevikvespw gddsrqfgpf vdgtsayyrl
       61 fnrskmgitl dfkddndkev lrdlvrradv vvenfrpgvl eklglgpeel levnprlvvt
      121 sisgfgqtgs lakepaydlv aqamsglmsi tgwpnskptr vgislgdlip glyaaigtvs
      181 alyqrestgk gqhldlamyd slisvmesvg mralyddtpp trigndhgls apfstyatkd
      241 gdvviaittn rlferlanal gipematdhr faepvarsen rvalreliee alstktraet
      301 ialfeehgvp tarvydldea lrspfaeerg viaeetdgfr tlasplklag meapkpapel
      361 gqhndriesw lsedpr
//
LOCUS       WP_284872392             517 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Corynebacterium sp. MSK008].
ACCESSION   WP_284872392
VERSION     WP_284872392.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..517
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=55200
     Region          5..331
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(7..8,11..12,41,44,98..99,151)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(96,99,176..182,211,235..240,271,297..301,303)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mraaalwfpd wpvqaarles gdelaepiai aaqhrvkvcs haarqvgirr gmrvrnaqav
       61 apeltvvedn pdrdgrmfas laasfddvaa svevvrpglv vvdveaaarf hgsedkalem
      121 lidaasrrgi dtqagaadei ataliaaras qvippggsae flaaqplgvl vaeeslaadm
      181 dtvkalgqlg ittlgelakl ppnavttrfg tkgmrihria saapdrrvap elpvedlava
      241 itpedpierv daaafaaral aaslherlkd tgrnclrlkv iaelhdgtrv ervwrtrepl
      301 teaatadrvr wqldgwltng gsgaitslil eplefaapep vgelwsdgas tdtarrvver
      361 vqsqlgidav lqprlvggrg vaervamvpf geepedvdrq swpgaipkpl parlgggidh
      421 pasrimlida sgapvivtae allssepygl awgekrylvt gwagpwpvda dwwtqtelpa
      481 grvarmqvvg reggeggavt gwllvwsrrs wrveavy
//
LOCUS       WP_284872397             534 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Corynebacterium sp.
            MSK008].
ACCESSION   WP_284872397
VERSION     WP_284872397.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..534
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=57187
     Region          1..520
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mttpmlevsg ltvaygdadp vvrdisfsve agkmtaivge sgsgkttsam aaldllgpsg
       61 nvlsgsirfk gqelsgltna ewrklrgtki glvpqdpnns lnplktigas vedgleihgv
      121 gdaaerrrka iallervgid dperrynqyp helsggmkqr vliaaavale pevliadept
      181 saldvtvqkt ildlldkmra elglgivfit hdlavagdra ddvvimergr vvehgpvgqv
      241 ltspqqdysk rllanvpsla vadayrrppv tpepllsvsg ltkrygdfta vedisfdvar
      301 gsthalvggs gsgktttgra ismfnqptag sitldgtelt gltpkqqrgl rgrvqmvyqn
      361 pyssldpkmr vgeivaeplr nlagaskrea ltradeflar valdpakfas rtpaqlsggq
      421 rqrvaiaral ivepelvvld eavsaldvtv qaqilelled lqrelgltyv fishdlavvr
      481 qisdtvsvfs rgrqveygat ndvfahpqhd vtrelinaip gtvfrarqlg efvv
//
LOCUS       WP_284872455             288 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Corynebacterium sp. MSK008].
ACCESSION   WP_284872455
VERSION     WP_284872455.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..288
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29900
     Region          1..280
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(33,228,231)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(180,199,226,229..230,233)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mitvygealv dlvpsapgpl apltpalggg pfnvaralgr fgasvafqsr lssdaygaal
       61 rqslldadvd lslcpsgeep tplavtalrd dgsasytfyv ngtadrlaep epvedgyavf
      121 gtlslalepg slryaeaarv sadngatvcl dpnlrpafss ekhrlflrgl lesvtvlkls
      181 deevdflgdt sdvpvvvttl ggdgirvrap fgsvevrapa vevadtigag dtimaalvhq
      241 fdargldrsa llalgegewr eildfaaraa aitvsrtgad tpylhela
//
LOCUS       WP_284872474             321 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Corynebacterium sp.
            MSK008].
ACCESSION   WP_284872474
VERSION     WP_284872474.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..321
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33214
     Region          5..321
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mnvassprvt vvynpvkvhl erlrravery awegaeiewa atstegpgfs qavgaleqga
       61 dliiaaggdg tvrmvalavs gsktpmaivp agtgnmlarn lgvpllleaa vhrafsgtdr
      121 lidlcrvemv ypdgrtehsg favmagvgad agmihrtres lkaavgplay vpavfqslgg
      181 gnsvdvditl dgdptvttsv htcivgncsd lvggipllpd alpddgvlda vvlraedvad
      241 wagiggklal dtvrgginal lpseaqlrpp aslpptmeyl egrritlefs epeqleldgd
      301 aagavsavtf dvmpgtlrvv c
//
LOCUS       WP_284872502             920 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium sp. MSK008].
ACCESSION   WP_284872502
VERSION     WP_284872502.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..920
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=102108
     Region          11..918
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mlspdpgtsf lrefaeakpf alddfqlqac qaveqdrgvl vcaptgsgkt ivgefavala
       61 lhrgtkcfyt tpikalsnqk yhdlvaehge davglltgdt singsaeivv mttevlrnml
      121 yaespqldrl thvvmdeihy ladrdrgavw eeiilnldds vsliglsatv snseefgewl
      181 davrgdtevi vsehrpvpls qymmvgrkmf plfepgtggr vnrslehaie rieagssdeg
      241 rrdfeegrgf rsrsrsgrsr gqdkvrpvgr pevvsalqgq dmlpaivfif sragcdgalf
      301 qclrsrkelt taeeraeieq iidegvdgip eedlevlnfr qvrtawmrgf aahhagllpa
      361 fkhiveqlfv rglvkvvfat etlalginmp artvvlekmv kfngeahvdl tpgqytqltg
      421 ragrrgidhi gnavvqwapa mdphqvagla strtyplisq fqpgynmain mlamngfdds
      481 irlieqsfaq fqtdrsvvge vrdierlqqk vrslrtkler disafappsd daaaelveys
      541 qlrrdlseee kqarrdhlds rhaetikilg alqvgqvial pskrkpelaa vvqpagkphd
      601 prpwvtterg wsgridaaaf knpplvvgri kvprhmqdqp rrharkvasl lhrghfnapk
      661 rlreqsrvrp nkkvtalrea irnhpvhdwp aadreilart aeeivreert laklerrvdt
      721 stdslgrtfe riiglltemd yvelidgepq vtdegerlsr ihnvsdllva qclkrgiwde
      781 ldpaelagva smvvfenrra tggspeaatd amadamnetm riygelvade qrhnlpatrl
      841 pdpgfclsih qwtagaplgy alaaaaesga eltpgdfvrw crqvidlleq ikktgysdqi
      901 rdnanravda irrgvvaign
//
LOCUS       WP_284872506             322 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium sp.
            MSK008].
ACCESSION   WP_284872506
VERSION     WP_284872506.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..322
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34814
     Region          49..318
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtndndmvvr qvgltfalla spakrdvawv qkhvdgyggr trdaathlie rdvrelrdlg
       61 vparyqdgev wvvkdlyelp avdltaeeas vvglaadlsk pgslgefars gwtklaasga
      121 trsmeapalm svsndifqlr pdtlraivkc vqakqrisfd fvrapgkdpe rrvadpwgvv
      181 slnnrayfvg ydidrddvrv frlkkisklk kvrhsdafhe ragdlqalve etlrgelida
      241 tvtvthgtge elaqrgtras kvgaggdagt ggatdtitlr gvdrdwavrt iaslagsvva
      301 vepsevredv vkllraalgg en
//
LOCUS       WP_284872520             222 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium sp. MSK008].
ACCESSION   WP_284872520
VERSION     WP_284872520.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..222
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23525
     Region          3..193
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 msrphavlwd mdgtlidtep lwgkatfelg ellgrpltpe vraktiggsf pntlnvvaew
       61 agyelqdgdl eryrtwmfdr maellaggie lnpgiggvle slarrgtpmf vctntervva
      121 dpcidaigre ffagtitgde vahskpapdm yleaarlaga apgeclvved swhgmsagaa
      181 agcavlglae evpvgvtrfd pinfvgagas dvddwfsaar qa
//
LOCUS       WP_284872738             537 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Enterococcus faecalis].
ACCESSION   WP_284872738
VERSION     WP_284872738.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 537)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..537
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=61892
     Region          6..456
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(20,22,24,28)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(59,62,99,102,143,162,166,198,247,398)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(198,247,316)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          463..533
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; pfam16657"
                     /db_xref="CDD:435493"
ORIGIN      
        1 mdqwwknavg yqiyprsfkd sngdgigdlq giieklpylk elgvdflwln piytspnvdn
       61 gydiadyqgi qpefgtmedf qelldqahql glkiildlvv nhtsdqhpwf veakksldnp
      121 yreyylwada tpdrmpnewq sffggstwty degtkqayfh vfakeqpdln wknpkvreei
      181 yamirwwldl gidgfrldai shiqkepwdf kittnpwapf mnvkgiedym ldlkaifaey
      241 dimtvgeasg vsskkavgwt ndagylnmif elehnvregk pgeerlnilc ykkvmarwqk
      301 higtegwnal yvenhdnpri nsilgnetsh sakaigtial llrgtpfiyq gqeigmvnyp
      361 fqqideldak dshnhyrlli esgydakqal kevahwtrdh srtpmqwtsq eassftsghp
      421 wlaihpnfke invadqetda qsvlnyykkl ialrkenpvf tdgqfellap nhpsvfaflr
      481 ktteatalvi vnlsgekcqf dlpnkllgrk wqqllgnqdf tvrkrmqlap yqagvfq
//
LOCUS       WP_284872785             362 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Corynebacterium sp. MSK008].
ACCESSION   WP_284872785
VERSION     WP_284872785.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 362)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 362)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 362)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..362
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39580
     Region          6..315
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 matnpierlq arsfgpfgdl dlnfspklnv itgdngtgkt qllklmysls ktleparidt
       61 psktslaapl ankligvfkp dtigrlasrv rgrsrasisl kyagirdplk vefssasdtr
      121 vavnsvpnrt lddtavflps rellsiypgl vslyesrevs fdetwrdtal llgmtpllgp
      181 rgdrandmla pllrilegtv seengkfyvr lktatggtgk ieaplvsegy rklamlvrlv
      241 qsgalldggy lfwdepeanl nprtqravak tihllakhgt qvfvathsvf ilrelrllid
      301 ddpietqyvg lertepsves kaltgvrgvt asnqndlpal ialeeeaaqa lrylnrdfdd
      361 se
//
LOCUS       WP_284872804             428 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Corynebacterium sp. MSK008].
ACCESSION   WP_284872804
VERSION     WP_284872804.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. MSK008
  ORGANISM  Corynebacterium sp. MSK008
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Corynebacterium sp. MSK008"
                     /db_xref="taxon:3050188"
     Protein         1..428
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45975
     Region          1..422
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtrtivvgag mtglatawhl qeyghevevl eridvaagss wgnagwlapg ktiplanssl
       61 waygptalfd khaaldvpvr idpklwrfca nfmahatgra wdktmagltk adlgalaafd
      121 eleaggvkat tnegpfiigf enekkaggfl kevegaqrhg qeipfeqitl ddarrdapml
      181 tdkvgatfrm ggqrfiepgp ycqaiadsiv erggkvttgv evvevtstrk pavklatgew
      241 lhadnvvlat gewlhadnvv latgawlprl akdlgvttli qagrgysfsv etaepatcpv
      301 ylpdpkiact pyqgrfriag tmefrgpdep fqpgrvasmi httkpffrgi dwedrqdewv
      361 gsrpvtpdgl plvgatkvpn vytngghgmw giilgplsgk mlakqietge vdetiapfdp
      421 lrgpfggl
//
LOCUS       WP_284872977             305 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284872977
VERSION     WP_284872977.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..305
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34451
     Region          7..238
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mnhprptlwa vadlhaavra nrlrldeitp rhpddwllva gdvaerldli stvlselrsr
       61 faqviwvpgn helfsrstda hrgrakydal vqicrsidvl tpedtfpvfg dttvvplftl
      121 ydysfrpagt gveealelaa qknvvmtdei aiapfadira wcwdrlaysi trlsrvngpt
      181 vlvnhwplvq eptlrmalpe lalwcgsrht rtwpqrynak avvyghlhmp aifeldgveh
      241 hevslgypre wgrsdqnriw pcpvlelaad pnggqiaqrv gleqcreshp elrmprrrgk
      301 gsdgv
//
LOCUS       WP_284873019             286 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284873019
VERSION     WP_284873019.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..286
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=31895
     Region          29..272
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 mthihaaqtr taqheqnqse apeqpeitgf rlalanfegp fdlllqlihs kkmditdial
       61 hevtdeflay trfldasagl derteflvva atlldlkaar llprgevdde edlallesrd
      121 llfarllqyr aykqvaelfa dwqrdaqqry pravaieerf aellpplhlg hnpesfaela
      181 agvfrpkppe evgtdhvhrv avsvpeqagv mlnslkllga sewttfatlt rdcpdtmhiv
      241 grflallely karavdteqp ealeklsvaw tgldvdpavv gaanwe
//
LOCUS       WP_284873026             446 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284873026
VERSION     WP_284873026.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..446
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46616
     Region          17..427
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 msraggpaph prevvtrral vvwvagvacy ivaitgrtsf gvagveaiar fdvdasriav
       61 faavqlgvya laqiptglgi drfgpravvm fgavvmglgq fllalttsyp laivtrvlig
      121 agdasaflav mrllpywfpl rktplftqlt gaigqtgqfi savpflallg sagwtgafvt
      181 lgatsillag laglaikdlp dvdrhaahas essmpvsgrd slrtrmrtll rtpvawqgff
      241 mhysclmfql vflmmwgfpl mtlgmglsaq qagavlaint vvtvfsgplh glfsarigav
      301 rhwavvgfsv tivltwavff asatprglaa ivvvnvival cassanygfd nvregvprev
      361 vatatglanm ggflagmaas qgigvvldis saggeyawgd fqvaalaagv vwavgvigll
      421 vasawrkypg pahrilphrl ralrsh
//
LOCUS       WP_284873122             334 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284873122
VERSION     WP_284873122.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..334
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35127
     Region          <129..334
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 msdspdetsh hhisvptdae alvftdpyrp nieltdsmst vdvsipanss vtysfqsgel
       61 kypdpnnayg agpqasllng gsvdqtfwpp rssaviadlp garlsidrnv fgrrctarld
      121 drgaditavf ldgddwihlh dltgaldlav taglipqinr vflpaakdrs eeytsqafas
      181 alatelpaii ksshivlvgq slgglsalra tlaastettp aikgaiaqsp avwwfadrst
      241 eqadtlsdgp aggdiaaqla hpsleipaah sgsglpriil tcgaeeppmq rhvdavadal
      301 trrgfpttnh rtpgghdpam wrhgiipala ellg
//
LOCUS       WP_284873134             517 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284873134
VERSION     WP_284873134.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..517
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54735
     Region          17..514
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mssgfarssf ahnggarvav igagpnglta aavlaqagcr vevfesaddi ggsartypaf
       61 gagsavdfga aahpfgavsp vfrqlgleny glewkhpqyp mahplvdapa vilhrdlgtt
      121 aaqfsdhder vwnhlhkplv ddvgklvnsv lpvrprypla larlglrgvw parsltsrll
      181 vdeparallv gsavhairpp sqpgtaafgl lfnslgmttg wpvvsggtgq lvmalarvik
      241 hnggiiktga evqdlsgfat ydavvttqtp rqllalqgle lsrlrsrslr rwkygtavyk
      301 vdylvngpvr wndprvagag tvhvggtvse mqlaesqaaa gtlperpfvm vcqqqaadpt
      361 rfsgnrrsvg agrvlsaqld agripedarl philwayahv phgyqekfpg evaglietqi
      421 sryasgfsaq iierhqaspg qlqeananli ggdiaggamn laqmlrqrqy vgtltmnpev
      481 pvvqasgasl pgagvhgmag wraaqmilrr fgatelr
//
LOCUS       WP_284873167             313 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284873167
VERSION     WP_284873167.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..313
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33941
     Region          137..295
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 msssrnafqr kpallwtlva lvvalavliv vavvrsgdde smsaggqdam hgpqapssaq
       61 sgnsdsqstp mpggeyspeq arelakqvep gtdfsrpnsp dptiigpgae itsnddilnv
      121 hrrnaedpfa mgaldapvvl sefsdfecpf ctrfavetap klkekfvdtg llriewndlp
      181 vngphaetga qagraagnqg kfyefhdvly nntydnqtgg hpgydvadyv rfakeagied
      241 lekfrteien eeyrdvvrqa lhyassigmr gtpafilgdr fisgaqpyev fedevyrqla
      301 kvadgtvphp tsk
//
LOCUS       WP_284873180             227 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284873180
VERSION     WP_284873180.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..227
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24051
     Region          <119..227
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mmnkqialis viglvlsvav gfgayamlhs stghvageta vsnkaessag eamegsvaqd
       61 egaglrrpac psleipgaqv qlpclseqav tdadkndels tdekneaigg dagaagdeit
      121 vvnvwawwcq pcreeipylq evqdkhpewq vvgvhadkna kngagmldem gvdfvsyqda
      181 hntfaselgl pgvipitivy vgneqrkvfv qpfrsteeii esiegvl
//
LOCUS       WP_284873254             208 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284873254
VERSION     WP_284873254.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..208
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23536
     Region          8..78
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 msdwqkgmta tvgvnvkrlr gdrshlwlqn eteklgfrvs rsgiseletg krssisvaew
       61 lilaraleva pvvllmpdyp dgetqylpgh hamgyevadw itgqrttntn ptkqnsaplq
      121 tptqlaalla eredleqtew ediketfkqa mnakdheqka qilnkrtdis ertvqriaan
      181 dndinrlgyy anqnhrseig maryteei
//
LOCUS       WP_284873378             555 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium pseudodiphtheriticum].
ACCESSION   WP_284873378
VERSION     WP_284873378.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..555
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=60630
     Region          145..540
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
     Region          <410..>461
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
ORIGIN      
        1 msqpepqkap epsagwgtqg erkrrsyray rthrplrlrt wlvvltvlvs afglfassfa
       61 vysvmrevfy qrvdddltqs magwaqnsel fsgnlsaspp tdyavihifp dgssrvyndr
      121 dtlpqinnlv igggprsvas vdgpqqpewr alanqqngvv tivaknlere ngllrglaml
      181 qalislvmlg flallafavi rqtlkplqiv ertasdiaeg dldlrvpkwp lntevgqlaa
      241 alnimlerlq dsvetaqske eqmrrfvgda shelrtplts lrgyvelyrs gatndvdhvf
      301 atiddesgrm kllvedllal traegsrldk rtvdvlelsl avvgtaraay pertirvenk
      361 ttdipvvsgd pdrlhqvlln litnglnhgg peasvtltlr kesqddcmrl aaeqqetddn
      421 heaeekttgw sqddgkngka gkdgkagrdg nkgtdgesak dyvciditdd grgmskevtg
      481 liferfyred psrargaggg sglglaivks lvdqhdgeit vdsepgvgst ftvripalde
      541 psaseetfdd ygegy
//
LOCUS       WP_284873296             519 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284873296
VERSION     WP_284873296.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..519
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=59044
     Region          9..512
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mpsekdapqp almwfrddlr lhdnaalawv akqgpviavv idenatvtga ralgaatrww
       61 wqrsvhqlqh klhahgvpll yyqgdpraii pavvkefavs avgwsrryhk plreldaqlk
      121 hllqekgvaa ksfpghllte pwevqtqqgk qykvytpfak targvaednv asylntgndq
      181 apsptshdel apiglagpga dlasahplpd wdeadwthsl aqhwspgena awqlaegfld
      241 qltaaarkqa phyaadrdrl dkqatsrlsp ylrfgeisih rlwamvtean dtgriageda
      301 saflsellwr dfawhrlyhl pdlhrrnvre qfdhfdwhwg ekearriast rrdprwpete
      361 kdipeiatad dfrsvfsawr agktgiavvd agmrelwatg tmhnrvrmvv asfltknlgi
      421 hwrhgeawfw dtlvdadpas npfnwqwaag cgddaapyfr ifnpdtqakr fdpdyryiqh
      481 wvpeyatpmy pqpvvdlkas rrqalaayee mknfhprpe
//
LOCUS       WP_284873633             305 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_284873633
VERSION     WP_284873633.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     Protein         1..305
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34326
     Region          7..238
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mnhprptlwa vadlhaavra nrlrldeita rhpddwllva gdvaerldli stvlselrsr
       61 faqviwvpgn helfsrstda hrgrakydal vqicrsidvl tpedtfpvfg dttvvplftl
      121 ydysfrpagt gveealelaa qknvvmtdei aiapfadira wcwdrlaysi trlsrvngpt
      181 vlvnhwplvq eptlrmalpe lalwcgsrht rtwpqrynak avvyghlhmp aifeldgveh
      241 hevslgypre wgrsdqnriw pcpvlelaad pnggqiaqrv gleqcreshp elrmprgrgk
      301 gsdgv
//
LOCUS       WP_284873712             415 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Corynebacterium suedekumii].
ACCESSION   WP_284873712
VERSION     WP_284873712.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..415
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46492
     Region          84..413
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mapkntqrtr rrfgslrtlp sgrvqarysh apapnspavs yrapgtfedq daaiawlkgq
       61 ermidrgdwm ppeeqdrrsk adavtvaeyv dlyhdrkqis geirastvqt yrnttnnrik
      121 pysiadirit qlttmdcyrw wdqmgvdhad tpetnrkgyv rlkaamadav ersyieinpv
      181 avkaaskksk sydkqlptts elkaivdnvp vthkvvavlc afhglrvgea lavriqdvif
      241 dgdggacvrv rgnfqrikdt dghvkmvrqd aktsagerdv palpqyvdll rhavvqarar
      301 ahdeakpned aravrsrred flisttrtgq pimdtsfrsi wnrarerggv rdditphygr
      361 nwltvmlaeq gstpaeigqv lgqrdistvv giymkvrggr padlmrrvaa tmdah
//
LOCUS       WP_284873713              64 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            suedekumii].
ACCESSION   WP_284873713
VERSION     WP_284873713.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 64)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 64)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 64)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..64
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..64
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=7105
     Region          4..64
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mankatnrkl ltltdaaemy sisrrtlera akageirlyr lnrrvvrvse aeldalfgld
       61 arva
//
LOCUS       WP_284873740             270 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Corynebacterium suedekumii].
ACCESSION   WP_284873740
VERSION     WP_284873740.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..270
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29296
     Region          8..270
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mtqhriridd ptdprfddvr dlnrsdaadr rlviaegnlv vgrllesrfp vrcvvgfpak
       61 ldafleehei pdgvpvyevt retlaavagf dlhrgllaaa hrapetplad ilttartvav
      121 legvgdheni gsmfrnaagm gvdailfgng cadplyrrvv rvsmghvlrt pfahlegsyt
      181 twqrsleqlr eagfhlvslt pdpaaehlad alagrekval lvgaegpglt ehamratdvr
      241 aripmapgtd slnlatsaai afyererslr
//
LOCUS       WP_284873807             100 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium
            suedekumii].
ACCESSION   WP_284873807
VERSION     WP_284873807.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..100
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11242
     Region          31..87
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(35,39,64)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(38,63)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(45..46,57,60,64..65)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mttldelhqr rpvnrgrvee hkqrmlaqvr asrlrelrea tgltqaqlae rigvgqrqvs
       61 kiehgdldna kigtirryle avggdlsiey vrgdsriqva
//
LOCUS       WP_284873930             261 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Corynebacterium suedekumii].
ACCESSION   WP_284873930
VERSION     WP_284873930.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..261
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=26189
     Region          <27..176
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mtstnslirr waaagaaall tttaliptat aederrgspt mlvldssgsm taddaggqtr
       61 idaardaaht fidevdgtld lglvtyggnt gdtpeeydag crditmvtap gndtadqikd
      121 hiddldargy tpigeslrta adelpdsggt ivlvsdgiat ctpprsarlp rtspirasts
      181 sstpsastst tppaknsnas ptqpaaptpt pptptpsptn snapppaata ptsptpnasp
      241 pppttskptp spstpppssp a
//
LOCUS       WP_284873993             254 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium suedekumii].
ACCESSION   WP_284873993
VERSION     WP_284873993.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..254
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27182
     Region          2..239
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(16..17,19..20,23..24,62,66..67,70..71,101,105,112,
                     115..116,121,137,141..142,144..146,148..149,152..153,
                     156..157,177..178,180..182,184..186,188..189,191..192,196,
                     199..200,208,210)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(140,144,147..148,150..151,191,194..195,197..202,205,
                     208..209,213,215)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(161..168,179,182..183,186)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mnllrdinpv trilglillt tplllsvdvv sagvalaftv lvapfcgvsw grllrrgwpi
       61 llaaplaaip malygrpege tyaqflfahv tdnslqlaaa ifvrvlavgl pvivlsadvd
      121 ptdlgdglaq vlrlperfvl gavaaarlvs lfrddldsmr rarrargiad qgriryfltl
      181 afgllvlslr rgaklatame argfnrvaeh grtwaressl sardwivmav clvvsvasig
      241 iavavgsfrf lgva
//
LOCUS       WP_284874032             142 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Corynebacterium suedekumii].
ACCESSION   WP_284874032
VERSION     WP_284874032.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..142
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15575
     Region          43..>100
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mkhpnlstlg lpgnrsgrsr prrsrkpref asvehlspea vaafvdgelt dgalhrarvh
       61 lvhcgecrae ierqrnasew lrgsnitpev rapedllarl agiasgplrp gpdaestptp
      121 lpeglldkme mirrairrnq gr
//
LOCUS       WP_284874060             511 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Corynebacterium suedekumii].
ACCESSION   WP_284874060
VERSION     WP_284874060.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12045581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..511
                     /product="SLC13 family permease"
                     /calculated_mol_wt=53787
     Region          <27..170
                     /region_name="CitMHS"
                     /note="Citrate transporter; pfam03600"
                     /db_xref="CDD:460985"
     Region          106..505
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mstpatavae tdnaknqttk knrnwvwlll gpvlgallfl llpdslsfeg ravagcalwm
       61 alwwvfepap ipvtsmlplv lfplfgmgtm kevaapyadt viflvlggvi lglateksgl
      121 hirialltvr tvgtkasqiv lglmvasafi sawvsntata vimvpiaasi iqlvrqvdek
      181 aagtkfaaat llgvaygvti gstatligqp pmalmkayvg eslgidiafg twmlvgvpwa
      241 vimtllcwlv ltkfvyrpev deipggkkli qdeiaklgam staerrvgti flvaiffwvf
      301 vpfiadipfv adalpflgsi sdsqvavaaa iacfltpagr asddegagpr nllkwedske
      361 vpwgllllfg gglslsamft atglsewigt qveglgsmps wviivavmiv slglteltsn
      421 tataaaffpi fgavavgagv dpllmtfvvt lavcsafmlp vatpsnavaf gsglitikqm
      481 tragiwmnfv algmiliviy tlipwvfgva p
//
LOCUS       WP_284874102             444 aa            linear   BCT 25-DEC-2024
DEFINITION  nitrate/nitrite transporter [Corynebacterium suedekumii].
ACCESSION   WP_284874102
VERSION     WP_284874102.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Yan,H., Huang,W., Yan,C., Gong,X., Jiang,S., Zhao,Y., Wang,J. and
            Shi,Y.
  TITLE     Structure and mechanism of a nitrate transporter
  JOURNAL   Cell Rep 3 (3), 716-723 (2013)
   PUBMED   23523348
REFERENCE   6  (residues 1 to 444)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   7  (residues 1 to 444)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..444
                     /product="nitrate/nitrite transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48188
     Region          32..432
                     /region_name="MFS_NRT2_like"
                     /note="Plant Nitrate transporter NRT2 family and Bacterial
                     Nitrate/Nitrite transporters of the Major Facilitator
                     Superfamily; cd17341"
                     /db_xref="CDD:340899"
     Site            order(42..43,46..47,50,83,138..139,141..143,146,165,
                     168..169,172,255,258..259,262..264,267,306,310,365..366,
                     370,374,390,393..394,397..398,401)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340899"
ORIGIN      
        1 mstalntdgr vlhgwdpene etwdsgiawr tlwistatlf mafctwylvs aiapvlnqig
       61 fdlstaqlyw ltslpglagg llrlifmflp pilgtrrlvs issllfvipm lgwffavqnt
      121 gtpfwwllvl afltgigggv fsgfmpstgy ffpkrlsgta lglqaglgnf gvsfillvap
      181 wlmgltlmgi gfvapqrsgd telfvhnpai vmvpwaivma vvawiflkdv pvtanfrqqi
      241 difgnkntwi ltiaylmtfg afsgfaaqla liinnvygan sefaatyave dlpkgaafaf
      301 lgpligslvr aawgplcdkf ggaiwtfvsg vgmtlstiva alfltpdnpd qfwwflgaml
      361 flfffsgign astfkqmpmi lpkrqaggvi gwtgaiaafg pfivgvllsm mapavffwgc
      421 vvffafattl vwiyyarpna pfpg
//
LOCUS       WP_284874130             118 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium suedekumii].
ACCESSION   WP_284874130
VERSION     WP_284874130.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 118)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 118)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..118
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12554
     Region          27..115
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mstaarptil pitdlsaccs lgsgpltaee agryatlfkv ladparlril ssiaeegcdp
       61 vtasdltell glgqptvshh lkklteagll estrvgrmmq yrvlpdlfae lrtvlqmd
//
LOCUS       WP_284874147             334 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium
            suedekumii].
ACCESSION   WP_284874147
VERSION     WP_284874147.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..334
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34750
     Region          40..332
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mqtktttala vavvvglava aaalvlgpdh itpsdertgd ealaarlaeh aesghrniaa
       61 ftvagdevtf aglgadehte feigsvtktf taqilinqie agrvtldttv geiidagdaa
      121 vadvtlrela dhtsglprlg gsngiitsvv tsltganpye gtspedvidd altaslsgrg
      181 efdysnlgva llgqllavea dttyghllde qileplgmtd tylmetgtvp adaprglltt
      241 grvaqpwetd gygptgglrs tpadmarwar flldsgvpei twgegpdgsh shnggtygys
      301 stlivdpeqq ravftvgdtm hdvdavadhl wkeq
//
LOCUS       WP_284874195             197 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Corynebacterium
            suedekumii].
ACCESSION   WP_284874195
VERSION     WP_284874195.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..197
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21329
     Region          37..138
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mhdhgrpepd dverfyadgp rwsglpneal vheagrltpg raldigcgeg adavwlaeqg
       61 wevtaidpva aalerartla dahgvthrit frqqdltgfl dsalgtfdlv agsyvplped
      121 rdlatgicrl vgpggalvwi hhlfdireer mildpgylep favaefggsm typaernvts
      181 gagahhhmdv vlratrf
//
LOCUS       WP_284874283             356 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Corynebacterium
            suedekumii].
ACCESSION   WP_284874283
VERSION     WP_284874283.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..356
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=37832
     Region          6..329
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mhstptsrqa avvynpvkvd vdelkslvha aaekhgwgdv awfettvedp glgqakqaae
       61 egaemvvacg gdgtvraaaa glrdtgaslg iipqgtgnll arnlslplem edaidtvfgg
      121 qdtridtcta eltrpdgste sldfvvmagv gidaqmivnt dddlkkkigf laygvaiaks
      181 laggnrirvd yrldggarhr trvhsliign cgdlvasvpl lpdaqandgi fdlvairptg
      241 vfgwaqvfgk ighqmwekfr lrvlrrderi tggdddikal qyvtgtrlev tlkhpevfev
      301 dgdeagevta ftitidpesl vvrepvpepv tepgepapgt kkfdedgqva ehgdsa
//
LOCUS       WP_284874303             197 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Corynebacterium
            suedekumii].
ACCESSION   WP_284874303
VERSION     WP_284874303.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..197
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21087
     Region          45..146
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mptwkevtaa npahsenyar rwrmmaeqge didgearlvd alspraaril dagcgtgrlg
       61 gyltarghdv vgtdidpvli eharrdhpda rwevgdlsvd pvpvsdvdva vsagnvmgfl
      121 apegreaalr niagslaadg rfvvgfgagr gwgfddfiat aervglelen vfeswdlhpf
      181 tadsdflvai frndadg
//
LOCUS       WP_284874310             430 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Corynebacterium suedekumii].
ACCESSION   WP_284874310
VERSION     WP_284874310.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..430
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=45558
     Region          182..311
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mrhprssaid adawpgvatv pagrlvsvra rlaeaafara cdaagldldp tgepdlvveh
       61 eglfarlava gwlglaesyl agewhaddlv dvlaallatg yrpraglprg rslgaytgge
      121 lptelvrlss gdgmsafggv fatgvpttvr tavpshvpgg rgpdthfidl ttiseptsae
      181 rddlgdaqar avtmlldaar vtagthllef pstggavaig asarratvdt ltadpeqahv
      241 vgerltlagv ddsvstqvid hpvpgprdvr grfdaivsvd kfhvlaprdr valvrgfdrl
      301 ltvggniglq tvvatdamtp sgraavealr ayiwpdldyp tatdihrlvd resglrvvgq
      361 thlgshtals lamqhslfda hareaaaagf dvvfrrlwdy qfalrqalfr lgmldavqlt
      421 lthrnrrgrr
//
LOCUS       WP_284874327             325 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            suedekumii].
ACCESSION   WP_284874327
VERSION     WP_284874327.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..325
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36089
     Region          12..320
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 marhkdspak idtlvrslnl ipyfqshpdr tvmeaakdlg rdpgelladl hrlslcgvgs
       61 wpeelvdlta dyrevritns qgmdralrlt pteagalllt leslegipgl tdreavvsaa
      121 aklrsildpr avaifdslat ddpaestaqv ilreamqsdr rvrftyrsas sdtetvrtvd
      181 pvrifvngge tylagweeas grhknfradr msdmtvldeq atphldrmpf daddpfsfrt
      241 vaehahllvr adatwladyy plelgqdrgd gmvearmpvg saewfirfvi gqsdrltvta
      301 padlveqvrh raeagltayd erpdr
//
LOCUS       WP_284874328             317 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            suedekumii].
ACCESSION   WP_284874328
VERSION     WP_284874328.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..317
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35046
     Region          53..316
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mpaaehavqr ltrlvfalld adrqggrmlt pawirthvdg yqdisddafl tklhrdidtl
       61 aragvplesr qsrdgegtsy rlqsdqyelp evtftpeeaa vlglagemgq tselgvfars
      121 gwtklaasgv srdlsqapvf aavndltsls pavltdilti vragyrmtfd yaatptaepv
      181 rrvmdpwglv tlhdrlylvg hdidrdaprs frirrinnvr arrekathpt pptslqhive
      241 eslrygrqrv davltipegt ahelaaaghr rtdgrvelvd vdrdwlarta agfapavivh
      301 epadirhdiv ellrkad
//
LOCUS       WP_284874341             216 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Corynebacterium suedekumii].
ACCESSION   WP_284874341
VERSION     WP_284874341.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..216
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23080
     Region          1..185
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mdgtlvdtep lwgiatydms erlgrrltpe lrattvggsf rntldvcarh agvqvaeedy
       61 prhkrvmfdq magllaehlt pnpgvtells qlrgagvpml vttnterela apcisavggh
      121 fftdsvtgde vpapkpapdm yleaarrvgh dpadclvfed swagmtaavd agcrviglad
      181 rapagvvtlt elhgrndfvg vtadsvaewf arlppr
//
LOCUS       WP_284874446             236 aa            linear   BCT 25-DEC-2024
DEFINITION  1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase
            [Corynebacterium suedekumii].
ACCESSION   WP_284874446
VERSION     WP_284874446.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Ju,T., Goldsmith,R.B., Chai,S.C., Maroney,M.J., Pochapsky,S.S. and
            Pochapsky,T.C.
  TITLE     One protein, two enzymes revisited: a structural entropy switch
            interconverts the two isoforms of acireductone dioxygenase
  JOURNAL   J Mol Biol 363 (4), 823-834 (2006)
   PUBMED   16989860
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Dai,Y., Wensink,P.C. and Abeles,R.H.
  TITLE     One protein, two enzymes
  JOURNAL   J Biol Chem 274 (3), 1193-1195 (1999)
   PUBMED   9880484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..236
                     /product="1,2-dihydroxy-3-keto-5-methylthiopentene
                     dioxygenase"
                     /EC_number="1.13.11.53"
                     /EC_number="1.13.11.54"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0010308 - acireductone dioxygenase
                     (Ni2+-requiring) activity [Evidence IEA]"
                     /GO_function="GO:0010309 - acireductone dioxygenase
                     [iron(II)-requiring] activity [Evidence IEA]"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /GO_process="GO:0019509 - L-methionine salvage from
                     methylthioadenosine [Evidence IEA]"
                     /calculated_mol_wt=26284
     Region          1..175
                     /region_name="Adi1"
                     /note="Acireductone dioxygenase (methionine salvage),
                     cupin superfamily [Amino acid transport and metabolism];
                     COG1791"
                     /db_xref="CDD:441396"
ORIGIN      
        1 mtllykwnat apdvellrtd npteiaaelq tlgvrydrwa tkeladdadq davlaayaee
       61 vrriseeenf vtvdvarlrd tgqpdfaata kgarekflde hthaddevrf fvegsgtfyl
      121 hiddtvygvv ceagdllsvp egathwfdmg vndpqfcair ffhdgegwvg dftgrrsppp
      181 spattnsspe ssthdhpapp qrhrprhrgh hvldvvrprh plpllpgafr rdpvap
//
LOCUS       WP_284874447             513 aa            linear   BCT 25-DEC-2024
DEFINITION  xylulokinase [Corynebacterium suedekumii].
ACCESSION   WP_284874447
VERSION     WP_284874447.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437490
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..513
                     /product="xylulokinase"
                     /EC_number="2.7.1.17"
                     /GO_function="GO:0004856 - D-xylulokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0005998 - xylulose catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0042732 - D-xylose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53746
     Region          5..506
                     /region_name="XylB"
                     /note="Sugar (pentulose or hexulose) kinase [Carbohydrate
                     transport and metabolism]; COG1070"
                     /db_xref="CDD:440688"
ORIGIN      
        1 mtvtvgvdvg tqgskagvyt adgvqvgkay aphtidylgp graemdvehl vtaafaaiad
       61 alddavaagi hrsevagial sgilvgqvll dedgqilhpv itsldtraeg haaaaardle
      121 plwltesgts tldayaapfq lqwirdhrpe vfdrvarsvs vapyvsarla gltqqemvtd
      181 pthvsgwmvg wdyatgdfsp rqfaafglpt dilprvvpsd svighvtaea adrtglpegt
      241 pviagagdvm qstlatgmtd tgqatdsagt tsiltvgvdg iipevtdmpg mlfslgtlpg
      301 qaiywgyira gglslrwfrd hvarldgdds iyatfdalae qvapgsdgvl flpylaggnp
      361 dsphasgtwl gmdsgtdtar lwrsaleava feyaatlgvv erggvdlsev lvtgggagst
      421 vwnqikadvt gvpwrrphrv dgpplanaal vnqalgltsd maaqladwts ggetvttded
      481 aheiyrraae irtrllagpm qevfasvrql rhl
//
LOCUS       WP_284874456             762 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Corynebacterium suedekumii].
ACCESSION   WP_284874456
VERSION     WP_284874456.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 762)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 762)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 762)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 762)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 762)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..762
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..762
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=84134
     Region          33..762
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mteerprsrn avgvrsmsar larsltgtrv ksnpvldpll sihrqfhpka daevlsraye
       61 taerlhegvv rksgdpyith plavatiaae igmdtttlva allhdtvedt dygleqltde
      121 fgaevarlvd gvtkldkval gaaaeaetir kmivamaqdp rvlvikvadr lhnmrtmrfl
      181 ppekqakkar qtleviapla hrlgmanvkw eledlsfail ypkkydeivr lvadrapsrd
      241 ralkaiteqv taalrennie advmgrpkhy wsiyqkmivr grdfdeifdl vgirilvdni
      301 nncyaaigvv hsifsalpgr fkdyissprf gvyqslhtsv malegkplev qvrthemhyn
      361 aefgvaahwr yketkgshkg dreevdqmaw mrqlldwqke aadpneflds lrydltarqi
      421 fvftpkgdvv nlpadatpvd fayavhtevg hrcigakvng klvalestlk sgdrvevfts
      481 kdenagpsld wqdfvispra kakirqwfak erreehldag rdalaaevqr gglpmhrlft
      541 aqsmktvatq lhypdvdaly taigaghvsa qhvanqlmai fgdqddavda laarapisel
      601 issqakaads eagtgilveg spdvmakmak ccqpvpgdei fgfvtrgggv svhrtdctna
      661 dklndeparl vsvawaprgi sggafaatlq lealdrqgll feitrvfsdq klsvmsmnsh
      721 aaddhiatir ltftvsdtkq lgqllttlrn tegvfdvyrv ta
//
LOCUS       WP_284874538             203 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium suedekumii].
ACCESSION   WP_284874538
VERSION     WP_284874538.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..203
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21390
     Region          5..200
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(163..170,180,183)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mrniplgvyl pgdspihqlp aggkfilllv filastilvk dplvaaawla vvvagyivar
       61 ipvrtalgqt lpvlpvllvl gafqwwqrgw efaattvlil lasvaaaall tlttsiaelm
      121 aaierglspf erfglpveti slavsltlrl iplqlatvqd vlaarkarga gfsvtafgtp
      181 vmvrsirrar llaealiarg aad
//
LOCUS       WP_284874560             269 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Corynebacterium suedekumii].
ACCESSION   WP_284874560
VERSION     WP_284874560.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..269
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30682
     Region          3..238
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mtttlwavsd lhaavkanaa rideiqpadp sdwlivagdv aertdlviqi lgqlrrrfaq
       61 viwvpgnhel fsrsterhqg rekydelves craidvltpe dpypvfngvt lvplftlydy
      121 sfrgagmtve qavaaardkq immtdefaia pfvdirawcw drlaysikrl sringptili
      181 nhwpliqept ldmripeial wcgtrhtrtw aerynaqavi yghlhmpger evagvrhiev
      241 slgyprewer hghlnpwpyp vmtmgesda
//
LOCUS       WP_284874669             211 aa            linear   BCT 25-DEC-2024
DEFINITION  IMPACT family protein [Corynebacterium suedekumii].
ACCESSION   WP_284874669
VERSION     WP_284874669.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Park,F., Gajiwala,K., Eroshkina,G., Furlong,E., He,D.,
            Batiyenko,Y., Romero,R., Christopher,J., Badger,J., Hendle,J.,
            Lin,J., Peat,T. and Buchanan,S.
  TITLE     Crystal structure of YIGZ, a conserved hypothetical protein from
            Escherichia coli k12 with a novel fold
  JOURNAL   Proteins 55 (3), 775-777 (2004)
   PUBMED   15103642
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Okamura,K., Hagiwara-Takeuchi,Y., Li,T., Vu,T.H., Hirai,M.,
            Hattori,M., Sakaki,Y., Hoffman,A.R. and Ito,T.
  TITLE     Comparative genome analysis of the mouse imprinted gene impact and
            its nonimprinted human homolog IMPACT: toward the structural basis
            for species-specific imprinting
  JOURNAL   Genome Res 10 (12), 1878-1889 (2000)
   PUBMED   11116084
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..211
                     /product="IMPACT family protein"
                     /calculated_mol_wt=22635
     Region          15..200
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 mqtsyalpaa grtwthrwev krskfltfar rvmseeaard fiaevrreyp darhhcsayl
       61 lhvdganpve rssddgepsg tagtpmldml rgsglidvav vvvryfggvk lgagglvhay
      121 sqsvqqvlpl vdrvtrsrre lytvtaphae agrleaelra rdlvvdvayg aevtmtlava
      181 pggrtelast lasltagvae paeagtawve s
//
LOCUS       WP_284874683             287 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Corynebacterium suedekumii].
ACCESSION   WP_284874683
VERSION     WP_284874683.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..287
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29020
     Region          4..284
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mripspgtgi aapavmlasg lslyagaava vglfdalppv ivawfrisaa avillvlvrp
       61 gvqeflgrsg aqaavygiat mgmnmsfyea iarlplgtav aveflgpvlv aalgsrnvrd
      121 wvalvlalag vvvisgavws tsadglffal lagglwavyi vvgtrivggs tsprksmtvg
      181 fsiaallalp vmvalwpdav vtaegvtlpa tqllalalgl gvlsavipys ldqvvmrmag
      241 asyfallqal lpvtaallga valgqwlsvp eiigivlvva avalrrp
//
LOCUS       WP_284874750             177 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium suedekumii].
ACCESSION   WP_284874750
VERSION     WP_284874750.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 177)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..177
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19317
     Region          4..155
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18879"
                     /db_xref="CDD:467590"
ORIGIN      
        1 mpipdfivsl rekigheqlw lpgvtavvvr dvpadapiwa vpevllvqra dngdwtpvcg
       61 icepgeqphv tavrevkeet ridahveall gvgavgpvty dngdvtsymd tamrlsvvgd
      121 dtpsvgddes vdvgwfpisq lppisprfrm viadavaqmk hphgyrprmg yekrdrs
//
LOCUS       WP_284874756             454 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Corynebacterium suedekumii].
ACCESSION   WP_284874756
VERSION     WP_284874756.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 454)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 454)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..454
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48294
     Region          16..428
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 msetrlvphp reqvtrkalt vwvaavlvyi vaitgrtsfg vasvdaigrf dvdasriavf
       61 tavqigvysl aqiptgmlid rfgprrmlvi gavimaigqi tlglttsysv aivarvliga
      121 gdataflsvm rilpywfplk ktptftqlta algqsgqfls avpflallhg pgwtpaflsl
      181 gavglliaia agvavadspe tweaarkgkd pdavrekkla aqdrmpigta latvfreplc
      241 wqgffnhysa mlpqivftll wgvplmslgm glspatvglv ltvnvitsmv agpllgpisa
      301 rlgrnrilas ltfagfigta wiifflpaep rgvtaiivvn ivmaaftass nygfddireg
      361 ldrrivatat gmanmggffa gmfaaqivgf mldysaggqa yswadfrfaw wavtitwaig
      421 maglitsria vtrrraarak sgennvrivd steg
//
LOCUS       WP_284874783             269 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Corynebacterium
            suedekumii].
ACCESSION   WP_284874783
VERSION     WP_284874783.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..269
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29323
     Region          5..269
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mnalelvkdw pvdnvaaavi dgddihrigd lgqvfelasv tkplsaygfl maveegifel
       61 dtplgpdgst vrhllahasg vgfregdkvr evgerriysn ygfeilasav eeaagmtfae
      121 ylqagvmdpl gmkwtrlrgs agweaegtvh dlitflielm hptllhsstm eeattvqfpe
      181 lngivpgygm mkpcpwglgf eikgtkdphw tgpsmpentf ghfgqsgtyl wlapgtgram
      241 valtdrpfgd wakplwaetn eavwreleg
//
LOCUS       WP_284874792             546 aa            linear   BCT 25-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Corynebacterium suedekumii].
ACCESSION   WP_284874792
VERSION     WP_284874792.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..546
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59697
     Region          7..527
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 msllprlsrr rflqstalag tavaagttrv qaatvplpfl hgvasgdplp tsvvlwtrit
       61 pdadalpgsg lgaatrvrwe vgidaafhhv vssgevrtda asdhtihvdp fdlepdmvyf
      121 yrftvldgph agsqsptgrt rtapafdssp eqltaavasc anwesgyfsa yadmatrgra
      181 geldlvvflg dyiyeygrge yvgkngavrp hepaheiitl qdyrirhghy rtdpdlqaah
      241 aalpwvliwd dhetadnswr egaenhdpat egawlsrrda alqaylewlp vrtaspsagg
      301 hlyrsfrfgd laelmmldlr syrdqpaaws ptaladfndp artmmgseqf ewlrrtidts
      361 pahwtvigss vmfsptnllp lqqnpqtssv aeflgartaa gipmnpdqwd gfaadrgrll
      421 ellrvsgrpa lfltgdihse wahdvwagdq ligvelvcts isapnvdeil klpadnaish
      481 laealvrevn phirhvdlda hgysiarlrr dgvemrwlrt vdvvvpgtgv etaiglawqp
      541 grgfgi
//
LOCUS       WP_284874820             110 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium suedekumii].
ACCESSION   WP_284874820
VERSION     WP_284874820.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 110)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 110)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..110
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12090
     Region          17..92
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(22..23,27..29,42..44,53..56,58..59,62..63,65..66,
                     72..74,79..81)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mslehrlepd adlltlaset lkllaeptrl hlmwqldkke hnvgelveat gasrtvvsqh
       61 laklrlgglv atrkdgrhvy yriadghagr lvtealsrad hertgapthd
//
LOCUS       WP_284874830             154 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium suedekumii].
ACCESSION   WP_284874830
VERSION     WP_284874830.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 154)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..154
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16485
     Region          6..82
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 meqfsttdie aadsiisald srlrvliilk lakrdhfvhe lvssleksqp lisqhlrvlk
       61 rsgivdserr grevvyrlaq egaadliaaa valgrtivre gegadvisld rgkgtramde
      121 ggqlahapaa isqdvvsdtv pdpsptpplp rsft
//
LOCUS       WP_284874965              80 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium
            suedekumii].
ACCESSION   WP_284874965
VERSION     WP_284874965.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 80)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 80)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10648172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..80
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=8639
     Region          22..75
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 maercaserr iggvgagprs nphgltpqee qitarvadga tnsevarels lstktveyhl
       61 trvyrklgvk trqalrehlg
//
LOCUS       WP_284874979             885 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            suedekumii].
ACCESSION   WP_284874979
VERSION     WP_284874979.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 885)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 885)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 885)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 885)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12130740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..885
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..885
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=97263
     Region          17..135
                     /region_name="AAA_16"
                     /note="AAA ATPase domain; pfam13191"
                     /db_xref="CDD:433025"
     Site            39..46
                     /site_type="other"
                     /note="Walker A motif"
                     /db_xref="CDD:99707"
     Site            order(40..47,107,139)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:99707"
     Site            order(102,104..108)
                     /site_type="other"
                     /note="Walker B motif"
                     /db_xref="CDD:99707"
     Region          <104..885
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Site            152
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:99707"
     Region          825..878
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mftthnlgsq qstttllrtv idevtelepg ggllflatgp agsgksslvr eiarslpgws
       61 girvtalswq agndgqlleh ilqraghdgs lldlvdrega staividdvh wadpdtlrql
      121 ieatrrlrhg rlavimtasd addaneelpm srlreiadha vmlapldied vaalvlsivg
      181 ahltpltaae lrditggrpg rirevlqaap adhwrlsnpq ipipkpwraa larrsrdldl
      241 gailtavail pgtgrgtpel irfladdadg rlldtavtad lleivpragd rivqfshptd
      301 ravirattgp aemnrlhrra aqfhradhnv daalihealg aeghndatsl eladraeqlg
      361 aggqwlnaae mftlasrvas npdvihdqhl nsiealiaaa diprarlhag slsrvardvk
      421 vdsmraylal hegrrsesvs lidrawqtle etrstdaamr srvasrkvli hlanwepeqv
      481 vhwagvtdew apthsptrie aqyiamigks aitrtippdv plpgetptqa qrrnmaagwi
      541 slvhddtvsa rqylqynsag egserislwm dgwlartlfv lgeyrqgerv verglaraer
      601 ygikflepll lwtgaqiaay rgdrelaray vnrltfshdt fviqripsam crmliasieg
      661 dtsgmtrage tlvnignevd isqpgfwpwe dvwaqqlvls grideadeiv trteeraaes
      721 gigslhakla vpragilmhr gdieggirrf eeaielietl ampsyqaril yeygrvlrrl
      781 grrrqadeif aragdvfaam gatefvdrcn rerragglgt rttgaggltp qeeeiaklva
      841 egatnrevar elflsaktve yhltrvyrkl gvrtrtelpk alrdl
//
LOCUS       WP_284875013             540 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Corynebacterium
            suedekumii].
ACCESSION   WP_284875013
VERSION     WP_284875013.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..540
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=58108
     Region          1..527
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtrqpllevt dlvvsyatag grevhavngv slavhagqit aivgesgsgk sttaqaiigl
       61 lpgnadidag eirldgrdla glsekqwrgi rgtriglipq dpnnslnpvk tigesvaegl
      121 avhrrgtaat rkarvlelle qvgiddparr ydqyphelsg gmkqrvliaa avalepdlii
      181 adeptsaldv tvqkiildll ddmrrqlsig ilfithdlav agdradhivv mqrgevresg
      241 yaatvltdpr dpytrqllad apslavadvh rrrpvpdgda ppllvvdgvt qrfgdftavd
      301 dvsftvdrgt thavvgesgs gkttlgrsia lfnqptagsi tvdgteittl grkqrrdlrr
      361 siqlvyqnpy ssldprqtig atvaeplrnf trsgkaeaat rveryldlva ldsgtaarrp
      421 aelsggqrqr vaiaralile pellvldeav saldvtvqaq ilrlldelqh elgltyvfis
      481 hdlavvrqis dtvsvmsrgr qveagpterv frapesdftr qlidaipgrr yrggdlnlgl
//
LOCUS       WP_284875300             410 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Corynebacterium suedekumii].
ACCESSION   WP_284875300
VERSION     WP_284875300.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..410
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44899
     Region          1..410
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 msrvivigag mvglstawhl qergfdvevf dregvaagss wgnagwlapa ktiplsdpsl
       61 wrygptalld pdaalsmpir fdpklwmfla rfmaqatqra wddtmanltp idkvaleafd
      121 elelggvdav thqgpfvigf eeesqsagfl reiegairhg qeapmerlad pqelapmlsd
      181 kvkvayrleg qrfiepgpym ealaqavekr gghirtdadv ahvaradgpg rpavilasge
      241 rieadkivia tgawmsrlar efgvrtlvqa grgysftvat qepaehsvyl pyhrmactpy
      301 qgrfriagtm efrrpdeply prrieaivnk ardimqgvdl ddrqdewvgs rpvtpdgmpl
      361 vgqtnaeniy vagghgmwgv vlgpatgryl aqlmdtgevh paiapfdplr
//
LOCUS       WP_284875417             461 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Corynebacterium suedekumii].
ACCESSION   WP_284875417
VERSION     WP_284875417.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..461
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=49857
     Region          178..416
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 msalivtgli cgliflaalk rpqwgvlaia alvpfhglli iapvalslwk eaavlavava
       61 allasrardr atvapwlapa avlvlfgvis tvwvlrtnag fpikiaffyl lvavivyyhp
      121 ftrrdkdhlv tillttgtls alfglaqqvl ggerlvemgy dwneslrttg pllrsfgtfn
      181 qpfpfglylm lvlvvvgtva lsqpgrlrsr ifwllspvlv aamlssvvra afvglivavf
      241 vvgviihrrl liyagillaa vvvaipfava vdqrgvlaal fssssledrg ghwaatlprm
      301 lvrplgdglg ttgsaaekvl eafyprtgly qpdnqylkvg lelgvlglal yavtigmaiv
      361 vlrrvirvvr dpleqgvaag vlaataaacv aaafstylei fpmdfffwfl lavaaslpre
      421 earavggwrr ernperrarq errealgevr rgrtyvpmir p
//
LOCUS       WP_284875520             104 aa            linear   BCT 25-DEC-2024
DEFINITION  Rieske (2Fe-2S) protein [Corynebacterium suedekumii].
ACCESSION   WP_284875520
VERSION     WP_284875520.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..104
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=11088
     Region          1..104
                     /region_name="NirD"
                     /note="Ferredoxin subunit of nitrite reductase or a
                     ring-hydroxylating dioxygenase [Inorganic ion transport
                     and metabolism, Secondary metabolites biosynthesis,
                     transport and catabolism]; COG2146"
                     /db_xref="CDD:441749"
ORIGIN      
        1 mgdiacavdd lspgeslvit idgrkvtvvr dleggfhaid dacphvgwpl nkgsvhpdav
       61 iecslhhglw clrtgeprry partpatvha vevrdgqvwv slgd
//
LOCUS       WP_284875608             153 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium
            suedekumii].
ACCESSION   WP_284875608
VERSION     WP_284875608.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..153
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16432
     Region          90..136
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(90,94,119)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(93,118)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(100..101,112,115,119..120)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mtmtfrnvda hvdddpaswp feakiiaver gvlshyhriv racrrdpqva qefleacdvl
       61 greggagvva yliegsdegs hrracafdmr ravemsglsq nqvaevlgts asrlstylag
      121 rvvpsavmqe rilalappkp wpvgvlpsas mag
//
LOCUS       WP_284875777             368 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium suedekumii].
ACCESSION   WP_284875777
VERSION     WP_284875777.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..368
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38389
     Region          70..360
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mhhltrprlt vaalaltcal lpapalaggp tpasppaata tltpvttplt ddapswrhav
       61 aahsdervdv levtahspam grdvplvvit ptgdaprptl yllngadgge gaanwidqsd
      121 ildfyadknv tvvipmagaf syytdwlepa pdlggvqkwe tflteelpgp ledrfhgngq
      181 ravagismsa tsslllaqhh pgfyravgsm sgcaatttga gnfglgltlq rggatpemmw
      241 gpvdgpvfre hdalinaerl rgteiflsng sglagpwdlp sspylagqtq qqasesmatt
      301 igvggaieaa snscthdlka kldslgipad vdftdvgtht wgywqdalrs swptfarafn
      361 laddlagg
//
LOCUS       WP_284876163             104 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Corynebacterium suedekumii].
ACCESSION   WP_284876163
VERSION     WP_284876163.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..104
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=10594
     Region          2..104
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mswiilllsg afeavwaval dksagfsrlg psivfvvali ismgglawal ktlplgtaya
       61 vwvgvgasla viysfvtgqe avsalkilfl lmvvggivgl klas
//
LOCUS       WP_284876235             228 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            suedekumii].
ACCESSION   WP_284876235
VERSION     WP_284876235.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..228
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24369
     Region          1..202
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mllkhapita sdlaerlems aagirrhldi lvaeglaeqd arrprpagtp srgrpakafr
       61 lterghvqfg hsfdqlaada ldslreaggq davralarrr irrivegiep atddpesvqr
      121 vaaelaeafd rhgyaatvne aghgvqicqh hcpvasvaad hpelceaehe tisslvgvhv
      181 qplatitggh gicttniplt psptqtptsq kkgadhdpgn aehrdprr
//
LOCUS       WP_284876245             843 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium suedekumii].
ACCESSION   WP_284876245
VERSION     WP_284876245.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium suedekumii
  ORGANISM  Corynebacterium suedekumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 843)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 843)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Corynebacterium suedekumii"
                     /db_xref="taxon:3049801"
     Protein         1..843
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=94563
     Region          14..836
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mlpdltdvpe slldesifds flswvrgrgi elypaqeeaa lgilagdnvi latptgsgks
       61 mvanaahfia margqrsfyt apikalvsek ffalceifgp envgmmtgda tvngrapiia
      121 ataeivania lrdgrdadid qvvmdefhyy sdpergwawq vpllelpqaq fllmsatlgd
      181 ttflqedltr rtgrttslva gstrpvplef syvytpvhet ieellkdgka piyvvhfsqr
      241 eateraqalt slkiiddetk ekivaeigdf kftttygrtl skllrrgigv hhagmlpkyr
      301 rlverlsqtg llkvicgtdt lgvginvpir tvlftglaky dgvkqrilks refhqiagra
      361 gragydtegt vvieapehei enwrlrqrag tdekklkklr kksaregevt wsektferlt
      421 taepepmvsq frvsnsmlin viarpgngye hlknllrgnh dtrakqnrdi ltalelfrgl
      481 vnagivvkaa dgvdsegrpy hlteelqrdf alnqplspfa laavtlldre aesythdvis
      541 tyeailddpr qvlvaqqkaa rgeeiaalka egvdyterma iiedvtwpkp laeeledafd
      601 tfaeghpwvr efelspksvv rdmiehamtf sdliatygla rsegvvlryl tdawrtlrqs
      661 vpqeamtdql ddvvewlgel ikqvdsslvd ewahmsddet piskealere lafgvedpsa
      721 ltsnrrafti mvrnlmwrfv elfayekedd larlteyler ddrpdfgaam ddyfdeyadl
      781 dtgmdarste yfhltqdgrl wtvrqtikdp egdnsfafva vvdldasdea gevrltslei
      841 eqr
//
LOCUS       WP_284876306             349 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Acinetobacter pittii].
ACCESSION   WP_284876306
VERSION     WP_284876306.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter pittii
  ORGANISM  Acinetobacter pittii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426811
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Acinetobacter pittii"
                     /db_xref="taxon:48296"
     Protein         1..349
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=38618
     Region          62..347
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mnkffkvmtl saaigvlgls qanaeydpnl ksidtppavs qqmfnkvkse glgqyayakg
       61 lsskfieseg vklhyveggs kgtpivfihg fgstwkmwep vmlsymkdhk viaidlpglg
      121 qsspilnddy saentskili gaikqitkne piyyvshdig ntasyplvan nqdyvkkvvf
      181 mdspipdmet fnhpgyspkg pglgwhfgyf sfgdiaekqi andpnlflsy fiktyagkkd
      241 iftpellael iepystrdnl kaafgyyrsk kdsalqneal lannkklfip amalsgekgv
      301 ndvlikemra kfvedpakle avilpntghw lieenpegve kslsnflfk
//
LOCUS       WP_284876307             480 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Acinetobacter pittii].
ACCESSION   WP_284876307
VERSION     WP_284876307.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter pittii
  ORGANISM  Acinetobacter pittii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Acinetobacter pittii"
                     /db_xref="taxon:48296"
     Protein         1..480
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=56030
     Region          6..480
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 msnvnqliwf rqdlrvrdha alwhasqqgp cigliilspe qwkmhhdapi kinfylrqlq
       61 qlkkeleqln ipliiqvipy wkdiadyige lstqlnienv ysnieigvne lkrdktvqdf
      121 lnqqgkelfl fhdrtifplc sirnqsqqpy qvfgafkkac yskldisglp qcypipekqs
      181 sypasfskin sltledieaf fdpsvskeqq glwpagenfa leqldifikd rlsdyklerd
      241 fpnvrgtsql spylnigils irqclqalfr aehgnfhltn egqqtwldel iwrefyqhil
      301 fdfphvskhi pfkkdtqkik wnhnpehlia wqtgqtgipi idagmrqllk tgwmhnrvrm
      361 itamflcknl lidwrvgeqw fmehlidgdl aannggwqwc astgtdavpy frifnpiaqs
      421 kkfdpngdyi rqwveelahl dnkaihepys tktniqlnyp kpivdfketr lkaietfksi
//
LOCUS       WP_284876328             744 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Acinetobacter pittii].
ACCESSION   WP_284876328
VERSION     WP_284876328.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter pittii
  ORGANISM  Acinetobacter pittii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 744)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 744)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 744)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 744)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Acinetobacter pittii"
                     /db_xref="taxon:48296"
     Protein         1..744
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=80522
     Region          60..744
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mefiksrkki aksaiassls ivattamaaq ensvalplih vqadaevaqs lkvdksansk
       61 fvapllntpk svsviskqli edtkvntlsd alrtlpgitl gageggnpng drpfirgyns
      121 essmyvdgir nsssqnremf aieqvevtkg sassmggags vggsinmisk vakkgdfleg
      181 svqagtdnyq ritldgnkdf gngtagrvvl mghknekagq sdgaeykrvg iapsitfgld
      241 tptratlsyy ylrsddtpds gvpynydtak katvgkpvdf kqgiyyglkg rdfqkqenhi
      301 gtfkvehdln enltlantvl yskskndylw tqpddskgnv angkvwrrin sritdtdift
      361 dqlslrgkfn tgaikhsfnv gaeysdqesd kgsytttypg yagsttggfn sdcaindawc
      421 tsltnpnskd awlggriank attttttknt svylldnief npqwlldlgv rwdkfdteqv
      481 tnatgakies nkdfvtynag vtfkptengs iyasyatsan pvgvdggdgs esigqaymdl
      541 kpeesqtiel gtkwnvlnek lnltaaifrt ekqntriqvd sstytnggds kvdgielsan
      601 gnitdkwavs agytyldsen tdpgpscsra gvcnpenaak gkqlpnvpkn satlwttykv
      661 lpqftvgaga fyadkvygda antkwvpsyv rydamarynv nknvnlqlnl nnlsdkryft
      721 kayashyate aegrsavlsv nfky
//
LOCUS       WP_284876346             265 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Brevundimonas sp.
            MEB006b].
ACCESSION   WP_284876346
VERSION     WP_284876346.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 265)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..265
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27980
     Region          1..248
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mnrtvlitga sagigaalar iyaaegwnvi ltarrqaplq aladdltaah gvtatviped
       61 lsdpaaperl vatietrglt vdglvnnagf srvtgfldtd lgahrammqv mltapvelsr
      121 lllpgmiqrg fgrvlnvasl agqmpatggd tlygpiksfl ikasqglhle tqgtgvhvtv
      181 lnpgytltef hdvngsreqv ssaypawmwm daarvarigy daceanrpsv tpgvmnnvma
      241 glarflpdgl alrmvanhak rldri
//
LOCUS       WP_284876358             222 aa            linear   BCT 25-DEC-2024
DEFINITION  Crp/Fnr family transcriptional regulator [Brevundimonas sp.
            MEB006b].
ACCESSION   WP_284876358
VERSION     WP_284876358.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..222
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=23449
     Region          45..206
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 msqsnlahal lsalavqgld egdaffaeag artsttqhge avvtlilsgv larigldgtl
       61 shglassddv infdavlggg gpesavwlta gryltvsark laqkidrdsl vemalidlrr
      121 rnialqaels rhatlkvsqr laallldvhd rkggdvlalr qtelshlmav rrasistact
      181 elcaagavrl rrgaiqitda dalrrmtdea ystvtdlarl rg
//
LOCUS       WP_284876375             298 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Brevundimonas sp. MEB006b].
ACCESSION   WP_284876375
VERSION     WP_284876375.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..298
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33508
     Region          2..215
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mnptisivip lynhkkyias tiysvlcqty paaeiividd gssddgvrqv ellaearpei
       61 ivwkqsnrga hntinsgigr atsdviciln sddlyhperl davasafrnd gdlaavftam
      121 dfvdgqgspt efpwyeqala fyretglwga slvngnflvt tsnlaarrtv fediglfgdy
      181 ryahdldffl rmsrsdqkvr fmdqrlmsyr ihdtntiseg hdrvkveway italhlfrlc
      241 qgrseaivey aeildrhgll kavlttwafm igapdtatdf rafrrnqdqy galveals
//
LOCUS       WP_284876450             306 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Brevundimonas sp.
            MEB006b].
ACCESSION   WP_284876450
VERSION     WP_284876450.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..306
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32438
     Region          13..305
                     /region_name="COG4798"
                     /note="Predicted methyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:443826"
ORIGIN      
        1 madrlasasg lsrrfllsga aalgltgvaa cgrkdeaaka paapptsagp pegslewave
       61 gswrsaqdka rdafrhpmet lrffglqpkm tvvefwpgsg wyteilapyl akgagiyvaa
      121 lfpegptadp aqavlntafr trfssdkkly gepqfsvfga gsgpviaagt aemclfmrtl
      181 hgwmaagiae kafadafaal rpggilgveq hrlspaedqd pvaangyvqe afvrqlaaea
      241 gfvfveasei nanpedtkdh pfgvdtlapt rltaprgepa dpafdrskyd aigesdrmtl
      301 kfrkpe
//
LOCUS       WP_284876455             126 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Brevundimonas sp.
            MEB006b].
ACCESSION   WP_284876455
VERSION     WP_284876455.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..126
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14192
     Region          <23..84
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 maddidlhlg rrlrrrrrll gltqqqlavq vgirfqqiqk yecganrisa arlwqlaeal
       61 etpiayfydg laeameadap tpkggevfsr ketldliqay yqlderprrr lldlarslha
      121 gdaaaa
//
LOCUS       WP_284876497             142 aa            linear   BCT 25-DEC-2024
DEFINITION  HPr kinase/phosphorylase [Brevundimonas sp. MEB006b].
ACCESSION   WP_284876497
VERSION     WP_284876497.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..142
                     /product="HPr kinase/phosphorylase"
                     /calculated_mol_wt=14594
     Region          7..128
                     /region_name="HprK"
                     /note="Serine kinase of the HPr protein, regulates
                     carbohydrate metabolism [Signal transduction mechanisms];
                     COG1493"
                     /db_xref="CDD:441102"
ORIGIN      
        1 mtpgqpvhat tvavrrrgaw qgvmilgpsg agksdlalrl iargwrlvsd dytqvwasdg
       61 avhasapasi agrievrglg ivaartrpvc rvalavacma egverlpepq tqafagvdlp
      121 llaldprpas avdvvaaale tl
//
LOCUS       WP_284876582             303 aa            linear   BCT 25-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Brevundimonas sp.
            MEB006b].
ACCESSION   WP_284876582
VERSION     WP_284876582.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..303
                     /product="isopenicillin N synthase family dioxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33702
     Region          5..302
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 mtqydadfqa fsdalgasfs rygfavvadh gldearitaa iddakaffal peevkrqyhq
       61 pgtggarglt pfgveaakda ktvdlkefwh vgrelpeghp yrrymrdnvw ptevegfreh
      121 lygmfedlda lgakilraia rylrlgddff adkvemgnsv lrmlhyppvp adapgvraga
      181 hedinvitll lgaeeaglql kdkdgswldi apppgalvvn igdmlqrltn hvlpstthrv
      241 vnpaperrgf arystpfflh fnpdfpietl psaitpdnpd ryagktilae dylterlrei
      301 rll
//
LOCUS       WP_284876598             256 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Brevundimonas sp.
            MEB006b].
ACCESSION   WP_284876598
VERSION     WP_284876598.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..256
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27021
     Region          4..254
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 melfdltgkv aiitgssrgi gkaiaerlae hgakvvissr kagpcdevaa eingkygegr
       61 aiavpanias kddlqrlvde tnaafgqidi lvcnaatnpy agpmagiadd qfekilqnnv
      121 isnhwliqmv apqmverkdg ailvissigg lrgnaligay niskaadmql vrnlavewgp
      181 snvrvnciap glvqtdfaky lwenpellkq vtepaplkri gqpdeiagta vylcspasay
      241 vtgqtlvvdg gltiaw
//
LOCUS       WP_284876644             193 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Brevundimonas sp.
            MEB006b].
ACCESSION   WP_284876644
VERSION     WP_284876644.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..193
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=21350
     Region          1..193
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 madpslgady fedvfagdpd pwgldsrpye aekhartvas lgdrrfrrgl evgcaggalt
       61 arladrceal valdisrtal drarrrlghr pqlvfrqaaf phgmdlagpf dlivlsevay
      121 ywsdedlaaa aefvrahlvs gglvllvhwt getdypqtgd gavtklwrdl edsltvslde
      181 rqpayrldlw rrp
//
LOCUS       WP_284876747              80 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Brevundimonas sp.
            MEB006b].
ACCESSION   WP_284876747
VERSION     WP_284876747.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 80)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..80
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8702
     Region          2..65
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mpvrvtldrl itakglkard laqqvglset qlslfrsgkv kgirfrtlar lcaaldckpg
       61 dlldylyeps dqaigpdedn
//
LOCUS       WP_284876808             221 aa            linear   BCT 25-DEC-2024
DEFINITION  glutathione S-transferase family protein [Brevundimonas sp.
            MEB006b].
ACCESSION   WP_284876808
VERSION     WP_284876808.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..221
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24690
     Region          1..218
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mikvhhlnds rsqrvlwlle elgldyevvr yernpgnrla ppellaihpl gkspviedga
       61 vkvaetgaiv eylldtygqg rlrpaagted grrftywlhy aegsamppll lklvfsmlpr
      121 rapallkpiv ngvankaits fvdpqlrthv gfwedelgrs ewfagdhfta adimmsfpve
      181 agadrafnae tkprlkafln riharpayqr alerggpysy a
//
LOCUS       WP_284876820             286 aa            linear   BCT 25-DEC-2024
DEFINITION  metalloprotease [Brevundimonas sp. MEB006b].
ACCESSION   WP_284876820
VERSION     WP_284876820.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005085
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..286
                     /product="metalloprotease"
                     /calculated_mol_wt=30046
     Region          67..220
                     /region_name="SpoIVFB"
                     /note="Zn-dependent protease (includes sporulation protein
                     SpoIVFB) [Posttranslational modification, protein
                     turnover, chaperones]; COG1994"
                     /db_xref="CDD:441597"
ORIGIN      
        1 msntdttdqt pgrtpgpwda kpeatsaret aptpaveapv ekdqslvwam lstalmggfl
       61 wwitgsaiva gavliglfvh eaghalvmnk lgmgpariyi ipflgglaka rrepksewdg
      121 vlvslagpaf gllamipfvg vwivlgqgew ligaffiaml nlvnlvpapp ldgskalgpv
      181 ltrvhprleq ivllvigvav vwwglttgrf ilaaflalsv fshlkrgvwr pawgtlswpe
      241 aakslalyll tlavcaaaav galmpmtggd pagavqlgln ylgfgr
//
LOCUS       WP_284876874             404 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Brevundimonas sp. MEB006b].
ACCESSION   WP_284876874
VERSION     WP_284876874.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..404
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42617
     Region          1..392
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mpglktlavv vtvkggarwe pldrsgwshl lehlvfkgag dmaareiver ieaeggtina
       61 stgyertsfe vrgldgslpl amkvlsdlvf rptldpaeie rekdvvaqei aeafdtpddh
      121 vfemvqtraf akqplgrpil gsvaslksad katveawrar lyspdrmvvs vsgavdetel
      181 lalaerwfgd avatpadapa paafvgghak ltrkieqanl vfqlpalsat dpalsamrlf
      241 geilgggmas rlfqsareer glayaidayq epyedtgvlg iyagaaadra kelaevsaae
      301 vralaetgpt ekelsrakav mkaglwmsde npmsragrna aqtlifgapr sslsmteqle
      361 aqtiedvrav ggrvlasgha asavlgpksa apageafata lfgg
//
LOCUS       WP_284876881             349 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Brevundimonas sp. MEB006b].
ACCESSION   WP_284876881
VERSION     WP_284876881.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426811
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..349
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=36449
     Region          53..314
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 msnvirpcrg vfapsrlaii lgvviacava sdharaqsap pvassatpfv sdrlsvevvg
       61 qgpdvilipg lassrevwra tadrlkashr vhlvqlagfa gepwthgdga fiqpevdela
      121 ryirqarldr pavighsmgg lsglllaqqq pdlvgrvmtv dslpfysamf gptataesak
      181 pladqaanmi lsadtasfrt qqeataqals ltpseqariv awslatdrha masamkdvmt
      241 tdarpglatm ttpvtalyaa dadggapvam adamwtreya alpgvslirv dgsrhfimad
      301 qparfaelvd aflancalki lpanggglvq pffgvtspal tgapsnwsa
//
LOCUS       WP_284876913             949 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Brevundimonas sp. MEB006b].
ACCESSION   WP_284876913
VERSION     WP_284876913.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 949)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 949)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..949
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..949
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=99410
     Region          414..663
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          562..846
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
ORIGIN      
        1 msgasptkri lkttvaaata gavvfapmap laqevgrsrd plsinigana eftrvefggv
       61 igvrsrisre gdkvvvrlgt taapdvsrlk vdppagvksv etrpsrgagg tdliltleqg
      121 adarsgvadg avwlnlyapg kapeggdaaa pqttkavvpv raetaggktv ltfdwgapvg
      181 aavfrrgdav wvvfdtaarm dmsgakalgs aknaqwaagp gytalriaep eglgvsaqgq
      241 ggtwtvtlgg pdgaaggvev grsddgapvl vaqmagatka vwltdplvgd rfaavtalap
      301 gkgyaggrrt vdlsliptaq glavetaadd lkieaagdlv tlsrpkglal sspaagletg
      361 dhnadapkra aypalideaw aatgeagfsd ryrrlqdaag letiaaadnp rapiearmal
      421 arflvgsgln yeaigvlnal iakapnlqge pevrglrgva rvgvgrleea qvdfagaala
      481 ndpatkvwlg yiasemgdwe garrnfaaga paidsfpkew rarfgaaham aaiqlndlpa
      541 aqqllayvfs qdapavdqlt arlvqarmfe lngdknrala vykavarapl dgiatpaklg
      601 aisleldkga itpdqataql eqlkwrwrgd atemavvrkl sgiylqqgry realdalrga
      661 gkrmagvpga aevqadqana fralfldgaa dglqpvqala lfydfreltp igadgdemvr
      721 rlsrrlidvd lldqaaellk hqvderldgv akaqvatnla tvylmdrqpe kalqaiwgsr
      781 ttllpnamns erralearal mdlgrfdhal evldrdqsnp arevradifw kqqkwgeaap
      841 iyearlgdry ktattpltpa eeswliragv gyslagdraa lqrlsgrfgp mvpgarsaaa
      901 lrvalddnls gvagtgdfan lssqadtfvg wvnsakqafr keadaksaa
//
LOCUS       WP_284876963             170 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Brevundimonas sp. MEB006b].
ACCESSION   WP_284876963
VERSION     WP_284876963.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..170
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18169
     Region          10..148
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 madishepsp daavdatasl vrsvrriaqa idvrsreisr ltgltlpqll vlqsiralge
       61 vstsaisrdv smsaptvvav ldkleakgma aryrstvdrr vvhmrltdag rqalqtspgl
      121 lgdgflaala elphserlam aeaverlavl mqprdsqasl kphyqavrps
//
LOCUS       WP_284877096             495 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Acinetobacter pittii].
ACCESSION   WP_284877096
VERSION     WP_284877096.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter pittii
  ORGANISM  Acinetobacter pittii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Acinetobacter pittii"
                     /db_xref="taxon:48296"
     Protein         1..495
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=56269
     Region          6..449
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mfnstsnsnk nvriaiigtg fgglglairl kqagfeqftl fekaadvggv wrdntypgaa
       61 cdvpshlysf sfeqelgwkn rygtsqeiyq ylrhcadkyd irphvqfnte iasaefdalq
      121 gvwhiqsttg eqfeaeflvg avgqlnrpay pklkgienfk gkafhsarwd hdydltgkrv
      181 avigtgasai qfvpeiakqv ahldvyqrsa pyvipkpdrv yqplekkafr klpilqsldr
      241 alqyghheir llafttslne mplveylfqr hirkvvkygk lrhrlmpdyp igckrilisn
      301 hwyetltqph vdvintgiqe itengildtd gnlrevdtii ygtgfaatef mapmqitgld
      361 grtlkdtwkd gaeaylgltv sgfpnffmly gpntnlghns ivymiesqvn yildaiqttl
      421 qnkllftnvr aevqhefnqs iqekmkktvw aqgctswyqt adgkntnnwp gftleyrqrt
      481 rrfdvenytq vsais
//
LOCUS       WP_284877266             246 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Brevundimonas sp. MEB006b].
ACCESSION   WP_284877266
VERSION     WP_284877266.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426811
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..246
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27086
     Region          11..240
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mtdiqhlcrp dgetlafkrv egggptviwv ggfrsdmegt kalaldvaar ergwnfvryd
       61 hfahgqssgd wrkatigrwr edavalidsl sgpvipvgss mggwvsllat larpdrikgl
      121 vlvnpaqdft erlmwpglad herqailreg etliveeglg eyvltrrmfd eardwllldg
      181 vidiaapvhv lqgraddvvp wrhqvelver ltggdvrldl ieggdhrlst padldrlvaa
      241 veamrg
//
LOCUS       WP_284877524             172 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Brevundimonas sp. MEB006b].
ACCESSION   WP_284877524
VERSION     WP_284877524.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..172
                     /product="YceD family protein"
                     /calculated_mol_wt=18918
     Region          10..170
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 msatlpyset vrvnqigagl srrlepdadt rkriarsldl qglddfavdl eikptpstse
       61 wtmkgrvtah avqtcgltle plpvdvnrrf fiqlveakpe etdeievtld eedadviedg
      121 kidlgqyave qlvlsldpfp rkpgaefvqp eepteispfa alkalkskdd qg
//
LOCUS       WP_284877533             278 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Brevundimonas sp.
            MEB006b].
ACCESSION   WP_284877533
VERSION     WP_284877533.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..278
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29724
     Region          22..277
                     /region_name="COG4798"
                     /note="Predicted methyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:443826"
ORIGIN      
        1 mrayrdksme tvmigklaag atalvlaagl sgciiidsdg gertvvapaa daqpagyssl
       61 yadavadpkr paeevardpl rhpaeilafa qlepgdkvad irpgagyftr lfsdvvgptg
      121 rvyafvpert marenagada lvaaysnvtr vnglldsmtf aepldmifms qeyhdfhipg
      181 fntdvarmna avfaalkpgg ryilidheaa pgtgisavqt lhriegdylk reveaagfvf
      241 egasqavanp addhslnvfd ekirgktdqf vyrfrkpg
//
LOCUS       WP_284877666             310 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Brevundimonas sp. MEB006b].
ACCESSION   WP_284877666
VERSION     WP_284877666.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 310)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..310
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=34256
     Region          38..292
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mtqgaedgvr iglsavvmtl rdrqavvltt ptedgsralp fgpfdpvrdr tferalrdfv
       61 tdqtgfrlgf veqlytfgda graspratpg pgrhrevsvg ylaltpdaae gqthdarwda
      121 vfeffpwedr rgghdarite glhawadgde hrlararalf altpdhrwne ervleryell
      181 yearlvaeaw rdadlsptqp mpgrimssdh rrilatalgr lrsklkyrpv lfdltpgvft
      241 lsqlqagaea vsglslhkqn frrgvertgl veptgqlsst tggrpaelfr fkgvdaqtga
      301 apglslpaqr
//
LOCUS       WP_284877699             337 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Brevundimonas sp. MEB006b].
ACCESSION   WP_284877699
VERSION     WP_284877699.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..337
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34749
     Region          7..336
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtssspiviv gagvlglcta felhrrgrav lvvdpgevna slvaagmiap amesaiddvs
       61 ldraqlfrag cdlwsefasa agialarrpa ewrggdvgam earlralgfd arrdgasvtt
      121 dddyqveptq alaalrqalg eavvagtvtt iaradggwrl eigdqwldae avvlatgacd
      181 aiaglpdvar rlieeiqpir gqigvaaehl vdhvvrgpga yvapmasgav igatmepgrr
      241 dttpdaease rltqaawaal grspepltie wrvgirgata dglplagsap geeglflala
      301 prrngwllgp lvgavvadai egrtasphar aldpgrf
//
LOCUS       WP_284877766             302 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Brevundimonas sp. MEB006b].
ACCESSION   WP_284877766
VERSION     WP_284877766.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..302
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31028
     Region          12..291
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mtslalkthl nsplaarlip ylalfagmvt lacgtsfakt lfpvigaegt sayrvgisav
       61 llvavfrpwr frltradlga ialygvvlga mnlsfymalr tiplglaiai efmgpltlal
      121 ihsrkpihfa ciglavvglg lllpikagag aldpvgmala afaglcwaly ivfgkrlshl
      181 hagqsvalgm svaamvvvpf gvahagaall npaiilagva vaifssalpy slemvalrsi
      241 pkrtfgvvls aepavgalag llilhehltg qqwlaiaaiv aasvgaiatt retkieleps
      301 ap
//
LOCUS       WP_284877892             512 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Brevundimonas sp. MEB006b].
ACCESSION   WP_284877892
VERSION     WP_284877892.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 512)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 512)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 512)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..512
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=54308
     Region          11..510
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          277..510
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mlssiigmag vlaivsrgid ahqarkeegl vrlrltrale tigenlttas vwdeavdrmt
       61 agdvawydrn fgafyaaqhk hqftlgydgt grlfristlg rpaetqvgep fgqaarplid
      121 alraeaagrd rsvtadagvr lkaafvrvgd dvyvlgastv vrhtaggstp asdpvvasfk
      181 pfagelnllr trlaldrihf qpgdaeppkg migvdvrdvg gallgrvvwa peqpgyqilt
      241 kagplllllf ivlligtgsl lwnttadvrr lkasevalsa aleraeaanr aktrflsnvs
      301 helrtplngv lgmaeiigad lvtpqqrerl eilkasgrqq lrlveelldv vrlrdgaval
      361 etrpfrpdnl lqrvandfrg aaeakglkis veaaegewlg dpvhveklma altdnavrft
      421 rtggvmlrav agaglaleve dtgpgmepae aarlfeaftq gdesatrtae glglgltaah
      481 glaalmggki eivtapgags tfrvvlplka va
//
LOCUS       WP_284877908             441 aa            linear   BCT 25-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Brevundimonas sp.
            MEB006b].
ACCESSION   WP_284877908
VERSION     WP_284877908.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..441
                     /product="metal-dependent hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46099
     Region          49..>100
                     /region_name="PRK09060"
                     /note="dihydroorotase; Validated"
                     /db_xref="CDD:181632"
     Region          81..425
                     /region_name="Met_dep_hydrolase_A"
                     /note="Metallo-dependent hydrolases, subgroup A is part of
                     the superfamily of metallo-dependent hydrolases, a large
                     group of proteins that show conservation in their
                     3-dimensional fold (TIM barrel) and in details of their
                     active site. The vast majority of the...; cd01299"
                     /db_xref="CDD:238624"
     Site            order(97,99,262,282,356)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mkrfgialaa lmasalgaha qqtpvatgvs tqpnttfvea grlladpsng vvqrdktlvi
       61 rgnqlvevrd gfvgdasqgk vvdlrqafvl pglidshvhl tsqqnpnarl eevtlsdadq
      121 amvgvryarr tlmagfttva dlgasnqaif alrnavrngd vpgpriiaag ssvsihgghg
      181 dingyredvm hllssesics gpedcmravr tqvragadii kitatggvls ntaaglnqqf
      241 sddelaaivg sahrmgrqvt ahahgvdgin aflraggdsi ehgtylddqs irlfksngaw
      301 liptllagdf variasgpdn fftpaqtaka leagpkmldm arraheggvr iafgtdsgvs
      361 ahgdnaqefa llvragmspl eaiqtatvga aehlrianea gkiavgmpad ivavsgdplt
      421 dvtelermkf vmksgviyra d
//
LOCUS       WP_284878022             209 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-L-isoaspartate O-methyltransferase family protein
            [Brevundimonas sp. MEB006b].
ACCESSION   WP_284878022
VERSION     WP_284878022.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Edwin,R.K., Challa,N., Sharma,R., Satyamoorthy,K., Parsa,K. and
            Misra,P.
  TITLE     PIMT/TGS1: An evolving metabolic molecular switch with conserved
            methyl transferase activity
  JOURNAL   Drug Discov Today 27 (8), 2386-2393 (2022)
   PUBMED   35462043
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Furuchi,T., Sakurako,K., Katane,M., Sekine,M. and Homma,H.
  TITLE     The role of protein L-isoaspartyl/D-aspartyl O-methyltransferase
            (PIMT) in intracellular signal transduction
  JOURNAL   Chem Biodivers 7 (6), 1337-1348 (2010)
   PUBMED   20564550
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Kagan,R.M., McFadden,H.J., McFadden,P.N., O'Connor,C. and Clarke,S.
  TITLE     Molecular phylogenetics of a protein repair methyltransferase
  JOURNAL   Comp Biochem Physiol B Biochem Mol Biol 117 (3), 379-385 (1997)
   PUBMED   9253175
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..209
                     /product="protein-L-isoaspartate O-methyltransferase
                     family protein"
                     /EC_number="2.1.1.77"
                     /GO_function="GO:0004719 - protein-L-isoaspartate
                     (D-aspartate) O-methyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0030091 - protein repair [Evidence IEA]"
                     /GO_process="GO:0036211 - protein modification process
                     [Evidence IEA]"
                     /calculated_mol_wt=22005
     Region          12..192
                     /region_name="Pcm"
                     /note="Protein-L-isoaspartate O-methyltransferase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2518"
                     /db_xref="CDD:442008"
ORIGIN      
        1 mdftaerkam vdsqvrvndv tdraihlamm avprekfcap drafaaysee svviagerrl
       61 mpardvakll qaadaredek alaiaapyaa avlarmgvsv taqesddavf avvgealsea
      121 gvttvvapla qptgegwdli iseggveslp eswgaalrpg grivvverrg aigkaalyvq
      181 treglsrrel fdsspavlae ltpaptfal
//
LOCUS       WP_284878105             384 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Brevundimonas sp. MEB006b].
ACCESSION   WP_284878105
VERSION     WP_284878105.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..384
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41654
     Region          10..358
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mtpvqtpadl rpitalrfga amwvavysfw enlagagqsg lvakgylgve lffvlsgfil
       61 shvylaaage krfsyrgflw ariarvyplh iatligvgll aaaalfagms vdanvlswas
      121 lpaylfmvha wglapvagwn hpswsisaew faylcfplfa fvfwrlrhrp iaavvgaaaf
      181 lvilyfafeq lagfalteat irwgalrivp cfalgcalyl vyrraplkap wlcaavsfgl
      241 mvlsaalglw dgatvllaga lilslaslpn aragwlasep avylgeisys vymvcvpwkl
      301 lavglaaklf dapdkqlqif vwlailallp vvaavsyhlv erparkalrd madkrakrhn
      361 kvsegnmkhg dmpkqlatgr dpva
//
LOCUS       WP_284878121             677 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Brevundimonas sp. MEB006b].
ACCESSION   WP_284878121
VERSION     WP_284878121.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 677)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..677
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=72431
     Region          36..657
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mrpssvsrsl lmaaagstil agaaaaqsap qapaelgdii vtgapygisq rasviatdvv
       61 deqtlatapa aslgdmlsgr pgirstdfap gasrpvirgl sgprvqvltn giglidassv
      121 spdhavatdp aeanrieiir gpatlvyggs aiggvvnvld dripteipeg gvsgvvstqa
      181 ssvddgrsaf grvtvgggnf afnvdgvkrk tddydipapa isarraaaeg laredtgtqp
      241 nsytdleawg vggsyigdkg fggvsykntd seygtvaees vfiklnqkrw dargeyrfds
      301 gpfsvlrgsy ghadythtef eavgepgtif nsdgwegrad lvqrerngwn gavgvqalsr
      361 nfeaigeeaf vpsvkidelg lytvqrldlg nhgfegglry drrelsgtpi ggasevtref
      421 dnwsasaaaf irpaaglflg lslahnerap sevelfadgv hiataayetg dltlnsekvt
      481 tlegtahydr grftgdlhvy hswyngfide rptgdqfyfe eedeffpiyr fvqtdakfyg
      541 felegayalw qdgdrklsle gaadyvhaqt dfgpaaripp ysvtgrlawt stkfdasaev
      601 rhvgeqdrva nafelptddy tlvnasvavr pfaqqnvtlf aearnltdee arehvsflkd
      661 iaplpgrnlr vgvayrf
//
LOCUS       WP_284878134             378 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein [Brevundimonas sp. MEB006b].
ACCESSION   WP_284878134
VERSION     WP_284878134.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..378
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41293
     Region          16..378
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mtdtlaapas tasanskipv tvltgylgag kttllnrilt edhgkryavi vnefgeigid
       61 ndlvvgaded vfemnngcvc ctvrgdlirv vaglmkrqrp gkpafdaiiv ettgladpgp
      121 vaqtffvded vkaktqldsv ttlvdakhvm arlddsrear eqvafadrii lnkvdlatad
      181 eldavearlr alnplapivr aersnvpldq vlglhafdld rilevkpdfv npphgadghv
      241 hdehcghdhh hhdhdhkhdh dhhdhahgah shgarghahq ddikgislsl drpldgakft
      301 awldrllgeq gqnilrakgi idvkgenrrl vfqavhmile gdmqrewgaa errwsravfi
      361 grdldeaalk agfeacaa
//
LOCUS       WP_284878172             562 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Brevundimonas sp. MEB006b].
ACCESSION   WP_284878172
VERSION     WP_284878172.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..562
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58928
     Region          13..>260
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mktfdldgri agwrgpvlaa lltliaglpg llllppldrd esrfaqatsq mlesgdyvdi
       61 ryqdeprwkk pvgiywmqal avgltsdved reiapyrips llgamlaawa vawagsamlg
      121 grvgffggai mgatfllste agiaktdaml cgattlamaa lariymatka gerpirphkl
      181 lfwigiglsi likgpigflv valaiialsi wdrnikwlyr lgwgwglplv almvgpwaia
      241 itiatdggfw reaiggdlap kiagaheshs gfpgmyllla pllffpstll lpaavstgws
      301 rraepairfl vcwlvpgwlm felaptklwh ytlptfgala llaaaalaqp igkvsritga
      361 vlgafaalli igitvygltv ygtstaqtwa altvvmalaa gamggfllln rapvaalvas
      421 lafgivahaa lsgtirqlrp laiapqleka leaadlhprq grtpgpvait gfhepsfvfl
      481 tgrdtdltda qgaaealaeg rpaivegrda dafraaaarl gvsgravgtv ngynysagdp
      541 vsltvyappp rsgngnaaag ae
//
LOCUS       WP_284878179             283 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: metallophosphoesterase family protein
            [Brevundimonas].
ACCESSION   WP_284878179
VERSION     WP_284878179.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas
  ORGANISM  Brevundimonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Brevundimonas"
                     /db_xref="taxon:41275"
     Protein         1..283
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30895
     Region          3..246
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mgrvlqfsdv hfgcehkrac aaaldyahat pndlvlitgd itqkgfpdef taagewmram
       61 peprfvivgn hdvpywdaia rvfhpwrafe tatgfpahdg qfcsdavmvr gvvtargwqa
      121 rpnwskgvid ldqtrraaea lrqapigalr ilachhplie mvgtpmtgdv krgdeaalif
      181 aeagvdlimt ghvhvpfamp ipladrcsya vgcgtlshre rgappgfnqi dwdaktitvt
      241 alawdgtsyr shqvwrlprr qdtrkattap spvepgalek aav
//
LOCUS       WP_284878190             371 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Brevundimonas sp.
            MEB006b].
ACCESSION   WP_284878190
VERSION     WP_284878190.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..371
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37969
     Region          27..96
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
ORIGIN      
        1 mtlnagvape aiesiadrpd ptaafvdaat lgdgfraare rsgkspaela aetkvhrrfl
       61 taleqndwss lpsrvfalgy vrayasalal deqtaverfk respdtsvpl kapigiafed
      121 vkrhspriva giaavvvavi gwnvfqrasl hqtahpsdia avpktwtgaa dpdpqvalsa
      181 pmsappdqtt palyitpgle aeltgvdptd paviaaaanp epvqkafnpr gavygasana
      241 smvviqakta galvvrlgdg qalfarqmap geawrapigv aatvdvsdpa afdvflngey
      301 ggplagvltp laqlnsradq aakalaasqa raqvqaqvqa qaaqartqaa atlgatpspa
      361 papsspapap n
//
LOCUS       WP_284878210             141 aa            linear   BCT 25-DEC-2024
DEFINITION  TadE/TadG family type IV pilus assembly protein [Brevundimonas sp.
            MEB006b].
ACCESSION   WP_284878210
VERSION     WP_284878210.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..141
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=14926
     Region          1..>101
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mrtfgpipsv rrrgregvaa vefalvgpil vllligivvy ggwflmaqsv qalasegara
       61 aiggldpver dglarrevse avrgvalnpk httievmeda grlrvivvyd asdslimalg
      121 gmlprppsvi rrsavihvgd y
//
LOCUS       WP_284878239             193 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent DNA methyltransferase
            [Brevundimonas].
ACCESSION   WP_284878239
VERSION     WP_284878239.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas
  ORGANISM  Brevundimonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Brevundimonas"
                     /db_xref="taxon:41275"
     Protein         1..193
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=21087
     Region          1..181
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 maerslpaay fegifagdad pwslasspye aakfdrtiaa lsvrraafal evgcaggvlt
       61 erlsavcdhl laidvsptal grarqrlsgr snvrfeaadf precpavdgl dlvvlsevay
      121 ywsqadldfa tqrisdglve ggrvllvhwt getdypqtad daverlwlgl savmkvdlae
      181 rhpnyrldlw srr
//
LOCUS       WP_284877390             372 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA dehydrogenase family protein [Brevundimonas sp. MEB006b].
ACCESSION   WP_284877390
VERSION     WP_284877390.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..372
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38726
     Region          1..369
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mplilteeqt mlqdaadgfl neqapiahlr klrdehdddg vsrdlwrafg emgfagviip
       61 ealggmglga veagviaesl grtltpspyl gssilaakvl idggsqaqqa wlpriaagea
      121 ilslavdega khapsrittr aeragngfkl ngakafvldg hvadalivaa tteegttlfl
      181 vdpatagvdi ertvmvdahn aaritltdva vdadavigav gggealldga lnlgracaas
      241 sltgagdqaf kttmdylrtr kqfgkligef qalqhraahl fselelaraa tigaqiaide
      301 gredaslaas iakakagrva elavqeavqm hggvgmtdef dvglfmkrvr vlnellgdas
      361 fhaervaraq gf
//
LOCUS       WP_284878240             284 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Brevundimonas sp. MEB006b].
ACCESSION   WP_284878240
VERSION     WP_284878240.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..284
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30748
     Region          1..247
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mttlsaltlv rnrqahldrl vegltisasp pdelividms dapvtlpsvd fpvrverlag
       61 dalplaaarn laaalasgds llfldvdciv ssavcgrmka lladndavvc pevlylpaga
      121 vrpgplsetd lraagrphpv rpfpqkgesl ernpglfwsl afalrrstfh riggfdetyv
      181 gygaedtdlg friareglpl lfagrapvfh qhhdgydppl qhfraliana krfhaawsiw
      241 pmdgwlrama dlglidwssd elticrdptp aeiaaarkdt anpf
//
LOCUS       WP_284878244             267 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Brevundimonas sp.
            MEB006b].
ACCESSION   WP_284878244
VERSION     WP_284878244.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..267
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28253
     Region          4..263
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mdlgikgria lisgadsgmg ketarlllea gvrvaltdkp dgtldeavqe lsalgecigv
       61 tgdvtkaddv erlwaevrdr mgdpdiyvna agvtgatgdf ldvddagwle tldinlmgav
      121 rmcrqaipam rrsgwgrivl fasedavqpy vdelaycask agilslakgl skaygcdnvl
      181 vntvspafia tpmtdammkk raeergetfe eaiksflkee rpgmtldrrg kpeevaaava
      241 flcserasfi ngagirvdsg svatiav
//
LOCUS       WP_284878433             355 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Brevundimonas sp. MEB006b].
ACCESSION   WP_284878433
VERSION     WP_284878433.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..355
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=38403
     Region          <57..354
                     /region_name="COG3920"
                     /note="Two-component sensor histidine kinase, HisKA and
                     HATPase domains [Signal transduction mechanisms]"
                     /db_xref="CDD:443125"
ORIGIN      
        1 mlglhssvar rmpsstgaap mpalidafdw attplgpkrd wspalsityd mmmgmgfaas
       61 vmwgpertll yngayipllg qkhpsalgrp ldqvwhevwd dlrplteral agetvfledl
      121 pltmvrngys edtcwvlsys pvrdgdaivg ilniaiette rvrgeqhrqm lvdecghrvk
      181 ntlalvqava rstlsgvdrd vlerfderln aiaktqqtld ekawnggdlg eivrdavgnl
      241 vrrpvsisgp svhlsprvaq tvaliihelt tnafkhgala kpggrvsvdw rldegqlvlt
      301 wiegggapah pplktgfgvk llargllgcg gadlrygveg fsatftapvs rltds
//
LOCUS       WP_284878333             596 aa            linear   BCT 25-DEC-2024
DEFINITION  autotransporter assembly complex protein TamA [Brevundimonas sp.
            MEB006b].
ACCESSION   WP_284878333
VERSION     WP_284878333.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..596
                     /product="autotransporter assembly complex protein TamA"
                     /GO_component="GO:0097347 - TAM protein secretion complex
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=64279
     Region          24..596
                     /region_name="TamA"
                     /note="Outer membrane translocation and assembly module
                     TamA [Cell wall/membrane/envelope biogenesis]; COG0729"
                     /db_xref="CDD:440493"
ORIGIN      
        1 mtfrptllva laafsacaha aaaepraqir gdmdgdlrra leravgevdg apasrfearr
       61 raesavtsat allrsegyyq pvvedivege etpiavvlve pgrrflltdp tiqwadpape
      121 aeaadkakda ialkvgdpgr aadvisgegr avaalvrdgy adakanprrv vvdhaaftva
      181 peyriasgal vrldgvrlts qgrtnpawva glapwnegdr ydpemvaele rrlldtgvyd
      241 gvsvalspld qitadghrpv vvslqdrprr vleagatwst aegagvdviq trynrfgrad
      301 tlrlearlad idsrigadls lphwrrpgrt lklgaavvne dtdaylrtav vlyadlqqri
      361 gktsyfnygi gldagryset rydfttlppq rvtfdrdlai itartsayid rsndplnptk
      421 gwrvnlavqp tavtgesnil flrtetqgta yfpvagdrti lagrmkigsi vggselnvpa
      481 drlfysgggg svrgysyqnv npqlpdgtpr gglslfetsf evrqsigqsf qavgfvdags
      541 vgfqetpnlt nmrygagvgv rymlpfgpir advamplnkr egdsafqiyi sigqaf
//
LOCUS       WP_284878453             653 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Brevundimonas sp. MEB006b].
ACCESSION   WP_284878453
VERSION     WP_284878453.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 653)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 653)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..653
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=68698
     Region          1..463
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          586..640
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(608,617..619,626)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            618
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mfksvlvanr geiacrvfrt akrmgirtia vyseadanal hvreadeavl igpaaaresy
       61 ldgakvlaaa katgaeaihp gygflsenad faeavaaagl iwigpdpssi ramglkdaak
      121 elmiqagvpv tpgyqgadqs eetltaeaar igypvlikav aggggkgmkr vddpadfaag
      181 lasakregaa afgddrvlie ryitrprhie vqvfgdkhge vvhlyerdcs lqrrhqkvie
      241 eapapgmsea vraavtgaai kaaravnyvg agtiefiada sdglkadgvw fmemntrlqv
      301 ehpvtesvtg vdlvewqfrv aageriplkq dqiqlngwam earlyaedpa ngflpsigkl
      361 ehfvtpdgir vdtgveqgge vsqfydpmia klivhedtre aaaarlaeaa gevevwpvka
      421 nagflkrcle hprfvagdvd tgfiaaeeaa lqpqpsdeat laaltliaea aadavearsd
      481 rfspwggqpg lsygvrlnaa aqttvwahvd gqgvsaavtp vetgwrgsqg elahvgfdqv
      541 qagdrlfgyq tiddgfvlfv dgearrvtpy raavgsgpga vsdgslrapm pgkivatpvk
      601 agdavtkgqp vvvleamkme haltapfdgv vesvaslgdq vveaavlavv kan
//
LOCUS       WP_284878461             738 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Brevundimonas sp. MEB006b].
ACCESSION   WP_284878461
VERSION     WP_284878461.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..738
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79210
     Region          59..711
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msldaaltrl lagsgcrhai rqdgaviisr qssappapar piaprpaaav aspedvaqvs
       61 evvvtaprrp eliqssssam tavgadritr agvtgmqgld slvsgmtvtn lgpgrnkill
      121 rgisdgvftg ltqstvglyl dltpvtyaap dpdlklidid rvevlrgpqg tlygtgpigg
      181 vvrivtrapa mgeeslslsa trsrtdgggw nsdyglvanl piagdraair aalygetysg
      241 yindvelnlr rvndgtrrgg rlsaaleiap gwtaragvvh qsivtedthy vyrglgplrr
      301 anlvrephqn rfdqgsasie grgawgrlna svsvvehgfk srydassalr rfgsgwriga
      361 ldegkdihlv vgeanfaspd igrwrwlagg lvssnttrtn pvlsaltpep rtvysearrd
      421 rlneaavyge asldlphdlt ltagaryyal eydttslvrq fsrsrsfdgr gesagftpki
      481 alawqpserl nlsalvsqgh raggfntagv igqdfsglsd sparqykpds lwnaefgaky
      541 rsadgrarfr aafyaarwrn vqsdqflpsg layvvnvgdg adkgfevean wrpsetlelf
      601 anglvadpri tspsarfdsr rdaslpgvpr asanvgfswr rplgvrlvll adgglsyvga
      661 srltfdgrqq yrmgdygtgr lafgveasaw tatifvdnlf dteantfays dpfrlpdaqa
      721 itplrprtig ltlrwtah
//
LOCUS       WP_284878478             240 aa            linear   BCT 25-DEC-2024
DEFINITION  M48 family metallopeptidase [Brevundimonas sp. MEB006b].
ACCESSION   WP_284878478
VERSION     WP_284878478.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..240
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=26400
     Region          18..237
                     /region_name="YgjP"
                     /note="UTP pyrophosphatase, metal-dependent hydrolase
                     family [General function prediction only]; COG1451"
                     /db_xref="CDD:441060"
ORIGIN      
        1 mayrngqrlp ldesgagagp vlrlsvnpra rrlsvridar ageavviapt erglsqavaf
       61 arskavwise rlavrpksrp lepgqvislr grpvrleavs gasaarlved gtiirsggeg
      121 eayarrvenl lkreardtll ertdhhlral gqgpvkmgia dtrsrwgscs phnrtirysw
      181 rvimapppvi dylaahevah lvhadhspay wsvverlvgd ykpwrkwlkd ygaalhavgr
//
LOCUS       WP_284878770             307 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Aerococcus sp.
            UMB10185].
ACCESSION   WP_284878770
VERSION     WP_284878770.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB10185
  ORGANISM  Aerococcus sp. UMB10185
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Aerococcus sp. UMB10185"
                     /db_xref="taxon:3046357"
     Protein         1..307
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34110
     Region          2..289
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mhiicnpkse mgrgrrrlne vtsyleswgv dyqiyltqyp ghmrelltac lgqfkeedsl
       61 ilvggdgslh elvnlladrg ldlplafvsa gtgndfsryy qagketiedl lapmfkgqvr
      121 rlrigridps lgkaggvfvn slgfgfdgqv ihesegfkak ggiwqvpwan rvrylvslfq
      181 slrrvpnfal dvrlsghsqh fsdvslvavm lnpyfgggiq ldprvaeled dltlvvvhdl
      241 dwraipglly qilwrkgqgd skhlafyrgp rcelnltpai pgqvdgeaif saarsvgcrl
      301 dqqafyl
//
LOCUS       WP_284878814             334 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Citrobacter portucalensis].
ACCESSION   WP_284878814
VERSION     WP_284878814.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..334
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37429
     Region          9..323
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 minrekllql eqrmneqvlg qeelvrmlii allcdghvll eglpglaktr avrelarhve
       61 gdyrriqftp dllpsditgs eiyqqnasre edqfrfrpgp vfgniilade inrasarvqs
      121 alleameerh vtvagnswpl pgvfmvlatq npvdqegtwp lpeaqldrfl mkvlvhypsk
      181 eneqkvmqlv rreqqqkyqq ltnitpaape qpdalmlsqq eiaecwqais avhvsatven
      241 yivnlvdlsr hpqsvsdtla gyltfgispr gtlalercgr aqawlegrda vlpedikkia
      301 pavlrhrlml syqasadnct pddavrmlld avva
//
LOCUS       WP_284879147             334 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein [Acinetobacter variabilis].
ACCESSION   WP_284879147
VERSION     WP_284879147.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..334
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38339
     Region          8..329
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mkvlaaqqpi pvhiisgflg agkttllkyl lsqkleqevw avlmnefgqi gvdqqllpqd
       61 qgyavkellg gclccssqlp mqialsrlls etkpdrlfie ptglghpgql leqltephwq
      121 shlkmqalvt vvdgsrlhdr dwthqnlyad qlkvanivvi shadlmtetd haaltelkse
      181 yqpyaqhwlm iengqldieq ikqdyqgasr qiqpllkqqr qvlgevpavv hqlpyhyves
      241 aqgyqvagwk lpkrwqfdfy dlldllceqq dwlrikgifn tnqgwksfnf npdqfnyqsa
      301 eegidnrvev iyqtsrdwle fetalmqcri vqek
//
LOCUS       WP_284879433             336 aa            linear   BCT 25-DEC-2024
DEFINITION  lipase family alpha/beta hydrolase [Acinetobacter variabilis].
ACCESSION   WP_284879433
VERSION     WP_284879433.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18498059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..336
                     /product="lipase family alpha/beta hydrolase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36531
     Region          44..155
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
     Region          49..278
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mrtfikttqm lalslaaglg fgfstqtqaa asavqvteka ksdyaktkyp ilmvhgwlgw
       61 qrigtdtigl dywyqilpdm arngstvfaa qlspanttth rgeqlihqvd evlaitgkek
      121 inlighshgg ptvlyvaatr pqqiasitgv agtyhgskva ddiqnntltr tafnvlgdyi
      181 igplialgqf kpeleidfda smksltqtgs rsfnasvakq mvqdgvlast encnknlksk
      241 drngiyyysw tgvaqatnal didtilmqlg plsygnkdnd gmvarcsafi gkvindqykl
      301 nhtdlanmmf glkglfapdp vamyrqhanr lklqnl
//
LOCUS       WP_284879491             521 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Acinetobacter variabilis].
ACCESSION   WP_284879491
VERSION     WP_284879491.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..521
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=59600
     Region          175..515
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 maqtssysel nqyhlglwys ayrliistgl lliflltypd mttdyqypkl yhyalmisva
       61 vntvqlftlr wvkrliqpqf ilifasdvff lslltlasqg pnvhlglifv itifsaslll
      121 dakkaliitl iavisiiyqh figsifafss lsnignsall aflffvvygs gqiavrrfqi
      181 lenlnfsqsl elyrlqninr yileqietgy lvldenyhvv lsnpaachll giepmyaher
      241 fslyqsqndl felirfenle ngerfqfesq qsrynihvqv qklivphqtl tllvlqdark
      301 lnqqvqqlkl aalgqlsasi aheirnplaa ivqandlyld sepeqqqvlh qmisrqatri
      361 driiqdtlnm vknkethpvv iqlnefiprf iqedladvad qiqfnidapl aiqfdeaqlr
      421 qilinlirna irhnspdsph iqlnihpyeh kvwidvrdfg sgvathdqel lfkpffstsi
      481 hgtglglyls hsfceanqaq lnyisqeqga cfriscqrvt a
//
LOCUS       WP_284879573             234 aa            linear   BCT 25-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Acinetobacter
            variabilis].
ACCESSION   WP_284879573
VERSION     WP_284879573.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..234
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26216
     Region          1..228
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mkklvvfsga gmsaesgint frdsdglweq yrieevatpe awaknpelvq rfynarrkni
       61 leaqpnaahq liaeleddfd vhvitqnidd lheragsskv ihlhgnirla ktsdpncqnt
      121 tefypiegtd ldltkhfckd gyplrphvvw fgeavpayee aqdcvqdadi fvvigtslqv
      181 ypvaglihei tahctayyid pkadqqhlpa qfhkisqtat egmktllkll esei
//
LOCUS       WP_284879673             371 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Acinetobacter
            variabilis].
ACCESSION   WP_284879673
VERSION     WP_284879673.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..371
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41370
     Region          1..369
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mipfldlkai ntqyrdqlia actqvidsgw yicgkeleef ehnfanycgt ryaigvangl
       61 daliltlraw kelgklhegd evivpsntyi asilaisqnn lkpvlvepdi ttfnidtkki
      121 etaitpktkv ilpvhlygql aampeimtia kkynllvled saqshgaein gqkagnwgna
      181 agfsfypgkn lgalgdggai ttndaelaqm lkairnygsh ekyknlvpgv nsrldeiqaa
      241 ilnvklkfld qenqhrrhia dlylkeihnp aielpcknid tetyaqhvwh lfvirtkyre
      301 klqqylaeng vqtlihypip phqqqaykew nglsfpvseq ihaevlslpi gptlsmdeak
      361 qvvqlcngfq a
//
LOCUS       WP_284879633             624 aa            linear   BCT 25-DEC-2024
DEFINITION  polysaccharide biosynthesis protein [Acinetobacter variabilis].
ACCESSION   WP_284879633
VERSION     WP_284879633.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 624)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 624)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 624)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 624)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18500220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..624
                     /product="polysaccharide biosynthesis protein"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=69034
     Region          129..243
                     /region_name="FlaA1"
                     /note="NDP-sugar epimerase, includes UDP-GlcNAc-inverting
                     4,6-dehydratase FlaA1 and capsular polysaccharide
                     biosynthesis protein EpsC [Cell wall/membrane/envelope
                     biogenesis, Posttranslational modification, protein
                     turnover, chaperones]; COG1086"
                     /db_xref="CDD:440703"
     Region          286..576
                     /region_name="Polysacc_synt_2"
                     /note="Polysaccharide biosynthesis protein; pfam02719"
                     /db_xref="CDD:426938"
     Site            order(290,292..295,315..316,341..343,364..366,368,383,406,
                     422,446..449,452..453)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(316,318,322,326,339..342,345,348,366..369,372,376,
                     379,382,453..454,459)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187548"
     Site            order(368,408..410,418,447..448,454..456,459..460,
                     471..473,477,479,514,547,550)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(384,408,418,422)
                     /site_type="active"
                     /db_xref="CDD:187548"
ORIGIN      
        1 mksiilplve spraakqtfl vildfcifpv liwlcyairq fdlgaevvpn ipfgtiwvsa
       61 iailalfvcg vyrfivrtfn effivklgla tvlaviglyl layathafip tsiplmfgfm
      121 mfawvwfsrg lirfivrsyl yagiskkria iygagyagqq vaatlnrsne hlpvmfiddn
      181 pslngqnigg iqvyapetal rcftklride ilialpsvgr irkseivkfl epahlkitei
      241 pgltklvnge irvsdiqevd iidllgrdpv ppvaellekn ikdkvvmvtg aggsigselc
      301 rqiiknqpvk liiyeltefa lysidkelrl sasceiipil gsvvdeskle rvieqygiqt
      361 vyhaaaykhv plvecnplag lknnavgtaf svnaavkkgv etfvlistdk avrptnvmga
      421 tkrmaelycq amaeaqnqtq isivrfgnvl gssgsvvplf kqqiakggpi tvtdpevtrf
      481 fmtipeasql viqagalgtg gdvflldmge pvriqdlarq mislsglkvk dsqnpdgdie
      541 iqytglrpge klyeellidq enteitshkr ilrsvekhyp laeilevfnr mhvltatqsd
      601 vdwalmqleh yvdgyqrgqe ikvn
//
LOCUS       WP_284879761             279 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Acinetobacter variabilis].
ACCESSION   WP_284879761
VERSION     WP_284879761.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..279
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32042
     Region          35..164
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mqwfqalrqr lpqhkyaida sllgdhsqlp wsnlgywqag qqdyvaacrt ladhlaetvg
       61 lnskdklldl gcgqgasllh wqqryqvqyl agvelqpacv aniqqhlpdl navypasflr
      121 lkdiyfsqrf dvvlcldaay hspvpelleq vcsvlntnaw igfhhlilse kweslnalqk
      181 rkyqfllksa dvdlknlmse nelyhclenf efkniqiedl seavfsgfad yvnqylnskk
      241 lkqkgkrldq fkirmtaklc qklyqdgivr yvqvtarai
//
LOCUS       WP_284879745             469 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Acinetobacter variabilis].
ACCESSION   WP_284879745
VERSION     WP_284879745.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..469
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=54634
     Region          1..469
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mqliwfrqdl rihdhaalwh atqqgpcial avlspeqwql hqdariktdf ylrrlkylkq
       61 qlqqlnipli ilniplwkdl apeilnlcqt lkieslhani evgvnelkrd aqvqqlleqq
      121 qirvelyhdr tlfplgsirn qsnqayqvys afkkkcyerl ildipacype ieaqdpiqls
      181 tklpnvdlek fsadyvveha aqlwpaedrt aldllddfie dkmahyktdr dlpavdgtsr
      241 lspylnigvi svrqcmqalf qdgyfqiedv gqqtwldell wrefylqtlf dfprvskhqp
      301 fkqntnkiqw rntpedlaaw qqgqtgipiv dagmrqmlat gwmhnrvrmi tamflcknll
      361 idwrlgeswf mqhlidgdla annggwqwca stgmdavpyf rifnpvsqsl kfdpngdyir
      421 ewvpelahld aksihepyar npdlqldypk pivdlkasrv raieafkqi
//
LOCUS       WP_284877833             423 aa            linear   BCT 25-DEC-2024
DEFINITION  NupC/NupG family nucleoside CNT transporter [Brevundimonas sp.
            MEB006b].
ACCESSION   WP_284877833
VERSION     WP_284877833.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. MEB006b
  ORGANISM  Brevundimonas sp. MEB006b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Hirschi,M., Johnson,Z.L. and Lee,S.Y.
  TITLE     Visualizing multistep elevator-like transitions of a nucleoside
            transporter
  JOURNAL   Nature 545 (7652), 66-70 (2017)
   PUBMED   28424521
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Johnson,Z.L., Lee,J.H., Lee,K., Lee,M., Kwon,D.Y., Hong,J. and
            Lee,S.Y.
  TITLE     Structural basis of nucleoside and nucleoside drug selectivity by
            concentrative nucleoside transporters
  JOURNAL   Elife 3, e03604 (2014)
   PUBMED   25082345
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Munch-Petersen,A., Mygind,B., Nicolaisen,A. and Pihl,N.J.
  TITLE     Nucleoside transport in cells and membrane vesicles from
            Escherichia coli K12
  JOURNAL   J Biol Chem 254 (10), 3730-3737 (1979)
   PUBMED   374403
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Brevundimonas sp. MEB006b"
                     /db_xref="taxon:3040283"
     Protein         1..423
                     /product="NupC/NupG family nucleoside CNT transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005337 - nucleoside transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:1901642 - nucleoside transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=44327
     Region          14..419
                     /region_name="NupC"
                     /note="Nucleoside permease NupC [Nucleotide transport and
                     metabolism]; COG1972"
                     /db_xref="CDD:441575"
ORIGIN      
        1 mfsllnlqsl lglvvivavc waisenrkaf pwrltigail vqaglvlalf aipgsqavla
       61 avtgavdgla vattegtkfv fgylaggdqp ytvsnqgalf tfafqvlpli lvisalsall
      121 whwkilkwvt lgfgflfqkt mglggasala vaaniflgmi espivirayl dkltrseifl
      181 mmvvglatva gstmvayati lspvlpnaag hvlvasivsa pagvllarii ipekegmgga
      241 vadydsalky dsaidaivkg tsdglmvvln isavlivfva lvalvnvmlg gfvvldaplt
      301 vermlgwifa pvawligvew kdadvagwll gvkltltefv afidlgkvpa aemtertrml
      361 mtyalcgfan igsvgitvsg lsvlmperre evlgmvwkgl fagflatlmt aaivgampsv
      421 vfg
//
LOCUS       WP_284879850             258 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Acinetobacter variabilis].
ACCESSION   WP_284879850
VERSION     WP_284879850.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..258
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29785
     Region          2..232
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 milhlsdlhf gterpeclea iqqfcqdhpl eavvvsgdlt qrarlgqffa ckrfldqlnt
       61 pylvipgnhd iplyhlwnrl ftpftryqlf fgelepvlet ehfyligvns irrryhtkgh
      121 lsleqiqrid lklqqapask ikiivshqpf yvpfqnkrgf kdiplmakia leswsqhglf
      181 avlhghlhrt avydlnrife lggdhpvydv hagtsashrl hknqpnsfna idetgkitqy
      241 cfdeqlktfv pqpdpink
//
LOCUS       WP_284879838             499 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Acinetobacter variabilis].
ACCESSION   WP_284879838
VERSION     WP_284879838.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..499
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54646
     Region          6..>420
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mgsffflqll tvvfalsiat tmfnkrvlsf pqaigvpivs aifvfilqwc asllqgnpff
       61 sinidnieka vrhvdfydfl ingvicfilt ssalkfkvsd lrnhwrpigi laslalvfca
      121 vffgialygy qflignhvdi lvllllgaal gatdpigikg vlssvraphh livklegesl
      181 fndamcialf mtllnvlqge nfivlavlqt llyeivvavl igigfglail rilrgkheme
      241 slilttalla cgsylvalla hasapiacvi gglivgnkwk eiladadigd vnhfwhtveg
      301 iinsflftli glelfiidls tslvlggiva fiilhlarfl anhlsfalfp rmrkksyngs
      361 ltilswggvr ggislalila vanipqleay ssiligytfi vvllsgvvcg lglpavmnaf
      421 yynpneetqg fkgwyqrmch kmnrrgfqyi vgedangnet itifqpemli dkkdadgvat
      481 vhhpdkvqev krlenpenf
//
LOCUS       WP_284879976             138 aa            linear   BCT 25-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Acinetobacter variabilis].
ACCESSION   WP_284879976
VERSION     WP_284879976.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..138
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=14866
     Region          3..133
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mktkhyltls daefllnqay eyalengfnv siavadetgn llamkrmdga spmtanlcle
       61 karcsaisrr psklfediik ggqmgfltmd sfsgmlegge pilyqgqlvg amgvsgvksf
      121 qdaeiaqqai ekflakqs
//
LOCUS       WP_284879987             347 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Acinetobacter variabilis].
ACCESSION   WP_284879987
VERSION     WP_284879987.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..347
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=37598
     Region          7..346
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mslleklgik hpiflapmag vstpelaaev snqgglgslg lgassvesar qqilktqelt
       61 dcpfqvnffc hdsqpldenv aqawidqfkd kfaeyginpp tqlnciypsf kdnddflnlv
      121 letrpcaisf hfgiplphqv qalkdagilt mvsatnfaea kaiqeagidi iiaqgieagg
      181 hrgifstkfd asvktsnlvk lmkqhfslpv vaaggimnge qarqmmdfga eavqlgtafv
      241 qckssnanda yrkallskpl tqvsasisgr pargiinhwh ievdtpnrld vpaypytydl
      301 akqlhaaask ygdqgygafw agsnvtqire measdlinql vlemkqk
//
LOCUS       WP_284880006             205 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase [Acinetobacter variabilis].
ACCESSION   WP_284880006
VERSION     WP_284880006.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..205
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=23194
     Region          75..205
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mtepdpllky reqhkhrlny mpwlywslkp knrgwaeawq keyqtylmem etveigencf
       61 isplahifae pgrkisigdn tfiaadctlh gpleigseva inhhcildgg rvgiklhdqv
      121 riaaychlya fdhgmeleqs iyqqpvrskg ieigrdvwlg ahvgikdgvk iadkaiigmn
      181 smvtkdiear aivagnpakl iryrd
//
LOCUS       WP_284880007             668 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Acinetobacter variabilis].
ACCESSION   WP_284880007
VERSION     WP_284880007.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 668)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 668)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..668
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=75345
     Region          377..475
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mhekinkial lctvlmtall sgcqvvsvke qainvtinne rdsiltrdkl seaslnvlsm
       61 tgreaqvcen npeecvkelq eipqildeql lstsselyla kslqlgksae cktgalaktr
      121 seekqqlqtq nlqkcqeqql qmldksirys yaylfqtera pqdrifdnrq vqirdfynla
      181 iahliqiyae ryktkeagqr lqvgnsvyti nldnfpqlkn qsieqlmsty nmnfsglrsi
      241 trrdgfgsef lvvlpeekis kkdkkylvdp lnhqyqngvn pfihsaryla ttitaipesa
      301 nsveqilnns nfylklydpy kydkikvank eyalaanfsa pyglwlaenn lgraayltli
      361 nrddnlvmph lfmlepynpn kkvlvlihgl asspeawirl tndimgdpvl renfqvwqvf
      421 ystnmpiles rfqinallqq gfarisnnap akkeavlvgh smggviarll vsdaditepa
      481 fnivknsklt kfrdnplfka rlkmqpvpnf sraiflaaph kgtdyadrwh tklarkiirv
      541 psaflgafad tvqgeiglsd flhevgrdli qngpsdlskk skftaltkdi npapgfkfhs
      601 iignntdsdd enimtddvva yqsaylegaa snkiikgghs vqetpeavle lrrllrlhlv
      661 dlglydpd
//
LOCUS       WP_284880091             211 aa            linear   BCT 25-DEC-2024
DEFINITION  OmpW/AlkL family protein [Acinetobacter variabilis].
ACCESSION   WP_284880091
VERSION     WP_284880091.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006882
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..211
                     /product="OmpW/AlkL family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22730
     Region          5..211
                     /region_name="OmpW"
                     /note="Outer membrane protein OmpW [Cell
                     wall/membrane/envelope biogenesis]; COG3047"
                     /db_xref="CDD:442281"
ORIGIN      
        1 mlkqvalial mglsasamag qwqvkvgasv laptqetdli pgvvedakas selnftpsve
       61 yffndnisae lllatpfkhd vemagdvkia slkhlpptit akynfknssr ftpyigvgat
      121 vfipwdeefs qtakdalsva kldadvaygv agqvgfnfqp adaknwgvfv daryadlntd
      181 leaktadgtk inlgefgidp wvytigysyk f
//
LOCUS       WP_284880217             201 aa            linear   BCT 25-DEC-2024
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Acinetobacter variabilis].
ACCESSION   WP_284880217
VERSION     WP_284880217.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..201
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22599
     Region          9..180
                     /region_name="YdeN"
                     /note="Predicted esterase of the alpha/beta hydrolase fold
                     [General function prediction only]; COG3545"
                     /db_xref="CDD:442766"
ORIGIN      
        1 mknitkkvyi vpdyqatsnd hwypwlsrqi kdagfeakri mlanpfqpdl eewqhnlklq
       61 iphldehsfi vahglgglsa lkfleehynr tqlkigglml vaafdtplva wselnkmvqa
      121 vkldlnnlsh gakrfvmlls sndpyvpapi slrlghslna qifeiknagh fnkldgyadf
      181 skllellklc landlqnaag l
//
LOCUS       WP_284880280             496 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Acinetobacter variabilis].
ACCESSION   WP_284880280
VERSION     WP_284880280.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..496
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=55126
     Region          1..445
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mekqvdiliv gagisgigla ahlskhspqr sfeiierres fggtwdlfky pgirsdsdms
       61 tfgfnfkpwk kesvlasgsa iknylaevvq efnlsskihf qhrvvsanyd satrkwsvvv
      121 enaqgkkqtw ianfvlgctg yynydqgfqp efpnqevfkg tfihpqhwpe nlvysgkkvv
      181 iigsgatait lvpamvkgga ghvtmlqrsp tyiasvpsid miyskmrkll pedvaykltr
      241 arnigmqrgi yalaqkqpkl lktlllksvq fqlkgkvdmk hftpnyepwd qrlcvvpdgd
      301 lfkilregha svetdhiekf tetgillksg khldadiivs atglniqilg giqatmdgkp
      361 ldtskhmlyq gvmvsdvpnm aliigyinas wtlkvdiaae yicrllnymd qhgydevipe
      421 gdatelledt vmgsltsgyi araadvmpkq gkhapwkvsn nyladrkelk tasfedgilk
      481 fkskssvvps kprlvs
//
LOCUS       WP_284880466             255 aa            linear   BCT 25-DEC-2024
DEFINITION  dimethyl sulfoxide reductase anchor subunit family protein
            [Citrobacter portucalensis].
ACCESSION   WP_284880466
VERSION     WP_284880466.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..255
                     /product="dimethyl sulfoxide reductase anchor subunit
                     family protein"
                     /calculated_mol_wt=27165
     Region          5..242
                     /region_name="DmsC"
                     /note="DMSO reductase anchor subunit DmsC [Energy
                     production and conversion]; COG3302"
                     /db_xref="CDD:442531"
ORIGIN      
        1 mekyelplvi ftvlsqmsvg itliltlrvl qgkleskrly wlvsglvlaa asvaailhla
       61 hpdraydali nlqhawlsre ilgatlygaa vgvtflakgh kapavlasvl gialvavqgm
      121 tyaapamvai angltmllff itvwvmgcav ipllnlvpav aalrqgivvc mavmiaapii
      181 wlsggtimqm tahawltspl ylaslvclav afvlsrqgeh rakalfvllf vgiflsrltf
      241 fgdtissien ighly
//
LOCUS       WP_284880520             368 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Acinetobacter variabilis].
ACCESSION   WP_284880520
VERSION     WP_284880520.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..368
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=42305
     Region          16..356
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mnstpnklsp yfslqleslr gisaivvlfs hsfqafiapf dlslyswvrl lgqaavmiff
       61 vlsgyligts iqnniqqhen fnlrqyirqr yrrilppflf asafslilya laptffashs
      121 hefqnsfgmm irtaynidtq dflgslffln gfitptvsan aplwslsfev wfyvlagflp
      181 flkdsgiaki gffilllgls llnyqflfyf llwlvafans frqiqlrfls rlqpiklglf
      241 glafmiacad ayqfhvieqa dlyrvnyfvp fnlcmglafv cwivqlqhqq sqyqpvwpqs
      301 anfsytlyvt hfplllfilg cfpatldhgl egavlslfms mcsliffawf makwlepqrk
      361 kalsttlq
//
LOCUS       WP_284880546             376 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Acinetobacter
            variabilis].
ACCESSION   WP_284880546
VERSION     WP_284880546.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..376
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41451
     Region          1..372
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 msyalkglki ldfstllpgp fatlyladmg aevvhiespt rpdlvrlmpp fahgqatthn
       61 ylnrnkhsva ldlknpehik qiksriadad ydivveqfrp gvmqrlgldy ptlsalnprl
      121 iycsitgygq tglykdragh dinylalsgi aghsgriesg pppmgiqiad vaggsmhalv
      181 ailvavierq ssgqgqyidi smtdcaatln nmaasaslag nqhqqiesgy lnggifydyy
      241 qtqddrylsi gslepqfmqg laqlldlpii lekgasfape dhalvkqair dkirsqplsh
      301 wqalfsqadf cvepvlklde alhselaqqr ewvvqvpvkv dqreqteaql acpikfsrst
      361 mryqfigqal getkew
//
LOCUS       WP_284880604             333 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Acinetobacter
            variabilis].
ACCESSION   WP_284880604
VERSION     WP_284880604.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12820769
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..333
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38795
     Region          92..327
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          250..327
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msfecdysyi pahhqlsili dlaasheveh hvllsgssif ledifsgqkl isqqqlqqvl
       61 knaeqcfrnq disflfgqrs lttpfndaik smlyastfde alsryltfsa svspwlcprl
      121 mysqnhihiy wldenklenr fliesamsai qafsrqlyqt klawkfefnf sepdyieqyw
      181 thlgsalefn rpinmmslpr dliyeklpna sstlaaisyq halkemtaqn iqqsfllslh
      241 qyfmqniqnn iqleqtadyf qmssatlkrk lkkhqthfqa qldqsrlhta iilyrvhgfk
      301 teqisqylqi ndatnfrraf krwsgltvqa aqs
//
LOCUS       WP_284880883             193 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase
            [Citrobacter].
ACCESSION   WP_284880883
VERSION     WP_284880883.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..193
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21941
     Region          23..133
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mtleyyqrha qdffsstvnv dmeslyqpfl qriteggcil dagcgsgrds kaflekgyrv
       61 eafdassemv nlasqhaglh vrrmtfndia diehydgiwc casllhvsae elpsvmskla
      121 halkkggtwy vsfkygeter vkdgrhftdl teqrleklia pltditliss wttrdkrpdr
      181 demwlnallq krp
//
LOCUS       WP_284881289             606 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Citrobacter portucalensis].
ACCESSION   WP_284881289
VERSION     WP_284881289.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..606
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=68268
     Region          1..515
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mkliridiqn frgissasin lenfttligs nnigkstilk aikilvdttn ptsedwpyrt
       61 astdemvitg ifsdiqdter akpaisnlvh egklsirvrt kwdhdndcmg vptyeafysk
      121 ediedyttsi iaarnipwll eiineldcnn aksykdmqsd viglikqryp ekvsstlcwt
      181 sdginfknsl qqalphvlyi pacfkieddl ksqkgtpfgf lfsnrvypvl qsdpsftqyt
      241 sslyllhkkm kgevdgevie glhelmesit eslnqvmdlk skvklsltei dinaalmkaa
      301 tlviedklet qleyqgsgvq ralayalles nalfevtssq rstiilyeep elyihphlmr
      361 llrdklreks tnascqvivs thspflidia enpsslklik dtnegtrtvh eiddtifhvd
      421 esyderemlr aaldfhptvc eaffakrviv vegdtevail rfaselcekf gistelvkdt
      481 tivsaggkwt ipaiarilsk lnipfkivhd tdrkgmteeq inqisainay ranakieniv
      541 gadrvfrvdd tfehllwdpi idgnapsdgg kpfnawkrvr ayldgtitln avcenklrav
      601 iqfiye
//
LOCUS       WP_284881369             604 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase, partial [Actinotignum timonense].
ACCESSION   WP_284881369
VERSION     WP_284881369.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum timonense
  ORGANISM  Actinotignum timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Actinotignum timonense"
                     /db_xref="taxon:1870995"
     Protein         <1..604
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
     Region          10..598
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 evftpgkihi tdemtipwvf rniareqper tvvarkaslg qwvpvawrtf eseyralarg
       61 fiamgvqpgd rialmchtry efcvvdfalw sigamavtvy etdsteqarw ivedahcrfa
      121 vvenqqmaav mapfrsdfdf ftdifvisdd dlarisargt mdldaeidrr idamhaddea
      181 tviytsgstg rpkgvvlshr nllhvvingp lddnlapils gekhtllflp mahvfarfin
      241 lvafyagnti ghcpdthnlv edmksfkphy ilavprvfek iynaadaqst gvkqkifryy
      301 akvaiaysra ldsaagpsla lraqhevger lvyskikeit ggnlenvisg gaplgarlgh
      361 ffrgiginif egygatetsa pttvnrfnhq rigsvgpayp gchvaidtdg evlvkgdhvf
      421 hkylnnpeet akaftedgwy rtgdlgkied gfvwitgrkk elivtaggkn vspailedrl
      481 rghplisqvv vvgdqrpfvg alitldaeml piwlknknlp amsvseavhd pqiiasvdra
      541 ikrtneavsr aesirkfvil pidftpengy ltaslkvkrt avlrdfatvi grdiygdkgd
      601 knrd
//
LOCUS       WP_284881398             555 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Citrobacter portucalensis].
ACCESSION   WP_284881398
VERSION     WP_284881398.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..555
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=61959
     Region          171..386
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mmnvlnriap lpaqklllgi slffwcgamh lywpnnggsg lslplnitsw iyavvlaasv
       61 lmlvprqrwr itvpaagftv gafiltllcl ltpdvwqaea llvavallgg vsvylvtlqi
      121 plaarsltal lallwgasai eclafvyqyw hlpgveywef awrrgtrpyg ifqqvnllas
      181 ftacgvllsv llflrlrdgy rivigmglvm mgfvlhesqs qtgylslvig evlllavfpa
      241 qwrtllllll plalgvaiga tarhflsvvt vdhlttsqvr wtvlktslal faerpwmgwg
      301 vgsfaavfle cagplglgsi shphnelvlw lvegglvgla galcfiaggl wlwlhgncwr
      361 raclvaalpv vihmlteypv rqstphwlll illlrcadsa rtgirlalts tsliraagfi
      421 slltiaplll ltlhtqqqlt laerqstqwq laeplpvggw lltsryrfdv qmgylqryqr
      481 srdarwleev rrwapdyvrv hpdpnvsftq illalqqrdl veahrlatrf cliypndrri
      541 pwlqdarrpf nkime
//
LOCUS       WP_284881970             139 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor, partial
            [Aerococcus urinae].
ACCESSION   WP_284881970
VERSION     WP_284881970.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 139)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 139)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 139)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..>139
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
     Region          1..>134
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mkvlivddeq marqelaylv kehdqvsqvk tadsidqait mmldekpdil fldihleget
       61 gfdlakklka vhnppylifa taydqyalea feanandyil kpfeeskiha aidkyyqsle
      121 rasgqvdqdq eskrheaip
//
LOCUS       WP_284881406             193 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein, partial [Actinotignum timonense].
ACCESSION   WP_284881406
VERSION     WP_284881406.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum timonense
  ORGANISM  Actinotignum timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Actinotignum timonense"
                     /db_xref="taxon:1870995"
     Protein         <1..193
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
     Region          <1..170
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 iidqdaeafr klpedfpgqq itgvgfdrdv laraniddaa gfaavssgdn sniiaarvar
       61 etfgltnvva rvydptraii yerlgiatva pvrwtadrvl reliplgphh efrdplaris
      121 lievavdrrw fgrtvadvee etgarvayii rslagllphs dtviqdgdtl kvlvasenas
      181 gvqhvllkse gaq
//
LOCUS       WP_284882603             387 aa            linear   BCT 25-DEC-2024
DEFINITION  integrase [Escherichia coli].
ACCESSION   WP_284882603
VERSION     WP_284882603.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..387
                     /product="integrase"
                     /calculated_mol_wt=44917
     Region          4..351
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
     Region          182..351
                     /region_name="INT_Rci_Hp1_C"
                     /note="Shufflon-specific DNA recombinase Rci and
                     Bacteriophage Hp1_like integrase, C-terminal catalytic
                     domain; cd00796"
                     /db_xref="CDD:271177"
     Site            order(191..192,195,207,210..211,248,250,252,319..320,
                     323..324,326..327,337,347,350)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271177"
     Site            order(215,314,317..318,349)
                     /site_type="active"
                     /db_xref="CDD:271177"
ORIGIN      
        1 mslfrrneiw yasyslpggk rikeslgtkd krqaqelhdk rkaelwrvek lgdlpdvtfe
       61 eaclrwleek adkksldsdk sriefwlehf egirlkdise akiysavsrm hnrktkeiwk
      121 qkvqaairkg kelpvyepkp vstqtkakhl amikailrta erdwkwleka pvikipavrn
      181 krvrwlekee akrlidecpe plksvvkfal atglrksnii nlewqqidmq rrvawvnpee
      241 sksnraigva lndtackvlr dqigkhhkwv fvhtkaakra dgtstpavrk mridsktswl
      301 sacrragied frfhdlrhtw aswliqsgvp lsvlqemggw esiemvrrya hlapnhlteh
      361 arkiddifgd nvpnmshsgi medikka
//
LOCUS       WP_284882075             114 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase, partial [Aerococcus
            urinae].
ACCESSION   WP_284882075
VERSION     WP_284882075.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..>114
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
     Region          6..>109
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mktnqyalfs evyhqifdqs lyqawqnyle dqvetrlthq eglkildmac gdgrltlela
       61 kagydvtgmd lseemlaiaq aemqeagiyi pyfqadmrsf ktetsydlis ifcd
//
LOCUS       WP_284882059             165 aa            linear   BCT 25-DEC-2024
DEFINITION  LysM peptidoglycan-binding domain-containing protein, partial
            [Aerococcus urinae].
ACCESSION   WP_284882059
VERSION     WP_284882059.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10061503
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..>165
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
     Region          7..>45
                     /region_name="Agg_substance"
                     /note="LPXTG-anchored aggregation substance; NF033875"
                     /db_xref="CDD:411439"
     Region          113..154
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
ORIGIN      
        1 mkgnffqekk skktmhkskg kwvvasllla gslgavslgn eevranvntl asqgiknfss
       61 sdfagkdqls engqikqasq dalkrikgtw tknsvdqvka eiarqqaagy qayvvqwgdt
      121 lsvlaeatgq dlnslaqanh lgnihliftg dlltgvlspl sqnng
//
LOCUS       WP_284882957             402 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter freundii].
ACCESSION   WP_284882957
VERSION     WP_284882957.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..402
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=45663
     Region          5..396
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mplndtklrr iagkpydgpe eiadggglsa rispkglitf qyryrfngkp arlklgtygk
       61 msikeardam eeckgwleeg rdpamqrkka rdivssspsi stlvdewlet psvkemvkye
      121 ywkrmlklhv tdnygrliad emspveweqi flritkggsp vqagnvlvkm kqviryalrr
      181 kritsnslml leindvgsrp ddgerflndd eigvfwnaid ktkmswqnkm lirlvaltgc
      241 rgvelrlark gdfdlkarew vipkensktr krfvrgisql aadylqkvfd vypdqtivfp
      301 paklqvdrpm sastlisiar qveevmggeh wslhdlrrtc ktkmaelgva phvsekilgh
      361 kltgmlavyd qydyipeqqa aaelwaekiq acaansplsl qn
//
LOCUS       WP_284883337             350 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease [Actinotignum].
ACCESSION   WP_284883337
VERSION     WP_284883337.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum
  ORGANISM  Actinotignum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 350)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Actinotignum"
                     /db_xref="taxon:1653174"
     Protein         1..350
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36325
     Region          38..342
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msaksadsat stiarrrtaa favlvittia llgamvvamg mgqlsisapd vvrilfsspd
       61 dvdrsalvai nqiraprvil avvlggclav sgavlqslfr nplvspdivg vssaaafggv
      121 lailvgtssf ilmgstfifg lsavvcvmli grirshsatl tivlagvvvs affnamvslm
      181 tyvadpyskl psitfwlmgs laaaswakvt tiiipviigl ivvvalrwri nvlslgdeda
      241 ralginpstm rwvcifaval ltaasvaaag iigwvglvip hlvrllvghd nrvvipesfl
      301 mggmylliid tiarnatsve ipvgiltati gapvfiglli rrarkgrala
//
LOCUS       WP_284883063             187 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Citrobacter freundii].
ACCESSION   WP_284883063
VERSION     WP_284883063.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..187
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21090
     Region          2..>108
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mpdmslfdvl drlpsltrmw frqhpllvdl qpvqlsalmy larcnrysnt plgvtdylgl
       61 tkgtvsqslk llenkglivr kpddrdkrsv hlhlsesant lleallpptf lvegesamge
      121 rasvlrelll ellrgiqrtn nvpgfglchs crfhqkidgq gfcnltkerl seedsllicr
      181 ehqppet
//
LOCUS       WP_284883461             293 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Actinotignum].
ACCESSION   WP_284883461
VERSION     WP_284883461.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum
  ORGANISM  Actinotignum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Actinotignum"
                     /db_xref="taxon:1653174"
     Protein         1..293
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32230
     Region          118..286
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <227..288
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mrtnlqfsqr ltdaiqalhs atdrrtiary vvalladvap nadyiyfyaf lprqnvfavl
       61 gvygfphyns tlvveanspf grtlgrreqy wartpaevae lysfpadssl ayermgplfr
      121 fasaathasa viqpciigqe lqgtlwlesh sragafsatd rtrisqlstl valllravpq
      181 atilnsdgla evwdvlprtt qitaetpans asenrpprtd srhapaltlr ekdvltqiaq
      241 gltnseaaaa lhisintvrs hrrslmrkfa vhnavellda aakyglepkv lrd
//
LOCUS       WP_284883465             153 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)-dependent oxidoreductase [Actinotignum].
ACCESSION   WP_284883465
VERSION     WP_284883465.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum
  ORGANISM  Actinotignum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Actinotignum"
                     /db_xref="taxon:1653174"
     Protein         1..153
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=16132
     Region          2..152
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mriaiigang sagklltqea vargheiiav trsenetvap vslrrdvfdi ergdiagfda
       61 mvdaltpsad agedfperaa shlidlvsgl ptrlivldsg dgkvptaven ariakwtyis
      121 pevtsaelav avieeiergp ltahirqrvv vgk
//
LOCUS       WP_284883532             577 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: glycoside hydrolase family 13 protein [Citrobacter].
ACCESSION   WP_284883532
VERSION     WP_284883532.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 577)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..577
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=66385
     Region          16..489
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(30,32,34,38)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(69,72,109,112,159,178,182,214,271,431)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(214,271,347)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          496..572
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; pfam16657"
                     /db_xref="CDD:435493"
ORIGIN      
        1 mtlapnmhsk plawwkkata yqiyprsfyd tnqdgigdin giiakldyla dlgidliwic
       61 pfyaspnddn gydisdyqai hpdfgtledv delisaahkr giriimdlvi nhtsdehpwf
      121 iesrdnknsp krdwyiwrdg ceptaekptc dpnnwesifh gsaweydkkt aqyylhlfsk
      181 kqsdlnwenp evkqtlfkmi ywwlergidg frvdaishiq kqpglpslpn pkgekyvssf
      241 dyhmnvagie khlhelkeqa fdpfnivtvg eangvtadna llwvaeateh dqggvfnmif
      301 qfehmklwse eqsnvpldlv efkrilsrwq dalegkgwna lylenhdqar sidtfadpts
      361 ryasatalas cyflmkgtpf iyqgqeigmv nhqftsldef ndvsarnliq klsqqgqsda
      421 dilallnqvs rdhsrlpmqw naqdfagfse vqpwfsvnqq yadinveqqq ndpnsilsfy
      481 kqlialrksn vslvvgryql llpndpniya yqrvaqdmtw tiitnlspqe sivdidrmql
      541 gelmldnqni nnehvrsdfi atqiappyaa yifarkh
//
LOCUS       WP_284883631             271 aa            linear   BCT 25-DEC-2024
DEFINITION  tRNA dihydrouridine synthase, partial [Actinotignum timonense].
ACCESSION   WP_284883631
VERSION     WP_284883631.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum timonense
  ORGANISM  Actinotignum timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Finet,O., Yague-Sanz,C., Kruger,L.K., Tran,P., Migeot,V.,
            Louski,M., Nevers,A., Rougemaille,M., Sun,J., Ernst,F.G.M.,
            Wacheul,L., Wery,M., Morillon,A., Dedon,P., Lafontaine,D.L.J. and
            Hermand,D.
  TITLE     Transcription-wide mapping of dihydrouridine reveals that mRNA
            dihydrouridylation is required for meiotic chromosome segregation
  JOURNAL   Mol Cell 82 (2), 404-419 (2022)
   PUBMED   34798057
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Bou-Nader,C., Bregeon,D., Pecqueur,L., Fontecave,M. and Hamdane,D.
  TITLE     Electrostatic Potential in the tRNA Binding Evolution of
            Dihydrouridine Synthases
  JOURNAL   Biochemistry 57 (37), 5407-5414 (2018)
   PUBMED   30149704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414563
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Actinotignum timonense"
                     /db_xref="taxon:1870995"
     Protein         1..>271
                     /product="tRNA dihydrouridine synthase"
                     /EC_number="1.3.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0017150 - tRNA dihydrouridine synthase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
     Region          13..>271
                     /region_name="DusA"
                     /note="tRNA-dihydrouridine synthase [Translation,
                     ribosomal structure and biogenesis]; COG0042"
                     /db_xref="CDD:439812"
ORIGIN      
        1 maenaawpai qlgdltlatp vmlapmagvt nppfrqlcre eaeagirram assapdapsp
       61 ephapgsyap aglwvcemit srallertpe tmtmiqpdps dpvrsiqlyg vepkvvaaav
      121 rllieenrad hidinfgcpa pkvtrkgggs alpwkldlye dlvreataaa saanrgrdha
      181 vpitvkfrig idaahetfrd varisedygv agltlhartt aqhyaghanw dfiaelvdst
      241 dlpvfgngdv fdaadaaalr ahtgcagvav g
//
LOCUS       WP_284884088             488 aa            linear   BCT 25-DEC-2024
DEFINITION  mannitol dehydrogenase family protein [Citrobacter portucalensis].
ACCESSION   WP_284884088
VERSION     WP_284884088.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..488
                     /product="mannitol dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=54103
     Region          9..482
                     /region_name="MtlD"
                     /note="Mannitol-1-phosphate/altronate dehydrogenases
                     [Carbohydrate transport and metabolism]; COG0246"
                     /db_xref="CDD:440016"
ORIGIN      
        1 mktiasapla envmmpqynr qqlktrivhf gfgafhrahq alltdrvlna qggdwgicei
       61 slfsgdrlms qlreqdhlft vlekgangnq pivigavnec lnarldslaa iiekfcepqv
      121 aivsltitek gycidpatgs ldlsnpriah dlqtptephs apgiivealh rrrerglqpf
      181 tvlscdnipd nghvvknavl gmaekrspel atwiqehvsf pgtmvdrivp aateeslaei
      241 arelgvadpc aiscepfiqw viednfvcgr pqwetagvqm venvlpweqm klrmlngshs
      301 flaylgylag fqhisdcmqd safreaayrl mlneqaptlq itdvdldqya lsllerfanp
      361 alkhktwqia mdgsqklpqr mlegirvhla rqsewpllal gvagwmryvs gvddsgtaid
      421 vrdplsekia alvkqstese rvnallslre ifatdlvqnp qfvaaiqqaw qriaqygahq
      481 avietlks
//
LOCUS       WP_284883837              66 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein, partial [Actinotignum
            timonense].
ACCESSION   WP_284883837
VERSION     WP_284883837.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum timonense
  ORGANISM  Actinotignum timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Actinotignum timonense"
                     /db_xref="taxon:1870995"
     Protein         1..>66
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
     Region          1..>66
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mrirvitvaf npgpeleafl aslpaalqea heciivdngs ehaevdrvar ahgaqvvrtg
       61 enigyg
//
LOCUS       WP_284884176              69 aa            linear   BCT 25-DEC-2024
DEFINITION  transcriptional regulator [Citrobacter portucalensis].
ACCESSION   WP_284884176
VERSION     WP_284884176.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008341
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..69
                     /product="transcriptional regulator"
                     /calculated_mol_wt=7183
     Region          4..60
                     /region_name="YdaS"
                     /note="DNA-binding transcriptional regulator YdaS,
                     prophage-encoded, Cro superfamily [Transcription];
                     COG4197"
                     /db_xref="CDD:443351"
ORIGIN      
        1 mtgienailr sgsasalgal igvskmavsl wrrkgipaer vlpvfeatgv tphelrpdly
       61 pnstdglpk
//
LOCUS       WP_284884304             230 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Citrobacter
            portucalensis].
ACCESSION   WP_284884304
VERSION     WP_284884304.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 230)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..230
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26486
     Region          3..>223
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msrradrlfq ivqilrgrrv ttaallaerl evsertiyrd irdlslsgvp iegevgsgyr
       61 lmagfdlppl mlthheseal mvairllktw ggyslsqale saqekvlail ppesrrraeq
      121 trifapdfgn qphsrsafdl ihravsaqqv lalhyrdesg nlswrdvqpl glffwgehwl
      181 lvgwcekrdd yrcfrvdrcl kitpldrhfr esadrslsdf lrkvrcedqp
//
LOCUS       WP_284884327             506 aa            linear   BCT 25-DEC-2024
DEFINITION  FGGY family carbohydrate kinase [Citrobacter portucalensis].
ACCESSION   WP_284884327
VERSION     WP_284884327.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Yeh,J.I., Kettering,R., Saxl,R., Bourand,A., Darbon,E., Joly,N.,
            Briozzo,P. and Deutscher,J.
  TITLE     Structural characterizations of glycerol kinase: unraveling
            phosphorylation-induced long-range activation
  JOURNAL   Biochemistry 48 (2), 346-356 (2009)
   PUBMED   19102629
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426119
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..506
                     /product="FGGY family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=54552
     Region          6..500
                     /region_name="GlpK"
                     /note="Glycerol kinase [Energy production and conversion];
                     COG0554"
                     /db_xref="CDD:440320"
ORIGIN      
        1 mcaakkefii aldegttnak avaldaqgnv vakfsqplai qtprdgwveq sgevlidvsi
       61 gviakavnhv gaenvaalai snqretaigw yrqtgrplns aitwqctrsa ayceelrhen
      121 keqliksttg lpiaplfsas kmrwllesvt dgpqlaaqgq iclgtidswl lwnltageaf
      181 ccdysnaart qllnlhsgew deamlalfhi praalpeikp ssglfghtrg lngipdgipv
      241 msmvgdshaa lfghalgemg cvkatygtgs svmapvksaq cdidalatti awhdgnsiiy
      301 glegniphtg davawmadst glselsdael tyelntlpas vdstlgvyfv paltglgapw
      361 wddsargvic glsrgvkrah liraalesit yqiadvvvam qqhddfklta lmvdggptkn
      421 dwlmqyqadl lgypvmrsdv pelsaigaal larkalypgs ltdlkafltv hstfqpdmdr
      481 hhrlqkrwqe wrhavnrtlw kpapsa
//
LOCUS       WP_284883806             259 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein, partial [Actinotignum timonense].
ACCESSION   WP_284883806
VERSION     WP_284883806.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum timonense
  ORGANISM  Actinotignum timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Miller,J.M. and Enemark,E.J.
  TITLE     Fundamental Characteristics of AAA+ Protein Family Structure and
            Function
  JOURNAL   Archaea 2016, 9294307 (2016)
   PUBMED   27703410
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Actinotignum timonense"
                     /db_xref="taxon:1870995"
     Protein         1..>259
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
     Region          1..>259
                     /region_name="COG1373"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440984"
ORIGIN      
        1 mayirravdt vlqqdleimg gvviegargc gktetgifha hsefrvdqas nqrlaelnpq
       61 gvlegdvprl vdewqlapil wneirheidv rrapgqfils gsatpadsit rhtgagrlsr
      121 vrmrpmalge aypredritl nelrtatqvr yvpgalsype lateavrggw pflvssqnpa
      181 firfvqnyvd niahvdlaqv darfdpervr rllrslarni asetaattls qdisadggel
      241 spqsvrsyld altrifive
//
LOCUS       WP_284884514             377 aa            linear   BCT 25-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Citrobacter portucalensis].
ACCESSION   WP_284884514
VERSION     WP_284884514.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..377
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41131
     Region          1..375
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkevriglig tgyigkahai ayaqaptvfn lrgklvremv aevspelaae raqafgfnrs
       61 tgdwralvad paidvvdics pnhlhkemal eairhgkhvy sekplalnah daremveaaq
      121 ragvktlvgf nymknptaql akeiiergei gevihfygth nedymadpla pihwhcfket
      181 aglgalgdla ahivnmaqyl vgdiqqvcgd lkivvpqrpa qvgssqmvtv enedqahamv
      241 rfaggaqgvi etsrvacgrk mglsyvitgt kgtisftqer maelklylhd dpvnrqgfrt
      301 llvgpahpdy gafcmgaghg igfndqktve vrdlvdgiaa dapmwpdfee gwkvsrvlda
      361 ialshqegrw lnvndif
//
LOCUS       WP_284883365             433 aa            linear   BCT 25-DEC-2024
DEFINITION  chromosomal replication initiator protein DnaA, partial
            [Actinotignum timonense].
ACCESSION   WP_284883365
VERSION     WP_284883365.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum timonense
  ORGANISM  Actinotignum timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Kaguni,J.M.
  TITLE     DnaA: controlling the initiation of bacterial DNA replication and
            more
  JOURNAL   Annu Rev Microbiol 60, 351-375 (2006)
   PUBMED   16753031
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Skarstad,K. and Boye,E.
  TITLE     The initiator protein DnaA: evolution, properties and function
  JOURNAL   Biochim Biophys Acta 1217 (2), 111-130 (1994)
   PUBMED   8110826
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13571298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Actinotignum timonense"
                     /db_xref="taxon:1870995"
     Protein         1..>433
                     /product="chromosomal replication initiator protein DnaA"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003688 - DNA replication origin binding
                     [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006270 - DNA replication initiation
                     [Evidence IEA]"
                     /GO_process="GO:0006275 - regulation of DNA replication
                     [Evidence IEA]"
     Region          9..72
                     /region_name="DnaA_N"
                     /note="DnaA N-terminal domain; pfam11638"
                     /db_xref="CDD:463316"
     Region          <92..256
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          216..>433
                     /region_name="dnaA"
                     /note="chromosomal replication initiator protein DnaA;
                     PRK00149"
                     /db_xref="CDD:234667"
ORIGIN      
        1 maemnparda wlaalellrm qgdlsdsqsa fvrmahplat aedifmivvg sefvknwiee
       61 hvadlmtgal snilghsirl visidpsvne splpaterre trpveaapap rraetptals
      121 pdsewnksat yrdftleepg afpdapgepv apaapsalnt shasaphtpa phvpaphata
      181 pvetteptsl atqmmasgee kiygnsadps faamstaagl npkytfdnfv igdsnrfpta
      241 tslavseapg ttynplflys dsgmgkthlm haignyaisl ypnihvryis aeeftnafin
      301 avrdgrqsef kdsfrkvdil liddiqfigg rdttveeffh tfnaltnsnk qivitsdvap
      361 nllngfeerm lsrfnsgvva sidrpnletr iailekkahv dgisvprevh eyiathmttn
      421 vremegalrr vta
//
LOCUS       WP_284884567             249 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Citrobacter
            portucalensis].
ACCESSION   WP_284884567
VERSION     WP_284884567.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..249
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27615
     Region          4..248
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mkrkimvvta ayghdqvraa ggqtamlpii aeagadgvei rrelltdael ktlstmasai
       61 eifgllacys apeplfledg nlnprlpell eeaqalqalw lkvslghffh teqfdvlrqw
      121 ldnsgmelvv endqtdcgrl qpmqrfneac qaqnlpislt fdmgnwlwvg dspeeaaqnl
      181 astvgyihvk aavayhdsyr avppdtadpr wlallktlpn dvprgiefpl egqdlvavtr
      241 ryvellree
//
LOCUS       WP_284884540             133 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Aerococcus sp.
            UMB8608].
ACCESSION   WP_284884540
VERSION     WP_284884540.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB8608
  ORGANISM  Aerococcus sp. UMB8608
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Aerococcus sp. UMB8608"
                     /db_xref="taxon:3046347"
     Protein         1..133
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15397
     Region          1..68
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mafadrlkdf rekeklsqad fakmigistr tlvhyedger yprdvevykk iaevmdcdyn
       61 ylleesdefl nrvynmggkr elekaralte glsslfagge isdedkdaaf eaitraywea
      121 kkenkkygrk kkd
//
LOCUS       WP_284884589             258 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Citrobacter
            portucalensis].
ACCESSION   WP_284884589
VERSION     WP_284884589.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..258
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27254
     Region          7..254
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mntlfvgkkl lvvggtsgig fetaklilqg ggrvvlvgnr aekaerarqa laelgdvsvi
       61 vadlmseagv kqvmamvnae hkdinllvna agvffpkpft dhevedyely mslnratffi
      121 trdvvrnmva aniqgaivni gsmwaqqaig atpssaysma kaglhaltkn laielgangi
      181 rvnavspavv htpiyegfip kedvqgvmss fdsfhpigrv gtprdvaesv afllsdkaqw
      241 vtgaiwdvdg gvmagrng
//
LOCUS       WP_284884603             367 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Citrobacter portucalensis].
ACCESSION   WP_284884603
VERSION     WP_284884603.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..367
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39205
     Region          2..359
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 miesdvivig agiigaacaw qlaargqrvt lvdddnagat aagmghlvcm dddpaelals
       61 awslacwrkl tprmpescaw rgcgtlwlae tpqelalaee kkqrmaqyqv vsemqtrdrl
      121 aareplltag lagglwvpgd givyapnvar wfindadlth lrdsalsvda pyvtlhsgkr
      181 lraraivias glgantllge nwlrpkkgql aitdrygpll shqlvelgyg asahaggtsv
      241 afniqprptg qlligssrqf dntdrevdlp llaqmlarar hflpsletln iircwsgfra
      301 asadgnplig phparpgiwl algheglgvt tapataellc aqilgerpav spdawlparl
      361 hkqeaia
//
LOCUS       WP_284884679             332 aa            linear   BCT 25-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Citrobacter portucalensis].
ACCESSION   WP_284884679
VERSION     WP_284884679.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..332
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36434
     Region          1..252
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mirfavigtn witrqfvdaa hetgkyklta vysrsleqaq tfandysveh lftsleamaq
       61 seaidavyia spnslhfpqt elflrhkkhv icekplasnl aqaeaaiaca renqvvlfea
      121 fktaylpnfl qlqqslprvg kirkafinyc qyssryqryl dgenpntfnp afsngsimdi
      181 gfyclasava lwgepqsvqa sasllesgvd ahgvvvlnyg dfsvtlqhsk vsdsvlasei
      241 qgesgslvie hisecqkvcf vprggktqdl ttpqhintml yeaeafahlv esgevdhpal
      301 avscitaklq teirrqtgvv fpadeaetsl ta
//
LOCUS       WP_284885090             187 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Citrobacter portucalensis].
ACCESSION   WP_284885090
VERSION     WP_284885090.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..187
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21121
     Region          2..>108
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mpdmslfdvl drlssltrmw frqhplladl qpvqlsalmy larcnrysnt plgvtdylgl
       61 tkgtvsqslk llenkglivr kpddrdkrsv hlhlsesant lleallpptf lvegelsmge
      121 raivlrelll ellrgiqrtn nvpgfglchs crfhqkidgq gfcnltkerl seedsllicr
      181 ehqppet
//
LOCUS       WP_284884791             217 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [unclassified Aerococcus].
ACCESSION   WP_284884791
VERSION     WP_284884791.1
KEYWORDS    RefSeq.
SOURCE      unclassified Aerococcus
  ORGANISM  unclassified Aerococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="unclassified Aerococcus"
                     /db_xref="taxon:2618060"
     Protein         1..217
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24365
     Region          8..211
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mlnqkthlff dmdgllidte rlyyetrret lsqfgyaytq adhmafagrg wrytlarlqd
       61 wagpdqgqvm fdqalerfrt avlagklqlk pgvrqvldfa qavglssyvt sastrynvlt
      121 mteqtgirsy ftaylcgedi erskpypdly lealrrsgve adrvlvleds psgltsavga
      181 gldtvlvpdl vrpsqdmqdq avlsldrldd lipylkn
//
LOCUS       WP_284885463             370 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Acinetobacter nosocomialis].
ACCESSION   WP_284885463
VERSION     WP_284885463.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter nosocomialis
  ORGANISM  Acinetobacter nosocomialis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Acinetobacter nosocomialis"
                     /db_xref="taxon:106654"
     Protein         1..370
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=42146
     Region          1..370
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mrnykidilr gmsillvllh hfnipyklkd twlgfdflge afstviarng nygvtmffvi
       61 sgflithhtl krdkqfsain lkhfyirraa rilpclvlli lgvsilgsfd lkpfmnqapn
      121 gievsyplti faaltfwmni liikfgwvny algvlwslsv eevfyfvfpl lclltrsnkv
      181 fiavligvii ygpyfrslhs geesgaylyh yfssfdgiav gcltaifshk yqpnwhckkl
      241 lswliilgmt alylyapike vstwgislfa fatgllilcf qhpsetqahn lltkvmvwlg
      301 qrsyetylfh lvvlglmkva fvpaqtdasi kimlligylv ltfvisaaie kyystplnsy
      361 irkifikdks
//
LOCUS       WP_284885487             260 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Acinetobacter
            nosocomialis].
ACCESSION   WP_284885487
VERSION     WP_284885487.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter nosocomialis
  ORGANISM  Acinetobacter nosocomialis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Acinetobacter nosocomialis"
                     /db_xref="taxon:106654"
     Protein         1..260
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28466
     Region          1..227
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 msaqskvlit gassgigsvy adrfaqrghh lilvardtnr ldkisrdlqa kygvqvefiq
       61 adlskdqdis kiedvlknda dieilvnnag itlsgnfltq dikeietlmt lnmtavvrls
      121 havseqlvrk gkgsiinlgs vvglspefgs tiygasksfi hffsqglhle lkdhgvhvqa
      181 vlpsatktei wersgidlsq vpplmdvndl vdaaligfdr ketitipvlk denqwnnfek
      241 scmtllpnfs saevaqrytn
//
LOCUS       WP_284885649             395 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter koseri].
ACCESSION   WP_284885649
VERSION     WP_284885649.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter koseri
  ORGANISM  Citrobacter koseri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Citrobacter koseri"
                     /db_xref="taxon:545"
     Protein         1..395
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=44941
     Region          2..393
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mkltarqist akptekpykl sdggglyllv npngsrywrm kyryagkekl lsigvypdvt
       61 laeardkrte skrmlaagdd psevkqaare akslavnnsf ellalewheh kkpnwssgya
      121 ddileylrkd ifpyigkkav tdikpmtmls vlkkmeergv ldklkktrqa crqiftyaii
      181 tgraefnpva dlagalktpk qqhfphlmpa qigpfiqavn aytgskvtra atlllmytsv
      241 rtielrasew aefdldndlw qipkermkmr rphlvplsqq vkshllelke itgwgkyvfp
      301 grndarkpms easinqvikr igfagrvtgh gfrhtmstvl hekgfnsawi eaqlahadrn
      361 tirgtynhaq yldgrremlq wyadyldela kksvg
//
LOCUS       WP_284885812             238 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Citrobacter koseri].
ACCESSION   WP_284885812
VERSION     WP_284885812.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter koseri
  ORGANISM  Citrobacter koseri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Citrobacter koseri"
                     /db_xref="taxon:545"
     Protein         1..238
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=25705
     Region          5..232
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 metkksltte qledakrlka lyeskkkelg vtqytiadel gitqgavghy lngrnalnvd
       61 vasgfarllq vsisdfsksl aakaaeqaes lngesnvkyi gsyrpgkryp vlssvqagaw
      121 seacepytlk didlwlesda hvqgdafwlk vegdsmtapv glsitegtfv lfdtgrepin
      181 gslviaklsd sneatfkkli idggrhylkg lnpawplvpv ngscriigva ietklkli
//
LOCUS       WP_284885923             258 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Aerococcus urinae].
ACCESSION   WP_284885923
VERSION     WP_284885923.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..258
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29382
     Region          2..256
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mtllqttlys dslrmdvhvn iifpqncart pegkrqslkp pyrvlyllhg lssnedgwlr
       61 ftsleryard ldlvivlptt hrgwyinnai gypysnfisv elpeiiqtml pvstkredty
      121 iagasmggfg alkaaftype kygyvaslsg vtdlvnafaq gpdpespfeh qmlfdeespa
      181 htdndiyylv qqaidnkidl pqvymtcgte dslieqnrlf kerfgdalel syhenpgehg
      241 wdywdpeikk vldwlpti
//
LOCUS       WP_284886039             310 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Aerococcus urinae].
ACCESSION   WP_284886039
VERSION     WP_284886039.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..310
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=32126
     Region          8..305
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mnrvcellni eypifqgsma gvaeaplaga vseagglgvi atagrkgdwl reqikavrei
       61 tdktfavnlm lmshnteeim eviidegikv vttgagnaap liaplheagi kvvpvvanar
      121 qakkmedaga davvcegsea gghvgevttm plaraviaav dipviiaggi sdghglaaaf
      181 alggegvqlg tvfcaseeap iaqgykeaiv ncgltdtvvv grsigapvrl iqndmvaklq
      241 eeidngstrd efeksnlqml ltaitkgdte kgivtigqva gniteirpvk eiinsiveea
      301 realknmptl
//
LOCUS       WP_284886493             239 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Citrobacter freundii].
ACCESSION   WP_284886493
VERSION     WP_284886493.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 239)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..239
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27049
     Region          52..226
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mtaeadylnq ydasrfpspl vtvdsalftl hqqalcvllv erakhpqkgr wglpggfidi
       61 enddstrtta lrkltektgv spswleqldt fsgpdrdprg wsltvtwfal iawvdcaphi
      121 asvsnarwvp vdelknysla fdhekiitaa lhrlrqktmy sllpvyclpe tfthgqllea
      181 tevilgqsiq rkslirrfea sgmfedtges vatgtrkarl wrrkpnvdfh ffsrnlltd
//
LOCUS       WP_284886477              77 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase, partial [Aerococcus sp.
            UMB9870].
ACCESSION   WP_284886477
VERSION     WP_284886477.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB9870
  ORGANISM  Aerococcus sp. UMB9870
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 77)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 77)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Aerococcus sp. UMB9870"
                     /db_xref="taxon:3046351"
     Protein         <1..>77
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
     Region          <1..>77
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 laetestqav favmplpepl sleqltssai llldglqdpg nlgtiirtad algyhslilg
       61 kgsvdpynsk alramqg
//
LOCUS       WP_284886524             142 aa            linear   BCT 25-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Citrobacter freundii].
ACCESSION   WP_284886524
VERSION     WP_284886524.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..142
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=14834
     Region          6..140
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mnksqqiati tlaaakkmaq aveakaleis vpvvfsvvdh ggntllmqrm ddafvtscdi
       61 slnkaytacc lrqgtheitd avqpgaslyg lqltnqqriv ifggglpvil ngkligavgv
      121 sggtveqdrl laetalncfs el
//
LOCUS       WP_284886191             243 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Aerococcus urinae].
ACCESSION   WP_284886191
VERSION     WP_284886191.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..243
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28056
     Region          1..239
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mkvlivddeq marqelaylv kehdqvnqvk tadsidqait mmldekpdil fldihleget
       61 gfdlakklka vhnppylifa taydqyalea feanandyil kpfeeskiha aidkyyqsle
      121 rasgqvdqdq eskrheaipi qsndrvyllr peeiflvsvq ghtlsiesyd ktyemagsls
      181 aiekklpkdl flrthrsyli nidqiqeiqp wfnqtyqvtl rngskvpvsr sylkdfkdrl
      241 pie
//
LOCUS       WP_284886756             103 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Citrobacter freundii].
ACCESSION   WP_284886756
VERSION     WP_284886756.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..103
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=11109
     Region          4..>75
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mknkidvsii ipaynaaatv gclvnkilse phvaielivv ddgstdgtgn iihqihddql
       61 iliektnqdv yaarkvlcls wtcvsvhtqn mfiavsvsit rsh
//
LOCUS       WP_284887676             408 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Acinetobacter ursingii].
ACCESSION   WP_284887676
VERSION     WP_284887676.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter ursingii
  ORGANISM  Acinetobacter ursingii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616068
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Acinetobacter ursingii"
                     /db_xref="taxon:108980"
     Protein         1..408
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=46784
     Region          164..301
                     /region_name="Methyltransf_32"
                     /note="Methyltransferase domain; pfam13679"
                     /db_xref="CDD:379330"
     Site            order(195..201,224..225,250..252,266)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
ORIGIN      
        1 maalathspq eqqflelihq tiqsqqferl ilsqyqgtet elekitfrmv elqqqtklsa
       61 lyhyktkdvt knyelkesld vieklvhlck qanlfahnve aqlkknkkkv llniqqhtkp
      121 slehskptqq hnrekeryvd qaspflqylg iteangkiip amarkwkqin kfieifshay
      181 dqievkkdqv nivdfgsgkg yltfalydyl qqqtatqpvv tgvelrsnlv efckeiatka
      241 gfdrldffeg dvrtyqteql dvmialhacd iatdfaihtg irlnasmimc apcchkelrp
      301 qlhspsvlkp mlqfgihagq qaemltdtlr alllkaygyd vkvfefvsle htsknkmila
      361 tkrkdidqpd pkileqiqal kqmygiekqt lelllndqia ienvgckc
//
LOCUS       WP_284887891             209 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Citrobacter amalonaticus].
ACCESSION   WP_284887891
VERSION     WP_284887891.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter amalonaticus
  ORGANISM  Citrobacter amalonaticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Citrobacter amalonaticus"
                     /db_xref="taxon:35703"
     Protein         1..209
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=22880
ORIGIN      
        1 metvgqrikh lrerlrlsqa dlaekcgwey qsrvgnyetg arkvsvedav vlasalgvsp
       61 gellfgtpdn aefvsaghrs vpivsyiqag mftepdyils pegveetisf dgpasnlifa
      121 lrikgdsmep efregdtviv dpavaphpge fvvakngdhe atfkkyraka dggfelvpln
      181 pdypsldsak nkvtiigtmi ehrihrrkr
//
LOCUS       WP_284888179             365 aa            linear   BCT 25-DEC-2024
DEFINITION  AcrVA2 family anti-CRISPR protein [Acinetobacter ursingii].
ACCESSION   WP_284888179
VERSION     WP_284888179.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter ursingii
  ORGANISM  Acinetobacter ursingii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Koonin,E.V. and Makarova,K.S.
  TITLE     Anti-CRISPRs on the march
  JOURNAL   Science 362 (6411), 156-157 (2018)
   PUBMED   30309933
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Marino,N.D., Zhang,J.Y., Borges,A.L., Sousa,A.A., Leon,L.M.,
            Rauch,B.J., Walton,R.T., Berry,J.D., Joung,J.K., Kleinstiver,B.P.
            and Bondy-Denomy,J.
  TITLE     Discovery of widespread type I and type V CRISPR-Cas inhibitors
  JOURNAL   Science 362 (6411), 240-242 (2018)
   PUBMED   30190308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19225148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Acinetobacter ursingii"
                     /db_xref="taxon:108980"
     Protein         1..365
                     /product="AcrVA2 family anti-CRISPR protein"
                     /GO_function="GO:0140721 - nuclease inhibitor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42714
     Region          93..356
                     /region_name="AcrVA2-like"
                     /note="Anti-CRISPR type V subtype A2 and similar proteins;
                     cd22987"
                     /db_xref="CDD:467859"
     Site            order(96,174,203..204,242..243,245..246)
                     /site_type="other"
                     /note="putative Cas12a binding site [polypeptide binding]"
                     /db_xref="CDD:467859"
     Site            order(123,126,160..162,241,245,248)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467859"
ORIGIN      
        1 mnlnyantni tlekvnngln rkleelnpin tleyisktyt giwnkvediv inekfsnskw
       61 snniflpfty wlpitldiky pnwhknykek ympnwgidyv sisaigtwry tkgiykldde
      121 ianyffidds dikipsklle nqpewsiyvd trnldisldg ervigfwsci dcypssnqpy
      181 snlkalsiip lfsnrlgyml sasipldenk flsieqstnd llnhipknfa vddkrdsddl
      241 kelicfkkkv tqillfiiqp epditehdqp iestivnpyp kiikgkyrly eakkpryfnv
      301 gtqagknlkq afatykatgk kqaphirkah whgywkgskk lekqeffykw ippvlvnsyl
      361 eeekn
//
LOCUS       WP_284888121             453 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Acinetobacter ursingii].
ACCESSION   WP_284888121
VERSION     WP_284888121.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter ursingii
  ORGANISM  Acinetobacter ursingii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Acinetobacter ursingii"
                     /db_xref="taxon:108980"
     Protein         1..453
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=52012
     Region          14..452
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mahsreqqti ikkalsakai ekmkigdpdk adigeyvglr vhcgktgmkt ffyryrspvd
       61 dsikqykigt fpqvslaear ielgrlkaer sqgvcpkqkk eqeklqqqie qelaqknmcq
      121 ltvhqmiemy lteviedhsi tdpktgekkk vlgvrkpkgq aetrrtlygd avrvlgnlva
      181 levtrkdvva ltkeiinrgs nvqagrvlse ltlayeyaig leqfpsnfan pallakmsik
      241 qsrlkvtckk gtrvlndqel khvwawlpts gftthqkhil fltlwtgcrt gelcdarwrd
      301 fnldqgtwhl kasknstery vqlsrqcinf llnlyrpdqe ylfassrtgl piqqksltei
      361 kwqmknpdkv qanfrpeqlw ldnmddwnph dlrrtvrtgl srlgcpsdia eavlghskkg
      421 iegtynlhny ekecaewlqk wadyldeiie nkf
//
LOCUS       WP_284888414             402 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Citrobacter portucalensis].
ACCESSION   WP_284888414
VERSION     WP_284888414.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 402)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 402)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..402
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43075
     Region          50..277
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
     Region          212..384
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mrnvtilaac lftasvsaae sngeyiaris dcvachtaeg gaamaggkkf ptpvgdiyst
       61 nitpdktqgi gnysyedfek avregiakdg hplypampyp syaklsdedv kalysyfmhd
      121 vtpsaqpnke naipwllsar wplhiwnwlf tdapvmaveg aktddnaalv krgaylvegp
      181 ghcgschtpr gmamnekayt nadaeylsga midgwyapsl rgtgmseqel ksllltgksk
      241 haavsgsmae vvtqstqylt dedataiaqy llslksgkpe tvraaattas wsnspevgkv
      301 tynrycstch glegkgtddn apslvnnplv mvddptplfr viahgaetpt trgsvsfkmp
      361 ayggllsdne mrdvinyvrk swgegnsevs qedlagvkka sh
//
LOCUS       WP_284888457             372 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Acinetobacter baumannii].
ACCESSION   WP_284888457
VERSION     WP_284888457.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..372
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40415
     Region          1..369
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mttalnglkv ldfstllpgp fatmyladmg aevihiesps rpdlirimpp yangqatahs
       61 ylnrnkqsiv ldlkdaasid likakisefd ivieqfrpdv mrrlgldyat laeinprliy
      121 csitgygqtg sykdraghdi nylalagiag ysgrqdsgpp plgiqvadia ggslhaviai
      181 laavversrs gigqyidism tdcvaslnsm aasatlaaqv eqapeqgmln ggifydyymt
      241 qdgrylsigs lepqfmagls aaldlpvllq kgasldeqdr qevkqaiqek ikaktfkewh
      301 eifanldvcv epvlslseal nsplaqqrgw ivnvplqnnt pdtepqiacp ikfsrsqmry
      361 sfvgkklgeg qw
//
LOCUS       WP_284888568             318 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: amidohydrolase family protein [Burkholderia].
ACCESSION   WP_284888568
VERSION     WP_284888568.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..318
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35002
     Region          24..318
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mcsqaraerh gdappphalp aalvdahhhl wqlgagahyp wlqerydpar fmfgdyaalc
       61 rdfgvddyry aaqrapivas vhveaerarg ealaetrwlh evaaahglps avvawvdlla
      121 ddaherlaeq aawprvrgvr fkprtaaapd afvdgpgtlr dprwpaaler vaahglgwdl
      181 rvpfwhlgda aalladapgi dvvlehaglp wdrseaglar wrggmealaa sprvtvkise
      241 lglrdavwne adnariirdt iaifgwqrcl fasnfpvagl rvsypallrt faramadlde
      301 aarqaiwhdn amrvyris
//
LOCUS       WP_284888891             218 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: protein-L-isoaspartate O-methyltransferase family
            protein [Burkholderia].
ACCESSION   WP_284888891
VERSION     WP_284888891.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Edwin,R.K., Challa,N., Sharma,R., Satyamoorthy,K., Parsa,K. and
            Misra,P.
  TITLE     PIMT/TGS1: An evolving metabolic molecular switch with conserved
            methyl transferase activity
  JOURNAL   Drug Discov Today 27 (8), 2386-2393 (2022)
   PUBMED   35462043
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Furuchi,T., Sakurako,K., Katane,M., Sekine,M. and Homma,H.
  TITLE     The role of protein L-isoaspartyl/D-aspartyl O-methyltransferase
            (PIMT) in intracellular signal transduction
  JOURNAL   Chem Biodivers 7 (6), 1337-1348 (2010)
   PUBMED   20564550
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Kagan,R.M., McFadden,H.J., McFadden,P.N., O'Connor,C. and Clarke,S.
  TITLE     Molecular phylogenetics of a protein repair methyltransferase
  JOURNAL   Comp Biochem Physiol B Biochem Mol Biol 117 (3), 379-385 (1997)
   PUBMED   9253175
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..218
                     /product="protein-L-isoaspartate O-methyltransferase
                     family protein"
                     /EC_number="2.1.1.77"
                     /GO_function="GO:0004719 - protein-L-isoaspartate
                     (D-aspartate) O-methyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0030091 - protein repair [Evidence IEA]"
                     /GO_process="GO:0036211 - protein modification process
                     [Evidence IEA]"
                     /calculated_mol_wt=23994
     Region          12..210
                     /region_name="Pcm"
                     /note="Protein-L-isoaspartate O-methyltransferase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2518"
                     /db_xref="CDD:442008"
ORIGIN      
        1 mnienarfnm ieqqirpwdv ldldvlglls ivkrenyvsp ehrdlafadl elplpggrsk
       61 mlfprvearv lqelavkkhe nvlvigagsg ylaalfahrt lhvtaveidp aiakfaadnl
      121 rndgvtnaev algdgslgwp dkapydvicv agglpvvpqq mleqlkiggr lsafvggrpv
      181 mkaqiitrid dkqyrvadvf etyvdhlvna iepsrfkf
//
LOCUS       WP_284888903             297 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: SIR2 family NAD-dependent protein deacylase
            [Burkholderia].
ACCESSION   WP_284888903
VERSION     WP_284888903.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..297
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=31759
     Region          30..292
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mplsdspelp dssgstdssa agaqlpahli asavdalara dallvtagag igvdsglpdf
       61 rgtdgfwray palrherfef heiaspqafr ahpqlawgfy ghrlalyret vphagfailr
      121 rwmdampngg fvltsnvdgq fqkagfdpar vaeihgsihs mqclrpcsdd twdampftpd
      181 vdaaacrlvg elprcprcgg larpnilmfg ddgwlgeryd aqeralqdwi aqagwvtvve
      241 igagtaiptv rllserlgad virinareah arradvvglk ggalatlgal drawrgg
//
LOCUS       WP_284888991             396 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Burkholderia].
ACCESSION   WP_284888991
VERSION     WP_284888991.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..396
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43605
     Region          226..389
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 metrwapqes qstseeadig vadfselmar iyqgpletpp wagalelvrr llqanyvtli
       61 lraaasdrra plsvhasefg pvvpgdgeas ynnyyysldp fvglpadrvv tvddvfgdtg
      121 wlsselykqf lkpqdvryil gadlrapsgv ecrfrvcrnh askqfsardk aicalllphl
      181 kravelhsrl dtaeversiy anainrmqig titldengti idlnsvaddi lkqnngltia
      241 rgtieatdaq enrtlkrlir havmghhgta aatveampit rsfdkprlgl lvrtvllsdw
      301 sednkrrpav tlflrdpdrk pqgaqeiirk lfdltpaets lallltnglt leeaaeesgi
      361 skntarthlr aifsktgvtr qatlvrillg svvplg
//
LOCUS       WP_284889007             345 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sigma-54 interaction domain-containing protein
            [Burkholderia].
ACCESSION   WP_284889007
VERSION     WP_284889007.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..345
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37353
     Region          <40..336
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 miniatretr gadfqngplt pmaetanrpk qradarqlsg rstamrtllg riekiaptra
       61 svmiagesgv gkdivarrlh dlsarrdgpf vpvncgaipa diaeaqlfgh ekgsftgaia
      121 qregffeaac ggtllldeia empaalqvkl lralesntiv rvggteaipl dvrivsatrh
      181 npaeavrdgr lredlfyrla afalyvpplr qrngdvetia qefvdalner hrshkrltda
      241 aiaalraysw pgnvrelhnt ierayiladd gidvalpkpt llpdqtsdda malplgatlh
      301 htqqrfiaat ldhfdgnkpq aakalgislk tlynrlalmr dggpa
//
LOCUS       WP_284889039             350 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Burkholderia sp.
            lyk4-R2A-23].
ACCESSION   WP_284889039
VERSION     WP_284889039.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. lyk4-R2A-23
  ORGANISM  Burkholderia sp. lyk4-R2A-23
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Burkholderia sp. lyk4-R2A-23"
                     /db_xref="taxon:3040284"
     Protein         1..350
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=38922
     Region          1..337
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 milvyryrvk slngllnkqs ravnyvwnfc ndtqkhalkw skkwptgfdl nvlttgsska
       61 lgihsgtina tceqyaksrs qhrrpylryr gkkslgwvpl kgrdlkregd afrfagntfr
      121 vfhsralpeg kikdgtnfaq dargnwflni viempdvqar pvrsgvgidl glkdfatlst
      181 geklpndrfg rraaeklaka qrarkhkrhi aklhakvana radfqhklal dlvrrfdyia
      241 vgnvsaakla rtrmaksvyd aswssfrskl rykaiahgat feevdesgst qscsacgskd
      301 sttrpkgiag lrvrewacdg cgvvhdrdin aalnilrcgr aspgvgitcl
//
LOCUS       WP_284889105             113 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Actinotignum].
ACCESSION   WP_284889105
VERSION     WP_284889105.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum
  ORGANISM  Actinotignum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Actinotignum"
                     /db_xref="taxon:1653174"
     Protein         1..113
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11758
     Region          1..>66
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 msasearigq riaaaracvg msqrdlaass glsqstihri eagerpatli elsliadacg
       61 vlvdhlrgtd siqsevryag rtdtagaegl ydylvyalgl arrlddigip eaa
//
LOCUS       WP_284889326             357 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [Actinotignum].
ACCESSION   WP_284889326
VERSION     WP_284889326.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum
  ORGANISM  Actinotignum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 357)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 357)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Actinotignum"
                     /db_xref="taxon:1653174"
     Protein         1..357
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=37784
     Region          19..318
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrarslrmti rtalaaillv gipalvmggv tiprnaldea rarrdmllfl gaeilaiiva
       61 ilvavgiamr vsrrisapli ylaaaaeqlg agttrpqmap sgieeidlvf eeiaraadrm
      121 agrlsaerqf aadashqlrt pltslsmrle eiqylsndpd vkeeatrcle qverltgvvt
      181 dllhasraqe sateavalqp iftqqgvewe rafaaagrkv vftvgdhgpv lsdpgalsqi
      241 iatcvenslk ygagtttvts rpagrgviid isdegegvap efveaiftqg fslggstgfg
      301 lplarqlaer nggrlelsqa qppifsvvla alpaaldpak vfpaggeisv garrrrf
//
LOCUS       WP_284889348             266 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: potassium channel family protein [Burkholderia].
ACCESSION   WP_284889348
VERSION     WP_284889348.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..266
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=29007
     Region          55..>260
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mwifrvdepr lgvirirewr rharftilll llllggaatg lvlldpsnts fhdkvftalw
       61 dganlvttlg nftdfnrpqk ifmllamfat lliggfavsr ltgmlsgddv mayrenrvme
      121 rklehlanhv vlvgfhslge lvanrlreag qtvlvlvgdr dqaeraadrg hmvvlgspgv
      181 fddvlrrarl dsakalvvtt pdsnnnlait llahtlnasl aivapgensl rkglfeiaga
      241 sdvvivdeiv analvgkltt qveerp
//
LOCUS       WP_284889355             183 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NADPH-dependent FMN reductase [Actinotignum].
ACCESSION   WP_284889355
VERSION     WP_284889355.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum
  ORGANISM  Actinotignum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Actinotignum"
                     /db_xref="taxon:1653174"
     Protein         1..183
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19835
     Region          1..159
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mkiaiisgsi regqategva ryvaqlaaqr ageatyelvn ikdfdipllt spvvpaaang
       61 qydhpaiqrw adkisefdaf ifvtpeynhg vpgafknavd glgvewmnkp vafvghgsig
      121 gvraieqwrq itanfnmpai rsevnfmmfe dwadgaftpl errageveav lsglekltaq
      181 lak
//
LOCUS       WP_284889385             222 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FtsB family cell division protein [Actinotignum].
ACCESSION   WP_284889385
VERSION     WP_284889385.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum
  ORGANISM  Actinotignum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Actinotignum"
                     /db_xref="taxon:1653174"
     Protein         1..222
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=23795
     Region          14..99
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
     Region          144..>221
                     /region_name="kgd"
                     /note="multifunctional oxoglutarate
                     decarboxylase/oxoglutarate dehydrogenase thiamine
                     pyrophosphate-binding subunit/dihydrolipoyllysine-residue
                     succinyltransferase subunit; cl39092"
                     /db_xref="CDD:476867"
ORIGIN      
        1 mesgqrqhtv slravaialf ailaiiivtp tvsrfseqqh elravraele nvqqhtrele
       61 vekalwndpd yvraqarvrl gyvvpgqrlf vgadpnegta qeqleervat vnrerrantp
      121 wyitgwdsit iagnsvdgqi dnpdeapmyt pptpqpdsat qpegetpadg sapapaeqpa
      181 eqpaeppaeq papedaanpa sdtapaqdta paqdtapaae ge
//
LOCUS       WP_284889951             341 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [Actinotignum].
ACCESSION   WP_284889951
VERSION     WP_284889951.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum
  ORGANISM  Actinotignum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Actinotignum"
                     /db_xref="taxon:1653174"
     Protein         1..341
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=35127
     Region          104..310
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mttqsamhmd ntrvvaeqlr ratmrgvlag glgtialvfv avaglsllgg fspipiiigl
       61 agllalggaa wivwrgngra ladvapasst wmarpsdhrd vvhaqrsiaa afeierrrie
      121 rdlhdgaqqy lvatsmdvge aafllegdan gavssadlaa arermasaqd raelaltslr
      181 rtvagihpkv lsdlgleaav rdlvvsapvp atlrvprplp eipegviaaa yftvaevltn
      241 vakhapaata tvlliadddl hlsitdtgpg gvipgsglrg igerlaafgg slrisspvgg
      301 pteiraripl llhrgewgsg agvaplseni rtegtdasgc c
//
LOCUS       WP_284890230             120 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Actinotignum].
ACCESSION   WP_284890230
VERSION     WP_284890230.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum
  ORGANISM  Actinotignum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Actinotignum"
                     /db_xref="taxon:1653174"
     Protein         1..120
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13411
     Region          1..51
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
ORIGIN      
        1 mdsavfkgtr aamglstasl adrlgiskrm vdlweagrcp vpeditkrll efwdhwvgel
       61 drlmnptyad aetliyyrte ksytdahpha sfdyheynal vtaafaacaa eglprkiiwa
//
LOCUS       WP_284889639             188 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: CinA family protein [Actinotignum].
ACCESSION   WP_284889639
VERSION     WP_284889639.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum
  ORGANISM  Actinotignum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Galeazzi,L., Bocci,P., Amici,A., Brunetti,L., Ruggieri,S.,
            Romine,M., Reed,S., Osterman,A.L., Rodionov,D.A., Sorci,L. and
            Raffaelli,N.
  TITLE     Identification of nicotinamide mononucleotide deamidase of the
            bacterial pyridine nucleotide cycle reveals a novel broadly
            conserved amidohydrolase family
  JOURNAL   J Biol Chem 286 (46), 40365-40375 (2011)
   PUBMED   21953451
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Martin,B., Garcia,P., Castanie,M.P. and Claverys,J.P.
  TITLE     The recA gene of Streptococcus pneumoniae is part of a
            competence-induced operon and controls lysogenic induction
  JOURNAL   Mol Microbiol 15 (2), 367-379 (1995)
   PUBMED   7538190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Actinotignum"
                     /db_xref="taxon:1653174"
     Protein         1..188
                     /product="CinA family protein"
                     /calculated_mol_wt=18785
     Region          12..162
                     /region_name="PncC"
                     /note="Nicotinamide mononucleotide (NMN) deamidase PncC
                     [Coenzyme transport and metabolism]; COG1546"
                     /db_xref="CDD:441155"
ORIGIN      
        1 mmtaqpsgaa dlaaltetcv rhlrerglsl acaesltggl ltaqfvtipg vsavlrggvv
       61 syatdlkasi lgvsserlas hgpvdreval qmargvcdva gadigmattg vagpgphdgh
      121 pagtvwiavs trsgahlare lhiaggrsdv rsgavrgave llgtflhdga tdqcansavs
      181 gltpvrsq
//
LOCUS       WP_284890347             311 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [Actinotignum].
ACCESSION   WP_284890347
VERSION     WP_284890347.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum
  ORGANISM  Actinotignum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426811
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Actinotignum"
                     /db_xref="taxon:1653174"
     Protein         1..311
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=33602
     Region          18..305
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 msslpadnsc vwipgpwehr lvtangaqfh layagshstr tplvlfvhsy peywyawrhq
       61 iepvaqagye vaavdlrgvg gsdktpsvqs gpelaqdlis lteslgassa vivaagsnaa
      121 lgwaaaamap diitglvtva sphplglrhf grgirprgll glltsrlgnr spralgdarn
      181 mrrlllewsa phshgaadea eqyaaamrlp eaaasaveql rwtatwrrrp sgkawrdils
      241 tpvdvpvwav rgladrmine rawaddrsfa tgsyrliavp gaghfipees preftnivld
      301 flsqlersar v
//
LOCUS       WP_284890603             254 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: YczE/YyaS/YitT family protein [Actinotignum].
ACCESSION   WP_284890603
VERSION     WP_284890603.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum
  ORGANISM  Actinotignum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Actinotignum"
                     /db_xref="taxon:1653174"
     Protein         1..254
                     /product="YczE/YyaS/YitT family protein"
                     /calculated_mol_wt=27238
     Region          28..184
                     /region_name="YczE"
                     /note="Uncharacterized membrane protein YczE [Function
                     unknown]; COG2364"
                     /db_xref="CDD:441931"
ORIGIN      
        1 mrdtffsare wtlrpgsllr rclvcllgvi itsmgitval kghagvdpft amlqgvsyvt
       61 glsfswvvpl vniallaiii pfdrkifglg tvlnftlvgv lvteftkvld siyvftysvp
      121 gmlihlavgl llfafglsly itpdlgqgaa dgiapvlvrr fpqrsyrffr iaqdftviii
      181 alllfrfdls ggvigvgtvv mvvgigvvvd ffnrtvagkl vgapshlttq aqaqpepaae
      241 lshtsavlhq rsas
//
LOCUS       WP_284890861             213 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: OmpW/AlkL family protein [Burkholderia].
ACCESSION   WP_284890861
VERSION     WP_284890861.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006882
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..213
                     /product="OmpW/AlkL family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22394
     Region          27..213
                     /region_name="OmpW"
                     /note="Outer membrane protein OmpW [Cell
                     wall/membrane/envelope biogenesis]; COG3047"
                     /db_xref="CDD:442281"
ORIGIN      
        1 mhktirtcvt aaaiaaslaa lpslshaasp gdginqgdvl vrlraisiqp nerasdtlga
       61 intgvnnaiv peldftymir dylgvelilg tsrhqmtssl gnlggvgvlp ptlllqyhfn
      121 hagkvrpyvg aglnytyfyn nglnvggegv sinkssfgpa lqfgvdvqvt kkvfmnvdvk
      181 kiwmstdatl gdkgigtlhi dplivgvgvg mkf
//
LOCUS       WP_284890860             396 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)H-dependent flavin oxidoreductase
            [Burkholderia].
ACCESSION   WP_284890860
VERSION     WP_284890860.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..396
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=42275
     Region          30..384
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mtartsfppl kirgrtllpv vqggmgvgvs ahrlagsvar egalgtiasi dlrhhhadll
       61 arcranpdrp tleaanldal areirlakty segrgmiavn vmkavsahad yvrvacdega
      121 daivmgaglp ldlpdltqgh dialipilsd srgialvlkk wmkkgrlpda iviehpahag
      181 ghlgvtqidd lhdarfdfar vldetaqvma slglardtip livagginsh dtvraalvag
      241 angvqvgtpf avteegdahp nfkrvladal pddivefvsv tglparavkt pwldrylrne
      301 trirdklgaf rqrcptalec lsvcglrdgi ekfghfcidt rlaaalrgdv anglffrgre
      361 alpfgnairs vrdlldlllt graaepatnr pmftla
//
LOCUS       WP_284890928             183 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: KdsC family phosphatase [Burkholderia].
ACCESSION   WP_284890928
VERSION     WP_284890928.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..183
                     /product="KdsC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=19533
     Region          10..163
                     /region_name="KdsC"
                     /note="3-deoxy-D-manno-octulosonate 8-phosphate
                     phosphatase KdsC and related HAD superfamily phosphatases
                     [Cell wall/membrane/envelope biogenesis, General function
                     prediction only]; COG1778"
                     /db_xref="CDD:441384"
ORIGIN      
        1 msgamyrgpv rlvlfdvdgv ltdgllhvta egefmksfha hdgvavallr vhgiragils
       61 gkhsgalawr akqlgidvlv tgcddkgagy adikarqqvd dheiayvgdd vndlavierv
      121 gvsyapadah rlvrarvdhv artaggrgva revaehllte aglslddayr pllerwsghd
      181 ivq
//
LOCUS       WP_284891103             371 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Actinotignum
            sanguinis].
ACCESSION   WP_284891103
VERSION     WP_284891103.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum sanguinis
  ORGANISM  Actinotignum sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Actinotignum sanguinis"
                     /db_xref="taxon:1445614"
     Protein         1..371
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39766
     Region          80..352
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mstdivttlg mllylherpe gaslaeltah fqfpswkrtl dylwdanlae tadfdipfel
       61 elperaasag rvaesdtagg pesrvylrsm tddpvipftl ddamvvaall daardvtapg
      121 paattltatr nalgeavrea gyegalwppt rpaadaatme avhaalqggc yldfnyerav
      181 aepfahakag hehviplvil agdapllral taqglrhfrl dritaarpga klnrseraaa
      241 rkalaeveks ekvqrtrged tweprgtqvr itvtgasrwv aetlpgarvr eadeeygtaa
      301 apggaellti evrarslswl vsllvqiddv ialeppavar avgrycarlr aqkgddaaac
      361 vsdesapege r
//
LOCUS       WP_284891142             427 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: aromatic ring-hydroxylating oxygenase subunit alpha
            [Burkholderia].
ACCESSION   WP_284891142
VERSION     WP_284891142.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468625
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..427
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47745
     Region          20..423
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
     Region          191..425
                     /region_name="RHO_alpha_C_AntDO-like"
                     /note="C-terminal catalytic domain of the oxygenase alpha
                     subunit of Pseudomonas resinovorans strain CA10
                     anthranilate 1,2-dioxygenase and related aromatic ring
                     hydroxylating dioxygenases; cd08879"
                     /db_xref="CDD:176888"
     Site            order(198..199,203,206..207,210,212..213,215,217,327..328,
                     369..371,373..377,388..391,413,416,420)
                     /site_type="other"
                     /note="putative alpha subunit interface [polypeptide
                     binding]"
                     /db_xref="CDD:176888"
     Site            order(207..208,210..211,213..214,218,301..302,304,312,314,
                     319,353,356..357,363..364,367)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176888"
     Site            order(207..208,210..211,213..214,218,301..302,304,312,314,
                     319,353,356..357,363..364)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:176888"
     Site            order(213,218,367)
                     /site_type="other"
                     /note="Fe binding site [ion binding]"
                     /db_xref="CDD:176888"
ORIGIN      
        1 msdipyqtid tralhgfaqp driapamyhd palfeaeldr ifyrtwiwva heselpnpgd
       61 fitttigrqp vivvrdktge invlqnrcrh rgatvceshk gnakgftcpy hswsyaldgt
      121 lralpygdgy egvcekgdlp lvklrvgvyq glifasfndd iepledflgg akpwidlfmk
      181 qgagypikan gehkfkfkgn wkiqlenttd lyhfpvvhks wmksiddeta aaitsfmtse
      241 hafcralgng hslavlmpel idldeddgap lperfaplaa klaerhapde vrrivrsllg
      301 vgfnlnlfpn lalsmaffrv lrpisanete irhvalamdg gpdeanrerl rihehfqgpf
      361 gfgspddaea wervqrgaha gpdvpilvnr glnrettaan gektahatde tgmreayqqw
      421 rklmeqa
//
LOCUS       WP_284891233             350 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: RNA-guided endonuclease InsQ/TnpB family protein
            [Burkholderia].
ACCESSION   WP_284891233
VERSION     WP_284891233.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..350
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=39113
     Region          1..337
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 milvyryrvk slngllnkqs ravnyvwnfc ndtqkhalkw skkwptgfdl nvlttgsska
       61 lgihsgtvna tceqyaksrs qrrrpylryr grkslgwvpl kgrdlkregd afrfagntfr
      121 vfnsrplpeg kikdgtnfaq dargnwflni viempdvqar pvrsgvgidl glkdfatlst
      181 geklpndrfg rraaeklaka qrarkhkrhi aklhakvana radfqhklal dlvrrfdyia
      241 vgnvsavkla rtrmaksvyd aswssfrnkl rykaiahgat feevdesgst qpcsacgsrd
      301 sttrpkgiag lrvrewacse cgvehdrdtn aalnilrcgr aspgvgitcl
//
LOCUS       WP_284891291             314 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Burkholderia].
ACCESSION   WP_284891291
VERSION     WP_284891291.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..314
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34008
     Region          5..310
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mrrlalpfav allagflata hatpggpavs passapaaai vspatiapaa qeppvnpgss
       61 vvlrafrsas lkrdwsytvy lppgynpega rypvlyllhg nagnandwit qgrlqatadt
      121 lierheippv vivmpqggtd wyvdrkekmq saflndllpe veahfavsnq ragraiggvs
      181 mggfgalrfs llepglfcga mllspaiyan epplnsaary vgvfgdrqfd prvwhefnyp
      241 almrgyfarn wrvpmfiavg dddltiqaes svlythlrra qnpaelrivd gghtwevwrg
      301 llgqglkyal ecvk
//
LOCUS       WP_284891304             332 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Burkholderia sp.
            lyk4-R2A-23].
ACCESSION   WP_284891304
VERSION     WP_284891304.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. lyk4-R2A-23
  ORGANISM  Burkholderia sp. lyk4-R2A-23
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Burkholderia sp. lyk4-R2A-23"
                     /db_xref="taxon:3040284"
     Protein         1..332
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=33667
     Region          9..332
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(46..47,51,128,132,135,153,156..158,177..178,182,197,
                     221..222,243..245,248..249,270..273,320,322)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(140,236..237,252..257,265..272,275..276)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mtqvvtatri gidrygdagv lrsvdapvgp pgagevrirq tavgvnfvdi yfrtgahplp
       61 alpdalgvea agvidavgpg vtalvpgqrv ayaglptgsy aslrtlpaer vvpvpdgvsd
      121 daaaagllkg itvymllhrv rqvgagdtvl vhaaaggvgl latqwarahg arvigtvgsa
      181 akaalvrahg aeavvdyree dfvaaarafg ggagvdyaid giggdvltrt lgavrpfgmv
      241 asigqvaaig arqtidldel gparsialar psvlgfiard vagyreaara tldrladgmh
      301 veigarlple raadahrlle srqttggvvl vp
//
LOCUS       WP_284891330             277 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: arylamine N-acetyltransferase family protein
            [Burkholderia].
ACCESSION   WP_284891330
VERSION     WP_284891330.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Zhou,X., Ma,Z., Dong,D. and Wu,B.
  TITLE     Arylamine N-acetyltransferases: a structural perspective
  JOURNAL   Br J Pharmacol 169 (4), 748-760 (2013)
   PUBMED   23517104
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Sim,E., Walters,K. and Boukouvala,S.
  TITLE     Arylamine N-acetyltransferases: from structure to function
  JOURNAL   Drug Metab Rev 40 (3), 479-510 (2008)
   PUBMED   18642144
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Sim,E., Westwood,I. and Fullam,E.
  TITLE     Arylamine N-acetyltransferases
  JOURNAL   Expert Opin Drug Metab Toxicol 3 (2), 169-184 (2007)
   PUBMED   17428149
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Sinclair,J.C., Sandy,J., Delgoda,R., Sim,E. and Noble,M.E.
  TITLE     Structure of arylamine N-acetyltransferase reveals a catalytic
            triad
  JOURNAL   Nat Struct Biol 7 (7), 560-564 (2000)
   PUBMED   10876241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..277
                     /product="arylamine N-acetyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30758
     Region          5..259
                     /region_name="NhoA"
                     /note="Arylamine N-acetyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2162"
                     /db_xref="CDD:441765"
ORIGIN      
        1 mtdsfdlpry farigydgpa eptldvlrrl hllhpqaipf enlnpltgar valdlpaiid
       61 kvighrrggy cfelnklfyt althigfrvt pliarvrwmr ppevvtaqth mllridldga
      121 twladigfgs atltaplrfv pdarqltphg afrvvgapvd gefdmqfeip dgwqttyrfs
      181 lkraewidyd aanwftstyp esifvndlia crvlpdgraa lfntvltlrd aagagrtvtf
      241 ddaaawgacl rdtigidttg fdldalfarv varanmm
//
LOCUS       WP_284891469             634 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: DUF3857 domain-containing transglutaminase family
            protein [Burkholderia].
ACCESSION   WP_284891469
VERSION     WP_284891469.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12125919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..634
                     /product="DUF3857 domain-containing transglutaminase
                     family protein"
                     /calculated_mol_wt=68662
     Region          56..186
                     /region_name="DUF3857"
                     /note="Domain of Unknown Function with PDB structure
                     (DUF3857); pfam12969"
                     /db_xref="CDD:432907"
     Region          207..376
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mmrfpfrstg rlpyraaafa vavaaaalaq paladsgdea pvtlvsdvhv fviqhdgsld
       61 eeddstlran dangidaiaq ryvwfdknle kvdlvaaeti drggvahpvg pdgirdvqep
      121 rsagaptfqd gllrtvvfpg veagsstria frkartkpvn agyfgyyvep srepvenqrl
      181 ifdvpadmpl qadargyval ppvtangrtr ytfdyrhgay driesgsvgy ptygdrlvvs
      241 tlpdyaafaa ryrnaavdsg andpavvqla raltadvadp hdkarllydw vqanvryval
      301 flgetaaaph rvtdilrnry gdckdhvalf gallaavgir sepvlinlgs vytlpsvpgy
      361 gggainhait wlpglglyad tttsgiafgy lppivmdrpa llvdsgvlsr tpatqpkrrt
      421 arveidaaqp gaarfhalvv ddgwtaeler tlfrrapper vrqlanerlr qsglrgrari
      481 stgerratdg pfdvtydgtl dhvvwpdgtt avpalssvtg giatqvegwl aepmrtqpwv
      541 clggtfdetg qialpagvav tdlptdtavh drfvdftshy vfdaaahivq vtrrmtatfg
      601 rqvctpdeyt alraslerie rdtqaqivvr arqr
//
LOCUS       WP_284891534             199 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Burkholderia sp. lyk4-R2A-23].
ACCESSION   WP_284891534
VERSION     WP_284891534.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. lyk4-R2A-23
  ORGANISM  Burkholderia sp. lyk4-R2A-23
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Burkholderia sp. lyk4-R2A-23"
                     /db_xref="taxon:3040284"
     Protein         1..199
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=21009
     Region          <2..196
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mpgtaragta iawpatlaak rggplhaghl rfrkqagapr alhcfvldcs asmlsherla
       61 lakglivayf dqaardrvet alicfggnga aqrfgpavpr wwnarwlepv dggggtplad
      121 giaaaaqlla raacrtpdqq rwlwvlsdgr tretppkpaa adhvvfvdfd daavrigqgr
      181 rladawgaqw ttaaslcpg
//
LOCUS       WP_284891550             352 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Actinotignum sanguinis].
ACCESSION   WP_284891550
VERSION     WP_284891550.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum sanguinis
  ORGANISM  Actinotignum sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Actinotignum sanguinis"
                     /db_xref="taxon:1445614"
     Protein         1..352
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36525
     Region          40..344
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtlsaksads atstiarrrt aafavlvitt iallgamvva mgmgqlsisa pdvvrilfss
       61 pddvdrsalv ainqiraprv vlavvlggcl avsgavlqsl frnplvspdi vgvssaaafg
      121 gvlailvgts sfilmgstfi fglsavvcvm ligrirshsa tltivlagvv vsaffnamvs
      181 lmtyvadpys klpsitfwlm gslaaaswak vttiiipvii glivvvalrw rinvlslgde
      241 daralginps tmrwvcifav alltaasvaa agiigwvglv iphlvrllvg hdnrvvipes
      301 flmggmylli idtiarnats veipvgilta tigapvfigl lirrarkgra la
//
LOCUS       WP_284891787             289 aa            linear   BCT 25-DEC-2024
DEFINITION  urea carboxylase-associated family protein [Cobetia amphilecti].
ACCESSION   WP_284891787
VERSION     WP_284891787.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10558624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..289
                     /product="urea carboxylase-associated family protein"
                     /calculated_mol_wt=32419
     Region          41..214
                     /region_name="DUF1989"
                     /note="Domain of unknown function (DUF1989); pfam09347"
                     /db_xref="CDD:430546"
ORIGIN      
        1 msdvpaayqa skgsildvdr dfydsltegk aertlvatht vplrdglawe vpaghvlrik
       61 itegsqvgdf nmwnlqnpre rmwasrtrql qrahvstydr lwstlpylrp matiiddtla
      121 dygvdaeggr vhdllgtrcd pyvnrlltge dfdhhchsnl vravepwglt efdihdvlni
      181 fqctglnned kyfmkacpar kgdyleffae tdllcamscc pggdlsvdlw gpdardplet
      241 cnplgveiyr legdvlagwe spkvaayagn hgrqhpttdw atikrercc
//
LOCUS       WP_284891684             835 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: heavy metal translocating P-type ATPase
            [Actinomycetaceae].
ACCESSION   WP_284891684
VERSION     WP_284891684.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetaceae
  ORGANISM  Actinomycetaceae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 835)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 835)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Actinomycetaceae"
                     /db_xref="taxon:2049"
     Protein         1..835
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=85432
     Region          33..833
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mseppqaaaa pssptaqnta staaenlatt pvaevnlais gmtcascvar vekklnklpg
       61 vratvnlatd eahldlseag aqldttdfla qvsaagyear lisrteltpr avrsedanas
      121 artrdtdpsa aahpttahpn tsaesaraas evreaaeart sariaalrrr fwislalsip
      181 vvglsmipal qfpywqwvig altlpialwc gwpfhrsaaa alrhgsttmd tlislgtlas
      241 lgwstwallw ggaggadyrm smtgihalat gaahgshvyf etaamivtfl llgrwletrs
      301 rrsagdalrs llalgaddar rvrtasgadv deiipasela vgdeflvapg tkiatdgvvv
      361 sgttavdasl ltgestpidv gpgdevtgat lttagairvr atrvgrdttl aqmgrlltra
      421 qsgkapaqal adrvsavfvp avilialvtf gvrlalgnpl dlaimtaitv lvvacpcalg
      481 latptalmvg sgrasqrgil ihgpetlesa hsvdtiildk tgtlttgtma vdrvvlppag
      541 aggrgavatr tealalaasv enysehplar aivagaraeg lelrpatdfe nlagqgvrat
      601 iggqryyaas pralreagvd vadwestlee aassgaslvm larcdaargs ealalitvrd
      661 qlrptsaaav aelknlgltp ilasgdnaat travaraagi dtvhaevlpa dkvrvveaar
      721 aagarvamvg dgvndaaala aadlsiamgs gtdvakaasd itivnsdlrn vgaalrisaa
      781 tlrvirqnla wafgynliai paavagiilp glaaaamaas svivvlnslr lrrae
//
LOCUS       WP_284891901             434 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Cobetia amphilecti].
ACCESSION   WP_284891901
VERSION     WP_284891901.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..434
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47640
     Region          29..402
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtnssklgis lwsqtaiert eypalhdhhq advtiigagf tglragfelv sqgtnvmild
       61 sqepgfgasg rtggqvnpma hetpdqmrsk lgdvfgtrls qayinsadel fsviksnnld
      121 cepvqkgwir aahcrkaeks lhsmqqgwar egldiemidt eellrlsgsn syrigtltks
      181 agcihplsyc rsmakkissm ggkihgntrv tsvvpegnkw rvnfhdgsvl sdwvlfctng
      241 ytdnvlagln ktfiplvslq aatkplsneq ykkilpeght iadtrrviyy srrdnrnril
      301 lgslgrtpec slasdkrrli tafktvypsi sendieyfwg grvaftpdll phlhepapgi
      361 laglgfngrg vamgstmgrv maqrvlgkas kdldipttdl pryrfsdaks laiglvipyl
      421 etrdrwdiki sgva
//
LOCUS       WP_284891978             451 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Cobetia amphilecti].
ACCESSION   WP_284891978
VERSION     WP_284891978.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..451
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=48841
     Region          159..420
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mpsfasaars dssgvapyfs pmisravscs vflfgllslv mpsgyslgpa llvlisgycl
       61 lreprpllga ahkedlavig vvaglaalll vsillqgdaw qttsvpirll lavpvlllvl
      121 syppslgamw gglilgsvlt gswamwqklv wgvhraggft ntinfgdicm lmglmclagl
      181 gwamsqagar rrywllalli ggafgiigsl msgtrggwig fpfaawvlyr sygevisrrv
      241 lrlsvfmcag vialmvmtpa tgiqqrveag vsdvtkyved rnagtsagar lemwrgallm
      301 iaeqpwlgrg etgyaeards mieqgelsrh vhpyehphne fldawvkrgv lgllallaly
      361 lvplrlfyrr ldsddltlrs lavagvllpl tfldfgmtwv mfsqasgvmv yaywlaivwg
      421 tlraherrle aashaacdka qakhvcmecq t
//
LOCUS       WP_284891905             224 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Cobetia amphilecti].
ACCESSION   WP_284891905
VERSION     WP_284891905.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..224
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24864
     Region          5..209
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 maelcllfds dgtlvdseil laeamsstlp ryglpftsdr ymnefrgmrf msivrtleat
       61 hgvleeaptr rmegemrall eelmkarlta mpgmsaalme legypcgvvs ngperkvrla
      121 ldttrlarff dghiysaytl gvwkpdpriy rlaaeqmgfs pshcvvidda ivgvqaglda
      181 gmqvihfahh ddghetprga lrmhharelp rlvaqisqkl aaqy
//
LOCUS       WP_284891981             340 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Cobetia amphilecti].
ACCESSION   WP_284891981
VERSION     WP_284891981.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..340
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=39608
     Region          5..323
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mneervyild virmlaalsv alyhytwfga ddierinfgf iseifaygel avqlffmisg
       61 fviawsvynk safgflrsrv lrlyptywic llatcmvlff nqsldlnvaf fnltmfqqfv
      121 gvahidgsyw tltnevifyv ymcliiklgl tsklmeifsi hiflcvvywv yrifmhhepp
      181 ivgtlflley ghlfiaghvl yrmffsdldn sillcrtill vsfvlaniev shdsqninkt
      241 viscsiislf flffifmnrf slsrfnkfki keisitiggv sypfyllhqe igyqlfnatn
      301 swlnlivcis siiflsyiin kllgfvlrrk dsslesfvrn
//
LOCUS       WP_284892060             418 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Cobetia amphilecti].
ACCESSION   WP_284892060
VERSION     WP_284892060.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..418
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45513
     Region          5..417
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 msdsehteva vigagavgva calwlrrsgh evtmieregi asgtsfgnas tladygclpi
       61 arpeiwrsmp slllspdspf vidwkclprl spwlmrfmgq cnatrfrans emlaqllsht
      121 ytdyqplldd apaaaamiqr kgclyaygka enlqaaqgdi rlrdqlgihq qvltadelia
      181 lepameghta ggvlfpssch lddpqvfidt latplreegr ivsaevtrls rqasgmlley
      241 adgrrlmadr vvlaagawsa hlarqigdri pldtergyhi efdlehspln rptcpvesaf
      301 ymtplhspeg vrlrvagtve lsslagpanp arfdylesrv rkvlgidapv arrwlgfrpt
      361 lpdsvpvigp spneprviha fghqhigvtl agvtgrlvse clakgspewi mpcsparf
//
LOCUS       WP_284892117             405 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Cobetia amphilecti].
ACCESSION   WP_284892117
VERSION     WP_284892117.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469162
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..405
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=45440
     Region          22..141
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
ORIGIN      
        1 matpsdwfap ahatwsagqr hkalqqlidh fnqrprprea glfkqisyyl flladyrsas
       61 qilaqghvec padeeialnq vvclsranda agslaageal aargclnpvl fdslassaar
      121 lkrhdeareh gsralalkde qhgslalakg wrlpaespsa vaagktrvls fglwgkgpry
      181 lngmlhnlll apvlypgwrv rlyhddsvpd dflalareld aelierpssd tlrqrlcwrf
      241 avaddptvgy fvvrdcdsvi slrevravqm wltsgrffhv mrdwwshtdl vlaglwggva
      301 gvlppletll aqwqpqhvet pnidqwfmke cvwrylresl vshdrcyslq ikgrdslkfp
      361 ddvlgeapgg tahvgsdewt rdrafqlrql gpwlkeaswm rdsdd
//
LOCUS       WP_284892138             252 aa            linear   BCT 25-DEC-2024
DEFINITION  HesA/MoeB/ThiF family protein [Cobetia amphilecti].
ACCESSION   WP_284892138
VERSION     WP_284892138.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..252
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26230
     Region          3..248
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mqdsqllrys rqillpqvdi agqqrllaar vlvigagglg cpaalylaaa gigtlvvadd
       61 dhvelsnlqr qiahgdadid qpkaqslaas llainpdtev ialserlege alaeqvaaad
      121 vvldctdrfs srfpinaacv tagtplvsga airfsgqlav fdrrdpeapc ygclypldel
      181 gdeeltcaes gviaplvgii gafqalealk lisgagsvhr glatfdgltg ewrrmglkrd
      241 pgcqvcggre pa
//
LOCUS       WP_284892188             645 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Cobetia amphilecti].
ACCESSION   WP_284892188
VERSION     WP_284892188.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 645)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 645)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 645)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 645)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 645)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..645
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=69422
     Region          3..498
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mtepalaltl iglmalgcqw lawrmrlpai lpllivgila gpvtgwlkpd ellgdllfpl
       61 vslavavilf egsltldfkd lrghghivrr lvttgvvitg vigtvaahyl ldmrwemaav
      121 lgallvvtgp tvvmpllqtl rargnltqil rwegimidpv gallavlvye yvalgmtgna
      181 ashtlllfaq tvglglgmga lggwcwglvl rhfwlpqklh nfgtlmvmlg lfaisntlfh
      241 esglltvtvm gvwlanmrgv ptqqiiefke tltvllisgl flllagrltv eqlsllswpa
      301 wiflavlmwv arpltvwlct lgsgltlrek allawlsprg ivaaavaslf alklesqgie
      361 gaemlvpmtf lviigtvvvq sllsrpivkv lgvgepppsg flilgansvs rqvarelvda
      421 gfsvrltdtn wdavqearma glpvyygnpl sehaaqhlel tgighlmpls pyrelnslaa
      481 lhfehilghg rvfrlaedng knakrqqdqa lghlpllfdg kityaklasl lsqgaqfrra
      541 ritesfsled yrriheerll plfcissqgr iriantaval epkagetlis lihadspeln
      601 kssqprtdka eapqadkgag gkssqtppgs gsgplpasrl pgagt
//
LOCUS       WP_284892570             208 aa            linear   BCT 25-DEC-2024
DEFINITION  IMPACT family protein [Cobetia amphilecti].
ACCESSION   WP_284892570
VERSION     WP_284892570.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Park,F., Gajiwala,K., Eroshkina,G., Furlong,E., He,D.,
            Batiyenko,Y., Romero,R., Christopher,J., Badger,J., Hendle,J.,
            Lin,J., Peat,T. and Buchanan,S.
  TITLE     Crystal structure of YIGZ, a conserved hypothetical protein from
            Escherichia coli k12 with a novel fold
  JOURNAL   Proteins 55 (3), 775-777 (2004)
   PUBMED   15103642
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Okamura,K., Hagiwara-Takeuchi,Y., Li,T., Vu,T.H., Hirai,M.,
            Hattori,M., Sakaki,Y., Hoffman,A.R. and Ito,T.
  TITLE     Comparative genome analysis of the mouse imprinted gene impact and
            its nonimprinted human homolog IMPACT: toward the structural basis
            for species-specific imprinting
  JOURNAL   Genome Res 10 (12), 1878-1889 (2000)
   PUBMED   11116084
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..208
                     /product="IMPACT family protein"
                     /calculated_mol_wt=22094
     Region          1..204
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 mtylipalap eahhehsiei eksrfiawla haptpegmtr llaqahlahp narhhctafi
       61 agapneqnai gfsddgepgg tagrpmyqvl egsgvgqvac vviryfggik lgtgglaray
      121 sravlealeh lpttaftprt prrlkvgfah eadvrhwlsg ydvpvdasdy gadgvvltag
      181 wpqggaqppl eelharlkga levldscd
//
LOCUS       WP_284892612             562 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein [Cobetia
            amphilecti].
ACCESSION   WP_284892612
VERSION     WP_284892612.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 562)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..562
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=61064
     Region          52..520
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mhnlqdsaat ygaaagssvs daqtdacars lssspraalf spanmdawqt gmdrisqlva
       61 eqldsvqkpf sgitpealrp afadldletp lenleaglee lkslylkdav yfhhpryiah
      121 lncpvvlpgv waesllgain ssldtwdqsa ggtlieqrli dwtterlglg ptadgiftsg
      181 gtqsnlmall lardavcekl pnhpgnqthg lppeagrlrv fasgishfsl qkacallglg
      241 hnavipvavd errrmdpval rdaldnarae glipmavvat agttdfgsid plqaigrech
      301 argiwfhvdg ayggglitsr rhghwlkgte madsvtidyh ktffqpvscs acvvrdrtql
      361 rhvtyhadyl npelqaregt pdqvnkslqt trrfdalklw mtlrlmgada lgdmldcvid
      421 ltregyqlle aapdidvvqa pelstlvfrf hdaseetlsa eqwdalnrei rkrlsrsgea
      481 ivaatkvsgr qylkftllnp etrqedlaav velirqhgqa lvkahhlavs ttaqpnhgap
      541 ladipaasrr shtteakesr ha
//
LOCUS       WP_284892830             298 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD-IIB family hydrolase [Cobetia amphilecti].
ACCESSION   WP_284892830
VERSION     WP_284892830.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467317
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..298
                     /product="HAD-IIB family hydrolase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32213
     Region          5..284
                     /region_name="YedP"
                     /note="Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP,
                     HAD superfamily [Carbohydrate transport and metabolism];
                     COG3769"
                     /db_xref="CDD:442983"
ORIGIN      
        1 msetqaplll ltdldgslld hhdyspgpar swltrlrarg awivpntskt aaelaplmds
       61 lglagqpwia enggvvalpa dwlsayplee asapdahglc riavamprdr ilavleelsg
      121 efafegfasm svariseltg lgegdaalag qrdaseplvw rdaperledf rmrlaghglk
      181 ltrggrfhhv tgdsdkgvaa ryliaryrlc ervrpwtlgf gdgandlpll aavdnavlip
      241 gvgdtsqrdr eladypllad errcfranlp gpqgwveglr hwlangqpee wtsrglga
//
LOCUS       WP_284892849             487 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Cobetia amphilecti].
ACCESSION   WP_284892849
VERSION     WP_284892849.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..487
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=54078
     Region          71..447
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 metivqhgar psdmgneseq rpatqasrpy dpaydplvsa tpgegrdyap tywvatagep
       61 paddgpvmgd idadvvivgs gftgltaaiv laekygikat vleanrvswg cstrnggqaq
      121 catgrlkrsq wierygleaa hglhrecveg menfkelikd idcdpqpggh lyiahrermm
      181 pglekearll retfnydari idgatvrnew vgdeeacgam hepegigvhp gklafgylrk
      241 arrlgvkvhp aspveswetr dgvhylttpg gvvkarsvgm atggytsgkl hpeldkrlmp
      301 vlsnslvtrp ltaqeieatr fhthqvltdt rvlrhyyrll pdnrlqigsr savsgrdapk
      361 ahyeqlliad mhrkfpalsg ievdyswwgw vdvshdmmpr ihqpdpkqsi yyamgyggng
      421 vmysaqagkr laqwiardaa dlvlpifqsr lpypnvlnkv esplfapfrr tgqrclyrwy
      481 amkdeaq
//
LOCUS       WP_284892882             575 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Cobetia amphilecti].
ACCESSION   WP_284892882
VERSION     WP_284892882.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 575)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..575
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=63947
     Region          <152..570
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mpldilikll ssieeplwih drfgqlawts prarqedrvp elpsplpkqp epcgisgqpg
       61 fwlmgitgel gewllvqkan lpwrmaifda eclvantcgw qelfgterpr lepvserrvr
      121 lkapfsglae araagvddkv lialrrlqpi nllsrdrfna qidelllees vdgsigggii
      181 ylslthleii nsahgaerid pllervaeam slqyrdalvc rplgnafalf fvgdeaslia
      241 ranelcerlv mlmrldgkal pvtarvgisl apqharrahr lmhlaelaml hgeyddidvc
      301 gplhvfspga hmqhlndyrl tsdlrehlee ldlafqpqfd lasgeavgve vlvrwdhpel
      361 gtigpgrfip laeqygligt vgarvmdtal satrdlvtpn gkplsvainv saqefrdpgf
      421 pervsealar hdfaperlel eitessrvpd ldrvverltg liergvrlai ddfgtgfasl
      481 lyvrdlracr lkvdqrfvgs ldhdardrai vshaislads lgmevlaegv etaeqerllv
      541 emgchlvqgf ryarpkrlpe lvewlkrkps ihpcp
//
LOCUS       WP_284892905             463 aa            linear   BCT 25-DEC-2024
DEFINITION  class II fumarate hydratase [Cobetia amphilecti].
ACCESSION   WP_284892905
VERSION     WP_284892905.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Woods,S.A., Schwartzbach,S.D. and Guest,J.R.
  TITLE     Two biochemically distinct classes of fumarase in Escherichia coli
  JOURNAL   Biochim Biophys Acta 954 (1), 14-26 (1988)
   PUBMED   3282546
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..463
                     /product="class II fumarate hydratase"
                     /EC_number="4.2.1.2"
                     /GO_component="GO:0045239 - tricarboxylic acid cycle
                     heteromeric enzyme complex [Evidence IEA]"
                     /GO_function="GO:0004333 - fumarate hydratase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006099 - tricarboxylic acid cycle
                     [Evidence IEA]"
                     /GO_process="GO:0006106 - fumarate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49452
     Region          2..458
                     /region_name="FumC"
                     /note="Fumarate hydratase class II [Energy production and
                     conversion]; COG0114"
                     /db_xref="CDD:439884"
ORIGIN      
        1 mssqtrrerd smgelevpas alygaqtqra vdnfpvsgqp lpaafirava riklaaaevn
       61 rdlellddvr aeaiikaarq iidgehadqf pvdvfqtgsg tstnmnvnev ltqlanqhlg
      121 dkdvtvgand hvnmgqssnd viptaihlsa viavsdtllp alrhlhevis rkasevddvv
      181 ktgrthlmda mpirmsqelg awqaqvgqai erieqvlprl erlaqggtav gsginahpef
      241 aeriadrlsh qtghafrpae sffaalssqd tavelsghlr tyavammkis ndlrwmnsgp
      301 laglgeiele alqpgssimp gkvnpvipea aaqvaaqvmg ndatigiagq sgnfqlnvml
      361 pliannllss itlsanvsrl ladkaiatfn vrqynieapl aknpilvtal npvigyneaa
      421 rvakvayqag rpildvaeee telsreeler lldpakltag giq
//
LOCUS       WP_284892925             423 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Cobetia amphilecti].
ACCESSION   WP_284892925
VERSION     WP_284892925.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..423
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45043
     Region          2..>406
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mlnlaalfit itavcmwfnh rvlrlpptig vmaiglvlsl gvigldhfav ttvvadtaed
       61 wlgrinfnsl lmdgmlsfll fagalhvdls rlkayrrsig llatlgvlis tlvigsaaww
      121 lfqwagievp ylyclvfgal isptdpiavl gimrsagapa dmeirivges lfndgvavvl
      181 ftallsaasa gsgevelghm gllfleeagg gillglalga lvyqlmhsid qyqvevmlsl
      241 alvlggyala salhvsgpia mvvagliign mardgamsdn trryldgfwe lvdeilnavl
      301 fvliglelvl mpitltsigi alvlvavill srlaliglpl sllrrwytfr pgttrvltwg
      361 glrggisval alaipegdfr eplvvttyii vlfsilvqgl sigklvtavv gdrchpeeph
      421 dkh
//
LOCUS       WP_284892947             192 aa            linear   BCT 25-DEC-2024
DEFINITION  chorismate--pyruvate lyase family protein [Cobetia amphilecti].
ACCESSION   WP_284892947
VERSION     WP_284892947.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Meganathan,R.
  TITLE     Ubiquinone biosynthesis in microorganisms
  JOURNAL   FEMS Microbiol Lett 203 (2), 131-139 (2001)
   PUBMED   11583838
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Siebert,M., Severin,K. and Heide,L.
  TITLE     Formation of 4-hydroxybenzoate in Escherichia coli:
            characterization of the ubiC gene and its encoded enzyme chorismate
            pyruvate-lyase
  JOURNAL   Microbiology (Reading) 140 (Pt 4), 897-904 (1994)
   PUBMED   8012607
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Nichols,B.P. and Green,J.M.
  TITLE     Cloning and sequencing of Escherichia coli ubiC and purification of
            chorismate lyase
  JOURNAL   J Bacteriol 174 (16), 5309-5316 (1992)
   PUBMED   1644758
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..192
                     /product="chorismate--pyruvate lyase family protein"
                     /EC_number="4.1.3.40"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0008813 - chorismate lyase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006744 - ubiquinone biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21328
     Region          1..184
                     /region_name="UbiC"
                     /note="4-hydroxybenzoate synthetase (chorismate-pyruvate
                     lyase) [Coenzyme transport and metabolism]; COG3161"
                     /db_xref="CDD:442395"
ORIGIN      
        1 mpaasaavrr hwqpaaalqg vmpagwwawl sstdsltqrl asamqqqdec dgqpiqglrv
       61 rlllqdtgpa rldearllgi gprrhvwrre valchgdtpw viarslaald lahghrlstl
      121 gerslghwlf rqpdltrsai dvsraplvls sprplartts lwmrrsmfsh grfnvlvqeg
      181 ftpafqhalq lt
//
LOCUS       WP_284893142             391 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Actinotignum timonense].
ACCESSION   WP_284893142
VERSION     WP_284893142.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum timonense
  ORGANISM  Actinotignum timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Actinotignum timonense"
                     /db_xref="taxon:1870995"
     Protein         1..391
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39287
     Region          <8..47
                     /region_name="PHA02030"
                     /note="hypothetical protein"
                     /db_xref="CDD:222843"
     Region          74..384
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msgqrgnqgh aatalsavpg apampaepgt pgapgasamp alpavpagik arrhrrfwtf
       61 liltvllalg mllsahlgqf pvtvgdvgrg iaarfglaap pedplvmaal wnirfpricl
      121 gvlvggalav agavmqavfs nplaepgiig vssgcafgaa ltmvfvpgal ggfsvplgaf
      181 aaglvtsatv yllarshgra etltlvltgi avtavasalt siatyladtn areqivfwqm
      241 gslagaswfq vavvgavvgi gilgalalag rldllslger eaghvgvnva alrasaivlt
      301 ailtaaavcf agvigfvgli vphvlrllmg pmnrmlipaa llggavllty adlaartlvp
      361 faelpngift alvggptffi llrknlrgar g
//
LOCUS       WP_284893380             113 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Actinotignum
            timonense].
ACCESSION   WP_284893380
VERSION     WP_284893380.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum timonense
  ORGANISM  Actinotignum timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Actinotignum timonense"
                     /db_xref="taxon:1870995"
     Protein         <1..>113
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
     Region          <23..>113
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 tyssksrgek alaaglphtp dylsvktikn ihgllssilk yqvqmrtipa npafairlpr
       61 aarkryptfl tanefaaiyd atpadwrpll allagtgmrw seatalkgsd fdl
//
LOCUS       WP_284893386             510 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sigma-54 interaction domain-containing protein
            [Burkholderia].
ACCESSION   WP_284893386
VERSION     WP_284893386.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..510
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=55042
     Region          45..494
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mmndwarlpv nygdvlrraa eslfrtfeds sagtvvvdrd arvvwmnery aarfgfadpq
       61 qavgldceav ipnslmrevv stgqpilldi metgreplvv trlplknevg etvgaigfal
      121 fdqlktltpi fsryaqlqqq liatqrslaq arrakytfas fvgtsaasle tkrqarraaq
      181 vdspvlllge tgtgkellah aihaasaral qplvtvnvaa ipdtlletef fgaapgaytg
      241 adrkgrvgkf eladrgtlfl deigdmplpl qgkllrvlqd kefeplgsnr ivradvriia
      301 atsadlpalv eagrfradly yrlnvltiha pplrerasdi aalvyatlee laaqhgraah
      361 celtddalrv lcaypwpgnv relrntlera lmlsdrsvid aralapflgp mrvapdsvpa
      421 garvapspag rdagdasagp gapvvsytda laawerqfli dalaacdgkv veaaarigig
      481 ratlykklaa lgidrwpaaa dargheerhr
//
LOCUS       WP_284893525             437 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [Burkholderia].
ACCESSION   WP_284893525
VERSION     WP_284893525.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..437
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46233
     Region          6..404
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mndrqpasal pyegvrviem thmvmgptcg mlladlgaev ikiepiagds tralrgsgag
       61 ffgmfnrnkk slavdvkdpr gleivrrlva tadvfsenfk sgtmdrlglg haalsslnpr
      121 lvyvshkgfl pgpyehrtal devvqmmggl aymtgpegrp lragssvndi mggmfgaiga
      181 maalaqrert grgqqvqssl fennvflvaq hmmqfavtgq aaspmpsris awavydvfsv
      241 rdgeqiflav vsdtqwalfc dafglaalkd darlatnnlr vqarewllpe lrarlaahsa
      301 aeigaifesi glpyapitkp qdlfddphll atggleavtl padassagrp vdtrtallpl
      361 tlagerlrlr sappalgqdt cvllgelgyt pdearalida gvvagrhghg anglppdvps
      421 gpsvpsdmrs pneaasa
//
LOCUS       WP_284893560             285 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Cobetia amphilecti].
ACCESSION   WP_284893560
VERSION     WP_284893560.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..285
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31145
     Region          <68..>104
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
     Region          153..280
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mdaialgpal isverlyafv aalvmliefs llirllarmh argttapahd spplspsrwf
       61 nrmlvswvig arlthvalhw asyqqapldi lklwqpgyhl lggmlaaala slwllrrhga
      121 irqvialgsl tlgltaflgl kqldplgnds aieampaitl nhldrrpval ndirderviv
      181 nlwatwcppc rrempllaea dqrpgvtvvl anqgeqalav trflqseqlt leyalldpam
      241 qlmalaeaqg lpatlvfdgd gqlierhige lsraqldall pasrp
//
LOCUS       WP_284893617             365 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease [Burkholderia].
ACCESSION   WP_284893617
VERSION     WP_284893617.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 365)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..365
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36338
     Region          50..360
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mpvhaspfpa rsptsptsrs gaarvgtsrr fapfalaala clvcamsvva lcvgayripl
       61 aeawaaltgd aaaqqaravl fdiraprvvl allvgggfga agaamqalfr npladpglvg
      121 vssgaalgat ttivlgpalf aahasatvlp vaafagalav aalvyrlaas rgrlalplll
      181 lagiainalv gaaiglltfv addaqlrslt fwslgslgga qwsalaavtp cvaigcvlla
      241 rerdalnalq lgetealhlg vpvqrlkrrv lvavalavga lvscagiigf iglvaphcvr
      301 lacgpdqrvv lpgaallgal ltlaadlaar tiaapaeipl gvltallgap fflvllwknr
      361 galgg
//
LOCUS       WP_284893629             239 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Cobetia
            amphilecti].
ACCESSION   WP_284893629
VERSION     WP_284893629.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..239
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25981
     Region          17..220
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 malllsavvl vplaaclplq aryrvlhsyn hivlwwfrlt cgvkvqvtgr dalpegacvl
       61 lanhqsewet iylqvakrpl ctvlkqellk ipvfgwglkl lepipldrtq pakalkqvls
      121 vgtqrlkdgf tvlifpegtr iapgtrkkfn ksgaaiacra gvpvvpvahn ageiwpndsw
      181 ikrpgtihva ygpaietagr kpdaviadve awvenklqei ssvqrpplee eaaadsvga
//
LOCUS       WP_284893690             521 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Cobetia amphilecti].
ACCESSION   WP_284893690
VERSION     WP_284893690.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..521
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=56755
     Region          21..477
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mtahapstpr etrrsgsdpl ptasvlivdd epgmrrylek alssrfalie caesveqaea
       61 lrsrlhfdli lldirlpgrd gldwdealap ssvsdvifmt ayadletavr alragacdfi
      121 ikpfrleqlq aaldrclerr qltrenfllr rdnarhqqee aslkgespam qelahiiarv
      181 apapspvlil gesgtgkela ardlhrlsgr rgafvpvncg aispellese lfghlkgaft
      241 gahrgrdglf sfadggtlfl deigemplam qakllrvlet rrvrpvggeq eqavdvriva
      301 athrtletev aagrfredly yrlnvlsltl palrerpedi palaqhfsrq lsrelnlpav
      361 pwqhsdltrl chyswpgnvr elknvieral llgrlpgdtl pvdsqaaqas ghpawddsgd
      421 attsieeeav ssgyplewsl davekahlca vlerhannks aaarqlgisr ktldrklttw
      481 raeqqiggdg gaengtesga esdqpapats saapcgadgs a
//
LOCUS       WP_284893712             195 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Cobetia amphilecti].
ACCESSION   WP_284893712
VERSION     WP_284893712.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..195
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21471
     Region          2..167
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          88..181
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtpilrpair adldalvele evsfdsdwfs rrqlshlilr ahartlviiq pdddviptap
       61 avddvmaalw pagsverdda tplrsvlgyg tvlfrrnsrr arlysfclhp esrgrglaqr
      121 mltsleqlai aqgctqfdle vhtgngaaia lyerhgfekc grlrdyyadg aaawkmrkal
      181 tldspapvae elaag
//
LOCUS       WP_284893743             513 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Cobetia
            amphilecti].
ACCESSION   WP_284893743
VERSION     WP_284893743.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..513
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=53693
     Region          59..499
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 msrfrslapw aaamaalmaa ssaraegmdq aisdivgpiv npivstifys vpvagtqfpl
       61 ivgwliiaai iftlyfgfvq frlfghairl vkgdytdpkd egevshfqal atalsgtvgl
      121 gniagvavav slggpgatfw milagllgma skfcectlgv kyrnvnadgs isggpmyyls
      181 kgfaengkag lgkilaiffa icaiggsigg gnmfqanqsy qqavnvtggd asflvgygwl
      241 fglvmaaivg mviiggiksi arvteklvpm maviyviaal iilgfnfsai paafgaiieg
      301 afapvavggg ivgvliqgfk raafsneagi gsaaiahsav ktsqpategi vallepfidt
      361 vvictmtalv ivitgayqve glggvqltsy afetafpwfp yvlalavlmf afstmlswsy
      421 yglkawtylf geskgseivy kliflafvvi gssmslgpvi dfsdamifam sianiiglyy
      481 lmpvvkrela qymaklksge iapvdkeakr qna
//
LOCUS       WP_284893756             601 aa            linear   BCT 25-DEC-2024
DEFINITION  single-stranded-DNA-specific exonuclease RecJ [Cobetia amphilecti].
ACCESSION   WP_284893756
VERSION     WP_284893756.1
KEYWORDS    RefSeq.
SOURCE      Cobetia amphilecti
  ORGANISM  Cobetia amphilecti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Cobetia.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Cheng,K., Xu,H., Chen,X., Wang,L., Tian,B., Zhao,Y. and Hua,Y.
  TITLE     Structural basis for DNA 5 -end resection by RecJ
  JOURNAL   Elife 5, e14294 (2016)
   PUBMED   27058167
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Lovett,S.T. and Kolodner,R.D.
  TITLE     Identification and purification of a single-stranded-DNA-specific
            exonuclease encoded by the recJ gene of Escherichia coli
  JOURNAL   Proc Natl Acad Sci U S A 86 (8), 2627-2631 (1989)
   PUBMED   2649886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Cobetia amphilecti"
                     /db_xref="taxon:1055104"
     Protein         1..601
                     /product="single-stranded-DNA-specific exonuclease RecJ"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=65171
     Region          32..581
                     /region_name="RecJ"
                     /note="ssDNA-specific exonuclease RecJ, DHH superfamily,
                     may be involved in archaeal DNA replication intiation
                     [Replication, recombination and repair]; COG0608"
                     /db_xref="CDD:440373"
ORIGIN      
        1 msrpdertla asiarviqpr vrderlyqqg iatglselqa rvlagrltle sckaplealv
       61 tpalrhiehp erladgrraa eriaravaeg ehigiltdyd vdgitshvvm lrtltelfdv
      121 pyyrvhslig hrihdgygis lplverimtl sprpslivta dcgssdearl allkeagiev
      181 vvtdhhalpq egppasayat vnptrddcay pdatiagcmv awltmsltrn vlieqgmlps
      241 dapklspwls yvalgtvadc vslggsainr avvnlgltli nrmqepcwra maerlgadsv
      301 pfnaetlafq mgprinarsr lddpyaalhf mlareddaaq ralevldqdn qsrkaieaem
      361 vesaralalt slreghqviv vhledghpgv qgivasrlvq qfgrptvvlt paavpgmltg
      421 sgrsieglhl rdalqrahdl apqclprfgg hrgaagvglp ltekdtftra lqqaaaeqlg
      481 eralnplils dgelvegqls letldelerl apfgrefeap lfegsflves lrpvgadgth
      541 lslelslgrt rlkaiwfral spgespafgv gaslkcaykl srnrwrgres lqlmlehavp
      601 a
//
LOCUS       WP_284893841             496 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: flavin-containing monooxygenase [Burkholderia].
ACCESSION   WP_284893841
VERSION     WP_284893841.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..496
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=56073
     Region          10..461
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mtekqtaacs pehvdvliig agisgidaac hlrmnlpgrs faileamdgf ggtwwthryp
       61 garsdsdlyt yafgfrpwqg rsiataeeih sylgevidey dlgskihygh rvqtvnwsse
      121 qkrwivevsr ndsgerftmt tgflwlgagy ydhrqgftpk wngfdrfkgt vvhpqhwped
      181 ldyagkrviv igsgataatl vpalagtaah vtmlqrsptf ftavpwthql datlrelslp
      241 eewrseilrr ahlkqtfdli nlstanpdav rdwlinetrq qlpegfdvdk hfnpsyrpwq
      301 qrvaavpdgd lfaairdgka svvtdtieaf desgitlasg ehldadivvt atgfdmsafg
      361 qiafqldgap vdmskrvsyr gmmiegipnm afvygyyrss wtlradlvce ftcrvlahmd
      421 kvgaktvepr lrdedadmqr lpwtdpnnfn agyvmrsqhq mhmrgdrmpw qhhfefeeer
      481 ktipelspda evlvyr
//
LOCUS       WP_284893827             372 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase family protein [Burkholderia].
ACCESSION   WP_284893827
VERSION     WP_284893827.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..372
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40591
     Region          1..357
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mrevryvkgl dglraiavil vflshkghvl avdvgklgvw tfffisgfli vgelhrnrqa
       61 iecgtmtrrh alalflakra lrifpvyyll laalaiahal fyqrgvnlgl awhaaflsny
      121 wigivkdgwp gstshfwsla veqqfyliap ltllavpaar hvalgvaava lcalahlaly
      181 aldaspvliy afspwnfali alggvggmal adrgptvvrr ippgwlgavg vvffltlpaf
      241 talpdivsgl vdlglsvslg almlwivtep dhpavalldr aplvylgtis ygfylfhnli
      301 parfgempal fahvpmpgiv realpellqf alavllahls wrylerrlld fkkpiaamla
      361 rhfvarpsts pr
//
LOCUS       WP_284893844             322 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: WD40/YVTN/BNR-like repeat-containing protein
            [Burkholderia].
ACCESSION   WP_284893844
VERSION     WP_284893844.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Rengstl,B., Oster,U., Stengel,A. and Nickelsen,J.
  TITLE     An intermediate membrane subfraction in cyanobacteria is involved
            in an assembly network for Photosystem II biogenesis
  JOURNAL   J Biol Chem 286 (24), 21944-21951 (2011)
   PUBMED   21531723
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Komenda,J., Nickelsen,J., Tichy,M., Prasil,O., Eichacker,L.A. and
            Nixon,P.J.
  TITLE     The cyanobacterial homologue of HCF136/YCF48 is a component of an
            early photosystem II assembly complex and is important for both the
            efficient assembly and repair of photosystem II in Synechocystis
            sp. PCC 6803
  JOURNAL   J Biol Chem 283 (33), 22390-22399 (2008)
   PUBMED   18550538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..322
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=33799
     Region          54..208
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          137..287
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
ORIGIN      
        1 mnhkmraisa aivvgatllg gmqcavsape lkpvpavqss iatqsavlda twagqrvvsv
       61 gangiillsd nrgatyrqak avpvsstlts vsfidantgw avghwgailk ttdggetwqi
      121 qrfattedrp lfgvhfvdan hgvavglwsl ilvtddggkt wtkkepvlpn gkksdlnlfg
      181 ifsngngdif ataekghllv skdkgntwet ietgykgsfw cgvalpdgvl lvgglrgtlm
      241 rsddnghtws ratldtrnsi taltssgstv lavgvdglqa qsaddgktfk rmhtdtgtty
      301 taalpspgdk wlvfsrdgai sr
//
LOCUS       WP_284893865             318 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: TauD/TfdA dioxygenase family protein [Burkholderia].
ACCESSION   WP_284893865
VERSION     WP_284893865.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..318
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34918
     Region          26..299
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 msdvqhaahp sshashaaap htagvplqlr qvagrigaei agvrlsstld datfdaiqaa
       61 llrhkvlffr nqdhlddtaq eafarrfget vahptvppvd gsahllelds ahgaranswh
      121 tdvtfvdayp kvsilravvi ppfggdtvwa ntaaayahlp eplraladtl walhtnaydy
      181 asthvhaddt qlkryrevft stvyetehpv vrvhpetger tlvlghfvqk ikglssqdsa
      241 hllqvlhehv trlentvrwr wqqgdvaiwd nratqhyaid dygdarrvvr ratvhgdvpv
      301 gidgrrsvvl kgpgatlq
//
LOCUS       WP_284893920             383 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase family protein [Burkholderia].
ACCESSION   WP_284893920
VERSION     WP_284893920.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..383
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=43065
     Region          1..362
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mnhrvkqltg lravavtmvv vghaehvlpg gytgwlaplr liadgrlgvl iffvlsgfli
       61 tnvlraefar tggialtsfy vrralriwpa cyvylvivgi lavagwldvd rrqwlyaalh
      121 lwnysawfgl agdnalhpdg awylghfwsl aleeqfywfw pllfvygtrh rgtrwlavli
      181 lavplvrtlt yfvapalrgq lammlhtgvd piligcyaal nrerleawig swrgetrivt
      241 aivfivlfgm plaerrlggf wnatygvtie aaliaivivv lnfrsefwca rwlraapvvf
      301 vgtisfslyl wqqpfanpgl pvahafplgi vwallaatas yfliekpflr lkdrytarea
      361 rrvrddalrm paptdaigpk vve
//
LOCUS       WP_284893962             264 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: lysophospholipid acyltransferase family protein
            [Burkholderia].
ACCESSION   WP_284893962
VERSION     WP_284893962.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..264
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29276
     Region          52..257
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 miarldygwr lfatgmslaf faccgsvfsv laivvgalwp hrrsrqrcvt lvihyffrvl
       61 vallqrigvm klelsgverl akdgpaivva nhptwldvmv llsltpkacc vvkrghwgnp
      121 cfwgivraae yvsnadavgl veagarqlaa gytmivfpeg trspggnrlh afsrgfahma
      181 lqsrsriqpv lidcdppvft ktlqwyhvps rafrmridvl epmdlnrlas dvtspsiaar
      241 siarevevhi tqslfqygyf ktan
//
LOCUS       WP_284893981             389 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase family protein [Burkholderia].
ACCESSION   WP_284893981
VERSION     WP_284893981.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..389
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=42501
     Region          1..380
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mathkqkfei ldglrgiaai svmlmhflqd lpipilqsay lsvdvffmls gfiltysyge
       61 klrqaswrge yvkrrvirly pmicigltig fvslvvmrvn asaafsfgnl aaatgqnyfl
      121 ipylgrfsvs gfvgatnhgl pavddpgvfp lnppawslff elfasvvlia avkmteqnll
      181 rlayaclgaf vaygwlvgld hdkvtvilnq gwaadnffgg ffrvgygfll gvaiakmhda
      241 slparphwfv aglvrndwml fvafllvvlf ptsikgiyal avllfvapal vyrgamlaps
      301 gkvvaristf lgwisyplyc vhypigrlvf ayapqgdihv vrtamlaacl sivsaaflak
      361 fveepirsyl gkrlfgnqpa vtgspvnva
//
LOCUS       WP_284893967             225 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: LolA family protein [Burkholderia].
ACCESSION   WP_284893967
VERSION     WP_284893967.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Tajima,T., Yokota,N., Matsuyama,S. and Tokuda,H.
  TITLE     Genetic analyses of the in vivo function of LolA, a periplasmic
            chaperone involved in the outer membrane localization of
            Escherichia coli lipoproteins
  JOURNAL   FEBS Lett 439 (1-2), 51-54 (1998)
   PUBMED   9849875
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..225
                     /product="LolA family protein"
                     /calculated_mol_wt=23793
     Region          44..205
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mgltlrsrrf aatmlgacmm laggelaaap aptaatavar panaalvadv atrlarvgai
       61 radfrqtqtl samkqplvst gsmlfdrrsg vvwrietpyk atyvitdggm revgadgrlv
      121 apggggrgva qvsrmmrdml ggdlsalyaq fdveasgtpe rwrmvlrpnq pqlaqairvl
      181 emsggaylgk ldmtfangnv tvlefvrptp vdapapverg wlear
//
LOCUS       WP_284894092             383 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [Burkholderia].
ACCESSION   WP_284894092
VERSION     WP_284894092.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..383
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41290
     Region          3..377
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 metnarlpld gvrviefthm vmgptcgmil adlgaeviki eppggdktrt lpglgigffr
       61 tfnrnkksvv ldintpegkd aaveligtcd vmlenfrpgl mtklgldydt lskafprlvy
      121 vshkgflpgp yekrlaldev vqmmgglsym tgpvgrplra gtsvndimgg mfgaigvlaa
      181 lrerevtgrg qevqsalfen cvflcaqhmq qyamtheapp pmparvsaws vydvftladd
      241 eqlfigavsd kqfvtlcdvl grpdlpaepr fasnalrvav rpalldvlgd ilkghrvdel
      301 tpkleaagip yapivrpeql lddphlkasg glvpmeaddg tttdvvllpl tmggrrpgvr
      361 qalarvgeht heilsrltgr aaa
//
LOCUS       WP_284894065             160 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: YybH family protein [Burkholderia].
ACCESSION   WP_284894065
VERSION     WP_284894065.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..160
                     /product="YybH family protein"
                     /calculated_mol_wt=17446
     Region          29..153
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mqqirfctaa laacvsffaf tapataggtq rppeaaikae narwanafar gdyeaigrly
       61 tddgtllppg gdkvtggrai aeyltkgyag tkpgtvsfsh yefygddrmv tevsdaevrd
      121 hdgklqirgk qilvfvkqag ewklhrdmwn dyppvktadh
//
LOCUS       WP_284894057             813 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Burkholderia sp.
            lyk4-R2A-23].
ACCESSION   WP_284894057
VERSION     WP_284894057.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. lyk4-R2A-23
  ORGANISM  Burkholderia sp. lyk4-R2A-23
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 813)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 813)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 813)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 813)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14311963
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..813
                     /organism="Burkholderia sp. lyk4-R2A-23"
                     /db_xref="taxon:3040284"
     Protein         1..813
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88930
     Region          14..>613
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          725..786
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; cl38983"
                     /db_xref="CDD:476840"
ORIGIN      
        1 mlataagavr gpldlpadgw iaapapgtva qalalagqpd dtaslderdh wyrvelrghg
       61 prvlrfhgla tlaeawldda pilrsdnmfv ahdvpvsldg thrltlcfra laphlrdara
      121 srrarwrtrl aepatlrtvr tsllghmpgw fprcvptgpw rpvdvldpad gpvlvhcdlh
      181 aridgdtgwl daelafaapl pdafaarlsc gehyatleri gadrlhasva vpnvrrwwph
      241 thgepvlydv alhigaerrp lgatgfrtie pdagddgkgf glrvngvrvf argacwssad
      301 plalhaddat ygrllghard agfnmirvgg tmtyeadafh awcdrlgllv wqdfmfanfd
      361 yalddrafad avdreaeqfl trhraspsla vlcggseiaq qaamsglgpk qrfleltaer
      421 laghaaarrp dalyvpdspd ggalpflpre rvshyygvga ylrplddarr advrfasecl
      481 afanvpcdam laslgwpgvh eprwkaavpr dpgtswdfdd irdhylqtly dvapdrlrre
      541 dpsryfelsr aaiadlmrdt faewrrtgsr cagalvwqfq dvmpgagwgl idathrpksa
      601 wyalrqvlqp vqvllvdegl ngldvhvine rpaplsaave lvalrdgrtp varaggpvri
      661 aahdtvrlgs aellgrffdw tyayrfgpce hdtvvatlra ddgtllsqaf yfpsrthpav
      721 farrepgiea cvsrigdtwh vdidtrhvar hvqidapgfv prddwfdlap gtparvalmp
      781 ladtgdraaa gapptvdira vnaartvraa pag
//
LOCUS       WP_284894201             245 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: OmpW/AlkL family protein [Burkholderia].
ACCESSION   WP_284894201
VERSION     WP_284894201.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006882
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..245
                     /product="OmpW/AlkL family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26125
     Region          6..245
                     /region_name="OmpW"
                     /note="Outer membrane protein OmpW [Cell
                     wall/membrane/envelope biogenesis]; COG3047"
                     /db_xref="CDD:442281"
ORIGIN      
        1 mnfrrttrfa gvavcigsal laddvqaqta gsittsvgwl hispqgsatp ltvqsvggvt
       61 vnheltgssa hasstdtlgi tneyyvtdhf gvamlfgmpl kvnligdgtl qkygtlgttr
      121 pmppaielry hlfsatskfr pylgiganyt wftqvratns rfvsdsfgpg gsaratlsas
      181 wnpvfeigan yavtrhwsvg tsvnympvkt hltlygqtat gtqivskstl rlnpvsvfln
      241 vaytf
//
LOCUS       WP_284894323             742 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Aerococcus sp. UMB8623].
ACCESSION   WP_284894323
VERSION     WP_284894323.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB8623
  ORGANISM  Aerococcus sp. UMB8623
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 742)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 742)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 742)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Aerococcus sp. UMB8623"
                     /db_xref="taxon:3046348"
     Protein         1..742
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=84712
     Region          10..740
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 msekqnytke evldlcksym pedklafvak aadfaerahr dqvrksgepy fthptqvasi
       61 laelhmdpdt vatgflhdvv edtgislddi ayffsdtvat lvdgvtklgk lkyrsqeqqq
      121 aenhqkmlla mandlrvimv kladrlhnmr tlkwhksekq vsisretlei yapladrlgm
      181 sqikweledt clryinpeay yqivhlmntk rderenyine tiaklqgqme gviaepfeiy
      241 grpkhiysiy rkmkkqkkdf seiydllair vlvdtvkdcy avlgvvhtnw kplpnrfkdy
      301 iampkanmyq slhttvlgdk gvpveiqirt yqmhevaeyg vaahwaykkg vtgevekdel
      361 ddqiawfkqi qdlqddsvda eifvesvked ifkdkvyvft pqgdvqelps gagpldfayq
      421 ihtevgnkti gakvnskivp lnyqlengdi veiltsknsa gpsrdwvklv atnraknkik
      481 rffklldree nlekgrqave davnesgfaf kelytktkqa dllerfnfss lddlfaavgf
      541 gelsasavan rltekarakr reelhkknle evihdeeeke rkpamtvrhn dgvfvegadn
      601 llfrlahcct pvpgddivgy itkgrgisvh rrdcknvdld delsdrliev ewentqpdad
      661 isfevelvie afersgllne iiqvvspltk sisningnvd hktnmakiri rlaiqnidql
      721 dkiidkvkdi pdiyvveras tq
//
LOCUS       WP_284893433             349 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [Burkholderia].
ACCESSION   WP_284893433
VERSION     WP_284893433.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..349
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36243
     Region          1..341
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mslnaplsgv hivefeglgp gplagwmlag mgaritliar pagrtsapda lqgrdgdllr
       61 egktivaldl ktpdgrdaal aliaqadali eglrpgvmer lglgpdacar rnpklvygrm
      121 tgwgqdgpla taaghdlnyv altgllslsa prdgrpgvpp tvvgdaggal glafgivcal
      181 fdvrgggpgr vvdgaivdiv smlgslalwa rangqldgaq pslfhdapfy dvyrcadgec
      241 vtigaleppf yallverlgl advdpasqyd rarwpalkar faevfaqqps ahwrallegs
      301 dacfapvlsv aeavahphna argiyrvdgn gnvrarvapr flplmgdea
//
LOCUS       WP_284894450             246 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Aerococcus sp. UMB8623].
ACCESSION   WP_284894450
VERSION     WP_284894450.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB8623
  ORGANISM  Aerococcus sp. UMB8623
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Aerococcus sp. UMB8623"
                     /db_xref="taxon:3046348"
     Protein         1..246
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27119
     Region          8..246
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mthkgssywp gqankpalll mhflgdspek veplaenlha egypifllsy rshqqgdlsa
       61 iltaplstyl edaraamktl qakghqkiiv gglsigafla lalacecdqv aavislscpi
      121 ltdlrqtkip yfmrqsyyrs ldreptasdr nqaeklfaqf devlsgmnqw mednfealaa
      181 ikqavfighg qadevvpvql aerlsrllaa egnphlhlyp qadhylsgel vqerlsedil
      241 afldal
//
LOCUS       WP_284894729             228 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [Burkholderia].
ACCESSION   WP_284894729
VERSION     WP_284894729.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 228)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..228
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24505
     Region          1..211
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mldhlicdcd gvlvdsevia drvlfetlsa tfphldfeda aksafgqqts rflagleahf
       61 girmpddfie tiernietgl aqslapitgv rdallkvglp aavvsnsrlv rvrsslkras
      121 lteifgdrvf sseqvarpkp ypdvylhaah tlgvaperci vvedsvsgln aaraagmkti
      181 afvgashipd nyadalramg itrimrrmde lpalvaaglr gefgdvqs
//
LOCUS       WP_284894873             473 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Burkholderia].
ACCESSION   WP_284894873
VERSION     WP_284894873.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..473
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=51024
     Region          63..432
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mttynkpliq gesrfdqtql nvekdnwnwc epsrydgerp anwyeaslsr resgaplahd
       61 avcdvlvigs gllgasaalh laeagvdtil vdkhhvgsaa sgrnggqltp glarweaadm
      121 idylshddak rlwrfastes mdlideigar yaldldrkng hvtaavhpgh msalldgada
      181 rrhlgdagvt lvgrhqlhde yvrsglyhga aidalggqlh plalvrglvh gfqlnggaly
      241 egtevlelde tpagvvattp ggtitarrgv vlalhnttfr llddggattv pfftyvsvta
      301 pldvdvatlm pagmpvydtq fqidyyrpvr gnrllfggqg tgtcwaqqdv naylltrlnt
      361 vfpqhdgrfa ldycwsgvsd ftlngatdsr ktdgrvpmym vqgwsghgva qtvrigkaic
      421 ddfvgrnddf smltgidhre iplgrqlspi aipaakaams vmsalnpgrm isf
//
LOCUS       WP_284894891             138 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: VOC family protein [Burkholderia].
ACCESSION   WP_284894891
VERSION     WP_284894891.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..138
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15157
     Region          12..135
                     /region_name="PhnB"
                     /note="Zn-dependent glyoxalase, PhnB family [Energy
                     production and conversion]; COG2764"
                     /db_xref="CDD:442048"
ORIGIN      
        1 mtdprpanvp wltpylavrn aqaaiaffqs afgfelrdvl dedgaimhve mtyrgqlivm
       61 fapegafgst altpksadat apqsfylyvd dvdttwqral dagaksltap qdqfwgdrfa
      121 qiedlngyrw algcrlsa
//
LOCUS       WP_284894952             203 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsB family cell division protein [Actinotignum timonense].
ACCESSION   WP_284894952
VERSION     WP_284894952.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum timonense
  ORGANISM  Actinotignum timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Actinotignum timonense"
                     /db_xref="taxon:1870995"
     Protein         1..203
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=21886
     Region          5..90
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
     Region          <135..>201
                     /region_name="PspC_subgroup_1"
                     /note="pneumococcal surface protein PspC, choline-binding
                     form; NF033838"
                     /db_xref="CDD:468201"
ORIGIN      
        1 mslravaial failaiiivt ptvsrfseqq helravrael envqqhtrel evekalwndp
       61 dyvraqarvr lgyvvpgqrl fvgadpnegt aqeqleerva tvnrerrant pwyitgwdsi
      121 tiagnsvdgq idnpdeapmy tpptpqpdga tqpevetpad gsdpapaeqp aeppaeqpap
      181 edaanqapdt apaqdtapap ege
//
LOCUS       WP_284895182              84 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate ABC transporter permease, partial [Actinotignum
            timonense].
ACCESSION   WP_284895182
VERSION     WP_284895182.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum timonense
  ORGANISM  Actinotignum timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 84)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 84)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Actinotignum timonense"
                     /db_xref="taxon:1870995"
     Protein         <1..>84
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          <1..84
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 ynalillaam qavphelyea atvdgagpvr qffsvtvpql rstlifviit stigglqifd
       61 eprmfdtmgg ggadkqwltl tmym
//
LOCUS       WP_284895353             747 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: TonB-dependent receptor [Burkholderia].
ACCESSION   WP_284895353
VERSION     WP_284895353.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 747)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 747)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 747)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..747
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=81522
     Region          64..747
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mksrpdelkl gkfttlcsvl aaspafadgt pspapvsteg hlapieiqgk tehsykadfs
       61 asakftaplv dtpksvtvip qeliqnsgat tltealrtvp gitfgagegg nplgdrpfir
      121 gydtqgsmfv dgmrdtgatt reifnterie itkgsdgayg grggaggsin litkaphlgt
      181 taaasaglgt dryrrftadg nwqfadhaaf rlnlmshnnd vagrdvvnne rwgvapsiaf
      241 glgrptrvta syyhlstddm pdggipyfyt tsnkpanvdt iypapvdrhn fyglidrdfr
      301 kttsdistir iehditsglt vrntmrytes tqdyiwtqpd dsqgnvvngk vwrrnnnrds
      361 sinslanlte lfgefrtgpf khsfttgiel srewgkrdsy tvatdtgkic qkgigaasgy
      421 nctslwspnp ndpwagsvtr nndyahartt tksiygfdti eitprwqvng gvrvddystr
      481 ftdttanggk tttrddtlvn wqaglvfkpa qngsiyasya tsstpagmll gegsetqslt
      541 pgrggvgpna dqmapeknrs ielgtkwnvl ndklaltaal fqidttnarv tlpnnqyamv
      601 gnkrvqglel gvagqitkqw qvfggytymk selrdngkda andghrfpnt pkhsltmwsn
      661 ydvtpkftig ggafymsevf gdpanlravp sywrfdamaq yrinkkldlq lnvnnlfnrt
      721 yfdqaypahy asiapgrsaf itlnary
//
LOCUS       WP_284895447             340 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: zinc-dependent alcohol dehydrogenase family protein
            [Burkholderia].
ACCESSION   WP_284895447
VERSION     WP_284895447.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..340
                     /product="zinc-dependent alcohol dehydrogenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36803
     Region          1..337
                     /region_name="MDR7"
                     /note="Medium chain dehydrogenases/reductase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cd08276"
                     /db_xref="CDD:176237"
     Site            order(40..42,45,144,148,169..174,192..193,197,212,
                     237..238,240,259..260,284..286)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176237"
ORIGIN      
        1 mrvyqvenew tmanlriger pipeprdgqv rirmraaaln yrdsliplrg ygkrmqelpl
       61 vmlsdgfgiv davgagvtrm qpgdrvcplf yqswlggppg nerfryslgc eqdgtmadyl
      121 vlsaegvska pvhlddveaa tlptaavtaw rslvtegnlr pgetvliqgt ggvslfalqf
      181 akllgaraiv tsssdeklar vralgadetv nyrdnpqwgk iareitggqg vdhvvevgga
      241 gtleqslrav rtggtlsmig vlagseptip lgqivtrhir lqgitvgnrd dfeamaaaia
      301 lhelrpvidr vfefealrsa ldymargqhf gkicirhasn
//
LOCUS       WP_284895474             699 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Corynebacterium
            accolens].
ACCESSION   WP_284895474
VERSION     WP_284895474.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..699
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73808
     Region          30..515
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mqfrrigqlv aattvtaval sgthalaqed tttisvtnit dlhghledgl sdpaktgdei
       61 gvarlqslik qvnegqefnl tssgdnvggs afvsaisddk ytlealnamg mkvtavgnhe
      121 fdkgtedlmd riqpgsdypi lganvlkdgk plldashvee idgvkvgyvg tvtqntkfkv
      181 saakipgvtf tdpveatnke atrlkesgea dvvvslfhed aeeyaqgfnk dvdilfggdt
      241 hqttqgtver egalplqwaq gyeygkllnd aditydkaar kvksielkqy dataaaqvep
      301 daeiagivkk aqdeaevegs ktagtvetdl frgsdegqkp gsnrgvestl nnfiaegqry
      361 amskqvgedi dlgvmnaggv radlqggdvt ykdifevqpf gnsvitakvs gkdfitalen
      421 qwqegssrpr lamglsnnvq vvydykaaqg ervksvting epldpnkdys ialssflass
      481 dtekggdgyf eagsikdknd vgymdaqami dyiasgesev rkgqgqigah iegdivpgke
      541 itvdlsslny tsegepmakt vtvklgdeea tadidnskqe gddqfgergr aqvtltvpqg
      601 ltgsqnleit tdagtqailp vevgeaggde sgshedgsqg ngsdgedspk lpegssfgga
      661 alaivaalaa giafiglnpq vlpaplraif ddlrktfhi
//
LOCUS       WP_284895759              62 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            accolens].
ACCESSION   WP_284895759
VERSION     WP_284895759.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 62)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 62)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 62)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..62
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..62
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=6432
     Region          1..62
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mttkhllgta gaaetlglsr qgvlkrvkdg rlapigalgk rgiyvfdrae iealadeeka
       61 ak
//
LOCUS       WP_284895798             119 aa            linear   BCT 25-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Corynebacterium accolens].
ACCESSION   WP_284895798
VERSION     WP_284895798.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..119
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12943
     Region          2..115
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 mnllfvligg ffggaarygf trllpspyct fvsnilgslv fglavgfaql advpfahplf
       61 alglagglst wstmakelge mvkqrhwwpl ckylfwtigi gvvlawrgvm wagliyrgi
//
LOCUS       WP_284895814             143 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ExbD/TolR family protein [Burkholderia].
ACCESSION   WP_284895814
VERSION     WP_284895814.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..143
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=15080
     Region          7..140
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mgmkagagag rddpevmvdi nttplidvml vllimliiti piqmhsvkmn lpvgnppvpp
       61 hppqvvqidi gadgsvnwng vavrgaaald akfrevatea dqdeirlrpd kaapyravae
      121 vlasaqrega tkigligneq flq
//
LOCUS       WP_284895823             825 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Burkholderia sp. lyk4-R2A-23].
ACCESSION   WP_284895823
VERSION     WP_284895823.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. lyk4-R2A-23
  ORGANISM  Burkholderia sp. lyk4-R2A-23
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 825)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Burkholderia sp. lyk4-R2A-23"
                     /db_xref="taxon:3040284"
     Protein         1..825
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87162
     Region          71..779
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mrhtrgegvs pktrrtvisv avaagvfhga awaqdagaga aaaaaatpas saaapassas
       61 aapdgkvqvq drvvitgsrt etrasksltp idviggdqlr atgqtnlrda lvklspsitr
      121 tsnsgdtgvl tdtlslhglt pdhvlvlvng krrhttanit ldpglnqgst gvdidtipvg
      181 lidhievlrd gasaqygsda iagviniilk rntrggelst tngqtysgdg fktsesatig
      241 lniadkgfld lsagfdrqnh tirtgpddyf grflqgqgyy npilgdpsss retvgfnagy
      301 yldddvelyg fgtyahrngd ayqnfrppsv lpqvypngfv pvetinendy svtagvkgkn
      361 lfgwawdlst tyggdysvfg mrnsantgly aatgftpstf hlstvsntql tnnldlsraf
      421 nvpllpapln vavgveqrre tytirngeqa swidggsaal pglapvsasd isrnvigtyv
      481 dlstyltpkw qvnlagryeh yndvgdttng kistryqfsp aiavrgsvss gfrapslaqe
      541 sytsvttspa svggilatts pgarligaqa lkpeqstsyn fglvlnpvrn lqltidayqi
      601 nirnrivlgg tasgaaaiaa legaglsvpg svpasavsas yftngantrt rgidlagtyh
      661 tgfgrygqvd wdfgvnlntt svthvangsn gkpslngqqi aslstttpkn kiiiggtwrl
      721 dkwavtlhet rygktsgegt yfvgpnafst sqfvhyeeaa ryvtdlevry dvtkqfqiaa
      781 gaqnlfdarp sklpfetqle giqysggsti gvnggfyylr arylf
//
LOCUS       WP_284895831             659 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD/NAD(P)-binding protein [Corynebacterium accolens].
ACCESSION   WP_284895831
VERSION     WP_284895831.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11816065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..659
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72217
     Region          1..627
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
     Region          9..202
                     /region_name="NAD_binding_9"
                     /note="FAD-NAD(P)-binding; pfam13454"
                     /db_xref="CDD:433222"
ORIGIN      
        1 mtdntssial iglgprgisv lerlvaqlnt vshppekltl hliddaqhgg gkiwdinqpk
       61 ylcmntfahg mtlfsetnst veapvvegpt iyewirltlg dahvspgard yvaahpldpq
      121 vleefgrael eklrpesylp ralyghyilw ffrsvlqdvp ewvevkqhha rvvdiesrdg
      181 adilhlnndt tvaagstlav tgwqnqgyte nerwilktle enpslrwira dnpidqgids
      241 ikdnekvlvr glgmgffdil ilstvgrggk fvedsskpwg mryeatgtep tfaaasrrgy
      301 pflpqsdegs lppaaeiprl kkvvaelshr tgarsinydt evwpavarda yqayidslar
      361 vepeslrasr eeiiaaldat pvdagvayng laqldeviar yttkdfsllr wmhlltedfs
      421 nqqeltehiv qnlcedlaea qkgpdspvra alwsvgfsrk ptqvlgaegr ytlesrhhmf
      481 dkaislgqtt csgpppfrtq qllalvdagi vsfvggnpvl gtnadagewt isssasggkr
      541 ipgttlldaw vhkpdirrtp hdsfmhslve sgrvraftet ardgievptg spaedpdtrq
      601 vhnadgtvde rlhlvgipah aeypdttlap pipgtdswfi qeadkaavha aqvalagqa
//
LOCUS       WP_284895885             407 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [Burkholderia].
ACCESSION   WP_284895885
VERSION     WP_284895885.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..407
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43925
     Region          1..401
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mqarplegir vvdyshflag pyvgrclaal gaevikverp gtgdagrqha tvlddqqsgy
       61 flqlnmgkrg vsvnmkdarg kafmqrlcds advfienyrp galdklglgy aelsarnpal
      121 vycsisaygh tgpdahragf gliaeaksgi mqmvgtpger ppllrislgd mytgihavaa
      181 inaallgrvk sgrgqhidma lydtlvsmhe yavqcytlqg vlpeqtghdm ptstlygvfr
      241 aadgdlviaa qvddawkrfa alieahggpv gfgadtrfhd svgrnahrve ilsvvepwva
      301 aqsvasvldl ldridvpcak vqridevmad pqiqargmvv eqehprygtl rlpnlpfrfs
      361 dcdttirdva pdlgqhnadv arslgfepae ieamqadgvl yskasqr
//
LOCUS       WP_284896154             219 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            accolens].
ACCESSION   WP_284896154
VERSION     WP_284896154.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..219
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23508
     Region          10..218
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mpnslprpss dlfpealkls pkqrevltql qhyprgaraa eiakdlgmhv ntarghidel
       61 ihvgavtavp erssgrgrps lifqarvpdn raiadeyvsl isvlttmlag keelddfssp
      121 qarelgrqwa ratgadihsg aldtlfatlr dmgfdpsqga dpseielnac pfvssgttps
      181 pfvcaihagf lqeasgtdtd ialtpmqrpe vcqieikpv
//
LOCUS       WP_284896192             158 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Corynebacterium accolens].
ACCESSION   WP_284896192
VERSION     WP_284896192.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..158
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17247
     Region          53..>114
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mnvrrvsmds lrgrrtlsgl svrgdftpaq akardkakar arrsdsighl gpeavvafvd
       61 gemepkamhr vrihlvhcae cradvhhqrh asewvrhcsd dsavkapqsl laklagmate
      121 gvapgpdast pahrpeqdfl dkvetvvrai khnqrgqn
//
LOCUS       WP_284896365             548 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Actinotignum timonense].
ACCESSION   WP_284896365
VERSION     WP_284896365.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum timonense
  ORGANISM  Actinotignum timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Actinotignum timonense"
                     /db_xref="taxon:1870995"
     Protein         1..548
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=58805
     Region          107..358
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mrltdlpytp ptdnpppgrt lvpashlesa ertarrgwrr wlpthkrfvt wlivvlaagl
       61 igsafgpgwn pqpmtaaiap qtpdttistg vptarlgtyq vasstvtitl rdgtlipavv
      121 krpvgaasvv pgmlfihgtg tssardfgre teaiastgii tvvpekrvan yttthrdylq
      181 laadfedvyr emlswedvda rhsglyavse gcfvapivat sakavnyval isapvlpirq
      241 qgayaadayl reihaparlr aaipkligqd fgpdtfryid fdaapyekqm tmpvlmlygt
      301 adnsmptiqg pqmmarylee agnsaltvry ykdadhglqi nrsklsraam qdtadwvngl
      361 pftataqprv agdqprqafv aptlaaggwf taqtalyial ggvallavsi vlvavcwipv
      421 rghrlsnfsg sgaalnlasl svvgawavfl vylvavahia ltyshnlliv qggfalvhla
      481 algaawmhvr aafrswnarp gmgriarvtt lltlcaqavl lmslgywnaf pavllvshrg
      541 qicaysas
//
LOCUS       WP_284896379             223 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium accolens].
ACCESSION   WP_284896379
VERSION     WP_284896379.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..223
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23378
     Region          2..217
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(5..6,8..9,12..13,50,54..55,58..59,79,86,89..90,95,
                     110,114..115,117..119,121..122,125..126,129..130,156..157,
                     159..161,163..165,167..168,170..171,175,178..179,185,187)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(113,117,120..121,123..124,170,173..174,176..181,
                     184..186,190,192)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(134..141,158,161..162,165)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mllsvlvina valshghlpt llisiafssi alatvkphyg liclcafals ylgywgllql
       61 pgstffafsa aifswlsrfv ismsigafgl ltltpstlts alrdlrlpgw atippavflr
      121 vlpiivaeak airdamvlrg lqpgvkswft qptqssamli ipllgavvra gdelaasalv
      181 rglggptrpt ttadlsfklv dataiaglgl vvasvwlpte vrl
//
LOCUS       WP_284896467             473 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium accolens].
ACCESSION   WP_284896467
VERSION     WP_284896467.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..473
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=50649
     Region          8..404
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mkttthgals rlhkfagviv apflivaals gffyalaptl eqwvyhdeit ataqgsprsl
       61 deqiaaaqrq hpgaavaave asedpeettr vlftdpdaks psythavfvd pvdlritgee
      121 qqyggsralp lrtwlsnghr tlwlgepgri yaelaaswlg altiagvylw lkrrkktqkk
      181 nnkalrihar lgswllpgfl fltitgltws mvagsnigkv reelnwkeps vatsvaeaga
      241 gtgagegsga haghaghegh aghsggevtd ndvvegaqta lstarseglt gvlrmtppeq
      301 agdawtvreg raayklrsda vavtadgrvi drinsadwpl aarltswliq lhmgtlfgiy
      361 sqvalaalal gllvisiagl wmwwnkprrr lpelkitpav vagvviysii aplfgaslll
      421 ffagdwlvrr lrpqsrsrsr sqsgtgrsng dsgptarprg esssripstv qng
//
LOCUS       WP_284896575             408 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Corynebacterium accolens].
ACCESSION   WP_284896575
VERSION     WP_284896575.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..408
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44139
     Region          27..222
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mlevmseakq rvstrqmlrv vdrsvvsrlq rirsrfvyii qatvgaalay wvassvvghp
       61 qpffapisav iilglsggdr mkravemslg givgvalgdl lfqvvgqgpf qilfivgagl
      121 vvgsfitksp lvsnqivfgs iliatifppt egpgglhrai damigsgigl itialipnsp
      181 lkearrevsk vlriassiln dvthgirdtn peiirdarda vrgtqndvnt llsaaqsgre
      241 asevspllwt srrnirsler illpvdnavr gvrvlsrral vltedgdtvs dkqlelleel
      301 seiilavgel ygrqkrdhde aieipelvqr lryvggqagm dlieedatls aytilaqtrs
      361 ivvdmlmvcg lsresavahl vptsahpayp pevwgrddkp sdkqkgqd
//
LOCUS       WP_284896634             381 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Corynebacterium accolens].
ACCESSION   WP_284896634
VERSION     WP_284896634.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..381
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41742
     Region          11..356
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mrtqasvkrl pqhlpeldgl ravaalgiiv thvsfqtgtg wgfagrfdff vavffalsaf
       61 llwrrrglht vrgyahsria rlapayyacv vsvvlllpda hsitptqila nltstqiyva
      121 dglapglthl wslcvefffy lvlpllvwai gglpqrwrmg viagvavlsw gwgfipfvad
      181 ygedqvnsqi wppayaswfa vgmlaaevee rgigkrtari lqvrwawvvl aglvlwvasr
      241 dwfgpaglvh pepaefarri iagavfaacv vvpvalvprg tswltsplmq algawsysif
      301 lwhvavlava fpltgvalfs gkpldfwvil avtvigtvvv saasytlier pgrdllmgrg
      361 rgrdrgrrrr kgrpaprhis t
//
LOCUS       WP_284897200             611 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Actinotignum timonense].
ACCESSION   WP_284897200
VERSION     WP_284897200.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum timonense
  ORGANISM  Actinotignum timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 611)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Actinotignum timonense"
                     /db_xref="taxon:1870995"
     Protein         1..611
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67631
     Region          17..605
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 maeiertevf tpgkihitde mtipwvfrni areqpertvv arkaslgqwv pvawrtfese
       61 yralargfia mgvqpgdria lmchtryefc vvdfalwsig amavtvyetd steqarwive
      121 dahcrfavve nqqmaavmap frsdfdfftd ifvisdddla risargtmdl daeidrrida
      181 mhaddeatvi ytsgstgrpk gvvlshrnll hvvingpldd nlapilsgek rtllflpmah
      241 vfarfinlva fyagntighc pdthnlvedm ksfkphcila vprvfekiyn aadaqstgvk
      301 qkifryyakv aiaysralds aagpslalra qhevgerlvy skikeitggn lenvisggap
      361 lgarlghffr giginifegy gatetsaptt vnrfnhqrig svgpaypgch vaidtdgevl
      421 vkgdhvfhky lnnpeetaka ftedgwyrtg dlgkiedgfv witgrkkeli vtaggknvsp
      481 ailedrlrgh plisqvvvvg dqrpfvgali tldaemlpiw lknknlpams vseavhdpqi
      541 iasvdraikr tneavsraes irkfvilpid ftpengylta slkvkrtavl rdfatvigrd
      601 iygdkgdknr d
//
LOCUS       WP_284897327             469 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium accolens].
ACCESSION   WP_284897327
VERSION     WP_284897327.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..469
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51466
     Region          5..400
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msrttlrsfi qrihfyggmf vgpfiliaal tgclyalapt lekfayrdvm tveevnnpvs
       61 ledqisaaqk ehpdmpvsqv wpaesatdst rvlvadpgid eslqrtvfin padgevigdy
      121 ptysglgemp lrrwisslhe sfhlgqpgel yselaaswlw vlacgglymw wirrrpkkaa
      181 aplkkqpqrs krwkatrlhs tmgawifigl iglsatgitw sqlagenvns vvekmnwkat
      241 pvetalttda thdahagheg hgahgahggd aeapgeapep eviakqaerv yatgraeglt
      301 gplrlyaped tdsgwkvser wvewrytsde vsvngstgev idrfpfselp lfsklsswgi
      361 ylhmgimfgl plqialfalg laiaamvvlg yymwwkrrpq fapgskrhfs wattglgalf
      421 aatvgvfmpl lgitlaaflv ldiivmntgk rkatapkkkd edaelvpvg
//
LOCUS       WP_284897377             938 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium accolens].
ACCESSION   WP_284897377
VERSION     WP_284897377.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..938
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103737
     Region          4..936
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtethldtfa aglpypldef qvqgceaven gqgvlvcapt gagktvvgef avslalsrgt
       61 kcfyttpika lsnqkyhdlv aehgddavgl ltgdvsinad aeivvmttev lrnmiyadsp
      121 aldrlthvvm deihfladas rgavweevil nladhvsiig lsatvsnsee fgewlatvrg
      181 dtsvivtehr pvpldqwmml grkiyplfep esggqvnsel erriqrleag dsddgradyk
      241 sgkgfrarar hkgggrsefh gkaggrsgss rpqdryrplg rpevlkvlqs qdmlpaitfi
      301 fsragcdgal yqclrsrmvl ttqeeaeeik aivdagvegi peedlqvldf rrwrealsrg
      361 faahhagmlp afrhivedlf vrglvravfa tetlalginm partvvlekl ikfngeahvd
      421 ltpgqytqlt gragrrgidt lgnavvqwap amdprfvagl astrtyplis tfapgynmai
      481 nllgmlgfed slrlleksfa qfqadgsvve etreleraeh rvrelreqld davdalappa
      541 kdgedpaevl mdyirlrrel taeekqskvd kehqrtqevi avlarlqlgd viaiagkkrp
      601 tlaavvtpan qtedprpwvt tesgwsgrid atgisnppiq lgrikipkpv rknprrntky
      661 iqdvfrrekf drpkrmkskp rlrpnkrvge lrdairehpa hkwpatdreq lagvaqklar
      721 rerdleklqa kvdkatdtlg rtferivdll aemdyvefsg vcsdrtpvit eegerlakih
      781 sesdllvaqc lkrgiwdeld paelagvasl ccfenrkatg gqpeaatdrm adamnatwri
      841 ytelsaderr hrlpptrepe agfalaihqw sagaplgycm aaaneagael tpgdfvrwcr
      901 qvvdllqqia ktgydgqiqr narraidaiq rgvvaiga
//
LOCUS       WP_284897492             699 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Corynebacterium
            accolens].
ACCESSION   WP_284897492
VERSION     WP_284897492.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..699
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73683
     Region          30..515
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mqfrrigqlv aattvtaval sgthalaqed tttisvtnit dlhghledgl sdpaktgdei
       61 gvarlqslik qvnegqefnl tssgdnvggs afvsaisddk ytlealnamg mkvtavgnhe
      121 fdkgtedltd riepasdypi lganvlkdgk plldashvee idgvkvgyvg tvtqntkfkv
      181 saakipgvtf tdpveatnke atrlkesgea dvvvslfhed aeeyaqgfnk dvdilfggdt
      241 hqttqgtver egalplqwaq gyeygkllnd aditydkaag kvkkielkqy dataaaqvep
      301 daeiagivkk aqdeaevegs ktagtvetdl frgsdegqks gsnrgvestl nnfiaegqry
      361 amskqvgedi dlgvmnaggv radlqggdvt ykdifevqpf gnsvitakvs gkdfitalen
      421 qwqegssrpr lamglsnnvq vvydykaaqg ervksvting epldpnkdys ialssflass
      481 dtekggdgyf eagsikdknd vgymdaqami dyiasgesev rkgqgqigah idgdiapgke
      541 itvdlsslny tsegepmakt vtvklgnaea tadidnskqe gddqygergr aqvtltvpqg
      601 ltgsqnleit tdagtqailp vevgeaggde sgsqesgshe dgsdgedspk lpqgssfgga
      661 alaivaalaa giafiglnpq vlpaplraif ddlrktfhi
//
LOCUS       WP_284897609             389 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Corynebacterium accolens].
ACCESSION   WP_284897609
VERSION     WP_284897609.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..389
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40896
     Region          11..388
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mneslekvas arldkwredg lwrspsvfgs gqvpesslrt atgktvqdav lfsssnylgl
       61 aehpeiknav kdsvdhygag sggsrlttgt sdlhvaveaa aaqltgypds vffatgyqan
      121 lstlqalasp eltiisdarn hasiidgcrl akasgaslvv tahrdtrave dalatrttky
      181 alvitdglfs mdgvlaplpe lsrvarkyga wlmvddahsf gtvgdrgfgl peyfgvqpdi
      241 qlitaskalg aegglvatsk pvaqllrqqa rsfvfstspt patsaavlaa fkliesdpsl
      301 vsqlqdniay whntrgttpq qgpiipvhvg deaaamdasa alldqgfvvp airwptvarg
      361 aailrvtlma thtraqidal caeldqlgl
//
LOCUS       WP_284897634             242 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [Burkholderia].
ACCESSION   WP_284897634
VERSION     WP_284897634.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..242
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24368
     Region          21..226
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 msaagkgaag egmvghglnv licdcdgvli dseavaadvi vreldarwpg vdarpavmpl
       61 lglriervla gaseavgrtl saddvdairr aveaaavnap mvdgietala aislptacas
      121 nsyrayveaa lartglarff gdrlfcadav arpkpapdvy laaaralgav paqclvveds
      181 vtgitaaaaa gmtvlgfvgg ghasaaqvda lrgigarhvf ddmhelpgyv arwqatgavl
      241 pg
//
LOCUS       WP_284897646             399 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Corynebacterium accolens].
ACCESSION   WP_284897646
VERSION     WP_284897646.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..399
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43913
     Region          60..379
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 maiqkrltka gktvyiarwr dpagkehsks ftrqkeakah vqemerasrl gidptagdnv
       61 tvrelmtlwi edreirpssl alytrtrdkh lgpladwpak dvtpkvvrdw qaqlrsgrtw
      121 iskddtgmsp ryvqtaashl rsaykwgien elvaknpvrv ervqaavepd dvptmeeiqa
      181 vidrarygga aytevkakge eprklvlrpd pmfadmltva aftglrigel cgllveevnl
      241 glgvvqvrkq ldkrpphgrv vlksknsrrd vpisaelrpv lervtagrmp geflftnrdg
      301 rpflpsgagd kvlrvamfek aprvhfhalr hhfassllla gvpvpdvarv lghtpaqllk
      361 tythalpgsg drvaaaisas vgcgisagst hlrvvgkta
//
LOCUS       WP_284897715             181 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Corynebacterium accolens].
ACCESSION   WP_284897715
VERSION     WP_284897715.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 181)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..181
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19628
     Region          4..156
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18879"
                     /db_xref="CDD:467590"
ORIGIN      
        1 mptpdyivkl resigrdqif vpacsaiilr dvptgaalwe vpsvllvkra dnavwtpveg
       61 icepgeeitt talrevkeev gldakveall gvgqsgpvty pngdecmfmg talrlsvadg
      121 aepvisdeen teaqwfsvah lpdslsrrhr lmiadavahl khpqgfsprm gwmkrseqpg
      181 l
//
LOCUS       WP_284897767             592 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: PglL family O-oligosaccharyltransferase
            [Burkholderia].
ACCESSION   WP_284897767
VERSION     WP_284897767.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..592
                     /product="PglL family O-oligosaccharyltransferase"
                     /calculated_mol_wt=63888
     Region          172..416
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
     Region          382..554
                     /region_name="Wzy_C_2"
                     /note="Virulence factor membrane-bound polymerase,
                     C-terminal; pfam11846"
                     /db_xref="CDD:432124"
ORIGIN      
        1 mpstfsrslp lvalavaliv pysitnhtyp iptfysefaa lvlyllvgls vvllartgrp
       61 aepfaapaaf vaplgfaavl laqvalmplk vpsmnwlalg ylaaalvamq agytlaregl
      121 aeatarmmag allvggvfav asqvvqlfhl esavspfvvi yniavdrrpy gnmaqanhla
      181 tyiafalaga lylvqtrrla vwawfalsiv lsiglaltvs rgpwlqvavm vvagfwmawl
      241 esrrtpgtrr awlipaalav afvavnvavr wanlhfhlgl aesaaermrd agqiaprlal
      301 wkyglamfre hpllgvgwge fpshqfalvr tlggveiann shdifidlla ksgllglgvl
      361 vvalvtwfvr avrapqsstr vfglaligil lmhalveypq qymffllpam fviglldvkp
      421 lrllpgraaf glfavlsvgg vlaavpvlrd yqraevlyyg ndpaaqyrda psllfgawgd
      481 ygvatlltis peslplklva heraiallpg etvlrryaal qalagreada ldtverlhvf
      541 akelkdwpqq lallyklcdq qpalkafkaa vvakygevpa daddddsddd se
//
LOCUS       WP_284897847             350 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Burkholderia sp.
            lyk4-R2A-23].
ACCESSION   WP_284897847
VERSION     WP_284897847.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. lyk4-R2A-23
  ORGANISM  Burkholderia sp. lyk4-R2A-23
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Burkholderia sp. lyk4-R2A-23"
                     /db_xref="taxon:3040284"
     Protein         1..350
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=39089
     Region          1..337
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 milvyryrvk slngllnkqs ravnyvwnfc ndtqkhalkw skkwptgfdl nvlttgsske
       61 lgihsgtvna tceqyaksrs qrrrpylryr grkslgwvpl kgrdlkregd afrfagntfr
      121 vfhsralpeg kikdgttfaq dargnwflni viempdvqar pvrsgvgidl glkdfatlst
      181 geklpndrfg rraaeklaka qrarkhkrhi aklhakvana radfqhklal dlvrrfdyla
      241 vgnvsaakla rtrmaksvyd aswssfrnkl rykaiahgat feevdesgst qscsacgskd
      301 sttrpkgiag lrirewacsd cgvehdrdtn aalnilrcgr aspgvgitcl
//
LOCUS       WP_284897902             241 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium accolens].
ACCESSION   WP_284897902
VERSION     WP_284897902.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..241
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25319
     Region          14..235
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(23..24,26..27,30..31,68,72..73,76..77,97,104,
                     107..108,113,128,132..133,135..137,139..140,143..144,
                     147..148,174..175,177..179,181..183,185..186,188..189,193,
                     196..197,203,205)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(131,135,138..139,141..142,188,191..192,194..199,
                     202..204,208,210)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(152..159,176,179..180,183)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mslqkqgvlr rasidprtvl lsvlvinava lshghlptll isiafssial atvkphygli
       61 clcafalsyl gywgllqlpg stffafsaai fswlsrfvis isigafgllt ltpstltsal
      121 rdlrlpgwat ippavflrvl piivaeakai rdamvlrglq pgakswftqp tqssamliip
      181 llgavvragd elaasalvrg lggptrpttt adlsfklvda taiaglglvv asvwlptevh
      241 l
//
LOCUS       WP_284898176             111 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: Rieske (2Fe-2S) protein [Burkholderia].
ACCESSION   WP_284898176
VERSION     WP_284898176.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..111
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=11725
     Region          1..101
                     /region_name="NirD"
                     /note="Ferredoxin subunit of nitrite reductase or a
                     ring-hydroxylating dioxygenase [Inorganic ion transport
                     and metabolism, Secondary metabolites biosynthesis,
                     transport and catabolism]; COG2146"
                     /db_xref="CDD:441749"
ORIGIN      
        1 mgatqlcrfs evpdggarvv deagigrpvi vvrrgeqvwa yvnrcphfsv pldfvpgnvs
       61 cyrsqvmmca hhsalfrfdd gvcidgpcsg agleavavev dsaawvvcrg a
//
LOCUS       WP_284898249             479 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ATP-binding protein [Burkholderia].
ACCESSION   WP_284898249
VERSION     WP_284898249.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..479
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=52760
     Region          34..>461
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mntvmeqpar pqyrstpehs vialgefeln lgmralykag revplgsraf dilsvivlas
       61 grivskdelm dtvwpgvfve ennihvhlsa vrkalgdhrq lidtvpgrgy rfkvfhgmsa
      121 epgrdvpter haplfrnadt mtpprhrlpg rrtllgrata ldeiegrfal srvvtltgpg
      181 gvgktclaie hahrttaagt sdvvfidlee agslaavsqi gpapsrpagt llvldnaehi
      241 vdevadlver ligqwhslrv lltsrerlri apetvfrvep lalpadescr dklmqspave
      301 lflerasrcg vrvddehqlr lvaeichrld glplaielaa grasvlgieg vhqrleerfl
      361 llaggyrtaq prhrtlraaf dwsfqrlthn eqavvrriar fdhaftldsa ysvvcddsvd
      421 rttaldciaq lveksildvs fvgvtasyrl sesartyala lgsgnepcnv akqrarylq
//
LOCUS       WP_284898311             430 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Actinotignum sanguinis].
ACCESSION   WP_284898311
VERSION     WP_284898311.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum sanguinis
  ORGANISM  Actinotignum sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 430)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 430)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 430)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 430)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Actinotignum sanguinis"
                     /db_xref="taxon:1445614"
     Protein         1..430
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47398
     Region          10..422
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 millgaggan fkslrdewel sllrpslrhn ippegelwre hvwpcaaiyg anasgkstvl
       61 ealnfirdav nnsarswasa dklpvasfal dpekrnadts lwidfvtddi ryvysftlnt
      121 svivreelra yysarattli erdvrghkvh ptrvgkisev sprelvlsra svldtkvlgh
      181 lartigkdll myrvgnsdyd mqfqkltsyl srdiakrrly aslakvadvg iddisvesre
      241 fppelldmlk nlipeehrde eitaelvkql alvlrfshkg akdsitfgag qeslgttswl
      301 algslaveal rsgkvvcvde idaslhpmla teliaafqdp elninggqii ftshnpyfls
      361 hdsgagltpg qvwlteknne gatdlfsvad fpdvkpgtdm aslymsgrlg atpllepwlf
      421 rkmiggradg
//
LOCUS       WP_284898321             165 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Corynebacterium accolens].
ACCESSION   WP_284898321
VERSION     WP_284898321.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 165)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..165
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17733
     Region          86..161
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mnivesrlsd learvakleg qssappqpps eestywlvda lapstqlpdg svifggnial
       61 gkrtyayqwq rpttaitdee wsenlerlaa lahpvrgeil rrllaapata aelvdedivs
      121 stgtayhhls altsagwttk tsgeysirpa rvipllaiit asedh
//
LOCUS       WP_284898322             277 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Actinotignum
            sanguinis].
ACCESSION   WP_284898322
VERSION     WP_284898322.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum sanguinis
  ORGANISM  Actinotignum sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Actinotignum sanguinis"
                     /db_xref="taxon:1445614"
     Protein         1..277
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29690
     Region          35..230
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mselepidpy lddskarrrh rvrraltkpv mstilrptvl geenienldg afilvpnhss
       61 hldapmifsl lpdklterla tgaaadyfyr rrgisnltsl ffntypierg kkptgkagse
      121 yqpgrakgmt grllaagvpi lifpegtrsr tgelgtpkag aaalaqrfnv pivpiamsgg
      181 hevmpvgavl pkfrgevflf igrpmyglae edsadfmgrv ftaiqmmleq ksahpltpeg
      241 tspfdaaqag qaptagvape agdpseagea gefpete
//
LOCUS       WP_284898354             463 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Burkholderia sp. lyk4-R2A-23].
ACCESSION   WP_284898354
VERSION     WP_284898354.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. lyk4-R2A-23
  ORGANISM  Burkholderia sp. lyk4-R2A-23
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 463)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 463)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 463)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia sp. lyk4-R2A-23"
                     /db_xref="taxon:3040284"
     Protein         1..463
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50504
     Region          131..456
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mdadraanft rrwhtttfrw lcayaaifsv sllllagvin vaathtmard tdevlawqli
       61 yfdsipdael plaihrrleh ehmhtnfygl fdasgrrvag diatppalrt drrgrtldrt
      121 lvpldgqpap itramavhrd dgmtlvvard lshfiqirev airglviggv liliagiagg
      181 smlgmrqirr vaairrvtrq iaegdlgkrl pvgrydeldl lahlvnhmld everlmgevr
      241 htcdgiahdl rtplarvhtm larlaeqphc ahdpasaqll asardetdrl lerframlri
      301 seigtlsrrg gfaavdvaal lrdvcelyep laeaggvafg ldampvdgih gdrallfeaf
      361 snladnaikf tppggrvrva lhatpngplv rfedtgpgia pgerdavler fyrgartrhv
      421 ngsglglsiv savmrvhgfa lrigdaqpag aaitvecwpr slg
//
LOCUS       WP_284898389             317 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Actinotignum sanguinis].
ACCESSION   WP_284898389
VERSION     WP_284898389.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum sanguinis
  ORGANISM  Actinotignum sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Actinotignum sanguinis"
                     /db_xref="taxon:1445614"
     Protein         1..317
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33424
     Region          3..299
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(34,242,245)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(180,211,240,243..244,247)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 marfvsagea lvdiiirege tgpgtevvgg sllnvasgva rlgqhvelat wfgrderger
       61 iaaqatamgv divpgsdgas rtttasafld aegraryefd vesdfpeipd pdtvghlhcg
      121 sysavvgass kkilravkrq altgtvsydp narpdlmgsp ekvresieel valcdvvkas
      181 dedlewlypg epverimrrw vtsgpgmvvv trgpwgayvk lagerdmlvv dplnvelgdt
      241 vgagdsfmag mlaglmeagl lgsveakqrl raahfsdvrp alhqavitag ltvshdgays
      301 ptpaevdtvr tgdpalr
//
LOCUS       WP_284898479             377 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Actinotignum sanguinis].
ACCESSION   WP_284898479
VERSION     WP_284898479.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum sanguinis
  ORGANISM  Actinotignum sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Actinotignum sanguinis"
                     /db_xref="taxon:1445614"
     Protein         1..377
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=37862
     Region          204..370
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 msqgtpdsvd rgqsgfqgqy gapaaagsda gvgpdpsvga aggaapsagt gadpagpawp
       61 psappavpag eqeqhpssrg fwvmitvlai ialvvfavll tlgssngrfg gsaaphpttt
      121 atapatpgag apgqggsapg apgtipntap gpvetrytql atdrgwvagq dyiptqpdei
      181 rtqlqalpql epssgqtagd pkapvhvtiy sdyacsfcnk lhaesvpqll elakkgdiyl
      241 ayvqvpifkd tvssdraaaa ahaaglqgkf weysallfdg aaaaghdpdk aasmfsdenl
      301 dafasqagld veafraards settsfiaaq eslgletlgl rgtpaiiing tastgyqpls
      361 aitntielek alvdsag
//
LOCUS       WP_284898486             916 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Actinotignum
            sanguinis].
ACCESSION   WP_284898486
VERSION     WP_284898486.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum sanguinis
  ORGANISM  Actinotignum sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..916
                     /organism="Actinotignum sanguinis"
                     /db_xref="taxon:1445614"
     Protein         1..916
                     /product="class I SAM-dependent DNA methyltransferase"
                     /calculated_mol_wt=103080
     Region          58..915
                     /region_name="YeeA"
                     /note="Type II restriction/modification system,
                     endonuclease and methylase domains [Defense mechanisms];
                     COG1002"
                     /db_xref="CDD:440626"
ORIGIN      
        1 maitlqsiee hvkkltsrap ftrdfffdll laygiskssv trlrsttass lnvaanperd
       61 ivwknkiyla etsndliata qemktseaal rfntrfviat nyealaaidt ktgdslsipl
      121 akladdftff lpwanmekqh fssdthadrr aaehmskvyd ellsanptlf hedksphsln
      181 ifftrllfcf faedtgiftk gqftsavgsh tqrdgsdtaa fltalfhald tpspadkpvy
      241 lqdfpyvngr lfrinnddaa sltvpqftkh ardsllelgt ldwseinpdi fgsmfqavvd
      301 kdqranlgqh ytsvpnilkt ikplfldelw reydkacesv prlkklltri skiklfdpas
      361 gsgnflviay kelrklehai ldridslssa grwgllgmge eeklgaatlg fgssvinien
      421 fygieiddis vemailslwi akhqmnqefk akfgldipli plketghivh gnatrldwne
      481 vcpnngtdei ylignppyvg ssmqsasqke dlasyfgeqk ysknldyisl wflkgadyir
      541 gtaaqlafvs tnsitqgdhv gllfpfvltg gieisyayts fkwsnnashn agvtvivlsl
      601 rnssdspkll fsdgiekqvk hinaylaegd dvivtkrrqp lshqlpqmty gskptdgghl
      661 tlepedvekl laaypesekf ikqyvgssey irgndrfclw ieddcvteaq hipaiakrle
      721 rvrderlrsk alstvefaeq phrfkqrsyk ptdsiivpsv sserrdyvpv gyldantvis
      781 nlafavydae pwlfalltsk mhmawlravg gqletrlrys ntlvyntfpv pelsasskee
      841 ltkralrvld vreyhcektl aelydpdlmp rnlreaheki deavdrlyks tpfasdeerl
      901 avlfakyqqm ieaegk
//
LOCUS       WP_284898513             658 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Actinotignum sanguinis].
ACCESSION   WP_284898513
VERSION     WP_284898513.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum sanguinis
  ORGANISM  Actinotignum sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 658)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Actinotignum sanguinis"
                     /db_xref="taxon:1445614"
     Protein         1..658
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=71519
     Region          18..598
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mkkhrdgsls qkapfknesy htvpwllaqr qrkhprdiav hiqnsiggnw kpltitefle
       61 qvrltarglv glglghgeri gilaatsyew alldaaalhi gvvpvpiyet ssakqiawmv
      121 adaeithift dtrahaelvd svtppaippa tvmtedwraa lnaaalevpe edleariaav
      181 tadslatiiy tsgttgdpkg velthgnfar tvlgtwhyep eilnnpqasl ilflpmahvm
      241 gricayfgla trisvgfvgn lknlmsdlet fkptlllvvp rvlekvynaa eakagagvrr
      301 rifrwaadia vqngtrrrrs pifavkrala rklvfnklre amggrirfai sagaplgtrl
      361 grfyrgiglt vvegygltet tgpanatraa npvlgtvgwp lpgmriklad dgevlvkghs
      421 vfrgyhnnpe atavafadgw fhtgdlgtld krgnltitgr kkhlivtagg knvapavled
      481 klsshplisn vvvlgdgepf isalitldaq mlpswlsshg lpkmtpaeam nseavqaslq
      541 raidrtnaqv sraesirkfv ivpgdfsean glltpslkvr revvleryrd vvdgiyganh
      601 sestkkseek errraarker raqrrlgrlr rrgaagqqgg rsgrqdgqqp gepgsaek
//
LOCUS       WP_284898612             347 aa            linear   BCT 25-DEC-2024
DEFINITION  lipid II:glycine glycyltransferase FemX [Actinotignum sanguinis].
ACCESSION   WP_284898612
VERSION     WP_284898612.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum sanguinis
  ORGANISM  Actinotignum sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Rohrer,S. and Berger-Bachi,B.
  TITLE     FemABX peptidyl transferases: a link between branched-chain cell
            wall peptide formation and beta-lactam resistance in gram-positive
            cocci
  JOURNAL   Antimicrob Agents Chemother 47 (3), 837-846 (2003)
   PUBMED   12604510
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Hegde,S.S. and Shrader,T.E.
  TITLE     FemABX family members are novel nonribosomal peptidyltransferases
            and important pathogen-specific drug targets
  JOURNAL   J Biol Chem 276 (10), 6998-7003 (2001)
   PUBMED   11083873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006395
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Actinotignum sanguinis"
                     /db_xref="taxon:1445614"
     Protein         1..347
                     /product="lipid II:glycine glycyltransferase FemX"
                     /EC_number="2.3.2.-"
                     /calculated_mol_wt=39136
     Region          1..332
                     /region_name="FmhB"
                     /note="Lipid II:glycine glycyltransferase (Peptidoglycan
                     interpeptide bridge formation enzyme) [Cell
                     wall/membrane/envelope biogenesis]; COG2348"
                     /db_xref="CDD:441916"
ORIGIN      
        1 mstlslsrid dttyldlaag hglpleqlpa wdryedalpg hapfgrflwr dsagaprali
       61 sltrmegrgf tylwakkgpv wlgerptage elefrtalaq lvrradrgla fmrihawhra
      121 pdlhellqtv tydrtvvvdv arpdaeiran fsksgrrqar kaeaeglefc deterarevf
      181 pelyailtet atrddfgaap msqyvtmles lgpdharlfv araegralaw qivlatddlg
      241 eayygatnae arqrhasmfm dmhtmtwlre tgrksydlmg vhserapqle gvtgykqkfa
      301 adftevagaw dvplrpryyr alklalhakr avartvraar erlgrsr
//
LOCUS       WP_284898615             337 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Corynebacterium accolens].
ACCESSION   WP_284898615
VERSION     WP_284898615.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..337
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36669
     Region          103..209
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 maveslaelk siiseqllkf grvneedape ekdsprlgia spaaasalqd dvadeivdrl
       61 kaekdksspg dsaldadaar tlplgartkp rgvfeddwga rpsderpwpv ilihgtcdtk
      121 gvwqimgnil rqdgwavfap dyghratqti pessqqlgay idtvlavtga ekvilvghsq
      181 ggllarywmr mdggaekvvh lmsisapnhg tthggiasrl irtqrqeavi rsiidgwfgp
      241 agmdqvvgse vlrdvnrdgd lesgvsytci atrsdavvvp petcfldpeg apegavrniy
      301 iqefdrhavv mhedmpmdrr vhaivrtllr mvehtpr
//
LOCUS       WP_284898667             476 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Corynebacterium accolens].
ACCESSION   WP_284898667
VERSION     WP_284898667.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..476
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=50901
     Region          8..407
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mkttthgals rlhkfagviv apflivaals gffyalaptl eqwvyhdeit ataqgsprsl
       61 ddqiaaaqrq hpgaavaave asedpeettr vlftdpdaks psythavfvd pvdlritgee
      121 qqyggsralp lrtwlsnghr tlwlgepgri yaelaaswlg altiagvylw lkrrkktqkk
      181 nnkalrvhar lgswllpgfl fltitgltws mvagsnigkv reelnwkeps vatsvaeaga
      241 gtgagegsga hagheghagh eghaghssge vtdndvlega qtalstarse gltgvlrmtp
      301 peqvgdawtv regraayklr sdavavtadg rvidrinsad wplaarltsw liqlhmgtlf
      361 giysqvalaa lalgllvisi aglwmwwnkp rrrlpelkit pavvagvviy siiaplfgas
      421 lllffagdwl vrrlrpqsrs rsgsqsgtgr sngvsgptar prgesssrip stvqng
//
LOCUS       WP_284898694             439 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: cation:proton antiporter [Burkholderia].
ACCESSION   WP_284898694
VERSION     WP_284898694.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 439)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 439)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..439
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46250
     Region          8..>432
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mhetlwylii gavlmamgva tsalrrlpcs tamiylalgv algpsgvgll hldiardarl
       61 lreivevall vslfaiglrl rvplsdklwl vpcrlgllam lvtvpllagc avltlgldwg
      121 palllaaila ptdpvlahdv qvhdpgdrdl vrfalsgegg mndgialpfa laglalcgvp
      181 dtphgpppls gtfalaalwg iagaaaiggl lgaattkaig rlrsryaqal gfegffalal
      241 ivlsfgaaqf ahtfgfiatf aagvamrrie hrasgdrppr evigqvdsed vsatekhpek
      301 vhafmaesvl dftieleria ealvmtmigs vlgtlsaplv twgaialalv lfvavrpfav
      361 lltltgshat laqrrlmawf girgigsfyy llfalehgps stvrplaapv lavvvasvia
      421 hgisatplmd wyyrlqhrr
//
LOCUS       WP_284898771             288 aa            linear   BCT 25-DEC-2024
DEFINITION  YczE/YyaS/YitT family protein [Actinotignum sanguinis].
ACCESSION   WP_284898771
VERSION     WP_284898771.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum sanguinis
  ORGANISM  Actinotignum sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Actinotignum sanguinis"
                     /db_xref="taxon:1445614"
     Protein         1..288
                     /product="YczE/YyaS/YitT family protein"
                     /calculated_mol_wt=29745
     Region          15..199
                     /region_name="YczE"
                     /note="Uncharacterized membrane protein YczE [Function
                     unknown]; COG2364"
                     /db_xref="CDD:441931"
ORIGIN      
        1 mdmhtvrepg qwtlrpgsll rrclvcligv cvtalgtait lkghagvdpf tamlqgvslv
       61 tglsfavvvp lvnigilafv ipfdrkifgl gtvlnftlfg vlvdgytvgl dalyvftysi
      121 pgmlahlaag llifsfglsl yitpdvgqga adgiapvlvr rfpqrsyrff rilqdftvil
      181 ialalyrgdl stgvigvgtv imvvgigvvv dffnrtvsvk lvgsasayta ppaplaaaep
      241 dgaepetapl aapappaapa laepgpapal aepgpapapa svtqrris
//
LOCUS       WP_284898774             817 aa            linear   BCT 25-DEC-2024
DEFINITION  glycyl radical protein [Actinotignum sanguinis].
ACCESSION   WP_284898774
VERSION     WP_284898774.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum sanguinis
  ORGANISM  Actinotignum sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Actinotignum sanguinis"
                     /db_xref="taxon:1445614"
     Protein         1..817
                     /product="glycyl radical protein"
                     /calculated_mol_wt=90197
     Region          32..817
                     /region_name="PflD"
                     /note="Pyruvate-formate lyase [Energy production and
                     conversion]; COG1882"
                     /db_xref="CDD:441486"
ORIGIN      
        1 mtaqlsgpah asasehasap ahapvlfrla pertaflnar mraavpsict erarivtesa
       61 rategepavl rrakalratl aqmsifidea elivgnhgst prsaplfpef gplsekeldl
      121 mpvrkvdtlr vtpeqkrell eeiypywvnr snedlarhll dpetnrvlds dnrpfdtrsr
      181 arsgyghyip hvrriinggf iaveeearar lnglergepd ysdrrvfyea ilivvdavri
      241 fqerfaalae dmasatrdag raaelriiae ncrqvpyrpa rtfweacqsy wfvmlidycs
      301 qngsaisagr fdqycypylk adldsgrltr peaqtildal wvkhidiika ctyssarnng
      361 gfstsvaltl ggvdengena vnelsymcld aeqavfnsep nvsirvshvt pdafldrvlr
      421 ilvtneggkd pffnddviip glvkhrhmsl tdardwaivg cveptgqgnt mgrtnschfn
      481 lakclelalh ngrcplsgdq lgprtgdftq mtsfdqvkea yaaqvdyfve mmvstlntie
      541 llharetphi yssavldgcl esgrdctagg ahydatgvng vglpdvvdsl eviremvfek
      601 ktmsaaqlle atasdfadev iqhrclnvpk ygndlswvdd lasfvtdqyt ssvyrfrsph
      661 ggyfipglfs lssntpmgrq vgalpsgraa rtplgdggis pkhgmdtngp tavvssvasw
      721 dhsaaingvn lnmkfvpaml kqpadrqkli dlirsyfvmg gmhiqfnils getlraaqre
      781 pekyrglvvr vagysaffve ldreiqdeii srtvqel
//
LOCUS       WP_284898935             314 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Actinotignum sanguinis].
ACCESSION   WP_284898935
VERSION     WP_284898935.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum sanguinis
  ORGANISM  Actinotignum sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Actinotignum sanguinis"
                     /db_xref="taxon:1445614"
     Protein         1..314
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=34753
     Region          34..270
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mnklkkwtvp dgweealcdw ektqtlaghr essrayriat lrsfartvdk ppnevteqdi
       61 idwasgkdia petrhgyyia iraffdwfsk gaspakvlgp vhrlratarp tpeavyedal
      121 dgapprtqii lrlagevglr aneiaqikke hlgkdllgyc lqvcgkggkt rmvplptdiy
      181 lemeeilnmt gtwlfpgskn ghlsaawigr larrelpdpw tlhtlrhrfa trayleghdi
      241 mavkdllghe svattqryvg sdphamrnam lgarqdryky caplpadtam pagtampana
      301 atlampapth ipgl
//
LOCUS       WP_284898973             119 aa            linear   BCT 25-DEC-2024
DEFINITION  FluC/FEX family fluoride channel [Corynebacterium accolens].
ACCESSION   WP_284898973
VERSION     WP_284898973.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   McIlwain,B.C., Gundepudi,R., Koff,B.B. and Stockbridge,R.B.
  TITLE     The fluoride permeation pathway and anion recognition in Fluc
            family fluoride channels
  JOURNAL   Elife 10, e69482 (2021)
   PUBMED   34250906
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Li,S., Smith,K.D., Davis,J.H., Gordon,P.B., Breaker,R.R. and
            Strobel,S.A.
  TITLE     Eukaryotic resistance to fluoride toxicity mediated by a widespread
            family of fluoride export proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (47), 19018-19023 (2013)
   PUBMED   24173035
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Stockbridge,R.B., Robertson,J.L., Kolmakova-Partensky,L. and
            Miller,C.
  TITLE     A family of fluoride-specific ion channels with dual-topology
            architecture
  JOURNAL   Elife 2, e01084 (2013)
   PUBMED   23991286
  REMARK    Erratum:[Elife. 2013;2:e01700]
            Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..119
                     /product="FluC/FEX family fluoride channel"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:1903425 - fluoride transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:1903424 - fluoride transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12974
     Region          5..106
                     /region_name="CRCB"
                     /note="CrcB-like protein, Camphor Resistance (CrcB);
                     pfam02537"
                     /db_xref="CDD:460582"
ORIGIN      
        1 mnlffvligg ffggaarygf trllpspyct fasnilgslv fglavgfaql adapfahplf
       61 alglagglst wstmakelge mvkqrhwwpl ckylfwtigi gvvlawrgvm waeliyhgi
//
LOCUS       WP_284899014             383 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Actinotignum sanguinis].
ACCESSION   WP_284899014
VERSION     WP_284899014.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum sanguinis
  ORGANISM  Actinotignum sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Actinotignum sanguinis"
                     /db_xref="taxon:1445614"
     Protein         1..383
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=41563
     Region          5..382
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mpktlsfatr vvndysasrp ddqyravipp iylastfeqp tdgsagpygy qrssnptrgs
       61 vesavayveg aehalafatg maatatvfss lttgdrvllt ssvyggtfll vdeffarrgi
      121 taefvddfne lteipedtam vflesptnpt lrvtdishva slakkvnakv vvdntfstay
      181 lqkpldlgad avvysgtkyf gghsdvlagf iltnddawya slkiaskalg nplspfdsys
      241 ilrglktlvi rldrqqenaa ilrdylehhp avsrvldpgw yspkekaihs rqskgdgalf
      301 afelaegidf hafaknlklm rfavslgsve tlichpasmi henlspeerd kagisdrllr
      361 lsvgiedvhd lkadlenals aid
//
LOCUS       WP_284899063             359 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)H-dependent flavin oxidoreductase
            [Burkholderia].
ACCESSION   WP_284899063
VERSION     WP_284899063.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..359
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=36166
     Region          14..357
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 msarafstpf serfglrlpl vqapmvgatt aamvaaasna galgslgaga feperlatev
       61 gairaatarp favnlfvlse aapdaasvar alaaidplna elglppgtap aryapdfraq
      121 ldalvalrvp vasftfgvld aadvarlkaa gtyvigtath vaeglawqaa gadalsaqga
      181 eagghrgtfi gsaddaligt lalvpqlvda tglpvlaagg imdgrgiaaa lalgaqasql
      241 gtafltcaes aiaadwkarl lassdtstqv traitgrhar glrntlmarl gervadaasy
      301 pvqnaltqpl rqaaarandg dylslwagqg aplarrrdaa lttsqlvdal daewraiav
//
LOCUS       WP_284899327             359 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium accolens].
ACCESSION   WP_284899327
VERSION     WP_284899327.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..359
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35985
     Region          50..350
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msattkdgqt iqtgstaqnp tatpvmargk grttflvali laslvlavas lalgsrsipp
       61 deviaalrga geqdirdivw nlrmprtfla yfagaalava gvlaqswtrn pladpgfigi
      121 tagasffval gtaigiattt gmrtalalvg agittllvla vsrrfqdplt lilvgagvsa
      181 algsgaviig lystdvldsm rrwtigstfg rgpedatiag iglliglaca amaarpldll
      241 amgeesslal ggspttarvg aalsvvvlag sataatgpia fvgfaiphiv rrvvgpsvat
      301 milpsallgg cavlaadiig rlivgnsele msivlaivga pfliwgahrg vgrawgdna
//
LOCUS       WP_284899563             684 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Corynebacterium
            accolens].
ACCESSION   WP_284899563
VERSION     WP_284899563.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..684
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=72599
     Region          30..515
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mqfrrigqlv aattvtaval sgthalaqed tttisvtnit dlhghledgl sdpakagdei
       61 gvarlqslik qvnegqkfnl tssgdnvggs afvsaisddk ytlealnamg mkvtavgnhe
      121 fdkgtedltd riepasdypi lganvlkdgk plldashvee idgvkvgyvg tvtqntkfkv
      181 saakipgvtf tdpveatnke atrlkesgea dvvvslfhed aeeyaegfnk dvdilfggdt
      241 hqttqgtver egalplqwaq gyeygkllnd adivydktak kvksielkqy dataaaqvep
      301 daeiagivkk aqdeaevegs ktagtvetdl frgsdegqks gsnrgvestl nnfiaegqry
      361 amskqvgedi dlgvmnaggv radlqggdvt ykdifevqpf gnsvitakvs gkdfitalen
      421 qwqegssrpr lamglsnnvq vvydykaaqg ervksvting epldpnkdys ialssflass
      481 dtekggdgyf eacsikdknd vgymdaqami dyiasgesev rkgqsqigah vdgdivpgke
      541 itvdlsslny tsegepmakt vtvklgdeek tadidnskqd gddqfgergr aqvtltvpkd
      601 ltgsqnleit tdagtqailp levgeaddde ddspkapqgs stggailaiv aalaagiafi
      661 glnpqvlpap lraifddlrk tfhi
//
LOCUS       WP_284899569             292 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Corynebacterium accolens].
ACCESSION   WP_284899569
VERSION     WP_284899569.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..292
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32110
     Region          2..274
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mtvgtisevl alegtqeadv fsgpaipsqi ertfggqvaa qalsaaqrtv dnkqvhslhg
       61 yfvgpgdtkk plelrverlr dgrsfasrqv rviqdgrlvf imlasfhrdg dtgpehqdma
      121 pqvlspdeaa rrgggapyst riilkewtdw dirlvpdegr ddaaaevtga gyrhiwfrnt
      181 gelgsdpdfh raaltymsdm tlirsaliph qgekiqlasl dhavwflrpf rvdewllyeq
      241 vsptasqgta iargklfteq gelvalvnqe gltrfldenl gsgsahgnwh nv
//
LOCUS       WP_284899635             322 aa            linear   BCT 25-DEC-2024
DEFINITION  DHH family phosphoesterase [Corynebacterium accolens].
ACCESSION   WP_284899635
VERSION     WP_284899635.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..322
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33892
     Region          7..319
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mtrkeyqdav daisgaqsic iithlrpdad aigsatalll amqqsgkdac avigqdkdfa
       61 pnlysipgad qvkvtrelpq rydlyvtvdc gsidrtglfs adiaelaaag rvlcidhhss
      121 npgfgsvnlv dsecesttva iltildmlsv qientiahcl yaglltdtgs frwgrpamhd
      181 vatrlmhygl dtkqiatdll dattpddlqm vgrvlaglri eyagelgigi liagladieg
      241 hsdsaveslv dfvralegtq lgvvfkeqsp giwavslrst aincaelaaq fgggghvpaa
      301 gymtsgsees ivaelvsaid eh
//
LOCUS       WP_284899650             451 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Corynebacterium accolens].
ACCESSION   WP_284899650
VERSION     WP_284899650.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..451
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48968
     Region          1..451
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mhlhhdyakh lpdlvsathg eeqpdpqlvv lneelavqlg ldtdwlrsae gldfllgrdg
       61 ghamaysgfq fgsfnpqmgd gramllgeve kdgklwdlha kgtgltpysr lgadgrgtls
      121 smlreylvse amhalgvptt rslavistgr piqrghvqpa gvlvrvaash irvgtfhyaa
      181 qsghlqalad yaiarhypga dyreffqgvm drqiatvssw mrlgfihgvm ntdnttisge
      241 tidygpcafm esyspdtvfs sidqqgryaf gnqpailgwn larlteslvp lfdadinagv
      301 dfaqetingf qekfatqrrs diaaaldttt evasaylaam qlsrpditla hraladaarg
      361 htlpaqelfp dsdfldsyla ihpapdavda amprviprnm aveaalraae tgdmqpftel
      421 lhavthpwqp hpsyeqpdpn glagfltycg t
//
LOCUS       WP_284899877             513 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium accolens].
ACCESSION   WP_284899877
VERSION     WP_284899877.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..513
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55995
     Region          169..510
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 madsqenpaa grpaqaqsqp qraqqpqqpp kkwheqldql pqqgqgkkkr skrdyikqip
       61 qamplrtwlv vllvvisglg ltgssfavns imrnvlynnv dselrsasss wardvgndff
      121 lgdhtkrppt eyvvlnylpd gtirysgpts ttpdvegvpl ggypttvgsi enntkwrala
      181 fadsngvitv iakdmtheke ilhglamvqv siaaialaam agvgfwfirr alrplrvves
      241 taseiaagdl dkrvpewplh tevgqlaaal nimlghlqrs vvtaqekeeq mrrfvgdash
      301 elrtpltslr gytelyrsga tndvdlvfsk idkeskrmsl lvedllaltr aegtrldlrp
      361 vdllelslsv gssaraafpe revkvvnnaq sipvvngdad rlhqvllnli snglrhgged
      421 atvalqlrrd nkdilvdvid dgkgmsseda ahiferfyra dssrtrdtgg sglglaivhs
      481 lveqhggsis vdsklgqgtt ftvrlpalee ped
//
LOCUS       WP_284899890             392 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Corynebacterium accolens].
ACCESSION   WP_284899890
VERSION     WP_284899890.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..392
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42455
     Region          125..387
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mkivarllsv plslvaflal wlavapftph ipywgagali gpqyigpvli fslillvlav
       61 lgrfgsrsfy vpgafaaval iagtalfgtq ihaakeqgtd vdiratlswa gvestdegpd
      121 htvaydsfhg edldmdiyvp kvggthpvmm yvhgggwdqm nkhsqafnmr qmaqrgylvl
      181 sidytlsswg qptwkvvagq vgcamnwvna haadydgdpg rfftygesag gqlvlnatad
      241 aaahpnhlps adcpgtpavp ravyadspal dvrhiydsdd pyaaqgsrdt vqkylggtpe
      301 eypdradfvt sathlttdmp pikivrsdnd rlvppesydd frriaqekni dlseyvrpha
      361 dhasalsahg vwnqhllqam pqffaehdpq gs
//
LOCUS       WP_284900020             258 aa            linear   BCT 25-DEC-2024
DEFINITION  inositol monophosphatase family protein [Corynebacterium accolens].
ACCESSION   WP_284900020
VERSION     WP_284900020.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..258
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=26929
     Region          5..252
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mmdprelvaf aeaavdqvep ifrsgigapp ahfksrgdfa tevdlaiekq lrdilqqmtg
       61 ipvygeesgg sihdtvwvvd pidgtanysa gnpmagilva lvhegqtvaa isdfpllgrr
      121 lvasdgsplr saggpsggfg ggeespefdd arghvgcfsn lptaafhelr esglrpritg
      181 svgldnafva qgvfdgavnf sphpwdnaag allikaaggi itdpegnpwt vqsrgmvsgt
      241 pqvhetilei lshhsnyp
//
LOCUS       WP_284900116             280 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase, partial [Burkholderia sp.
            lyk4-R2A-23].
ACCESSION   WP_284900116
VERSION     WP_284900116.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. lyk4-R2A-23
  ORGANISM  Burkholderia sp. lyk4-R2A-23
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Burkholderia sp. lyk4-R2A-23"
                     /db_xref="taxon:3040284"
     Protein         1..>280
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
     Region          7..277
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mkesdsrfrg wllretgidp dslgndflsr altervhalq gdgerlpsaa rppvtpeald
       61 aywqqlnasa derralielf vvpetwffre reafvtlarl averlaatpg rvirvlsapc
      121 stgeepysaa malldagldp asftidaidl saraieqarl gcygrnafrg tatefraryf
      181 tpaadgwlld ervrarvqfr qanliepgvd tgirydfvfc rnvliyfdrd aqdrvigsle
      241 swladdgmlf vgpaetgvam rhglrsarvp lafafhrdhg
//
LOCUS       WP_284900158             753 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: xanthine dehydrogenase family protein
            molybdopterin-binding subunit [Burkholderia].
ACCESSION   WP_284900158
VERSION     WP_284900158.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..753
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=80622
     Region          66..>186
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          200..753
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mnapddideg rrhfmvsgal fvafslapaa raaaevviad egaavhvsra tetlagslkt
       61 nplldawiki tpdgkvtvft gkvelgtgvr tallqvaaee lnmkpslitf ltadtgaspd
      121 egltagshtm adsgsallna aaqvrgllvd gaakqfgvdp rtltvadali kapdgrtmry
      181 gdavrtvdlh rnatptsplk ppatfavigt slprvdipnk vtggasyvqd melpgmlhar
      241 vvmppvydak llsfdeaail kmpgvvrivr ngsmlavvaq gewqavvaqr alaaacrwsp
      301 grtlperntv hedlkristq hieianthap aapavktlsa tflknyllhg sigpscsvar
      361 lengmltvwt hsqgvyplrd alaemlsmpk anvrcihteg sgcyghngad daaahaalia
      421 aampgkpirv qwmreqehtw dhftpamvte lsasldasgr ivdwkyalws sshnerivna
      481 grllparmle ppfvpapstp mlqpegggdr naiplyalpn lhivnnfspt mplqtsamrs
      541 lgahtniwsi esfmdelaha agvdpvefrl rhmqdhraqq viklaatkfg wprpprarnr
      601 gvgfafgkyk nlmayvamai eisvvpetgq vtldhaevav dagqvvspdg irnqieggiv
      661 qaaswtlyea lkydtqrirs fdwssypilr fsaapqsvkv hlinrpgapf lgaaeasmgp
      721 tagalanaif datgqrprem pfagdglrkr ida
//
LOCUS       WP_284900168             121 aa            linear   BCT 25-DEC-2024
DEFINITION  Rieske (2Fe-2S) protein [Corynebacterium accolens].
ACCESSION   WP_284900168
VERSION     WP_284900168.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..121
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=12655
     Region          34..118
                     /region_name="NirD"
                     /note="Ferredoxin subunit of nitrite reductase or a
                     ring-hydroxylating dioxygenase [Inorganic ion transport
                     and metabolism, Secondary metabolites biosynthesis,
                     transport and catabolism]; COG2146"
                     /db_xref="CDD:441749"
ORIGIN      
        1 mticsrrmfl lgsattfaga yltacgseps aeiaatdipv gsgiivdgvi ftqpkegefk
       61 aysqtcphqq npiteidgmt atcpahhtsy nlqdgsvieg pgrdplkeye vsqegskvst
      121 a
//
LOCUS       WP_284900186             504 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: aldehyde dehydrogenase family protein [Burkholderia].
ACCESSION   WP_284900186
VERSION     WP_284900186.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..504
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=52623
     Region          19..491
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mtqhadqllt afahffpgaa tigsyidgel vagqgdtiql ydaatgeatl ayrdagaavi
       61 dhaaesarra qrewwaltha argrvmqeva rairaeaeai arlealgsgk pirdcrgevg
      121 kvaemfeyyg gwtdkfygsv ipvptshlny trrepagvvl qitpwnapvf tcgwqvapav
      181 amgngvllkp seltpftsla varlgeragl prglvnvlag fghtagqaai ahrvvskvvf
      241 vgspatgari aeaaarrvlp cvlelggksa nivfadadlk raaltaqaai fagagqscva
      301 gsrllvqrav ydefvamvaa gakkirvgap lddatevgpi nnrkqydhvm smiargvaag
      361 atlacgsaer vgegggyfva ptvltgvsna mevarteifg pvvaaipfdt edeaiaiand
      421 tdfglagaaw ttdvarahrv aaqvnagtfw vngyktinva spfggygmsg ygrssgveal
      481 yeytqtksvw vetaeappta fgyl
//
LOCUS       WP_284900201             157 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Corynebacterium accolens].
ACCESSION   WP_284900201
VERSION     WP_284900201.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..157
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17386
     Region          66..156
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 meiratqesd rtyiarlnfl tdtfgderge lssgfaddfs fyvenwepnq ggfiawedlv
       61 paggvwlnwg tednhgygfv epsipefaia vesrfagqgi atalidaais laqtlkapgi
      121 slavhpdnpr alrlyerlgf ehvgvyaehy imvkrfl
//
LOCUS       WP_284900222             454 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Corynebacterium
            accolens].
ACCESSION   WP_284900222
VERSION     WP_284900222.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..454
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=48372
     Region          5..241
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mtlklnffak sdrglirgnn edsgyagshl liladgmggh aagevasqlm vnhleildqd
       61 pgkedteall aaaaddanea isehvtahpe tegmgttlst mlfngttfgv chvgdsrayl
      121 lrdgkleqit kddtyvqslv dkgelaaedv sshpqkslil kaytgravep tlftfeakag
      181 drillcsdgl sdpvtastie talgqgsieq agstlvdlai rsggpdnvtv vigevteekp
      241 athepfrvga lagsveepth pdssasraak ltrkpqvipp avmadednaa kdsdeeeaed
      301 epsrrkvgwk llialiiila lvigaglwvk nflsnnyyae tndaqeitil kgadysvfgk
      361 dlssthqyvc indknsllfs aqkckgdftp lkvsdlpese rgavnhisag dlskvqdqin
      421 dlgekalkpc itapsqkdnk dtkenkpgvt crev
//
LOCUS       WP_284900450             543 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Corynebacterium
            accolens].
ACCESSION   WP_284900450
VERSION     WP_284900450.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..543
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=59234
     Region          6..215
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mnaatnflyr qithigrglt laqglqmrls geenipddgg avlvcnhtgy mdflfgafia
       61 yrkkrlvrfl akasifstpg vgallramgh vpvdridgke slrkavelae agelvgvfse
      121 gtisrsfeir smktgasria feagvpvvpq vmfgsqrlwt kghkknlgrt ktpvfitale
      181 pyyptgdpea dtaeirrrmq ealeglwedy eaefgpmpag eywvparkgg saptleeaea
      241 rdaeveterh rvrrlrddlv glkdrvsvst velvrnhmas akdeegqdeh dgkepqekkh
      301 iaadtlewvk tnlnavveea trgldegkdk vadvmaqlkt dvaqaqasia asskeiwegs
      361 vveqgllaaa tqsrlivsrl phrlkaqfsa iprvvvahqs tlnweddalt prlkaalesi
      421 ypaaevlivv scdadldvpq avwhiqldeq aekplldkea mkvtsataaa gvdcilddld
      481 akpsealvfg nepgdegfln hipvvaleta pievvkdaqa vtysaeragm sevleamarl
      541 qkd
//
LOCUS       WP_284900651             101 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium
            accolens].
ACCESSION   WP_284900651
VERSION     WP_284900651.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..101
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10701
     Region          17..74
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(21,25,50)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(24,49)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(31..32,43,46,50..51)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mttsfasggk ipewntadrv rkaresagmk qdelasrigm srgglakieq gksaprrtti
       61 iaiafatgva lewleygetp apdnpgggev vrhqgieprt h
//
LOCUS       WP_284900654             514 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Corynebacterium
            accolens].
ACCESSION   WP_284900654
VERSION     WP_284900654.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..514
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=54837
     Region          1..472
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 manfldalns iiwspalvfl clgagvyftv vtrglqvrcl pdmlrqiskg eksddgvssf
       61 qslmvslsgr vgvgniagvs taiafggpga vfwmwavall gsstsfiect laqiykekdq
      121 dtgeyrggpa yyiekaykht kaapfmmvyg ilfaiamila tsyflpgiqa navaaaadta
      181 wgvnstwaav vlagilaiii iggvkrianf atlvvpfmav iyigisivvm linysqipev
      241 fglifksafn leagfsgmlg vaimwgvkrg iysneagqgt gpqsaaaaev shpakqgfvq
      301 sfavyidtlf vcsatafmii stdmytvfrg esedgevvyq gslpddvavg pgfvqsglds
      361 vfagwgptfi avsiaffaft tvlayyymse vnltyfnrwv ksrpirrglv walriliivs
      421 vivgatttpg sawalgdigv gttawlniia ilflqapaik vlkdyekqkk agkdpefdpe
      481 avgiknadfw vdrknaraaa qaaskqaade naes
//
LOCUS       WP_284900710             370 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium accolens].
ACCESSION   WP_284900710
VERSION     WP_284900710.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..370
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=38288
     Region          25..368
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mrrnkaaqav qdkqntpwqm pggvpfragp isflwrprvv lvcviaaali vflgalsigl
       61 gdypisvprv levifqgegs rverlvvlew rmprvataia vgcalglsga ltqtvtrnal
      121 aspdilgitt gasamavtvi vlgsgggfag wlagigipla allgailsat viwalawrrq
      181 adsyrlvlvg iiitallssy inflmvrael rdasqaqfwl tgslarsews ttipiavlvi
      241 vcapllawia yqalattlgp dlaralgqrv navqvamlal avalaavavs aagpigfiaf
      301 vapqvalrlc gvpspplaas altgavlllg adivtqavlp velpvgivts alggifliyl
      361 lvqrtrstda
//
LOCUS       WP_284901000             284 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FAD binding domain-containing protein [Burkholderia].
ACCESSION   WP_284901000
VERSION     WP_284901000.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..284
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=29481
     Region          1..271
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mnylrantid evlgrlaaqp rprivcgatd afadiglvpa rsawvdisrv dalraieqhd
       61 gvirigaast weaiarttwl pvaltaaaac vgprqirvqg tiggnvchas pvadgipall
      121 aldarvelas lrgvrrlpla efllgngrta lhadellvav lfapprahdr tsfikctnrd
      181 gtaiavvsaa aqlrvgtdgt vdavavaigg asdvarrmpa leaalagrrl delagviaaa
      241 plaelspvdd cratalhrih larlavtraf tccieenarg asta
//
LOCUS       WP_284901112             335 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Actinotignum
            timonense].
ACCESSION   WP_284901112
VERSION     WP_284901112.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum timonense
  ORGANISM  Actinotignum timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Actinotignum timonense"
                     /db_xref="taxon:1870995"
     Protein         1..335
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34940
     Region          22..324
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 msdsaaqqhq hngypegqrq irrvvlltnp tagkgratsl aahitaellk hgvdvvgnya
       61 ttvaetrkna raaladpgid alvacggdgl anlivqeqag tgkplglvag gtgndiargl
      121 gipldvagaa rtiasgytlm tdlglatrev ngvsqperry fasilaagid trinarakei
      181 rwpggsaayf lavlaevaam rtapltlsid ggepftleat lcavgntrsy gggirmcsha
      241 dprdgklalt vvgpvsrrta arnlrniytg dfsklqdivt qiqvnsvrle mpdlipavdg
      301 edlfptpltv tvaagagcfl vppprqyrsq thktn
//
LOCUS       WP_284901141             277 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Burkholderia].
ACCESSION   WP_284901141
VERSION     WP_284901141.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..277
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30448
     Region          84..269
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          211..267
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 msaalstpdl plshvafvtd tlgdiaqaig tpqfmravyd tlvryvdfda vhldyersaa
       61 sgrrsvgwig sfgrepelva qvmrhyyrsy asedltyaai asesdtqllq vssqrvasel
      121 rhlffdagdi hdecviagvt ggtrysisia rsrrlppfsl kelsvlkqls qvvlpmasah
      181 krllgavcad egprdeldld rvaqwlpelq erltaremhv casfiqgmts aaiaqsmglk
      241 tstvdtyakr afaklgvdsr rqlmalvlrn asrrhda
//
LOCUS       WP_284901222             420 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: saccharopine dehydrogenase family protein
            [Burkholderia].
ACCESSION   WP_284901222
VERSION     WP_284901222.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..420
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45289
     Region          1..417
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 mtqpthdldl vvfgatsfvg qiltrylsey lsgsgetlrw aiagrseakl rhvrdalgaa
       61 wqtlpiivad aaddtqlqal cartrvvvst vgpyalygep lvricaqtgt dycdltgetq
      121 wikrmierye paarqsgari vhccgfdsvp sdigvlflqq harrqwgvpa tqvkmrvktl
      181 kggasggtva svinvvreaa adpalrrall dpyalcpaeh rftvrqhavr saefdrdggt
      241 wiapfvmaav nervvhrsna laddaygsrf aydeavitgt glkgrlaalt mvaglgafma
      301 gvlippvrgl merfllpkpg egpsvaaqla grydlrffgr addgrtlrvk vtgdrdpgyg
      361 stgkmlgqaa lslaldctrd gaktgrgggf wtpatmfdar fverlerhag lrfellppda
//
LOCUS       WP_284901312             213 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: antibiotic biosynthesis monooxygenase family protein
            [Actinotignum].
ACCESSION   WP_284901312
VERSION     WP_284901312.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum
  ORGANISM  Actinotignum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Actinotignum"
                     /db_xref="taxon:1653174"
     Protein         1..213
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23784
     Region          3..99
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
     Region          124..211
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mtvvkinais vpegagehfe arfaaregav dqrpgflsfr llrplneger ylvvtewese
       61 edftawcsdp tahprkmeen rhaaahadls aqllefdvvn lpevehgetp qagfvslval
      121 sflpgmekvi eqrfaarkaa vdaapgfsff elwrpvrgve eyyvvtgwds qdsydawaea
      181 reraphntad qpknrgldvt lhgyavvqqs tkr
//
LOCUS       WP_284901333             413 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: citrate synthase family protein [Burkholderia].
ACCESSION   WP_284901333
VERSION     WP_284901333.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10578585
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..413
                     /product="citrate synthase family protein"
                     /calculated_mol_wt=44100
     Region          4..52
                     /region_name="HTH_17"
                     /note="Helix-turn-helix domain; pfam12728"
                     /db_xref="CDD:463684"
     Region          60..379
                     /region_name="citrate_synt_like_2"
                     /note="Citrate synthase (CS) catalyzes the condensation of
                     acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form
                     citrate and coenzyme A (CoA), the first step in the
                     oxidative citric acid cycle (TCA or Krebs cycle).
                     Peroxisomal CS is involved in the glyoxylate...; cd06102"
                     /db_xref="CDD:99856"
     Site            order(60,214,217,247..250,252,255,281..288,291,296,323,
                     326,328,349,353,369,372)
                     /site_type="active"
                     /db_xref="CDD:99856"
     Site            order(60,247..249,252,255,281..288,291,323,326,328,369)
                     /site_type="other"
                     /note="coenzyme A binding site [chemical binding]"
                     /db_xref="CDD:99856"
     Site            order(60,214,217,248..249,281..282,284..288,296,326,353)
                     /site_type="other"
                     /note="citrylCoA binding site [chemical binding]"
                     /db_xref="CDD:99856"
     Site            order(62..63,65..69,214,218,221..222,225..226,229..231,
                     235,242..243,246..248,288,369..377)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:99856"
     Site            order(214,217,249..250,287..288,296,328,349,353,372)
                     /site_type="other"
                     /note="oxalacetate/citrate binding site [chemical
                     binding]"
                     /db_xref="CDD:99856"
     Site            order(249,287,328)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:99856"
ORIGIN      
        1 mhnwitltea arrlgvraqt vyayasrgsi avmqdpddpr kslyraedvi alcrkkqvgr
       61 kraalaasti fgaepcipsg ittfskgraw yrgrdsiqls dtatleetaa llwqattpvt
      121 fdapavalpa gerdrqcaft mlatlaahgh stlgrldsal hteagqlvai varafgaqdd
      181 gglpwthqrl aagwgldgrg adllrramvl vadheitssa faaritastg aslagclltg
      241 latlsgplhg dasgrvravf ddverlgaah vvdhhlksai pipgfghhly pdgdpraaal
      301 larldppael arfidkvttl tgqrptidva lamlsvqlrl prdaafglfs iarsvgllah
      361 cieqlrvgkv irprsrytgp alderhllpk aeddgklpka gvieknrvfk ivd
//
LOCUS       WP_284901337             320 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: 2-hydroxyacid dehydrogenase [Burkholderia].
ACCESSION   WP_284901337
VERSION     WP_284901337.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..320
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=34111
     Region          63..313
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(79,107..108,111..112,114..115,118,122,124,132,134,
                     135,138..144,146..150,168..169,172..173,269..270,277,
                     283..289,291..294,296)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(80..82,105,240,287,290)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240626"
     Site            order(81..82,109,158..162,180..182,185,212..214,238..240,
                     264..265,287,289..290)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 mpdnnrprll varrvpaava araeaefhay vtdadmdaps vvefcnryat pavligkksg
       61 lqaehiaalp psvkiianas agydhldvaa arergivvsn apdaltdcta dftmllilaa
      121 crraseyeri vragwgksfg mtdmlgtrvn gktlgivgfg rigravaqra rgfgmkivyt
      181 drrpappeve agarycadld tllpqcdilt lhvpgggtpl mtrrafglmr dgavfvnaar
      241 gslvdedalh ealtshrlfg agldvyrnep didprfaald nvflsphmas atietrdqmg
      301 ftaldnvaav ldgraapnal
//
LOCUS       WP_284901421             498 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: aldehyde dehydrogenase family protein [Burkholderia].
ACCESSION   WP_284901421
VERSION     WP_284901421.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 498)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 498)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..498
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=53376
     Region          14..496
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mlslvptldr lnvrpgrlfi dgqwldwpda rfdqfnpntn evmtsfadag prgvdlavaa
       61 arkafddgpw prmraqdrkr llqpivdrly aaeeeiarlq tldngipytf srnsrvsaka
      121 aadifdhflg widkingetl pifsgasnmq ymtfrdpigv vaavlpyngp vmtfamkvap
      181 alacgctviv kpseltnlav srlaqilaes dlppgvfnlv tggietgtal tshagvdkvt
      241 ftgsplvgek itvasaptmk rlslelggks aalvfpdtrs vqataqalmg lcstflsgqv
      301 cttpsravvh rsimdeflqh aqaqlgkvrf gdpfdaatts apmisrrhqa rvldyvesgr
      361 qqgakllagg gmpggefgng nwvepalfad vrndmkiaqe eifgpvlsvi pfdteeeavr
      421 iandseygla gcvyttdvsr afrvaravks gsigvngfas ipnapfggik rsgvgreggw
      481 stieaftelk tinfnlda
//
LOCUS       WP_284901440             865 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Actinotignum timonense].
ACCESSION   WP_284901440
VERSION     WP_284901440.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum timonense
  ORGANISM  Actinotignum timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 865)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 865)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..865
                     /organism="Actinotignum timonense"
                     /db_xref="taxon:1870995"
     Protein         1..865
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=95049
     Region          3..863
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtdllledyr esyasrgihl ddfqleacaa lgrghdvlvc aptgsgktvv ahyavylala
       61 sskkciytap ikalsnqkya elareigeeq vglltgdqsi nreaqilvvt tevlrnmllh
      121 espdildvgy avldevhfla dpdrgpvwee tilslpehvr laalsatvan teelaawmrs
      181 vrgptdvvvs tkrpvplaqy vnvgrklfpl yradtlepdp alvnalgrls gerkkrvsdr
      241 erraiidklg ergmlpaief ifsrkgcdka veallrhnev lttraqradi kqeiaalret
      301 ltesdrravh feraaaaler gygahhagvf paikelterl mergllsivy atgtlalgid
      361 mpvrtvvlee lqrwdghgfv dlsateytql igragrrgrd tvgygvvvad adtdpeylad
      421 lasgrvepli safqpsyntv tnllarmsya aardlmgrsf aqfqrnaelg glaarrariq
      481 rrveteetrl scsrgdlldy lrlrgnagra akaerkaakr ryreriaksf aavrqgyvya
      541 yamgtdlvya lvlsaapdrv rvidwfgdla wlyedslase mreigpvtvp fgmstkkavv
      601 reqiaedild lvggradlgi drdllaswar fatprdpkva ahpvascphl yahldnaqtw
      661 vslhhrieei dqriaaftds agrefdataa vlrevgvlqg dndairmgpg aaqlrelhte
      721 adllmyqcla qlpegsldap alagwvsmfl aderlgtalp rdtrlcdaar varaevqylq
      781 sleyqhgitr tpdlspgcad vfaawaggvg leaclesahm tagdfisaar riidvlgqvt
      841 vategtwlsd iarqardlmg rselm
//
LOCUS       WP_284901513             263 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Burkholderia].
ACCESSION   WP_284901513
VERSION     WP_284901513.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..263
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29020
     Region          104..258
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 msgtaiesnh sldnligaig saafaeriga tlrelcgael afifrladsi pvefasigcd
       61 gsnrvehvrd tylggkwwqf ddeinelgts dgdacrlfkt dfklsasprl rqalygelni
      121 rervlmcsri dgaplvlgit rseqngpfat rhmdalaera atllsivarh cdlamrarrl
      181 pnlltdlvei erqialsger mtaresevca rylyglstsg iaadlgigte tvvtyrkrly
      241 erlaigshre lllwyldlcs qlh
//
LOCUS       WP_284901547             388 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [Burkholderia].
ACCESSION   WP_284901547
VERSION     WP_284901547.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..388
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41204
     Region          9..386
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 msaapsrcgp lagikiveia gigpgplaam fladlgatvi rvdrkepsgl gaprpvqfdl
       61 glrnrksirv dlkdpaavem vleliaeada liegfrpgvm erlglgpepc lsrnarlvyg
      121 rvtgwgqdgp laqvaghdln yisitgalha mgragqaptp plnvlgdyag gslylafgll
      181 agileargsg kgqvvdaamv dgvasimtvt mglhaagmld kargtnlldt gapfyevyac
      241 adgkyvsvgp iegkfyrlll eklelqdhpm lqaqmdrahw pdakqilaak fkertrdewa
      301 qllghldvcv apvldfdeap dhphvkargt fidlngvthp apgprfsrtp aprpeapatp
      361 ttdnaiaalq dwlpdvqiea yrargifi
//
LOCUS       WP_284901771             400 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein, partial [Actinotignum timonense].
ACCESSION   WP_284901771
VERSION     WP_284901771.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum timonense
  ORGANISM  Actinotignum timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Actinotignum timonense"
                     /db_xref="taxon:1870995"
     Protein         1..>400
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
     Region          39..398
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mpqssrttss plpaagtsap gtpaqaagrp aqaarpeqpa prttrirald giralaiiav
       61 vlyhmrpall tggfvgvtvf fvlsgflitr svlrelsrer rfsyrrylrr rflrlwppvl
      121 vtiagaalls yliapsllpk vqadalpaal fasnwvyifr evpyfaasgl psplthlwyl
      181 gvlaqfyllw pfillalrrv rystlrivag lalasallma vlffagpdst rayygldtra
      241 aelligalaa lvspyvaslw pradstttpq ppthsataaf alrvgtgaal lallalavwa
      301 dgesaltyag gltttallta livltvhnpr lglsrvlasa pfayvgsrsf slylvhypll
      361 llmnpatrta eisgaakigq llvvglvael fyrcveqpsa
//
LOCUS       WP_284901774             276 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase, partial [Actinotignum
            timonense].
ACCESSION   WP_284901774
VERSION     WP_284901774.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum timonense
  ORGANISM  Actinotignum timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Actinotignum timonense"
                     /db_xref="taxon:1870995"
     Protein         1..>276
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
     Region          4..268
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mkstpashtq ltraarlhrp qqrerfrqtl vegpgavqel lahranlvrd vyytkaslis
       61 npelgdlikn agvyhhplna deiqalseda rgvvavidip etpaltptvk eaklvlatan
      121 iqdpgnvgai iraadvagcd avllgrgsve lwspkvirss agsifhlpvl dsinvskldg
      181 vleragisfl aatgegewdl atlvasanda aylgqpplgp dltrpvcwll gneahgfadv
      241 danvdatvai piygkaescn vamaaailss ttamiq
//
LOCUS       WP_284901896             342 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Corynebacterium accolens].
ACCESSION   WP_284901896
VERSION     WP_284901896.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..342
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37145
     Region          75..337
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mtlillvlaa lgrlgsrsfy vpgafaaval lagialfgtq ihaakeqgtd vdiraalswa
       61 gvestdegpd htvaydsfhg eeldmdiyvp kvggthpvmm yvhgggwdqm nkhsqafnmr
      121 qmaqrgylvl sidytlsswd qptwkvvagq vgcamnwvna haadydgdpg rfftygesag
      181 gqlvlnatad aaahpnhlpt adcpgtpavp ravyadspal dvrhiynsdd pyasqgsrdt
      241 vqkylggtpe eypdradfvt sathltsdmp pikivrsdhd rlvppesydd frriaqekni
      301 dlseyvrpha dhasalsahg vwnqhllqam pqffaehdpq gs
//
LOCUS       WP_284901857             489 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: aldehyde dehydrogenase family protein [Burkholderia].
ACCESSION   WP_284901857
VERSION     WP_284901857.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..489
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=51841
     Region          14..488
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 msvnipnfvq gnkklliggk wvepaggehi eainpatgev lcqiakggtq dvdravaaar
       61 cafegpwsrf tpherrklll rvhdvildhf delalietld mgaplartrg ykewlsqllq
      121 fyasqtgaga vqtapmsiap gftalkqlmp vgvvggiipw ngplmglwwi ygpalatgct
      181 avlkpaedas lsslrvselm meagvpdgvi nvvtgygkdv gqalaehpdv drvaftgsvg
      241 taqaivrasa gnlkrlqlel ggkspdivfa dadldkavpg aamgvftntg qvcvagtrif
      301 vqrtihdefv qriaafakti rigdglapdt qigplisqrq lervmhyvdi ggkeaslvqg
      361 gqrpggalar gyfveptvfa nvsndmtiar eeifgpvasv ipfdtmedal qlandtpygl
      421 aggvwtnsls tahkvsqgir sgtvwvncyg vidpavgfgg tkmsgygwkg gkehvesfly
      481 pkatyinlg
//
LOCUS       WP_284901927             230 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Corynebacterium accolens].
ACCESSION   WP_284901927
VERSION     WP_284901927.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..230
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24529
     Region          1..227
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(13..14,16..17,20..21,58,62..63,66..67,91,95,102,
                     105..106,111,126,130..131,133..135,137..138,141..142,
                     145..146,165..166,168..170,172..174,176..177,179..180,184,
                     187..188,194,196)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(129,133,136..137,139..140,179,182..183,185..190,
                     193..195,199,201)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(150..157,167,170..171,174)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 myrlhpstvl tiaacgwlli lalntplasa vvagamlayg vwatrslaiv lasaalcvpv
       61 alsmlvihap ygdnqlipli tsdglliaat lalrffalmv cfivamsvlr isdiakwlqv
      121 sraghkiayi vgaslqslpq gaqawqtvrd anqlagikvt wrntisrvvi pvisrlliqg
      181 terghalaav gfdeegtrtl lrpvpdsavs rvlryiipig tigvmvfvwi
//
LOCUS       WP_284901915             938 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium accolens].
ACCESSION   WP_284901915
VERSION     WP_284901915.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..938
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103785
     Region          4..936
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtethldtfa aglpypldef qvqgceaven gqgvlvcapt gagktvvgef avslalsrgt
       61 kcfyttpika lsnqkyhdlv aehgddavgl ltgdvsinad aeivvmttev lrnmiyadsp
      121 aldrlthvvm deihfladas rgavweevil nladhvsiig lsatvsnsee fgewlatvrg
      181 dtsvivtehr pvpldqwmml grkiyplfep esggqvnsel erriqrleag dsddgrayyk
      241 sgkgfrarar hkgggrsefh gkaggrsgss rpqdryrplg rpevlkvlqs qdmlpaitfi
      301 fsragcdgal yqclrsrmvl ttqeeaeeik aivdagvegi peedlqvldf rrwrealsrg
      361 faahhagmlp afrhivedlf vrglvravfa tetlalginm partvvlekl ikfngeahvd
      421 ltpgqytqlt gragrrgidt lgnavvqwap amdprfvagl astrtyplis tfapgynmai
      481 nllgmlgfed slrlleksfa qfqadgsvve etreleraeh rvrelreqld davdalappa
      541 kdgedpaevl mdyirlrrel taeekqskvd kehqrtqevi avlarlqlgd viaiagkkrp
      601 tlaavvtpan qtedprpwvt tesgwsgrid atgisnppiq lgrikipkpv rknprrntky
      661 iqdvfrrekf drpkrmkskp rlrpnkrvge lrdairehpa hkwpatdreq lagvaqklar
      721 rerdleklqa kvdkatdtlg rtferivdll aemdyvefsg vcsdrtpvit eegerlakih
      781 sesdllvaqc lkrgiwdeld paelagvasl ccfenrkatg gqpeaatdrm adamnatwri
      841 ytelsaderr hrlpptrepe agfalaihqw sagaplgycm aaaneagael tpgdfvrwcr
      901 qvvdllqqia ktgydgqiqr narraidaiq rgvvaiga
//
LOCUS       WP_284901932             245 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Corynebacterium
            accolens].
ACCESSION   WP_284901932
VERSION     WP_284901932.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..245
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26413
     Region          16..235
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mansqraaaa hvavkesrst dgdtrrqvll lllkdgpvta sylgerlgls tagirrhldi
       61 lveeeltevv errpasrsrm hsgagrgrpa khfrltdrgr aqfghaydel asealtalrs
      121 aggseavknf akarferiia dvrplvdaee sveevarkla etldkhgyaa tvdragqgvq
      181 icqhhcpvah vaakhpelce aeqevfsall gkhvqplasi adghgicttn ipltpvktnt
      241 erses
//
LOCUS       WP_284901946             600 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Corynebacterium accolens].
ACCESSION   WP_284901946
VERSION     WP_284901946.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 600)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 600)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..600
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=66626
     Region          11..470
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 maeatpkslw lshltirnfr sckktevkfq pgvtllagen nagksnivda irlgldplsg
       61 ratryfeadd ltedaagpid ialefkdptd fqkalfingl dlktetiqyq tsylpptqqi
      121 prgkrvrtag eprgadsdfe arakincvyv eplrdakyql asgngrrlgt ilnallseee
      181 krdfeqnakd afdklssegp istvsgtiqs hlaaltdpir sqtvevdfet pkleklaral
      241 rmkmaekgid prdldssglg yanllflstv llelsvvres eltillieep eahlhpqlqg
      301 vlldflqsaa kgefdvttgv sirgrlqvia tthspsiasa vgvndiviik sdnesgthal
      361 dlqsvdfgng kkrdhsirki nqyldatrse llfarrvilv egiseavllp aiaerfldne
      421 serlrkfkac ttiivgsvdf epyikllths spnqqsivek lvlltdqdpn mcgaanstar
      481 gpafedndrf crvvspytle vsllgdenen idllkeaylq qhsrsgdkwd kindsenpqr
      541 tmyrmmgqnq sadeflniqk gqfahdlail lrewkpdgsf knefecpeql aqlinfitcd
//
LOCUS       WP_284901950             764 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Corynebacterium accolens].
ACCESSION   WP_284901950
VERSION     WP_284901950.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..764
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=84400
     Region          33..764
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 matdksakrq anngmrsmsa rlarsltggr vkinpvldpl msihrkfhpk adaellnaay
       61 ntaerlhegv frksgepyit hplavatiaa eigmdtttiv aallhdtved teytledlsr
      121 dfgpevarlv dgvtkldkva lgaaaeaeti rkmivamand prvlvikvsd rlhnmrtmrf
      181 lppekqekka rqtleviapl ahrlgmasvk weledlsfai lypkkydeiv rmvaerapsr
      241 dralkeiinq vsaalkengi eaevmgrpkh ywsiyqkmvv rgrefaeifd lvgirvlvdd
      301 inscyaaigv vhsiyqalpg rfkdyisspr fgvyqslhtt vladggatle vqvrthemhy
      361 naefgvaahw ryketkgkns ghqeevdqma wmrqlldwqk eaadpnefld slrydltarq
      421 ifaftpkgdv vdlpagstpv dfayavhtev ghrcigakvn gklvalespl ksgdkveift
      481 skdpnagpsr dwqeflvspr akakvrqwfa kerreehlea grdalasevq rgglpmhrlf
      541 tassmkqvae qlhysdvdal ytaigaghvs aqhvanqlva mfgdrddavd alasrtplse
      601 leqsraqhtk dsasgtgilv egspdvmakl akccqpvpgd aifgfvtrgg gvsvhradca
      661 naeklksepe rmlkvewssg tsstgafsat lqlealdrqg llseltrvls dqninvltmn
      721 snrgedqiat mrftfsvsdt kqlgslmttl rntegvfdvy rvta
//
LOCUS       WP_284901959             847 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium accolens].
ACCESSION   WP_284901959
VERSION     WP_284901959.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 847)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..847
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=94908
     Region          19..841
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mnlsqqlpdl tevpeslide aiwdtfnswt tskgidlyra qeeaslgila gdnvilatpt
       61 gsgksmvana ahfialargq rsfytapika lvsekffalc eifgaenvgm mtgdatvngn
      121 apiiaataei vanialrdga eanidqvvmd efhyysdpdr gwawqvplle lpkaqfllms
      181 atlgdtdwlq edltrrtgre tnlvagstrp vpldfsyvfs avhetieell tdnkapiyvv
      241 hfsqreaaer aqaltslsgi inkeekedia eeiggfrftt afgkdlskll rkgigihhag
      301 mlpkyrrlve rlaqrgllkv icgtdtlgvg invpirtvlm tglakfdgqr qrilksrefh
      361 qiagragrag ydtegtvvve apeheienak arrrigddpk rlkklkkksa regevswsek
      421 tfarlteaep eqltsqfrvs nsmllnvlar hgdgyahmhh llrdnhdprs kqnkdiltal
      481 dlfrglldsg vvqkstkgld iygrpyhlvr elprdfalnq plgpfalaal slldpeadsy
      541 hldvisifea ilddprqvlq aqqkkrrgee iaalkadgvd ytnrmnived itwpkpleel
      601 leqaydtfae tnawvkefel rpksvvrdmv enamtfsdlv atyglarseg vilryltdaw
      661 rtlkqsipde yttpqiedii vwlgelirqv dsslvdewaq magedspidq dtldrelafg
      721 vedptaltan rrafgimvrn ymfrlaqlfa leeedrlaev ldyldevpdf gavlddyfde
      781 yddidtgpea rgpeyfrlee sssrswpvrq iikdpagdra yqfvatvdld asdeagevrl
      841 selrvey
//
LOCUS       WP_284902107             218 aa            linear   BCT 25-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Corynebacterium accolens].
ACCESSION   WP_284902107
VERSION     WP_284902107.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..218
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=24520
     Region          3..200
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mlicqemfll ltkdngkkev lsnnetalra glfsdlllhe avyiapknkv hatdkkpehp
       61 vlawawdslh ehrtssvktl lqarwfspre kiaqdfqdrg qleiedsaww qlggdryimt
      121 dtalenevre rlaavldgtq npsakdviil dilreingay pllkedapem krremrnrik
      181 elkqqveydd aaasavktil qettaiiaav avstagtt
//
LOCUS       WP_284902246             560 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Actinotignum timonense].
ACCESSION   WP_284902246
VERSION     WP_284902246.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum timonense
  ORGANISM  Actinotignum timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 560)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Actinotignum timonense"
                     /db_xref="taxon:1870995"
     Protein         1..560
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=59724
     Region          209..543
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtqrhdpfpa esagapgapg rpanpgtsar pdrpanpgts aqpgrpstda partrrdgif
       61 rralrpartl agrliiafvi lvgtaatflg fasvtllkqy lvstidqdlt tnarsvermf
      121 lqempgasqs slnlsdffvr vnwgiagqrd vttyelpnpg aveefgypre leriaslgse
      181 epvtvpstly gsdwrvlvhp isptstggli tgniiiaqpl gpieftiarl rlifvlagla
      241 tvlaaglavt glvsrtlrsl rdieaathti aeghlaervp hgedddevgm lansinvmla
      301 qiehafaeke rseakmrrfv sdashelrtp latvrgysel yrlggvpper vpeamerves
      361 eanrmaglve dllqlarlde nrplnldcvn lakladnail dfrvrapqrt atvvaldgst
      421 pppkvvevhg dadritqvia nllsnvlaha peaspvkvav giaegqptie vrdhgpgise
      481 adsqriferf yrpdysrsre sggsglglai vaaimaahhg taralttpgg gltvqltfpa
      541 psepcqspda lapahpsgqe
//
LOCUS       WP_284902250             589 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Citrobacter freundii].
ACCESSION   WP_284902250
VERSION     WP_284902250.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 589)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 589)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..589
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=65077
     Region          4..470
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mshrlskisi knfrsckein lnfslftpli gynnagksti lnaiewlfkr kllspsdyfn
       61 neneievege vegiteeils alteenrnri tpfitegtlt fkrtqpvdai aakdvkllik
      121 npengqfrps psgidnaika lfpdpiriga menaaedssk skagttiskl lselsakiqk
      181 qhsnrilkhi eavnrrmtas gnkrlsdlvd idnsisdkva dffpginlkl hfelprfedi
      241 fkagtvkvye dslpdiardc ssyghgtqrs iqmalirhla dittnenvdt ttlllidepe
      301 lylhpfaieq ireslntlsq hgyqiifsth ssqmitsdla kdtilirknn qqgthcrlti
      361 seavnqvivq rpaqarhlfs ltqsskilfa nnvvltegkt ettllpfifk kinnkttgqm
      421 qvalietgsv dsisktmqil asmdiptkai vdldfalrga iinnflqand pdiiglkail
      481 vgmqnggeca ldasglptkn glitaaqaye lmsqkanaap lisslankll nsniwiwqkg
      541 aienhlglte ksesawaefk snaeaqplsd ictdydsved lvtwitpvv
//
LOCUS       WP_284902415             342 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: zinc-dependent alcohol dehydrogenase family protein
            [Enterobacteriaceae].
ACCESSION   WP_284902415
VERSION     WP_284902415.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..342
                     /product="zinc-dependent alcohol dehydrogenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36594
     Region          5..341
                     /region_name="MDR7"
                     /note="Medium chain dehydrogenases/reductase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cd08276"
                     /db_xref="CDD:176237"
     Site            order(43..45,48,149,153,174..179,197..198,202,217,
                     242..243,245,264..265,289..291)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176237"
ORIGIN      
        1 maqmmkhwql ssfgtenlhl aevplpepgh nellvkvsav slnyrdklvl egkllpdlte
       61 mpftpvsdma gvivatgpgv srfttgnrvt gnfwtqwldg dapedmvhhg rslggplpgm
      121 laeyvilhed vavaspdsls deevstlpva altawfalve tgnlrkgqrv lvqgtggval
      181 aglqlaralg aevtvlsrse eklqrakalg asglintslt pewslrvael tggcgfdhil
      241 eliggdnlrq sadalapggr iaqigflkgn emilpafplm lkraviqgit vghrraledl
      301 cqtvdrhqik pvidkiynfa daqaafthle egpfgkivir ig
//
LOCUS       WP_284902443             729 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium accolens].
ACCESSION   WP_284902443
VERSION     WP_284902443.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 729)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 729)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..729
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76365
     Region          2..723
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mshvdlgvsg mtctscssrv erklnkvdgv easvnfates asiefdpets tpadlikvve
       61 gagysafdms gsddgdqded aegtpvddar aaeqqsllrr tiisavlsap imvvsmvpal
      121 qfqnwqwaca mlativfifg gapfhsatwt nlkhgsftmd tlismgtsaa ylwslyalff
      181 gnagepgmtm smswssssae mdhiyfesvg mvitflllgr wfevkakgqs sealrtllsm
      241 gakeasvlrd gkekripisq lqvgdvfvvr pgekiatdge visgnsavda smitgesvpe
      301 evgvgdtvtg atinasgkle vkatqvgedt vlsqmaalvt naqaskapvq rlvdriaqvf
      361 vpvvigisvl tllvhlifgg vapafiaavs vliiacpcal glatptailv gtgrgaqlgl
      421 likgpeiles tkqvdtivmd ktgtvtagem svtavhgdvl eyaaaverns ehpiaqaiar
      481 erdvepgtdf ststagveat vdgvrvgvgk prgdlgqyae afreaeaaga tpvavyldda
      541 laglievrdt vkptsaeavq qmkqlgltph lltgdnegaa krvaeevgit evtagvipee
      601 kvdvikklqs eghnvamvgd gvndaaalaq adlglamgag tdvaieasdi tlmngdlrsa
      661 adairlsrrt lqiikgnlfw afayniilip vaafgllnpl fagiamalss vfvvsnslrl
      721 rkfssqryd
//
LOCUS       WP_284902565             710 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Citrobacter freundii].
ACCESSION   WP_284902565
VERSION     WP_284902565.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 710)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 710)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..710
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77304
     Region          60..710
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mlnnkitpva sglltfacls tvvtahaedt vivsapatsq sslseheppa sekkatlgsl
       61 gerelidvpw svqtlskkvl dqqqikdvkd ayrylpsvqg dgvrpqtrgm qgsvvqnhmi
      121 dglnavstte ysteqfqnie vlsgiagsly gpanpagmfn lvskrpvdtp lhrvtvgqgt
      181 gsgtltsmdf sgpidagdrv kyrlnllnde ghsyttdshv rrqyaglgld fqltdqtvle
      241 snfsyyhyye kgmpgsfala kgvhfpaafd ptdskygqsy aghddetttv dmhikhdfdg
      301 nwmldlgalh qvadrestav tntltnnqgd yttttansaa srftinsyla nltgsvdtgw
      361 ltqdiatgmr gfvwknynpr nggtftlghs slnqhpdypr ppypdfndry hsatttqhaf
      421 llsdtlhfsp qwslllsgse nlftvsnynk aghessrqkd ngmsgstslm ykpvenvtly
      481 ttwadslqqg dtapagarna gqvldpyrsr qievgakyap vkdllltaal feakrpfayt
      541 ndngdfaqdg tqknrglelm adghithnlr vlgggawldp tlhntaasna dgkqivglpr
      601 fasnilaiyt iervpgldvd tnvhyvgrra tdnandswvg syttvdigtr yatrlwntpt
      661 tfrfditnlt drhywtnivp galtgytgag aasaqlgapr qaqvsvqvdf
//
LOCUS       WP_284902780             219 aa            linear   BCT 25-DEC-2024
DEFINITION  YczE/YyaS/YitT family protein [Aerococcus sp. UMB8487].
ACCESSION   WP_284902780
VERSION     WP_284902780.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB8487
  ORGANISM  Aerococcus sp. UMB8487
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Aerococcus sp. UMB8487"
                     /db_xref="taxon:3046346"
     Protein         1..219
                     /product="YczE/YyaS/YitT family protein"
                     /calculated_mol_wt=23868
     Region          6..202
                     /region_name="YczE"
                     /note="Uncharacterized membrane protein YczE [Function
                     unknown]; COG2364"
                     /db_xref="CDD:441931"
ORIGIN      
        1 mtrytwkral vltleiaina lgivlitkan lgttavsslp lvlslatpls lgtllfifns
       61 lyivgqmaly rrdfqawqwl qlgvnlilsl vtdwssaals wlqpgqlwsq ilclvlgcav
      121 lafgialeva vdwlyvsaeg ivqaistcfa wpfgrvkitf dgtitglavv fsflllggle
      181 gvgwgtlisa fligrfvafy qknlpvlaqi aawkerdri
//
LOCUS       WP_284902846             359 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Aerococcus sp. UMB8487].
ACCESSION   WP_284902846
VERSION     WP_284902846.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB8487
  ORGANISM  Aerococcus sp. UMB8487
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Aerococcus sp. UMB8487"
                     /db_xref="taxon:3046346"
     Protein         1..359
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39308
     Region          6..359
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 merrinqlqd llksegipaf yvsnpyniry lsgftgtsak vlvsqekayi itdfryreqa
       61 ekqcqglevv vaggsasqds plafiqrtls qacydklafe dedvsvaaym aldealdvel
      121 ipfsgaievl rqfkddeeia liekacdiav etydfmlntv kagmteiela naidfhmrsl
      181 gasgvsfeti vasglrsamp hgvashkvie qgdlitvdyg cyyqgycsdm trtfalgdpg
      241 dklkeiyaiv qeanrrvsev arpgltgqel davardyirq agygeafghs lghsfgleih
      301 eapnaspsyd eelqagqlit nepgiylegi ggvrieddll ltkdgnrilt pasreliil
//
LOCUS       WP_284902881             638 aa            linear   BCT 25-DEC-2024
DEFINITION  polysaccharide biosynthesis protein [Citrobacter freundii].
ACCESSION   WP_284902881
VERSION     WP_284902881.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 638)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 638)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18500220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..638
                     /product="polysaccharide biosynthesis protein"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=71388
     Region          126..237
                     /region_name="FlaA1"
                     /note="NDP-sugar epimerase, includes UDP-GlcNAc-inverting
                     4,6-dehydratase FlaA1 and capsular polysaccharide
                     biosynthesis protein EpsC [Cell wall/membrane/envelope
                     biogenesis, Posttranslational modification, protein
                     turnover, chaperones]; COG1086"
                     /db_xref="CDD:440703"
     Region          280..574
                     /region_name="Polysacc_synt_2"
                     /note="Polysaccharide biosynthesis protein; pfam02719"
                     /db_xref="CDD:426938"
     Site            order(284,286..289,309..310,340..342,363..365,367,382,405,
                     421,445..448,451..452)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(310,312,316,320,338..341,344,347,365..368,371,375,
                     378,381,452..453,458)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187548"
     Site            order(367,407..409,417,446..447,453..455,458..459,
                     470..472,476,478,513,546,549)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(383,407,417,421)
                     /site_type="active"
                     /db_xref="CDD:187548"
ORIGIN      
        1 mltqllslpr nikriimvai dfillliafw gafwvrmdis apytsyehwk llacliaitv
       61 fifikmglyr tvlryvtaki fvtvlfgmci stlflitmay ffdvflprav piiyfafsll
      121 ficgsrlffr mmltyavrgr vpviiygaga sgrqlltalr qvdeyfpvaf vddnpllskv
      181 vihgvtvypr ksleklipry gikkillamp sisvekrrev itnlenfpce vlsipgmvdl
      241 vegkaqimsl kkvsiddllg repvapseel laknirgkvv mvtgaggsig seicrqiitq
      301 kpkililfev sefalysiek elsmavnksd ndtviiplmg svqklhrlet imrvfnvntv
      361 yhaaaykhvp lveynvvegv rnniygtfyc akaaissqve tfilvstdka vrptntmgat
      421 krvaelvlqa lakeqsvtcf smvrfgnvlg ssgsvvplfe kqiekggpvt lthkdiiryf
      481 mtipeasqlv iqagamargg dvfvldmgdp vriydlatrm vklsgltikd esnpdgdiei
      541 sitglrpgek lyeelligeq vlatthprim tahedmlswq elevylkqmd eacnnfehdk
      601 irelllkipt gfqptdgicd lvwhaknnal esnfnvtc
//
LOCUS       WP_284903002             694 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Corynebacterium
            accolens].
ACCESSION   WP_284903002
VERSION     WP_284903002.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..694
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73365
     Region          30..515
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mqfrrigqlv aattvtaval sgthalaqed tttisvtnit dlhghledgl sdpakagdei
       61 gvarlqslik qvnegqkfnl tssgdnvggs afvsaisddk ytlealnamg mkvtavgnhe
      121 fdkgtedltd riepasdypi lganvlkdgk plldashvee idgvkvgyvg tvtqntkfkv
      181 svakipgvtf tdpveatnke atrlkesgea dvvvslfhed aeeyaqgfnk dvdilfggdt
      241 hqttqgtver egalplqwaq gyeygkllnd aditydkaar kvksielkqy datgaaqvep
      301 daeiagivkk aqdeaevegs ktagtvetdl frgsdegqks gsnrgvestl nnfiaegqry
      361 amskqvgedi dlgvmnaggv radlqggdvt ykdifevqpf gnsvitakvs gkdfitalen
      421 qwqegssrpr lamglsnnvq vvydykaaqg ervksvting epldpnkdys ialssflass
      481 dsekggdgyf eagsikdknd vgymdaqami dyiasgesev rkgqgqigah idgeivpgke
      541 itvdlsslny tsegepmakt vtvklgdeea tadidnskqe gddqfgergr aqvtltvpeg
      601 ltgsqnleit tdagtqailp vevgeagsde agsqedgsed edspklpqgs siggaalaii
      661 aalaaglafi glnpqvlpap lraifddlrk tfhi
//
LOCUS       WP_284903043             154 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Citrobacter freundii].
ACCESSION   WP_284903043
VERSION     WP_284903043.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..154
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=17450
     Region          53..154
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mrhfltklrv wlppplilil fliadaltai prftfgvati visallasas lamilhtawq
       61 mrkkrttlnp lhaeksttlv tggcyawsrn piylgmsglq lafalyvgsl igilvaplfm
      121 lavarlhidf eeeqlrkhfg lewkhyeqrv rrwl
//
LOCUS       WP_284903044             393 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter freundii].
ACCESSION   WP_284903044
VERSION     WP_284903044.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..393
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=44451
     Region          2..390
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mmlnarkvea akgkeksykl sdggglylqv epngsrywrm kyrfagkekr lsfgvyptvt
       61 ladarqkred akkllvaged pgevkkakkh alnaaietln pfrevalewh kmkspkwseg
      121 yasdiieafe kdifphighr piadiqplel levlrliear gamekakkvr qrcgevfrya
      181 ivtgraiynp apdlasamqg heavhypflk anelpeffta lnaysgspiv llgahllilt
      241 glrtgelrag ewrevdfdna vweipkermk mrrahvvpls nqalahletl keltgnyplm
      301 fpgrndpskc mseasinqvf krigyagrvt ghgfrhtmst ilhekgfnsa wietqlahld
      361 knairgiynh aqylegrrem mqwysdfigg tes
//
LOCUS       WP_284903512             530 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Corynebacterium accolens].
ACCESSION   WP_284903512
VERSION     WP_284903512.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium accolens
  ORGANISM  Corynebacterium accolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 530)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Corynebacterium accolens"
                     /db_xref="taxon:38284"
     Protein         1..530
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57187
     Region          1..503
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mevllvligl mlltvfvvai gdrvglpwpa lltiitacav fvpglpqfdi ptelilpifl
       61 ppllwalarr tswgvirgqw vtilslsvll vvattlavga tayaflpgis iaaailigaa
      121 iappdpvavd avaepagipr riittlqteg lfndaasiva fhlalaavtr ggdisfgsgv
      181 lsflyssvva laigwligrl talfithvhd vvarnaltwv vpfatflvae eleasgviav
      241 viaavelnsr adiqaedrls gqsfwetmel lftgvafgli gltvntaiae vgsdlwhsvm
      301 vgvilslvaf vvrfvwmffy yrlnvsrgrp hvaplrmqev llmtwsgmrg lvtlalvlsi
      361 ptgvfafhhe lavialtvll vtmvlpglll pwlmrqldlt easqaandkm raavvsrara
      421 asidalsqfr peddatgeae tvdpeisanv iqwfedrlgd genpaennde rkqraeearr
      481 valearrtal naaqsellal rkdkafnpai vdeileeidr mvigtkhrei
//
LOCUS       WP_284903913             416 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter freundii].
ACCESSION   WP_284903913
VERSION     WP_284903913.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..416
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=47488
     Region          2..404
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 maltdikvrt tkpsdkpfkl tdgqgmhlli npngskywrl qyrfngkqki lalgvyptvs
       61 lgearrkrdv akklvsdgid psekkkadki eqsealtfea vardwhtack rkwsdshser
      121 vlkslednlf ssigkrkiae lktkdllvpi kaveasgrle vasrlqqrtt avmryavqng
      181 lidynpaqem sgaiavakrt hrpalpferf selleridnf kgrkltklav kltllifirs
      241 selrfarwse idfenamwti paereplpgv khshrgskmr tphlvplscq alavlteike
      301 isgdhklvfi gdhdfrkpms entvnkalrs msydttvevc ghgframacs aliesglwsk
      361 daverqmshq ernsvraayi hkaehlderk lmlqwwadyl dllrirqvsp fdfkri
//
LOCUS       WP_284904349             567 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: bifunctional folylpolyglutamate
            synthase/dihydrofolate synthase [Actinotignum].
ACCESSION   WP_284904349
VERSION     WP_284904349.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum
  ORGANISM  Actinotignum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Actinotignum"
                     /db_xref="taxon:1653174"
     Protein         1..567
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=60377
     Region          <13..>77
                     /region_name="PHA03169"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:223003"
     Region          118..558
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mgtnnakhdg tghngagydd aqnycegele hagdfgpggt seapdaeepr dpegardled
       61 prdpkealdp eaareaelda altevlssgl fgdeavirev kespdpiiel adttaeedrv
      121 ediyrdiltr apehkvqpsl ervqmcldll gnphhsyrcv hvtgtngkts tvrmieallr
      181 ehglrtgrft sphlvsvrer iaidghnisr adfiqawedv apfvelvdqr sqaeggprms
      241 ffevfvvmay vafaaapidv avvevgmggr wdatnvidgd vavltpiald herwlghtia
      301 qiagekvgii kpgasvvsaa qpedaaaaia qaahqarahv svygkdievl gretavggql
      361 mtvrtpaary ddiplalrgs yqaenaalal taveaffggr alsgdvveha lmavtspgrl
      421 evvrtsptvl vdaahnphga ahtaaaleey ypgrrvgvla mmadkdvegt lgqfepvlda
      481 vvvtdmpger amdaeelael arevfgedrv rverdllaai deaagwaeae ageelatpvv
      541 avlgsvylag marqimgkgt pdeapte
//
LOCUS       WP_284904388             264 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Citrobacter freundii].
ACCESSION   WP_284904388
VERSION     WP_284904388.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14398448
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..264
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29033
     Region          20..113
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          180..255
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mtsrlantff dpdstsspav arhidfvdya aevpvhthrk gqliialyga vicraendiw
       61 ivppdcavwi pggvphsaka twnahlnylf iepgtaalpe kcctlaispl ikelvdrltn
      121 egvdyapqsh vgrltrvtld elvtmpqkkl slpvsanpki ramadalvsn pddrstfkvw
      181 akrlalsers larlmlretg ltfgrwrqql hliialrela sgvsvqnvaa nlgyesvnaf
      241 itmfrktmgs tpahyfsvrk tads
//
LOCUS       WP_284904547             375 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease [Actinotignum].
ACCESSION   WP_284904547
VERSION     WP_284904547.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum
  ORGANISM  Actinotignum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 375)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Actinotignum"
                     /db_xref="taxon:1653174"
     Protein         1..375
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38355
     Region          63..367
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 maasgapgav pgtmstttag atapapaasa pttavstiar rrtaafavll ittiallgam
       61 vvamgmgqls isapdvvril fsspddvdrs alvainqira prvilavvlg gclavsgavl
      121 qslfrnplvs pdivgvssaa afggvlailv gtssfilmgs tfifglsavv cvmligrirs
      181 hsatltivla gvvvsaffna mvslmtyvad pysklpsitf wlmgslaaas wakvttiiip
      241 viiglivvva lrwrinvlsl gdedaralgi npsamrwvci favalltaas vaaagiigwv
      301 glviphlvrl lvghdnrvvi pesflmggmy lliidtiarn atsveipvgi ltatigapvf
      361 igllirrark grala
//
LOCUS       WP_284904619             136 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: fluoride efflux transporter FluC [Actinotignum].
ACCESSION   WP_284904619
VERSION     WP_284904619.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum
  ORGANISM  Actinotignum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Actinotignum"
                     /db_xref="taxon:1653174"
     Protein         1..136
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13441
     Region          1..120
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 mllvflggga gtvaralvps vaapiivnla gafllglits cfitgvhryg arlrlllgtg
       61 fcggfttyss fvalsahlat gevlsgapse larlaglaag gtlfggflla fagmacgral
      121 grrflaarrr aggdaa
//
LOCUS       WP_284904745             120 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Actinotignum timonense].
ACCESSION   WP_284904745
VERSION     WP_284904745.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum timonense
  ORGANISM  Actinotignum timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Actinotignum timonense"
                     /db_xref="taxon:1870995"
     Protein         1..120
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12526
     Region          2..105
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mawailvgsg ifeaiwatal gdsrglsrpl palvfgvali vsmwglsral reiplgtaya
       61 vwtgtgavlt vviaaargve elsvlkvvfl cgvvgavigl rvverreelg knetrakpen
//
LOCUS       WP_284904969             342 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Citrobacter freundii].
ACCESSION   WP_284904969
VERSION     WP_284904969.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..342
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=39222
     Region          1..328
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mnnkkivafd iiraisvimi isfhfmstvv nhggnwddfn ifspmgsigv sffimisgag
       61 lyvssqrwng viqfykkril siyppyifsy ffiaclmfml ageiyfgnnv flwvltitgf
      121 dgymlwhapn yymigewflg fiviiyaiyp iiriainkni yysllisvfi acityannke
      181 issylpifna tpewnpliri pefifgamva khiiegsnlf kkiipicliy sfiavykfdn
      241 lnsgvlsips lcaifyvltf tmlhikfndg ilsiinffsv nsfvaflihh kiiylsvlfv
      301 kpipasytat ylylyaiili vfsisyflsk pinsitkifi nk
//
LOCUS       WP_284904995             319 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Actinomyces
            urogenitalis].
ACCESSION   WP_284904995
VERSION     WP_284904995.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces urogenitalis
  ORGANISM  Actinomyces urogenitalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Actinomyces urogenitalis"
                     /db_xref="taxon:103621"
     Protein         1..319
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33570
     Region          1..318
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mrvgfvanpt sgkgrftdaa eiarwtlerl gyevalaqgq dydstrraat alvedgsgld
       61 alvviggdgt vhlgldvvat tsvplgivpv gtgndiarhl giqardvaaa lrlvhlalcg
      121 qegatvaeld aihatrpdgt pvpdehewcl avvsagidaa vnarantlaw psgegrymra
      181 ipyeirhmap ygyrvttdag tweggavlla vantryiggg ldivpvadps dglldvirld
      241 pvsrtglvgh larlrqgshm dhpavhhers rvvtieawsg rqglrtpphp madgepvagl
      301 plrleavrra vrvivpsrg
//
LOCUS       WP_284905008             816 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Actinomyces urogenitalis].
ACCESSION   WP_284905008
VERSION     WP_284905008.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces urogenitalis
  ORGANISM  Actinomyces urogenitalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 816)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 816)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 816)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="Actinomyces urogenitalis"
                     /db_xref="taxon:103621"
     Protein         1..816
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=87971
     Region          20..814
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mppssqppts eqpeaqatss vrdreihaeq hvvnlaygel drqleaarrs laateaqgvs
       61 gthqsrgerd ayavhysgli aslegvedrl vfgrmdlahg avdgasagpv thggqrhyvg
      121 rtglqdarhr evvldwrapl arafyqatas rpmglvrrrh idtrarrvig ledevidvss
      181 ldqagtypsg sqprvaaegl qgegaliaam saardgrmgd ivatiqaeqd rivtaqgrgv
      241 lvvqggpgtg ktavalhrva ylfysererl ersgvllvgp srtflryveq vlpslgetgv
      301 vattiadlvp gvrargtesp alhelkgrtv waeilrravr slqrlpdqpr eiivqgtrll
      361 lepadvream srarrsgkph nlaretfvlw llerltdqya tatrqdasdp etrawiredi
      421 rttrdarrei nlcwmpttpt gllerlwarp plleqvapel saaereslar tpgspltpad
      481 vplidelael lgpsedaqar qarlearrra elvdyaarai esqglgdgmv saemladrme
      541 dagpsltlae karadrgwty ghvvvdeaqe lgdmawrala rrcpvrsftv vgdlaqysgp
      601 hapsswaevl qalgtspsqp rrggrtsrpv astplreevl tvcyrtpati mdtadavtta
      661 lghppvypvr svrdlpgcle aedlsasala hdeagwaghl ravvsqelaa ldeavgpqgg
      721 rvaviapdap avaawlgqda alaeamtapg gdvlqarlav mgpvlskgle fdvvvlvdpa
      781 migrqsagdl yvamtrptrr lrvvsrqelp qglalg
//
LOCUS       WP_284905017             408 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter freundii].
ACCESSION   WP_284905017
VERSION     WP_284905017.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..408
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=46547
     Region          7..393
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 magelnklsd rklkglhgip askiefyadg aglsakvtka ggiswvftyr ldgqklhrlt
       61 lgrypdmslk earssrdkcr qwlasgkdpk hqlalttqet lkpvtvkeai eywireyaee
      121 nranverhka elrkhiypyi gkmpladcet rywldcfdrm kkktpvaagy vfqmckqalk
      181 fcrvrryavs taledltipd vgkkqakkdr vlndkeagdl waaitsgtcf mpyytrllti
      241 lmvfgcrtqe arlsewsewd mdawvwtvpk ehskggekiv rpvpdamrrf ieilhdetkl
      301 sglllgsvkg seavsqwgrs vykklghsep wtlhdlrrtl athmnnmgia phvveqllgh
      361 smpgvmaiyn rslylpekld alnkwherle llagnhqnvv llpvanrd
//
LOCUS       WP_284905152             274 aa            linear   BCT 25-DEC-2024
DEFINITION  N-acetylmuramoyl-L-alanine amidase family protein, partial
            [Actinomyces urogenitalis].
ACCESSION   WP_284905152
VERSION     WP_284905152.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces urogenitalis
  ORGANISM  Actinomyces urogenitalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474208
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Actinomyces urogenitalis"
                     /db_xref="taxon:103621"
     Protein         <1..274
                     /product="N-acetylmuramoyl-L-alanine amidase family
                     protein"
     Region          <1..72
                     /region_name="COG5263"
                     /note="Glucan-binding domain (YG repeat) [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:444077"
ORIGIN      
        1 yylhgdghma tgwlqlgstw yyldpatgkm atgwlhlgpt wyyltpsgam vtgrqvvdgr
       61 esafaasgaw qgyttasgaa sdagsrspav qhaimsapaa srrattaamv rayqrsgaty
      121 paqalgrgga tsieafvglv ydeavaegvs pellfvqamk etawlrfggd vrvtqlnfgg
      181 igatgggagg asfgsvregl raqvqhlray adpsvtqakl ahpvvdprfa yvrkgsaryv
      241 ehlgasenpq gvgwatdkgy gtslaqmmsp ifgi
//
LOCUS       WP_284905425              68 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Citrobacter freundii].
ACCESSION   WP_284905425
VERSION     WP_284905425.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 68)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..68
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=7643
     Region          1..64
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mknqatrlir lpevlertgy gkawiyrlis esrfpvpvki gvravafves eidawiqsvi
       61 etsrnnva
//
LOCUS       WP_284905405             585 aa            linear   BCT 25-DEC-2024
DEFINITION  terminase large subunit [Citrobacter freundii].
ACCESSION   WP_284905405
VERSION     WP_284905405.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..585
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65891
     Region          4..583
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 makvsdgiry aervvagevi acefvrlacq rflddlkhge ergiyfsepr aqhilnfykf
       61 vphvkgslag qpielmdwhv filinifgfv iplvneetge ivlrndgsgr pvmvrrfrta
      121 ynevarknak stlssgvgly magadgegga evysaattrd qarivfedak nmvkkakptl
      181 grlfefnkla iyqeqtaskf eplssdannl dglnihcgiv delhahktrd vwdvletatg
      241 arlqsllfgi ttagfnkegi cyelrdyaik vlrgynseve gavkddtffa iiftldkddd
      301 pfdetvwqka npglgickrw ddlrrlakka keqvsarvnf ftkhmniwvt aesawmdmik
      361 wencefiapr helktypmwa gvdlahkidi caavklwrad nghahadfkf wlpegrlekc
      421 saqmaqmyrk waelgklelt dgdvidhaqi kadflewisg enlketgfdp wsatqfslal
      481 aeegvplvev pqtvrnfses mkeveslvyg grfhhsnhpv mnwmmsnvtv kpdkndnifp
      541 nkstpeakid gpaalftams rmlvnggeqq dslsdhlesy gvrsl
//
LOCUS       WP_284905437             422 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Actinomyces
            urogenitalis].
ACCESSION   WP_284905437
VERSION     WP_284905437.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces urogenitalis
  ORGANISM  Actinomyces urogenitalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 422)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Actinomyces urogenitalis"
                     /db_xref="taxon:103621"
     Protein         1..422
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44996
     Region          44..417
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(150,152,275,277,305..307,348)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mtslmtrrgf lgatataala svaactqgsa trdseevaad gsvtitymnf sanggheedl
       61 qaiadafhee npqitvklet vpydsyftkl qtavaggtas dafelnyenf vtyasngslk
      121 aldgidsssy rpslfeaftr dgaqyglpes fsnvvlfynk tlfeehglgv ptsewtwkee
      181 reaaerltdt atqtfgdyqp vsfhefykvl aqsggqflsd dgtrtafnsp egvaaaswlv
      241 rkpgavmpta adgagapdfd selfksgkla mwhsgiwmfd glqdvpfdwd ivvepgettk
      301 asamftngav vsattakaea atkwitylts sstmseirls sawelppvad daafesylds
      361 gqpanrqavl esldktvlpp viasqqemqd amtqalesaa agalsveeal aqaaskidsl
      421 lg
//
LOCUS       WP_284905524             130 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Actinomyces urogenitalis].
ACCESSION   WP_284905524
VERSION     WP_284905524.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces urogenitalis
  ORGANISM  Actinomyces urogenitalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 130)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Actinomyces urogenitalis"
                     /db_xref="taxon:103621"
     Protein         1..130
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=13896
     Region          6..127
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 mgqeiivsav iirdcngrll tvrkrgtqlf mfpggkpepg etasqtaare areelgiaid
       61 tedlqplgtf tapaaneegy vvlahvfshp yvdgaqpahe iaelrwtdlt aplpqdlapl
      121 trvvipalis
//
LOCUS       WP_284905582             110 aa            linear   BCT 25-DEC-2024
DEFINITION  fluoride efflux transporter FluC, partial [Actinomyces
            urogenitalis].
ACCESSION   WP_284905582
VERSION     WP_284905582.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces urogenitalis
  ORGANISM  Actinomyces urogenitalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Actinomyces urogenitalis"
                     /db_xref="taxon:103621"
     Protein         <1..110
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          <2..104
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 yvgivvvntv gcfllgfltg ilpllavlva ggstvdypgv tgtmrfvlst gflggfttfs
       61 tavldawtev warrvragms livvgwvsgl vsyllglglt alvsyllgig
//
LOCUS       WP_284905874             562 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Actinotignum
            timonense].
ACCESSION   WP_284905874
VERSION     WP_284905874.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum timonense
  ORGANISM  Actinotignum timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Actinotignum timonense"
                     /db_xref="taxon:1870995"
     Protein         1..562
                     /product="class I SAM-dependent DNA methyltransferase"
                     /calculated_mol_wt=63058
     Region          <2..561
                     /region_name="YeeA"
                     /note="Type II restriction/modification system,
                     endonuclease and methylase domains [Defense mechanisms];
                     COG1002"
                     /db_xref="CDD:440626"
ORIGIN      
        1 mcdpgcgsgn flviaykalr qlehrileri dslstsgsws llgmgeeekl gaatlglass
       61 vinienfygi eiddvsvema ilslwiakhq mneefaekfg vdipliplke tghivhgnat
      121 rldwnevcpn ngtdeiyiig nppyvgstyq tkdqkedfay vfdsakypkk ldyvalwfik
      181 ganyirgtra klafvttnsi tqgeqvallh pyvftggiei gyaytsfkws nnashnagvt
      241 vavislrnes sepkclftdl vrtpvenina yliagestfv tarsttlspf lpkmtkgsqp
      301 tdggnlilsd qeaedlltsh pelsevlkqf vgaddyingk dryclwltee nrheaaeipe
      361 vkrrlehvsa mrsastkkqt qefaaipwrf gevrykptds iivpsvsser reyvpvgylg
      421 pdtiisnlaf aiydaepwlf alltskmhma wlravggqle trlrysntlv yntfpvpels
      481 asskeeltkr alrvldvrey hcektlaely dpdlmprnlr eahekideav drlyrnkpfa
      541 sdeerlavlf ekyqqlvaae gk
//
LOCUS       WP_284905907             140 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: TlpA family protein disulfide reductase [Bacillus].
ACCESSION   WP_284905907
VERSION     WP_284905907.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..140
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16131
     Region          <29..137
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 metqklnwpe hlpwifpsdq rslsegqqll yfwsvncphc eeltdhilyr vnqlgihltc
       61 vhvpytedek svdvvseyae eknmtapivl dqdyeivaky kiqglpsfcl ideegnlidr
      121 kmgdsgleki lkkiekhsis
//
LOCUS       WP_284906197             929 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ATP-binding protein [Bacillus].
ACCESSION   WP_284906197
VERSION     WP_284906197.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 929)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 929)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 929)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 929)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 929)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 929)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 929)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18767243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..929
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..929
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=108289
     Region          1..929
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          1..198
                     /region_name="AAA_27"
                     /note="AAA domain; pfam13514"
                     /db_xref="CDD:433272"
     Region          <565..>696
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mkirslhiah fgkfsnqtfh fsddgfqlvy glnesgkttl ktfiesmlfg fpknkmyktk
       61 qgsfyggslt cqddelgvih iertsdrggq aqvflpngev kdeaflqtll kgtdrrlyqs
      121 iysfdvfglq nvqalnqdqi gefllfsslf gsdaatkmds rllkqqeqlf kpngrkpeln
      181 qqldhlkelt gqlkqarlie gsytekkreq seltetiekl qnemkqaeeq lqkltesiqv
      241 ypmiekkvdl kkelarypdr vkrfrveteh eldkleshlh pkkaqltalk qkldhlqtsl
      301 vqvqplydkd tlmemkrvvd easnaelvkk riagcrancd slkqkideav aklkwerpik
      361 leqiddslef ewelketvtq yvrlmdrkaq lderfdharh eldeaeaalk glkeqqvrlh
      421 gteddakgtr tkkkrvyslt slfrgliafd vvflcvlffl tewwitllfa gfsvflffvi
      481 ysfsqmrpmk qrsgedalds fqvqaasaet lmrqkellye riirqyedwe lelepvqqqv
      541 eekkrqlgls selsflveaf hilkqlkmnt aayeelqrei dvlsdqqsiy erkvsalssl
      601 lqnkegtiqe nisafqeilk deakrekerq slhvsiqham qqfstlegei qyyekqtdel
      661 frqveaeske dyqvlshlsk eyrkrlselq qlnqelhrsg cfdeeewivh kglslleeec
      721 aeakqhlhdv qlnaenmekr laelaveirq ieasgtvsdl thqlvaeqeh akhlakkwaa
      781 iqlvrsvire klnehketrl pallqtassf iqpltndrye ailfspeddl lmvkrmdgri
      841 frpeelsqat ceqiylairf alalshqqdc qlpfmmddsf vhfdhvrlgr vlemmdeltr
      901 fetqlfyftc hehmkqaaed gqvtslvve
//
LOCUS       WP_284906216             604 aa            linear   BCT 25-DEC-2024
DEFINITION  IucA/IucC family protein [Bacillus sp. lyk4-R2A-2].
ACCESSION   WP_284906216
VERSION     WP_284906216.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. lyk4-R2A-2
  ORGANISM  Bacillus sp. lyk4-R2A-2
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Bacillus sp. lyk4-R2A-2"
                     /db_xref="taxon:3040282"
     Protein         1..604
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=69560
     Region          13..596
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 msvqdelkka vnpaawkkan qrmvakmlse ymyedmlhpv qldqkdgiaq yeliihehkk
       61 yrylakprlf dsfdtiaesi eccqdgkwsk dvsaivflld iqplipmssd ttghlikelh
      121 htlladvhll skkalradel tdtdyawieg emtghpwivy nkgrigfsyd dylayaperq
      181 esvqlswiav hrdlatfhav dhenyeqvia keldevtirq flrvlkdegl iaadyylmpv
      241 hkwqwthmii qhfpedlalr rivyvgegld qyipqqsirt ftnisnkgkh hiklpmsiln
      301 tlvyrglpse rtviaprita hikgiadqds flsdvcrvil pgenasinvd hpyysklpga
      361 pyqylemlgv ifresiysyl degenpvtla altyedhege pyvkqlieks glsakewmak
      421 ffhvvmppll hfmyqygtvf sphgqntilv lkdhqphrla ikdfvddvni sdqplpelas
      481 lgddlkevlr seppeglvqf iftglficnl ryvsnvlenh qlldevtlwr llaeeiqqyq
      541 kqfpqlkdrf dlfdlfqpkl tklclnrnrm idygygdgdd rphasehgkv tnalahvlss
      601 igek
//
LOCUS       WP_284906545             295 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Actinotignum sanguinis].
ACCESSION   WP_284906545
VERSION     WP_284906545.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum sanguinis
  ORGANISM  Actinotignum sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Actinotignum sanguinis"
                     /db_xref="taxon:1445614"
     Protein         1..295
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=32401
     Region          8..251
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 mttlfdvssd fdvdldvysg pfsvllsmis kknlditeva laevtdefia wirsrpevdl
       61 sttseflvva atlldmklar llprheseee dwelleqrdl lfakllqyra fkevardfga
      121 rlaetgrrvg rdvpleemya kalpevrlpl gvmdlallaa raftrdtsep vvqlqhlhsp
      181 vvpvasqvay leerfragds ftfaqlcada psvqmvvarf lavlellrrg aiaaeqdepl
      241 gtlvlrptpd ddrgaagegd vaaeygevep rvinpsravp aggaplrraa trlgl
//
LOCUS       WP_284906704             902 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase, partial [Actinotignum
            sanguinis].
ACCESSION   WP_284906704
VERSION     WP_284906704.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum sanguinis
  ORGANISM  Actinotignum sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..902
                     /organism="Actinotignum sanguinis"
                     /db_xref="taxon:1445614"
     Protein         1..>902
                     /product="class I SAM-dependent DNA methyltransferase"
     Region          58..902
                     /region_name="YeeA"
                     /note="Type II restriction/modification system,
                     endonuclease and methylase domains [Defense mechanisms];
                     COG1002"
                     /db_xref="CDD:440626"
ORIGIN      
        1 maitlqsiee hvkkltsrap ftrdfffdll laygiskssv trlrsttass lnvaanperd
       61 ivwknkiyla etsndliata qemktseaal rfntrfviat nyealaaidt ktgdslsipl
      121 akladdftff lpwanmekqh fssdthadrr aaehmskvyd ellsanptlf hedksphsln
      181 ifftrllfcf faedtgiftk gqftsavgsh tqrdgsdtaa fltalfhald tpspadkpvy
      241 lqdfpyvngr lfrinnddaa sltvpqftkh ardsllelgt ldwseinpdi fgsmfqavvd
      301 kdqranlgqh ytsvpnilkt ikplfldelw reydkacesv prlkklltri skiklfdpas
      361 gsgnflviay kelrklehai ldridslssa grwgllgmge eeklgaatlg fgssvinien
      421 fygieiddis vemailslwi akhqmnqefk akfgldipli plketghivh gnatrldwne
      481 vcpnngtdei ylignppyvg ssmqsasqke dlasyfgeqk ysknldyisl wflkgadyir
      541 gtaaqlafvs tnsitqgdhv gllfpfvltg gieisyayts fkwsnnashn agvtvivlsl
      601 rnssdspkll fsdgiekqvk hinaylaegd dvivtkrrqp lshqlpqmty gskptdgghl
      661 ilepedvekl laaypesekf ikqyvgssey irgndrfclw ieddcvteaq hipaiakrle
      721 rvrderlrsk alstvefaeq phrfkqrsyk ptdsiivpsv sserrdyvpv gyldantvis
      781 nlafavydae pwlfalltsk mhmawlravg gqletrlrys ntlvyntfpv pelsasskee
      841 ltkralrvld vreyhcektl aelydpdlmp rnlreaheki deavdrlyks tpfasdeerl
      901 av
//
LOCUS       WP_284906713             466 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase, partial
            [Actinotignum sanguinis].
ACCESSION   WP_284906713
VERSION     WP_284906713.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum sanguinis
  ORGANISM  Actinotignum sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 466)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 466)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Actinotignum sanguinis"
                     /db_xref="taxon:1445614"
     Protein         <1..466
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
     Region          1..199
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 iassvtvghl vavddvhaad dllpllrrav eaahddmlal vaenpkmagm gttciamlra
       61 snklamvhig dsrayllrdg klgqvthdht lvqylvdhgr ltpeeaehhp qrnvimralg
      121 dtpgevelde svrearvgdr wllcsdglfg vvahdtieha msaipdlhql gehlidlala
      181 agapdnvtvi ladviddaal tsplpsqpiv vgsaardyrr ptrggnsaaa kaatltrnan
      241 agtgagagag gaassdqlrs atpssnsgns snpnsgegqa gsagsgtsta sgagtvsgaa
      301 sgagrgnpga egaprarwga rlaviltvla lavaglfgay rwtqsryyva nnngtvtiyq
      361 gipqrlgple fshaaeatdl qvrdltpvaq drlatpitra slrearavva alreqkaqnn
      421 eptpapatpg asatptpasa spapeapaap apapaaptpa npgenr
//
LOCUS       WP_284906794             434 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: bifunctional folylpolyglutamate
            synthase/dihydrofolate synthase [Bacillus].
ACCESSION   WP_284906794
VERSION     WP_284906794.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..434
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48340
     Region          5..434
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mtlfttyhea iewihsrlaf gvkpglermk wlmnklshpe qrikavhvag tngkgstiaf
       61 trsvlqaagy svgtftspfi ltfnerisvn gapiqdeewl slvnkikpfv deldqtelga
      121 atefeiitac afayfadvqq vdfvlletgl ggrldstnva vpiltaitsi ghdhmailgd
      181 tleqiaseka giikegipmi tavhqpeala viqniakekk vecislqdtc tfshqqptet
      241 gerftlstsk rqypqletgl igthqqqnas lavlliewle qegyisvtee qvyegirhav
      301 wagrfekvkd hppvyldgah neegidrlie tvqahfsskq vhvcfsalkd kpykqmiqkl
      361 eaisssihfv sfdfpraesa eklyacsqle aksydddprt vlefiqkksd dpsavilvtg
      421 slyfisdirn rilr
//
LOCUS       WP_284906856             600 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase, partial
            [Clostridioides difficile].
ACCESSION   WP_284906856
VERSION     WP_284906856.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>600
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
     Region          31..492
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mkirrylilv iiilittsqs fisyglerfe eitifhtndi hgryaegddh iqignlatlk
       61 ketpnsilvd agdclhglpi vnmdrgksai elikcagydy itpgnhdfny gkdrlfelsk
      121 sanlgentlk flssnifeng kkvfdsndik eidgikigff glstqetksk tgfknvegle
      181 fknpiesate qvnelkgkga nvivaichig tnslskpnsi dianevqgid liidghshtk
      241 fengkqvgdt livsagqyle nigeikltld tndvedikie nksarligke ealkykldsv
      301 vskkvdkike qqekildkvi gvttntldgs yenvrtketn lgnlisdill dktkadislf
      361 nggnirdtie kgnitrrdiv dvfpfsntiv tkeltgaqik dvlehgvkly pekssaflqv
      421 ggisyyfnpk qkegekitni qkegkpldln kkyvvatndy iasggdefpc fskepvlkef
      481 gnlesaviey ieykkeiskn vdgrigiksk delisknhes dlilsenekn indneenlsn
      541 nikssdsdkn ksldktssre ssnlgiskre akekspktgd lgfsnsiiif ivsstlicll
//
LOCUS       WP_284906877              84 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Actinotignum
            sanguinis].
ACCESSION   WP_284906877
VERSION     WP_284906877.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum sanguinis
  ORGANISM  Actinotignum sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 84)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 84)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Actinotignum sanguinis"
                     /db_xref="taxon:1445614"
     Protein         1..84
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=9100
     Region          14..80
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mktnvldhql gnddnrvlss aqaaqylgvs mktlanwrrl gigprffrrs ntvdsrghsv
       61 grvgykfgdv sayanerfag nggl
//
LOCUS       WP_284906928             587 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Actinotignum sanguinis].
ACCESSION   WP_284906928
VERSION     WP_284906928.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum sanguinis
  ORGANISM  Actinotignum sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 587)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Actinotignum sanguinis"
                     /db_xref="taxon:1445614"
     Protein         1..587
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=62835
     Region          6..324
                     /region_name="DinP"
                     /note="Nucleotidyltransferase/DNA polymerase DinP involved
                     in DNA repair [Replication, recombination and repair];
                     COG0389"
                     /db_xref="CDD:440158"
ORIGIN      
        1 mrqatvwvpn wpiiaaemag iatretpval vehhrvanin vwawregarv dmptrqlqsl
       61 vpqctviqrd rarelrffdp vlraisnrva rfslvepgmv ifsaagpart eggeerlcen
      121 lvgdivdaag cearvgiaeg tlpslwaart sriiapgase qalagqpisl fllvatpatr
      181 palrdcvell rdlgiatiad viglgqrslv trfgnigqym wdlavartlp ahestpdtrd
      241 isvvatfdpp lthaehaafa arnlagqlet kmragaagsa rldirasaah gevmtrswhl
      301 elltqedvvd rvrwqisawi aqprenreal agspggasgv eadaagmenr ggitqlelia
      361 rditpagnhp aplwgartas daaaargahr lqsllgeedv rvprrvggrl peedvqeipw
      421 gqavdtsraq lpwpgrlpep apvqllrtpy pvtvlctcgk plaiaattal hcpgecrhpf
      481 patvravlpa ehagpcvgda avaggatspa ggatlstgss gfptaslhal fgveefltvl
      541 dyagpwvseq rwwaratrra yiqvvtttga vllyveqerw ylaasyi
//
LOCUS       WP_284907272             303 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284907272
VERSION     WP_284907272.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..303
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          74..300
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 giiyyfiryi nkrlskiyfi vdkmsqenyl kdtteseetg ylveyneyfk egifskinnc
       61 lyelnrslki kfiklekeke svkslvtdis hqlktplasl klyntlliee eleedeanef
      121 lltnkasink lenlinslvn isrleismin ikkedndikn tilnavksvt pkaksksitl
      181 nlnefnsrii phdkkwtees ifnvldnavk ytqvngeini sveetanffk iiiedngigi
      241 eksefnnifk rfyrgsadei esvegsgvgl ylsrkileeq ggniivsskv gigskfslfl
      301 ttm
//
LOCUS       WP_284907338             248 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Bacillus].
ACCESSION   WP_284907338
VERSION     WP_284907338.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..248
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28476
     Region          1..246
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mkvvtpkpft fkggekavll lhgftgntad vrmlgrylne rgytchapqy kghgvppeel
       61 vhfgpddwwk dvqeayqflk degyeeiavc glslggvfsl klgytvpvkg ivpmcapmyi
      121 kseevmyqgv leyarnykkf egkseeqieq emeefkktpm dtlrslqeli advrnnvdmi
      181 ysptfvvqar hdhmintdsa niiynevetd qkhlkwyees ghaitldker ekvhqdvyaf
      241 leslhwsv
//
LOCUS       WP_284907356             624 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: polysaccharide biosynthesis protein [Bacillus].
ACCESSION   WP_284907356
VERSION     WP_284907356.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 624)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 624)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 624)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 624)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18500220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..624
                     /product="polysaccharide biosynthesis protein"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=69642
     Region          118..237
                     /region_name="FlaA1"
                     /note="NDP-sugar epimerase, includes UDP-GlcNAc-inverting
                     4,6-dehydratase FlaA1 and capsular polysaccharide
                     biosynthesis protein EpsC [Cell wall/membrane/envelope
                     biogenesis, Posttranslational modification, protein
                     turnover, chaperones]; COG1086"
                     /db_xref="CDD:440703"
     Region          280..564
                     /region_name="Polysacc_synt_2"
                     /note="Polysaccharide biosynthesis protein; pfam02719"
                     /db_xref="CDD:426938"
     Site            order(284,286..289,309..310,337..339,360..362,364,379,402,
                     418,441..444,447..448)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(310,312,316,320,335..338,341,344,362..365,368,372,
                     375,378,448..449,454)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187548"
     Site            order(364,404..406,414,442..443,449..451,454..455,
                     466..468,472,474,509,535,538)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(380,404,414,418)
                     /site_type="active"
                     /db_xref="CDD:187548"
ORIGIN      
        1 mtyaqrlsii valdsylilv avffgfqfvq eaaltvytfe mlvisslsll ighhlfsyif
       61 hvykqvwayt gvrelfslmk tfvcsflfsm amlylfvqtw pfrflfivwl fhvlfigasr
      121 masrllhdga krlqvekera liigagsagt iivrqlqqss dvhiepvafi dddktkhrle
      181 imglpvlggk eqiqtavvmm diqkiiiaip sksshtlkgl ykecvatgik tqimpemeqi
      241 lkgthalnql rdvqpedllg repiqldssr lsvhlkgkti mvtgaggsig seicrqicvf
      301 apqaivlvgh gefsihsill elkeiygdti slypqiadiq dkqkmseivg qfqpdmiyht
      361 aahkhvplme ispkeavknn iigtknvaea ahehgietfv lissdkavnp anvmgatkrf
      421 aemlimqmga ssdtkfvavr fgnvlgsrgs vipifkkqie qggpvtvthp amtryfmtip
      481 easrlviqag alaegrqifv ldmgepvkiv dlaenlihls gyttdqipit ftgirpgekm
      541 yeellnqhek aqeqifpkih ighaldgdpy vlnrfihefd mmseeqmrea lfaaieshdl
      601 lseqmtrege aladeekslv lrng
//
LOCUS       WP_284907478             808 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: S8 family peptidase [Bacillus].
ACCESSION   WP_284907478
VERSION     WP_284907478.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 808)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 808)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13717683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..808
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..808
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=86464
     Region          57..143
                     /region_name="Inhibitor_I9"
                     /note="Peptidase inhibitor I9; pfam05922"
                     /db_xref="CDD:428674"
     Region          180..590
                     /region_name="Peptidases_S8_subtilisin_Vpr-like"
                     /note="Peptidase S8 family domain in Vpr-like proteins;
                     cd07474"
                     /db_xref="CDD:173800"
     Site            order(189,233,291..293,323,534)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:173800"
     Site            order(189,233,534)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173800"
     Region          360..497
                     /region_name="PA_C5a_like"
                     /note="Protease-associated domain containing proteins like
                     Streptococcus pyogenes C5a peptidase. This group contains
                     various PA domain-containing proteins similar to S.
                     pyogenes C5a, including, i) Vpr, a minor extracellular
                     serine protease from Bacillus...; cd02133"
                     /db_xref="CDD:239048"
     Site            409..411
                     /site_type="active"
                     /note="putative integrin binding motif [active]"
                     /db_xref="CDD:239048"
     Region          711..>799
                     /region_name="FLgD_tudor"
                     /note="FlgD Tudor-like domain; cl29105"
                     /db_xref="CDD:452922"
ORIGIN      
        1 mkkvvsrssv llfstifils tfftgqqasa apsnkqvele kaeifgeinv nsrkhttviv
       61 elkekslvea kqegkaqtka slkksrtkvk nealkeidka svrqeyekvf sgfsmklpan
      121 eipkllavdg vkavypdvty qtdevkkesi qlpnedvspl mdksapfiga pkawdagysg
      181 kgvkvavidt gvdythpdlk gnfglykgyd fvdndyspqe tpkgdprges tdhgthvagt
      241 iaangqikgv akdasllayr vlgpggsgtt envlagidra vtdgadvmnl slgnsvnnpd
      301 yatsialdwa msegvvavts ngnsgpnswt vgspgtsrda isvgatqlpy slynvkfpny
      361 stakvmgyyq esdlkaldqk qvtlvhagig dekafedidv kgkvavierg aiafvdkvdn
      421 akaagaigvv mynntdgeip vdvpglalpt iklskaegta lvkaieagnn tttfsiqfvk
      481 elseqvadfs srgpvvdtwm ikpdlsapgv sivstipthd psqpygygsk qgtsmasphv
      541 agvaaimkqa kpsysteqik allmntaekl fdangspfph ntqgtgsvri ieslqassiv
      601 sdasysygtf lkekgvqikt kkfkvenlsk apktytidyk fdgsgistng tkkitvkgns
      661 tgsftsavqv kygktkkgty qgsitlreng rkvteiptll ivkepdyprv tsvsvepdnr
      721 agsyvissyl pggaenlafl vystdgeylg eagvyqhvdk gehrvkwngt inqgqklepg
      781 eytmlayasl kgksdtvqtk epfdiype
//
LOCUS       WP_284907618             468 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: phospholipase D-like domain-containing protein
            [Bacillus].
ACCESSION   WP_284907618
VERSION     WP_284907618.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..468
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=53553
     Region          51..433
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mlhllfylil lyvvyvflta fvlfylpvrk tckehciyka ssisgddqgt nqvmlldagf
       61 esgqvriqmi reakkmirls yysiqkgkta ewilgaliea adrgvkvqll ldgichslrg
      121 plkhlryava nhpnmsirfy epfrlfkpwt whnrlhdkll ladgrvavmg grnigdkyfa
      181 dqppkdfafd rdvllynpkk gkvldemeqy fvylwnhdft krtkavfskp kakkglklrk
      241 qllrsyhdav rtkepfvmss fdwaadstsv kqvafftnpv erfnkrplvl kklndlahra
      301 krsvliqtpy viptrpmksg ltplpseiqt tvvtnsltat pnplafagyl stkkelmktg
      361 vhlyeyegpy sihaksmvid dylsiigtyn ldarssflnt esilvidsap falsltqaie
      421 rkiaysylva kdrtvyqtsa ygqkkkplmk rlllnglsai tvlwrrli
//
LOCUS       WP_284907688             377 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FAD-dependent oxidoreductase [Bacillus].
ACCESSION   WP_284907688
VERSION     WP_284907688.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..377
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=43048
     Region          1..347
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mksqhviiig sgvaglatsl flkkagmest iyesrsdeel etgagfllsp ngvkildeig
       61 cknevianat vikkiqqins eneveaifhn ysekyydapl lnvmrdqiik sllkevhrqg
      121 ievkynkklt sikqqphsvq vlfedetvit ggivigadgt fsktreaiaf nakldysgfw
      181 glqgvsfvkd fvldeatsyf yndgnfqfif gkahptnkmn ilwqafsqcp eklptkhfek
      241 anketirqll ykqmehwnip khlsdiidht dmffprsiye ikdlpvwskg rvvligdavh
      301 tanpfvgqga sysledamvi akmlrdhddr dalyyyekdr rkrteelnal lqhisiqndi
      361 dkkmneytie wdeetyv
//
LOCUS       WP_284907740             208 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NUDIX hydrolase [Bacillus].
ACCESSION   WP_284907740
VERSION     WP_284907740.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 208)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..208
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=24346
     Region          6..148
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04692"
                     /db_xref="CDD:467574"
ORIGIN      
        1 meqeklniln eqhetigvaa rsdihaqglw hetfhfwllk kehdtnylyf qlrspakkdf
       61 pslfditaag hllaneqpsd gmreveeeig ltipfedltf agviqdeihl psftdrecch
      121 vylyvhqeeq mniqlqkeev aglyranlmd aqqlftrkye nmqlegfeid eagerreesr
      181 vvciqdfvph epsyyqhlfq ainqflsq
//
LOCUS       WP_284907779             351 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD-IIIC family phosphatase [Bacillus sp. lyk4-R2A-2].
ACCESSION   WP_284907779
VERSION     WP_284907779.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. lyk4-R2A-2
  ORGANISM  Bacillus sp. lyk4-R2A-2
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Bacillus sp. lyk4-R2A-2"
                     /db_xref="taxon:3040282"
     Protein         1..351
                     /product="HAD-IIIC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40914
     Region          1..342
                     /region_name="FkbH"
                     /note="Predicted enzyme involved in methoxymalonyl-ACP
                     biosynthesis [Lipid transport and metabolism]; COG3882"
                     /db_xref="CDD:443090"
ORIGIN      
        1 makqikcvvw dldhtlwdgi llesdevklk psmkevltel dergillsia srndeaavke
       61 klsafgiehf flypeihwna kssslerise rlnihkdtil fiddqpfere evkavhpeit
      121 cwdavdylsl ltddrlrpvf itedarrrrr myleadkrqq eeekyegppe kfltslhmkf
      181 viseageqdl qraeeltvrt nqlnasgkty dyeeldffrq sdshlllvce ledkfgsygk
      241 iglslieetg dtwhvklllm scrvmsrgvg tillttilqe akkrgkrlva dfkqtdrnrm
      301 myitykfanf keiekgedgy ilfendlsmi qpfpeyvdvn ielnqkdpak q
//
LOCUS       WP_284907927             434 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC1 kinase family protein [Acinetobacter radioresistens].
ACCESSION   WP_284907927
VERSION     WP_284907927.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..434
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0004672 - protein kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=48983
     Region          9..410
                     /region_name="AarF"
                     /note="Predicted protein kinase regulating ubiquinone
                     biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport
                     and metabolism, Signal transduction mechanisms]; COG0661"
                     /db_xref="CDD:440425"
ORIGIN      
        1 mkkniwfesm rsvarigeta viaaktgiky ataaekpnna kmmrqtfesl gstyiklgqf
       61 iastpslfpr efveefqgcl dqtptlpfsy iqqvlasefa drdlseifas idetplasas
      121 iaqvhaaklk sgedvvikvq kpgvetilyt dlnvlhwatk llekvvpkvk fasladivde
      181 iktrmvrevd fieeaqnldd fieylkisqn qaatapkvyh qystrrvltm qrlygvpltd
      241 fevvkkyakd psqvlitamn twfgslmlck sfhadlhagn lmlledgrvg fidfgivgql
      301 kpevwtacia fmdalqhtny qamaenmlnm gmtdqqidvq vlaadlerlf sgvlladpqe
      361 ilssnpadln dimmdmvavg erhgirfprd fallfkqmly fdrfmrvlap ytdiyadqrl
      421 qmvqnmdpnl llkh
//
LOCUS       WP_284908010             104 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Acinetobacter radioresistens].
ACCESSION   WP_284908010
VERSION     WP_284908010.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..104
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11059
     Region          2..104
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mawvvlilag vfeivwaysm klsegftrlt pslitlffmv lsfgmlayam rtlplgtayt
       61 iwtgigaigs favgililge pitavrmlaa vlivsglilm kiss
//
LOCUS       WP_284908017             233 aa            linear   BCT 25-DEC-2024
DEFINITION  XRE family transcriptional regulator [Acinetobacter
            radioresistens].
ACCESSION   WP_284908017
VERSION     WP_284908017.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..233
                     /product="XRE family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=25900
     Region          1..64
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          <131..224
                     /region_name="COG2932"
                     /note="Phage repressor protein C, contains Cro/C1-type HTH
                     and peptisase s24 domains [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442176"
ORIGIN      
        1 mflheriqqk lkeknlkqad iarstgksta avtkwlrgen ipkaenlkai akllevsdew
       61 lltgknltvl dsqdlqplse wdettpieed eieipffqnf sfdcgsgsvg ealkaqsqal
      121 riskatlrdl giekenavat gasgdsmkpt ikdgdtiyld lgrktikdgk ifaichgglf
      181 vakrlynlpm ggvrivsdnt aeypevllta kerkeqefev igwvwritst esw
//
LOCUS       WP_284908202             198 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Acinetobacter
            radioresistens].
ACCESSION   WP_284908202
VERSION     WP_284908202.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..198
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23124
     Region          1..181
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mpeqdyfdtl yhynddpwgy tqrwyeqrkr qiclallprq rygrilelgc angvfsqela
       61 srcdellgld anskavelar qrlkgqlhid iqqkripqqc peekfdlivi seiayylnen
      121 ellqliewvq rslndtgtll cchwrypidg fslngnlvhq llkqhlklyh ylglddpdfl
      181 vdlwttdsgs lahqeglt
//
LOCUS       WP_284908204             776 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Acinetobacter radioresistens].
ACCESSION   WP_284908204
VERSION     WP_284908204.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..776
                     /product="PhoX family protein"
                     /calculated_mol_wt=85121
     Region          20..770
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mtqltpyhed qeldnntssn ihfrdileqr mtrrslitkt asgavalala stltgcnddd
       61 dnsnsgtapv tpndlnqkps klsftpvakn lddivtvpeg yqatviyalg dpinpmlgdw
      121 ndndippgps fqfrsgdchd gmhffglnsa tdrfddtvsa qgllvmnhey inqtflhlkg
      181 ptkvegrrpe deviretnah gvsvvhikkd patqkveivk nsvfnrrita stemdfagaa
      241 agssllatrf spagrqtrgt hnncgngytp wgtyltteen figyfqrsgh deyqrtnaek
      301 ialkryglgl kkdepylyel deqgapkkge dgkivyrkds ngnlipnidd qgrpvylgas
      361 sryawetvig qvesqdlydr wnadvkadqp tqdyrngpnt fgwmveidpf dggqrpvkrt
      421 slgrfaheds acravagqpl afymgddskg eyiykfvssa vwdpkdvnrg ytagdkymns
      481 gklyvakfns dgsgqwiels ygknglness stypftsqad vvtfarlagd avgatkmdrp
      541 ewatvnpvng eiyvtltnns nrgtsyptda anprnyddlk dkktqsgnvn ghiirfketd
      601 dkttaetfkw diylfgaeas masninlsgl tdnndlsspd gmwfdprgvl wiqtddgayt
      661 dvtncmmlaa lpgqigdgtt attssgqqtl mgakvtdstl rrflvgpkqc eitgiamtpd
      721 ykaifinvqh pgedsasyat pashwpatqt drnnttarpr satvvitrkd ggaiag
//
LOCUS       WP_284908212             202 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Acinetobacter
            radioresistens].
ACCESSION   WP_284908212
VERSION     WP_284908212.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..202
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23226
     Region          13..181
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 msdqqyadni ipiykkyaie wdkvrsqhfy eqawleqfln lipeqssild lgcgtgipta
       61 qyfsakkcqi tgidssaaml eiarnrfpeh nwleadmrql dlkqsfngii awdsffhlah
      121 ndqramfhif kkhaktgtal mlttgpshgt algemqgevl yhasldpdey knlfemfgfr
      181 vvnmrfedpd carhtiwlaq lm
//
LOCUS       WP_284908280             518 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Acinetobacter
            radioresistens].
ACCESSION   WP_284908280
VERSION     WP_284908280.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..518
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=59413
     Region          3..361
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mqksirqsma slhswtglll gwllfaiflm gstayyrhnl nlwmqpalaq iqvnqataln
       61 tayqylqnea shaktwylei atqekpfnkm ywqkqdgsyg sallnpatgq elklsgtqgg
      121 effylfhfql fgipvligrl iacfaaliml ialisgiith kkiltdfftf rtfkgqrswl
      181 dfhnicsvia lpffltitft glailfylyl pwslekfype nkyqyfeein qkiltkedhp
      241 kpaamlpiqq vlaisqqqwg itdyarlevk npnttsakit lvqstdysit rdapqltvng
      301 isgqiitdtk nrsaiatlns gvyglhmatf aqpllrfalf fsgilgclmi asglllwslk
      361 rhlqnktqaf hlgfylvdrl nvatfiglpt amlcylyanr lvsvqpggtn yeiysffisw
      421 lilfilaimt kkqwlwkiql aificlafsl piydlyylsq qnyisglshy wnflridlml
      481 wlfaflaffi yrniepiqlk ssqklsakii rntqevns
//
LOCUS       WP_284908392             258 aa            linear   BCT 25-DEC-2024
DEFINITION  DODA-type extradiol aromatic ring-opening family dioxygenase
            [Acinetobacter radioresistens].
ACCESSION   WP_284908392
VERSION     WP_284908392.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Vaillancourt,F.H., Bolin,J.T. and Eltis,L.D.
  TITLE     The ins and outs of ring-cleaving dioxygenases
  JOURNAL   Crit Rev Biochem Mol Biol 41 (4), 241-267 (2006)
   PUBMED   16849108
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Siegbahn,P.E. and Haeffner,F.
  TITLE     Mechanism for catechol ring-cleavage by non-heme iron extradiol
            dioxygenases
  JOURNAL   J Am Chem Soc 126 (29), 8919-8932 (2004)
   PUBMED   15264822
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..258
                     /product="DODA-type extradiol aromatic ring-opening family
                     dioxygenase"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016701 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28983
     Region          7..257
                     /region_name="45_DOPA_Dioxygenase"
                     /note="The Class III extradiol dioxygenase, 4,5-DOPA
                     Dioxygenase, catalyzes the incorporation of both atoms of
                     molecular oxygen into 4,5-dihydroxy-phenylalanine;
                     cd07363"
                     /db_xref="CDD:153375"
     Site            order(13..15,48,113,169,224,249..250)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:153375"
     Site            order(13,48,224)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:153375"
ORIGIN      
        1 mnlqtlpglf ishgspmlal dpeqvgpvle rlsinlpkpe aiivmsahwe sqalevsiat
       61 rpetwhdfrg fpaelyeihy rapgnpelae eilhllaeaq iqahannirp rdhgvwmpll
      121 hmypeaeipv ieislpmgms adeiyqigqv laplrerqil ligsgsithn laelnwhgnt
      181 sevpewastf rnhvvsklsh ssydevlewq hlpyiawnhp tlehlaplff amgtgsrfsl
      241 vhssfsmgal gmdiyrfd
//
LOCUS       WP_284908529             203 aa            linear   BCT 25-DEC-2024
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Acinetobacter
            radioresistens].
ACCESSION   WP_284908529
VERSION     WP_284908529.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..203
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23002
     Region          7..180
                     /region_name="YdeN"
                     /note="Predicted esterase of the alpha/beta hydrolase fold
                     [General function prediction only]; COG3545"
                     /db_xref="CDD:442766"
ORIGIN      
        1 mssihtvivp gvggseyehw qswlqrqlrs csrvqqtdwn mpvlqewivq fvktvslhqe
       61 slqivahsfg cltsiaalae ypelthrikn lvlvapanpe rfgeagfarn sqynyaeyfq
      121 nlkirvpaql iisdndpwfk ledaqffana wnlkpvslgk vghinvasgf gsfpeifdfl
      181 iaeknslnin itdntelffr fai
//
LOCUS       WP_284908574             669 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Bifidobacterium
            breve].
ACCESSION   WP_284908574
VERSION     WP_284908574.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium breve
  ORGANISM  Bifidobacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Bifidobacterium breve"
                     /db_xref="taxon:1685"
     Protein         1..669
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=73117
     Region          18..662
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtdntnatml amqkehgpll evrnlaidft tdtgkpvhav rdanftvypg qwvaivgesg
       61 sgkstsamav lgllpgtghv vngsikldge eiagakqsef dklrgtkmgl vpqdpmsnln
      121 pvwrigtqvk ealkannmdv dhekrsalak alagdevevk gnddetflga kelpelmtea
      181 kkalteagvs geafdkavar ftnewvpgse trwrvaddli kagvaddqaw ylakkyvigs
      241 tmddriagll seaglpdaat rarqfphefs ggmrqralia iglacrpdll iadeptsald
      301 vtvqkrildh lhmltdslgt avlfithdlg laaeraqhiv vmykgqvves gpslevlqhp
      361 qhpytkrlva aapslasqri isakergena dalldhhvag ertleksehi itvdhltkef
      421 klprkkemfk avddvsfsvk rgttlaivge sgsgkstvan mvlhllkpts gkvfyegrdt
      481 stfkakdllg frrhvqpvfq npygsldpmy sifrsieepl rihkigdkks ranrvkelld
      541 mvemptsvmg rypnelsggq rqriaiaram aldpdvivcd eavsaldvlv qdqvlrllnd
      601 lqaekglsyl fithdlavvr qiadevvvmq hgklvehatt devfdhpqkq ytrdlldaip
      661 ggklqlgld
//
LOCUS       WP_284908625             597 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Bifidobacterium breve].
ACCESSION   WP_284908625
VERSION     WP_284908625.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium breve
  ORGANISM  Bifidobacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 597)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 597)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Bifidobacterium breve"
                     /db_xref="taxon:1685"
     Protein         1..597
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=63466
     Region          13..584
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mkatiarivh lykvktfafk ciavgvalgi vatmclaqla stqliggrqt aqaatasrts
       61 rvtlsakrgr ildangtvla qsverytiva npeaaqefvp tdcnektkdy cdeidgkpvg
      121 atgaaavgrl lakaldmnam elgadlsisg qyvvlkkdvt pqvkrtiddl nlggivwgel
      181 sserlypdge lmgsllggvn dkgvgvagfe qmenktltgt dghqiyqrgn yggeeipgtm
      241 tesvaakdgk dvtltidrdv qwyakkimke ataqysaqwg iavvqnvqng eilaladsde
      301 iaagsdeakm nvsravsqtf epgsigkvis msgylqtglr kptdqytvpg qltvdgqtyk
      361 dafehgdehw tlagilqkss nigmvmagdg ytdeqryeyl tkfgigqstg ldlpgessgv
      421 ltspsswdar trntvlfgqg gytvnalqls nivatiankg vkqqqsiiks ddgntenksk
      481 atrvvdeqva aqmmdamesv sdsysafikv dgyrmaaksg taevqgadgk lssiisdysv
      541 aipadnprfv vtvvlkdptg fggltagpvs aqicaflmqk yevpistprk daipvtw
//
LOCUS       WP_284908681             249 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Acinetobacter
            radioresistens].
ACCESSION   WP_284908681
VERSION     WP_284908681.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..249
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28804
     Region          29..126
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mknliintsy dedfynsqvs dslrsakvya eylcqfvqpn svvdfgcgwg twlhafalng
       61 venligydgs wnsqekmind rinfigadln kpincstkfd laislevaeh lrresadtfi
      121 eslvrasdii lfgaaypgqg gtdhineqpq sywaekfisl dyspfdvlrp vfwgckdvey
      181 wyrqnsfiyi knntlafnkf ikngfrpier lefmncvhpe ayalsilhrn nlykfkrlln
      241 fiklikhdk
//
LOCUS       WP_284908701             341 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Bifidobacterium breve].
ACCESSION   WP_284908701
VERSION     WP_284908701.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium breve
  ORGANISM  Bifidobacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Bifidobacterium breve"
                     /db_xref="taxon:1685"
     Protein         1..341
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37352
     Region          1..341
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mlsfendysr aahpavleal aeannhlysg ygsdelteqa kakireacgq pdadvwflvg
       61 gtqtnqvvid titpayagvi tvasghpnvh eagaiefsgh kvltiphhng kmdpaeldef
      121 cktfyadgny ehmvfpgsvy vsqsteygti yskaelqaia dvahtydmpl fvdgarlgya
      181 ltvtgsdmtl edmaniadvf yiggtkvgal fgeaivftkh ntpkhfltri kqhgallakg
      241 fvlgaqfdal ftddlyfkia rnaneaadri realhakgyt ltfeaptnqi fvtmdqptid
      301 rlerdvklgf tekaddthtv mrictswatt peevdqliel l
//
LOCUS       WP_284908715             923 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Acinetobacter radioresistens].
ACCESSION   WP_284908715
VERSION     WP_284908715.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 923)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..923
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..923
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=104579
     Region          23..446
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          486..911
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mltrfktltl slcllglnta vfaqpilvks qqkieeykld ngfrvvlapn dkenkvyint
       61 iyltgslndp qgkgglahll ehlafkgtqn vkgeefqrrl dqytlmtnas tdyystryln
      121 ivrpdskaln evlyleaerm dklvlqqkfv pseieivkre reirldqpfa vlmdqmwksa
      181 ygnqylgrlp igdleelksi rmdelnrfyr twyapnnavm viagkfdkaa ilktidqqfs
      241 piparsvpeq vkvpkldstq iknrnfivrk gsdlakfhiy mdgkntkiqp alalapylyt
      301 mqpsghlyqs mvesglstav qsttwldqdf nlvfmgaiya pshdenkven tllssveknq
      361 nfndtelkrv qslmqnqads imnnataigs rlsdyvvssq gnwnqyfndl qavrnlntae
      421 lnqtlksflv pqhrisgdik ptpeeqkkal eqkqaaeqpk tldqqavsae plldasvykq
      481 qvtqyltnsk qlldqaekki qrgtlkngmq yalfptatrd dktyatitlq fgdektlfdr
      541 getlelmayl llrgtdqysl qdiadrsiea ggqasasade ngiviriqak kekfddffrf
      601 viellkkpkf eqsqfdliks qtlatldrpy tepdtvaalt marlieiyqp gdlryhfepe
      661 lakskiqtak veqvkqlyqq ffamdhaqva vtgefkpeqi kkllqrelgn wkggqpykkl
      721 tsehrvyqaq kvhvlseqre fgnyqsiltf pvgvdhpdap aliifshilg nsqlssrlaq
      781 elreknalvy gfgsdlqldp daavgglsie anytagrsaq vsqsvhkvld dllkqgvteq
      841 eleaakadim kqrvtalede rnihgmlnsq lergkrmesr akrdmaiagl nkadidavir
      901 kyikpehlve vmadqysqpq kgs
//
LOCUS       WP_284908716             354 aa            linear   BCT 25-DEC-2024
DEFINITION  amidohydrolase family protein [Acinetobacter radioresistens].
ACCESSION   WP_284908716
VERSION     WP_284908716.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..354
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40251
     Region          9..354
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mqdlgfnfid shihqwdpln tphsariavk vfgrypavld kvirlvkpke lieslgqtvy
       61 vtspylpqny qqdlgpyqae qvvhieahwh ddrdkgvige trfieslpfd ttrtqlgaiv
      121 atadprqsnf kkilklhakn ssrlrgirrm gavhedrgil awadqphlyt dkkflkgfeq
      181 laqhqlsfea wvystqlqdl iqlarqfpet sivldhlgtp agifgkvgkn tgltqtgrdn
      241 ifyqwqedia elatcpnvyt kmsglmmpvl ghqfhknkrl atkqqmidll spmilhalks
      301 fgtyrvmfgs nfpmdkvsts lvslidaysd ivasynasal knifydnarq fyrl
//
LOCUS       WP_284908749             239 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Bifidobacterium breve].
ACCESSION   WP_284908749
VERSION     WP_284908749.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium breve
  ORGANISM  Bifidobacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Bifidobacterium breve"
                     /db_xref="taxon:1685"
     Protein         1..239
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=26272
     Region          8..239
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mfadfntmve elggietmkn dfvsnvshei rnplavikny atmmrdmdmd kaqreecvrt
       61 iisaserlna lvtnilklnk lesqtivsqa vdydltrqlt deiltlddlf teknidlgcd
      121 ledramvhad lgittliwsn ilgnalkyte sgghvsftqr shgnmvsvei sddgcdmtpd
      181 eaahmfdkfy qgdtshaaqg nglgmamvkr avdlsrgfid vtstkgqgat iivrlpaaq
//
LOCUS       WP_284908820             406 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Acinetobacter
            radioresistens].
ACCESSION   WP_284908820
VERSION     WP_284908820.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616068
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..406
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=47069
     Region          163..299
                     /region_name="Methyltransf_32"
                     /note="Methyltransferase domain; pfam13679"
                     /db_xref="CDD:379330"
     Site            order(193..199,222..223,248..250,264)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
ORIGIN      
        1 mtspesfseq eqqflkefqq sldlnhferl ilsqyqgkle glqkitfrlv elqnqvklsg
       61 lyhyqtqdvt knytleeavl hitsllhdck qanlliashe lqlkknkkkv mltrtkrkdi
      121 iskdtplish drekqryvaq drlflkylgi tdekaqiips markwkqink fieifsgafe
      181 qitkqdkvri vdfgsgkgyl tfalydylke qkqklplitg velrpnlvsf cqeiaqksgf
      241 ehldffegdv rtyhpehldv mialhacdva tdfaihtgir lnasmimcap cchkelrpql
      301 espevlqpml qfgihagqqa emltdtiral llkaygyetk vfefvsleht sknkmilatk
      361 rknfkqpdqs vleqiralke mygirkhsle lllndqwdqq digckc
//
LOCUS       WP_284908933             429 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Bifidobacterium breve].
ACCESSION   WP_284908933
VERSION     WP_284908933.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium breve
  ORGANISM  Bifidobacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Bifidobacterium breve"
                     /db_xref="taxon:1685"
     Protein         1..429
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=47083
     Region          89..386
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
     Region          <355..>428
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
ORIGIN      
        1 mrrrrglsrr fgsvvkrknh ngvptcllar ypnpkepgkr vvrrfplgae alayawldge
       61 egfvrdyerg lsdwvppeer ervvklared favyaedfld syrtvdggrl rdstmrlkrs
      121 dmallvkafg gmpvseigrs dvgawlddgv sspytrrrcy qllrammsrl vedgviassp
      181 cvfpvprlpe srqamipaat rgelaliyda mpddtavavy lgavcglrig evcglrvgdv
      241 dlarrvlhvr havmrslsge wvlkepktaa sagdmpipeg laamleahik ahcdgggdam
      301 llsgartggi lppstlrgqf drarraagrp dlhfhtlrat aitaaaqsga spkeaqrygr
      361 hadarislel yqratedggr rvaeavfdsl vqtgrdrarv eaelaqager leaarrdver
      421 lekelsslg
//
LOCUS       WP_284908952             198 aa            linear   BCT 25-DEC-2024
DEFINITION  IMPACT family protein [Acinetobacter radioresistens].
ACCESSION   WP_284908952
VERSION     WP_284908952.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Park,F., Gajiwala,K., Eroshkina,G., Furlong,E., He,D.,
            Batiyenko,Y., Romero,R., Christopher,J., Badger,J., Hendle,J.,
            Lin,J., Peat,T. and Buchanan,S.
  TITLE     Crystal structure of YIGZ, a conserved hypothetical protein from
            Escherichia coli k12 with a novel fold
  JOURNAL   Proteins 55 (3), 775-777 (2004)
   PUBMED   15103642
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Okamura,K., Hagiwara-Takeuchi,Y., Li,T., Vu,T.H., Hirai,M.,
            Hattori,M., Sakaki,Y., Hoffman,A.R. and Ito,T.
  TITLE     Comparative genome analysis of the mouse imprinted gene impact and
            its nonimprinted human homolog IMPACT: toward the structural basis
            for species-specific imprinting
  JOURNAL   Genome Res 10 (12), 1878-1889 (2000)
   PUBMED   11116084
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..198
                     /product="IMPACT family protein"
                     /calculated_mol_wt=22477
     Region          1..191
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 mpftisspvq feeeikksrf laiaapvdne qavkdflety kdhstthqcw awkiehqirf
       61 nddgepsgta grpilatieg neltniivlv nrwyggvklg tgglvraygg cagqclllae
      121 kveviekkqa yfcchfnewa ilqyelnqqq iefqenytat gvevelllqv hqihsfnlkl
      181 qdisrgreql klqeqeha
//
LOCUS       WP_284908972             471 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Acinetobacter radioresistens].
ACCESSION   WP_284908972
VERSION     WP_284908972.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..471
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=51986
     Region          62..418
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mlniskpiil ndvvfkqstt qqagkewnwv nprhlqadhp anyyesslad whefnalqtd
       61 cecdvvvigs gllgastalh laeqgvetvv leknrvgsaa sgrnggqltp glarweagem
      121 aehfgyedak klwhftstea mqlideisek ygldfqrkrg hitaavhqgh lvgltqgada
      181 rkylgedhtr ivgkhelgey iksdyytggl idelggqihp lalnrgliya fcknggivye
      241 qteviaieea edgvyvrtat gtvkarksvv mavhhasfkl lpqkkqttlp fytyvsttap
      301 leldihellp eehpvydtqf qidyyrpvtq nrllfggqgt gscwspektl nylknrihtv
      361 fpqlkqveid fvwsgttdlt vngavdsrkf gskfpiyavh gwsghgvaqt vrigkaiavd
      421 figqssdfkm ltqidhanil fartlapvvi piaksaygvg almnpgkmvs f
//
LOCUS       WP_284908984             257 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Acinetobacter
            radioresistens].
ACCESSION   WP_284908984
VERSION     WP_284908984.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..257
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30122
     Region          2..242
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mllhlsdlhf gterpecina lrvfckeqqp ealvvsgdlt qrarfiqfyy ckqfleslqi
       61 pylvvpgnhd iplyhlwnrv fspftcyqyf fgnlenvlet ehfyiigvns vrrryhtrgh
      121 vsleqihetr ekleqaplhk lkiitshqpf ytepddphgl kdcpvlgrma levwgqyelf
      181 gilhghlhkt aiydltrlyn lkvdhpiyni hagtatswrl hknlpnsfnt vsisgeilqy
      241 wfneesqsfv lrtdvik
//
LOCUS       WP_284909065             514 aa            linear   BCT 25-DEC-2024
DEFINITION  acid phosphatase [Bifidobacterium breve].
ACCESSION   WP_284909065
VERSION     WP_284909065.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium breve
  ORGANISM  Bifidobacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130290
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Bifidobacterium breve"
                     /db_xref="taxon:1685"
     Protein         1..514
                     /product="acid phosphatase"
                     /EC_number="3.1.3.2"
                     /GO_function="GO:0003993 - acid phosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=54720
     Region          25..283
                     /region_name="PAP2_acid_phosphatase"
                     /note="PAP2, bacterial acid phosphatase or class A
                     non-specific acid phosphatases. These enzymes catalyze
                     phosphomonoester hydrolysis, with optimal activity in low
                     pH conditions. They are secreted into the periplasmic
                     space, and their physiological role remains...; cd03397"
                     /db_xref="CDD:239491"
     Site            order(150,157,206..208,241,247,251)
                     /site_type="active"
                     /db_xref="CDD:239491"
ORIGIN      
        1 mkmfrrlssv vvivllmpli lvampvpaaq adrlpnpdwv allsdyekdy wqaptdaahg
       61 gkvldaktme ldqnlavain hkaaedldnk glnaqrkral vdsdlqaeet mpdalgpvlg
      121 aymseglkqg klnavadvfs fnvastyask raamhprpyl nraessfggt ndlaglpatl
      181 dikqspswle hvpgysnlqk nssypsghtt gayswgiala gmipelapqi martseagnn
      241 rivlgvhypl dimggrigas aqngqywhne frssivpaar qlrgylterc qadehgstla
      301 acianvkang aggytngfld svasepvkdq asavrvytar ltytfpqnts qsgadfmapr
      361 gaadvlrlay pelhadqrna ilkataldsg yplwqssdgw qrinwakalc arvtldkngd
      421 vskvetadhv tftgpsvina qyanigkhpa sdsaagenss vsagpdlavl haaqrpalmv
      481 gagvlvtilg agatkavmgk rsekkraess tvrp
//
LOCUS       WP_284909191             572 aa            linear   BCT 25-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Acinetobacter radioresistens].
ACCESSION   WP_284909191
VERSION     WP_284909191.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..572
                     /product="long-chain-fatty-acid--CoA ligase"
                     /EC_number="6.2.1.3"
                     /GO_function="GO:0004467 - long-chain fatty acid-CoA
                     ligase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=63156
     Region          30..563
                     /region_name="FC-FACS_FadD_like"
                     /note="Prokaryotic long-chain fatty acid CoA synthetases
                     similar to Escherichia coli FadD; cd05936"
                     /db_xref="CDD:341259"
     Site            order(224,227..232,234..235)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(227,347..348,368..373,451,463,466,477,556)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(227,272..273,321,323..324,327,347..348,368..373,451,
                     463,466,474..477,537)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(272,323..324,327,347,474..476,531,537)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 miyaqrpwkk nlpaslqdyq fdatsipqnl selfdkavhd fsdaaafslv lptglaktls
       61 fkqiqyysdl laryfqhelq lqpgdvvglq mpnclhypia vfacwkagli itninplyta
      121 releyqlnds qakalivsdm flatfekvia knndlkslal vtvslsdffd apyqaliakk
      181 ietdaeaqgr lltpsidycs fsqvfkeaeq lpelqsqttt ialyqytggt tgrskgaiit
      241 hqnllslvrm tgdylrahns afnqqdsilt aiplyhifaf svnflmffeg gshnilvpsp
      301 rpisnlrpaf eqfkitwltg vdtlyaglla edwfvqnppe ltcaisggta lrpataehwk
      361 akigniiegf gmtetscaam lhppisiirq gsvgfplpgs eikivdvqgn evplgsagel
      421 cvkgphivqg ylnrpeesad tfvegwlhtg diaqldedgf cyildrkkdm vlvsgfnvyp
      481 neieaviaeh pdiievavig vpdvqtgeav kayiatrnps lftdeilahc kehltaykvp
      541 kvieilpelp kstvgkilra elrnlqqqlq sa
//
LOCUS       WP_284909149             610 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Acinetobacter radioresistens].
ACCESSION   WP_284909149
VERSION     WP_284909149.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 610)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..610
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=67422
     Region          9..573
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 msilfqptrl vgaiaiamgc spaifaedtt isaqldpivv tasksaekas evparitiie
       61 pevleqspia slpqllqtda ainmvqsggy gqlaeiylrg tesdhtlvlr dgirlnnass
      121 gsaslafidt tdiqqievlk gpasvlygtd aiggviqlvs kipeknsafi tgevgenkty
      181 kavigadlye egfyaqirgq rlesdatkvt nqktdttdta sfdqkgfstk igvkqkdygi
      241 svdyshnegs slydaytfng allkqdfene iinlrsrlnv adnfelntrl sqfkdevnqk
      301 dsadfvhskt qelelyskwn flpqqilltg vthrsldgyi lsygtpynen vdstgyylqh
      361 qfngsklntq vgvriednek ygshtvgqla aryqlldkts iytnigtafk sptlnelfns
      421 fngnpnlkpe estsyeigid qnlplgfktg lsayyteved ligsvnfgkl tninkatyqg
      481 gefyigwqke dlfakatysy vkpeneethq dlnrrprqgl tlttglqnki ygisaslvak
      541 skskdwnsny rnpgyatvdv naywnmnpni klftniqnig dvdyktayqd qgyyyvnggr
      601 lasagvtfry
//
LOCUS       WP_284909252             325 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Bifidobacterium breve].
ACCESSION   WP_284909252
VERSION     WP_284909252.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium breve
  ORGANISM  Bifidobacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Bifidobacterium breve"
                     /db_xref="taxon:1685"
     Protein         1..325
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=35017
     Region          118..283
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 msdpkrqakr atraerraae aaaqqaqaeq aakerkqqti igcivmaiiv vlvaiagfav
       61 ykamqpsnts sssqqsnmtv deaysklkkv stqpanaddk agfvisnkgy gqkaegapti
      121 siymeplcpg casvnrqldq tlvklmnsgq lnidlhflnf qdnkssdnys nrtfngaiyi
      181 aehdddpdhl msylsniyae dfqpgelsny epvsnaklek qavkagvsed vaaaafsgkn
      241 eyldwltasn nytilrpelf nssgafsspt ltingeywdl kqltladtsm vdgflksigl
      301 dadqvgvegk mpsigadgkp isvas
//
LOCUS       WP_284909263             443 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 30 protein [Bifidobacterium breve].
ACCESSION   WP_284909263
VERSION     WP_284909263.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium breve
  ORGANISM  Bifidobacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Bifidobacterium breve"
                     /db_xref="taxon:1685"
     Protein         1..443
                     /product="glycoside hydrolase family 30 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004348 - glucosylceramidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006665 - sphingolipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49176
     Region          35..442
                     /region_name="XynC"
                     /note="O-Glycosyl hydrolase [Cell wall/membrane/envelope
                     biogenesis]; COG5520"
                     /db_xref="CDD:444271"
ORIGIN      
        1 mgakifrtis qrhlmepieq ashegtfdve immkpgetmq rvvgfgaslt dssayllnet
       61 lddesrkqam tdlfdpdqgi glsmlrnpmg asdyardvys yddmpdgkrd dsmehfsiar
      121 dernviplih eakrlnpdle vvmspwsapa wmktngsmka gslredcrei yaryfvqclr
      181 ayrshgievh avtpqneply epthypsmam saqeetvfvr dhlrtamrea gfktlilgyd
      241 hnwdrcdypl alldgaaesf dgiawhwyag dpqsqsvvse rhpgklsyvt easggewipg
      301 fepafshlvg miiqalnhga nafvlwnial dehrgptvpg fgestcggll rvdserrkas
      361 keidyyglah fsrhirpgah vvptiatgnt dgarcvaaln edgsramvll ndgespitvr
      421 agwednaanv tltpkavati vwr
//
LOCUS       WP_284909417             254 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Actinotignum timonense].
ACCESSION   WP_284909417
VERSION     WP_284909417.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum timonense
  ORGANISM  Actinotignum timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Actinotignum timonense"
                     /db_xref="taxon:1870995"
     Protein         1..254
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26822
     Region          5..241
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mkatlpknqf kaefaaspqr arsgiwmtma satsaeicag sgadwllfdg ehapytvasl
       61 ldqlraasgy pmplivrpve ttpahikqvl dlgaqnlllp mvdtpeqara amravryapr
      121 girgvgasva ragnwgryts ymeeaeaelf vllqiesrea lshldellev egpdgffigp
      181 adlgaslgnp paeelhaivc dalakiraag lvagslafdd avaeqyiaag anfiattads
      241 tllvealaak fper
//
LOCUS       WP_284909937             602 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284909937
VERSION     WP_284909937.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 602)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 602)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 602)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..602
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <178..594
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 kkkydfliys aiwlviiilf ifslyhsieh ikiishtgti rsetqkvvkq elnnernddl
       61 ikrldnilik lrtgngengf qrcdnkefqq klnqmdsmwe smkkeiikvr ngasgdklyk
      121 lseeysvlsn qivfisekhs naklysfata lfiylifsti slliweyynk krfkrifytd
      181 nltkiknqva fenraieilh nasnkeyvll nididnfkyi ndthgyeygd kvliivaaal
      241 sktfniketc arigsdnfvi lakyrdslle diremltnai iseldmnvtq tisycigayl
      301 veidnlgyks insimdkani ahkvsktrgi sstvwynenl lkqlqmensi ynymykaien
      361 eefhmylqpk fqisslnvvs aealvrwfsp elgflspdef iplfeksgfi ieldfymlkk
      421 acsfvrktfm kknqytypia vnfsrvtiyq nsfyqrfldt vkeyeipfky ieievtesaf
      481 neisqpvisi leelkklgfl ismddfgsgy sslsllcsls inglkldksl lketfnrekv
      541 ysiiqciiem shrigmsvvc egietkkdle flntvkcdvg qgfyfskpie ekeffnkyvt
      601 kk
//
LOCUS       WP_284909959             742 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: RelA/SpoT family protein [unclassified Aerococcus].
ACCESSION   WP_284909959
VERSION     WP_284909959.1
KEYWORDS    RefSeq.
SOURCE      unclassified Aerococcus
  ORGANISM  unclassified Aerococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 742)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 742)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 742)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="unclassified Aerococcus"
                     /db_xref="taxon:2618060"
     Protein         1..742
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=84784
     Region          10..740
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 msekqnytke evldlcksym pedklafvsk aadfaerahr dqvrksgepy fthpiqvasi
       61 laelhmdpdt vatgflhdvv edtgislddi ayffsdtvat lvdgvtklgk lkyrsqeqqq
      121 aenhqkmlla mandlrvimv kladrlhnmr tlkwhkpekq vsisretlei yapladrlgm
      181 sqikweledt clryinpeay yqivhlmnak rderenyine tieklqaqme gviaepfeiy
      241 grpkhiysiy rkmkkqkkef seiydllair vlvdtvkdcy avlgvvhtnw kplpnrfkdy
      301 iampkanmyq slhttvlgdk gvpveiqirt yqmhevaeyg vaahwaykkg vtgevekddl
      361 ddqiawfqqi qdlqddsvda enfvesvked ifkdkvyvft pqgdvqelps gagpldfayq
      421 ihtevgnkti gakvnskivp lnyklengdi veiltsknsa gpsrdwvnlv atnraknkik
      481 rffklldree nlekgrqave davnesgfaf kdlytktrqa dllerfnfss lddlfaavgf
      541 gelsasavan rltekarakr reelhkkdle evihdeeekd rkpamtvrhn dgvfvegadn
      601 llfrlahcct pvpgddivgy itkgrgisvh rrdcknvdld delsdrliev ewentqddad
      661 isfevelvie afersgllne iiqvvspltk sisningnvd hktnmakirl rlaiqnidql
      721 dkiidkvkdi pdvyvveras tq
//
LOCUS       WP_284910067             400 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Aerococcus sp. UMB7834].
ACCESSION   WP_284910067
VERSION     WP_284910067.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB7834
  ORGANISM  Aerococcus sp. UMB7834
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Aerococcus sp. UMB7834"
                     /db_xref="taxon:3046342"
     Protein         1..400
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41666
     Region          5..399
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 mtqgvvvtgm aaisplgesv eenwqrvreg qhglktleaa gmtcpnlgvk vcaplpdrsl
       61 yastsgeevy ailtraaaka cyqmsglqve dfdpyragcy lgnglgglta iegalkgqsk
      121 sqiflqnlag qtamklaqdl sfrgpalaia tafassnsav geafraikng hldlamaggs
      181 eaclnpaglt ffdnltalsh rsdpnrasip fdrdrdgfvm gegaafllle slesaqarqa
      241 piygeivgyg atsdayhlta paphaqglgq amaqalaeaq idptaidyin ahgtstpand
      301 aseseaikqv fgvhaqelav sstksftghl lgaagaieai ftlcalsdrf lpptlglenp
      361 dqgldldyvp kqgrpanlry alsnsagfgg hnavlcfkrn
//
LOCUS       WP_284910170             358 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Clostridioides
            difficile].
ACCESSION   WP_284910170
VERSION     WP_284910170.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..358
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
     Region          58..356
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 fiyswklvpt dktpagkrdd islrekeaqi kkdlndgidt vggkmtvcql ydkknsqrkn
       61 ikratekgrq ylmnalkndp lgmraidtvk qsdakewair msekgyaykt idnykrslka
      121 sfymaiqddc irknpfefkl sdvleddteq kviltpeqeg rllafmekdk iyskyydevv
      181 llletglris efcgltthid mqnrilnidh qllkdsemgy yietpktkng krelpltera
      241 yqaiqrilkn rgkaqplivg gysnflflnr eglpkvagny egmvrglikk ynkyhtdklp
      301 nitphsfrht yctnmanrgm npntlqylmg hanitmtlgy yahgtfqsak aelerlac
//
LOCUS       WP_284910250             254 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Aerococcus sp.
            UMB7834].
ACCESSION   WP_284910250
VERSION     WP_284910250.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB7834
  ORGANISM  Aerococcus sp. UMB7834
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Aerococcus sp. UMB7834"
                     /db_xref="taxon:3046342"
     Protein         1..254
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29370
     Region          6..149
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 madknyqvfq evydllfdks lypawadfcq ealdrylpgq dryrlldvac gdgefaleml
       61 ergfdargyd lsedmvdraq arleeagyrd riyqgnmled qaetgydllt lfcdslcyle
      121 gpeelsqcfm aqakalkagg lfifdihsay qmnqvypgyq yieewddavf twrseqvrge
      181 gtidhllnif vedpetgyye rheelhreqi fplscyqdll kqagfvnvqv sadfsfeapg
      241 pesqrlfftc vkea
//
LOCUS       WP_284910397             222 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Aerococcus sp. UMB7834].
ACCESSION   WP_284910397
VERSION     WP_284910397.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB7834
  ORGANISM  Aerococcus sp. UMB7834
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Aerococcus sp. UMB7834"
                     /db_xref="taxon:3046342"
     Protein         1..222
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25001
     Region          4..213
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mkalkavifd mdglmfdtek vgyeqtkraa delgldydie vfkgylgtne qetlayihkh
       61 yegqpqvddf ialtvryiee alkdpdnidd kkglydlldy lrsrqiklyi asssrrdeii
      121 rnlegkgiag yfegivagne vkrakpdpei ylkafdltht edkqevlvle dskngvraay
      181 raglptivvp dlipadeevm kkavavkesl advipyiese ya
//
LOCUS       WP_284910437             219 aa            linear   BCT 25-DEC-2024
DEFINITION  YczE/YyaS/YitT family protein [Aerococcus sp. UMB7834].
ACCESSION   WP_284910437
VERSION     WP_284910437.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB7834
  ORGANISM  Aerococcus sp. UMB7834
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Aerococcus sp. UMB7834"
                     /db_xref="taxon:3046342"
     Protein         1..219
                     /product="YczE/YyaS/YitT family protein"
                     /calculated_mol_wt=23634
     Region          6..202
                     /region_name="YczE"
                     /note="Uncharacterized membrane protein YczE [Function
                     unknown]; COG2364"
                     /db_xref="CDD:441931"
ORIGIN      
        1 mttttwkral vlilgiaina lgivlitkan lgttavsslp lvlslatpls lgtllfifns
       61 vyiigqmvly rrdfqawqwl qlgvnlilsl vtdwsaaald wlqpahlwsq vlcliigcav
      121 lafgialeva adwlyvsaeg ivqaistcfa wpfgrvkiaf dgtitglavv fsflllggle
      181 gvgwgtllsa fligrfvaly qknlpvlgqv aawkerdri
//
LOCUS       WP_284910450             371 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Aerococcus sp. UMB7834].
ACCESSION   WP_284910450
VERSION     WP_284910450.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB7834
  ORGANISM  Aerococcus sp. UMB7834
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Aerococcus sp. UMB7834"
                     /db_xref="taxon:3046342"
     Protein         1..371
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40662
     Region          1..364
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mkiavigggi vgstaafyls qnpdidlsly dygvgqaska aagiicpwfs qrrnkawyrl
       61 anagahfype mlqdlkaagq psqayqgket wllkkktstr edvyqialsr rpeapligdi
      121 eiltpaqqsd qldewtydqd lvairqgaai vdgqglcedl qaaatkngmt syqakaqidf
      181 qddqilvite dgqsqafdqv ilatgawlgd llqphgyqvd vrpqkgmltv ydrdvsnwpl
      241 impegeadii phgqdtlylg athendkgfd lepdmtsman ifdtirtiip aidpedyrdv
      301 kvgtraytsd yapfygpvpg hsnlyaasgl gssglttgpi igyqlaqacq dkpqrlnped
      361 ydpspylekr v
//
LOCUS       WP_284910572             479 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Aerococcus sp. UMB7834].
ACCESSION   WP_284910572
VERSION     WP_284910572.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB7834
  ORGANISM  Aerococcus sp. UMB7834
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 479)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 479)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Aerococcus sp. UMB7834"
                     /db_xref="taxon:3046342"
     Protein         1..479
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=54661
     Region          2..466
                     /region_name="his_kin_PieS"
                     /note="two component system sensor histidine kinase PieS;
                     NF041210"
                     /db_xref="CDD:469114"
ORIGIN      
        1 mryfyqllla fivvilftls glsyvmirip eerfqnqtaq qldsmadyfe etsvnpdyla
       61 dkkellestg ikvflydqda qlvypktegq gtepvsnyld qqdlaslksg trqpmrafdm
      121 gfskedgdal atfvprfdgd ryqgfvaigk nnfefghrll gnrmdtlvaa llvggaalvi
      181 algisyflnq rigrirqatk evadgnyavr lpqdyddeig dlsrdfnrma aslegsieei
      241 nrrenirrqf mldvahemrt plttmnglle glryglipek hfdrsielvh netqrltrlv
      301 nqnldyekir sqeiflmpmt fklrqmledl alqldeaaks kedqilidcs detevyadwd
      361 rlrqilfnit qnaiqftdqg qvklqarets eateiqiidt gigmteeela niwerfykad
      421 esrkssayge sglglaivhe lihahgaqve vesrpgqgtr filtfpkake edcdnqddr
//
LOCUS       WP_284910648             431 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Aerococcus sp. UMB7834].
ACCESSION   WP_284910648
VERSION     WP_284910648.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB7834
  ORGANISM  Aerococcus sp. UMB7834
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Aerococcus sp. UMB7834"
                     /db_xref="taxon:3046342"
     Protein         1..431
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47537
     Region          17..425
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mdyetleell plaeegkmvl gldtmaqlma dlgnpqdqlp tihiagtngk gsaammlati
       61 leeagykvgl ytspsimsfn erimvnrmpv sdeaiiraaq aikgscerld lhltefevyt
      121 amawlifadk dcdlvvlevg lggrldatnl vkaplvtllm kiafdhvgil ghslgeiage
      181 kagiikagrp visypqdpea ktviqakaee mgapylevdp ddirdlpsdq arkqvfsykg
      241 qtwqlnllea hqlqnasvvl eaveslrqqg ypvtdqalar gldqvkwqar feimhdqpti
      301 vvdgshnldg vsqlklnler yfpdqgivai mgmladkdvt havaeivpil dqivtvrpnt
      361 pralsaqelr dkivsiypeq ydtivpsdsy edafnkamky lsqddvlvif gsfyyvgymr
      421 nlinkklgnd i
//
LOCUS       WP_284910748             319 aa            linear   BCT 25-DEC-2024
DEFINITION  DHH family phosphoesterase [Aerococcus sp. UMB7834].
ACCESSION   WP_284910748
VERSION     WP_284910748.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB7834
  ORGANISM  Aerococcus sp. UMB7834
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Aerococcus sp. UMB7834"
                     /db_xref="taxon:3046342"
     Protein         1..319
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=34385
     Region          2..305
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 medilqaiea ydtiiihrhq rpdpdalgsq lglkavleat ypdkkiyavg qtepslaqfa
       61 amdqvddetf nqalvivndt antaridddr yssgerlvkv dhhpdneayg dfsyvdttas
      121 scseiwartv ldpqnalkmt dqaaqnfflg ivgdtgrflf dntspetlai agkllafdfp
      181 asqlmqasme itpgqarlqa yvldhtqrsq dglvasvsls qaslselgls eaeshsivqm
      241 pgqikgvlaw vifveqadgt yrcrirskgp tintvaqafd ggghpkasga sipsaadqvk
      301 vlqalhdaaq tyqdqlgqa
//
LOCUS       WP_284910877             253 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Aerococcus sp.
            UMB7834].
ACCESSION   WP_284910877
VERSION     WP_284910877.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB7834
  ORGANISM  Aerococcus sp. UMB7834
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 253)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Aerococcus sp. UMB7834"
                     /db_xref="taxon:3046342"
     Protein         1..253
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28355
     Region          6..252
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mptytlitga ssgigeayar laasqgenli lvarreekla alkeeledky psikvdylvq
       61 dlsqidelet fyqktkayhi kcwinnagfs nskdflslts eevlelmkvd mlaptllsqy
      121 ylrdyqaneg aclvnvssva ghelmesspf yspmkfyisa fsenigrylh nqeaavqvki
      181 lapaavntaf invasqdesl taddvwkryn eadeiaafld qliksdkvla kvnldsrefe
      241 lldpqlpnrw akd
//
LOCUS       WP_284910965             198 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Aerococcus sp. UMB7834].
ACCESSION   WP_284910965
VERSION     WP_284910965.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB7834
  ORGANISM  Aerococcus sp. UMB7834
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Aerococcus sp. UMB7834"
                     /db_xref="taxon:3046342"
     Protein         1..198
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=21346
     Region          <1..189
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mekiyrevga dggfsfepiv aygangadph hlsdhsrpqv gdaivvdigc rhqgycsdmt
       61 rtfyygqvsd kdralyqltl eaqeagiaav kvgqatfqai dsacrttiaq agygdcfihr
      121 tghfigqeth eagnvsqant qvvqagqcfs iepgiylege tavriedlvi aqadgvevin
      181 hypkeltvip vkgererg
//
LOCUS       WP_284911005             563 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfatase family protein [Aerococcus sp. UMB7834].
ACCESSION   WP_284911005
VERSION     WP_284911005.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB7834
  ORGANISM  Aerococcus sp. UMB7834
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Sardiello,M., Annunziata,I., Roma,G. and Ballabio,A.
  TITLE     Sulfatases and sulfatase modifying factors: an exclusive and
            promiscuous relationship
  JOURNAL   Hum Mol Genet 14 (21), 3203-3217 (2005)
   PUBMED   16174644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Aerococcus sp. UMB7834"
                     /db_xref="taxon:3046342"
     Protein         1..563
                     /product="sulfatase family protein"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=63440
     Region          6..482
                     /region_name="ARS_like"
                     /note="uncharacterized arylsulfatase subfamily; cd16143"
                     /db_xref="CDD:293762"
     Site            order(14..15,54..55,109,111,270,322..323)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293762"
     Site            order(14..15,55,109,111,270,323)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293762"
ORIGIN      
        1 mtqkkpniil ifaddlgmgd vsafnpeski htehidalaq dgmrftdsha tsalctpsry
       61 glltgrynwr sqlksivipg daqsliekdr rtlpqmlkdh gyqtaaigkw hlgmewtlkd
      121 hkdyerygvd gdkyrdqead yqkgrpyfgn ataepifrgt didysqpikf gplnygfdyf
      181 ygtaasldqg pftiiendra lyqpeymagd hnisrvepet nrsieagvia pehspyhvpd
      241 qmqakaldvl ddmieadapf flyypnhlvh gpiipqerfr gksgigdygd fvlqldayvg
      301 eiadklkeag iyedtlfift sdngaspivd idrlkeeegh dpsnglrghk mhiwegghre
      361 ptivtyprmi eantvsnhmv shsdfyntia dilgedkrdn vaedsysnlp lwqgedqavr
      421 ediihsagng gfsirrdfwk limvkdgglg gydrnvdsyk etfqatelyd lrddlseshn
      481 viddhpdvvt elsqalvdyi kegrstpgep qtnqadlptg dweqvafmpd yedyvqglnq
      541 aavekgqisq eeldknsalk dkd
//
LOCUS       WP_284911009             264 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Aerococcus sp. UMB7834].
ACCESSION   WP_284911009
VERSION     WP_284911009.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB7834
  ORGANISM  Aerococcus sp. UMB7834
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Aerococcus sp. UMB7834"
                     /db_xref="taxon:3046342"
     Protein         1..264
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29966
     Region          6..246
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(29..30,32..33,36..37,74,78..79,82..83,113,117,124,
                     134..135,140,155,159..160,162..164,166..167,170..171,
                     174..175,200..201,203..205,207..209,211..212,214..215,219,
                     222..223,229,231)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(158,162,165..166,168..169,214,217..218,220..225,
                     228..230,234,236)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(179..186,202,205..206,209)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mkdkfilgry lpgdsfihrl dprakllamv lllififfan nvwsyallfa fvmfmvaltn
       61 islsvfikgl rpmvvlilft vilqlfftrt geviwqwgfl vltkdglmna afiflrfvli
      121 ifistlltlt tqplaitdal eslfspfrkv lpvhemalml sialrfvptl idetdkimna
      181 qrargvdfne gnlfervkaf ipiliplfvn afnraydlat ameargyrga egrtkyrelt
      241 wqgrdtlslv vvglvclgll llkd
//
LOCUS       WP_284911105             248 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Aerococcus sp. UMB7834].
ACCESSION   WP_284911105
VERSION     WP_284911105.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB7834
  ORGANISM  Aerococcus sp. UMB7834
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Aerococcus sp. UMB7834"
                     /db_xref="taxon:3046342"
     Protein         1..248
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28646
     Region          1..243
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mlsiyicedn diyrekleek ianylmindy dlkiaqstaq gtdilkeiqa spkqealyil
       61 didlgdqkmn glalggeirq ydpyacivfl tshsemmpyt ftyavealdy iikdsgqlsl
      121 trlqkaidty ykrytktqka ekrhfvvrva dtsrifpidd ilyfenseks hkvrlvhkqg
      181 eiefrsqlse ieavqevffr chqsyvvnle qiesvdhkla vlhmvdgsqc lvahrkkkal
      241 mnklksls
//
LOCUS       WP_284911176             254 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Aerococcus sp. UMB7834].
ACCESSION   WP_284911176
VERSION     WP_284911176.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB7834
  ORGANISM  Aerococcus sp. UMB7834
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Aerococcus sp. UMB7834"
                     /db_xref="taxon:3046342"
     Protein         1..254
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28736
     Region          1..241
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mhpvylledn psqlqaitgi iedyilfhdk sfylakasse peeiaaafsd qpkqpglyff
       61 dieikgqaeg islaqeikrl dpygriafit ahssyapltl qqhleplayi hkvdldslrq
      121 eiitcfelfy qrlypgqetk qaslqikags qtylvdlqdl fsiqttqkph ilefttrsst
      181 lqsygalkdf dqlpgffrls qsalvnldhi dqvspltrrl tlsngqvfaf srkykaalnq
      241 alaerenqsd qkak
//
LOCUS       WP_284911209             248 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Aerococcus sp. UMB7834].
ACCESSION   WP_284911209
VERSION     WP_284911209.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB7834
  ORGANISM  Aerococcus sp. UMB7834
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Aerococcus sp. UMB7834"
                     /db_xref="taxon:3046342"
     Protein         1..248
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27727
     Region          8..247
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mtrkrtsywp gqadkpaill mhslgdspnq veslaeslqq egyalylpyy rshqegdlkm
       61 vltaplstyl edarsalsfl kkeghqnvva aglslgafla lalacetdrv qavislscpi
      121 ltdlrqtrip yfmrqkyyrs legvptvadr dqaqelfeef dqvlsgmnqw mdenferlas
      181 ldqpvfighg qadevvsvqv aerlcrllst kgkpslhiyp qanhylegds vknclvqdic
      241 hflaslsi
//
LOCUS       WP_284911262             307 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Aerococcus sp. UMB7834].
ACCESSION   WP_284911262
VERSION     WP_284911262.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB7834
  ORGANISM  Aerococcus sp. UMB7834
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Aerococcus sp. UMB7834"
                     /db_xref="taxon:3046342"
     Protein         1..307
                     /product="metallophosphoesterase family protein"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33965
     Region          <139..275
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mrpgrlcpsd yaieeklyek dfpdhdkgly iigglygnpy aldeieamqv rdpepvslcf
       61 ngdthwfdcd pdlfqgleer lnchyrslgn veaellrtgd qeigcgcayp sstsdaavsr
      121 snaihkrlke mvrkaqipvd slqdlgksqv ftvyglrllv lhgdekflag wgcsaeslqe
      181 pgrqqeleaf mesyqidvia cthtcsqviy egkatlvinn gsagmgtlag dpagliirlg
      241 qvahpdaiys kkmnhvyvel lrvaydldlf msdfdqlwps gsaaavsyre rliqgtslpl
      301 riyspsl
//
LOCUS       WP_284911559             242 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor, partial
            [Clostridioides difficile].
ACCESSION   WP_284911559
VERSION     WP_284911559.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 242)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..242
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
     Region          10..231
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 lkgdkkltsi cicddekqqr nmlnkiitre mdlwgypyqi keysngeslv ynlehenyyi
       61 diifldielg ksngvdiakt irkhskdtii ifvtgfsdyv fhgydvgaln yilkpyktek
      121 ickvlkealk kleqwkenfi tvqigtnlck intkdilyfk selrkltvvt fdktleyygk
      181 lndmetvlps nfirthqryi vnlnhvdsit qtyakvqnek ipisrkkyqe vvgkftryml
      241 es
//
LOCUS       WP_284911722             661 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284911722
VERSION     WP_284911722.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 661)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 661)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..661
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>661
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          205..612
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mdkkklilit ydklnsdhyk eeltnffgde iiietqnild gikenlegdv vlslspltsn
       61 flikhfkedi eiihgtkals klgyekmmkl ppgtksllmt tnktsafema tylykiginh
      121 idfvptypdc deiydldtai tpgqirfipk yiknivdlgw rkisldtyms llvvlklkne
      181 kfieklykls ketlshdfln tsldnisklk tilymtidei gdgliffntf nkvtfvnksl
      241 lnmlgldekl ikspslmeym pksfldkitk nlnidnmiiy ideidkkfil skkpfylykn
      301 iegclitlkd vnnieileqk irsdsvkrgy vakykfnnii gnssiikdci kkakkmaltd
      361 npilitgetg tgkeaftqsi hnhsnrknkp fvaincaslp selleselfg yedgsftgak
      421 kggkkglfel ahtgtiflde igdmphdlqv kllrvlqeke irkiggtsii pidvrilaat
      481 nkdlekliie nkfrmdlfyr ismftldlpp lrkrledipl llesflkelp yknikldksl
      541 lealnsytwm gnirelrnci eymaymgsny ltindlpqni ssklnnnhms snmsifndln
      601 qydknicisi lkslhmkpmg rtklmkfmey nvteyevrnm leyltrngyl isskgrkgss
      661 i
//
LOCUS       WP_284911734             451 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284911734
VERSION     WP_284911734.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..451
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <7..443
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 ilqyskkmvr leklnvdlkn iaykdeltgv ntiekfklda nqnicihkdk kfavfyidfe
       61 nfkyindifg ydygdmilkr yanlmmndig kyeifareia drfvalrcyv dkedlvvrqr
      121 dvdnelinit neiknkhsit vvsgiccied vneklsidgl inranfaqkt vknkpgtnya
      181 fyndsirkkm ieentiksri heaiekrefi vylqpkvnlh sqkincaeal vrwltpdkgi
      241 ispaifipvl eknffialvd kyvfeevckw irkrldenkp fvqisvnvsr iqfyntkfve
      301 tysniqnkyr ipkntieief tesvafenqk hlleiihdlh engftcsldd fgkgysslsv
      361 lkdlpfdvlk ldsmffkasl dkdkekivik nivhmlkeln ittvaegiec keqveflrdi
      421 gcdlvqgfvf ykpmpilefe kildkefvyn s
//
LOCUS       WP_284911853             384 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Actinobaculum
            massiliense].
ACCESSION   WP_284911853
VERSION     WP_284911853.1
KEYWORDS    RefSeq.
SOURCE      Actinobaculum massiliense
  ORGANISM  Actinobaculum massiliense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinobaculum.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Actinobaculum massiliense"
                     /db_xref="taxon:202789"
     Protein         1..384
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=40867
     Region          7..380
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mseipsyafs trtvnttpde qygaitapiy lstsyrlpad gsaapysyqr snnptreaae
       61 kaianlegaa yaigtatgmg aistifshlk pgdhvvlsss vyggtflyvg effaergita
      121 efapdinhle evpgntamvy ietptnptfr vtdiahaahl ahgvgaklvv dntfstsylq
      181 rplehgadav vysatkfigg hsdvlagflv lddaeaydry ktaakalgnq lspfdsysil
      241 rglktltvrm dkqqenaaki ramlaqhpav arvlapgwys aeeaeiharq srgdgavfgf
      301 eladgvrhed faaglrlipy avslgsvetl iahpatqihe sltpqeraaa gisdqlirvs
      361 igiedsadli adltraldga laah
//
LOCUS       WP_284911863              88 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Actinomycetaceae].
ACCESSION   WP_284911863
VERSION     WP_284911863.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetaceae
  ORGANISM  Actinomycetaceae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Actinomycetaceae"
                     /db_xref="taxon:2049"
     Protein         1..88
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8986
     Region          1..>54
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mkktipaall teefkqrved tgmtdaavaa aigvtkqyfs avkngkeaps ikflagavia
       61 glgqnfgdia rpnpyafsqa ladskgaa
//
LOCUS       WP_284912007             288 aa            linear   BCT 25-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Aerococcus sp.
            UMB1112A].
ACCESSION   WP_284912007
VERSION     WP_284912007.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB1112A
  ORGANISM  Aerococcus sp. UMB1112A
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Aerococcus sp. UMB1112A"
                     /db_xref="taxon:3050609"
     Protein         1..288
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=32736
     Region          18..276
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mnkiwkalqg aeeksesell aelfkgaeal vigigagmsa adgftyvgpr fkenfpdfia
       61 kyglfdmlqa flndfeslee ywafqsrfvk lngldqeaga sylklkdlla dknyhiitsn
      121 adnafeaacf dldkvfyyqg kyvlfqcskq cqdvtyrddd miremvdrqe dmkvpselip
      181 ycpncgaple inkrdtvrgm vedahwheqe aaytdflaan egkkvlylei gighttpeli
      241 repfqeetld npqalyvmmn qkpyhipsel adqslrlsdd laqtfanm
//
LOCUS       WP_284912058             374 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal-phosphate-dependent aminotransferase family protein
            [Aerococcus sp. UMB1112A].
ACCESSION   WP_284912058
VERSION     WP_284912058.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB1112A
  ORGANISM  Aerococcus sp. UMB1112A
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Koper,K., Han,S.W., Kothadia,R., Salamon,H., Yoshikuni,Y. and
            Maeda,H.A.
  TITLE     Multisubstrate specificity shaped the complex evolution of the
            aminotransferase family across the tree of life
  JOURNAL   Proc Natl Acad Sci U S A 121 (26), e2405524121 (2024)
   PUBMED   38885378
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Koper,K., Han,S.W., Pastor,D.C., Yoshikuni,Y. and Maeda,H.A.
  TITLE     Evolutionary origin and functional diversification of
            aminotransferases
  JOURNAL   J Biol Chem 298 (8), 102122 (2022)
   PUBMED   35697072
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Aerococcus sp. UMB1112A"
                     /db_xref="taxon:3050609"
     Protein         1..374
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41143
     Region          1..371
                     /region_name="PucG"
                     /note="Archaeal aspartate aminotransferase or a related
                     aminotransferase, includes purine catabolism protein PucG
                     [Amino acid transport and metabolism, Nucleotide transport
                     and metabolism]; COG0075"
                     /db_xref="CDD:439845"
ORIGIN      
        1 mlnlspgpsh vtdkvlkafa qsktntdldh dytnyqrqve kkvsqvlqtd apsffmigea
       61 litleaaifs mveagdrvlv lsngvygagf adfvrfvgge pvlfeqdwrh gikldeleaf
      121 lekdsdfqva tfvhcetptg isndihgign llhrydilsi vdsvsgigge aidfdraqvd
      181 vllggsqkcf sapvgigtvt lsqkaldrld qrqspipsfy snfksylnfd ndhfdfpytm
      241 senlvyamda aldqtlshdf aakhakwagk trqifqeagf elyakdhpan tltavllpeg
      301 fnsfdvmaev keeglliang dgplgerilr iahmgsnmev ayfeamykal dkafqklgip
      361 sqislaeafr asdl
//
LOCUS       WP_284912266             281 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Aerococcus sp. UMB1112A].
ACCESSION   WP_284912266
VERSION     WP_284912266.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB1112A
  ORGANISM  Aerococcus sp. UMB1112A
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Aerococcus sp. UMB1112A"
                     /db_xref="taxon:3050609"
     Protein         1..281
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30637
     Region          15..281
                     /region_name="COG4132"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443307"
ORIGIN      
        1 mkqglgvfka fitvffllil avlvypvitm ilasfqdaas gaftlnnyke ifttniytea
       61 frnsilisly sslvglfvts latyaivsyl pkmreaflvl anltnnyvgv plafgfiill
      121 gnsgvlvmld qvlgwnilsd fniysltgll ivfiyfqlpm gitllipifd gldkrwseaa
      181 ellgansfqy wtkiglpila psligtfcim fanamgayds aialtgssin llsvrigntv
      241 sgdlfakpei gsslavvlam ilainmvfgh yvsnrlrrdl r
//
LOCUS       WP_284912267             259 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Aerococcus sp. UMB1112A].
ACCESSION   WP_284912267
VERSION     WP_284912267.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB1112A
  ORGANISM  Aerococcus sp. UMB1112A
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Aerococcus sp. UMB1112A"
                     /db_xref="taxon:3050609"
     Protein         1..259
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28551
     Region          1..258
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mskifkplvi fillayllip liitiiysfs sswtfsvlpd sltlkwyiql fsdpeflmai
       61 artvflatvt vvlslavivp tifaiaiyfp klmkyinlii ifcyslpgvi svmslseayn
      121 sigvpkmill fgsyvvgtlp lmtlgttnsl rsinakelie saeilgaskl esftkiilpn
      181 isngvissal fifsglfaey vtvnlllggk fttiqiylre qltanghyss aivvtyftla
      241 tlftvialvl vnrkrvkki
//
LOCUS       WP_284912353             260 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Aerococcus sp. UMB1112A].
ACCESSION   WP_284912353
VERSION     WP_284912353.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB1112A
  ORGANISM  Aerococcus sp. UMB1112A
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Aerococcus sp. UMB1112A"
                     /db_xref="taxon:3050609"
     Protein         1..260
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29716
     Region          2..256
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mtrlhatfys dtlrmdmhln ilvpqncert peairqkrrp pyrvlyllhg lssnedgwlr
       61 ftsleryard ldlvivmptt hrgfymntak syaysdfisl elpayiqnll pvsskredtf
      121 iagasmggyg alkaaftype qygyvaslsg vtdlsaryqe gpdpkspfef dllyggqdpk
      181 gtdkdiyqlv dqaieadidl pkvfltcgre dellgqnhdf rdryqdqlql sfqeadgghg
      241 wdywdthiqd vldwlptlsd
//
LOCUS       WP_284912373             347 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Aerococcus sp. UMB1112A].
ACCESSION   WP_284912373
VERSION     WP_284912373.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB1112A
  ORGANISM  Aerococcus sp. UMB1112A
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Aerococcus sp. UMB1112A"
                     /db_xref="taxon:3050609"
     Protein         1..347
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39052
     Region          1..345
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mseielrnis ksydgktysv knlklkieeg efivlvgpsg cgksttlrmi agleaitsge
       61 lliagekvnd kapkdrnlam vfqdyalyph mtvyknmayp lkmeklpkde idqkiqeaar
      121 llgieayldr rpkelsggqk qrvalgraiv rqpqaflmde plsnldaklr sqmryeiskl
      181 hrrlqttmvy vthdqteamt mgdrivvmdq gevqqiaspt eiyedpanrf vaeflgtpkm
      241 nfipaqelaq slvdipaplv nqtgidfgir penlslkdgs ryrvslienl ggslyvyldh
      301 qqfpdqhlii eipakeavee gktydlavdd wqkvrafsqe ttlavei
//
LOCUS       WP_284912393             540 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Aerococcus sp. UMB1112A].
ACCESSION   WP_284912393
VERSION     WP_284912393.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB1112A
  ORGANISM  Aerococcus sp. UMB1112A
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 540)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 540)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 540)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 540)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 540)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Aerococcus sp. UMB1112A"
                     /db_xref="taxon:3050609"
     Protein         1..540
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59397
     Region          20..532
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 makwtknlla sllaisliif ilwpvlavfi safqvgetsf slqpfwaylq ghrdlikqsl
       61 gvsltvmllt talalslaly yvgaplkiqk llrfflllsl isppfissla yinlfgrrgl
      121 itydllglrl dpygfwgivs metlgfisfs tlllinalqa ldqemiessr slgasvtqlm
      181 atvllpmirs siivvmlltf irsladfstp tiiggnysvl ateaylqmia ygnpekaali
      241 nviiilpacl afyfylkenn rqlssskvtr egrlftatks ktymglgllt wlvlllllaq
      301 ygsivylait dkikgesyft lsafrevlpy ledsllrtlv yalisalvav llssllayle
      361 hiqnqsyfka mdlvsmlpyi ipgsffglgy ilafsgkpla ltgtaaivvl nmtfklmpls
      421 tkimgtaavg mdpsifeasq dlgghwyqdy lrlflplskr agqlalvngf issmttfgsi
      481 iflvypgqkv ltlvlfdiig sgkyrlasal scilmgiciv fagltftlgd rkeyghainr
//
LOCUS       WP_284912413             228 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Aerococcus sp. UMB1112A].
ACCESSION   WP_284912413
VERSION     WP_284912413.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB1112A
  ORGANISM  Aerococcus sp. UMB1112A
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 228)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 228)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 228)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 228)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Aerococcus sp. UMB1112A"
                     /db_xref="taxon:3050609"
     Protein         1..228
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25386
     Region          2..>226
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mresktttfl swtiiaffll allyplinsf gvafleegqf tlqhfqnvfq tgnigqifkn
       61 slvialssal lsvfiaflma favnftnmsp glkralslli mipmllptit ygftiiysig
      121 nqglftrlln idapdfygfk glllgytiyt lpvtflminn gmsfidkrft lvsrlmgdky
      181 fkrlwtttlv pllpslgaav iqaffmaftd ygipsyiggn yeviatsl
//
LOCUS       WP_284912425             381 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Aerococcus sp. UMB1112A].
ACCESSION   WP_284912425
VERSION     WP_284912425.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB1112A
  ORGANISM  Aerococcus sp. UMB1112A
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Aerococcus sp. UMB1112A"
                     /db_xref="taxon:3050609"
     Protein         1..381
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=44289
     Region          10..371
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 myhskrskyr vflevffeav vwtailllgy fgimfvlifa ydyyyvqimq qnpfsiilqp
       61 yfqqnfflgf tlcyvviglg avawriyrry rtvqlgyild elhfisqgny dhrisskhld
      121 smkpvvssin rlvdstveam eeerrieqsk delivnmshd irtpltsvig ylgllesghy
      181 ndeeemkhya hiayikslql qrmvndlfey tkisqvniql nvmpinvvrm lqqmlvefem
      241 eaeqagrelr ldvpedqeii vdvdpeqlar vfsnlltnaf kyggdgdyvr vavsqdaket
      301 tfvvendgdq ipeealdrlf qrfyrvdssr sqeksgsglg laiaegvvfh hhgkiwaesd
      361 sqstrfifki pnhyqeerln g
//
LOCUS       WP_284912435             243 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Aerococcus sp. UMB1112A].
ACCESSION   WP_284912435
VERSION     WP_284912435.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB1112A
  ORGANISM  Aerococcus sp. UMB1112A
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Aerococcus sp. UMB1112A"
                     /db_xref="taxon:3050609"
     Protein         1..243
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=27741
     Region          1..241
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 misiyicedn kqelenittc iedyvminal dmkvelatdd pvsllnhvkr qsrgnnlyfl
       61 didlgndtig giqlaasirs fdvlspivfv tshdelvltt fkhavealgy iikdgpdsca
      121 gqirqildlv nkryltnpnn yrvftvrced svrifnvndi iyfqtsdthr vimthnkgqi
      181 efrmsmkeve kadpdfirch esfivnrshi seiskskrll klsngsicem sfrrmkqvld
      241 ain
//
LOCUS       WP_284912533             920 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Aerococcus sp. UMB1112A].
ACCESSION   WP_284912533
VERSION     WP_284912533.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB1112A
  ORGANISM  Aerococcus sp. UMB1112A
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 920)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 920)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 920)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 920)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 920)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18767243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Aerococcus sp. UMB1112A"
                     /db_xref="taxon:3050609"
     Protein         1..920
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=105297
     Region          1..903
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          1..201
                     /region_name="AAA_27"
                     /note="AAA domain; pfam13514"
                     /db_xref="CDD:433272"
ORIGIN      
        1 mkiqkieifg ygkwvdqtfy lepnlnvfig gngsgkstlm sfilsimfgf pnmrrkhsrn
       61 ydvnpnvnyg grlyltdtiy gqvmierikq qgrqqlfmtv ndnpreevss fdelfeglsk
      121 edyltyfgfd eedlmafvwe dedqfakslv slgvsgrqvl ngitpeleaq aadlylpngq
      181 kpqlnqelnq vaassqrldq aaaneqnyfa leeelqanqa eledlrkqes qaqdeqvklq
      241 iasqetgsve eknalgfela gydfhnfpeg aaetwhdlnq dlaryedqmd qtdgflvlde
      301 dqaeeepaqd slltigqewv lnhdhvsdqm laearayreq lnsdealkeq liqkryeehr
      361 llaalgaesi delpeeltas erqewqnrrq eldnrrifye ntkhdlqdlm aenqdlhdey
      421 devqseynsf kgtikertss wlktfglili vlalilaily fvtdkpfmmg sglaagalga
      481 lftiigflqs glgkrsvkke sqafdldlrd ieseqaeiqr ridiqndqla elenesqnfm
      541 aelqalvqek ggseyiqpli wldhdyvaqi naleaesnql iqatgaaqya aahdqewqdy
      601 aqaisnnpls qdsvfqafed dyhslrqlem dhaftaqtyq aeknqkqelh qsiqslrrar
      661 qdfldrygfe sadevedvla keaemlakke rfdllnhsln pqaaqlhdkd etidqqledn
      721 vhtlgqltqr iqdlvqrnaq lemqirelea sglvsklqad hasdvdqayd savewaankm
      781 avstfeqasv geegealerv lghanrylyd lsngemeklr yqnetvevls ednlwlavdq
      841 lsrgekallf vamrfaflna qlgqlnmpil ideafahidd yyrqniyrfl dersqdqqii
      901 lltidesaal nraskevtri
//
LOCUS       WP_284912634             420 aa            linear   BCT 25-DEC-2024
DEFINITION  NRAMP family divalent metal transporter [Aerococcus sp. UMB1112A].
ACCESSION   WP_284912634
VERSION     WP_284912634.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB1112A
  ORGANISM  Aerococcus sp. UMB1112A
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Aerococcus sp. UMB1112A"
                     /db_xref="taxon:3050609"
     Protein         1..420
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45813
     Region          6..417
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 msqvvttsqs twaskvkamg pgilmasaav ggshivsstq agasygwsll flvilanifk
       61 ypffrfgaey taetgktlve gyaekgkfhl wvffilnvfs alvntagvai lcsaiiasaf
      121 pminltitqw siilialiwa mllfggykll dgmakwimsa ltiatvlavi iaaiehpeys
      181 adfvertpwq laalpfivsl vgwmpapiei sainslwlae krksvdfnte dalfdfnvgy
      241 igtailavff valgaliqyp tgqaveaasa kyisqfvgmy asvlgdwsry litfiaflci
      301 fgtvitvidg ysrvneislr lllnkkeagq nslkiwmtlt aiiglvliqf fagqvatmlr
      361 famigsfltt pffallnyil vtrenknlps wlkilailgl iflfgfalff vyalligqag
//
LOCUS       WP_284912655             159 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284912655
VERSION     WP_284912655.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..159
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
     Region          <71..158
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 eeiqdiieki iielyepsvv nkvkikllvg lllvelvkns edvenhavdn yekmmiieil
       61 kyidkdykkg slseiasnln qgdykisklv kkhlgytfkd lvqekrlska cellvstnls
      121 iaeiienvgy enltyfykif knkygitpke ykkniknsq
//
LOCUS       WP_284912682             431 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284912682
VERSION     WP_284912682.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..431
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <7..423
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 rfkrifytdn ltkiknqvaf enraieilhn asnkeyvlln ididnfkyin dthgyeygdk
       61 vliivaaals ktfniketca rigsdnfvil akyrdslled iremltnaii seldmnvtqt
      121 isycigaylv eidnlgyksi nsmmdkania hkvsktrgis stvwynenll kqlqmensiy
      181 nymykaiene efhmylqpkf qisslnvvsa ealvrwfspe lgflspdefi plfeksgfii
      241 eldfymlkka csfvkktfmk knqytypiav nfsrvtiyqn sfyqrfldtv keyeipfkyi
      301 eievtesafn eisqpvisil eelkklgfli smddfgsgys slsllcslsi nglkldksll
      361 ketfnrekvy siiqciiems hrigmsvvce gietkkdlef lntvkcdvgq gfyfskpiee
      421 keffnkyvtk k
//
LOCUS       WP_284912774             136 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA polymerase sigma factor [Aerococcus sp. UMB1112A].
ACCESSION   WP_284912774
VERSION     WP_284912774.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB1112A
  ORGANISM  Aerococcus sp. UMB1112A
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Aerococcus sp. UMB1112A"
                     /db_xref="taxon:3050609"
     Protein         1..136
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=16299
     Region          <55..136
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mnkeyylfve gkkvfvskev ylayhselnk ekyqtrrdrl nncfffcsyd hdgnfeenle
       61 dlefdvekii etkemieevr raisklnpve rdlieslfyk eetirevaak lnishpavik
      121 rcnkvleklk emledf
//
LOCUS       WP_284912875             184 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator, partial [Clostridioides
            difficile].
ACCESSION   WP_284912875
VERSION     WP_284912875.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..>184
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
     Region          <1..>184
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 iqtdkaieil senrllnlmd rciirkveat ltkklsdldv nladsayigl vvhislalqr
       61 ikngenitmd keflkelsit eefklakeiv kgmetdfnmd ipvdevgyit mhirgakqrs
      121 ssnhkalnld dieimeitnk midlaedefk islknderlf kdlanhlgps inrlnmglei
      181 rnpl
//
LOCUS       WP_284912896             667 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284912896
VERSION     WP_284912896.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 667)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..667
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          203..579
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 svalvndsrk dlidflennl klvfgdsini nryfineind ndlinddvil vmsverldki
       61 innildkkkv ivvrrtfred kiynllslpq gtnvlivnds dettletisl fykigvtnir
      121 pipymndnny knikiaitpg vpekvpsfis difdlghryi distfieiin llqidskeiq
      181 snlvkyseei isldtgikdk ykelflkiee ldtilnlskd gilftskdge intynskvkd
      241 ildinediyg kyiedifvds lkvllsekei ldkvvvfnkk yinvnkkniy nrdekmgtyy
      301 slqeityikk leqnltkklr ekgqiakytf kdiktnspkm fecidlakkv sksdlsilir
      361 gesgtgkeli aqsihnnsnr knqpfiavnc aavpenlles qlfgydkgtf tgglkdgkqg
      421 lfelanngti fldeigdmpl elqtkllrvl qekqimpvgs hnvinidvri isatnknleq
      481 midnsqfred lyyrlntipi nipplrerke diliimedli nkklvitpea kkliqnymwk
      541 gnirelqnvt sylnimcedi vlekdlppnl rssdnkntsl klkyskndil nileililnk
      601 esdvgigrgl ilkalldknl qitegkikki feylkkeeli icssgrygsk itqkgedfyn
      661 klkykgl
//
LOCUS       WP_284912891             141 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A, partial [Clostridioides
            difficile].
ACCESSION   WP_284912891
VERSION     WP_284912891.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>141
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
     Region          1..>137
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 mkyniqlqvy egpldllydl itkhkidikd isiiditkqy lnylkmldkm dleitsefit
       61 masklleiks kyllykqkde eedprielme kleeyrkfkv asqdikenit yvnerfyrnk
      121 eeiiiddnvd ledisieaik n
//
LOCUS       WP_284912932             102 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284912932
VERSION     WP_284912932.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..102
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
     Region          <7..93
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 iqnsgnissq eiskkvfyss rhlnrlfnqy lglsmksfsr lvrinksikl lnnnktslms
       61 icnelgfydi phfikdfkiv cgitpqkyra nmsdfyseia kf
//
LOCUS       WP_284912952             130 aa            linear   BCT 25-DEC-2024
DEFINITION  deoxycytidylate deaminase, partial [Clostridioides difficile].
ACCESSION   WP_284912952
VERSION     WP_284912952.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Maley,F. and Maley,G.F.
  TITLE     A tale of two enzymes, deoxycytidylate deaminase and thymidylate
            synthase
  JOURNAL   Prog Nucleic Acid Res Mol Biol 39, 49-80 (1990)
   PUBMED   2247612
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788416
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>130
                     /product="deoxycytidylate deaminase"
                     /EC_number="3.5.4.12"
                     /GO_function="GO:0004132 - dCMP deaminase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006220 - pyrimidine nucleotide metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0009972 - cytidine deamination [Evidence
                     IEA]"
     Region          4..126
                     /region_name="ComEB"
                     /note="Deoxycytidylate deaminase [Nucleotide transport and
                     metabolism]; COG2131"
                     /db_xref="CDD:441734"
ORIGIN      
        1 mnkklenrcs wqeyfmrlce tvaergtcdr ayvgaiivns enrivstgyn gsisgdkhcs
       61 evghemrdgh cirtihaeqn alyycakegi svkdcsiyvt hfpclnctka iiqagikhiy
      121 yrtgyridey
//
LOCUS       WP_284912957             569 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease, partial [Clostridioides difficile].
ACCESSION   WP_284912957
VERSION     WP_284912957.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 569)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..569
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          <104..416
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 kkiielknii sekniedfks fskfmskyfa nffetkkysr gfdveankit qdrseeidnk
       61 diqkvikvag iradravsnd drnhvlsglt gkyfssykaa kdesesvftr leekleeadk
      121 elykiyngek seseepidgi fsdvidvikt yggaengidi aiessisekn llsdntnlsy
      181 rqggdcslpe tynglgylnl igilfeietk iqelfeqpad inllyieepe ahthpqlqyi
      241 firnikshik ahrkklledk nkqlqilits hsshivsecn fddiiylkkn enmviaksfn
      301 slkeeyggde qkgfkfvkqy ltmnrselff adkaiciegd terilmpmmm hkidnkekpk
      361 adlipllsqn isiievgahs hifmplfsfl gtkvlfvtdi dsvkaekkid kngkertvyt
      421 schpdegtht snasikeffk dtgidtsnnq fkelvgknae dkikdnmria yqipesdgey
      481 qassfedafi alnkdfilkn kegfyqygal kdfaadeies gdyykfalnn vkkksafass
      541 llyfdkedgn edekwtvphy ieegllwiq
//
LOCUS       WP_284913013             221 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator, partial [Clostridioides
            difficile].
ACCESSION   WP_284913013
VERSION     WP_284913013.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>221
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          1..>212
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mskvkrltdv wiyindkqkf tikelseefn lsaktiqryl kelnkmglpi qaeqgrnggy
       61 rvlnnsyipp viftekevmi ilfalkslqi ynyklmeiei nsimrkvsye rkssikvgie
      121 nikryigfva ndtndgdfks snvteffras seslilniky kcgnqilekn vcpigiylnk
      181 gawfspaydc ksgkiilvhi dniidikrtg eskkihinle e
//
LOCUS       WP_284913083             357 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284913083
VERSION     WP_284913083.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..357
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <1..353
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 eemfarisad nfiiimkyie eeditkrlkt ifeeldlfnn nqeekyklvl scgiyfilpe
       61 drdinsiidr aniphkmakg ghkssyafyd nkihdqeike kementmfss lenkefiiyl
      121 qpkielntge iqgsealvrw krpdkglipp nefipffern gfvinldlyv leevciylrk
      181 widaginpvt vsvnvsrihl ycnnfietyk niidkynipa kyieleltes iifdnfdili
      241 dimnnlkkig flismddfgs gysslnmlke ipmdilkldq kfimetynsk rskiivtkvi
      301 emakelgmkv isegveteeq fkllkevkcd maqgylfgkp mpieefehli vsnlvrg
//
LOCUS       WP_284913075             242 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Clostridioides difficile].
ACCESSION   WP_284913075
VERSION     WP_284913075.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..242
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27993
     Region          1..228
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mkniaaffdi dgtlyrdslm vehfkkliky diidqknwyk hardtfmdwd krqgnyddyl
       61 leicdlyvds lkgldktcin ftsdqviklk adrvykytrs riewhinqgh ivifisgspg
      121 flvekmakky nvtdflgsdy vfenniftgt vipmwdsisk nnaindfvvk ydldlsnsya
      181 ygdtngdinm lkrvgnpiai nptkellsqi sldeeisknv eiiverkdii yslstdvniv
      241 di
//
LOCUS       WP_284913153             135 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284913153
VERSION     WP_284913153.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..135
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <1..132
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 vtpkaksksi tlnlnefnsr iiphdkkwte esifnvldna vkytqvngei nisveetanf
       61 fkiiiedngi gieknefnni fkrfyrgsad eiesvegsgv glylsrkile eqggniivss
      121 kvgigskfsl flttm
//
LOCUS       WP_284913283             396 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284913283
VERSION     WP_284913283.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..396
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <1..388
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 yidfenfkyi ndifgydygd milkryanlm mndigkyeif areiadrfva lrcyvdkedl
       61 vvrqrdvdne linitneikn khsitvvsgi cciedvnekl sidglinran faqktvknkp
      121 gtnyafynds irkkmieent iksriheaie krefivylqp kvnlhsqkin caealvrwlt
      181 pdkgiispai fipvleknff ialvdkyvfe evckwirkrl denkpfvqis vnvsriqfyn
      241 tkfvetysni qnkyripknt ieieftesva fenqkhllei ihdlhengft cslddfgkgy
      301 sslsvlkdlp fdvlkldsmf fkasldkdke kiviknivhm lkelnittva egieckeqve
      361 flrdigcdlv qgfvfykpmp ilefekildk efvyns
//
LOCUS       WP_284913324             143 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284913324
VERSION     WP_284913324.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..>143
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
     Region          1..142
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 pdrgnivias nhksnldpif laaaienrei aaiakkelfk vkplgfilkk lhvmpinrek
       61 pdvstiktil rsvrdgyvlg ifpegtrikg dsfgkakagl svftiksksk vvpvsiisky
      121 klfskvivyi gepisfeehf kek
//
LOCUS       WP_284913396             353 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Actinomyces urogenitalis].
ACCESSION   WP_284913396
VERSION     WP_284913396.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces urogenitalis
  ORGANISM  Actinomyces urogenitalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Actinomyces urogenitalis"
                     /db_xref="taxon:103621"
     Protein         1..353
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=38071
     Region          131..353
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mstslplwqp aprraerswv waaklrvlvl viaelvllaw tpmaqfgffl vcpllwvvhd
       61 smrggmiatl sfaaavivva lltwpepwda vviavitsgy smfmglwiwr esqareaata
      121 alaakndald rlaqaqegla avereagrqa ererwsrdvh dtlaqgfvsv itlseaarae
      181 lgprapqpvl rrfdeleqva renlaearal vegsgpsrlr shgletalqr lgaaqeahgc
      241 stemtlrlpp hltqaiqvvv lrtvqeslsn varhararta rvlveqeatp ggvelvvrvs
      301 ddgvgiggrp egvgqsgmrs rveavggslt idplhapddg grtgtvvear ipl
//
LOCUS       WP_284913427             227 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284913427
VERSION     WP_284913427.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>227
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
     Region          32..216
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mnnylkfaty qligftssip rlikikknpd kfslkekfef mqkqakksld ivnielniig
       61 ketlpkepll fvvnhssmld sfiltasver pigcviadep vwrnipifke wakllrcvyv
      121 nrknnregik siaqasqnil tgqsmavfpe gdltwikepn slvsefrsga lkiaykakcp
      181 ivplviknsk dtyegyqpig kinsvpveve flepiydhie nprlkss
//
LOCUS       WP_284913419             134 aa            linear   BCT 25-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator, partial [Clostridioides
            difficile].
ACCESSION   WP_284913419
VERSION     WP_284913419.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 134)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 134)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 134)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 134)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..134
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
     Region          <9..97
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 ntlfgdttkh tsekyssgel ssydnhigdm gtdlymqnmq nslinheegr lyqidlalsk
       61 iengtygicd lchnqidler ldilpdtslc ndcakkennl lgdamqnpdv edsnfysedl
      121 tnltdlnkng ilrd
//
LOCUS       WP_284913449             244 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc ribbon domain-containing protein [Actinomyces urogenitalis].
ACCESSION   WP_284913449
VERSION     WP_284913449.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces urogenitalis
  ORGANISM  Actinomyces urogenitalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Rigden,D.J.
  TITLE     Ab initio modeling led annotation suggests nucleic acid binding
            function for many DUFs
  JOURNAL   OMICS 15 (7-8), 431-438 (2011)
   PUBMED   21348639
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446337
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Actinomyces urogenitalis"
                     /db_xref="taxon:103621"
     Protein         1..244
                     /product="zinc ribbon domain-containing protein"
                     /calculated_mol_wt=26326
     Region          4..243
                     /region_name="DR0291"
                     /note="Predicted nucleic acid-binding protein DR0291,
                     contains C4-type Zn-ribbon domain [General function
                     prediction only]; COG1579"
                     /db_xref="CDD:441187"
ORIGIN      
        1 mtraplaqqr llielqalds alarlrherr hlpvlariea tverlkankr eaviadagls
       61 eakkeatrre devgqvvrra gvlrerlssg gagardltai qgeidqlgrr qavleeaqla
      121 amesleaaqg evdrlaeeet afraagrelt aerdaefarl daaiaeeqgk rdflagsvaa
      181 dlladydavr eatggvgava lygrrvegaa veispqehar iaaadedevi haedgdviiv
      241 rmer
//
LOCUS       WP_284913455             356 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284913455
VERSION     WP_284913455.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..356
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <3..347
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 sndnfaiife kknnresiie icelirkkls miktslgvel nlipsigvyf veegetnist
       61 cldkamiakt tvkrkylkvy eiyaenlket lieerdieqe mhdalkneqf kvylqpkvdl
      121 sttkivgaea lvrwqhpkkg lispgvfipi fekngfitel dmfvftqvck nfkrwenenf
      181 ptfpisinls rvhlenpgfi seleritkey eiepnlieie ltesaifdnt kilfkimqtl
      241 ksvgfkismd dfgsgyssln mlkdmpidvl kldrqffitv gnakksqivv ssivqmakql
      301 dikvvsegve tveqaeflrf igcdmaqgfl farpmpieey eklildrysl nrketn
//
LOCUS       WP_284913463             317 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC1 kinase family protein, partial [Clostridioides difficile].
ACCESSION   WP_284913463
VERSION     WP_284913463.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..317
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0004672 - protein kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
     Region          <1..225
                     /region_name="AarF"
                     /note="Predicted protein kinase regulating ubiquinone
                     biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport
                     and metabolism, Signal transduction mechanisms]; COG0661"
                     /db_xref="CDD:440425"
ORIGIN      
        1 lvmekvngtk lsdvekirrl gyntktivei gvrsfftqvl shgffhadph pgnifvvakn
       61 kiayidfgmi giidnktlnq lneialagve knvdkiiyll iemdalngea dikglrqdll
      121 ylihyyydis iekinvtdil nelfrffrqy kivmpaqfvt laktvitleg tsrtlntdfs
      181 fgsmgkefmk hhykskfnpk nvvlssrqnv eeilldikti pkqlkailkn iernnikmqi
      241 edvkmtrlen ciieltsqis lslvlasiiv gssliiaspn ienniwikft aiagffisfi
      301 iglclvirsi rskykkd
//
LOCUS       WP_284913470             109 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284913470
VERSION     WP_284913470.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..109
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          1..97
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Region          23..57
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          62..85
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 keyekaidnf ksvvssgktk kyisesiyql aitnkllgnk deaikyykky intytkndqy
       61 yddsyyelgm lyydngdlkn aqqtfyslrs evpdsmynns kikeilsek
//
LOCUS       WP_284913493             544 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter, partial [Clostridioides difficile].
ACCESSION   WP_284913493
VERSION     WP_284913493.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 544)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 544)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 544)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>544
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..>431
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 msilvtllgl lvcttistvf skkwsnipla iyqivlgiil silpfkfsfs fnpeifvici
       61 iapllfsegq nvsrkellel rkpilllafg lvlitvfagg ifihflipgm plsvsfalaa
      121 visptdlvav ksitqglnfp knmmsilege sllndaagvv afkvavlatv tgvfsieeag
      181 iqfmitafgg iivgsilgyi iikirlslhk wnleeipmvi viqimtplfv yfvaeeigvs
      241 gilavvmagi ahgiekehlq ntttklriis dntwyvleyv lngfvftllg fllpsiytgl
      301 ssknenmale ltfistlivl ilfvirfiwv ylwhnsfikp kknplnnffv gflgfkdeev
      361 vkesiskcky slivatcgvh gtftlatals ipfyladkdv fpmrdtvlfi ssevilislv
      421 latvllprll knnvqesepl lsdkeaykli lkeailklsn ekaqevqpvi hdlneqlvds
      481 ekgilntpdn klismmiaea dqqgllavlk lledgkisdr afklyrfyit ksrksvqksi
      541 fkiv
//
LOCUS       WP_284913513             224 aa            linear   BCT 25-DEC-2024
DEFINITION  YczE/YyaS/YitT family protein, partial [Clostridioides difficile].
ACCESSION   WP_284913513
VERSION     WP_284913513.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>224
                     /product="YczE/YyaS/YitT family protein"
     Region          6..203
                     /region_name="YczE"
                     /note="Uncharacterized membrane protein YczE [Function
                     unknown]; COG2364"
                     /db_xref="CDD:441931"
ORIGIN      
        1 mgkislksmi rlfsgffifa issvlminah vglmpwdvlh qglsiklgit igqasimvgv
       61 vivildavfg enigwgtlln mtfigifidl vifsgvipha sntyigvfmv vigiilaaia
      121 sflylgvclg sgprdglmia lqkktnksvr lvrtileila lvvgwllggs vgigtlvsal
      181 glgyvlqivf rifkfdtkll khrfiiddir ewkekksneh kcks
//
LOCUS       WP_284913548             232 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284913548
VERSION     WP_284913548.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..232
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
     Region          1..192
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 fieatiksvl nqtyqeweml iiddcstdns pnivksymqq dsrikcikte tnkgvsnarn
       61 lalskatgqf iafldsddqw nssklekqvn fmlendyvis ftsyelmden dkklnkvikv
      121 ppnvdykrll kgnilgcltv vidkskldfe irmsgvrhed yvlwlsilkk ghiahginev
      181 lalyrkssns lsgnkikaam wtwniyrnie kiplykaiyy finygingik ks
//
LOCUS       WP_284913581              75 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator, partial [Clostridioides
            difficile].
ACCESSION   WP_284913581
VERSION     WP_284913581.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 75)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..75
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          <7..67
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 nkiksideel lytglkfinn dlnisktsts mflhrntlvy rlekineilg fdlknfenam
       61 ifylsvksyf lykki
//
LOCUS       WP_284913716             425 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Actinoplanes oblitus].
ACCESSION   WP_284913716
VERSION     WP_284913716.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..425
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45615
     Region          35..425
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mlrrtlltaa agavgvvtgg gavrasagtg ascragladl hdamaarvar gqlvgavylv
       61 ahrgrrhvgt vgtvaldsae pmrratpfri asltkpivaa aammlvedgr laldepidrl
      121 lpeladrrvl trldapldrt vpaarpitva dvltfrmghg mifepsfqpp ypivtrgdel
      181 rlvlaqpdpr tpldpdewtr rfgtlplmyq pgtrwqynta alvlgvliar aarrplgdfl
      241 hdrlfrplgm dhtgftlpra eaarlpglya tdpatgrlar qpgspprewt rppafpsgas
      301 glastlddya afsrflldrg vhhgrrllsa esvrllttnq ltpaqlaeag pypltgrgwg
      361 ygmsvsvvpd aisqpgrygw eggygtvwfn dpnrdltaia ltqtvdflfn ggadefqrla
      421 aaacp
//
LOCUS       WP_284913724             479 aa            linear   BCT 25-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Actinoplanes oblitus].
ACCESSION   WP_284913724
VERSION     WP_284913724.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Pereira,J. and Lupas,A.N.
  TITLE     The VCBS superfamily forms a third supercluster of beta-propellers
            that includes tachylectin and integrins
  JOURNAL   Bioinformatics 36 (24), 5618-5622 (2021)
   PUBMED   33416871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..479
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=49489
     Region          234..302
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          291..359
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          348..415
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          404..460
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 magaasrwvl alllgsstal vaatpaeavp aascavgavs aadraiaaql kpsmngrrlg
       61 qsvsgraiac arvvvgvvqq rklgqraali aittaiaese ltnhivavdh dslglfqqra
      121 sqgwgrpeql idptyatnaf lnamlrkypd srwmsgdiga icqkvqisar paayapevhd
      181 aalivaavws rpagtstprp attttpigpf qktlvtaqvp tagwdgrhal amadwngdnk
      241 pdlfvvtgag attgrteiri mdgatnflsl llvtatvlgp tderhayaft dwngdkkpdl
      301 iltqrsgtas grtevrvvdg asnfqkdlln tatglpatdd ryqfavadwt gdgradlvaa
      361 qtagtrsgkv evqvldgasn fqqvapavvs gtpagagvqv aaldwnadkr ldlvtlqngg
      421 lrawdgtglg rslaqanaav vgkevvvtdw nadghpdlaa vqaagttpgl aevsvlagq
//
LOCUS       WP_284912321             752 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Aerococcus sp.
            UMB1112A].
ACCESSION   WP_284912321
VERSION     WP_284912321.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus sp. UMB1112A
  ORGANISM  Aerococcus sp. UMB1112A
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Ingmer,H., Vogensen,F.K., Hammer,K. and Kilstrup,M.
  TITLE     Disruption and analysis of the clpB, clpC, and clpE genes in
            Lactococcus lactis: ClpE, a new Clp family in gram-positive
            bacteria
  JOURNAL   J Bacteriol 181 (7), 2075-2083 (1999)
   PUBMED   10094684
REFERENCE   4  (residues 1 to 752)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11909043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Aerococcus sp. UMB1112A"
                     /db_xref="taxon:3050609"
     Protein         1..752
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=83890
     Region          1..>35
                     /region_name="McsA"
                     /note="Protein-arginine kinase activator protein McsA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3880"
                     /db_xref="CDD:443088"
     Region          92..723
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 micqrcgkrq aaihmyanvn gkrqainlcq hcyrevindg gsqenykqnk pnqdlpwndl
       61 dsifrslrqn pagfqasskq genpfanfta gqgqssnneq sllstygtnm tdlaqnnhfd
      121 piigrdneir rvieilnrrn knnpvligea gvgktavveg laqkivakev peklqnkevi
      181 sldvaslvqg tgvrgqfeek mqqliqevsa nddiilfide iheivgagsa egsmdagnil
      241 kpalargelq lvgattlnef rqiekdgala rrlqpvyvee psveetleii qgitdkyeky
      301 hnviyspgai eatvrlsdry itdrqlpdka idlldesgsr knltipfvdl esldkqitql
      361 ndlkqmatea edyekaayyr dqlakyqemr dnhvdvpekr prvevediqs iveektgipv
      421 sdlqeqeqnq linleenlqs rvigqdeaie avsrairrnr vgltagerpi gsflfvgptg
      481 vgktelarql arelfgskda mvrfdmseym ekhsvsklig sppgyvgyee agrlteqvrr
      541 rpyslillde lekahpdvln lflqimddgr ltdsqgrvvs fkdtiiimts nagsagvess
      601 vgfaasqqgk tktvldkldd yfkpeflnrf daivefeplt keeliviidl mikemnhllk
      661 gqgiqvqvsp eakdelvelg ynpklgarpl rrvlqehied qiadaylkhp glkeisfdld
      721 gdkkitvsdl eennasdses gtdsasddge te
//
LOCUS       WP_284913730             278 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Actinoplanes
            oblitus].
ACCESSION   WP_284913730
VERSION     WP_284913730.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..278
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29001
     Region          2..274
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrifvagatg qigrllvpkl iadghevtgi rrgdtalral aeqgatgvrv dvydrealta
       61 amraaapdvl mhqltalgag nladnarirr agtrnlvdaa aaagvrriva qsiawayqag
      121 dtpageeapl dlgadgmrgv tvggvhalet qaaeiaehvi lrygmfygpg twyhrdgrig
      181 rqlldggftv gtgvtsflhi edaasaaala vqwpagvyni vddqplpgpv wagalaeaig
      241 apappvtpvr agwergadna lareklswtp ehpvfrmt
//
LOCUS       WP_284913784              76 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Actinoplanes oblitus].
ACCESSION   WP_284913784
VERSION     WP_284913784.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..76
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8334
     Region          9..69
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mppeeehrve vhldkllaer gltltelaer vgltlanlsi lkngrarair fstltalcdv
       61 lrcqpgdlft vrepva
//
LOCUS       WP_284913898             254 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Actinoplanes
            oblitus].
ACCESSION   WP_284913898
VERSION     WP_284913898.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..254
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27063
     Region          7..232
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 metsttwrpp llwrfllals rvviypfcrl rvtgdipaal rtgpiilaan hispsdpiim
       61 vaachkagla primmtgglf dapivgaamr acehirvdrg taqvadalpt aaqalkdgat
      121 vlvypegrig ldpwmwperg ktgvarmaaa agapvvpvam wgahavlpye aprnigrall
      181 rallhrprva vnfgapvdlt svtgspgaqa mqatrlimng idaaltplra demqtpkhvd
      241 tsrphdtsrv rprp
//
LOCUS       WP_284913912             253 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfite exporter TauE/SafE family protein [Actinoplanes oblitus].
ACCESSION   WP_284913912
VERSION     WP_284913912.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..253
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25289
     Region          37..250
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mivtllvaaa aagwvdavvg gggllllpal lvaapqlplp talgtnklaa icgtstaavt
       61 yarrtkidwg vagpsaalal lcagcgaala gsiqasvyrp ivlvvliava ifvtvrpamg
      121 laehmekrtp lrrgiavava ggliaaydgl igpgtgtflv lafttivgad fvhgsamakl
      181 vntgtnlgal ivfaatghvh wwlgagmavc niagavvgar malrkgsgfv rivllivvla
      241 livklgvdqm rmt
//
LOCUS       WP_284913940             640 aa            linear   BCT 25-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Actinoplanes oblitus].
ACCESSION   WP_284913940
VERSION     WP_284913940.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Pereira,J. and Lupas,A.N.
  TITLE     The VCBS superfamily forms a third supercluster of beta-propellers
            that includes tachylectin and integrins
  JOURNAL   Bioinformatics 36 (24), 5618-5622 (2021)
   PUBMED   33416871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..640
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=68316
     Region          365..427
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          419..485
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          475..537
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mrysggrrla tvlavagaia vpggtpapaa aaeavcpaad tllaalradp ltdeaagspa
       61 vlenvscalp watavvpaeg dydasfalfh vddatrqwkp lnvgsggvcd esvpadlaaq
      121 ldgcqpndpg ddlpdddpvd giegpvsaqa tasastlaas siggpitrae vlqraqgwvd
      181 nqpgpynqha fswdpthtrk yrrdcsglvg mswhlnadps trtlhlysnq isksdllpgd
      241 ilnlpaahtv ifkswksdhr hftyytfgst pvkirtaaid agtidshrat syvarrytki
      301 tgatpsptpt kptgkdaptv aydqgdgsmr myrwlsdgds fnrtsdydsg afhlsavgdr
      361 maagdvngdg kddvvmayql adgtfsfyvw rngnsaasvw ytsgrfslaa vggrlvlgdf
      421 ngdkkaepal aydqgdgtmr iyrwlsdgds fnrttdydsg afhlsavgdr maagdvngdg
      481 kddivmayqq adgtfsyyvw rngnsaasvw ytsgsynlnr vagrlvlgdf ngdkkaepal
      541 aydqgdgtmr tyrwlsdgds fnrttdydsg afhlsavgdr maagdvdgdg rddivmayql
      601 aggtfayyvw rngnyaarvw ytsgsfdltn vagrlvlgnw
//
LOCUS       WP_284913954             170 aa            linear   BCT 25-DEC-2024
DEFINITION  flavodoxin family protein [Actinoplanes oblitus].
ACCESSION   WP_284913954
VERSION     WP_284913954.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..170
                     /product="flavodoxin family protein"
                     /calculated_mol_wt=17551
     Region          3..160
                     /region_name="FldA"
                     /note="Flavodoxin [Energy production and conversion];
                     COG0716"
                     /db_xref="CDD:440480"
ORIGIN      
        1 mralviyesm fgnsatvars iaaglaltcd vtvadvremp tldgvgllvl ggpthafgms
       61 rpatradaar qgtirpgaeq tgirefldra pqlagmavaa fdtrsdtplp sgsagrkair
      121 rlrglggrpv levasfrvqs aqgplvagea drarqwgetl aasvrpgvtl
//
LOCUS       WP_284914041             294 aa            linear   BCT 25-DEC-2024
DEFINITION  amidohydrolase family protein [Actinoplanes oblitus].
ACCESSION   WP_284914041
VERSION     WP_284914041.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..294
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32086
     Region          5..288
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 msdhglvdah hhlwdlrrrp qpwldedgne pirrsfgmad lraaatrpig grplratvlv
       61 hclatveetr ellalaadep ligavvgwad ltspaigdri delragrggt rlrglrhlvq
      121 geadpawlqr peverglrav qlrglgydll irshqfeqgi rlaerwpglp ivldhagkpp
      181 iagrdlhgwe rqvrrlaayg nvvgkfsgli teadrrgwts pdirpvaevl lsafgperlm
      241 fgsdwpvctl aggwnrwaat vdellsgcta deadavlggt atsfyqlssv pkga
//
LOCUS       WP_284913964             114 aa            linear   BCT 25-DEC-2024
DEFINITION  VOC family protein [Actinoplanes oblitus].
ACCESSION   WP_284913964
VERSION     WP_284913964.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..114
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12569
     Region          9..111
                     /region_name="PhnB"
                     /note="Zn-dependent glyoxalase, PhnB family [Energy
                     production and conversion]; COG2764"
                     /db_xref="CDD:442048"
ORIGIN      
        1 mategieavf lethnwgkaa kffqalgyel efstdhnsgq lrngdgpyvf laevpetqvp
       61 rtqivlkvpd adtfradaav evvtpfedth ygtremtvrd pdgrlwslqa paks
//
LOCUS       WP_284914069             406 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Actinoplanes oblitus].
ACCESSION   WP_284914069
VERSION     WP_284914069.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..406
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42549
     Region          91..406
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 msaagpdrql lrrarralav qntvtvalil lmfglvtayt varaqraelq rslwktaata
       61 edvidppdgt wifrvapdgr ltstahpphg lpdraaldrv raggaaettg ididgsdylm
      121 vtrsrghstv qvvgslagee derhrlltal gvaglfglaa agaagtllar rataplgeal
      181 arqrrfvada shelrtpvtq lhtraqllqq dllagasrda maadvaqlvt gtgqlgevie
      241 dlllstgpah nagataevdl gvlaagvvaa faarahhqnv elalnpdpds pslvhgreaa
      301 lrrvvvalvd nalshtpagg hvtvelrfqr qensvrltvr ddgtgfdpad aerifdrfar
      361 ghgdhrrfgl glalarevva ghggtieagg epgrgatfti rlpapq
//
LOCUS       WP_284914152             123 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Actinoplanes oblitus].
ACCESSION   WP_284914152
VERSION     WP_284914152.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..123
                     /product="YybH family protein"
                     /calculated_mol_wt=12707
     Region          4..118
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mpgtpadvit efaaalhdgr vddavalyep daafiaepga dplrgtdqir aalagfaalr
       61 ptltpeirkv veaggvatvr hawtlegtgp dgtplrlsgt sadvvrrrpd gtwglliddp
      121 wga
//
LOCUS       WP_284914208             114 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [Bacillus cereus group].
ACCESSION   WP_284914208
VERSION     WP_284914208.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus group
  ORGANISM  Bacillus cereus group
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Bacillus cereus group"
                     /db_xref="taxon:86661"
     Protein         1..114
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12884
     Region          2..104
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mkqynipvea tlevigskwk vvilchltkg tkrtselkrs mpgitqkmlt qqlreleddg
       61 viqrkvynqv ppkveysltd ygwslesild slcswgechl ekegktsmli aege
//
LOCUS       WP_284914222             112 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Actinoplanes oblitus].
ACCESSION   WP_284914222
VERSION     WP_284914222.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 112)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 112)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 112)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..112
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12076
     Region          2..91
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtvplyqaka emfrtlghpv rirvlellqt gprpvrhlld eidieasnls qqlavlrrag
       61 ivvsfrdngl vmyalstpav adllaagrai laeiltdrgg llaqlqahqk sg
//
LOCUS       WP_284914231             676 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Actinoplanes oblitus].
ACCESSION   WP_284914231
VERSION     WP_284914231.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 676)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 676)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 676)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..676
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=73169
     Region          33..668
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mgalptarrr hggvdgrgek stagsddpsg rprplghlqr aaprrrttiy llilaalavp
       61 agsavaitrl qqsaatrgel rvllaeveka awqqnalrsr allakslpat laqtrdqidr
      121 tvdtigatfe rrdpgdryar avqdafltyd avvdrefdll esgdlltaer vdenqavptf
      181 ialraaldda arhydrlarq ssgrarigtv lilalaacgl aglvsrahri rtrafrravh
      241 qathdaltgl pnrvrlhdei tatiattdad atsgaallli dldrfkeind tlghhygdrl
      301 lilvarrmrd tvrggetvar lggdefavll pgitgaqdaa aaatrlheal qqpfdlggis
      361 lavggsigaa lyphhgttad ellqhadiam ytaktrrtgf tvfepgqgst dprklslaad
      421 lrhgmardel tlhyqpkvda rtgdvlgaea lvrwqhpehg mippsefipl aehtglitpl
      481 trivldsalr qcrawrdegh qlsvavnvsa hglldrdlat evadrlrrwr vpahlltiei
      541 tetaimtdpg ralqvveqlh algvrlsidd fgtgysslay lknlpvhelk idrsfvscmt
      601 tshrdavivr stvelgrnlg lrvvaegved datwraleaa gcdvvqgyli srpvppaefs
      661 awlhhrgsaa pvavan
//
LOCUS       WP_284914237             353 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Actinoplanes oblitus].
ACCESSION   WP_284914237
VERSION     WP_284914237.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..353
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36542
     Region          7..187
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mipvseavla atlawylaas gvghpapvfa assalvvlae srgrrlrqsa eivlgvaagv
       61 lvadlavqll gpgtltiavv llltvgpmia agasttlivq aaisaiyivg vaeprtdvmq
      121 grcvdaligg vlavavsqla varnplaplv aearqtftdl aglldtidqa lrdgdrdaad
      181 galrrardah arverletav latgetlklr vrrrrhlsqv rqveatavel drvvdniwvl
      241 arnavtltrl dvpappalsr algalgeail aageslatdl tgaddpqqha gradhtalea
      301 vriaaklles qpalpltmii gqirataidl lrgvghddnv lnrvdeavgl ttp
//
LOCUS       WP_284914262             225 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Actinoplanes oblitus].
ACCESSION   WP_284914262
VERSION     WP_284914262.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..225
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23595
     Region          <67..158
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mtapalvcpa aldiydrals laatgrrspl ilrgddgrea rvdaaqwcld rrpgddgllr
       61 rcagatldig cgpgrltaal lrlgraalgi dvsaaavrla rqrgatalrr dvfaplpghg
      121 rwehllladg nlgiggdpaa llrrcrella ptgrlhvele ppgsgswsgv atlhdggdgp
      181 gaplswarva addldplarp aglrtvanwt eegrwfaslt pderh
//
LOCUS       WP_284914280             377 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Actinoplanes oblitus].
ACCESSION   WP_284914280
VERSION     WP_284914280.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..377
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38360
     Region          1..364
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 msaalsglvv adfsrvlagp latmtladlg avvvkverpg sgddtrawgp pwgtrsssyf
       61 eglnrskysi aldfadaddr ataldlagra dvvvqnlnlt gfgldyesva avnpgvvycs
      121 itgfgagagl pgydflvqav gglmsitgea ggeplkvgva lvdvltakda tigilaalhr
      181 rratglgehv qvdlmssllg glvnqasgyl atgvaparmg nrhpsiapye tlrcadvpia
      241 iacgndrqfa rlcevlgvpe lagdarftdn psrvahreal vtlleaalaa apaavweerl
      301 taagvaagvv rdigqaidra salglaplvd gqirhpvryg sgpvaspapp pglgehsslv
      361 rdwlagkgpl ahpgaga
//
LOCUS       WP_284914274             250 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Actinoplanes oblitus].
ACCESSION   WP_284914274
VERSION     WP_284914274.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 250)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 250)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 250)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14398449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..250
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26927
     Region          21..105
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          166..246
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpvarqsriw psggvhlwss gdtgeahshr rghflyaasg vlsvhtargt livpanraaw
       61 lpagavhhhr ahgdtdlriv flppslarla pahpavllas glarevlltl tgtrqldgga
      121 rarlhrvlvd elreapeqpt rlpeprddrl ravarilddd padtsslaal gqrvgagart
      181 lsrlfhdelg mtfyewrtql riahalvlla eghdttrvar acgwsnpshf iaaftavvgt
      241 tpgrhrattg
//
LOCUS       WP_284914295             267 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Actinoplanes oblitus].
ACCESSION   WP_284914295
VERSION     WP_284914295.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 267)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..267
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27741
     Region          10..260
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mttpsenpfa vvtgassgig yelarrlaeh ghdlliiaed egiedaaadl rrdgrnqvva
       61 vradlaerag veqawaavea tgrdidalal nagrgiggaf vggtdlaael diidvnitst
      121 vhlaklalpg mvargygrvl itssiasmmp gtyqavynas ksftqsfaea lraelkdtgv
      181 tvtalmpgpt dtnffhraem ddtrvgtgpk ddpaqvaeqg irallagkek vlagsaktra
      241 qavaskimpd sakaemhrkm aepgsgn
//
LOCUS       WP_284914315             493 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Actinoplanes oblitus].
ACCESSION   WP_284914315
VERSION     WP_284914315.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 493)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..493
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=52882
     Region          28..480
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 meaplersds phlfsgstld gytsgvwhas alladrvkav rqpysgagva elqeqvdtid
       61 ldrplgdtga alheiarlyl dnavwfhept yvahlncpva ipalsaevli savnssvdtw
      121 dqstagtlie rrlidwtagr igfdpgadgi ftsggtqsnl qalllareet lagpagdrat
      181 tipklrifat teshfsvsks agvlgmaada vvgvatdgtg rmdpealaaa iddvrrdggi
      241 pmavvatagt tdlgridpvd aiaaicesrg iwlhvdaayg cgllvsrrrn lldgierads
      301 vtvdfhksyf qpvsssaivv rrgetmrria vhadylnprt aavpnqvdks lqttrrfdal
      361 klwmtlrtmg aeqigamfda vidrahevyl eicddpdfea vaaptlstvl fryrpagttv
      421 aecddlmprl rqrlfhggra ivagttiggh ywlkftllnp nttmddlrsv ldlirgigae
      481 mtgerdeaaa vma
//
LOCUS       WP_284914327             217 aa            linear   BCT 25-DEC-2024
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Actinoplanes
            oblitus].
ACCESSION   WP_284914327
VERSION     WP_284914327.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439579
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..217
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21759
     Region          18..>182
                     /region_name="PssA"
                     /note="Phosphatidylserine synthase [Lipid transport and
                     metabolism]; COG1183"
                     /db_xref="CDD:440796"
ORIGIN      
        1 mstaprtspv vfgeyldaan vvtlangavg glalwlalag ragaclgllf lavvldhvdg
       61 yvarrflepg tarrafgara dsladllnfg avptavislt assaqpvaal vgatfvvlgi
      121 vrlahfdita epdphlstgl pttyagflvg clsaltvtgl vatgpylvlc avvavaqiar
      181 lrlrmpgtgr clglvtgaav vttlvavvlg dagalvr
//
LOCUS       WP_284914335             317 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Actinoplanes oblitus].
ACCESSION   WP_284914335
VERSION     WP_284914335.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15747380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..317
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34678
     Region          31..190
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          228..311
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mivttppqrv dvhtqdrdda vaavnrivah earidalagh dlsltfhsvs ygdlsalrlr
       61 msgvhytata atmpavfagi ytdglaairt sqgeqslgpq dgllypeglp stadfrdtgq
      121 qflvvprsva aeltgitdlr frfggpvsea krrfwvrtvg ylseqltipd lvhpplvveq
      181 flrqavaaml ivfpnttmte ayppgpgrae psvvrramef methadqpls vtriaaaagv
      241 gprglqeafr rhrsstpmaq lrrirldrah rellahdgtv eriarrwgfa dpgrfagyyr
      301 eaygrtpaqt lrsgtap
//
LOCUS       WP_284914421             898 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Actinoplanes oblitus].
ACCESSION   WP_284914421
VERSION     WP_284914421.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..898
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=94599
     Region          9..826
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mtaadvssre aevltlvgrh lsnaeiaakl fisvrtvesh vsallrkldv adrralarra
       61 gaggaprnpl ptpltsfvgr aaeraalagm lathrqvtav gpggvgktrl alavaaeigg
      121 dhpdgvwfvd lvpvtgpgpc vvaaavaaam gigeqlgram tesvvdalad rdvllvldnc
      181 eqvrdgvapf lekllstcpr vtvlatsrar lmvpfervyp vpplsldggg esdavalfmd
      241 raaaaswppn halrdpiaaf carldgmala ielaaarwpt lgldgltagl adplrmlegg
      301 srtderhrsv raaldwshal lapadrallr rlsvfvapft reaasevaga tadglarlae
      361 qsllvvlpss sgtefrllet irqygteqlt amgelaeara rhlrwcerqa delrgfaegw
      421 rvrfdavadd lraaqawsdd ypltrklael tfarklaaes qirfeqaaal atdpaeaaem
      481 frqaaavagc rirgddayry llaaaeitpd paaaardlat aattthrfwg kfdhlparqe
      541 tielverarg lagddpaara avalaeagvl sdafgaaqgp adnavpetva raeravdlah
      601 qlgdplaesa aldaligarc wagdtfgtaa tarrrivlla atpdtpaash elldalgmat
      661 etalgagdlp garrtgrqla ehplmsevgh rgtcwlvvte alagdtgavl rygerflesw
      721 qragrpaksa lapaaaavam vhglrgerde rerwlavlaa mgvtaeytyg ygavfdaivl
      781 ldrdrvaeaa drlepepdev wkwvtwiwlh wyvalraeaa vlsghpraaa riaaarrtva
      841 gnpvatalvd ragallagdp agvrataaaf eaagcayqaa rsrrlsgspa paastrtg
//
LOCUS       WP_284914445             344 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Actinoplanes oblitus].
ACCESSION   WP_284914445
VERSION     WP_284914445.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 344)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..344
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=35884
     Region          49..344
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mgvrlrftll ygvlflisga gllaitaafs isrtthvapq gtgvppaeqi arlqeelasa
       61 saaqsrqlav galvalavml lvslalgraa agrvlrplrr itaatrrita dnlhsrlavt
      121 gpadevkala dtidellgrl eeafaaqrrf vadashelrt platvraaid vaeakpappv
      181 evvrlagrvr neldqlerll egllvlaraq hgaldgrtpv avrslipagv pvegtdfrtv
      241 gnpvllarmv snvvdnarrh nepggwmrvt lapgelvven dgpvldpgqv atlgrpfrrl
      301 gadrtgggtg lglaiasava sahggslglr arpegglrve irlp
//
LOCUS       WP_284914501             358 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Actinoplanes oblitus].
ACCESSION   WP_284914501
VERSION     WP_284914501.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..358
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=38203
     Region          1..358
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mtrilisgag igglalaqal rqggldvavy erepsprsrn qgyrlhvdpn gnaglraclp
       61 tavldrvrdt ggvngdlvas fthelrqvha qefpgvpdse ltnvdrdafr qglltgleev
      121 vffgrpvtgy eitpagrvsi gfdegdllvg adgvgsavrr rllpgvaprd lgircvygrm
      181 plpgaplppd fergfcwvad rkgfgagfap mrfrdgrpgy lmialvaaad rfdrrqhdsa
      241 elwrtvadat adwhpeiqki iayadstsff piairasdrv dawptgpvtl lgdavhtmpp
      301 aggvgantal qdaatlagel lagkplleav aayekvmlpr gfdtveqsvr miaqmtap
//
LOCUS       WP_284914578             332 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Actinoplanes oblitus].
ACCESSION   WP_284914578
VERSION     WP_284914578.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..332
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35736
     Region          2..301
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtrptarvlt llellqsggl rtvgdlasrl gvdertvrry aahlidldip veavrgrhgg
       61 yrlarghrlp plmlsddeal avllgltsqa ggtagetaaa klrrvlpvrl arrldavpas
      121 laftgprpaa pdgavllpla aavrdrqpvr ltyadrgeri fhpyglvvhs grwyavgldp
      181 aaaeertlrl driadvrglp gtfdrpaevd pvdrlltgfa taayrhrvrl riratvaeir
      241 aafpagvavi heetapwlrv elraenldwi parlagvdrp fvvdhpaelr dlvvaladrl
      301 avsarrsaae aepvpgpggt adrpehdagp gr
//
LOCUS       WP_284914613             317 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Actinoplanes oblitus].
ACCESSION   WP_284914613
VERSION     WP_284914613.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18123688
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..317
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34559
     Region          1..207
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          <253..309
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mvvryrldgp dlggvrfais plnelvlslh awrdpgrypl hlpwiremrr vrgrldaell
       61 dclvnddlwt pdfltprpws pltrladela airrtgngvv drdlrllhgp grlpaplrga
      121 dvldrildal tgyweacfap hwsrmralle gdvtfrgrei aqhglaamfa glagrvrlrg
      181 dtvevhvrsq vhytrpaagg ltlvpsmwts sasapilpae ppmviylarg lgtlwepqpl
      241 papgalagll gthragllvq latpasstel aarlgvtvta vnqhlralra ggllvsarhg
      301 rsvlyrrsdl adrllag
//
LOCUS       WP_284914697             108 aa            linear   BCT 25-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Actinoplanes oblitus].
ACCESSION   WP_284914697
VERSION     WP_284914697.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 108)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..108
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11585
     Region          3..107
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mvrdellrrr adaeseaatl ardlqalfaa srdsnaddeh dpegatigfe raqltallaa
       61 ardriaeldd alrrvdaggy gicercgrpi aparlaarpf arccvecs
//
LOCUS       WP_284914839             651 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Actinoplanes oblitus].
ACCESSION   WP_284914839
VERSION     WP_284914839.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 651)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469209
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..651
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=72184
     Region          291..651
                     /region_name="COG4867"
                     /note="Uncharacterized conserved protein, contains von
                     Willebrand factor type A (vWFA) domain [Function unknown]"
                     /db_xref="CDD:443895"
ORIGIN      
        1 marnvfryga wrdgpdplap pydvraavde mgervmrgdt lrdalrdlir rgprdaggld
       61 alrerarrlr realrrgnld gavtrarqml dqalaaerda lsarddmaar fneavldnlp
      121 rstsqaisel seyhwesaea rdiyqqildg lrrevveqrf agmrdalrng dladvsemvs
      181 dlndllakha rgeetgdafr dfmakhgrff pddpqnidel idslarqaaa aerlmrslsp
      241 qqreelrqlm aqalgegpla gqlaeltdnl kalrpgmnwd rgermrgpgd lgygdaaaal
      301 geiadldeli dqlgqehpga tlddvdvdav erqlgrsaad dlrrlreler elrrqgwvqr
      361 dgdgltlspk alrrlgqtal srifhdlaag krgehdmrda gaagdligss rrwefgddqp
      421 ldvvrtigna vrrraasrgv atlpvrlepd dfevaeterr asavvalcvd lsysmfadgr
      481 wgpmkqtala lshlvatkyp qdalqiigfg kyamplsqge laaieptmek gtnlqhalkl
      541 agrhlrrhpg sepvvlvvtd geptahledd geaafwwppl petvqatvre vdlltrygat
      601 lnvfmlgedp glqrfmgava rrnggrvfsp daaelgryvi ddyvrarrgr r
//
LOCUS       WP_284914925             118 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Actinoplanes oblitus].
ACCESSION   WP_284914925
VERSION     WP_284914925.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 118)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 118)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..118
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13053
     Region          3..86
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mhafdvlgdp vrrrilella dgeqssgavt tviraefgis qpavsqhlkv lrdngfatvr
       61 pdgarrlytv ddtalreada wlsrfrrfwt phlaamatev argkrlrrla asdetrpg
//
LOCUS       WP_284914964             407 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Actinoplanes
            oblitus].
ACCESSION   WP_284914964
VERSION     WP_284914964.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..407
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=41156
     Region          95..388
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 miltecdsca egratgasfc eacgrrltdt asvgaagete atpadapgpg rstglagrdc
       61 phcaavgava adgyceecgm lagrprdhte adgdlmaaav sdrgrrhhrn edamwlavgs
      121 davdvvvcdg vsasfdpdva sevaakaage llaraqhpgh aaagpadrpg trpdeatapd
      181 tgeeptepve pdepalpiae vvgraiqgag eavaqlagtg dprratsnpa ctivaaavrg
      241 phvgfgwvgd srvywipatg paeqlsedds warhviamga dprvamndpk ahaitawlga
      301 dagrisprvg aftagapghl vlcsdglwny ltdpadfgda vrsalrvatg prplleaara
      361 lvayansagg adnitvaivp vppqtdadma eaegdavtds dnetsea
//
LOCUS       WP_284914984             312 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Actinoplanes oblitus].
ACCESSION   WP_284914984
VERSION     WP_284914984.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..312
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32228
     Region          19..311
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 msqplrvpip saavtrdfia vlanpragrg rhrgllpevv ralgaaghpv rlleagsgtg
       61 aeqachravg dgavalvavg gdgtvhrvlq aaagqpvgfg vvpagtgndf agavavpgnp
      121 ldaaagiaas laagrdqrid aalaadaagr erwfcavlaa gfdalvnera nrmrwprgpr
      181 rydlaimlel arlrarsytl eidgetltvp aevvavgnaa sygggmrilp aadpvdglld
      241 viyasplgrg glvrlkprlr qgthvtdprv tvrrarhvrv haegivgyad gerlgplpld
      301 ikvvpgairl lr
//
LOCUS       WP_284914999             439 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Actinoplanes oblitus].
ACCESSION   WP_284914999
VERSION     WP_284914999.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..439
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=47512
     Region          7..401
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mssviikprl awldalrgfa alvvvlfhls piaigaenha vmgryfdmgk ygvllfflvs
       61 gyvipmsler hgsprkfwig rlfriypayl isvalfvali aagvftfprs larestagll
      121 ghatmlqefv garslvrpfw tlsfemtfyl ivaglfvwgl hrfsawwaag lilvaavggt
      181 glpknllgat vgdrrylavl lallvgvsll ayvsgrrwlv lpagllglcf valpllnghs
      241 tkygianssw qatfmlavmf agtviyraqh gqlsrwaavp vlalvaagva lttwlsvggr
      301 yelikwcatt aavvitfaig falrerrvpa vlvwlgavsy slyllhsvil hglqhvapes
      361 aldnllgraa fsvafgiltl ggawlsyryv eqpgqnlgrr vqqwvdarlg pdawrrpvtv
      421 paparpveag eaavasspm
//
LOCUS       WP_284915093             577 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Actinoplanes oblitus].
ACCESSION   WP_284915093
VERSION     WP_284915093.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..577
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=61129
     Region          1..405
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mlgdyellgr lgeggmgtvy larpkngtal vavkvvrldl adddefrrrf rseverarqv
       61 ppfctaevld adpeheqpyl vvefvdgptl aevveqrgpl tsanlhsvai gvataltaih
      121 gagvihrdlk prnvllapgs pkvidfgiar amtatsgntr pdqmvgtvay maperfdtda
      181 gtpitpaadv fawgsvvtya gtgktpfyad spaataaril tqpprlhels rplrglvaha
      241 lekdpanrps arelldllis gerpaataaa lagqpdlraa aaeaqavtgy aiparamaga
      301 tttaptlnip pglvgydens ivtvpisspp mdtagtapep peprrrwvfp lvltlltavl
      361 vagativami mrasdhpgrd gdttqsvddp vlgtpriada lsgpgfwkat dtagqgrcef
      421 rdgmlaahrd tngvyrcsgp sdelpanlti eattrletad scaaiwfrfa dqhgyqaric
      481 ernlyigvhn rdgkglvttk rtfvlkdpip lgtptrirlg vlgdtvtvtr dgaevgvaql
      541 tepdfgvgka ylgifcerda paagpyqasf sdvriwa
//
LOCUS       WP_284915278             253 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Actinoplanes oblitus].
ACCESSION   WP_284915278
VERSION     WP_284915278.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..253
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26508
     Region          177..244
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mpvhpdpasf llygddgtpl aalrlkdddg ervaarvrpl pgipasrvaa qarrdfagmr
       61 letpddalla afvatglepr raatemihdl sglpaprdlp dgwslaepgw dedlagamaa
      121 aygpdhpdgr fteadrayig gmfatgepvp plvpasarla dpagrsaghi lcagpvpwtd
      181 ypcawvlnls vgphaqgrgf grdlllhalh gtreaglpal alsvvdgnpa rrlyesagfr
      241 tenrvlsvtl paa
//
LOCUS       WP_284915301             477 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Actinoplanes oblitus].
ACCESSION   WP_284915301
VERSION     WP_284915301.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..477
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=52092
     Region          1..434
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mtriliigag fggvavanel lkagftditm vekadrvggv wrdnnypgca cdipaplysy
       61 syaqnpawtr rfppqpeila ylercvadfg lagkvrlgte vtaaewtdgv wrvrtasgev
      121 leadvlipav gqlsrpvtpq lggefagpam htarwnpavp lagrrvavig tgasaiqlvp
      181 alagvasrvv vfqrtapwtl pkpnrrygpv rrslyrrlpa lmgparagtw lmtvvtgral
      241 tghriagall hglsaaqrrw qvrdpelrrk vtpdepmgck rvlftsdwlp tlarpdveli
      301 tekvvaltpg gvrtadgveh padvlvygtg faateflvpi rvtgragtrl devwrdgaha
      361 ylgmavpgfp nmflvygpnt ntgntsvvff heaqarwiaq avrhlshhrn plevrpeiaa
      421 aydaelqsrl aesvwtscqs wyrtasgrvv tnwpgmasey rrrtarlrpa dflptrd
//
LOCUS       WP_284915307             490 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA synthetase [Actinoplanes oblitus].
ACCESSION   WP_284915307
VERSION     WP_284915307.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..490
                     /product="acyl-CoA synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016405 - CoA-ligase activity [Evidence
                     IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0032787 - monocarboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=52225
     Region          10..478
                     /region_name="FACL_FadD13-like"
                     /note="fatty acyl-CoA synthetase, including FadD13;
                     cd17631"
                     /db_xref="CDD:341286"
     Site            order(145,148..153,155..156)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341286"
     Site            order(148,263..264,284..289,369,381,384,395,475)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341286"
     Site            order(148,188..189,236,238..239,242,263..264,284..289,369,
                     381,384,392..395,456)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341286"
     Site            order(188,238..239,242,263,392..394,450,456)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341286"
ORIGIN      
        1 mhnaglgswp grraamspgr talifegrrv syaelhqria rlaaalrssg vrrgdrvayl
       61 gpnhpsfvet mfatwvlgai fvplnfrlta aelayqlths gasvlvraag mpavtapvtf
      121 aadavpaadp ihpdetvgld dvaailytsg ttghpkgaml thgnlvwncy nllvcvdvag
      181 devtlvsapl fhvaaldqcl lptflkggts vimpgwdvdg cfdliarhrv twmfgvatmy
      241 agltqsprwa dadlssvrsl mtggasvpaa lihryqergl lfcqgygmte tapgatflea
      301 resrehagsa glpvffadvr cvrpdltdaa vgepgevlvr gpnvtpgywn dpaateaafv
      361 dggwfrsgdv avvdedghfh ivdrtkdmyi sggenvypae veaaifehpg vaevavvgvp
      421 dgkwgevgra fvvprqgyal spddvpgflr erlakykipv yvdvvadlpk tgsnkvrkgp
      481 lralplpdra
//
LOCUS       WP_284915327             396 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Actinoplanes oblitus].
ACCESSION   WP_284915327
VERSION     WP_284915327.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..396
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=41841
     Region          156..383
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mtiapgrpgp vvvmafivtl agrftlsrag vdipivndvr vplffvlllc laleahrmgp
       61 hpvsggeall gvlallgyqg lsalwvppgt ptgpvvgdlc avagllvvyy tlanwdrdqv
      121 tgttlvlfqv tawiyflaaa sgrghapgnr waalgggpnv fvrlmilgvi ssiylylrsg
      181 drliwlvpip aflfgaiasg srggiaalgi tagvallair pkldfdrlak plglllvvga
      241 vlvitagpyi agfvqsrfve atigegyasq rdvlfrmalr iflqrpilgt gvsgfytvtd
      301 lgpgekyvhn lplataaegg fvglalltma wlglwhayia vpkpersles rtaaycgifi
      361 ggaslfsgdy ydarlmwill llasvrpaha pvpsrr
//
LOCUS       WP_284915426             409 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Actinoplanes oblitus].
ACCESSION   WP_284915426
VERSION     WP_284915426.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..409
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=43300
     Region          <202..373
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mpdrsaaprv flapglllvl iavggrftld ragftglgwv dlrvvgliva lvllivdisr
       61 rprtatgrde twlvvtllff lfqiasalwa ppaarigaqt ldmillgalt lafyhwtlgd
      121 pdrairytfl lfyvtaivfg laaifingpg eqgrysafgg gpnvfvriel lgvisaialt
      181 lihrrlvpll atpllllaal lsgsrgalma gavvggyalw kirgrlkpgp vlaagaflvv
      241 aaivvwftap paftslfqer fveqtvqeqy msnrtdiwaa alklgwehpi ggagldgfyg
      301 siginqmiey phnyvlavva eggliglgll tvavilwart vrgggarpqa vglavsaavf
      361 valsslfsgd yydarlawif aamaaaaava qartapaaap arereavgr
//
LOCUS       WP_284915420             343 aa            linear   BCT 25-DEC-2024
DEFINITION  lipid II:glycine glycyltransferase FemX [Actinoplanes oblitus].
ACCESSION   WP_284915420
VERSION     WP_284915420.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Rohrer,S. and Berger-Bachi,B.
  TITLE     FemABX peptidyl transferases: a link between branched-chain cell
            wall peptide formation and beta-lactam resistance in gram-positive
            cocci
  JOURNAL   Antimicrob Agents Chemother 47 (3), 837-846 (2003)
   PUBMED   12604510
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Hegde,S.S. and Shrader,T.E.
  TITLE     FemABX family members are novel nonribosomal peptidyltransferases
            and important pathogen-specific drug targets
  JOURNAL   J Biol Chem 276 (10), 6998-7003 (2001)
   PUBMED   11083873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006395
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..343
                     /product="lipid II:glycine glycyltransferase FemX"
                     /EC_number="2.3.2.-"
                     /calculated_mol_wt=38249
     Region          18..286
                     /region_name="FmhB"
                     /note="Lipid II:glycine glycyltransferase (Peptidoglycan
                     interpeptide bridge formation enzyme) [Cell
                     wall/membrane/envelope biogenesis]; COG2348"
                     /db_xref="CDD:441916"
ORIGIN      
        1 mlrlqrveps aaltadraty qdrlifhtpe wlafvaecqr aepvlatvsd gdttvghftg
       61 lltrryglri lgspmagwtt syqgfnllpg isrrdalral tgfafdelgc ahlevrdrga
      121 teadfaglgl rwdsaptavi dlspdedalf gamagacrrn irkaaksgvi ieeaepdpaf
      181 adefydqlrd vfakqnlvpt ysvervksli rhlapagris llrardgdgr ciatavlpwy
      241 hrtmyfwgga syrehqhlrp nealiwyalr warargvtef dfvgansyka kygtvevpvp
      301 warhsrspli aglrdtakra falkqrttar ltrfrapepa srr
//
LOCUS       WP_284915462             244 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Actinoplanes oblitus].
ACCESSION   WP_284915462
VERSION     WP_284915462.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 244)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..244
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25619
     Region          8..237
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mtpaeltqar adrglavleg fhalkhalrf gatvrtvlav dpeqlesmaa glapdllgrf
       61 relarpvsrd dfrrlsrnpv rteviavadr ppvdvaavlr atsaepivll edprnlgnvg
      121 avirvaaaag aaavltsgvs dpwdpaairg aaglhyalpv aridvaaltg rpivaldpdg
      181 veispaaipd ravlafgter dglsaellsr advrvripmr advsslnlat svaitlysrr
      241 wmav
//
LOCUS       WP_284915470             193 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Actinoplanes oblitus].
ACCESSION   WP_284915470
VERSION     WP_284915470.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..193
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20176
     Region          12..90
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
ORIGIN      
        1 mtavqpyasg qlvkaallas kdlgkterav lvtvaahgng mgdafpsvat iadyvgvser
       61 tvsrvlaklv algrlvarir kgattvyrlt veainrvvkp rqneatpptd qattpdtqev
      121 spevgsklgs skggfrrffp srvsnpqtsp vkpwerrgaa lppaageqkc hrhpgqlarn
      181 cgacraealg ggl
//
LOCUS       WP_284915568             929 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Actinoplanes oblitus].
ACCESSION   WP_284915568
VERSION     WP_284915568.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 929)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 929)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 929)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 929)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467590
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..929
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..929
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=97521
     Region          <2..846
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          487..515
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          529..554
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(530..531,534..535,537,569,574..575,577..578,607,
                     610..611,614..615,618)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          567..601
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          866..923
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 msghivgrag elavlrqald dtkdgrggch vvvgppgigk srlllaagdh aderdiavaa
       61 reafrhdlaa plvtlagalr acspptgdfa wlsgvddqpa gnyakilrlr dslerfaaaq
      121 pllividdah wmdelsalav relvpalasf pirwllasrt qpgdtpggqt lswlsqrgta
      181 ihldvlddea terlcterig arvdntvlal vagcggyplr ieqlldalva tkqimiadgi
      241 atvvgedlps sfvatvremv gslspdaqrl lrsasvldrp fdiesaarlm gstdpaelfg
      301 lidevttsgl lvedqdglvf rhalvhqavq nslgnsqarl lhgkaavlar ehgrptaeia
      361 ghllrsgrvg agaavdmlrg taagvaatap ataadlmcqa lqaigehdpa rpaivadtvg
      421 llaaagrvtr ahelgtealr teldpptrat vllglaeafq hagrnaeaar yaedglnqsk
      481 iaeevrarll airahtafal ddlavaeasg aeasrigreh epgaavlglt arslvagaeg
      541 rlddalrhas eateladaag gpaphrhprl wlanaltald rfdeaeqalr hgrpesdalg
      601 aawaqplwhy ywaalltarg rlddavaead agvttaeqlt ayrlavpllg tlirlavlrg
      661 dlpqarglld rmrqlratgi taapedaawa eatllcaega gpeafalmrg fydtaidrpt
      721 llvrdpgava glvrlaaaag ereraeavva saarlarrnp lshaaagaae hatgvlgrdp
      781 rrlraamtef rlgrrplala aacedaadls raagdragar arydealalv tsagahgvrr
      841 rlesglgvwl gvsapepapg rhgtglpgls paerpvallv argmtnivva rqlnlsphtv
      901 dshlrkifmk ldirsrvela alvarecpd
//
LOCUS       WP_284915602            1299 aa            linear   BCT 25-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Actinoplanes oblitus].
ACCESSION   WP_284915602
VERSION     WP_284915602.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 1299)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 1299)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 1299)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 1299)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1299
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..1299
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=135914
     Region          5..1269
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 mtetqiqgfg lspqqdlvwr takdndgrva attavveltg pldsarlgaa vrhvltqhei
       61 lrtrlvlpsg yvapvqtiad rvdariepag peaasapgtp aealladepv rlrlvrlgdd
      121 rhlllvggsa gvfdrasaal ftaglaeaya gpvaasdees lqyadlaewl nermrdgrfe
      181 rprfldgiad gvtvprlpfe lpgaggadra vvpvpdllpa gvegalhrlg cslrdlllaa
      241 wtvtlhrysg advvltgvae ngrmlpelss aigplarllp vavpiagdtt frqvvdvvrg
      301 taavlesdae lfdprwwsgr dadaihpvpa fdlvepgapg taggvtfalr evhgghpsaa
      361 lslcflqagp aggdgelcfd pgrfpaedvr algsvlrtvl ahavddldgg vatmpvadla
      421 lstdpedahd pvtvldqvlr rvaeapeava vedaggtlty reldrvaaal aarlaergag
      481 pggvvpillp rgtaavaaml gawragaaft vidqttpagr iaailadtaa tvaisnadla
      541 gglagavpav lvddpagtgp agtdpattag papddpayvv ftsgstgtpk gvvvshgala
      601 ayvrglggth pgtrggsfai vstlaadlgy tavfsalasg grlsvvpmev atdavrmadw
      661 faahpidclk ivpshlaall agadhpervl prrllvlgge acpadlverv aalapdlevv
      721 nhygptetti gvctfrtgra pvdpraksvp igtplpgtra evldpagrpl pawiagelhv
      781 agpqvargyl nqpaltaerf vtvagsaqrw yrtgdtvrrl pggaleylgr vddqvkingy
      841 rvepqeveav lrrhrgvrec vvavvgepdr altayvvgdg sslsvdalre hardllpeym
      901 lpravvlvde lprtangkid kaalaaigae raagavhvpp rdslemrvle iwqallkksr
      961 lgvtddffes gghsllslql lgeisrqlgh rlpisvlfds gtvegmarai reqdswqspt
     1021 lipiraggsr ppvfcvhagg gsvlgyldlv raldadipvy glesvgldgg qapltrvdem
     1081 veryaadiea ldpsgpvsvv gwglggifaf alaqrlraag rpvgnlaivd gaapdpaala
     1141 eviagratdp hyvgmldddv varfaahyql pvaeedlagr sdeeqravlt aamhqqnvlt
     1201 edagverlet lfrvyrania avrdyvqnrr laaapdypll llrakhdfnt derdpllgwp
     1261 alfgdriave sfagdhyevm rsptvdglaa lverahttd
//
LOCUS       WP_284915606             317 aa            linear   BCT 25-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Actinoplanes oblitus].
ACCESSION   WP_284915606
VERSION     WP_284915606.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..317
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35270
     Region          29..297
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mmtesggraa revggtrvma rpdairqsdh felrpctpti gadisgldls vplagpalad
       61 lkrafldwkv lffrdqalsp qrhvelarhw gnpvvyplpd kgefpelvnl nhgpedpgve
      121 niwhsdvsyd eapslgsilr avrlpdtggd tlwadmaaay dglapevker iaglravhdl
      181 lalfgdertg arevagrgmf rgaehpvvrv hpetgqkviy vnrmyttril dvseresdel
      241 lkllcdqahh peyqvrfrws edavvmwdnr stqhyavsdy ypnrrilerv siagdrprsa
      301 arslrsvarr gatpvps
//
LOCUS       WP_284915627             440 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Actinoplanes oblitus].
ACCESSION   WP_284915627
VERSION     WP_284915627.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..440
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46572
     Region          2..326
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mfqqklteia qkheipgmaa gilmgdqivy ashgvtnlgn pqpvdehtlf hlasitktft
       61 atalvrlaaa grldlsapvr ryvpelrlad pgstaeitvg qllnhtagle wnlidgeqat
      121 ldgfaaeldr lpiiappgtr asysqagynl aglviekvtg qpyekvvadl alrpaglert
      181 cfgldevvrh rfaightadg dgvprpatpw aawpagmran npgggiassv sdllrwarhh
      241 lgsadlhamt eptvplrast lgdafgicwf lrdvggvrti ghggsgngqf aellivpsrd
      301 favvslanag pagypanqev vgwaladrlg lrerevrpla ydesrareia gryeldamdl
      361 eiatdgaglt lavgikpair raseadmppd ypaatlgllp ddeyvitdgg lagqrgyvtr
      421 daagavigad lagrlfrrir
//
LOCUS       WP_284915629             924 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Actinoplanes oblitus].
ACCESSION   WP_284915629
VERSION     WP_284915629.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 924)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 924)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 924)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 924)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467590
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..924
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=99633
     Region          <3..874
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          866..916
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mglverdevl aaldgllvaa vagkgriatv tgsaatgkta llntfadrvv drnalpltav
       61 gsraerdlpl gvfgqllmda plvaresrra mdllhegvqs ipadpggaar ldpqivhalc
      121 ailldlsqrc plvivvddvd qadpasivcl sylarrarfa pmlavfshat hprphelaae
      181 leawsrtphg ahlelaalsp ggvrrlaads lpdgdadrla prwhqlsggn pllvtgliad
      241 qrqvaaegga pdgvpvaggh yaqavvallh rsdplpaqva rgvallpets llgqllgvda
      301 vqlgqalrel taagvlrdgd frhpvareav laeipdaerr amhrraavla hyggagarvv
      361 adqllgagra depwavavle eaarqdlrdg wvdaaigylr lawqncpdgp rrakimttml
      421 raawrinpgt staylpelta alrhgfllgd daltlarall wdgrfasard viehlngvld
      481 eldedgrtel aiarpllqct ypefftllre psrqqpaaat vgashrleaa qalatvlsrg
      541 paeevsvamq rilhnsrlde msldavesal ltltyggwsg qaaswcdrfv eeavtrraps
      601 rlarlsaira evslrtgdlp gavrharfal dtmpapswgv aigaavapli vaatamgryd
      661 lardqldrpv peemfetryg vhylqargry smavgqhqla lrdfercgel agrwrldvpg
      721 lvpwrvdaae allqlgqpgr arplieeqlq rcgrinprvr gmamrlyaai srpehrptyl
      781 rqaadlqlvd qyeharalid lseaylalge trrasmiarr aravaektea eplraklggr
      841 lteasgeprp alpnlasaal alsdaerrva vlaadgytnr eiaaklyitv stveqhltkv
      901 yrklrvnrrt dlpthlfrep aaag
//
LOCUS       WP_284915662             373 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Actinoplanes
            oblitus].
ACCESSION   WP_284915662
VERSION     WP_284915662.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..373
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40522
     Region          16..370
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mttrvwdyla eyakekddil davqkvfgsg qlvlgesvre feaefagyhg lahctgvdng
       61 tnavklglea lgigpgdevi tvsntaaptv vaiagagatp vfadiraddf lidvdqvaaa
      121 itprtkaivp vhlygqcadm aalnrlageh glkiledcaq ahgarqhgri agtmgdaaaf
      181 sfyptkvlga ygdggavlts deeidrnlrq lryygmekvy yvvrspghna rldevqaeil
      241 rrklrrlddy iagrnavarr yeerlgdltg pgglllpatn pgnthvyyvy vvrhprrdei
      301 iealkshdif lnisypwpvh tmsgfaglgy rpgslpvtee lageifslpm ypslpeseqd
      361 rvidalrtvl ekl
//
LOCUS       WP_284915681             391 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Actinoplanes oblitus].
ACCESSION   WP_284915681
VERSION     WP_284915681.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 391)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..391
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42383
     Region          49..372
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 marapgwsvr lkltlsyagf lmlagallla vvwvfllryv pdqphpppld tlggtvyrad
       61 dlilqgpsrh dllsafapra aevmvfllvf gllggwilag rmlspvtrit eatrlagtgs
      121 lshrirmpgh sdefrelada fdtmlerles hvaeqqrfaa nashelrtpl sitktlldvv
      181 rkdpshltee fldrlhavns raialteall mlsradqrsf epervdlslv aeeatetllp
      241 laekcdttve tsgdlahalg spalllqltt nlmqnaivhn lpkagsvwvt talhdrsval
      301 tventgeelt pelistltep fqrgteriha dhagvglgla ivkaivtahd gtltlaprdg
      361 gglrvtvrlp aappperdgr rlppaprrsp e
//
LOCUS       WP_284915744             246 aa            linear   BCT 25-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Actinoplanes oblitus].
ACCESSION   WP_284915744
VERSION     WP_284915744.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..246
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28025
     Region          16..245
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mssspisils qtdfngdpld eellqrtfrq lmdehgyvlm cnvpdsfdqv kfcrglggfv
       61 pnytgavvgd vrpepgmddv yhagntrplt phsegydftv lppryialwc vtpasgpgge
      121 ttladtapwv aeldererel legtefewkt tegvnrlgld lhtkhpvleq hadgmivrfs
      181 cnnlvraddd evvplqerwk enfyrdqisi dyhpndmlvw dnwrllharn afsdrsrhlr
      241 riqian
//
LOCUS       WP_284915687             420 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Actinoplanes oblitus].
ACCESSION   WP_284915687
VERSION     WP_284915687.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..420
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44329
     Region          46..395
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mdsnsvrgvd rrrllrwggl aaagvasagv slagtsfagt rervarapga spdpdrippa
       61 tlpggaydry laglaaqgkf sgvvllahrg rtvlsraygl adrereipns eatafnlssa
      121 gkpfsavavl qlaqqgrlhl tdpvgrhltg fpkdvaervt ihhlltgtsg lylgaqdrdr
      181 vfrsrrevhd yyerrarqar lrgipgapst vhaepdallp alivqavtgk tywdhveeni
      241 frrcgmtgag fyttaqwltd prlahpymtv tggatvdavr hldqgspspy algvnpgrvf
      301 idapgdggfa sardlarfag altggkllnr pwtdvllaar tplgpvtfga ygivmdivdg
      361 qwvyqrsggn pgvganwsvy pqtgwtgvil snaegvplqd iiaretqavt gaapmagagg
//
LOCUS       WP_284915847             749 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Actinoplanes oblitus].
ACCESSION   WP_284915847
VERSION     WP_284915847.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 749)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 749)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..749
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=80837
     Region          1..745
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 msslsslaee qshlsviygr ldelraqarq rlaetqrhrg gtkealslrd vaaygyaerl
       61 aqyeaveegl cfgrldlrdg drlhigrigi hdtdhpllvd wrapaarpfy vataitpydv
      121 tvrrhirtre rtvvelndei ldldragdra lvgeaaliaa ldanrtgrmr divetiqaeq
      181 drviraepgg vlvvqggpgt gktavalhra ayllytyreq ltargvliig pnatflryis
      241 qvlpslaetg vllatlgdlf pglpahrpes pataevkgra vmvevlaeav rdrqrvpaep
      301 ieievdgqvl rltaadcepa rqraraagpr hnlarpifet gvldvlagqv adrigadpfw
      361 ddplgaddal tspnvldead ladlradlas nplvraalda lwpvltpael ltglyaapev
      421 asgllgpadr ellrrepgag wspadvplld eaaellgddd raaraaagre lairlsyaqg
      481 vlditagsks feledddeaa ipniadimqa dmladrladr ehrtaaeraa adrdwvfghv
      541 ivdeaqelsp mawrllmrrc psrsmtvvgd laqsgslgap dgwaevlapy vadrwrlael
      601 tvsyrtpaei mdytrdrlaa adpaivpprp vrstgvppwe atgsldelva rvayekdtvg
      661 dgrlavivpa dllttltaal pqlaggpspd leepavlltv aqakglefdt vvvvdpdril
      721 agsprgandl yvaltrptqr lgvftldhe
//
LOCUS       WP_284915904             321 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Clostridioides
            difficile].
ACCESSION   WP_284915904
VERSION     WP_284915904.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..321
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
     Region          8..319
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 stgkkmtlcq lyakqnaqra nvkkstqkqr eqlmrllked klgarsidti kpsdakewal
       61 rmkdkgfsyn tinnhkrslk asfyiaiqdd cvrknpfdfk lsevlendtk ekvalteeqe
      121 qallsfiktd nvyhkyyddv lillktglri selcgltvad iafknevvii dhqllkskeq
      181 gyyietpktk sgarqvplsk etiqafqrvm kkrpkaepfa idgrgnflfv nqkgkpkvai
      241 dynmlfvriv kkynkhhkdn plphitphtl rhtfctrlas knmnpkdlqy imghsnisit
      301 mnwyahasid taksevqrli a
//
LOCUS       WP_284916000             379 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator, partial [Clostridioides
            difficile].
ACCESSION   WP_284916000
VERSION     WP_284916000.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>379
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
     Region          12..>379
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mslnitarqi niikillnsk dtisgialsq eigcssktiq neikdinkqf rngkilsirg
       61 vgyklegsfd evninsnlyd dvdrveyiir kiltlsneek ntikledlad smyvsvstvk
      121 ndlkevkrml ekysisvksk hkqgicvles edkilncivd lsnkrdnqls lndflnddik
      181 erkllikkll ldilnenglv ltdiefksvl nnilvmlsrh kynekefien yienyrskrs
      241 sileneqnke iiinsiktfc knlklatsid isndkvfeef lykhisslck kiklginqsp
      301 imaqdikiky pfafelania kktiekdlki einedevani alhiggaver asynnkdkvf
      361 ktiivctsgi gtsmlikak
//
LOCUS       WP_284916027             283 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Actinoplanes oblitus].
ACCESSION   WP_284916027
VERSION     WP_284916027.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..283
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=30612
     Region          14..261
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mptvdeyaqg rpapplrdri afysgyrqcg lppgrhrglp spyltliftm ddplvisehp
       61 dgrqtpdtyr allgglhlrp amiahdgrqs gvqvalhplg crellglpag elagldidpa
      121 ailgesfvar vrerlcaavd wparfavlda afgalpatrp arpgtervah vwaalrrgap
      181 asiaelagqv gwtprhltdr fraevglrpk eaariarfdr arralrpgtr ladlaaehgy
      241 adqshlvrdf qafagcapsr wlsdefgfvq aaaaaddhdg vhd
//
LOCUS       WP_284916032             847 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Actinoplanes oblitus].
ACCESSION   WP_284916032
VERSION     WP_284916032.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..847
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=90019
     Region          <3..845
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mallerdhel aelataarra ragrgsvvlv tgeagigkss vaaavrsvlp aegrlltgwc
       61 ddlatprvlg plrdligrvg tgltealasg drvrvleafr aeldwpghpt vlvvedvhwa
      121 deatldvllf lvrriatlpv vllltyrdde vdaghhlhqv laratpvhrl plsrlsadav
      181 ralvgergld pdrvfsvtsg npffvtevlg agdadavpat vteavharlq gldepcraal
      241 gtlavvphav erwlveavvp gglatiaeae rrgllqvspe rvafrheltr ravaaaltay
      301 rkivanqavv aalrdrggvd lsrlvhhaae agddeliirw apaaaaeaar agahraaaah
      361 yrlalareaa fapgsradll egyaeelyll adatravttq rtalalrrel adpaalglal
      421 rrlsrlhwwa gdrpeaerca veavsvlaaa gdpaalafgl snqaqlhvln gqaaeaievg
      481 draialarss gadgvlshal nnvgfarwea geadrgrall deslavalaa geadhaaray
      541 aniswllldh lrldeaagvl taaidyaern evlgflrylh lgrgrlhlar aewaaaerea
      601 awaldappnm rctalvvggl arlragrlga edliteawsv alrigeaqrv gpagaamaea
      661 awlrgdraaa grlapayrpv freegfgywl rrlgaavplp anshfyrlqa agavraaaag
      721 wsktgfryea avalshsddp tdlltaiadl damgaapmar rlrqqlrdsg mtrvprgprp
      781 atrdnpaglt grqlevlrll aaghsnpeia aelvlsvrtv dahvaavlak lgvhdrkeav
      841 awyrhhc
//
LOCUS       WP_284916082             257 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Actinoplanes oblitus].
ACCESSION   WP_284916082
VERSION     WP_284916082.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..257
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27413
     Region          28..149
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mtstftpgek twlaqlgtlr qvvrqevvar qlaahlrsda prvldvgcgq gsqalrlarl
       61 gfevtaldss aemlaelrra lehepapvrd rvqvvhadas rlagtfspgc fdvvlchgll
      121 myfaapgpml tdlarmlapg gilsllvrng dglamrpglr gdwatavaaf dttaygnrlg
      181 itaradrrae ltaaltgrgl evfawygvrv ftdtaaddap lptatelnhi ldaetragst
      241 dpyrgvaalt hvfarrp
//
LOCUS       WP_284916172             451 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Actinoplanes oblitus].
ACCESSION   WP_284916172
VERSION     WP_284916172.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..451
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=46811
     Region          209..444
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mrdffrtltg ravlvtvata vvavivtalv avpvavrsvn aqvraelvek saiavqlltd
       61 rrpavrenia erlrrddiei yvirrgvadr pglpprviaq vtggalvnvr arvggrasfv
      121 agsplpgvda gvvltrpads gvawqvlggv wwallagllg gilagallar fltrpielaa
      181 aaatrlaagd rsvriarhgp aeahrlaeav nqlaaalqts egrerdflls vshelrtpla
      241 tirgyaeala dgvvgadgaq qagatmlgea drldrlisdl lvlsrleaad lpidvvavdl
      301 velvreagta wsarcaadgp glavelpdap vtvdtdpgri rqvldglcen alrvvpagap
      361 lvlavragas ggvievrdgg pgfsdddlav afergalnrr yrgirkvgsg lglalaarlv
      421 grlggrieag hapeggamft velpyrtrti g
//
LOCUS       WP_284916183             353 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Actinoplanes oblitus].
ACCESSION   WP_284916183
VERSION     WP_284916183.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 353)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10543770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..353
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37880
     Region          73..211
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
ORIGIN      
        1 mtvlrphaed qyadelaqla aaddrprppg wrlsphavvt yllgdgakit pkyvgprrli
       61 evavstlatd rallllgvpg taktwvsehl aaaisgdstl lvqgtagtae eairygwnya
      121 rllaegptea alvpspimra mrtgsiarle eltrvpsdvq dalitilsek tlpvpelgte
      181 aqaergfnli atandrdrgv nelssalrrr fntvvlpvpa naddeveiva rrvaqlgksl
      241 dlpevpaald eirrvvtvfr elragltedg rtklksptgt lstaeaisvi tngmalaahf
      301 gdgtlhpgdv aagivgavik dpvsdavvwr eyletvvrer pdwldfyraa rda
//
LOCUS       WP_284916221             312 aa            linear   BCT 25-DEC-2024
DEFINITION  ribose-phosphate diphosphokinase [Actinoplanes oblitus].
ACCESSION   WP_284916221
VERSION     WP_284916221.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Sinha,S.C. and Smith,J.L.
  TITLE     The PRT protein family
  JOURNAL   Curr Opin Struct Biol 11 (6), 733-739 (2001)
   PUBMED   11751055
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Becker,M.A., Smith,P.R., Taylor,W., Mustafi,R. and Switzer,R.L.
  TITLE     The genetic and functional basis of purine nucleotide
            feedback-resistant phosphoribosylpyrophosphate synthetase
            superactivity
  JOURNAL   J Clin Invest 96 (5), 2133-2141 (1995)
   PUBMED   7593598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..312
                     /product="ribose-phosphate diphosphokinase"
                     /EC_number="2.7.6.1"
                     /GO_component="GO:0002189 - ribose phosphate
                     diphosphokinase complex [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004749 - ribose phosphate
                     diphosphokinase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0006015 - 5-phosphoribose 1-diphosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009156 - ribonucleoside monophosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009165 - nucleotide biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33942
     Region          1..311
                     /region_name="PrsA"
                     /note="Phosphoribosylpyrophosphate synthetase [Nucleotide
                     transport and metabolism]; COG0462"
                     /db_xref="CDD:440230"
ORIGIN      
        1 mrdiavftgs ahpelaaeic ehlavplmpt kisrfandci evqlqgncre rdvfliqplv
       61 pptqehlael lfmldaarga sagritvvlp hyayarsdkk daprisiggr lvadllttag
      121 adrvlamtlh spqvhgffsi pvdhlhalre lahhfrgydl sntvvvspdl gnakeaaafa
      181 rllgievaag akqrfaddkv vinsiigeva drdvivldde iakgstvfel ldrlrernvr
      241 svrvacthgl ftndavrrla aekeieeivc tntvpipaak rhekltvisv asalaeamrr
      301 ihngesvsal fh
//
LOCUS       WP_284916556             299 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Actinoplanes oblitus].
ACCESSION   WP_284916556
VERSION     WP_284916556.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..299
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=31772
     Region          3..295
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mrtprkiavv ahqkktlggg ldelrrrltd hdikdlfwye vpksrkapgk vrqalaekpd
       61 llvvwggdgm vqrtldvvag kpvpvaimpa gtgnllagnl giptdleqav eiaftgarrr
      121 ldlgklggeh favmagvgfd gamikdadga lkdrlgklay vwtgirhvdg eaprtkikvd
      181 gvpwfddeas cvlignvgti tggvrafdda apddgwldvg vataqgalqw aralgtmavk
      241 rsdsspfvrt trarkvsvkl eskleyeldg gartrtksfq asvvpgavev cvprsdgaa
//
LOCUS       WP_284916690             829 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Actinoplanes oblitus].
ACCESSION   WP_284916690
VERSION     WP_284916690.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..829
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..829
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=88463
     Region          92..239
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          209..821
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 magrtppasr graastsrga atsrarqpar pvkkaaakpa arkraaanrp paigpgvsrg
       61 vsalwmglah svgwvargag rnarnigpeh rrdgagllml gfsiltavav wahgagplgq
      121 rladaihlff gglgvflpll ffygavrlmr epvdpdhrgr npvgwsaviv atasllylsd
      181 dptpdvaltg nggllgygvg svleravsaw vavpllillf vfgllvitat piakiperfa
      241 llgdlvlgrs aprapailpd eideveevva pvkprrrrps pipipapgde pvepvepded
      301 lilhdtvalp klpatrkkpp ppehseppvr aeqldissvd sgdyrlppan llgtgtppks
      361 rsrandeima altgvfdqfn vdaavtgftr gptvtryeve igpgtkveri tqlsrniaya
      421 vkspdvrils pipgksavgv eipntdpenv algdvlrsra atadhhpmvv algkdieggf
      481 vvanlakmph iliagatgag kssclnsllv slltratpeq vrlllvdpkr vemtayegip
      541 hlvtpivtnp kkaadalewv vremdmrydd laangvrhvd dfnrkvrsge itappgserv
      601 mkpypyllvi vdeladlmmv aprdvedsvv ritqlaraag ihlvlatqrp svdvvtglik
      661 anvpsrlafa tssladsrvi ldqpgaekll grgdglflpm gaskptriqg awvdekeiak
      721 vvkfckdqre pefqegvtda ppskkkeide eigddlqlli qaielvvtsq fgstsmlqrk
      781 lrvgfakagr lmdlmetrgi vgpsegskar dvlikpdele eslaalrvd
//
LOCUS       WP_284916712             339 aa            linear   BCT 25-DEC-2024
DEFINITION  DHH family phosphoesterase [Actinoplanes oblitus].
ACCESSION   WP_284916712
VERSION     WP_284916712.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..339
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=35110
     Region          18..335
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mtlpsdgpaa gqwdaavaav ralggeaeiq lichvspdgd algsmlgfgl glrrlghsrv
       61 ratfpgefsv ptpyaempgl ellvpeaeay papalimifd vaaesrlggl aalvaaapvs
      121 vvldhhasnt gfgtirlvdp raaatsvlae qligrlgvpl daeiaecfyv alatdtgsfk
      181 fdattvavhe laarliatgl rpgdisrrif dtrpfgamkl agevlgravl epaaaggrgl
      241 vwtyatladl drhqqppyvl dtlidpvrsv aeadvtllvk qvaagewavs lrskgavdvs
      301 rlaisqgggg hrlaagftgh geagdvvdtv rrllddyls
//
LOCUS       WP_284916809             187 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Actinoplanes oblitus].
ACCESSION   WP_284916809
VERSION     WP_284916809.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..187
                     /product="YceD family protein"
                     /calculated_mol_wt=20242
     Region          12..187
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mpkspqshld prqplvvdtt klprqpgatr alkrvapapa dlglelisvp egsdleldls
       61 ltsvsegvyv sgtvrgslkg ecgrclneid esfevslgem fayedsttee ttdedevgrm
      121 qgdlidlepv vrdavvltlp tnplcrpdcp glcpdcgvhf ddlpaehshe evdprwaalr
      181 nlpknee
//
LOCUS       WP_284916898             395 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Actinoplanes oblitus].
ACCESSION   WP_284916898
VERSION     WP_284916898.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..395
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=41390
     Region          21..377
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mtktaavigg giagtaaaia lrhagfdpvi herhqrgvad ergafltvav nglaalrslg
       61 ldpekvlakg fptpvmalrg asgrvlaems lgretrtvrr adlyaamlae aeacgipvvh
      121 gaaltravsg pdgveaefad grrvraellv gadglrsrtr qcldpaaaap hylgllnagg
      181 ftagpveprl apppgvmqma fgrkaffgwa tapdgsvwwf anppskrpve sgaftpqswk
      241 ahlvelfdgd psspaaelir lsdevvgpws tedmgpvrvw rdermvlvgd aahalaptsg
      301 qgasqaveda vvlghslrdn asigaglaay ekarrsrvek vaahgrrgns gkvqgpvgaa
      361 irdamlplvf rllqrrgdpq awifehrlpr laaga
//
LOCUS       WP_284917042             433 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Actinoplanes oblitus].
ACCESSION   WP_284917042
VERSION     WP_284917042.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..433
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=46787
     Region          62..379
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mtnetlaprv rtgpttqkta lvvpasgtrr pvrlatldal rlvaalavaa yhltvswrid
       61 ghrqpehflp hvshvtiygf lgvelfflis gfvicmsswn rslgdfftsr vsrlypaywv
      121 cllitaavvt iapitggvpv tgspgllqia anltmlqepm gigsvdtvyw tlfvelrfyl
      181 lfaalaafgl tyrrvvlfca awmtvavisp mlgskaievl aipgyapyfi agvaaflihr
      241 fgrspllfgi vgmawlislq hvigrvsdvn pgfpvptwpg pviitaayaa llaialgwtd
      301 rirwawltta galtypfyll hqrigytvir htyeatrlpa avlvpgamll tlglawlvyr
      361 lvekplaarm raglrqafad lraasardaa pageaapvpg aaparearaa apstrprtgv
      421 rvirqvpgrs ger
//
LOCUS       WP_284917126             439 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Actinoplanes oblitus].
ACCESSION   WP_284917126
VERSION     WP_284917126.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..439
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46368
     Region          22..425
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mttktlpdlv pdaeltlprq aerklpnglt viairresvp lvevrlripf graplaaatl
       61 lsqslftgta tmtmldiaae lqavggglaa gtdpdrlqis gnalvdglpr tleilagvlt
      121 gaaypgeevv tererlvdni qvalsqpahl arvallkrmy lthpyavqtp apedvravep
      181 ealrelhadr vrpggavlvl vgdidpeqai dvaektlggw tgeardgdip ptpalqpgpl
      241 llvdrpgsvq sslrialpal trtdpdyaal tlanlvfggy fssrwvenir edkgytygsh
      301 svvehfvags allaaadvat evtgpsllet syelgriasl ppgeeeleqa rryalgtlrl
      361 gmstqaglag vasvyagfgl rlehlrehsa alaaatreqv aevaarhlap sravivvlgd
      421 aekiegqlaa ltvversaq
//
LOCUS       WP_284917153             604 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Actinoplanes oblitus].
ACCESSION   WP_284917153
VERSION     WP_284917153.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..604
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=64523
     Region          399..>584
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mdypglagrt ggfrhgapha vevgadgara aflrspgafd pdpalwvldl fsfeerliap
       61 gpiasyavdr darvaafarg grlfradllt davtaiptsd pvhdprpdpq gvrvgyvtdp
      121 drsatlrvhg pdgdrllage pgnawrehgg siawgvagsg agefgrtrgw wwspdgsqvl
      181 avrtagstsl hlldlddgwv dvhwdretyp hlaqvrwagg gplitvlrrm qqhglvlsvd
      241 prtgetqvha eladarwvep ipgtprhlpd grvlvggela hdgfdarclf adgslltppg
      301 lyvrrvagtl pratgpagap dlivegslgd pavrevfrvr tslggggpev trltgrytge
      361 pvaggdvlia gdqvwrgdrr vgtvrslaaa lpyrpepvfe rvtdrrlpag vlyptghlgg
      421 slpvlvtlgd gpghqqvrsd dhawqerqww adagfavlsv dsrgtpgvap sfekavhrrl
      481 adlaladqvd alhaltgkhp dldlsrvvvr grglggwlaa lavlrrpdvf rcgvardpvl
      541 dwsqlpppia erylgdpads ahiyrnhsls dalaeadphg plllagaels lpgerdwfre
      601 qlas
//
LOCUS       WP_284917178             517 aa            linear   BCT 25-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Actinoplanes oblitus].
ACCESSION   WP_284917178
VERSION     WP_284917178.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..517
                     /product="long-chain-fatty-acid--CoA ligase"
                     /EC_number="6.2.1.3"
                     /GO_function="GO:0004467 - long-chain fatty acid-CoA
                     ligase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55653
     Region          6..511
                     /region_name="FC-FACS_FadD_like"
                     /note="Prokaryotic long-chain fatty acid CoA synthetases
                     similar to Escherichia coli FadD; cd05936"
                     /db_xref="CDD:341259"
     Site            order(167,170..175,177..178)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(170,285..286,307..312,394,406,409,420,504)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(170,211..212,259,261..262,265,285..286,307..312,394,
                     406,409,417..420,485)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(211,261..262,265,285,417..419,479,485)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mttlslatvl aesarrypdk vavidagari tyrelwqqtr eyaaglrelg igaghtvavm
       61 ipnvadfprv yyaalavgar vvpvslllta eevgyvltds qadllvthsa flqvgaaaag
      121 lsgtplvnvg plpaelpnpp rrledvaasv palhtyvtre aedvavilyt sgttgkpkga
      181 llthlnlvmn aavnvfdvhp itgddvvlgc lplfhtfgqt vgmnatfrlg gtlvllprfs
      241 geaaielmlr envsifhgvp tmyiglleaa graeqlpklk lcvsggaslp vavlerfaea
      301 fgshiwegyg lsetsptatt nqpaygakpg tvghpiwgve veiarpevpe rieflsagel
      361 geivvrghnv fagylnrpea taeaivdgwf rtgdlgvkdd egfisivdrt kdliirggfn
      421 vypreveevi arhpaiqqva vigvadethg eeicavvvld dakpdenrlt eqelidwsre
      481 rlgkhkyprq vrfaealplg psmkvlkrel rkqyssk
//
LOCUS       WP_284917208             259 aa            linear   BCT 25-DEC-2024
DEFINITION  S1 family serine peptidase [Actinoplanes oblitus].
ACCESSION   WP_284917208
VERSION     WP_284917208.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12184331
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..259
                     /product="S1 family serine peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=26834
     Region          32..251
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; smart00020"
                     /db_xref="CDD:214473"
     Site            33
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(69,116,207)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            order(201,227,229)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
ORIGIN      
        1 mvrnvaslvl avavavaiap gaadasgrpv levvggnvak agefpwvvrl smgcggalta
       61 prvvltaghc vdgtgparni tvtagvtdlk arnavtahsl evirapgfqt etrgddwavi
      121 kldrvltlpt lalvpdassd hgdvtvmgwg qtregslrqe rklhyatvpt ipdaacaksy
      181 laakvtlvtt dsicagrhgv dtcqgdsggp mvrrgrdgrw aqvgivswgl gcardaypgv
      241 ytqisrfrta ilaatrkls
//
LOCUS       WP_284917243             227 aa            linear   BCT 25-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Actinoplanes oblitus].
ACCESSION   WP_284917243
VERSION     WP_284917243.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..227
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=24007
     Region          6..201
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mtsiplaeel lllsyddqtg katgsrigld lgmaaavlid lalagrvayv dgylqvtdps
       61 pigdtiadav ltkiagdpph tpaqwlqrlr hrlrtrvled lcargvvkdv detqlefihv
      121 hrypttdpaf eteirsrlae alttdkipde rtaalatllc aarmepalkl paeqaeqahr
      181 rleaisagag faggasmeds ivrpsvalvv atlgkaisaa lgapkvs
//
LOCUS       WP_284917360             420 aa            linear   BCT 25-DEC-2024
DEFINITION  MDR family MFS transporter [Actinoplanes oblitus].
ACCESSION   WP_284917360
VERSION     WP_284917360.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023665
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..420
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43999
     Region          17..375
                     /region_name="MFS_MdtH_MDR_like"
                     /note="Multidrug resistance protein MdtH and similar
                     multidrug resistance (MDR) transporters of the Major
                     Facilitator Superfamily; cd17329"
                     /db_xref="CDD:340887"
     Site            order(26..27,30..31,34,66,116..117,119..121,124,144,
                     147..148,151,223,226..227,230..232,235,262,266,315..316,
                     320,324,340,343..344,347..348,351)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mrgwlrqaag glprqfwflw tgtlinrlgs fvvlflsiyl tgerhlsqsq aglvlglygv
       61 ggavgtmtgg vladrwgrrp tmltaqfgaa almltlgfad syprilvvta llgvftegvr
      121 pafsammvdv vperdrvray slnywavnlg falaaiaagl aaqadflllf vvdaattvat
      181 atitliflte srpahrpiag gaprggmltv ltdrvflayw vvnllvvlvi mqhmstlpla
      241 mladgfsaat ygwviavngi mivsgqlfvp rlldghrahr vlaigaviig agfglvavah
      301 sawmyavtvv iwtlgemiqs psnaatvadl spaalrgryq gltslswsig salapilggl
      361 vlqgfgsatl wvgcfglcal aaaghllagp arerraalrr aeedallnta gttaapapas
//
LOCUS       WP_284917368             533 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Actinoplanes oblitus].
ACCESSION   WP_284917368
VERSION     WP_284917368.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 533)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 533)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 533)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..533
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55610
     Region          48..533
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          325..532
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mriaargvgr ssrliagcag vtvtvlglln thtsdlnapp eglspapafv lmpaglallv
       61 rvlplagpat rlrtgaaavl alsaavlgaa aisrhpaagl atglaglala gldvrllrig
      121 rvavritdpl llgaatialv alvarlftat gmmpldlagg lllltagavl arpeaeppsa
      181 pdtadqrlva elrdrqdfad tllqsmneav mvldanyrvi dvnrrwrelt gqpddvrepp
      241 plpppghggd wllpradgte vpvlatmaai pdaagaprgy vatcvdigsr kqaeealseh
      301 aaelergnaq laaansqlaa alsfkndlts mlthdvaqpi ssiaslaell cadwadlped
      361 irlelslkid kntrrlvkmm ndlqllfrld tgavtarrvp vpllevvraa raetagadev
      421 eiaidedlsa ladrghlavv venllknaia hgaapirvga erqdgtvllr vqdsgagipe
      481 dllpnlfgrf irgaglglfi vrhlveangg svryehavpr garllvtlea apr
//
LOCUS       WP_284917549             242 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Actinoplanes oblitus].
ACCESSION   WP_284917549
VERSION     WP_284917549.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..242
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25589
     Region          44..204
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 msrgvllnrp gdlpswfepl ltgaarsrae dfsvlrqpag gggrssavlv llgesppdad
       61 tpggpdvlvl qraatmrnha gqpafpggat dpedadavat alreadeevg ldrgsaepla
      121 llpelwipvs rfsvtpvlaw wrrphpvrpr qvtevahvar lpiseladpa nrirvrhpsg
      181 wigpafqvrg mlvwgftagv isvlldmagw trpwepgrvv elpdaaapvp aarggapdev
      241 vp
//
LOCUS       WP_284917695             916 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Actinoplanes oblitus].
ACCESSION   WP_284917695
VERSION     WP_284917695.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..916
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..916
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=95756
     Region          <6..888
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mqgrvllgre terrvlaalv eqaasgsgga vvvlgaagig ksslvaeaaa qaarrgtrvi
       61 tavgveseen vpcaglhqlv hqlregiddl pgpqraalrg avglvdeavp dlylvglaal
      121 tllsdaagka pllvvvedah wmdrasldvl gfvarriesd plvlvvvtrg lddrlagagl
      181 pvlplnpltd evsgelldtv apglgqqvrk rlleeaagnp laltelpval qsvggayalt
      241 pgplplterl ertftarvsr lpvdtrtvll laalngdgtm declaaatrm lgrpvdiaal
      301 spavgaglve awgmvfrhpl vrsamhhaat aaerqaahaa laaelqgqpd rqawhraaat
      361 sghdeqaard ldstagralr rggvaaalaa mrraaeltad pharadrllr aaelalesgq
      421 gdvathllaq arsldlsvrd qgraawvgia liegaargeg iataelaela vgiaaggepv
      481 lglrmlwgav lhcywgepgp aarrrvaaav grmpvdadna dlvalrayca pvergravle
      541 slagqlerss edaegdqllg gaavtvgapa lasrltarsl dvlrargrls mlaralcvqa
      601 gssarlgdvr agslaaeeaa elasetgqpl vramvhaira qlaavcgdpr veawaaeaer
      661 aalpagarpa lailqtargh aalcqgrygd afghlhrvfd padpafhpwl rfyalaelve
      721 agvrsesaea vrdileeltp lgeltpspal lcglrlgral lspadaaepl yraalaavpv
      781 dwpferarvq lalgewlrrq rrpaesrvvl qaarevfdal gasawaerar qelraagass
      841 prqdpaavdr ltstelhvaq laaqgltnre igerlyvspr tvsthlqrmf pklgvtarge
      901 lagvlrstmt yaedva
//
LOCUS       WP_284917866             433 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Actinoplanes oblitus].
ACCESSION   WP_284917866
VERSION     WP_284917866.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..433
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=45683
     Region          11..>419
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 masdqwsgfg avlrahrrra gltqeelagr aaigvrtvrd lergrssrpq rttvellara
       61 lgltgsdlea flsaargrpa atlppaplde ligrdadiae lvarltdgdg prgvtlagva
      121 gvgktslavv vahrlseayp ggvagvavad eiaagellsa vaaefgapgp rdlpgyldgr
      181 palilvdavd raplavgaal aelleqvprl rflvtgrepa glpeervwpv aplatppvsl
      241 svdtagelmv ypavglfler lgrvrrtrla pheigplaal vrrlgglpla ielaaargrv
      301 ltvpeilery aasaepprsp avsldavvae tyralapteq walrqlavfr hrwsrdlaev
      361 llgtadvvhl ldrlvalgll svsdnqvvhf rlpsavrefa aeraaaegel adarkrhtrl
      421 laerpipgvq avf
//
LOCUS       WP_284917905             172 aa            linear   BCT 25-DEC-2024
DEFINITION  SixA phosphatase family protein [Actinoplanes oblitus].
ACCESSION   WP_284917905
VERSION     WP_284917905.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..172
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18742
     Region          6..147
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mtlrtlillr hakaetpgel pdfdrglter gmsdadaaga wlvderlhpd lvicspakrt
       61 rqtwqaasma laqgdhahga pevhyadqly yggrtevfdl lhavpetvrt illvghnptv
      121 sevsallipd dqwdglavel ktsglavhta etpwseaqpk gmrlsrrhta rg
//
LOCUS       WP_284917960             359 aa            linear   BCT 25-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Actinoplanes oblitus].
ACCESSION   WP_284917960
VERSION     WP_284917960.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..359
                     /product="Glu/Leu/Phe/Val family dehydrogenase"
                     /EC_number="1.4.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016639 - oxidoreductase activity, acting
                     on the CH-NH2 group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37795
     Region          14..356
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mgvfdtdgsd atgheqvvfc qdrvsglkai igiystalgp alggtrfypy esedaaladv
       61 lklsrgmayk nalagldlgg gkaviwgdpa tvksesllra ygrfvetlkg ryytacdvgt
      121 yvpdmdviar etryvtgrsv ehggagdssv ltawgvfqgm raaaehtwgs ptlagrtvgv
      181 aglgkvgkyl vghliedgat vvatdvnpaa lewartthpa velvadnqal itadldvyap
      241 calggalndd tvpvlrakvv tgaannqlah pgigkllddr gilytpdyvv naggviqvad
      301 eiegfnfdra klrataifdt trrilqlagd egvppavaad rlaerrmaev grlrsiylr
//
LOCUS       WP_284918053             108 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix domain-containing protein [Actinoplanes
            oblitus].
ACCESSION   WP_284918053
VERSION     WP_284918053.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..108
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11955
     Region          20..101
                     /region_name="HTH_34"
                     /note="Winged helix DNA-binding domain; pfam13601"
                     /db_xref="CDD:463932"
ORIGIN      
        1 msdtrselpe ldpvihaqar lrvvsalsql readsiafpr lqeilrmtag nlsvhlrkle
       61 dagyvavvkt hrgrtpatlv rltrrgrlaf ddyvialral lnqpeegs
//
LOCUS       WP_284917980             436 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Actinoplanes oblitus].
ACCESSION   WP_284917980
VERSION     WP_284917980.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..436
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=48931
     Region          1..431
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 maarialltr dlrvhdnpll sgdgeivplf vldprlagls anrqrflhqc ladlrdslrd
       61 rgadlvireg dpvaetvrla revdtatvqv agdvtdyaqr rerrlrtagl dlrvtpgvtv
      121 lppgavrpag ggqsyrvftp ywkswertgw repaatprti ampdgiapgr lpetpagesp
      181 dalaggetea rrrlrawsge lsryadehdd maadntsrls aylrfgclsp lelalaakat
      241 dspgaqaflr qlawrdfyyq vtaafprist qpmrpsadtt wrsdedalqh wqdgltgvpi
      301 vdagmrqlra egwmhnrarl itaafltkhl gidwrlglrw fsrwlidgdv pnnsgnwqwt
      361 agtgndtrpy rrfnpirqaq rfdpqgeyvr ryvpelkdvd ggavhqpwrl pepvrrgldy
      421 pgpleshrde avwlrn
//
LOCUS       WP_284918146              74 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284918146
VERSION     WP_284918146.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..74
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          <2..62
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
ORIGIN      
        1 llgnkdeaik yykkyintyt kndqyyddsy yelgmlyydn gdlknaqqtf yslrsevpds
       61 mynnskikei lsek
//
LOCUS       WP_284918187             345 aa            linear   BCT 25-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Actinoplanes oblitus].
ACCESSION   WP_284918187
VERSION     WP_284918187.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..345
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=37633
     Region          18..>184
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mtarprrwlt lalaplvtaa ifvapitpah aapggsgtta eegeasddls dqieatnrrf
       61 vnakaavaks kktqiqlaaq iktaearrdq lvpevnaiak qqyqvgnlss lsfllrasds
      121 adfldkavsl eeinklhdek lhelntllqd itadktrlda evknqeqqls vqkklhdsae
      181 dqlellgggt ginktitagf vdaksptaap aprnsdggfs pescnqddpt tdgcitkrtl
      241 hlykevkkag fnmfvgchrd ggpfehpkgr acdwslqksg fssatgnakm mrygndltaf
      301 lvrnadrlgi yyviwykqiw fpatnnwhay hgpsdhtdhv hvsll
//
LOCUS       WP_284918197             157 aa            linear   BCT 25-DEC-2024
DEFINITION  cysteine dioxygenase [Actinoplanes oblitus].
ACCESSION   WP_284918197
VERSION     WP_284918197.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Chen,M., Zhu,J.Y., Mu,W.J. and Guo,L.
  TITLE     Cysteine dioxygenase type 1 (CDO1): Its functional role in
            physiological and pathophysiological processes
  JOURNAL   Genes Dis 10 (3), 877-890 (2022)
   PUBMED   37396540
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Joseph,C.A. and Maroney,M.J.
  TITLE     Cysteine dioxygenase: structure and mechanism
  JOURNAL   Chem Commun (Camb) (32), 3338-3349 (2007)
   PUBMED   18019494
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14410663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..157
                     /product="cysteine dioxygenase"
                     /EC_number="1.13.11.20"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0017172 - cysteine dioxygenase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17080
     Region          38..132
                     /region_name="cupin_CDO"
                     /note="cysteine dioxygenase, cupin domain; cd10548"
                     /db_xref="CDD:380416"
     Site            order(38,40,52,63,65,112,126,128)
                     /site_type="active"
                     /db_xref="CDD:380416"
ORIGIN      
        1 msaatavrld hlaiarqfad apqgwvvppr fdpverwyar lhaadnhevw lltwlpgqqt
       61 elhdhggsag afhvfsgtlt edtvggpaes prvvtrdlge gagrrfgshh vhrivnrgad
      121 paisihvygp altrmtkyrl spagleirav eragaew
//
LOCUS       WP_284918221             639 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Clostridioides
            difficile].
ACCESSION   WP_284918221
VERSION     WP_284918221.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..639
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=74014
     Region          8..625
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mkerakkild fiiknnnvts qelqekfnvs krtiyydila ineqlgksgn iknvkhkfif
       61 egnlcdarki isteedkfld sdyrktfiln killgekisi ekltnemlls kntvvqtitd
      121 vkkylqtmgl rleykgkyki igdeyvirel fliivqenil einsiseevs sfdtkghikl
      181 tdysllnltk fveflnkrir dgktlysyky lneakkisyf snckellcee aneneqayic
      241 tyisslpsln sevkedvvee yvdklidkfe vntaiklesk hefkknilrh lhssynrirf
      301 kfpirnpmld etkykhesly kiiksiiene eefpvfegir eeeigfiaay frgylrgsrd
      361 nglrrnkvll vcpnglmvsk sleiqlykyi ptieivgivs ikqlkevnvy ydyiittidi
      421 qnvnnvivvn plltssdvql lmnklisvke nekyfnleli iqairkngvi nneealkadl
      481 lniihkideg emyqpmlkel inaervniik svrdwkeaik iaskplledn sieelyienm
      541 iksvekygpy ivladrfalp hasskegvnk lamsllived evdllgkpvn ifmvlaavdn
      601 tthiralasl semmyeeenv kliingdkss ilelinkqn
//
LOCUS       WP_284918265             229 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Clostridioides difficile].
ACCESSION   WP_284918265
VERSION     WP_284918265.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..229
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=25808
     Region          1..218
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mlrsishdlr tpltsilgss stilenddvi dketrvellk niyedtswlt hsvenilsmt
       61 ridegkldie krpevvdeii aesilrvkkf ansrdiktni pdeiiivhvd vllieqvlvn
      121 lidnairhtp knskieltvk kesnqvlfev adngkgipne dignifnrfy tknksrnler
      181 rgiglgleic ksiveahgge ivafnnpsgg atfrfsipmy deegkdkwk
//
LOCUS       WP_284918371             719 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Actinoplanes oblitus].
ACCESSION   WP_284918371
VERSION     WP_284918371.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 719)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 719)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 719)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..719
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..719
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72096
     Region          51..>289
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mtstspveps apvavidgea ivgetpadgt ppspprdrsg aarlllgrad apwvrpalva
       61 lligtavlyl wglgasgwan afysaavqag saswkaffyg ssdaansitv dktpaslwim
      121 alsvrvfgls swsilvpqal lgvastglly atvrrgfgpv agllagtvsa ltpvavlmfr
      181 fnnpdallvl lmvagayatl ravengstrw ivlagvlvgf gfltkmlqal lvvpayglay
      241 lfagppklgk riwqlllalg alvvsagwyi aivelvpasa rpyiggsqnn slleltlgyn
      301 glgrlngdet gsvggggrgg naggmwgsps vtrlfesaqg gqiswllpaa livlvaglvi
      361 tarrsrtdlq raglllwgsw llitglifsf mqgifhayyt valapavgav vgmgvtllwk
      421 hranlvaalt lgatiavtaw wsyrllgrss dflpwlrtpl lvagiaaava vvaafrlsrr
      481 ialvggvval vtalagpaay avqtasqpht gsipsagpav aggfggpggg rggfpggggn
      541 rggfpggagn ggagnggagt ggfpgggqnq gqpqgglpgg lpgagggpgq dggrgpaggm
      601 ggllnaasvs aemkalleqd aaeytwvaaa vgsqnasgyq lateqpvmai ggfngtdpsp
      661 tlaqfkeyva agkihyfigg ggfggggsgs ndssqiaswv adtftartvg natvydlts
//
LOCUS       WP_284918448             471 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Actinoplanes oblitus].
ACCESSION   WP_284918448
VERSION     WP_284918448.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..471
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=50062
     Region          23..83
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(29,33,58)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(32,57)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(39..40,51,54,58..59)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mkseipgsiw trpdmltalq srdiahvfrl vrqhagmsqt aigsligmsq gkvsgimags
       61 qqvttldvye riadglrlpd tarmtlglap rsisardgsh sdatgtvnst rsverdprpe
      121 ednavrrref vgltgaalfg ailaeteptp kpaasgiddl ataltemptp aagpvnltrl
      181 satvaaakrd yqackygevl tmlppllrsl rtastatdga qqrkaqalsa eayhvaasil
      241 lkqgdkglaw laadrsvqta qqtevplmig ssariithal mdgghhgaaa inassaaqrm
      301 daaltqptdn dlsvygslll rgaiaaahng drhtttelld eaeqagdrlg hegnhmwtaf
      361 gpnnvlchrv naalrfgdag taidyarrid ldalpinerk avllldvtra flmwgkheqa
      421 lhtmraagqi apeeitgrpr ihklvgdlva tapitvrrea refadaygia a
//
LOCUS       WP_284918611             304 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Actinoplanes oblitus].
ACCESSION   WP_284918611
VERSION     WP_284918611.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..304
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33699
     Region          4..199
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mnwpsvgvvi ptrnrpelvr rsiaavreqr ypgelkvivv ydqtepdyll actedvpvlv
       61 ltnwrsagla garntgvlal dtelvafcdd ddqwvpdklr rqvaallaep daefatcaie
      121 vefegrttpr lagrsrvtve dlarsrmaml hsssflirre alaedavglv aedapgsqne
      181 dwdlllraar rapivhldep lvrvlwgrss hyayeyatki sslrwmmqrh peisgcrpga
      241 arvygqlacw saatgnrsqa wqfskeavra nwkeprtaia laamtgavkv envlsalhkr
      301 grgi
//
LOCUS       WP_284918624             457 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Actinoplanes oblitus].
ACCESSION   WP_284918624
VERSION     WP_284918624.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..457
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=48840
     Region          211..440
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mtavapaapp agsaqqragr dlslpawpvt gilllyplww alglgvlifp lfavpmlvll
       61 irrraagrpl rlppgfawwa ifliaavvsi aalgadpaqt vveraagrlp avlyklamya
      121 sltvlllyag nlterelprr rlvrllagmf vltvlggllg mvagtfefta pvewllphgi
      181 rskgfvrslv hpyaaqimdi vggekprpaa pwgytntwgn nfcllvpwlm vaaaathrrg
      241 rrvlawlcll vsvapavvsl nrglwiglgv vvlyagiryv lagklwvlga lalaaaaiav
      301 allatplggt vqarldngks ngvrsflier amdgfadspv igyggtrntl ggrnsitvge
      361 ssecercgnf tiggngqlwq llyaygavgt agylgffgyg lwrfrrdrsa igvagsaalv
      421 ssfsamlwyn slvtplafmv layallwrnw iegkttn
//
LOCUS       WP_284918643             198 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsB family cell division protein [Actinoplanes oblitus].
ACCESSION   WP_284918643
VERSION     WP_284918643.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..198
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=21625
     Region          82..165
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 mtqrrmpsgq gpsrratgat grpgsrtrvt gpvrtearpt vrvptsrsar pagsrrtsqs
       61 ggpaakrtaa prprsltsra tvllaifvvl alaytyplri ylqqeaqiae meraqaaqqa
      121 kiaetrkela kwgdddyiri qareqgffvr pgetplrvys dpdaaaresd qkspaaapdr
      181 wydtlwhsvq aanaepsn
//
LOCUS       WP_284918674             113 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Actinoplanes
            oblitus].
ACCESSION   WP_284918674
VERSION     WP_284918674.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 113)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..113
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12633
     Region          14..102
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mpgravrgss tgrplmaald lfgrrwnlri vwelrhgpvg fralrercdn msssvlrqrl
       61 telldaalve qhpdasyalt elghsarral rplirwsaew aetlsaadse ear
//
LOCUS       WP_284918750             384 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Actinoplanes oblitus].
ACCESSION   WP_284918750
VERSION     WP_284918750.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..384
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=40698
     Region          1..382
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mhpdtrmvhv iapipehstp lavpiyqtss fafadpelma dgmhrpdgay vysrfanptv
       61 raletavadl eggaaaiaas sgmgaitmll hsllgtgdhv iaqhgvyggt hallhdlvar
      121 rgvtvtrvdg rdpeevraal tprtkvlyle tianptghvs dlpalapvar aagvltvvdn
      181 tfatpvfcrp iehgadvvvh satkflnghs dvtggllvfa dpelhqrtwe yaaefgatad
      241 pfaawltirg lqtlalrmer haanvtrvat wladhpavss vswtgpapak hvtgypgafc
      301 fdlaggydag vrllsrvrli raapslggtq tlmlhpasts hrqltpeelr aaritpgtvr
      361 iavgiehpdd litdleqald vasr
//
LOCUS       WP_284918825             561 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Actinoplanes oblitus].
ACCESSION   WP_284918825
VERSION     WP_284918825.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 561)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..561
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=60658
     Region          1..551
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 markalldrm rrvvddgivl aslvllvwpa adaaggtwtt rlvpvaaalc lglamllvap
       61 erpilrfapt aaalavsgir hlqgelarga iwlllamavt vlarrwigag sdkaliremt
      121 tqrallvrqa yrdpltgvgn rtmfleraeh elaeasrtmt avivvdldgf relndthghe
      181 igdgllraaa drlaanvran dvvarldgde fvvllpgled eqaavavaer vltelhrpie
      241 vdgvrmtira sagvaltdgg dgidhvlrea dqalhrakld gggavrrfdp elfaleeqrr
      301 kaegdiiral dlgefevhyq pivdldgeht vgvealirwq hpekglvppg lflelaeqlg
      361 llprlggwvl eeacrqavhw qrqfpgfemn vnlsasqlsn pnlvaevrav lertgldpeh
      421 lvleltesva lvdlvesari lselkelgvr ialddfgtgf sslshlsalp vdvvkidrsf
      481 vqampesgga svaeavlhia rtfnlapvae gvedaaqaew lrelacsraq gyhfakpmpa
      541 lgvtelldkq adserdipla g
//
LOCUS       WP_284918899             213 aa            linear   BCT 25-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Actinoplanes oblitus].
ACCESSION   WP_284918899
VERSION     WP_284918899.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..213
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=23477
     Region          2..173
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mladqyylia hedrtgrsrl hpratglgla aallselvle grigvsegdl fiidqrpprd
       61 alshdildll caqsqhrdvr twlaflaqds alrvaerlmr vgaveavtrr rmlgstqtly
      121 mpntarqrna aawastrian mlvrgmelsa sdrmlvgivv atgltrhvmy gfenyphiyh
      181 glpsmiaslp ndlrelvect essvgsaltv grr
//
LOCUS       WP_284919025             106 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Actinoplanes oblitus].
ACCESSION   WP_284919025
VERSION     WP_284919025.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..106
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12372
     Region          5..87
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtdddrvfka ladpsrrfll dllyardgrt lteleselem trfgvakhlr vleeaglvvt
       61 rrsgreklhf lnpvpireih drwidkyteh qitalidlkr tleees
//
LOCUS       WP_284919056             222 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Actinoplanes
            oblitus].
ACCESSION   WP_284919056
VERSION     WP_284919056.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..222
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23652
     Region          2..216
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mpllysigkl tvgnalmvgw kprieglehv pktggaifag nhlsvadelf lgaavprhla
       61 fwaksdyfvg kgvkgffsrk lmeglgairv eraggraalt afdaaipalk sgdlvavype
      121 gtrspdgrly rgrtgvarla vaagvpiipv gmlgteivqp igrlapklmr gvvtvkfgkp
      181 ietigrsddr tslreltdqv mgeiqkltgq eyvsryapkr ae
//
LOCUS       WP_284919194             421 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Actinoplanes oblitus].
ACCESSION   WP_284919194
VERSION     WP_284919194.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..421
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=47315
     Region          94..407
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mpkkrkpedy ptisqgadgk whawvtvgtk pngrpdqrhv krqnyegaea rvdellaqkr
       61 tgqvqnagra ptvqawfeev yfetvapltm dlttiegark klrryayptt gkirmdrlqp
      121 snvtavyvam vrsgladttv lqvhriivrg lrvafrtrvi tcnlaelitp ptakkkvlaa
      181 ptkgeadrvl aatdnrrsst rwrcgfglgl rqgealglrw pwldidseqp earihwqlhr
      241 rpflhgcsgs pcgrrragnc pqrilplkag eiqvegglil kppkgssyge iplpaelvee
      301 frrhreiqdf ekmmagdayv drgfvfcdrl ghpispeadw kefqeieaea gvhlrvhdgr
      361 hftasflial gvdssvvqki lrhssikvte gyldastelk reatsrmgqa lrrpqregng
      421 w
//
LOCUS       WP_284919302             196 aa            linear   BCT 25-DEC-2024
DEFINITION  YdeI/OmpD-associated family protein [Actinoplanes oblitus].
ACCESSION   WP_284919302
VERSION     WP_284919302.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Pilonieta,M.C., Erickson,K.D., Ernst,R.K. and Detweiler,C.S.
  TITLE     A protein important for antimicrobial peptide resistance,
            YdeI/OmdA, is in the periplasm and interacts with OmpD/NmpC
  JOURNAL   J Bacteriol 191 (23), 7243-7252 (2009)
   PUBMED   19767429
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..196
                     /product="YdeI/OmpD-associated family protein"
                     /calculated_mol_wt=22007
     Region          3..192
                     /region_name="YdeI"
                     /note="Uncharacterized conserved protein YdeI,
                     YjbR/CyaY-like superfamily, DUF1801 family [Function
                     unknown]; COG4430"
                     /db_xref="CDD:443542"
ORIGIN      
        1 maepstaatf fpdaaalraw feenhesate lfvgywkkga getgvshpea ieqalcfgwi
       61 dsvvrriddr ryrvrftprr kgsvwsevnv tkmaelaerg llrpagrraf derrparvge
      121 ysyeqaapvt lddaqlarfq adqgawtwfa gqspayrrsa thwvlgakra dtrerrlaql
      181 iadsgagrrv pplisr
//
LOCUS       WP_284919474             339 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Actinoplanes oblitus].
ACCESSION   WP_284919474
VERSION     WP_284919474.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..339
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35061
     Region          1..339
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mvdlrsdtvt rptpgmream aaavvgddvf gddptvnale qhvaqlfghe aalfcpsgtm
       61 anqialqlvv ppggellaga dahvvtyelg aaallggist rtwpatgaal nvdriaamir
      121 pagfpsvpta aiaveqthnl ggggaiplat lrdlravada hrvalhcdga riwhahvadg
      181 vplasygalf dtlsvclskg lgapvgslvv gsreriarar virkrmgggm rqvgilaaag
      241 ryaldhhver laedhararr laeglaplgv vdpdrvrtnl vpldltkapl dapelateaa
      301 rrgvliaaml pklarlvvhl dvddagidea vsvlsvlla
//
LOCUS       WP_284919628             110 aa            linear   BCT 25-DEC-2024
DEFINITION  Rieske (2Fe-2S) protein [Actinoplanes oblitus].
ACCESSION   WP_284919628
VERSION     WP_284919628.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..110
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=11490
     Region          1..104
                     /region_name="NirD"
                     /note="Ferredoxin subunit of nitrite reductase or a
                     ring-hydroxylating dioxygenase [Inorganic ion transport
                     and metabolism, Secondary metabolites biosynthesis,
                     transport and catabolism]; COG2146"
                     /db_xref="CDD:441749"
ORIGIN      
        1 mtfenigpas giakgtslqv evdgveiavv hadddnfyav rdecshasva lsegevdgct
       61 lecwlhgsrf dlrtgepsgp paidpvavyp veirdgdiyv sttpsngvep
//
LOCUS       WP_284919570             389 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Actinoplanes oblitus].
ACCESSION   WP_284919570
VERSION     WP_284919570.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..389
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=40864
     Region          21..378
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mrtavvvgag maglaaagal srtgwrvtll eraeriaapp tavvlwpngr raldaldpdg
       61 gwsaiasplp dggvrrpdgq wlvaprpria aagprpavah ledlydalva glgdteirtg
      121 fevhtvrtgr rerpavgdgh tlieadllva adgidsrvrt alapestvvg sgfaawqavi
      181 pgyrmprpae gqvlggetlg agyrfvaipl gahaagkggv ywvataagaa rpeppatqla
      241 llqrwfagwh epvgellslt rpeelvpqgv relrplprsy afpsgpggvl ligdaahamp
      301 hhlgqgacla fedaatlhsl fagaapgdal traldaytrl rqprttsvvr qsrrmsavvq
      361 argrlalrar daalnhmrpr tlvdwsppe
//
LOCUS       WP_284919625             321 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Actinoplanes oblitus].
ACCESSION   WP_284919625
VERSION     WP_284919625.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..321
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=33552
     Region          17..296
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mprvksfepl yrpfatwlrp lalaslvanv vlivtgaavr ltdsglgcpt wprctdasyt
       61 ttsamgvhgm iefgnrlltf vlaglaiacf lgalgrprrq slvrlsvlvg lgipmqgvlg
      121 gitvlthlnp wvvglhflls ialitlayaf wrrigegdgd prplvpaplr tlarvtalas
      181 lavvaagvvv tgsgphsgdr gakrngldpa avsqvhadlv flliglsmav wfalravsap
      241 paavraalil vavelgqgli gfvqyfthlp vllvaahmlg aglvwwatlg vlwslrerpt
      301 htpadpapas pspaeepvpa a
//
LOCUS       WP_284919657             388 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Actinoplanes oblitus].
ACCESSION   WP_284919657
VERSION     WP_284919657.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 388)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..388
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41715
     Region          26..322
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 maqpstpete tspepvppah dasqleramf evkrvivgqd rmvermfval larghclleg
       61 vpgvaktlav etlakvvggt fsrvqftpdl vpadivgtri yrqsseqfdv elgpvfvnfl
      121 ladeinrapa kvqsallevm aehqvsiggk sydvpdpflv matqnpieqe gvyplpeaqr
      181 drflmkiivg yptdaeerei vyrmgvsape pkqvftpadl lalqrradqv fvhnalvdyt
      241 vrlvlatrap aqhgmpdvaq liqygaspra slgivratra lallrgrdya lpqdlqdvap
      301 dilrhrlvls ydaladdvpa dqivarimqm vpmpsvasrq gtspngahvp papngaqpts
      361 gvpagaaypv ngagtpfppn gpgwpgqa
//
LOCUS       WP_284919678             268 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Actinoplanes oblitus].
ACCESSION   WP_284919678
VERSION     WP_284919678.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..268
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28738
     Region          6..264
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mpaiaittpd dprigdyral tdlelrtrwe ppnglfiaeg elviqralra gyrmrsalvd
       61 ekragqltgl pgdaplyaaa ppvlesitgf hvhrgilasf hrrplpsldd llgtarnlav
      121 leglnthtnl galfrsaaal gidaivlspn cadplyrrav rvsmgevfai pytkteswpd
      181 plvairdagf tllamtpapd avalqrltpe qrrrpalllg aegpgltada ltasdvrvai
      241 pmhndvdsln vataaaitfy eltrdatr
//
LOCUS       WP_284919735             371 aa            linear   BCT 25-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Actinoplanes
            oblitus].
ACCESSION   WP_284919735
VERSION     WP_284919735.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Rengstl,B., Oster,U., Stengel,A. and Nickelsen,J.
  TITLE     An intermediate membrane subfraction in cyanobacteria is involved
            in an assembly network for Photosystem II biogenesis
  JOURNAL   J Biol Chem 286 (24), 21944-21951 (2011)
   PUBMED   21531723
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Komenda,J., Nickelsen,J., Tichy,M., Prasil,O., Eichacker,L.A. and
            Nixon,P.J.
  TITLE     The cyanobacterial homologue of HCF136/YCF48 is a component of an
            early photosystem II assembly complex and is important for both the
            efficient assembly and repair of photosystem II in Synechocystis
            sp. PCC 6803
  JOURNAL   J Biol Chem 283 (33), 22390-22399 (2008)
   PUBMED   18550538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..371
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=40887
     Region          46..248
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          169..352
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
ORIGIN      
        1 mtgvrllvgt rkgafvltsd gtrkdwqidg phfagweiyh lngspvdpdr iwasqtsgwf
       61 gqvmqrsddg gknwqavgnd fayappvgdh lwydgtprpw efkriwhlep srtdpdtvwa
      121 gaedaalyks tdggqkweel talrqhrtgp qwqpgaggmc lhtivlhptd pdrmyiaisa
      181 agafrtddgg atwqpinagl rsqgipdeda evghcvhrla mhpsrpdtlf mqkhwdvmrt
      241 ddaggrwrei sgdlptdfgf piavhahepe tvyvvpitsd slhyvmdgkl rvyrsrtgga
      301 eweplsaglp qshcyvnvlr damavdtlde cgvyfgtsgg qvyasadsgd twtaivrdlp
      361 pvlsveaqvl p
//
LOCUS       WP_284920008             358 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Actinoplanes oblitus].
ACCESSION   WP_284920008
VERSION     WP_284920008.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..358
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=39298
     Region          40..328
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msggakpevl qaartllqqm gitpadllnt avpgrsaptf aeylpivaaa vapgsqrmyg
       61 tywakalerw aerridsvip seievamrei qatalrrrnn rggrsaaehf isamrcfykr
      121 avadgyigeg dnparkvpkp arlastrsal addrlaelte tagtsgndpe ldtlilrfhi
      181 etacrrggll alrpmdldve qclvllrekg dtfrwqpvsp tlmaflqqha qergspqrgs
      241 llryrngkpv grrrydylft rvgdllpwvr vqmisahwlr httltwverv ygyavalaya
      301 ghaetpndag ttaryvkatl qevatalsgl tgephplalp gnlpvlnlag dalvgeyd
//
LOCUS       WP_284920050             110 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Actinoplanes oblitus].
ACCESSION   WP_284920050
VERSION     WP_284920050.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 110)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 110)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..110
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12397
     Region          3..98
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mpadelsrvf aaladptrrd mvarlatgda tvnqlaepyr mslqavykhl kvleeaglvs
       61 rpagpqprsv rlerdvfdev ggwieqyrrr aearyqrlda vlrtmneqeg
//
LOCUS       WP_284920137             124 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Actinoplanes oblitus].
ACCESSION   WP_284920137
VERSION     WP_284920137.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..124
                     /product="YybH family protein"
                     /calculated_mol_wt=12882
     Region          8..123
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mtvttafdms aafqelvngr dldglldlfg pgavsrtvgg evltdpdrir adlagllagn
       61 phlvntprht lvsgdvalml idwtlevdtp dgraqlagtt tnvvrqtldg gwrfavlnpa
      121 gtaa
//
LOCUS       WP_284920173             293 aa            linear   BCT 25-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Actinoplanes oblitus].
ACCESSION   WP_284920173
VERSION     WP_284920173.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..293
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32435
     Region          1..274
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 msieiqrigg rigaavtgvd lkhpiaadva ekirdalveh kvlvfrgqhl ddeqhqrfas
       61 ifgeltlahp tvpsvdgqan vlevaggega ranawhtdvt fvaappkatt lrslvvppyg
      121 gdtlfantaa ayddlpehlr lladrawaeh sneydyaehp qfrsaeveey hkvfvstryr
      181 tahpvvrvnp dsgrpnlfig nfvtgilgls ktesrdilrl lqhyvtrpen tlrhkwqvgd
      241 lvvwdnrstq hyaaddygdl prklhrvtva gdvpvsvdgv ksyviegefs dvr
//
LOCUS       WP_284920200             173 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase, partial [Clostridioides difficile].
ACCESSION   WP_284920200
VERSION     WP_284920200.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>173
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
     Region          23..158
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mindiknkfk nykpyingyk nmkrasvlip iveinnthyi lfevrsknlk hqpseisfpg
       61 gkiesgetpy eaviretcee lgtfsdniev issldllitp vkfiihpylg yikninnlni
      121 nkdevdhtfl vpikyllenp pntysntvkv fpdenlpygs ipnqkdykfe sgs
//
LOCUS       WP_284920227            1007 aa            linear   BCT 25-DEC-2024
DEFINITION  NACHT domain-containing protein [Actinoplanes oblitus].
ACCESSION   WP_284920227
VERSION     WP_284920227.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 1007)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 1007)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1007
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..1007
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=110978
     Region          180..989
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 marslgysda vrllggqdsk vvaaiekitg gvllaatpav pallglfdak aelvrlghdl
       61 vrgfaerrsg lsrfsrtqrl qaahtvivvt affeamadag lpfrfdelem tgqeqeslag
      121 raelltfpgr ldaaalldrs pvrapeavaa dlrnyyqgla qvflafctgl hvwdrlsage
      181 rdrvagataa vpdravarye etlrrlivdf pevacwanqr ehratraala gleetllais
      241 tgrapdqrra glarayrael gkrivesgdv pdgirvpelg egyvpprfra gdvhaaarvs
      301 eeswwagspv rddlqeflig hltspravra pllvlgqpgs gksvltrila arlpaadflp
      361 irvilrdtpv ldevqdqiey airqatgerv ewpalarsag dampvvlldg fdellqavgv
      421 sqtdylmkva rfqrreidqg rpvavivtsr tavadrarap eetvalrlep fddervtawl
      481 diwnrtnaan faaaglqplr petvlqhrgl tgqpllllml alydadrnal qragadlrah
      541 elyeqllrsf alreigkhre glpdrelraa venelrrlsv vafamfnrsv qwvteadldr
      601 dlaalqicgp vstataaglr aplpeaeltl grfffihrar alpdetafqt yeflhatfge
      661 ylvarltwqv lndlgardaa ssmsfgagpa eddllralls fqplsargpi ldflgqmada
      721 adpdrrrslr dllvrlyrav nhtppglryt dyrpqapsep aryavyaanl lllalccdhv
      781 lsgselypqp pdpvdawhgq tllwrallss dgwtglvdri rlsrvlvdgh rdlrlalhgh
      841 tdptfepewt fnlfpdarpd tfrlddlnfd qirrkayfqc siledmvhha vapldevpvp
      901 linsfvrggd gtisaarvlv dlwanpsaet crrtadllaa glpwseeacr yllstlltgl
      961 raippeaage ivrqlaesep ltgddraqqm iaewagrgvk gihrrlq
//
LOCUS       WP_284920348             319 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Clostridioides
            difficile].
ACCESSION   WP_284920348
VERSION     WP_284920348.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..319
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36356
     Region          <2..257
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
     Region          253..>316
                     /region_name="COG1693"
                     /note="Repressor of nif and glnA expression
                     [Transcription]"
                     /db_xref="CDD:441299"
ORIGIN      
        1 maltdnpili tgetgtgkea ftqsihnhsn rknkpfvain caslpselle selfgyedgs
       61 ftgakkggkk glfelahtgt ifldeigdmp hdlqvkllrv lqekeirkig gtsiipidvr
      121 ilaatnkdle kliienkfrm dlfyrismft ldlpplrkrl ediplllesf lkelpyknik
      181 ldksllealn sytwmgnire lrncieymay mgsnyltind lpqnisskln nnhmssnmsi
      241 fndlnqydkn icisilkslh mkpmgrtklm kfmeynvtey evrnmleylt rngylisskg
      301 rkgssitekg ikiiennii
//
LOCUS       WP_284920396             312 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284920396
VERSION     WP_284920396.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..312
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          83..309
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 flmmfivvig iiyyfiryin krlskiyfiv dkmsqenylk dtteseetgy lveyneyfke
       61 gifskinncl yelnrslkik fiklekekes vkslvtdish qlktplaslk lyntllieee
      121 leedeanefl ltnkasinkl enlinslvni srleismini kkedndiknt ilnavksvtp
      181 kaksksitln lnefnsriip hdkkwteesi fnvldnavky tqvngeinis veetanffki
      241 iiedngigie knefnnifkr fyrgsadeie svegsgvgly lsrkileeqg gniivsskvg
      301 igskfslflt tm
//
LOCUS       WP_284920582             216 aa            linear   BCT 25-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Actinoplanes oblitus].
ACCESSION   WP_284920582
VERSION     WP_284920582.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..216
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=23501
     Region          10..190
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 malppqlppa ddlyltahdt irgksllspa tlglglgaal lgelmlwrrv dlietellvi
       61 derptgdaat talleqirre agqhgvrdwi aylstgiate lverrlargg lirrqekrgl
      121 lgtkismvpa dsmtagwpat rirtkvsrde qldvadllla glilatgldq hvlatlnard
      181 rarlfdqfrr lfpamlqhlv ahaeaavgda vmarra
//
LOCUS       WP_284920628             229 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Actinoplanes oblitus].
ACCESSION   WP_284920628
VERSION     WP_284920628.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..229
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25120
     Region          <3..225
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mgagrwrrir lplprlhttv tasvwspdqr tdrllvahdg peyaerggla ahaaaagryh
       61 lallppgdrl dwyaacpawa dslaldilpr lrarlgagra vgtgvslgal amlhaqrshp
      121 agfaglflqs gsyfqprhdr qeagfrhwar iiryvrrvrt adsgpavpat ltcgsaeenl
      181 annrdmkdal akhgypvdla vtrgghdwdn wrntldphlt tlldrvwpd
//
LOCUS       WP_284920641             261 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Actinoplanes oblitus].
ACCESSION   WP_284920641
VERSION     WP_284920641.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..261
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28158
     Region          29..131
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mpthryrqaa esfgvdaary drtrppypae llrrildasp gravlnagcg tgiearqlrd
       61 lgctvlgvep dprmaafars tgiaaevatl edwdpagrtf dlvvagtawh widpvagaak
      121 aaavlrpggr lapfwhtfkl pdelaagfge vyrrlvpdsp fqlgrmpags aldgyrpild
      181 raaegiraag gfgepelwhv dwdreytree yldqlptsga ltrvapaqla eildavgeri
      241 dqlggtfvms ytsaavtasr r
//
LOCUS       WP_284920673             235 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Actinoplanes oblitus].
ACCESSION   WP_284920673
VERSION     WP_284920673.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..235
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24595
     Region          9..222
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mldpaapafd avlfdcdgvl vdseritnav lramlhelgw liseadcfrl fvgraladev
       61 gvitantgft vtagwlaefr rrrndalaag llaipgavaa aheidrlfdg rlacasgadr
      121 akvelqltkv gldrvfagki fsgmemprsk papdvylaaa aafgvdpara avvedtptgv
      181 ragvaagavv fgycppdspa hqdprvllea gathvfttma dlptlltrlp savre
//
LOCUS       WP_284920868             226 aa            linear   BCT 25-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Actinoplanes oblitus].
ACCESSION   WP_284920868
VERSION     WP_284920868.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..226
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=24320
     Region          13..179
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mwrpgldptl vreqfyllah detrqmrphl hlpalsagla gatvmdllia qrvtvesgsl
       61 rpdwyqrsst gdpitddvla limqaapgpp lpvliraasg glyerttaal vhkgvivegp
      121 prrwrkgrey aiahegiavr ararvgyrme grdgpspead slctlvsaln lhavlvrgtr
      181 sevepllqrv irdlpenaag hpigeaaava aavlkviqdm atsamm
//
LOCUS       WP_284920895             335 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Actinoplanes oblitus].
ACCESSION   WP_284920895
VERSION     WP_284920895.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..335
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=34611
     Region          12..324
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 melrtrftea yglttpiaqa gmafvastpe lpiavsnaga lgalgvgllp apaltqviag
       61 iragtdrpfh vnfitgftqp dqidaacaaa vpvasfhwgh pprdwidrlh aagsrvfeqv
      121 gsvdaakrav ddgvdvvvaq gleagghnfa tlptfalvpl vvdavapalv laaggiadgr
      181 glaaalmlga dgawigtrlv atdesgahqa ykerllaara tdtvrtsvfg petpdfnpmr
      241 vlrnrvtdew pseppagvar pvvgrtslgg peidiprfsn lvpirattgd ldempllagq
      301 gvglvdavks aasviadlta qakemitrfe pgewa
//
LOCUS       WP_284920947             222 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Actinoplanes oblitus].
ACCESSION   WP_284920947
VERSION     WP_284920947.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 222)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..222
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=24587
     Region          39..212
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mtlnmaavtv dlvlltirqa dlrvllirrg ippfegrwal pggfvhdded ldeaairelr
       61 eetgidpsag hleqlatygt pgrdprgrvv tvaylallpd lpapvagsda ahaewrpide
      121 pdlafdhhri ladgverara kleytplata fcppeftvad lrlvyekvwh ttldprnfhr
      181 kvtsaddfie ptghsatrer grpaqlfrrg patllhppll rp
//
LOCUS       WP_284920952             496 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Actinoplanes oblitus].
ACCESSION   WP_284920952
VERSION     WP_284920952.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 496)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 496)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 496)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 496)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..496
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=54558
     Region          1..496
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mtdsardrqw ttqqwfaavl vamvvlilga savgaralnr taqvsnrlnd rispartvvv
       61 qlddalrnqd talrgyllsg apqfldlyre svaaeqaaat tlrgfltaep gplaelaave
      121 deaarwragi aepalrtrdr gvaaaafdpv rgrlatlder lvtaraegra algdarrlrd
      181 tvflaavtal llligvitvl lrttvvrplr rlgaaarrva dgdftheltp dgpaevtqlg
      241 rdveamrrrl vdaltvtqqa rdeleqreae lsrsnadleq fayvashdlq eplrkvasfc
      301 qmlerryaea lddrakqyig favdgatrmq rlindlltfs rigrvyddeq pvdlnevmdr
      361 veetlaasie etrarivrpr lpvvagdvtl ltmlwqnllg naikfhrpee ppvieisata
      421 dgagwsfavs dngigidpey adkifvifqr lhprdrydgt giglavckkv iehhggviel
      481 dpayrdgarf vftlpa
//
LOCUS       WP_284920974             334 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Actinoplanes
            oblitus].
ACCESSION   WP_284920974
VERSION     WP_284920974.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..334
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36991
     Region          4..319
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtrpitlftg qwadlpfekv celasgwgyd gleiacwgdh ldvargatdd syvssrkail
       61 dkyglkvfai snhltgqavc ddpidhrhrd ilpaavwgdg dpagvrdraa qalkdtarta
      121 arlgvdtvvg ftgsaiwkyv amfppvsqdv idagyqdfad rwnpildvfd evgvrfahev
      181 hpseiaydyw ttrraldaig hrpafglnwd pshfiwqdld padfilefad riyhvdckdv
      241 klavgngrng rlgshlawad lrrgwdfvst ghgdvpwerc fralnaigyh gpisveweda
      301 gmdrlvgape alafvrdrlf dapsaafdaa fssr
//
LOCUS       WP_284921058             495 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Actinoplanes oblitus].
ACCESSION   WP_284921058
VERSION     WP_284921058.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..495
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=55271
     Region          31..449
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mttvehldvl ivgagisgig agrylktelp gksfailear gasggtwdlf rypgirsdsd
       61 lhtfgyefkp wrdeqsiada prilsylret itengldahl rfhhrvlavs wsterarwtv
      121 everadtger itltcgwifs asgyyrydeg ftpdfagree fgglvvhpqh wpadldhrgk
      181 rvvvigsgat avtivpamag daahvtmlqr tptyimpvgr kdpianalkr ylgpergyaw
      241 trrkniaqqk aiwsfcqryp kaarkvirwv ntrqlpagfp vdehfnppyd pwdqrlcavp
      301 dgdlfkairr gqasvvtdri arftatgvll esgkhldadi vvtatglnvq afggvpvtvd
      361 drpvalpdtv sykgmmlsgv pnfayaigyt nsswtlkigl lcehfcrllk hmeaqgydic
      421 rpevadpdmp trpfldfgag yiqrvvdqlp rqgsrmpwlt smdyqsdvkl lraddvtdre
      481 lhfervsvlt qgdsl
//
LOCUS       WP_284921077             380 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Actinoplanes oblitus].
ACCESSION   WP_284921077
VERSION     WP_284921077.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..380
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=40213
     Region          1..370
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mstptisivg aglgglilar vlhvngiaat iyeldaspaa rtqggmldih dyngqvalre
       61 aglfeqfqai ihpggqatri ldkhntvlad etdedsdgnr pevdrgqlrq illdslpagt
      121 iewgrkvtaa ralgdgrhel tfdggetvtt dlligadgaw srirpllsga tpaytgisfi
      181 eadhldaarr hpvpasivga gmlfalapgr gflahretdg slhvyialkt sqewldgidw
      241 adtdkgkavl laefadwape iktliteadg aliprsinal pvghrwdrip gvtllgdaah
      301 vmspfagega nlamfdgael gkaivahpgd ieaaltayek elfvrsaeva kesadnlevi
      361 fndqapqsll dmfasfggpe
//
LOCUS       WP_284921095             505 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Actinoplanes
            oblitus].
ACCESSION   WP_284921095
VERSION     WP_284921095.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..505
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=54998
     Region          51..391
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mpeidlgayr adqgfylvgs rtgarfeqgp aepggyahrf syrgsattia daavdlvrga
       61 rgkiflasyr igdgplleal yeavdrlrgg vyvitswdek alrkdlpdla peetahevka
      121 qlkrfdemtr rgitvrghps chakflvvdd raalvssanl etsalrgtad ravtgesgtl
      181 ltdageaqll grfftrmwfa gctgearpgd kyalkdrgve pspcdvpvpp vgpragviwt
      241 hedehgilet indivdrsrd elllasyslv glaeqprrll daiaracarg vrvsllvrgr
      301 nlprdlrdar mltelgvrlf pdslthakga ladgrtgalf sanfdfdhgl ingvemgvrl
      361 dgtpaladah rylrhamrna dmeyaarpsq relaagypar wrkawplpaa vpittdpstw
      421 arfaaaaahp pvlfeaqgde valvtardrw lleragnrwr lagqqsaddp lsllgrwsra
      481 ggrrtgteer pttrgfadat fslgd
//
LOCUS       WP_284921202             145 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Actinoplanes
            oblitus].
ACCESSION   WP_284921202
VERSION     WP_284921202.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..145
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16152
     Region          32..128
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msshdhsqae samahqtvsr wdaelvpdda grtdrpdtec pveialaaig grwttlvlre
       61 lmhrplsfse lsetlpqlsd kvlderlrrl rtqnlverra vtgfpsrvty sltpagqqlr
      121 pllvelyrtg lhlrqslrpa pappa
//
LOCUS       WP_284921219             378 aa            linear   BCT 25-DEC-2024
DEFINITION  RCC1 domain-containing protein [Actinoplanes oblitus].
ACCESSION   WP_284921219
VERSION     WP_284921219.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Hadjebi,O., Casas-Terradellas,E., Garcia-Gonzalo,F.R. and Rosa,J.L.
  TITLE     The RCC1 superfamily: from genes, to function, to disease
  JOURNAL   Biochim Biophys Acta 1783 (8), 1467-1479 (2008)
   PUBMED   18442486
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Renault,L., Nassar,N., Vetter,I., Becker,J., Klebe,C., Roth,M. and
            Wittinghofer,A.
  TITLE     The 1.7 A crystal structure of the regulator of chromosome
            condensation (RCC1) reveals a seven-bladed propeller
  JOURNAL   Nature 392 (6671), 97-101 (1998)
   PUBMED   9510255
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..378
                     /product="RCC1 domain-containing protein"
                     /GO_function="GO:0003682 - chromatin binding [Evidence
                     IEA]"
                     /GO_function="GO:0005085 - guanyl-nucleotide exchange
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=39017
     Region          34..373
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
ORIGIN      
        1 mrtfmarllt taaltvlalg gtagpataap psattvaagy shtcairada slwcwgdntk
       61 gqlgdgttvk ktspvrvgta ttwasidagt sytcgtqadg slwcwgantr gqlgdgsttn
      121 rntptrvgtl tgwasvsagd shtcatrtdg tlwcwgfnrl sqlgvtssvy yataplqvgt
      181 atnwagvstg fghtcgtrtd gtlwcwgdng dgqlglgrlt aattpaqvgt gttwasvsag
      241 yafacatrtd atlwcwgdng ygqlgtgtty qtapvqvagt twsrvdagfn svcadrtdgt
      301 lwcwgnnmag qvgddtttnr tapvrvgtat twtpqhvtgy htcgfradas lwcwgnnans
      361 qlgdgtttah ltpaqvtf
//
LOCUS       WP_284921407             240 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Actinoplanes oblitus].
ACCESSION   WP_284921407
VERSION     WP_284921407.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 240)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..240
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=24616
     Region          1..210
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtqtiaiiga gpglglaiar tfgrqgfqvg lvardaakla glvgllqadg vtaaafpadi
       61 rdrdaltral sevcerlgpi dvleyspgpq gapissavqm tvdsataqfe lnvlgaitav
      121 eavlpgmlqr gtggllfttg vssvipvafl sntgiamagl rnwalalheq ladkgiyvgt
      181 vtiatqlaeg agegdpaava drywtmyqkr dhveetvgdi eafrstvaai tarrqaaagq
//
LOCUS       WP_284921430             134 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Actinoplanes oblitus].
ACCESSION   WP_284921430
VERSION     WP_284921430.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..134
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14815
     Region          <66..124
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(68..69,90,96,100..101)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mtvfvadsvg lahqerytqa advlswaprm ggdepamdls ssedrdpdsg lsfgrrlrra
       61 rmqrrwtqlq larrmgevaa khggtagsrs liemiskwen girkpsqynm hllaaaldvd
      121 vaslglpvdp dffw
//
LOCUS       WP_284921497             778 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Actinoplanes oblitus].
ACCESSION   WP_284921497
VERSION     WP_284921497.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 778)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..778
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=88296
     Region          <461..650
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mtqgelitpr dhplgrldrs didkvldalp qlptwpavga drnrcrrgtg qilewlatyp
       61 gdgwqarwla adihdrswrd mvmaatypap edqllqgmra llllrvlrps ywflhrykay
      121 alfdevrltv spdlftraas eatrlgmigr qanqplitla klvlhsgkdv gelgpedffl
      181 arawsvraig rhlpglhaaw evlrglgilp gdhtfraair vgqrptaemi dvfnlrsqtv
      241 rdvlirycee rrpamdygsf rglighlvgn fwadlekhhp eidslhlhpd valawkeraq
      301 fvtdprypgr prrdrialfm rvrafyldlq ewaledpswa pfaapspirk sdtegyakvk
      361 ksataemhqr irdrlphlpl lvqaaernra yhqallssve atlvgdtfdy ngtvfrrtap
      421 qtathrshrq rgpehvhatn lasdeqinvt vaensafwrw alletlrhtg vrleellemt
      481 hlalisyklr dtgevvpllq ivpsksnser lllvtpelas vlatiikrir dpqtgrvplv
      541 arydphertt gpmlphlfqh vlgwrrevis qrlvqrnlnd ilrlagltda agealrytph
      601 dfrrmfvtea vagglpvhia arllghanln ttqaylavfq ddlirsyraf vaerralrpa
      661 geyrdptdae weefqqhfql rklelgtcgr pygtpcnheh acircpmlrv dpdqrhrlve
      721 iatnleerit eahengwlge vqglrvslda arsklgaldr qpstgpvdlg lpvvrdpg
//
LOCUS       WP_284921550             320 aa            linear   BCT 25-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Actinoplanes oblitus].
ACCESSION   WP_284921550
VERSION     WP_284921550.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..320
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=33973
     Region          105..316
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mfspeppdhh dprhapvapr haaglttnhp agpaafpagg sggtlpgpaa hglaggasqp
       61 vvadapgwpp aaptgrydti atrppstyrf gdepartrrq wprfadelfr lahdgaklfv
      121 drdlaavgla cavlaelvat dhlavgqdrl vvigrqpppd alahtiaeqv agepeslpve
      181 dwlrylsgdi ydqvakrmvm agdlvevtra rlfgrsrtvy qpadnnaayw scarlataar
      241 rgqslleqgh vnpftsvfdd fdrvlvglcl stgvyqrvfa gtpqhvitql advgqrsrap
      301 ipellgaldr lvggavlira
//
LOCUS       WP_284921675             998 aa            linear   BCT 25-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Actinoplanes oblitus].
ACCESSION   WP_284921675
VERSION     WP_284921675.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   3  (residues 1 to 998)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 998)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..998
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=109021
     Region          6..235
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          142..993
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          742..774
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          782..810
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          828..857
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          862..890
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(863,866..867,870..871,873,897,906..907,910..911,
                     913..914,943,946..947,950..951,954)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          895..931
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          942..970
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdgptgtvri ppgrqeiila cllmeagrvi gtsrlldliw pdeapdtart qiqicvsrlr
       61 ksfaeagltv svvsrapgyl lrtgdetvdl qvfnrqvmas rvlvkegrda eaaemlraav
      121 alwrgpclsg ipnetmrswg vrldedrlaa ietylglelg lgrshdlvge isrqvhenpl
      181 rerlrgqlml alhrsgrqae aldvyragrq lladelglep geelrqlera ilagdpalla
      241 ptarptvtev aarsgdpqpp pdrnraaapq pvepatpgyg eerprqlpad tadfvanepv
      301 lrtveaallg ddgqralglv viagkpgvgk salathvahr igrtrfpdgq lycdlrgvga
      361 dpvspqdalg rflralgipg pmipddider aemyrtllas rqllvvldda aneaqispll
      421 pgssscavvv tsrsrlaglp gamrielevl drtqalells rvigearvar epaaadalvr
      481 tvgglplalr ivaarlaarp hwtlasmghr laserhrlde lahgemtmra slslthdgls
      541 naeqrllrlf sladgptvpg wtagallddd spfpsdlvep lvdvqmldav avertgefry
      601 rfhevirlfa reqlalhdsp avqlaaterm iggwvalaeq aharvyggdf tvlhgsgrrw
      661 qppaayaesv lsepidwlds eqpnlclavd qaaraglhel cwdlattlvt lfeargyfdq
      721 weythrrale atraaqnrrg taavlgslgt mhlsrqqpde arrslglalk ifeelddrhg
      781 lalcrrdlal lerqvgaedv alalyeqair dfeavgdvvg ragvltqssy iwmrrgstal
      841 ahdqleeala vfrevgythg eahalrragq vllrrgehae aervllrvld nvrrnrdlig
      901 eghllrnlge vheagkrydq aqeayrqala vrekiidvgg vavvrldlar vllrsgraae
      961 agalldqare sfrdrgmrpe qeqadllare lagpsvrp
//
LOCUS       WP_284921815             483 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Actinoplanes
            oblitus].
ACCESSION   WP_284921815
VERSION     WP_284921815.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..483
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51096
     Region          29..413
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mavtpdlttq eqaatparsp rqpsafggll lrlhfyagil vapfllvaat tgilfaftpq
       61 iekavystel tvdtpgspal pmadqvaaar aahpagdlvt vrpgegsatt qvdfsdpsld
      121 adhqhtvyvn pytgkvtgql ttwwaatpln ewldnlhanl hlgetgalys elaaswlwvl
      181 alggvilwwr rqrdrnrrmf vpdlaakkgv rrtrgwhaat glwitigllf lsatgltwsg
      241 hagenfndli dsldasrpav stdlvgaaap atagghhggt ttggsstaav dpaaittvlr
      301 sardagitga vsitvpadaa tawsvtgnds lwpvgrdsva vdstgtivqr idfadwplla
      361 kltqwgiyah mgqlfglpnq ivlaalalgl icviiwgyrm wwqrrptrag rralvgvapa
      421 ggnwtglpns aiavglpvlf avgwflplfg vpllaflald lvltglrgrr rpnipvspap
      481 arq
//
LOCUS       WP_284921852             419 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Actinoplanes oblitus].
ACCESSION   WP_284921852
VERSION     WP_284921852.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..419
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43478
     Region          1..71
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          <45..419
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 msedvgrrih rlrtareltq relaapryta ayvssveagr rvpstdalah faerlgvsae
       61 elatgsspdr rvrlglelal aeaapaeavf rrlvnetaaa gdelrqarch lglghlalgr
      121 adlaaagraf aeagrlsaga pahlraapva gqaeclrrqg dpryavfllt raldelagag
      181 lpdpeallgl htrlalchrd lddedaaana asaalalvgp gdpgsvadlh lavartlleh
      241 gdtraaegal lqaglarrqa alavelahcr lirgrarhaa gdrdgavrdl taahagfaaa
      301 gltgpladat valaavlrgl grrtearnli vdrpaagpaa drllaalaad dgdvraaerh
      361 lrdaadgyrr sgprrslaav lldladnlea qhrpaeaval lrdgladver lsgdsprsg
//
LOCUS       WP_284921857             211 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Actinoplanes oblitus].
ACCESSION   WP_284921857
VERSION     WP_284921857.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 211)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..211
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22998
     Region          6..95
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mpdddlpeti hvstaeqlra vsnltrhrim avlrfepati tqiadrvgla kgsssyhvrl
       61 leraglvtvv rtrkvrgvve ryyamaarsi tlpdpgpgqp evlmrhavad leaaprdder
      121 hvrmahlrlt deqftelgak lqaladeyra lsdpalpdvs lvfalfrpak ageaeqaeqg
      181 eqaeqgeqae qgeqgeqaeq geqaeqtggd a
//
LOCUS       WP_284921859             320 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Actinoplanes oblitus].
ACCESSION   WP_284921859
VERSION     WP_284921859.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..320
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34330
     Region          1..313
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msrptarvla lleifqsgga fnvgdlarrl dvdertvrry ashlldlgip vearrgrygg
       61 yrlapgyklp plmltdeeav aialglaagr ragmvtadha atesataklr rvlpaalarr
      121 idallitmdv tgpvrqpapp gtevllvlae aarhrhpvql tyttwhgrss ergldpygvv
      181 fhngrwyvtg rdhasgsart frldrisair atdgafevpa gfdptghvla glasvpyahd
      241 vsvllhtsla qarrrippsv gtltevangv rlttraehld gaaqmlaglg wsftierpae
      301 lraevralaa rlltyadaaa
//
LOCUS       WP_284921891              67 aa            linear   BCT 25-DEC-2024
DEFINITION  tautomerase family protein [Actinoplanes oblitus].
ACCESSION   WP_284921891
VERSION     WP_284921891.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..67
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=7425
     Region          2..59
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mpyinvkitr egvtreqkrr iigemtqvlv dvlgkdprtt fvvideveld dwgiggvpvp
       61 efrksga
//
LOCUS       WP_284921973             196 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II [Actinoplanes oblitus].
ACCESSION   WP_284921973
VERSION     WP_284921973.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..196
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21066
     Region          5..187
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 mrsrllvidn ydsftynlvq mfqnypleis vvradqlavd dvarerpdyv lvspgpkspg
       61 aagistelvr ryhgafpilg vclgmqcvne afggstvhap vpmhgktsav hhdgtglfag
      121 vpepvtvary hslavtglsa dlrvnarsad gvpmgiehvr dplfgvqfhp esfltqhgft
      181 mienflrtgp lkgala
//
LOCUS       WP_284921976             364 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Actinoplanes oblitus].
ACCESSION   WP_284921976
VERSION     WP_284921976.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..364
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=38534
     Region          14..361
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mriaiagggl ggltlarilh rhgieavvye repsraargq gglldlhpes gqralaeagl
       61 terfrsavrp egeehrilap dgrvlvhhrp ppgsfdgrpe idrgvlrdll ldalpedavr
      121 wrhrlvgaap rpaggfalsf adgrdagcdv ligadgarsa vrslltdapv savgtlvelt
      181 iadadrrhpd ladlvgpgsl wcvgecrila aqrqgddtir vgitlpaveh dldtyrskda
      241 vlkvfdgwsp rltalieagd rppiprrieq lpigtrwahh pgltligdaa hlmppvgega
      301 nqamldaavl gaalaadpgs alqayekemf arihpiaems arvqammlap taaddlvrff
      361 ggga
//
LOCUS       WP_284921994             454 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Actinoplanes oblitus].
ACCESSION   WP_284921994
VERSION     WP_284921994.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..454
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47586
     Region          87..431
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mtvweivvvl gsvalvlsrw lpavarrpta ltaagvvvlg taltlpdprw qllpvlaadl
       61 lvgvawllrr rrgragwrla lpgsvaclal vasgtgaawa lpvpefpqps gpsavgttvm
      121 qwtepdrrtv vvqlwypaqs pgpdapraqy lgrtrheaei vagaeagylg apaflldgpt
      181 rahshaapda apaagrfpvv lfspglggtr tqntawaedl asrgylvagv dhpydsaavv
      241 ladgrvlrtr iastgnraed drrragwvav raadlsfvlt qlgrldrgel pgpftgrfdt
      301 araaatghsv ggaaamraae rdprftavin ldggpdpdqg plrqpvlalt hpiedradtd
      361 ylalltaild rgtatsyrlt vpgsahltft daplflpplp altgslgrtg svrmttetta
      421 afldatlrgr pgdlpaalsr hgdlrvhppa aavk
//
LOCUS       WP_284922095             891 aa            linear   BCT 25-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Actinoplanes oblitus].
ACCESSION   WP_284922095
VERSION     WP_284922095.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 891)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 891)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 891)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 891)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..891
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..891
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=93440
     Region          1..875
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mttapaevde rqpptelfrh lrsgptglrs reaarrltvy gpnelsrrqt rhwprqllaq
       61 ftqplavllm vaavlawfgh tvalaaavva villnagfaf vqeqqaerav ealaaflpms
      121 arvlrdgelv eaparelvpg dvievtegdr vcadarlieg avavdlsaln gesapavrta
      181 dgdlvpgpll earelvfsgt sctagqarav vthtgmhtei griaalsqrg rveasplerq
      241 vrratwiiaa aavaagvafl pigvlaglgw aaaisfaigl ivanvpegll ptitlalaag
      301 vrelaragav vkrlsavetl gsttvictdk tgtltenrmr vtqlwlpgge qdaaaralal
      361 aaatcttaha adrgdptela llrlaaergv pvdaaardaa rtalyafdpr tkrmstvtgd
      421 rlytkgapes vlplctrvld aggiaeltea vraeatatvd ryaraglrvl avaqrvasag
      481 llaagrenae agltllglva mvdppraavp aavadahrag irvhvitgdy gptaatiaae
      541 vgigdghqrv vtgaeldamg dadldrllgd gqeivfarss pegklricea lrseghivam
      601 tgdgvndapa lrradigvam grsgtdvare aatmvltddn fativraiea grrvfdnvrk
      661 fvlyifahav pevvpflifa lsggavplpl tvlqilaidl gtetlpalal greraepglm
      721 arpprspkag vidrrllwra wgllgvtsai lvtagffwsl wragwqpgaa lsgadydrat
      781 tmtfagivac qigtafaart dyaslrsigv fsnrlllggi afelvfaavl iylpplqavf
      841 gtaalggael aflapfpllv wgvdelyraw lrrrgsrtah qeapscesst s
//
LOCUS       WP_284922117             534 aa            linear   BCT 25-DEC-2024
DEFINITION  B12-binding domain-containing radical SAM protein [Actinoplanes
            oblitus].
ACCESSION   WP_284922117
VERSION     WP_284922117.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Banerjee,R. and Ragsdale,S.W.
  TITLE     The many faces of vitamin B12: catalysis by cobalamin-dependent
            enzymes
  JOURNAL   Annu Rev Biochem 72, 209-247 (2003)
   PUBMED   14527323
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Ludwig,M.L. and Matthews,R.G.
  TITLE     Structure-based perspectives on B12-dependent enzymes
  JOURNAL   Annu Rev Biochem 66, 269-313 (1997)
   PUBMED   9242908
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..534
                     /product="B12-binding domain-containing radical SAM
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0031419 - cobalamin binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=59641
     Region          57..422
                     /region_name="YgiQ"
                     /note="Radical SAM superfamily enzyme YgiQ, UPF0313 family
                     [General function prediction only]; COG1032"
                     /db_xref="CDD:440655"
     Region          447..>482
                     /region_name="TFCD_C"
                     /note="Tubulin folding cofactor D C terminal; cl19887"
                     /db_xref="CDD:473247"
ORIGIN      
        1 mrvllmsglg panlnsgyls gsllerdrsp ratqvlqrad rpdldvsqla fekggrryal
       61 lrprpdsvph ltsvtltsil assghdfvrv pleevwtsqa rppsgdidvv llsstfiwnd
      121 givaaalnwi gthvpdtpvi mggqytnlkf mpvmrdhpev lavvrgdaee slprvldalq
      181 agasldgipn vvwrdgpriq inpiayvdme rfpsptvagp apivpyesmr gcpfdckfcs
      241 fpaaspkwry ksaekivhdw tayatenhak misamdstft vpptrmrrll ellpgagtpp
      301 wegfsranti nspelvenla rsrcqqlhig fesmndetlk rmskrvsvrq nrragellsr
      361 sdigyyvffi vgypgetpea fadtsaflvd eyvghfalsk fsitdetmpl wqdrdelriv
      421 sddptdptaa wshigmdsae asrlqketld rvrhgsetav lhlwqhafqh wlmphrdrlt
      481 niraekcver mamapvdypd vaqaakvvnd eldklrdlgi ervedsrtlc rdai
//
LOCUS       WP_284922151             673 aa            linear   BCT 25-DEC-2024
DEFINITION  NACHT domain-containing protein [Actinoplanes oblitus].
ACCESSION   WP_284922151
VERSION     WP_284922151.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..673
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=71127
     Region          156..>431
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mprwsrqprf wfgvslvvll llvcalawfl qhqgldradk wasvvfggag taavvvgals
       61 wlwrlggpra vpvgddttva ldwlagaqre qwqaeqaarr vrdpwplnvr wlssaraqav
      121 maswasvrgr pgaapaelag eyagiadlft vpggprrlvv lgepgagksm lvvhlalqll
      181 arrtahepvp vvlsaagwnp vlglddwvae qivmidrrla rqvpgpggap rslardlvar
      241 glilpvldgl demadslqqa airgiaqsag tghglvvtcr trpyeaavag sgpvpaaavv
      301 eiqpvaaraa arhladsaal tdrrwqpvvv hltevpdapl aralstplmi wlartvyqdp
      361 vrdpgellta gwattrggie qhllehlvga ayasalgryp artaedaarv rrwlgtvaah
      421 lreqrtyela wwhfnelrpv pdaqfvsvaf svivalftac aampagmaaf dhgrvspwlm
      481 swysgatigl vtayarllft drsvprqltl agavtmylvv gaplgvvatl agqpvvglgl
      541 mlsagtvsal vagssvaaaa trpsrslhvd rrtalvaglt aglatgflca valgdsspgi
      601 waaiaviaaa avvsfsawgq fclarlvsav aggmplrmmg aleeahargv lrraggvyqf
      661 rhnllqdhla thr
//
LOCUS       WP_284922309             384 aa            linear   BCT 25-DEC-2024
DEFINITION  LolA family protein [Actinoplanes oblitus].
ACCESSION   WP_284922309
VERSION     WP_284922309.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tajima,T., Yokota,N., Matsuyama,S. and Tokuda,H.
  TITLE     Genetic analyses of the in vivo function of LolA, a periplasmic
            chaperone involved in the outer membrane localization of
            Escherichia coli lipoproteins
  JOURNAL   FEBS Lett 439 (1-2), 51-54 (1998)
   PUBMED   9849875
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..384
                     /product="LolA family protein"
                     /calculated_mol_wt=38989
     Region          <102..268
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 msvwksrpal rwlvpgatal vvigggaaag tivasadpsl pdrsaaqllv dlqganpagl
       61 sgtvvqsadl glpgvaglag slgkstggng ltsliagsnt arvwyagqdk vrvalqgtqg
      121 etdvirngsd vwqwsssdnt grhltlpada gkpakhslps avpstpqeaa daalaaidpt
      181 tkvettgaaq vagrnayelv lspkdteslv gqvrlaidae qhiplrvevy aknavkpair
      241 vafdtisfav pdaeqftfnp ppgakidetg pkelgspgtv kkpvphpaap agsnqaepkv
      301 igkgwttivt asvpkdglae ltkagkgkge eaqqvqalls mlpevsgswg kgrllsgslf
      361 svlitddgqv laglvtpeal ykva
//
LOCUS       WP_284922325              92 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Actinoplanes oblitus].
ACCESSION   WP_284922325
VERSION     WP_284922325.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 92)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 92)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 92)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..92
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=10026
     Region          <5..68
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mldlllaegg gtattlssrl tvtrqavakh lgvldrvglv rstpagrerr yhvddrqlar
       61 avaqltavgs awdarlrrir rlaetiqktr np
//
LOCUS       WP_284922369              83 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Actinoplanes oblitus].
ACCESSION   WP_284922369
VERSION     WP_284922369.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 83)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 83)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..83
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=8768
     Region          1..73
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(2..3,5,8,11..12,15..16,19,49,68..69,71..73,75..77)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(3..4,8..10,23..25,34..37,39..40,43..44,46..47,
                     53..55,60..62)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(23,26,68)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mlsmladptr lrllaallpg erdvsaltaa tgsarpavsq hlgklrlagl vrvrregrrq
       61 vyavsgphva rlvaevlraa arh
//
LOCUS       WP_284922454             298 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Actinoplanes
            oblitus].
ACCESSION   WP_284922454
VERSION     WP_284922454.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..298
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=32178
     Region          26..276
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 msrrltpper yqfaasvrsl lvpkhdpcgl lrdgelwlav rspagpatlh larvagelva
       61 tghgagadwv veradaiagl rddlrgftel arrhplvarl attfsgvrmp atgqvfhrll
      121 raileqkvtg teahrsyrki crhlgepapg pvalvlppdp aavaarpywe fhplgveqrr
      181 tqallraaqa aarlaecads aeatrrmtal pgigpwaaae vvrtafgdpd avsvgdfhip
      241 ntvayalage prgtddrmle llepfrghrg rvcdllamgg vtaprygprm pvrsfarf
//
LOCUS       WP_284922457             391 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Actinoplanes oblitus].
ACCESSION   WP_284922457
VERSION     WP_284922457.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes oblitus
  ORGANISM  Actinoplanes oblitus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Actinoplanes oblitus"
                     /db_xref="taxon:3040509"
     Protein         1..391
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41605
     Region          15..376
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrptlrlrlt llngillvaa gavlvvlawl lvdeslhpad ellagstvtl ndgrveearg
       61 wqaemvdqas dellvkglsa lvaigiigta ggylvtrral rplhtvtqta qrlgeetldq
      121 riryagadde vaelartfda mldrlagafe sqkrfvanas helrtplavm rteidvtlsd
      181 pdadvaeyrr marvvrdast ranglvdall vlarseaqsg rrlvrkvpad latsvynals
      241 avkteaermk levttdlgaa pvvgdpslld rlagnliena irynhllgrl wlrtasvdgq
      301 arlivgntgh eveqsevpgl fepfrrggwe rtgsrgsglg lsivravcda hggtvsaial
      361 adgglevtvs lpaadttpvv aatasvprig r
//
LOCUS       WP_284922630             291 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Clostridioides
            difficile].
ACCESSION   WP_284922630
VERSION     WP_284922630.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..291
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=34030
     Region          17..283
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mnvyekgngv ilegvtdfdp vhifecgqcf rwhkqedgsy tgvakgriln vkkendkiyl
       61 nntnlkefns iwynyfdlgt dyteiknklk nmdeylnkat efgwgirilr qdgwemlisf
      121 iissnnripm iqraienlsr kfgkyigeye gneyyafptp eelnkasqee iracqtgfrd
      181 kyiksttqav ienndevsey tnlstedcrk ellkfngvgp kvcdcialfg mqkydsfpvd
      241 vwvkrvmqef yidedmslpk mrtygidkfk emsgfaqqyl fyyarelcig k
//
LOCUS       WP_284922649             866 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-mannosidase [Clostridioides difficile].
ACCESSION   WP_284922649
VERSION     WP_284922649.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..866
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..866
                     /product="alpha-mannosidase"
                     /calculated_mol_wt=99745
     Region          1..866
                     /region_name="MngB"
                     /note="Alpha-mannosidase [Carbohydrate transport and
                     metabolism]; COG0383"
                     /db_xref="CDD:440152"
ORIGIN      
        1 mikahivnht hwdrewyfts gdalvlseql ftdvideler npdvsfvldg qlsilddyvq
       61 lhkekieiik klikedrlhi gpwftqtdaf fargesilrn lmigifeskk ygkymkigyl
      121 pdtfgfnaqm pillkhvgld niffwrgihl gkqvqspyfk wkslngesyi yavnmphgyg
      181 tgmllepslk yvngrldpai dfiksytdvd evlipsgndq lniigdfknk ikaindigky
      241 syitssyqef lkyiksiesl esyrgefrep vlarihksig ssrmdiklac dklenklikr
      301 iepllviakk skieisnqll intwkklleg qahdslagcv tdtvtedilh rireaneicd
      361 sientivkki seglklsknd ilvfnteakr fngykeiqvv sdskniyfkd nldatiieet
      421 yvkprenvle etpagnifie epgyyilkvr invqlpalgy kvvsfelsdk emvsldksnd
      481 tfisndnyki iyedgslnlq lkdgtyisnf ltlkdsgnag dtydfsplkn dediklsfdk
      541 vytekalgye kmvvkgttll pltledrknk ylngklnvkv sivlskenpl mdvkpcvdnt
      601 iynhrlrvhi ktdikdnkni aslpfgyitr kngvldnwey iysempidle plesnitltn
      661 qnrsctvftr gikeyqhied eialtllatt delgkpdlly rpgrasgdtt kkghiriktd
      721 kaqmlkelef sfaiymdsks fdeleianlt hnylrecvny qlqdynffly ridnkiqksi
      781 vnktvsrele iislpenyli sacypsyysk dkfiirvenp ssnrmildeq ifknrngkiv
      841 naiedveeeq vyeiapfdvi silldl
//
LOCUS       WP_284922719             522 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Acinetobacter baumannii].
ACCESSION   WP_284922719
VERSION     WP_284922719.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..522
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=59033
     Region          114..520
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mqfplnssls htifrlgtwy glyrliiavs lniilvltda qtdnslqqpa lysytllgys
       61 llsliqllcf kfiatqatrq lilffivdii clslltfsvg epnlqlslly viaiftsail
      121 lsarmsllit llaviaviyq rfvgslfdyn nlntignsal laflffvvhg igqiavqrfk
      181 llealtfhqs ielyqlqnin ryileqieeg ylvldenydi vvsnpaacsl lgippqfane
      241 kyplakwhad lfeilklgdl kegdrfifes rlsaysinik vqhllvpqqt ltllilqdaq
      301 qinqqaqqlk laalgqlsas iaheirnpla aivqanellk dsdpeqqntl rhmigkqtkr
      361 idsivqdtlg larserthpi qidvkhfivt lleedlfdvk hsiqlkisds slkflfdekq
      421 lrqvminlvr nalrhnapds pyitinihsq tnkiyidvid ygegvskrdi sqlfkpffst
      481 eingtglgly lshsfceanh akltyveqkq gacfriecpi iy
//
LOCUS       WP_284922721             617 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284922721
VERSION     WP_284922721.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 617)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 617)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..617
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <197..613
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 kfiptlqnki ycallifsfl fiisnilgsf clnnidkipi fitfllnqiy llllpipaal
       61 vsfyvmaiiy qdirymkkrl lflsipliic iilsitnpft hilfglsket gyirgcgyva
      121 tfasfffyai ysaflsfkyr kamheskiwa irgflivsiv aiilqaiflq ylltgtacac
      181 sllltylsmq nrgliiddlt gvlnrqsfiq eldlninteq sgfiitiald dfkfmnetfg
      241 tkngdialke vgkyliqihd vnhvyriggd ifsivvnsql giepddiirk ieerfkkpwl
      301 veeisfnlat siavvyypen aettedviva idfsiheakr sesrrvvyad asisekikkk
      361 hviknclkea lkndgfevyy qpifsnsrgr ftsaeallrl ehkelgfipp defipiaeqt
      421 glinsiglvv fekvcrfias defenlkldn iavnlsvvqc mqknladdll ylmnkynvsp
      481 tkfkleitet vamgsfniik etmerlidlg vkfalddfgi aysgvtnmls lpfsvikldk
      541 sliwsmneds rhkltvetii alinklnmka vaegvetikc aedliamece ylqgyyfskp
      601 vpedvfknll kentfts
//
LOCUS       WP_284922741             377 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284922741
VERSION     WP_284922741.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>377
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          101..361
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(203,206..207,210..211,213,246,249..250,253..254,
                     256..257,289,292..293,296..297,300)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          203..236
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          241..283
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          288..316
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          328..354
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mnfrlpkkrl pkkiificii lisiilfikh dqnglkerei inkgkymses lvadkeydea
       61 kkvvktsfes ipekkynkvy nevwdmlkti syvpdgtkiv idslekmres dvklsdecrf
      121 niekrlasvy imdnnyskav dltvksikla eklgnnyeka rldvdlasif lkiggyetge
      181 klikdsfkid idegekngmv rlyaiinlae iyveegeydk aieissrikd ykkfvntdny
      241 ndfdimasim qsnayvgknn iqkaktflek adyliksdrt vyildkdmyy ymamgnleyk
      301 senynsaidn ykksleistk rkltqekikn lnkilniyek qgnieslney qkmlineyke
      361 nksirdsets fyiidkv
//
LOCUS       WP_284922742             186 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase, partial [Acinetobacter baumannii].
ACCESSION   WP_284922742
VERSION     WP_284922742.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         <1..186
                     /product="DNA-methyltransferase"
     Region          <91..181
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 sksrryyfdh vaikepvaes sikrlsqnld dqqgsdrvvn khngpmkavy srssrdsfkr
       61 snskravahp nqsmgthrad rkesnydllt rnkrsvwqvs tkpykgahfa tfpmdliepc
      121 ilagsrvndv vfdpfmgsgt taavakklkr qylgcelnpk yehlqkerls qihtnmelqf
      181 eggchv
//
LOCUS       WP_284922876             672 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284922876
VERSION     WP_284922876.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 672)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>672
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          205..612
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mdkkklilit hdklnsdhyk eeltnffgde iiietqnild gikenlegdv vlslspltsn
       61 flikhfkedi eiihgtkals klgyekmmkl ppgtksllmt tnktsafema tylykiginh
      121 idfvptypdc deiydldtai tpgqirfipk yiknivdlgw rkisldtyms llvvlklkne
      181 kfieklykls ketlshdfln tsldnisklk tilymtidei gdgliffntf nkvtfvnksl
      241 lnmlgldekl ikspslmeym pnsfldkitk nlnidnmiiy ideidkkfil skkpfylykn
      301 iegclitlkd vnnieileqk irsdsvkrgy vakykfnnii gnssiikdci kkakkmaltd
      361 npilitgetg tgkeaftqsi hnhsnrknkp fvaincaslp selleselfg yedgsftgak
      421 kggkkglfel ahtgtiflde igdmphdlqv kllrvlqeke irkiggtsii pidvrilaat
      481 nkdlekliie nkfrmdlfyr ismftldlpp lrkrledipl llesflkelp yknikldksl
      541 lealnsytwm gnirelrnci eymaymgsny ltindlpqni ssklnnnhms snmsifndln
      601 qydknicisi lkslhmkpmg rtklmkfmey nvteyevrnm leyltrngyl isskgrkgss
      661 itekgikiie nn
//
LOCUS       WP_284922914             884 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Acinetobacter baumannii].
ACCESSION   WP_284922914
VERSION     WP_284922914.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 884)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 884)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..884
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..884
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=99051
     Region          10..884
                     /region_name="PRK10490"
                     /note="sensor protein KdpD; Provisional"
                     /db_xref="CDD:236701"
ORIGIN      
        1 mqsnrenqae allnhvnryq agrltvflga apgvgktyam larakelfqq gtdvvvgive
       61 thgrietlki leglpqiark emqyqghile emdldaillr hpqivlvdel ahrnvpnsrh
      121 errwqdvnel ldasidvfta iniqhlesln dvvyqitgir vnetvpdrvf drirdirlid
      181 lpvselierl hqgkvyvpeq anlalqgffs isnltalrel amqcvaehvd sdlkesyask
      241 glksislqne lmiaidgqgs seylvragcr laerygatwt vvnvaksldf gqssgnsykk
      301 eyieidrafe larqlggrte ilyghrvasv lmdaavdrgi snlvigksis pwwlklfkkn
      361 laqqllnqen sialtilhpe qgtkkinqle kpsflslkes vfvlavtcas ifiahfaevl
      421 fgiedfsvif iisvlivatk trmlaavvaa licflaynff fiaprytfqi sahqgvvtvv
      481 affaaaliag rlasqlrqqv lslkaanayt tvmqdlarkl ssavnleevm qtgrmtletq
      541 lqtkvwisir dkiissdiel ndkekvaaew clkhqqpcgr ftdtlsqsnw wflplleqkn
      601 slgivgiyfk devvslnfeq kkltesviey iaqaalrtql vneleqakvt seterlrsal
      661 lssvshdlrs plasiigaad tlanfkaemt eqdqqdllet ihlegerldr yiqnlldmtr
      721 lghegltlkr dwigvdelig satrrlkryk pdtqvvvqlp eqsislyvhp alveqaifnv
      781 lenaanfspp desvmiraql ssedevkiei edkgagiped erhrifdmfy tiergdrgkf
      841 gtglgltivk aiigahmgti eafsgrqnkg tliqiklpih pvke
//
LOCUS       WP_284923305             157 aa            linear   BCT 25-DEC-2024
DEFINITION  ferritin-like domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284923305
VERSION     WP_284923305.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..157
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          32..155
                     /region_name="Rubrerythrin_like"
                     /note="rubrerythrin-like, diiron-binding domain; cd01046"
                     /db_xref="CDD:153105"
     Site            order(44,77,80,107,140,143)
                     /site_type="other"
                     /note="diiron binding motif [ion binding]"
                     /db_xref="CDD:153105"
ORIGIN      
        1 ckvgadkfee mkgeknwade hrigvaqgvd eeiieglran fvgectevgm ylamsrqadr
       61 egypevgeay krialeeaeh aakfaellge vvvadtkenl rvrvdaeyga tdgklklakk
      121 akelgldaih dtvhemckde arhgkaflgl lnryfgk
//
LOCUS       WP_284923391             358 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Clostridioides
            difficile].
ACCESSION   WP_284923391
VERSION     WP_284923391.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..358
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
     Region          47..356
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 fiyswklvpt dktpagkrdd islrekeaqi kkdlndgidt aggkmtvcql yekknsqrkn
       61 ikratekgrq ylmnalkndp lgmraidtvk qsdakewair msekgyaykt idnykrslka
      121 sfymaiqddc irknpfefkl sdvleddteq kviltpeqee rllafmekdk iyskyydevv
      181 llletglris efcgltthid mqnrilnidh qllkdseigy yietpktkng krelpltera
      241 yqaiqrilkn rgkaqplivg gysnflflnr eglpkvagny egmvrglikk ynkyhkdklp
      301 nitphsfrht yctnmanrgm npntlqylmg hanitmtlgy yahgtfqsak aelerlac
//
LOCUS       WP_284923656             655 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidase U32 family protein [Citrobacter freundii].
ACCESSION   WP_284923656
VERSION     WP_284923656.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..655
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=73170
     Region          6..307
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
     Region          444..505
                     /region_name="DUF3656"
                     /note="Collagenase; pfam12392"
                     /db_xref="CDD:463557"
ORIGIN      
        1 mrqqphhlel lspardtaia reailhgada vyiggpgfga rhnasnslkd iaelvpfahr
       61 ygakifvtln tilhddelep aqrlitdlyq tgvdalivqd mgileldipp ielhastqcd
      121 irsvekakfl advgftqivl arelsleqin aihqatdati effihgalcv aysgqcyish
      181 aqtgrsanrg dcsqacrlpy tlkddqgrvv syekhllsmk dndqtanlga lidagvrsfk
      241 iegrykdmsy vknitahyrq mldaiieerg dlarssagrt ehfftpstek tfhrgstdyf
      301 vnarkgdiga fdspkfiglp vgevlkvakd hldvevtepl angdglnvli krevvgfran
      361 tvektgnnry rvwpnempad lhkvrphhpl nrnldhnwqq altktsserr vaidielggw
      421 qeqliltlts eegvsithtl dgqfeeanna ekalsnlqdg laklgqtmyy arniqvnlpg
      481 alfvpngqln qlrreavdml daarlqsykr gsrkpvsqpa pvypqthlsf lanvynqkar
      541 efyhrygvql idaayeahee kgevpvmitk hclrfafnlc pkqakgniks wkatpmqlvn
      601 gdeiltlkfd crpcemhvig kmkhhilkmp lpgsvvasvs peelmktlpk rkvnr
//
LOCUS       WP_284923753             714 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Citrobacter
            freundii].
ACCESSION   WP_284923753
VERSION     WP_284923753.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 714)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 714)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 714)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..714
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78921
     Region          10..675
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mlprnnqrpf ilsaltlcms gaafaatspt hastsdedtv ivtanrtess lwdspatiqv
       61 idrqtlqnst svsiaddlqd ipgvevtdna lagrkqirir geassrvlil idgqvvsyqr
      121 agqnygagll idesalerie vvkgpysvly gsqaiggvvn fitkkggdkp lggsvkavyn
      181 satagweesa aawgsignfd yringsysdq gdrdtpdgrl pntnfrnngq gvwlgynfdr
      241 hkiglsldry klstqtwfdd pegqfddfsv kipklereki glfydyaadg dylknihvda
      301 ysqtierkfe nrvkttqvip spmikaltvs nqtntndkqy tqgvtlqsnf slpannelvi
      361 gtqyqhdkik qdtdgstrqt aatgyfdtqt rtlsyneaeq sntslfaqnd wrfaddwtwt
      421 vgarqywlss klkrndtqtl qssgstwqst ggnsvhddel vtstslrysg fkdlelraay
      481 aqgyvfptlt qlfmqtsagg svtygnpnlk aehsnnyelg arykgnmwli dgaiyyseak
      541 dyiaslacsg qpvcsgntts srggyyyydn idraktwgme ltaeyngwav spylsgnlir
      601 rqyegntlkt wdtgeptltg rvglkhtwlm naanltsdvf iraassakdn tgtteinypg
      661 watlnlafnt efgpqdqyqv nlalnnltdk ryrtahesip dagfnaavgf awnf
//
LOCUS       WP_284923816            1644 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Citrobacter freundii].
ACCESSION   WP_284923816
VERSION     WP_284923816.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 1644)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1644)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1644)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1644)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1644
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..1644
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=180368
     Region          53..1643
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mkhlrvaacm lmlalvgcdn nneksptaak pdapapqtap akdkaqlqkl mqqsqgkslt
       61 lldasevqld gaatlvltfs ipldpdqdfs rvvhvvdkks gkvdgawela pnlkelrlrh
      121 lepnrelvvt ierdllalnk atfaidyekn ittrdvqpsl gfasrgsllp gkvieglpvm
      181 alnvnsvdvn ffrvkpeslg afvsqweyrn sltnwesdnl lkmaelvytg rfdlnparnt
      241 reklllplsd ikplqqagvy iavmnqagqy nysnaatlft lsdigvsahr yhnqldvftq
      301 slengaaqqg ievtllnekg qtlaqatsda qghvkletdk daalllarkd gqttlldlkl
      361 paldlaefdi agapgyskqf fmfgprdlyr pgetvilngl lrdsdgktlp dqpvklevvk
      421 pdgqvlrsvv sqtenglyrf swpldtnapt gmwhirantg dnqsrmwdfh vedfmperma
      481 lnlsankipv aptdevkfsv vgyylygapa sgnalqgqly lrplrdavqa lpgfqfgnia
      541 eenlsrslde vqltlddhgr gevttnsqwq ethsplqvvl qasllesggr pvtrrveqai
      601 wpadtlpgir pqfaakavyd yrtdttvnqp ivdensnaaf divyadaqge kkavsglqvr
      661 lirerrdyyw nwsegegwqs qfdqkdlveg eqtldlkade tgkvsfpvew gayrlevkap
      721 ndavssvrfw agyswqdnsd gsgavrpdrv tlkldkpsyr pgdtmklhva apaagkgyam
      781 vessegplww qeidvpadgl disipidktw nrhdlylsal vvrpgdksrs atpkravgll
      841 hlplgdenrr lalalenpak irpnqpltvk ikasvkngdv pkqvnvlvsa vdsgvlnitd
      901 yatpdpwqaf fgqkrygadi ydiygqvieg qgrlaalrfg gdgdelkrgg kppvnhvniv
      961 aqqalpvtln dqgegtvtlp igdfngelrv maqawttedf gsseskviva apviaelnmp
     1021 rflaggdtsr ltldvtnltd kpqtlnikla angllelmgq dpapvnlapg vrttlfipvr
     1081 aregfgdgei qaeisgltlp getlpvqhkq wkigvrpafp aqtvnngval qpgatwqlpg
     1141 deltnfspvt mqgqllfsgk pplnlaryir elkaypygcl eqtasglfps lytnatqlka
     1201 lgivgdsdek rraavdigis rlvqmqrdng gfalwdkngs eeywltayvm dflvraneqg
     1261 ysvpvevinr gnerllrylq dpgmmsiryt ddssasrfav qayaalvlah qqkaplgalr
     1321 eiwerraqaa sglpllqlgi alknmgdanr seqaltlaln tprrdtqqwm adygsalrdn
     1381 almlalleen kikpdvqntq lntlseqafg qrwlstqenn alflaartlq dlpgtwqaqt
     1441 slseqplagd ksltrnldad alstlsvtnt gnlplwlrld vsgypqtapt pasnvlrier
     1501 qilgidgnsk sldslrsgel vlvwlevkas qnvpdalvvd llpaglelen qnlangsasl
     1561 qdsgsevanl lnqmqqadiq hvefrddrfv aavavnegqp vtlvylarav tpgtyrvpvp
     1621 qvesmyipqw ratgategll ivrp
//
LOCUS       WP_284923895             239 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Citrobacter freundii].
ACCESSION   WP_284923895
VERSION     WP_284923895.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 239)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..239
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27074
     Region          52..226
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mtteadylnq ydasrfpspl vtvdsalftl hqqalcvllv erakqpqkgr wglpggfidi
       61 enddstrsta lrkltektgv spswleqmdt fsgpdrdprg wsltvtwfal iawvdcaphi
      121 asvsnarwvp vdelknysla fdhekiitaa lhrlrqktmy sllpvyclpe tfthgqllea
      181 tevilgqsiq rkslirrfea sgmfedtges vatgtrkarl wrrkpnvdfh ffsrnlltd
//
LOCUS       WP_284923971             467 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284923971
VERSION     WP_284923971.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..467
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          2..464
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 kileashdei cvsddkgiii ycnkafeeny glkkedilgk nvsfledsgy stkspipivl
       61 ktktkfsleq dtqtgkklii tatpifdeng nleftvencr ditelnnikn kledtkkqvk
      121 kyksevetly rtalriedtv imdgivmrpi intvnhvskt dvsvlllges gtgksslary
      181 ihhnsnrsng pfitincati spqlleself gytsgaftga stkgkvglve langgtlfld
      241 eigdipqnlq akflqliqdr tftpvgslkn kkvdiriisa tnvdlvskvk ekkfredlyy
      301 rlnvieiklp plrerrdnlv eiikyyfnry ssdfnlnkti skeamdaian yrfpgnirel
      361 qniiqkillt ctdnhitidd lpniltknih itnngnkthi sqinkviisd skstnyknkn
      421 fdtlikeyek niildayekf gssykvakhl eisqskanrl irkytnt
//
LOCUS       WP_284924049             344 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284924049
VERSION     WP_284924049.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>344
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          <23..344
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mdkhsdsvmy ggmevyniwg tttvdsiige sdvmralknr ickignsdst vaitgesgtg
       61 keliaraihl agnrgnktfv aincaaipep lleselfgyt kgafsgadsk gkigkfelan
      121 ggvvfldeig dmpiqlqskl lrvlqekkft rigsnelidi dvriisatnr dlfelvkenk
      181 fredlyyrln viplevpplr ergddiqili nnfidkysrk mkknvyhiep dveqmllkyp
      241 wpgnirelen tielalnlle edgiihkgii nrkileyfkl nninikllee sdyeismeqd
      301 iltleefera yikkvlkfyg ndtkskklaa kklgislatl yrki
//
LOCUS       WP_284924020             402 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter freundii].
ACCESSION   WP_284924020
VERSION     WP_284924020.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..402
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=45550
     Region          5..396
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mplndtklrr iagkpydgpd eiadggglsa rispkglitf qyryrfngkp arlklgtygk
       61 msikeardam eeckgwleeg rdpamqrkkv rdivssspsi stlvdewlet psvkemvkye
      121 ywkrmlklhv tdnygrliad emspveweqi flritkggsp vqagnvlvkm kqviryalrr
      181 kritsnslml leindigsrp ddgerflndd eigafwnaid ktkmswqnkm lirlvaltgc
      241 rgvelrlark gdfdlkarew vipkensktr krfvrgisql aadylqkvfd vypdqsivfp
      301 paklqvdrpm sastlisiag qveevmggeh wslhdlrrtc ktkmaelgva phvsekilgh
      361 kltgmlavyd qydyipeqqa aaelwaekiq acaasnplsl qn
//
LOCUS       WP_284924163             193 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Citrobacter freundii].
ACCESSION   WP_284924163
VERSION     WP_284924163.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..193
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22018
     Region          23..133
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mtleyyqrha qdffsstvnv dmkslyqpfl qriteggril dagcgsgrds kaflekgyrv
       61 eafdassemv slarlhaglh vrqmtfndia diehydgiwc casllhvsae elpivmskla
      121 halkkggtwy vsfkygeter vkdgrhftdl teqrleklia pltditliss wttrdkrpdr
      181 demwlnallq krp
//
LOCUS       WP_284924136             227 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor, partial
            [Clostridioides difficile].
ACCESSION   WP_284924136
VERSION     WP_284924136.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 227)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 227)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>227
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
     Region          1..226
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 myrivicedd itqiaflrec ilkslegiss qielfefnsg eelletnleg idiffldikm
       61 lqltgmdvak iiretndtse iifitsivdy iqegykvray ryllkpidfg dlnesilsci
      121 sdiikkrenf mlienkdiin kilinsimyi evrkkvltih tkndtyytkn smdkielele
      181 kynffrchks ylinleyiqf ickntvvind edvpvskyrm adlkkkl
//
LOCUS       WP_284924189             440 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator, partial [Clostridioides
            difficile].
ACCESSION   WP_284924189
VERSION     WP_284924189.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..440
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
     Region          <1..435
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 lrevinyivv lvyrvkeekk vkdydvkfdl lksydeyfia reikhiisgm fectlndeei
       61 iyltiplvsg napasecaln ssrisknide lmenifnqiy vdmgifined elrvglgyhl
      121 sftlnrllfn iklknvllee ikqnyilpfk laqiagkvie kkynlevsed eigyiaihfs
      181 gylernssrf ysikkiaiic stglgtakll kirveklign npkidtlssf nlrninldey
      241 divfttidld tsnintivlk intifdenkl reqlktvlcl regnidttns tnllinnlld
      301 edkfmilnek tilaslekmm dhlmdlgcid dkfrknivnr eeksptvfdk gllfphsvne
      361 ksdkflmavg ileepieyan rsikiilmtm fpcenkidsd llvkiyeevl kigqdvkltn
      421 kiskcrtfle fkkvllknli
//
LOCUS       WP_284924198             104 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284924198
VERSION     WP_284924198.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..104
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
     Region          <6..92
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 kymdkitlke lasrvnlsah hfcrtfkqit gkttidfing irldkaiyyl ketdlnmtei
       61 amrcgfdsin yfsrlfkkny nisptkyrne hrevsnvilk edmk
//
LOCUS       WP_284924289             241 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Citrobacter freundii].
ACCESSION   WP_284924289
VERSION     WP_284924289.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14974002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..241
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26940
     Region          31..209
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          155..211
                     /region_name="LuxR_C_like"
                     /note="C-terminal DNA-binding domain of LuxR-like
                     proteins. This domain contains a helix-turn-helix motif
                     and binds DNA. Proteins belonging to this group are
                     response regulators; some act as transcriptional
                     activators, others as transcriptional repressors. Many...;
                     cd06170"
                     /db_xref="CDD:99777"
     Site            order(156..158,171..173,181..182,184..185,187..191,202)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:99777"
     Site            order(167,169,171,202..204,207,210..211)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:99777"
ORIGIN      
        1 mlqgrcknai iiskspiiqt glkgiiqaqf adyeltyccs aeeltllqlr yadlviadlt
       61 gdcnyprsvc eqyysllsqy rdihwvflvs rifyplaiel lmcpvsslls daepieslvs
      121 vihagnarae risktllspp ampqlldhsa rsivltlser kvlrllgkgw ginqiamllk
      181 ksnktisaqk nsamrrlsin snaemyawin ssqgsrelnl psvygettew kaessketlh
      241 w
//
LOCUS       WP_284924476             357 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Brevibacterium sp.
            UMB1308A].
ACCESSION   WP_284924476
VERSION     WP_284924476.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..357
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37233
     Region          46..352
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 milhsrtsae qgasvhahir stqrrlgvlg llatllivag fadawiggap mpaeaffhal
       61 ispatsekid tqivwdvrlp mtataitcga alamsgaqmq ttlgnplaep ytlgiasaas
      121 fgaslavvtg fgstalgsvl gvagsawvfa migygiilgi aklrgpsaes milvgiaivf
      181 ffdallalmq ymasvveleq vvfwtlgslt ratwpqialm gvmltiggff fvskawtlta
      241 frmgddrars mgipvertrs qallvaslla atavsmagti gfigligphi artlvgedqr
      301 fflpastmtg allltsasmv akiiqpgvil pvgiitavvg vpvfltlils rrrkvws
//
LOCUS       WP_284924509             302 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Brevibacterium
            sp. UMB1308A].
ACCESSION   WP_284924509
VERSION     WP_284924509.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..302
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34051
     Region          42..296
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mphrkaftrk nsakkssvrh rehfaknpvy ehgvqhvste ririalstss vypmdvptcf
       61 nmahelgydg veimithnrt tqnaqliqne irrsglpvvs fhaptllflp gvldkdhwrk
      121 lrktcdlale cgaesvvlhp pfrwqgdyat gfvdgvrelv ketglkiave nmypwraglr
      181 evlvyypdwn pldedydhmt fdfshastag mnaletvaei qdklaivhlt dgsgslrdeh
      241 lvpgrgkmpv aetlqylakh nwsgdvvvev ntrlvakkst rtamlkesld farkhlglne
      301 at
//
LOCUS       WP_284924517             259 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284924517
VERSION     WP_284924517.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..259
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27725
     Region          6..245
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(22..23,25..26,29..30,67,71..72,75..76,107,111,118,
                     121..122,127,143,147..148,150..152,154..155,158..159,
                     162..163,186..187,189..191,193..195,197..198,200..201,205,
                     208..209,214,216)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(146,150,153..154,156..157,200,203..204,206..211,
                     214..215,219,221)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(167..174,188,191..192,195)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mgfevrstpl trtnpltkia imllitvgvv lsidvvsasl mmvfvivffp ltgfpvkrlf
       61 thlwfiplaa fatgwatvll aegagpvlft fgpyevtars vevgfalflr slamslpcvv
      121 lafsidstel adslvqllkm perfvlgalg aarlagllse qletirfarr argvahegff
      181 gglldffpia fallteairr avrlamameg rafgtkgrtw trrvslgagd wvamgcagal
      241 aatcitasva tgnwnfils
//
LOCUS       WP_284924525             324 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284924525
VERSION     WP_284924525.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 324)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18950610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..324
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=36180
     Region          19..147
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
     Region          159..307
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 msptpvsnag esarlnadvl aagavlwrka ggrlevllvh rpkyddwawp kgkvekgetl
       61 pecaireiee etgyrvvlgl plpsarytvg kklskhveyw aarvateapp rpsnpkeidk
      121 avwlpiedar nkltrfsdre qldrleqahq tgslygfpvi ivrhgkafpr skwheteqvr
      181 pllglgtrqs laliglldaw epkrlvsspw krcvatlkpy sastgknikt ikwlseknna
      241 nkpektvqal ekliakeqav avcthrpvlp tvfrtlasfa ptglaeklps edpymnpgei
      301 liayfrpgpv priveveryr pidt
//
LOCUS       WP_284924540             372 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284924540
VERSION     WP_284924540.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..372
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40030
     Region          35..221
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mtqaskkkpl yrrlssalgv rvrlggrrai enssqilqvv igatsgyafc hyvlghpapf
       61 laavaavigt gvtadkrlrr sieiglgatl gvlvgeilvh vfgigiwqia vvifaglvvg
      121 nilnsgalfv nqiaiqavyv vavpmsiatk pfdrtidaiv gaviailmal ivpsdarkrp
      181 rnraanllye isvllkgtak alrtadtdla ervlerares qefvdswrss isvsqeatri
      241 narsrryaae vtrlaracey adramrlvrv iarrvvamaa tgverpgvah pieqlgegaa
      301 mlrialrrgt srvpaemfla qvartlspka dfvtdrhdet lvlllrplsn dlmsaagmte
      361 daandvlpel de
//
LOCUS       WP_284924637             215 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284924637
VERSION     WP_284924637.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..215
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22099
     Region          <35..212
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mnehhddlgs gepaqnpaev epadrgyrll etwdpprwvl valfgaggvl avatlvaygw
       61 nhpsayvaav fvavspilaa idfaerrlpd vvtlpaagas vialvagglt sgdwgpalrg
      121 gagmvilfaa ffvmfifagg afgfgdvklg lsmgavlgty swfalllgpf igmllgfavg
      181 vvlmimrkat mktaialgpy liigtlviiv igalg
//
LOCUS       WP_284924686             508 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284924686
VERSION     WP_284924686.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..508
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <77..504
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 klmfflfici ilqityttpv yslcklyknn sinnfesivs nnqliskhai qiilimaiic
       61 vilifyiiyd klnfkiklqr iaytdnltga ntidkfvida nkilckntqv kyallyidid
      121 kfkyindlfg yevgneilrn ltkiikrnif eeemfarisa dnfiiimkyi eeeditkrlk
      181 tifeeldlfn nnqeekyklv lscgiyfilp edrdinsiid raniphkmak gghkssyafy
      241 dnkihdqeik ekementmfs slenkefiiy lqpkielntg eiqgsealvr wkrpdkglip
      301 pnefipffer ngfvinldly vleevciylr kwidaginpv tvsvnvsrih lycnnfiety
      361 kniidkynip akyielelte siifdnfdil idimnnlkki gflismddfg sgysslnmlk
      421 eipmdilkld qkfimetyns krskiivtkv iemakelgmk visegvetee qfkllkevkc
      481 dmaqgylfgk pmpieefehl ivsnlvrg
//
LOCUS       WP_284924713             266 aa            linear   BCT 25-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Brevibacterium sp.
            UMB1308A].
ACCESSION   WP_284924713
VERSION     WP_284924713.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..266
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28987
     Region          20..259
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mfsdylrere idevpgrgvk pwviahrgys gavpentmaa vdaarligcd fievdlhvta
       61 dgvpvvvhdp tlqrttdiqg tiahmsydri sladagyghg lgfagqripr ldamlknvae
      121 mggrmllelk gewspgavar vgqeiaevgm adrvilqsfn arsvevcrdi aphvprgllr
      181 lvpreedmgl aqrlevvavn psirgfharr dfveevlgrd lavfvyttds prdweklvga
      241 gvtgiitnqp grlqgflaak ydiahs
//
LOCUS       WP_284924747             151 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284924747
VERSION     WP_284924747.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 151)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..151
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=16463
     Region          6..138
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 mknitvsalv iqhpsepall mvrkrgttsf mlpggkpepg etaqdtvvre ireelglhld
       61 esqlfflgtf tapaaneaqh mvtghvfvce tvpadlsvea pqclheieei gwfsyeqlpp
      121 dtdaqqfapl trtrvipalm qrsgsageeh s
//
LOCUS       WP_284924761             186 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284924761
VERSION     WP_284924761.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..186
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=20218
     Region          1..>150
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mrkfrpeiql lraiavlavv vyhiqpswlp ggfvgvdvff visgylitah mlkevestgr
       61 lslsqfwanr arrilpaatl aivvtsivsl fvlpstqlvd atkqgiasal yiqnflladq
      121 svdylgqdaa pspfqhfwsl sveeqfyvvl rlpslsghpi sadlvsvgkd vhcestaqev
      181 hsgvsa
//
LOCUS       WP_284924787             747 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Acinetobacter baumannii].
ACCESSION   WP_284924787
VERSION     WP_284924787.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..747
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=72277
     Region          <14..726
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mfllknlvss iskvtqdlgn ivsitpvvnt gssvnvnvsd inianvsttg llsnvistvt
       61 dtvshtttdl vsnvvgtvtg tvgstnpidt vtniiggvtg gvtgnplevv tdiiggvtgg
      121 vvggtspisp vidvvqggid ilqgveslkt eiintgietv adavigvlpq aehpvseiad
      181 lgtltfetsr dtvngalevv sdlvggdiqg atesatgild tlitngttat givtgvvgsv
      241 tdviggvtgg vdgnplevit diisgvtggv dgnplevitd iiggvtggvg gdnplgvvtd
      301 iiggvtggii gggtspispv idvvqggidi lqgveslkte iintgidtva dtiigvlpqa
      361 ehpvseiadl gtltfetsrd tvngalevvs dlvggdiqga tenatgilgt liqngstatg
      421 ivtdilggvt gtiggvtggi ggdnplgvvt diiggvtggi ggdnplgvvt diiggvtggi
      481 igggtspisp vidvvqggid ilqgveslkt eiintgidtv adtiigvlpq aehpvseiad
      541 lgtltfetsr dtvngalevv sdlvggdiqg atesatgild tlitngttat glvteiiggv
      601 tgtiggvtgg dsplglvtdl lggltgsvgg dsplgvvtdl lggltgsvgg dsplgvvtdl
      661 lggltggvtg gtdnpigivt divgsltggi tgegsldvis nllggltggs llggvtstvs
      721 svtntthtiv ptslltdnfl ensfhtv
//
LOCUS       WP_284925261             124 aa            linear   BCT 25-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284925261
VERSION     WP_284925261.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..124
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12439
     Region          8..117
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 msrllppllv faggalgtwg rvavfqlget aglitvntvg tlilaflsgl lldartpwaa
       61 pvklfvgagi cgalttqstl almtvqssfg gltltlvslv tgvcaaisgw ligsavrpsp
      121 rslc
//
LOCUS       WP_284925262             117 aa            linear   BCT 25-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284925262
VERSION     WP_284925262.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..117
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12255
     Region          2..117
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 mliavvlagg vgavcrwacd taltrwlnas wpvavflinv vgsfftgvlt gatvefpvfn
       61 vcttgfcgaf ttfstlmvgw leltlrkrpv hgvlyvggtl lacvlsvwlg latgsrl
//
LOCUS       WP_284924118             216 aa            linear   BCT 25-DEC-2024
DEFINITION  MORN repeat-containing protein, partial [Clostridioides difficile].
ACCESSION   WP_284924118
VERSION     WP_284924118.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Zhou,J., Liu,H., Lin,Y. and Zhao,J.
  TITLE     Membrane occupation and recognition nexus (MORN) motif controls
            protein localization and function
  JOURNAL   FEBS Lett 596 (14), 1839-1850 (2022)
   PUBMED   35568981
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Sajko,S., Grishkovskaya,I., Kostan,J., Graewert,M., Setiawan,K.,
            Trubestein,L., Niedermuller,K., Gehin,C., Sponga,A., Puchinger,M.,
            Gavin,A.C., Leonard,T.A., Svergun,D.I., Smith,T.K., Morriswood,B.
            and Djinovic-Carugo,K.
  TITLE     Structures of three MORN repeat proteins and a re-evaluation of the
            proposed lipid-binding properties of MORN repeats
  JOURNAL   PLoS One 15 (12), e0242677 (2020)
   PUBMED   33296386
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..216
                     /product="MORN repeat-containing protein"
     Region          <74..187
                     /region_name="COG4642"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443680"
ORIGIN      
        1 yfttilcvfi clssvfiftq larvfinkkk inqkiksrng frydrdfiea rreeihikdn
       61 nnnknksnnk klkeekvfky dngdlykgef vdgkkngfgi yifsskekye glwkddkmhg
      121 igkytyrdgs iytgefkygl knglgkltyp nndiykgyfl dnkkngkgvl ykndgnkqag
      181 iweddeqcks ldfkdlnnnk innvyqnrln nnklkv
//
LOCUS       WP_284925445             402 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284925445
VERSION     WP_284925445.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   5  (residues 1 to 402)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13213516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..402
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=43192
     Region          17..>125
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Region          131..394
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrrmgrvvrd dtqtvgssii pltlaglfal aslldqstya lglaavvivl visvgialmv
       61 vtpwiavgvc almvvvsviv dvtffgvaal llpvtagymv vrgnkwagya fmitvavlls
      121 gavmtsevsh avlvssvvfw vivgaialgg ghlvryllmr earlkeharl sldelrtels
      181 rdlhdsiggv ltrvsllaqq armsepakvt anldqivnea hsatgevrvl isrlrtlddk
      241 ihgarpprda eltrgdnsde asataeadvk raiqrfseql dafgfevnvy ttpggiyalq
      301 nytgvvsrll heallntvky adpqwpvsfi vglndhvslv fsntiredas gvdssgfgle
      361 sltrdlgahg gslttrrdrl cegkeqwvle irlpgahqrt vs
//
LOCUS       WP_284925483             587 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284925483
VERSION     WP_284925483.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..587
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=61888
     Region          2..459
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          520..586
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(543,552..554,561)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            553
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mplksvlian rgeiavriar aaadhglrsv avysdadana lhtrvaseay rlpgttpadt
       61 ymnipaiiei alrakvdavh pgygflaena qfasavtaag ltwigpsadv ietlgnkvta
      121 rdiavsvgap lapgsdgpve hwedahafaq ehglpiaika ayggggrglk vvhelsdied
      181 afaaagresr aafgrdecfv ekflvkprhv eaqvladthg ntvvvglrdc slqrrnqklv
      241 eeapapfltd dqeemirras vaicesvgyt gagtaeflva ddgtisflev ntrlqvehpv
      301 temttgvdlv geqfriadgl plsfaddvqg galpqnghai efrlnaedva agyvpcpgtv
      361 trfeaptgpg irvdsgvtsg stvpgvydsm maklivhgst reqaisrarq afkelviegv
      421 atvvpfhqav lehpdfvddf avhttwieqd fasdfersqi yadhsaeqpl trfgieldgk
      481 rvelgipaql lsqvaaatpk adgarergdt sadaadsdnt vtspyagklv twkvadgekv
      541 dkgqtiavie amkmesniva paagtvecea lsagdeiaag atiaria
//
LOCUS       WP_284925529             117 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284925529
VERSION     WP_284925529.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..117
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11992
     Region          2..101
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mnwlillmsg aleavwahal agdlpyapvw fviglclslg glsyamrtip mgtsyavwsg
       61 vgaattavwa alrgepfglg tivclvaiia gvvglqlatr sskpsgeiaq dtmndak
//
LOCUS       WP_284925560             316 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284925560
VERSION     WP_284925560.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..316
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34066
     Region          16..292
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mstpteaeia siadlaarar nsmntvldgk drvvelslit llagghllle dvpgvgktll
       61 akalgrvvdg svrriqftpd llpsdvvgvn lfnqetrhfe fragpvfsnv viadeinras
      121 pktqsamlec maegqasvdg ttylmpqpfi vvatqnpidm egtyslpeaq rdrfmirtsv
      181 gypsveseaq mlahntgrdp ldelspvttl deierartvv tnvtatdelr aymvrlltat
      241 rshdaisvgv sprggvlllr aaqahavlng rnyvtpddvq nlaeevlahr iiavesdhpe
      301 htsqlirdvv aatpvs
//
LOCUS       WP_284925654             598 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284925654
VERSION     WP_284925654.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..598
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65227
     Region          17..598
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 msvreastpv eenlsypasi pavlverlrd ypndvycerr gasgmfeqit vrdyardvft
       61 margliahgl kpgdrvglmg ntsydwvvcd lavmcaggvv vpiyqtsstk qvewiaensd
      121 lttlivesee yekvtapvve qmsldlhvid rgdvkrlqda anetpqdevd trihalqpdd
      181 iativytsgt tgnpkgalls hanfmhhavn gvenpalggt vlagqdsril mflplshvfg
      241 rfiefvclys rcvvgytpsm ktvvddlgdf kptwllavpr vfetvfnkar nagklqkmif
      301 dwasrvayay svaqdrggpg lalkaqhaaa davvfsklrk alggdvayai cggaplgqwl
      361 ghfyrglgiq ilegygatet aaptsvnlpg hlkvgtvgta fpgaslrvve sgeiqikgph
      421 vfrgyldnpe atkeafddgw yktgdlgkld degyltvtgr vkellvtagg envqpavled
      481 alrrhtlise vvvvgdrerf vgamitldge mlpgwlktng lpsmsveeag rhpkvreaid
      541 tavkyanenv nraqsirkyv vlprdleqtk delsaslkvr rpvvlkhfar eyaalydk
//
LOCUS       WP_284925669             242 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Brevibacterium sp.
            UMB1308A].
ACCESSION   WP_284925669
VERSION     WP_284925669.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..242
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26276
     Region          18..143
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mtdsysvnae wyaalvipwq dgmdsavrtl lgpidggavv diasgvgtgl pllhelgaer
       61 lyavepseam riglvttvar dpklmsvttv vphafpqase llpaewsagv mlnalghldd
      121 tdreelwatv akrlvpggrf vlslqppetv teipwadfgs vqigdhvlqt rgkaeplsdt
      181 hvewtmewtl mdqdravida rtttypwrvl shdqvvdeas rhglvevhge aiptfvalek
      241 pv
//
LOCUS       WP_284925677             261 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284925677
VERSION     WP_284925677.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..261
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=27665
     Region          93..255
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 maghsspkqg rsrrayaiia ivaalafiav vgiaqltsgn knasgkdpaq sgatssasse
       61 dhanngaqas gnegewvrrd addsaaigdv napvvitewt dprcpfcahf hndilpelkk
      121 kyvdtgkvrf efitvaffge qsaaagaame aagkqgkyre fsdalyaaap ekghpdlpee
      181 tlvkfaktag vedieqfrkd mndqtlidtv ndatakaqqy ygiqavpffa asdgesamrg
      241 aqpvenfskf ideqltkaga q
//
LOCUS       WP_284925679             115 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Brevibacterium sp.
            UMB1308A].
ACCESSION   WP_284925679
VERSION     WP_284925679.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..115
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12218
     Region          25..112
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtelleapma gaeactpggg iismeqaerv alvakaladp vrlrilhhia asrcssvcac
       61 hmpevfgvtq ptlshhlkkl veaglvdkem rgkwahftpr peglaalhey lamlg
//
LOCUS       WP_284925745             426 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284925745
VERSION     WP_284925745.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..426
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45592
     Region          12..423
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mltetllgeg sgiyrttlpn girvisetip giqsetvgvw vgsgsrdetd dnagsthfle
       61 hmlfkgtatr sakdiartfd rtggeanamt akectayysr clvadlpdvc atlwdmvlas
      121 tldvaefere rtvildelam gaddpedvlf eaydeliyag splgrpvgat keriqalvhd
      181 elqhhyrday vgprlifsaa ggadhedlvd lvwratqhlp eaaapvgtts grmtpvfspg
      241 erhiarpteq qslimgvagl hdghddrftl tvlasllggg mssrlfqtvr eerglayavh
      301 ttgsqysdvg dfgiyagcap avaqqvvdlc veqcqrlase gpmaaevadt aaqvsaatvl
      361 gmestairmn rlakselsnr plvdaaelve rvrgvtaedv qalaqrlfgg pwalcslgpa
      421 dnvrlk
//
LOCUS       WP_284925795              93 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein
            [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284925795
VERSION     WP_284925795.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..93
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10494
     Region          4..>66
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 malvkinqls vpegkgeele arfaarkksv dqepgflgfe llrptgdntd yfvvtrwede
       61 esfqnwvakr hprnpnetvs aakgmlefev vel
//
LOCUS       WP_284925814             274 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Brevibacterium sp.
            UMB1308A].
ACCESSION   WP_284925814
VERSION     WP_284925814.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..274
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29582
     Region          1..274
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mattvkpawl fvpgdrndry tkaaersdvv ivdledavsp ahkadarkaf lefqnsdqal
       61 dptktvvrin pvgsewfhsd lkllselpgs gysvmlpkve dtealehirg lkvyalietv
      121 kgvvnvdtia ahegvtglmw gaedlfaslg gghsrtaagd yrapavytra rvlmaakahg
      181 klaidsvwtd idnlddlgve addavncgfd akalihpkhv evvrnafrps geqlewargv
      241 iqaassadag awtyqgqmid epllqqarni lara
//
LOCUS       WP_284925948             837 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284925948
VERSION     WP_284925948.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 837)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..837
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=92359
     Region          15..827
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mfalphlyrv peefadsdtl fetfveytkd tgitlypaqe eailailtgd ntvmatptgs
       61 gksmvalaaa ffalcrgqrt yytapikalv sekffdlthi fgadnvgmvt gdstvnadap
      121 iicataeila nqalregatl dvgmivmdef hyygdpqrgw awqvplltlp aaqfvlmsat
      181 lgdtsaiqks lteltgrdcs litsahrpvp lsyayseepl hetlsklvrd nkapiyvvsf
      241 aqaaavelas svvnanlatr eqreeiaeei rgfgfskgfg valkrmllag vgvhhagmlp
      301 kyrrlvehla ssgklsvisg tdtlgvginv pirtvvltgl tkfdgfrqrr lrvrefqqiv
      361 gragragfdt egfvvaqape hvienkkall kagddpkkrr kvvkkqapeg fvnwsettfn
      421 hlvegkpeel ksrmrmthst vinllsrpha svdtvkdfid sshdentldm ylralrigrn
      481 lldagvierr vvgarveyap vkdlgpqfal nqplspfala alelfdpesd tyamdvlsvi
      541 eattevsyav lkgqlnrikr eelaalkadg vdyaermeil deitypqpng evleeafdaf
      601 thsapwlrei gitpkavvad mvehsmnfsq fvnyyglarv eggllryltd vyrslvqnvp
      661 hdlrneelta iiewlgatvm rvdsslveew ealknagdea evlpaldmsr tfsadtqaft
      721 ravrnamfhr vilaeraayd algdldgesg wtqkkwedai edfydeygdl gvsndsrgpk
      781 ffnildkede awtvrqildd pegdmdwait arvdlpasde agevvveild vgpltgn
//
LOCUS       WP_284925963             313 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284925963
VERSION     WP_284925963.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..313
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=33335
     Region          9..289
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 msksswqate vnryvywlav gllllqaliv ftgaavrltg sglgcpnwpm ctdssltntp
       61 emgihgfief gnrvlgvvlg lyslfvvial wplrstrsdl frmavllfav vpfqailggv
      121 tvrtqlnpwi vaahfipsal avalsaymvk rtrdtganpr piasrtlvtv awavgilcai
      181 vvamgvlvtg agphagdeis arnglntllm srlhaipvwl mtagtiyglv larkeklasa
      241 traftflliv evaqgiigyt qfftglpvpl vmahiaglcl vitaavfvvd svyqrdplpt
      301 sasrnaqpet tsa
//
LOCUS       WP_284925967             241 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Brevibacterium sp.
            UMB1308A].
ACCESSION   WP_284925967
VERSION     WP_284925967.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..241
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25775
     Region          10..217
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 msarpgqdlr trqqvlaivl dqgpisasgi armvdltpaa vrrhldalek enaievrela
       61 gvkagrgrpa rhyvvtsagh aqishaydqv avealdfvss elgreaverf artraqelre
      121 klearveegg svstrsrgla aaldkegyaa satpvavgtp leamqlcqgh cpiqhvaeey
      181 pefceaeleq fgeilgvdvr rlstlasgah vctthiptst lnrpllgsqd gksnpkkgge
      241 r
//
LOCUS       WP_284925997             221 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284925997
VERSION     WP_284925997.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..221
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23402
     Region          4..206
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mslnydavlw dmdgtlvdte pywmaaetel maahglewrh eqamlmvgnt ltksadimrs
       61 fglplatdev vqtllrgvia rvheripfrp gaqeliaslk aadvpmalvt msyrtlaqav
      121 vdglpegtfr tlitgdevsr gkpdpepylt gaaslsvdpa acialedsvp gmasaiaagt
      181 ltvgipnhvp leeqpgaili etldglnaes lgnlvrplqg s
//
LOCUS       WP_284926010             291 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Brevibacterium sp.
            UMB1308A].
ACCESSION   WP_284926010
VERSION     WP_284926010.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..291
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32152
     Region          11..291
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msstpqvvtt lislvayitk keevpiaela avfglkestv rdyldvllvs gmpgdygaki
       61 dvwendgivs lsntegvdvp vrlssleahl llmalesags etpevaqsvi eklrnavgew
      121 esdavsfepa evspelrsav tqalktdtal tidyyvrsrd eittrtispi efnldgqwyl
      181 daychdkqgh rsfrvdyirn wettsepaqk gndennnget critfarega wlvdeltpra
      241 vsfdthgsgt vtleltvfsa dwivqllmmh grhvlaiepa eyaraalerl e
//
LOCUS       WP_284926098             283 aa            linear   BCT 25-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Brevibacterium sp.
            UMB1308A].
ACCESSION   WP_284926098
VERSION     WP_284926098.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Bagautdinov,B. and Kunishima,N.
  TITLE     Crystal structures of shikimate dehydrogenase AroE from Thermus
            thermophilus HB8 and its cofactor and substrate complexes: insights
            into the enzymatic mechanism
  JOURNAL   J Mol Biol 373 (2), 424-438 (2007)
   PUBMED   17825835
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..283
                     /product="shikimate dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29350
     Region          6..257
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 mdnfnacvag spiahskspd lhtaaltalg ipgqygsvel tedqlaghid ahpelvgmsc
       61 tmplkttlaq lahernwnid ptvtatrvan tfvntptpsv yntdvagivg alrtsatsaa
      121 vvgsgatats alvalkelgt tsvdiyarnq rtradlaqla qslgmdatha gleninwdhd
      181 vivstlptgv dldvptrlsa tvldvayahg svgekardag aevvsglaml veqavaqfvh
      241 fvgvtgrslt seevhrvtva myeavnltpp vtppkgdsws psh
//
LOCUS       WP_284926129             444 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Brevibacterium sp.
            UMB1308A].
ACCESSION   WP_284926129
VERSION     WP_284926129.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..444
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46828
     Region          4..433
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mqetsktess defigaddya lervpsgkre hwlkvavqrf gqlsalsqfl lgaalgfgmt
       61 fwdsmlaifl gtvilevvai mtgilgqreg lstsmlarwt gfgrygssli slvislslig
      121 wfgvqsgvaa dglasfvpgv ptwvwailmg lgvtaivlyg fesmawtayi tipaflglag
      181 wsiiselqkh digelvtqpa pgpvltlaag ttlvaggfiv gmvitpdmtr fnrsaadvvk
      241 qtvvsvtige igvalagvll ahalktndii nivtstsgfi gaiiivagti kmngwnlyga
      301 slgivsfmst vfgknvsrak vtiliglags llaaagildy fiqfltllgv tfppiagimv
      361 aeyyivrtwr tllsesaprl pdqepgwvig tlivwliavv igatlpigip slnsllasiv
      421 lyvlagklgl iralqvipve nkqn
//
LOCUS       WP_284926132             404 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284926132
VERSION     WP_284926132.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..404
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42495
     Region          37..369
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mthtnqghds hsgtpagtla etpstspasa nlthvrspvp villtgylga gktsvlnnll
       61 rhpsarvgvi vndfgelnid aglisnqvne pvaisggcic cltdaggled alaamaapkh
      121 qldaivveas gfaepltlar lvsrwgrgrf rlggvidvid acehfstvdq ggipplryav
      181 atlvlvnkld lippnqrdah iskirdrvhs rnprahvvst vlgridphll fdgspepntq
      241 tattsagets panpewqqte lplhdlfmas yrerdearla sidapahdht hahsvtvevp
      301 gavnaevvld fledlppgay rakgfvtvpt grgtqafvvq avgpnvfasr akdtvagsal
      361 vvigadldeh taevatrtal telpadgpas pglerlrtlv rlhs
//
LOCUS       WP_284926236             756 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Brevibacterium sp.
            UMB1308A].
ACCESSION   WP_284926236
VERSION     WP_284926236.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 756)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 756)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 756)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..756
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=78040
     Region          13..751
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mstpaplsag sdielevggm tcascanrie rklnkldgvt asvnyateka kvtvpagydp
       61 allvaevekt gytaalprpe aattdsegnd qdpaddpelt slkqrligsi vltvpviama
      121 mipvlqftyw qwaslalaap vvvwagwpfh kaawtnlkhg tatmdtlvsm gtsaaflwsl
      181 yalffghagm pgmkhpfeft iapsdgagni yleaaagvtm filagryfek rskrqagaal
      241 ralldlgake vsvlrdgvet kiptselavg defvvrpgek iatdgavvsg tsavdasmlt
      301 gesvpvevva gdavtgatvn asgrlvvrat rvgsdtqlaq maklvedaqs gkaavqrlad
      361 risgifvpiv iaialvtlga wlifgpgvsa aftaavavlv iacpcalgla tptallvgtg
      421 rgaqmgvlik gpevlestrk vdtvvldktg tvttgkmtlv daitepgidr tellrlagal
      481 edasehpiaq aiakaaaveg gqlptpedfa niegkgvqgv vdgrvvlvgr eslladwsqq
      541 lssdvaaaka eaedegktvv avgwdgrarg ilvvadavkp tsaeaiqglk dlgltpvllt
      601 gdneavarri aaevgiekvi aevlpkdkvd vvtglqnegk vvamvgdgvn dapalaqadl
      661 glamgtgtdv aieasditlv rgdlraavda irlsrktlgt iktnlfwafa ynvaaipiaa
      721 lgmlnpmlag aamafssvfv vgnslrlrgf rsvakq
//
LOCUS       WP_284925415            1041 aa            linear   BCT 25-DEC-2024
DEFINITION  PD-(D/E)XK nuclease family protein [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284925415
VERSION     WP_284925415.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1041)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19831098
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..1041
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=113053
     Region          26..942
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
     Region          777..1036
                     /region_name="Slr0479"
                     /note="RecB family exonuclease [Replication, recombination
                     and repair]; COG2887"
                     /db_xref="CDD:442133"
ORIGIN      
        1 mkdffsvrta tdavvdslnr gdslavlgvp gagkstvmkn sfarlaasrn adsvlvltpn
       61 rehadvlrde lkspvrssat arsvhsyafg ivaahtattt gvpalfvsga dqdvrlaeql
      121 qgyfdstvag pqwtrsmtpe lartdvfrtq lrdsiseimg hdfsydhive lahthnrpew
      181 evlsfigrey eelltflgeg avdtsavftk akhiveesrv vpgkawdfap evlpawilcd
      241 svqdfpdsal gflhalyqrg vcfaltcspd satqsfrggs gdvfagrhql gvhtdialdp
      301 ldphirgaga ithtvdslmr dsadpvhalg ymapkgsaeg stqvfscecs sgsnaarmia
      361 smiydrhqdg vpfadiavvt rrassaaqls delaasgipv rtsvralasd patmpllqil
      421 slppdspewp naatacvtga yggldaltlr slqreltqls gvegslealm ewaletdtel
      481 paaverakrm vkaaqesshe laqyavwavw naaqvadewq enalrnpsgh hssyldavir
      541 llalaeklte gatsqvtgrd famkvmsqkf aqdslahtal ndivtvttpa gvahthfdtv
      601 ivtdlqegvw pnptvrgtif ktpqlmrvlk dpasqeelss enfsqqdfla rrretirdeg
      661 klfiaalsra rsravvvavn ghgelpsplf tavkdmpwts qywvdepdil pstlseiagy
      721 arlqvnqale sadedaakpw aqllqtlrcs gvsaadpstw wlnpsselpa mptdepvris
      781 psqvetydqc plkwffnqns sqtvdtypqa fgnliheiaq typggdladm lnhfdekfee
      841 ftfesewerq reyadgratv enlseylknr gdktfvaaev vvrsdldvpl gparvsgrid
      901 rlektsdgaa yivdfktgkn lpskpsvqen pqlatyqvai etgqatfidd geliggitkc
      961 aggelvyprk aagqgkapsn vreqgpikdt evytktlati eslvrsarth tftatpsdda
     1021 crtcaftqsc pafamgesee s
//
LOCUS       WP_284926360             114 aa            linear   BCT 25-DEC-2024
DEFINITION  GroES family chaperonin [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284926360
VERSION     WP_284926360.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Hayer-Hartl,M., Bracher,A. and Hartl,F.U.
  TITLE     The GroEL-GroES Chaperonin Machine: A Nano-Cage for Protein Folding
  JOURNAL   Trends Biochem Sci 41 (1), 62-76 (2016)
   PUBMED   26422689
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Horwich,A.L., Farr,G.W. and Fenton,W.A.
  TITLE     GroEL-GroES-mediated protein folding
  JOURNAL   Chem Rev 106 (5), 1917-1930 (2006)
   PUBMED   16683761
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Levy-Rimler,G., Bell,R.E., Ben-Tal,N. and Azem,A.
  TITLE     Type I chaperonins: not all are created equal
  JOURNAL   FEBS Lett 529 (1), 1-5 (2002)
   PUBMED   12354603
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Fenton,W.A., Weissman,J.S. and Horwich,A.L.
  TITLE     Putting a lid on protein folding: structure and function of the
            co-chaperonin, GroES
  JOURNAL   Chem Biol 3 (3), 157-161 (1996)
   PUBMED   8807841
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11277705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..114
                     /product="GroES family chaperonin"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0044183 - protein folding chaperone
                     [Evidence IEA]"
                     /GO_function="GO:0051082 - unfolded protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=12296
     Region          15..101
                     /region_name="Cpn10"
                     /note="Chaperonin 10 Kd subunit; smart00883"
                     /db_xref="CDD:197951"
     Site            order(15,17,19,22,53..54,66,76,81,83,99..101)
                     /site_type="other"
                     /note="oligomerisation interface [polypeptide binding]"
                     /db_xref="CDD:238197"
     Site            33..46
                     /site_type="active"
                     /note="mobile loop [active]"
                     /db_xref="CDD:238197"
     Site            order(62,64)
                     /site_type="active"
                     /note="roof hairpin [active]"
                     /db_xref="CDD:238197"
ORIGIN      
        1 mtdtqarssn ldsvpvrmlh drllvepdke sgerkssagi vipatarvgr rlawgtvvaa
       61 gplvrqvslg dsvlfdpeeq aeveldartf tllrerdvhg iadqpddsst glyl
//
LOCUS       WP_284926447             650 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Brevibacterium sp.
            UMB1308A].
ACCESSION   WP_284926447
VERSION     WP_284926447.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 650)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 650)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 650)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..650
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..650
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=68101
     Region          6..633
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtskararis lisgallvla lvawgiaqwv ddpalsavsg wafatgaipi vswrslqmvs
       61 llgaaltagw piaktafqal ryktfsidll vtiavtgalv igefveagvv aflfvfgswi
      121 earsmertrr svsdlidmap qeadvirdge tvtvpasgvk vgehvvvrtg srvpvdgtvv
      181 dgrghidest itgepvpalk ndsdsvfsgt ivadgyltir aehvgsdtaf sriielveda
      241 qdsksstqrf ldrfsrwytp tiivlavvaf lvtfdahfal tflviacpga lvistpvsmv
      301 agigngarhg vllkggdave rlaavdtlvv dktgtlthgr ptvvevvgig sdahevlrla
      361 aavetasehp lgtavveaaa evslspvsdv rvhagsgisg tvegtevavg srrlvneycv
      421 tlgswekkaq eletagatvf fvivagklag miavadtirp eakalsqlhe wgirdivmlt
      481 gdnprtatav arelgidqvk aellpehkvd avqeltaqgr kvamigdgin dapaiaaahv
      541 giamgtgtdv sidtadvvla ggrfdqlvha rqlvqatvrn vrqntfiala tvvallvgvv
      601 agavfmsvgi lvheasvlvv vlnavrlvrf kakirkldad qgekstveln
//
LOCUS       WP_284926518             410 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284926518
VERSION     WP_284926518.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..410
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43025
     Region          105..408
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mpnphtkpss qsiiivgggi vgsflayeca lagwnvevfd pmpepaasca nagilalsya
       61 qpmsnpralf tgakavlagg ggielatplt prtlgwlpkf awasrpghak rhirtiynma
      121 rtsvdlyael eqrestdlhl rrtgwlyvat spkalraqar eaasvapagv rsqlldaaet
      181 racepalasd iaggvfypdd vsfhpghvta tvrnaaqsrg arfhkatvts graatgggva
      241 svetdlgehf rarhvviaag aqsdqvarlf ggrvavepgv gwsveiptdg pvasralmsi
      301 ddhvvinpad trvrlsggmr fggesrtapt pveidalvra atrlvpavge ldregavari
      361 gsrpmtaegl pvfkeigrgv tvltghgtlg mtlapftarr vlellskrye
//
LOCUS       WP_284926567             323 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Brevibacterium sp.
            UMB1308A].
ACCESSION   WP_284926567
VERSION     WP_284926567.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..323
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34249
     Region          3..322
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(40..41,45,120,124,127,145,148..150,169..170,174,189,
                     214..215,236..240,261..264,311,313)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(132,229..230,243..248,256..263,266..267)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 myavqaqrag gpevleyvev ddptpgegev lvdvkatgin fidtyrrsgv ypmqfphipg
       61 tegagvvsqv gegvtsvqvg drvawhdafg syaqkvavka dmlvpvpddi dfdtaaaill
      121 qgltahylvt gshriepgqt alvhaaaggv gllltqlith mggtvigtvs teekaqlark
      181 agakhvflyg egvdiaqtvr dltdgegvhv vydgvgkdtf dasldslrvr gslvvfggas
      241 gqvppfdvqr lnsaggvfls rpslqwfvrt peelrersed lftglkegwl kfrvgatfpl
      301 eeaadahral egrkttgkvv lka
//
LOCUS       WP_284926579             630 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Brevibacterium sp.
            UMB1308A].
ACCESSION   WP_284926579
VERSION     WP_284926579.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 630)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..630
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64894
     Region          28..624
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mssacgcehe pateiedldr pwwkdpelll pifsgvalgi glaldwagle tpatilfwvg
       61 lllgaytfap gairnlvtkr klgigllmti savgavilgf vgeaaalafl ysiaealedk
      121 amdraqgglr allklvpqta tvlrdgtave vaakdlvvge lmlvrpgeri ptdgiirsgr
      181 ssldtsaitg esipeevapg devpagains agvlevetta agtdnslttl vdlveqaqae
      241 kgdrariadr iarplvpgvm ilavlvgvig sllgdpetwi tralvvlvaa spcalaisvp
      301 ltvvaaigaa sqfgvviksg aaferlggir hlavdktgtl trnqpevtgv vladgfdraq
      361 vlafaaaveq qsthplaaai vaavpeapda qdiseeaghg iggtvegrrv lvgsprwida
      421 gplnadvkrm esegqtcvlv tvddalagai gvrdelrpev peavqtlhan dvkvsmltgd
      481 ntrtaralae iagiddvrae lrpedkasiv aelssktpta migdgindap alagatvgia
      541 mgatgsdaai esadvaftgh dlrlipqalq harrgsriin qnivlslaii ivlmplaisg
      601 vlglaavvlv hevaevivil nglraaqakr
//
LOCUS       WP_284926641             455 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284926641
VERSION     WP_284926641.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..455
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48947
     Region          5..451
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mdftselara qallqarage tevelrldat rracellgdi htsapvitvt gtngktstar
       61 midtlirahd lrtgrfssph mqdlterfsv dgepvsaekf veivddiqpv lhivdqelaq
      121 sdrppltffe altvvafaif adapvdvmil evgmggewds tnvadaqvcv ftpvsldhqq
      181 flgdtveeia rtkagilnrn vdpspaphpv avvgpqvpev edvlasefsg rdaqsrwlgr
      241 dfglqnrlna vdgqvihvrt qlgdypdlfl plhgehqavn aavalaavea flgtedkpln
      301 aevvgegmsa vtspgrveil rseptvivdg ahnahaaqvl aetvgdafdf aevvavvamy
      361 adkdphgvfe hihrfakrvi vtqaqspram eaeklasaas ewweeddvmv endmnsalmk
      421 aldlaleesg tgvvvtgsls tvgeartllg rkdqs
//
LOCUS       WP_284926655             180 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Brevibacterium sp. UMB1308A].
ACCESSION   WP_284926655
VERSION     WP_284926655.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..180
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19537
     Region          19..172
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 msfqlvnpll tgaftrvlle lrwgdmdayg hinnvtqmrl leearvrvfg sptadrdapn
       61 iagplgvvps cvgveippvf sevshthdil vashaieyra pipyregpva idtviskvap
      121 vvmtvgyvia epdgskaytv aetdvvfvdr esgraqrlqe ehaealravv npgpamrrrk
//
LOCUS       WP_284926697             252 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Brevibacterium sp.
            UMB1308A].
ACCESSION   WP_284926697
VERSION     WP_284926697.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 252)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..252
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26904
     Region          7..243
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mdtqprtnpq pralitgats gigrafvhql aaegydviav arthedlaql natplpadls
       61 tqhgiaavth aletqpidvl incagfgvrt stlntpvdql taqsmvmnes vrtlswyavk
      121 kmvargrggi vnvtslaavt tqgtyaaeka aatiftesla hdlrgtpvtc tavlpgfvat
      181 dfhrrmgvgr efpdcvwmep drvaqialrd aragkvisvp glgyqllyal sqvtprplmr
      241 alsggfqwkr ar
//
LOCUS       WP_284926741             322 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Brevibacterium
            sp. UMB1308A].
ACCESSION   WP_284926741
VERSION     WP_284926741.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..322
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=33709
     Region          2..320
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mricvtgasg llgsgvaral veqghhvttl qrrpsgvdga qdvlgsvtdp acvegaltga
       61 eavihlaakv smagdsaqfd rvnidgtrtv veaaqatgvk rfvhisspsv ahtgssiige
      121 gaqpanpqta rgdyartkaq geiialeads dsfpvivlrp hlmwgpgdtq lteriierak
      181 qgripilgsg tplidtlyst navdailaal evvphthgea lvvtngqprp vgellnriav
      241 aggadpirlh vpagaakaag saietvwnlt ehddepplth flaeqlstah wfdqrrtrea
      301 lnwtpavsie qglkilaqhy gk
//
LOCUS       WP_284926782             233 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein [Brevibacterium sp.
            UMB1308A].
ACCESSION   WP_284926782
VERSION     WP_284926782.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium sp. UMB1308A
  ORGANISM  Brevibacterium sp. UMB1308A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Brevibacterium sp. UMB1308A"
                     /db_xref="taxon:3050608"
     Protein         1..233
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26203
     Region          173..229
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mpwylapsla qlraevnarw phrskasdgt igdrahsart sdhnpnsrgs vnaiditakg
       61 idtralidaa kkhpsvryii fnrqimnrdi ggfkprrysg snphtahvhi siyqrasaen
      121 drrswgiaaa tapqpdpkpk askappfplp kghwygpesr dprnhsgywk rdrdgirtlq
      181 qrlkdrgwri svdgrygpdt rdvvrkfqre krlrvdggvg aetwaalwea pit
//
LOCUS       WP_284926813             290 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284926813
VERSION     WP_284926813.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..290
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <15..284
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 ntimdranta rktikgghkn sfafydkemh kkilkekeie nsmvdalnng efivyfqpky
       61 slsdyqiiga ealvrwdnpq kglippiefi pvferngfiv nidfyvfeev ckkirewmde
      121 gqkvvpisvn lsrmhfvnsn fiekfklivd kykiptrlie leltetavld nieglldtmn
      181 nlkekgfvis mddfgtgyss lnllkelpvd ilkldrafft ekdesnneki visnvikmak
      241 elkmkviseg vetisqvefl kqigcdmvqg ylfskpmpvk efekiafkke
//
LOCUS       WP_284926847             150 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284926847
VERSION     WP_284926847.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..>150
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          <1..>150
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 atiskepsgr yyvslcctdv dievfentnn qigldlgike fcisscgefi enpkylkksl
       61 nklaklqrel srktigslnr nkarlkvarl qehianqrnd flqklttkli kendiicied
      121 lqvknmiknr klsrlisdvs wsefirqley
//
LOCUS       WP_284926880             856 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Bifidobacterium breve].
ACCESSION   WP_284926880
VERSION     WP_284926880.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium breve
  ORGANISM  Bifidobacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 856)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 856)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..856
                     /organism="Bifidobacterium breve"
                     /db_xref="taxon:1685"
     Protein         1..856
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=95746
     Region          27..849
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtdekeygsl grlapewdgd erernltadd iyerffgwve evkgiepwph qeeaimdlla
       61 gdhvilntpt gsgkslvalg mhfaalctgr rsyytapika lvsekffdlv evfgrdnvgm
      121 itgdshinad apiicctaei lanqalregt hadvglvamd efhyygdper gwawqvpllt
      181 lpqtqfllms atlgnvdaia dklsdlndtp dvdviadapr pvplsyeytl dplertvela
      241 frngetpiyv vhfsqdaale taqalastgv sskeqrqaia eaikgvkftt afgkilqrll
      301 rtgvgihhag mlpryrrlve qlaqqgllpv icgtdtlgvg invpihsvvl taltkfdgtk
      361 mrrlrarefh qiagragrmg fdteglvvae apeyeienqk aiakaggdpk klkkvkrkka
      421 pegfvtwneg tfnklidaap etlvphlkit hsmvlnevaq ggdararidd liddsaqtpd
      481 qkehlhqrad eifrtlfdte vietedradg gkdyymtldm pddfaldqpl spfllaalel
      541 ldpesdtyal dvismaeatl edpkqvlraq erqardkama dmkadgldyd ermdklqeit
      601 ypkpledmle aafdqyrhdv pwandywlsp ksvvrdmvet asdftgyiar yniarsegtl
      661 lrylsdayrt lartvppekr deqlediisw lrvlvrsids slvdewenag dsadqseaaa
      721 slaapgaksa vvedrrgltv lvrnalfrrv qlmdldqpdk lgaldkdwdy gvhewedvld
      781 dyydeheyvg igaearspel fmldskhend ehtwkvrqii ddsdgdhdwt iegivdldat
      841 qdtgevvfhd yrvsns
//
LOCUS       WP_284926920             253 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284926920
VERSION     WP_284926920.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..253
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
     Region          31..215
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 nnylkfatyq ligftssipr likikknpdk fslkekfefm qkqakksldi vnielniigk
       61 etlpkepllf vvnhssmlds filtasverp igcviadepv wrnipifkew akllrcvyvn
      121 rknnregiks itqasqnilt gqsmavfpeg dltwikepns lvsefrsgal kiaykakcpi
      181 vplviknskd tyegyqpigk insvpvevef lepiydhien prlkssvlge niknkminti
      241 enfrksnktf kef
//
LOCUS       WP_284926971             374 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator, partial
            [Clostridioides difficile].
ACCESSION   WP_284926971
VERSION     WP_284926971.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>374
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          1..373
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mkillvddel eygvvmkkil qkkgylvdia lsgeeainii kkdknydlvl sdvmmknmdg
       61 vqlldriksi nrdievilvt gygsienavd amkrgalsyf iksnpienll eevekvkask
      121 isvsvqknnf eftlesknrd fnniikiakk aackdvnili lgesgvgkdi laryihsisp
      181 rkneifvpvn ccsfsenlle selfghekgs ftgavdsrkg rfelsnkgtl fldeigdipl
      241 nvqvkllrtl edksierigs nksikvdfrl icamnkepkv eisngnired ffyristiti
      301 tipplrkrre dlttlieffl nkyqiehdkk ihsidkevkd fllnynypgn irelkniinr
      361 lvvlseegnl skdn
//
LOCUS       WP_284927240             543 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator, partial [Clostridioides
            difficile].
ACCESSION   WP_284927240
VERSION     WP_284927240.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..543
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
     Region          2..529
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 kisiekltne mllskntvvq titdvkkylq tmglrleykg kykiigdeyv irelfliivq
       61 envleinsis eevssfdtkg hikltdysll nltkfvefln krirdgktly sykylneakk
      121 isyfsnckel lceeaneneq ayictyissl pslnsevked vveeyvdkli dkfevntaik
      181 leskhefkkn ilrhlhssyn rirfkfpirn pmldetkykh eslykiiksi ieneeefpvf
      241 egireeeigf iaayfggylr gsrdnglrrn kvllvcpngl mvsksleiql ykyiptieiv
      301 givsikqlke vnvyydyiit tidiqnvnnv ivvnplltss dvqllmnkli svkenekyfn
      361 leliiqairk ngvinneeal kadllniihk idegemyqpm lkelinaerv niiknvrdwk
      421 eaikiaskpl lednsieely ienmiksvek ygpyivladr falphasske gvnklamsll
      481 ivedevdllg kpvnifmvla avdntthira laslsemmye eenvkliing dkssilelin
      541 kqn
//
LOCUS       WP_284927357             115 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284927357
VERSION     WP_284927357.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..115
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <2..115
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 pmdaklieqv linlidnslk yskedckiei nvyekddyvw fevsdngpgi skelkkhifd
       61 rfftgeegak dsrkgvglgl sicksiiqah kgeimvennk dkgstfkfsl pkene
//
LOCUS       WP_284927515             415 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Bifidobacterium
            bifidum].
ACCESSION   WP_284927515
VERSION     WP_284927515.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium bifidum
  ORGANISM  Bifidobacterium bifidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Bifidobacterium bifidum"
                     /db_xref="taxon:1681"
     Protein         1..415
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44346
     Region          1..65
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          <156..>392
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 msfrtnlqyl raqrnmtqer lamllgvsrq aiskweseka ypemdkllmi cdlfgctldd
       61 lvlgdvsvst srpdshgasa tgcgttvegr tgedagspah agnakgsigd adepahlgaa
      121 gaiepsltgv ptgetpygtg sprpavhant dtlpqdltgy dehrrrfall isggvaaiia
      181 avgicnlfds snsilgvtrl ndfltflcic igviaglaml vpggmshaef krrhpyiedf
      241 yteedrsret rllvvgivgg iaailigiav tvyaddvlgi sdgwpnaiml mlysvavfsf
      301 vycgirhgml didgynkkad tdgkkeraag hdfydnltgt vcgiimllat italcllflg
      361 pwmlhddwss vglfwlpwpi ggvlcgiasl iiqlvkdyrr rnddgqgagq pgrtk
//
LOCUS       WP_284927609             371 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284927609
VERSION     WP_284927609.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>371
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          <2..330
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
     Region          300..>366
                     /region_name="COG1693"
                     /note="Repressor of nif and glnA expression
                     [Transcription]"
                     /db_xref="CDD:441299"
ORIGIN      
        1 mgnkagiyyn lqeityikkl eqnltnklre qgqiarytfk diktknknmv kcvelakkis
       61 ksdlsvliig esgtgkells qsihnasnrs nqpfiavnca avpdsllesq lfgyekgsft
      121 galregkkgl felanngtif ldeigdmppl lqtkllrvlq ekqvmpigsh nvinidvrvi
      181 aatnknllkm iregkfredl yyrlnvlpid vpslrnrked iitlmnfflk nnirlspevi
      241 tilekynwpg nirelqnvas yvslmcdsmv frddlppyir vecannyedg fgytrkefee
      301 ilrilyerre sssgigrgfi iekliqegie iseskvrkvl sylsecgyis sksgrggsqi
      361 tsegiklynn i
//
LOCUS       WP_284927855             313 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284927855
VERSION     WP_284927855.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..313
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          77..313
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 ffdggkfigg ksivfsiigi ifliilvsgi aygywvtkci snitsavsdi skrsylpvni
       61 kgvfadiyns lnilneeihk sdeiqnktdi mreewisnit hdlktplspi kgyaelltds
      121 stnyspekvy kyasimlkni eytntlindl kltyqlkngi iplnknnydl vrflkelsid
      181 ilnypeyesn ivefksnidn infdfdctll krafsnlivn aftygdkntk vcvhvtlner
      241 ieiiisdngk gmsreeasnl fnryyrgsnt kqkiegtglg laitkqiiev hggnisvesi
      301 pglgssfyit fpi
//
LOCUS       WP_284928105             576 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Candidatus Phytoplasma sp. AldY-WA1].
ACCESSION   WP_284928105
VERSION     WP_284928105.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phytoplasma sp. AldY-WA1
  ORGANISM  Candidatus Phytoplasma sp. AldY-WA1
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Acholeplasmatales;
            Acholeplasmataceae; Candidatus Phytoplasma.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 576)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Candidatus Phytoplasma sp. AldY-WA1"
                     /db_xref="taxon:2852100"
     Protein         1..576
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=67826
     Region          16..>571
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 megqlikkle neediykelm vqinsyitdk dilkkihkay llaqlkhkkq kretgedfii
       61 hpirvtqila dlksepntlm agllhdvled tdltfdelks sigedvayiv erttkltkiv
      121 fnqrqrqien qqkmflaman dirvvlvkls drlhnmqtlk imrpvkrlri seetltiyvp
      181 lahrlglfki kseledlsfr yinpeqyyrm srlinmkkne reksiqqiid nirilfvqsn
      241 iqnfsisgrs kniysiykkm kqrkvsfeei fdllairiiv devdecyrcl giihsnyspl
      301 plrfkdyiai pkpnlyqslh ntvlskdgtl fevqirtkkm deiaekgiaa hwgykenkiy
      361 skqdkqleia kklrwyqeli kitkdsdndl hknsqnfvds ikndiltenv yvftpkqevy
      421 elpkgsttid faffihssig yrmtgaivng kivpleyilk ngdiisirtn knifrvnkkw
      481 lnivktsyvk klikkflnke nielvkngke ildkelynhk idfvidkafl aknfrkqyiq
      541 ninelyiaia nkkinchlvi tkinsflamk krfqkk
//
LOCUS       WP_284928259             393 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Clostridioides difficile].
ACCESSION   WP_284928259
VERSION     WP_284928259.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 393)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..393
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=44597
     Region          <182..391
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mktprninst vvfiifcliv tflltviltt itsfneynvl skalgasyey npkstesilk
       61 slknssdkdf ktgneilskh gyskstfwsk nffyflvisf giistmatvv yiikhrtnkq
      121 klsrinnltq yleevnlgke svllrcedef shledeiykt vgelrcskef alkerqtlsd
      181 nladiahqlk tpitsmslma qllsencpde eidyinrltn qisrlerlvs slltlsklda
      241 stlifeskli dvhslltyai epiegslrek hqtftieasp svefeidinw tleallnilk
      301 ncsehiedgg yivayysqnp lyveiiiedn gkgfaqeelp yifnrfycgk naskdsigig
      361 lalsksiier qngtihaenc hnggarfiik fyt
//
LOCUS       WP_284928362             240 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Candidatus
            Phytoplasma sp. AldY-WA1].
ACCESSION   WP_284928362
VERSION     WP_284928362.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phytoplasma sp. AldY-WA1
  ORGANISM  Candidatus Phytoplasma sp. AldY-WA1
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Acholeplasmatales;
            Acholeplasmataceae; Candidatus Phytoplasma.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Candidatus Phytoplasma sp. AldY-WA1"
                     /db_xref="taxon:2852100"
     Protein         1..240
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27648
     Region          54..240
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 micwgflgff isiivawifi lfflfiamml skrfsvdhpf rqkiissisk liirffriki
       61 vvhnkdlipl qnkliiysnh ktnfdpfiia sifprtisft pkdelyrgki gwllsyyfna
      121 ancikiirgn nketiknvlk ginnikknma mvvfheggii hktsdkivss sdgsfkiavk
      181 sqsnilpitl kgacamrgkc wfkrkkvdvv ihepinyenf knkntqeinr evtqiinsvl
//
LOCUS       WP_284928952             578 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284928952
VERSION     WP_284928952.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 578)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 578)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 578)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..578
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <158..574
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 ifitfllnqi yllllpipaa lvsfyvmaii yqdirymkkr llflsiplii ciilsitnpf
       61 thilfglske tgyirgcgyv atfasfffya iysaflsfky rkamheskiw airgflivsi
      121 vaiilqaifl qylltgtaca csllltylsm qnrgliiddl tgvlnrqsfi qeldlninte
      181 qsgfiitial ddfkfmnetf gtkngdialk evgkyliqih dvnhvyrigg difsivvnsq
      241 lgiepddiir kieerfkkpw lveeisfnla tsiavvyype naettedviv aidfsiheak
      301 rsesrrvvya dasisekikk khviknclke alkndgfevy yqpifsnsrg rftsaeallr
      361 lehkelgfip pdefipiaeq tglinsiglv vfekvcrfia sdefenlkld niavnlsvvq
      421 cmqknladdl lylmnkynvs ptkfkleite tvamgsfnii ketmerlidl gvkfalddfg
      481 iaysgvtnml slpfsvikld ksliwsmned srhkltveti ialinklnmk avaegvetik
      541 caedliamec eylqgyyfsk pvpedvfknl lkentfts
//
LOCUS       WP_284928967             252 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator, partial [Clostridioides
            difficile].
ACCESSION   WP_284928967
VERSION     WP_284928967.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>252
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          <148..247
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 meelkdfler qlnkkiniyp yenqkldass hlvtfnnaiy vidfldknnl dnlkgnfyli
       61 yqshidfeyl knifynlfed iniiqhngff ivnskynldi nvttqniiet etyqstyify
      121 lgeldskadf dfrlqlcsdl lphiikdnae nkflnlfdli ryktldline dnilnklidf
      181 nkiksideel lytgikfinn dlnisktsts mflhrntlvy rlekineilg fdlknfenam
      241 ifylsvksyf ly
//
LOCUS       WP_284928984             172 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284928984
VERSION     WP_284928984.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..172
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <1..170
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 kldflmqsmv ktsrletgii tlskkknsiy etiatalsgi lfdaekknie vtvdcdpnly
       61 iihdkkwtse aifnildnav kytssngkir vatecwvmyt kidiidngkg isesrqaeif
      121 krfyreedvh diegigigly lsrkiislqg gyikvtsdig kgstfsiflp nk
//
LOCUS       WP_284929030             389 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Bacillus subtilis].
ACCESSION   WP_284929030
VERSION     WP_284929030.1
KEYWORDS    RefSeq.
SOURCE      Bacillus subtilis
  ORGANISM  Bacillus subtilis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Bacillus subtilis"
                     /db_xref="taxon:1423"
     Protein         1..389
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43057
     Region          8..385
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mvqkrnhflp yslpligkee iqevtetles gwlskgpkvq qfekefaafv gakhavavns
       61 ctaalflalk akgigpgdev itspltfsst antiihtgat pvfadident lnidpvklea
      121 avtprtkavv pvhfggqscd mdailaiaqn hglfvledaa havyttykqr migsigdata
      181 fsfyatknla tgeggmlttd deelankirv lslhgmskaa wnryssngsw yyevespgyk
      241 mnmfdlqaal glhqlkrldd mqkrreeiag ryqtafqqip glitpfvhdd grhawhlyvl
      301 qvddkkagvt rsemitalkd kynigtsvhf ipvhihpyyq kqfgykeadf pnamnyykrt
      361 lslplypsms dddvddviea vrdivkgad
//
LOCUS       WP_284929068             468 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Acinetobacter baumannii].
ACCESSION   WP_284929068
VERSION     WP_284929068.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..468
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50615
     Region          2..439
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 msqnensnna faieshsidy vapserngkv rdlftlwfct niaplavitg amsiltfnln
       61 ivsallaicc ghffgaaila ltsaqgpqvg ipqmiqsraq fgrygallvv lfttliylgf
      121 fisniilsgk tlhtvvpaip vptatvigai aattigvigy hfihkfnkig twfmggslli
      181 glmimvphin advlakgsfn mkgwfarfgl cavwqisfsp ytsdysrylp ksigiykpfi
      241 ftylgaslgt ifamafgtia vsigsttdam eavksgtglf gyvlmilflc niighnamnl
      301 ygavlscits iqtfagqwmp srnirvvlsi ivlvlatlta lwassnfisf flnvifallf
      361 ilvpwvsinl ldfyvvnkks ydiqsifard ggiygkfnak altayfigia vqipflknaf
      421 ftgaladvip dadiswvigl vvslvvyyvf nlgkikcsap alnaklpq
//
LOCUS       WP_284929192            2149 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Acinetobacter
            baumannii].
ACCESSION   WP_284929192
VERSION     WP_284929192.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..2149
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         <1..2149
                     /product="beta strand repeat-containing protein"
     Region          <7..1322
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          864..>2137
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 gpdavdgtvv nvngtnytvt aadlangyit atldataadp vtgqivihae avdaqgnvdv
       61 adadvtltid ttpqdlitai tvpedlngdg ilnaaelgtd gtfnaqvalg pdavdgtvvn
      121 vngtnytvta aditngyita ilaataadpv tgqivihaea vdaqgnvdva dadvtltidt
      181 tpqdlitait vpedlngdgi lnaaelgtdg tfnaqvalgp daidgtvvnv ngtnytvtaa
      241 ditngyitai laataadpvt gqivihaeav daqgnvdvad advtvtldvt ppditttvla
      301 idpvtadnil dateaggtvt ltgtltnvpa datttgvvvt ingndytatv daiagtwtvn
      361 vagndlaldp dltvdakatf tdlagnsstl qdtqtytlag sitafdntdh avlspkpalv
      421 gddvslgsts ylvltsvagl dlqlggnslg ftvdaghegd vtfqysglid aavlsdyklv
      481 vqkfntttnq wesihgdans slislhllgi gtgnvpgavl dgldagqyra flaydgllgl
      541 gvlgtlsatm ddydlsvagg yeignaegnv itdpdpttgq vdqvtantyv ssvnghpida
      601 dgetfagtyg titfyqdgsy vyvpnadgsg vgqtdvftyt ltdsvtgatg qanlnivfds
      661 iraadnlvev elnpqyqlvg tetdsafygv llnvgnivdl qlltvdtvdf tigagqegva
      721 tfnfnsliga salgdynvvl qkyndvtgqw eavngtgdrs llnltllgnt ptaqigglte
      781 geyraflsfn glvggavavt lngsvdvynp avitgydvva ahgnlisdpn tngdvdiatp
      841 nsiisevngv avsaspteii gthgtlliya ngdytytpna dsaglgqvdq ftytlldpas
      901 nitsqatfyv hldskvvdmn wdaadpsqpa tvtitavdda vnaaiaaeph lieddralgs
      961 atylallsla ginlqaplpf vnstvefnvg agetgtatfk ysslinegal gdyqlvvqkf
     1021 ntatnrwesi tgsseaslln lsvlgigvna tpgvvvegld egqyrafmty nglygksilg
     1081 tlsgtmdvyd pnqidftgla segnvitglg vgtnadavtg ytivdsvtvn gvttnvdpnt
     1141 gtiiqgqygt lqifangdyi ytpnntnanl glvdhftytl adplggnisa sldftignst
     1201 pviavddlav avvnpeylqi gndvavdsyl yvallsltdn fdfqlggqgi dftltdstln
     1261 dvtfnysali daslladyvl vvqkfdtatn qwvavngtge adllslaafg gnsvtlegla
     1321 agqyraymty agsgvgvsll gtlsvqkdvf datnitgyst qvaegnvihd vglnghadta
     1381 sgfstvtsve fngtafavna tgvttivgdh gtlsiyangn ysyqpngeaa slgqvdqfty
     1441 tlsdglntsq atlylhidsd avdmtwntsd psqpavitvt pvdaidnvvs agvdivpqge
     1501 lgvavgsaty lalvgitedl nvsllgtpsv aftidaghea dvtfayapvl slslfndykv
     1561 vlqqkgadga whnidggsst gllnigllgn ggigvtvpdl gqgeyrafmv ytglgvgilg
     1621 tmsvvkddfd ytvaptntav vadgnvltdd vttlttqvtt vtsevvgalp qtvgtdtvin
     1681 gaygtlvist nghytytpnt tdlsaigkvd sftytirdvl tgatdtatlh vqvgspdvti
     1741 awdaanpand gvvqltanpd hvvtttdfsn aadlpvdvas pvvsvnligs nsvvsdqfvv
     1801 gagtvanidl savytaqpla svlptvsyvi qswngtawvn tiysgsqtal gsvatiqags
     1861 vafqdtvehl aagtyrvqyt ltgvslgats ldtnvstttv hldtyrsdwi sgnvlagdni
     1921 ggvadtgils hegaklqvwd naqnayvdav gqtintgngv limqsngeye yrpndvtttt
     1981 qlastdsiny kivsvtggve sqstltidlt htdynllyts tsandtfttg tgsdtviyql
     2041 lngtaatann gantggngvd twtdfhvgnv atdkqadlid iralldgdqt danigqylnv
     2101 ttsggnttiq idrdglsgli pgnnfttllv lqgvtttete llnngqily
//
LOCUS       WP_284929406             302 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284929406
VERSION     WP_284929406.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>302
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          10..>284
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 msnriknihy gtqrqqlknl tkkeyqalre mcflaknlyn vgtynvrqhy fnqgehlnye
       61 anyhvckene nykllnsnia qqilkevdss frsffglikl akegkydfrg ikspkyldke
      121 gffsiiigqi rikedgilnv pmspafkkly gkvsikvpqn ilekkikeir iipkhkarff
      181 eiqycyeipk seevsnqkna laidlglenl ctcvtnlgds fiidgkrlks vnqwankqnd
      241 kiealklkkn itaitrkqfk vwnkrnnqvk dyvnktcfyi idycvknnig nlivgynakl
      301 ek
//
LOCUS       WP_284929636             343 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Bacillus subtilis].
ACCESSION   WP_284929636
VERSION     WP_284929636.1
KEYWORDS    RefSeq.
SOURCE      Bacillus subtilis
  ORGANISM  Bacillus subtilis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Bacillus subtilis"
                     /db_xref="taxon:1423"
     Protein         1..343
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35868
     Region          14..341
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mklrfgvtaa ekkawivfli llgltaavli isaglgqrfi ppwdvaktff gagskldelm
       61 imsfrmpril talcagvcla aagailqglv rnplaspdii gitggaavav vllmmffsdr
      121 sssltislsw lpaaafigas avglivylla ykngastfrl vligigfsms aqamttllmi
      181 kgpiyrasqa nvyitgsvyg snwqhvkiai ilsvillfic fvalknmniq vlgediaaga
      241 gsavqrnrff llllstaltg cavsvagtig fvglmaphia rrlvgssyga llpasaliga
      301 llvltadivg rtlfapvevp agvftaaisa pyfiyllykt rns
//
LOCUS       WP_284929729             145 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284929729
VERSION     WP_284929729.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..>145
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          1..>145
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 lkepdkfslq nalkdldnay kkffkekagf pkfkskkinr fsyktnftng nimycgqyik
       61 lpklgmvkvr dkqvpqgril natiskepsg ryyvslcctn vdievfentn nqigldlgik
      121 efcisscgdf ienpkylkks lnkla
//
LOCUS       WP_284929736             381 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284929736
VERSION     WP_284929736.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..381
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          <2..339
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
     Region          309..>375
                     /region_name="COG1693"
                     /note="Repressor of nif and glnA expression
                     [Transcription]"
                     /db_xref="CDD:441299"
ORIGIN      
        1 nvnkksifsm gnkagiyynl qeityikkle qnltnklreq gqiarytfkd iktknknmvk
       61 cvelakkisk sdlsvliige sgtgkellsq sihnasnrsn qpfiavncaa vpdsllesql
      121 fgyekgsftg alregkkglf elanngtifl deigdmppll qtkllrvlqe kqvmpigshn
      181 vinidvrvia atnknllkmi regkfredly yrlnvlpidv pslrnrkedi itlmnfflkn
      241 nirlspevit ilekynwpgn irelqnvasy vslmcdsmvf rddlppyirv ecannyedgf
      301 gytrkefeei lrilyerres ssgigrgfii ekliqegiei seskvrkvls ylsecgyiss
      361 ksgrggsqit segiklynni n
//
LOCUS       WP_284929769              77 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284929769
VERSION     WP_284929769.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>77
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
     Region          <13..75
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 maiqliiqns gnissqeisk kvfyssrhln rlfnqylgls mksfsrlvri nksikllnnn
       61 ktswmsicne lgfydip
//
LOCUS       WP_284929775             346 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator, partial [Clostridioides
            difficile].
ACCESSION   WP_284929775
VERSION     WP_284929775.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>346
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
     Region          18..>346
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 miclnkrqen llttlllkee finvnkiand fecsertirn dckyidewls tfcnayikrk
       61 pnigikfsgd gtdkilvnqk lrgevkrvns elhkqveiln lllcnnkkvt lndlsnklyi
      121 nknivreeis klsvalnnyn lnistkkgsg iyiegdekdi rimlvsflfk yidkyrlnid
      181 eieyfhivdi iivknimlti eedmdirltd isfkqlmlfl liniirirlg nslkvsntkk
      241 elklkmlild iedelksnls ivlnyeeklf ieslilgmnk qinsnnikks lylneelasy
      301 tkkiinlvse esginfnndi llyeqlichl nvtmhqmksn vylenp
//
LOCUS       WP_284929778              80 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284929778
VERSION     WP_284929778.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..80
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          <8..68
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Region          33..56
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 laitnkllgn kdeaikyykk yintytkndq yyddsyyelg mlyydngdlk naqqtfyslr
       61 sevpdsmynn skikeilsek
//
LOCUS       WP_284929978             400 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Clostridioides
            difficile].
ACCESSION   WP_284929978
VERSION     WP_284929978.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>400
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
     Region          29..390
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mnqeyvkgnp iftninkvpr qfpyltddid tdviivgggv tgcicayyla knniksvile
       61 kgriahgsts vttsllqyel ddnlidltev mtlkdalkay nlctsaleel dtfielygnk
      121 cdyakrdtll ytanklevka ikeeynlrke ngfdveyide stnpfsfdlk sgliaknggr
      181 eldpykyshh lidvslkngl qvyentevkk vdlsndkvta evsyghkvhg kklivatgyn
      241 tslftkrnfa tksntfniat kplkniaswk nnilirdncd pynylrttkd nrliiggedv
      301 sfddienetl anekydileq rlksmfkdik dieveykycg cfastldnlg figpdnknnn
      361 lwyclgygan gilfailggi mlselylgkq nknmklfkvd
//
LOCUS       WP_284930008             392 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284930008
VERSION     WP_284930008.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..392
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <1..387
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 dvnkfkyine mfgyaegnki lihisqvlnn ntnkyeicar mdndhfilli acntedelln
       61 rlskinkeic nlnttnssky kivmssgiyk itkkddikki dllidrania akskkekyeh
      121 sysffnedtr nrlykekrle dnmnkalekg efivyyqpky slddvneieg aealirwnsp
      181 efgfispidf vplfekngfi vnidmfvfee vcktlnkwin kgytpvpisv nmsrvhlyrd
      241 nfienitdli skynispefi eleltesvvf dnlnilidim kkikeigfli smddfgsgys
      301 slnllkdlsf dilkldrgfl iettdtkrgk iiiskivema kaidikvice gvetyeqvef
      361 lkeigcdkvq gylfakpmvl defekhlnfk fd
//
LOCUS       WP_284930065             592 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284930065
VERSION     WP_284930065.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 592)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..592
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <139..584
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 hnvgdygkli nyvgivrgas qrltklemnh qpndelieyi deilqelitg hgdyglvitd
       61 cneynedlll lekkwedlni eikkvrmkeq nnqllsisee ffslandtvf kienfskeks
      121 nylmtliiii siigilacii lilqyskkmv rleklnvdlk niaykdeltg vntiekfkld
      181 anqnicihkd kkfavfyidf enfkyindif gydygdmilk ryanlmmndi gkyeifarei
      241 adrfvalrcy vdkedlvvrq rdvdnelini tneiknkhsi tvvsgiccie dvneklsidg
      301 linranfaqk tvknkpgtny afyndsirkk mieentiksr iheaiekref ivylqpkvnl
      361 hsqkincaea lvrwltpdkg iispaifipv leknffialv dkyvfeevck wirkrldenk
      421 pfvqisvnvs riqfyntkfv etysniqnky ripkntieie ftesvafenq khlleiihdl
      481 hengftcsld dfgkgyssls vlkdlpfdvl kldsmffkas ldkdkekivi knivhmlkel
      541 nittvaegie ckeqveflrd igcdlvqgfv fykpmpilef ekildkefvy ns
//
LOCUS       WP_284930113             418 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [Citrobacter].
ACCESSION   WP_284930113
VERSION     WP_284930113.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..418
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=47872
     Region          2..408
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mklnarqiet akpkekaykl adggglylev tprgskywrm kyrrpndkke drlafgvwpt
       61 vtlsdarakr deakrflsag ldpkeqqrga qaeadgaftf etitrkwhtg mlkrwtetha
      121 navlrsleqy ifphignsdi rklttrqlla avhevdatak hdvakrlrqr itsvmryavq
      181 nglidsnpal dmagaltaak vkhrpalspa ripellsria ayrgraltrl avemtlltfv
      241 rsselrfarw defdlaravw nipaqreave gvryswrgmk mkephivpls kqmlkileqi
      301 qnlcgdsdrl fpgdhdprkv msentvnkal rqmgydtqte vcghgframa cgalvesgrw
      361 sydaverqms haerndvraa ythtseylee rrlmmqwwad yldanresfv tpydfsli
//
LOCUS       WP_284930115             370 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Citrobacter].
ACCESSION   WP_284930115
VERSION     WP_284930115.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..370
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=41521
     Region          5..77
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          184..275
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mfnserlria rerrgltqra laeateltsk tisnyekagi fdaiasdtme risavlgypi
       61 effrdrdvpt lspeavsfra mtkltaqkrd salgagklaq elsawideqf klpkpnvpdc
      121 sfdgyseper aaravreswg igelsisnli hlleangvrv fslaencvev dafsfwmdek
      181 pfmllntmkt persrfdaah elghlvlhkh stnngrqael dadrfasafl mpersilasv
      241 prmpsldlli slkknwkvsl aalvrrtfdv glstewhyrq lsielarrgf rtgepqgmee
      301 rekslvldkv fsalrskgvk rgeileqlrl padeasaltf snsffmeain ggklctqesg
      361 irpshlrlvk
//
LOCUS       WP_284930212             127 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284930212
VERSION     WP_284930212.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..127
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <1..125
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 kknievtvdc dpnlyiihdk kwtseaifni ldnavkytns ngkirvatec wvmytkidii
       61 dngkgisesh qaeifkrfyr eedvhdiegi giglylsrki islqggyikv tsdigkgstf
      121 siflpnk
//
LOCUS       WP_284930308              64 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Bifidobacterium
            dentium].
ACCESSION   WP_284930308
VERSION     WP_284930308.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium dentium
  ORGANISM  Bifidobacterium dentium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 64)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 64)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 64)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..64
                     /organism="Bifidobacterium dentium"
                     /db_xref="taxon:1689"
     Protein         1..64
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=7156
     Region          4..60
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 metigvadva kmlgitesav ynrrcyhpeq lppsikvgnr vryrpdtvka wmddheevan
       61 dank
//
LOCUS       WP_284930358             496 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284930358
VERSION     WP_284930358.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 496)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..>496
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <25..446
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 lskeldsrnf klktlneidf fskipnrefm yqyiddcisk nihigimlln idnfklfndi
       61 ygylvgenll itltqnllhf ipeskgivay lkgegflivl pnvsnkelnn mgatiiesar
      121 elkiklpnek eiysnvtfsi gstiwngepn mttlmlfnqv ysalkkakse gknryilfdf
      181 kdnsfynkle ndkeflseis hvlqtkqiev fyqplynikn ntivgceala rwrhpikgll
      241 tpdkfmplfe qfgliteldl hlfeenckni rrwidnndvf vpiccnfsrl hffnpnfpsm
      301 lkgitekysv stsnfsieit enilientnt iiqqlaelrs ygfsvsmddf gsgyssfgml
      361 qnlpfdiiki driflshnln dfknttilys iiniaralgm ltvcegvete qhvefiksin
      421 cdiaqgyyya kpmeckefek llskennsek mfikysdigk sliekifdgf fimqdmkklr
      481 anvtediqwf dfynkt
//
LOCUS       WP_284930432             115 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284930432
VERSION     WP_284930432.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..115
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <1..115
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 dninfdfdct llkrafsnli vnaftygdkn tkvcvhvtln erieiiisdn gkgmsreeas
       61 nlfnryyrgs ntkqkiegtg lglaitkqii evhggnisve sipglgssfy itfpi
//
LOCUS       WP_284930586             572 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Acinetobacter baumannii].
ACCESSION   WP_284930586
VERSION     WP_284930586.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..572
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=61956
     Region          4..455
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          506..571
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(529,538..540,547)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            539
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mntekllian rgeiavriih acrdmgiasv alyadddins mhveladeaw glagataset
       61 ylnipaiiev akkskatmvh pgygflsera efaqavidag lkwvgpspsa ieklgdkiea
      121 rkiaasvgap lvqgtqdpln naeealefak qyglpiaika afggggrglk vawkleevke
      181 lyesavreak aafgrgecfv eqyldkprhv eaqviadqhg nivvlgtrdc slqrrnqklv
      241 eeapapfisd eiyqqilssa knicqaanyv gagtveylls rdgklsflev ntrlqvehpv
      301 teetskvdlv veqirvaqge vlsiketpka qghaiefrin aedpargfip afgvlslfea
      361 pfghgvrvdt gvrtgslvss hfdslmakli vsgptrevai arakralkqf knegvasvld
      421 fhravlnepg ftdefnvhtr wiendfkqel kptkrgipnh qqpmllsyie idgklhrlgl
      481 pagmfaqgpa tavqaqiaep evsaehllap ingvisawkv engeqvtegq vvaimeamkm
      541 evqvlahrsg viqigaekgt tchaetvias ih
//
LOCUS       WP_284930739              89 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial
            [Bifidobacterium dentium].
ACCESSION   WP_284930739
VERSION     WP_284930739.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium dentium
  ORGANISM  Bifidobacterium dentium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10475648
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Bifidobacterium dentium"
                     /db_xref="taxon:1689"
     Protein         <1..89
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          7..71
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 qklleqkhlg vaikqvlaev dmtqialadr sgiprntlnr kinvgifnfd elrriacavn
       61 rplssivasa erldsaedai palgeggae
//
LOCUS       WP_284930882            2324 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Acinetobacter
            baumannii].
ACCESSION   WP_284930882
VERSION     WP_284930882.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..2324
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         <1..2324
                     /product="beta strand repeat-containing protein"
     Region          1..1497
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          1039..>2312
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 aipvtgegpv aihaeavdaq gnvdvadadv tvtvdtvpad ligaitiped lngdgilnad
       61 elgtdgsfna qvalgpdald gtvvnvngtn ytvtaadlan gyitaaipvt gegpvaihae
      121 avdaqgnvdv adadvtvtvd tvpadligai tipedlngdg ilnadelgtd gsfnaqvalg
      181 pdaldgtvvn vngvnytvta adlangyita aipvtgegpv aihaeavdaq gnvdvadadv
      241 tvtvdtvpad ligaitiped lngdgilnad elgtdgsfna qvalgpdavd gtvvnvngtn
      301 ytvtaadltn gyitatldat aadpvtgqiv ihaeavdaqg nvdvadadvt ltidttpqdl
      361 itaitvpedl ngdgilnaae lgtdgtfnaq valgpdaidg tvvnvngtny tvtaaditng
      421 yitailaata adpvtgqivi haeavdaqgn vdvadadvtv tldvtppdit ttvlaidpvt
      481 adnildatea ggtvtltgtl tnvpadattt gvvvtingnd ytatvdaiag twtvnvagnd
      541 laldpdltvd akatftdlag nsstlqdtqt ytlagsitaf dntdhavlsp kpalvgddvs
      601 lgstsylvlt svagldlqlg gnslgftvda ghegdvtfqy sglidaavls dyklvvqkfn
      661 tttnqwesih gdansslisl hllgigtgnv pgavldglda gqyraflayd gllglgvlgt
      721 lsatmddydl svaggyeign aegnvitdpd pttgqvdqvt antyvssvng hpidadgetf
      781 agtygtitfy qdgsyvyvpn adgsgvgqtd vftytltdsv tgatgqanln ivfdsiraad
      841 nlvevelnpq yqlvgtetds afygvllnvg nivdlqlltv dtvdftigag qegvatfnfn
      901 sligasalgd ynvvlqkynd vtgqweavng tgdrsllnlt llgntptaqi ggltegeyra
      961 flsfnglvgg avavtlngsv dvynpavitg ydvvaahgnl isdpntngdv diatpnsiis
     1021 evngvavsas pteiigthgt lliyangdyt ytpnadsagl gqvdqftytl ldpasnitsq
     1081 atfyvhldsk vvdmnwdaad psqpatvtit avddavnaai aaephliedd ralgsatyla
     1141 llslaginlq aplpfvnstv efnvgagetg tatfkyssli negalgdyql vvqkfntatn
     1201 rwesitgsse asllnlsvlg igvnatpgvv vegldegqyr afmtynglyg ksilgtlsgt
     1261 mdvydpnqid ftglasegnv itglgvgtna davtgytivd svtvngvttn vdpntgtiiq
     1321 gqygtlqifa ngdyiytpnn tnanlglvdh ftytladplg gnisasldft ignstpviav
     1381 ddlavavvnp eylqigndva vdsylyvall sltdnfdfql ggqgvdftlt dstlndvtfn
     1441 ysalidasll adyvlvvqkf dtatnqwvav ngtgeadlls laafggnsvt leglaagqyr
     1501 aymtyagsgv gvsllgtlsv qkdvfdatni tgystqvaeg nvihdvglng hadtasgfst
     1561 vtsvefngta favnatgvtt ivgdhgtlsi yangnysyqp ngeaaslgqv dqftytlsdg
     1621 lntsqatlyl hidsdavdmt wntsdpsqpa vitvtpvdai dnvvsagvdi vpqgelgvav
     1681 gsatylalvg itedlnvsll gtpsvaftid agheadvtfa yapvlslslf ndykvvlqqk
     1741 gadgawhnid ggsstgllni gllgnggigv tvpdlgqgey rafmvytglg vgilgtmsvv
     1801 kddfdytvap tntavvadgn vltddvttlt tqvttvtsev vgalpqtvgt dtvingaygt
     1861 lvistnghyt ytpnttdlsa igkvdsftyt irdvltgatd tatlhvqvgs pdvtiawdaa
     1921 npandgvvql tanpdhvvtt tdfsnaadlp vdvaspvvsv nligsnsvvs dqfvvgagtv
     1981 anidlsavyt aqplasvlpt vsyviqswng tawvntiysg sqtalgsvat iqagsvafqd
     2041 tvehlaagty rvqytltgvs lgatsldtnv stttvhldty rsdwisgnvl agdniggvad
     2101 tgilshegak lqvwdnaqna yvdavgqtin tgngvlimqs ngeyeyrpnd vttttqlast
     2161 dsinykivsv tggvesqstl tidlthtdyn llytstsand tfttgtgsdt viyqllngta
     2221 atanngantg gngvdtwtdf hvgnvatdkq adlidirall dgdqtdanig qylnvttsgg
     2281 nttiqidrdg lsglipgnnf ttllvlqgvt ttetellnng qily
//
LOCUS       WP_284930947             250 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfite exporter TauE/SafE family protein [Clostridioides
            difficile].
ACCESSION   WP_284930947
VERSION     WP_284930947.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..250
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26784
     Region          1..250
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mfaiiflcig gflaafvdsi agggglismp vlmaigvpvh laigtnkfaa sagcissayr
       61 yaksgkinnn llkklvpfti agsilgvrcv lsisedilnv lvvvmiliva iytfvsknlg
      121 qednfesink knlrlgmlma limgfydgff gpgtgtfltf gfikiygydf lhasantkil
      181 nltsnitsll lfmingqvdy kiaivfalvm lmgayvgakv aikkgskmik piflvmalfm
      241 vvklvyqtlv
//
LOCUS       WP_284930964             657 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF2345 domain-containing protein, partial [Acinetobacter
            baumannii].
ACCESSION   WP_284930964
VERSION     WP_284930964.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         <1..657
                     /product="DUF2345 domain-containing protein"
     Region          <1..657
                     /region_name="COG4253"
                     /note="Uncharacterized conserved protein, DUF2345 family
                     [Function unknown]"
                     /db_xref="CDD:443395"
ORIGIN      
        1 adalqqeegs gsvqgtqkhs ehydnaslnl edawhvspaw mqdlngedqa tasgnsqieq
       61 lnqhinayhh lsskqftvag nvrdaqvgyw felndhpeld qhdsadkefl ilskhyynqn
      121 nlpkelqqql erllpqgklk aaqldsqnpe qrhfaelnvv rrnikavpey nplehrpaah
      181 pqrarvvgle gesihvdqwg rikvrflftr addhshdgga gsndndtdsa wvdvltpwag
      241 agygarflpr vgeivvidff dgnvdrpfvv griheaerhp tqfdqkgqlp dtkklsgirs
      301 eevdgkgfnq lrfddttgqi saqlqsshaa sqlnlgnlsh pkdkaesdgr gegfelrtdq
      361 wgavragsgl lvsthkqdqa qgvhldasea kqqiegglnn akalsevakn qqtdplemle
      421 nlktfieqie ekdqdkaaaf kqalmiltap nsialasned ihlsadgqln qtagdsinls
      481 tqknliahaq nkislfaaqq garlyagkgk veiqaqgdga dliarkavqv istedkieat
      541 aakeivltag gsqvkitgsg ifmttsgkfe vkagqhlfmg ggsvnsslpy lpeqgkqkyg
      601 vwfdvmdkqg nklkpgteyi ifdehdkeie rgkldrtglv kleteepnkq ykihvvn
//
LOCUS       WP_284931013              42 aa            linear   BCT 25-DEC-2024
DEFINITION  thioredoxin family protein, partial [Clostridioides difficile].
ACCESSION   WP_284931013
VERSION     WP_284931013.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 42)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 42)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 42)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 42)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..42
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>42
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
     Region          1..>42
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 mvkiinnnef inevenkdgl vvvdffatwc gpckmlspiy ea
//
LOCUS       WP_284931031             100 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284931031
VERSION     WP_284931031.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..100
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <1..100
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 livnaftygd kntkvcvhit hitlneriei iisdngkgms reeasnlfnr yyrgsntkqk
       61 iegtglglai tkqiievhgg nisvesilgl gssfyiifpi
//
LOCUS       WP_284931147             464 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator, partial [Clostridioides
            difficile].
ACCESSION   WP_284931147
VERSION     WP_284931147.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>464
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
     Region          8..>463
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mhkrlltlfk llnesddkit cktlsnhlkv sertirndit singtlekng aiikikkgeg
       61 yyidilnlal yqqylalisd dimdsseipd spiernqyil kyilynntyi kledlansly
      121 vskftilndi krikpillky nlilvskpyy gvkiegkeid irrcisnnmi nrnfenyiig
      181 itdreielfn nidlielqkv vlseinkfni nfldfnlknf iihlaitisr ildgycldnv
      241 ldvvltdfqs nttvenifny ieskytiiis kadrvylynh fitksslldn vsnrvdtkii
      301 eyveeilevi nnqytfdlrn dsvlfddlvl hfksilnsks ynlnkvnpli ntiksnypla
      361 feitlnaiek vfknsiyslt edeigyvslh igagierffq nnikcknvvl vcgsgygssr
      421 llevqlnkvf hdkinilqcl sfnqflasel sdvdiiisti plnh
//
LOCUS       WP_284931338             665 aa            linear   BCT 25-DEC-2024
DEFINITION  BCCT family transporter [Citrobacter freundii].
ACCESSION   WP_284931338
VERSION     WP_284931338.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..665
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73566
     Region          1..510
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 msenetipkk shsqinkavf ftsallifll vtfaaafpdv adknfkllqq qiftnaswfy
       61 ilavalills vtflglsryg diklgpdhaq pdfsyhswfa mlfsagmgig lmffgvaepv
      121 mhylsppvga petvaaakea mrltffhwgl hawaiyaiva lilaffsyrh glpltlrsal
      181 ypiigdriyg pighavdifa vigtvfgvat slgygvlqvn aglnhlfgvp inetvqvili
      241 vaitglatis vvtgldkgir ilselnlgla llllalvlcl gptvlllksf ventggylse
      301 lvsktfnlya yepkssnwlg gwtllywgww lswspfvgmf iarvsrgrti refvtgvlfv
      361 pagftlmwmt vfgnsaiyli mnqgatdlan tvqqdvslal fnflehfpfs svlsfiamam
      421 vivffvtsad sgamvvdtla sggvantpvw qrifwaslmg vvaialllag glsalqtvti
      481 asalpfsvil lisiygllka lrrdltkres lsmatiapta arnpipwqrr lrniaylpkr
      541 slvkrfmddi iqpamtlvqe elnkqgtish isdaaddrir levdlgneln fiyevrlrgy
      601 ssptfalaam dndeqqtdqh ryyraevylk eggqnydvmg wnqeqlindi ldqyekhlhf
      661 lhlvr
//
LOCUS       WP_284931341             267 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284931341
VERSION     WP_284931341.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..267
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          46..249
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 ikivtdkmmk ldkktrlkvs sndevgelkq qindlystll rtiddlefkn keilkleklk
       61 ydffkgashe lktplaslki ilenmkynig kykerdiyin ecieivdslt knisqilsvh
      121 sienlnndee ylkindtled ilkkyeilan qkkitvnnyi ldenvyigkt alkiilsnli
      181 snavkytdvn gvinigivnd wlyiensygn nrisnmdkif dvkfdlnken snglglyivs
      241 nilnnyniey kalqdeeffi fkikifs
//
LOCUS       WP_284931374             178 aa            linear   BCT 25-DEC-2024
DEFINITION  YczE/YyaS/YitT family protein, partial [Clostridioides difficile].
ACCESSION   WP_284931374
VERSION     WP_284931374.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..178
                     /product="YczE/YyaS/YitT family protein"
     Region          <1..148
                     /region_name="YczE"
                     /note="Uncharacterized membrane protein YczE [Function
                     unknown]; COG2364"
                     /db_xref="CDD:441931"
ORIGIN      
        1 imvgvvivil davfgenigw gtllnmtfig ifidlvifsg viphanntyi gvfmvvigii
       61 laaiasflyl gvclgsgprd glmialqkkt nksvrlvrti leilalvvgw llggsvgigt
      121 lvsalglgyv lqivfrifkf dtkllkhrfi iddirewkek kneehkckss ivikneqn
//
LOCUS       WP_284931517             165 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase, partial [Clostridioides
            difficile].
ACCESSION   WP_284931517
VERSION     WP_284931517.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>165
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
     Region          1..>152
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mgvgisrssl agavaklggv gvisgvqigy deedfetnti nanlraikkh iskakeisng
       61 giiginfmva mkeyetyvke avkagvdlii sgaglpnklp slvkgsnvki apivstakaa
      121 nvilkmwdrk ekttadlivv egpkagghlg ysneeldnid sidyd
//
LOCUS       WP_284931518             380 aa            linear   BCT 25-DEC-2024
DEFINITION  metal-dependent hydrolase family protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284931518
VERSION     WP_284931518.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..380
                     /product="metal-dependent hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          11..>57
                     /region_name="metallo-dependent_hydrolases"
                     /note="Superfamily of metallo-dependent hydrolases (also
                     called amidohydrolase superfamily) is a large group of
                     proteins that show conservation in their 3-dimensional
                     fold (TIM barrel) and in details of their active site. The
                     vast majority of the members have a...; cl00281"
                     /db_xref="CDD:469705"
     Region          39..366
                     /region_name="Met_dep_hydrolase_A"
                     /note="Metallo-dependent hydrolases, subgroup A is part of
                     the superfamily of metallo-dependent hydrolases, a large
                     group of proteins that show conservation in their
                     3-dimensional fold (TIM barrel) and in details of their
                     active site. The vast majority of the...; cd01299"
                     /db_xref="CDD:238624"
     Site            order(50,52,203,223,295)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 gtgnsimqnk giiidgdtiv eiediradln eydvydyldk tvmpgimnch vhltmepvgn
       61 pkvyydnvsd velvvntikq ldayldsgvt yirslgcpky vdvqlknlid kgsidgpgiv
      121 tsgpvicmtg ghgyyfgies dgvdecrksa rtvlkngvdc vkimatggvt tdgvepgspq
      181 ltleemkaav deaikagkit athaqgrtgi knavlagits iehgvyldde iidlmlergt
      241 ylvptvaapy filnagkesg iteatlrkce vvaiphkesf lkaykkgiki avgsdagtsy
      301 nehgktyyem klmsdygmdn mdvivaatkt asellkidkn ygtlekgkka dvivvngnpi
      361 edidvladvl avfklgkkvr
//
LOCUS       WP_284931612             106 aa            linear   BCT 25-DEC-2024
DEFINITION  deoxycytidylate deaminase, partial [Clostridioides difficile].
ACCESSION   WP_284931612
VERSION     WP_284931612.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Maley,F. and Maley,G.F.
  TITLE     A tale of two enzymes, deoxycytidylate deaminase and thymidylate
            synthase
  JOURNAL   Prog Nucleic Acid Res Mol Biol 39, 49-80 (1990)
   PUBMED   2247612
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788416
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..106
                     /product="deoxycytidylate deaminase"
                     /EC_number="3.5.4.12"
                     /GO_function="GO:0004132 - dCMP deaminase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006220 - pyrimidine nucleotide metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0009972 - cytidine deamination [Evidence
                     IEA]"
     Region          <2..106
                     /region_name="ComEB"
                     /note="Deoxycytidylate deaminase [Nucleotide transport and
                     metabolism]; COG2131"
                     /db_xref="CDD:441734"
ORIGIN      
        1 senrivstgy ngsisgdkhc sevghemrdg hcirtihaeq nalyycakeg isvkdcsiyv
       61 thfpclnctk aiiqagikhi yyrtgyride yaikllqssn vlytkl
//
LOCUS       WP_284931615             474 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284931615
VERSION     WP_284931615.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..>474
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          29..436
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 lknekfiekl yklsketlsh dflntsldni sklktilymt ideigdglif fntfnkvtfv
       61 nksllnmlel deklikspsl meympksfld kitknlnidn miiyideidk kfilskkpfy
      121 lykniegcli tlkdvnniei leqkirsdsv krgyvakykf nniignssii kdcikkakkm
      181 altdnpilit getgtgkeaf tqsihnhsnr knkpfvainc aslpselles elfgyedgsf
      241 tgakkggkkg lfelahtgti fldeigdmph dlqvkllrvl qekeirkigg tsiipidvri
      301 laatnkdlek liienkfrmd lfyrismftl dlpplrnrle diplllesfl kelpyknikl
      361 dknllealns ytwmgnirel rncieymaym gsnyltindl pqnissklnn nhmssnvsif
      421 ndlsqydkni cisilkslhm kpmgrtklmk fmeynvteye vrnmleylth ngyl
//
LOCUS       WP_284931617             390 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284931617
VERSION     WP_284931617.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..390
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          161..387
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 klyeyqiknt qniagiliek ypndeidivk siynsdyskv sigekafkkf gyglenkmsn
       61 dknfslylks ffkesffifl mmfivvigii yyfiryinkr lskiyfivdk maqenylkdt
      121 teseetsylv eyneyfkegt fskinnclye lnrslkikfi klekekesvk slvtdishql
      181 ktplaslkly ntllieeele edeanefllt nkasinklen linslvnisr leisminikk
      241 edndikntil navksvtpka ksksitlnln efnsriiphd kkwteesifn vldnavkytq
      301 ingeinisve etanyfkiii edngigiekn efnnifkrfy rgsadeiesv egsgvglyls
      361 rrileeqggn iivsskvgig skfslflttm
//
LOCUS       WP_284931915             455 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Clostridioides
            difficile].
ACCESSION   WP_284931915
VERSION     WP_284931915.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..455
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48073
     Region          3..446
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mnlidilnkv dafiwgppll vllvgtgill tvklgvvqit klpralklif saenkgsgdv
       61 ssfaalctal aatvgtgniv gvataikagg pgalfwmwia affgmatkys egvlaikyrt
      121 kdkngqvsgg pmyyivngmg ekwrplaiff aisgilvall gigtftqvns itdainnsfg
      181 idsritgvvl avfvalvvfg glksisnvat kivpfmaiiy vvicgiilis fwnkipetfm
      241 liiksaftpt aatggflgat mslairngia rgvfsnesgl gsapiaaaaa ktewpaeqgl
      301 ismtgtfidt iiictltgfs lvisgvwcsd lngavmtqaa fngaiptfgp illtvsltlf
      361 afttilgwsy ygercfeflf gvkgmngyrt vfvamvllga flklevvwii adivnglmai
      421 pnliallals piivsetkky fehinspenq ikkna
//
LOCUS       WP_284932013            1083 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            fragilis].
ACCESSION   WP_284932013
VERSION     WP_284932013.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=119664
     Region          22..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktiflilc ilcslgamaq kksitgvvmd asgesiigas vvevgttngv itdisgkftl
       61 mvdpngkikv syigyqsqvl dvkgrnsfni klkedsemld evvvtgyggk qlrtkvtnsi
      121 skvseeslkv gvfsnpaqal sgavsglkvt qssgnpgstp tivlrggtew dgsgsplvmv
      181 dgqlrdglnd inpediesme vlkdagatal ygarasngvi littktgkvg kaeinlkakv
      241 gmnyinnpyd flgakdfita irtaydttpw askssldgas aygtgnkygs dlvwnllvkd
      301 sgnefllnkg wqqmqdplns sitllykdik psdynlnnps ltqdynvnms ggndkgtyya
      361 glgynksegl pissfyerys fifngsykla dwitansnfn ynranwrsmp gsqdnegnyf
      421 grimplpptv ryededgnpv lgpnhsdgnq syqpekwlvd nqtdkftmiq sleirpmknl
      481 vikgtanwyy segvyesftk dfetapgkfn ttrassakfe rdfsqtynvv lnynntfaqn
      541 hnidvmlgse yydkktkgfs asgsgaptdd fadlnltdng egkrtidswh sqyrilsyfg
      601 rlnydyqgky llsgvfrydg yssllgdnrw gffpgvsagw ifgkedfikn avpdlsfgkl
      661 rfsygvngna tgigaytlqg synsqkyngn vgyligalpn pglkwektrt tevgldlsff
      721 dnrlnanfty ynrltmdkya dlslptttgf ssvknnngdf rnsgiemels gtilkikdwt
      781 wkmggnisyn knkvvtlpdn gqpknriggq qiytgrkvld eagnqvdevi fvggkqerqe
      841 pgilvgykae glykswddip enlivktgny qgkyqygpka yaalsdaeka kalqiapgdv
      901 kwkdinndgt idafdqvvmg nttphwfggf nttltwkglt lygrfdfald ywiydnttpw
      961 flgcmqggyn tttdvfntws eenpnakypr yvwadqlgta nyyrtstmfa ykgnylaire
     1021 islsyslpqn iarkfycqkl dvsvtgqnlg yitsanvasp evstagsgya lprtllfgvn
     1081 vtf
//
LOCUS       WP_284932064             891 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Bacteroides fragilis].
ACCESSION   WP_284932064
VERSION     WP_284932064.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 891)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 891)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 891)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 891)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14311965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..891
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..891
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=100712
     Region          48..>611
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          731..808
                     /region_name="Glyco_hydro2_C5"
                     /note="Glycoside hydrolase family 2 C-terminal domain 5;
                     pfam18565"
                     /db_xref="CDD:436582"
ORIGIN      
        1 mkksiillfi slllsplcik ahqpefstag ffrladsgrd vysmnpawrf ykgncpgaet
       61 gnfddrswtv vslphgieyl pteasgciny qgevwyrkhf tpdaalkgkk lflhfeaimg
      121 kskiyvngkl laehfggylp vvvdvtdale fgkenliavw adnsndpnyp pgkqqevldf
      181 tyfggiyrdc wliahnqvfi tdpnyeneea ggglfvaynn vsdhsaevll kiqirnsgrk
      241 afkgvveyel qqpdgqqvas lnsvirikpg kstyssdklt vkspmlwspe npalynlivr
      301 irdekgnpid gyrrrigirs iefkgedgfw lngkpyeapl iganrhqdfa ivgnavpnsi
      361 hwrdakklrd agmkvirnah cpqdpafmda cdelglfviv ntpgwqfwnd apvfaqrvys
      421 dirnlvrrdr nhpcvwmwep ilnetwypad farnahdive aeypypycys gcdseakgke
      481 hfqilfthpl ngdggaystn dikkqltyft rewgdnvddw nshnspsrva rnwgeqamli
      541 qaqhyarpsy kytsydalyr tprqhvggcl whsfdhqrgy hpdpfyggvm dvfrqpkysy
      601 ymfmaqrspi keerlfqtgp mvyiahemtp fsgkdvtvys ncdevrltyl kggqtqtyvh
      661 kqekegmphp vitfenvydf mkdkalsrqg kqadvyllae glidgkvvat hkvaparrpe
      721 klllwvdneg tdlkadgsdf vtviaavadk dgnikrlnny tikfqiegeg rilggagnla
      781 npapvrwgta pilvqstlkp gkikitasvl fegsqmpssa vleleskpgd fpqiydrees
      841 alipnftgqe aanalapkse aalekerlqk aenaaklkev eqqqeefgek k
//
LOCUS       WP_284932343             102 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II, partial [Clostridioides
            difficile].
ACCESSION   WP_284932343
VERSION     WP_284932343.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..>102
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /note="Members of this family of hydrolases with an active
                     site Cys residue belong to MEROPS family C26.; Members of
                     this family of hydrolases with an active site Cys residue
                     belong to MEROPS family C26.; Members of this family of
                     hydrolases with an active site Cys residue belong to
                     MEROPS family C26.; Members of this family of hydrolases
                     with an active site Cys residue belong to MEROPS family
                     C26."
     Region          <1..>102
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 lspgpcspke agicidiveh fkgkkpilgi clghqtighv fggdiikaqq pvhgkvysin
       61 htnkgvfrgl knplnvtryh slivdsntvp keleitaitd kg
//
LOCUS       WP_284932358             334 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Bacteroides fragilis].
ACCESSION   WP_284932358
VERSION     WP_284932358.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..334
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35189
     Region          22..328
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mkhyrlflll igllvlafla diaigsvsls irdvwntfig sndnliyqei ilnhrlpkal
       61 tailagasls vagvlmqtlf hnplagpdvl gvtsgaslgv alltlgtssl plwlitgwgq
      121 vtaaiigaig vlllviivsi kipqtislli igmmfgnfag aivsilqsms npdtlklfit
      181 wtfgslssvg weqmsvmapv iacgiltall lqkqlnilll gknyanglgv svprlrlwii
      241 latallagts taftgpiafi gitmphvarg lfgspnhrii lpasmlcgai tllvcdlisq
      301 lpgmqgtlpi navtalfgsp iivwiilrns yink
//
LOCUS       WP_284932416             320 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Clostridioides
            difficile].
ACCESSION   WP_284932416
VERSION     WP_284932416.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..320
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37049
     Region          1..319
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 makidnmmsi lwmlssdkki takqiaekle inirtvyryi dvlsasgvpi isdtghnggy
       61 sllnnftkap lffdieeqka llhaalfakk egyfldeald kailklkmys nqkqediltn
      121 hlialevikp igklsiesvl kklensilke lsveinyhtd rkakskyrii npygivhwnn
      181 nwyvvafcnm rneirsfrvd riseiietsn tfnrptefsa seffikgiip eikneqgiiq
      241 lvvegsidsl dslsqhwflg hylkertpnk iifmleeevi ckyipnillp yrktiqviqp
      301 lslrkkmied llelidyyqi
//
LOCUS       WP_284932621            1024 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Bacteroides fragilis].
ACCESSION   WP_284932621
VERSION     WP_284932621.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13208672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..1024
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=116812
     Region          299..>330
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Site            306..312
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:350670"
     Region          <487..1022
                     /region_name="DNA2"
                     /note="Superfamily I DNA and/or RNA helicase [Replication,
                     recombination and repair]; COG1112"
                     /db_xref="CDD:440729"
ORIGIN      
        1 mnymqilscw hklehfspai lpkdkslkpl kelpwmrple akdpkktiqy tiylgvfsqi
       61 svsdfvkdff kdernnpnvt dakvcyaslk ldnlgvyiqn tfgfstmpwa lrqleagkvn
      121 tnswsedfdk lrknllerlg enrkelaedy ssylsetqtl enlqqiqali iqdlkwstsp
      181 eteiyvriee vykknntsdk eeanadllns fyiddlerii tssvkgsynt afrnylsacl
      241 nkdfvhfdls lqpeilkecl vpenypdgcw psphtaslmq qfavntiske lsgekqegif
      301 svngppgtgk ttllrdiiaa ilvkrakkmv nftepakafr kigevqvsek ytpfiyepds
      361 sicdggivva ssnngaveni skelplkkea rgysdqvgyf rqvseecvge eswgliaavm
      421 gnkenqrkli ysiwdgdsee esytlkqqlk dykpteeewl nivvsfknkl geveieksrl
      481 tgfmkdaesi eklriqleda eshlshvdke leglleeknl lsteikrgkq qkedamtelk
      541 llqstrpgff iywfnktvrt qykkaltatl tkynqlseei tkqktslqal dlrvekqrki
      601 qeqsqkdydr insdyarlse lteaarqelk gayadasfwk qieskevqei spwyskrlkq
      661 lqselfieam kvnelfilra natssriktt ldgffnflkt ggdltereiq amwntfwlmv
      721 pvvsstfasi qrmfsqmktg tipwlfvdea gqavpqaaag aiwrskravi vgdpfqiepv
      781 vtipeqivnn ishhfgldkt qiqtslsvqs madranpygw itndtwtgsp lrvhrrcvdp
      841 mfsianeiay ngmmynstla essqlfmrng flqvegkvsg rhyvpeqgvl irqmiideih
      901 hlqdlpdlfv ispfseipsi lkkelrqpik qalatyksie dnelkkwlda higtvhtfqg
      961 kqaagvilcl gldekskgaa swasskpnll nvaltrakqr fvavgdgdiw lrqpyfsklk
     1021 alnr
//
LOCUS       WP_284932723             245 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Bacteroides fragilis].
ACCESSION   WP_284932723
VERSION     WP_284932723.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..245
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28156
     Region          1..234
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mikciavdde plaleqltgy iarvpflqli ascqdafsam qvlseeevdl mfvdihmpdl
       61 ngldlvrslv vkplivftta ypeyavegfk vdavdyllkp fefqdllkaa dkarrqfeyh
      121 lqdngggtet dllekdgslf vkseykiiri nvadicyieg mseyvriytd tadkpvvtll
      181 slrkleerlp qemfmrvhrs yivnlrkite vsrlriifnk niyipvgdny kerfteyink
      241 icvss
//
LOCUS       WP_284932792             837 aa            linear   BCT 25-DEC-2024
DEFINITION  M1 family metallopeptidase [Bacteroides fragilis].
ACCESSION   WP_284932792
VERSION     WP_284932792.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Evnouchidou,I., Koumantou,D., Nugue,M. and Saveanu,L.
  TITLE     M1-aminopeptidase family - beyond antigen-trimming activities
  JOURNAL   Curr Opin Immunol 83, 102337 (2023)
   PUBMED   37216842
REFERENCE   2  (residues 1 to 837)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   3  (residues 1 to 837)
  AUTHORS   Peer,W.A.
  TITLE     The role of multifunctional M1 metallopeptidases in cell cycle
            progression
  JOURNAL   Ann Bot 107 (7), 1171-1181 (2011)
   PUBMED   21258033
REFERENCE   4  (residues 1 to 837)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   5  (residues 1 to 837)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..837
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=96336
     Region          33..466
                     /region_name="M1_APN"
                     /note="Peptidase M1 family including aminopeptidase N
                     catalytic domain; cd09602"
                     /db_xref="CDD:341065"
     Site            order(146,148..149,282..286,315,318..319,322,337,341,404)
                     /site_type="active"
                     /db_xref="CDD:341065"
ORIGIN      
        1 mkihilfgmi gfillsgcnr aaeknprfyd agvsrelagh rkaqiknlky elsfniprqk
       61 evaiegditl rfdlasrqev lidfreerek ikeviangvp vdkvrfeneh iilpasstve
      121 ganeirirft agnqslnrnd eylytllvpd rartvfpcfe qpnlkaeftl qlelpadwka
      181 vsntyirset vtddrktvcf apteplstyl fsfvagkler reytrdgrti aayyretdpk
      241 kvaqldivfg qvmaslhwle eytgiaypfa kydfivlpgf qfggmehtga tlyndngifl
      301 sehptpdeel nraeliahet shmwfgdlvt mdwfddvwtk evfanyfaar iveplfpein
      361 htqnklktft aaslsedrtm gtnairqpld nlrnagliyg qiiynkapvm meklvdkmge
      421 anfrsgiqey lktysygnat wddlirilds kttedlaafs dvwvnrkgmp tltfrtdgqe
      481 leirqhdpyn rgllwpqrfa vtlcgerdsv irvnmtdtlf rmqlpfvpsr vlpntdgrgy
      541 gvfvpdepal hwlaahwwei eddtarqsll mvlyenylak hisaddwvns litglpaekn
      601 alvastasgy lanvmweiap anraeveari ytmtqnhplp scriqlmrlf mqnaisepmv
      661 kklyilwqqq sdkhlnrqdy ttlayelair mpleseqilr tqrariddpd rlrqfdfisr
      721 aavsdtarld tlfnsllaae nrriepwtta virylnhplr edqsvkyirp glevleevqr
      781 tgdiffpknw aaallgnhls ssayeevvrf lnerpdyspl lknkilqaay plyrann
//
LOCUS       WP_284932828             507 aa            linear   BCT 25-DEC-2024
DEFINITION  adenosine deaminase family protein [Bacteroides fragilis].
ACCESSION   WP_284932828
VERSION     WP_284932828.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Cristalli,G., Costanzi,S., Lambertucci,C., Lupidi,G., Vittori,S.,
            Volpini,R. and Camaioni,E.
  TITLE     Adenosine deaminase: functional implications and different classes
            of inhibitors
  JOURNAL   Med Res Rev 21 (2), 105-128 (2001)
   PUBMED   11223861
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004592
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..507
                     /product="adenosine deaminase family protein"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=57582
     Region          53..491
                     /region_name="Add"
                     /note="Adenosine deaminase [Nucleotide transport and
                     metabolism]; COG1816"
                     /db_xref="CDD:441421"
ORIGIN      
        1 mktcyfsyfl fllfgvfnhi tvyaqpdsvv vseyfssihn denrlrqffa empkggdlhn
       61 hltgaayaes yfkfatedgl wvdmatgkly qpkdstkgke mlrlspdmpn lhntrmalid
      121 kwsirnfnpg kfplgadeyf fgafglfntv agkhtvelmq elrkraaren vqyleimlss
      181 pginaakida lcgndfytry ndrlqkaila dterakgreg tdkvlddifk ewekipamsk
      241 wvdkyvayid sidihstlss gydrtpvcfy qgyasrnaap lvvyaqlyia fksclregsk
      301 lvgvnivsae nseiamadyt ahmkmfryld katgnrvkts lhageltlgl vkpedmcshi
      361 reavfvagad righgvdvaf kegsisllda mqkrqipvei nltsnefilg vkndahpfml
      421 yrqaevptvl stddpgilrt nlaqqyvlaa mryglgyyei kqlvrnsirf gfmpekekqa
      481 llkrvekefa tfekmwrkni slifvri
//
LOCUS       WP_284932839            1071 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            fragilis].
ACCESSION   WP_284932839
VERSION     WP_284932839.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=120041
     Region          68..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkpfmlisv lpitvhishd tdtgsnrigg ipekyafknk vlrsicfvlf llsiglnsaf
       61 aqvrnaaglv vdengqplig vqiklegttt gvitdvdgnf sinakkgdil lfsyvgyepq
      121 ritykgekil aikmlpntel ldevvvigyg kqkknsvvss inaigpkela vssnrnltns
      181 lagqvpglia vqrsgepgyd nsefwirgvs sfkggtnplv lvdgvprnmq dvepdeiesf
      241 tllkdaaata vygaegangv ilitskrgns qkpkislrae stlltptrlp kfmnsvetld
      301 lynealnneg tasirtaeei amygpgadrd lypdtdwlke mlrehtynmr ytlnvrggse
      361 raryfvsgaf yqengifkeg kkneydnnig lkrynlrsni dfdatkttlv kvdisgqylq
      421 tnypgtstnt ifnsmcrtps ylmpaeysdg tiaghprpsg nrvnpynllm nsgyakewrt
      481 siqsklevdq kldfitkgln wkglisfdad mkyiakrtkt ptqylatgrd engglqfkkv
      541 vegsdvltek lenssnkkiy fetsfnynrt faqkhdvtam vlymqketqy hnnalpyrkq
      601 glvgratygy dgryfiegnf gytgsetfak gyrfgffpam glawyvsnep fypevlkkvv
      661 nklkfrfsig rtgnddtggd rflyrgtmkq dnggydlgfs dtggmggign gitearfeap
      721 ylsweieekk nygidlglfd nridlqvdyf nnkrksillq rntvsnvtgf qqmpwqnfgi
      781 vknhgvdasl tlnqkigqvn lsargnftfa rneiieydqv pqvypwlekr gtrlnsnkly
      841 iaeglytydd fiingeglnr tyelkpgvvs glssgvrpgd ikykdlngdg kidsndqked
      901 vgnptvpevv ygfgfnaewk gfyagiffqg agntstvlgt gadatffpfq wgveesavrs
      961 vvadrwteqn psqnvmfprm hsnnfqnntv astwwlrdas flrlknielg ynfdkkllkk
     1021 lniealrfyv qgnnlcvwdh ikmwdpeqgn snggfpypln rtftfgldft f
//
LOCUS       WP_284932858             954 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Bacteroides fragilis].
ACCESSION   WP_284932858
VERSION     WP_284932858.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 954)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..954
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..954
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=109276
     Region          24..452
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          524..942
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mkrnnknryl yiaaifiaam lpciacpqst pillptgtve grlpnglhyl ilhnaspasr
       61 vefrlimrvg svqeteqekg cahflehvtf ggtrhfpkrs lveyleslgm kygqdinaft
      121 gfdrtiymfa vptdhakdev ldrsllilcd wldgvtidpe kvenekgiil eelrgfdped
      181 dfyplkigqg ifchrmplgt tddirkvtpq vlknyyrkwy vpslatlviv gdispleies
      241 kikerfkslp grpvndfrny pleytrgihl asirdslqpr tkvelmiphp ctvertmeda
      301 iakekgrlli saissrfrar klktdvtdqw ylsdknhfvl tvegenrkei ltsisttvsl
      361 lndlirngwq edelqdiknn fcrrmklstd apsrpssmwc ddfadyvisg dryltdpsqq
      421 qqlkeamsrv sgqslqtllk ewmsyreetl lvacsthpgl gaplseteia sawaqgeqve
      481 ctpflyfrpe kqeeidietp pclaarfpfd pasvlrqtey pqnrirevel kngirlvlkp
      541 tleadstlli tsfapfgtss lsdeeyplle gfagyidmgd iakvdgqvls dylfrkeisl
      601 smavenhwhg figmsptana pelfnliyek ifdpelkyde feeirqdlle nqdketilek
      661 mlqrspdrll sarineltgt gfarssqkls seqiknlnld siaafykkly tnpqgttyvi
      721 cgnfnadtlm qqfvsvfgri pvsshlsrfs yphfnfpvrk hiegfpndnd tqtlfdyllp
      781 ghyqpglknt ltlklmrdli rnrlisvlre qkslvyspyi slmyegipqg ifyfdinasa
      841 dndnmpqieq llkeilhqlk qqevdneeln tlkrsfliak realneesps awraalvgll
      901 kngetisdfd hyeqcldsit pamlreafrr yldtenyill ylsknklknd tsnh
//
LOCUS       WP_284932891             229 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase [Bacteroides fragilis].
ACCESSION   WP_284932891
VERSION     WP_284932891.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..229
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=25283
     Region          105..224
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mkkiliqila fitvkywskl kgihihdsvi ifghfsnssa snqidirhsi lkrtsievng
       61 nnnkinlqgp fsatkikvig nnnqiniqki ngitlseiii rgeecsisig nnsgfgnylk
      121 licmgklnsi sigedcmlad hvelwntdsh piyndqgeii npsrpiiign hvwigkdsrv
      181 tkgvnignna iigfnslvtk niksntlnag sptrqiregv nwdqrfiti
//
LOCUS       WP_284932904             545 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Bacteroides
            fragilis].
ACCESSION   WP_284932904
VERSION     WP_284932904.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..545
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=59699
     Region          50..528
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 meklhirkia slglmlcfft gvgaqtpvkv ekrkehksnt vipvvkgnvt dtlslvsfnd
       61 fhgafacdkg vpgagqlvqt vltqkeknkn tivlsvgdnf sgsyfsritr gnplpemfqe
      121 mdvrmsavgn hefdwglpyl tdtakvymnf vaaniitdrg dtlewakpyr ivtlnlkngg
      181 tvrvafiglt ttdtahktsp enikglafvh pvyaarveta crlkkegkvd mvvllmhigt
      241 nmknrdiiee enakllpflk gvdaiisghs hevvlskvnd vpiiqagvng thigkldfrv
      301 vkeeggnris yiggdtirte gpsnahidsl vdkvlavygl seklilakda lihdrtinkw
      361 eytpvgayvt aayvrsflen ekvpaelkvl pvigvnhfgg lrasipagev trlragnvlp
      421 fggnvvayef tgerlkqlld dgrrnkngfl qtsylklhln skgnvetitd crtnkiirdd
      481 dkcivvldaf itsggdgyds klfsgyeigd fnsqnlettv afidylkslk gfvsseaapi
      541 pivqk
//
LOCUS       WP_284933012             610 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Bacteroides fragilis].
ACCESSION   WP_284933012
VERSION     WP_284933012.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13939702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..610
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=66826
     Region          28..>114
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
     Region          151..464
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
     Region          426..610
                     /region_name="DUF3520"
                     /note="Domain of unknown function (DUF3520); pfam12034"
                     /db_xref="CDD:432277"
ORIGIN      
        1 mktnqframv fallmavisl atvsakaitv sgtvtdakdg tplvgcsvqi kgttkgtvtn
       61 mngqytiqsk kgetllfqyi gykqekrvvk sstldvkmea delvleecvv vgyghelrat
      121 ksmstaymav cpasgimyna vnaeeygeiq engfknvsda plstfsidvd aasysnmrrf
      181 inkgklppvd airteelvny fsydypkptg sdpvkitmea gtcpwnadhr liriglkake
      241 iptdnlpasn lvflidvsgs mwganrldlv ksslkllvnn lrdkdkvtiv tyagnagvkl
      301 eatpgsdkqk ireaidelea sgstaggegi mlaykiaqkn fisggnnrii lctdgdfnvg
      361 vssdkelekl ieqkrksgif ltvlgygmgn ykdnkmqtla ekgngnhayi dnlqeanrvl
      421 vnefgatlht vakdvklqve fnpaqvqayr ligyesrlla dedfnndtkd agemgaghtm
      481 tafyeviptg iksdfagkid dlkyqkkqkp stplnesdel ltiklrykap dsntskkiel
      541 plidhksnrv sadfrfaaav amfgqllrds efkgnatydk vislaktgle ndekgykref
      601 irlaetaksl
//
LOCUS       WP_284933006             311 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Clostridioides difficile].
ACCESSION   WP_284933006
VERSION     WP_284933006.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..311
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=36411
     Region          18..310
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 makqrskris ingepnpeni klwkqykrak qiagksekti ynyecdimqf fkflniecfd
       61 alltdineee ieayigycme qgnnekrirr rississlls flkkkrkitd nwcemierpg
      121 tgeevqkrtf lteeqlsklk eklseqdnlq levyinlgla tmarsneisq frwdnidldn
      181 rwihgitakg gvsrdfrfse evqhlliewk dnlsqnnidy pyifftrygg kynqvnsnvl
      241 sswvkkafrf igieggynhd lrhsmsnllk drgvpittvs kllghsgvdv tinhytienk
      301 nklaeeydkf m
//
LOCUS       WP_284933036             413 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284933036
VERSION     WP_284933036.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..413
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <9..405
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 danqnicihk dkkfavfyid fenfkyindi fgydygdmil kryanlmmnd igkyeifare
       61 iadrfvalrc yvdkedlvvr qrdvdnelin itneiknkhs itvvsgicci edvneklsid
      121 glinranfaq ktvknkpgtn yafyndsirk kmieentiks riheaiekre fivylqpkvn
      181 lhsqkincae alvrwltpdk giispaifip vleknffial vdkyvfeevc kwirkrlden
      241 kpfvqisvnv sriqfyntkf vetysniqnk yripkntiei eftesvafen qkhlleiihd
      301 lhengftcsl ddfgkgyssl svlkdlpfdv lkldsmffka sldkdkekiv iknivhmlke
      361 lnittvaegi eckeqveflr digcdlvqgf vfykpmpile fekildkefv yns
//
LOCUS       WP_284933152             637 aa            linear   BCT 25-DEC-2024
DEFINITION  lipase family alpha/beta hydrolase [Acinetobacter baumannii].
ACCESSION   WP_284933152
VERSION     WP_284933152.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 637)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 637)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18498059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..637
                     /product="lipase family alpha/beta hydrolase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=72190
     Region          357..499
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
     Region          <522..622
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mtksghylvl timgllsgcq vihlkesnls salksknesi ltdntlshqt qnllylvkes
       61 etsclqnfnv clnkiqglsd nssreeryaa lseiylakal dvgrssqcnv alksnscveq
      121 elalfdkslr ysyvylfdse espfdrvfdh rqnqvrifyn valsklmtty fnhlntlhfp
      181 pllkadghey hvnfdhavdv qhievdtfrs synmnfsgfn tvnrkdglga efivgrkehd
      241 vnhgfildpd afyahqsnpn ihlprffpvt aiaypkqkat adqvidgael eiamfdpyrq
      301 drvkvegvdy pltanysapy glwlskynlg aagywslink eanlimphly mlepfnpnkk
      361 iivfihglas speawvsltn dimgdaelrq nyqvwqvfys tnmpifesrf qiysllnqaf
      421 qnvakdsyaa hdavlvghsm ggvisrllvs dadvsdlamq kmneaqlkrl kenpvirerf
      481 qfkdlpyfkr vvfvsaphhg tdyadrwftq iarriirlpa dffiavemrd eknaklrkgl
      541 iengasnlsr ssnfmqltqa iqpssnvvyh simgningtt dkskmsdgiv pyqsshlgge
      601 qseliikggh siqtspeail elrrilrlhl kqsppsk
//
LOCUS       WP_284933177             690 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Bacteroides
            fragilis].
ACCESSION   WP_284933177
VERSION     WP_284933177.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 690)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 690)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..690
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76816
     Region          10..642
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mnkrclltil lggcaamgaf aqqhatgkkt emsvdlnpvv vtgtgthqrl kntpapvevv
       61 taneikkagi tdfqqamtml vpslsfstns mgsylmmngl snkyvlilin grkltgdtsn
      121 nidlsridms rvkrievldg agsslygsda iagviniitn epkelmqvts ttryedhrql
      181 tqmvnadiat ekfgsytsyk heqsagwqns dlayvtdkkg nvstvptvsa tsngfhsnlv
      241 nqkftfepte klsfyanggy ywkltdrpvy tadidggsky dlhyesynfg lggrykinkr
      301 ssiqldlmnd nymqnykytv addknkiaig dyaktkeqhf ydaelkgifn faknnmtvlg
      361 vdyrsesldr psarvdksvy tasayaqhei klwncltgia gvrydyhela ggrftpkvav
      421 mysvgafnir gtystgyrap gldelyyymn kgktitqgnk dlkaehsnyy svnleyntnr
      481 lnvsvtgyln yiddminstt yrlvdlpnge elraqaqkef nltdsetkal anyklygnld
      541 kgvvrgfevn aatnlgagfs lngnyayaya rgksvdgvwg niersvrhtg tvagnythaw
      601 ndymlnvnin grfqskrfhp ghsygdapgy gvwnlnvkhs ltgfqhlgld fgmgldnifn
      661 krdtrpngvn yallspgrma yvsltlrfkk
//
LOCUS       WP_284933199             628 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 35 protein [Bacteroides fragilis].
ACCESSION   WP_284933199
VERSION     WP_284933199.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 628)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 628)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 628)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 628)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 628)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12015514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..628
                     /product="glycoside hydrolase family 35 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=70884
     Region          34..356
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
     Region          <568..603
                     /region_name="BetaGal_dom4_5"
                     /note="Beta-galactosidase jelly roll domain; pfam13364"
                     /db_xref="CDD:463857"
ORIGIN      
        1 mrtksiflll llavmplcvf sqskstfeik nghfyrngki tpvlsgemhy ariphqywrh
       61 rlqmmkgmgl ntvatyvfwn lhepepgkwd ftgdknlaef iktageegmm vilrpgpyvc
      121 aewefggypw wlqnvkgmei rrdnpeflky tkayidrlyk evgslqctkg gpivmvqcen
      181 efgsyvaqrk dipleehray nakikqqlad agfnvplfts dgswlfegga tpgalptang
      241 esdienlkkv vdqyhdgkgp ymvaefypgw lshwaepfpq igasgiarqt ekylqndvsf
      301 nfymvhggtn fgftsganyd kkrdiqpdmt sydydapise agwvtpkyds irnvikkyvk
      361 ytipeapapn pvieipsiql nkvadvlafa ekqkpvssdt pltfeqlnqg ygyvlytrhf
      421 nqpisgtlei pglrdyavvy vdgeqvgvln rntktysmei evpfnatlqv lvenmgriny
      481 gseivhntkg iispvqiagk eivggwdmyq lpmdempdlt klkadthknv psevaklkgc
      541 pvlyegtftl dkvgdtfmdm eswgkgivfv ngvnigrywk vgpqqtlyvp gvwlkkgenk
      601 ivifeqlnet pqtevktvkt pvlmklkg
//
LOCUS       WP_284933220             447 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Bacteroides
            fragilis].
ACCESSION   WP_284933220
VERSION     WP_284933220.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..447
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=49766
     Region          1..444
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mrsilivedd itfgmmlktw lgkkgfkvss vsniaraqkh idaqpvdlil sdlrlpdhdg
       61 ihllkwmgek elhipliimt gyadiqsavq amklgaqdyi akpvnpeell kkmsealqkk
      121 eaplpktplt ekspktkqes hsylegesda akqlynyvsl vaptnmsvli ngasgtgkey
      181 vahrihqlsk rsdkpfiaid cgsipkelaa seffghikgs ftgalsdktg afvaanggti
      241 fldeignlsy eiqiqllral qerkirpvgs nseitvdirl vsatnenleq aiekgtfred
      301 lyhrineftl rmptlkergg dillfanffl dqankeldkq ligfdanask alleyhwpgn
      361 lrqmkniikr atllaqgsfi glaelgseil etqlstpkmt lrdedaekeh ilealrqtgn
      421 nksraaqlld idrktlynkl klygidl
//
LOCUS       WP_284933230            1059 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            fragilis].
ACCESSION   WP_284933230
VERSION     WP_284933230.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=118053
     Region          56..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkrtnlfps liktcemncl kiagasllll cispqfavad glkqdavtim qqqnlkvsgv
       61 vtdeagepli gvsvlvkgtt lgnitdlngr fsldvpegsi leisyigykt qsikaqrepm
      121 nivlkedaqk ldevvvvgfg tqkkvnltgs vsavtgddis krpvanaail lqgqipglrv
      181 nqglgqpgge gtsfrirgqg tfssagsdpl ilingvpgsm tnldpsvies vsvlkdaasa
      241 aiygaraang vilvttkqga vgdkvhisyh gnvglhtptk lydrvtnsve ymelanlawk
      301 nsgtgkqytq dqinlyrnnv gdpqypnfdw qdymfrtavv qthnlsmags tekttynval
      361 nfvdqpgtmr gfkyrkynat idltaritnf ikvgtyanlm ygeteqprqg qndaflstls
      421 qaptympwlp ddgtgirrwt ssaysfeshn knmpaiigdn amkrdnnfdi naqlwleinl
      481 akgltwytkg aarlqsnksk dwrgsttyty dyhtgersse ldkgglglsv gdgrrfytnl
      541 ysylkydlsl vdnahnfslm vgynqeseky etlnayrkdf afdlpvlnag gtadwsnsgg
      601 eeewaiqslf grfnydfker ylfeanmryd gtsrisdenr wgvfpsfsva wrateeefik
      661 nlnlnwlnnf klrgswgqlg nqniglypyq amisgvddyp ftktsdgvii gyqqtayanr
      721 nikwetttit digfdlqvfd glsvtfdwyk kttddilrss qvssllglsa ptvnngsven
      781 kgievalnya nmvkggtfrg frynagvyfd rsrnkltefg aeeigsysik reglpydeyy
      841 mlecigvfad qaeinaspkq fndntqpgdl kykdisgpdg kpdgvidnyd rrtfsgrfpg
      901 feyginasat wkgfdlslig qgvadkkyyt tdwgvqpfmq gsspnkdyik hmwteenpyg
      961 akhpklywqd mgggkntrpn syylkdasff rlknvtlgyt lprvwtekan iskvriyfsg
     1021 dnlltltpyk gldperngdg rdaiypqnri ysfglnvef
//
LOCUS       WP_284933240            1056 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            fragilis].
ACCESSION   WP_284933240
VERSION     WP_284933240.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=117166
     Region          39..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlkdlnnlr adtegrikav flicmfvlvs aggfaqntks isgtvrekgs netvigatvq
       61 vkgthngvit nengeytikn vspgqvlvfs migmntvekt vgsqnridvl mdagvlidev
      121 vvtgyqtqrk vdltgsvssl ssdqfmqtnp lsleqalkgk isgvqvmnnd gapgggitik
      181 irgassitag ssplyvidgf plpisddple splatispda iesisilkdv sstaiygaqg
      241 angvvlittk kgsagmseis vkatygiskl ansipmlgae dymraymrdm imsgrwqnad
      301 fyqeykdqiw ntnpsrfqfy pdlclqngtk qnyevsyrgg tdriqnstif slmnedgiai
      361 ntgfkrfyfq tnnsikllpq ltlntnlsye hnirsgafwt egnifneiqt fsplvpkewt
      421 fqeiddnlyy tgkmdnpyrk lkdidysnkn ntffgqaelv ynindnwfvk ggigvripkg
      481 evkefipkti qrgydnngla tyatqsglnm rgvvqagfnk vfnkvhslsv navyeantnk
      541 yetfnqeysq fntdlgwegi ydaksgnhvk spgvsyekia mlsgvlmany sykgryllka
      601 smradgsskf spdnrwgffp sgalgwrvse eeffknvswl eknvnnlklr fsygqvgndq
      661 iapyayaqtl sssqrqaifg dgaipalyts rmanpeiswe vteefnggld ldmfnnrlni
      721 sldlytkttr dmlleqnlpr tsgfgkvtrn igsvrnrgfe isvggvlidk kdftwnatvn
      781 fssnqskvms lgaetqmleg rpvgsasgse svlikkgypl glfyglqmeg irsnwhsdyn
      841 gigsadspww yaterempyg fpsfadtngd gkvdmsdrvv igdvnpvfig glntrlrwkf
      901 ielamdfsws ygndiingnv ynlmnngdir nksavyykda wfannptgtf tgpgaidwsg
      961 ymwaasnsem vedgsflkmn nlavtfrmpk nilkawkikd laltytinnv fcltnysgyd
     1021 pevrsgssvn nrilpgvdis aypyarshif slnfky
//
LOCUS       WP_284933276            2447 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Acinetobacter
            baumannii].
ACCESSION   WP_284933276
VERSION     WP_284933276.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..2447
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         <1..2447
                     /product="beta strand repeat-containing protein"
     Region          1..1620
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          1162..>2435
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 ngyitaaipv tgegpvaiha eavdaqgnvd vadadvtlti dttpqdlita itvpedlngd
       61 gilnaaelgt dgsfnaqval gpdavdgtvv nvngtnytvt aadltngyit atldataadp
      121 vtgqivihae avdaqgnvdv adadvtltid ttpqdlitai tvpedlngdg ilnaaelgtd
      181 gsfnaqvalg pdavdgtvvn vngtnytvta adlangyita tldataadpv tgqivihaea
      241 vdaqgnvdva dadvtvtidt tpqdlitait vpedlngdgi lnaaelgtdg sfnaqvalgp
      301 davdgtvvnv ngtnytvtaa dlangyitat ldataadpvt gqivihaeav daqgnvdvad
      361 advtltidtt pqdlitaitv pedlngdgil naaelgtdgt fnaqvalgpd avdgtvvnvn
      421 gtnytvtaad itngyitail aataadpvtg qivihaeavd aqgnvdvada dvtltidttp
      481 qdlitaitvp edlngdgiln aaelgtdgtf naqvalgpda idgtvvnvng tnytvtaadi
      541 tngyitaila ataadpvtgq ivihaeavda qgnvdvadad vtvtldvtpp ditttvlaid
      601 pvtadnilda teaggtvtlt gtltnvpada tttgvvvtin gndytatvda iagtwtvnva
      661 gndlaldpdl tvdakatftd lagnsstlqd tqtytlagsi tafdntdhav lspkpalvgd
      721 dvslgstsyl vltsvagldl qlggnslgft vdaghegdvt fqysglidaa vlsdyklvvq
      781 kfntttnqwe sihgdanssl islhllgigt gnvpgavldg ldagqyrafl aydgllglgv
      841 lgtlsatmdd ydlsvaggye ignaegnvit dpdpttgqvd qvtantyvss vnghpidadg
      901 etfagtygti tfyqdgsyvy vpnadgsgvg qtdvftytlt dsvtgatgqa nlnivfdsir
      961 aadnlvevel npqyqlvgte tdsafygvll nvgnivdlql ltvdtvdfti gagqegvatf
     1021 nfnsligasa lgdynvvlqk yndvtgqwea vngtgdrsll nltllgntpt aqiggltege
     1081 yraflsfngl vggavavtln gsvdvynpav itgydvvaah gnlisdpntn gdvdiatpns
     1141 iisevngvav saspteiigt hgtlliyang dytytpnads aglgqvdqft ytlldpasni
     1201 tsqatfyvhl dskvvdmnwd aadpsqpatv titavddavn aaiaaephli eddralgsat
     1261 ylallslagi nlqaplpfvn stvefnvgag etgtatfkys slinegalgd yqlvvqkfnt
     1321 atnrwesitg sseasllnls vlgigvnatp gvvvegldeg qyrafmtyng lygksilgtl
     1381 sgtmdvydpn qidftglase gnvitglgvg tnadavtgyt ivdsvtvngv ttnvdpntgt
     1441 iiqgqygtlq ifangdyiyt pnntnanlgl vdhftytlad plggnisasl dftignstpv
     1501 iavddlavav vnpeylqign dvavdsylyv allsltdnfd fqlggqgidf tltdstlndv
     1561 tfnysalida slladyvlvv qkfdtatnqw vavngtgead llslaafggn svtleglaag
     1621 qyraymtyag sgvgvsllgt lsvqkdvfda tnitgystqv aegnvihdvg lnghadtasg
     1681 fstvtsvefn gtafavnatg vttivgdhgt lsiyangnys yqpngeaasl gqvdqftytl
     1741 sdglntsqat lylhidsdav dmtwntsdps qpavitvtpv daidnvvsag vdivpqgelg
     1801 vavgsatyla lvgitedlnv sllgtpsvaf tidagheadv tfayapvlsl slfndykvvl
     1861 qqkgadgawh nidggsstgl lnigllgngg igvtvpdlgq geyrafmvyt glgvgilgtm
     1921 svvkddfdyt vaptntavva dgnvltddvt tlttqvttvt sevvgalpqt vgtdtvinga
     1981 ygtlvistng hytytpnttd lsaigkvdsf tytirdvltg atdtatlhvq vgspdvtiaw
     2041 daanpandgv vqltanpdhv vtttdfsnaa dlpvdvaspv vsvnligsns vvsdqfvvga
     2101 gtvanidlsa vytaqplasv lptvsyviqs wngtawvnti ysgsqtalgs vatiqagsva
     2161 fqdtvehlaa gtyrvqytlt gvslgatsld tnvstttvhl dtyrsdwisg nvlagdnigg
     2221 vadtgilshe gaklqvwdna qnayvdavgq tintgngvli mqsngeyeyr pndvttttql
     2281 astdsinyki vsvtggvesq stltidltht dynllytsts andtfttgtg sdtviyqlln
     2341 gtaatannga ntggngvdtw tdfhvgnvat dkqadlidir alldgdqtda nigqylnvtt
     2401 sggnttiqid rdglsglipg nnfttllvlq gvtttetell nngqily
//
LOCUS       WP_284933283            2447 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Acinetobacter
            baumannii].
ACCESSION   WP_284933283
VERSION     WP_284933283.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..2447
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         <1..2447
                     /product="beta strand repeat-containing protein"
     Region          1..1620
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          1162..>2435
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 ngyitaaipv tgegpvaiha eavdaqgnvd vadadvtlti dttpqdlita itvpedlngd
       61 gilnaaelgt dgsfnaqval gpdavdgtvv nvngtnytvt aadltngyit atldataadp
      121 vtgqivihae avdaqgnvdv adadvtltid ttpqdlitai tvpedlngdg ilnaaelgtd
      181 gsfnaqvalg pdavdgtvvn vngtnytvta adlangyita tldataadpv tgqivihaea
      241 vdaqgnvdva dadvtvtidt tpqdlitait vpedlngdgi lnaaelgtdg sfnaqvalgp
      301 davdgtvvnv ngtnytvtaa dlangyitat ldataadpvt gqivihaeav daqgnvdvad
      361 advtltidtt pqdlitaitv pedlngdgil naaelgtdgt fnaqvalgpd avdgtvvnvn
      421 gtnytvtaad itngyitail aataadpvtg qivihaeavd aqgnvdvada dvtltidttp
      481 qdlitaitvp edlngdgiln aaelgtdgtf naqvalgpda idgtvvnvng tnytvtaadi
      541 tngyitaila ataadpvtgq ivihaeavda qgnvdvadad vtvtldvtpp ditttvlaid
      601 pvtadnilda teaggtvtlt gtltnvpada tttgvvvtin gndytatvda iagtwtvnva
      661 gndlaldpdl tvdakatftd lagnsstlqd tqtytlagsi tafdntdhav lspkpalvgd
      721 dvslgstsyl vltsvagldl qlggnslgft vdaghegdvt fqysglidaa vlsdyklvvq
      781 kfntttnqwe sihgdanssl islhllgigt gnvpgavldg ldagqyrafl aydgllglgv
      841 lgtlsatmdd ydlsvaggye ignaegnvit dpdpttgqvd qvtantyvss vnghpidadg
      901 etfagtygti tfyqdgsyvy vpnadgsgvg qtdvftytlt dsvtgatgqa nlnivfdsir
      961 aadnlvevel npqyqlvgte tdsafygvll nvgnivdlql ltvdtvdfti gagqegvatf
     1021 nfnsligasa lgdynvvlqk yndvtgqwea vngtgdrsll nltllgntpt aqiggltege
     1081 yraflsfngl vggavavtln gsvdvynpav itgydvvaah gnlisdpntn gdvdiatpns
     1141 iisevngvav saspteiigt hgtlliyang dytytpnads aglgqvdqft ytlldpasni
     1201 tsqatfyvhl dskvvdmnwd aadpsqpatv titavddavn aaiaaephli eddralgsat
     1261 ylallslagi nlqaplpfvn stvefnvgag etgtatfkys slinegalgd yqlvvqkfnt
     1321 atnrwesitg sseasllnls vlgigvnatp gvvvegldeg qyrafmtyng lygksilgtl
     1381 sgtmdvydpn qidftglase gnvitglgvg tnadavtgyt ivdsvtvngv ttnvdpntgt
     1441 iiqgqygtlq ifangdyiyt pnntnanlgl vdhftytlad plggnisasl dftignstpv
     1501 iavddlavav vnpeylqign dvavdsylyv allsltdnfd fqlggqgvdf tltdstlndv
     1561 tfnysalida slladyvlvv qkfdtatnqw vavngtgead llslaafggn svtleglaag
     1621 qyraymtyag sgvgvsllgt lsvqkdvfda tnitgystqv aegnvihdvg lnghadtasg
     1681 fstvtsvefn gtafavnatg vttivgdhgt lsiyangnys yqpngeaasl gqvdqftytl
     1741 sdglntsqat lylhidsdav dmtwntsdps qpavitvtpv daidnvvsag vdivpqgelg
     1801 vavgsatyla lvgitedlnv sllgtpsvaf tidagheadv tfayapvlsl slfndykvvl
     1861 qqkgadgawh nidggsstgl lnigllgngg igvtvpdlgq geyrafmvyt glgvgilgtm
     1921 svvkddfdyt vaptntavva dgnvltddvt tlttqvttvt sevvgalpqt vgtdtvinga
     1981 ygtlvistng hytytpnttd lsaigkvdsf tytirdvltg atdtatlhvq vgspdvtiaw
     2041 daanpandgv vqltanpdhv vtttdfsnaa dlpvdvaspv vsvnligsns vvsdqfvvga
     2101 gtvanidlsa vytaqplasv lptvsyviqs wngtawvnti ysgsqtalgs vatiqagsva
     2161 fqdtvehlaa gtyrvqytlt gvslgatsld tnvstttvhl dtyrsdwisg nvlagdnigg
     2221 vadtgilshe gaklqvwdna qnayvdavgq tintgngvli mqsngeyeyr pndvttttql
     2281 astdsinyki vsvtggvesq stltidltht dynllytsts andtfttgtg sdtviyqlln
     2341 gtaatannga ntggngvdtw tdfhvgnvat dkqadlidir alldgdqtda nigqylnvtt
     2401 sggnttiqid rdglsglipg nnfttllvlq gvtttetell nngqily
//
LOCUS       WP_284933263            1082 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Bacteroides fragilis].
ACCESSION   WP_284933263
VERSION     WP_284933263.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         <1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
     Region          49..1081
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 lirfretnrl kmaiaasiml wcatpqqaaa dtyekheias vqqqkvkttg tvvdqngeam
       61 igvsvkvkdn atmgaitdle gkfsidtpkg atleisyigy ktvtvkaegt alnitmqeda
      121 evldevvivg ygsqkkvnvt gavsmvdskv iesrpvsnvs qalqgvvpgl nltvptagga
      181 ldagmnisir gagtigdgss ssplilidgm egdmnsinpn dienisvlkd aaassiygsr
      241 apfgvilitt ksgkagrtsv nystnvrfks pmsmpemmds wsfanywnea ginqngnikf
      301 tqdvmdkila fqqgtltgpd aagiswqdge wkkyagawan tdwfkeqyhs ivsnehnisv
      361 nggtdkvtym vsagymgdkg ltrhgddrlt rynlsgkina tlskyvklmy ntkfiredyd
      421 rpsyltsnfy hniarrwptn pvkdangyyl dhseiiqmee ggrdvtqkdq fyqqiqlvve
      481 plkdwlihae gnmkivnnqn qwevlpvyyh dgegspvama wfdgytpgms rvnqsywkdn
      541 nyslnlytdy fkqigdhyfk vmggfnaely krtnlsgqrd elitpdvptl ntgtteqkan
      601 ggyshwanag ffgrinynyk erylleingr ydgssrfigd krwgffpsfs agwnvsrepf
      661 wrdlehivnn fkirgswgel gncnttafyp fyqtmptgve nsgwlingkk pntasapgiv
      721 saemtwetvr swnigfdfgl lnnrltgsfd yfvrntldmi gpapqlpatl gatvpkvnna
      781 dmkawgfeve vswrdrikdf nygvkfvlsd dqrkvtrypn eelnrnqwya grmdglvwgy
      841 etvgiaktda emeahlaslp nggqsqlgsk waagdimykd lngdgkissg dgtlndlgdl
      901 kvvantqlrf kygltldasw kgfdfsaffq gvgkrdvvvg gpyfwgangq gmwqaaafkd
      961 hmdyfrpedt esvfgpnvda yyprvifggg sseggkntlt qsryvqngay irlknlqlgy
     1021 tlpstitkkf avnslrvyvs gdnlwtgtkm rvfdpevlgs tgdagkaypl arvwsvglnv
     1081 nf
//
LOCUS       WP_284933443             416 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Bifidobacterium
            breve].
ACCESSION   WP_284933443
VERSION     WP_284933443.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium breve
  ORGANISM  Bifidobacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Bifidobacterium breve"
                     /db_xref="taxon:1685"
     Protein         1..416
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=46831
     Region          4..394
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 masikryryr ayptkgqaha lsclygccrf vynrfvavre tmfkvggrmp tftqlardlt
       61 qskndpdtsw lktvsavplq qslrhartay dnyfawkkgd rkgpevgkpt fktrrgtqsa
      121 eftlnsrfkl ehepgckwaf ltlpkvgrvk lrwtrdlptv pktvtvirrp cgryeasftt
      181 ittsritpka lhaeagvdig llslgvvrrs dgtceaienp rflknserrl rhldrelark
      241 rkgsrnyeka ctrraracqk vkdtrldyla ktarrliden qaialetlsi tglaktrlgk
      301 svldagwgtl irlvtqmgre agrdirrisr wyastqtccv chvkdkpkpl nirewdcpnc
      361 garldrdana avnimlaagl aeslnacggd vnrklampaa tstpmkqeps etiplh
//
LOCUS       WP_284933573            2515 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Acinetobacter
            baumannii].
ACCESSION   WP_284933573
VERSION     WP_284933573.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..2515
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         <1..2515
                     /product="beta strand repeat-containing protein"
     Region          2..1688
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          1230..>2503
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 vtvdtvpadl igaitipedl ngdgilnade lgtdgsfnaq valgpdavdg tvvnvngtny
       61 tvtaadlang yitaaipvtg egpvaihaea vdaqgnvdva dadvtltidt tpqdlitait
      121 vpedlngdgi lnaaelgtdg sfnaqvalgp davdgtvvnv ngtnytvtaa dltngyitat
      181 ldataadpvt gqivihaeav daqgnvdvad advtltidtt pqdlitaitv pedlngdgil
      241 naaelgtdgs fnaqvalgpd avdgtvvnvn gtnytvtaad langyitatl dataadpvtg
      301 qivihaeavd aqgnvdvada dvtvtidttp qdlitaitvp edlngdgiln aaelgtdgsf
      361 naqvalgpda vdgtvvnvng tnytvtaadl angyitatld ataadpvtgq ivihaeavda
      421 qgnvdvadad vtltidttpq dlitaitvpe dlngdgilna aelgtdgtfn aqvalgpdav
      481 dgtvvnvngt nytvtaadit ngyitailaa taadpvtgqi vihaeavdaq gnvdvadadv
      541 tltidttpqd litaitvped lngdgilnaa elgtdgtfna qvalgpdaid gtvvnvngtn
      601 ytvtaaditn gyitailaat aadpvtgqiv ihaeavdaqg nvdvadadvt vtldvtppdi
      661 tttvlaidpv tadnildate aggtvtltgt ltnvpadatt tgvvvtingn dytatvdaia
      721 gtwtvnvagn dlaldpdltv dakatftdla gnsstlqdtq tytlagsita fdntdhavls
      781 pkpalvgddv slgstsylvl tsvagldlql ggnslgftvd aghegdvtfq ysglidaavl
      841 sdyklvvqkf ntttnqwesi hgdansslis lhllgigtgn vpgavldgld agqyraflay
      901 dgllglgvlg tlsatmddyd lsvaggyeig naegnvitdp dpttgqvdqv tantyvssvn
      961 ghpidadget fagtygtitf yqdgsyvyvp nadgsgvgqt dvftytltds vtgatgqanl
     1021 nivfdsiraa dnlvevelnp qyqlvgtetd safygvllnv gnivdlqllt vdtvdftiga
     1081 gqegvatfnf nsligasalg dynvvlqkyn dvtgqweavn gtgdrsllnl tllgntptaq
     1141 iggltegeyr aflsfnglvg gavavtlngs vdvynpavit gydvvaahgn lisdpntngd
     1201 vdiatpnsii sevngvavsa spteiigthg tlliyangdy tytpnadsag lgqvdqftyt
     1261 lldpasnits qatfyvhlds kvvdmnwdaa dpsqpatvti tavddavnaa iaaephlied
     1321 dralgsatyl allslaginl qaplpfvnst vefnvgaget gtatfkyssl inegalgdyq
     1381 lvvqkfntat nrwesitgss easllnlsvl gigvnatpgv vvegldegqy rafmtyngly
     1441 gksilgtlsg tmdvydpnqi dftglasegn vitglgvgtn adavtgytiv dsvtvngvtt
     1501 nvdpntgtii qgqygtlqif angdyiytpn ntnanlglvd hftytladpl ggnisasldf
     1561 tignstpvia vddlavavvn peylqigndv avdsylyval lsltdnfdfq lggqgidftl
     1621 tdstlndvtf nysalidasl ladyvlvvqk fdtatnqwva vngtgeadll slaafggnsv
     1681 tleglaagqy raymtyagsg vgvsllgtls vqkdvfdatn itgystqvae gnvihdvgln
     1741 ghadtasgfs tvtsvefngt afavnatgvt tivgdhgtls iyangnysyq pngeaaslgq
     1801 vdqftytlsd glntsqatly lhidsdavdm twntsdpsqp avitvtpvda idnvvsagvd
     1861 ivpqgelgva vgsatylalv gitedlnvsl lgtpsvafti dagheadvtf ayapvlslsl
     1921 fndykvvlqq kgadgawhni dggsstglln igllgnggig vtvpdlgqge yrafmvytgl
     1981 gvgilgtmsv vkddfdytva ptntavvadg nvltddvttl ttqvttvtse vvgalpqtvg
     2041 tdtvingayg tlvistnghy tytpnttdls aigkvdsfty tirdvltgat dtatlhvqvg
     2101 spdvtiawda anpandgvvq ltanpdhvvt ttdfsnaadl pvdvaspvvs vnligsnsvv
     2161 sdqfvvgagt vanidlsavy taqplasvlp tvsyviqswn gtawvntiys gsqtalgsva
     2221 tiqagsvafq dtvehlaagt yrvqytltgv slgatsldtn vstttvhldt yrsdwisgnv
     2281 lagdniggva dtgilshega klqvwdnaqn ayvdavgqti ntgngvlimq sngeyeyrpn
     2341 dvttttqlas tdsinykivs vtggvesqst ltidlthtdy nllytstsan dtfttgtgsd
     2401 tviyqllngt aatanngant ggngvdtwtd fhvgnvatdk qadlidiral ldgdqtdani
     2461 gqylnvttsg gnttiqidrd glsglipgnn fttllvlqgv tttetellnn gqily
//
LOCUS       WP_284933935             458 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase, partial
            [Clostridioides difficile].
ACCESSION   WP_284933935
VERSION     WP_284933935.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..458
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
     Region          <1..337
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 kigffglstq etksktgfkn veglefknpi esateqvnel kgkganviva ichigtnsls
       61 kpnsidiane vqgidliidg hshtkfengk qvgdtlivsa gqylenigei kltldtndve
      121 nikienksvr ligkeealky kldsavskkv deikeqqeki ldkvigvttn tldgsyenvr
      181 tketnlgnli sdilldktka dislfnggni rdtiekgnit rrdivdvfpf sntivtkelt
      241 gaqikdvleh gvklypekss aflqvggisy yfnpkqkege kitniqkegk pldlnkkyvv
      301 atndyiasgg defpcfskep vlkefgnles avieyieykk eisknvdgri gikskdelis
      361 knhesdlils eneknindne enlsnnikss dsdknksldk tsaressnlg iskreakeks
      421 pktgdlgfsn siiifivsst licllnfnqk elkdkksk
//
LOCUS       WP_284933982             458 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284933982
VERSION     WP_284933982.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>458
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          1..458
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mnqeiffkim neilenideg vhfvnkdgkt iiynnsvqkm ekmnrhdilt nsffdivnkm
       61 kinrstllev lekrevikdn iqkyldkngk eitainttip idikgefvga leisknmtti
      121 enllnrnykk nlvnkvsirq kkgyefddil gesnlikeai akskkacksd asvfiygetg
      181 tgkelfsqsi hygsnrrnyp fiaqncaalp eslfegilfg tskggftgai drpglfeqan
      241 kgtllldein smpimlqakl lrvlqegyvr rvggtkdipi dvriiattne spkvilnehk
      301 mrkdlyyrln iihikipplr drkedipllc kkfiskynkk lnkkvvgisd eaikilknyd
      361 wqgnirelen iiyctmsmme devqietsmi nlndyytlke nkesnnysln dledktlski
      421 iseieekyiy eslekasyni tkaasilgmn rqnlqyki
//
LOCUS       WP_284934005            2481 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Acinetobacter
            baumannii].
ACCESSION   WP_284934005
VERSION     WP_284934005.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..2481
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         <1..2481
                     /product="beta strand repeat-containing protein"
     Region          16..1654
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          1196..>2469
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 gsfnaqvalg pdaldgtvvn vngvnytvta adlangyita aipvtgegpv aihaeavdaq
       61 gnvdvadadv tvtvdtvpad ligaitiped lngdgilnad elgtdgsfna qvalgpdavd
      121 gtvvnvngtn ytvtaadltn gyitatldat aadpvtgqiv ihaeavdaqg nvdvadadvt
      181 ltidttpqdl itaitvpedl ngdgilnaae lgtdgsfnaq valgpdavdg tvvnvngtny
      241 tvtaadlang yitatldata adpvtgqivi haeavdaqgn vdvadadvtv tidttpqdli
      301 taitvpedln gdgilnaael gtdgsfnaqv algpdavdgt vvnvngtnyt vtaadlangy
      361 itatldataa dpvtgqivih aeavdaqgnv dvadadvtlt idttpqdlit aitvpedlng
      421 dgilnaaelg tdgtfnaqva lgpdavdgtv vnvngtnytv taaditngyi tailaataad
      481 pvtgqiviha eavdaqgnvd vadadvtlti dttpqdlita itvpedlngd gilnaaelgt
      541 dgtfnaqval gpdaidgtvv nvngtnytvt aaditngyit ailaataadp vtgqivihae
      601 avdaqgnvdv adadvtvtld vtppditttv laidpvtadn ildateaggt vtltgtltnv
      661 padatttgvv vtingndyta tvdaiagtwt vnvagndlal dpdltvdaka tftdlagnss
      721 tlqdtqtytl agsitafdnt dhavlspkpa lvgddvslgs tsylvltsva gldlqlggns
      781 lgftvdaghe gdvtfqysgl idaavlsdyk lvvqkfnttt nqwesihgda nsslislhll
      841 gigtgnvpga vldgldagqy raflaydgll glgvlgtlsa tmddydlsva ggyeignaeg
      901 nvitdpdptt gqvdqvtant yvssvnghpi dadgetfagt ygtitfyqdg syvyvpnadg
      961 sgvgqtdvft ytltdsvtga tgqanlnivf dsiraadnlv evelnpqyql vgtetdsafy
     1021 gvllnvgniv dlqlltvdtv dftigagqeg vatfnfnsli gasalgdynv vlqkyndvtg
     1081 qweavngtgd rsllnltllg ntptaqiggl tegeyrafls fnglvggava vtlngsvdvy
     1141 npavitgydv vaahgnlisd pntngdvdia tpnsiisevn gvavsaspte iigthgtlli
     1201 yangdytytp nadsaglgqv dqftytlldp asnitsqatf yvhldskvvd mnwdaadpsq
     1261 patvtitavd davnaaiaae phlieddral gsatylalls laginlqapl pfvnstvefn
     1321 vgagetgtat fkysslineg algdyqlvvq kfntatnrwe sitgsseasl lnlsvlgigv
     1381 natpgvvveg ldegqyrafm tynglygksi lgtlsgtmdv ydpnqidftg lasegnvitg
     1441 lgvgtnadav tgytivdsvt vngvttnvdp ntgtiiqgqy gtlqifangd yiytpnntna
     1501 nlglvdhfty tladplggni sasldftign stpviavddl avavvnpeyl qigndvavds
     1561 ylyvallslt dnfdfqlggq gidftltdst lndvtfnysa lidasllady vlvvqkfdta
     1621 tnqwvavngt geadllslaa fggnsvtleg laagqyraym tyagsgvgvs llgtlsvqkd
     1681 vfdatnitgy stqvaegnvi hdvglnghad tasgfstvts vefngtafav natgvttivg
     1741 dhgtlsiyan gnysyqpnge aaslgqvdqf tytlsdglnt sqatlylhid sdavdmtwnt
     1801 sdpsqpavit vtpvdaidnv vsagvdivpq gelgvavgsa tylalvgite dlnvsllgtp
     1861 svaftidagh eadvtfayap vlslslfndy kvvlqqkgad gawhnidggs stgllnigll
     1921 gnggigvtvp dlgqgeyraf mvytglgvgi lgtmsvvkdd fdytvaptnt avvadgnvlt
     1981 ddvttlttqv ttvtsevvga lpqtvgtdtv ingaygtlvi stnghytytp nttdlsaigk
     2041 vdsftytird vltgatdtat lhvqvgspdv tiawdaanpa ndgvvqltan pdhvvtttdf
     2101 snaadlpvdv aspvvsvnli gsnsvvsdqf vvgagtvani dlsavytaqp lasvlptvsy
     2161 viqswngtaw vntiysgsqt algsvatiqa gsvafqdtve hlaagtyrvq ytltgvslga
     2221 tsldtnvstt tvhldtyrsd wisgnvlagd niggvadtgi lshegaklqv wdnaqnayvd
     2281 avgqtintgn gvlimqsnge yeyrpndvtt ttqlastdsi nykivsvtgg vesqstltid
     2341 lthtdynlly tstsandtft tgtgsdtviy qllngtaata nngantggng vdtwtdfhvg
     2401 nvatdkqadl idiralldgd qtdanigqyl nvttsggntt iqidrdglsg lipgnnfttl
     2461 lvlqgvttte tellnngqil y
//
LOCUS       WP_284934443             378 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284934443
VERSION     WP_284934443.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..378
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <1..378
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 nfkmindtfg yefgdnllit iakalkeelt egevyarlss dyfaifcdyk ngrnkiirkl
       61 dnirsniesn lsivfeislc vgiyfveege vdiqkavnka nmarsvakgk ninyaiyned
      121 vrnklseesm ilddikialv knqfevyyqp kfslvtgemi gsealirwnh pehgfispav
      181 fipiaekskl ilkigrfvfe rvcndlsewk kqgkkivpvs vnlsrvelyq pdivkfinkt
      241 iqmynlssdf ieieitetva inelnilknv lnelrkhgfs ismddfgtgy ssisclrdmp
      301 idilkldksf lggiehders rniaksivsl aksldlvvii egveskeqae lmkqfgcdlv
      361 qgfyfarpmp aknfldll
//
LOCUS       WP_284934607             413 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [unclassified Brevibacterium].
ACCESSION   WP_284934607
VERSION     WP_284934607.1
KEYWORDS    RefSeq.
SOURCE      unclassified Brevibacterium
  ORGANISM  unclassified Brevibacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="unclassified Brevibacterium"
                     /db_xref="taxon:2614124"
     Protein         1..413
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43890
     Region          16..413
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mtdltrepts asagadssrd algglkvldm stlfagpmca tllgdygaev ikvenprqpd
       61 aarghgfqkd giglwwktlg rnkktlavnl keaagadlir slvadvdiiv enfrpgvmak
      121 wglgfealse inpglivvsv tgfgqfgpks sepgfgtlae amsgfasmtg qpdgpptlpp
      181 laladsiagi mgafaamtav hsrlsdgqgq hidmsliepm laalgpqvsv fdqlglvpkr
      241 lgnrsennap rnlyetadgr wlavstssqs iaervielvg hgeyveqewf ksakgrvehs
      301 delddavatw vrtkssqdal vafreahaaa slvynaedii edeqytalgs vididdqdlg
      361 smkmlnvpfr mshtpgrvqw tgrghgkdtd evlsglgvde etiadlrsrg vvs
//
LOCUS       WP_284934666              80 aa            linear   BCT 25-DEC-2024
DEFINITION  L7Ae/L30e/S12e/Gadd45 family ribosomal protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284934666
VERSION     WP_284934666.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>80
                     /product="L7Ae/L30e/S12e/Gadd45 family ribosomal protein"
     Region          6..>80
                     /region_name="Rpl7Ae"
                     /note="Ribosomal protein L7Ae or related RNA
                     K-turn-binding protein [Translation, ribosomal structure
                     and biogenesis]; COG1358"
                     /db_xref="CDD:440969"
ORIGIN      
        1 mknnkekvls flglatragk ivsgddstll dlkkgkvnli liaedasnnt kklfkdkstf
       61 rnipylffst keeigfaigk
//
LOCUS       WP_284934919             316 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator, partial [Clostridioides
            difficile].
ACCESSION   WP_284934919
VERSION     WP_284934919.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..316
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
     Region          <5..316
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 feeflykhis slckkiklgi nqspimaqdi kikypfafel aniakktiek dlkieinede
       61 vanialhigg averasynnk dkvfktiivc tsgigtsmli kaklenifke kleilkiips
      121 ylveyikvid vdfvistvpi evgdvpvini spilsekeir liekyietgn iyldldiksl
      181 fdselfftdl vfkrkeevid fmasklvqkg yidedmkksy ferekiatte ignmvtiphg
      241 aigkifdnki aigilkkpis weisdvrlii mlaldkdkil dyevifskiy krvdsiakvi
      301 sicenssfek fvnlfn
//
LOCUS       WP_284934870             176 aa            linear   BCT 25-DEC-2024
DEFINITION  IbrB-like domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284934870
VERSION     WP_284934870.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Maindola,P., Raina,R., Goyal,P., Atmakuri,K., Ojha,A., Gupta,S.,
            Christie,P.J., Iyer,L.M., Aravind,L. and Arockiasamy,A.
  TITLE     Multiple enzymatic activities of ParB/Srx superfamily mediate
            sexual conflict among conjugative plasmids
  JOURNAL   Nat Commun 5, 5322 (2014)
   PUBMED   25358815
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611634
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>176
                     /product="IbrB-like domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0071453 - cellular response to oxygen
                     levels [Evidence IEA]"
     Region          6..106
                     /region_name="IbrB_like"
                     /note="immunoglobulin-binding regulator IbrB activates eib
                     genes; cd16397"
                     /db_xref="CDD:319255"
ORIGIN      
        1 meykspvygi iavpiekies ndynpnavap pemqllyksi kedgytmpiv cyyneekdky
       61 iivdgfhryr vmlenediyd rengllpvsv idkslderma stirhnrarg shnvdlmski
      121 itelceigks dewiskhlgm evdeilrlkq itglaylfkd kefgnawipf gsdiee
//
LOCUS       WP_284935128             516 aa            linear   BCT 25-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284935128
VERSION     WP_284935128.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..516
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
     Region          1..516
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 npgfygdiai kdnliakids kinsninkei dccgkvmtpg fidphvheei vaildgkfek
       61 flkqgvttti ngncghsitp yssenvyeym ykngllleee kkylidknkc wnnfteycdl
      121 isksgisvnm gfllghgtir wsvmggskdr tptekeknei tdiindgmks gafgistgla
      181 yipskyadid elvdiarqik eydgiytshi rdyigrynav keaievgqks garvqvshls
      241 pveieafdei lkaryngvei mvdtvprssg hcmkkkrviq fimaissslf elgidgvmda
      301 lrneegrtli lkeafilgdr gsiillntkd inmekksire iatqkgided kllldllldg
      361 deelifclgg myradfpdkl hddkiidnpf vmvgsdclfs vggdmswfel qrrgafpiff
      421 nmyrksgvrl eeivrrvtsl parqfkiknr gilkegliad iavidmdnys ysrsedidfs
      481 kpqllangve yvivngkial engeitenkc gevlkr
//
LOCUS       WP_284935163             261 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284935163
VERSION     WP_284935163.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..261
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
     Region          10..107
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          <153..252
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 ivcednfvyl lpciqlrnwi snftisfpnq tiisdnytii phgsvtlvff ydatglhsll
       61 fgpttkpktv gnianrcdvi liiefqpagf fpligiqqse lidkvvpfsi intsldleik
      121 kifneslsid klilkleell isnikieysy efilaiqlii qnsgnissqe iskkvfyssr
      181 hlnrlfnqyl glsmksfsrl vrinksikll nnnktslmsi cnelgfydip hfikdfkivc
      241 gitpqkyran msdfyseiak f
//
LOCUS       WP_284935183             112 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284935183
VERSION     WP_284935183.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..112
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <1..112
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 aklieqvlin lidnslkysk edckieinvy ekddyvwfev sdngpgiske lkkhifdrff
       61 tgeegakdsr kgvglglsic ksiiqahkge imvennkdkg stfkfslpke ne
//
LOCUS       WP_284935184             443 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284935184
VERSION     WP_284935184.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..443
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          1..440
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 afeenyglkk edilgknvsf ledsgystks pipivlktkt kfsleqdtqt gkkliitatp
       61 ifdenghlef tvencrdite lnniknkled tkkqvkkyks evetlyrtal riedtvimdg
      121 ivmrpiintv nhvsktdvsv lllgesgtgk sslaryihhn snrsngpfit incatispql
      181 leselfgyts gaftgastkg kvglvelang gtlfldeigd ipqnlqakfl qliqdrtftp
      241 vgslknkkvd iriisatnvd lvskvkekkf redlyyrlnv ieiklpplre rrdnlveiik
      301 yyfnryssdf nlnktiskea mdaianyrfp gnirelqnii qkilltctdn hitiddlpni
      361 ltknihitnn gnkthisqin kviisdskst nyknknfdtl ikeyekniil dayekfgssy
      421 kvakhleisq skanrlirky tnt
//
LOCUS       WP_284935244             265 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284935244
VERSION     WP_284935244.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..265
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
     Region          4..226
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 lgtevsfrdr vriakeagfd giglraenyi daknagvtde emiailneyd mkvteveyit
       61 qwgreedrte aqrekeqnvy hmahlfnvkh incgllemip eeqiitalge lcdragelii
      121 glefmpysgv pdlatawrvv kgcnrenaml ildtwhwara kqtaedlapv padkivsiqv
      181 cdvletpyek lrdeslhdrl apgegygnte efvkiikehn isprvigaev isdsliskgl
      241 staaetvfna tkkvldkaws evspk
//
LOCUS       WP_284935372             213 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284935372
VERSION     WP_284935372.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..213
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          <16..>91
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
ORIGIN      
        1 llisilsifl vgcsfnkkde inlveqgkty lekhnykkam eslssaleed stnenaramy
       61 mqamrmsnmt efeelknyeg aikelkliek ikngssvike eatkkkeelt klekeqneae
      121 eqrkkkakdt agedryrves darkssysgs sknnkssskn ndkksdsnks dnsnsssqnq
      181 ekpnnsnptp aptpqdttgg sdsggnsqns nnq
//
LOCUS       WP_284935495             228 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Campylobacter vicugnae].
ACCESSION   WP_284935495
VERSION     WP_284935495.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..228
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26193
     Region          12..152
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mkhsvndyke hfefwenlil sgdriypsef vvrfafknkf ksvldfgcan grhlecfsra
       61 gatrligidl nqkpldlars rlepimksrg atlelysnkn csideilkdt kvdailawei
      121 vylytpnivi ellkslkshl nqngkilinf istddslksd akmlednmye iteathrgli
      181 ftfyslemie dllkkaglki isieknhywl dngaikhdyi niqathds
//
LOCUS       WP_284935567             612 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284935567
VERSION     WP_284935567.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 612)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 612)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..612
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <192..608
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 lqnkiycall ifsflfiisn ilgsfclnni dkipifitfl lnqiyllllp ipaalvsfyv
       61 maiiyqdiry mkkrllflsi pliiciilsi tnpfthilfg lsketgyirg cgyvatfasf
      121 ffyaiysafl sfkyrkamhe skiwairgfl ivsivaiilq aiflqylltg tacacslllt
      181 ylsmqnrgli iddltgvlnr qsfiqeldln inteqsgfii tialddfkfm netfgtkngd
      241 ialkevgkyl iqihdvnhvy riggdifsiv vnsqlgiepd diirkieerf kkpwlveeis
      301 fnlatsiavv yypenaette dvivaidfsi heakrsesrr vvyadasise kikkkhvikn
      361 clkealkndg fevyyqpifs nsrgrftsae allrlehkel gfippdefip iaeqtglins
      421 iglvvfekvc rfiasdefen lkldniavnl svvqcmqknl addllylmnk ynvsptkfkl
      481 eitetvamgs fniiketmer lidlgvkfal ddfgiaysgv tnmlslpfsv ikldksliws
      541 mnedsrhklt vetiialink lnmkavaegv etikcaedli ameceylqgy yfskpvpedv
      601 fknllkentf ts
//
LOCUS       WP_284935632             653 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF262 domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284935632
VERSION     WP_284935632.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 653)
  AUTHORS   Bair,C.L. and Black,L.W.
  TITLE     A type IV modification dependent restriction nuclease that targets
            glucosylated hydroxymethyl cytosine modified DNAs
  JOURNAL   J Mol Biol 366 (3), 768-778 (2007)
   PUBMED   17188297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>653
                     /product="DUF262 domain-containing protein"
     Region          1..553
                     /region_name="GmrSD"
                     /note="DNAse/DNA nickase specific for phosphorothioated or
                     glycosylated phage DNA, GmrSD/DndB/SspE family, contains
                     DUF262 and HNH nuclease domains [Defense mechanisms];
                     COG1479"
                     /db_xref="CDD:441088"
ORIGIN      
        1 mkageiefls ylegsnksfv vpvyqrnynw kkeqckrlfd dlediidsgf rthflgsvvs
       61 iysmgkeyli idgqqrvttv silliamcqi ikefgeskgi itteeqikec ylinkhsrdk
      121 dgkiklkpia edrkayyelf eeemntdrns nivsnylyfy nrikednisi ddlfdaiqkl
      181 tiveielkng eddpqlifes lnstgldlse adrvrnfvlm grssklqeef ynnywykiek
      241 ntssnvssfi rdyltikers ipnknkvyfs fkryvsdngi dieillkdll kfsnyyreis
      301 ysctddndvn kvlkrinkle ifvsypfile lfddynegii nkkvlvesln lvecfilrri
      361 vcdvppnaln kvfmnlgrei kkfsdykeny snilryifin kkssqrfptd sefsnafetk
      421 diyntksknk lyilerleny nnkeivdlen linnnmlnie himpqtltnk wkeslgdnyk
      481 eihdkylhti gnltltgyns klsnktfeek kemedgfkds rlylnkyiss idkwneeeik
      541 nrtkilldra veiwkypsvt yeppsnseni ftledddvnf tnesivsfsi lgesykaknw
      601 tefyeqvalt lydldsvrfn sivdktykrd fidniksrda yklrkgikis eni
//
LOCUS       WP_284935654             355 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: MlaE family ABC transporter permease [Campylobacter].
ACCESSION   WP_284935654
VERSION     WP_284935654.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter
  ORGANISM  Campylobacter
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Campylobacter"
                     /db_xref="taxon:194"
     Protein         1..355
                     /product="MlaE family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39237
     Region          111..350
                     /region_name="MlaE"
                     /note="Permease subunit MlaE of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG0767"
                     /db_xref="CDD:440530"
ORIGIN      
        1 mgrfefngdi lrlsgawdyr askselkrlk slkpskidla nlehidysia ifisknlgef
       61 elinsndkfd kifalvrdkg ilglaiykps kinslekigk iiidirvnii nfciflgqfl
      121 fvliagikep fkirfqelsn hivsaglgav givgltsfli givlayqgas mlnqfgasiy
      181 vvdimgimtl revgpliaai viagrsassf taqigvmkit eeieamktmg fdpfkfvvmp
      241 rivaliiavp lvvflanais ifaqmivckl yldfsfyeyl qrfkesvelr hffvgmlktp
      301 ffgaiiglig cmrgfevsgs tssvgelttr svvnaifwii aldalfsviy teldi
//
LOCUS       WP_284935685             264 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase, partial [Clostridioides
            difficile].
ACCESSION   WP_284935685
VERSION     WP_284935685.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..264
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
     Region          39..161
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 levekmndtv keklaeslts dttdilpylp yllqdfwelg sspeqmlqlf rkhipfnedt
       61 kvldlacgkg avsvklakel nihikgidli pefidyarrk aieykvdalc dfemndanss
      121 vkiehdydcv ifgavgdilg nyketiskll ptikskgfil iddayvvdks tneqlnferv
      181 yptynewcil fkelglklie cipclelend veeemnwiit ranelikkyp sqkdmfeqyv
      241 isqkneytdl qqdlvgatwi lqke
//
LOCUS       WP_284935715             149 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: c-type cytochrome [Campylobacter].
ACCESSION   WP_284935715
VERSION     WP_284935715.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter
  ORGANISM  Campylobacter
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 149)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 149)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Campylobacter"
                     /db_xref="taxon:194"
     Protein         1..149
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15988
     Region          79..149
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mnigkvialf lgglivvlml fmlfssdspt qatqepvkne pkpvtqttss ssefqtsdel
       61 nkikelkqsv sissdgvskl ylqscapcha kdgsgilaps iigrskedil arlneykagk
      121 ipnslmegll dnvsdenlti laeeiskfk
//
LOCUS       WP_284935730             257 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Campylobacter
            vicugnae].
ACCESSION   WP_284935730
VERSION     WP_284935730.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..257
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29147
     Region          4..256
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mnykiglklw slnenyiapa idlferevyd yielyavpns lemlpkwktl akehkikfai
       61 haphfssgld fsnpnklkhn lmlcdevkry snelealytv fhpgiggsln esirqmkmvq
      121 nlkfamenkp yivpmnsgea fcigadfnsi arildevgce fcldaghalc sanyqglnpy
      181 eyiaklnkln pkiyhisdnd enakldahmh fgdgsidlar vlrllrggef laietikdsk
      241 dnlddfiids nylksit
//
LOCUS       WP_284936132             704 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Campylobacter vicugnae].
ACCESSION   WP_284936132
VERSION     WP_284936132.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..704
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..704
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=77930
     Region          <21..107
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          213..703
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 mlvylgvati vpyasfvgsy ggvlgwynvr lfgyasyfyp fillypvynl yksytkfslk
       61 vagniigslm lfysfllfcs mfepmaggvv ggfssealrs vigsagtfif ilmiffiacg
      121 ltfddrldvm vkkafvvksk iepeakpkak eleptkleqs ksksqildsn ddvtsleinl
      181 etsknenlen epnilndeln inepkepkst ssgaiilsev aenkellnqi ekgkvekpkd
      241 fklpsldflk dppkrsksin eaeidqkiad lldklkrfki dgdvvrtysg pvvttfefkp
      301 aahvkvskil tlqddlamal kaqtiriqap ipgkdvvgie ipnknietiy lkeilesdiy
      361 knakseltla lgkdivgdpf itdlkklphl liagttgsgk svginamvls llyrnspktl
      421 rlimidpkml efsmyndiph lltpvitepk kaiavlanlv aemerryrim sqtrtknies
      481 ynekmkkdgg etlpfivvii deladlmmts gkevefhigr laqmarasgi hlivatqrps
      541 vdvvtglika nlpsrisyrv gqkvdskvil dqmgaesllg rgdmlftppg spgivrlhap
      601 faseeeidhi aeflkaqesv vyensflkdd sasssggvge fsgeidelyd eaksivlsee
      661 ktsisylqrr lkvgynraas iieqleqngv ltppnskgqr diir
//
LOCUS       WP_284936170             321 aa            linear   BCT 25-DEC-2024
DEFINITION  pseudouridine synthase family protein [Campylobacter vicugnae].
ACCESSION   WP_284936170
VERSION     WP_284936170.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kaya,Y. and Ofengand,J.
  TITLE     A novel unanticipated type of pseudouridine synthase with homologs
            in bacteria, archaea, and eukarya
  JOURNAL   RNA 9 (6), 711-721 (2003)
   PUBMED   12756329
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Ofengand,J., Malhotra,A., Remme,J., Gutgsell,N.S., Del Campo,M.,
            Jean-Charles,S., Peil,L. and Kaya,Y.
  TITLE     Pseudouridines and pseudouridine synthases of the ribosome
  JOURNAL   Cold Spring Harb Symp Quant Biol 66, 147-159 (2001)
   PUBMED   12762017
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10120734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..321
                     /product="pseudouridine synthase family protein"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=37117
     Region          80..301
                     /region_name="PseudoU_synth_RluA_like"
                     /note="Pseudouridine synthase, RluA family; cd02869"
                     /db_xref="CDD:211346"
     Site            order(116..119,247)
                     /site_type="active"
                     /db_xref="CDD:211346"
ORIGIN      
        1 mayikmkige fygqkiyqil lsngynmkea qklcdkgrli dsfdmvlnkn siangeifli
       61 dyecksvgle pifesdefgv fdkpsgvlth pngrncnysl cdeiwslwgk nasvahrldk
      121 etsgvivvgk siettkklks mfenrevfks ylalvngkve vdkfdkfklk nyidfmnkld
      181 fidsnnwlii dkamdlakdy ndikirmqic dngkraitlf rpikfdykrn ltlveciplt
      241 grqhqirlhm fyvkhkilgd piyglerddi erildgkmse neridktgan rlmlhsnrlk
      301 fnyngaefdi sskmkfglsi e
//
LOCUS       WP_284936181             191 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: anthranilate synthase component II [Campylobacter].
ACCESSION   WP_284936181
VERSION     WP_284936181.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter
  ORGANISM  Campylobacter
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Campylobacter"
                     /db_xref="taxon:194"
     Protein         1..191
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21426
     Region          3..190
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 mrvllidnyd sftynivyyl kelgvkvkvv kndfattkka ikyatkfdki iispgfgtpd
       61 dsgicvdiik alsskkpilg vclghqclak afggdiirmp rpfhgisiec efrksllfkg
      121 vkkplkialy nslcvkniae fdiladikve nksiimaikh kkyhcygvqf hpesilqaqg
      181 kkilknflnl k
//
LOCUS       WP_284936219             144 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: molybdopterin synthase catalytic subunit
            [Campylobacter].
ACCESSION   WP_284936219
VERSION     WP_284936219.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter
  ORGANISM  Campylobacter
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10091526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Campylobacter"
                     /db_xref="taxon:194"
     Protein         1..144
                     /product="molybdopterin synthase catalytic subunit"
                     /EC_number="2.8.1.12"
                     /GO_component="GO:1990140 - molybdopterin synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=16171
     Region          8..126
                     /region_name="MoaE"
                     /note="MoaE family. Members of this family are involved in
                     biosynthesis of the molybdenum cofactor (Moco), an
                     essential cofactor for a diverse group of redox enzymes.
                     Moco biosynthesis is an evolutionarily conserved pathway
                     present in eubacteria, archaea and...; cd00756"
                     /db_xref="CDD:238385"
     Site            order(14,18,27,29..33,35,37,86,95,97,105,109)
                     /site_type="other"
                     /note="MoaE homodimer interface [polypeptide binding]"
                     /db_xref="CDD:238385"
     Site            order(48,50,53,56,60,76,112..113,115,117..119)
                     /site_type="other"
                     /note="MoaD interaction [polypeptide binding]"
                     /db_xref="CDD:238385"
     Site            order(112,119)
                     /site_type="active"
                     /note="active site residues [active]"
                     /db_xref="CDD:238385"
ORIGIN      
        1 meiydgnlda neitsrwysd nklknygaim sfvgvvrden gisglsfdly epilkawfdr
       61 wqevaksqna iilmahskgd vavhessfia gvcspqrkva lklinefved fkanapiwky
      121 dligqkrvya lersqklqna gila
//
LOCUS       WP_284936261             161 aa            linear   BCT 25-DEC-2024
DEFINITION  SixA phosphatase family protein [Campylobacter vicugnae].
ACCESSION   WP_284936261
VERSION     WP_284936261.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..161
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18261
     Region          4..157
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mktiyfirha kakkiadsdf irelnnkgke aaklmskrlk nrnitpdiii sssanrtakt
       61 akifaknlkf nkdikfeksl yeasikeyld iikqidsvvn tvfivghndt ltqicellsd
      121 shigniptag vfgiefdvme fkeieartgk vllfdypkkf e
//
LOCUS       WP_284936351             209 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Campylobacter vicugnae].
ACCESSION   WP_284936351
VERSION     WP_284936351.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..209
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23555
     Region          38..137
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mlrdsaywde fykvehkeis qpslfakfif dsflnkkegk nliefgcgng rdslyfakng
       61 isvtaidssh iaiqklqkqn sdiswicgdf sakldidikf dicysrftlh aiddiaeqnl
      121 iqnvknllkp dglfvvears inddkfgvgk avgerefisd ghyrrfidpd ifqsnliang
      181 fkvisieqsn qfaptpgqnc vcirviakl
//
LOCUS       WP_284936354             429 aa            linear   BCT 25-DEC-2024
DEFINITION  ANL family adenylate-forming protein [Campylobacter vicugnae].
ACCESSION   WP_284936354
VERSION     WP_284936354.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10138310
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..429
                     /product="ANL family adenylate-forming protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=48588
     Region          121..425
                     /region_name="AFD_class_I"
                     /note="Adenylate forming domain, Class I, also known as
                     the ANL superfamily; cd04433"
                     /db_xref="CDD:341228"
     Site            order(122,125..130,132..133)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341228"
     Site            order(125,234..235,257..262,319,331,334,345,425)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341228"
     Site            order(125,160..161,207,209..210,213,234..235,257..262,319,
                     331,334,342..345,406)
                     /site_type="active"
                     /db_xref="CDD:341228"
     Site            order(160,209..210,213,234,342..344,400,406)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341228"
ORIGIN      
        1 mikslnlhan snkiaiidnl aefsyqdlls kvyelcqylk engvnsnqii aiygkysfdn
       61 ialfialyln qntiamipni ehtkiyldss nahklitldr kiidlktpnp innklknkng
      121 lilfssatlg kpkailhdls rlidshkdkk ernlrvllfl lfdhiggins llaglisgst
      181 lviakdftpq nicksiekfk vnilpttpsf lnllliskey qnydlsslrl itygtermnq
      241 nllkrlkstf knlkfiqtfg tsetgilrti sksssstrfk ldpneykivd grlflrsdtm
      301 flgylnhden inqwfdsgdl vdidkdgflq ilgrskelin vagnkllace vetcimeleq
      361 isdvivyskp slitgemvvc dvvstlnkde tkalikshck aklerykvpv kinlvnkinl
      421 tnrfkkvmk
//
LOCUS       WP_284936431              83 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Campylobacter vicugnae].
ACCESSION   WP_284936431
VERSION     WP_284936431.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..83
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=9526
     Region          <8..47
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
ORIGIN      
        1 mrgtiteali yenqglrdea levyknilkn dpsnqearsa irrlsglkrk dgetneqmle
       61 fylnlkdgda agirefkrwl iki
//
LOCUS       WP_284936450             355 aa            linear   BCT 25-DEC-2024
DEFINITION  GGDEF domain-containing protein [Campylobacter vicugnae].
ACCESSION   WP_284936450
VERSION     WP_284936450.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 355)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 355)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..355
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39868
     Region          <162..340
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mvtldkdkga kpaikqptss paatptkpvs rpdtssadse nvdlnkfssa vlkqllaeni
       61 qptpdnfdiy frklleskpa nfqkkvlell dfskedkldr qaliekdikt gfaqirsmmq
      121 iisliyknlg imkgiakkrl nemsasanpl evqgnikafg geleklnilm erhinaikas
      181 yeevdkifkn vednsiydsk fevynkkyll kilydefedv krykynvsim lihvkdsvln
      241 sipslkdkng ilrniakill ktsrrsdiva hygdgcfamv mkhtdlesak kasqrvaell
      301 yqttffmged eldmnmeisv gainpdssie eilsalldal prsgkgvklf esvev
//
LOCUS       WP_284936497             458 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284936497
VERSION     WP_284936497.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..>458
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <32..453
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 lnkkvevlsk eldsrnfklk tlneidffsk ipnrefmyqh iddcisknih igimllnidn
       61 fklfndiygy lvgenllitl tqnllhfipe skgivaylkg egflivlpnv snkelnnmga
      121 tiiesarelk iklpnekeiy snvtfsigst iwngepnmtt lmlfnqvysa lkkaksegkn
      181 ryilfdfkdn sfynklendk eflseishvl qtkqievfyq plyniknnti vgcealarwr
      241 hpikglltpd kfiplfeqfg liteldlhlf eencknirrw idnndvfvpi ccnfsrlhff
      301 npnfpsmlkg itekysvsts nfsieiteni lientntiiq qlaelrsygf svsmddfgsg
      361 yssfgmlqnl pfdiikidri flshnlndfk nttilysiin iaralgmltv cegveteqhv
      421 efiksincdi aqgyyyakpm eckefeklls kennsekm
//
LOCUS       WP_284936546             812 aa            linear   BCT 25-DEC-2024
DEFINITION  efflux RND transporter permease subunit [Campylobacter gastrosuis].
ACCESSION   WP_284936546
VERSION     WP_284936546.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 812)
  AUTHORS   Sandhu,P. and Akhter,Y.
  TITLE     Evolution of structural fitness and multifunctional aspects of
            mycobacterial RND family transporters
  JOURNAL   Arch Microbiol 200 (1), 19-31 (2018)
   PUBMED   28951954
REFERENCE   2  (residues 1 to 812)
  AUTHORS   Hand,N.J., Klein,R., Laskewitz,A. and Pohlschroder,M.
  TITLE     Archaeal and bacterial SecD and SecF homologs exhibit striking
            structural and functional conservation
  JOURNAL   J Bacteriol 188 (4), 1251-1259 (2006)
   PUBMED   16452406
REFERENCE   3  (residues 1 to 812)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
REFERENCE   4  (residues 1 to 812)
  AUTHORS   Arkowitz,R.A. and Wickner,W.
  TITLE     SecD and SecF are required for the proton electrochemical gradient
            stimulation of preprotein translocation
  JOURNAL   EMBO J 13 (4), 954-963 (1994)
   PUBMED   8112309
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..812
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=91830
     Region          1..804
                     /region_name="MMPL"
                     /note="Predicted exporter protein, RND superfamily
                     [General function prediction only]; COG1033"
                     /db_xref="CDD:440656"
ORIGIN      
        1 mlkkifkflv aypkfiltal lflslffgyw atrleidass etlliendkd latwreisqr
       61 ykspnflvva ytpkgdilsd eslkfiddls selgknelvn nvisilnvpl lksvkggisa
      121 ildhtptlkd adidknlard elknspiysq nliskdlktt aivlnlktde rfnqlldern
      181 hlltlennat avkkleeiks efkayrdalr lkehknldai katlakfnse enalflggam
      241 miaddmvgfv ksdistygvs valllalslw lffrqvrwil lpificvlsv ffsmglfgff
      301 gweitvissn fislvliisi svvihlivsy reffikyphf sqrqlvyltl ldkaspsfwa
      361 ifttiigfis lmsadikpvs mlglmmsagi gvslilafvi fssvvcllkk lppkrtfedk
      421 fsftkkcanf aindkrliyt asfvlvlfgi ygileikien sfigyfkkdt eirrgmevid
      481 nklggtipld iivkfkktde kndeisdefe defnadknds kywfnsyhtr vaekihdylt
      541 gqnfvgqvss latlikvike lnngvvddfl laamyeklpe nykeillspy vmvsddelrf
      601 slrvvdsder lrrdkflkel ksglenltqn dgveiqiagm mvlynnvlqn lvssqvktfg
      661 vsvlvlfvlf clifrdlkia tiaimtnlvp lcvifgimgv fgipldvmsi tiaaislgig
      721 vddiihythr flqerrtngv iksiqnshas igyamyytsf givlgfsvmm tsnfiptiyf
      781 glltdlvmgl mllsalvlmp rliistylkd kr
//
LOCUS       WP_284936566             273 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase [Campylobacter gastrosuis].
ACCESSION   WP_284936566
VERSION     WP_284936566.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..273
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=31771
     Region          2..231
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mlilgntlde lkkladdsvd mgvtsppynk qenkkgwlvs nikyanvtdk kpeniyqeeq
       61 ilvlnelyri ikpggsffyn hkvrwekgim lhpyawisks kwnirqeiiw draiaanirg
      121 wrfwqieeri fwlhkpkdkk dligkellsk halmtsiwri rpegknphpa pfpltlptrc
      181 iysilenngv vidpycgsgt tlvaakllgh kfigidiset ylqqaktrle nsqnelkiid
      241 dekklhfvae tfsekkargm hkkftqkqkl lfe
//
LOCUS       WP_284936678             356 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Campylobacter
            gastrosuis].
ACCESSION   WP_284936678
VERSION     WP_284936678.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..356
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=39740
     Region          6..356
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mfkknrlvfn lhllltflaf lplfimsisg sivayraeik eiinqnlfsv evgenkqkis
       61 eiltnlkakn gdfeirnidi nkdgvyhiyt qgvggrnayf anpyngeiyd dvgfkamfva
      121 lmfhrnlgls llenktasti gkhivaissi slallilsgi wlylplikkn ftkslmfkia
      181 lkgrafwyql haslglwtai lllimslsgl fwsygfvrda intafgvkte qravknakss
      241 vnfsdfdrav lalnadfdka tissnaknls ykkggenfsf lvennatltp lnkaenigkm
      301 daravsrlml sihqgdifge vgrvmfclsc llinlfiisg fvmlfkrinp ksalkk
//
LOCUS       WP_284936752             435 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Campylobacter
            gastrosuis].
ACCESSION   WP_284936752
VERSION     WP_284936752.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..435
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47471
     Region          1..432
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mkhydiailg fgkagktlav ranalnksva vveksaqmyg gtcinvgcip tkklitlskm
       61 akfhenkdef fkkavglkne lilalraknf amldslknve vitqtasfvd kntillspsg
      121 ekitadkiii ntgsksikpn fsvksdivyq sdeilelghl pkhlvvvggg figlemasmf
      181 anfgskvsvv lrseilkned ddvrevlikn lenqgvnfiq nakiseingd kiyfndsfle
      241 adafllslgr tpniddlelk nagvlvnkrg gvatdeclrs eisdifavgd argdefftyi
      301 slddfrivns ylfgdktrtk nnrspyakvl ftdtpfakig lsereagenv kvlkvmmqnv
      361 pnakilgndt gflkaicdka sgeilgasfi canaheiine iaiamkfrak asdlagqift
      421 hpstsealnd lfsqf
//
LOCUS       WP_284936693             588 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Campylobacter
            gastrosuis].
ACCESSION   WP_284936693
VERSION     WP_284936693.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 588)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 588)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 588)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..588
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=65414
     Region          1..567
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mnsrksktti lflfiavglv iflsviiyra tidkrhlylq treensalrg siitkdgfsv
       61 aisqklytak intksidpnk kemfirlysl ysgedekkir klingtngll vlsdkidakt
      121 amhlkelsrk lyqkkifvpi ddsstiqsln ifeskesrkn rtymaqnalt pvlgyisqkd
      181 dksigakgve ryyneflspi qdarivgfkd igrniiftsd lnlqnridgy nlaisvnlkf
      241 qtmvekivda qasfvdakei iacvmdsktg eilalasslr ydpssikqqd iqalnstate
      301 yayeigsvfk pfifsillse tklnkmalvn thngsyklgk riikdthpap fltaedviae
      361 ssnigmiela kkltgtqiyn gllnfgftqk sgidmpyeqt gaippaqkld sqtykatvsy
      421 gygvsatfmq lmkaynvfnn kgfavvphfa lflelngkky apqikppkei isqeiakqmk
      481 svlikvvekg tgkkaltpgl evggktgtah iarkgvygni yngsffgfan dkkgnaytig
      541 vlarepkkky yyygaqsalp vfkkivdlmv aegylmpdet ainqinnk
//
LOCUS       WP_284936774              79 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284936774
VERSION     WP_284936774.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 79)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 79)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..79
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
     Region          <1..74
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 spnylssifn ernkvsitey inllrieesk kylldrsmsi sdickkvgfn nssyfsqifk
       61 kfnsitpney rknmldnky
//
LOCUS       WP_284937055              87 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy-metal-associated domain-containing protein [Campylobacter
            gastrosuis].
ACCESSION   WP_284937055
VERSION     WP_284937055.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 87)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086127
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..87
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9504
     Region          23..80
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(26..28,31)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
ORIGIN      
        1 mrkililalf lafsfgkdie ifvqgihcpl ctsvvrksll kvngvksarv elktqtafvi
       61 addfldekdl leaiknvgyp gvikglk
//
LOCUS       WP_284935551             211 aa            linear   BCT 25-DEC-2024
DEFINITION  MORN repeat-containing protein, partial [Clostridioides difficile].
ACCESSION   WP_284935551
VERSION     WP_284935551.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Zhou,J., Liu,H., Lin,Y. and Zhao,J.
  TITLE     Membrane occupation and recognition nexus (MORN) motif controls
            protein localization and function
  JOURNAL   FEBS Lett 596 (14), 1839-1850 (2022)
   PUBMED   35568981
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Sajko,S., Grishkovskaya,I., Kostan,J., Graewert,M., Setiawan,K.,
            Trubestein,L., Niedermuller,K., Gehin,C., Sponga,A., Puchinger,M.,
            Gavin,A.C., Leonard,T.A., Svergun,D.I., Smith,T.K., Morriswood,B.
            and Djinovic-Carugo,K.
  TITLE     Structures of three MORN repeat proteins and a re-evaluation of the
            proposed lipid-binding properties of MORN repeats
  JOURNAL   PLoS One 15 (12), e0242677 (2020)
   PUBMED   33296386
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..211
                     /product="MORN repeat-containing protein"
     Region          <69..182
                     /region_name="COG4642"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443680"
ORIGIN      
        1 lcvficlssv fiftqlarvf inkkkinqki ksrngfrydr dfiearreei hikdnnnnkn
       61 ksnnkklkee kvfkydngdl ykgefvdgkk ngfgiyifsg kekyeglwkd dkmhgigkyt
      121 yrdgsiytge fkyglknglg kltypnndiy kgyfldnkkn gkgvlykndg nkqagiwedd
      181 eqcksldfkd lnnnkinnvy qnrlnnnklk v
//
LOCUS       WP_284937079             263 aa            linear   BCT 25-DEC-2024
DEFINITION  cell division protein FtsX [Campylobacter gastrosuis].
ACCESSION   WP_284937079
VERSION     WP_284937079.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..263
                     /product="cell division protein FtsX"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=29744
     Region          <89..253
                     /region_name="FtsX"
                     /note="Cell division protein FtsX [Cell cycle control,
                     cell division, chromosome partitioning]; COG2177"
                     /db_xref="CDD:441780"
ORIGIN      
        1 mrsisfilal isllfavqfs vlcanvvkey eklmnsdyni iivstkelte pelrplvptl
       61 ssllplsakk ivdrlnndis sknlsilqna lpkfytlkln alpsteymkq irqkllnidg
      121 vskvetflrt hdkvyktlnl lkfisyifig ivgftglllm srqiriwsfe hrdrieimsl
      181 fgasfwqksa vlyryaifss ivatlvvtai fyflpdfiss kelisqisia vpkislidea
      241 ptllgislfi sifmvsvvtk rvs
//
LOCUS       WP_284937156             206 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Campylobacter gastrosuis].
ACCESSION   WP_284937156
VERSION     WP_284937156.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..206
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=23290
     Region          <26..196
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mrpigstker laiyerefin llcliscdks lqpstrhklt raftllyltg crvseivnls
       61 fediqnifth kslalngatk trkprtiffn knmlnmllkl tyydtnehng flfyengkdi
      121 pmskkgltal lnthlakhls plytthsfra gyvtriveat gnlktaqdii ghksinttig
      181 ylstskqqkl daldkifgdd kctlsh
//
LOCUS       WP_284937287             146 aa            linear   BCT 25-DEC-2024
DEFINITION  molybdopterin synthase catalytic subunit [Campylobacter
            gastrosuis].
ACCESSION   WP_284937287
VERSION     WP_284937287.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10091526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..146
                     /product="molybdopterin synthase catalytic subunit"
                     /EC_number="2.8.1.12"
                     /GO_component="GO:1990140 - molybdopterin synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=16294
     Region          8..125
                     /region_name="MoaE"
                     /note="MoaE family. Members of this family are involved in
                     biosynthesis of the molybdenum cofactor (Moco), an
                     essential cofactor for a diverse group of redox enzymes.
                     Moco biosynthesis is an evolutionarily conserved pathway
                     present in eubacteria, archaea and...; cd00756"
                     /db_xref="CDD:238385"
     Site            order(14,18,27,29..33,35,37,86,95,97,105,109)
                     /site_type="other"
                     /note="MoaE homodimer interface [polypeptide binding]"
                     /db_xref="CDD:238385"
     Site            order(48,50,53,56,60,76,112..113,115,117..119)
                     /site_type="other"
                     /note="MoaD interaction [polypeptide binding]"
                     /db_xref="CDD:238385"
     Site            order(112,119)
                     /site_type="active"
                     /note="active site residues [active]"
                     /db_xref="CDD:238385"
ORIGIN      
        1 mqiydgsldv caifnqwhke svsqncgali tfvgivrged giealsfdiy epllqkwlns
       61 wqdiaksqna kvffahskgd vkvgessyia gvlspkrkva lrlinefved fkanapiwky
      121 dvkngvriya kersqklpna gilskd
//
LOCUS       WP_284937314             358 aa            linear   BCT 25-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Campylobacter gastrosuis].
ACCESSION   WP_284937314
VERSION     WP_284937314.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..358
                     /product="MlaE family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39478
     Region          108..354
                     /region_name="MlaE"
                     /note="Permease subunit MlaE of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG0767"
                     /db_xref="CDD:440530"
ORIGIN      
        1 mkkivfsddk illngdlsyk drqfcvvfad lsrknstidf sslvsidyac aillanfrdk
       61 tgakfinmse kislifalvd dkkidksail kpkrenffai lgrnfalfwq hfiplcsflg
      121 efiinffkaf ltpknfrake lsnyikdsgi navfivllts fligivlayl gsamlaqfga
      181 sifivdimgv ltlreiapli gaivvagrsa ssfaaqigvm kiteevdamk tmgldpfkfl
      241 vlprvlamii alpvviflad lvsvfgqmlv sknildigfs eylgrfkdsi elrhlyvglv
      301 kapffgaaia ligcfrgfev sqnaqslgek ttisvvnaif aviaidsvfa vffmwygv
//
LOCUS       WP_284937460             337 aa            linear   BCT 25-DEC-2024
DEFINITION  GGDEF domain-containing protein [Campylobacter gastrosuis].
ACCESSION   WP_284937460
VERSION     WP_284937460.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 337)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..337
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38029
     Region          <157..321
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mlkidnapky hqtrqgvakq eekdiyqfse svlkelsqdn ipsipsnysi yfeklldert
       61 sefkeklgsa ltfyeeggqk mtessifiek eikqgfvqik smlqavaliy knlglmkgit
      121 kkhiatlhsn tdllavqnvl svfnddlikl vslmdkhvev iranyeeigk mfkaieeqtv
      181 ydanyevynk kflinameie vtsskrygyh tsfvitkvde kilfttnnlk erndllksva
      241 qillktsrrs divahygdgf fiivmkhtdl dgaklacarl nklfsgikhn vggaeivvnl
      301 nmvageltke gssmeevlsk aldtiastda kepifle
//
LOCUS       WP_284937548              70 aa            linear   BCT 25-DEC-2024
DEFINITION  tautomerase family protein [Campylobacter gastrosuis].
ACCESSION   WP_284937548
VERSION     WP_284937548.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..70
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=7654
     Region          2..62
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mpyinikitk engtptkeqk erlalgvtel feqilgrsgk navvvideie penyaigget
       61 isqkiqkgvr
//
LOCUS       WP_284937552             275 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Campylobacter gastrosuis].
ACCESSION   WP_284937552
VERSION     WP_284937552.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..275
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=30530
     Region          42..>142
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Site            order(165..166,169..170,172,196,199..200,203..204,
                     206..207,233,236..237,240..241,244)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          165..189
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          169..270
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Region          194..224
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          232..259
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkkkilsvai lsailpllae vsafdagnln sqnpygltds ekevlknrqn vaslesslgs
       61 ieeqiqgmqs llegvsarms rleqrvnele iringdtnss gesiaslkay vddtralqek
      121 nyknitdtln klgslidkks sqtitktesa spktelskks nkeifdeavk lfnsnkndea
      181 kayfehlisk nnrpatsnfy lgeiaykeks yataikhyqk sielddkasy lpkllyhtgi
      241 sfdkvgdtns anrfyralkv gypdtkeaqa tperk
//
LOCUS       WP_284937582             190 aa            linear   BCT 25-DEC-2024
DEFINITION  cytochrome c3 family protein [Campylobacter gastrosuis].
ACCESSION   WP_284937582
VERSION     WP_284937582.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..190
                     /product="cytochrome c3 family protein"
                     /calculated_mol_wt=21138
     Region          5..170
                     /region_name="NapC"
                     /note="Tetraheme cytochrome c subunit NapC of nitrate or
                     TMAO reductase [Energy production and conversion];
                     COG3005"
                     /db_xref="CDD:442242"
ORIGIN      
        1 mpntkkkifv wssvivgvii gliasmgvad vlhatgsgyt ctmchtmdam naayhedthg
       61 gknklgikae csachldhts aytyvltkik vsindgyktf ftdtdkidwq kkrehrshfv
      121 ydsgcltchs nlkdviqagk sflphreyfi lgnknnktcv dchenvghkn lgfhidkaek
      181 lkiekttske
//
LOCUS       WP_284937657             144 aa            linear   BCT 25-DEC-2024
DEFINITION  Dps family protein [Campylobacter gastrosuis].
ACCESSION   WP_284937657
VERSION     WP_284937657.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Choi,S.H., Baumler,D.J. and Kaspar,C.W.
  TITLE     Contribution of dps to acid stress tolerance and oxidative stress
            tolerance in Escherichia coli O157:H7
  JOURNAL   Appl Environ Microbiol 66 (9), 3911-3916 (2000)
   PUBMED   10966408
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   6  (residues 1 to 144)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..144
                     /product="Dps family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16422
     Region          6..142
                     /region_name="DPS"
                     /note="DPS protein, ferritin-like diiron-binding domain;
                     cd01043"
                     /db_xref="CDD:153102"
     Site            order(19..20,24,26..27,38,49,53,56..57)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:153102"
     Site            order(26,38,42,53,57)
                     /site_type="other"
                     /note="DPS ferroxidase diiron center [ion binding]"
                     /db_xref="CDD:153102"
     Site            order(118,125..126)
                     /site_type="active"
                     /note="ion pore [active]"
                     /db_xref="CDD:153102"
ORIGIN      
        1 mskviaqlnq iqadahalyv kfhdlhwnvk giqffsvhey tekayddmse ifdavaeral
       61 mlggrpvvkq dellklshvk ydvkdsytpt evlelvlady khllaefkkl delaegdstt
      121 qtyaqdeiak yekaiwmlna tlgr
//
LOCUS       WP_284937855             460 aa            linear   BCT 25-DEC-2024
DEFINITION  MBOAT family O-acyltransferase [Campylobacter gastrosuis].
ACCESSION   WP_284937855
VERSION     WP_284937855.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Hofmann,K.
  TITLE     A superfamily of membrane-bound O-acyltransferases with
            implications for wnt signaling
  JOURNAL   Trends Biochem Sci 25 (3), 111-112 (2000)
   PUBMED   10694878
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004295
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..460
                     /product="MBOAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53031
     Region          1..460
                     /region_name="DltB"
                     /note="D-alanyl-lipoteichoic acid acyltransferase DltB,
                     MBOAT superfamily [Cell wall/membrane/envelope
                     biogenesis]; COG1696"
                     /db_xref="CDD:441302"
ORIGIN      
        1 mtffsvefll iflaffaiyw afskhykaqn tlilifnyal ifsfspyfml viflhtffvs
       61 yfglfiaykg sknaifsgvf fsilylcffk yydvihadfr avllffkfdf iannldialp
      121 igisfytfss vtylvsiykk eqapsdflsl acylsffatl iagpiakstf mlpqfntkre
      181 fkngdlivvl llfgvvkkvl ianylsgfvt eifndpksfn pleiltaiyc ygvwlycdfs
      241 gyvdivsala lsigfalpln fnmpyvalnl rdfwrrwhis lsnfirdyiy iplggnkvtf
      301 fhtqvnilia fslsgiwhgv glnfviwgll hgfgivflnl malfkinfsk hlplvsmllt
      361 ytfvsfswvy faksdlnean liikslfyne nfinlsqivt lfalfllfvi ypffkdlkei
      421 lvqflkatpl llkplllsii ftfifavckd gipdfiyasf
//
LOCUS       WP_284937895             238 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Campylobacter gastrosuis].
ACCESSION   WP_284937895
VERSION     WP_284937895.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..238
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26572
     Region          16..>172
                     /region_name="SmtA"
                     /note="SAM-dependent methyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG0500"
                     /db_xref="CDD:440266"
ORIGIN      
        1 mlnndfgfys eqiklwdkla vsgdliyphe avarfaattk ppcvidfgca tgrhllafan
       61 kgskrligid intsplalta lkfgvidels qfkqgkylln dgqlelysne grnlgeilgs
      121 vqadavlcwg vlhlyhkdla lkllidfksq lksggevfin lrsdtdglkn eaikigeniy
      181 kitrkshenl tysfyslddl neifsksglk ilsidkeeft qnngkifnsf wivrakkd
//
LOCUS       WP_284938324             193 aa            linear   BCT 25-DEC-2024
DEFINITION  6-pyruvoyl trahydropterin synthase family protein [Campylobacter
            gastrosuis].
ACCESSION   WP_284938324
VERSION     WP_284938324.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Phillips,G., Grochowski,L.L., Bonnett,S., Xu,H., Bailly,M.,
            Blaby-Haas,C., El Yacoubi,B., Iwata-Reuyl,D., White,R.H. and de
            Crecy-Lagard,V.
  TITLE     Functional promiscuity of the COG0720 family
  JOURNAL   ACS Chem Biol 7 (1), 197-209 (2012)
   PUBMED   21999246
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Colloc'h,N., Poupon,A. and Mornon,J.P.
  TITLE     Sequence and structural features of the T-fold, an original
            tunnelling building unit
  JOURNAL   Proteins 39 (2), 142-154 (2000)
   PUBMED   10737935
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..193
                     /product="6-pyruvoyl trahydropterin synthase family
                     protein"
                     /EC_number="4.1.2.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22338
     Region          1..148
                     /region_name="QueD"
                     /note="6-pyruvoyl-tetrahydropterin synthase [Coenzyme
                     transport and metabolism]; COG0720"
                     /db_xref="CDD:440484"
ORIGIN      
        1 miirkmfkfe nahivrdcss krcrtsihgh sykaeillss nyldnagmvy dfglmkqgik
       61 ciidsfdhat tifsgdndey kndlkkhser wieiplnpsa eqfcriffvi idrllsatkm
      121 qngerdvkih sviihetdtg yaqcfkeday nakmgeinln eiifseaiis ewedkklfek
      181 ikfkdeivnp kdv
//
LOCUS       WP_284938340             380 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Campylobacter gastrosuis].
ACCESSION   WP_284938340
VERSION     WP_284938340.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..380
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=41612
     Region          1..376
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mnlntllvkg isahtdqhka vvppiylsst faqdgldefg kfcysrglnp ttdafetlfa
       61 kiegakccis fssgmaatta afhllksgdk vllnnnvygg tfryahtifa dngikyelvd
      121 dlnviteddl tpdvkmifve tpsnpllrvt dikkivelah kkgilvvadn tfltpyfqkl
      181 ldfgvdvvvy satkyiggha dviagiattn deklgeklrf ikntlgsnls ptdayslirg
      241 lktlsvrfdr qmqnthkiie flksneaidv vhyagsrsey eakvqksqag digalisiel
      301 nqnydykkfa kslklfdlav slggveslic qpssmthesy paelqekigi kpnllrlaig
      361 vedandliad lanaiklskk
//
LOCUS       WP_284938389             364 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Campylobacter gastrosuis].
ACCESSION   WP_284938389
VERSION     WP_284938389.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..364
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42250
     Region          1..349
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mvlfvaksit tfglieqddt lkslfqiikf eekvkqsfie qkflpnslif kyaiydengt
       61 eifsnlakkp sdlkfvtlkd ddtlfykdff finktpyfli isqeissrrn lfiitlmltf
      121 tfilvafvly lsylasikpy qnaqkymnnf fndamhelkt plgiaginle mlgienkqtk
      181 riknalkqmq ityedieyyi krgyiifpne iidlseylie rvkfllsmad akrmkvvfdd
      241 idrgvnivms kmalqrvidn titnaikysp qdsqiiiklk rqddgiaifs vqdfgcgikd
      301 vkkafkryer enlaqggfgl glsivsdice kysinydvkt klnegstffy kfhiakldft
      361 kvke
//
LOCUS       WP_284938544             554 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Clostridioides difficile].
ACCESSION   WP_284938544
VERSION     WP_284938544.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 554)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..554
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=64741
     Region          7..471
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(21,23,25,29)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(60,63,100,103,142,161,165,197,254,413)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(197,254,328)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          481..>522
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; cl02706"
                     /db_xref="CDD:445893"
ORIGIN      
        1 mekkwwqkei vyqiyprsfq dsnndgigdl qgiisrldyl knlgitslwl cpifkspmdd
       61 ngydisdyld iasefgsmed lkelikeskd rgikiildlv lnhtsdehpw fqealknpes
      121 syhdyyifkk gndlpnnwrs vfggsvwekv enrdeyyfhs fgkkqpdlnw enpilrsely
      181 qmintwsqmg vagfrvdait fikknlsfqs lesdgvdglv kctktvrnqp giekmlyelk
      241 entfkkydcm tvaeaagisy dqlgdfiged gffsmvfdfk hadldvasgs ewfkriswti
      301 pdlrkcilds qmyvqehgwa anfienhdqp rattkyllqy ernddavkml gamyfflrgt
      361 pfiyqgqelg mtnfkrdtin dfndlssidq yyrsidegys eeealefvnl rsrdnartpf
      421 pwadkenagf sdttpwlkvi enykdinaqs qinnsesile fykkmiklrq dseysdcliy
      481 gsiepidies edviayrrql dlvvidcyyn fsdkpveirv eekydivfqn lddinplnkt
      541 vrlkpfhavl lkar
//
LOCUS       WP_284938672             313 aa            linear   BCT 25-DEC-2024
DEFINITION  lipase family alpha/beta hydrolase [Acinetobacter baumannii].
ACCESSION   WP_284938672
VERSION     WP_284938672.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18498059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..313
                     /product="lipase family alpha/beta hydrolase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33527
     Region          27..138
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
     Region          32..282
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mlsglsvsat hatnaeqvks sfvystyaqt kyplvfnhgm agfnrvgtdt lgldywyqil
       61 hdlarnggnv watrvspfns tevrgeqlaq qveeiiaitg kpkvnlighs hggptiryva
      121 gimpekvasl ttigaphkgs pmadvilnve gtplsglatl vnwfsaaitw aggldpnsyp
      181 hdslagahsl stqgsaqfns qfpmgvptts cgegayqekg iymysfsgnk altnpldpfd
      241 ialtgsslvv dpfgdndglv srcsakfgkt irddynwnhl devnqvmgir sifaadpvsv
      301 yrqhanrlkl qgl
//
LOCUS       WP_284938761             313 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284938761
VERSION     WP_284938761.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..313
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          77..306
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 klvletikin iilvciifil ifvlvvryfk siyndlsdmt kyvyyssegk qfdmknknqe
       61 gqigllktel lkmttilnek vellkrekif lnntisdish qlktpmtsli mlndllyndv
      121 pyevkidfln kiknqlnrmd wliksmlkls kveakvinfk kdkvkfseli hramlsmkip
      181 meiknqklti egndnvsyig didwsvealv niikncveht pefgniiity kenplfseli
      241 ikdegegidk kdiphvfkrf yrgrsssked svgiglamsk siiesqngdi yvnsekgkgt
      301 efhiifhkmy dsd
//
LOCUS       WP_284938791              77 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Campylobacter
            gastrosuis].
ACCESSION   WP_284938791
VERSION     WP_284938791.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gastrosuis
  ORGANISM  Campylobacter gastrosuis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Campylobacter gastrosuis"
                     /db_xref="taxon:2974576"
     Protein         1..77
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8504
     Region          7..>33
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
ORIGIN      
        1 maddsivkrv ckelnitqre laerigmsad slrtlsakgq issqteaaln lvleneqlkk
       61 elenykvlkv aiktmid
//
LOCUS       WP_284938868             240 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor, partial
            [Clostridioides difficile].
ACCESSION   WP_284938868
VERSION     WP_284938868.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 240)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 240)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..240
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
     Region          6..228
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 clrivinigi cddelhyrik ikdilseils sypinyniye fsageellnn ypkdldilim
       61 diqmktingm dtarkirefd hkleiifvts fvefmqegye vkayryilkp inkekisksv
      121 lpcinemmkk rnnyltinvk nyvdrikids ityietdrpn iliythddmy itkmsiskie
      181 kilneygffr chnsyivnlk lvesmsgstv ivdgksipis kyrvkglkla itnilgdivc
//
LOCUS       WP_284938879             371 aa            linear   BCT 25-DEC-2024
DEFINITION  C45 family autoproteolytic acyltransferase/hydolase [Clostridioides
            difficile].
ACCESSION   WP_284938879
VERSION     WP_284938879.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   True,J.R., Yeh,S.D., Hovemann,B.T., Kemme,T., Meinertzhagen,I.A.,
            Edwards,T.N., Liou,S.R., Han,Q. and Li,J.
  TITLE     Drosophila tan encodes a novel hydrolase required in pigmentation
            and vision
  JOURNAL   PLoS Genet 1 (5), e63 (2005)
   PUBMED   16299587
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tobin,M.B., Cole,S.C., Miller,J.R., Baldwin,J.E. and
            Sutherland,J.D.
  TITLE     Amino-acid substitutions in the cleavage site of acyl-coenzyme
            A:isopenicillin N acyltransferase from Penicillium chrysogenum:
            effect on proenzyme cleavage and activity
  JOURNAL   Gene 162 (1), 29-35 (1995)
   PUBMED   7557412
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Tobin,M.B., Fleming,M.D., Skatrud,P.L. and Miller,J.R.
  TITLE     Molecular characterization of the acyl-coenzyme A:isopenicillin N
            acyltransferase gene (penDE) from Penicillium chrysogenum and
            Aspergillus nidulans and activity of recombinant enzyme in
            Escherichia coli
  JOURNAL   J Bacteriol 172 (10), 5908-5914 (1990)
   PUBMED   2120195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF040521.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..371
                     /product="C45 family autoproteolytic
                     acyltransferase/hydolase"
                     /calculated_mol_wt=42169
     Region          12..328
                     /region_name="C45_proenzyme"
                     /note="C45 family autoproteolytic
                     acyltransferase/hydolase; NF040521"
                     /db_xref="CDD:468523"
ORIGIN      
        1 metlevrnie lsgtnyeigy rlgelvanmp eilegqinks nvvskkeeke mielfdkycp
       61 glneelqgfa daiqvncnqi lyytmtylkp gcsqvalape ltenghvlfa rnfdfshnme
      121 dfvlcktkvn gkyahigttv mqfgrgegmn ecglgvsqss cgipvgnsdg lrkpaivglq
      181 fwavirylle nckdvdeale ylkdmpiayn inllladksg nialvetldg kkevniinsl
      241 eskreyflhs tnhthidklh klepqsmkns ihryklikey inkskkigek elmnllssky
      301 pnglscnyyn dffgtlkniv mdlnigkfni lwgglenkwe syylkndiks itqrininie
      361 kapsdffdfi e
//
LOCUS       WP_284939026             203 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Clostridioides difficile].
ACCESSION   WP_284939026
VERSION     WP_284939026.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..203
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23443
     Region          23..197
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mindiknkfk nykpyingyk nmkrasvlip iveinnthyi lfevrsknlk hqpseisfpg
       61 gkiesgetpy eaviretcee lgtfsdniev issldllitp vkfiihpylg yikninnlni
      121 nkdevdhtfl vpikyllvnp pntysntvkv fpdenlpygs ipnqkdykfe sgsypilfyk
      181 ykdyviwgmt akilenflnf lse
//
LOCUS       WP_284939067             666 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Clostridioides
            difficile].
ACCESSION   WP_284939067
VERSION     WP_284939067.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..666
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=75860
     Region          203..624
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
     Region          594..>660
                     /region_name="COG1693"
                     /note="Repressor of nif and glnA expression
                     [Transcription]"
                     /db_xref="CDD:441299"
ORIGIN      
        1 mkqsiaivtd kitklssfle enirlvlgny idinhyylev lkendkiqgd fvlvmnddrl
       61 nsmrkhlvqd skiivirrtl keneiyglfs ipngtevlvv ndtkettlet islfykigvk
      121 nlkftpyieg kiyknidiai tpgvkgkvps yinkvidlgn ryidistfie iinglridvk
      181 eirknlmays eslisldngv kdnyrqlflk ieeqdvilnl skdgiiftsa dgiintfnke
      241 alkilginen pqgkniedii sedlnilled keiidevvft nkkyinvnkk sifsmgnkag
      301 iyynlqeity ikkleqnltn klreqgqiar ytfkdiktkn knmvkcvela kkisksdlsv
      361 liigesgtgk ellsqsihna snrsnqpfia vncaavpdsl lesqlfgyek gsftgalreg
      421 kkglfelann gtifldeigd mppllqtkll rvlqekqvmp igshnvinid vrvisatnkn
      481 llkmiregkf redlyyrlnv lpidvpslrn rkediitlmn fflknnirls pevitileky
      541 nwpgnirelq nvasyvslmc dsmvfrddlp pyirvecann yedgfgytrk efeeilrily
      601 erresssgig rgfiiekliq egieiseskv rkvlsylsec gyissksgrg gsqitsegik
      661 lynnin
//
LOCUS       WP_284939144             285 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein, partial [Clostridioides difficile].
ACCESSION   WP_284939144
VERSION     WP_284939144.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>285
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          2..170
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mklqkmgmrt iktgisvtlc milgdylven mfyslvacii svqdtvkgsl ktginrvegt
       61 ilggiigfif aiikagdpfl cglgvmcsiy lcnlfkiksv vvacvtflai hlgvgnsdpv
      121 yyslhrvldt svgvlfgvlv nyyvarpnyl nsvidefkki eelsmllied kilrkenlnv
      181 ekfeeevekl eeiysklide ldyslsetni ekienalric reihfhmqsi ellenklylk
      241 ehtykylkkt ynvdkldwni deekspvfny hlmkimieie llrkl
//
LOCUS       WP_284939377             382 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Campylobacter
            vicugnae].
ACCESSION   WP_284939377
VERSION     WP_284939377.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..382
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42351
     Region          1..376
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mnvviveddi nmrksleial gdyeefsvks yksatealkk lssdtdvivt dinmpgmdgl
       61 efikeldgky dviimtgnat lnraiesvrl gvkdfltkpf didtlataik rtsvitqktk
      121 tkkpdtttei kssnflaasa nldktlniak kaaqtdvsvm imgesgvgke lfsryihens
      181 krknsalmai nmaaipenll eselygyekg aftdatatkk glfelanggt lfldeigemp
      241 lnlqpkllra iqereivrvg askpikidvr ivsatnanle qkvangefre dlfyrlntvp
      301 lkipplrerk deivdianat lkrvcveyel gqkefsqeai dellsydypg nirelisive
      361 raailsegss iskedlfiya kk
//
LOCUS       WP_284939419             239 aa            linear   BCT 25-DEC-2024
DEFINITION  TRM11 family SAM-dependent methyltransferase [Campylobacter
            vicugnae].
ACCESSION   WP_284939419
VERSION     WP_284939419.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Kozbial,P.Z. and Mushegian,A.R.
  TITLE     Natural history of S-adenosylmethionine-binding proteins
  JOURNAL   BMC Struct Biol 5, 19 (2005)
   PUBMED   16225687
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437146
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..239
                     /product="TRM11 family SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27509
     Region          28..211
                     /region_name="Trm11"
                     /note="tRNA G10 N-methylase Trm11 [Translation, ribosomal
                     structure and biogenesis]; COG1041"
                     /db_xref="CDD:440663"
ORIGIN      
        1 mteekfelet ntiwsfpnrg kwathdakyr gnfspyiakn iilrysnend lvldqfvggg
       61 ttliecklnn rnaigidinp navkitknkl nfncdndvsv diklgnacfl dlenesidli
      121 cthppyadii kyseridgdl shlkykdflv evekvanecy rvlkkdkfca ivmgdtrkng
      181 mvqplgfevm qrfinagfkq keiiikeqhn ckatgfwktn sqkynfllla heyififkk
//
LOCUS       WP_284939426             145 aa            linear   BCT 25-DEC-2024
DEFINITION  Dps family protein [Campylobacter vicugnae].
ACCESSION   WP_284939426
VERSION     WP_284939426.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Choi,S.H., Baumler,D.J. and Kaspar,C.W.
  TITLE     Contribution of dps to acid stress tolerance and oxidative stress
            tolerance in Escherichia coli O157:H7
  JOURNAL   Appl Environ Microbiol 66 (9), 3911-3916 (2000)
   PUBMED   10966408
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 145)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 145)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   6  (residues 1 to 145)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..145
                     /product="Dps family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16212
     Region          7..144
                     /region_name="DPS"
                     /note="DPS protein, ferritin-like diiron-binding domain;
                     cd01043"
                     /db_xref="CDD:153102"
     Site            order(19..20,24,26..27,38,49,53,56..57)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:153102"
     Site            order(26,38,42,53,57)
                     /site_type="other"
                     /note="DPS ferroxidase diiron center [ion binding]"
                     /db_xref="CDD:153102"
     Site            order(120,127..128)
                     /site_type="active"
                     /note="ion pore [active]"
                     /db_xref="CDD:153102"
ORIGIN      
        1 mknvvtqlnq lqadahslfv afhdyhwnvk glqffsihey tekeynelae lfdemaerai
       61 qlggkaitkt dellkvakap vvskdsytpv eviealkdaf vyllaefkkl egiaesagdn
      121 ttvaiaqeny aslekkiwmi katla
//
LOCUS       WP_284939449             170 aa            linear   BCT 25-DEC-2024
DEFINITION  HIT family protein [Campylobacter vicugnae].
ACCESSION   WP_284939449
VERSION     WP_284939449.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..170
                     /product="HIT family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19499
     Region          21..142
                     /region_name="FHIT"
                     /note="FHIT (fragile histidine family): FHIT proteins,
                     related to the HIT family carry a motif HxHxH/Qxx (x, is a
                     hydrophobic amino acid), On the basis of sequence,
                     substrate specificity, structure, evolution and mechanism,
                     HIT proteins are classified into...; cd01275"
                     /db_xref="CDD:238606"
     Site            order(48,50..51,58,60,106,114,116,120,122)
                     /site_type="active"
                     /note="nucleotide binding site/active site [active]"
                     /db_xref="CDD:238606"
     Site            order(118,120,122..124)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238606"
     Site            120
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238606"
ORIGIN      
        1 mkdefapwra eyfsrtksce cifcdiaqnp qndtenfvlf rakncfgvmn rypytlgefm
       61 vipykhidni enlnldiwle istivqkgva vlkkslnasg vnigmnlgaa agagiaehih
      121 yhlvprwerd tnfittiayt rvhgvpfmqq ynslksefqr leredpifsk
//
LOCUS       WP_284939476             249 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Campylobacter
            vicugnae].
ACCESSION   WP_284939476
VERSION     WP_284939476.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..249
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28888
     Region          45..221
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mvliirillv gflfswfgii clignfiflp lvilklnkfk lfenlardlv ylawkffifs
       61 tkilgyleyd fkdfdrlgkp sqiiianhps lldvvfilsk vrrincvvks qlakniflsl
      121 aikasnyiin nedeelinks ievlkngdsl lifpegtrtk deikfhkapf ylaingakil
      181 tsifinmhpr slqkgvkwyk tpkskikyki tigddlkidd flnntqntir vrmlhknine
      241 iykkeikld
//
LOCUS       WP_284939518             335 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Campylobacter vicugnae].
ACCESSION   WP_284939518
VERSION     WP_284939518.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..335
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=38078
     Region          22..>205
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(80..81,83,107,113..114,117..118,120..121,144,
                     147..148,151..152,155)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          105..138
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          143..167
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdfffieyrd pifglivlfs vlllvaifsy fwgvfslkdq knsidkfvnk fqsqsnldqk
       61 yqdmllnldi dsnslgvlag ifarsgdfnk aisiylialk katkksekef iflnlgkvyl
      121 kagfiqrste vflesikisp kniealshlg lgfeklrmyd qslevldals eqeievaeqi
      181 aytkalklkn snvnfdqkia kfkklssefk lidrmilely ivnnkdinei kskpnlnhci
      241 dilytndgvl dgdeymelys akgkndipin dfnlkllkta nanglnatls fsyicsecks
      301 syplffyrcn hcarlgscai ipnvikesde dsiaf
//
LOCUS       WP_284939592             312 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein [Campylobacter vicugnae].
ACCESSION   WP_284939592
VERSION     WP_284939592.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..312
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34525
     Region          1..307
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mskvkisiit gflgsgkttf lseilsdids snlaiivnef gqnslddtil nasyakektt
       61 vigsgcmccn krddliiklk dilnsyelng krldrviiet tglanpapil wtvlsdpfls
      121 nhfeiaglft cvdainglnh lnhqeainqi sasdsviitk sdlnsdykel cktlksiyag
      181 vkiydkryik fsdlfndvkk dysnieqnsh tqglssisln fnkpvewsaf tiwlslllhr
      241 ygaqilrtkg iistkqnhli sinsvchivh pprhidnpng gnpgsclvii aqnldlnlvk
      301 eslksflkve le
//
LOCUS       WP_284939621             791 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Campylobacter vicugnae].
ACCESSION   WP_284939621
VERSION     WP_284939621.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..791
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=91831
     Region          173..433
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          332..583
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          615..>775
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
ORIGIN      
        1 mryiifflfl csclhaftfs insgkhsgnp yyiihlqddk emicdernne knkiysckif
       61 tkldqnlknq dlpfarisfh rlsdgfvvii qpksisrifn annrlfdshn skadktnrsk
      121 hftininkhl neldtsyidg idfpikypnl ihpsvgaldl nkepitynen gdmgiylsik
      181 rsyerqnyke vifesqkain mhpdsiflge fllyqirsmd klikeesqyq aiqkmnknii
      241 esaktwmrfn gsdrnypevl yismiahlss dlrddaeyil dmlmtehgnd qwtkraimgy
      301 adylvahgkl tdgmrfyedv lyssndidia seaslklvri ylsqqrfsea aqyidrvvta
      361 npkyilahks ysieiadelr annlfdtaak iyksvfmdsh lhdsyyemsl rrlgttivrg
      421 kdpvsaydyl qrykkefpdn efsseiehsl dylffdmpgk ssdekhthyn nllekypgqe
      481 lakkalieev klsfeekkya nilklnrlia dlnqsnisdm mqasalnlan rynqnldcld
      541 aialvdeydl eskiadqlkl fncydrtkry asaynlveqn lnepnlnnrv vwlnnltkin
      601 yklsrftsai dssfkavdla skvpysdpse aiiyrfysll kldrfdeats alktiednkg
      661 idimlieayd tammyandkg dklakdyakk vldlqdklni dtfspeanfv yidnlvanse
      721 fkeakneile lllkslkpqn raralqkmaq ieisqnryka avsyinecln isensqwkel
      781 ckeqkrlvdg i
//
LOCUS       WP_284939728             144 aa            linear   BCT 25-DEC-2024
DEFINITION  molybdopterin synthase catalytic subunit [Campylobacter vicugnae].
ACCESSION   WP_284939728
VERSION     WP_284939728.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10091526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..144
                     /product="molybdopterin synthase catalytic subunit"
                     /EC_number="2.8.1.12"
                     /GO_component="GO:1990140 - molybdopterin synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=16143
     Region          8..126
                     /region_name="MoaE"
                     /note="MoaE family. Members of this family are involved in
                     biosynthesis of the molybdenum cofactor (Moco), an
                     essential cofactor for a diverse group of redox enzymes.
                     Moco biosynthesis is an evolutionarily conserved pathway
                     present in eubacteria, archaea and...; cd00756"
                     /db_xref="CDD:238385"
     Site            order(14,18,27,29..33,35,37,86,95,97,105,109)
                     /site_type="other"
                     /note="MoaE homodimer interface [polypeptide binding]"
                     /db_xref="CDD:238385"
     Site            order(48,50,53,56,60,76,112..113,115,117..119)
                     /site_type="other"
                     /note="MoaD interaction [polypeptide binding]"
                     /db_xref="CDD:238385"
     Site            order(112,119)
                     /site_type="active"
                     /note="active site residues [active]"
                     /db_xref="CDD:238385"
ORIGIN      
        1 meiydgnlda neitsrwysd nklknygaim sfvgvvrden gisglsfdly epilkawfdk
       61 wqevaksqna iilmahskgd vavhessfia gvcspqrkva lklinefved fkanapiwky
      121 dligqkrvya lersqklqna gila
//
LOCUS       WP_284939835             377 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Campylobacter vicugnae].
ACCESSION   WP_284939835
VERSION     WP_284939835.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 377)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..377
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=43721
     Region          97..371
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mhskkyilpi fllytlssmf fligfatmyy keakskiveh hkihlerfsk eleyllrlnn
       61 nidsimklks iyqinlynik thryiyksfd mpkfkgefyl andalymken ihsrmrkiel
      121 ivelknqdia ddidnlfwrv wfvagvvfvf igiiafvlvr laylpllaqi ralnnfitdt
      181 theintplsv ilmssemfdk nppkyldnik iaaktlsgiy ndlalnlknn pnniskfdvq
      241 kliesriklf elsanakgie feissisfel nsdmqklgki idnlisnaik yssknskiii
      301 nldknsfeii nfgtaisken ldkiydkfsr fdtqnggfgi glslvkrycd elgfsivcqs
      361 rdnqtkftit lrdfnik
//
LOCUS       WP_284939900             548 aa            linear   BCT 25-DEC-2024
DEFINITION  polysaccharide biosynthesis/export family protein [Campylobacter
            vicugnae].
ACCESSION   WP_284939900
VERSION     WP_284939900.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12809731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..548
                     /product="polysaccharide biosynthesis/export family
                     protein"
                     /GO_function="GO:0015159 - polysaccharide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0015774 - polysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59530
     Region          75..237
                     /region_name="Wza"
                     /note="Periplasmic protein Wza involved in polysaccharide
                     export, contains SLBB domain of the beta-grasp fold [Cell
                     wall/membrane/envelope biogenesis]; COG1596"
                     /db_xref="CDD:441204"
     Region          <449..516
                     /region_name="Wza"
                     /note="Periplasmic protein Wza involved in polysaccharide
                     export, contains SLBB domain of the beta-grasp fold [Cell
                     wall/membrane/envelope biogenesis]; COG1596"
                     /db_xref="CDD:441204"
ORIGIN      
        1 mkkvlsilti fataaiaimp vssinsvnst tansqaalip qdanltisat eptqmvfgen
       61 lfngnftmvs qhiynpdyil aigdvvnvkl wgayefeqql tidsqgnifl pkvgvikllg
      121 vknsnlvavi sksvkrvfke nvhvyadmgi yqnvsifvtg nvnkpglyqg lssdsliqfi
      181 dkagginpqy gsfrnitvvr nnkpyknidl ydfmvdgkie mfalkngdvi ligsvgayms
      241 asgevlrsyr feakdssmsl kelarlagik pvvtqaivks ynnnqiqits ypltkfdsvk
      301 lragdavefm tdhaatevri nidgehsgar aivvpkgttl geimekigfn aqsnvdaiql
      361 frksvakmqk nlidshlrel esialttssa ttqeaqiraa eaksilefie rarqvepkgq
      421 vvisnkddin qivlqeddti yiptkdnivi vqgevsmpga fthvadsdie dyiemagdls
      481 aradssrvil vaangkagkf rassgedvyp gdsilvlpkv egktlqatsi ltqilyqlai
      541 aakvvidl
//
LOCUS       WP_284940004             401 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Campylobacter vicugnae].
ACCESSION   WP_284940004
VERSION     WP_284940004.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..401
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=46122
     Region          14..399
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mtfttdsqlk sliiannkke qyakdgsikn lyvmlretsk tfifrykidg skiksitigq
       61 ypsislaear qkanefktll argidprdyt neheltfkdv aqkwlkekak qklsslkkae
      121 grlnnhilpk ignikikdlk rdklincile velkstrgdg yetktrifmi lkdilkyiti
      181 qgiiqdytsp laefnfsdic kdkhivsnhr fikdptrlke fltaidnykg niytkfalql
      241 gaytalrsgt irtlkweyid ftqdiinipa eqmkmkkpfi lpissqvkai lkelkayqlg
      301 eylfsinski msentlnkai kslgfgdeav fhgfrglfst ichdntqdhg ltsevielcl
      361 ahtdnnkvrs aynhserlqe kaklmewygn yidnlkkakn d
//
LOCUS       WP_284940007             179 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Campylobacter vicugnae].
ACCESSION   WP_284940007
VERSION     WP_284940007.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..179
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20042
     Region          40..179
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mkfkiflaav lltvftgcdr ssndqstsps tmqadyskpf klplndgtel kmqkrddgyn
       61 idikdkaifl nffatwcppc kveipylvsl qdkfkdklqi igvsideisl eqanefkell
      121 ninypiaytk aneylisslg gvvgipfsil yypngkfaas ysglvpieml endikkvik
//
LOCUS       WP_284940161             932 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Bifidobacterium catenulatum].
ACCESSION   WP_284940161
VERSION     WP_284940161.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium catenulatum
  ORGANISM  Bifidobacterium catenulatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..932
                     /organism="Bifidobacterium catenulatum"
                     /db_xref="taxon:1686"
     Protein         1..932
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=100043
     Region          45..186
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          409..907
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 martassntk ssgkrsagka rsgetkvmdt vepspvmgvl tkyrrdiacf vlvilavlfc
       61 asewfrvqga fgqvlhamas glfglmsvil pvflmlvvfs lmhktqrksd narmatgwsm
      121 ilwsicsild aalasdiqgf dmallqkagg llgyvlgcpl awglskafai vifvvvilfs
      181 llmithtrvd eipdkvcslm srfgfstnka dddeteqfpn evrigdatls faegvpahdg
      241 tdnaaaeekk pmllsrlrql issktkkqga qdgleyydgd eafrnaaerh getaetmlde
      301 pyqsvsqprs issgehsaqd sggtvvmpqm pvarslssdp igtasgtmpq ipetvpamvg
      361 avpsseiksv gvasddpwav idengtsngt qvmvdaatne vvndpnggls eegvsdesdg
      421 ipegpyhlpd lgmlkqgaph avhtpendrv iraltvtfqq fnvdakvigf lrgpsvtmye
      481 velgpgvkve kvtnlqknia yavassdvri lsviegksai gieipnadre tvvlgdvlrs
      541 dkarndpnpm ltgvgkdveg hfvtadltkm phllvagatg sgkssfinsm ltsvimratp
      601 dqvrmimvdp krvelsayag iphlltpiit dpkkaaqale wvvkemdary gdleffgfrh
      661 ikdfnaavra gkvhapagsk rkvapypyil vvvdemadlm mvakndvess iqritqlara
      721 agvhlvlatq rpsvdvvtgl ikanipsrla fatssatdsr vildstgaet ligqgdalfl
      781 pmgqakplrv qgawvdesei rravefvrtq rkphyredie emakeadkka iepdediggd
      841 mdvllqaael vvtsqfgsts mlqrklrvgf akagrlmdll esrgvvgpse gskarevlvq
      901 pqdlpqvlaf ikgetsslns gasstadsev am
//
LOCUS       WP_284940292             604 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Bifidobacterium catenulatum].
ACCESSION   WP_284940292
VERSION     WP_284940292.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium catenulatum
  ORGANISM  Bifidobacterium catenulatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Bifidobacterium catenulatum"
                     /db_xref="taxon:1686"
     Protein         1..604
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65750
     Region          10..595
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mykeytrple qqidtdknif svleervnrt pndslveykn ehgewasfsa tefrdkviai
       61 akgliaqgim pgdsvsiish tcwqwtaldv aimsigaltv pvyetnspaq vemifndanv
      121 kmafaeddaq rdkiesirse cpnlgdvyvi gldaidtmve yghavsdaef qerehavkgs
      181 dlativytsg stgtpkgiel thsnfvfity sginsmpdia mkpnrrlllf lplahvfary
      241 mqffcfagnv slglsgnlkt iladfkafkp tfilavprif ekiynaasqk agdglkgrif
      301 agatqtardw shaqqsgegi pvvlnlkral ynklvyssim dvfgghveya vsggapldss
      361 iahffngigl pllegygmte tcapssvnpt sgykigtigl plqgvtmgvd eegelciksp
      421 avcagyhnnp dvtkqqivng wlhtgdlgsi ddegfvsivg rkkdliitag gknvspceme
      481 asimtspvvs qcvmigdrkp fiaaiisldl getnawlask gaecvtslee asrnpivrae
      541 veravnkane lasraesirk feivpdefte englvtpsmk arrqavvdhy rtlidtviyv
      601 pknk
//
LOCUS       WP_284940295             211 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Bifidobacterium catenulatum].
ACCESSION   WP_284940295
VERSION     WP_284940295.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium catenulatum
  ORGANISM  Bifidobacterium catenulatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Bifidobacterium catenulatum"
                     /db_xref="taxon:1686"
     Protein         1..211
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24142
     Region          8..205
                     /region_name="HAD_sEH-N_like"
                     /note="N-terminal lipase phosphatase domain of human
                     soluble epoxide hydrolase, Escherichia coli YihX/HAD4
                     alpha-D-glucose 1-phosphate phosphatase, and related
                     domains, may be inactive; cd02603"
                     /db_xref="CDD:319790"
     Site            order(14..18,117..118,151,175..176,179..180)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            146
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mtspsanvtd vvfdfcgvli dwqtracleg rypqvvvdri cadddpcgfy dyedrmdhge
       61 dfediypdvv reqgeeiaei frdyierygd alprmipdme qllrdlkaag ygvwgltnws
      121 hetfhfafer fpqleellqg tvvsgvekmh kpnadiyela lsrfnlrpes svffddtakn
      181 vtgaqavgmy afrftnadqa rrdlkslgmd f
//
LOCUS       WP_284940455             483 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Bifidobacterium
            catenulatum].
ACCESSION   WP_284940455
VERSION     WP_284940455.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium catenulatum
  ORGANISM  Bifidobacterium catenulatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Bifidobacterium catenulatum"
                     /db_xref="taxon:1686"
     Protein         1..483
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50899
     Region          9..476
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 msnekgtlsi eeqgidtise eerkgtpasl fwpwfaanvs mfamsygawa lgfgisfwqa
       61 tamtiigvvv sfllvgiisi agkrgnaptm vltratfgve gakvpaalsw iatlgweisl
      121 tttavlalss tieklgwgsg aapkiistiv vvglvvvagi fgydlimrcq qvitivtgvi
      181 tvgffilgwg hidfsainsv ptgslpamlg ccffvmtgfg lgwvniaady srylprkssn
      241 ggivfwttfg asianvflif yglllavsna dmaenvgndp igamasilpt wylipytiva
      301 vlglmsgsim dnysnglall sfgvklprtv aaaltaaltv lgvvyvtffs dtfigpfqgf
      361 lttlgvpmav wagmfvadvi irkkdystad lydpkgcyga wngksfailv vgtvlgwglv
      421 vntaaswlnw qgyllfligg kegswaaanl gvivaliigl agslmfqrgd iaeqeadlpa
      481 sea
//
LOCUS       WP_284940575             475 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Bifidobacterium
            catenulatum].
ACCESSION   WP_284940575
VERSION     WP_284940575.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium catenulatum
  ORGANISM  Bifidobacterium catenulatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 475)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Bifidobacterium catenulatum"
                     /db_xref="taxon:1686"
     Protein         1..475
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51997
     Region          37..350
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(138,140,264,266,300..302,343)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 megiglklvk riiaiccaai mavsaaacga nvdsrteitv wswepsmkqv iagfekenpd
       61 ihviwkntsg ydnlnnaiqd gygipdvvql eyyalrqyav ssqlmaitgr tkdygdfytp
      121 gtwasvqlng rvyglpmdsg pmaffynksv fdqvgvdask irtwddyyea akklkeigvy
      181 iaadsgdasf ydtmiwlagg rpfstsndgk nvtinltgde gtrtftefwq kmineglvdt
      241 sltawsdgwk eavgegkias mfsgawlpsl lmsnlpgtag lwrvaqmptp dgsattseng
      301 gsalavlqrs rkpeasyrfi eyachkaegi karvdggafp adnntlsdpe flhkttvtde
      361 rgieipyfgg qeynrvlsea aenvstgyqy lpfevyarsd frstvgkayk wssllckeqd
      421 rlniiaaggk vsdksaigda lketdsadrl tlksgialwq kdlkeygtnq gftiq
//
LOCUS       WP_284940635             327 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Bifidobacterium catenulatum].
ACCESSION   WP_284940635
VERSION     WP_284940635.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium catenulatum
  ORGANISM  Bifidobacterium catenulatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Bifidobacterium catenulatum"
                     /db_xref="taxon:1686"
     Protein         1..327
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=36148
     Region          116..276
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 maqnskdaqk rasraerraa eaaamkarae qmekerkqqt iigaivvavl vilvaigaft
       61 vyhnmhknte tqastqtvee aydrlqkvkn tpklvddkgg lllskngygk svdgaptvai
      121 ymdflcpgcg nlhrqldadl qkmvdagqin ldlhfmafmd kwstdeyssr aanaaiylae
      181 hdsnpthlit fmekmyaedf qpeessnyks vsddqikeqm iasgvsedva dkafdrdyqd
      241 wldaidtytp krselwntsg tykdsmttpt vtingkfwnm nqlstaqeti eeglleaigi
      301 ksddigkegv mpsigsdkdp isnttge
//
LOCUS       WP_284941067             262 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF1700 domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284941067
VERSION     WP_284941067.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>262
                     /product="DUF1700 domain-containing protein"
     Region          4..>76
                     /region_name="COG4709"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:443744"
ORIGIN      
        1 mnlnktefle ilkdylkkdf sesevndilr dyeeyfvdgl iegksdmeii aslgspksia
       61 kelilqtkek nieeekiint dvlndkfskf ksdmkkgysi lkdeakekys kskenidgki
      121 mntdilngkf srfksnvkkd ysilkdeake kynkskenin dkltpsieeg vgglsrqvik
      181 gllvvlslfl ivpafafvca ivsatialvc sliafvilip fvikfiamvp dvmmfcifat
      241 iafvgleila wqillftikl gk
//
LOCUS       WP_284941090             471 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284941090
VERSION     WP_284941090.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..471
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <18..463
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 ylmtliiiis iigilaciil ilqyskkmvr leklnvdlkn iaykdeltgv ntiekfklda
       61 nqnicihkdk kfavfyidfe nfkyindifg ydygdmilkr yanlmmndig kyeifareia
      121 drfvalrcyv dkedlvvrqr dvdnelinit neiknkhsit vvsgiccied vneklsidgl
      181 inranfaqkt vknkpgtnya fyndsirkkm ieentiksri heaiekrefi vylqpkvnlh
      241 sqkincaeal vrwltpdkgi ispaifipvl eknffialvd kyvfeevckw irkrldenkp
      301 fvqisvnvsr iqfyntkfve tysniqnkyr ipkntieief tesvafenqk hlleiihdlh
      361 engftcsldd fgkgysslsv lkdlpfdvlk ldsmffkasl dkdkekivik nivhmlkeln
      421 ittvaegiec keqveflrdi gcdlvqgfvf ykpmpilefe kildkefvyn s
//
LOCUS       WP_284941235             307 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Bifidobacterium
            catenulatum].
ACCESSION   WP_284941235
VERSION     WP_284941235.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium catenulatum
  ORGANISM  Bifidobacterium catenulatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Bifidobacterium catenulatum"
                     /db_xref="taxon:1686"
     Protein         1..307
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33853
     Region          12..302
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mgainmfndf vklieseslp veavaiadgd aiiaerhfvp dqdrniysht ksyvstaigi
       61 aiedgllsld srlvdsfpey vpsdaqlelg qitlrhlltm ssgfnhaylm npdrrsgvga
      121 pdylrymfsr rvevepgstf cyssadsdla grmleqaagm rlgeylygmi fskldqgwpv
      181 wecdpqghpi agggiymsla nmlklgqvyl ndgtwhgtri vseswvkqas gkqidtpysn
      241 iwtcgygyqf wmspyegayr adgaygqitt vlpnqglvva iqcpesgdfd nivrpalheh
      301 lllplta
//
LOCUS       WP_284941287             448 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Bifidobacterium catenulatum].
ACCESSION   WP_284941287
VERSION     WP_284941287.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium catenulatum
  ORGANISM  Bifidobacterium catenulatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Bifidobacterium catenulatum"
                     /db_xref="taxon:1686"
     Protein         1..448
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48612
     Region          63..425
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtlehvamai vvvavavvaf llgrargvql gedeidpndp slfgaqknms lfgprvpvqp
       61 terqliavmp ealivvdsla svkyvspgaq rfgivedham tlaeirdilr lvstdsvvre
      121 relsipldra araaakntng kgieagkfrp sdtlylhvrv gqisddlfai fisdmseqrr
      181 feimrrdfvt nvshelktpa gaisllaeti gdaaddpdmv kyfagrvske serltelvhr
      241 lidlqkaqsa aavlnaerls vlalvreaiv enqvnaeskh ismvlslngk qklvyvegae
      301 naidqddvfi nadhetikta vknlvenain yspeyttvav dvgssdgkvs irvvdqgigi
      361 pessldrife rfyrvdpars retggtglgl aitkhcvqdc ggtiavwsce gegstftitl
      421 pqaeseqdee saksktteis esaqlpie
//
LOCUS       WP_284941488             290 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Bifidobacterium catenulatum].
ACCESSION   WP_284941488
VERSION     WP_284941488.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium catenulatum
  ORGANISM  Bifidobacterium catenulatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Bifidobacterium catenulatum"
                     /db_xref="taxon:1686"
     Protein         1..290
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31207
     Region          8..278
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mpiksevian pkservrrvs eladrkgrkr sgrfmvegpq svrelltyhp glvedlyvev
       61 esaqpdasfa tpvvaqmagk amqsgvyvhk vthavmhrms adaqgvlava dmqafldssa
      121 vlddfdghtm vaafwqvrdp gnagtvirsa daagcsavvl vddcvdmfnp kvvrstagsl
      181 fhlpiltmgt ddffawcdth elavyaadvy gtdsrqpesl tdviampetl agakavlfgn
      241 eargltkevl ertdrivsip lygkaeslnl gtsssvmlls lamsshverm
//
LOCUS       WP_284941517             604 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Bifidobacterium catenulatum].
ACCESSION   WP_284941517
VERSION     WP_284941517.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium catenulatum
  ORGANISM  Bifidobacterium catenulatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Bifidobacterium catenulatum"
                     /db_xref="taxon:1686"
     Protein         1..604
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65754
     Region          10..595
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mykeytrple qqidtdknif svleervnrt pndslveykn ehgewasfsa tefrdkviai
       61 akgliaqgim pgdsvsiish tcwqwtaldv aimsigaltv pvyetnspaq vemifndanv
      121 kmafaeddaq rdkiesirse csnlgdiyvi gldaidtmve yghavsdaef qerehavkgs
      181 dlativytsg stgtpkgiel thsnfvfity sginsmpdia mkpnrrlllf lplahvfary
      241 mqffcfagnv slglsgnlkt iladfkafkp tfilavprif ekiynaasqk agdglkgrif
      301 agatqtardw shaqqsgegi pvvlnlkral ynklvyssim dvfgghveya vsggapldss
      361 iahffngigl pllegygmte tcapssvnpt sgykigtigl plqgvtmgvd eegelciksp
      421 avcagyhnnp dvtkqqivng wlhtgdlgsi ddegfvsivg rkkdliitag gknvspceme
      481 asimtspvvs qcvmigdrkp fiaaiisldl getnawlask gaecvtslee asrnpivrae
      541 veravnkane lasraesirk feivpdefte englvtpsmk arrqavvdhy rtlidtviyv
      601 pknk
//
LOCUS       WP_284941676             669 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Bifidobacterium
            catenulatum].
ACCESSION   WP_284941676
VERSION     WP_284941676.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium catenulatum
  ORGANISM  Bifidobacterium catenulatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Bifidobacterium catenulatum"
                     /db_xref="taxon:1686"
     Protein         1..669
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=73105
     Region          19..662
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtemntennl eamqrahgpl levknlqvdf ttdegkavha vrnssfsvyp gqwvaivges
       61 gsgkstsama vlgllpgtgh vvggsikldg qeisgfkqkd fdklrgskmg lvpqdpmsnl
      121 npvwrigtqv kealvannmd idhekrsefa kaladdevel kgnddetflg skelpdltaa
      181 akealakigk sgdeldkima rfaeewvpgs etrwrvadgl ikagvkddda wyiakkyvvg
      241 stmddriagl lseaglpdaa trarqfphef sggmrqrali aiglacrpel liadeptsal
      301 dvtvqkkild hlhmltdslg tavlfithdl glaaeraqhi vvmykgqvve sgpslevlqh
      361 pqhpytkrlv aaapslasqr iisvkehggd atavmehavn edslkkgeai itvdhltkef
      421 klprkkemfk avddvsfsik kgttlaivge sgsgkstvan mvlkllepta gtvtydgrdi
      481 sgfkgkelld frrhvqpvfq npygsldpmy siyrsieepl rihgigdkks rakrvrelid
      541 mvelpesvmn rypnelsggq rqriaiaram aldpdvivcd eavsaldvlv qdqvlrllnd
      601 lqaekglsyl fithdlavvr qiadevvvmq hgklvehatt devfdhpkkq ytrdlldaip
      661 ggklqlgld
//
LOCUS       WP_284941681             265 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Bifidobacterium catenulatum].
ACCESSION   WP_284941681
VERSION     WP_284941681.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium catenulatum
  ORGANISM  Bifidobacterium catenulatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 265)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Bifidobacterium catenulatum"
                     /db_xref="taxon:1686"
     Protein         1..265
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29464
     Region          61..230
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mimgnvserr kqppqvgvsv vilalgpash gtqehartsa gstlwiplvr rvrqpflgqw
       61 alpggglrag hsleqsayva lesttslhpr yleqlytfgd parshgglpm vsivywalvd
      121 dlngqlgqsi ddnvkwfpvd dlpevafdhg divdyalsrl rgkieypqiv trlvgerftl
      181 sqlhdvyeav agqsidlanf rrkmlasgql edtgdklrvg rnrpatvyry tmdvlrqstw
      241 sdardrhdfd vretqddvls altti
//
LOCUS       WP_284941688             759 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Bifidobacterium catenulatum].
ACCESSION   WP_284941688
VERSION     WP_284941688.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium catenulatum
  ORGANISM  Bifidobacterium catenulatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 759)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 759)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Bifidobacterium catenulatum"
                     /db_xref="taxon:1686"
     Protein         1..759
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=84492
     Region          1..758
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mssysaqlre eqqavsrayg rlddlraqar arldtvraag shgsptqrte rdsfatmyed
       61 rltqlraved rlvfgrlddv hgthryigri glsdehhepi ltdwradaar pfyeatpshh
      121 gdivmrrhit lsfrevvgve devldvhsdq vgqassdgtl tgegallasl nakrtgkmtd
      181 ivatiqaeqd riiradlnqa vvvqggpgtg ktavalhraa yllythrrml ersgvlvvgp
      241 sstflhyidq vlpslgetgv vsrtiadlip gvvatahddp faaklkgdrr makaianava
      301 arervpsqlp siringftvp ivrtdieqai tdakrtrqqh nkaretfvhs mliamrnryv
      361 dkldyepeqa eltdvmqqlc mndalrktln lawlpmtgew lvdqlfckpq qlrrfapwle
      421 erdiealtrp kgspftvsdv plldeamell gpdpkaiarq keldakraee eqfaqdtlaq
      481 agigsgivts qmlvdningm daeltaqraa sdrewtyghi vvdeaqelta mdwrmlirrc
      541 psrsftivgd vaqtsalggt rswrrmmdsl fgphnwqlne ltinyrnpke vsqlacdfaa
      601 aeglyistvn avrgvpdsvk rltladesli fdavaqqtvd lvrsyisadg tgrvaiiapd
      661 dmvkplrrrv yeqlretlpa kefdrldaqs swdeqvtvcs tqmvkgleyd avmvvqpgii
      721 eenapsriva aadlyvamtr ptqrllivrt nadekllkl
//
LOCUS       WP_284941748             607 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Bifidobacterium catenulatum].
ACCESSION   WP_284941748
VERSION     WP_284941748.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium catenulatum
  ORGANISM  Bifidobacterium catenulatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Bifidobacterium catenulatum"
                     /db_xref="taxon:1686"
     Protein         1..607
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65668
     Region          10..606
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mlteytapge svevgddesi ysllteriar tgedtviaer ktapgqwmkv ttgefhkdvi
       61 aaakgliafg iakgdavtif sttryewgvl dfalaaigav nvpiydtdsa aqaerilnds
      121 dvklaiadnr erfdrldsvi drcpslkhil mldsnamgal eglgvtvsde elearidsvh
      181 addlativyt sgstgapkga elshrnfisi tragslalhe iiledhprll lflplahcfa
      241 rfiqyasias ddgvvgylpd tktllpdlrs feptyllgvp rvfekvynaa srkagmgwkg
      301 rlflkaaeaa rdwsrmqqag ekptmkqtae hlsyeasvyr tvrgalgpri ryvacggapl
      361 dvslahffng iglpmiqgyg mtetaapfaa nrvtdnvigt vgqpapgssv risddgelqv
      421 kgpnvfrgyh nlpektaeaf tedgwlktgd lasiddegri titgrkkdii itaggknvsp
      481 ipmeqeivkc pivehavvvg dnrpfigalv tldpeglaaw lpsvglsadt pldriatvaa
      541 vhdeiqkyvd kanatvsrae svrkfvvlnt qftqenkclt pslkvvrpav nrvfaqvidq
      601 qlysgkr
//
LOCUS       WP_284941920             355 aa            linear   BCT 25-DEC-2024
DEFINITION  GGDEF domain-containing protein [Campylobacter vicugnae].
ACCESSION   WP_284941920
VERSION     WP_284941920.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter vicugnae
  ORGANISM  Campylobacter vicugnae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 355)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 355)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Campylobacter vicugnae"
                     /db_xref="taxon:1660076"
     Protein         1..355
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39910
     Region          <162..340
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mvtldkdkga kpaikqptss paitptkpvs rpdtssadse nvdlnkfssa vlkqllaeni
       61 qptpdnfdiy frklleskpa nfqkkvlell dfskedkldr qaliekdikt gfaqirsmmq
      121 iisliyknlg imkgiakkrl nemsasanpl evqgnikafg geleklnilm erhinaikas
      181 yeevdkifkn vednsiydsk fevynkkyll kilydefedv krykynvsim lihvkdsvln
      241 sipslkdkng ilrniakill ktsrrsdiva hygdgcfamv mkhtdlesak kasqrvaell
      301 yqttffmged eldmnmeisv gainpdssie eilsalldal prsgkgvklf esvev
//
LOCUS       WP_284941941             431 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Clostridioides difficile].
ACCESSION   WP_284941941
VERSION     WP_284941941.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 431)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..431
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47179
     Region          16..403
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 msvevnkpsi wknfkvliil fvagafiyal pylknyyydt faqafnltnt qmgslgsiyg
       61 llamvsylfg gfladrisar kllsgsliit gisglvltly ppyivvflih alwgittilt
      121 fwpalvkavr mlaseneqgk afgfmesgrg itnaihlslv lilfgyissk vsdksgltai
      181 ivlysainvi vgvlvffklk dnekevsakf dkeaffavik mphtwiitii mfcsysanms
      241 fyyftpyste afgatvvfas aisilaqycr pvasaasgll gdkvgsskii sygfilmiag
      301 llgviftptk ssmiyillig cvatyvsmya iqglhyslle egnyslsisg taigivatlg
      361 ylpevlcpla agkildafpg vtgyryyfiv ltivaiiglv ftfiwmnmtk errkeliemn
      421 nnsnenttkv s
//
LOCUS       WP_284942014             336 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284942014
VERSION     WP_284942014.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..336
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          <8..333
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 lfkdkltkef ieeakkigks dyttllyges gsgkeiiahs ihniskrkdr pfvaincati
       61 aenlleself gyeegaftga rkggkrglfe lahggtlfld einslsfniq tkllrvieer
      121 qimrigsdyi ipldiriiaa tnesltekiv mgtfradlfy rlssleinip plrdrredii
      181 plfnnfvnev lkddglngin sidenfvltk demdklynys wpgnvrelkt iaqkyvvtgk
      241 iklrqdrdfk tkkllpnsev dkfnsettas vevqdesini skindgkisi dikevnkyve
      301 ekiismlfaq glsknevaqv lgisrtslwk kynkni
//
LOCUS       WP_284942082             669 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284942082
VERSION     WP_284942082.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>669
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          205..612
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mdkkklilit hdklnsdhyk eeltnffgde iiietqnild gikenlegdv vlslspltsn
       61 flikhfkedi eiihgtkals klgyekmmkl ppgtksllmt tnktsafema tylykiginh
      121 idfvptypdc deiydldtai tpgqirfipk yiknivdlgw rkisldtyms llvvlklkne
      181 kfieklykls ketlshdfln tsldnisklk tilymtidei gdgliffntf nkvtfvnksl
      241 lnmlgldekl ikspslmeym pnsfldkitk nlnidnmiiy ideidkkfil skkpfylykn
      301 iegclitlkd vnnieileqk irsdsvkrgy vakykfnnii gnssiikdci kkakkmaltd
      361 npilitgetg tgkeaftqsi hnhsnrknkp fvaincaslp selleselfg yedgsftgak
      421 kggkkglfel ahtgtiflde igdmphdlqv kllrvlqeke irkiggtsii pidvrilaat
      481 nkdlekliie nkfrmdlfyr ismftldlpp lrkrledipl llesflkelp yknikldksl
      541 lealnsytwm gnirelrnci eymaymgsny ltindlpqni ssklnnnhms snmsifndln
      601 qydknicisi lkslhmkpmg rtklmkfmey nvteyevrnm leyltrngyl isskgrkgss
      661 itekgikii
//
LOCUS       WP_284942171             397 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Clostridioides
            difficile].
ACCESSION   WP_284942171
VERSION     WP_284942171.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..397
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43369
     Region          1..397
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mkkgalsnik vldltrvlag pyctmmladf gadvikiemp rkgddtrgfg pfvngeslyy
       61 aninrnkkgi tlnlkseegk niflemvkha dvvvenyrpg vmeklglgyd elakvnnqii
      121 ygavsgfgcy gpyserpgyd iiaqamgglm sitgqeggep trvgnamgdv lggmnltigi
      181 ltalnarkii gkgqrvdvsl vdsvvsslet giqryfdsgq pelmgnryas aypydsfkas
      241 dgsfvigcgn dklfeklckk vlfredllid erfktnlnrc ehykalkpei eklsvkhtik
      301 eavdliseag vpaapiynld cvttdehiak aremivdish piignmkvng npvklmttka
      361 kidmpapslg esneeiyngw lgfdsdkikd lkengvi
//
LOCUS       WP_284942228             727 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Enterobacter sp. MEB024].
ACCESSION   WP_284942228
VERSION     WP_284942228.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. MEB024
  ORGANISM  Enterobacter sp. MEB024
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 727)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 727)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Enterobacter sp. MEB024"
                     /db_xref="taxon:3040288"
     Protein         1..727
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=78626
     Region          68..727
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mnntkrhktl lalaigavth salaadekke dtlivqsapa sdfkpggdql vpafldgqva
       61 nggrmgmlgq qnamdvpfni isytsklved qqaktiadvv andagvqyvq gygnsaetfr
      121 irglkfdgdd mtfgglsgvl prqvvdaqmv drieifkgan almngaassg vggminlepk
      181 hadetpqakv gvdytsdsqf gttldagrry gdndqfgarv nlvhregesg vpndrrrttl
      241 lstgldykgd nfrtsldvgy qkktfhgspt svnisavdfv peppkndrnf sqkwaysnie
      301 nefgmwrsey ditdnwtayt glgaqhahee giysapklld ksgkatvsrl dtnrisdsvs
      361 gmagirgnfa tgfvthkvnv gysamtknek igwkmssaad npttniyhnt gvdmpdsssf
      421 nglggkysdp ltsgrtrtqg wllsdtlgvl ddkllftaga rhqkvvirgy nkitgqenka
      481 dgfdgsrwmp tygvvykpwg aislyanhte alqpgqtapn tatnygqstg ivhskqnevg
      541 vkadfgrvgg slalfeikmp sailnsnghy gldaeqrnrg velnvfgepl lgvrlnasat
      601 wlqaeltktn nglnqgndai gvpnfyavlg aeydikpidg ltatarvnhs gtqyadlant
      661 kkldsyttld lgmryrfavn hnqnqmtvra gidnvtneny wssvddsgty itqgeprtfk
      721 vsvgyaf
//
LOCUS       WP_284942230             341 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Enterobacter
            sp. MEB024].
ACCESSION   WP_284942230
VERSION     WP_284942230.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. MEB024
  ORGANISM  Enterobacter sp. MEB024
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Enterobacter sp. MEB024"
                     /db_xref="taxon:3040288"
     Protein         1..341
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37747
     Region          8..323
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mrtikgpgif lsqfisaeap fnsldglagw aagkgykavq ipcnhphifd vekaaesqty
       61 cdditgtlae hglaiselst hlegqliavn pvygdafdhf apagvrgnda arrawatskl
      121 nqaaaasakl gltahatfsg slawpffypw pphnaqrfqd afqtlatrwr pildtfdehg
      181 vdvcyelhpg edlhdgvtfe rflalvdnhp rcnilydpsh mllqqmdylt fidlyharik
      241 afhvkdaefr pngrsgaygg yqpwihragr frspgdgqid ftgifskltq ydyegwavle
      301 wecclkdgdt garegsefir rhiipvsgra fddfaaggsh d
//
LOCUS       WP_284942394             400 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Enterobacter sp.
            MEB024].
ACCESSION   WP_284942394
VERSION     WP_284942394.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. MEB024
  ORGANISM  Enterobacter sp. MEB024
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Enterobacter sp. MEB024"
                     /db_xref="taxon:3040288"
     Protein         1..400
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43951
     Region          27..383
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mqnitqhfrw lllvipslsg cgtlsqmssp agtqellthk sldgdvdsvv rhymaqksvp
       61 gmtvavihny gspqfyswgv tdaanrypig sntlfalgsl skgitaevva clvnegrlsw
      121 ddnlatllpp gtplsadaqk itllelvtht sglprqnmdv pmlgkfisyl ssgdnfygel
      181 dsdnvlryla nwhapqhkmp qysntgyali gyilkhktge diqslasryi fqplqmanss
      241 fipqtlkgyp qralghagdq pkfiprgqlt pdwhfsnnmv aaaslysnae dlaayaryhv
      301 attdnrllds vfaevsntdi qradgvqgia wttdfiglek ityqvgyigg yssfigfdkq
      361 kgnavvvlqn afnwsnyigi allmdmaknd sqreeysral
//
LOCUS       WP_284942511             243 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Enterobacter sp. MEB024].
ACCESSION   WP_284942511
VERSION     WP_284942511.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. MEB024
  ORGANISM  Enterobacter sp. MEB024
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Enterobacter sp. MEB024"
                     /db_xref="taxon:3040288"
     Protein         1..243
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28449
     Region          1..240
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mkviivedei laqqelswli kthsqmeivg tfedgldvlk flqhnrvdai fldinipsld
       61 gvllaqninq fahkpfivfv tawkehavea feleafdyil kpyqesrivs mlrkleaawq
      121 qqttpanasp airendtinl vkderiivtp iddiyyaeah ekmtfvytrr esyvmamnit
      181 efcnklpaah ffrchrsfcv nlnkireiep wfnntyilrl kdldfqvpvs rskvkefrql
      241 mhl
//
LOCUS       WP_284942597             580 aa            linear   BCT 25-DEC-2024
DEFINITION  IucA/IucC family protein [Enterobacter sp. MEB024].
ACCESSION   WP_284942597
VERSION     WP_284942597.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. MEB024
  ORGANISM  Enterobacter sp. MEB024
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Enterobacter sp. MEB024"
                     /db_xref="taxon:3040288"
     Protein         1..580
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65543
     Region          15..577
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mrtlprsagt dvaaqcflna llretkdwry lpatvadels qihiplsstq airvpvryfs
       61 ptqhhqyhfp atliqrdsds gdavtftqli dlilekpsvk gsldtetlar fkqralesha
      121 htwqaidlrh nwatlrdkpl nfaqaeqall vghafhpapk shepfnesea rrylpdfasr
      181 fplrwfavkr eliagdslav slrerllrfa aqsapellgh ftdtcwllpm hpwqaehllg
      241 qawcqrlvan gdlqdlgeag aqwlptsssr slysetnsdm ikfslsvrlt nsvrtlsvke
      301 vkrgmrlarl aktarwqtlq aryptlrvmq edgwaglrde ngviqeeslm alrvnllfet
      361 pesqtnvlvs ltqaapdggd sllvaavrrl shrldlplae aarcwvqayc drvllplfsa
      421 eadyglvlla hqqnilvemq qdfpvgliyr dcqgsawteg anewlkeage hdvenrfges
      481 qllryfpyyl llnstlavta alaaagfdse eslmaqvrda laelrktakq trcldyvlds
      541 ptwnckgnff cylhdrnent iadpaviyfd fsnpfykeka
//
LOCUS       WP_284942636             435 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Enterobacter sp.
            MEB024].
ACCESSION   WP_284942636
VERSION     WP_284942636.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. MEB024
  ORGANISM  Enterobacter sp. MEB024
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Enterobacter sp. MEB024"
                     /db_xref="taxon:3040288"
     Protein         1..435
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47729
     Region          106..404
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mnypslnrtl lagvvislcs alfapvalaa cdgtdlntcp apfdkqlpdt hkmltwsqad
       61 rvvgfrndyr nyagdvfhhg natpllsaek pltdaryqvn gktynlqdyl krqnvsgmll
      121 lkdgkiawky lgegntdttl wtsrsvgksv vstlvgvalk egkirslddl vtqyepdlkg
      181 tawdgvtlkq lithtsgvaw nedytnpasd faqlteceak pgtydcvrkl vsglkrehpa
      241 gqhwsyssgg awllgdvler atgmtlaayl eksiwqpygm asdgvwhayr kgqhdvgahg
      301 fnatledwgr fgefilhngt lpngkqilpd nwvkdasrwt qadgsvsdah ptglygyqww
      361 nnevpvtatk vvpaaneslk gslwalgifg qmimvnqaen lvivqwstwp qaepsfsaqp
      421 leaslmfsai analr
//
LOCUS       WP_284942744            2406 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Acinetobacter
            baumannii].
ACCESSION   WP_284942744
VERSION     WP_284942744.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..2406
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         <1..2406
                     /product="beta strand repeat-containing protein"
     Region          1..1579
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          1121..>2394
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 vtvdtvpadl igaitipedl ngdgilnade lgtdgsfnaq valgpdavdg tvvnvngtny
       61 tvtaadlang yitaaipvtg egpvaihaea vdaqgnvdva dadvtltidt tpqdlitait
      121 vpedlngdgi lnadelgtdg sfnaqvalgp davdgtvvnv ngtnytvtaa dltngyitat
      181 ldataadpvt gqivihaeav daqgnvdvad advtltidtt pqdlitaitv pedlngdgil
      241 naaelgtdgs fnaqvalgpd avdgtvvnvn gtnytvtaad langyitatl dataadpvtg
      301 qivihaeavd aqgnvdvada dvtltidttp qdlitaitvp edlngdgiln aaelgtdgtf
      361 naqvalgpda vdgtvvnvng tnytvtaadi tngyitaila ataadpvtgq ivihaeavda
      421 qgnvdvadad vtltidttpq dlitaitvpe dlngdgilna aelgtdgtfn aqvalgpdai
      481 dgtvvnvngt nytvtaadit ngyitailaa taadpvtgqi vihaeavdaq gnvdvadadv
      541 tvtldvtppd itttvlaidp vtadnildat eaggtvtltg tltnvpadat ttgvvvting
      601 ndytatvdai agtwtvnvag ndlaldpdlt vdakatftdl agnsstlqdt qtytlagsit
      661 afdntdhavl spkpalvgdd vslgstsylv ltsvagldlq lggnslgftv daghegdvtf
      721 qysglidaav lsdyklvvqk fntttnqwes ihgdanssli slhllgigtg nvpgavldgl
      781 dagqyrafla ydgllglgvl gtlsatmddy dlsvaggyei gnaegnvitd pdpttgqvdq
      841 vtantyvssv nghpidadge tfagtygtit fyqdgsyvyv pnadgsgvgq tdvftytltd
      901 svtgatgqan lnivfdsira adnlveveln pqyqlvgtet dsafygvlln vgnivdlqll
      961 tvdtvdftig agqegvatfn fnsligasal gdynvvlqky ndvtgqweav ngtgdrslln
     1021 ltllgntpta qiggltegey raflsfnglv ggavavtlng svdvynpavi tgydvvaahg
     1081 nlisdpntng dvdiatpnsi isevngvavs aspteiigth gtlliyangd ytytpnadsa
     1141 glgqvdqfty tlldpasnit sqatfyvhld skvvdmnwda adpsqpatvt itavddavna
     1201 aiaaephlie ddralgsaty lallslagin lqaplpfvns tvefnvgage tgtatfkyss
     1261 linegalgdy qlvvqkfnta tnrwesitgs seasllnlsv lgigvnatpg vvvegldegq
     1321 yrafmtyngl ygksilgtls gtmdvydpnq idftglaseg nvitglgvgt nadavtgyti
     1381 vdsvtvngvt tnvdpntgti iqgqygtlqi fangdyiytp nntnanlglv dhftytladp
     1441 lggnisasld ftignstpvi avddlavavv npeylqignd vavdsylyva llsltdnfdf
     1501 qlggqgidft ltdstlndvt fnysalidas lladyvlvvq kfdtatnqwv avngtgeadl
     1561 lslaafggns vtleglaagq yraymtyags gvgvsllgtl svqkdvfdat nitgystqva
     1621 egnvihdvgl nghadtasgf stvtsvefng tafavnatgv ttivgdhgtl siyangnysy
     1681 qpngeaaslg qvdqftytls dglntsqatl ylhidsdavd mtwntsdpsq pavitvtpvd
     1741 aidnvvsagv divpqgelgv avgsatylal vgitedlnvs llgtpsvaft idagheadvt
     1801 fayapvlsls lfndykvvlq qkgadgawhn idggsstgll nigllgnggi gvtvpdlgqg
     1861 eyrafmvytg lgvgilgtms vvkddfdytv aptntavvad gnvltddvtt lttqvttvts
     1921 evvgalpqtv gtdtvingay gtlvistngh ytytpnttdl saigkvdsft ytirdvltga
     1981 tdtatlhvqv gspdvtiawd aanpandgvv qltanpdhvv tttdfsnaad lpvdvaspvv
     2041 svnligsnsv vsdqfvvgag tvanidlsav ytaqplasvl ptvsyviqsw ngtawvntiy
     2101 sgsqtalgsv atiqagsvaf qdtvehlaag tyrvqytltg vslgatsldt nvstttvhld
     2161 tyrsdwisgn vlagdniggv adtgilsheg aklqvwdnaq nayvdavgqt intgngvlim
     2221 qsngeyeyrp ndvttttqla stdsinykiv svtggvesqs tltidlthtd ynllytstsa
     2281 ndtfttgtgs dtviyqllng taatanngan tggngvdtwt dfhvgnvatd kqadlidira
     2341 lldgdqtdan igqylnvtts ggnttiqidr dglsglipgn nfttllvlqg vtttetelln
     2401 ngqily
//
LOCUS       WP_284942768             307 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Enterobacter sp.
            MEB024].
ACCESSION   WP_284942768
VERSION     WP_284942768.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. MEB024
  ORGANISM  Enterobacter sp. MEB024
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 307)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Enterobacter sp. MEB024"
                     /db_xref="taxon:3040288"
     Protein         1..307
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35670
     Region          10..294
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 makstrsrsa erlvdilvel hlngvvnrsa lmekfkiter tvyrdlnals pivehtgngl
       61 yrlihsaqsp ggqglhhtia nflnadsffp erntefwqkl etrvdenhil ililgneaeh
      121 tvehdirryl skieksiknr nvcqivykgk trlinpykli nnkniwylqa tensrlksfs
      181 lsqiswfdiq qktftpeena lglleksldp wvsedtfevk ifikdtishy fmrrdllpeq
      241 elvgeqhngv tlrcqaahen qilpllfywl pniqilepnw lkekllktle nylavertad
      301 nhvisit
//
LOCUS       WP_284942809             636 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Enterobacter sp. MEB024].
ACCESSION   WP_284942809
VERSION     WP_284942809.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. MEB024
  ORGANISM  Enterobacter sp. MEB024
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Enterobacter sp. MEB024"
                     /db_xref="taxon:3040288"
     Protein         1..636
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=72583
     Region          14..608
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mrfpnqrlaq lfdllqnetl pqdelaqrls vstrtvradi talnallash gaqfilsrgn
       61 gyqlkiddae ryqqlqsshp ralriprtgp ervhylvvrf ltsafslkle dladewfvsr
      121 atlqsdmvev rewfhrynlt letrprhgmk lfgsematra cltdllwela qqdslnplvt
      181 dvalnagvae qmvpvlhdal trhhirltde gelflrlyca vsvrrisegy plpefhaedv
      241 aenvreaakd iavtiqqlad kalspseesw lcvhiaarqi qeiapsaina dddealvnyi
      301 lryinthyny nllsdeqlha dllthiktmi trvryqimip nplldnikqh ypmawdmtla
      361 avsswgkytp yviseneigf lvlhigvgle rhynigyqrq prvllvcdag namvrmieav
      421 lqrkypqiev trtltlreye laepigedfv istarvseks kpmvmiapfp tdyqleqigk
      481 lvlvdrtrpw mldkyfdaah friidrpidq qtlfrelceq leeegfvgae fldsvverea
      541 ivstmlgdgi alphslglla qktvvytvla pqgivwgdet ahvifllais kreyeeamai
      601 ydifvtflre ramsrlcscn dfagfkamam esvsrf
//
LOCUS       WP_284942851             403 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: O-antigen ligase family protein [Enterobacter].
ACCESSION   WP_284942851
VERSION     WP_284942851.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..403
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=45754
     Region          154..393
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mekiklrlyq ltlflsfisl mlalvnsgkq reffyiaiyi ailglafeyk kitlkpfsia
       61 lpifliglln fvwymvyeyh seglnmysdy lgaskkllla silvfyidrf kdyidrdnfk
      121 kyfllatatg falatgyglw qasqgmarve mainratvsa yvysvlslaf vyslylqqnv
      181 klyvlagfti lvsffvillt gtraamglyl llaivmtlyh frrihlkstl iflcivagiv
      241 vvsykplisp kimqtqtele nyekgndrts lgarfsmwti giqnglahpl gqsvedreaw
      301 tkryvsdghp hlaaaldfik vhlhnefiek yslqgipgla illfffvsmm gyairnkngl
      361 lltamlllll ygltdvills sealiffmil falstpfsqt kqq
//
LOCUS       WP_284942867             341 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: zinc-dependent alcohol dehydrogenase family protein
            [Enterobacter].
ACCESSION   WP_284942867
VERSION     WP_284942867.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..341
                     /product="zinc-dependent alcohol dehydrogenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36795
     Region          5..339
                     /region_name="MDR7"
                     /note="Medium chain dehydrogenases/reductase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cd08276"
                     /db_xref="CDD:176237"
     Site            order(43..45,48,149,153,174..179,197..198,202,217,
                     241..242,244,263..264,288..290)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176237"
ORIGIN      
        1 mtemmqrwsm dalgrenlrl tqapvpqpgp gevrvrvnav alnyrdkmvi egnmpialtf
       61 pftpasdmag vvdstgegvt rfkpgarvis tfspewvdgk pkgdarnlpy qtlggyfqgm
      121 lseyvimren wlvaapetld daeastlpca gltawfalve rgqlragqsv lvqgtggvai
      181 falqiakahg aevfvtsgsd eklalaktlg adrginrlkg nwadeiyalt qdrgidhiie
      241 tvggenlrhs lravavhgri svigvlagse islpaselll kspviqgigv ghrraledlv
      301 ravdvtglkp viehryrfnq leealvhldr gafgkivltr e
//
LOCUS       WP_284942907            1650 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alpha-2-macroglobulin family protein [Enterobacter].
ACCESSION   WP_284942907
VERSION     WP_284942907.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 1650)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1650)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1650)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1650)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1650
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..1650
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=179507
     Region          44..1650
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mtpfrlaais lallttfslv gcdnsddnsq aaapaastat tpkapekpda eklatlaaqs
       61 qgkaltlldt sevqldgaat lvltfsvpln pdqdfaktvh vvdkksgkvd gawelapnlk
      121 elrlrhlepn rnlvvtverd lqalnkatfg idyekalttr dveptvgfas rgsllpgkvv
      181 eglpvmalnv nnvdvnfyrv kpeslasfvs qweyrnsltn wesdnllkma dlvytgrfdl
      241 nparntrekl llplrdikpl qqsgvyiavm nqaghynysn aatlftlsdi glsahryhnr
      301 ldiftqsled gaaqsgvtvt llndkgqtla eansdadgha kletdkeaal ilaskdgqtt
      361 lldlklpald laefdiagsp gyskqffmfg prdlyrpget vilngllrds dgkplpaqpv
      421 kldvlrpdgq vartvviqpe nglyrfnysl dggaqtgmwh irantgdnqq rlwdfhvedf
      481 mpermalnlt gqkapvsted nvdfniagyy lygapangns lqgqlflrpl reavaalpgf
      541 qfgdiaeenl srsldevqlt ldeqgrgqvs tesqwkeahs plqlilqasl lesggrpvtr
      601 raeqaiwpaa dlpgirpqfa skavydyrtd ttvnqpivde ngnasfdivy adasgakkav
      661 sglqvrlire rrdyywnwse sdgwqsqfdq kdlvegeqel tlkadetgkv tfpvewgsyr
      721 levkapddmv ssvrfwagys wqdnsdgtga arpdrvtmkl dkpsyqpgdt iqlhiaapaa
      781 gkgyamiess egplwwkeid vpangldlsi pvdkawkrhd lylstlvvrp gdksksatpk
      841 ravgllhlpm gdenrrlnva lenpqkmrpn qtlsvkvkas vkegavpqkv nvlisavdsg
      901 vlnitdyvtp dpweaffgqk rygadiydiy gqviegqgrm aalrfggdgd elkrggkppv
      961 nhvtiiaqqa qpveldange gtvtlpigdf ngelrlmaqa wteddfgsse gkvivaapii
     1021 telntprfla sgdtsrltld vtnltdqpqt lnvaftatgk lslegaqpqp vklppgarst
     1081 lfipvraldg ygdgevtaqv tglklpgetf aaqqkswkig vrpafpaqtv ntgamlnpge
     1141 swsapaqhln gfspatlqgq lllsgkppln laryirelqa ypygcleqtt sglfpslytn
     1201 aaqltalgik gdtddkrraa idigisrllq mqrddggfal wdkngpeeyw ltayvtdflv
     1261 rageqgysvp aeavnnansr llrylqdpgm msirysddtq askfavqaya alvlarqqka
     1321 plgalreiwe rhgqaasglp lmqlgmalkl mgdaprsqqa lglaiktprn dsknwmadyg
     1381 salrdnalml slleeykllp daqntllnal seqafsqrwl stqesnalfl agrslqtlsg
     1441 awqaqtslad tasggdkalv qnvngdqlga lqvtntgstp lwvrldstgy pasapqpssn
     1501 vlqierhila tdgstkslts lksgelvlvw levkasqnvp dalvvdllpa glelenqnla
     1561 sssaslqdsg sevqnllsqm qqadiqhmef rddrfvaavp vnegqpvtlv ylaravtpgt
     1621 yevpvpmves myvpqwratg aasgplivvp
//
LOCUS       WP_284943077            2300 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Acinetobacter
            baumannii].
ACCESSION   WP_284943077
VERSION     WP_284943077.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..2300
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         <1..2300
                     /product="beta strand repeat-containing protein"
     Region          1..1473
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          1015..>2288
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 tidttpqdli taitvpedln gdgilnaael gtdgsfnaqv algpdavdgt vvnvngtnyt
       61 vtaadltngy itatldataa dpvtgqivih aeavdaqgnv dvadadvtvt idttpqdlit
      121 aitvpedlng dgilnaaelg tdgsfnaqva lgpdavdgtv vnvngtnytv taadlangyi
      181 tatldataad pvtgqiviha eavdaqgnvd vadadvtlti dttpqdlita itvpedlngd
      241 gilnaaelgt dgtfnaqval gpdaidgtvv nvngtnytvt aaditngyit ailaataadp
      301 vtgqivihae avdaqgnvdv adadvtltid ttpqdlitai tvpedlngdg ilnaaelgtd
      361 gtfnaqvalg pdaidgtvvn vngtnytvta aditngyita ilaataadpv tgqivihaea
      421 vdaqgnvdva dadvtvtldv tppditttvl aidpvtadni ldateaggtv tltgtltnvp
      481 adatttgvvv tingndytat vdaiagtwtv nvagndlald pdltvdakat ftdlagnsst
      541 lqdtqtytla gsitafdntd havlspkpal vgddvslgst sylvltsvag ldlqlggnsl
      601 gftvdagheg dvtfqysgli daavlsdykl vvqkfntttn qwesihgdan sslislhllg
      661 igtgnvpgav ldgldagqyr aflaydgllg lgvlgtlsat mddydlsvag gyeignaegn
      721 vitdpdpttg qvdqvtanty vssvnghpid adgetfagty gtitfyqdgs yvyvpnadgs
      781 gvgqtdvfty tltdsvtgat gqanlnivfd siraadnlve velnpqyqlv gtetdsafyg
      841 vllnvgnivd lqlltvdtvd ftigagqegv atfnfnslig asalgdynvv lqkyndvtgq
      901 weavngtgdr sllnltllgn tptaqigglt egeyraflsf nglvggavav tlngsvdvyn
      961 pavitgydvv aahgnlisdp ntngdvdiat pnsiisevng vavsasptei igthgtlliy
     1021 angdytytpn adsaglgqvd qftytlldpa snitsqatfy vhldskvvdm nwdaadpsqp
     1081 atvtitavdd avnaaiaaep hlieddralg satylallsl aginlqaplp fvnstvefnv
     1141 gagetgtatf kysslinega lgdyqlvvqk fntatnrwes itgsseasll nlsvlgigvn
     1201 atpgvvvegl degqyrafmt ynglygksil gtlsgtmdvy dpnqidftgl asegnvitgl
     1261 gvgtnadavt gytivdsvtv ngvttnvdpn tgtiiqgqyg tlqifangdy iytpnntnan
     1321 lglvdhftyt ladplggnis asldftigns tpviavddla vavvnpeylq igndvavdsy
     1381 lyvallsltd nfdfqlggqg idftltdstl ndvtfnysal idaslladyv lvvqkfdtat
     1441 nqwvavngtg eadllslaaf ggnsvtlegl aagqyraymt yagsgvgvsl lgtlsvqkdv
     1501 fdatnitgys tqvaegnvih dvglnghadt asgfstvtsv efngtafavn atgvttivgd
     1561 hgtlsiyang nysyqpngea aslgqvdqft ytlsdglnts qatlylhids davdmtwnts
     1621 dpsqpavitv tpvdaidnvv sagvdivpqg elgvavgsat ylalvgited lnvsllgtps
     1681 vaftidaghe advtfayapv lslslfndyk vvlqqkgadg awhnidggss tgllnigllg
     1741 nggigvtvpd lgqgeyrafm vytglgvgil gtmsvvkddf dytvaptnta vvadgnvltd
     1801 dvttlttqvt tvtsevvgal pqtvgtdtvi ngaygtlvis tnghytytpn ttdlsaigkv
     1861 dsftytirdv ltgatdtatl hvqvgspdvt iawdaanpan dgvvqltanp dhvvtttdfs
     1921 naadlpvdva spvvsvnlig snsvvsdqfv vgagtvanid lsavytaqpl asvlptvsyv
     1981 iqswngtawv ntiysgsqta lgsvatiqag svafqdtveh laagtyrvqy tltgvslgat
     2041 sldtnvsttt vhldtyrsdw isgnvlagdn iggvadtgil shegaklqvw dnaqnayvda
     2101 vgqtintgng vlimqsngey eyrpndvttt tqlastdsin ykivsvtggv esqstltidl
     2161 thtdynllyt stsandtftt gtgsdtviyq llngtaatan ngantggngv dtwtdfhvgn
     2221 vatdkqadli diralldgdq tdanigqyln vttsggntti qidrdglsgl ipgnnfttll
     2281 vlqgvtttet ellnngqily
//
LOCUS       WP_284943207             170 aa            linear   BCT 25-DEC-2024
DEFINITION  YczE/YyaS/YitT family protein, partial [Enterococcus faecalis].
ACCESSION   WP_284943207
VERSION     WP_284943207.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         <1..170
                     /product="YczE/YyaS/YitT family protein"
     Region          1..170
                     /region_name="YczE"
                     /note="Uncharacterized membrane protein YczE [Function
                     unknown]; COG2364"
                     /db_xref="CDD:441931"
ORIGIN      
        1 vdpftamnig lssmfgmqlg ifqiivnafi lfyvylknkk aiglgtilnm llvgiliqqi
       61 stwlqpyans lggstigkll slffgvlift fgcalymatd qgespydaia pticqqinkp
      121 yasvrkaqdl lvlligfiag gpigigtiic afgagplisf wnkllqplvk
//
LOCUS       WP_284943391             329 aa            linear   BCT 25-DEC-2024
DEFINITION  integrase catalytic domain-containing protein, partial
            [Acinetobacter baumannii].
ACCESSION   WP_284943391
VERSION     WP_284943391.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Ballandras-Colas,A., Maskell,D.P., Serrao,E., Locke,J., Swuec,P.,
            Jonsson,S.R., Kotecha,A., Cook,N.J., Pye,V.E., Taylor,I.A.,
            Andresdottir,V., Engelman,A.N., Costa,A. and Cherepanov,P.
  TITLE     A supramolecular assembly mediates lentiviral DNA integration
  JOURNAL   Science 355 (6320), 93-95 (2017)
   PUBMED   28059770
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (5), 302-307 (2001)
   PUBMED   11774877
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Dyda,F., Hickman,A.B., Jenkins,T.M., Engelman,A., Craigie,R. and
            Davies,D.R.
  TITLE     Crystal structure of the catalytic domain of HIV-1 integrase:
            similarity to other polynucleotidyl transferases
  JOURNAL   Science 266 (5193), 1981-1986 (1994)
   PUBMED   7801124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10461024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         <1..>329
                     /product="integrase catalytic domain-containing protein"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016893 - endonuclease activity, active
                     with either ribo- or deoxyribonucleic acids and producing
                     5'-phosphomonoesters [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          97..215
                     /region_name="rve"
                     /note="Integrase core domain; pfam00665"
                     /db_xref="CDD:459897"
ORIGIN      
        1 rgwtteksrl spqvsniikq aindeylnak kpsisktiei vkaecsrlql eaphensirr
       61 riealndyqv tkarlgskaa idkfkaaags fpnadyplay vqidhtpldi eivddefrea
      121 igkphltlai dvfsrmivgy ylsleapstt svamciasci lskkrkliel didaewqveg
      181 imdsvhtdng pdfrtnhisk aclkygihwe yrpiggarfg ghiermlgiv nlemhvldgt
      241 tfsnvqqrgt ydsakqacmt lkeleyyivy witkvyhqkk hsalgtspiv kweegvwgtk
      301 ttagtglker vsdedtlfid flpefeati
//
LOCUS       WP_284943451            2192 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Acinetobacter
            baumannii].
ACCESSION   WP_284943451
VERSION     WP_284943451.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..2192
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         <1..2192
                     /product="beta strand repeat-containing protein"
     Region          1..1365
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          907..>2180
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 vtvdtvpadl igaitipedl ngdgilnade lgtdgsfnaq valgpdavdg tvvnvngtny
       61 tvtaadlang yitatldata adpvtgqivi haeavdaqgn vdvadadvtl tidttpqdli
      121 taitvpedln gdgilnaael gtdgtfnaqv algpdavdgt vvnvngtnyt vtaaditngy
      181 itailaataa dpvtgqivih aeavdaqgnv dvadadvtlt idttpqdlit aitvpedlng
      241 dgilnaaelg tdgtfnaqva lgpdaidgtv vnvngtnytv taaditngyi tailaataad
      301 pvtgqiviha eavdaqgnvd vadadvtvtl dvtppdittt vlaidpvtad nildateagg
      361 tvtltgtltn vpadatttgv vvtingndyt atvdaiagtw tvnvagndla ldpdltvdak
      421 atftdlagns stlqdtqtyt lagsitafdn tdhavlspkp alvgddvslg stsylvltsv
      481 agldlqlggn slgftvdagh egdvtfqysg lidaavlsdy klvvqkfntt tnqwesihgd
      541 ansslislhl lgigtgnvpg avldgldagq yraflaydgl lglgvlgtls atmddydlsv
      601 aggyeignae gnvitdpdpt tgqvdqvtan tyvssvnghp idadgetfag tygtitfyqd
      661 gsyvyvpnad gsgvgqtdvf tytltdsvtg atgqanlniv fdsiraadnl vevelnpqyq
      721 lvgtetdsaf ygvllnvgni vdlqlltvdt vdftigagqe gvatfnfnsl igasalgdyn
      781 vvlqkyndvt gqweavngtg drsllnltll gntptaqigg ltegeyrafl sfnglvggav
      841 avtlngsvdv ynpavitgyd vvaahgnlis dpntngdvdi atpnsiisev ngvavsaspt
      901 eiigthgtll iyangdytyt pnadsaglgq vdqftytlld pasnitsqat fyvhldskvv
      961 dmnwdaadps qpatvtitav ddavnaaiaa ephlieddra lgsatylall slaginlqap
     1021 lpfvnstvef nvgagetgta tfkyssline galgdyqlvv qkfntatnrw esitgsseas
     1081 llnlsvlgig vnatpgvvve gldegqyraf mtynglygks ilgtlsgtmd vydpnqidft
     1141 glasegnvit glgvgtnada vtgytivdsv tvngvttnvd pntgtiiqgq ygtlqifang
     1201 dyiytpnntn anlglvdhft ytladplggn isasldftig nstpviavdd lavavvnpey
     1261 lqigndvavd sylyvallsl tdnfdfqlgg qgvdftltds tlndvtfnys alidasllad
     1321 yvlvvqkfdt atnqwvavng tgeadllsla afggnsvtle glaagqyray mtyagsgvgv
     1381 sllgtlsvqk dvfdatnitg ystqvaegnv ihdvglngha dtasgfstvt svefngtafa
     1441 vnatgvttiv gdhgtlsiya ngnysyqpng eaaslgqvdq ftytlsdgln tsqatlylhi
     1501 dsdavdmtwn tsdpsqpavi tvtpvdaidn vvsagvdivp qgelgvavgs atylalvgit
     1561 edlnvsllgt psvaftidag headvtfaya pvlslslfnd ykvvlqqkga dgawhnidgg
     1621 sstgllnigl lgnggigvtv pdlgqgeyra fmvytglgvg ilgtmsvvkd dfdytvaptn
     1681 tavvadgnvl tddvttlttq vttvtsevvg alpqtvgtdt vingaygtlv istnghytyt
     1741 pnttdlsaig kvdsftytir dvltgatdta tlhvqvgspd vtiawdaanp andgvvqlta
     1801 npdhvvtttd fsnaadlpvd vaspvvsvnl igsnsvvsdq fvvgagtvan idlsavytaq
     1861 plasvlptvs yviqswngta wvntiysgsq talgsvatiq agsvafqdtv ehlaagtyrv
     1921 qytltgvslg atsldtnvst ttvhldtyrs dwisgnvlag dniggvadtg ilshegaklq
     1981 vwdnaqnayv davgqtintg ngvlimqsng eyeyrpndvt tttqlastds inykivsvtg
     2041 gvesqstlti dlthtdynll ytstsandtf ttgtgsdtvi yqllngtaat anngantggn
     2101 gvdtwtdfhv gnvatdkqad lidiralldg dqtdanigqy lnvttsggnt tiqidrdgls
     2161 glipgnnftt llvlqgvttt etellnngqi ly
//
LOCUS       WP_284943505             481 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Acinetobacter baumannii].
ACCESSION   WP_284943505
VERSION     WP_284943505.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..481
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=53290
     Region          71..440
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mkiiskpqll kdveykpsqs lqvgkewswl npkhakfdat tingtsvdnp anyyesslsn
       61 whtfdslnad iecdvvvigg gllgsstalh laeqgvdtvl leknrigsaa sgrnggqltp
      121 glarweaqem adrlsyedak klwhftstea mqliddisek yqlnfdrkyg hitaavhegh
      181 lvgltqgada rkylgedhtr ivgkhelmdf iksdyytggl idelggqihp lalnrgliyg
      241 fcqnggtvye qtevisieek edgiyvhtan avvkakksvv lavhhasfkl lseqnnttip
      301 fytyvattap leldtkellp fghpvydtqf qidyyrpvfn nrllfggqgt gtcwgpektl
      361 nylehrihtv fpqiknlemd fvwsgttdlt vngavdsrkf gnkfpiyavh gwsghgvvqt
      421 vrigkaiand figqsndfem lskidhqnii fgrtlapvvi plaksmygig aminpgkmvs
      481 f
//
LOCUS       WP_284943612             118 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Acidisoma cladoniae].
ACCESSION   WP_284943612
VERSION     WP_284943612.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 118)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 118)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..118
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12303
     Region          <17..91
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 meksdaiaal aalaqdsrld vfrllvqagt dglpagqige rlglpsatls fhlnqlkqag
       61 lvtfrregrs liymaeydam nallgylten ccqgdpagcg igacdgstli atkegtrq
//
LOCUS       WP_284943683             280 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Acidisoma cladoniae].
ACCESSION   WP_284943683
VERSION     WP_284943683.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..280
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31991
     Region          5..276
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 msetaiteee frrlcdfvyr rtgmifteak ryyverrvse rmaatgttsf aryfarlrtd
       61 algeiepfvn aftvnetyfy redhqlrclt adllprrtaa kapfaplrvw sipcstgeep
      121 ysiavwllen wsdvdaydie iigsdidtrv leaaqegvyg sralmrlsad ivtkyfiplg
      181 gdlwrvmddl rqsvrfapan lidaaeirtf grfdvifcrn vliyfddasr rlaaenlyes
      241 llpggyiclg haesmsrisp lyevcryada ivyqkpmega
//
LOCUS       WP_284943795             347 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Acidisoma cladoniae].
ACCESSION   WP_284943795
VERSION     WP_284943795.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..347
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35793
     Region          28..347
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mlvlilalsv agnaavaaap psnqgavvgv kiiavsvper gadidvtlwy patgpgrsil
       61 vgvgsplfqg taalagaama kgrwpliils qgglrsgani gawmasrlaa ggfmvamlrq
      121 pdptrltdaq tlpelwlrpa dvsaaltgil gdgalstrid qnqigvlgfq iggtaalsla
      181 ggllddarvr ascdaggvgv dcgrfrkagl dlhtvrlpql grsnfdtrik aivvidpefs
      241 rsftprslah isipvglinl gnpgtmwpgl naegltrfip qaryavlfda lqysafpeck
      301 pgasarlret geeaicddtk ggrtraliha alaqsvgaif rsdfaad
//
LOCUS       WP_284943796             361 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Acidisoma cladoniae].
ACCESSION   WP_284943796
VERSION     WP_284943796.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..361
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=38604
     Region          88..339
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mlfvplpfva aaflavlfas ivrrdeaqag nrafltliaa cavqsalmgl rwgygveair
       61 svmpivaaal pplvyasfgs ltapstthrp piawmhlvpa cvvgslvafw rqpidatlia
      121 idfgyaaall wvarsgpdgl rharlevgls ayralqlaaa alvasalida fiawdvawth
      181 gahaaqvisv adliglfalg yaasvagksr pesepvaapq ttplidnqed havlatiddl
      241 mrtqklfrda nlnldrlark agmparrism ainqlttrnv sqyvndhria aacdllktts
      301 lavttimfdv gfqtksnfnr efrrvtgtnp sdwrtqsgsv sgdehrnadl sdcgttpsrv
      361 s
//
LOCUS       WP_284943811             175 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Acidisoma cladoniae].
ACCESSION   WP_284943811
VERSION     WP_284943811.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..175
                     /product="YceD family protein"
                     /calculated_mol_wt=19271
     Region          35..173
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mtstptpefs rllplaqism tetlreisat peecaaiaar lalpqlaafs asfkiqrarr
       61 gggyeaegrl raratrncvv tlddftertd iafkvrfvne espseevese asfafedgpd
      121 elvyenevld lgeaavqeya lslapyprkp gaklaepeve tpnpfavlkd frrrt
//
LOCUS       WP_284943877             348 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Acidisoma cladoniae].
ACCESSION   WP_284943877
VERSION     WP_284943877.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..348
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=37936
     Region          11..346
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 msalddrrad lpdltaargv lalwvfayha nlhldfagag gvighgylgv dgffllsgfv
       61 lthrhpdppq tvsayaqfww krlvrlypth lavllllava yltasaggir phhalradgh
      121 elllqillln gwgfsrgwtw dypswsisve wagyllfplg awaafrfdrr gtiaalavgv
      181 aclevvdrts ssglnlsyhg allrffpefa agillvrllh llprrppawi pgtagaflla
      241 lgfalgdavt vaglwcllwt latprapilt svpglvalga lsypvymvyt pvelvfariw
      301 atthlnptes ssywlvamfa svlllawiva tlverpalrs laarrpdl
//
LOCUS       WP_284943951             395 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Acidisoma cladoniae].
ACCESSION   WP_284943951
VERSION     WP_284943951.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..395
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41735
     Region          27..383
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 msltktaspp atvaaatvpf ldlraqqari gtemrrridt vlghcqfvlg pevleletel
       61 arragaahcv svssgtdall iammaedigp gdavflpaft ytataevpll lratpvfvdi
      121 dpdtfqmdvv dldakvaavl aagklrprav igvdlfgqpa dwdainnvad rhglvtiddc
      181 aqafgaslqg rplgsqahst aisffpskal gaygdggalf tqsaeraaly rslrthgegk
      241 mrydvqrigi ngrldtlqaa vllakltvfd eelaardrva rhydsrlgnl lqtpvrvphs
      301 tsawavyavl lpteaararv qaacqaagvs tavyypkplh hqpayaphhd gsrlpvseav
      361 atrimalpih pdltaaqvdq vcdavaaala atalt
//
LOCUS       WP_284943893             367 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Acidisoma cladoniae].
ACCESSION   WP_284943893
VERSION     WP_284943893.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 367)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..367
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39981
     Region          35..345
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mnashhtkrd rtpllklwvg rlfassfrnl vlggifvllv cllasvgyti agwtesdaiy
       61 mvvltiftvg ygevhpidtp flrgntemli ilgctgmifl tgaliqfiti tqfqqlfgtr
      121 rmkqeidnlt dhviicgfgr iglmlaselt tgqapfvile rserrfaear dlghlciqad
      181 atdetallha giararclat vlpddaanvf itlsarslna gleiiargea asterkliqa
      241 ganrvvmpth igaeriaqmi lfaeterflq gsdrmrafqr qlldlglnvl ahpiatdsac
      301 igltvsever rgegsffiva idrpedsgit rpppdtvier gdgvvlvsrd grallvkrlf
      361 gpaealv
//
LOCUS       WP_284944016             712 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Acidisoma cladoniae].
ACCESSION   WP_284944016
VERSION     WP_284944016.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 712)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 712)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..712
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=75833
     Region          51..701
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mrveirsqag gagismligi lvlagyglgf eplwcpvpsl pgthpvtaic lvllglgawp
       61 ttsqaatwrv ipqmavgiav llavlcvcdh lldthvigwi tpfhatlraq aasgrpihfa
      121 mnsalallgl glaqfllphg rirtsqvalf fsgailmtal igfldglgrf hdfmgpltll
      181 gsaalivsvl aaassggfla avlkdsepgr larmlllsct viilgigaiv arsvsaeddp
      241 iltyqtvall altwvivvas tiradmidll rrqadakliq dastdaltgl lsrnqldkvl
      301 sephgdstrt amltidvdrf rsannalgta lgdalliqtg krlsavaphy kvarsggdef
      361 vifcesidra aalqlaeavv atmavpfelg grqfrvtssv gvahggtsga adlrdaadea
      421 mfiakqqggn qavpfvkalh darmervrle qdlhramgcd deltlvyqpi islrdrgivs
      481 levlarwmhp vlgaippsrf iaiaedsglf lelgrklrem avrqaatwav tqngclpvin
      541 lnvsplelar sdvpgqlmaa ierhglrtsg fclevtegsf sderaleglq darrrgflia
      601 mddfgvgyss laqlprlpls svkldrsflt ratenddgls llatmvqlsh vlklpvvaeg
      661 vetlkeldiv sacgcdsvqg fifsrpltaa qlepfllanr pwpteqpvfv as
//
LOCUS       WP_284944030             422 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Acidisoma cladoniae].
ACCESSION   WP_284944030
VERSION     WP_284944030.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..422
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44937
     Region          27..391
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mreasapsyy eatravslvt qpldqditvd vaivgggitg csaaldlaer glrvallesn
       61 aigwgasgrn ggqvlpgfai aqtklkrmvg aedarrlwam sieavalveq rvrdhaipad
      121 yargylhaai rerqvhelee eaeelaalgv egvellkgaa iqahvasphy ravlreevsa
      181 hlhplnytlg laraaqaaga qlysdtpvtk iepgtavrlt targtvtagt allgggaylg
      241 rlwpsvagyv mpvgtyivat eprddvpall ptnaaasdln fvldyyrrsa drrllfggrv
      301 syssvpprrl aetmlararv vfpqlknara dftwgglvdi trhrapqfgk lapnilmaqg
      361 fsghgvalag lagrvlaeaa agqagrfdvf aripharfpg gralrvpall latsyyrlrd
      421 ml
//
LOCUS       WP_284944048             477 aa            linear   BCT 25-DEC-2024
DEFINITION  MBOAT family O-acyltransferase [Acidisoma cladoniae].
ACCESSION   WP_284944048
VERSION     WP_284944048.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Hofmann,K.
  TITLE     A superfamily of membrane-bound O-acyltransferases with
            implications for wnt signaling
  JOURNAL   Trends Biochem Sci 25 (3), 111-112 (2000)
   PUBMED   10694878
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004295
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..477
                     /product="MBOAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51839
     Region          1..477
                     /region_name="DltB"
                     /note="D-alanyl-lipoteichoic acid acyltransferase DltB,
                     MBOAT superfamily [Cell wall/membrane/envelope
                     biogenesis]; COG1696"
                     /db_xref="CDD:441302"
ORIGIN      
        1 mlfgtplfvl aflpltllgf hcighrwgsr aalifllaas llfygwgnpw dlpllagsil
       61 anfwlgqrqg atwfaagiaa nltllglfky agfaasllgl pnphvalplg isfftfqqim
      121 ylsacrnggp gerflpyaac iaffahliag plvrpsqiip qfqrasgigf qadavaeglm
      181 lfllglakkl vlgdsfapla drgfdaaasg asltaieawy avlafalqiy fdfsgysdma
      241 igiarmfnir fpinfaspyk ardiqdfwrr whitlshflr dflyiplggn rhgeprrlln
      301 lmitmllggl whgaawkfll wgglhgaylm lhqiwqglrp gwarlpapla qaltlvaviv
      361 awvpfrahdl tsagsmlcgm agwhglafpa plialmpilg rvgqsvpvla algdartlal
      421 pdatgilllg wiivlclphl hetsprlraw allggggftl qalffagaat pflyfrf
//
LOCUS       WP_284944080             292 aa            linear   BCT 25-DEC-2024
DEFINITION  class II glutamine amidotransferase [Acidisoma cladoniae].
ACCESSION   WP_284944080
VERSION     WP_284944080.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Zalkin,H. and Smith,J.L.
  TITLE     Enzymes utilizing glutamine as an amide donor
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 72, 87-144 (1998)
   PUBMED   9559052
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Zalkin,H.
  TITLE     The amidotransferases
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 66, 203-309 (1993)
   PUBMED   8430515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..292
                     /product="class II glutamine amidotransferase"
                     /EC_number="2.4.2.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006541 - glutamine metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31200
     Region          2..288
                     /region_name="GlxB"
                     /note="Glutamine amidotransferases class-II
                     (Gn-AT)_GlxB-type. GlxB is a glutamine
                     amidotransferase-like protein of unknown function found in
                     bacteria and archaea. GlxB has a structural fold similar
                     to that of other class II glutamine amidotransferases...;
                     cd01907"
                     /db_xref="CDD:238888"
     Site            order(2,142..143,168..169,193)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238888"
ORIGIN      
        1 mcgivglflk tpelepqigr ltsemleilt drgpdsagfa vyghqrpdrm kftlrggdfa
       61 tlpaliggga eieirddhal ltvaaseeaa vrailreksp atkivgvgdr melykgvgrp
      121 revsarfglp gmsgthaigh trmatesavt tagahpfstg rdqclvhngs lsnhnnvrrn
      181 lvregqtfet andsevaagy lswrmaqgap leealhgama dldgfytfvv gtasgfgvlr
      241 dpvackpavm aetdsyvafg sefraltklp gidsahifep epsrvyvwer aa
//
LOCUS       WP_284944221             453 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Acidisoma cladoniae].
ACCESSION   WP_284944221
VERSION     WP_284944221.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..453
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=49493
     Region          124..453
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 msfggrvrlw prslgtrtaf vvilglvvvq tlglgihtld rndlvrlaav rvftfrvmsv
       61 yrdlvetpai drparlgrip lptgfatrlt dditpllvnt vpapppirhs illnmdnfpl
      121 ppelrpqhvr ivadpdtrrq itaiqmpdns wlvissrlpr pdalegvefl vafllmtvla
      181 aalivwavrr ltapvrtlaa aaerlgrdvn applpedgps eiaaaaaafn tmaarirrfv
      241 ddrtllltai ghdlrtpitr mrlraefmed deqrakmlgd ldemesmvsa tltfgriaas
      301 neplspidla ellrtvldea gdaspdfadk lsysgpdhwt arvrpqamkr altnlisnai
      361 kygdgaevrl itatgqgaml rievadngpg ippehmervm qpfqrletsr nretggvglg
      421 lpiardiara hggdlvianr peggarmtlt lpv
//
LOCUS       WP_284944256             497 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Acidisoma cladoniae].
ACCESSION   WP_284944256
VERSION     WP_284944256.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 497)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 497)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 497)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..497
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=53286
     Region          149..476
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mkvglpkagv lpmpdarrvf ltslrrapfl rsaglrfaal yaiifglsal alaiflwwat
       61 agllnrqvea ainadaqglg eryqegnlpa lvvtiqdrla qsiddnaiyl lvddslqkva
      121 gnlttwpvgv saadswfelt vkrgdresla rmhrfdlpgg fhlligrdvg sraklrsllt
      181 agllwavlvm vvlgsagaia iqslfkrsla dvsataaaia rgdlsnrvri sgrgdefdrl
      241 aetindmldr iarlmdgvrq vsnaiahdlr tpitrartrl edaalharda sdlhaavera
      301 tsdldgivsv fqgllriaei eagsrrsafa sidlyallsd mhelyaaaae eqgmhidlla
      361 kpplpvfgdr dllqqavanl lenalkfspq gkhillgagr lgdrieivva dsgpgipaed
      421 rnrvterffr gesarstpgs glglsmvqav vqlhngslrl esnhpgvrav vslpaefsss
      481 rrlakpaapp ahlppag
//
LOCUS       WP_284944272             310 aa            linear   BCT 25-DEC-2024
DEFINITION  thioredoxin family protein [Acidisoma cladoniae].
ACCESSION   WP_284944272
VERSION     WP_284944272.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..310
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33458
     Region          18..128
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
     Region          137..>284
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          137..166
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          171..198
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          223..309
                     /region_name="TPR_20"
                     /note="Tetratricopeptide repeat; pfam14561"
                     /db_xref="CDD:434039"
     Region          240..271
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          276..308
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
ORIGIN      
        1 mdlilgqkpp agdtasfimd gtqatfmkdv ieasrtmpvi vdfwatwcgp cktltpmlek
       61 vvtaaggrvr lvkidtdanr alvqqlsqlg lplqsiptva afwqgqiadi fqgalpesei
      121 rrfieamlkv aggsmpaadl laeakaaqde gdyeaavaly qamlaeeper peawggmirc
      181 flavgrmeea tallaevpak iaehaevvga rsalalaieg ekangqvqel earlaadpad
      241 hearydlata fnaqdrreea aaalldimkr ergwnedaar lqllkffeaw gfgdpatmaa
      301 rrrlsallfs
//
LOCUS       WP_284944362             434 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Acidisoma cladoniae].
ACCESSION   WP_284944362
VERSION     WP_284944362.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..434
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46093
     Region          15..432
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mstavmssre rsldprvdgi lerllrlypr aidlsmdrll sllaklgnpe qrlapvlhva
       61 gtngkgstca faraiaeaag lhvqvytsph lidfnerirl tdglvhhrrl adtleqverv
      121 ndgapitvfe vitaaafllf aadpadlcil evglggrgda tniiarpaac gitsisidhr
      181 dflgdrltgi aaeksgiiks gvpvvtgeqk pevlaviadf arakgttlla rdrdwqieps
      241 ghglrftdaa gslalplpsl sglhqhdnag iaiaalrasg ltfpdaafqr gltqvewagr
      301 mqrldgrlaa llpndwelwl dgahnpgagv alarhlkdwa drplhlvigm kqgkdaaefl
      361 kpllpyaktv wavaepdqhl alsvdeviaa sggiarsggt vsqalrrlaa eetaparvli
      421 cgslylagai lrgv
//
LOCUS       WP_284944459             204 aa            linear   BCT 25-DEC-2024
DEFINITION  HD domain-containing protein [Acidisoma cladoniae].
ACCESSION   WP_284944459
VERSION     WP_284944459.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..204
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22808
     Region          17..180
                     /region_name="YfbR"
                     /note="5'-deoxynucleotidase YfbR and related HD
                     superfamily hydrolases [Nucleotide transport and
                     metabolism, General function prediction only]; COG1896"
                     /db_xref="CDD:441500"
ORIGIN      
        1 mqvetwrdtl gtrldsqltf lmeadrlktv lrasriadns rrentaehsw hitvfaitla
       61 eyavgpveig rvvqmlilhd iveidtgdtp lhdgagavtq vareseaadr lfgllpldqa
      121 rryralwdef eaastpdarf akaidrlqpi llnhavgggt wktfdidetm eramtrried
      181 gspelwrvae avfadavakg wlrp
//
LOCUS       WP_284944444             573 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Acidisoma cladoniae].
ACCESSION   WP_284944444
VERSION     WP_284944444.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 573)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 573)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 573)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..573
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62733
     Region          1..573
                     /region_name="COG4986"
                     /note="ABC-type anion transport system, duplicated
                     permease component [Inorganic ion transport and
                     metabolism]"
                     /db_xref="CDD:444010"
ORIGIN      
        1 mtvlalpafv tgrrmpnlwd iaailcvlgv lvlvahaasg tlaplpaana vtihldprwl
       61 pyyalrttir mfvalvcsmg ftlivaplaa ksrriglilv paldilqsvp ilgflsftvl
      121 ffmnlfpgrv lgaelaaifa iftsqawnmt fsfyqslttv prdldeasra frlsiwqrfw
      181 rlevpfampg lvfntmlsms ggwffvvase avtvgkttfl lpgigsyvav alqqsnllav
      241 fyailamlav iliydqllfr plvawstkfr femtsggela dpwvlsllrk trllqllgaa
      301 lgdvatavgg wrlrivparr qsagppsrvv dglwfgfitv lvalalwkia tfvahevtla
      361 qfahvlllgf ytllrvaaal tivtlvwvpi gvwiglrprw aqmiqpvaqf laafpanllf
      421 pivvivlvrf slnpniwlmp lmivgtqwyv lfnvvagasa fptdlkeasa nlrvkgflww
      481 rrviipgifp yyvtgaltas gaawnssiva eiaswghttl vatglgsyia eatnagnsag
      541 imlgvcvmtg yvfvlnrvlw rplhayavrr ltf
//
LOCUS       WP_284944659             829 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Acidisoma cladoniae].
ACCESSION   WP_284944659
VERSION     WP_284944659.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 829)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 829)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 829)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 829)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..829
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..829
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=92108
     Region          141..809
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mlaqpfgklr rrnrarlplf avllcfgvat vytfylslqq dqtvdslvsy ddafdsaqgt
       61 iemmrlqvav safemrrpdt saelvnlrfa ilenrmsvls rpsflqfisg hpetdgives
      121 lsetiaqikl llphltdpgv aaqiitllnp ldaemtqlas vanslvgnqf efdqsrlknq
      181 hlifsgvmfa liaigillii mllrdnrlmm etnrdlnllt gdlqatsaal aaahsataka
      241 nedlaaqnaa lrnrdealri qnarfnaaln nmshgllmad khdrlivsnt rflemfglrg
      301 eetepgasle tvfrlmverk vqptilieqi rahtrelvas narglfyseg enrsiqvshv
      361 pmfeggwvat yediterrki eantdylahh daltglpnrl mfslflgtal rnrtendfss
      421 lllldvdhfk dvndtlghlg gdallvmias rlqgcirddd vvarlggdef aviqmrpssr
      481 detialadrl vgavgqpyti dgrrvvigvs igvsicndet qdaeqllrna dmalyrskae
      541 grstwrffes emeaevrvrs tiaadirdal emdhlevvyq pvidvvtgql cqfegllrwn
      601 hptlgviqps rfipiaeetr miipigeavl rracldaaew paevrvavnl spmqfedrsl
      661 trvvesalrd arldpsrlel eitegallrd gdevratlve lralgvtial ddfgtgyasl
      721 sylrrfpfdk ikidrsfigd svlqtdsiai ieaivslatk lgmtttaegi ettdqwrlln
      781 aigctyaqgy yfdrpqslqs ikrkmksgay plktpieaer tigsattvi
//
LOCUS       WP_284944879             215 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Acidisoma cladoniae].
ACCESSION   WP_284944879
VERSION     WP_284944879.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..215
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22929
     Region          3..212
                     /region_name="Nnt1"
                     /note="Protein N-terminal and lysine N-methylase,
                     NNT1/EFM7 family [Posttranslational modification, protein
                     turnover, chaperones]; COG3897"
                     /db_xref="CDD:443104"
ORIGIN      
        1 mdteaflrlh trpgfaaivp eialhlasei tpiwqategw lvetgieppf wafawpgsqa
       61 larvvldrpe lvagkrvldf aagcglaaia cvqagaasve aaeidplaia atrlnarsng
      121 vevlaetrdv vgdacrwdli lcgdvcyeap mtghilpwlr amvaagaevw iadpgraylp
      181 regmeviaam tvpttlelen tltrpvtiyr lssls
//
LOCUS       WP_284944899             209 aa            linear   BCT 25-DEC-2024
DEFINITION  LolA family protein [Acidisoma cladoniae].
ACCESSION   WP_284944899
VERSION     WP_284944899.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Tajima,T., Yokota,N., Matsuyama,S. and Tokuda,H.
  TITLE     Genetic analyses of the in vivo function of LolA, a periplasmic
            chaperone involved in the outer membrane localization of
            Escherichia coli lipoproteins
  JOURNAL   FEBS Lett 439 (1-2), 51-54 (1998)
   PUBMED   9849875
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..209
                     /product="LolA family protein"
                     /calculated_mol_wt=22567
     Region          18..205
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mnrrtllaal lpltalpfag amaqlaaspp lsaqdqadva rieaylngih tlkarflqvd
       61 angnsiggta ildrpgrmrf eydppdkmll vaghgllvyy dpavkqttnl flsntplgil
      121 lesnlrlaga vtvtgiarat gqiqltmvrt arpgdgtitl ifatdpltlr swvirdaqgr
      181 qtqislfdvt yggeypdrmf tfvgpqfeh
//
LOCUS       WP_284945107             365 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Acidisoma cladoniae].
ACCESSION   WP_284945107
VERSION     WP_284945107.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..365
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=39513
     Region          69..344
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          69..97
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          105..131
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(107..108,111..112,114,139,142..143,146..147,
                     149..150,173,176..177,180..181,184)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          137..167
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          172..200
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          216..242
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(218..219,222..223,225,249,252..253,256..257,
                     259..260,283,286..287,290..291,294)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          247..277
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          282..310
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          316..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrrylfgias amflsvllvg tfhaeaqtpp ptpasalldq cknnsddvea laacqtilqd
       61 kaqtprtraa vygfagndal desqldlalv nfgnalaldp nsdlayagra nvefikgqyd
      121 qaitdaqkai klspnthpda ylvlgtladr ngdhdariay mtraidimps faaayagrgh
      181 gyldekkftq altdfskaia lqpalaaslk ssflivyier asdsmnlgry qagiedltka
      241 lqvdgtnarv lgdlgdaynv tqhyykavvv ltkditinpd ypfahtnrgi aylnigkfdq
      301 aladinkgie lgdtaattyf vrgevyqsls nktaalkdyq ksleltppds syrsniqkai
      361 nqfgq
//
LOCUS       WP_284945126             273 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Acidisoma
            cladoniae].
ACCESSION   WP_284945126
VERSION     WP_284945126.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..273
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28720
     Region          1..271
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mqigifaktf sgtsveailm avreagyavs qfnlscagla smpdavsekv lrkiraatka
       61 sgvslvalsg tynmihpdea vrarglrqlg vviaaashlg iplvtlctgt rdaedqwrhh
      121 qnnadpsawh dlvtemakal alaerfgvdl giepepsnvv tsaldarrli ddmasprlrv
      181 vldpanlfet ataeaaaalv rdaverlgar iamahakdra adgrlvpvgh givdfadfva
      241 rlrgvgfdgp lvthglsaee apsvarylra aat
//
LOCUS       WP_284945140             790 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-glucosidase [Acidisoma cladoniae].
ACCESSION   WP_284945140
VERSION     WP_284945140.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 790)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 790)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 790)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 790)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 790)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444957
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..790
                     /product="beta-glucosidase"
                     /EC_number="3.2.1.21"
                     /GO_function="GO:0008422 - beta-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0030245 - cellulose catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=85222
     Region          26..471
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          614..683
                     /region_name="Fn3-like"
                     /note="Fibronectin type III-like domain; pfam14310"
                     /db_xref="CDD:433860"
ORIGIN      
        1 mtgsaksdht aladnalaar sriaemtpqe ktdllsgfgm wktarlerfg vepivmtdgt
       61 ygvrysmsqi dgdqrggadl ddflaivaqr asdvaiawge mkpatcfpng samgcswdvp
      121 lmerlgellg recramgvhm llgpginirr iplagrsyey ysedplltgk lasavirglq
      181 dqgvgaslkh facnnseier ttmdsivder alreiylrgf eiavkdsdpw tvmssynrln
      241 gvqtsqdrwl lttvlrddwg yegvviadwn gikdraaslv agneldmpes prrkgdllaa
      301 leagdipkdv vdracarvle liarghagqa rpvtavdava hhaearamaa aamvllkneg
      361 vlpigpdvrr ilvvgrdaav pviqgsgcat ttptqvdqpi gelravlght vevllhpalt
      421 eetlalcsqv dlvivftste gaydgegsdr ttlalgpdqd dmiatlaatg armavviacp
      481 davvmpwaed vgaiittfya gqamggavad vlsgrvnpsg klsvsfprsl gdvpgfltyp
      541 gergrhvysd gihvgyrgyd qrgcaplfpf ghgltytqfr ysdlalsdta lgktgriqvs
      601 ftlentgdia gaevaqlylr akgvrlrrsp lelkgfakip lepgerrgiv ldlaghdltv
      661 wdpdrqdwvi eaeeaeivia assrdlrlaa plslrpsvls wprvqtdtqp vyvlgnpiar
      721 pilrqefaqw agiseadadk vlehcansfi gifptlerrl rmtvpedrar hilgrinaam
      781 daaeqslakp
//
LOCUS       WP_284945142             432 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Acidisoma cladoniae].
ACCESSION   WP_284945142
VERSION     WP_284945142.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..432
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46948
     Region          1..404
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mpteqidtlv vgagqagval sehltrsgvs hivlekdria erwrtgrwds laangpawhd
       61 rfpnmefpvt gpdgfapkde vatyfetyaq rfnapircgv avtrvtrlsg ragflvetsa
      121 glmeaqrvva atgpfqrpvi paliperegl qqlhssayyn paqladgavl vvgsgssgvq
      181 iaeeialagr rvylsvgphd rpprsyrgrd fvwwlgvlgk wdaapkargt ehvtiavsga
      241 rggetidfrn laakgitlvg rteactdgvl rfasdlaati argdanyltl ldeadayvar
      301 ngldlpeqpd arrflpdpdc vrdplrqldl aaaevgtviw atgyaldfsw lqvdafdeag
      361 lpmhqrgvap ergiyflglp wlsgrgssfi wgvwqdarhi aehiviqrsy ldyqpqvard
      421 llvtdslpgk tt
//
LOCUS       WP_284945185             323 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Acidisoma cladoniae].
ACCESSION   WP_284945185
VERSION     WP_284945185.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..323
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=33725
     Region          3..323
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(41..42,46,122,126,129,147,150..152,171..172,176,191,
                     214..215,236..240,261..264,311,313)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(134,229..230,243..248,256..263,266..267)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mthairihat ggpevlqweq vptpdpgpgq vliqhaavgl nfidvyfrsg lyktalpmtp
       61 gvegagtvig lgagvtdfke gdrvaysstp igayaerrvm padrlvhlpd sisftaaagm
      121 mmkgltsqyl lhrtykvapg dsvliyaaag gvglvlcqwa kllgaivigv vsteakaafa
      181 hahgadhvll vsddiparvr eitggamvpv vydsigkdtf ltsldclapl gmmvsygnas
      241 gpvppvelsl laakgslflt rpslatytak ratllaaadd lfrvvldgtv kievdqtfpl
      301 rdaaaahham esrkttgstv llp
//
LOCUS       WP_284945247             710 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Acidisoma cladoniae].
ACCESSION   WP_284945247
VERSION     WP_284945247.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 710)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 710)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..710
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73001
     Region          9..708
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mdqgildvsr qeigvsgmtc agcvrrvera iaavpgvrdv svnlateras vtsspgfdms
       61 avarallaag yaaqpigqpa pvtrdglaaa lalilaaplv lpmllgfswp awvqlilagv
      121 vqavfgarfy vsawkalrag tanmdtlval gttaafalsl welsagrhdh lyfeasaavi
      181 alvrlgkwle ararrqagga iraleqmrpe rarirrngre tevstaalrv gdvlvirage
      241 riaadatlre gsggndesll tgeslpvfkt pgsrliggam ngeallvadv taigaesqlt
      301 rmvrlvedaq sakppvqrlv drvsaifvpv viglaaltcl gwwldgagve vaiinavtvl
      361 viacpcalgl atpaaimvgt giaarhgili rdaaaleqaq airtvvfdkt gtltegrpal
      421 vellpapgtt edslrhlaas lqagsehpla ralrdtmtdl rpasglraip grgvegeveg
      481 rrlllgsgrl maerciaiga laedarrlea dgrtvsylae aegavlglla fgdalkpgaa
      541 eavaslrarg ltvvlltgdn agaarvaaaa lgiddvraea lpadkaaait dlrrngavam
      601 vgdgvndaaa laaadlglam atgtdvaaaa aaitlmrgdp mlvpaaldia artyrrirqg
      661 lfwafvynli giplaaagll spmvagaama fssvsvvgsa lllrrwkpga
//
LOCUS       WP_284945311             246 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Enterococcus
            faecalis].
ACCESSION   WP_284945311
VERSION     WP_284945311.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..246
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28833
     Region          2..140
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mayetfafvy devmdeslyq kwldfsnrhl pqgtqqilem acgtgalavd faksgydvta
       61 ldlseemlml aserafeeev pvqfvqgnml dlsevgqyqa itcfsdslcy manrqevqqv
      121 fdevyqalee egtfifdvhs tykidsvfpe ysyhyqteef aflwdsyage kehsiehflt
      181 ffvkeqetde hfvrydelhq ertysldnyl rmlesagfmn vkvyadftde aptetserwf
      241 fvcqrd
//
LOCUS       WP_284945312             287 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Acidisoma cladoniae].
ACCESSION   WP_284945312
VERSION     WP_284945312.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..287
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29891
     Region          6..287
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mtgwrdaagr ipvtlwlvaa mvsaqlaaal svplihrfgs amttevrllw aagflmlvar
       61 prlwglggpr llggialgvv tagmsffyfa aigriplgtv vsieflgplt valvgsrhgr
      121 digwavlaaf gvwlltrgaa vgvdllgyaf aaasavcwgg yilltrrvgk vftglqgvtl
      181 slsvaavigl pigivphlpd lrwtlvilma fialltpvlt yalemaslrr meprrfgilm
      241 slepatgavm gflvlgqrls lgqlggmacv mgaslgasla aspkkks
//
LOCUS       WP_284945508             250 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Acidisoma cladoniae].
ACCESSION   WP_284945508
VERSION     WP_284945508.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..250
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26722
     Region          22..249
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 msgetagrmd rgdgvalawr rlegngptiv flpgfrsdme gskavhlaaf aaargqamlr
       61 ldysghgasd grfedgtigv wtadalhvvd qltegplllv gssmggwigl nlalarpdrv
      121 vgfvgiaaap dftetliwat mdrhertrlm aegtiflasa ygdpvpitla liedgrkhlr
      181 lagpipllcp vrllhgqkds evpwrsaltl adrldspdtq illikdgdhr lscesdlgll
      241 edvvaralkv
//
LOCUS       WP_284945904             499 aa            linear   BCT 25-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Acidisoma cladoniae].
ACCESSION   WP_284945904
VERSION     WP_284945904.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..499
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=52889
     Region          19..499
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mlipdpktlm seaafrfvne shklligdrw ldaqsgatvd vidpgtgrvi akvpaadsad
       61 vdlavaaare afdngpwsrm tasargkliw qfadlieana rslaevesld tgralyecqi
      121 vdvpgsveml rymagwaski ngetmnvamp cdfhtytvre avgvvaiivp wnyplelavw
      181 rmapalaagc tiilkpaeqt plnairlgql aqecgfppgv invvtgyget agaalsahmd
      241 vdaisftgst etgrlivkaa agnmkrvfle lggkspaivf adadltaaip gvagsiffsa
      301 gqvctagsrl lvhasifdrv vagvaeiaat mtlghglaag tqlgplvssd qmdrvsgyld
      361 agrrdgvtiv tgghrvgteg yymqptvitn tsaqmsiyre evfgpvlcav pfddddmdrv
      421 aamandtvyg lhasiwtqnl rlahmmarkv kagnvcinth nffdpafpmg gykqsgwgra
      481 sgfqaiehyt evkgvvakl
//
LOCUS       WP_284946021              91 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Acidisoma cladoniae].
ACCESSION   WP_284946021
VERSION     WP_284946021.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 91)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..91
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9626
     Region          19..85
                     /region_name="AF2118"
                     /note="Predicted transcriptional regulator, contains an
                     XRE-type HTH domain (archaeal members contain CBS pair)
                     [Transcription]; COG3620"
                     /db_xref="CDD:442838"
ORIGIN      
        1 miiamnasgn gieiaispaq vraargllgw sqdrlvekse vpkrtlarfe leqgtaqkrt
       61 lsairaalea agvifveeng egpgvrlkkv d
//
LOCUS       WP_284946050             381 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Acidisoma cladoniae].
ACCESSION   WP_284946050
VERSION     WP_284946050.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..381
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41349
     Region          12..371
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 msepiaaass rparsrptig sleigrfvaa svvvidhlls digrhsavag tsilgglafp
       61 gaiavqfffv lsgfvmmtah hadfgraaal prfwwrricr iypaywitll ipihylyafl
      121 tpsylanlvs lwpvdvveyn ppawtlryev afylvfglcl lpkvgrplla lwvaavcwvw
      181 cppallsqvg lvppaaltrf athaasrfla pfefyffagl lggwivvarp vgrwaafgal
      241 tvgvaalaam lpathwghdf gspamavpgg lafaavilgl avlerhgvlr fgrmakrlga
      301 msyplyilha plllivtvht kgrtyglptl yvvallglvs iyalsaifaf gidqpiqrll
      361 rrlsaptrrr sivpvivgde r
//
LOCUS       WP_284946065             262 aa            linear   BCT 25-DEC-2024
DEFINITION  HesA/MoeB/ThiF family protein [Acidisoma cladoniae].
ACCESSION   WP_284946065
VERSION     WP_284946065.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..262
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27798
     Region          11..259
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mdgtdldldf teeevqrysr hillpevggi gqaqlrrarv livgagglgs plllylaagg
       61 vgtigivddd hvdlsnlqrq iahttaslnq sktasaataa rainplvtvv ehpfrlteae
      121 apdliagydi vcdgsdnftt rylvadaclr arrtlvsaav lrfegqlsvf kphlhpegpc
      181 yrclypeapp pgfapscaea gvlgavtgvm gtlqatetik eilgigesls grlllwdala
      241 trfrtirvpr dphcpacssp hv
//
LOCUS       WP_284946095             303 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Acidisoma
            cladoniae].
ACCESSION   WP_284946095
VERSION     WP_284946095.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..303
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32688
     Region          18..289
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mstiaianap vsfgafemtv gidpntpdge avldavsnag yvgidlgpvg yfgegevlar
       61 rlserklgla gaylelpfse peplrdmlpq ldalldalda vrdlgpfppr ptlgdfsdlg
      121 rrarpgqaak dhslgldetr fqrfvigves vtdrcrrrgy eptfhnetgt yieapweier
      181 mldrtsvnlc ldtghliigg gdpvaalrdw gprinhihik dakraaiadi vrdaapaeai
      241 wergafcalg hgdvdldevl rlihtsfsgw vvveqdilpd aggiakaaad qsanlrflqa
      301 rgf
//
LOCUS       WP_284946114             231 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Acidisoma cladoniae].
ACCESSION   WP_284946114
VERSION     WP_284946114.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 231)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..231
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25814
     Region          1..>208
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrptdrlfqi iqilrrsshp ktaaalagel gvstrtiyrd iadligqrvp iegeagfgyl
       61 lasdydmppl mltpneieaa vlgaqwvasr sdtvlahaar dlmakiaavi pahlrpfiae
      121 psvgtrpaig gpgdtidtsi frtairdsrk lrlryrsdtg qdserivwpa mlgyaethcl
      181 liawcelrhd frhfrldrii eaesledsng lrkgelrrry rlwretnagi s
//
LOCUS       WP_284946150              93 aa            linear   BCT 25-DEC-2024
DEFINITION  BolA family protein [Acidisoma cladoniae].
ACCESSION   WP_284946150
VERSION     WP_284946150.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..93
                     /product="BolA family protein"
                     /calculated_mol_wt=9680
     Region          1..88
                     /region_name="BolA"
                     /note="DNA-binding global transcriptional regulator BolA,
                     affects cell shape, cell division and biofilm formation
                     [Transcription, Signal transduction mechanisms]; COG0271"
                     /db_xref="CDD:440041"
ORIGIN      
        1 mtrsdritet ltrtfaplsl dvvddsgsha ghsgaavgge thfnvimaae cfegmtrvar
       61 aravndalad efaaglhala ltlrtpaera ktl
//
LOCUS       WP_284946215             316 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Acidisoma cladoniae].
ACCESSION   WP_284946215
VERSION     WP_284946215.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..316
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33065
     Region          4..303
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(37,250,253)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(190,221,248,251..252,255)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mtglilacge almdfipvet vggarayrpc pggssynvar algrlgvptg llaavsrdff
       61 gedliaglre sgvrtdflqr ldlpstlgfv sldrvepvya ffdtgaaers wqpapgdtlp
      121 aevtalhvgs ialvrepaga afaalalaea ggtrivsldp nirpelvrde acyrarlarl
      181 lavadiikis ahdldwlmpg vspddaassw fqgraalvvi trgaegvtgw trrariaaps
      241 iptemvdtvg agdsfmagll arlheagdlt padlprlsgs glrnalalgq tvasltcarq
      301 gadapwrkdl grqelv
//
LOCUS       WP_284946542             128 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Acidisoma cladoniae].
ACCESSION   WP_284946542
VERSION     WP_284946542.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..128
                     /product="YybH family protein"
                     /calculated_mol_wt=14328
     Region          11..127
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mdedwtavav atqkawkqaf etrdleslga lyadktafyg statfydtpd gvreyfrvlp
       61 psykrsdyav phivrlgpda maatgevnfy rqendgsmtl lpfrmthvlv rengawkiat
      121 hhasprpv
//
LOCUS       WP_284946548             280 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Acidisoma
            cladoniae].
ACCESSION   WP_284946548
VERSION     WP_284946548.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..280
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30408
     Region          32..270
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mmtklayhan cwgplggapv gvtsvkdlfy qtfgdmnpaf aeiaaagyea velfdgnlid
       61 larepgalrr qlamhglkll atysggnfiy pdileeefwr ieraaalaae agaihlvvgg
      121 gakrsggprd gdyerlgaal drvstvaesy glsahyhphl ttmaetpdei rrvfahtrig
      181 fcpdtahlaa aggdpaglva efwdrisyvh lkgwqrkpfa ftpidrgdld lratmhvlqt
      241 rnfdgwiave ldswpdpaeg arasmawlrd qadpfapqeg
//
LOCUS       WP_284946704             324 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Acidisoma cladoniae].
ACCESSION   WP_284946704
VERSION     WP_284946704.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..324
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=34206
     Region          1..290
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 maelcdayie daasgriltr rgvakkatti etdrsrisgh ikpligalkv pavsrddvea
       61 fmydiaagkg agkaktgkkr glsnirggkg aatrtlgllg aiftyavrnq lradnpvhgl
      121 lrfadgrrer rlseaeyaal gtaldlavea kiwppaiaaa rflvltgwrs geatglrwde
      181 vdvsrrtarl adtksgfsir plsedacail raqtkagdlv fpasrgkgkm sgfpsvweri
      241 iglggisaei tpnvlrhsfa slasdlgyse asiaalvghk rhsitsryvh aadaillaaa
      301 davaektvsl meeacgvspq sska
//
LOCUS       WP_284946728              51 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor, partial [Enterococcus
            faecalis].
ACCESSION   WP_284946728
VERSION     WP_284946728.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 51)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 51)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 51)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 51)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 51)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 51)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..51
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..>51
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          6..>51
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
ORIGIN      
        1 mdylglskim kaiaepnrlq ildmistgen cacdildnfd ftqptlshhm k
//
LOCUS       WP_284946836              44 aa            linear   BCT 25-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin, partial
            [Enterococcus faecalis].
ACCESSION   WP_284946836
VERSION     WP_284946836.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 44)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 44)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..44
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         <1..44
                     /product="type II toxin-antitoxin system RelE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0017148 - negative regulation of
                     translation [Evidence IEA]"
     Region          <1..44
                     /region_name="RelE"
                     /note="mRNA-degrading endonuclease RelE, toxin component
                     of the RelBE toxin-antitoxin system [Defense mechanisms];
                     COG2026"
                     /db_xref="CDD:441629"
ORIGIN      
        1 alsanragqw ryrignyrvi veiederlvv taiqvghrrn vydk
//
LOCUS       WP_284947054             304 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Acidisoma cladoniae].
ACCESSION   WP_284947054
VERSION     WP_284947054.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..304
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32851
     Region          1..192
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mrvavviaar dvapfigaav gsvlgqshtd ltltvvddgs rdetaplvaa fpdarlrlvr
       61 qtnhgtsatr nrgaldaget daflfldgdd wlapdavsrl vralrsdpaa vaahaafafv
      121 getatasapg pldrrrapra rdllprlvvg nvfangghvl iradawraag pfsttlsyge
      181 dwefwlrlal qgpfaaisgt palfvrrrag skmhggatlp qtyrpvleai rsnpriaarl
      241 gggrfarlcr raeaefawtm grellrrdrv reawaplcrg vfgrprplrl mllamvavkr
      301 lrkp
//
LOCUS       WP_284946959             516 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Acidisoma cladoniae].
ACCESSION   WP_284946959
VERSION     WP_284946959.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 516)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 516)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 516)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 516)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..516
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54555
     Region          1..511
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mrwtptrrpp aallaaglla gllvlvpivw tgglalgvgf sdarlllfrp lvaqlllntv
       61 aliaatalvt cvvatavawc vertdllgrr lwavlavvpl avpsfitsfa wvslsprlqd
      121 fggallvvsc syfpliylpv aaalramdpt leetaralgl gpwrvflrvv lphlrpallg
      181 gillvalntl tefgafallr frtftteifa iyrtsfdsse aalfgmvlil lcllclagea
      241 wargdarygr vargaarpap rialgvwhlp vfagfaalal vtlgvplgmi lywltqhtsa
      301 atsvagaslp alaratwasl rlalggtavt mllalplgfl atrydgrlia llertaylaq
      361 gvpgivvals mvsltitllr plyqsafllm ivyavlflpl alvsvraafg qvqrgledas
      421 raaglgwfat vwrvllplag pglgaaaamv fvsvvtelta tllmapigtr tlavqvwant
      481 ttlafaaaap yaalmtvlsl isawvlarrf glsrtp
//
LOCUS       WP_284947216             374 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Acidisoma cladoniae].
ACCESSION   WP_284947216
VERSION     WP_284947216.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..374
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41032
     Region          6..369
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtatgkvliv gcgiaglata wsllrrgfei emfeqgpipn pkqsswdehr itrhaygefe
       61 gyaalmpqaf rlwdqmwkdi gavhydptga vyfmrgdnpw yhgtstalik mnighrdisl
      121 araaarfpmf nldgvtrive tdgagmlfps riivdlinyl gsrgvtfhsy hqvsdidpea
      181 gtvtangtvf tgdrvvvsag awadrlvpsl rpeglpsrqa vmflappanv arawaespvm
      241 adigedtscy ilpplrgtrl kfgdhvftrr gdadedrtat dldvtrlmrv lklvlkdfdr
      301 yqilerkacf ytvtddehfi qraigakgwl isacsghgfk lapvtgelaa qaiagersan
      361 evtmiaagra lela
//
LOCUS       WP_284947295             415 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Acidisoma cladoniae].
ACCESSION   WP_284947295
VERSION     WP_284947295.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..415
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46647
     Region          108..>311
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mppfhsgtra ggkdlqdlrg larspfhafl rkvarpprpr vktatpeapa payrmiaafa
       61 ssqtwrwlae yvrhrfgprh pfqtyqghgs giyrlqgdeh gdevrvalag dwgtgtdeaa
      121 lvarqiegfr ahytihlgdv yymgdgreva enflgqpvqg shftpiawpl gsrgsfsllg
      181 nhemyargia yfrhilpslg emrngvsqgq qasffclend dwrvigidtg ydsvnwpfie
      241 silepdcalp pllidwlekt lkpseddarg iivlshhqyf safdhaypka atqlatffkr
      301 pvlwfwgheh rltiydkfsv kdgveafgrc ighagmpvdl apttpahpev pivfldervy
      361 hndehlhlgm ngfarltfrs kqllvdyvdl hgtciytetw taedaqllre dagpv
//
LOCUS       WP_284947354             222 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-L-isoaspartate O-methyltransferase family protein
            [Acidisoma cladoniae].
ACCESSION   WP_284947354
VERSION     WP_284947354.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Edwin,R.K., Challa,N., Sharma,R., Satyamoorthy,K., Parsa,K. and
            Misra,P.
  TITLE     PIMT/TGS1: An evolving metabolic molecular switch with conserved
            methyl transferase activity
  JOURNAL   Drug Discov Today 27 (8), 2386-2393 (2022)
   PUBMED   35462043
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Furuchi,T., Sakurako,K., Katane,M., Sekine,M. and Homma,H.
  TITLE     The role of protein L-isoaspartyl/D-aspartyl O-methyltransferase
            (PIMT) in intracellular signal transduction
  JOURNAL   Chem Biodivers 7 (6), 1337-1348 (2010)
   PUBMED   20564550
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Kagan,R.M., McFadden,H.J., McFadden,P.N., O'Connor,C. and Clarke,S.
  TITLE     Molecular phylogenetics of a protein repair methyltransferase
  JOURNAL   Comp Biochem Physiol B Biochem Mol Biol 117 (3), 379-385 (1997)
   PUBMED   9253175
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..222
                     /product="protein-L-isoaspartate O-methyltransferase
                     family protein"
                     /EC_number="2.1.1.77"
                     /GO_function="GO:0004719 - protein-L-isoaspartate
                     (D-aspartate) O-methyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0030091 - protein repair [Evidence IEA]"
                     /GO_process="GO:0036211 - protein modification process
                     [Evidence IEA]"
                     /calculated_mol_wt=23106
     Region          17..214
                     /region_name="Pcm"
                     /note="Protein-L-isoaspartate O-methyltransferase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2518"
                     /db_xref="CDD:442008"
ORIGIN      
        1 masttlpfaa arqmmadsql rpnkvtnpav lvamrdipre tflppalgal ayadqdvrlg
       61 ddrvlmspma farlaqliap vpgerilvvc ggtgygaavl arcgarvtvl dtdaglmdvg
      121 aaavralgls isfqkgdpeq glpgvepwda iliegaveti ppvfaaqlrp gqgrlvtvva
      181 ksghpgvavl aerqgtalat admfdctttv lpgfrkvief qf
//
LOCUS       WP_284947491             318 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Acidisoma
            cladoniae].
ACCESSION   WP_284947491
VERSION     WP_284947491.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..318
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=34543
     Region          2..292
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mhilltgssg wlgrflaprl raaghkvtgl dvapgpdtdi lgsvgdrnav drafeqgiea
       61 vihagalhkp divryppqaf idinvtgtln llaaakaagh drfvftstts lmvsqtirde
      121 sgeaaiwlde asgplvprni ygvtklaaeg lcrlyaaehg lscvvlrtar ffpedddthr
      181 mpsgenlkan eflnrrltve daadahival erapalgfet filsaptpfd radaselkrd
      241 asaviaryfp dapmlyakrg wtlpaslgrv ydwrhaerrl gfrcstgfae vlnalregra
      301 mpfahdpsyl spkeqiat
//
LOCUS       WP_284947534             559 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Acidisoma cladoniae].
ACCESSION   WP_284947534
VERSION     WP_284947534.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 559)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..559
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=60642
     Region          2..549
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 msrlslahfe rlvadtprav icadasltvt ywnaaaetlf gwraddavgr tiddlipgpl
       61 raaigaslar lraetgatfi setmelvseh pdgteisaev tlscwyeedg qpglwisard
      121 vtgkrdaetr llhlahndpl tglanraflt ealqraedtg vlvalillnl dgfshandal
      181 gheagdavlr evaarmklrl gdrgllvrlg gdefavlltd paasaapeai ahelqdslip
      241 kllflgdrvf nigasagiaa fhageagtll anadlalyra kglgrgmslt fepamradyd
      301 arqilerevr qateqgqftl fyqpqvrlpd raiisvealm rwrhptrgll tpaeflavle
      361 vsapsaevge wvideacrqa avwwatglsl rvavnvfpeq lrrgnldtvv eaalarhklp
      421 paaielelte rlvmtsadat laplwrlher gvaiafddfg tgfaslstlk rfpmtrlkid
      481 rsfvtnlgad pydaaiveav ltlgrslkld iiaegvetet qedylirhgc leaqgyrygr
      541 pmppeeigat agtvqyrgs
//
LOCUS       WP_284947592             114 aa            linear   BCT 25-DEC-2024
DEFINITION  HesB/IscA family protein [Acidisoma cladoniae].
ACCESSION   WP_284947592
VERSION     WP_284947592.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Lu,H.M., Li,J.D., Zhang,Y.D., Lu,X.L., Xu,C., Huang,Y. and
            Gribskov,M.
  TITLE     The Evolution History of Fe-S Cluster A-Type Assembly Protein
            Reveals Multiple Gene Duplication Events and Essential Protein
            Motifs
  JOURNAL   Genome Biol Evol 12 (3), 160-173 (2020)
   PUBMED   32108236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..114
                     /product="HesB/IscA family protein"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=11640
     Region          10..113
                     /region_name="IscA"
                     /note="Fe-S cluster assembly iron-binding protein IscA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0316"
                     /db_xref="CDD:440085"
ORIGIN      
        1 mstqtsnfgl tdraairise llgsqptpaa lrvavlaggc sgfqykfdld eappaaddfv
       61 ieqagarvlv dpssldllgg aqldytdalm gahfaiknpn atsscgcgts fsid
//
LOCUS       WP_284947702             359 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Acidisoma cladoniae].
ACCESSION   WP_284947702
VERSION     WP_284947702.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..359
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37277
     Region          10..341
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 madgtkgawn fgsdnvapis peimaaiaaa nsgnvgsyga daltaqvtak lrdifetdlv
       61 afpvatgtaa nalalsvlvp pygavlcaed ahistdecga pefftggakl vclptpdgri
      121 aaaqiaepla haaalgvhfm qpaaisitqs tewgavysrd elsalgaaaa ahrlplhmdg
      181 arfanalvhl gcspaemtwk agvkvlsfga tkngamaaea vvffdpalar gfeqrrkrga
      241 hlwskmryms aqlvayleqd lwlrnaraan glatrlaegl saipgvsllh pvqanelfvi
      301 mpegmvaall aegfgfyrws srvegdntvi rlvtsyasdp haaealiaaa arlgnqppg
//
LOCUS       WP_284948007             289 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Acidisoma cladoniae].
ACCESSION   WP_284948007
VERSION     WP_284948007.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..289
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=31262
     Region          39..270
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 msdgptvgee reedaaegsg dpiwddwstp prvaempmlh ldgfdgpmdl lldlaerqri
       61 dfgrmsirdl aeqfvasmer lvgrvslehr adwlvlatrl vllrsrllfp aspeaaiaae
      121 qdaaaevrrl eemvfvraaa awltarpqlg tdvfarpaat apsreggyva lmeaclvvlr
      181 grggrpdeap pyqpvipdlw rvtdalarir ltlaehpegg elsaflpais advanrdlra
      241 raavastlla glelaregvl aieqeedygp msfahrated aviggvapq
//
LOCUS       WP_284948085             337 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Acidisoma cladoniae].
ACCESSION   WP_284948085
VERSION     WP_284948085.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18605378
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..337
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=36273
     Region          <119..>190
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
     Region          130..285
                     /region_name="AdoMet_MTases"
                     /note="S-adenosylmethionine-dependent methyltransferases
                     (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes
                     that use S-adenosyl-L-methionine (SAM or AdoMet) as a
                     substrate for methyltransfer, creating the product
                     S-adenosyl-L-homocysteine (AdoHcy); cl17173"
                     /db_xref="CDD:473071"
ORIGIN      
        1 mdaplaaata spqlrilrde larllderde rstqtadlds hlpqspfyhy nasfdpleim
       61 rrhsvpglpp aqghltnflg vlidpkffpt ildgkagtve aipipanwha diaewgaalr
      121 avdlargtft vlelgcgwgc wminsgvaar ragldvhvig vegdaghiaf ateacatngf
      181 apnqitlrrg iaapengmal fprqgqagvs wglepifgat eeqrreaaas gnydelpmia
      241 lrelagarer fdlvhidiqg geadfiagcl pamndrvayl lvgthsrqle grimdtllpa
      301 gwileierpa ifalgadgpr itvdgvqgwr nprltia
//
LOCUS       WP_284948133             377 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Acidisoma cladoniae].
ACCESSION   WP_284948133
VERSION     WP_284948133.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..377
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38933
     Region          6..363
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtevfdiavi gagvmgataa lflarggmrv alidrggicq easgvnagtl tlhmtraali
       61 phamrgremw ldapnwlgmd vgarsapgls vaftaderdm lekraaarre agapitlita
      121 aqaaeielgv nptilaaayc aldghvtayl tgrayrqalt vagvtlfege aaagiaresg
      181 awavrvgagc vratrivlag gvwleemlsw lgltvpircl inqlvvterl gpvmrsvlgi
      241 angllslkqf engtvliggg wqgrgdvvrg gveaipdnli gnvrlarhtv palgkariar
      301 iwlgleseta dampaigplp gvpdafvvgc vhsgytsgpf mgrlladivl gvaesphafn
      361 parllaaags slqdsva
//
LOCUS       WP_284948210             300 aa            linear   BCT 25-DEC-2024
DEFINITION  amidohydrolase family protein [Acidisoma cladoniae].
ACCESSION   WP_284948210
VERSION     WP_284948210.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..300
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33622
     Region          5..300
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 maplpvidph fhlwdlesnv ypwlmqrplp asvagdvgpi ahsyrlkdyr aesarwqiia
       61 aihvdagfdp adpiaethwl qgiaeaehfp qgivaaaqld hpaiaevlaa qarfpnvrgi
      121 rhiinwhrdp aktyvqranl ltdplwnagf aqlrdyslsf dlqlypsqma eaanlaarhp
      181 etaiilnhag mpvdrdedgl aqwrggmkql aaqpnvsvki sglgmvdwhw ttetlrpfvl
      241 dtivifgprr cmfasnfpvd slysdfdtlf dafdtivadf tdaerralfa enarriyrlp
//
LOCUS       WP_284948189             332 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Acidisoma cladoniae].
ACCESSION   WP_284948189
VERSION     WP_284948189.1
KEYWORDS    RefSeq.
SOURCE      Acidisoma cladoniae
  ORGANISM  Acidisoma cladoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidisoma.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Acidisoma cladoniae"
                     /db_xref="taxon:3040935"
     Protein         1..332
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=34094
     Region          1..327
                     /region_name="Tdh"
                     /note="Threonine dehydrogenase or related Zn-dependent
                     dehydrogenase [Amino acid transport and metabolism,
                     General function prediction only]; COG1063"
                     /db_xref="CDD:440683"
ORIGIN      
        1 mravrlhavq dlrvedidap qppkpgevtl avtaagicgs dlhnfktgaw israpwvagh
       61 eftgtvsaig fgpshvsvgq rvivdsrcic gdcppcrdgf gqvcdrlgfl gevidggfae
      121 svtlparnvv aapdgvpdrh lamaeplava lhalrrltpt agaviaitgc gpigglvall
      181 asraghpvkv idrneqratr vaaatgaevi slailrtlrv ryavettgsh avllslvdsv
      241 vgcgcialvg iagsaavvdp vklverelsl lgshaftdad lndicamlpk ltdalepfva
      301 etislsdvpn ayvrhlagav dglksiilcg gg
//
LOCUS       WP_284949054             426 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Enterobacter roggenkampii].
ACCESSION   WP_284949054
VERSION     WP_284949054.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter roggenkampii
  ORGANISM  Enterobacter roggenkampii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Enterobacter roggenkampii"
                     /db_xref="taxon:1812935"
     Protein         1..426
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46962
     Region          26..393
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtehttsyya asanayepfp tlnesiscdv cvvgggytgl ssalhlaemg ydvvllegar
       61 igfgasgrng gqlvnsysrd idvieknygp daarmlgsmm feggeiirer iqryqiqcdy
      121 rpgglfvaln hkqletleeq kanwerygnt qlelldasai rrevdseryt galldrsggh
      181 ihplnlaige adairlnggq vyeqspvtai qhtspavvst qhgqvtaryv ivagnaylgd
      241 kiepdlakrs mpcgtqvvtt aplpeelart lipnnycved cnylldyyrl tadnrllygg
      301 gvvygardpd dverlvmpkl lktfpqlagv kidyrwtgnf lltlsrmpqf grldkniyym
      361 qgysghgvtc thlagrlise llrgdaerfd afanlphypf pggrslripf tamgaayysl
      421 rdrlgv
//
LOCUS       WP_284948371             376 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Enterobacter chengduensis].
ACCESSION   WP_284948371
VERSION     WP_284948371.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter chengduensis
  ORGANISM  Enterobacter chengduensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Enterobacter chengduensis"
                     /db_xref="taxon:2494701"
     Protein         1..376
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42995
     Region          93..354
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mpilelrfsn kslhqlphpl tgcqeyrdih cqnlralvyp nritlsfrat innqriyetl
       61 gqfpqlcved arqhvmklla dknrlavqsr rftveqaind lwlpdlqlyk kspqselskl
      121 nlyvrpfwgk rqlrditage iehyaaglre klrpstvnrn lailskicsl avragwiths
      181 pmthvrylke nniryrtlsa teiprfidaa talqtpaads illalytgmr igevctlkwe
      241 ywhpdmhqli lpdtksghpf tcplappaia vvecqqdlml sktyifpqlt dnarplaypr
      301 atfaricrda nidnlrmhdl rrtfatrvlq atgdiaiash llnhhsltat rryafhnaat
      361 shavvsqvie sydtkk
//
LOCUS       WP_284949118             455 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Enterobacter roggenkampii].
ACCESSION   WP_284949118
VERSION     WP_284949118.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter roggenkampii
  ORGANISM  Enterobacter roggenkampii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Enterobacter roggenkampii"
                     /db_xref="taxon:1812935"
     Protein         1..455
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49401
     Region          24..436
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,152,
                     155..156,159,268,271..272,275..277,280,307,311,360..361,
                     365,369,385,388..389,392..393,396)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mmnqntlsaf ldsskstrfh klllglctfi iifsgyelsv fgaivpvvir ewkispteig
       61 figssamfgm mfgaivlssl adkfgvkkll ivsififnff ivmatftesg lmfglcrfma
      121 gvgsggatpi visllteysp ktnkakmvav aicgnqvggm lapfvaihim peygwqpvlw
      181 lsvlplilip lfiklipesa rflaktqqse klnsilvrid ndyekklaat eqvliksddg
      241 nkpvekvsyl nlfskkyfvg tvfitliyic glltingvni wlpqvmnqng yalgssltfs
      301 ivlnlgtlig tilwavtvdk vgfkvlmpli yiagsvslfc mgvkvnlivm ylfvgligmf
      361 afaahslmns fasqyypgei rttgvglana tgrvggmlgp ivggmlltan vsitvwfltf
      421 aipgivaals mviinmhkky ierknivqdk vmlgg
//
LOCUS       WP_284949181             310 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Enterobacter
            hormaechei].
ACCESSION   WP_284949181
VERSION     WP_284949181.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..310
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=35682
     Region          4..303
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mikkqafkfl lepnkgqlsd flafagscrf vynkglalln enyrsgkkfi gynqlaselv
       61 ewkneeslsw lkeapsqclq qslrdldkaf rnfftgksqy pkfkkkgrhd sfrtpsqtvr
      121 vdqekklvsl pkvgwvkyrk sreiiaelkn vtismkqgkw yisfntehtv pdpihpsdik
      181 tkivlnnvns vhlssgiggd ntsqaeekkk lirlnkrlar rkkhsknwlk tkgkidrvks
      241 kaarlrldni hkattaicks havievvnlm gsvsdkndnt lsmryefvrq liykqewlgg
      301 evirreskpl
//
LOCUS       WP_284949529             636 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Enterobacter asburiae].
ACCESSION   WP_284949529
VERSION     WP_284949529.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Enterobacter asburiae"
                     /db_xref="taxon:61645"
     Protein         1..636
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=72238
     Region          14..636
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mrfpnqrlaq lfdllqnetl pqdelaqrls vstrtvradi talnallash gaqfilsrgn
       61 gyqlkiddaq ryqqlhashp ralriprtgp ervhylvvrf ltsafslkle dladewfvsr
      121 atlqsdmaev rewfhrynlt letrprhgmk lfgsemstra cltdllwela qqdslnplvt
      181 dvalnagvae qmvpvlheal trhhirltde gelflrlyca vsvrrisegy plpefhaedv
      241 eenvreaakd iavtiqqlag kalspseesw lcvhiaarqi qeiapsaina dddealvnyi
      301 lryinthyny nllsdaqlha dllthiktmi trvryqimip nplldnikqh ypmawdmtla
      361 avsswgkytp yviseneigf lvlhigvgle rhynigyqrq prvllvcdag namvrmieav
      421 lqrkypqiev artltlreye laetisevfv iatarvseks kpvvtiapfp tdyqleqigk
      481 lvlvdrtrpw mldkyfdaah friidkpvdq qtlfrelcaq legegfvgae fldsvverea
      541 ivstmlgdgi alphslglla qktvvytvla phgvqwgdet ahvifllais kseyeeamai
      601 ydifvtflre ramsrlcscs dfaefkavam eslsrf
//
LOCUS       WP_284949549             493 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Enterobacter bugandensis].
ACCESSION   WP_284949549
VERSION     WP_284949549.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter bugandensis
  ORGANISM  Enterobacter bugandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Enterobacter bugandensis"
                     /db_xref="taxon:881260"
     Protein         1..493
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53853
     Region          110..348
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 manlpwrisv rlaalakktg mvvgivlvvl lavrvylsqq gpdlhlwhtw rademsvrel
       61 dnanfagyva renaifaelg ravtaktage eqtplnryyr qslvwpgqft pdanrsfvlm
      121 pagkprgavv llhgltdspy svrhlaenyq rhgfvavvpr lpghgtapga ltdvdwemwl
      181 aatrlavrea trltgdnvpl hlvgysngga lamkyaldal dssalrrpqq villspmigv
      241 tafarfagfa glpallpafa kaawlnispe ynpykynsfp vnaarqswll tkalqeqigr
      301 aarenrlanl ppvlafqsvm dstvstravv tglfdqlpan gselvvfdin qaasfrplfk
      361 psswtatsal lpvaqrrysv tiitnadahs fstvakttpa gstretvvpl vqtwpqdvys
      421 lshiavpfpp dddlygrepg vknrygislg tialwgetsv lsvgkealmr vtsnpfydym
      481 leridsrigd gek
//
LOCUS       WP_284949654             223 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Enterobacter
            bugandensis].
ACCESSION   WP_284949654
VERSION     WP_284949654.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter bugandensis
  ORGANISM  Enterobacter bugandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Enterobacter bugandensis"
                     /db_xref="taxon:881260"
     Protein         1..223
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25720
     Region          10..194
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mlnilikesd llfqyglqvf ltdlfqrgfr eevqfsshfn hqgvsvadvv vlslcvgevf
       61 tcipelqsrk kgiviglvdd esreamtpsc fediilisrr asiskireii yfawyetqlp
      121 gyrwnknacl dchhkklspq qvrimasfyk glsvmeiahe lnisdktvft hkymlmqkfd
      181 lrtdyeliml lnrlaeknga pnffrdsldm dikeyevaas sar
//
LOCUS       WP_284949724             657 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Enterobacter bugandensis].
ACCESSION   WP_284949724
VERSION     WP_284949724.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter bugandensis
  ORGANISM  Enterobacter bugandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Enterobacter bugandensis"
                     /db_xref="taxon:881260"
     Protein         1..657
                     /product="PhoX family protein"
                     /calculated_mol_wt=71811
     Region          26..651
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mgrplksvfk kehrddianr sanpvfseva evflsrrrfl qmgavagaav sfpflikpei
       61 aiaavskpsa lakavslgft sidvstedtv rvpegyiarp fyrwgdptgi knnmpafkpd
      121 asnttdeqav qagmhhdgma wfslpqgeqn pehgllamnh eyidngmlft dgtanwsldk
      181 arkgqnamgv svvevkkags gwevvrpssf arritvntpm qltgparhqd lmktaadpqg
      241 ervlgtmqnc anghtpwgty ltceenwsdi fvkkadlnpl ekrygisdsd esyrwnevdd
      301 rfsvdktpne pnrfgwvvei dpydptstpr khtalgrfkh egaavtlaad nrvvvymgdd
      361 qkfeyiykfv sdkkydpanr eanmqlltsg tlyvarfned gsgdwlplif gqngldkskg
      421 fesqgdllik trlaadavga tkmdrpewia vdphasgsvy ctltnnsdrg kegkapvdaa
      481 nprannvfgh imhwhedgad paaarfkwdi lvmagrtdgd dskakgsmqg aafgspdgls
      541 fdhqgvlwiq tdvssstink kayegmgnnq mvatipgtne yrrfltgprg ceitgiaftp
      601 dnrtlfiniq hpgeggddit dpanpravsn wpdaspngrp rsstvvivka dggiigs
//
LOCUS       WP_284949745             248 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Enterobacter bugandensis].
ACCESSION   WP_284949745
VERSION     WP_284949745.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter bugandensis
  ORGANISM  Enterobacter bugandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Enterobacter bugandensis"
                     /db_xref="taxon:881260"
     Protein         1..248
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27216
     Region          11..141
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mdipriftvs esehrihnpf tpekyaalgr vlrmkpgarl ldlgsgsgem lctwardhgi
       61 tgtgidmspl ftaqatrrae vlgvservhf vhndaagyva deqcdvaacv gatwiaggva
      121 gtmdllaqsl kpggimlige pywrqvpate etaracgvss tadfltlpdl vasfdrqgyd
      181 lvemvladqe gwdryeaakw mtlrrwldqn pdddfaqevr teltaapkrh vaytreyigr
      241 gvfaliar
//
LOCUS       WP_284950170              70 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Enterobacter
            hormaechei].
ACCESSION   WP_284950170
VERSION     WP_284950170.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 70)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 70)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 70)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..70
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=8093
     Region          1..61
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 msqslirlse vqkrtgyska wiyrllkekr fpqsvkigsr siafveseve ewinqriear
       61 dalistkpql
//
LOCUS       WP_284950241             213 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Cutibacterium avidum].
ACCESSION   WP_284950241
VERSION     WP_284950241.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium avidum
  ORGANISM  Cutibacterium avidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Cutibacterium avidum"
                     /db_xref="taxon:33010"
     Protein         1..213
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=22744
     Region          3..200
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mttrfvlask sparlrmlrs agiepvvias gadesrlpge daatmtarlc rlkahsvigs
       61 galdehpadr tivvacdsvl nldgrvlgkp htadrarqww rrmrghqgvl vsghhiavie
      121 ngqireqtrv gqtvvtfadl tdaeidayas sgepakvaga ftidglggaf itringdphn
      181 vtgislplvr qmlmdldvew sslwngprgg hls
//
LOCUS       WP_284950257             574 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Cutibacterium
            avidum].
ACCESSION   WP_284950257
VERSION     WP_284950257.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium avidum
  ORGANISM  Cutibacterium avidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Cutibacterium avidum"
                     /db_xref="taxon:33010"
     Protein         1..574
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=60363
     Region          51..493
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 msspvsaile apipaplsld qaidkffspi attisdavfw aiplpggnef plilawllaa
       61 gvfftiylgf qqlrpasirh sshvvrghfs rhtdpgdvts fqalatelsg tvglgniagv
      121 aiaiatggpg asfwiavagl vgmsvkmsea tlgvkfrvvn edgttsggpm yylrdglasi
      181 dkpklgrvla tlfavctafg vigagnmfqs nqaayqlamf aggkdswigt hmwvvglvfa
      241 ilvgvvivgg askigaatsk ivpfmgilyv imclavigan itevgdafka iwsgaftghg
      301 iaggvlgvli vgvqraafsn aagvgtagia hsavktrrpa qegfvamwep fidsvvictm
      361 taitiiitgv ykdhdadgvq mtahalktva pwfsslltla vvlfafstml sysfygkkav
      421 gflfgnsata eriyngifll llvvgaatnm asilaladam lflmavpnvi gmyflarvva
      481 reikghrerv dagvipqvpe daqagmivan eatpeqleta deeyalraaa mdarseeldl
      541 ghtapdterd yldhlpedhe lfntmdrdgk plkd
//
LOCUS       WP_284950412             230 aa            linear   BCT 25-DEC-2024
DEFINITION  XRE family transcriptional regulator [Enterobacter hormaechei].
ACCESSION   WP_284950412
VERSION     WP_284950412.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..230
                     /product="XRE family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=25182
     Region          1..74
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          90..219
                     /region_name="COG2932"
                     /note="Phage repressor protein C, contains Cro/C1-type HTH
                     and peptisase s24 domains [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442176"
ORIGIN      
        1 mgfserlaqa mkhagytqgr lakdvgmaqs svnkllkean gsrktveias vlgvrpewls
       61 tgegemasss akeppalyqv kpslngiyrv dvldvkasag pgsivtsdfi etiraieytt
      121 eqaralfgnr paahvkvitv ngdsmdgtis pgdqifvdtg vthfdgdgvy vfvfgktlhv
      181 krlqmqrdrl avisdnpiye kwyvepeded afyvmakvll rqsvdykrfa
//
LOCUS       WP_284950419             747 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Cutibacterium avidum].
ACCESSION   WP_284950419
VERSION     WP_284950419.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium avidum
  ORGANISM  Cutibacterium avidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 747)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 747)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 747)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Cutibacterium avidum"
                     /db_xref="taxon:33010"
     Protein         1..747
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77791
     Region          20..743
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtavttdeqg ddepvlhppv qlqiggmtca acantiekrl aridgvhasv nfaseratvt
       61 gidvedaiaa vkdvgytaap lsdvdlavea erritmlrrr livavlltlp lmdiglvlal
      121 epqlrfpawd wllvvlslpv vfwsawpfhk atwsnlrhgm tsmdtlvslg vlssfgwsfv
      181 siligaqdee gywlgygitp agadtlyldv aagvtcflla gryfearakr sarsvltalg
      241 qlaarnarvl rdgvetlvpi eklhkgdlfv tlagetlaad geivegsssv dtsmmtgepm
      301 pvdttvgstv lggtmnltgr ivaratgvga hsqlaqmavm aeeaqarkan vqrlvdkvve
      361 ifvpavlavv vltffgwwia gagirhalsa alsvlviacp calglatpta lmvgvgrggq
      421 lgilikgpea leasgridtv vldktgtvtt gdmtlteria adgqdidrah ryaaaldqhs
      481 thpvakaiva avegtipecs splavagrgs egevdghdvm vgnpafltea gitipgeltd
      541 tvdqaastgr stilvaidgr asaalvisdt vkpevpavia qlkgmglrtv lltgdskaaa
      601 davasqlgtd evladvlpte kakvidelrg ggrvvamvgd gindaaalas sdlglamvtg
      661 tdiamrsadi icvrhhlgvv pdaiglsrrt lrtirgnlaw afvyniaaip iaaagllnpl
      721 isglamslss lfvvthslrl rnfgahs
//
LOCUS       WP_284950630             408 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase 5 family protein [Cutibacterium avidum].
ACCESSION   WP_284950630
VERSION     WP_284950630.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium avidum
  ORGANISM  Cutibacterium avidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Sharma,K., Dhillon,A. and Goyal,A.
  TITLE     Insights into Structure and Reaction Mechanism of &#946;-Mannanases
  JOURNAL   Curr Protein Pept Sci 19 (1), 34-47 (2018)
   PUBMED   27739373
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Ketudat Cairns,J.R. and Esen,A.
  TITLE     beta-Glucosidases
  JOURNAL   Cell Mol Life Sci 67 (20), 3389-3405 (2010)
   PUBMED   20490603
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467628
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Cutibacterium avidum"
                     /db_xref="taxon:33010"
     Protein         1..408
                     /product="glycoside hydrolase 5 family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45622
     Region          1..333
                     /region_name="COG3934"
                     /note="Endo-1,4-beta-mannosidase [Carbohydrate transport
                     and metabolism]"
                     /db_xref="CDD:443135"
ORIGIN      
        1 mrigvnhtps qgwfhswldl didaarrdfe aiarlgldhv rifplwpllq pnrglvrpra
       61 lddvvsivra agefdlevtv dalnghlssy dflpswvvtw hesnlftdpl vkagqtelis
      121 qlatrlreep nvtgmtvgne fpqyaalapg hhhptrsgct vdeaqtwlet mlgtmrdqwp
      181 dgrfwfgfdd dlwfvddhpf tprhavtlgs sttihswvfa qvgphfgeeh paltwfpryl
      241 lelarawspd phrplwlqei gaprshvpdd raadfvtssl asvattpsle avtwwcshdv
      301 sdqlldfpkl eyslglftnd gkpkpealam sdmlpdlhna qpqeqadepl efsadwatga
      361 grsvsfpmgd lfarwvdeak qtgraprlvf hpthgltgre alagalar
//
LOCUS       WP_284950442             339 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Cutibacterium avidum].
ACCESSION   WP_284950442
VERSION     WP_284950442.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium avidum
  ORGANISM  Cutibacterium avidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Cutibacterium avidum"
                     /db_xref="taxon:33010"
     Protein         1..339
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34620
     Region          26..332
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mpagpvllvl avalalsvvl slafstirlp veqawhvldv hvrggaveat adqivwglrl
       61 prtvlavvag aglsvggavm qtlvrnplad pymlgvsaga svgatavitt gtlaafgvys
      121 lylgallgal vataavfgia maqgglsplr lvltgvvmss afsamssflv fhsndpksaq
      181 svlfwllgsv agaswqtlvp tavvvlvtll llmigsrwld alaagpelas slgvpvtglr
      241 valfivqail vsaivavsgg igfvglviph ltrllvgprh rvvlpvsalf galflvwvdv
      301 lsrvasrpqe tplsivtgll gapvfllllg rrhyqyaga
//
LOCUS       WP_284950711             448 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Cutibacterium avidum].
ACCESSION   WP_284950711
VERSION     WP_284950711.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium avidum
  ORGANISM  Cutibacterium avidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Cutibacterium avidum"
                     /db_xref="taxon:33010"
     Protein         1..448
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47695
     Region          1..431
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mydsiiigag lagltaaeel asaghsvvvl earsrvggrl enaelsngqv ielggqwvge
       61 gheelrslia sqglelvdst egdvvvkarg rvshvtnsss sahtlspfel sdlgqgllrf
      121 rrladrvann kgwttangtw lnqslsqwvv snvrtdagre yitnlfrraf gvspddttll
      181 dgltkansgv dleslvavng glkqqrvkgg vaqvarnlae rlgddiklsc pvrsihaddd
      241 tvtvatsvgt eyqgrsvivt vpprllkeie fdpalpaerl emaekvpagn vikaylvyds
      301 pwwrtsgasg qmgadegavr vifdtsddet grgvlmgffe gteasgygkl svslrqrafe
      361 evvesafgea prsaieyldr dwlsepytgg chgahfapsl wtatgpilaq plgrvlfaga
      421 eyassfngym egalragara aqeavdll
//
LOCUS       WP_284950791             635 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Cutibacterium avidum].
ACCESSION   WP_284950791
VERSION     WP_284950791.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium avidum
  ORGANISM  Cutibacterium avidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Cutibacterium avidum"
                     /db_xref="taxon:33010"
     Protein         1..635
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69588
     Region          18..622
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mrrtsdeesl alqhkliass aknfaamldr qadahpnria fltpsgadde pnawlpmtfa
       61 efrrqaheva aglmelglpr egrvallsgt rtewiiadma issaggattt iypnsgpdea
      121 sfiladsess ilfvdstaqv akiqgrpevd avvrhiisfa ddseetgvrd drlttmaeii
      181 angrrrlave pdlvrrmids vepddlctli ytsgttgtpk gvelthrawt ymgqawknld
      241 mfrggdvhml wlplshafgk cliaicveig itqavepris rlarslgevk prvmcgvpri
      301 fekiragvmt aypqgrlasr vsrwafatgr daqryrnagd rvptvleakr kiadalvfst
      361 lrrklggief micggaklse qvrqwfssag ipiiegygat evgavaffsg pdairpgtvg
      421 pvapgclari aedgeilvsg pivargyhsm pektakaftd gwfhtgdige ldemnylrit
      481 drkrdlfkts ggkyvapqkv eatlmancpy lsnavvlgeg hkyavalltl ekgalmtwgr
      541 rhgrpdasya eltadpdvrr siqryvdran srlerwetvk kfaildhelt edshsvttsl
      601 kvrrgvvaek ysdivdemfa deneqssvar gddas
//
LOCUS       WP_284950827             644 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Cutibacterium avidum].
ACCESSION   WP_284950827
VERSION     WP_284950827.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium avidum
  ORGANISM  Cutibacterium avidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Cutibacterium avidum"
                     /db_xref="taxon:33010"
     Protein         1..644
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=71128
     Region          32..630
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mtssthrfhk aeldpagell gqpipgeslv enhlahmfrd tvanhgfrpa trvrqdgqwi
       61 lrtyaetgrr vaglarafvt pgvltedglq rgdrislfag ncpewieadl agmtigvvpv
      121 piyptstpdq ivhivtdagv raivtagpke ldrileargq mpcletvvli dpadrvgdhd
      181 gltvlsleqv rqagaseemq pvveermrqs caddvaaliy tsgttgepkg vmishraala
      241 elqaldaffd ftpadhslsf lplshalewg wsmvvirhgc lntfvpnpkt isemlaevrp
      301 tlfvsvpkly eqvmkvarek vadspaklki fewslavgre wwqtkqdgrr psvslearhk
      361 vadrlvlkai rdavggpktv laaggaplrk eveeffaacg llvcqgyglt easplvsfns
      421 pggckfgtag rplvgsrmst tddgeilyrg pnimkgywka peetaaaied gwlhtgdigy
      481 idddgflvit drlkdiivtl ngknispqpi enslmkdplf ehavllgdnr pcltllvkps
      541 lpqveeiaer lhissmtgpe mlrseelaee irrrvaeite klphqeqird lrvlwdeftm
      601 dnglltptlk vrrrevekrf teiveemysr iavrrkagke nskd
//
LOCUS       WP_284950878             216 aa            linear   BCT 25-DEC-2024
DEFINITION  IMPACT family protein [Cutibacterium avidum].
ACCESSION   WP_284950878
VERSION     WP_284950878.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium avidum
  ORGANISM  Cutibacterium avidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Park,F., Gajiwala,K., Eroshkina,G., Furlong,E., He,D.,
            Batiyenko,Y., Romero,R., Christopher,J., Badger,J., Hendle,J.,
            Lin,J., Peat,T. and Buchanan,S.
  TITLE     Crystal structure of YIGZ, a conserved hypothetical protein from
            Escherichia coli k12 with a novel fold
  JOURNAL   Proteins 55 (3), 775-777 (2004)
   PUBMED   15103642
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Okamura,K., Hagiwara-Takeuchi,Y., Li,T., Vu,T.H., Hirai,M.,
            Hattori,M., Sakaki,Y., Hoffman,A.R. and Ito,T.
  TITLE     Comparative genome analysis of the mouse imprinted gene impact and
            its nonimprinted human homolog IMPACT: toward the structural basis
            for species-specific imprinting
  JOURNAL   Genome Res 10 (12), 1878-1889 (2000)
   PUBMED   11116084
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Cutibacterium avidum"
                     /db_xref="taxon:33010"
     Protein         1..216
                     /product="IMPACT family protein"
                     /calculated_mol_wt=23342
     Region          1..205
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 mneyivltdp veaeleikrs ifrtklvrve teeeardvia qarrdghdar hhvsafvigp
       61 drhaqrcsdd gepagtagvp tlkaltasns ddqphlsdvv avtsrwfggi klgaggltra
      121 ygnavtkvld saslhrrvlm dtfttlldlr qagheegvir aaghevvtvd ytadgalltl
      181 acragqadhl avelaellgr dvdltpraqr wvdlth
//
LOCUS       WP_284951361             358 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Cytobacillus oceanisediminis].
ACCESSION   WP_284951361
VERSION     WP_284951361.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus oceanisediminis
  ORGANISM  Cytobacillus oceanisediminis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Cytobacillus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Cytobacillus oceanisediminis"
                     /db_xref="taxon:665099"
     Protein         1..358
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42232
     Region          36..340
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mgnkhlftvv nnkqemslst yedsrefqak lmglweqqqr vlgyteetia lgtkclnefl
       61 disnkfiwev tmedadsfyl glvgrglays trrkyqstis tfldylktrh aheiweryki
      121 qvpnlldkfn ryyhrkddyd gqvipprpei lerfwhgmke emkrarkynt vardyalfrm
      181 meltglrthe iimmdvkdcr fdlgekgkvh vrfgkgskgs gfkrrwvpml ddvdlllkwy
      241 lktvrplfts ddegplflse nrerlnkhta rkslgrrqkk lgftdaevfs phqlrhsfat
      301 rqtelgvdll tlkellghad vattfnysnp gsdhvekrvr maqekwrkhl lnfdkege
//
LOCUS       WP_284951391             198 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Cytobacillus
            oceanisediminis].
ACCESSION   WP_284951391
VERSION     WP_284951391.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus oceanisediminis
  ORGANISM  Cytobacillus oceanisediminis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Cytobacillus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Cytobacillus oceanisediminis"
                     /db_xref="taxon:665099"
     Protein         1..198
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22387
     Region          22..137
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 manlweekfs aegylygeep nefirehawr leghkrvaal aegegrnavf larkghevta
       61 wdytqsglik tqqlaerhhv rvetgqknli hdsvpsgeyd asimvfghfl kkdqktvfdk
      121 lvsvvkpggi vmlevysedq llygtggpks vdmvydpedl lqwiksykvl hffygeqerv
      181 egkghtgtgh viqailqk
//
LOCUS       WP_284951438             336 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Cytobacillus
            oceanisediminis].
ACCESSION   WP_284951438
VERSION     WP_284951438.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus oceanisediminis
  ORGANISM  Cytobacillus oceanisediminis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Cytobacillus.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Cytobacillus oceanisediminis"
                     /db_xref="taxon:665099"
     Protein         1..336
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34763
     Region          32..332
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtkdaqpfip fiyklaagfv ifagmfvaac vfgaadvtvk dvwlaltsna sgekisiire
       61 irlpreiaav fvgaalsisg aimqgmtrnp ladpgllglt aganaalalt lvvipsanyi
      121 gilfacfiga avgaslvfgi gamkkggfsp irivlagaav saflfaiaeg vgiyfkiskd
      181 vsmwtaggii gtswsqlqvi vpvisigilv slflskqlti lslneevavg lgqnttqikt
      241 ilfilvtlla gasvalvgnm afiglmvphi vraivgtdyr filpmsaltg asfmlladtl
      301 grtinapyet paaafiavmg lpfflfivhk ggkafs
//
LOCUS       WP_284951558             320 aa            linear   BCT 25-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Cytobacillus oceanisediminis].
ACCESSION   WP_284951558
VERSION     WP_284951558.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus oceanisediminis
  ORGANISM  Cytobacillus oceanisediminis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Cytobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Cytobacillus oceanisediminis"
                     /db_xref="taxon:665099"
     Protein         1..320
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=35268
     Region          3..312
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(9..10,12,53..55,75,103..104,107..108,110..111,114,
                     118,120,128,130,132,134..140,142..146,164..165,168..169,
                     267..268,276,282..288,290..293,295)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(54,76..78,101,238,286,289)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240626"
     Site            order(77..78,105,154..158,176..178,181,208..210,214..215,
                     236..238,262..263,286,288..289)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 mkpyvfisrk lpenviailk ekytvemwdr edvpvpydvf lqearkadal ltmlsepvne
       61 evlgaggklk iianmavgyd nvdvetakrl gitvtntpev lndstadltf alvlaaarrm
      121 veaaefvkkg nwkswsplll agqdvhhkti givgmgnigk tvakraagfd meilyhnrsr
      181 kpdaeqelga qyvsfdelle rsdfvvcltp lteetrnlfn rnafqkmkgk avfvnasrgp
      241 vvnehdlyea lkageiaaag ldvfaeepig edhpllelkn vvamphigsa sietryammq
      301 lcvenidlvl sgkkpktpve
//
LOCUS       WP_284951499              98 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Cytobacillus
            oceanisediminis].
ACCESSION   WP_284951499
VERSION     WP_284951499.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus oceanisediminis
  ORGANISM  Cytobacillus oceanisediminis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Cytobacillus.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 98)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Cytobacillus oceanisediminis"
                     /db_xref="taxon:665099"
     Protein         1..98
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11268
     Region          28..>73
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(32,36,61)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(35,60)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(42..43,54,57,61..62)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mmiatilidf ddvkneqere temkvhwgef vknmrmaagl skakfaeklg vspnsikqye
       61 kaqafprhae dlelkirevv kleiqrkrsk ivqlqlav
//
LOCUS       WP_284951818             688 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Dialister micraerophilus].
ACCESSION   WP_284951818
VERSION     WP_284951818.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 688)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 688)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..688
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=79098
     Region          1..534
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 milkkmkvkn frllknfeln fkdelslvig knncgktssi ivldkmlnss klfwedinle
       61 cqkdlykkii gfditkldev qlletinmql fieyndndsy eniqkfmmdl npdnniivle
      121 fisliaakki ielknimsek niedfksfsk fmsknfgnff etkkysrgfd veankitqdr
      181 seeidnkdiq kvikvagira dravsnddrn hvlsgltgky fssykaakde sesvftrlee
      241 kleeadkely kiyngeksea gepidgifsd vidviktygg aengidiaie ssiseknlls
      301 dntnlsyrqg gdcslpetyn glgylnligi lfeietniqe lfeqpadinl lyieepeaht
      361 hpqlqyifir nikshikahr nkllkeknkq lqilitshss hivsecnfdd iiylkkngnt
      421 viaksfnslk eeyggdeqkg fkfvkqyltm nrselfftdk aiciegdter ilmpmmmhki
      481 dnkekpkadl ipllsqnisi ievgahshif iplfeflgik vliitdidaa tknnngryvk
      541 shpqeakyts nasikdffkd tcldesnnef eellkktped kiknniriay qipetdgeyq
      601 assfedafia lnkdfilknk eglceygalk dfsndeieng dyynfalnnv kkksafassl
      661 lyfddengee dekwvvphyi eegllwir
//
LOCUS       WP_284951976             299 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase [Dialister micraerophilus].
ACCESSION   WP_284951976
VERSION     WP_284951976.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..299
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=35060
     Region          35..281
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mdktisifii serlnkvnna ksekkykdkp ikielyndnf qnykrynipk aqlviadipy
       61 rleekayass pkwykngdns ngeskfanks ffktdeifri aeymhfcskl likepkergk
      121 apamivfcsf eqipivveyg kkygfahnyp iffiknysaq vlkanmkivg avehavvlyr
      181 dklpkfnntd engdrhmifn yfmwkrdnqk iypkihptqk pvnilkklie iftdekdvvi
      241 dpvagsgstl racmelnrsc ygfevekefy rsakekmlnv kindnlfske fkhenrtii
//
LOCUS       WP_284952415             382 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Dialister
            micraerophilus].
ACCESSION   WP_284952415
VERSION     WP_284952415.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..382
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42292
     Region          5..382
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mnkrkkilia vligsltfss smysvfaddl enelstiqsq idesrstqas wqsiieevst
       61 klraiqaeld satqklkdie kqknqineqi kqteneiqka qnelvkrqni lnkrvraiym
      121 ngqlsylevi vgsknfsdfa nrvellkrii radfnlikdi qqkkagieak kfelelkhne
      181 leklaqeakk ttdeiakkks eqqdvlneak thkdaaqqle ndllarseqv reminervrq
      241 rqtqsqqsgg sytqgtgals wpcngpitsp fgyrvhpifg ttiyhsgidi gvdygtpiha
      301 adsgtviyag widgygntvi idhgnnittl yghnsslavs dgqsvskgtv iayagstgns
      361 tgphchfevq vggsavdpmg yl
//
LOCUS       WP_284952502             284 aa            linear   BCT 25-DEC-2024
DEFINITION  thioredoxin family protein [Enterobacter hormaechei].
ACCESSION   WP_284952502
VERSION     WP_284952502.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..284
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31602
     Region          5..110
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
     Region          114..143
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          127..190
                     /region_name="TPR_19"
                     /note="Tetratricopeptide repeat; pfam14559"
                     /db_xref="CDD:434038"
     Region          148..175
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          195..284
                     /region_name="TPR_20"
                     /note="Tetratricopeptide repeat; pfam14561"
                     /db_xref="CDD:434039"
     Region          215..246
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          251..283
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
ORIGIN      
        1 msvqnivnit eanlqqtfeq smtkpvlfyf wsersqhclq ltpvleslaa qyngqfilak
       61 ldcdaepmva sqfglraipt vylfqngqpv dgfqgpqpee airalldkvl preeelkaqe
      121 amalmqegky dealpllkda wqlsnqnsqi glllaetqia lhrpedaeav lktvpmqdqd
      181 tryqglvaqi dllkqaadtp eiqqlqqqva dnpqdaalas qlalqlhqvg rneealellf
      241 shlqkdlgaa dgqarkmfqe ilaalgtgda laskyrrqly ally
//
LOCUS       WP_284952570             477 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Enterobacter
            hormaechei].
ACCESSION   WP_284952570
VERSION     WP_284952570.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..477
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51088
     Region          1..449
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mpdffffine vlwgsimiyl lsgagiwftw rsgliqfryi rkfgrslkns vtpqpgglts
       61 fqalctslaa rvgsgnlagv alaigaggpg avfwmwvtai igmatsfaec slaqlykekd
      121 gkgqfrggpa wymarglgmr wmgvlfsifl liayglifnt vqanpvahal rfafncpewl
      181 tggalalltl ltivtglkgv arlmqwlvpl mallwvstsl mvcaihidev pnvivtifqs
      241 afgwreaasg algytlsqal tagfqrgmfs neagmgstpn aaaaaaswpp hpaaqgivqm
      301 igvftdtivi csasamimll agaaeqpsgs tagihwvqqa lvslvggwga glvalvvglf
      361 afssiavnyi yaennliflk vdsrlarnil ragvlamvfv gcllsmpmiw qitdvimalm
      421 aitnltaill lspvvaliar dylrqrklgv qpvfdasryp eiesqiapgt wddlprq
//
LOCUS       WP_284952711            2789 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Enterobacter cloacae].
ACCESSION   WP_284952711
VERSION     WP_284952711.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2789
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..2789
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=271171
     Region          5..1635
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          930..2643
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mpapnditvs sgsaisgdns qnwlvtiddg atvnggsygl nlgsasqgtv lnlsgdvttt
       61 gggsggnaag vklnnggtln ilstgsidsn sdgifltsgg tvnnsgvvsg adggtsvyfs
      121 ngtgsyvgds tssigggygi ivdsgtstis nagkidllhn gvwfrgsssg svdnqaggii
      181 nststsnygi disasgtvti snegsitgnt gillgtsght ltnsgiiigs ggtaisltgn
      241 nnavtldtgs nitgnitatg tgntltlngq gtlssnvtgv qsitvaadvg qswilsgsst
      301 ttgitnqaly vqsgtlilng aldnggtggg ttingdavlq lgnnsasgsv tgnivdngtl
      361 rfsrsddisf anfisgsgrv nqagsgqttl tsantytggt vvdagtlnas dvdalgtgnv
      421 tinnagtldl sftgdvftnt itnngvldvi aadnsldgni sgtgenrvsa lnttfngdns
      481 gfsglwnils sgsmfakttq nlgegavqla gilnvvpvtg gflfsnaltg agilkvelts
      541 gnafnfassv gnlftgtlem gsgtfsldgd ntlaltnatl qldlggtttv gaaqqnvgnl
      601 tlnggilrfp dlpagtintg qlnmlsgtir vdpdaivdts nllkaddgag vqlvtstsnt
      661 gaasalslqd ltgntlttse anvtqggntv avatygdfgl tesgglavgy tlsqldiqag
      721 qtlilsgdas tpsgaadmka llsgsgnlav natdaitltn agntytgttt vtggtlraga
      781 lnviddssqv tlnsgttfdl ngfdqsvnnl sgagnvtlga ntltentagt vtyggvisgt
      841 gavtaagtgt wiltgdnnwt ggttidsgvl qlgsggttgg itgditnngs lvvnrssalt
      901 lggaidgtgt ltqsgtgett lsgansysgg ttvsagtlna asatalgtgd atvgsgatld
      961 lsftggtltn nianagllav tganatlsgs itgagenris alnttlsgdn tlftgnwnit
     1021 ngasanvtgg qnlgdaavnl dgtlniapas ggytftnalt ggglmtatvt ggnafafdgt
     1081 vgsaftgtlq lgqgtfalsg vntttltnat lqldggnttt vgsgtqtpgn ltlnggtlrf
     1141 anlasgviat gqlgltsgtv qidptqvass ggsllteddg sglqlitats tsgaasnltl
     1201 tdlsggalss slvnidqnga tvaigtygys lnntnglgvg ytlnqldlqs gqtltlsgdt
     1261 atpagasdmk alisgsgnla idatnaltlt nagntytgtt tvtggtlrag alnviddssq
     1321 vtlnngttfd lngfnqsvnn ltgtgnvtlg astltenttg svtyggaigg tgsvttagtg
     1381 twiltgnnaw tggttlgggv lqlgaggtsg sivgnvvnna glvinrsddv tlagaisgsg
     1441 tltqnstatg tttltgtnsy tgattvqqgt lqlgnggttg slagtsaitl dsgaalafnr
     1501 snamtvanai tgdgrvtqvg sgttvmsgts aytggttvaa gtlnaanssa lgsgvatvds
     1561 gaslllsfsn gtfanavang gllnvtgagn alnstltgag enrisalntt lggdntlftg
     1621 nwniisggea nvaggenlgn aavnldgtln iapasgnytf tntltgsglm taalasgssf
     1681 afdntvgiay tgtlrlgqsl fnlagdntaa ltnatlqldn nsettvgagt qtignlting
     1741 galvfngevp pgqpdgavav gdltlnsgei rteaptagip npaptgqnlm eeddrailsr
     1801 lvsasgtvtg tannltltdh dgnvisdpqq faiteggtav anatynyals tgtsndglyi
     1861 qyglttldll saqtlhltsd agatgaaatl saqvtgvgnl dvdasaaggq tvtlnnnsnn
     1921 ytgttsvsgg tlrlgsnqal gntslltint gananingmt qtigalagdg glainggnlt
     1981 isnggtfggv tsgalgnltl tggtltltga ntftglttin sgavmqvgag gttgsvagpi
     2041 adngtlsfnr sdnvaltgav sgsgelhqdg agtlfinssv gvtgpvvins gtvsigdgtt
     2101 dgsvagnivn nsalqfnrsd wryggvisga gtveqvsgsq ttltaantys gattvsagtl
     2161 naanvaalgt saatvnsgat lalsfangtf gnavdnngvl nisgagntlt tditgtgtnr
     2221 isalqttiag dnsgfngswd itgsggvtvt aqenlggspv qlngilnvsp asggftfina
     2281 ltgngllaat lgsisdafnf aatagnafng ivalrrgtma legdntsala natlslgiga
     2341 iatlnsdqti gnltfnggll dvamstpssa niltvnnlnv dsavtppdvg vvnlqttslp
     2401 pgtkpdgnfl dqdnevdngi qlvkattvss egthltllld gaapadetdq vsdgfghddv
     2461 latygytavm taganapggp glyagymlkv lnsqstavid ttgatdstlg aqltgvgdfe
     2521 frandgtltl antandyqgn tqvtsgtlll ggnntlgqtr alniadgatt nlngfsqsig
     2581 alngaagstl alnggvltvt nggqsdgalt gggnlnltgg elivtnanda ltatvdidsg
     2641 atarlknaag lgsgavtldg tlvldtvkgs lanavqgaga mnlvnssdvi lagnnadfsg
     2701 dinigtanrl taqqpaslgt stlinngelv lnasdnwafa ntmggsgllt kagagrvtla
     2761 sdyahtggth vesgtlaldn rarwgrhgg
//
LOCUS       WP_284953288            1655 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Enterobacter cloacae].
ACCESSION   WP_284953288
VERSION     WP_284953288.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 1655)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1655)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1655)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1655)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1655
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..1655
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=180531
     Region          44..1655
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mkpfrlaals lallttftlv gcdnsddkpq aaapaastat tpkaaekpda dklaklaaqs
       61 egkaltllda sevqldgaat lvltfsvpln pdqdfsktvh vvdkksgkvd gawelapnlk
      121 elrlrhlepn rnlvvtverd lqalnkatfg idyekalttr dveptvgfas rgsllpgkvv
      181 eglpvmalnv nnvdvnfyrv kpeslasfvs qweyrnsltn wesdnllkma elvytgrfdl
      241 nparntrekl llplkdikpl qqsgvyiavm nqaghynysn aatlftlsdi glsahryhnr
      301 ldhnrldift qslengaaqs gvtvtllndk gqtlaeansd adghakletd keaalilask
      361 dgqttlldlk lpaldlaefd iagspgyskq ffmfgprdly rpgetvilng llrdsdgkpl
      421 paqpvkldvl rpdgqvartv vvqpenglyr fnypldsgaq tgmwhirant gdnqqrlwdf
      481 hvedfmperm alnlsgqkmp vspqdnvdfn vvgyylygap angnalqgql flrplreavp
      541 alpgfqfgdi aednlsrsld evqltldeqg rgqvstesqw kevhsplqli lqasllesgg
      601 rpvtrraeqa iwpaaelpgi rpqfaskavy dyrtdttvnq pivdengnas fdivyadasg
      661 akkavsgvqv rlirerrdyy wnwsesdgwq sqfdqkdlie geqeltlkad etgkvtfpve
      721 wgsyrlevka pddmvssvrf wagyswqdns dgtgaarpdr vtlkldkpsy qpgdtiqlhi
      781 aapaagkgya miessegplw wkeidvpang ldlsipvdka wkrhdlylst lvvrpgdksk
      841 satpkravgl lhlpmgdenr rlnialdnpq kmrpnqtlsv kvkasvkegp vpqkvnvlvs
      901 avdsgvlnit dyvtpdpwqa ffgqkrygad iydiygqvie gqgrmaalrf ggdgdelkrg
      961 gkppvnhvti iaqqaqpvtl dangegsitl pigdfngelr lmaqawteed fgsseskviv
     1021 aapvitelnt prflasgdts rltldltnlt dqpqtlnval tatgklsleg aqpqpvklpp
     1081 garstlfipv ralegygdge vtaqvtglql pgetfapqqk swkigvrpaf paqtvntgam
     1141 lnpgeswtap gqhingfspa tlqgqlllsg kpplnlaryi relqaypygc leqttsglfp
     1201 slytnasqlk algikgdtdd krraaidigi srllqmqrdd ggfalwdkng peeywltayv
     1261 tdflvrageq gysvptdavn nansrllryl qdpgmmsiry sdntqaskfa vqayaalvla
     1321 rqqkaplgal reiwdrhgqa asglplmqlg malklmgdap rsqqaldlal ktprndsrnw
     1381 madygsalrd nalmlsllee ykllpdaqnr llnalseqaf sqrwlstqes nalflagrsl
     1441 qtlsgawqae tslsgsalsg dkalvqnmng dqlgalqvtn tgttplwvrl dstgypdsap
     1501 qpssnvlqie rhilatdgss kslsslksge lvlvwlevka sqdvpdalvv dllpaglele
     1561 nqnlasssas lqdsgsevqn llsqmqqadi qhmefrddrf vaavpvnkgq pvtlvylara
     1621 vtpgtyqvpv plvesmyvpq wratgaasgp livvp
//
LOCUS       WP_284953301             326 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Enterobacter hormaechei].
ACCESSION   WP_284953301
VERSION     WP_284953301.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..326
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=35321
     Region          1..324
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mkkqllstla asvlllsasv vqaqdapsrt eciapakpgg gfdltckliq vslletkaie
       61 kpmrvtympg gvgavaynai vaqrpaeagt vvafsggsll nlsqgkfgry dvndvrwlat
      121 vgtdygmiav radspwkslk dlltamekdp nsvvigagas igsqdwmkaa llaqqakvdp
      181 hkmryvafeg ggepvtalmg nhvqavsgdl semvpylsgd kirvlavfse nrlpgpladv
      241 stakeqgynl vwpiirgffv gpkvtdaeyq wwvdtfaklq qteefkkqrd lrglfefnln
      301 gkqldeyvkk qvndyreqak afglak
//
LOCUS       WP_284953387             676 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF262 domain-containing protein [Enterobacter hormaechei].
ACCESSION   WP_284953387
VERSION     WP_284953387.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..676
                     /product="DUF262 domain-containing protein"
                     /calculated_mol_wt=78418
     Region          5..542
                     /region_name="GmrSD"
                     /note="DNAse/DNA nickase specific for phosphorothioated or
                     glycosylated phage DNA, GmrSD/DndB/SspE family, contains
                     DUF262 and HNH nuclease domains [Defense mechanisms];
                     COG1479"
                     /db_xref="CDD:441088"
     Region          541..661
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 msdakvtsft vrsllgdasr ylipmyqrny awgegeitql vqdildyqqk slhslypqty
       61 yigtlvvftr pdgdaeiidg qqrfttlsll anwlkkhags tldmswyqgi nlgfesrpks
      121 getfarlwqg vephklrske fneglikgye ligkvlrdlk lvgeslthfc tylfdhvqia
      181 rievpvdtdl nhffevmnnr geqlekhevv karlmavlne itdqkarqss lntlsrvwda
      241 csnmeryvqy gftpaerhql fgqenwgqfv ptdfnsladm lipsaselgt renqtnrtla
      301 niikssstfs gdrdeedegs serfnsvinf snfllhvlrv ysqtekdrvd vplddkqlid
      361 qfelrllkqn dpvktvqdfv fallkckylf dqfvikrefa kgsdswslkr lrwysemsts
      421 ytntfneded nntsinrqil mllsafhvst ptlvykhwln galyylfnah saenqidarr
      481 yleylehlas afvfqnflae qepksyfeii fgkevplqtt vlsdkiqkkm rfgmiannlv
      541 fnyldyllwc rdrnkaevvk rfeftfrssv ehfypqhpmd syktlpdvsl hsfgnlclis
      601 hsknsrlsnf qpkqkqehfe aslerneids lkllamvelm kknnqwgeee iathetemla
      661 vltcaggsds vfrevl
//
LOCUS       WP_284953420             264 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Enterobacter cloacae].
ACCESSION   WP_284953420
VERSION     WP_284953420.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..264
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28167
     Region          1..238
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mttqittali tgassgigav yadrlaarga nlvlvarred rlqtlaadlr arygvtvdil
       61 vadltdetgi ravedelrsn taidalvnna gtaqmapfla gdvaqhqain tlnttalmrl
      121 tyailprlaq nnhgtlinia svsslhvrag salysatkaw vlsftrglqe efadsnlriq
      181 avlpaatate iwqhsgvtvn dlpegsvmtt ddmvdaslag ldqgelitip pmhdaslwdr
      241 yetarlelfn sartgipapr yvkq
//
LOCUS       WP_284953644             524 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Enterobacter cloacae].
ACCESSION   WP_284953644
VERSION     WP_284953644.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 524)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 524)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 524)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..524
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56418
     Region          23..520
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 msglsldigk nrvrvparrr palpmvalav lfslmallpl gfiiaigiet gwetikalvf
       61 rprvaellsn tlwltalavp lcivtgvaia wltertqlag rgiwsalava plaipafvqs
      121 yawvsvvpsm hglsagvfls vlayypfiym pvaavlrrld ptledvaasl gtppwrvffr
      181 vvlpqlklai cggallvalh llaeyglyvm irfdtfttai ydqfqstfsg paanmlagvl
      241 alcclailll egvtrgkary arigagaare qtrwplkpva aalgqlfflv livlalgvpl
      301 ivlcrwiwlg gvqnwmsadl whslrqtlml gvggalltta cvipiawlgi ryphrifrml
      361 egciyitssl pgivtalalv tvtihyarpi yqteitlfla yllmfmpral inlragiaqa
      421 pvelenvars lgstpakalw svtmrlaapg aaagaalvfl gvsneltatl llsplgtrtl
      481 stgfwaltse idyvaaapya mlmilislpl tailymqskk iagl
//
LOCUS       WP_284953654             215 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Enterobacter cloacae].
ACCESSION   WP_284953654
VERSION     WP_284953654.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..215
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=24277
     Region          21..>210
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mvvkskvrkw gkweakensf arggqglvyr vrdtscvnsd ifvlkellnp krnerfsnei
       61 kaitllskha hvidiidyga ykdpdkptyv mpeadnnles yindeavkls vieclslfqk
      121 ivsgvehlhn sriihrdikp dnvlmfsgep kisdfglcli gdmprvtetq eavgpryyma
      181 peledgffld vdfkadiysl gkilyfllsg gkvis
//
LOCUS       WP_284954084             250 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: DNA-methyltransferase [Enterobacter cloacae complex].
ACCESSION   WP_284954084
VERSION     WP_284954084.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae complex
  ORGANISM  Enterobacter cloacae complex
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Enterobacter cloacae complex"
                     /db_xref="taxon:354276"
     Protein         1..250
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=27788
     Region          10..247
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mqkadigaat iycgdsleil reltgefdav itdppyssgg mtrsdrqakp sgkyvgnnny
       61 heffgdnrdv rswafwmtqw msqvnrlvks ggyamvftdw rqlptltdvf qaggfvwrgl
      121 ipwdktlstr aphtgyfrhq ceyvvwgsng plpkslhggp wpgmvtrrvi psqklhmtgk
      181 pielmeslva pvppgghild pfmgsastgv aalrkgykft giemsqqyfd iscerleken
      241 adiragvlcd
//
LOCUS       WP_284954734             402 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Enterococcus
            faecalis].
ACCESSION   WP_284954734
VERSION     WP_284954734.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..402
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=46019
     Region          1..392
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkrlqafkfq lrpngqqere mrrfagacrf vfnralarqn enyeagnkyi pytkmaswli
       61 ewksdtetqw lkeapsqplq qslkdleray knffqkrtaf prfkkrgknd afrypqgvkl
      121 dqsnsrislp klgwmryrns revvgevrnv tvsqscgkwy vsiqteyeat epqhestsiv
      181 gldagvtkla tlsdgtvypp vssfkvnqrk larlqrklsr kikfsanwqk qkrkiqrlhs
      241 hianirkdsl hkvtseiskn hamiviedlk vsnmsksakg tterhgrnvk aksglnrsil
      301 eqgwyemrrq leykqlwrgg qvlaippayt sqkcaccght akenrqsqsq feclecgyta
      361 nadingarni laaghavlac ggrvqsdrpl kqepaeviqt sv
//
LOCUS       WP_284954746             284 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Enterobacter
            hormaechei].
ACCESSION   WP_284954746
VERSION     WP_284954746.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13303747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..284
                     /product="helix-turn-helix domain-containing protein"
                     /calculated_mol_wt=31919
     Region          30..280
                     /region_name="PRK13500"
                     /note="HTH-type transcriptional activator RhaR"
                     /db_xref="CDD:184091"
     Region          198..280
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mratllpadq qffadllsgl vlnpqqlgrv wfaqrgasda vgsvsrdwpr ldvvlrgeyg
       61 nrlvagqqil rhgemlflpa qaasvpvfer pvmllsilfa psrlglvfhd srhgqsvpaq
      121 rhvelphper gecsamlmal thlsaspqdq aiiqplvlsl lhwcrkvvss lpepglsrgd
      181 flyqsicnwv qenyaeslsr esvaalfnis anhlsrlfsq qgtmsfvdyv rwvrmakart
      241 ilqkyhlpvg evakrcgyad sdyfsrlfrr qfgltpgeyr arfq
//
LOCUS       WP_284954822             400 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Enterobacter hormaechei].
ACCESSION   WP_284954822
VERSION     WP_284954822.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         <1..400
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <5..389
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 klnlqaekkh isvtvmlfdl drfkevndty ghdtgdlllr evstrlnals rfsetfyrlg
       61 gdefaflsng lteaaavsra reisdsiskp ytinnqliki atcvgivlsd nerrsdylyk
      121 fadlalyeak kegsqqikvf rqrmlqklqe srtlendmar aiendefvvy yqpivnsvsk
      181 eiygyealir wmhpvkgmls pesfifaaek tgmineigkt vlklacreav swavparisv
      241 nvspvqlgsk sfintvqsvl aetglpanrl elevtesslf sdrnnpitil kklralgvri
      301 siddfgtgys slsrlselnf dkikidksfv npistqedal nivklitgma qslnmgviae
      361 gveteeqler lqalgcelvq gylfskpqpq vdskiksgqq
//
LOCUS       WP_284954994             477 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Enterococcus faecalis].
ACCESSION   WP_284954994
VERSION     WP_284954994.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..477
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=56292
     Region          1..465
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mkrvmwfrrd lrlqdnkala halqnsaade lillfqmnpq qfiqesanhn affaslasfk
       61 eridqeahlq imvgepldlf srlkrklpdw qaiyfnedtc gfgakrdqqa mrffeenniq
      121 sfsfqdaylh gseeikkndg skyqvftpyy nkwkeapket pipvsytaek ifsaclfpee
      181 eaaygeqiar iplkhysvge ktarrclntf inqklrsyen krdfpyqdqt shlstflrtg
      241 elsirtiwqe lasapsslsk etfkkelawr dfynmiystf pqqkeeaiqe kfryiqwtnd
      301 pemfakwqkg etgypiidaa mrqlnqtgwm hnrlrmitas flvknlhidw rwgekyfqkm
      361 lidydaanni ggwqwaastg tdavpyfrif npiiqskkfd ndgqfikkyv pelkqvpqky
      421 ihqpnlmnea lqtqyhvhlg enypkpivdy asskkqtlfl yeaskeihqe mnnprfq
//
LOCUS       WP_284955106             537 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Enterococcus faecalis].
ACCESSION   WP_284955106
VERSION     WP_284955106.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 537)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..537
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=61862
     Region          6..456
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(20,22,24,28)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(59,62,99,102,143,162,166,198,247,398)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(198,247,316)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          463..533
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; pfam16657"
                     /db_xref="CDD:435493"
ORIGIN      
        1 meqwwknavg yqiyprsfkd sngdgigdlq giieklpylk elgvdflwln piytspnvdn
       61 gydiadyqgi qpefgtmedf qelldqahql glkiildlvv nhtsdqhpwf veakksldnp
      121 yreyylwada tpdrmpnewq sffgsstwty dagtkqayfh vfakeqpdln wknpkvreei
      181 yamirwwldl gidgfrldai shiqkepwdf kittnpwapf mnvkgiedym ldlkaifaey
      241 dimtvgeasg vsskkavewt ndagylnmif elehnvregk pgeerlnilg ykkvmarwqk
      301 hlgtegwnal yvenhdnpri nsilgnetsh sakaigtial llrgtpfiyq gqeigmvnyp
      361 fqqideldak dshnhyrlli esgydakqal kevahwtrdh srtpmqwtsq eassftsghp
      421 wlaihpnfke invadqetda qsvlnyykkl ialrkdnpvf tdgqfellap nhpsvfaflr
      481 ktteatalvi vnlsgekcqf dlpnkllgrk wqqllgnqdf tvkkrmqlap yqagvfq
//
LOCUS       WP_284955177             347 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Enterococcus faecalis].
ACCESSION   WP_284955177
VERSION     WP_284955177.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..347
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39564
     Region          9..335
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 myektkwkiq nmmkkgvfsg asfcfiegek eesncwglaq ikptkeqlts amlfdvaslt
       61 kvvgtttvil qlveegkiil dqslqtyyps fqdpnitirh llthtadlqg yipnrdqlna
      121 qelkdaynhs fhagkaigkk vvytdagtil lgfmleemfq qsmieilser vllplgmnes
      181 tflpknplnc vptelheqrg lirgtthdpk afvlrehagn aglfsnvydl tkfvrmylnr
      241 gsyhnhqflk ketidlllvn qvpaadkprs lgwdfkydva tqrpllfhtg ytgtfllidv
      301 rqqsafifls nrvhpedhrn tyieerdqll atylkekssv sdemtsf
//
LOCUS       WP_284955212             364 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Enterococcus faecalis].
ACCESSION   WP_284955212
VERSION     WP_284955212.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..364
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41943
     Region          13..348
                     /region_name="WecH"
                     /note="Surface polysaccharide O-acyltransferase WecH [Cell
                     wall/membrane/envelope biogenesis]; COG3274"
                     /db_xref="CDD:442505"
ORIGIN      
        1 mskeqpinln isdflkvfav asvilqtvls yvlthspqte amnsigsfyr mskysapmfi
       61 faiiynmvlk sqaksylefl kekfyelvlp yvvwsslyly afpslqqrmp yetplgflgk
      121 vlsgdgaahl wyavmmlqfq lfmpyfiwla tritknkkvi lpivfftiga hilwcfwyqk
      181 mifpyvetsl wylidrsgls yliygifgvi aakyqgkift flkktrvalf llflfifwqa
      241 vqgnlfdgtq mtpndlpyld plqsayslli iglvfylgtq giakkirllp mvkwiatyay
      301 rsylanvfif qvvlklvhpf ltnqpvslvi lvlymgtfvg sfgltvvveh ffksifklgr
      361 lvsv
//
LOCUS       WP_284955245             155 aa            linear   BCT 25-DEC-2024
DEFINITION  Dps family protein [Enterococcus faecalis].
ACCESSION   WP_284955245
VERSION     WP_284955245.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Choi,S.H., Baumler,D.J. and Kaspar,C.W.
  TITLE     Contribution of dps to acid stress tolerance and oxidative stress
            tolerance in Escherichia coli O157:H7
  JOURNAL   Appl Environ Microbiol 66 (9), 3911-3916 (2000)
   PUBMED   10966408
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 155)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 155)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   6  (residues 1 to 155)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..155
                     /product="Dps family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17688
     Region          8..145
                     /region_name="DPS"
                     /note="DPS protein, ferritin-like diiron-binding domain;
                     cd01043"
                     /db_xref="CDD:153102"
     Site            order(21..22,26,28..29,40,51,55,58..59)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:153102"
     Site            order(28,40,44,55,59)
                     /site_type="other"
                     /note="DPS ferroxidase diiron center [ion binding]"
                     /db_xref="CDD:153102"
     Site            order(123,130..131)
                     /site_type="active"
                     /note="ion pore [active]"
                     /db_xref="CDD:153102"
ORIGIN      
        1 mkfektkeil nqlvadlsqf svvihqthwy mrgpefltlh pqmdeymdqi neqldvvser
       61 litldgspfs tlsefaentk iedeignwdr tipermeklv agyryladly akgievsgee
      121 gddctqdifi anktdiekni wmlqaklgka pgida
//
LOCUS       WP_284955343             517 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Enterococcus
            faecalis].
ACCESSION   WP_284955343
VERSION     WP_284955343.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..517
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57851
     Region          1..501
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mqikilatsd mhgyimptsy sekkmdlpfg takaatmlkk lrasakgpvf qiengdfiqg
       61 splsyyvrka ethsvaaitk iinqmnydvs ilgnhefnyg ldylketias yqqpvlaani
      121 lgkdgqpyfg qpyviiekqg vkvailgvtt qyiphweqpa tvkdltfksv vetaaeyvpk
      181 lreeadlvvv ayhggfekdl etgeptellt genegydlle kvpgidalvt ghqhreiatk
      241 lngipviqpg frgafvgeit leiepmakgy hvigsdaaih pvgneqpdte vlalttalhd
      301 eveewldqpv gnvegdmtiq npnavrlkeh pyiefinnvq massgtdisg talfnnegkg
      361 fnnqitmrdi itnyiypntl avlrvtgqdl realeqsaty fvlekgqpif npkyvdpkpq
      421 yynydmyegi eytldlrqpf gervtklnyh dkavqaedvl eivtnqyrav gggnyqmfqp
      481 ekiireiqid mteliaeylk khpiiqastn dnfkviw
//
LOCUS       WP_284955380             371 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Enterococcus faecalis].
ACCESSION   WP_284955380
VERSION     WP_284955380.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..371
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43440
     Region          63..368
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mtvrkdkekg twiiditngk npitgkpnri ikrniptrke aielenhlrv tqlgdtsfas
       61 rimtmdmlye lvvetdkeeq rkesymatqe ynynrhikey fakakieklt hkelktfrss
      121 lsdkglsnnt vnklmiqmkk lldvavkhgv lkenpckqlk klpvkkkkmd ywtptefqef
      181 mtlftpeeyp fqlffkvayl tgmrmgellg ltwedidlrg dslevsktli hltgrmvins
      241 pktvagnrqi tlnhkladel yqwkdrqrel laeyvtepek lqvfqfvpsl mtrymitkky
      301 dkviersstl kririhdfrh shvallinng edpytikeri ghasisttld iyghlypnkq
      361 ksmsdkldcl i
//
LOCUS       WP_284955744             541 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Enterococcus faecalis].
ACCESSION   WP_284955744
VERSION     WP_284955744.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 541)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..541
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=62638
     Region          7..460
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(21,23,25,29)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(60,63,100,103,145,164,168,200,242,402)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(200,242,317)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          467..>507
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; cl02706"
                     /db_xref="CDD:445893"
ORIGIN      
        1 mekhwwqevv vyqiyprsfk dsngdgigdl pgiiekldyl etlgigaiwl spvyqspndd
       61 ngydisdyea imtefgtmad mdrlieeakk rkieiimdlv vnhtsdehrw fieakksken
      121 pyrdyyvwad pasdggvpnr lksafsgsaw tfdeasgqyy lhlfskkqpd lnwenqqmrq
      181 svyemmnfwi dkgiggfrld vidlvgkipg eeitangphl hrylqemnaa tfggkelltv
      241 getwgatpei akmyssperh elsmifqfeh msldqqpgke kwdlqpmeva klkqvfakwq
      301 telgndgwns lfwnnhdlpr misrwgndqe hwlessklfa illhmmkgtp ciyqgeeigm
      361 tntpitdire ardietinmy heylekgysk eeillkintk grdnarrpmq wtaeknagft
      421 tgtpwidvnp nyqtinvaaa ladknslfyt yqemirlrke hplivwgnfe lletvdevis
      481 fyrtygeerw lvvtnfsdkv qpfsadvhve qvmienmptd vtaladysla pwqafvvkvs
      541 q
//
LOCUS       WP_284955952             560 aa            linear   BCT 25-DEC-2024
DEFINITION  T6SS phospholipase effector Tle1-like catalytic domain-containing
            protein [Enterobacter kobei].
ACCESSION   WP_284955952
VERSION     WP_284955952.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter kobei
  ORGANISM  Enterobacter kobei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 560)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 560)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10561933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Enterobacter kobei"
                     /db_xref="taxon:208224"
     Protein         1..560
                     /product="T6SS phospholipase effector Tle1-like catalytic
                     domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=62547
     Region          117..319
                     /region_name="DUF2235"
                     /note="Uncharacterized alpha/beta hydrolase domain
                     (DUF2235); pfam09994"
                     /db_xref="CDD:462937"
ORIGIN      
        1 mtqyqgydvq dathktsihn ewktviakkk pvrgvtltig vffdgtgnnr entasrlmkf
       61 necsapkqgm nqkdaqsced fshainkdsl sngsyrgyys nihwlnslyi adqtllddqv
      121 qaqiqtyisg igtaadksds aigmglgtsi ldmyegvvtk tdeamegias ellafmkrnv
      181 qqdfciakiq fdvfgfsrga aaarhfanrv meqdtaiasa itkglrgdfy dgkpsgevrf
      241 lglfdtvaai ggisnffdin grsnprvkle lrpsvakkvf qitamneyry nfslnsiqgm
      301 wpelalpgah sdigggynpv gsplqenesl flscpefeiv sddtretdtr vyrnaekare
      361 mlmslpalkh ilphgkittk trsvgvinsn qsragiiqkq vgaavfferm avpnewanvc
      421 lrvmldaaqe aevmfyeiqe edekyslpte lkalcdkaia qgkavrlgqd pqaftederl
      481 ligkythcsa gwniesnrnl wvdpktgeif ihrfgpkedk afvfpnkpnd hwvrsvwymd
      541 dqqrlndnae knddvmvpny
//
LOCUS       WP_284955966             230 aa            linear   BCT 25-DEC-2024
DEFINITION  XRE family transcriptional regulator [Enterobacter hormaechei].
ACCESSION   WP_284955966
VERSION     WP_284955966.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..230
                     /product="XRE family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=25349
     Region          1..75
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          97..225
                     /region_name="COG2932"
                     /note="Phage repressor protein C, contains Cro/C1-type HTH
                     and peptisase s24 domains [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442176"
ORIGIN      
        1 mindrirear rnvrmtqdal akrigltkat isqwesgttt pngknlinla ealnvspewl
       61 ltgkgseske vtsnarvegg fsvwdsatpl eddeveipfy qevelsagng tyvdldrsgc
      121 klrfarstlr kagvdvncaa cvsvhgnsmd pvlpdgavvg vdtsktsvkd gqmyaidqdg
      181 llrvkllyrl psgirirsfn rdeyadeeyf nhdankikii gqvfwysvll
//
LOCUS       WP_284956995             265 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Enterobacter roggenkampii].
ACCESSION   WP_284956995
VERSION     WP_284956995.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter roggenkampii
  ORGANISM  Enterobacter roggenkampii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 265)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 265)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14398448
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Enterobacter roggenkampii"
                     /db_xref="taxon:1812935"
     Protein         1..265
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29633
     Region          21..116
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          180..256
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mptvidktpi hddaigwsrg airytrgeid pphqhsqgqf lfaikgvmlv etgskrwvip
       61 pqralwippf qehtysvlsa telravwfsp alisqcepfk rkdevhvima talfkeliag
      121 lfsaeyrpas qrsmavllld ilsetqqisa elpmpvdqrl hrvacdiian nlwdlslerl
      181 aeraamsert fsrafindtg fsfrawrqra ricasldlla ngypvkqvaw mlgfsgpaaf
      241 aaafraivga tpgdflpeqk rfpai
//
LOCUS       WP_284957099             283 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Enterobacter roggenkampii].
ACCESSION   WP_284957099
VERSION     WP_284957099.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter roggenkampii
  ORGANISM  Enterobacter roggenkampii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Enterobacter roggenkampii"
                     /db_xref="taxon:1812935"
     Protein         1..283
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=32329
     Region          12..>205
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mlelilskqp nsthmtkhfs aadgirgvac liviilhnvs kylptigqyt kgcekygvwi
       61 fftlsaflls iklmnkkptf peyakyiisr ffriippfvv avftyyymgy mnyqkmidti
      121 sfnssyfhfw tipvefkfyf tlplflisfl vadkikgimg ggallfllil lvqnaypyni
      181 tiensiqtlp ylsvflfgvf sailhcrhni kvsnamgdsi ilfiisilfi ispgvienvf
      241 rfqpidlmnk yvflgilfti lifilcntsg ysavflvtkh sdl
//
LOCUS       WP_284957389             438 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase
            [Enterobacteriaceae].
ACCESSION   WP_284957389
VERSION     WP_284957389.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..438
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=50354
     Region          5..420
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 maanltetai rglktkstsy yvwsnsaqrg tgrlgvkvqp sgskvfyfry yvekgkkekf
       61 iqlgiwpemk lvtanelakk ygawlvegke pqqeleqqrl aeqhimqihr sqgsfeelvh
      121 gyvnkmkldn krtwadvlkr lekecytvip retkakdvtp lqiktilsgi iqrdavvhan
      181 rvrsylmaaf nyglkadndp mntsvgitfg levnpvsaip kqssaekvgd twltleelrf
      241 vmehfseatg vgplmqhlir fctyvggqrp femiasqwsa idwqqktllv iadvsknkre
      301 hlipltesal qelasvkelt kesnspyifp lstngerpvr tdslarsimy frafnpefkv
      361 ftardlrrtc ktlmgeagis keirdriqnh alndvsskhy drydyltekr raleiwedrv
      421 nnyqrqqenn vvnlfgrr
//
LOCUS       WP_284957411             634 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ATP-dependent nuclease [Enterobacteriaceae].
ACCESSION   WP_284957411
VERSION     WP_284957411.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 634)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 634)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 634)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..634
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71219
     Region          1..482
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mklevirisg fqsfgpepte vslenityli gpngsgktaa lqalcklfaf dpalrrihrs
       61 dfhvpydeee vpeerqlwie adflfpelde eddnstvaph fshmrlddpg glprvrfrlt
      121 atmgldgdid enlvyvldvn adgspqntaq vpraernhiq vhylparrdp adhitygana
      181 llgrllravr wdaerdtikg ltdqisdsla anpsvkafsk slkttwatlh kgkffadpki
      241 tfvaseieal lrhlsvsftp ghdgslvdfs rlsdgqksml ylslvlssqa igravlaeed
      301 vsfdpdklrp pvftlvalee penslsphyl grivsalytm tknvdaqali athaptmlrr
      361 vapelirylr ltearktrvt ciklpekadd ahkfvreavq afpeiyfsrl vvlgegdsee
      421 ivlprllqak gapvdesait iaplggrhvn hfwrllsalq ipyltlldld varyaagwgr
      481 ikyvndqfsa yepykklpkd hgipswkdka qkvrdfdnyf elleergvff sspmdldfsm
      541 llaypeaydv dkekpdesti kavlgkshhd ssqysedelm lfstyhqrfk lgskpaahie
      601 altqlrdtel lenmpeslsr ladaviakle elpe
//
LOCUS       WP_284957587             352 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Enterobacter cloacae].
ACCESSION   WP_284957587
VERSION     WP_284957587.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..352
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=37288
     Region          9..352
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mnnklcekln iaypiiqapm agvstpemaa avsnagalgs isvgastpsq aeslirktrh
       61 ltagpfnvnv fcharaernd aletawierf rdvferygaa lpaalqeiyq tfhdndamae
      121 illetapaav sfhfgipper lvhrfksrgi itlatatslh earliesagi dfvvaqgtea
      181 gghrgmfdpr eedeqlstft lvqalrkgct lpviaaggim dgagiaamlk lgatgvqmgt
      241 afvlcpesaa neayrqalks eqamstvmts aisgrparcv sndfchltrd lpkesippyp
      301 ltyslgkila avaaakgahg fgaqwagqgv alarelpaad lvqtlvtewq dv
//
LOCUS       WP_284957613             387 aa            linear   BCT 25-DEC-2024
DEFINITION  sialidase family protein [Enterobacter cloacae].
ACCESSION   WP_284957613
VERSION     WP_284957613.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 387)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 387)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..387
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016997 - alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42858
     Region          25..385
                     /region_name="COG4692"
                     /note="Predicted neuraminidase (sialidase) [Carbohydrate
                     transport and metabolism, Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443727"
ORIGIN      
        1 msvtvtrdgi irpqqdtrvk aamlpsacpq nhaanllplp dgslmcvwfg gtqegiadis
       61 vwgsrlspgs qqwseaekls ddatrseqnp vlflapdnvl wllwtaqmsg nqdtaivryr
      121 qsrdlgktwg diatlldkpg tfirqpivvl engnwllpvf ycrtrpgekw vgnddisavk
      181 isedggktwr dvevpdslgc vhmnitplrn gtlvalfrsr wadniyysqs tdngeswsvp
      241 eptvlpnnns siqvttlasg elalvfnlms aagaqerras lydeiddgdg rkepvvthgr
      301 tafwgaprap mtvaispdgg kswpwqrhld egdgycmtnn sleklnrefs ypsikqspdg
      361 slhiaytyfr qaikyvrvtp ewvkesa
//
LOCUS       WP_284957718             231 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Enterobacter cloacae].
ACCESSION   WP_284957718
VERSION     WP_284957718.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18629715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..231
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27175
     Region          <82..191
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          145..191
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
ORIGIN      
        1 mdtsrvilsr chfsniglrh llsntfkkee ilsfynqhhf hdwvkgmkke sfftlylvlp
       61 dsiysniiyf qwlislkqkt nlhaieeiii ayhsdifpel facicshykh rlvninnltn
      121 deivrkmhtq rhpsksgivk khieltqmef cvlklmisgy tiddistlyn ikpkttytys
      181 nsimkqlgfn slkkiyscge iikssidhdi irekkkyysi ahikmyepqt a
//
LOCUS       WP_284958144             318 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Citrobacter
            werkmanii].
ACCESSION   WP_284958144
VERSION     WP_284958144.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter werkmanii
  ORGANISM  Citrobacter werkmanii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Citrobacter werkmanii"
                     /db_xref="taxon:67827"
     Protein         1..318
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36256
     Region          36..244
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mgkynqella erarniplyl hayafhlnmr yervlpddll diayqqklkg vkihvedges
       61 qslqklndrq lhdfkekakk ynldvhiets asdqatltda iriamatgat svrfypryeg
      121 hlndvmakia ndiawlsqhd dcglsftieq hedlqghelv tlvknsgmkn lsilfdfgnm
      181 inaneqplsa levmspwitq vhikdakiik egkgwgheac rsgygdlpme emlkallllg
      241 edkpqvhafg leeeveyyap afrfddegdn pwipwrdasy tplpdadmid arlvqekeha
      301 laqikyirdl cnkfignq
//
LOCUS       WP_284958239             580 aa            linear   BCT 25-DEC-2024
DEFINITION  IucA/IucC family protein [Enterobacter cloacae].
ACCESSION   WP_284958239
VERSION     WP_284958239.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..580
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65499
     Region          15..577
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mrtlprsagt dvaaqcflna llretkdwry lpataadels qihiplsqtq airvsvhyfs
       61 ptqhhqyrfp atliqtdsdr sdavtfpqlv dliiekpavk gsldadtlar fkqralesha
      121 htwqaidlrh rwanlrdapl tfaeaeqall vghafhpapk shepfnetea rrylpdfasr
      181 fplrwfaves eliageslnv slrerllrfa aqsapellgh ftdtrwllpm hpwqaeyllg
      241 qdwcqrlvak galqdlgeag aqwlptsssr slycetnsdm ikfslsvrlt nsvrtlsvke
      301 vkrgmrlarl aktarwqelq aryptmrvmq edgwaglrde sgviqeeslm alrvnllfdt
      361 pdtqtnvlvs ltqaapdggd sllaaavrrl sqrldlplaq aarcwldayc drvllplfsa
      421 eadyglvlla hqqnilvemq qdfpvgliyr dcqgsawteg adawlkeage sevenrfges
      481 qllryfpyyl llnstlavta alaaagfdse eslmsrvrda laslrqiakq trcldyvlds
      541 ptwnckgnff cylhdrnent iadpaviyfd fsnpfykeka
//
LOCUS       WP_284958180             446 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Enterobacter cloacae].
ACCESSION   WP_284958180
VERSION     WP_284958180.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..446
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48004
     Region          26..438
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,154,
                     157..158,161,267,270..271,274..276,279,306,310,360..361,
                     365,369,385,388..389,392..393,396)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 maysgkvdiq qviddsafsw fhwllivlgf lvlaidgfdt aamgyiaptl saewgihkqd
       61 lgpvlsaall glslgaliag pvsdrmgrkr vlvfsclffg laslgaawaq tlntltlwrf
      121 ltglglgaam pnaitlisef apkrcramai ntmycgfplg aagggaissw liphhgwrsv
      181 lltgaiapli ltlllalflp esvkflvqrg rdvmqirria srfardtldg vtgfflaeer
      241 vaskkgsvaq lfsmpwlpgt lmlwvtyfmg lviyyvllsw mptlmlgmgy plaesawlts
      301 lftfggtagi llagwmmdrw eahrvvaggf mltmalilll gmehnhialf ggliflmgia
      361 mngaqsgmqt laatfyptec ratgiawmqg igrfggvagt mtsaqllsmq wqadsilmil
      421 slpalvaaga tvykmlrcrp qepgva
//
LOCUS       WP_284958301             358 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Citrobacter werkmanii].
ACCESSION   WP_284958301
VERSION     WP_284958301.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter werkmanii
  ORGANISM  Citrobacter werkmanii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Citrobacter werkmanii"
                     /db_xref="taxon:67827"
     Protein         1..358
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41813
     Region          3..233
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mptplvsiiv tsynhdafle ealdsvfnqt wknteviivd dastdrsvei ikkyqqkync
       61 ktilretnyy sqkdktgdkp iieamnmatg kyiavvdsdd livptkishq vnvleknphc
      121 vmcysaiqvi mpdgsrfpys dlflngdvfh hllvsgnfsl yigslirrea ylkiersdpe
      181 lvqedwdmfl klsrqghfis tqrlvayyrr henntwyrkd nsklmyrnrm milnqwkhed
      241 awveamnsrw kqyahpdhtl vkedidellv khptdpllhf qgfiaaihtk dvnkaqyhiv
      301 qaiiycdirl eilpqlyyaa lksindnkir stilsslksr lpdqyqqisa kfsqdlqq
//
LOCUS       WP_284958583             370 aa            linear   BCT 25-DEC-2024
DEFINITION  fatty acid desaturase family protein [Enterobacter cloacae].
ACCESSION   WP_284958583
VERSION     WP_284958583.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..370
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42716
     Region          8..361
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mnlfkpdkll tfpadsprlv talhretkal lseqddhrya dsrmlaktav liaaclvcys
       61 valcqneiid fglwyfatvv famlltinvv hdashnaflr gkranawlnr iiafplgldp
      121 dcwrvrhvry hhaftnieyy dpdtaengll rqthrqrwrp fmqaqryywp lvaaltfpwy
      181 iwvvdwldrg gltpvtphla qrgvagwtlf llgkalhiaf clvfpawlma drfsfdtilm
      241 tyllaqmiss lifvmlvigt hwakgsvqlp pkegkmdvgr ishtfattfd wsirpafigy
      301 wlgglnlhlt hhlfphwnhr hypalsrive eiarqegmef rrlsfsdlif lqqqflkhmg
      361 kdpgnsgdkp
//
LOCUS       WP_284958651             494 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Enterobacter cloacae].
ACCESSION   WP_284958651
VERSION     WP_284958651.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..494
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54210
     Region          113..348
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 manlpwrvsv rlmalakkva mvigiivvvl lavrvylsqq gpalhlwhtw rademsvsel
       61 dkanfadyld rekaiftdld navtaktkge ertalnryyr qslvwpgkft pdanrsfvlm
      121 pagkprgavv llhgltdspy svkhlavdyq qrgfvavvpr lpghgtapga ltnvdwemwl
      181 aatrlavrea srlagdnvpl hlvgysngga lamkytldal espslrkpqq lvllspmigv
      241 tafarfagfa glpallpafa kaawlniape ynpykynsfp vnaarqswll tkalqeqigr
      301 aaqnhtldrl ppvlafqsvm dstvstravv tglfdqlpan gselvvfdin qaasfrplfr
      361 psswtalsel lpsaqrrysv tiitnasaer fatvakhipa gsteetvepl aqqyppevys
      421 lshvavpfpp dddlygrhpa vknrygislg tialwgetsv lsvgkdalmr vtsnpfydym
      481 kmridnriga eekg
//
LOCUS       WP_284958664             247 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Enterobacter cloacae].
ACCESSION   WP_284958664
VERSION     WP_284958664.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..247
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27661
     Region          1..237
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          156..237
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mthtrhirqt fnrlpglelr stwqstvayk rhchpqlsig aivegqtccr cndtqyilhp
       61 gdlivipahv phscnpvsgq prsyhmlyid tdyplaeqvi rdstlfalyq nvvenmsans
      121 lnmlisalpr casrtgelrt tsqhiqqafl adltsppsld dlahrfslrk etlirtfrqd
      181 tgltpgsfln isrveyakar lragddiadv gyqsgfadqs hfhktfvsyt aatprqyatg
      241 rsisdnk
//
LOCUS       WP_284959136             537 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Enterococcus faecalis].
ACCESSION   WP_284959136
VERSION     WP_284959136.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 537)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..537
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=61901
     Region          6..456
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(20,22,24,28)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(59,62,99,102,143,162,166,198,247,398)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(198,247,316)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          463..533
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; pfam16657"
                     /db_xref="CDD:435493"
ORIGIN      
        1 meqwwknavg yqiyprsfkd sngdgigdlq giieklpylk elgvdflwln piytspnvdn
       61 gydiadyqgi qpefgtmedf qelldqahql glkiildlvv nhtsdqhpwf veakksidnp
      121 yreyylwada tpdrmpnewq sffggstwty dagtkqayfh vfakeqpdln wknpkvreei
      181 yamirwwldl gidgfrldai shiqkepwdf kittnpwapf mnvkgiedym ldlkaifaey
      241 dimtvgeasg vsskkavewt ndagylnmif elehnvregk pgeerlnilg ykkvmarwqk
      301 hlgtegwnal yvenhdnpri nsilgnetsh sakaigtial llrgtpfiyq gqeigmvnyp
      361 fqqideldak dshnhyrlli engydakqal kevahwtrdh srtpmqwtsq eassftsghp
      421 wlaihpnfke invadqetda qsvlnyykkl ialrkenpvf tdgqfellap nhpsvfaflr
      481 ktteatalvi vnlsgekcqf dlpnkllgrk wqrllgnqdf tvkkrmqlap yqagvfq
//
LOCUS       WP_284959480             265 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Enterobacter roggenkampii].
ACCESSION   WP_284959480
VERSION     WP_284959480.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter roggenkampii
  ORGANISM  Enterobacter roggenkampii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Enterobacter roggenkampii"
                     /db_xref="taxon:1812935"
     Protein         1..265
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=29082
     Region          12..256
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mnglilvres ypvgfaamsg vfgailgsfl gvvvdrvpgm vleeesrsnl lfpashcpvc
       61 qhalraweni pllswlalrg rcrcckspip lrlfllellt avffgltarw ipdlaslfsl
      121 wvlaafllpl amidgqhqll pdcltqpllw agllfhafsh glllrdallg avagylslwl
      181 vywafrlltr reglgygdfk llaalgawcg wqslpaieli aalsgivgyl llnksnknnq
      241 tivfgpylaf agialytcql fvnty
//
LOCUS       WP_284959503             319 aa            linear   BCT 25-DEC-2024
DEFINITION  YbgA family protein [Enterobacter hormaechei].
ACCESSION   WP_284959503
VERSION     WP_284959503.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007153
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..319
                     /product="YbgA family protein"
                     /calculated_mol_wt=36232
     Region          70..315
                     /region_name="YbgA"
                     /note="Uncharacterized conserved protein YbgA, DUF1722
                     family [Function unknown]; COG3272"
                     /db_xref="CDD:442503"
ORIGIN      
        1 mttkpvlgis gcltgsavrf dgghkrmgfv mdelaqwvaf rpvcpemaig lptprpalrl
       61 vmttggetem rfskaphddv tqkmaaftad ylpkigdlag fivcakspsc gmervrlyde
      121 ngnrgrkegv glftaallet fpwlpveedg rlhdpvlren fvervfalhe lnvmrknglt
      181 rralldfhsr yklqllahhq agyreigpfv aslhewddld affvayrdkl mtilkkpasr
      241 knhtnvlmhi qgyfrnqlns rqrgelrdvi lhyrdgllpi lapltllkhy laeypdrylm
      301 tqnyfdpysd dlglrlavt
//
LOCUS       WP_284959832             706 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Dialister micraerophilus].
ACCESSION   WP_284959832
VERSION     WP_284959832.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..706
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=78205
     Region          1..144
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <236..700
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 mlflgvfvii silgfntgvi gdlitqafsv lfgilsifpa iglvvwggyy tlkasnfswn
       61 rklllaffsy fliatlythi mvptgyefdm kyiteyggii gssitwsfrw migeigttil
      121 itlllvidil fltkwslssg vqkiskktee klilvkktik eksqtlkkpe ffseneeesn
      181 dflyksskkk hikensisev knksikksin etlndkneel dkddskeikt rsgykfppie
      241 llhksikise nyfdiakeka dllektlksf gvsakvinis igpsvtrfei epapgvkvrk
      301 ienlsddial qlaatqirie apipgksavg ieipneknse valrdvledn kfkrgkgnil
      361 valgkdiagn avvadlskmp hlliagatgs gksvcintli tsilynsspd dvklilidpk
      421 vvelsiyngi phlridvvtd pkkaagalnw avremehryk lfsenkvrdi kgfniakpel
      481 klpymviiid eladlmmvas dsvedsicrl aqkaraagih lvlatqrpsv dvitgvikan
      541 ipsrisfavs sqidsrtild ragaekllgk gdmlfdpsgv aypirvqgaf itdkevenit
      601 nfikenssgl ikldnkpidl sipeikeivp fesqqdellg eaaewildtk rasvsalqrr
      661 frigytragr lmdtmeamgi vsgadgakpr eiliskdele iklknt
//
LOCUS       WP_284959850             208 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Dialister
            micraerophilus].
ACCESSION   WP_284959850
VERSION     WP_284959850.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..208
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23247
     Region          3..205
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mnlkktswnv faaavrfllk iifvhiyrid vqgqenipek gsiivapnhk syfdpplvsi
       61 afkkrlvhym akaelfknpf fakilricga fpvkrgrvdq gairtavkll kdghilgifp
      121 egtrirkeel gkfhsgmasi amltgtsilp iavvgsmtmp krgknlailv gkpvqvnkek
      181 pdsekikiln ekvkseiekl ikdyndkq
//
LOCUS       WP_284959834             138 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Dialister micraerophilus].
ACCESSION   WP_284959834
VERSION     WP_284959834.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..138
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16057
     Region          4..129
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mniikrrvnf yetdgmkvvh hanyfkwfee arveylragg iclnelmkkg ivfpivevqa
       61 rylksakydd viiiktylke inrikltfyy evvkeetgei lttattkgty tdintgkivr
      121 ipqekiakli siskedre
//
LOCUS       WP_284959843             351 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Dialister micraerophilus].
ACCESSION   WP_284959843
VERSION     WP_284959843.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..351
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=37986
     Region          14..351
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mlfsslrigd liakvpiiqg gmgigvslsk lagavakagg igvvsaaqpg fkdpdfkrht
       61 ydanirtlsy hiekakeisd ngiigvnimc ggqhyedyvk cavqsgadii fsgaglpknl
      121 pefvkgtntk iapiigsska atvllklwer hhkrtadlvv iegpkagghl gysrediaiy
      181 ehksyneeii kileivktfe nkfnkkipvv fgggifdksd inhcislgls gvqmatrfva
      241 teecdasref keayikakke diglvhspvh mpgraiinpy vkkilrgkki vrscfrcltg
      301 cspqttpyci tmalvravtg dvdnglifcg anawkikeit tvpkliselt e
//
LOCUS       WP_284959854             555 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Dialister micraerophilus].
ACCESSION   WP_284959854
VERSION     WP_284959854.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..555
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63790
     Region          22..320
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mqesfitrfd akikscknih liavlfivsf illsigssll pvtdpvesny altakemvls
       61 gnwmspqiyg vfwfdkpimi ywllsvsysi fgftnfasrl psiifgaisv pllyyyvshi
      121 lkdkqiafys gimlltsfef wlishgiitd avllmftipt lfsaytgikn nnikhmliay
      181 gaagfacltk gpvglvlpgl flliwcglmr ssvylkrcfp wqgiilfliv vlpwyggmyl
      241 ihgqdfingf lgihnvlrat ssehpsdnhw yyylivlpls llpwfgltvy qaikewkekt
      301 dlylflmtwl lgtfffytlm atkyitytyi avipgivlaa kaiksikkgs tkayiclsip
      361 ffiltvamgy lttrvhevnw tfmyfiiils ivfvglffkk nlrqgyiyvs tftllmyism
      421 ilqglpvymn trapvffade fknlpgkhyf fdtystsyvy ytsdlatrik psialetnve
      481 srnslwdfkf imptisdnef enkklnesaf vfvynknada fknwkfynhf vpvkkfddgt
      541 iyklvtidel sshna
//
LOCUS       WP_284959903             330 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Dialister
            micraerophilus].
ACCESSION   WP_284959903
VERSION     WP_284959903.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..330
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=36698
     Region          6..301
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mnkleknctv ivnptagrgr strylpmlsd vlkekyenit ikttkktkda trfariaakn
       61 nediicmggd gtinetingi ipvksststf gfvpfgtvnd laralhiprs pkgairmlkn
      121 atktkidvgk inkryfinvv aagliaetvg kvtikektlf gsmayfmkal qvinkqpsyr
      181 friemkngti iqisspliaa mltdsagsfh nfmptkdrnk gliklvlfkd fswintlkea
      241 pklitgeqfg pdtmtvidvk kahisieden telltnidge igsefpinie vlpsrlsvfi
      301 pnnaekenst fnvphliefl rkhlkltyte
//
LOCUS       WP_284959927             400 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Dialister micraerophilus].
ACCESSION   WP_284959927
VERSION     WP_284959927.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..400
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43357
     Region          23..238
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          147..399
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 msytnlpikn lksaplktaa mifltfllaf cvftgsivim slqngierle drlgadivvi
       61 pnsakrkidp qfmllngtpg yfympkqnfd mikhiegidk issqtflasl sasccsvpvq
      121 iigfdpqtdf iiqpwikksy gkplgygdvv vgssvnatvg dtiqfynkqc kivakleatg
      181 tgfdtavytn setinmlids sikmglnpvf qgkaedviss iyikvkkgyd itrvsndinl
      241 rvrkvkaipa ksmlsgiags lsavsksikf ltyavwfmvf iiliiafslp igsrkkefav
      301 lrmlgisrrn laqiimkesa visiigaisg iaagyifvip fsgliessln lpflipdfam
      361 igslsiltfi tvlavgvlas aysafrlsrv dtasilrggn
//
LOCUS       WP_284959948             174 aa            linear   BCT 25-DEC-2024
DEFINITION  KdsC family phosphatase [Dialister micraerophilus].
ACCESSION   WP_284959948
VERSION     WP_284959948.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..174
                     /product="KdsC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=19461
     Region          4..168
                     /region_name="KdsC"
                     /note="3-deoxy-D-manno-octulosonate 8-phosphate
                     phosphatase KdsC and related HAD superfamily phosphatases
                     [Cell wall/membrane/envelope biogenesis, General function
                     prediction only]; COG1778"
                     /db_xref="CDD:441384"
ORIGIN      
        1 mgalinikmi afdvdgtltn gklyenenge lykqfhvhdg lmlslahsig iktglitgrn
       61 spivkargke ldmdfvllgv knkvkamekl ksehnlswee iaymgddlnd lnllkkvafs
      121 gcpknareen kkicdfisey eggngaaref iekilkvqnl wetalnkfke itee
//
LOCUS       WP_284959965             267 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Dialister micraerophilus].
ACCESSION   WP_284959965
VERSION     WP_284959965.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..267
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30279
     Region          5..262
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(29..30,32..33,36..37,75,79..80,83..84,112,116,123,
                     126..127,132,155,159..160,162..164,166..167,170..171,
                     174..175,200..201,203..205,207..209,211..212,214..215,219,
                     222..223,229,231)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(158,162,165..166,168..169,214,217..218,220..225,
                     228..230,234,236)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(179..186,202,205..206,209)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mltdmtlgqy ypgesvlhhm dprakifcmm iavitifssn siysylfstl fviltvaisr
       61 vppamiwrav kplwfilvft mlihffttpg tdliayrwfh itkegftngi fmtlrlllli
      121 ifaslltftt spiiltdgie siltplqrfg vpahelammm tialrfiptl leetdrimka
      181 qasrgadfin gnflqraksm ipimvplfis sfrraddlat amearcyrgg egrtkmtqls
      241 ygtrdytamt itivalvivf lmryfsi
//
LOCUS       WP_284959968             270 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Dialister
            micraerophilus].
ACCESSION   WP_284959968
VERSION     WP_284959968.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..270
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=31678
     Region          46..264
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 meikinddfd ltkiinsgqc frgkeieeni yrfitndeii yirkksdday eiscderawn
       61 kvwknyfdme rnykeirkqi pendtfliks artgrgiril nqdpwemlit fitsqrksip
      121 airsaieklc ilagnkkttd yetiytfpti etlselalkd lescglgyra pyiykttqii
      181 rkgeinleel yayndeklie tlkifpgvgi kvancvalfa ygrtnrapvd vwieriikne
      241 yeginpfnny ktnagimqqy mfyymqvnkk
//
LOCUS       WP_284960022             410 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidase U32 family protein [Dialister micraerophilus].
ACCESSION   WP_284960022
VERSION     WP_284960022.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787090
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..410
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=46971
     Region          1..306
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
     Region          325..404
                     /region_name="Peptidase_U32_C"
                     /note="Peptidase family U32 C-terminal domain; pfam16325"
                     /db_xref="CDD:465094"
ORIGIN      
        1 mekmellapa gnmekmkmaf rfgadavfla gkqfglrayg gnfskeqlke avdyahergk
       61 kvyitvniip redelegldd ylkylyeikv davivsdlgi fsvcrevtpn lpvhistqas
      121 tanwraakmw kdmgaerivl arevsvsema dirkkvdvel evfghgamci swsgrcllsn
      181 ffthgkrqsn rgeciqacrf kysvmeesrp gqyfpieede hgtyifnskd lcliehipel
      241 aeagvsslki egrmksvyyv aaviatyrka idayyreken ykfrpewkee lekishrpyt
      301 tgfafaqade kaqeyeksqp vqpydfigmi kkydentkta qvqqrnhfkv geiveclsps
      361 gevfpleigk ltnkdgeqve kaphpleelt metyrklepy timrrkangr
//
LOCUS       WP_284960083              88 aa            linear   BCT 25-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Dialister
            micraerophilus].
ACCESSION   WP_284960083
VERSION     WP_284960083.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..88
                     /product="type II toxin-antitoxin system RelE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0017148 - negative regulation of
                     translation [Evidence IEA]"
                     /calculated_mol_wt=10328
     Region          2..76
                     /region_name="RelE"
                     /note="mRNA-degrading endonuclease RelE, toxin component
                     of the RelBE toxin-antitoxin system [Defense mechanisms];
                     COG2026"
                     /db_xref="CDD:441629"
ORIGIN      
        1 mkfevlyrkk vkksigkldt sikiliksri dknlvntenp rlygkaltgn lynyrryrvg
       61 nyriafeikd nelivlafde nrgikiyn
//
LOCUS       WP_284960121             253 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfite exporter TauE/SafE family protein [Dialister
            micraerophilus].
ACCESSION   WP_284960121
VERSION     WP_284960121.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..253
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26927
     Region          4..251
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mdpffqylfi ctlvfiagfi davaggggli sipayivsgv pvhaaiatnk msssmgtlwa
       61 tykfsrdgyi pwrlalscvv fafigsifga nialaidart flfcmlvlip itglyvlqsk
      121 slikekipfs fsktailsiv tssligvydg fygpgtgtfl ililtgvshv slkqangitk
      181 vinsttnlaa lsvfllnnqv llplgvvagl fgiagnhlga tyfkgkgakg vrpiiltvlt
      241 ifffrvvydl fik
//
LOCUS       WP_284960191             864 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Dialister micraerophilus].
ACCESSION   WP_284960191
VERSION     WP_284960191.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 864)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 864)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 864)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 864)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..864
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..864
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=95977
     Region          168..864
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mkinknlhhh ikdnnlkiei hhvleneaei skderrafgh iidknlhilt ghqqnchcdh
       61 cieedceycg keiesckcdf lgkeykrgly hienldcvqc aalmegkirk ipsvffasvs
      121 fnkkelrlis knnpdllipe itkisrtfne ninilppkqn tklntelyvi ptlncpscai
      181 klekninqqq gvfsatvtfs tkqlkitaen pdkllpeiin vcnkiepgtk ivkkinynkn
      241 eqnksksdky skfinstgff lyviglsgfy dlikfsdllt sslliisyfl lghdilmkai
      301 kniinknvfn eyllmsiatl galaiseype atgvilfyki geylehfaie ksrkqiteti
      361 dlrpetvhkl kngiietitp edvdigdiir ilpgervpld giiskgktqi dtslltgesi
      421 prsvtigdsi ysgtinlsst ielqvektls esmvsrilds ienalagkps idkfitkfsr
      481 iytpivvfaa ifliiflpff ttnsykdaly ialtflvisc pcalvisvpl sffsglgvas
      541 khgilfksgn iieilnkinv illdktgtlt egsfkireie tyqninedkl lalvagaeah
      601 sihpiaksii qaaedkklyi pkfsaineis gkgiitklgn kdiiignkkl lnengitidn
      661 nnysndfeti iyvainkkll gkikisdalk kdsfnglqkl tkknidiiml tgdnnavaen
      721 iakklnikkf ysellpldki kilkkyttnn sktlfvgdgi ndapvlatad igaamgsgsd
      781 aaieasdivf lnnnvsaist sisiaektit ttkinifiai fikiavmilg ligmadmwia
      841 vfadtgvtll cillsmnlfl rkfe
//
LOCUS       WP_284960249             312 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Dialister
            micraerophilus].
ACCESSION   WP_284960249
VERSION     WP_284960249.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..312
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=36185
     Region          <238..311
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mknfddlikk frlqlaetpl yspagktfsc nnseysgtyw iyegkdfyid ihnmyikedy
       61 vfneseilsd ylslisnyii scngewdtpy qnigpntili mdvfrennyi fhknsifygv
      121 slkfkenmlk kyvveslqlk rynvshvfls trdtitepik klankilnct mekpaadlff
      181 egiakewlsi tinaflkskn kksvplsdkk aiekvclyin dhysmkipqs llekiammsg
      241 tklkstfkki hnmsiteytq rkrinfaenl lmtsdidikn iakavgyssp grfsalykry
      301 kgqspkdark nk
//
LOCUS       WP_284960327             470 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Dialister
            micraerophilus].
ACCESSION   WP_284960327
VERSION     WP_284960327.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..470
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=50337
     Region          1..441
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mvlnilnqin givwgpwlli llvgtgilmt vrlrglqfhh lknalklifs arnkgsgdid
       61 sfkalctala atvgtgnivg vataiklggp galfwmwiaa lfgmatkyte gvlavkyrev
      121 dakgqisggp myyiekglgk kwkplavmfa ifgtltamlg ngtftqvnai tsslhltfnv
      181 piwlgstllt ilvaiiilgg lktiskaaek ivpfmsvtyf iitivilciy henlpfaimq
      241 vfegatsgta amggfagagm mlamrsgiar glfsnesglg sapivaaaak tkwpaeqglv
      301 smtgtfidti iictltgltv ivsgqwtgdv ngaaltqaaf sgaigyfgpl fltialtlfa
      361 fttilgwcyy gerclvylfg tksimpyrvv filiiasgtm lkleeiwtla divnglmaip
      421 nlvaiiglsg ivveetnkyf kflekrnnri ksykekkase fkninttpti
//
LOCUS       WP_284960329             355 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Dialister micraerophilus].
ACCESSION   WP_284960329
VERSION     WP_284960329.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..355
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=40217
     Region          6..349
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mqkrtekirk mmknnqidfv ivseeasiky ltdetidage rftvfvisrn dsfwirnklf
       61 plkkhtfkdi syldgsdyik llsdkipens kigidkflys kfllellsrr kdltfvngse
      121 ivdevrsikd eneiikmrks shlndlaike lvkhlkvgvt ekeaayklse iykklgadgf
      181 sfppivafge ssanphhevt dkkltentiv lidigcmkdg yasdmtrtyf fgtptdemkk
      241 vhnivkeane katkvikegv klsdidkiar thisnsgygk nfthrlghfi gltthetgev
      301 sptseiiake gmifsiepgi yipekfgvri enlvavtkng ceilnkvshn pyisl
//
LOCUS       WP_284960400             333 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Dialister micraerophilus].
ACCESSION   WP_284960400
VERSION     WP_284960400.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..333
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=38254
     Region          103..327
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 milyyqiynn nnfsdyffvy lislffvlhc iffiiiykkn adfikkilsv tnllklglhq
       61 ihhgikpiei yynnenefgq lckiykilsd kikekelknn indekrkvif sgiihdnktl
      121 lttllgysea lkmnknlste kkekyitgiy scaedlseln etlsvfnkis ktnsllnpkp
      181 ldfsqtihki vnpvadslal knvsitmnla enlyinldik afkrillnll antiryrkkq
      241 fskitlktyk egnfavfsys ddgpgvskdn lphlfeayyr npetkktiqg sglglaivak
      301 iieahkgtye aksdngltii tripliered syd
//
LOCUS       WP_284960406             490 aa            linear   BCT 25-DEC-2024
DEFINITION  YadA C-terminal domain-containing protein, partial [Dialister
            micraerophilus].
ACCESSION   WP_284960406
VERSION     WP_284960406.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10511181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         <1..490
                     /product="YadA C-terminal domain-containing protein"
     Region          <116..>250
                     /region_name="auto_Ata"
                     /note="trimeric autotransporter adhesin Ata; NF033481"
                     /db_xref="CDD:411124"
     Region          290..>320
                     /region_name="YadA_anchor"
                     /note="YadA-like membrane anchor domain; pfam03895"
                     /db_xref="CDD:427576"
     Region          395..>466
                     /region_name="por_somb"
                     /note="iron uptake porin; NF033921"
                     /db_xref="CDD:468246"
ORIGIN      
        1 kkaidknagd iktntdniaa nkkaieknat diaakmtswk lkaggvegea eikdgnavtf
       61 dvaakdqglt vtrdgstiky giegskidis enktvkelre eakkhtsvva gdyttvtest
      121 neaggkkytv tgpsvktdnn ltvqdiitgd kktgytigla kdlkdlnsvs aktvnaetvk
      181 adkvdtktvn vgdkvtlgtt gltikdgpsv taagidagkn kitgvaagav seksteavng
      241 gqlfgveqkv ninsrnisil ggkvvevnnr vnrvgagaas laalhpldfd pddkwdfaag
      301 ygnykganav aigayyrpne dtmfsvggsf gggenmvnag vsvklgqgnh vttsrvamak
      361 eikdlraeve vlrqavtgig qgqtpdpvkm klfpdiaknh wayeaveelt kqgllegypd
      421 gtfggdrmmt ryefaeivyr amqkglnvne klvqefepel erfridvitk dkdgnpvier
      481 irvnekkkak
//
LOCUS       WP_284960742             370 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Cutibacterium acnes].
ACCESSION   WP_284960742
VERSION     WP_284960742.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..370
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39186
     Region          5..365
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mtaqfippak pilgdderka vdeviasgmv aqgpqvhafe defssqvvdg vhcvavnsgt
       61 salhigllas gigegdeviv psftfaatgn svalsgakpv fadvdpvtft ldpasieasi
      121 tdktaaimpv hlyglpanma eivaiatkhg lkifedcaqa haasidgkhv gtfgtfgafs
      181 fyptknmtsg eggmittsdp eiarkaamlr nqgmekryan eyvglnnrmt dihasigrvq
      241 ltklagwtkt rqenaaflss niteaitpav pegyvhvyhq ytirlegatd eerdrfvtal
      301 keehqvgsgv yypipnhrlp slapyapgle lpntekvaae cvslpvhpsl sqadreriva
      361 avntcakaga
//
LOCUS       WP_284960858             530 aa            linear   BCT 25-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Citrobacter
            portucalensis].
ACCESSION   WP_284960858
VERSION     WP_284960858.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..530
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=58018
     Region          3..528
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mktifkngnv idgtgsegri advmvdegri veigqievgi neqvidatgk iicpgfidth
       61 thsdlsaiin palsakirqg ittellgqdg valaplpeey ipawrkniag ldgdtdkidw
      121 kykntdgyln llasrhpatn laylvphgnv rmeamgldgr pstredvakm cevlerelka
      181 gafglstgli ympcafgdta emielckvta kydgifvvhq rseaddiins tqelidiaka
      241 tgvwlhishm kvcgkknwgl idqmlgmleq aqeegirisf dqypyvagst mlgvilppwv
      301 hsggtdklle rlaspelrak middiqqgip gwdnfidfag ldqifvtsvk taknqdavgl
      361 nlvqlgelrg kdpynatfdl lfeeenavgm vdfygteehv ikflcrseqn vctdglmgag
      421 kphprvfgaf prvlgkyvre egclsweaai rkmtgkpaev lglqdrgllk vgyaadivmf
      481 dpntitdkgt fvepnqypeg ieivmvngri alingtesya csgtvirkqy
//
LOCUS       WP_284960839             327 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein [Citrobacter].
ACCESSION   WP_284960839
VERSION     WP_284960839.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..327
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37735
     Region          6..220
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mdtpfllsvi ipcyncqdyi yeclqsvssq iddsveiivi ndgstdnslk eiesfisenk
       61 nksiklitqk nqgvsaarna gidvcsgkyl afldgddlwd stfwekitpt lklndidlie
      121 fnanrfyddn kekvtevsiv stnetltids isnlretflk newfpwarvy krfifntlrf
      181 pvgrhyedia lipktyllsk kikrmtdtlv lyrvrknsit naprkkdidd iicamgvfne
      241 llnkkgksei etiapsvhqt yslakristk ingycsfnee qihyikkavt pfsgtqkfsk
      301 rinllfirey clikkikyql rsdrtkv
//
LOCUS       WP_284960739             476 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Citrobacter
            portucalensis].
ACCESSION   WP_284960739
VERSION     WP_284960739.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..476
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51364
     Region          1..448
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mpdffsfine ilwgsvmiyl llgagcwftw rtgfvqfryi rqfgkslkns ispqpgglts
       61 fqalctslaa rvgsgnlagv alaiaaggag aifwmwvsav igmatsfaec slaqlykerd
      121 srgqlrggpa wymarglgmr wmgvlfaifl liayglifns vqansvsral tfafdipplf
      181 sgialaivsl lvivggikgv arlmqwfvpm mallwigcsl viclwhfgql pgiimtiiks
      241 afgwqeaaag aagytlsqai asgfqrgmfs neagmgstpn aaasaaswpp hpaaqgivqm
      301 igvlgdtlil ctasamiill agngttyvpm egiqllqram vsltgewgag fvalivilfa
      361 fssivanyiy aennliflkl dnirviwllr iatvctvigg tlisfplvwq ladiimacma
      421 itnltailll spvvhtiasd ylrqrklgvr pefdprrypd irqqlapdsw detpre
//
LOCUS       WP_284960823             418 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter portucalensis].
ACCESSION   WP_284960823
VERSION     WP_284960823.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..418
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=47989
     Region          2..404
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mklnarqvet akpkdktykm adggglylev sakgskywrm kyrrpsdkke drlafgvwpt
       61 vtlaqarakr deakkllvqg idpkaeqkea qaensgaytf etiarewhas nkrwsedhrs
      121 rvlrylelyi fphigssdir qlktshllap ikkvdacgkh dvaqrlqqrv taimryavqn
      181 dyidsnpasd magalsttka rhypalpssr fpefltrlaa yrgrvmtria velslltfvr
      241 sselrfarwd efdfdkslwr ipakreeikg vrysyrgmkm keehivplsr qamilleqlk
      301 qisgdkellf pgdhdatkvm sentvnsalr amgydtktev cghgfrtmar galgesglws
      361 ddaierqlsh sernnvraay ihtsehlder rlmvqwwady ldanlhtkit pfdfakks
//
LOCUS       WP_284961270             441 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter, partial [Enterobacter roggenkampii].
ACCESSION   WP_284961270
VERSION     WP_284961270.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter roggenkampii
  ORGANISM  Enterobacter roggenkampii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Enterobacter roggenkampii"
                     /db_xref="taxon:1812935"
     Protein         1..>441
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          26..436
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,154,
                     157..158,161,267,270..271,274..276,279,306,310,360..361,
                     365,369,385,388..389,392..393,396)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mtysgkvdiq qviddsrfsg fhwllivlgf lvlaidgfdt aamgyiaptl saewgihkqd
       61 lgpvlsaall glslgaliag pvsdrmgrkr vlvfsclffg laslgtawaq slntltlwrf
      121 ltglglgaam pnaitlisef apqrcramai ntmycgfplg aagggaissw liphhgwrsv
      181 lltgaiapli ltlllalvlp esvkflvqrg kdimqvrria srfsrstleg vtgfflaeek
      241 vaskkgsvsq lfsmpwlpgt lmlwvtyfmg lviyyvllsw mptlmqgmgy alaesawlts
      301 lftfggtagi llagwmmdrw eahrvvaggf iltmglilll giehnhialf ggliflmgia
      361 mngaqsgmqt laatfyptec ratgiawmqg igrfggvagt mtsaqllsmq wqadsilmil
      421 svpallaaaa tvykmrhkgs a
//
LOCUS       WP_284961403             580 aa            linear   BCT 25-DEC-2024
DEFINITION  IucA/IucC family protein [Enterobacter roggenkampii].
ACCESSION   WP_284961403
VERSION     WP_284961403.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter roggenkampii
  ORGANISM  Enterobacter roggenkampii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Enterobacter roggenkampii"
                     /db_xref="taxon:1812935"
     Protein         1..580
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65632
     Region          15..577
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mrallraagt dvaaqcflna llretkdwry lpatdadals eihiplsqtq alrvpvryfs
       61 ptqhhqyrfp atriqsnsdr gdavtfpqlv dlilekpsvk gsldadtlar fkqrvlesha
      121 htwqaidlrh swatlrdkpl tfaeaeqall vghafhpapk shepfneaea rrylpdfasr
      181 fplrwfaves tlvagdslnv slrerllrfa aqsapellgh ftdtrwllpm hpwqadylle
      241 qdwcqrlaen gslqdlgeag aqwlptsssr slysetnsdm ikfslsvrlt nsvrtlsvke
      301 vkrgmrlarl akterwqelq aryptmrvmq edgwaglrde sgtiqeeslm alrvnllfdt
      361 pdtqtnvlvs ltqaapdggd sllaaavrrl sqrldlplaq aarcwldayc drvllplfsa
      421 eadyglvlla hqqnilvemq qdfpvgliyr dcqgsawteg adawlkeage tevenrfget
      481 qllryfpyyl llnstlavta alaaagfdse eslmsrvrda laelrrtakq trcldyvlds
      541 ptwnckgnfl cylhdrnent iadpaviyfd fsnpfykekt
//
LOCUS       WP_284961531             420 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Cutibacterium
            namnetense].
ACCESSION   WP_284961531
VERSION     WP_284961531.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium namnetense
  ORGANISM  Cutibacterium namnetense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Cutibacterium namnetense"
                     /db_xref="taxon:1574624"
     Protein         1..420
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=47525
     Region          59..419
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mtqaprqnlt vrralhwvag gmvaaqiati aglvtfngik rrgrrpyrfp tapveplkvs
       61 dhqveiftfg rdlyaamiad iesaqhtvyl etfiwkndei grrfrqalve aaargvavya
      121 mwdtfanlvv gprffrqleg vqaraqpllt pswiptlrnl grdhrklliv dskiayiggy
      181 nigalyadrw rdtharitgp avgelesvfv dmwnqrpkga lisrrnqpvl pspgvrywdt
      241 pfavhrnspr mavypirnmy leaidraser iwmtqgylip dddvvaalhq aasrgvdvri
      301 vipaesnhvi adwlsrgyyd rllhrgvrlf lyqgamvhak tctidgiwst igtanldrls
      361 lqgnyevnva itdstvaqrm aeifeidman cveltldewq srshvaklte allslwrpff
//
LOCUS       WP_284961673             642 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Citrobacter portucalensis].
ACCESSION   WP_284961673
VERSION     WP_284961673.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 642)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..642
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=72612
     Region          3..633
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mnrilagiif flfistgyis flvherqqel qklthytdsw saaqlvsqyy rfesllglyt
       61 iddtmnlddv rmrldimlsq sdlikegdlg ryiesniahr elavklentl sfldvnlekm
      121 nrlalqaylk kmhtldaplg rlssgalnkd vnsinnanqk iqtlyyiysa tsvlliilsa
      181 ilgvlifyqn rnilrahlqv kslaeelqks keklqmqnak leydvyhdsl temnnrqlfw
      241 sdlnktiera eknhdsvtvm lfdldrfkev ndtyghdagd mllrqisdrl vsmsltsdtl
      301 yrlggdefaf lssgltesha vsraqkicef isqpytiynt iinittcvgi visdterrsd
      361 ylykfadlal yeakgegsgk ikvfrqrmle klqesrtleh dmalaivnke fvvyyqpivd
      421 sfsqeiysye alirwlhplk gllspdnfip vaektgmine mgkavleiac reaacwevpa
      481 kisvnvspvq lsskafvgiv lsilketglp adrlelevte ssiftesttp mntlnklram
      541 gvkisiddfg tgysslsrls rlafdkikid ksfvhsistq edalniikli tgmakslnmk
      601 avaegvetqe qlkslqalgc dfaqgylfgk pqpcidekir ng
//
LOCUS       WP_284961674             319 aa            linear   BCT 25-DEC-2024
DEFINITION  YbgA family protein [Citrobacter portucalensis].
ACCESSION   WP_284961674
VERSION     WP_284961674.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007153
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..319
                     /product="YbgA family protein"
                     /calculated_mol_wt=36144
     Region          69..315
                     /region_name="YbgA"
                     /note="Uncharacterized conserved protein YbgA, DUF1722
                     family [Function unknown]; COG3272"
                     /db_xref="CDD:442503"
ORIGIN      
        1 mntqpvigis gcltgsavrf dgghkrmgfv mdelaqwvtf kpvcpemsig lpvprpalrl
       61 vqtaqgnvri cfshapgedv tdkmsdftns ylqglgglsg fivcakspsc gmervrlyde
      121 kgnrgrkegt glftgalmet ypwlpveedg rlhdpvlren fvervfalhe lnrlranglt
      181 rhgllnfhsr yklqllahhq agyreigpfv aslhqwddld affvvyrekl mtilkkpasr
      241 knhtnvlmhi qgyfrerlnt rqrgelrdii lnysggllpi lapltllkhy laeypdsyll
      301 tqnyfdpypn dlalrlmik
//
LOCUS       WP_284961829             732 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Citrobacter portucalensis].
ACCESSION   WP_284961829
VERSION     WP_284961829.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 732)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 732)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 732)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..732
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=79489
     Region          75..732
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mdntktyall mrktvlaati galsgtvnaa etpteaeeti vvqaaersdf kpggdtllpa
       61 fldgqvangg rlgmlgqqna mdvpfnvisy tsklvedqqa ktvadvvand asvqavqgyg
      121 nyaetyrirg lkldgddmtf gglsgvlprq vvdtqmidrv eifkgangll ngaagsgvgg
      181 minlepkhad dtpitrlgmd ytsdsqvgts ldagrrfgdn nqfgarvnll hregvgavdd
      241 dkrrttlasl gldyrgdrfr ssldvgyqkk tfhggnmgin vyyvpfvpdl pknthnysqr
      301 wgysdienef gmarteydlt enwtayaglg aqhaheigly sapeiynqag dakagrldtn
      361 riidafsgma glrgnfdtgf vshkvnvgys avtkedkiaw rmgsraarpd vniydtqnvp
      421 kpavtatggn ysdpltsgrt rsqgwllsdt lgvlddqllf tvgarhqkvv vrdynketga
      481 envknsfdds rwmptygvvy kpwqelslya nhteslqpgs tapssavnyg qstgiihakq
      541 nevgvktdfg rvggslalfe ikmpvaqlds qtryyainge qrnrgvelnv fgepmlglrl
      601 nasatwldat lsknqngvnd gktaigvpdf yavlgaeydi kpveglsata rlnhsgaqya
      661 naantkklds fttldlgvry rmslnqnqnq milragvdnv tnenywsgid dtgtylfqge
      721 prtlkvsvsy df
//
LOCUS       WP_284961869             692 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Citrobacter portucalensis].
ACCESSION   WP_284961869
VERSION     WP_284961869.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 692)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 692)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 692)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 692)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..692
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75912
     Region          145..679
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mshtlalhpv kkrdaiflwv llgwlafall pswsldygll estreeilaa ygwsqfnisw
       61 lwyllpslll vrpfhearre qrsrhyldag waffcmafiv asatlegrgl gyativlfva
      121 lgaimtlalt rlewlggdrf vigsltaiva livifivwps iaifipmftn dagefaplaf
      181 mnvlsqahii qvilnsimls iavgvgctff glvlaiyttr iarrsaiigr ifsilpivtp
      241 pfvvglgvtl mmgrsgyite fmvewfgltn tnwlygftgi wlaqvlaftp mafmildgai
      301 ktihpsleea sytlrasrwq tfngvfvpll kpalanafli vvvqsladfs nplvlggnfd
      361 vlatqiyfyi tgsqldyqaa stlgaflllf sllvfcvqym wigkrsyvtv sgksyrgdvq
      421 plpvtlvwsv vallavwiaf nallygsify gsftvnwgvd ytltlanftk lfgqgmsdga
      481 wpslldtlly agiaapitai fglliawivv rqqfkgkkti efttmlcfav pgtvagvsyi
      541 lafnsapvyl tgtaaiviis mvmrnvpvgi ragiaglgqi dksldeasls lragslrtit
      601 hillpllrpa ilsaliysfv raittvsaiv flvtpdtrva tayilnrved geygvaiayg
      661 silivvmlai ififdwlige srtsrskakn qa
//
LOCUS       WP_284961893             774 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Cutibacterium acnes].
ACCESSION   WP_284961893
VERSION     WP_284961893.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 774)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 774)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 774)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 774)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..774
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=86225
     Region          54..774
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mtddsvygpy gsgkgtlgkp kpgqqrpqpr mrmrerivrw gtpkppaptq svtdplisvv
       61 lanhpkadta iierayrtae hyhrgqsrks gdpyithpla vtmilaelgm dertlcagll
      121 hdtvedtsyt neqltadfge eiallvdgvt kldkvqygds akaetirkmv iamsrdirvl
      181 vikladrlhn mrtlgflrpd kqnriaketl eifaplahrl gmnaikwele dlcfstlnpk
      241 lydeivhmva erapqreaql kdvitivrqd ldeagikaiv ygrpkhyysi yqkmvvrgrd
      301 fsdiydltgl rilvdtprdc yaalgvmhvr wnplpgrfkd yiampkynmy qslhttvlgp
      361 ggqpvelqir themhrraey gvaahwkyke npnavgrgiq pdgtdlswvq slnqwskees
      421 dpsgfldslr feinsrevyv ftpkgdvmsl pqgatpvdfa yavhtevghr cigarvngkl
      481 vtldtklnng dvidiltsna pdaspsrdwl gfiasprars kiksyftker reesieagkd
      541 aiakqlrqag vplqslltve yltavaddlr vpginalyaa vgehnasaqs vveklialgg
      601 gpeeatadve eelavgvkap rrrrssetgv mvdgdpdmlv klarcctplp gdpimgfvtr
      661 ydgvsvhrtd csnaknlleh perivsvsws ddrqesyqvt iqvegldrag llvdtfrvfa
      721 eqgvsvisan mstskshlar lrltfeapdp thlkhltesi rrisgvydvf rvks
//
LOCUS       WP_284961922             427 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter portucalensis].
ACCESSION   WP_284961922
VERSION     WP_284961922.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..427
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=47922
     Region          3..398
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 msgyptgven hggtlriwfi yngkrvresl gvvdtaksrr iagelrasvc faiktgafdy
       61 arqfpqspnl kkfnisppgi tvaelaakwl dlkrmdltln ahlryvsyit igadilgggr
      121 mvdsithedv lnvrkelltg yqicgahqkn rsakkgrtvr tvnvyvtcmk gmfdfavlng
      181 yiskspfaav tplkksksdp spftrdeyhr flekcpceqi rnlwklafnt gmrhgeical
      241 awedidtknw tirisrnlai sdhftppkte sgnrtinltt paiealksqm aytrmgkqhq
      301 idvhlrefgr trqdectfif vprltarngk ggewyspgsf sgtwnnilrr sgiphrksye
      361 srhtyacwal sagvnpnfia aqmghtsaqm vysvygkwms dnndnqlail nanfggdapq
      421 mphaqne
//
LOCUS       WP_284962174             222 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Citrobacter
            portucalensis].
ACCESSION   WP_284962174
VERSION     WP_284962174.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..222
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25785
     Region          2..>181
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 miisrlvsge tlfirklate fgvsertlrr dfrerlmyld ldyyqgqcsl rsdihstrqe
       61 idiltfahrt glagvfpgfd rrlvsslldc ddrpclvwhq drphppagkl sfyrlvrais
      121 gcqritilte gerheavapy rlialdgywy lvaehnrqlr vfrldeihlv rpsretfirs
      181 ellhqlsedk hfisalphfr fiqqslnsfs psesrgqsgq td
//
LOCUS       WP_284962358             709 aa            linear   BCT 25-DEC-2024
DEFINITION  GumC family protein [Citrobacter portucalensis].
ACCESSION   WP_284962358
VERSION     WP_284962358.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 709)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..709
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=78120
     Region          7..681
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mklsivengk kressvefsr fakelkknaw kialagivag vvayplismm sskyvstatv
       61 likaqadnvs pfpqvdgfds trsgyyetqy almhsrivle qavrdmklde npeftgekag
      121 aqgadsnesr qlrmeqalkt laknlnvigi rttnlasity estspqvaad iangvaqafi
      181 nytveqkrlk vekarelnfe kmeeiqksia kqkdemdsyl knaglltfrg idgfeteqls
      241 ivtnrladat qrrvaaesvy nevngggksi esvislpsvs nhaqiqdlri aliqaqrtls
      301 eqrkvygpkn pailkaeadv qsiqsqtgrv lgelkvglrq qylaaladek nyqqqvdeqk
      361 eifqkmaskr dvwnsqklsl dkmedlyksl yqrtqelsls gvnadavlyd pavpalkpak
      421 pnksllllmv vmlvvvfcim yfivkaamdn sigtlsrmkk rlnvvplgei rrfsgtsgra
      481 qvrdmimknp lnadivhgir trimldrrpl qtlavasteh gdgrsllanl lansfsfdqk
      541 tllidadffn tggltselas atsaglaell rgeaeleqar iklsdnldfi phgkntissl
      601 lmlssehvel lmrelkshyq riiidvaavn qsqdvqlikr avdgvvfivk agvgsagqia
      661 naldkieenn gvvigavlna veekdletqe glrslnfstd qlmatpgrv
//
LOCUS       WP_284962719             418 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Enterobacter ludwigii].
ACCESSION   WP_284962719
VERSION     WP_284962719.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter ludwigii
  ORGANISM  Enterobacter ludwigii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Enterobacter ludwigii"
                     /db_xref="taxon:299767"
     Protein         1..418
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=47334
     Region          2..407
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 malsdvkvrs akpeakaykl tdgdgmvllv hpngskywrl ryrfggkekm lalgkypevs
       61 ladararrde arkllahgvd psenkkavkv eqeqetitfe vvardwhasn qkwsashsar
      121 vlkslednlf aaigkrniae lktrdllvpi kavessgrle vaarlqqrtt aimrfavqsg
      181 lidynpaqei agavatakrq hraalelnri tellhridhy sgrpltrlav eltllvfirs
      241 selrfarwpe vdfetamwti pgereplegv khsqrgskmr tphlvplsrq alvilekikc
      301 mngnrelifv gdhdprkpms entvnkalrv mgydtktevc ghgfrtmacs sliesglwsr
      361 daverqmshq erssvraayi hkaehlgerr lmlqwwadyl danrergisp ygfgkini
//
LOCUS       WP_284962732             252 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Enterobacter ludwigii].
ACCESSION   WP_284962732
VERSION     WP_284962732.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter ludwigii
  ORGANISM  Enterobacter ludwigii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 252)
  AUTHORS   Khuri,S., Bakker,F.T. and Dunwell,J.M.
  TITLE     Phylogeny, function, and evolution of the cupins, a structurally
            conserved, functionally diverse superfamily of proteins
  JOURNAL   Mol Biol Evol 18 (4), 593-605 (2001)
   PUBMED   11264412
REFERENCE   7  (residues 1 to 252)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   8  (residues 1 to 252)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18598964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Enterobacter ludwigii"
                     /db_xref="taxon:299767"
     Protein         1..252
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27836
     Region          1..242
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          18..98
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
ORIGIN      
        1 mntdfrpnnv vsfetllhpg gyhtpwhshq sgqlwrittg llvvetasgr svvpaqhigw
       61 ippgqehaaf sgsaidgrai yldpagceal pgettlfepd eltsalfsrl naegsgydpr
      121 kltllldela rgrqvryllp mpadprlkkv ashlmlrvdd nqtvehyasl agmsvrtfhr
      181 rfsaetgmnv vnwrqlarvm ramewlaagk pvgwialscg ynsisafiev fraftgktpg
      241 qwalkealsv rr
//
LOCUS       WP_284962830             262 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Enterobacter
            ludwigii].
ACCESSION   WP_284962830
VERSION     WP_284962830.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter ludwigii
  ORGANISM  Enterobacter ludwigii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Enterobacter ludwigii"
                     /db_xref="taxon:299767"
     Protein         1..262
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29297
     Region          1..262
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mkiatqnqaf fptsilekfq yikamgfdgy eidgkllvdn ldevkaaita tglpvttacg
       61 gydgwigdfi eerrlnglkq ierilealae vggkgiivpa awgmftfrlp pmtsprslag
      121 dceavsaslr yldevaartg ttvyleplnr yqdhmintls darryieena lrhvqiigdf
      181 yhmnieedsl tealhrnrdl lghvhiadnh ryqpgsgtld fatlfgqlca dnyqgyvvye
      241 crvraddpaq ayqdsltylr ec
//
LOCUS       WP_284962846             517 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Enterobacter
            hormaechei].
ACCESSION   WP_284962846
VERSION     WP_284962846.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..517
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56378
     Region          20..498
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mkikliaagi lttlpfwaca kdvtilytnd lhahvepykv pwiadgkrdi ggwanittlv
       61 keekskskat wffdagdyft gpyissltkg kaiidimntm sfdvvtignh efdhgwdntl
      121 lqlsqakfpv vqgnifyens sklfwdkpyt ivekdgvkig viglhgvfaf ndtvsaatrv
      181 gieardeikw lqryldelkg kvdltvllvh egtparqssm ggtdvrrald kdiqtasqvk
      241 gldilitgha hvgtpepiki gntlilstds ggidvgklvl dytkphqftm knfelktiya
      301 dewkpdpqtk qvidgwnkkl dkvvqqtvaq spveltrayg esaplgnlaa dallvaagkn
      361 tqlaltnsgg irneipsgai tmgdvistfp fpnelatmdl tgkqlrtlme haaslsngvl
      421 qvskglevky dsskpigqrv vvftlngkpi edatvyhiat qsfladggdg fttftegkar
      481 nttggyyvsn avidyfkagn titdeqlngm rvadvkk
//
LOCUS       WP_284962978              99 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Enterobacter
            hormaechei].
ACCESSION   WP_284962978
VERSION     WP_284962978.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..99
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11151
     Region          6..>52
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(10,14,39)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(13,38)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(20..21,32,35,39..40)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 msisqgeklg lirdserlsk rqltdlvgln ystyvgyelg rtkmtlesai klfghprfhk
       61 yqdwfmydri dpsrgqiapa lahygqettq sdpsgkqig
//
LOCUS       WP_284963701             356 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Enterobacter roggenkampii].
ACCESSION   WP_284963701
VERSION     WP_284963701.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter roggenkampii
  ORGANISM  Enterobacter roggenkampii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Enterobacter roggenkampii"
                     /db_xref="taxon:1812935"
     Protein         1..356
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41059
     Region          12..340
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mlelilskqp nsthmtkhfs aadgirgvac livvilhnvs kylptigqyt kgcekygvwi
       61 fftlsaflls iklmnkkptf peyakyiisr ffriippfvv avftyyymdy mnyqkmidti
      121 sfnssyfhfw tipvefkfyf tlplflisfl vadkikgimg ggtllfllil lvqnaypyni
      181 tiensiqtlp ylsvflfgvf savlhcrhni kvsnamgdsi ilfiisilfi ispgvienvf
      241 rfqpidlmnk yvflgilfti lifilcntsg ysavffsnka frfigkysfs iylyhwlflt
      301 nnqniyggpv etifantims ialgmlmfyl cetpmnyirk sienfafkrk eispqt
//
LOCUS       WP_284963776             246 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor, partial
            [Clostridioides difficile].
ACCESSION   WP_284963776
VERSION     WP_284963776.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 246)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 246)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 246)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..246
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
     Region          10..236
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 nkklykgcnm iniiicegkk servilndyi ntffynynfe ynikefengg dllkkypnnv
       61 diifmdidln dengfnvske ikkfdesvri ifvsssnkyi kkgyeigvyr ylekplkysl
      121 fkeaissylk ecykneails ikckckiyfi kvddilylev lkndltihte kgiytfkssm
      181 keiesnleeh nffrchksyl inlmkvnmld iennivfinq nsiivsryki kllreklnsc
      241 lvdvii
//
LOCUS       WP_284963779             294 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284963779
VERSION     WP_284963779.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..294
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <16..292
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 gytfrelnvd vgryqiqiir nidsemnslr qltsvliigi lisviityfv avyltrkali
       61 pietawknqa kfiqdashel rtpitivssk lesmlkspes tvndevetia tamketrrlk
      121 kmitdllslt kedsivkvnl eeidleklle eisedyidia efqekrfvfn sklknkviit
      181 dknklrqlil ifidnafkyt klgdeialel kediedevtl lisdtgigik keeiplifdr
      241 ffrsenvrnk dlegsgigls iarmislnls idinvtsdvd igttfelsip kklk
//
LOCUS       WP_284963830             148 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284963830
VERSION     WP_284963830.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..148
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <2..145
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 kinlvslvrd iiidilndnr yknrniefes nedlievyvd silfrraitn lifnsivhns
       61 egtlisveiv kkdnieiiik dngigisksd lkhifkkyyr gtntgemhkg sglgmaiske
      121 iieihkgkiy vsseigigtk iiieikqn
//
LOCUS       WP_284963853             374 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Enterobacter hormaechei].
ACCESSION   WP_284963853
VERSION     WP_284963853.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..374
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40019
     Region          26..366
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,151,
                     154..155,158,195,198..199,202..204,207,234,238,288..289,
                     293,297,313,316..317,320..321,324)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mtysgrvdiq qvidespfsg fhwllivlgf lvlaidgfdt aamgyiaptl saewgihkqd
       61 lgpvlsaall glslgaliag pvsdrmgrkr vlvfsclffg laslgtawaq slntltlwrf
      121 ltglglgaam pnaitlisef apqrcrxasr farstldsvt gfflaeekva skkgsvsqlf
      181 smpwlpgtlm lwvtyfmglv iyyvllswmp tlmqgmgyal aesawltslf tfggtagill
      241 agwmmdrwea hkvvacgfvl tmglilllgi ehnhialfgg liflmgiamn gaqsgmqtla
      301 atfyptecra tgiawmqgig rfggvagtmt saqllsmqwq adsilmilsv palvaaaatv
      361 ykmlysrsqe pgva
//
LOCUS       WP_284964108             303 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Cutibacterium
            namnetense].
ACCESSION   WP_284964108
VERSION     WP_284964108.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium namnetense
  ORGANISM  Cutibacterium namnetense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Cutibacterium namnetense"
                     /db_xref="taxon:1574624"
     Protein         1..303
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=31892
     Region          5..303
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mqtsqprkva vvhnsvktqh npawrdlier kcrehcgvtp lflpttaddh gqgqacravd
       61 qgaelvlalg gdgtirqvaa glantgipmg ilgmgtgnll arnlelphtn laasldaalt
      121 rpvraidlgy vrfdeseeic ftviigmgid aqtmagtrdr lkdkvgwlay aasgaltlvq
      181 pgfqasasvd grrpvvtrar tvlvcncsll pggvvlvpgg riddgtldvl tlsphgivgw
      241 vavfnhlvtr hrhghrlvrh atsrtalvts gsgpilaevd gdpmgtvttm rtrvapgall
      301 vra
//
LOCUS       WP_284964181             482 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Cutibacterium namnetense].
ACCESSION   WP_284964181
VERSION     WP_284964181.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium namnetense
  ORGANISM  Cutibacterium namnetense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Cutibacterium namnetense"
                     /db_xref="taxon:1574624"
     Protein         1..482
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50781
     Region          1..435
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 msshdqlvae lsarwpehri gpgldreqav ldllgnpqqa cpviqiagtn gkgstaimid
       61 sllrsaglrv grycsphlvd vtericidgr pishdlfdet wrqiepmvdl vdaqridgie
      121 mtffevmtam afaafadapv dvavvevglg grwdatnvah anvavvtpva mdhmhilgns
      181 idkiaaekag iikpgcapvi agqeseaapv llaqcadagv kpllegpdwg llnrrsavgg
      241 qvlrvqtasg plgelflpvf gehmahnaaq avaavealtg plqpaiieqg ltaveaparl
      301 evvrrsplvi ldtfhnphga asamagvres fevepliavv aamadkdidg vlavlsdtvs
      361 hlvvtsmpdl sralsvdela ekasshwdsd hvtcvadvpe aleeafriad syapgagvli
      421 agsvvlagra railrpdgtm ldapqtaive tpdlsedqvk ameghqlepl pdddmsdddg
      481 dw
//
LOCUS       WP_284964271             487 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Cutibacterium namnetense].
ACCESSION   WP_284964271
VERSION     WP_284964271.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium namnetense
  ORGANISM  Cutibacterium namnetense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Cutibacterium namnetense"
                     /db_xref="taxon:1574624"
     Protein         1..487
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51517
     Region          4..487
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mtqtatessa ttrtgiettg ieiieesqrt aqprdlflpw fasnvsvfgm sygafmlgfk
       61 vsfwqamaat lvgvivsfgf cgiiaiagkr gsaptmvlsr aafgtqgnki pgiiswmtsi
      121 gwetslaita vlatttifhr lgwssgssvk icativvall ivggavagyh iimklqavlt
      181 witgvltviy lvmaashidw hattslpcas vpafvgaltl vmtgtglgwt niaadwsryq
      241 srtspgfaia fwnvfgaslp livlitggll laassknlsd aigadpvgal atilptwfli
      301 pfllaailsl lagaingiys sgltlltlgi rvprpaasli dgtiltigtl yvvfvapnft
      361 spfqsflvtl gvplsgwtgi mmaditlrhr pydeadlfng sgrygrfdlt siitfvvvtv
      421 igwglvvnty eganwnnwqg fllgpiglgg rqgdwayanl gvfgalvlgy vvtliarrgk
      481 vrrqesr
//
LOCUS       WP_284964433             423 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Cutibacterium namnetense].
ACCESSION   WP_284964433
VERSION     WP_284964433.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium namnetense
  ORGANISM  Cutibacterium namnetense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Cutibacterium namnetense"
                     /db_xref="taxon:1574624"
     Protein         1..423
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45589
     Region          6..419
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mlglmsealq lrratlsngm rvvinpdmts pgvavniwyr vgsadeeagh fgfahlfehl
       61 mfsgttsgia ssehlaties vggsanasts fdrtnyfetv pagalelalw leaerlahla
      121 vteenlatqr evvkeekrqr ydntpygdll dllldgrfgn ehpyghptig svsdldaacl
      181 ddvtafhstw yrpdnavlvi sgcvdadegl tladkylgav ptatgnlper vqgpirhdnp
      241 rvvvtrplpr tavtrawatp pitdpdnlav amaadvlgsg mssrlirtle rkrhlvdgvg
      301 msdfglarga satlisahlk prvceeeltg avdeiitela tngpsqaele raraqvergw
      361 leslaivder adllnmhetl lgdatlvnty ldriravtgd qvagatqrwl apaqastvvh
      421 qea
//
LOCUS       WP_284964437             440 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Cutibacterium namnetense].
ACCESSION   WP_284964437
VERSION     WP_284964437.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium namnetense
  ORGANISM  Cutibacterium namnetense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Cutibacterium namnetense"
                     /db_xref="taxon:1574624"
     Protein         1..440
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=46949
     Region          173..402
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 msvvertavs pldrqtvasr atsgvwlgav aavlvmrlpm gfllflivpw vilavqtrfp
       61 srlrvaplaa vevccmvasg vavtlfhpsl ladtgnsafi mlavigttlv vfrsaepgrt
      121 arqvlsglyw gailvwligm geivtgikll pllypeantl gavsksrwiv tatypnyndy
      181 gvvmamlfta vlarlwfnpr ggairlgrlf vlvtclamil iggsrgallg cicavillfv
      241 lnvrrlhtaa mgvraffwgg alvlvlgagl wtspyvqdhs taergtiman alsmtlsdpv
      301 alllgygsls eyqarasalf ggvlmdphnl lleiilrygv iamilfvvcw lwilvrgflp
      361 rrpaadwqta fgltvvmlfp algvvpsstl ryhvtwlylv aascitaetv aangtgrpvl
      421 apdpdaeaht krsaggpgta
//
LOCUS       WP_284964308             604 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase, partial
            [Clostridioides difficile].
ACCESSION   WP_284964308
VERSION     WP_284964308.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>604
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
     Region          31..492
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mkirrylilv iiilittsqs fisyglerfe eitifhtndi hgryaegddh iqignlatlk
       61 ketpnsilvd agdclhglpi vnmdrgksai elikcagydy itpgnhdfny gkdrlfelsk
      121 sanlgentlk flssnifeng kkvfdsndik eidgikigff glstqetksk tgfknvegle
      181 fknpiesate qvnelkgkga nvivaichig tnslskpnsi dianevqgid liidghshtk
      241 fengkqvgdt livsagqyle nigeikltld tndvedikie nksarligke ealkykldsa
      301 vskkvdkike qqekildkvi gvttntldgs yenvrtketn lgnlisdill dktkadislf
      361 nggnirdtie kgnitrrdiv dvfpfsntiv tkeltgaqik dvlehgvkly pekssaflqv
      421 ggisyyfnpk qkegekitni qkegkpldln kkyvvatndy iasggdefpc fskepvlkef
      481 gnlesaviey ieykkeiskn vdgrigiksk delisknhes dlilsenekn indneenlsn
      541 nikssdsdkn ksldktsare ssnlgiskre akekspktgd lgfsnsiiif ivsstlicll
      601 nfnq
//
LOCUS       WP_284964304             240 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Cutibacterium
            namnetense].
ACCESSION   WP_284964304
VERSION     WP_284964304.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium namnetense
  ORGANISM  Cutibacterium namnetense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Cutibacterium namnetense"
                     /db_xref="taxon:1574624"
     Protein         1..240
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26031
     Region          6..213
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mgvgtlypla riltrfdhhg genlpgpgpa livsnhisny dpvvlgaflv angrwphwla
       61 kkelfsvpii gwvasasgqi pvdrkgpnpa kvlhdakaal dkgmtvvmyp egtitadplh
      121 wpmtgrtgaa rlaletgvpv ipvgqwgpqe vmgykemtfp klvprktmtl ycgtdvelsd
      181 lrgrrdlasv reatnrimda idaqvararg efpppdrydm rkgtrvpksi aparpvvdph
//
LOCUS       WP_284964475             476 aa            linear   BCT 25-DEC-2024
DEFINITION  protoporphyrinogen/coproporphyrinogen oxidase [Cutibacterium
            namnetense].
ACCESSION   WP_284964475
VERSION     WP_284964475.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium namnetense
  ORGANISM  Cutibacterium namnetense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Pawelek,P.D., Cheah,J., Coulombe,R., Macheroux,P., Ghisla,S. and
            Vrielink,A.
  TITLE     The structure of L-amino acid oxidase reveals the substrate
            trajectory into an enantiomerically conserved active site
  JOURNAL   EMBO J 19 (16), 4204-4215 (2000)
   PUBMED   10944103
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440906
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Cutibacterium namnetense"
                     /db_xref="taxon:1574624"
     Protein         1..476
                     /product="protoporphyrinogen/coproporphyrinogen oxidase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006779 - porphyrin-containing compound
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=48993
     Region          8..476
                     /region_name="HemY"
                     /note="Protoporphyrinogen oxidase HemY/PPOX [Coenzyme
                     transport and metabolism]; COG1232"
                     /db_xref="CDD:440845"
ORIGIN      
        1 mntsdpqhvd avvigggmag lvaawqftke glhpvliesr gytgglvags tlagisydig
       61 aegwairlpd tadlaaelgl tvekpasaps wvysddacfa mpdnailgip adlsdpavvi
      121 algaqeaaha aeldhapmpe dlprdlgtlv asrmgpqvlr rlvtpiaggi haadphllsa
      181 dvvapglraa aqatrslaag valcrsrmpa gpaiasvagg mftmpaelrr qaeqagattm
      241 trvgarglar hgdlwlveta etsrnpnpsl ppspdgaihs fltprvvvac sagpatrlls
      301 svidtvgpem vpgapighvn lavqapelds sprgngmlva pgtttvtaka lthmsakwps
      361 laescpqglh llrisygrsr eenvalsvdq aladasvllg eelsaeqvvd sqiihwtgsl
      421 apttpqtraw rdglhhqlea lnqsgrgkig lvgawasgsg iaalvpqarr tvrqlv
//
LOCUS       WP_284964491             279 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Cutibacterium
            namnetense].
ACCESSION   WP_284964491
VERSION     WP_284964491.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium namnetense
  ORGANISM  Cutibacterium namnetense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Cutibacterium namnetense"
                     /db_xref="taxon:1574624"
     Protein         1..279
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30149
     Region          6..256
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mgdlsmlsln tatakyasla ecasacaeag lgwigpwrnr iqevgsadaa kiisavglsv
       61 stvcrggfit atepdsrsra iventraiee aealgarelv mvvgglpagd knlvsarerv
      121 aqrlgdlvpi ahnhgvrlal epmhplftad rgvlttigqs ldiaeqfepe evgvvidtyh
      181 iwwdpdahes ieraghqgri styqicdwil pltantlnsr glsgdgyidf ptitrwvsea
      241 gytgpvevei fnenlwiqpv rqivdaisar yvdlvepyl
//
LOCUS       WP_284964581             333 aa            linear   BCT 25-DEC-2024
DEFINITION  proline-rich domain-containing protein [Cutibacterium namnetense].
ACCESSION   WP_284964581
VERSION     WP_284964581.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium namnetense
  ORGANISM  Cutibacterium namnetense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12172186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Cutibacterium namnetense"
                     /db_xref="taxon:1574624"
     Protein         1..333
                     /product="proline-rich domain-containing protein"
                     /calculated_mol_wt=35900
     Region          <227..323
                     /region_name="Pro-rich"
                     /note="Proline-rich protein; pfam15240"
                     /db_xref="CDD:464580"
ORIGIN      
        1 mfmlsvsrhm rrclvlvlap llllagcvkf dtameikden hihlkstvgv sksiasaysd
       61 rlatelsncn nsmgsagtgs gnkiekfedk dyvgcivagd ttaadlnkdr gmqatfdkke
      121 vsfrmtsdlf rdggrsdqai dasmfsdfkv svtfpgkvls hsgsskvdgn tvtwtdpkdl
      181 fsssgltats krsngiptwv wivvalgvla iigvvvvvln keknhkpgqp dnggvpwtmq
      241 ypgdgqplgq pqqwngqpyq gdphvqppyq ypnqyprqqg pgqpwanqsw dtasgdatna
      301 pqagpnptph qgsqpgqqtp sdpddfwknh gsh
//
LOCUS       WP_284964588             420 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Cutibacterium namnetense].
ACCESSION   WP_284964588
VERSION     WP_284964588.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium namnetense
  ORGANISM  Cutibacterium namnetense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Cutibacterium namnetense"
                     /db_xref="taxon:1574624"
     Protein         1..420
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44331
     Region          27..269
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(36..37,39..40,43..44,81,85..86,89,93,138,142,149,
                     152..153,158,171,175..176,178..180,182..183,186..187,
                     190..191,210..211,213..215,217..219,221..222,224..225,229,
                     232..233)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(174,178,181..182,184..185,224,227..228,230..235,238,
                     240,242)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(195..201,212,215..216,219)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 msrlvtrtpd pvveiavasa pdntktvhpw swwawaagcg iaisltnnpl lvvlitgava
       61 lvvalrrtde pwaqsagvya gmaltvliir vffqilmgan grgtvlfrlp evslpdwaag
      121 irlggpvtae glaatsydal rlagmlacfg aanslanprr vlksvpaalh disvavvial
      181 svfpqliasa qrvqrarrlr gdtrtgigtl aavlvpvled svemsmslar gmesrgygrt
      241 rdnrrvrpgt svllvvsvma ltlgcygvla nptgafaanp stcapgslcs wfladrmgqh
      301 igivliiagi igsviglris grrlqvsryr pdpwtwqata sclcgaavvv amiwlsrtsp
      361 kaitvstspv lwpplepaml llaitaalpg iftpapqrst qadpeqaasw tprkdevpqs
//
LOCUS       WP_284964810             351 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Cutibacterium namnetense].
ACCESSION   WP_284964810
VERSION     WP_284964810.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium namnetense
  ORGANISM  Cutibacterium namnetense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 351)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Cutibacterium namnetense"
                     /db_xref="taxon:1574624"
     Protein         1..351
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37966
     Region          35..339
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 msagttgqta gegrarrgdp grrspridpr evahahrlve aisrtfdskv vgqealrtal
       61 lvgliggghv llesvpglak tlaastlast vdasfsrvqc tpdllpsdii gtqvfnpgsg
      121 tfttelgpvh anvvlldein rssaktqaam leamqekqat igaktypmpd pflvlatqnp
      181 ideegayvlp qaqmdrfllk vivdypspad evemlrrlks gvlasrtvpp vvsrqdvlwl
      241 qnlarrvyvd eallryivqi vhatrhggdy lpqeqahcle ygaspratia fveaacahal
      301 ihgrdhvipd dvramrymvl rhrliltfea vatrvpveei idgifgavpt p
//
LOCUS       WP_284964868             347 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Cutibacterium acnes].
ACCESSION   WP_284964868
VERSION     WP_284964868.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..347
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36341
     Region          46..346
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtipaktktl tsttertssn shrrhhltai vfvilvaimi vsvitgigfg siqlspsdvv
       61 kglfgpsdfq whrvvwgvrf prvvlaalvg mnlatsgvil qavmsnplad psiigvssga
      121 gllgigtlli fperanlvpv mafigamlaa maiyalawrg gvqppriils gvavsalcga
      181 gisavmvlma dnvqgalmfm ngslamrswa evsliwpytv vgiiaavvls rrldiitlgd
      241 qvaqgmgmnv qanrlvltav aallaastvs aigllgfvgl ivphimrliv gnrhvilvpa
      301 cvlagaalvm lsytcsrvif dpfeipvgim ltalgvpffl fllrktl
//
LOCUS       WP_284964869             168 aa            linear   BCT 25-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Cutibacterium acnes].
ACCESSION   WP_284964869
VERSION     WP_284964869.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..168
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=17522
     Region          42..160
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 mgipssassg tpgadryrrl egfltmamrs gfldrrpvlv glvflggclg tlirsviaha
       61 wpsradgvpw gtlainlvga fvpatllell vhagpdrgvr ravrlcigtg llggfttysa
      121 ltveagqrvm sgqwlwgiay lltsvaagal lawvviaavr cvmgkrss
//
LOCUS       WP_284965069             602 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease, partial [Clostridioides difficile].
ACCESSION   WP_284965069
VERSION     WP_284965069.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 602)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 602)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 602)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18109159
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..602
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          <6..92
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
     Region          321..596
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 elntnaiill vgvfgaaavy sifhvsilqr isqygvlevl gannkqllfl lflelfllfi
       61 vgfpigcflg ievastiyeq fphiflssdi vpgaffisek siylgflfil llliliavrv
      121 vhqlnkyssi esmknfkitn kkkrilesvk hsnmtkvlsh kymtqkkgmf igilfslslg
      181 giiflcssys iqltknnnel tmkaddglns dyqitmqttd fdvgipkdki srlnnvegis
      241 kvypvrylfg amqikeeqlf wknffkplek dyriktffdg ictkqneggy llktniygyn
      301 ngmleglnsy iidgeinthd mvknnkvivr lpmdgtgmyd avdinpgdti kvkvpktmkp
      361 tdeivkfkee nkndyttkef vvaatvkrvm anniyfigdy gmdivmtngq mknnfdieny
      421 nsvsikkted snseelseni ksvvsdvkrc ivtdytiaie knntylnqkl lfiygivfvl
      481 laislfhiin tvsylifsrr hefgilramg itdnkfllmm iregflygfy asiimvigsv
      541 igqfmiyfmv krvylyinpi lkintplyig miilnitisi vaviipvrqi lksdiisein
      601 kn
//
LOCUS       WP_284965084             284 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Clostridioides difficile].
ACCESSION   WP_284965084
VERSION     WP_284965084.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..284
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33150
     Region          20..283
                     /region_name="COG4587"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443644"
ORIGIN      
        1 msnyneassn dsmfykfkqs irryyevaki nfkvqliwrf dvvvnmvfti vkilfayilw
       61 kaifgenkiv sgftfnsmls yyiissflag idmskstsee icnrvklgtf skymiipinv
      121 qnyfiaknfg mtcfyfvfnm isafvwifif kidfaftsnp vqilipilmi flgfifmmkl
      181 hffigilsfk fleisffkmi ienivefitg tmiplvllpe tivtvmkvfp fyyttylpsm
      241 lligrnsnea iqgliilalw vlffsvvnkv mykrmrtlfd gvgi
//
LOCUS       WP_284965088             680 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Clostridioides difficile].
ACCESSION   WP_284965088
VERSION     WP_284965088.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 680)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 680)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 680)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 680)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 680)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..680
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76571
     Region          1..>431
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 msilvtllgl lvcttistvf skkwsnipla iyqivlgiil silpfkfsfs fnpeifvici
       61 iapllfsegq nvsrkellel rkpilllafg lvlitvfagg ifihflipgm plsvsfalaa
      121 visptdlvav ksitqglnfp knmmsilege sllndaagvv afkvavlatv tgvfsieeag
      181 iqfmitafgg iivgsilgyi iikirlslhk wnleeipmvi viqimtplfv yfvaeeigvs
      241 gilavvmagi ahgiekehlq ntttklriis dntwyvleyv lngfvftllg fllpsiytgl
      301 ssknenmale ltfistlivl ilfvirfiwv ylwhnsfikp kknplnnffv gflgfkdeev
      361 vkesiskcky slivatcgvh gtftlatals ipfyladkdv fpmrdtvlfi ssevilislv
      421 latvllprll knnvqesepl lsdkeaykli lkeailklsn ekaqevqpvi hdlneqlvds
      481 ekgilntpdn klismmiaea dqqgllavlk lledgkisdr afklygfyit ksrksvqksi
      541 fkivklkism wiinrkvkke vkekitkivs enkeiikefh hayalstkta isfinkntde
      601 dnrhealiai rfynrylnwi trkiqnddkf earveyyrvm aiqsqrdsvq qlvetkqisr
      661 evakelleni lydemmmies
//
LOCUS       WP_284965089             307 aa            linear   BCT 25-DEC-2024
DEFINITION  C45 family autoproteolytic acyltransferase/hydolase, partial
            [Clostridioides difficile].
ACCESSION   WP_284965089
VERSION     WP_284965089.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   True,J.R., Yeh,S.D., Hovemann,B.T., Kemme,T., Meinertzhagen,I.A.,
            Edwards,T.N., Liou,S.R., Han,Q. and Li,J.
  TITLE     Drosophila tan encodes a novel hydrolase required in pigmentation
            and vision
  JOURNAL   PLoS Genet 1 (5), e63 (2005)
   PUBMED   16299587
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Tobin,M.B., Cole,S.C., Miller,J.R., Baldwin,J.E. and
            Sutherland,J.D.
  TITLE     Amino-acid substitutions in the cleavage site of acyl-coenzyme
            A:isopenicillin N acyltransferase from Penicillium chrysogenum:
            effect on proenzyme cleavage and activity
  JOURNAL   Gene 162 (1), 29-35 (1995)
   PUBMED   7557412
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Tobin,M.B., Fleming,M.D., Skatrud,P.L. and Miller,J.R.
  TITLE     Molecular characterization of the acyl-coenzyme A:isopenicillin N
            acyltransferase gene (penDE) from Penicillium chrysogenum and
            Aspergillus nidulans and activity of recombinant enzyme in
            Escherichia coli
  JOURNAL   J Bacteriol 172 (10), 5908-5914 (1990)
   PUBMED   2120195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF040521.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>307
                     /product="C45 family autoproteolytic
                     acyltransferase/hydolase"
     Region          12..307
                     /region_name="C45_proenzyme"
                     /note="C45 family autoproteolytic
                     acyltransferase/hydolase; NF040521"
                     /db_xref="CDD:468523"
ORIGIN      
        1 metlevrnie lsgtnyeigy rlgelvanmp eiiegqinks nlvskkeeke mielfdkycp
       61 glneelqgfa daiqvncnqi lyytmtylkp gcsqvalape ltenghvlfa rnfdfshnme
      121 dfvlcktkvn gkyahigtti mqfgrgegmn ecglgvsqss cgipvgnsdg lrkpaivglq
      181 fwavirylle nckdvdeale ylkdmpiayn inllladksg nialvetldg kkevniinsl
      241 eskreyflhs tnhthidklh kldpqsmkns ihryklikey inkskkigek elmnllssky
      301 pnglscn
//
LOCUS       WP_284965201             415 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Enterobacter hormaechei].
ACCESSION   WP_284965201
VERSION     WP_284965201.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..415
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=47289
     Region          70..380
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mriitnihar ygrvskldat epklkfepgf lyaeipyisg iqnrklsryv hfylmdkail
       61 qardlkplar aflrwirwle dngldpftpg alkyqsptyg freyllgavr qgriasstaa
      121 vyisvirrfy vflgkcgela assfftlvek vvdgrrkvis sdlairitst tkrtinplnd
      181 aevhildeal ksesglfslm ivlmkncglr ldemltlpss lfteeylasv pvseltirgl
      241 higprcgvht kfgmtrelfi trrlyeqvld ylsdeeyekk iqkwrarqgg egrheplflm
      301 angkrmseka fysrwysfrh rlarsapgnv frhkphdlra tfathflrsa lscypeqaan
      361 algtvkywmg hksenttmky ivflqqnqis davagvmdal idgaagrdga iyepe
//
LOCUS       WP_284965466             466 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284965466
VERSION     WP_284965466.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..466
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          230..466
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 hkpsyktvfh syiiffmifi cliltvigif lslitiqkpn gefirsdwpk kftenfneqi
       61 vfidnkpqvk qsgleklren qlwlqildss gnrvygflep kehkdyysns ellalanqnn
      121 ssngtvyfnt iknnkndyiy iiyfplnisk vnmffdggkf iggksivfsi igiifliilv
      181 sgiaygywvt kcisnitsav sdiskrsylp vnikgvfadi ynslnilnee ihksdeiqnk
      241 tdimreewis nithdlktpl spikgyaell tdsstnyspe kvykyasiml knieytntli
      301 ndlkltyqlk ngiiplnknn ydlvrflkel sidilnypey esnivefksn idninfdfdc
      361 tllkrafsnl ivnaftygdk ntkvcvhitl nerieiiisd ngkgmsreea snlfnryyrg
      421 intkqriegt glglaitkqi ievhggnisv esipglgssf yitfpi
//
LOCUS       WP_284965524             198 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator, partial [Clostridioides
            difficile].
ACCESSION   WP_284965524
VERSION     WP_284965524.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>198
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          1..>198
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mkinrlteii villnkklvt akeladrfev strtiyrdie tlsmsgvpvy mtkgkgggis
       61 lieeysinka ilskkdkesl ivalktlqat kypeinsvvn kigsifgeqn fsnwieidft
      121 ewgsnfnedd kftkikeail rcntinfnyv nslssqtnrt veplklmyks ktwylygfck
      181 lkddfrifri srirnlsi
//
LOCUS       WP_284965557             752 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Cutibacterium avidum].
ACCESSION   WP_284965557
VERSION     WP_284965557.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium avidum
  ORGANISM  Cutibacterium avidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 752)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Cutibacterium avidum"
                     /db_xref="taxon:33010"
     Protein         1..752
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77914
     Region          20..747
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mstlthsgtt pepdeetept svdlditgms cascaaritk klnkvdgvqa tvnyatskah
       61 vlttgpvsvh dlievveavg ygaampepaa ppedhaakir nklivavila vpvmllsmip
      121 alqfdgwqwl aialtlpvvf wcgagfhraa wtnlrhgatt mdtlislgsl aslgwsvwal
      181 vwgnagaigm rhhmtwalqr pdpssaiyle asvgvitfil vgrwiearnr aeagsalqal
      241 lqmgaksvrv vrdgqevtvp iealkvgdhf vvrpgekvat dgrvvegssa idaslvtges
      301 lpvevapedd vvgatvntsg rlvveatavg tdtelcrias lveaaqtsrs etqdladqvs
      361 sifvptvlai avltmivwgl lgqgvtaaft agvavliiac pcalglatpm allagtgrga
      421 rlgivikgar slerardida vamdktgtlt tgqmavtqvw desgravsis dnppvlgvaa
      481 aleagsehpi sravveacpg iapaedfral pglgvsgvvd glsaragrvs lfdaipdels
      541 knveqaqaeg rtvlvvgrgd dilgaiavsd eikpeaviav krllgagvrp vlvtgdnsga
      601 aarvaselgi devisevmpe dkvdvvkrlq adetrvammg dgvndaaalq aadlgvamgt
      661 gtdvaiaasd iictrgdprl avdalslaha tdrtirqnlf wafaynvvai pvaavgllsp
      721 viaaaamafs sifvvtnsmr lvrwhpevsd sn
//
LOCUS       WP_284965624            1404 aa            linear   BCT 25-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase, partial
            [Clostridioides difficile].
ACCESSION   WP_284965624
VERSION     WP_284965624.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 1404)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 1404)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 1404)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10594375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1404
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..1404
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
     Region          9..148
                     /region_name="SIR2_2"
                     /note="SIR2-like domain; pfam13289"
                     /db_xref="CDD:433090"
ORIGIN      
        1 ipiifgsgli ittnydkvle knyglhnktv lvshpghfea lnnalrnnel vlykihgdit
       61 epttsivltk eqyekaysnd elrkmltqvy tskellflgc slekdrplel lqqvseagtg
      121 hyaiipvsse kkkhrriele neyyiqtimy pegkhecvri ilerileivl pdeyrrlkdr
      181 slkesrltnl scrltekwfq nqnniqiknl gdrylpelnv elslentfna lgkneefkqr
      241 fdektdkvls sikkqkinev evdvlvieei iqqfydkane rldikllkkh fekisaaldd
      301 rinnfkniii nedcekskkr edeiyklkqt qkdiyvyiky ldskeikvvn spyillhsag
      361 gmgkshiiah tiekrnmdgh ksilflgqhf kldktpikhm leileiecef eelleilnei
      421 gekeqqrvil fidalnegqg kelwkyylng iveqikkypw iglilsirse yipslidnnn
      481 kikenlvfie hqgfssiehk amkkyfdyyg ipysnipmpn qefrnplflr imcetfkgee
      541 inldtisftd iyknylniln lrisescnys rhanvvtevl nemikykygd glgnnlipan
      601 ksveiiinia skykinnvii deliangivn ktvnlndeey mhvtyekled ylyanllvke
      661 lkeigvvdfs hkykylveye dilevlaivl seetgsdipn eifevfknke tnynvisafi
      721 nalkwrkkst itektldyin kivlgksyyk idfynvlili stkvnhtlna dyivkyilqn
      781 tmadrdaifi pifnevyeee essikrllgw cfdfegfdnt snetirlsam miatflissn
      841 rdlrdkstka lvnlltgkmd ividllktfe dvddpyiier lyavafgcvv seqseemiea
      901 lavyvynkif dvdyvypnil lrdyaknivd yakykidssv lkdmnveppy ksifpkvptd
      961 eeiegykydy kasdfkdyyw sqntilnsme veytrdgqpg wygdfgrymf qhyfhkwkgl
     1021 dyndlkniai kkvfdmgydv nkhgkfdrtv qngrlrdsky erigkkyqwi alyelaaqaa
     1081 dnykievytd aygtkkeiyc kgtfepdirn idptvmtvin nnnnkrvhnq lfqfspipnn
     1141 ewlgdfsdlp sindmvnsvy knqdflllng wytwkeendf knknyknpek dmwvlinsyi
     1201 ikndqlepiv nalkgkdfmg rwltepnsny tlynkeyywa dgyyffqnsy ycgeewvqid
     1261 ehknilekdy kvllptysyt teregdifqe dfsgtwhkpc stlfyglklr ygqgdsilyn
     1321 dygevvcfes sellneeigf finkeiflky lneqgysvfw tmlaekrvle epymdrkyiq
     1381 ptisgvytln genrlvgeti esey
//
LOCUS       WP_284965634             863 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Cutibacterium avidum].
ACCESSION   WP_284965634
VERSION     WP_284965634.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium avidum
  ORGANISM  Cutibacterium avidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 863)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 863)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..863
                     /organism="Cutibacterium avidum"
                     /db_xref="taxon:33010"
     Protein         1..863
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=95828
     Region          33..845
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mhlaealddm vdgrapvttd rgerqpgwds pgarpldadm aldhierava rdgismyehq
       61 eeaileilsg nhvivttptg sgksliataa hfacvaaggr syytapikal vsekffslce
      121 ifgatnvgmv tgdasvnsda piicctaeil anialregrh anvdqvvmde fhfigdpdrg
      181 wawqvplsel pqaqqivmsa tlgdvtdlse glttitgrpt svitgvvrpv plqyswsmkp
      241 dheaieelve eqkapvyivh psqkqalera qsmtsmklvs teerhgiaae iadfrfskgf
      301 gstvrkfits gigvhhagml pkyrrlvetl aqqgklkvic gtdtlgvgin vpirtvmfts
      361 ltkfdgrrtr vlksrefhqi agragragfd tvgyvvaqap ehvianekal akagddpkkr
      421 rkvqrhkppe gfvnyseetf tklvestpet lharmritea mllnllqrde dtaravqhlv
      481 dsstpvvaer rrlyrravqi glsllrsevf hrldeptpgg rkfamnealq ddfalnqpls
      541 afaseavatl dpespthald vvsvieatld npmsvliaqq haargeaiar mkedgydyed
      601 rmaaveeiew prpleetlda lfeifapshp wipsdalqpk svvrdmyera mtfgefcahy
      661 kvqrseglvl ryltdayral rqtvpesert eeladviswl gevvrstdss lideweelth
      721 pvdeepeevr pvrtftsnqr aftvmvrnal frkvilaadd dfealgalep dssamttnaw
      781 edtlgdywde hdeindgpda rapglfmiek esgrrdarvw lvrqiiddpa gnhdwsitat
      841 vdldecdeae dlvlrtrafs rld
//
LOCUS       WP_284965641             222 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase, partial [Clostridioides difficile].
ACCESSION   WP_284965641
VERSION     WP_284965641.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>222
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          12..214
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mekkyfeihg vpsilwgnps sklyiyihgq cgnkeeaeaf aniavphecq vlsvdlpehg
       61 erkreknsfn pwhvvpelvs imeyakchwn qislyansig awfsmlsfek enlrecifvs
      121 pildmqqlis nmmlwanvse eqlkheliip tsfghtlswe ylqyvkqhpi tqwnvptkil
      181 ygkhdeltei gvvekfvekf ncnltiieng khwfntpqel ns
//
LOCUS       WP_284965658             401 aa            linear   BCT 25-DEC-2024
DEFINITION  M20 family metallopeptidase, partial [Clostridioides difficile].
ACCESSION   WP_284965658
VERSION     WP_284965658.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Turner,A.J.
  TITLE     Exploring the structure and function of zinc metallopeptidases: old
            enzymes and new discoveries
  JOURNAL   Biochem Soc Trans 31 (Pt 3), 723-727 (2003)
   PUBMED   12773192
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10177061
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..401
                     /product="M20 family metallopeptidase"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          1..367
                     /region_name="M20_Acy1L2-like"
                     /note="M20 Peptidase aminoacylase 1-like protein 2,
                     amidohydrolase family; cd09849"
                     /db_xref="CDD:349947"
ORIGIN      
        1 ykefktteav snffeqelnl svekniavtg ckadansskk gphisilgel dgisckehkd
       61 aneigashtc ghniqiagml gaavglvksg vlehldgkvs fmatpaeefi eleyreqlkk
      121 egkityfggk qelikrgyfd didismmfha sdlgedkalv gpesngfvgk kvkfigkesh
      181 agsaphdgin alnaamlain nvnalretfk eservrfhpi itkggdivnv vpadvhmesy
      241 vrartingmi danerinkal maggmavgad veiteipgyl pilryksldn lfknnledlg
      301 lkgkvidggd ftgsfdfgdv shimptlhpm iggvkgalht rdfeivdedl ayiipakama
      361 ltvvdllfdn akdakdildt ftpvmtkeey ltflekhdkt l
//
LOCUS       WP_284965670             293 aa            linear   BCT 25-DEC-2024
DEFINITION  SPL family radical SAM protein, partial [Clostridioides difficile].
ACCESSION   WP_284965670
VERSION     WP_284965670.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Berteau,O. and Benjdia,A.
  TITLE     DNA Repair by the Radical SAM Enzyme Spore Photoproduct Lyase: From
            Biochemistry to Structural Investigations
  JOURNAL   Photochem Photobiol 93 (1), 67-77 (2017)
   PUBMED   28027411
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Frey,P.A., Hegeman,A.D. and Ruzicka,F.J.
  TITLE     The Radical SAM Superfamily
  JOURNAL   Crit Rev Biochem Mol Biol 43 (1), 63-88 (2008)
   PUBMED   18307109
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Sofia,H.J., Chen,G., Hetzler,B.G., Reyes-Spindola,J.F. and
            Miller,N.E.
  TITLE     Radical SAM, a novel protein superfamily linking unresolved steps
            in familiar biosynthetic pathways with radical mechanisms:
            functional characterization using new analysis and information
            visualization methods
  JOURNAL   Nucleic Acids Res 29 (5), 1097-1106 (2001)
   PUBMED   11222759
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18546879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>293
                     /product="SPL family radical SAM protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
     Region          17..270
                     /region_name="SplB"
                     /note="DNA repair photolyase [Replication, recombination
                     and repair]; COG1533"
                     /db_xref="CDD:441142"
ORIGIN      
        1 mynkikyipi nceiacnklk rsmpykwdln iyrgcehgck ycyaiyshky insnnyfeei
       61 yvktnivekl erqlksskwk keviniggvt dsyqpieady kimpeilnll ikyktpaiis
      121 tksdlilrdy dlidklsrit yinvastitt vnedtqrlie pngvdsmrrf kmlkefrktn
      181 asvglhimpi ipyitddfdn inslfrhake cnvhyvlpgt lylrgitrgv ffdfvkkefp
      241 elfdklsily segslnreyk nqlykmvnel rykyslsssy skimkeklkn sgd
//
LOCUS       WP_284965920             336 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284965920
VERSION     WP_284965920.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..336
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          106..333
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 kkhlniivgi psrdisriil tysqnnikkt lnkviiitlv idsvvalgvg ylfsrkltkp
       61 issvlwsiet mangnyslyl kdrgiyeevf kninmladtl rvneverken eelreewlan
      121 ithdiktpla siqgyaeiin dkdyefeede ireyteiiyn kskyikdlvd dlnlstrlkd
      181 ntivldkkki nlvslvrdii idilndnryk nrniefesne dlievyvdsi lfrraitnli
      241 fnsivhnseg tlisveivkk dnieiiikdn gigisksdlk hifkkyyrgt ntgemhkgsg
      301 lgmaiskeii eihkgkiyvs seigigtkii ieikqn
//
LOCUS       WP_284965940             589 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator, partial [Clostridioides
            difficile].
ACCESSION   WP_284965940
VERSION     WP_284965940.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..589
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
     Region          29..575
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 iknvkhkfif egnlcdarki isteedkfld sdyrktfiln killgekisi ekltnemlls
       61 kntvvqtitd vkkylqtmgl rleykgkyki igdeyvirel fliivqenvl einsiseevs
      121 sfdtkghikl tdysllnltk fveflnkrir dgktlysyky lneakkisyf snckellcee
      181 aneneqayic tyisslpsln sevkedvvee yvdklidkfe vntaiklesk hefkknilrh
      241 lhssynrirf kfpirnpmld etkykhesly kiiksiiene eefpvfegir eeeigfiaay
      301 fggylrgsrd nglrrnkvll vcpnglmvsk sleiqlykyi ptieivgivs ikqlkevnvy
      361 ydyiittidi qnvnnvivvn plltssdvql lmnklisvke nekyfnleli iqairkngvi
      421 nneealkadl lniihkideg emyqpmlkel inaervniik svrdwkeaik iaskplledn
      481 sieelyienm iksvekygpy ivladrfalp hasskegvnk lamsllived evdllgkpvn
      541 ifmvlaavdn tthiralasl semmyeeenv kliingdkss iielinkqn
//
LOCUS       WP_284965953             241 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284965953
VERSION     WP_284965953.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>241
                     /product="substrate-binding periplasmic protein"
     Region          38..238
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mkafkkhfli lsliflliis cfnnilcfad esenskkirv gycddygiis sskehsytgy
       61 gydylreisk ytrweyefvk gsweecldrl ekgeidllgp lqkndernkl fnfpklssgy
      121 eysalytkds nnnmfyedis sfkgmrvavl rgnfhntafe kyreennfsv eyiycnside
      181 liesvnekka dafvcgsiin akgmkivskf svepfyfata kdkpnlvkel dyalkelkin
      241 d
//
LOCUS       WP_284966033             218 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284966033
VERSION     WP_284966033.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>218
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          5..72
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 miilqigknl knirkqkelt qiqlaeisgi srnalinyen dkripsidtl sklakalkie
       61 ktifyfdien evmtnedvly flqslfpeey ysfdeflnai snlmedddir itsslllgaw
      121 sdkdqyyklg eklelnenqv ynwilsdcis nteldfslhp ddikeiiknd vltkqsidel
      181 ldiglseeni etiydyfsdp tdtgsnirlk klisqken
//
LOCUS       WP_284965955             142 aa            linear   BCT 25-DEC-2024
DEFINITION  GGDEF domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284965955
VERSION     WP_284965955.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 142)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 142)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 142)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>142
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
     Region          5..>142
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mkknrliakn isiafivlff fsvftffyvg ninrvleyet ndiitvtiag wiilsflflg
       61 iiiyilyska nsqktiekva ytdfvtgysn wrkfeldvtn llkktsqnnk yamvifdidk
      121 fkaindiygh kkgnlilkdi ad
//
LOCUS       WP_284966149             332 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Cutibacterium
            acnes].
ACCESSION   WP_284966149
VERSION     WP_284966149.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..332
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36514
     Region          3..325
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 msmnigayta clhnydlaea ldilktnglt gaevnvggfi psphcpvdtl mtsqtaredy
       61 mgifedkemr lavlntsgnp lsplpdvgpr haydlrraie lagklgitdl vcmsgtpgsd
      121 rhakypswvv npwngvelev leyqksvvdp fwremdlraq dagvklalel hphnlvftpv
      181 nflefaerid arnigvnmdp shlmwqgmdi iaaiellgdh ifhvhakdtv ilpgiatrgv
      241 ldssfgsvpd dpdvrvqtgm ehycsswpsd pawrfvaign ghdvtwwtnf lrairdvnpg
      301 mniniehedq slaqldgiav sarnllaaeq av
//
LOCUS       WP_284966174             457 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Cutibacterium acnes].
ACCESSION   WP_284966174
VERSION     WP_284966174.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..457
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49907
     Region          3..308
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtdsvldvta daleqagahp hrlvvrqhgq vvgrrrwapw spdvpslvys csktftsaav
       61 giavnrgafg yddtladlwp qactantgpv aksmtvrnal smstghspeq lleptlmsrr
      121 lpdlntaril latepegrpg idfaynnlat wmlsrlvaqh tgedvdtiit kevldpigag
      181 phtwvrdadg ipmgfsglhi daedlslfgq lllddgvheg arllpeawir qhrvrqvncd
      241 setdpewgmg ygwqtwmssh gyrldgafgq yvlivpevda vitmtnease gpgdkqailq
      301 avwdhllpal adgfqpqpee ivrtvptvtg efdsarsvqg iapdgsyivv sphkesrtwa
      361 mswrcpgtfs hptdetldia vgyeewqtsh crvgddaidi atsggwqget fvarlcvist
      421 phtltlrmtp eatttewdne plnpggllgl vhpelrr
//
LOCUS       WP_284966189             495 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Cutibacterium
            acnes].
ACCESSION   WP_284966189
VERSION     WP_284966189.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..495
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=52627
     Region          11..250
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
     Region          <269..>344
                     /region_name="PknB_PASTA_kin"
                     /note="Stk1 family PASTA domain-containing Ser/Thr kinase;
                     NF033483"
                     /db_xref="CDD:468045"
ORIGIN      
        1 mafsldirch seiglvrrnn qdsgyvsprm lvvadgmgga aagdlastva vrhvakadrr
       61 fsgegsparp qgeemltvls gavadandel adlvawdssl egmgttfcga mfsgtqlgiv
      121 higdsrgyll rqgrmkrmth dhswvqslid dgritpeeaa vhphrslllk vlngqpqhip
      181 dtqivdlrlg drilfcsdgl cglvnddtig ehlnttnldd vvdllttdah agggtdniti
      241 vvaevveadp nldasephii gaattrkvpe hevtaplpld qpasatnndg kstvlfnsea
      301 eesmryapvd smtrhrrhwl wpvvilafva vvvggifgar aylntqyyvg tdddtvaiyq
      361 gspdnlawiq lshvtektni ktadlpryyr drvlgnirvs smdsahatva elrtgaqqck
      421 vireaatapp ptkpatppst ppqpsasgpt anahhtpqps avptpamptp tsampspsaa
      481 ghevdlpavt sgdcq
//
LOCUS       WP_284966415             606 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Enterobacter cloacae].
ACCESSION   WP_284966415
VERSION     WP_284966415.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..606
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=68444
     Region          1..524
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mklvridiqn frgissasin lenfttligs nnigkstilk aikilvdttn ptsedwpfri
       61 asndemiitg tfsdiqdaer skpaisnlih ngelnirvrt kwdhdnecmg apsyeayysk
      121 esidefttsi taarnipwlf diireldcnn skaykemqnd vvglikqrhp ekvtselcwt
      181 seginfknsl qqalphvlyi pacfkieddl ksqkgtpfgf lfsnrvypvl qadssftqyt
      241 ssldqlhkkm kgeldgelie glqelmesit eslnqvmdlk skvklsltei dinaalmkaa
      301 tlviedklet qleyqgsgvq ralayalles nalfevtesq rstlilyeep elyihphlmr
      361 llrdklreks svsacqvivs thspflidia enpsslklik dnhegkrtvh eiddsifhid
      421 aeyneremlr aaldfhptvc eaffakrvvv vegdtevail rfaselcdkl nidknlikdt
      481 tivsaggkwt ipaiarilsk lnipfkivhd tdrkgmteee ienlsainay ranikiseiv
      541 gddnvhrvdd tfehllwdpv idgnapsegg kpfnawkrik ayldgdvnln ptcehklksv
      601 lqfiye
//
LOCUS       WP_284966448             141 aa            linear   BCT 25-DEC-2024
DEFINITION  ferritin-like domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284966448
VERSION     WP_284966448.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..141
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          16..139
                     /region_name="Rubrerythrin_like"
                     /note="rubrerythrin-like, diiron-binding domain; cd01046"
                     /db_xref="CDD:153105"
     Site            order(28,61,64,91,124,127)
                     /site_type="other"
                     /note="diiron binding motif [ion binding]"
                     /db_xref="CDD:153105"
ORIGIN      
        1 wadehrigva qgvdaeiieg lranftgect evgmylamsr qadregypev aeaykriafe
       61 eaehaakfae llgevvvadt kenlrvrvda eygatdgklk lakrakelgl daihdtvhem
      121 ckdearhgka flgllnrhfg k
//
LOCUS       WP_284966490             133 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284966490
VERSION     WP_284966490.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>133
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
     Region          2..>129
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mnfyrfvini fkgfskiffk yevigaenip drgniviasn hksnldpifl aaaienreia
       61 aiakkelfkv kplgfilkkl hvmpinrekp dvstiktilr svrdgyvlgi fpegtrikgd
      121 sfgkakagls vft
//
LOCUS       WP_284966537             265 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Enterobacter cloacae].
ACCESSION   WP_284966537
VERSION     WP_284966537.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..265
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28552
     Region          15..259
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mnsltllqgs qmpalcllsg tlggiigsfl gvvverippl ikeeegagnl lfpashcpac
       61 shtlawweni pvlswcclrg rcrccqtaip lrllllelss alffaltaay apsaaalmsl
      121 wvlwcgllpl aaidakhmll pdcltqpllw agllnhalfh tiplsdalfg aaagylslwl
      181 lywafrlttg reglgygdfk llaalgawcg wqalpsllla aalsgialyf vfykavkens
      241 vipfgpllsl tclvifilqt lqftf
//
LOCUS       WP_284966585             289 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284966585
VERSION     WP_284966585.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..289
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          <4..289
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 ackdvnilil gesgvgkdil aryihsispr kneifvpvnc csfsenlles elfghekgsf
       61 tgavdsrkgr felsnkgtlf ldeigdipln vqvkllrtle dksierigsn ksikvdfrli
      121 camnkepkve isngniredf fyristitit ipplrkrred lttlieffln kyqiehdkki
      181 hsidkevkdf llnynypgni relkniinrl vvlseegnls kdnlnlisnn vyiddkisir
      241 plreirkefe ceyiekvlsl cgnnisntak kleisrrqlt nkiseynik
//
LOCUS       WP_284966588              75 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284966588
VERSION     WP_284966588.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 75)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 75)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 75)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..75
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          12..73
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 eyilrgdnmi syaplwklli drkikkmefv nisgisisvl grlgndksvs mdtmekicla
       61 ldckiedvve ikkgi
//
LOCUS       WP_284966614             669 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Clostridioides
            difficile].
ACCESSION   WP_284966614
VERSION     WP_284966614.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..669
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=76344
     Region          205..578
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mktiavvtdg lsklecflnk nlemifkdkv miknyylnki tekelikddi ilvmivdrvl
       61 kikkyvedvs kiitinrsik qkdiyklfsl pegidvlvvn dnkhtvleti snlyniginh
      121 lnfipynpne eyrnikiait pgeaslvpky ieevidlghr yidsstfiqi iaklklddke
      181 iterlikytd eiislysgin tkykeltika delnsiinls nlgmamvsdk gniiicnnsl
      241 gdildiqsni igknidelen enikkifsls kahdevikfn nkylnvnkyn iesfgrvtgy
      301 yfciqeityi rkleqnlskk lrekgqvary tfddiktvst kmertkklgm kiaesdytil
      361 itgesgtgke lmaqsihnas prhsqpfiai ncaampenll eselfgyeeg aftgalkggk
      421 kglfeqanng tifldeigdm piylqskllr vlqenqvmrv ggenvididv rviaatnknl
      481 lemikgdrfr adlyyrinvl pinipplrer kedievmlkh fmkrkraisq dvqdiinaye
      541 wpgnirelkn tamyinimss edvilindlp hnllnitedf skeisilkdr tsiekvklvm
      601 eclknannln knigrngivn sinelgynit egevrgilnm lkeldliice sgrkgselnr
      661 rgknilnsi
//
LOCUS       WP_284966639             259 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Enterobacter cloacae].
ACCESSION   WP_284966639
VERSION     WP_284966639.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..259
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=29071
     Region          4..256
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mdsmlallfl iigllagstm gmvtwrlpim ivqqpnadea fsrfnlwlpa shcchcripl
       61 mwhdniplfs wlrlkgkcrh cgqsvswryp lleascalma plcyalhpnn lmlvsgllly
      121 fwfalalsvi dlqhfllpdk ltlpllwlgl lfnlltgvvp ckdailgava gyltlwllyw
      181 ivwliwrkeg lgygdfklla amgawtgwqn lptilyiasi agvlgglaww mkkrqftgal
      241 pfgpalalsg wgyfcwatl
//
LOCUS       WP_284966702             494 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Enterobacter cloacae].
ACCESSION   WP_284966702
VERSION     WP_284966702.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..494
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54226
     Region          113..348
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 manlpwrvsv rlmalakkva mvigiivvvl lavrvylsqq gpalhlwhtw rademsvsel
       61 ekanfadyld rekaiftdld navtaktkge ertalnryyr qslvwpgkft pdanrsfvlm
      121 pagkprgavv llhgltdspy svkhlavdyq qrgfvavvpr lpghgtapga ltnvdwemwl
      181 aatrlavrea srlagdnvpl hlvgysngga lamkytldal espslrkpqq lvllspmigv
      241 tafarfagfa glpallpafa kaawlniape ynpykynsfp vnaarqswll tkalqeqigr
      301 aaqnhtldrl ppvlafqsvm dstvstravv tglfdqlpan gselvvfdin qaasfrplfr
      361 psswtalsel lpsaqrrysv tivtnasaer fatvakhipa gsteetvepl aqqyppevys
      421 lshvavpfpp dddlygrhpa vknrygislg tialwgetsv lsvgkdalmr vssnpfydym
      481 kmridnrigt eekg
//
LOCUS       WP_284966937              87 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator, partial
            [Enterobacter cloacae].
ACCESSION   WP_284966937
VERSION     WP_284966937.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 87)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 87)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         <1..>87
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          1..85
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 nlfaaqcpsr eilkhvtsrw gililislrd gthsfsdlrr kiggisekml aqslqaleqd
       61 gfinrvsypv lpphveytlt dlgeqis
//
LOCUS       WP_284966998             669 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Clostridioides
            difficile].
ACCESSION   WP_284966998
VERSION     WP_284966998.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..669
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=76519
     Region          205..578
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mktiavvtdg lsklecflnk nlemifkdkv miknyylnki tekelikddi ilvmiddrvl
       61 kikkyvedvs kiitinrsik qkdiyklfsl pegidvlvvn dnkhtvleti snlyniginh
      121 lnfipynpne eyrnikiait pgesslvpky ieevidlghr yidsstfiqi iaklklddke
      181 iterlikytd eiislysgin tkykeltika delnsiinls nlgmamvsdk gniiicnnsl
      241 rdildiqsni igknidelen enikkifsls kahdevikfn nkylnvnkyn iesfgrvtgy
      301 yfciqeityi rkleqnlskk lrekgqvary tfddiktvst kmertkklgm kiaesdytil
      361 itgesgtgke lmaqsihnas prhsqpfiai ncaampenll eselfgyeeg aftgdlkggk
      421 kglfeqanng tifldeigdm piylqskllr vlqenqvmrv ggenvididv rviaatnknl
      481 lemikgdrfr adlyyrinvl pinipplrer kedievmlkh fmkrkraisq dvqdiinaye
      541 wpgnirelkn tamyinimss edvilindlp hnllnitedf skeisilkdr tsiekvklvm
      601 eclknannln knigrngivn sinelgynit egevrgilnm lkeldliice sgrkgselnr
      661 rgknilnsi
//
LOCUS       WP_284967017             168 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator, partial [Clostridioides
            difficile].
ACCESSION   WP_284967017
VERSION     WP_284967017.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..168
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          <61..160
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 gffivnskyn ldinvttqni ietetyqsty ifylgeldsk adfdfrlqlc sdllphiikd
       61 naenkflnlf dliryktldl inednilnkl idfnkiksid eellytgikf inndlniskt
      121 stsmflhrnt lvyrlekine ilgfdlknfe namifylsvk syflykki
//
LOCUS       WP_284967084             183 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284967084
VERSION     WP_284967084.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 183)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 183)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 183)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..183
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <1..154
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 kikavnfdii diterivtsi ssyakskgid lifdtdeetv mvgldpesie riilnilsna
       61 ikftleggei lvgiykkdet veiiikdtgv gidkeklndi fnrfkqiens gisnefgsgi
      121 glcltkslie iqngkiyids kvgegtnvkv ifpikevvee vydnsnyndn iekfeieffd
      181 iyk
//
LOCUS       WP_284967138             487 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Cutibacterium namnetense].
ACCESSION   WP_284967138
VERSION     WP_284967138.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium namnetense
  ORGANISM  Cutibacterium namnetense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Cutibacterium namnetense"
                     /db_xref="taxon:1574624"
     Protein         1..487
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51529
     Region          4..487
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mtqtatessa ttrtgiettg ieiieesqrt aqprdlflpw fasnvsvfgm sygafmlgfk
       61 vsfwqamaat lvgvivsfgf cgiiaiagkr gsaptmvlsr aafgtqgnki pgiiswmtsi
      121 gwetslaita vlatttifhr lgwssgssvk icativvall ivggavagyh iimklqavlt
      181 witgvltviy lvmaashidw hattslpcas vpafvgaltl vmtgtglgwt niaadwsryq
      241 srtspgfaia fwnvfgaslp livlitggll laassknlsd aigadpvgal atilptwfli
      301 pfllaailsl lagaingiys sgltlltlgi rvprpaasli dgtiltigtl yvvfvapnfi
      361 spfqsflvtl gvplsgwtgi mmaditlrhr pydeadlfng sgrygrfdlt siitfvvvtv
      421 igwglvvnty eganwnnwqg fllgpiglgg rqgdwayanl gvfgalvlgy vvtliarrgk
      481 vrrqesr
//
LOCUS       WP_284967147            1041 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-mannosidase [Cutibacterium namnetense].
ACCESSION   WP_284967147
VERSION     WP_284967147.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium namnetense
  ORGANISM  Cutibacterium namnetense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Cutibacterium namnetense"
                     /db_xref="taxon:1574624"
     Protein         1..1041
                     /product="alpha-mannosidase"
                     /calculated_mol_wt=115334
     Region          259..1040
                     /region_name="MngB"
                     /note="Alpha-mannosidase [Carbohydrate transport and
                     metabolism]; COG0383"
                     /db_xref="CDD:440152"
ORIGIN      
        1 mhdhtkltqd righlkerle reitqkicpl qvtawqvpge pvsfaeataa syqpfppgtw
       61 wgapwstwwl hvtgtlpash adeeidfsmd lgfvgdwagn qaeamvytpa grplkalnpr
      121 nhriglnhga laarfaaqge pligadgdve lwveaagnpd mtqhlaepte lgdrhtaghe
      181 plwqfkaael svrrnevwgl wldidvldgl mrqlpadsth rarllygleq aadevdrhgi
      241 iagaeparpi laryltsgan ssaqqmtaig hahidsawlw pvrktrrkvv rifsnvisla
      301 eeypdfhfac tsaqhyawfq dsspelfkrv qeaiergqwh pvggmwvesd tnlpageslv
      361 rqftsglrwm rehlgvrpnc lwlpdsfgyt galpqiarla gmnwfftqkl swnttnifph
      421 htfwwegidg triwthfppv dcydsivsaq evskaeanfk ekgaarrsil pfgygdgggg
      481 ptaeqvervh rfadledapq vrlgspddyf ngarddypga pvwrgemyle fhrgvytsvh
      541 alkdgnrrae aglaaaewla tvaarvghpc pyeqleqlwr rtlllqfhdi lpgssiawvn
      601 heavaeftai raeldqltdd awqalsqvsg detagmsvvn pshadrrevi tvsgrpalvq
      661 ipamaaksla damvapehpv yvqrgrdair ianglvevgi dtrdglvnsi tdlvagrell
      721 lagqranrlv lhpdypdcfd awelqrqyrh sanpvddvtd lsviedplra qvrverrvgn
      781 ssfvqaitvd adsravefsl dvdwaeqarv lrvdfpldva arssrdeiqf gyierpigtn
      841 tswddahfes cgqqwmllse pryavalvnq ssyghdvspa ggdehtptlg vmarltllrs
      901 pqspdphpdq grhhlsysll tdaevgsahv eaarlnqplq lrggtvelps tariepvhgt
      961 avidavkqaf dgsgdlviri heaagarstv rllldqdgcm sevdlleepv sdptqqlpas
     1021 tchgveltlr pfqivtlrvs q
//
LOCUS       WP_284967218             260 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Clostridioides difficile].
ACCESSION   WP_284967218
VERSION     WP_284967218.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..260
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30116
     Region          4..257
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mafieckfks kytggetdii vilpvangke lfsgkeiydf egkfktlylf hgleddqssw
       61 irytnvehya knknialvip rvetsfytdm ayghqyftfv seelpkfvra ifplsdkred
      121 nfvagmsmgg ygalklalsk pkeflavasf sgspdmihel enqqietnad ilfhdfgrpe
      181 darnsendlf yilknlkern edipkiyqfc gdrdflyknn qmfkkyaesl gvdveyeecv
      241 gghewrlwnl wikkfidiig
//
LOCUS       WP_284967271             259 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Clostridioides difficile].
ACCESSION   WP_284967271
VERSION     WP_284967271.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..259
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29828
     Region          34..156
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mndtvkekla esltsdttdi lpylpyllqd fwelgsspeq mlqlfrkhip fnedtkvldl
       61 acgkgavsvk lakelnihik gidlipefid yarrkaieyk vdalcdfemn danssvkieh
      121 dydcvifgav gdilgnyket iskllptiks kgfilidday vvdkstneql nfervyptyd
      181 ewcilfkelg lkliecipcl elendveeem nwiitranel ikkypsqkdm feqyvisqkn
      241 eytdlqqdlv gatwilqke
//
LOCUS       WP_284967279             706 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Clostridioides
            difficile].
ACCESSION   WP_284967279
VERSION     WP_284967279.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..706
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=81286
     Region          205..580
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mkqmelaivs lkkdageiye nqirqflgdn lkinlysfee gnlkffkekl illsaylkyd
       61 eivklshyda qiivpkltfe knsidmiskl ekdkiiyvyn lskdmaieti slihrlgidn
      121 inilpcypei eftptdavil tpgekilpkf kncevidlky riidlscive iatktklkhl
      181 ikddlikkyv ekiiptsyst gellldankf erqfdlllsi iddgiictnn dgiiqfynhm
      241 arkilsinan emidsfvgdc ikdinfqsil tnktpffekl ikinhidinl eikhiqlnvf
      301 dgfilkmtkf sqlekkqakl raqlvnsgni skytfddilg ssiqtintkk iankmaqsns
      361 siliigesgt gkelfaqsih sasrrkdgpf vavncstfqe nllqselfgy degaftgakk
      421 ggkiglfela nngtifldei gemdlnsqsk llrviqekqv rrigsnnvid idvriiaatn
      481 rtlkelvskn mfrrdlyfrl nvlplkihpl rerpadifei fgslkydipc nfilseevke
      541 ifkmyrwegn vrelrnlgey fcylekdiie icdlpeyild tidsnysrtv cnkvsdnikk
      601 yqfnigkdkn imkydynfkr sldeyifild nlkkaydlke rigrkslcki aleenrflte
      661 qqirnmllel qnfglvdilv grggsiitsk gveflkninr snklns
//
LOCUS       WP_284967345             681 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Clostridioides
            difficile].
ACCESSION   WP_284967345
VERSION     WP_284967345.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 681)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..681
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=78201
     Region          203..585
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mkkhnilfvs tddkinidis kqlenifgef cnidnlvyvn rinielssye lvvcsdndik
       61 eyihnnidkn ipivivhrti nieninqiis iendsdvmvi daykesadet skiirklgli
      121 hinlipyypg cdkskceigi itgsrnsipq nikqiidigd kvidintvie iftklnisid
      181 klhiikekyn edtvsgyryy ttmnktmksf leiidegias vdklgkfiyc nkvfsnlvgi
      241 dqneiisnnf mdlfsdkvvk kiffqedevn devvnlnnkk liinkvnvye nneriksiis
      301 iknisaiqvl edkiqnklqs kgfvskytfe svvgeskiik ekiniarkia ttdfsvlilg
      361 engtgkeifa qaihneslrk nkpfvavnls slsdtliese lfgydegsft gaikggkmgi
      421 ferahtgtif ldeigdisld vqqrllrvlq ekevmrmggs kiipidvrii aatnkdlkkk
      481 ikegsfredl yyrinvlhie iprlrerked ipliskyfld einsnkcfte esmqaltlye
      541 wpgnvrelkn liyyidtive edrvdyehlp eqfrfeknnt lvnenfdsii ldfkqsnffe
      601 esiciltsie twnnknillg rnklqeilke kdivlsvdqi rkridklksh glllsgvkkq
      661 gsfitdegkn fisyvkikgv i
//
LOCUS       WP_284967377             194 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Clostridioides difficile].
ACCESSION   WP_284967377
VERSION     WP_284967377.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..194
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=21655
     Region          1..191
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mniilasasp rrkeilentn vrfdiiknei deiilegetp khlvmrlafe ksmsvasehn
       61 edvvigadtv vvldsailgk pkdescardm lkrlsgrehq vitgislinl cedkkvidyv
      121 isnvkfktls eqdiedylkt nesfdkagay giqgygallv eeirgdyfni vglpisrlgd
      181 llkkyfsinl fygv
//
LOCUS       WP_284967546             833 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Clostridioides difficile].
ACCESSION   WP_284967546
VERSION     WP_284967546.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 833)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 833)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 833)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17597966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..833
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=96030
     Region          130..>320
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
     Region          601..825
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mifhevykiy sknslknnkl lkisciisiv fataillftr vltdtyssev krnmaitngg
       61 dikiqnieyn kyyftseqid nleelkdkes idfqlgssmn tnilsngmie steltvvnni
      121 kmqntylklr nendivlsqk tanklnvnig dkvflklhss vyddtyfkvs diipkrfsls
      181 taqkeaevgq evvgesyvyl pnetkynvay iniinkenvk nikneiknvf knhfevrttd
      241 eleqsiikri smqldsinli gaisllitgi clcstfivfi lnrindfstf kalgirkrsl
      301 sflvftelms itikgiiigi ilgipitify inlqhinlfn isilsiikni fisiviiiie
      361 tsifslipis fvkkipyegi nrdnsmlssy kfnfipdiil vifltsisft iyvksflgif
      421 filglilldl lvysliyall kmvclikkii kgkysitfiy lnndcktnaf ssslltitii
      481 fvlllfmise itfamfsnye vdnsiknsiv yqttlegkli tdkkliendi dyfqyypiki
      541 dsiesvnnis vsdyiekipy enrkdvmndl ndlsvdlfnt kqtilksdle ygnwfkendk
      601 ensiiinnyl hrylidyklg dtvklringk didfkvigfl spkslnkgvd lgyinineni
      661 spktldlskn qpviyffkek ldntllskll hndkyanled yndfaysmkt yvddqkslll
      721 niifavslss illiltsqii ifirrvldyq imyrvgmskr klikigllem iivsiiqsil
      781 iaifyelfrf llisllqray ninyllilie flvvlsincf ifilaqrnik ldl
//
LOCUS       WP_284967568             263 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Clostridioides difficile].
ACCESSION   WP_284967568
VERSION     WP_284967568.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..263
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29747
     Region          35..144
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 metkqylinf yntydedsrl alkhgmvefl ttvhyidkyi ksgdcvleig aatgryshtl
       61 arqgydvdav elvehnievf hkntqsneni sitqgnamdl svfpdnkydi tlllgplyhl
      121 ynkedkqqal heairvtkpg gvvfaayvis dgclidegfh rgninvseyi ekglidpqtf
      181 aaksepkdlf elvrkenidd lmsafnvtrl hyvasdglal ymreavdsmd ddafalylky
      241 hlatceredl vgvtshaidi frk
//
LOCUS       WP_284967569             494 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Enterobacter cloacae].
ACCESSION   WP_284967569
VERSION     WP_284967569.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..494
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54441
     Region          113..348
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 manlpwrvsv rlmalakkva mvigiivvvl lavrvylsqq gpalhlwhtw rademsvsel
       61 dkanfadyld rekaiftdld navtaktkge ertalnryyr qslvwpgkft pdanrsfvlm
      121 pagkprgavv llhgltdspy svkhlavdyq qrgfvavvpr lpghgtapga ltnvdwemwl
      181 aatrlavrea srlardnvpl hlvgysngga lamkytldal espslrkpqq lvllspmigv
      241 tafarfagfa glpallpafa kaawlniape ynpykynsfp vnaarqswll tkalqeqigr
      301 daqnhtldrl ppvlafqsvm dstvstravv tglfdqlpan gselvvfdin qaasfrplfr
      361 psswtalsel lpsaqrrysv tiitnasaer fatvakhipa dsteetvepl aqqyppevys
      421 lshvavpfpp dddlygrhpa vknrygislg tialwgetsv lsvgkdalmr vtsnpfydym
      481 kmridnrigt eekg
//
LOCUS       WP_284967590             664 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Enterobacter cloacae].
ACCESSION   WP_284967590
VERSION     WP_284967590.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10297442
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Enterobacter cloacae"
                     /db_xref="taxon:550"
     Protein         1..664
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=70560
     Region          182..451
                     /region_name="Peptidases_S8_S53"
                     /note="Peptidase domain in the S8 and S53 families;
                     cl10459"
                     /db_xref="CDD:415849"
     Site            order(234,294,413)
                     /site_type="active"
                     /db_xref="CDD:173787"
     Site            order(234,413)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:173787"
     Region          609..655
                     /region_name="ChiC_BD"
                     /note="Chitin-binding domain of chitinase C; cd12215"
                     /db_xref="CDD:213178"
ORIGIN      
        1 mkksalslfi caaisfsaaa etlvqnefaq dnatytaivl klkpttgllk atnnkitlsd
       61 asltttnmfr ptnlrsstqf seltelnkry gfdrylriel pkdksqdkty inhiiteleq
      121 nqnvefvype aepvslddta lkpqlkssln dnltsaavpd frnkqdylka pdvkrtgyym
      181 ggvnrdsvdr yagsagegvt iisaeidawn tshanlppms lssgkttyva shdhdtasvg
      241 imaakdmgtg irglawksrm gyaasasnnl ynlipqlkag dvvqigiqva ggypagcqkd
      301 cwvamesqta yydiikaltd kgvhvieaag ngninmdspg frgeydvnvr dsgailagaf
      361 cakdgkkasf ssygsritss awgcwdvvtt gygdlyknag vndsytatfa gtssanpiia
      421 gvvaslsgia kangitvtpr qmrqilaetg tplangdsak vgtqpdmera varimalkdg
      481 ntpvapapta aagadytmvs pttgvstypl dgskslnaks ynwsvtkgae tfsleanlng
      541 tlvksvdsah ayavipanse geavftlttt gadgrtatds mtikvtkpav pekddtpekd
      601 dtpvkpaapa ynakiayptk ctkvsyngki wfnqwyvnpg qetpgtggqw gawreqgsss
      661 nsck
//
LOCUS       WP_284967782             316 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284967782
VERSION     WP_284967782.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>316
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          <2..257
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
     Region          253..>316
                     /region_name="COG1693"
                     /note="Repressor of nif and glnA expression
                     [Transcription]"
                     /db_xref="CDD:441299"
ORIGIN      
        1 maltdnpili tgetgtgkea ftqsihnhsn rknkpfvain caslpselle selfgyedgs
       61 ftgakkggkk glfelahtgt ifldeigdmp hdlqvkllrv lqekeirkig gtsiipidvr
      121 ilaatnkdle kliienkfrm dlfyrismft ldlpplrkrl ediplllesf lkelpyknik
      181 ldksllealn sytwmgnire lrncveymay mgsnyltind lpqnisskln nnhmssnmsi
      241 fndlnqydkn icisilkslh mkpmgrtklm kfmeynvtey evrnmleylt rngylisskg
      301 rkgssitekg ikiien
//
LOCUS       WP_284967796             207 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease, partial [Clostridioides difficile].
ACCESSION   WP_284967796
VERSION     WP_284967796.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 207)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>207
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          1..>207
                     /region_name="COG4120"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443296"
ORIGIN      
        1 msvmtqslil simalgvyit ykildfpdms adgsytmgas ivafsltngi spvvatlmai
       61 lcgctaglvt gilhikfkis nllsgilvmg mlysinlrim gksniplfsf khlfngeisp
      121 ivlalafvfi ckvlldlflk tglgytlkgv gdnsqmiksl ginigsikil glmisnglia
      181 lsgslmaqfl gfsdvnmgig tlvlgia
//
LOCUS       WP_284967861             329 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Clostridioides difficile].
ACCESSION   WP_284967861
VERSION     WP_284967861.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..329
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=37075
     Region          98..329
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mfrnrefrkf ailfllitil tvalgfaisi mtgilsivsa ttfgiaffvf tknryksiaq
       61 iseqinlvlh nanhlyiaes degelsilqs eitkmtlrir eqnyalkkek ehladsladi
      121 ahqlrtplts vtlilsllen tsdederkel ireteellir mdwlitsllk lsrldagivv
      181 fqkeqidvnn lissalhqll ipmelhnitl hidipkgvri lgdlnwlsea iqnifkncme
      241 svsdngkidi icednflftq ltihdngagf kkedlpclfn rfyrgknsst agygiglalc
      301 ktiimrqggt itaqnhpqgg aifvirfpk
//
LOCUS       WP_284967958             316 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284967958
VERSION     WP_284967958.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..316
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          80..316
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 vnmffdggkf iggksivfsi igiifliilv sgiaygywvt kcisnitsav sdiskrsylp
       61 vnikgvfadi ynslnilnee ihksdeiqnk tdimreewis nithdlktpl spikgyaell
      121 tdsstnyspe kvykyasiml knieytntli ndlkltyqlk ngiiplnknn ydlvrflkel
      181 sidilnypey esnivefksn idninfdfdc tllkrafsnl ivnaftygdk ntkvcvhvtl
      241 nerieiiisd ngkgmsreea snlfnryyrg sntkqkiegt glglaitkqi ievhggnisv
      301 esipglgssf yitfpi
//
LOCUS       WP_284967967             168 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase, partial [Clostridioides difficile].
ACCESSION   WP_284967967
VERSION     WP_284967967.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>168
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
     Region          23..158
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mindiknkfk nykpyingyk nmkrasvlip iveinnthyi lfevrsknlk hqpseisfpg
       61 gkiesgetpy eaviretcee lgtfsdniev issldllitp vkfiihpylg yikninnlni
      121 nkdevdhtfl vpikyllenp pntysntvkv fpdenlpygs ipnqkdyk
//
LOCUS       WP_284968095             678 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284968095
VERSION     WP_284968095.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..678
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          422..672
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 itkerientm kklftsetfl eyqfisdcqi spdggyttfi vkkadikeng ytsqvyilnn
       61 ktgelkqits insvgayawe dentilfpal rnekvkeavk ngkqcmsyya lslnggeaee
      121 lfrlpikggk lnpigkglya vidsydndrp iveglpeeeq qkkinaynkr hyehfkeipy
      181 avngegyisr krkrlyiyds ninelkaita pmfnvvgmki sdgkilyigq efkdvkglkn
      241 gvyvfdtntn tnvcilekdk yiikgfelyq nqvilnltda lsygngengd fytididtke
      301 mkllsghqhh cigntvtsdv kmgagqttkv dgeyiyytst vdmdciieri hiptgkqekv
      361 tqtgsvdfid vkdgnivcvg clgnglpevy tvengtlckk thlndhilee ykisvpeyie
      421 skgsskweiq gyvykpvdye vgkkypavla ihggprltyg pyfmheiqvf tsagyfvffc
      481 nprgsegrgn afadirkqfg eidyidfmef tdtvlekytd idktklaveg gsyggfmtnw
      541 iightnrfav acaqrsianw sgmegttdig yyfckgqtga shmenhelqw kqsplayvdk
      601 cvtptlflhg ekdyrcymqe afqmfsalki hgcptklclf egenhelsrs grpkqklqrl
      661 vemldwfsvy ikkdnigq
//
LOCUS       WP_284968096             297 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284968096
VERSION     WP_284968096.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..297
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
     Region          <207..292
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 nefplnpksr lyvlkenllm msefiqeiak rnffenqlsi kdeeilksrk enirleealk
       61 kansrlleee yiinpidmfn nsskeypfel elyiekeikn mnlegvynli dtnklryndv
      121 rdtiqemifv lsrtvlrdle dlklisylrn kynkkislvn sdedlwnvlf efskecidkn
      181 rafwrkdkgn lienineyik ksykeninln sisdvffisp nylssifner nkvsiteyin
      241 llrieeskky lldrsmsisd ickkvgfnns syfsqifkkf nsitpneyrk nmldnky
//
LOCUS       WP_284968105             519 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284968105
VERSION     WP_284968105.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..519
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
     Region          1..514
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 diqvlkgdky kqsvesqsve kvelnsgrgi iydrnnkklt dtsksqvliv ekeklnnnyk
       61 ilelikkatk mndldiykav qeqltrpiiq iqtknidksm kkelekngim veektmryak
      121 dgllshtigy ikeddksgqs gieksmdsvl rnsnekyisa fkagdagnek slnilkgsvk
      181 tvdnkdkdrh lkttidyniq kkleqilnke enptaaiise astgeilamc srpnfdqndi
      241 skslkgknge fenrvikaty ppgsvfkmvv lfsalengvi denytynctg ktkvgntnei
      301 lrcnkrdghg fqnlrqafsn scnpafldia mklgkekilk saeklhlfek vdigldeeki
      361 reapknisir nlaigqenie ftplqinqmt qiianngtfk plylykslvd nnmntiktyk
      421 sskkeelisp yvctqvkeym ksvsrtgtak dlkdieggcg vktgtaqssl nkkaidhgwi
      481 tgfypeerpk yvitvlvegt qkgnksatpi fkeicesik
//
LOCUS       WP_284968122             244 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor, partial
            [Clostridioides difficile].
ACCESSION   WP_284968122
VERSION     WP_284968122.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 244)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 244)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 244)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..244
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
     Region          11..231
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 imirkkvyil isiaicddes ymlnhlkeni elymkqknll ynielfnkve dllcnhekfn
       61 ivfldiqmee ingmqaarkl rsygnecfii fvtvlnefvf dafevdainy likplsnekl
      121 yktldkivtk lddnesnyit iqkgysywkl kladilycev ikrkiyvhlk ketvdyyeti
      181 enlerslptn ffrchrsyii nlqyvygyen gnavmesgdr ipvsrlrqqi fskvmlefmk
      241 nrri
//
LOCUS       WP_284968306             378 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284968306
VERSION     WP_284968306.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..378
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          <4..285
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
     Region          306..>372
                     /region_name="COG1693"
                     /note="Repressor of nif and glnA expression
                     [Transcription]"
                     /db_xref="CDD:441299"
ORIGIN      
        1 kksifsmgnk agiyynlqei tyikkleqnl tnklreqgqi arytfkdikt knknmikcie
       61 lakkisksdl svliigesgt gkellsqsih nasnrsnqpf iavncaavpd sllesqlfgy
      121 ekgsftgalr egkkglfela nngtifldei gdmppllqtk llrvlqekqv mpigshnvin
      181 idvrviaatn knlpkmireg kfredlyyrl nvlpidvpsl rnrkediitl mnfflknnir
      241 lspevitile kynwpgnire lqnvasyvsl mcdsmvfrdd lppyisvefa nnyedgfgyt
      301 kkefkeilri lyerresssg vgrgfiiekl iqegieises kvrkvlsyls ecgyissksg
      361 rggsqitseg iklynnin
//
LOCUS       WP_284968469             399 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284968469
VERSION     WP_284968469.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..399
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          15..396
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 vsvesssngh elleididnk iyninakiip vypyinqydk iiifdktyin hkghvkvnsg
       61 wgnsdiesii gnseamlkvk ertkklaksn stvlitgesg tgkeliarai haegsrwnkp
      121 fiaincaaip enlleselfg yikgafsgas sggkvgkfel anegviflde igdlsmplqa
      181 kllrvlqerk farigsnkli dldirviaat nknllklvne gkfrddlyyr lnvipinlpp
      241 lrerkddiea immkfaskys lelgiqlnki eenvmnmlin ynwpgnirel enaveymmnl
      301 vgddgiiykd mlpldilnyy ningnicknk diniifeddi vggivenqer ilsikelelt
      361 yinkllnkyg rdtktkkkia kdlgiglatl yrkleeeqs
//
LOCUS       WP_284968644             400 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Citrobacter
            portucalensis].
ACCESSION   WP_284968644
VERSION     WP_284968644.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..400
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45241
     Region          <65..397
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mvtirwdikt idrlsmvedv lkefsccdin iismkvtpgr ilikswcrql qdiscvqscl
       61 sqhadiinva ylceeisels tpeperpryf sdiicssqsm haliekaiki adskytvlir
      121 gdtgtgkell araihnsgqr rfypfipvnc salpeslmes effgyekgaf sgadckgkkg
      181 lfemadkgtl fldefgemsl slqakllrvl qdggirrvgg aqiipvnvri ivatnanlee
      241 mveqrllrad lyyrinvlsl tipplrerpq disllirhfv qkyakefqrr iildkacfda
      301 lhhhtwpgnv relentiirl mlmaesdvit reelgmvnlp avergaterp fkeqvlcaer
      361 qlieqmvedn vssrhiakal gvshttvlnk irgyqlesvg
//
LOCUS       WP_284968794             386 aa            linear   BCT 25-DEC-2024
DEFINITION  cytochrome b [Citrobacter portucalensis].
ACCESSION   WP_284968794
VERSION     WP_284968794.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Tolkatchev,D., Yu,L. and Yu,C.A.
  TITLE     Potential induced redox reactions in mitochondrial and bacterial
            cytochrome b-c1 complexes
  JOURNAL   J Biol Chem 271 (21), 12356-12363 (1996)
   PUBMED   8647838
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Howell,N.
  TITLE     Evolutionary conservation of protein regions in the protonmotive
            cytochrome b and their possible roles in redox catalysis
  JOURNAL   J Mol Evol 29 (2), 157-169 (1989)
   PUBMED   2509716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..386
                     /product="cytochrome b"
                     /GO_function="GO:0008121 - ubiquinol-cytochrome-c
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=44358
     Region          14..384
                     /region_name="QcrB/PetB"
                     /note="Cytochrome b subunit of the bc complex [Energy
                     production and conversion]; COG1290"
                     /db_xref="CDD:440901"
ORIGIN      
        1 mrndlvcslr gripfprsvs glwvfaigai llimlgvqil tgivlamfyv ptaelafdsi
       61 ihimravrhg ellrnmhaig aslfffacyl hifrgmyynv yrkpwttmwm vsvtlyillm
      121 mtaflgysli wgqksywaat vitrfaqaip wvgdtlyayl vgshtpgtpm lgrffvihfi
      181 lpfvivvatv ihirtvqsaf aqamkkkfse kesrsllfdy kitdldaiki tlflmvfawf
      241 lffaphylss adnfitadpt itpaivapew yflpffsilr cfpnefvgla amcgsilify
      301 flpwldtsra rfrhysklvk cgfwlwvina fflgwlgska lvgpdlldgf rneegwiraa
      361 sqlstliwfa wflivlpcrr flekqd
//
LOCUS       WP_284968880             714 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Citrobacter
            portucalensis].
ACCESSION   WP_284968880
VERSION     WP_284968880.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 714)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 714)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 714)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..714
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78838
     Region          10..675
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mlprinqrpf ilsaltlcms gaasaatstt hastpdddtv ivtanrsess lwdspatiqv
       61 idrqtlqnst svsiaddlqd ipgvevtdna lagrkqirir geassrvlil idgqvvsyqr
      121 agqnygagll idesalerie vvkgpysvly gsqaiggvvn fitkkggdkp lggsikavyn
      181 satagweesa aawgsignfd yringsysdq gdrdtpdgrl pdtnfrnngq gvwlgynfdr
      241 hkiglsldry klstqtwfdd pegqfddfsv kipklereki glfydyaadg dylkkihvda
      301 ysqtierkfe nrvkttqvip spaikaltin nqtntndkqy tqgvtlqgnf slpannelvi
      361 gtqyqhdkik qdtdgstrqt aatgffdtqt rtlsyneaeq sntslfaqnd wrfaddwtwt
      421 vgarqywlss klnrndtqtl qssgstwqst ggnsvhddel vtstslrysg fkdlelraay
      481 aqgyvfptlt qlfmqtsagg svtygnpnlk aehsnnyelg arykgnmwli dgaiyyseak
      541 dyiaslacsg qpvcsgntts srggyyyyen idraktwgme ltaeyngwav spylsgnlir
      601 rqyegntlkt wdtgeptltg rvglkhtwlm nvanltsdvf iraassakdn tgtteinypg
      661 watlnlafnt efgpqdqyqv nlalnnltdk ryrtahesip dagfnaavgf awnf
//
LOCUS       WP_284968957             315 aa            linear   BCT 25-DEC-2024
DEFINITION  formylglycine-generating enzyme family protein [Citrobacter
            portucalensis].
ACCESSION   WP_284968957
VERSION     WP_284968957.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..315
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=35366
     Region          34..274
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 mtgkyslalv lllsgcdkpe pagqnnaela qylqritgdl vfipggtfwm gdfcsrthge
       61 garcssekdt kplhevtlts ysigrfkvth edyafylkma glpaqqfdke wrnkmladmt
      121 hfknspavvs wreadsycrw lkketglafs lpteaqweya ardrgqyilv atddgdwred
      181 ektgrgenya tsedrqatee atgvdssfvr yavdrypptp gglygmseng yewvsdwydp
      241 dyyvksprqn pqgpetpvik nkktgqylkv rrggdnpspg fdvgltffrg yaikdnyfpd
      301 gttvrcavna aeavk
//
LOCUS       WP_284969074             530 aa            linear   BCT 25-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Citrobacter
            portucalensis].
ACCESSION   WP_284969074
VERSION     WP_284969074.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..530
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=57984
     Region          3..528
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mktifkngnv idgtgsegri advmvdegri veigqievgi neqvidatgk iicpgfidth
       61 thsdlsaiin palsakirqg ittellgqdg valaplpeey ipawrkniag ldgdtdkidw
      121 kykntdgyln llasrhpatn laylvphgnv rmeamgldgr pstredvakm cevlerelka
      181 gafglstgli ympcafgdta emielckvta kydgifvvhq rseaddiins tqelidiaka
      241 tgvwlhishm kvcgkknwgl idqmlgmleq aqeegirisf dqypyvagst mlgvilppwv
      301 hsggtdklle rlaspelrak middiqqgip gwdnfidfag ldqifvtsvk taknqdavgl
      361 nlvqlgelrg kdpynatfdl lfeeenavgm vdfygteehv ikflcrpeqn vctdglmgag
      421 kphprvfgaf prvlgkyvre egclsweaai rkmtgkpaev lglqdrgllk vgyaadivmf
      481 dpntiadkgt fvepnqypeg ieivmvngri alingtesya csgsvirkqy
//
LOCUS       WP_284969234             402 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Citrobacter portucalensis].
ACCESSION   WP_284969234
VERSION     WP_284969234.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 402)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 402)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..402
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43158
     Region          50..275
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
     Region          212..384
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mrnvtilaac lftasvsaae sngeyiaris dcvachtaeg gaamaggkkf ptpvgdiyst
       61 nitpdktqgi gnysyedfdk avrqgiakdg hplypampyp syaklsdedv qalyryfmhd
      121 vtpsaqpnke naipwllsar wplhiwnwlf tdapatavds akkddnaalv krgaylvegp
      181 ghcgschtpr gmamnekayt nadaeylsga midgwyapsl rgtgmseqel ksllltgksk
      241 haavsgsmve vvtqstqylt dedataiaqy llslksakpe tvratattas wsnspeagkv
      301 tynrycstch glegkgtddn apslvnnplv mvddptplfr viahgaetpt trgsvsfkmp
      361 ayggllsdne mrdvinyvrk swgegnsevs qedlagvkka sh
//
LOCUS       WP_284969463             562 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Citrobacter portucalensis].
ACCESSION   WP_284969463
VERSION     WP_284969463.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 562)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 562)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 562)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..562
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=60394
     Region          29..555
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mdsinkplqf ptlrglvsgp qslltplhlg alcvalgvlt piialiwqat qadlshwdnl
       61 ltyvlpvalk ntvlllagva vmvgvigvgs awavtawdfp grkilswall lplamptyiv
      121 afawldllhp igplqtfirf llgfdsprqf rlpdlrslsg aiillglvly pyvylttram
      181 fisqpahlle aartlgcsat gtffrvalpm arpalavgis lalletlndi gaseflgvqt
      241 ltvtvyttwi srsdlsaaaq iacmmlmfif liltlefygr rkqgfssrsl reiqpsrvqg
      301 wrgwllggvi slpvvlgfla pvlflmwesa krigdenpls ssllsalqnt lslaagttlv
      361 vvcvsmlvaw sarhsaadna mpgfrrgvmr laslgyavpg tilaigflpp amavdrwlad
      421 lldvrglplm sagillvicc amrfqaiaig aldsglgrip psleqasrll gengagtfar
      481 vhfpllrpal vssallvfad amkelpttll lrpvnfetla tllyaeaarg tyeegaiaal
      541 mivlagtlpv illvrhqmtr rg
//
LOCUS       WP_284969711             474 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284969711
VERSION     WP_284969711.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>474
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          17..424
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 msketlshdf lntsldnisk lktilymtid eigdgliffn tfnkvtfvnk sllnmlelde
       61 klikspslme ympksfldki tknlnidnmi iyideidkkf ilskkpfyly kniegclitl
      121 kdvnnieile qkirsdsvkr gyvakykfnn iignssiikd cikkakkmal tdnpilitge
      181 tgtgkeaftq sihnhsnrkn kpfvaincas lpsellesel fgyedgsftg akkggkkglf
      241 elahtgtifl deigdmphdl qvkllrvlqe keirkiggts iipidvrila atnkdlekli
      301 ienkfrmdlf yrismftldl pplrnrledi plllesflke lpyknikldk nllealnsyt
      361 wmgnirelrn cieymaymgs nyltindlpq nissklnnnh mssnvsifnd lsqydknici
      421 silkslhmkp mgrtklmkfm eynvteyevr nmleylthng ylisnkgrkg ssit
//
LOCUS       WP_284969743             230 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase, partial [Clostridioides difficile].
ACCESSION   WP_284969743
VERSION     WP_284969743.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>230
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          12..227
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mekkyfkihg vpsilwgnps sklyiyihgq ggnkeeaeaf aniavphecq vlsvdlpehg
       61 erkgeknsfd pwhvvpelvs imeyakchwn qislyansig awfsmlsfek enlrecifvs
      121 pildmqklis nmmlwanvse eqlkheliip tsfghtlswe ylqyvkqhpi iqwnvptkil
      181 ygkhdeltei gvvekfvekf ncnltimeng khwfntpqel nslyewlntl
//
LOCUS       WP_284969799              97 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284969799
VERSION     WP_284969799.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 97)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 97)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..97
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
     Region          <1..90
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 ikledvsyev gfsvyyftkf fkkntgktfi tflneyrlek akwillnnni sivdlveevg
       61 fgstktfyrv fkekigvspl efkkrynsle kkggvsk
//
LOCUS       WP_284969844             469 aa            linear   BCT 25-DEC-2024
DEFINITION  MBOAT family O-acyltransferase, partial [Clostridioides difficile].
ACCESSION   WP_284969844
VERSION     WP_284969844.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Hofmann,K.
  TITLE     A superfamily of membrane-bound O-acyltransferases with
            implications for wnt signaling
  JOURNAL   Trends Biochem Sci 25 (3), 111-112 (2000)
   PUBMED   10694878
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004295
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>469
                     /product="MBOAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
     Region          1..469
                     /region_name="DltB"
                     /note="D-alanyl-lipoteichoic acid acyltransferase DltB,
                     MBOAT superfamily [Cell wall/membrane/envelope
                     biogenesis]; COG1696"
                     /db_xref="CDD:441302"
ORIGIN      
        1 mlfssliflf yflpitlvly ytfrfnrtiq nmillavslf fyawgepkfv vimitsiimn
       61 yifgllvdky reskikvrif lvlmcaynig vlfifkylaf alrniselin tqltipnivl
      121 pigisfftfq gmsyvidvyr rhgevqknpf yvglyiaffp qliagpivry esvaeqilnr
      181 ketwnkfsig tcrfitglgk kvlisnnmai vadyiytmns qgeiaaslaw lgsiaytlqi
      241 ffdfsaysdm aiglglmfgf kfeenfnypy isksisefwr rwhislgmwf ksyiyfplgg
      301 srvankdimi rnmfivwlft giwhgaewtf viwgilnfvf liierfimfe kienhnfikh
      361 iyallvvnfg wvlfrapnlk eaynyfkamf ggngviwsdy tymflkeywi ffifafifsv
      421 piakkinkfv veqakysmif nvfypisail lffisvtylv tgsynpfiy
//
LOCUS       WP_284969888             219 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase, partial [Clostridioides difficile].
ACCESSION   WP_284969888
VERSION     WP_284969888.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>219
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
     Region          1..>219
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mikltdeefi vlvnhvkkey gidlskkral iegrlyntmi erklssfsqy mnllfkdktg
       61 neainlinrl stnhtffmre pqhfefiqns ifpfweennk irniniwsag cssgeeaysi
      121 amtlddyfgy nkelwnikii atdistnsle kakrgiyies nvnnvpelwk kkyfidnkdg
      181 tfkicdkirk svifkpfnlm ndfsyqhfdl ifcrnvmiy
//
LOCUS       WP_284969889             457 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284969889
VERSION     WP_284969889.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..457
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <4..449
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 laciililqy skkmiklekl nvdlkniayk deltgvntie kfkldanqni cmhkdkkfav
       61 fyidfenfky indifgydyg dmilkryanl mmndigkyei fareiadrfv alrcyidked
      121 lvvrqrivds elinttneik nkhsitvvsg icciedvnek lsidglinra nfaqktvknk
      181 pgtnyafynd sirkkmieen tiksriheai ekrefivylq pkvnlhnqki ncaealvrwl
      241 tpdkgiispa ifipvleknf fialvdkyvf eevckwirkr ldenkpfvqi svnvsriqfy
      301 ntkfvetysn iqnkyripkn tieieftesv afenqnhlle iihdlhengf tcslddfgkg
      361 ysslsvlkdl pfdalkldsm ffkasldkdk ekiviknivh mlkelnittv aegieyeeqv
      421 eflrdigcdl vqgfvfykpm pilefeeild kefvyns
//
LOCUS       WP_284969964             583 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284969964
VERSION     WP_284969964.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 583)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 583)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..583
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <163..580
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 iekipifitf llnqiyslll pipaalvsfy vmaiiyqdir ymkkrllfls iplliciils
       61 itnpfthilf glsketgyir gcgyvatfss fffyaiysal lsfkyrkamh eskiwairgf
      121 livsivaiil qaiflqyllt gtacacslll tylsmqnrgl iiddltgvln rqsfiqeldl
      181 ninteqsgfi itialddfkf mnetfgtkng dialkevgky lvhihdvnhv yriggdifsi
      241 vvnsqlgikp edlikkieer fkktwlveei sfnlatsiav vyypenaett edvivaidfs
      301 iheakrsesr rvvyadasis ekikrkhvik ncleealknd gfevyyqpif snsrgrftsa
      361 eallrlehke lgfippdefi tiaeqtglin liglvvfekv crfiasdefe glkldniavn
      421 lsvvqcmqkn laddllylmd kynisptkfk leitetvamg sfniiketme rlidlgvkfa
      481 lddfgigysg vsnmlslpfs vikldksliw smnedsrhkl tvetiialin klnmkavaeg
      541 vetikcaedl iameceylqg yyfskpiped afknllkena ftg
//
LOCUS       WP_284969992             189 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284969992
VERSION     WP_284969992.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..189
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          10..>66
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Site            order(68,71..72,75..76,78,105,108..109,112..113,115..116,
                     143,146..147,150..151,154)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          68..98
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          75..177
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Region          103..137
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          142..165
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 ligmglyliq skkrienlnn qisskeekls etdkklgets kklektnkel nevknkeper
       61 kitvadeedl yyqaldlkkk keyekaienf ksivssgktk kyisesiyql aitnkllgnk
      121 deaikyykky intytkndqy yddsyyelgm lyydngdlkn aqqtfyslrs evpdsmynns
      181 kikeilsek
//
LOCUS       WP_284970043             340 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284970043
VERSION     WP_284970043.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..340
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <34..336
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 yieeeditkr lktifeeldm fnnnqeekyk lvlscgiyfi lpedrdinsi idraniphkm
       61 akgghkssya fydnkihdqe ikekementm fsslenkefi iylqpkieln tgeiqgseal
      121 vrwkrpdkgl ippnefipff erngfvinld lyvleevciy lrkwidagin pvtvsvnvsr
      181 ihlycnnfie tykniidkyn ipakyielel tesiifdnfd ilidimnnlk kigflismdd
      241 fgsgysslnm lkeipmdilk ldqkfimety nskrskiivt kviemakelg mkvisegvet
      301 eeqfellkev kcdmaqgylf gkpmpieefe hlivsnlvrg
//
LOCUS       WP_284970163             147 aa            linear   BCT 25-DEC-2024
DEFINITION  ferritin-like domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284970163
VERSION     WP_284970163.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..147
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          22..145
                     /region_name="Rubrerythrin_like"
                     /note="rubrerythrin-like, diiron-binding domain; cd01046"
                     /db_xref="CDD:153105"
     Site            order(34,67,70,97,130,133)
                     /site_type="other"
                     /note="diiron binding motif [ion binding]"
                     /db_xref="CDD:153105"
ORIGIN      
        1 mkgemvwade hrigvaqgvd aeiieglran ftgectevgm ylamsrqadr egypevaeay
       61 kriafeeaeh aakfaellge vvvadtkenl rvrvdaeyga tdgklklakr akelgldaih
      121 dtvhemckde arhgkaflgl lnrhfgk
//
LOCUS       WP_284970182             341 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284970182
VERSION     WP_284970182.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>341
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          <23..341
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mdkhsdsvmy ggmevyniwg tttvdsiige sdvmralknr ickignsdst vaitgesgtg
       61 keliaraihl agnrgnktfv aincaaipep lleselfgyt kgafsgadsk gkigkfelan
      121 ggvvfldeig dmpiqlqskl lrvlqekkfa rigsnelidi dvriisatnr dlfelvkenk
      181 fredlyyrln viplevpplr ergddiqili nnfidkysrk mkknvyhiep dveqmllkyp
      241 wpgnirelen tielalnlle edgiihkgii nrkileyfkl nninikllee sdyeismeqd
      301 iltleefera yikkvlkfyg ndtkskklaa kklgislatl y
//
LOCUS       WP_284970203             156 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator, partial [Clostridioides
            difficile].
ACCESSION   WP_284970203
VERSION     WP_284970203.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..156
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          <72..148
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 invttqniie tetyqstyif ylgeldskad fdfrlqlcsd llphiikdna enkflnlfdi
       61 iryktldlin edniinklid fnkiksidee llytgikfin ndlnisktst smflhrntlv
      121 yrlekineil gfdlknfena mifylsvksy flykki
//
LOCUS       WP_284970205             334 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284970205
VERSION     WP_284970205.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..334
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          98..334
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 nnkndyiyii yfplniskvn mffdggkfig gksiifsiig iifliilvsg iaygywvtkc
       61 isnitsavsd iskrsylpvn ikgvfadiyn slnilneeih ksdeiqnktd imreewisni
      121 thdlktplsp ikgyaelltd sstnyspekv hkyasimlkn ieytntlind lkltyqlkng
      181 iiplnknnyd lvrflkelsi dilnypeyes nivefksnid ninfdfdctl lkrafsnliv
      241 naftygdknt kvcvhitlne rieiiisdng kgmsreeasn lfnryyrgsn tkqkiegtgl
      301 glaitkqiie vhggnisves ipglgssfyi tfpi
//
LOCUS       WP_284970272             379 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284970272
VERSION     WP_284970272.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..379
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <1..375
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 gyevgneilr nltkiikrni feeemfaris adnfiiimky ieeeditkrl ktifeeldlf
       61 nnnqeekykl vlscgiyfil pedrdinsii draniphkma kgghkssyaf ydnkihdqei
      121 kekementmf sslenkefii ylqpkielnt geiqgsealv rwkrpdkgli ppnefipffe
      181 rngfvinldl yvleevciyl rkwidaginp vtvsvnvsri hlycnnfiet ykniidkyni
      241 pakyielelt esiifdnfdi lidimnnlkk igflismddf gsgysslnml keipmdilkl
      301 dqkfimetyn skrskiivtk viemakelgm kvisegvete eqfkllkevk cdmaqgylfg
      361 kpmpieefeh livsnlvrg
//
LOCUS       WP_284970310             230 aa            linear   BCT 25-DEC-2024
DEFINITION  tRNA 2-thiocytidine biosynthesis TtcA family protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284970310
VERSION     WP_284970310.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19235256
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>230
                     /product="tRNA 2-thiocytidine biosynthesis TtcA family
                     protein"
                     /GO_function="GO:0000049 - tRNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
     Region          16..195
                     /region_name="TtcA-like"
                     /note="tRNA-cytidine(32) 2-sulfurtransferase and similar
                     proteins; cd24138"
                     /db_xref="CDD:467514"
ORIGIN      
        1 msiqkllska rkaiqdfdmi qendkiavgl sggkdsltll hilksyqrfs pqnfeliait
       61 lntggvdnsp ldklckeinv pfyefqtdik eivfdirqek npcalcanlr rgalndnakk
      121 lgcnkvalgh hkddaietfl msmfyegrvn cfspktyldr qdltvirpmi yieeymtkki
      181 skdsnypiit npcpanghtr reyiknlian lnkempdfkr nvfgalnnse
//
LOCUS       WP_284970315             299 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284970315
VERSION     WP_284970315.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..299
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
     Region          <209..294
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 iynefplnpk srlyvlkenl lmmsefiqei akrnffenql sikdeeilks rkenirleea
       61 lkkansrlle eeyiinpidm fnnsskeypf elelyiekei knmnlegvyn lidtnklryn
      121 dvrdtiqemi fvlsrtvlrd ledlklisyl rnkynkkisl vnsdedlwnv lfefskecid
      181 knrafwrkdk gnlieniney ikkyykenin lnsisdvffi spnylssifn ernkvsitey
      241 inllrieesk kylldrsmsi sdickkvgfn nssyfsqifk kfnsitpney rknmldnky
//
LOCUS       WP_284970366             283 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284970366
VERSION     WP_284970366.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>283
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
     Region          1..274
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mrfidlrsdt vtmptdemre amakapvgds ifrddptvnk leelaaakvg kedaiflpsg
       61 tfgnqlalft hclrgqeiii gkgyhivthe vgapaviagv qlrtidedes galnpelvek
      121 airrddihep qtglicvena ysggtvvsld nlreikkiae khnlpvhldg arlfnaaltl
      181 gveakeiakc cdsvmfcvsk glaapmgsil agskefiaka rrkqkvmggg mrqvgivaaa
      241 giiaiekmtl rlnedhenak ylacelnkid gievnnvnpd ism
//
LOCUS       WP_284970394             210 aa            linear   BCT 25-DEC-2024
DEFINITION  MORN repeat-containing protein, partial [Clostridioides difficile].
ACCESSION   WP_284970394
VERSION     WP_284970394.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Zhou,J., Liu,H., Lin,Y. and Zhao,J.
  TITLE     Membrane occupation and recognition nexus (MORN) motif controls
            protein localization and function
  JOURNAL   FEBS Lett 596 (14), 1839-1850 (2022)
   PUBMED   35568981
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Sajko,S., Grishkovskaya,I., Kostan,J., Graewert,M., Setiawan,K.,
            Trubestein,L., Niedermuller,K., Gehin,C., Sponga,A., Puchinger,M.,
            Gavin,A.C., Leonard,T.A., Svergun,D.I., Smith,T.K., Morriswood,B.
            and Djinovic-Carugo,K.
  TITLE     Structures of three MORN repeat proteins and a re-evaluation of the
            proposed lipid-binding properties of MORN repeats
  JOURNAL   PLoS One 15 (12), e0242677 (2020)
   PUBMED   33296386
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..210
                     /product="MORN repeat-containing protein"
     Region          <71..178
                     /region_name="COG4642"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443680"
ORIGIN      
        1 cvficlssvf iftqlarvfi nkkkinqkik srngfrydrd fiearreeih ikdnnnnknk
       61 snnkklkeek vfkydngdly kgefvdgkkn gfgiyifssk ekyeglwkdd kmhgigkyty
      121 rdgsiytgef kyglknglgk ltypnndiyk gyfldnkkng kgvlykndgn kqvgiwedde
      181 qcksldfkdl nnnkinnvyq nrlnnnklkv
//
LOCUS       WP_284970449              51 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284970449
VERSION     WP_284970449.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 51)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 51)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 51)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 51)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 51)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 51)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..51
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..51
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <2..50
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 lykcdkgrse kgsglglsia hqlvekmngt itansiqgkg teftllfpla k
//
LOCUS       WP_284970512             312 aa            linear   BCT 25-DEC-2024
DEFINITION  C45 family autoproteolytic acyltransferase/hydolase, partial
            [Clostridioides difficile].
ACCESSION   WP_284970512
VERSION     WP_284970512.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   True,J.R., Yeh,S.D., Hovemann,B.T., Kemme,T., Meinertzhagen,I.A.,
            Edwards,T.N., Liou,S.R., Han,Q. and Li,J.
  TITLE     Drosophila tan encodes a novel hydrolase required in pigmentation
            and vision
  JOURNAL   PLoS Genet 1 (5), e63 (2005)
   PUBMED   16299587
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Tobin,M.B., Cole,S.C., Miller,J.R., Baldwin,J.E. and
            Sutherland,J.D.
  TITLE     Amino-acid substitutions in the cleavage site of acyl-coenzyme
            A:isopenicillin N acyltransferase from Penicillium chrysogenum:
            effect on proenzyme cleavage and activity
  JOURNAL   Gene 162 (1), 29-35 (1995)
   PUBMED   7557412
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Tobin,M.B., Fleming,M.D., Skatrud,P.L. and Miller,J.R.
  TITLE     Molecular characterization of the acyl-coenzyme A:isopenicillin N
            acyltransferase gene (penDE) from Penicillium chrysogenum and
            Aspergillus nidulans and activity of recombinant enzyme in
            Escherichia coli
  JOURNAL   J Bacteriol 172 (10), 5908-5914 (1990)
   PUBMED   2120195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF040521.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>312
                     /product="C45 family autoproteolytic
                     acyltransferase/hydolase"
     Region          12..312
                     /region_name="C45_proenzyme"
                     /note="C45 family autoproteolytic
                     acyltransferase/hydolase; NF040521"
                     /db_xref="CDD:468523"
ORIGIN      
        1 metlevrnie lsgtnyeigy rlgelvanmp eiiegqinks nlvskkeeke mielfdkycp
       61 glneelqgfa daiqvncnqi lyytmtylkp gcsqvalape ltenghvlfa rnfdfshnme
      121 dfvlcktkvn gkyahigttv mqfgrgegmn ecglgvsqss cgipvgnsdg lrkpaivglq
      181 fwavirylle nckdvdeale ylkdmpiayn inllladksg nialvetldg kkevniinsl
      241 eskreyflhs tnhthidklh klepqsmkns ihryklikey inkskkigek elmnllssky
      301 pnglscnyyn df
//
LOCUS       WP_284970517             576 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator, partial [Clostridioides
            difficile].
ACCESSION   WP_284970517
VERSION     WP_284970517.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>576
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
     Region          10..538
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mlvsrqiefl klilnenkyr pikyfkdkln vsdktlqkdl kmiekyletf nikidikrgy
       61 giliedlakk nidlinslni qskenkslsv eqrrmeilky lllnsnnits inqladkyyv
      121 sktsivndfk yieawikeyn lklnktlegt kiigkevdir ksiakmmddl ldenyeqhdi
      181 seltrldsat fsalinlfdi dsiifvetii teleynlgyt inqpyyinli thiliclkri
      241 eegnqiesqe ereisvdnld elvyknvttl idkienryrv kitkdelmyi yiflvssgfs
      301 sesnssynde sdrlsesekv ssimienmsr flninlkndd llqkslashv rpmlnrlryd
      361 iqiknpllge iqerfsdvlg lcmmtinimt eydnlknisi devsylatyf qaaiernmss
      421 krvivvchtg ygtsqllaar lkrefpewti vdivpmhqls krnlddvdfv istvnldlkd
      481 klhivvsvll mendinnikn allskpkksm nldtnllgmy ledniyfnfd vaqmesligv
      541 nlgskyesis lgkdlniyih kqsklnkgim ninnvt
//
LOCUS       WP_284970580             351 aa            linear   BCT 25-DEC-2024
DEFINITION  coiled-coil domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284970580
VERSION     WP_284970580.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>351
                     /product="coiled-coil domain-containing protein"
     Region          284..>340
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 msiilvkdik qdiesmprki ldisliednk sdltffniee edgdetlkal kqsyvttnyk
       61 eetllnlqga lnsksdttsk elklesykry nnaldlaykn yitsainmvn kaleinpkdi
      121 dilnlrgllk llkcdfaksf esfytalcye nnhisrkyvn lissedfktf lgrynhsirf
      181 ineelnyesi hileniieee peliepyvil sllydklgnv kkregyldkl keldkdnpvf
      241 ekneeekedt skkeeikkvk rkksilpyii vgcvligmgi yliqskkrie nlnnqisske
      301 eklsetdkkl getskklekt nkelnevknk epereitvad eedlyyqaln l
//
LOCUS       WP_284970622             581 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284970622
VERSION     WP_284970622.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>581
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          165..581
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mmimigleyi ksdiqniaea ivsvlnidvt ivnkelfria gtgvyidkig ekvdkytafk
       61 kslteqitil iddpkssdic recyksgacv efaevccpii cdgvshgvig liaftkeqaq
      121 iiennksgli nflgkmadli snklkaqikt yelelekkkl etllnnmdka vvsidvdgki
      181 dkynskfkel fnikdsitgk nifveldfik kpsinnfkkd kscsffykry gydskgiyni
      241 nkivlknelk gyvidfidkr daiknynkmn kdyrikleni igesvairns kkealiasks
      301 tstvlitges gtgkelfara ihnhsnrvdn pfiavncaai pdnlleself gyeegaftga
      361 kkggklgmfe vahkgsifld eigdmslhlq skllrvlqek elnkigsksn vsidvriiaa
      421 tnkdlekmvq ngtfredlyy rlnvipiklp slrerkedip liikhmvkey skkldknvid
      481 idsrvvdamm eykwpgnire lqniieysvn mssssiitmn vipqkiknts veelevksdr
      541 iipldelekm eiikalnkyk dykkdkelta kalgisratl y
//
LOCUS       WP_284970629             602 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase, partial
            [Clostridioides difficile].
ACCESSION   WP_284970629
VERSION     WP_284970629.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 602)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>602
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
     Region          31..492
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mkirrylilv iiilittsqs fisyglerfe eitifhtndi hgryaegddh iqignlatlk
       61 ketpnsilvd agdclhglpi vnmdrgksai elikcagydy itpgnhdfny gkdrlfelsk
      121 sanlgentlk flssnifeng kkvfdsndik eidgikigff glstqetkik tgfknvegle
      181 fknpiesate qvnelkgkga nvivaichig tnslskpnsi dianevqgid liidghshtk
      241 fengkqvgdt livsagqyle nigeikltld tndvenikie nksvrligke ealkykldsa
      301 vskkvdeike qqekildkvi gvttntldgs yenvrtketn lgnlisdill dktkadislf
      361 nggnirdtie kgnitrrdiv dvfpfsntiv tkeltgaqik dvlehgvkly pekssaflqv
      421 ggisyyfnpk qkegekitni qkegkpldln kkyvvatndy iasggdefpc fskepvlkef
      481 gnlesaviey ieykkeiskn vdgrigiksk delisknhes dlilsenekn indneenlsn
      541 nikssdsdkn ksldktsare ssnlgiskre akekspktgd lgfsnsiiif ivsstlicll
      601 nf
//
LOCUS       WP_284970641             550 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator, partial [Clostridioides
            difficile].
ACCESSION   WP_284970641
VERSION     WP_284970641.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..550
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
     Region          6..536
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 nkillgekis iekltnemll skntvvqtit dvkkylqtmg lrleykgkyk iigdeyvire
       61 lfliivqenv leinsiseev ssfdtkghik ltdysllnlt kfveflnkri rdgktlysyk
      121 ylneakkisy fsnckellce eaneneqayi ctyisslpsl nsevkedvve eyvdklidkf
      181 evntaikles khefkknilr hlhssynrir fkfpirnpml detkykhesl ykiiksiien
      241 eeefpvfegi reeeigfiaa yfggylrgsr dnglrrnkvl lvcpnglmvs ksleiqlyky
      301 iptieivgiv sikqlkevnv yydyiittid iqnvnnvivv nplltssdvq llmnklisvk
      361 enekyfnlel iiqairkngv inneealkad llniihkide gemyqpmlke linaervnii
      421 knvrdwkeai kiaskplled nsieelyien miksvekygp yivladrfal phasskegvn
      481 klamsllive devdllgkpv nifmvlaavd ntthiralas lsemmyeeen vkliingdks
      541 silelinkqn
//
LOCUS       WP_284970735             107 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284970735
VERSION     WP_284970735.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..107
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
     Region          47..102
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 niddyniepk afiirykkdl nrfdvtgpis ysvninttvv gyghiekgnp vhlvqllcqq
       61 ingssinpds kfgpdtynqv kilqgrlgvt kdgvvgkatw qaagery
//
LOCUS       WP_284970768              64 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284970768
VERSION     WP_284970768.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 64)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 64)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 64)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..64
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..64
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
     Region          <1..57
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 neyrlekakw illnnnisiv dlveevgfgs tktfyrvfke kigvsplefk krynslekkg
       61 svsk
//
LOCUS       WP_284970783             454 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator, partial [Clostridioides
            difficile].
ACCESSION   WP_284970783
VERSION     WP_284970783.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..454
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
     Region          <2..449
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 tlfkknnfyv tdemlrevin yivvlvyrvk eekkvkdydv kfdllksyde yfiareikhi
       61 isgmfectln deeiiyltip lvsgnapase calnssrisk nidelmenif nqiyvdmgif
      121 inedelrvgl gyhlsftlnr llfniklknv lleeikqnyi lpfklaqiag kviekkynle
      181 vsedeigyia ihfsgylern ssrfysikki aiicstglgt akllkirvek lignnpkidt
      241 lssfnlrnin ldeydivftt idldtsnint ivlkintifd enklreqlkt vlclregnid
      301 ttnstnllin nlldedkfmi lnektilasl ekmmdhlmdl gcidekfrkn ivnreekspt
      361 vfdkgllfph sineksdkfl mavgileepi eyanrsikii lmtmfpcenk idsdllvkiy
      421 eevlkigqdv kltnkiskcr tflefkkvll knli
//
LOCUS       WP_284970798             108 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator, partial
            [Clostridioides difficile].
ACCESSION   WP_284970798
VERSION     WP_284970798.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>108
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          9..106
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 myniddmiyn cpvealsnil gkkwvaiiiw kiqedkkrfg elqraipdcs kkmlvqqldf
       61 lieqgiivnq kklvnnvves tyflsesglr llpvmekmim wsnknlnc
//
LOCUS       WP_284970866             444 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator, partial [Clostridioides
            difficile].
ACCESSION   WP_284970866
VERSION     WP_284970866.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..444
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
     Region          <1..440
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 ineyainnil lhlmitidri kknnyiesve vvnyidnnnd isisrdisnf leseynitlt
       61 saelyylvfq ltnkttvlny hemdtkslpn yidehfvklt kkiiknvydl yfidlsddef
      121 vvkftlhvkn lisraknnqv lrnqipqklk dsypliydis vyicnqiqil enieidedei
      181 syislhvgsf fdrqklledk ilcalitpny ydlqfkivrd lekrfnesie iiqifsdthn
      241 ldfdnkvdmv ittlpisdrc pipfvyvnpy lnrkdydniq skfiqikdrk niltvqnhle
      301 myfseslfmk niyldsakdy irfmgnilye nkyvkpnyid dvlirekmss tafnnnvaip
      361 hsmkmdalkt gvclivndkp vkwgeekvqi iamipineke kekfnyifes fieilsewnn
      421 vkeltkadny ssfmnriayl iqni
//
LOCUS       WP_284970878             196 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator, partial [Clostridioides
            difficile].
ACCESSION   WP_284970878
VERSION     WP_284970878.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>196
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          1..>195
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mskvkrltdv wiyindkqkf tikelseefn lsaktiqryl kelnkmglpi qaeqgrnggy
       61 rvlnnsyipp viftekevmi ilfalkslqi ynyklmeiei nsimrkvsye rkssikvgie
      121 nikryigfva ndtndgdfks snvteffras seslilniky kcgnqilekn vcpigiylnk
      181 gawfspaydc ksdkii
//
LOCUS       WP_284970904             457 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284970904
VERSION     WP_284970904.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..457
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <39..427
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 klyedkinlg linnsdkfin itkdenflkh vqnyiisnek encvmacfdl crlklindiy
       61 gyelgdevln nilsnlknyf gkeaiygklk sdvfvliikl enreqkipyl vnliknkivi
      121 lsqidsfkmd inieasigiy kfnnneidik kaidnadmar lkskglkhie yvefdnamee
      181 eiqsimkier dlflaiknke fvihyqpkvd sstgniigse alirwlhpsl gmvgpnkfip
      241 iaeknglinn igrwliqevf itinkwiseg invlpvsinl srvelykndl vdffklmfnt
      301 ynipkeliel eitettalrd vkfiserlye ikslgmnisl ddfgvgnsnf inlkgipldi
      361 ikidrslild ivtntktkfm vkaivnlshd lnvtvicegv edmhqvkvls elgcnfiqgy
      421 vffkpldemn ykklltdgsy inlkdtlldk cmtveee
//
LOCUS       WP_284970947             444 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284970947
VERSION     WP_284970947.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..444
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <11..439
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 lwklsnakli eqlkklayyd slsgiknkek frkdsmyilk nyyqdnfylv qldvnkfkyi
       61 nemfgyaegn kilihisqvl nnntnkyeic armdndhfil liacntedel lnrlskinke
      121 icnlnttnss kykivmssgi ykitkkddik kidllidran iaakskkeky ehsysffned
      181 trnrlykekr lednmnkale kgefivyyqp kyslddvnei egaealirwn spefgfispi
      241 dfvplfekng fivnidmfvf eevcktlnkw inkgytpvpi svnmsrvhly rdnfienitd
      301 liskynispe fieleltesv vfdnlnilid imkkikeigf lismddfgsg ysslnllkdl
      361 sfdilkldrg fliettdtkr gkiiiskive makaidikvi cegvetyeqv eflkeigcdk
      421 vqgylfakpm vldefekhln fkfd
//
LOCUS       WP_284970956             448 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284970956
VERSION     WP_284970956.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>448
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
     Region          3..446
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mnlidilnkv dafiwgppll vllvgtgill tvklgvvqit klpralklif saenkgsgdv
       61 ssfaalctal aatvgtgniv gvataikagg pgalfwmwia affgmatkys egvlaikyrt
      121 kdkngqvsgg pmyyivngmg ekwrplaiff aisgilvall gigtftqvns itdainnsfg
      181 idpritgvvl avfvalvvfg glksisnvat kivpfmaviy vvicgiilis fwnkipetfm
      241 liiksaftpt aatggflgat mslairngia rgvfsnesgl gsapiaaaaa ktewpaeqgl
      301 ismtgtfidt iiictltgfs lvisgvwcsd lngavmtqaa fngaiptfgp illtvsltlf
      361 afttilgwsy ygercfeflf gvkgmngyrt vfvamvllga flklevvwii adivnglmai
      421 pnliallals piivsetkky fehinspe
//
LOCUS       WP_284971001             279 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284971001
VERSION     WP_284971001.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..279
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          100..>156
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Site            order(158,161..162,165..166,168,195,198..199,202..203,
                     205..206,233,236..237,240..241,244)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          158..188
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          169..267
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Region          193..227
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          232..255
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 lnyesihile niieeepeli epyvilslly dklgnvkkre gyldklkeld kdnpvfekne
       61 eekedtskke eikkvkrkks ilpyiivgcv ligmgiyliq skkrienlnn qisskeekls
      121 etdkklgets kklektnkel nevknkeper eitvadeedl yyqalnlkkn keyekaidnf
      181 ksvvssgktk kyisesiyql aitnkllgnk deaikyykky intytkndqy yddsyyelgm
      241 lyydngdlkn aqqtfyslrs evpdsmynns kikeilsek
//
LOCUS       WP_284971032             120 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284971032
VERSION     WP_284971032.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..120
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
     Region          <12..111
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 snikieysye filaiqliiq nsgnissqei skkvfyssrh lnrlfnqylg lsmksfsrlv
       61 rinksiklln nnktswmsic nelgfydiph fikdfkivcg itpqkyranm sdfyseiakf
//
LOCUS       WP_284971037             200 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase, partial [Clostridioides difficile].
ACCESSION   WP_284971037
VERSION     WP_284971037.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>200
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
     Region          23..197
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mindiknkfk nykpyingyk nmkrasvlip iveinnthyi lfevrsknlk hqpseisfpg
       61 gkiesgetpy eaviretcee lgtfsdniev issldllitp vkfiihpylg yikninnlni
      121 nkdevdhtfl vpikyllenp pntysntvkv fpdenlpygs ipnqkdykfe sgsypilfyk
      181 ykdyviwgmt akilenflnf
//
LOCUS       WP_284971135             374 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284971135
VERSION     WP_284971135.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..374
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <1..374
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 indtfgyefg dnllitiaka lkeeltegev yarlssdyfa ifcdykngrn kiirkldnir
       61 sniesnlsiv feislcvgiy fveegevdiq kavnkanmar svakgkniny aiynedvrnk
      121 lseesmildd ikialvknqf evyyqpkfsl vtgemigsea lirwnhpehg fispavfipi
      181 aeksklilki grfvfervcn dlyewkkqgk kivpvsvnls rvelyqpdiv kfinktikmy
      241 nlssdfieie itetvainel nilknvlnel rtygfsismd dfgtgyssis clrdmpidil
      301 kldksflggi ehdersrnia ksivslaksl dlvviiegve skeqaelmkq fgcdlvqgfy
      361 farpmpaknf ldll
//
LOCUS       WP_284971141             450 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284971141
VERSION     WP_284971141.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>450
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          1..450
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mnqeiffkim neilenideg vhfvnkdgkt iiynnsvqkm ekmnrhdilt nsffdivnkm
       61 kinrstllev lekrevikdn iqkyldkngr eitainttip idikgefvga leisknmtti
      121 enllnrnykk nlvnkvsirq kkgyefddil gesnlikeai akskkacksd asvfiygetg
      181 tgkelfsqsi hygsnrknyp fiaqncaalp eslfegilfg tskggftgai drpglfeqan
      241 kgtllldein smpimlqakl lrvlqegyvr rvggtkdipi dvriiattne spkvilnehk
      301 mrkdlyyrln iihikipplr drkedipllc kkfiskynkk lnkkvvgisd eaikilknyd
      361 wqgnirelen iiyctmsmme devqietsmi nlndyynlke nkesnnysln dledktlski
      421 iseieekyiy eslekasyni tkaasilgmn
//
LOCUS       WP_284971230             388 aa            linear   BCT 25-DEC-2024
DEFINITION  diaminopimelate decarboxylase family protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284971230
VERSION     WP_284971230.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Lee,J., Michael,A.J., Martynowski,D., Goldsmith,E.J. and
            Phillips,M.A.
  TITLE     Phylogenetic diversity and the structural basis of substrate
            specificity in the beta/alpha-barrel fold basic amino acid
            decarboxylases
  JOURNAL   J Biol Chem 282 (37), 27115-27125 (2007)
   PUBMED   17626020
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Kidron,H., Repo,S., Johnson,M.S. and Salminen,T.A.
  TITLE     Functional classification of amino acid decarboxylases from the
            alanine racemase structural family by phylogenetic studies
  JOURNAL   Mol Biol Evol 24 (1), 79-89 (2007)
   PUBMED   16997906
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..388
                     /product="diaminopimelate decarboxylase family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
     Region          1..366
                     /region_name="LysA"
                     /note="Diaminopimelate decarboxylase [Amino acid transport
                     and metabolism]; COG0019"
                     /db_xref="CDD:439790"
ORIGIN      
        1 cyiydetnii ekckelknni lgfdflysik tnpynkivks iaeqgfgada sstnevmiss
       61 kcgvskddiy ysspgkteid ietvldkcii iadsiteiel inkiskkhnq kvkigirinp
      121 dftmdddsak sskfgidied mssvfkmlsm cdyvsvvgih ihiksqvldf eklghyyekc
      181 ffialnlnks kyiniefinf gsglgvaydn lrenplnlke lskltqkiaf tnsntlksrl
      241 liesgrfivc ksgnyyvkiv gikvsrgkky livknglngf mrpiisnlie nitcgveleg
      301 qeplytsnha fslsvlnnlk eeeyvnvvgn lctsldvian nvklkkanig dlisisnags
      361 ysyslspllf ssyefpkqyy krkdgyie
//
LOCUS       WP_284971259             433 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator, partial
            [Clostridioides difficile].
ACCESSION   WP_284971259
VERSION     WP_284971259.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>433
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          1..433
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mkillvddel eygvvmkkil qkkgylvdia lsgeeainii kkdknydlvl sdvmmknmdg
       61 vqlldriksi nrdievilvt gygsienavd amkrgalsyf iksnpienll eevekvkask
      121 isvsvqknnf eftlesknrd fnniikiakk aackdvnili lgesgvgkdi laryihsisp
      181 rkneifvpvn ccsfsenlle selfghekgs ftgavdsrkg rfelsnkgtl fldeigdipl
      241 nvqvkllrtl edksierigs nksikvdfrl icamnkepkv eisngnired ffyristiti
      301 tipplrkrre dlttlieffl nkyqiehdkk ihsidkevkd fllnynypgn irelkniinr
      361 lvvlseegnl skdnlnlisn nvyiddkisi rplreirkef eceyiekvls lcgnnisnta
      421 kkleisrrql tnk
//
LOCUS       WP_284971268             433 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator, partial [Clostridioides
            difficile].
ACCESSION   WP_284971268
VERSION     WP_284971268.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..433
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
     Region          <1..428
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 ivvlvyrvke ekkvkdydvk fdllksydey fiareikhii sgmfectlnd eeiiyltipl
       61 vsgnapasec alnssriskn idelmenifn qiyvdmgifi nedelrvglg yhlsftlnrl
      121 lfniklknvl leeikqnyil pfklaqiagk viekkynlev sedeigyiai hfsgylerns
      181 srfysikkia iicstglgta kllkirvekl ignnpkidtl ssfnlrninl deydivftti
      241 dldtsninti vlkintifde nklreqlktv lclregnidt tnstnllinn lldedkfmil
      301 nektilasle kmmdhlmdlg cidekfrkni vnreeksptv fdkgllfphs ineksvkflm
      361 avgileepie yanrsikiil mtmfpcenki dsdllvkiye evlkigqdvk ltnkiskcrt
      421 flefkkvllk nli
//
LOCUS       WP_284971338             140 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_284971338
VERSION     WP_284971338.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..140
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <15..139
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 sqfeiyfkqe fmvsrinfne eklivkadpn klvrafenli tnavkygkdg hyvdivtekk
       61 edmavvkvin ygepipvldl pnifdrfyrv eksrnrnvgg sglglaitkn ivnlhdgeit
      121 vssdkyqtvf evqlpiiqsa
//
LOCUS       WP_284971466              81 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284971466
VERSION     WP_284971466.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 81)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 81)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..81
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
     Region          <2..76
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 fispnylssi fnernkvsit eyinllriee skkylldrsm sisdickkvg fnnssyfsqi
       61 fkkfnsitpn eyrknmldnk y
//
LOCUS       WP_284971498             193 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284971498
VERSION     WP_284971498.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..193
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
     Region          133..188
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 livtgcltli stslvfastn ndvnvsksne eqttnsftit gyefiyenap qpiksdyekk
       61 ckelninpsk ddtifinekf idsyninidd yniepkafii rykkdlnrfd vtgpisysvn
      121 inttvvgygh vekgnpvhlv qllcqqings didpdskfgp atynqvkilq grlgvtkdgv
      181 vgkatwqaag ery
//
LOCUS       WP_284971531             391 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284971531
VERSION     WP_284971531.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..391
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          3..329
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
     Region          325..>388
                     /region_name="COG1693"
                     /note="Repressor of nif and glnA expression
                     [Transcription]"
                     /db_xref="CDD:441299"
ORIGIN      
        1 idkkfilskk pfylyknieg clitlkdvnn ieileqkirs dsvkrgyvak ykfnniigns
       61 siikdcikka kkmaltdnpi litgetgtgk eaftqsihnh snrknkpfva incaslpsel
      121 leselfgyed gsftgakkgg kkglfelaht gtifldeigd mphdlqvkll rvlqekeirk
      181 iggtsiipid vrilaatnkd lekliienkf rmdlfyrism ftldlpplrk rledipllle
      241 sflkelpykn ikldksllea lnsytwmgni relrncveym aymgsnylti ndlpqnissk
      301 lnnnhmssnm sifndlnqyd knicisilks lhmkpmgrtk lmkfmeynvt eyevrnmley
      361 ltrngyliss kgrkgssite kgikiienni i
//
LOCUS       WP_284971582             139 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator, partial [Clostridioides
            difficile].
ACCESSION   WP_284971582
VERSION     WP_284971582.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..139
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          <32..131
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 yifylgelds kadfdfrlql csdllphiik dnaenkflnl fdliryktld linednilnk
       61 lidfnkiksi deellytgik finndlnisk tstsmflhrn tlvyrlekin eilgfdlknf
      121 enamifylsv ksyflykki
//
LOCUS       WP_284971701              69 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein, partial [Clostridioides
            difficile].
ACCESSION   WP_284971701
VERSION     WP_284971701.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..69
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          <1..57
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
ORIGIN      
        1 deaikyykky intytkndqy yddsyyelgm lyydngdlkn aqqtfyslrs evpdsmynns
       61 kikeilsek
//
LOCUS       WP_284971708             656 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284971708
VERSION     WP_284971708.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..656
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          192..568
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 lidflennlk lvfgdsinin ryfineindn dlinddvilv msverldkii nnildkkkvi
       61 vvrrtfredk iynllslpqg tnvlivndsd ettletislf ykigvtnirp ipymndnnyk
      121 nikiaitpgv pekvpsfisd ifdlghryid istfieiinl lqidskeiqs nlvkyseeii
      181 sldtgikdky kelflkieel dtilnlskdg ilftskdgei ntynskikdi ldinediygk
      241 yiedifvdsl kvllsekeil dkvvvfnkky invnkkniyn rdekmgtyys lqeityikkl
      301 eqnltkklre kgqiakytfk diktnspkmf ecidlakkvs ksdlsilirg esgtgkelia
      361 qsihnnsnrk nqpfiavnca avpenllesq lfgydkgtft gglkdgkqgl felanngtif
      421 ldeigdmple lqtkllrvlq ekqimpvgsh nvinidvrii satnknleqm idnsqfredl
      481 yyrlntipin ipplrerked iliimedlin kklvitpeak kliqnymwkg nirelqnvts
      541 ylnimcediv lekdlppnlr ssdnkntslk lkyskndiln ileililnke sdvgigrgli
      601 lkalldknlq itegkikkif eylkkeelii cssgrygski tqkgedfynk lkykgl
//
LOCUS       WP_284971941             422 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284971941
VERSION     WP_284971941.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..422
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <1..419
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 sqktiekvay tdfvtgysnw rkfeldvtnl lkktsqnnky amvifdidkf kaindiyghk
       61 kgnlilkdia dtlnelinin etfarvsadn fnilltynkk ediiniikki mvnnelvnls
      121 fgiyeikdka lsvsvysdra slakssiknn sdvnfaffnd elrekllled kiekemeyal
      181 esgqfvmylq pkyniklnkf cgsealvrwq ytekeviypg dfipvfeknr firkidmyil
      241 eqackeirsl fdkgisplpi svnfsrvdfl kkdfisnivn vcdrykipyg lieieitess
      301 mfgdtdilfn vsrnlqdigf ivamddfgsg yssvnmlkni plnvikldrg ffvddkdvdk
      361 sqiviksivs likqlgirvv aegietksqi emlkkancdi vqgyyfskpl pikefeklvy
      421 ki
//
LOCUS       WP_284972165             355 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase, partial [Clostridioides difficile].
ACCESSION   WP_284972165
VERSION     WP_284972165.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>355
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
     Region          7..355
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 msrvknvvel letkgvdaly ltkktnvnyi sgfpdeeaya vickdgnflv tdsrymelae
       61 kvckdfeiin whnfdrsvak avksvcdkvg ikklgfertn ivfdkyeelk nliekdngel
      121 iptenivetl ryvkdkdeik ntrkaceiad kaleeliphi kagvseiela tkleyfmkmn
      181 gaqnigfeti lisgaktsll hgkpsdkiie kgdfvlidyg amyngyisdt trtfivggas
      241 ekqleiynlv keaqnvgven mkagvhatip daeirkvvkk yedyyyqgig hgvgrdvhee
      301 pfignygdki ieegciitme pgiyfpgwgg vriedtvlit kngperltkf pkdlm
//
LOCUS       WP_284972206             462 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Clostridioides difficile].
ACCESSION   WP_284972206
VERSION     WP_284972206.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>462
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          1..462
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mnqeiffkim neilenideg vhfvnkdgkt iiynnsvqkm ekmnrhdilt nsffdivnkm
       61 kinrstllev lekrevikdn iqkyldkngk eitainttip idikgefvga leisknmtti
      121 enllnrnykk nlvnkvssrq kkgyefddil gesnlikeai akskkacksd asvfiygetg
      181 tgkelfsqsi hygsnrrnyp fiaqncaalp eslfegilfg tskggftgai drpglfeqan
      241 kgtllldein smpimlqakl lrvlqegyvr rvggtkdipi dvriiattne spkvilnehk
      301 mrkdlyyrln iihikipplr drkedipllc kkfiskynkk lnkkvvgisd eaikilknyd
      361 wqgnirelen iiyctmsmme devqietsmi nlndyynlke nkesnnysln dledktlski
      421 iseieekyiy eslekasyni tkaasilgmn rqnlqykikk yn
//
LOCUS       WP_284972341             568 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284972341
VERSION     WP_284972341.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 568)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 568)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..568
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <148..564
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 yllllpipaa lvsfyvmaii yqdirymkkr llflsiplii ciilsitnpf thilfglske
       61 tgyirgcgyv atfasfffya iysaflsfky rkamheskiw airgflivsi vaiilqaifl
      121 qylltgtaca csllltylsm qnrgliiddl tgvlnrqsfi qeldlninte qsgfiitial
      181 ddfkfmnetf gtkngdialk evgkyliqih dvnhvyrigg difsivvnsq lgiepddiir
      241 kieerfkkpw lveeisfnla tsiavvyype naettedviv aidfsiheak rsesrrvvya
      301 dasisekikk khviknclke alkndgfevy yqpifsnsrg rftsaeallr lehkelgfip
      361 pdefipiaeq tglinsiglv vfekvcrfia sdefenlkld niavnlsvvq cmqknladdl
      421 lylmnkynvs ptkfkleite tvamgsfnii ketmerlidl gvkfalddfg iaysgvtnml
      481 slpfsvikld ksliwsmned srhkltveti ialinklnmk avaegvetik caedliamec
      541 eylqgyyfsk pvpedvfknl lkentfts
//
LOCUS       WP_284972406             386 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Clostridioides difficile].
ACCESSION   WP_284972406
VERSION     WP_284972406.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..386
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <1..382
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 kyindlfgye vgneilrnlt kiikrnifee emfarisadn fiiimkyiee editkrlkti
       61 feeldlfnnn qeekyklvls cgiyfilped rdinsiidra niphkmakgg hkssyafydn
      121 kihdqeikek ementmfssl enkefiiylq pkielntgei qgsealvrwk rpdkglippn
      181 efipfferng fvinldlyvl eevciylrkw idaginpvtv svnvsrihly cnnfietykn
      241 iidkynipak yieleltesi ifdnfdilid imnnlkkigf lismddfgsg ysslnmlkei
      301 pmdilkldqk fimetynskr skiivtkvie makelgmkvi segveteeqf kllkevkcdm
      361 aqgylfgkpm pieefehliv snlvrg
//
LOCUS       WP_284972484             516 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Atlantibacter
            hermannii].
ACCESSION   WP_284972484
VERSION     WP_284972484.1
KEYWORDS    RefSeq.
SOURCE      Atlantibacter hermannii (Escherichia hermannii)
  ORGANISM  Atlantibacter hermannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Atlantibacter.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Atlantibacter hermannii"
                     /db_xref="taxon:565"
     Protein         1..516
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55987
     Region          22..498
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mnvkqlslvl lagwcshtla qevtviytnd lhahvepysv pwiadgkrpv ggfaniatlv
       61 kqekarnpat fyfdagdyft gpyissltkg kaiidimntm svdaasvgnh efdhgwdnal
      121 vqlsqakfpv llgnvfyqns slpfwnkpyt ilekdgvkig viglhgvfaf ddtvsasmrq
      181 gieardevkw lqhyldelrg kvditvalih egiparqssk gstdvkrald kdiqtasqvk
      241 gldllitgha hvgtpepikv gntlilstds ggidigklvl dvnpkagths vkrfelktlf
      301 adewkpdpvt qhtidnwnkq lrqtvsqtig etpvaltray gessslgnlf tdammaaapd
      361 aqfaltnsgg lradmdagti tlgdvistfp fpneltvmdl tgkqvrglme hsasltngvl
      421 qvskglemry dtrkapgsrv tqltlngkpi edkqvyrvat nsflapggdg fmaftegknk
      481 qvrggynlsd alidylkagn kidpavvnek rvaesq
//
LOCUS       WP_284972687            1653 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Atlantibacter hermannii].
ACCESSION   WP_284972687
VERSION     WP_284972687.1
KEYWORDS    RefSeq.
SOURCE      Atlantibacter hermannii (Escherichia hermannii)
  ORGANISM  Atlantibacter hermannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Atlantibacter.
REFERENCE   1  (residues 1 to 1653)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1653)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1653)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1653)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1653
                     /organism="Atlantibacter hermannii"
                     /db_xref="taxon:565"
     Protein         1..1653
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=179963
     Region          27..1653
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mirarhaala aalfamfslt gcddvksqaa gestpapaqk sqsaavsakp dsaklaqlag
       61 qsagkpltli dasevqldgs atlvltfsip ldpsqdfsrt vhlvdkkdgk vdgawelapn
      121 lkelrmrhle phrtlvasvd selkalneat fginwektie trdiapsvgf asrgsllptk
      181 vvqglpvmal nidnvdvnff rikpeslpsf vsqweyrssl tnwesekilq madlvytgrf
      241 dlnparntre klllplgdik plqqpgvyla vmnqagryny snaatlftls dvgvslhrfh
      301 nrldvftqsl engavqgnve iqllsekgqp laqaktdgdg hatletpkea alvlarsgdq
      361 ttlldlklpa ldlsefdivg eagyarqffm fgprdlyrpg etvifngllr dgdgkpvndq
      421 piklevvkpd gqvartevvq phnglyqftw plaasaatgn whiranigdn qprdwrfqve
      481 dfmpermalt lspqktpitp kdplaipveg hylygapasg nalqgqlflr plrdavpalp
      541 gyefgditee nlsrsldevq ltldeqghse valdsqwqda rsplkvilqa sllesggrpi
      601 trraeqpvwp avalpgirpq faskavydyr sdttvnqpmv degslagfdi vytnaqgekl
      661 avndlqvrli rerrdyfwdw sesdgwqspf dqkdlvegeq slnlaagetg kvsfpvdwgs
      721 yrlevkgpnd tvssirfwag yswqdnsdgs gsprpdrvtl kldkpayqpg dtiklhiaap
      781 aagkgyamie ssdgplwwqa idvpeggmdl sipvdkkwqr hdlyvstlvv rpgdksksat
      841 pkravgilhl plgdenrrla ltldapakmr pdrnldvklk vkpnaqgtip akvnvlvsav
      901 dsgvlnitdy rtpdpwqaff gkkaygadiy diygqviegq grlaalrfgg dgdelnrggk
      961 ppvnhvtiva qqalpvvlne ngegtvqlpi gdfngelrvm aqawtadsfg sseakvivaa
     1021 pliaeismpr flaggdesrl aldvsnltds aqnltvslta sglvsllesp elkvslkpga
     1081 rktlfipvra hegfgdgeiq aqisglnvpg etfapsqkqw kigvrpafps qtvnsgvmln
     1141 pgeswqvpas hiegfsadtl egrlllsgrp plnlaryise lkaypygcle qttsglfpsl
     1201 ytsaaqlkal giagesdkqr raaidlgisr llemqredgg fslwdktgpe eywgtayvtd
     1261 flvrateqgy svpadalera nnrllrylqd pglmalrysd nsaaskfavq ayaglvlarq
     1321 qkaplgalre lwnrhnaaas glplvqlgva lklmgdatrs qdainagist trnnrtewig
     1381 dygselrdna lilnlleenk llaqqqagll qklsdqafgq nwlstqesna lflagrawqn
     1441 qpaswqvess lsgeplqgdk aqafnlnadk laslhltnts dspvwvrlds vgypqsapqe
     1501 sgnvlkiqrh flasdgtaks ldnlrsgelv mvwldvyask tvpdalvvdl lpaglelenq
     1561 nlanasaslg essgtvtdlv srmqqqdiqh mefrddrfva alpvnageha tlvylaravt
     1621 pgrytvpvpq vesmyvpawr atgrsegtlt iap
//
LOCUS       WP_284972867             316 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Atlantibacter hermannii].
ACCESSION   WP_284972867
VERSION     WP_284972867.1
KEYWORDS    RefSeq.
SOURCE      Atlantibacter hermannii (Escherichia hermannii)
  ORGANISM  Atlantibacter hermannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Atlantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Atlantibacter hermannii"
                     /db_xref="taxon:565"
     Protein         1..316
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=33497
     Region          1..316
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mraftyqrvt tpaeaaasar qtpgakfiag gtnlldlmkl eietpghlid vnglgldtie
       61 ltaegglrig alvrntdlaa dervrrdyav lsrallagas gqlrnratta gnllqrtrcp
      121 yfydthqpcn krlpgsgcaa legfsrqhav vgvsdaciat hpsdmavamr vldavvetvk
      181 pdgserrial ddfyrapgtt phletvltpg elivavtlpp psggthiyrk vrdrasyafa
      241 lvsvaaviqp dgtgrvalgg vahkpwrldt adaqipqgaq avydalfaga kptpenqfkl
      301 ilakrtlasv lteara
//
LOCUS       WP_284973137             391 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Atlantibacter hermannii].
ACCESSION   WP_284973137
VERSION     WP_284973137.1
KEYWORDS    RefSeq.
SOURCE      Atlantibacter hermannii (Escherichia hermannii)
  ORGANISM  Atlantibacter hermannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Atlantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Atlantibacter hermannii"
                     /db_xref="taxon:565"
     Protein         1..391
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=44935
     Region          47..387
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mmahpieins ayviaslavm ffsmlaplff inkeiqpphp sgqntewidg vrgiaamlva
       61 lnhaplviin lglnpkifyf gehtlkafen fgaigvqiff citgmlftrn iflskkeidw
      121 niffkkrmlr lipayvfaas ialiiavwyt wnknasffdf lknipsllsf nflempvvag
      181 fdlsrlfgit wslayewrfy falpllfivf qtnsrltvit lflvalldci isnhsswvyf
      241 isgaacatlm nihiprtysk avsiliilpi laliytyydy plygyirwii isslfflial
      301 tkpsifkira lkvmgvisys fyllhamflf fffefihrhi kdvtsinift ftmiaggvls
      361 ftsmasyfsy ahierkmmyk kkpssnrvls m
//
LOCUS       WP_284973176             215 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: LexA family protein [Atlantibacter].
ACCESSION   WP_284973176
VERSION     WP_284973176.1
KEYWORDS    RefSeq.
SOURCE      Atlantibacter
  ORGANISM  Atlantibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Atlantibacter"
                     /db_xref="taxon:1903434"
     Protein         1..215
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=23402
     Region          1..214
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mekftmgdri qarrkelkin qatlgkmvgv snvaisqwer geteprgdnl lslakalqct
       61 pafllhgeqa gsnvvfagpy vrgirypvls nvqagawcea cepytlrdid lwlesdahiq
      121 geafwlqvdg dsmtapagls vpegtfvlfd tgrepvngsl viaklsdsne atfkklvidg
      181 gvrylkglnp swpmvhingn criigvavet kmrlv
//
LOCUS       WP_284973240             459 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Atlantibacter
            hermannii].
ACCESSION   WP_284973240
VERSION     WP_284973240.1
KEYWORDS    RefSeq.
SOURCE      Atlantibacter hermannii (Escherichia hermannii)
  ORGANISM  Atlantibacter hermannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Atlantibacter.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Atlantibacter hermannii"
                     /db_xref="taxon:565"
     Protein         1..459
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=50783
     Region          8..400
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mttctqrqaw itllrrlhfa iglfvgpfif vaalsgtlyv atpqleqyvy astlngsreg
       61 epqplarqid ianqvtqhal rlhavrpgle agqttrvmys dpalapsehr aifidpvtla
      121 vtgdmtvygt sgilplrqwi dylhrslllg dvgrlysela aswmwiaalg giflwwmtkp
      181 srkprtvkrs rlmaarqlhi tlgltllagl llfsatgltw sqyaggnvdk lraamgwmtp
      241 qvntllsgqa apadphaehh ghhpaamepq qeqgadidrv lalaqhhgin aslleirppr
      301 nphqawsvte idrrwptqvd avaingetmq vidhtsfeqf plmakltrwg vdfhmgilfg
      361 linqlaligf gialcvligm gyrqwwlrrp aaavnnpaet lcqawlmlsg vgrtcavivi
      421 vafgfampvl gislllfllf difrwkraqr rqaaqpavn
//
LOCUS       WP_284973754             177 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Atlantibacter hermannii].
ACCESSION   WP_284973754
VERSION     WP_284973754.1
KEYWORDS    RefSeq.
SOURCE      Atlantibacter hermannii (Escherichia hermannii)
  ORGANISM  Atlantibacter hermannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Atlantibacter.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Atlantibacter hermannii"
                     /db_xref="taxon:565"
     Protein         1..177
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19106
     Region          85..157
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mipassvivl sapqiyayid slsqllidcv ndgasvsfiw pmtvekahtf wkgvaesvtr
       61 eerivlaatd aqgnlagtvq livdqpenqp hradvakllv spgarrqgla qqlmtalenq
      121 aalhnksvlt ldtatgsgae afyqqagwqr vgdiphfalm pdgapcsttw yykqlkr
//
LOCUS       WP_284973858             210 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Atlantibacter
            hermannii].
ACCESSION   WP_284973858
VERSION     WP_284973858.1
KEYWORDS    RefSeq.
SOURCE      Atlantibacter hermannii (Escherichia hermannii)
  ORGANISM  Atlantibacter hermannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Atlantibacter.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Atlantibacter hermannii"
                     /db_xref="taxon:565"
     Protein         1..210
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23601
     Region          1..210
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mtrllrwift lciawplvwi wlgvsvtnrk klpikgpaiv vanhnshldv ltlftlfplt
       61 tlvnvqpvaa adyflknkcm awfalnvigi ipvqrhgraa nplapcidal aqqkililfp
      121 egtrgepgvm sefksgiwhl cqsqpdvpvi pvylhgldra mgkgqkipvp ffidiyvddp
      181 lfyhadkavf kqtllqrfld lqqqatrkep
//
LOCUS       WP_284973872             338 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Atlantibacter
            hermannii].
ACCESSION   WP_284973872
VERSION     WP_284973872.1
KEYWORDS    RefSeq.
SOURCE      Atlantibacter hermannii (Escherichia hermannii)
  ORGANISM  Atlantibacter hermannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Atlantibacter.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Atlantibacter hermannii"
                     /db_xref="taxon:565"
     Protein         1..338
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=37213
     Region          2..331
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkilvtgats glgrnaveyl rqqnisvvat grnrlageel tregavfvpl dlaqanheqc
       61 vslmagcdav whcaaksspw gdrdafwqan vnatstlaka agslgiprfv histpavyfd
      121 fqhhydvpet ylastfsshy asskreaerv iadaaacfgs ttfiilrprg lfgphdnviv
      181 prllrqlhqd ggvlrlprgg ealldltfvq nvvyamerat ysetlssgsi ynvtnhqpqr
      241 ladmldallr qqlglnytir svpwplmslv arcmelkgkc inkeppvtry sagtvcfdmt
      301 lstkkaveel gytprfsmeq gialtgewlr nngkdyri
//
LOCUS       WP_284974073             360 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Atlantibacter hermannii].
ACCESSION   WP_284974073
VERSION     WP_284974073.1
KEYWORDS    RefSeq.
SOURCE      Atlantibacter hermannii (Escherichia hermannii)
  ORGANISM  Atlantibacter hermannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Atlantibacter.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Atlantibacter hermannii"
                     /db_xref="taxon:565"
     Protein         1..360
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38217
     Region          1..342
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mfrfilliss allsavasas igfhqftlne patrpldvav wypthatgpt envgdnivfv
       61 gveaqrdaap tpglhpllll shgfggnwrn lnwlaqqmae qgyivaavdh pgtttrnkea
      121 aqaqmlwqrp qdvtrvlnal iagpeiagki deqriaaagh slggwtvmel agarfsakdf
      181 madcehhapl gackvartlg lhlpqaqarl aqplrdprin avvsldlgla rgftpqslkg
      241 vnipvlvmsa gadnddvpaa lesgflvsql ssahtravhv pgathfsfmq lckagaeavi
      301 eaqepgegiv crdgvgfsra aihqqltqqi sqflnqalry sppradsrpg sspqsaqthg
//
LOCUS       WP_284974225             333 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. efr-133-TYG-104].
ACCESSION   WP_284974225
VERSION     WP_284974225.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..333
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36637
     Region          34..305
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 maytakdwpi taallqfpgt daagqdinda dastwasvlq evkeagfena dltdswvrpg
       61 dlgkerlaef kqaaeqvgig vpvisairrs vihqtdwaen layshrtida aaelgcevvs
      121 fglhqaitpe qqkqlwfwtv egykdpvgdk eawgnavsri relgkhaaea gilvslemye
      181 dtflgtadss vqlvqdigld nvglnpdign lirlhrpied wremvaktlp ysnywhmkny
      241 lrdedvards yitmpapmes glinyreafk lalsvgfqgi lctehyggdg lsvtasnqey
      301 lrrhvlpktd gyalgksqva qgrqepatel agv
//
LOCUS       WP_284974265             135 aa            linear   BCT 25-DEC-2024
DEFINITION  SRPBCC family protein [Arthrobacter sp. efr-133-TYG-104].
ACCESSION   WP_284974265
VERSION     WP_284974265.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..135
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=14607
     Region          6..131
                     /region_name="SRPBCC_CalC_Aha1-like"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of Micromonospora echinospora CalC, human Aha1, and
                     related proteins; cd07814"
                     /db_xref="CDD:176856"
     Site            order(6,8,10,19..21,23..24,29,39,43,45,47,49,55,57..58,60,
                     63,69,71,81..82,84,86,96,98,100,102,112..120,122..124,127)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mtenairler tfphpkesvw aalttpqlla rwwtpgdiap vvghrftldm ggwgvqqcev
       61 lavelgtsis fafaegvldt titwtletvd ggttlhfeha gfrldtpmgq qalhgmgngw
      121 pgliaridqv lvnvg
//
LOCUS       WP_284974451             223 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Arthrobacter sp. efr-133-TYG-104].
ACCESSION   WP_284974451
VERSION     WP_284974451.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..223
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=23343
     Region          2..215
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mtrlilasqs partklltea giehevlvsd vdedavqaky gvtdahdtal llarakaeav
       61 aalpesdgal vigcdsvfef dgeshgkpyt edvarermlr msgsqgvlht ghwlvdcrdt
      121 aaeadeddae hgtpegtgat vgavssaevh ftqmneneid ayiatgeplh cagsftidgl
      181 ggafirkvdg dphavvglsi stlrdllgha nvpitdlwqa gna
//
LOCUS       WP_284974458             300 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family oxidoreductase [Arthrobacter sp. efr-133-TYG-104].
ACCESSION   WP_284974458
VERSION     WP_284974458.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Persson,B. and Kallberg,Y.
  TITLE     Classification and nomenclature of the superfamily of short-chain
            dehydrogenases/reductases (SDRs)
  JOURNAL   Chem Biol Interact 202 (1-3), 111-115 (2013)
   PUBMED   23200746
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   6  (residues 1 to 300)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10793067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..300
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31056
     Region          25..300
                     /region_name="PRK08278"
                     /note="SDR family oxidoreductase"
                     /db_xref="CDD:181349"
     Site            order(37,39..40,42,61..63,121..123,175..177,192,196,
                     222..225)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187663"
     Site            order(145,177,192,196)
                     /site_type="active"
                     /db_xref="CDD:187663"
ORIGIN      
        1 mtssndssaa sgmnrastns pyvatgslkg rtilmsggsr giglaiamra ardganivlm
       61 aktgqphpkl egtvfsaaeq leaaggqalp lvgdvrnded vaaavaaavk rfggidvvvn
      121 nasaidlsrt davdmkrydl mqdinvrgtf llsklalpal reagarsgra hiltlsppln
      181 ldpkwagmhl aytmakygms lttlglaeel kddavsinsl wpctlidtaa irnmpggaqm
      241 vqaargpeim adaahailtg gaatgnfytd eqvlraagvt dfapyslgap edrlvadifl
//
LOCUS       WP_284974549             288 aa            linear   BCT 25-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284974549
VERSION     WP_284974549.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Bagautdinov,B. and Kunishima,N.
  TITLE     Crystal structures of shikimate dehydrogenase AroE from Thermus
            thermophilus HB8 and its cofactor and substrate complexes: insights
            into the enzymatic mechanism
  JOURNAL   J Mol Biol 373 (2), 424-438 (2007)
   PUBMED   17825835
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..288
                     /product="shikimate dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29563
     Region          1..274
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 msrraavlgh pishskspal hmaayaklgv dieytakdie vgglrtfmes lrgdptwcgl
       61 svtmplksam vqevdevrgv aaalgvintv vfepdgdsvr rvgyntdvgg iveavryagv
      121 aatphaavlg gggtsaaaia avhdlgarhv dvfvrdsgra reaqaaaaav gislalrpii
      181 eaagavvasd lvistlppra adglaeelat ltgqgmgtga gvlldvaydp wpsrlaeawq
      241 ghggvvvpgl emlmyqaaeq irrfsgcdvd asvidvmcds vglprrgf
//
LOCUS       WP_284974601             129 aa            linear   BCT 25-DEC-2024
DEFINITION  HesB/IscA family protein [Arthrobacter sp. efr-133-TYG-104].
ACCESSION   WP_284974601
VERSION     WP_284974601.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Lu,H.M., Li,J.D., Zhang,Y.D., Lu,X.L., Xu,C., Huang,Y. and
            Gribskov,M.
  TITLE     The Evolution History of Fe-S Cluster A-Type Assembly Protein
            Reveals Multiple Gene Duplication Events and Essential Protein
            Motifs
  JOURNAL   Genome Biol Evol 12 (3), 160-173 (2020)
   PUBMED   32108236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..129
                     /product="HesB/IscA family protein"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=13631
     Region          25..129
                     /region_name="IscA"
                     /note="Fe-S cluster assembly iron-binding protein IscA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0316"
                     /db_xref="CDD:440085"
ORIGIN      
        1 mstatnenst gaqvitsdel pthevaltdv aagkvrslle qegrtdlrlr vavqpggcsg
       61 liyqlyfder lldgdavrdy dgvevvvdkm svpylsgasi dfedtiskqg ftidnpnagg
      121 scacgdsfh
//
LOCUS       WP_284974750             222 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: lysophospholipid acyltransferase family protein
            [unclassified Arthrobacter].
ACCESSION   WP_284974750
VERSION     WP_284974750.1
KEYWORDS    RefSeq.
SOURCE      unclassified Arthrobacter
  ORGANISM  unclassified Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="unclassified Arthrobacter"
                     /db_xref="taxon:235627"
     Protein         1..222
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23832
     Region          2..215
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mavfdairwt trglvsstcr ptviglenvp qegpfivapn hlsfldsviv qalmprpvaf
       61 fakaeyfttk gikgavmksf feavgsipve rgeqaasvqa lktlldiles gkgigiypeg
      121 trsrdgilyr grtgvgwlal ttgapvipvg ligteklqpa gknavrpqhf tmkvgeplyf
      181 ektgpdhslp arrevtdkim daiaslsgqd rstsynqskt vd
//
LOCUS       WP_284974755             844 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Arthrobacter sp. efr-133-TYG-104].
ACCESSION   WP_284974755
VERSION     WP_284974755.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 844)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 844)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..844
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..844
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=93157
     Region          18..830
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mklleqlpgs adaeslgpde iytrfvewte srglqlypaq deaimelasg anvilatptg
       61 sgkslvaiaa hfeamsrgrr syytapikal vsekffalce ifgaenvgmi tgdsgvnqda
      121 piicctaeil anialregaa aelgavimde fhfysdpqrg wawqvpllel pqaqfllmsa
      181 tlgdvsrfea glseltgrat ttvssaerpi plhyyyhltp vhetleella tkqvpvyvvh
      241 fsqaeaiera qnlmsinmcs rdekdriael iagfrfaagf gktlnrlvrh gigvhhagml
      301 pkyrrlaeql aqagllkvic gtdtlgvgin vpirtvllta lskydgvrtr vlnsrefhqi
      361 agragragyd tagtvvvqap ehvventkam akatakfgdd qkklrqvvkk kppegfvswg
      421 eptftrlves vpdpltssfs vshamllnlm erpgdpfhaa rrlltenhes rpaqlklmkk
      481 algiyrella agvveriped erdaegrsvr ltvhlqanfa lnqplspfal aalelldpes
      541 psyaldvvsv iestlekprq ilsaqqkkar geavaamkae gmeydqrmal ldevtypmpl
      601 aeilgeafev yrkaapwvgd felapksiir dmyeramnfg efvqfyglar segivlryla
      661 dgyralrqtv pqdllredle dliawlgelv rqvdssllde weeltsgltp tphdappplp
      721 psltsnaraf rvmvrnemfr rvelfadeds aalgeldaes gwdaerweev lddyfdehdd
      781 igtgpdargp glliiteepg iwkvrqifdd pahnhdwgis aeidlaasde tgtaavrvtd
      841 vnrl
//
LOCUS       WP_284974790             117 aa            linear   BCT 25-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284974790
VERSION     WP_284974790.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 117)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 117)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 117)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 117)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 117)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..117
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12530
     Region          6..114
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mmdtsrfrtl leqerarkls llqdlqtdit svnvarqdsn vddehdpegs tiafelsqas
       61 allaqsragl aqieaalnri segtygvcsv cgaaipegrl earpwtpfcv ahasgra
//
LOCUS       WP_284974817             291 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. efr-133-TYG-104].
ACCESSION   WP_284974817
VERSION     WP_284974817.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..291
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32543
     Region          1..286
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mkialdptpf hhshsllefp rvaadlgyky lqltphadmi pfynhpkadd elvaqlkaac
       61 rdadveiasv lpvlrwsgpd edareaavry wkraiqiavd lgvstmntef sgrpekaees
      121 erafyrsmee llpiieregm dvlidphpdd fvedglaair virgvnspni gmvyvashtf
      181 hmgnspveim rtagdklrlv hvsdtmdhha shglryitnp pgnavrvhqh lkigdgdvnw
      241 deffgglhei gfldkdntvm vssvfaeddn aedvsiyqle tmkqhiqkvn a
//
LOCUS       WP_284974838             482 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284974838
VERSION     WP_284974838.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..482
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=50792
     Region          22..457
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mpqtvppmdl tiarpgvvdh pnitvvgtgy lgathavcma llgydvvgld vdqakidqla
       61 dghlpifepg lqeklqevla sgklrfttdf alaadhgdvh ficvgtpqsk gsdaadltfv
      121 daavtalarn ltrkclivgk stvpistaar ltalvrntap agelielawn peflregyav
      181 vdtlqpdrlv fgtasawaea qlaacytsii qagtpvivtd lataelvkva ansflatkis
      241 yinamaevce atgadvalla kalsydsrig grflkpglgf gggclpkdir afahraealg
      301 vgqavsflrq vdainqrrrq rtvdlvtela ggnvtgvkia clgaafkpns ddirdapald
      361 vatmlheaga rvsvydpaam pnarrsypel eyansleeav tgagvvallt ewqqfreadp
      421 arllqltgap civdgrhald adayqaagwd yralgrpars gavvssfded fakarldaqe
      481 vg
//
LOCUS       WP_284974876             506 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Arthrobacter sp. efr-133-TYG-104].
ACCESSION   WP_284974876
VERSION     WP_284974876.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 506)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 506)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 506)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..506
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53490
     Region          8..502
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mplgvstisl lavlialfsl lplgyvvymt vatgwdtavg livrprvgel lantvlltvv
       61 tvplclvlgv ggawlverth lkghrwwava laaplaipaf vnsyawvsav psleglwsgv
      121 liatlsyfpl vyipaaatlg rldpaieqsa aslglgpwav ffkvvlpqlr iamsggallv
      181 glhllaeyga famirfdtft taimvqfqst fngaagnmla svlvllclll llgevksrgn
      241 aryarigsga qakalrlslr gyqipaqlgl laltalafgl pvffvvrwvi mggpgvwaae
      301 ellpallqtl lygafgaavt tvvafpmayl avrhpswfsk mlelsnyvts slpgivvgla
      361 fvtvsirvvp glyqtagvli aayvllflpr alvnirsgla qapkeldeaa qslgrpplvs
      421 ffrvtlrlta paaaggaalv flaivnelta tlllspngtr tlatqfwsks seidytgaap
      481 yallmillsa pmtyllfqqs kkvagq
//
LOCUS       WP_284971369             156 aa            linear   BCT 25-DEC-2024
DEFINITION  tRNA pseudouridine synthase A, partial [Clostridioides difficile].
ACCESSION   WP_284971369
VERSION     WP_284971369.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Hur,S. and Stroud,R.M.
  TITLE     How U38, 39, and 40 of many tRNAs become the targets for
            pseudouridylation by TruA
  JOURNAL   Mol Cell 26 (2), 189-203 (2007)
   PUBMED   17466622
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Foster,P.G., Huang,L., Santi,D.V. and Stroud,R.M.
  TITLE     The structural basis for tRNA recognition and pseudouridine
            formation by pseudouridine synthase I
  JOURNAL   Nat Struct Biol 7 (1), 23-27 (2000)
   PUBMED   10625422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414743
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..156
                     /product="tRNA pseudouridine synthase A"
                     /EC_number="5.4.99.12"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
     Region          <1..156
                     /region_name="TruA"
                     /note="tRNA U38,U39,U40 pseudouridine synthase TruA
                     [Translation, ribosomal structure and biogenesis];
                     COG0101"
                     /db_xref="CDD:439871"
ORIGIN      
        1 vktveevder fhsrynvksk tymykidnnk yhnpfirkya thvskkldld rmrkaseylv
       61 gehdftsfas skskkksnvr eiysiniked dnvieiyveg ngflynmvri ivgalidvgl
      121 krrapqdiky mleskdrcqs sdtapakglc lwkvty
//
LOCUS       WP_284975005             374 aa            linear   BCT 25-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284975005
VERSION     WP_284975005.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Pereira,J. and Lupas,A.N.
  TITLE     The VCBS superfamily forms a third supercluster of beta-propellers
            that includes tachylectin and integrins
  JOURNAL   Bioinformatics 36 (24), 5618-5622 (2021)
   PUBMED   33416871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..374
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=38628
     Region          178..239
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          228..289
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          278..338
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mgtlrrrmaa alltavvtam aisplpasaa psgpdpvvtg taivgqtlgt vigpytfygc
       61 gggtgpdfti ywtrdgflva getgrtyvlr pgdagsrmav hvsasrtacs aetinsaets
      121 pvgaanrasg ftgrafella rgtdgtlslf grtgkawdap rtvgwgwngf nlvfspgdfn
      181 gdgksdliar dasgvlylyp gdgtggwkpa qvigtgwdvf dsivgpgdfn gdgyndilar
      241 gkdgtlylyp gngaggwlpr tvvgtgwdvm dailtpgdfn gdgkvdvlar drngylyfyg
      301 gngaggwtrs wligtgwgal rflgaagdfn gdgfadvygv daqgrlvsyy sdgrtgwkgs
      361 evvgdgwggf taif
//
LOCUS       WP_284975009             315 aa            linear   BCT 25-DEC-2024
DEFINITION  polysaccharide deacetylase family protein [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284975009
VERSION     WP_284975009.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..315
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34483
     Region          22..278
                     /region_name="CE4_HpPgdA_like"
                     /note="Catalytic domain of Helicobacter pylori
                     peptidoglycan deacetylase (HpPgdA) and similar proteins;
                     cd10938"
                     /db_xref="CDD:200563"
     Site            order(28,30,103,107,241)
                     /site_type="active"
                     /db_xref="CDD:200563"
     Site            order(36..37,46..47,49..51,53..54,58,62,81,84..86,
                     105..106,108..109,112..113,116..117,120..121,124,144..145,
                     147,165..171,191..193,198..200,202..204,220..221,224..225,
                     228,247..249,251..252,255)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:200563"
ORIGIN      
        1 mnqpafadsl hpvvwpegfk aaasftfdvd aesctiahdp astrrmslms hqsygpkiav
       61 prllqildrq dikgtffvpg ftadsypdvv rriadaghei ahhgylhepm qgidaatean
      121 yldrgleala rvagvrpvgy rapwwelnwq spalladrgf lydsslldgd apyrmtvaed
      181 dsrdiveipv dwalddweqy afypgvsgsg viespakale mwtleaqahh aqgscfvltn
      241 hpfisgrpsr avaleqlier vkdlegmwvt tlaaiaghtk stvqevhtha ridvplfpga
      301 gatfrpaqvs apsll
//
LOCUS       WP_284975029             262 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284975029
VERSION     WP_284975029.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..262
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26921
     Region          3..251
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtmtyrgtta litgassglg aefaerfaar ganlvlvarr adrleelaee lrsqhgvtvt
       61 vlpmdlarpg agrelaadlg srgitvdtli nnagfgtrsp faeedpdaia seislnvaal
      121 vditraflps mlssakgalv nvastaafqp ipgmavygat kafvlsftea vahetrasgl
      181 svlalcpgat steffevlgs esaavgrmqm psqvvetaik aldrsgtpgs vvsgwanrla
      241 agfaqrlpra vtvaiaarav qd
//
LOCUS       WP_284975151             125 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Arthrobacter sp. efr-133-TYG-104].
ACCESSION   WP_284975151
VERSION     WP_284975151.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..125
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12573
     Region          15..113
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 matkttkttk stafwvilla saileavwat alglsngftq liptlvfava atmsmlglgi
       61 avkriplgta yavwvgigaa ltvgwamitg lesasplkll fiagivgcaa glkalptgkp
      121 aldse
//
LOCUS       WP_284975391             236 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Arthrobacter sp. efr-133-TYG-104].
ACCESSION   WP_284975391
VERSION     WP_284975391.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 236)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..236
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26672
     Region          55..222
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mspisanvae rrlappslai stvifalrps eksgrptlwl plvrrirepf kdmwalpggp
       61 lshdeslqda asrnlrettg lvphyleqly afgglhrsps qrvvsivywa lvqpteaala
      121 desenvrwfr adrlgelafd hneivdyalw rlrnkmaygs iayhllgeff tlaqvrevye
      181 avldrqldpa nfrrhikatp eieetgqylq ggkhrpprly rftgtpglgp dnrsts
//
LOCUS       WP_284975399             268 aa            linear   BCT 25-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284975399
VERSION     WP_284975399.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     BTLCP proteins: a novel family of bacterial transglutaminase-like
            cysteine proteinases
  JOURNAL   Trends Biochem Sci 29 (8), 392-395 (2004)
   PUBMED   15288868
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..268
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=29011
     Region          <117..211
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mernvaaela fktaadtkva laiavannsg ytsvseklsv tvdgrevpfr elddhhggrf
       61 qymefaqpse vlvaynatvq glgdqdtasa meliryvrps ryaesdrllp tsyaefgslr
      121 gvellqavrd wvnhelryvs gssrgtdgav etllhrrgvc rdfahlaial lrskdvparl
      181 aavyapglsp mdfhavaeay idgawhvidp tglaprgsml ritagrdssd taflstvggs
      241 lmlttlkvsa svngelpred prelmslr
//
LOCUS       WP_284975524             408 aa            linear   BCT 25-DEC-2024
DEFINITION  thiolase family protein [Arthrobacter sp. efr-133-TYG-104].
ACCESSION   WP_284975524
VERSION     WP_284975524.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 408)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..408
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41915
     Region          1..406
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mveaflvgga rtpvgrygga lsavrpddla alvvreavar agvdpdaide vilgnangag
       61 eenrnvarma tilaglplhi pgitvnrlca sglsaiimas hmiksgaadi vvaggvesms
      121 rapwvqekpt tafakpgqif dtsigwrfan pqftkgelsr dgkmtysmpe taeevarvdn
      181 isredadafa vkshelalaa iaggrfkdei vpvtvktrks etvvdtdegp regttmdvla
      241 glrpvvpggs vvtagnsstl ndgasaiiva seaaikkfgl tprariidga sagcepeimg
      301 igpvpatqkv lartgfsveq lgavelneaf atqslasmrr lgldpdivnn dggaislghp
      361 lgssgsriai tllgrmerel gsatgpkrgl atmcigvgqg tamllegv
//
LOCUS       WP_284975574             225 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Arthrobacter sp. efr-133-TYG-104].
ACCESSION   WP_284975574
VERSION     WP_284975574.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..225
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=24233
     Region          36..205
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 msaledlagl vtrfelgedh vsshwaqlav spettrpaav lmlfgmldga sadlrraiap
       61 tdldvlller ahtlgehpgq vafpggsvdp gdesvvhaal reaveetgld asgvrvlgvi
      121 pelglirsnf rvtpvlawwd spspvrvvdy aesaqvfrvp vrdlldpanr vtatisrfgr
      181 tfsspaftin gllvwgftgm vlsglfeelg wtvpwdkdrt heisl
//
LOCUS       WP_284975638             485 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284975638
VERSION     WP_284975638.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..485
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50656
     Region          6..483
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mtaensrefd vivigagavg envadrvvrg glsaviiene lvggecsywa cmpskallrp
       61 gsvlhaaqgi pgateavtgt idahsalqhr dwftnnwqdg sqaewldsag ielirgrari
      121 tgprevlvdg ldgnsyalka hhavvvatgs tpsipdidgl sdvpfwttrg ataakevpkr
      181 lvvlgggvag velgqafarl gsevavvarg rllssypeea aslvlaglra dgidvrlhtd
      241 vakveknddg sitvtvdgkn ltadqllvas grhpalanlg lenvgieapd gkplrlttdp
      301 sglvdgpasd gtsgfwlyaa gdaagmvllt hqgkyearat gdaivarang klhgapqpws
      361 pwahtaneha vpsvvftdpe vasvglsleq allqgrnvtg velpidvsga qlyspdykgw
      421 aqmvvdedrk viigatfvgp gvaellhsat iavvgevpld rlwhavpsyp tisevwlrll
      481 ekygl
//
LOCUS       WP_284975661             348 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284975661
VERSION     WP_284975661.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..348
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=37986
     Region          73..341
                     /region_name="2-desacetyl-2-
                     hydroxyethyl_bacteriochlorophyllide_"
                     /note="2-desacetyl-2-hydroxyethyl bacteriochlorophyllide
                     and other MDR family members; cd08255"
                     /db_xref="CDD:176217"
     Site            order(83,85,88,91,150,154,174..179,198..199,203,213,
                     230..231,233,253..254,280..282)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176217"
ORIGIN      
        1 mtisqqydkq ppapqgkhhi rlpgeaqayw vtesgagelr gesmptpgpg ealirtlysg
       61 vsrgtervvh egrvpervae rmqaphqege fpgpvkygyl nvgvveqgpq ewigktvfsl
      121 hphqdfyvip anqltavped vparravltg ivevainalw eagpklgdrv avvggglvgg
      181 vlatllrkyp lgrlqlvead pekrklaekl giefasteda kadcdivfhc sasneglkls
      241 lqlagddsdv ielswfadke vtlplgedfh arrlnirssq vgavalprrh rrtnaqrlql
      301 aasqlqdpvf dtfltsecqf qnlpttlvkl feqpggfchv vaypnped
//
LOCUS       WP_284975674             200 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284975674
VERSION     WP_284975674.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 200)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..200
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21225
     Region          1..>87
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mldieviedp aaaeasldpi rtrilqeltk pssatqlaar iglprqkvny hlkaleghgl
       61 velveerkkg nvtervlrat aasylispva lasvapnpar fadrfsafwl lalaartvqe
      121 mgkliagaaa akkklasfai dgeiafrsaa eraafaeelg vavtalvdky hdggadalas
      181 garkhrlvvv lhptlksttr
//
LOCUS       WP_284975732             484 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284975732
VERSION     WP_284975732.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..484
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52070
     Region          2..456
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mstattpgsg rglevrsidy vplgerhgkv shigplwfms naqiatlavg lisittggnl
       61 iwsliaiaig vlvgtlfmaa hssqgpqlgl pqmiqsrpqf gyvgallvwl faylqyagfn
      121 ifntvlagqa vagsvhfgse tlwfwvvtii aaavalfgyd lihgferylt yltivmlall
      181 tvaalthldl pggafdlgdf hlvpflgqlg vaagyqiswa iyvsdysryl ppesgrgtfk
      241 wtfwgsalgg iwvmflgsfi aasagkdfet iasiqdtadk lfpgfgsial fvaalglvsv
      301 talnmyggsl tlissidslr rirptvrirv itiaitaifs lvfaniasad flanfndfll
      361 lvlyffipwt avnltdyfiv rkghyaiaei fhpngiygrw gwagitaylv gfavmipffs
      421 agklfvgpaa samgdadisl figlpvagfl ywvltrhidt aaelrlaeaq aaeleeasns
      481 hlep
//
LOCUS       WP_284975727             460 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Arthrobacter sp. efr-133-TYG-104].
ACCESSION   WP_284975727
VERSION     WP_284975727.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..460
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48043
     Region          131..458
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mswlrslagr itlvtaavav lavlvtgsta fplirsaave qarqqlarqa dafaatpvas
       61 qaldlrerhl lgpdtyelst itvggavsga aaqllstget qqvlsgekvs rtvtkggvqf
      121 lvearalpkg gaivltrsld dvnaasaqll qrtllalaag lliavlagtl larrlsgplv
      181 rtaaaarrma agertvhldp dgvtevravg eaintldhal masegrqref llsisheirt
      241 pltamrgyae aledglipqe diagigrtls aetdrldgfv rdllalarle addftldiqp
      301 vniavvleqa qsawngaavq agveltlqlp etpdghpvla ltdgqrlrqi idglignalr
      361 itppgqplal rawleesgrv igvevhdsgp gltaedaava fergalsrry tgqrptgsgl
      421 glsiaarlaq rmglsltvep vpagqgarfc irlpraaavs
//
LOCUS       WP_284976027             429 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284976027
VERSION     WP_284976027.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..429
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46223
     Region          159..402
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 masnfvatdv paestmslrt kwalagmvag gtlaglvgag ssalavyfar rvitpgarhe
       61 dqevlavikg ddglqvilaa tpdttidgvf slffdggkgh arigrivsys paeqtvlrev
      121 qevysgdlfq arragwsgat ypdpaalgla aedveidvdg gkapawlvra gegpastwai
      181 mvhgrgatrl eglravktar slgmdtllis yrndglapst ldgryglgst ewrdveaaig
      241 yalsrgaaev vlfgwsmgga itlqtadlsk yrhviralvl dapvinwvnv mahhaqvnri
      301 pyrvgrygql mlshplgrrl tglaapvdfk amdwearaie lrtptllihs vdddyvpfgp
      361 sailaeknpe mvtfepfdga rhtkewnvdp ekwermvrsw lrmqlaprnn pgqsdrpgqs
      421 dpgqsdrpg
//
LOCUS       WP_284976219             659 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD/NAD(P)-binding protein [Arthrobacter sp. efr-133-TYG-104].
ACCESSION   WP_284976219
VERSION     WP_284976219.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11816065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..659
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70389
     Region          1..644
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
     Region          9..200
                     /region_name="NAD_binding_9"
                     /note="FAD-NAD(P)-binding; pfam13454"
                     /db_xref="CDD:433222"
ORIGIN      
        1 mpsrvpaiaf igggprtagv lerlaanrps lfdgplhvhv iephqpgsgr iwrydqspgl
       61 llnstaadvt mftdgsvvcd gpavdgpgls twaagvldgs irdvpvleph vleqlraltp
      121 asfptrqlqs kylewffrra vsalgtdvtv tvhrdtatav spasassgth rghddgthri
      181 rlatgaevva dvvvyalght dslpddesag lsdfaarhgg fhappsyttd vdysaigagq
      241 dvivsgmgla fvdllvllfe grggrfeegp dgelaylpsg aeprvwagsr rgvpyhskis
      301 stllgepaar pryftasaie sllgshaeld frahlwplia kdagyayyre lftghpfrvr
      361 gtwasfearf daldwyspgr edlvaasvpd paswldlerl dhplsgcafs dhgavqrsvs
      421 ayiqrdldlr tspehsetla lftallfvym dlgrlvpqer lnarsqqaih gwwhgffsfv
      481 dsgppahrlr emlalqragf lkflgpgmwv radesagrfv agsfqspvvv gaaayivarl
      541 psasversan paltdlhdag rgteqrllts egthstgkll vsgnhevlsp vgtpqkglfa
      601 vgpwtsgwga gafarpntna apfrendala rrvlstiaag aasrvpatql gdattkgli
//
LOCUS       WP_284976296             181 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Arthrobacter sp. efr-133-TYG-104].
ACCESSION   WP_284976296
VERSION     WP_284976296.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..181
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20700
     Region          25..163
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mhlllrtlml lftsskrsal gvwepsslel rvlptdidia mhvnngmyfs lmdlgrfdlm
       61 vrsgiwrrmr rrgwtpvaag etiafrkslq lwqkysietr iigldtkaiy feqrmvvege
      121 iyarahiatr lvskgkpvtq eeiiqefgap padlelpawi hewrgnnalp garrsaphdw
      181 s
//
LOCUS       WP_284976320             315 aa            linear   BCT 25-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284976320
VERSION     WP_284976320.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..315
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34425
     Region          7..282
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mtvitettle faklgsriga eirgldisgd lsadtvgqir aalnehkalv freaniltde
       61 aqvefashfg pltkahptva svdgeenvlp vdsengsann whtdvtfvvn ppqastlrsi
      121 dlpayggetl iassagayrd lpeelrnfad tlwaihtndy dysvpknleh anaeerrkef
      181 trlkfetahp vvrvhpltge rglfiggfaq rlrivglsnt esrdiirllq ayvtrpenvv
      241 rvnwepnqvv lfdnritqhy apdnydgqpr klnrvtiagd ipvsihgkps qalqgdssty
      301 svvapvdsva apaal
//
LOCUS       WP_284976387             296 aa            linear   BCT 25-DEC-2024
DEFINITION  tRNA pseudouridine synthase A [Arthrobacter sp. efr-133-TYG-104].
ACCESSION   WP_284976387
VERSION     WP_284976387.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Hur,S. and Stroud,R.M.
  TITLE     How U38, 39, and 40 of many tRNAs become the targets for
            pseudouridylation by TruA
  JOURNAL   Mol Cell 26 (2), 189-203 (2007)
   PUBMED   17466622
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Foster,P.G., Huang,L., Santi,D.V. and Stroud,R.M.
  TITLE     The structural basis for tRNA recognition and pseudouridine
            formation by pseudouridine synthase I
  JOURNAL   Nat Struct Biol 7 (1), 23-27 (2000)
   PUBMED   10625422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414743
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..296
                     /product="tRNA pseudouridine synthase A"
                     /EC_number="5.4.99.12"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=32447
     Region          18..284
                     /region_name="TruA"
                     /note="tRNA U38,U39,U40 pseudouridine synthase TruA
                     [Translation, ribosomal structure and biogenesis];
                     COG0101"
                     /db_xref="CDD:439871"
ORIGIN      
        1 mnerkpaapv mggsgflrvr ldlsydggpf sgwalqpgrq tvqgsleqal allfqrpvrv
       61 tvagrtdagv hargqvvhld vseaewlalp rgheldpava llrrlrgals rilgeltgav
      121 evhdaglape gfdarfsalw rrysyriadg perwdpvlrg itlwhksavd vdamnegsha
      181 llglndfrsy ckpregattv relqkfsfar rpdgvilatv qadafchnmv rslvgsalrv
      241 geglespgwl lerlverkrd aksilaaphp lvleevayps dsellarael trarre
//
LOCUS       WP_284976423             373 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Arthrobacter sp. efr-133-TYG-104].
ACCESSION   WP_284976423
VERSION     WP_284976423.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..373
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40740
     Region          25..371
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mdtrqhtevd tvivgggqag lalgywlare grdfvilden arageawrqr wdslrlftpa
       61 kydglpeapf pgdplafppk deladylegy vrrfdlpfrp atrvdeirhn gqrfiviskd
      121 htwhasnvvi argghripkt ppfaseldpr ilqlhsqdyk npgqlrqgtv lvvglgnsga
      181 eialetgrsh htvlagkpsg elpmrhgrta arfglpivrf aglhilnlnt pigrkvaprf
      241 ksmaaplirt ktkdlaasgv slvprlagvs ggqpvledgt eidaatiiwc tgyhedylwv
      301 klpafdghgs paqtrgvadk vhglyflgqe flysaasatl pgvtqdakyl arrismtrea
      361 akvsaptaer rma
//
LOCUS       WP_284976513             197 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: HIT family protein [unclassified Arthrobacter].
ACCESSION   WP_284976513
VERSION     WP_284976513.1
KEYWORDS    RefSeq.
SOURCE      unclassified Arthrobacter
  ORGANISM  unclassified Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="unclassified Arthrobacter"
                     /db_xref="taxon:235627"
     Protein         1..197
                     /product="HIT family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21768
     Region          55..181
                     /region_name="FHIT"
                     /note="FHIT (fragile histidine family): FHIT proteins,
                     related to the HIT family carry a motif HxHxH/Qxx (x, is a
                     hydrophobic amino acid), On the basis of sequence,
                     substrate specificity, structure, evolution and mechanism,
                     HIT proteins are classified into...; cd01275"
                     /db_xref="CDD:238606"
     Site            order(80,82..83,90,92,138,146,148,152,154)
                     /site_type="active"
                     /note="nucleotide binding site/active site [active]"
                     /db_xref="CDD:238606"
     Site            order(150,152,154..156)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238606"
     Site            152
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238606"
ORIGIN      
        1 mqeytgdaie yphdaevtdd fslagvpdaf arlwtphrma yikggqdqfk nkddcpfcvg
       61 ptrsdeesli vyrgktcyvv lnlfpynpgh llvcpyrhvp dytditeeet aefadltqta
      121 mrvlrkvsnp sgfnlgmnqg vtggagiaah lhqhvvprwg gdgnffpiia qtkaitqtld
      181 evrqlvaeaw pgeshae
//
LOCUS       WP_284976565             334 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. efr-133-TYG-104].
ACCESSION   WP_284976565
VERSION     WP_284976565.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..334
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37240
     Region          4..317
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mnrpitlftg qwadlpfeev arlasewgfd gleiacwgdh ldpqlvvddd aylqgkldil
       61 ekyqlkvhai anhltgqavc ddpiderhqd ilppsvwgdg spegvrqraa eamkttaraa
      121 arlgvdtvtg fsgssiwkcv amfppasdam iergyqdfae rwnpildvfd evgvrfalev
      181 hpseiaydyw ttkrtleaig hresfgvnfd pshfiwqdld pvmflqdfad kifhvhvkes
      241 irqlngrngr lgshlpwadp rrgwdfvtag hgdvnwepif rtlnaigyag pttiewedag
      301 mdrlvgapqa ldmvrklaai qppaaafdaa fasr
//
LOCUS       WP_284976571             443 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Arthrobacter sp. efr-133-TYG-104].
ACCESSION   WP_284976571
VERSION     WP_284976571.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..443
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46103
     Region          5..437
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 mnpvllfilg vvfvalgvai sialhevghl vpaklfkvrv tkymigfgpt iwstkrgete
       61 ygfkalplgg yvamigmypp nkddggvrps stgmfqtlat earsmaheev gpadearvfy
      121 klpvwkkiii mlggpamnml iglvllavll mgfgvatatt tiadvskcqv aagktvdpns
      181 tdckltpaaa aglqpndtik sfdgrpvtsw deltgwiras agkavaitve rngsevttsv
      241 tpvlssrpvv gadgrqeqda sgalkyqevg flgigaqsal vpqpassvlp magqniaqis
      301 gvifnlparv vgvakaafsa eprdpngpis vvgvgrvage vaameqvplq arigtlvgll
      361 aglnfalaif nlvpllpldg ghvagalyeg arrrvakwrg kpdpgafdia kllpatyvva
      421 allmamsall iyadivkpvn ifg
//
LOCUS       WP_284976594             447 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Arthrobacter sp. efr-133-TYG-104].
ACCESSION   WP_284976594
VERSION     WP_284976594.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..447
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48055
     Region          27..443
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtvvplpleq tlpggelihg aeggsvvrrs vlpggvrvlt eampgqrsat igfwvavgsr
       61 deaegqhgst hflehllfkg tkrrtaleia safdevgges naatakestc yfarvldtdl
      121 pmaidviadm vtgavldpae leqerdvile eiamdsddpt dvahekfvea vlgthplarp
      181 iggtpdaira vardsvwehy qryyrpeelv itaaggldhd vvcnlvldal teagwqlepg
      241 vspvqrratn qavisgtpgl hvvkrpveqa niimgcptmv atddrrfvms vlnavlgggm
      301 ssrlfqeire krglvystys ftaayadagy fgmyagctps kvrqvvdllg veldklaqdg
      361 iteeelrkav gqlsggivla ledtgsrmsr lgraelvsge fqdidetlar iqavtvdevq
      421 elarelaeap rtitvvgpfe dnetfgl
//
LOCUS       WP_284976631             303 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284976631
VERSION     WP_284976631.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..303
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31610
     Region          12..298
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mnqtgrpqdf pmtnpradrv rdvaklagrp arlkrgrfla egpqavreal tlhrertarg
       61 gpavvhevfa saacldrlpe ladlaegtll rlatdevlaa madtvnpqgi vavcsfvdvs
      121 ldsvldagpr liavmcqvrd pgnagtvlra adaagadavv ltgssvdiyn pkavrstags
      181 lfhlpvvlga diedvvarck glgigvlaad gygtldldrl qdenaarrlg qasvespyal
      241 erptawlfgn eaqglseael aladhrvavp vygaaeslnv gtaatvclya sarsqqgarv
      301 pnm
//
LOCUS       WP_284976652             742 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Arthrobacter sp. efr-133-TYG-104].
ACCESSION   WP_284976652
VERSION     WP_284976652.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 742)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..742
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=80931
     Region          3..742
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mhdadlvheq eyvaglyarl delreekraq laqvrragav gtmqnvserd afaalyedrl
       61 aqldavddrl vfgrldldsg eeqyigrigl ttadlqrlmv dwrapeaghf yqatafdrqg
      121 vrrrrhlilq grevkaiedd vldaglladd eplqgegall aalnskrtgr msdivgtiqs
      181 eqdriirssi sgalvvqggp gtgktavalh raayllythr drlksagvll vgpsssfmhy
      241 iervlpslge tgvvmaslgr lmpgihavpe edsnvaalkg kldmakvvan avanrqrtpa
      301 qdlilevdsr kltlsvrqvr rarekaratg kphnearltf vkillrelte qltdlveesn
      361 ignnadrayl aedvrsardv rialnlcwmp mtpeklisel fskpailevc tphltpeqrd
      421 llqrpadapw teadvpllde aaellgeldp aagrglaqqe adrardlana kqtlanmesm
      481 gvdvlvtaee ladqnqeres rltaaerats drswafghii vdeaqelspm qwrllvrrcp
      541 lksftivgdi aqtsaaagan swksalapsf gdrwsleelt vnyrtpsqia eaavrmanra
      601 glvvsapkav regkwspivd rvdaegivpr llevlpeeit aldggllavi adgpllpqaa
      661 aalrkvygrr vgggagsyeq divvmspkea kglefdgvvv lepaamlnhe hgkvgdlyva
      721 mtratqrlrl iaaaplpagi er
//
LOCUS       WP_284976727             476 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: purine-cytosine permease family protein [unclassified
            Arthrobacter].
ACCESSION   WP_284976727
VERSION     WP_284976727.1
KEYWORDS    RefSeq.
SOURCE      unclassified Arthrobacter
  ORGANISM  unclassified Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="unclassified Arthrobacter"
                     /db_xref="taxon:235627"
     Protein         1..476
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51264
     Region          14..460
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mspdtmrage dsvaedrgyr nsltkiepyg iehipdverh gkprsqfflw faagmnfpiv
       61 vlgfsatyfg lpfwaaalai ilagvtssag mgylsqmgvr lgvpqqmqgr gplgfignlf
      121 pvayvnvfag igwaavtvil ggkaislltd ipfwlsslal mgiqlgvavi gynlihflqr
      181 ilsfvlvigf vfitvvaaan grvetdfnva akgfdgvggw iiffgwffsf ivawmpfasd
      241 ysrylpntag nrrgagwatm lgnfvtlvwm gilgtllgtt ttasdsigal kelmgpwaav
      301 glgvvalssf tqnflnvygg aisiqtmgvp vkrhtavifi ciasylvaqw gqtgfnegft
      361 aflnltayci apyvavlvcd ylfggrrtdr glrelfdksr kfewgfvawa agvvlsspfw
      421 mssiytgpia aafpgigdls yyvgaavavg vyfathrrqr lsghemldrt pagqtl
//
LOCUS       WP_284976663             434 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: aromatic ring-hydroxylating oxygenase subunit alpha
            [unclassified Arthrobacter].
ACCESSION   WP_284976663
VERSION     WP_284976663.1
KEYWORDS    RefSeq.
SOURCE      unclassified Arthrobacter
  ORGANISM  unclassified Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="unclassified Arthrobacter"
                     /db_xref="taxon:235627"
     Protein         1..434
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=48762
     Region          37..428
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
     Region          192..430
                     /region_name="RHO_alpha_C_GbcA-like"
                     /note="C-terminal catalytic domain of GbcA (glycine
                     betaine catabolism A) from Pseudomonas aeruginosa PAO1 and
                     related aromatic ring hydroxylating dioxygenases; cd08884"
                     /db_xref="CDD:176893"
     Site            order(210..211,215,218..219,222,224..225,354..355,
                     392..394,396..400,411..414,418,421,425)
                     /site_type="other"
                     /note="putative alpha subunit interface [polypeptide
                     binding]"
                     /db_xref="CDD:176893"
     Site            order(219..220,222..223,225..226,229,324..325,327,335,337,
                     344,346,376,379..380,386..387,390)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176893"
     Site            order(219..220,222..223,225..226,229,324..325,327,335,337,
                     344,346,376,379..380,386..387)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:176893"
     Site            order(225,229,390)
                     /site_type="other"
                     /note="Fe binding site [ion binding]"
                     /db_xref="CDD:176893"
ORIGIN      
        1 msapanlpln trgklasslp aeqlaeisel fdfrragysl dapfytdpti fgvdmqaifg
       61 qhwifaasia elpepgdyvt vdygpysliv lrnddggvnv lhnvcrhrga rvltepagst
      121 gnlvcgyhsw tynpngdlih asapgeakfd kgcfglkrah srvfaglifv ciadeppadf
      181 detgkifepy laphdlsktk vayqqnivee gnwklvmenn recyhcdghp elacslfptw
      241 glteglipah leevwdrnke aqssleercr ryglpyevve eldtrvagir isresldgeg
      301 esfstdgrrl skkllgdlrd frlgrcsmhl qpnswfhflg dhvitfgvfp inehqtlvrt
      361 twlvaddaee gvdydleklt ytwkqtnlqd kafvelcqkg agspayepgp ymkseyqvea
      421 finwyvqrvq ehla
//
LOCUS       WP_284976822             387 aa            linear   BCT 25-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284976822
VERSION     WP_284976822.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Rengstl,B., Oster,U., Stengel,A. and Nickelsen,J.
  TITLE     An intermediate membrane subfraction in cyanobacteria is involved
            in an assembly network for Photosystem II biogenesis
  JOURNAL   J Biol Chem 286 (24), 21944-21951 (2011)
   PUBMED   21531723
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Komenda,J., Nickelsen,J., Tichy,M., Prasil,O., Eichacker,L.A. and
            Nixon,P.J.
  TITLE     The cyanobacterial homologue of HCF136/YCF48 is a component of an
            early photosystem II assembly complex and is important for both the
            efficient assembly and repair of photosystem II in Synechocystis
            sp. PCC 6803
  JOURNAL   J Biol Chem 283 (33), 22390-22399 (2008)
   PUBMED   18550538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..387
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=41314
     Region          69..243
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          175..345
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
ORIGIN      
        1 mgfmatpesy vlaigtkkgl wlatspdrkd wslsgphflm seipsigidt regktrimvg
       61 vrsehwgptv ahsddlgasw tepehgaitf pegtdaaler iwqiypdaes rpgvvwagce
      121 pisvwkstdg gehfelnrgl wdhphrsdwg agyggaaahs ivvspsgenv hiamstggvy
      181 rsldggaswe prnkgisayf mpdpqpefgq cvhkiaadaa vegrlyaqnh hgvyrtddng
      241 enwdsiaegl padfgfvmlt hprregtawv iplkadgeri ppggvlavhr tddagstwke
      301 lrtglperey navlrdaaav dtaepvgvyf gtrggavyas adegetftev aahlpdvlcv
      361 raavvvgdrs gsavdgaetr aaapvpg
//
LOCUS       WP_284976700             518 aa            linear   BCT 25-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284976700
VERSION     WP_284976700.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..518
                     /product="long-chain-fatty-acid--CoA ligase"
                     /EC_number="6.2.1.3"
                     /GO_function="GO:0004467 - long-chain fatty acid-CoA
                     ligase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55614
     Region          6..507
                     /region_name="FC-FACS_FadD_like"
                     /note="Prokaryotic long-chain fatty acid CoA synthetases
                     similar to Escherichia coli FadD; cd05936"
                     /db_xref="CDD:341259"
     Site            order(164,167..172,174..175)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(167,282..283,304..309,391,403,406,417,500)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(167,208..209,256,258..259,262,282..283,304..309,391,
                     403,406,414..417,481)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(208,258..259,262,282,414..416,475,481)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mtalslasil aesarkypdk tavisggqsy tysrlwqhar syagqlqqag igpgdvvalm
       61 spnvvefpta yygvqaaggv vvpvhllltv eevihvlrds gakilvchaa flaigrqaae
      121 etgipvllvg pvpegednvs rlrsdgdrel gsyvtreaed pavifytsgt tgrpkgavlt
      181 hlnmvmnatv savdandvrt sdialgclpl fhvfgqtasm nalfrlggtl vllprftgea
      241 alelmaahdv nvfhgvptmy mqllsaaegr pelpslrlcv sggaalplav mekfnstfna
      301 tiyegyglse tspvvstntp hsgvrpgsvg qaiwgvevqi gdhrvpervv pvptgelgei
      361 lvrghnvfag ylnnpqatqq amvegwfrtg dlgtmdedgf iyvvdrtkdv iirsgynvyp
      421 reveevlsrh paiaqvavig ipdelrgeev cavvvldpah adnapsaqdi idwsqehlak
      481 ykyprhirfv gefplgpshk vlkrelrrtv glgeqnqa
//
LOCUS       WP_284976825             925 aa            linear   BCT 25-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284976825
VERSION     WP_284976825.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 925)
  AUTHORS   Pereira,J. and Lupas,A.N.
  TITLE     The VCBS superfamily forms a third supercluster of beta-propellers
            that includes tachylectin and integrins
  JOURNAL   Bioinformatics 36 (24), 5618-5622 (2021)
   PUBMED   33416871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..925
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..925
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=95672
     Region          439..500
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          489..550
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          638..698
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          687..748
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          737..797
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          787..848
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          837..>884
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mdllrrstal saglavfaag llfvqapata vplpgptnpn vkffpgtphs ehvfetplgq
       61 aqplqqqtsp mksaplssaa psgpsaaplg qggaaagpng visirlvtak ladntnpvsm
      121 pdaekvvast sgywqamtnn rlsmtvtsev pefqskarst dsygtiisti sselswsssp
      181 ysamviiipt sslsggalga gyssgsysgr vllpqiskfs nnvmshefgh viglmhadal
      241 qcgsgapdvg tdsngqftdp scyireygdt tdlmgaaqha qpvvsstfwd yaglgrgdei
      301 rdvgvatgsq tytltpwggt asqravkftd pvskevyyle lrepagyddy lrygpsgnmg
      361 vkvaqrggat iasslilmps tkpfpeqwya knqtwqagst fttytgtqvt insvsatsas
      421 vtinadpklk armrfsagdf ngdklpdvis retdgslllf aglpgnrlad pvqigtgwgi
      481 fnavfgtsdf dgdgfpdila rasngalwly pgdgkggfla arqvgsgwqg ftnivgvgdf
      541 ngdghsdvva savdgtlwly pgdgtggfla asqigqgwdv fkslaaagsf gggtagllat
      601 atdgtlyvyp gdgkggflpr agvgsgwagv gdlvsgqdft gdqvtdvlta sstgtmrlyp
      661 gngsgfadrl pigtgwnqya qvweagdfng dgvadvlarg tdgalwlyrg ngsgsflppl
      721 qigsgwdmft avlstgdfdg dghpdlaard aqgnlwlyps dgkgnflark qigtgwqnft
      781 allapgdfsg dgkadivgra pdgslwlypg ngtggfqpwr qigtgwnmfn svvqggdfng
      841 dgkedvmarg tdgslwlypg dgrggflpkv slgsgwnmft sftalgnaft gtgapsvvgv
      901 agdgtlllyt gngsgrfqpv vlapr
//
LOCUS       WP_284976717             207 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284976717
VERSION     WP_284976717.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18527488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..207
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=22190
     Region          29..102
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          111..207
                     /region_name="COG3837"
                     /note="Uncharacterized conserved protein, cupin
                     superfamily [Function unknown]"
                     /db_xref="CDD:443048"
ORIGIN      
        1 mtigraekae vpetgpeald algplegvia aqvkrhrlda emsaaelatr aglskamisk
       61 iesastsssl ttlqrlaqgl nipvtalfqg adtereatft ragegsvtvr sgtrhgheyr
      121 slgslkrrdr aiepslvtlt sasdvfpqfq hagtefiyml egrmvyghgs yeyelrpgds
      181 lvfegegphg plrlvelpir flavtap
//
LOCUS       WP_284976906             458 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284976906
VERSION     WP_284976906.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..458
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49458
     Region          5..449
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mqnldrdvvi vgagpsglta arelkkagls vavleardrv ggrtwtdtid gamleiggqw
       61 vspdqtalia lldelglemy sryrdgesvy iaadgtrtky tgdtfpvnpt tkaemdklta
      121 ildglaaeig atepwahpka reldtisfhh wlrqnssdee acnniglfia ggmltkpaha
      181 fsalqavlma asagsfthlt dedfildkrv iggmqqvsll qaaelgadvv lnspvrsitw
      241 dengatvvse qatvnaryvi mavppnlysr vsfdpplprr qhqmhqhqsl glvikvhavy
      301 rtpfwredgl sgtgfgagal vqevydntnh gdsrgtlvgf isdekadavf elsaedrkka
      361 vlesiagflg ekaltpevyy esdwgseewt rgayassydl gglhrygkdq hanvgpiyws
      421 ssdlaaegyq hvdgavrmgq ataariveah klsalpva
//
LOCUS       WP_284976952             481 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284976952
VERSION     WP_284976952.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..481
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49911
     Region          1..469
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mvdvavvgag pnglaaalvm aragldvhvy eagatigggt rtteliepgh lhdicsavhp
       61 malaspffrs fdladrvelr vpevqhgapl dvggaalafq slertaaelg adgpaykrlm
      121 gpilehvegv vdltsnqllr vprdplgair fglatfdqgt plwnrrfcee aapalitgvm
      181 ahavsalpsl satgaglllg vlahsggwav pvggsasitn amaedlmahg gtihtdqrvd
      241 sldqvrpara illdvapptl arlggaeipg ryrkaletfr fgnaackvdf ilsgpvpwka
      301 aglakagtvh vggsrasiae aenqvasgkh panpyvlvsq psvvdptrap aghqilwtyc
      361 hvpagsdvdm aeavtarien yapgfrdvvv asktttaadl saynenyvgg dfsagrvdvr
      421 gllkrpvvst vpwrtpvkgv ylcssstppg pgvtgmpgyh aakhalkdif qkqvpglglr
      481 l
//
LOCUS       WP_284977104             108 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: histone-like nucleoid-structuring protein Lsr2
            [unclassified Arthrobacter].
ACCESSION   WP_284977104
VERSION     WP_284977104.1
KEYWORDS    RefSeq.
SOURCE      unclassified Arthrobacter
  ORGANISM  unclassified Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Gordon,B.R., Li,Y., Wang,L., Sintsova,A., van Bakel,H., Tian,S.,
            Navarre,W.W., Xia,B. and Liu,J.
  TITLE     Lsr2 is a nucleoid-associated protein that targets AT-rich
            sequences and virulence genes in Mycobacterium tuberculosis
  JOURNAL   Proc Natl Acad Sci U S A 107 (11), 5154-5159 (2010)
   PUBMED   20133735
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18741]
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Gordon,B.R., Imperial,R., Wang,L., Navarre,W.W. and Liu,J.
  TITLE     Lsr2 of Mycobacterium represents a novel class of H-NS-like
            proteins
  JOURNAL   J Bacteriol 190 (21), 7052-7059 (2008)
   PUBMED   18776007
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Oshima,T., Ishikawa,S., Kurokawa,K., Aiba,H. and Ogasawara,N.
  TITLE     Escherichia coli histone-like protein H-NS preferentially binds to
            horizontally acquired DNA in association with RNA polymerase
  JOURNAL   DNA Res 13 (4), 141-153 (2006)
   PUBMED   17046956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10570331
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="unclassified Arthrobacter"
                     /db_xref="taxon:235627"
     Protein         1..108
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11788
     Region          1..106
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 maqkvkiilv ddldegdade tvrfgldgvs yemdlstana aslrqalepf vakarktssg
       61 ratrgrattp rnqdsaqirq wardngytvn srgriqaeiq eayqkans
//
LOCUS       WP_284977132             568 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Arthrobacter sp.
            efr-133-TYG-104].
ACCESSION   WP_284977132
VERSION     WP_284977132.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-104
  ORGANISM  Arthrobacter sp. efr-133-TYG-104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Arthrobacter sp. efr-133-TYG-104"
                     /db_xref="taxon:3040324"
     Protein         1..568
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=61244
     Region          16..551
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtttptntpd rartvpsvla idrlqvtfat dggdvhavkd vsldvkagev vaivgesgsg
       61 ktvtaktilg llpetavssg avvingnnvi svskstlrki rgrdvamvfq epstalnpvf
      121 tvgwqiaegi rahakdghrv takaakerav ealrkvgipd petrvnyyph qfsggqkqrv
      181 viaaalalnp glivadeptt aldvtvqaei lqllrdlrdn ygtsivlith nmgvvadlad
      241 rvvvmyqgdv veeassrilf aepkqeytrn llaavphlgr nsasegarsr lhqdgkilve
      301 aknltieypg rfgrngfkav dnvsftisen evfglvgesg sgkstigrai aglnrttggs
      361 lkvlgyemld fkertfrplr keigfvfqdp aasfnphlti gecvaeplii hgkptaaear
      421 kkvgellesv qlpasysery phelsggqrq raslarslal nprlliadep tsaldvsvqa
      481 kvldlfkdiq eqfgfaalfi shdlavvdml ahwvgvlykg elveqgignh vmgspqhdyt
      541 krliaslpvp dpdeqarrre ahrallgr
//
LOCUS       WP_284977546             556 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Arthrobacter sp. fls2-241-R2A-200].
ACCESSION   WP_284977546
VERSION     WP_284977546.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..556
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=60253
     Region          181..556
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mthpspwdms ekkkllvfer sfhehslrir vvlsqlplsv cvcisailvw lyfpatldne
       61 lfviyllsqt illalcvllp wdrlpyasfl sipildmvsi gfaregsvds itglsvlvvl
      121 pviwlcasgl yprlaifmsf lgplgivwvp lfvrgalteq ditkpllfpi lmlgigisvs
      181 vltlsvvrqq ralkekdaal kkaldvsttq erllntvmea lplgvvavds dgqdilmnrr
      241 qrqthalaap pgnpnpaeae llifdrdrts plaadrrpvr ravlgerftd qlvwigtakd
      301 qraftasarp mtddggkfag svvvfsdvtd lvnalaakdd fvanvshefr tpltsilgyv
      361 elilddphgl daaakaqlni vrrnaerllt lvsdllsvrs ghiviqphav dvaelvrgsv
      421 tsaepraaka girlsmdvpd aleahvdssr maqvldnlvs naikyspdgg dvevaaweds
      481 nfvfcrvsdt gmgmtddeqa eaftkffrag gvrnstipgv glglpiskai veahggtitl
      541 dsqpgrgttf tvkvpa
//
LOCUS       WP_284977556             333 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. fls2-241-R2A-200].
ACCESSION   WP_284977556
VERSION     WP_284977556.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..333
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36688
     Region          34..305
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 maytakdwpi taallqfpgt daagkhinda dastwasvlq evkeagfena dltdswvrpg
       61 dlgkerlaef kqtahevgig vpvisairrs vihqtdwaen layshrtida aaelgcevvs
      121 fglhqaitpe qqkqlwfwtv egykdpvgdk eawgnaasri relgkhaaea gilvslemye
      181 dtflgtadss vqlvqdigld nvglnpdign lirlhrpied wremvaktlp ysnywhmkny
      241 lrdedvards fitmpapmes glinyreafk falsvgfqgi lctehyggdg lsvtasnqey
      301 lrrhvlpktd gyalgksqva qgrqepatel agv
//
LOCUS       WP_284977567             307 aa            linear   BCT 25-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284977567
VERSION     WP_284977567.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Niehaus,T.D., Elbadawi-Sidhu,M., de Crecy-Lagard,V., Fiehn,O. and
            Hanson,A.D.
  TITLE     Discovery of a widespread prokaryotic 5-oxoprolinase that was
            hiding in plain sight
  JOURNAL   J Biol Chem 292 (39), 16360-16367 (2017)
   PUBMED   28830929
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Fan,C., Li,Z., Yin,H. and Xiang,S.
  TITLE     Structure and function of allophanate hydrolase
  JOURNAL   J Biol Chem 288 (29), 21422-21432 (2013)
   PUBMED   23754281
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Wang,L., Grau,R., Perego,M. and Hoch,J.A.
  TITLE     A novel histidine kinase inhibitor regulating development in
            Bacillus subtilis
  JOURNAL   Genes Dev 11 (19), 2569-2579 (1997)
   PUBMED   9334321
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005226
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..307
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=34100
     Region          14..270
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 mttpstalss nsvrsearyt wggdeflfve vdesmslaan fkvmsiarkl adaelsgvvd
       61 icpanasllv rfnpdilpps tlestvrkie lelrnhdeqs letriievpv wyddpftaev
      121 aqrfregfhq epggtdldya akvnglkdaa efirrhheqp wlvsmvgfva glpflfqlve
      181 rdkqlqvpky lsprtdtpkl tvghggcfaa iysvrgaggy qmfgvaaapi ydpaqsladf
      241 kdfmvffrpg divkfkpvte deynaiqaqv edgsyryrqv pvtfdagral sdpqaynqel
      301 mealngi
//
LOCUS       WP_284977590             397 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284977590
VERSION     WP_284977590.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..397
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40778
     Region          143..>185
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 msthstdaps hetaelplra rrilhplriw aflltglvll gaafwagtlv kapndaaldn
       61 aqksvpvtfp lsmkvvdrql vlkgtvvrgq itaisppvip gaarqvvtkp gpapgtevap
      121 gsflgsvggr pvfllpddvp fyrdldvgds gddvvqlqka lqgmgfsavt atgkfdaasr
      181 davkriysgd gltapdkpif raqefaqipg nrgvvassag latlvtgtvp llviqttpdv
      241 vtaratvvda dsltaggkvr lsvgdqsivs tvlsvgaftd kagasgegpg kdvtvsvppe
      301 gsawlvpdkl vnvqgttdpq prlavpliai qhdgagsfid veqpasstgt rpssssstps
      361 qaptfqrvdi tvttqssgwa avessiplsv gqqvrvp
//
LOCUS       WP_284977644             258 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284977644
VERSION     WP_284977644.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..258
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27313
     Region          8..252
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 msrpekisfv gstgdvlagv vdvpegplrg wgvyshgltl gkdspaasri ckglaeqgig
       61 mlrfdnlglg gsggewsags fsvkvadtil aaafmqeqgr risllvghsf ggaavlaaar
      121 dipglnavvt vgapyepkhv ehmfdteida ilrdgsavvd lggrpmevrr hfvedvekad
      181 lrdcirglhk plmvmhsptd ntvgidnase ifrtarhprs fislegsehl ltgkgqaarv
      241 ariisawadp ylelpvtv
//
LOCUS       WP_284977699             910 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284977699
VERSION     WP_284977699.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 910)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 910)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 910)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 910)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..910
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..910
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=98204
     Region          <117..>312
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          760..910
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          853..906
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 msaellssgg rgaasaaapd lvgsaadrqt wsllarsrdl skaamqlesp gsygvvltgq
       61 rgigksglar alvsslgpkv qslqlrntva gsetpygclg fllarlpsea vatptgilhg
      121 itrliqseaa grdtvvivds aggmdpmsag vllnlmatgt akviatvqha sdlppdfhrl
      181 vlegqlgevh lemlteeqtk qvlgsvlghy vsatlvgslh savggnpmll halleeqrhs
      241 gnlvlndsvw tlreqiklvg apvvedfvrs klaresqahr tvvellscak rvrlvelaai
      301 vgtevvveme daglltvdrc aehwvclrds figevvggwl strrrrelrl mllgpkepsl
      361 eglasqdvla yarwiqaced dtapsaayal aagraaldaf dpafaitsie sldpkddewv
      421 pgqrvkaaay lmldlplhaa rtldevppdr aaaldplefa hlvaaqcqam lwidgrcgti
      481 pdvldqavav lenrseghpa aiiakarhrl qlsryeyrtf igdyasvves ledefangpg
      541 edydywmrac fylmearcil greleaqela rtmsrhvegm arspqleeaf vlplfltllm
      601 sgqwrkcvgl lsrtpshpar lqyrgalpel grglaftyag kpasaieplr savahlelrp
      661 smnlikvaya atafayaqig nsaeagryld lyrtsrgvgt yiaesiaefc aemagrwmgd
      721 pdvkqrllmr vhddvdnqrl tpagiclfga tvegsddeyr llediaarrq gplarisgdl
      781 argalhknan allaaanaaa smdllvvear cvamaldyar dagesttart aqlrlerleh
      841 lvsalpihpr sdapvltere rqiaklagkg vsnreiamdi gvsvrtvegh lyqvftklgv
      901 tsrgelqell
//
LOCUS       WP_284977752             223 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Arthrobacter sp. fls2-241-R2A-200].
ACCESSION   WP_284977752
VERSION     WP_284977752.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..223
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=23255
     Region          2..215
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mtrlilasqs partklltea giehevlvsd vdedavqaky gvtdahdtal llarakaeav
       61 aalpesdgal vigcdsvfef dgeshgkpyt advarermlr msgsqgvlht ghwlvdcrdt
      121 aaeadeddae hgapegtgat vgavssaevh ftqmneneid ayiatgeplh cagsftidgl
      181 ggafirkvdg dphavvglsi stlrdllgha nvpitdlwqa gna
//
LOCUS       WP_284977795             365 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284977795
VERSION     WP_284977795.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..365
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38127
     Region          17..355
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 masnydvviv gggigglsla salagkctva lveaeqslaf htssrsarql ipsygpavvq
       61 eltvrtlell herdstaaea vltprafmmv gddvtvraea sgnmlpishe ealrlcpaln
      121 pdsftaagld tgsfgcnapl lleehrriae tagvdiitga rvhsaqrlgs gwqvgagteg
      181 fqsgvvvnaa gawadelavi sgveklglqp yrrtaaivnv esplppetpm vcaadesfyf
      241 rpegnqvlis pseavpsgpe darpypgdve kliatlndvt smgirsvdra wtglrteaad
      301 aipvvgfdae apgffwlagq ggygfqtssg iaelaaalil gtvqpdspes rtaerlastr
      361 wsirr
//
LOCUS       WP_284977972             797 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Arthrobacter sp. fls2-241-R2A-200].
ACCESSION   WP_284977972
VERSION     WP_284977972.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 797)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 797)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 797)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..797
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=88646
     Region          72..792
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 meeratsapp sggedgnkav agpatsvagr slsavpvdtp gvrptfpgrr ertrsrlarl
       61 tgrgsapysp ilepllrtvr annpkedfdl iqrafevaer shqgqkrksg dpyithpvav
      121 atilaelgmt gttlaaallh dtvedtpytl adltrdfgpe vamlvdgvtk ldkvsfgeaa
      181 qsetvrkmvv amakdirvlm ikladrlhna rtwrfvsaes ssrkaretle ifaplahrlg
      241 mntikweled lsfaalypkv yeeivrmvgd rtpereksls virnqiaddl rtakikatit
      301 grpkhyysiy qkmivrdkdf ddindlmgvr vlvdsvrdcy aalgtlhsrw nplpgrfkdy
      361 iampkfnmyq slhttvigpg gkpveiqirt hemhrraeyg vaahwkykdq pnrtavgpgs
      421 prdgdmgwlr slvdwqqets dpgefldslr yeinarevfv ftpkgevmal pagstpvdfa
      481 yavhtevghr tigarvngkl vplnselnhg dwveiftska egagpsqdwq hfvksararn
      541 kirqwftker reeaidrgkd mltramrkqn lplqrlmthd alsavaedfh yvdisglyag
      601 vgdghtsaqs vmeklvehlg ghetpdedld evsiptqvak skfsdsgviv rgvgdvwvkl
      661 arcctpvppd pilgfvtrgs gvsvhrtdct nvsglrdqpd rivdvewapt qssvflveiq
      721 vealdrksll sdvtrvlsen hvnilaasvh tssdrvaisk fafemgdpky lhhvlnavrr
      781 idgvfdvyrt tgnrrrn
//
LOCUS       WP_284978129             251 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284978129
VERSION     WP_284978129.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..251
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27341
     Region          <64..174
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mpfirdsrqs wfmtehthdd gdtyvgglrp gglnlhedae navdmwdgmy rerpkvwsgn
       61 pnpqlvaear dlkpgraldl gcgegadalw laeqgwtvta ldvsavaler gaahaaeagh
      121 aeritwqqqd ltewvpepvf dlvsaqflhs pllswrdsla saaaavapgg tllvvghhph
      181 glppwsshhh dtaafftpeq laeelrpegg lrlhegpwrv dvltsrertm igpggepati
      241 ldtvlkatkr c
//
LOCUS       WP_284978227             659 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD/NAD(P)-binding protein [Arthrobacter sp. fls2-241-R2A-200].
ACCESSION   WP_284978227
VERSION     WP_284978227.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11816065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..659
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70560
     Region          1..639
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
     Region          9..200
                     /region_name="NAD_binding_9"
                     /note="FAD-NAD(P)-binding; pfam13454"
                     /db_xref="CDD:433222"
ORIGIN      
        1 mtsrvpaiaf igggprtagv lerlaanrps lfggplhvhv iephqpgsgr iwrydqspgl
       61 llnstaadvt mftdgsvvcd gpavdgpgls twaagvldgs irdvpvleph mleqlraltp
      121 asfptrqlqs kylewffrra vsalgtdvtv tvhrdtatav spasassgth dghddgthri
      181 rlapgaevva dvvvyalght dslpddesag lsdfaarhgg fhappsyttd vdysaigagq
      241 dvivsgmgla fvdllvllfe grgsrfeegh dgeltylpsg aeprvwagsr rgvpyhskis
      301 stlrgepadr pryftasaie sllgshseld frahlwplia kdagyayyre lftghpsrvr
      361 gtwasfearf daldwyspgr edlvaasvpd paswldlerl dhplsgcafa dhgavqrsvs
      421 ayiqrdldlr tspehsetla lftallfvym dlgrlvpqer lnarsqqaih gwwhgffsfv
      481 dsgppahrlr emlalqragf lkflgpgvwv radesagrfv agsfqspvvv daaayiearl
      541 psasversan paltdlhdag rgteqrllts egthstgkll vsgnhevlsp vgtpqkglfa
      601 vgpwtsgwga gafarpntna apfrendala rrilstiaag aasrvpatql rgattkgli
//
LOCUS       WP_284978308             994 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Arthrobacter sp. fls2-241-R2A-200].
ACCESSION   WP_284978308
VERSION     WP_284978308.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..994
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=109763
     Region          28..991
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 msstfgsssp adryqaaatr aaeaktylga farsldfald dfqreacrsl qegrgvlvaa
       61 ptgagktivg efaiflalqr glkafyttpi kalsnqkfae laakygqanv glltgdtsin
      121 gdapvvvmtt evlrnmlyad setlgdlgfv vmdevhylad rfrgavweev iihlpsevqv
      181 aslsatvsna eefgawldtv rgdtdvivse hrpvplwqhv mvgreivdlf agdvtfdaia
      241 pgsvaasaag ddvpglsesd eigeepvaar rkhktsaksa aaaavrqavt gpefevnpdl
      301 lamarsesrm nmgaryshgs rsrrrqdryr derqqteqrs pvrkasrpqv ieslrrqdll
      361 paitfifsra gcdaavaqca asglwltteq eqqiiaqrvd easheipadd ldvlgfwgwr
      421 dgllrgfaah hagmlptfke vveklfadgl vkavfatetl algvnmparc vvleklekfn
      481 geahvnitag eytqltgrag rrgidvegha vvlwqpgtdp aavaglasrr typlnssfrp
      541 tynmsinlia qfgrtrarei lessfaqfqa drsvvglarq vrgreeslag yaksmqchlg
      601 dfteyaklrr elsdaenfaa rdhhrarksr vadsltrlip gdvitiysgr laghalildv
      661 dpnareprps vltsdnqlrr igvhdldgpv spvtriripk afnakvpksr rdlaaamrha
      721 isedapqspr nsrhedfglg arlpdqeqhi adlrralrah pchgcsered harwserwwk
      781 lrketdglvr qiqgrtntia ktfdrvcdvl saygyletnd agrvtisdhg qrlrriygek
      841 dllisqsvrq galndldaae lasfattlvy qakredrglr prmpsvales avdivvrews
      901 qledteehyr lpltgepelg lmwpmyrwar grhlqdvlhg tdlaagdfvr wakqvvdlld
      961 qlakipqldp rvaricresi dlvrrgvvay stva
//
LOCUS       WP_284978311             673 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284978311
VERSION     WP_284978311.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 673)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 673)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 673)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..673
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=73302
     Region          45..324
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
     Region          349..665
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msasrterll nlllallntk vglpravlre kvykdsaend vafgrmferd kvdlkqfgfe
       61 ietivdrssf gnddpgttry rigkdsnrlp evvltpaest vlllaaqlwe raalgtaaas
      121 avrklqaagg ftdvdlpagv qprikpagqa fddvvaamhg rhtvrfgyla gstgreeqre
      181 vepwglgsrf gqwylvgwdr argakrffrl srmttavtav pgssceppag fnaraeldel
      241 nelplrqatl evdlgrllal rrravtaqep atgspardrv vvefrdpeql aeelasygpr
      301 vlvqepadlr aavvrrlqaa ldfhtspava ptfpdagrap rarkrtsedq larmlqlvpf
      361 lvhhqglhiq evadrfgisr rqliddlkil icsglpggyp ddlldiqwed dhvyisehld
      421 lnrpvkfsed eaaalltgla mlgdlpqlag mpedqpgsal esvtikltga agtagrlags
      481 vsgqsvapeq sqsfatitqa irdgqqlhlr ylslqkdeit erdvdplrly sldntwyfea
      541 ychsaagirn frldrvesla angraashta stgqdfparl ftpsdddvlv tleltrqgag
      601 laddyyaert aqrpdgglla evrfgnagwv pmfisqhgga arvlapeavh tetgtwlkas
      661 laqyesaags vag
//
LOCUS       WP_284978448             291 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. fls2-241-R2A-200].
ACCESSION   WP_284978448
VERSION     WP_284978448.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..291
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32571
     Region          1..286
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mkialdptpf hhshsllefp rvaadlgyky lqltphadmi pfynhpkadd elvaqlktac
       61 rdadveiasv lpvlrwsgpd edareaavry wkraiqiavd lgvstmntef sgrpekaees
      121 erafyrsmee llpiieregm dvlidphpdd fvedglaair virgvnspni gmvyvashtf
      181 hmgnspleim raagdklrlv hvsdtmdhha shglryitnp pgnavrvhqh lkigdgdvnw
      241 deffgalhei gfldkdntvm vssvfaeddn aedvsiyqle tmkqhiqkvn a
//
LOCUS       WP_284978506             207 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284978506
VERSION     WP_284978506.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18527488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..207
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=22184
     Region          29..102
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          111..207
                     /region_name="COG3837"
                     /note="Uncharacterized conserved protein, cupin
                     superfamily [Function unknown]"
                     /db_xref="CDD:443048"
ORIGIN      
        1 mtigraekae vpetgpeald algplegvia aqvkrhrlda emsaaelatr aglskamisk
       61 iesastsssl ttlqrlaqgl nipvtalfqg adtereatlt ragegsvtvr sgtrhgheyr
      121 slgslkrrdr aiepslvtlt sasdvfpqfq hvgtefiyml egrmvyghgs yeyelrpgds
      181 lvfegegphg plrlvelpir flavtap
//
LOCUS       WP_284978713             290 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Arthrobacter sp. fls2-241-R2A-200].
ACCESSION   WP_284978713
VERSION     WP_284978713.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..290
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31751
     Region          10..288
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mitgtltset flkaveltat epqvfdeaye attqyvpwpk ayggdmvaqa aaammrsves
       61 drqlhsmhsy fmrpvdvgss vryeverlrd grgystrtvr gfqngkpvya amgsfqvped
      121 gpdfqpeapa avepeslsta aealagvdgd ageywssgrs fdmrhipgpv yieleggsvp
      181 qqtiwvkafd elpddadlhr aalayvcdyt ilepllrvng lhwsspglat asldhsmwfh
      241 rdgradewvl yaqeaisgqs nrglamgrff drqgrllatv aqegmiraga
//
LOCUS       WP_284978812             374 aa            linear   BCT 25-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284978812
VERSION     WP_284978812.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Pereira,J. and Lupas,A.N.
  TITLE     The VCBS superfamily forms a third supercluster of beta-propellers
            that includes tachylectin and integrins
  JOURNAL   Bioinformatics 36 (24), 5618-5622 (2021)
   PUBMED   33416871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..374
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=38573
     Region          178..239
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          228..289
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          278..338
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mgtlrrrmav allaavvtam aisplpasaa psgpdpvvtg taivgqtlgt vigpytfygc
       61 gggtgpdfti ywtrdgflva getgrtyvlr pgdagsrmaa hvsasrtacs aetinsaets
      121 pvgaanrasg ftgrtfella rgtdgtlslf grtgkawdap rtvgwgwngf nlvfspgdfn
      181 gdgksdliar dasgvlylyp gdgtggwkpa qvigtgwdvf dsivspgdfn gdgsndvlar
      241 gkdgtlylyp gngaggwltr tvvgtgwdvm dailtpgdfn gdgkvdvlar drngylyfyg
      301 gngagswtrs wligtgwgal kflgaagdfn gdgfadvygv daqgrlvsyy sdgrtgwkgs
      361 evvgngwggf taif
//
LOCUS       WP_284978817             496 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284978817
VERSION     WP_284978817.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..496
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53275
     Region          11..466
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mapghdseaw lqpipesdrt rkvsgqfwiw aganlapinw vlgalginlg lgfadtvtvl
       61 vlgnligmll fgcfvllgqk tgatgmvlar aafgrrgnyl paaiqallvi gwcavntwii
      121 ldlvmalfgt lgwvdptahn yawkigvatv imaaqvaiaw fgykaiaafe kwtvpptiii
      181 lavmsavawf gmkidwgypg paghilagpd riaamsavmt aigigwgitw ftyaadysrf
      241 vstsvpkrkv ylasvlgqfi pvvwlgvlga slatnsgeid pgklivqnfg amalpvlllv
      301 lhgpiatnil niytfsvatq aldininrrk lnlfvgvfsl lavvffifqe dfasvldawl
      361 iglvawvaaw ggimlvhyfw lekrwpakvd rlfdpigtrr lpvvnwagit slvlgifatw
      421 lfmyglipim qgpiavalgg wdlswlaggl tsagayallg prahrkflra danhvsvtpp
      481 tpatpgspav pertta
//
LOCUS       WP_284978857             352 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284978857
VERSION     WP_284978857.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..352
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35399
     Region          47..348
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mrlgtttalq trgiggprpa dgvgkrttwl vlavvvlaaa caaslaigar glslatvwea
       61 ltifdpndgn havviaripr talgllagaa lglagaamqg varnpladpg ilglnagaal
      121 avvvgiylfg vsslsgyvwf aflgagaaaa vvyaiasrgr dgatpvklal agaalsaglf
      181 slmnvilvss qdtfdrfrfw qvgsiggrdw svllpalpfl vvgalivlas grvlnglalg
      241 ddlarglghn valsraitav gvvllcgsat alagpigflg lviphavrsi tgpdyrwilp
      301 fslvsapill itadiigrvi llpgevpagi vtallgapvf iwlirrgkga gl
//
LOCUS       WP_284979102             669 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284979102
VERSION     WP_284979102.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 669)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..669
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=68928
     Region          40..>274
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mtastaqgtd hstnpgnrdr drirdtngtr rgfrtfrqgs rrqrlelasm lvgtallylw
       61 glgasgwana fysaaaqaga qnwtawffgs sdaansitvd kppaalwvtg lsvrlfglns
      121 wsilvpqalm gvatawilyl avrraalpat gndrmahrag llaaavlalt pvatlmfrfn
      181 npdallvllm taaaygvlra iqeqrmrwlv lagvflgmgf ltkqlqvllv vpgfafayli
      241 aaqpkvgkrv mhllaaagam avsagwwlaa velvpaqlrp yiggsqdnsi mdltfgyngf
      301 grlngdetgs vgggngwgqp glfrmfgaef ggqiawlips alilggallw lgrraprtdv
      361 vhasvlvwgs wllvtglvfs fmagiihpyy avalapgiag ltglggvllw qrrsqvstaa
      421 vlalavvaag ltansvlasa ptflpwlrwi illgsiaaga allvpggwss vlvtrttagl
      481 aiaasltgpl aysvatasvp htgaivsagp avtagfgpgf ggnrpprgit rpnaalggtg
      541 agpaggpggg mgglldtaap ssdvvaalqt dagsytwaaa vvgsnnaagy qlatglpvma
      601 vggfngtdps ptlaqfqqdv tdgkihyfia sqmmrgdsgs dtatqiaawv aanyeaqtig
      661 nttvyslhg
//
LOCUS       WP_284979136             198 aa            linear   BCT 25-DEC-2024
DEFINITION  YdeI/OmpD-associated family protein [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284979136
VERSION     WP_284979136.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Pilonieta,M.C., Erickson,K.D., Ernst,R.K. and Detweiler,C.S.
  TITLE     A protein important for antimicrobial peptide resistance,
            YdeI/OmdA, is in the periplasm and interacts with OmpD/NmpC
  JOURNAL   J Bacteriol 191 (23), 7243-7252 (2009)
   PUBMED   19767429
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..198
                     /product="YdeI/OmpD-associated family protein"
                     /calculated_mol_wt=21541
     Region          1..191
                     /region_name="YdeI"
                     /note="Uncharacterized conserved protein YdeI,
                     YjbR/CyaY-like superfamily, DUF1801 family [Function
                     unknown]; COG4430"
                     /db_xref="CDD:443542"
ORIGIN      
        1 mpveleellv kdaaewrawl sanaatspgv wlvlhkkggn vtdldydaal dealcfgwid
       61 gqvkgrdaes fvqrmtprgp rsiwsarnvg hiarlesegk mteagraave aakangrwea
      121 aysgsadlvv pedlaaaiaa vpeaqamfdv ltsqnrfalv hrtnlvkrpe trarkiagfv
      181 emlarheapy pqkkrpap
//
LOCUS       WP_284979124             200 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284979124
VERSION     WP_284979124.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 200)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..200
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21270
     Region          1..>87
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mldieviedp aaaeasldpi rtrilqelte pasatqlaar iglprqkvny hlkaleghgl
       61 velveerrkg nvtervlrat aasylispaa lasvapnpar fadrfsafwl lalaartvqe
      121 mgkliagaaa akkklasfai dgeitfrsaa eraafaeelg vavtalvdky hdggadalas
      181 garkhrlvvv lhptlkstmr
//
LOCUS       WP_284979148             243 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. fls2-241-R2A-200].
ACCESSION   WP_284979148
VERSION     WP_284979148.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..243
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26025
     Region          1..241
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtyslqlytv rgpleedleg tvkrvaelgf tavepynfva nadalatals kngltapsgh
       61 apllranqde ifqaaqklgi gtvidphvda aqwtteadik etakalnaaa akgaeygiav
      121 gyhnhefele nringrsale vlaenldprv vlevdtywaa vggeepvall erlgdrvrfi
      181 hikdgpltkv dkdqvavgsg qmpiwdviea aknleagvve lddfngdifd avsdslaylk
      241 agk
//
LOCUS       WP_284979289             307 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284979289
VERSION     WP_284979289.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..307
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31492
     Region          14..293
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(41,247,250)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(187,218,245,248..249,252)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 msasphltpe plavvvvgea lidivkspeg dieypggspa nvayglgrld vkaglltaig
       61 rdergaaias hlegagvvll pgskslekta tatariaadg satytfeidw alppvalpya
      121 prilhtgsia tflepgagvv rglleqaqga smvtydpnir pdllgshqea lslfeemvpl
      181 tdvvrmsgsd arwlypgkdl edtarhllal gtglavitqg akgslmatkh iqltvpavps
      241 avadtigagd sytsalimgl llrgsdgmap tvlerigtia smassitvgr pganppthre
      301 llagmar
//
LOCUS       WP_284979347             552 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284979347
VERSION     WP_284979347.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..552
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=59029
     Region          238..542
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mepespseam prpaepgmqq svvrlsdciq lmqadlvhan ptpenlghpv sdvlmydpld
       61 twssvddrii lavgcsygsp dfdqllhraa nsnaaavvvk ahgalmeqlr aaavrhslav
      121 lvapdaadwt rlvalarasv mgaaadsvsg vrlgdlyafa naaasitnga asivdplgri
      181 lgystlpgqp idelrrittl tlqettqpaf dndfkavyaa pgavvvpapd dgmarlalav
      241 raggellgsi wiidpgeerr easlvaldrm aplaglhmlh arsasdfger rnadlirtlm
      301 ddaphasfaa aqlgldaang lavaafsiar petgslesvr dlhrllhlvt tvcnvqfsts
      361 hsallgsvvy allpsqgssp ravhariiqe ieayshtiss fpliasvggi aarvedlprs
      421 rseavhtmnh llsqrsrgia sprvalfedf qiplnllkig kfiednglag adeiariqar
      481 daeqqtdyld tlraylatng nisamaaqlh vhnntvryrv grlaedfnid ladpqkrlwl
      541 wlrltttdla aq
//
LOCUS       WP_284979349             241 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Arthrobacter sp. fls2-241-R2A-200].
ACCESSION   WP_284979349
VERSION     WP_284979349.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..241
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25377
     Region          12..240
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mtdhrnawtg akallfdldg vltptavvhe qawkelfdgy ltdaghpqgy rendyfdhid
       61 gkprfdgvrd flasraitlp egpvndhpdh etvqglgnrk naifsgivds rgvepypgsv
      121 kfinaavelg lkvavvsssr napavlraag ldhhfevvvd gqvaaavglp gkpdpatyvy
      181 garllgvpve ecvvvedavs gvqagaaadf favigvdrga grqtlleaga tlvvddlsdl
      241 l
//
LOCUS       WP_284979382             456 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Arthrobacter sp. fls2-241-R2A-200].
ACCESSION   WP_284979382
VERSION     WP_284979382.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..456
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=49275
     Region          25..362
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mernghpaae qrtaqgepap qrepaidlvr ftclllvvaa hclmvnpvlh rdgtvttrnt
       61 lmdqswfdpv gwvfmivplf fvlggetglq swrrlrargg ngfdfaqirl lrlvrpamal
      121 lammwgglwa alllgvdprv iqlmttgaam plwflaaylt aqlsipvmsr lhsrapmltl
      181 avlvvliitv dslrgalpil afinmifvwc avqqlgflra dgffdnrgrt wlvgaiassn
      241 vllglvtgvg vypgnmvvdl nppnlcllll aisqtaslql lrngidavan irwvqmviav
      301 agrrsmtvyl whlpvlvals glllltdisl ppddaaewww aripvffavi aallpvvwif
      361 grlenrptaa shargpshva vvtaavvvfv pvadaafngl tlallgggaa cfalavlllg
      421 rvptpvlppl eeivpepste iratlpepgl ranles
//
LOCUS       WP_284979437             423 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Arthrobacter sp. fls2-241-R2A-200].
ACCESSION   WP_284979437
VERSION     WP_284979437.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..423
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=45510
     Region          1..368
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mligvvaglv glslgvfgvl afriserqrs ivdldvtepl lpegaaevla vvgrafvvvd
       61 avdgvvrasp aayayglvrg htvvhkqlld mtakvrrdgv ileeqyelpr gplgkgtivv
      121 qvraamlgwe yivlladdrt eitrteeirn dfvanvshel ktpvgaisll aealeaspdd
      181 eeavrrfakr mhkesgrlaa lvqdiielsr lqgtnvaqqg navdinmvin eavdrsqlpa
      241 eskdiqivvg grvdslvfgd rdllvtalrn lidnairysp entrvgvgvr tregvvaisv
      301 tdqgegltpe dqervferfy rvdsarsrht ggtglglsiv khvvsnhgge vtvwsqpgqg
      361 stftirlpem egqepdgaea qdrehdggpr sqepgrstrs veqnlqqsqq ggassaqeqg
      421 asa
//
LOCUS       WP_284979519             603 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284979519
VERSION     WP_284979519.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..603
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63995
     Region          1..600
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mrefsvpplv nvapetnitd llireaakas npplfakrds sgvwqdisar dfladvnala
       61 kgliasgvgp gdrvaimsrt ryewslvdfa iwcagavsvp iyetsspsqv awnlgdsgav
      121 aafgeqahhe svirqavqte dlgsvanvwq legagldalr aaganvsdee legrrtlagl
      181 tdvatiiyts gttgrpkgce lthgnfvels enaraslaei inesattimf lplahvfarf
      241 isvlavaggv kvahtpdikn llgdlqsfqp sfilavprvf ekvynsaltk aedggkgaif
      301 hraaetaiay skarqsgtlg iglkvkhavf dklvygklra amgghvshav sgggplgerl
      361 ghffqgiglq ilegygltet tapisvntps mirigtvgap lpgnsvkiad dgeilakgvc
      421 vmrgyykred ltadtfvdgw frtgdigeld sngflkitgr kkeiivtagg knvvpalled
      481 qiradalvsq vlvvgdnrpf igalvtldde alpgwlerhg lppkttlkea sdhpavkaav
      541 qdlinkanqt vsqaesiksf rivpadftea sghltpslkv kraqvmkdfd avieemytap
      601 ras
//
LOCUS       WP_284979522             279 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Arthrobacter sp. fls2-241-R2A-200].
ACCESSION   WP_284979522
VERSION     WP_284979522.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..279
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29968
     Region          1..249
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mkilpdfspf lsswngtgpr vgvvmshgft gsphsvrpwa ehlaaagyav rvpllpghgt
       61 twqdmskrsw rewhqavdda yrelasecdf vfatglsmgg tlalriaatr pvagtvvvnp
      121 glvlddprav mvaalkyvlk stpaiandil kpdqdegays rtpvaaahel kkmyrdtagl
      181 lpristpvrv yrstvdnvis nasldflrak vqapvdvryl rnsyhvatmd ndapeifagt
      241 vefiqrtlaa magdglssgd glssddgrss ekdaadeqa
//
LOCUS       WP_284979524             259 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Arthrobacter sp. fls2-241-R2A-200].
ACCESSION   WP_284979524
VERSION     WP_284979524.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..259
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27879
     Region          1..251
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mtepkaplaf hypghgsnas igvaichgft gsplslmpwa eylagqgfav svpllpghgt
       61 swhdlsatkw qdwyttfegs yvdlarrtrs cfvaglsmgg avalrvaalh dvpgvvlvnp
      121 glsfydrrvk yvaalkyfkr tttpivedrp tpvstedgdy sqtplasvhe lkklfrsatr
      181 alpevlaptl ifkstedavv pptsvesitr higarrlkvv tlphsghvat ldadaptife
      241 esagffrqha sytvasess
//
LOCUS       WP_284979537             598 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Arthrobacter
            sp. fls2-241-R2A-200].
ACCESSION   WP_284979537
VERSION     WP_284979537.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 598)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 598)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..598
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=63877
     Region          8..582
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 maqnpgksnk akvpvarkrl rlglgimltl llvvggklfm vqgldvggma eaalakrltp
       61 mvlpaqrgki ldangavlas siiaynivvd qtvntntatf hryddatgkl neisrdqgit
      121 elagllgmdv nqvrasltge kkyfvvakdi kpeledrisk lyipglsseg vskrvypngs
      181 vaggvigflq dgttgqagie qtqdqilrgt agkrvfeiga dglripvatd eltpavdgsd
      241 vkltlntdiq yfaqqaiqsq vnklnaewgs ivvmdtktgn lvamadtnap dpndpgkvda
      301 kdrgvrsvta ayepgsvekm itaaaviqeg ksspldhftv ppaltidgqt ftdafehgte
      361 ertlagivgw smntgtvmag srltkeqryn wlknfgigeq pdiglpgeat gilatpdkwd
      421 drqqytvlfg qgvsqstlqt vrayqsiand glmlqprlid syinpkgeeq kvpakdsrqv
      481 vsketaqqvr dilesavteg eikdagidgy rvgaktgtse apredglpgf dgytasmvgm
      541 apmdnprfiv qvvvqrpkgn iygitngpvf rsvmsqvlra ynvapstgta ahlpqfvk
//
LOCUS       WP_284979628             364 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284979628
VERSION     WP_284979628.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..364
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39406
     Region          28..364
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mtsttesiqs dtgtdltkql hdpavrgfas dnysgvhpei laalaaangg hqvsygediy
       61 tkrlqeiler efgqgiecfp vfngtganvl slqsllprwg avvcastahi nmdengaper
      121 vggikllqvp tedgkltpel idreawgwgd ehraqplavs itqttelgtc ytpeevraia
      181 dhvhskgmkl hmdgarlana aahlgvplra ftrdagvdil sfggtkngll fgevvvalnp
      241 daaqglkflr kmnmqlaskm rfisaqfial ledglwlrsa ahanamasrl reavekidgv
      301 eptqatesng vfailpegaa drlrksfafy dwdaarrevr wmcsfdttea didafvaaik
      361 rela
//
LOCUS       WP_284979844             353 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284979844
VERSION     WP_284979844.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..353
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=38151
     Region          47..349
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 msdwilyvil aggvafavss wwgvrrlrar hvrsavreds hkpnpggqrv avilnpvknn
       61 ahvarhsite acdlagwdpp rffettredp gygqsrqala ygadvvvacg gdgtvrvvae
      121 slahknvamg lvpvgtgnll arnldldvtd lsgciqtalf ghqrfidtat mgisnnitgk
      181 ssshtflvia gmgldaevlg dtkedlkksv gwlayteagv rhlpgrrkrv titmddeteq
      241 prkirsvlfa ncglipggid fipqamiddg mldivvmspr safgwlamyv kilfkhnanl
      301 pmmsfyrsgk vtirsqepma tqldgdpsge atevtvqvep gsllvrvprt att
//
LOCUS       WP_284979877             311 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284979877
VERSION     WP_284979877.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..311
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32296
     Region          1..298
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(29,243,246)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(179,214,241,244..245,248)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mltvigealv dvvqsssgie ahvggsplnv avglarldhp vqfigrygrd pygdsvaahl
       61 rsssvmvplp pddkptsiat aridddgaat ynfdltwelp glgarlplml qgatllhtgs
      121 iatalepgaa evlaavehah psstisfdpn crptiitdve yarnqterfv vladvvkasd
      181 edlqwlypgv dplesarrwl tlggsagpal vvvtrgaegp wgvtrageag itapavdvvd
      241 tvgagdsfma gllsalvdrg ldgaqnretl rgmpaetlaa imehaaraaa itvsraganp
      301 ptraelndwm s
//
LOCUS       WP_284979953             443 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Arthrobacter sp. fls2-241-R2A-200].
ACCESSION   WP_284979953
VERSION     WP_284979953.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..443
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46115
     Region          5..437
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 mnpvllfilg vvfvalgvai sialhevghl vpaklfkvrv tkymigfgpt iwstkrgete
       61 ygfkalplgg yvamigmypp nkddggvrps stgmfqtlat earsmaheev gpadearvfy
      121 klpvwkkiii mlggpamnml iglvllavll mgfgvatatt tiadvskcqv aagktvdpns
      181 sdckltpaaa aglqpndtik sfdgrpvtsw deltgwiras agkavaitve rngsevttsv
      241 tpvlssrpvv gadgrqeqdp sgalkyqevg flgigaqsal vpqpassvlp magqniaqis
      301 gvifnlparv vgvakaafsa eprdpngpis vvgvgrvage vaameqvplq arigtlvgll
      361 aglnfalaif nlvpllpldg ghvagalyeg arrrvakwrg kpdpgafdia kllpatyvva
      421 allmamsall iyadivkpvn ifg
//
LOCUS       WP_284979985             266 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284979985
VERSION     WP_284979985.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..266
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28866
     Region          10..264
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mvlpksephp davvllhaat vlglqlsriv lslegrhrla gefmlqamdg rlgvaemesr
       61 ladfevpaqn fllasltved ggrladvhie lwrhgvasas lkrnnrlhva vsadvaddll
      121 vhcagvaasi gisapsavan iqralqeslw algsarankv glahyaqgps wlgltgfeeg
      181 talvrrllgp ifdyeqsqdg dliltlrtyl nsqrswqkta aalfahrqti iyrmrkigel
      241 tgldmgetst vaqlwfalqi heamhq
//
LOCUS       WP_284980003             407 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Arthrobacter sp. fls2-241-R2A-200].
ACCESSION   WP_284980003
VERSION     WP_284980003.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..407
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=43133
     Region          146..386
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mqgnelvtil awvllwavvi gagalallra lgrasvltqi clvvlatvav lvagmvsafn
       61 amfisardle vmwyilgmas avavclslml gagvsrnaak lveparrlgr getldsgved
      121 rrrpvpamts elaelatele assrnlaesr kreaametar relmswishd lrtplasvra
      181 mtealedgma tdvpgyyrki igqteqmtam vndllelski qagslllrae aldlydlvsd
      241 aisdltplaa qrgirldggg nrecmavadg pslaravrnv lhnailyskp dtdvhvsvgs
      301 ddgnavvsvq dhcggipaed lphlfetgwq kdssrsssdp lqgryngagi glsmvagivk
      361 ahggavavqn vdggcrfvls lpttpptrna rhleppttar ealheqa
//
LOCUS       WP_284980033             303 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284980033
VERSION     WP_284980033.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..303
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31596
     Region          12..298
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mnqtgrpqdf pmtnpradrv rdvaklagrp arlkrgrfla egpqavreal tlhrertarg
       61 gpgvvhevfa saacldrlpe ladlaegtll rlatdevlaa madtvnpqgi vavcsfvdvs
      121 ldsvldagpr liavmcqvrd pgnagtvlra adaagadavv ltgssvdiyn pkavrstags
      181 lfhlpvvlga dvedvvarck glgigilaad gygtldldrl qdenaarrlg qasvespyal
      241 erptawlfgn eaqglseael aladhrvavp vygaaeslnv gtaatvclya sarsqqgarv
      301 pnm
//
LOCUS       WP_284980055             742 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Arthrobacter sp. fls2-241-R2A-200].
ACCESSION   WP_284980055
VERSION     WP_284980055.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 742)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..742
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=80775
     Region          3..742
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mhdadlvheq eyvaglyarl delreekraq laqvrragav gtmqnvserd afaalyedrl
       61 aqldavddrl vfgrldldsg eeqyigrigl ttadlqrlmv dwrapeaghf yqatafdrqg
      121 vrrrrhlilq grevkaiedd vldaglladn eslqgegall aalnskrtgr msdivgtiqs
      181 eqdriirssi sgalvvqggp gtgktavalh raayllythr drlksagvll vgpsssfmhy
      241 iervlpslge tgvvmaslgr lmpgihavpe edsnvaalkg kldmakvvan avanrqrtpa
      301 qdlvlevdsr kltlsvrqvr rarekaratg kphnearltf vkillrelte qltdlveesn
      361 ignnadrayl aedvrsardv rialnlcwmp mtpeklisel fskpaileac tphltpeqra
      421 llqrpadapw teadvpllde aaellgeldp aagrglaqqe adrardlana kqtlanmesm
      481 gvdvlvtaee ladqnqeret rltaaerats drswafghii vdeaqelspm qwrllvrrcp
      541 lksftivgdi aqtsaaagan swksalapsf ggrwsleelt vnyrtpsqia eaavrmanra
      601 glvvsapkav regkwspivd rvdadgivpr llevlpeeit aldggllavi adgpllpqaa
      661 aalrkvygrr vgggagsyeq divvmspkea kglefdgvvv lepaamlnhe hgkvgdlyva
      721 mtratqrlrl iaaaplpagi er
//
LOCUS       WP_284980075             611 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Arthrobacter sp. fls2-241-R2A-200].
ACCESSION   WP_284980075
VERSION     WP_284980075.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 611)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 611)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12021846
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..611
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=66728
     Region          26..389
                     /region_name="FAD_binding_3"
                     /note="FAD binding domain; pfam01494"
                     /db_xref="CDD:396193"
ORIGIN      
        1 mssnftdivg aadlrdread pdtaydtdvv ivgtgptggt aalalasygv rtmmvsqwsw
       61 lantprahit nqravevlrd lgveeeaqry avpweqmgdt lfttslagpe iarlqtwgtg
      121 darsgeyvqa spctmldipq tymepllvkn aaergakvsf stkylghaqd ehgvtvrlln
      181 rnsgqeysvr aryligadga kskiaeeigl eivghtarag tayvrfhadl sryvehrpsi
      241 lhwimnpsaa fgeigmgllr cvrpwnewia gwgfdkdage pdlsidtvta qirtlvgdps
      301 leleiegvst wyvnqqhals mskgrvfcgg dathrhppss glgsntcmqd afnlawklaf
      361 aikgyagpal letystervp vgaqivaran qsrldyaplr dcfntdagdg trtveaglar
      421 lrattaegae lrerlskale lknyefnahg velnqryasa avvpdgtpee kferdpqlhv
      481 qsttrpgakl phawlvdasg rrvstldvtg hgkfslvtgl sgqawkqaae rlnlpflrtv
      541 vvgesgyedp yaywaktret eeagallvrp dgyvawrqls svweadeaea qlrealesil
      601 atslrhpvpa r
//
LOCUS       WP_284980170             518 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Arthrobacter sp. fls2-241-R2A-200].
ACCESSION   WP_284980170
VERSION     WP_284980170.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 518)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..518
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=56340
     Region          <9..513
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mseetaysad dprlgllleg ivrlaagdle trievsaard eidavimgtn llaedlqiiy
       61 eeleqrvear tqqlndarla mqhmamtdpl tglsnrsafs aalaeaqaas letstkpail
      121 lldmdgfkai ndslghtigd kvletvarri sgavreqdmv armggdefav llpdvspama
      181 asvgnrilaa ldglieiegh hlrcgasmgl rmadpgvsad dlmmevdiam yeskadgrgk
      241 lkafepsmlh vrqmrnqlva elkeaiagsq lvlyyqpiir ldtreiegve alvrwnhptr
      301 givmpdefip iaeetgmisq lggwvlraav eqlklwrsdp ltsshnfsmr invsapdlqr
      361 lefveevrea lsasgldpaa lvleltesav iqgnaldryt lsslqrlgvg leiddfgtgy
      421 ssisylrqlp vdavkvdrtl laalgsdpsq pallaavlql iracglnavw egieteeqad
      481 yllsigctsg qgyyfsrplp eaemteqlkl hkswpies
//
LOCUS       WP_284980257             181 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Arthrobacter sp. fls2-241-R2A-200].
ACCESSION   WP_284980257
VERSION     WP_284980257.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..181
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20743
     Region          25..163
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mhlllrtlml lftsskrsal gvwepsslel rvlptdidia mhvnngmyfs lmdlgrfdlm
       61 vrsgiwrrmr rrgwtpvaag etiafrkslq lwqkysietr iigldtkaiy feqrmvvege
      121 iyarahiatr lvskgkpvtq eeiiqefgap psdlelpawi hewrgnnalp garrsaphdw
      181 n
//
LOCUS       WP_284980265             177 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284980265
VERSION     WP_284980265.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..177
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19431
     Region          4..109
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mplrsdwsar scslargldv lgdpwgslvl reiffgngrf daikerleva dnvlskrlaw
       61 lldagllaqr pyrdgartrq eyvltpkgqd alpvlnaiii waekhldapn evshmkviht
      121 dcgrpttsad tcshcgthlt aantswhsfk rsdqpvplai appetrreta lgteipa
//
LOCUS       WP_284980279             315 aa            linear   BCT 25-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284980279
VERSION     WP_284980279.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..315
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34481
     Region          7..282
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mtvitetkle faklgsriga eirgldisgd lsadtvsqir aalnehkalv freaniltde
       61 aqvkfashfg pltkahptva svdgeenvlp vdsengsann whtdvtfvvn ppqastlrsi
      121 dlpayggetl iassagayrd lpeelrnfad tlwaihtndy dysvpknleh anaeerrkef
      181 trlkfetahp vvrvhpltge rglfiggfaq rlrivglsnt esrdiirllq ayvtrpenvv
      241 rvnwepnqvv lfdnritqhy apdnydgqpr klnrvtiagd ipvsihgkps qalqgdssty
      301 svvapvdsva apaal
//
LOCUS       WP_284980345             749 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-glucosidase [Arthrobacter sp. fls2-241-R2A-200].
ACCESSION   WP_284980345
VERSION     WP_284980345.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 749)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 749)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 749)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 749)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12807938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..749
                     /product="beta-glucosidase"
                     /EC_number="3.2.1.21"
                     /GO_function="GO:0008422 - beta-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0030245 - cellulose catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=79946
     Region          9..>324
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          65..652
                     /region_name="PRK15098"
                     /note="beta-glucosidase BglX"
                     /db_xref="CDD:185053"
ORIGIN      
        1 mkyvdvtmlt leekaslltg agfwtttaip aqnigsvtfa dgphgvrhqk qgmdhlglyn
       61 sepatcfppa vavgsswsve vaarigaala rearalgvdv llgpgvnikr splggrnfey
      121 ysedpllsgv lasayvnalq eqgvgaslkh faandqeter mvisadvder tlreihlsaf
      181 ervvteakpa tvmcsynkin gvhasenkwl ltdvlrtewg ytgavisdwg avrtrpaaaa
      241 agldlampgp geyatqslie avksgaveea tidaavgrvl gltaftgtdp atadlgahhd
      301 larelaaeca vllknkdmvl plkaqssllv vgefaqtpry qgggsshvna tqvdiplqql
      361 vgrarangtt vhycpgfsle padedslrea avaaaratdi avifagnpee eesegfdrrr
      421 ldlppaqvql ikavaaaapr tivvlanggv vsleewhddv dailegfllg qgggkaitdl
      481 lfgdispsgr laetipyrlk dtptflsfpg eqehvryseg vmvgyryyet vdqpvrypfg
      541 hglsytnfev sdlraeaagp dtisatvtvt ntgevaakhv vqmyvstaag pvqrpertla
      601 aftkillqag etrsvqltld rralrywdit rsdwvvpagn ytiqvaenas evllqqdvql
      661 dgdelpvtls lqsdvaewvs hpvagpalrd rlnqimaans qhldddsdgt kmmlsmpmnq
      721 ilsilggaid gdwllsmlne psqpaaata
//
LOCUS       WP_284980362             457 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Arthrobacter sp. fls2-241-R2A-200].
ACCESSION   WP_284980362
VERSION     WP_284980362.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 457)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..457
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=48930
     Region          41..395
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mraqdvrldd tviaelrqra kdlesystlw sggpaidaag saalsslver lanmypygda
       61 kyigqllkpp hpvawvaqai talinpnnha mdggpatavl ekevvaklaa mfgyeehlgh
      121 ltssgtianl ealwvarelh pgkvilsgtn ahythermcr llgtphetip eddlgrlsma
      181 dlrtrlaqgg vgtvvvtlgt tglgaldqvh eaadlaaefg arlhidaayg gfhallatgp
      241 eplvdpapfl airradsivv dphkhglqpy gcgsvlfadp svgklyshns pytyftssdl
      301 hlgeislecs ragasaaafw ttvealglsr egmgsiiadg rkaalqiadi iraadgaelv
      361 vepeldivca fprrpttgqi saatedtfaa maqdgwhlal yrvdskwlak nhpwvvvdsd
      421 yttvlrscam kpehlqlake fshrliasmd qqpsrks
//
LOCUS       WP_284980430              87 aa            linear   BCT 25-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Arthrobacter sp.
            fls2-241-R2A-200].
ACCESSION   WP_284980430
VERSION     WP_284980430.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-200
  ORGANISM  Arthrobacter sp. fls2-241-R2A-200
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 87)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Arthrobacter sp. fls2-241-R2A-200"
                     /db_xref="taxon:3040281"
     Protein         1..87
                     /product="type II toxin-antitoxin system RelE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0017148 - negative regulation of
                     translation [Evidence IEA]"
                     /calculated_mol_wt=9839
     Region          2..86
                     /region_name="RelE"
                     /note="mRNA-degrading endonuclease RelE, toxin component
                     of the RelBE toxin-antitoxin system [Defense mechanisms];
                     COG2026"
                     /db_xref="CDD:441629"
ORIGIN      
        1 msyavqvdqa alrqlrkldp qarqrvgaai ellsenprpp gakklvggdr ewrvrtgdyr
       61 viyeihdnvl tvlvvsvgnr rdiykkr
//
LOCUS       WP_284980544             455 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284980544
VERSION     WP_284980544.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..455
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=46858
     Region          220..446
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mrrwfgtlag rttaviaava tvavvlagll aaqlvnatav deakkylave adslskqssl
       61 gslqdlradl lthgarlaqi gtdgrvtggg arlvdaktva dvlagksvst svngpqntvv
      121 learplaagg gvvlaqpvse iraaaaplls rmlialavcl vfaivaggll aqwlsrplvr
      181 tahsahrlaa gersvavapg gpaevvevsq alaaldaalr tsegrqrefl lsisheirtp
      241 ltalrgyaea ladgvvsgdd vsgvgqtlva etnrldrfvr dllelarles ddfrvelqpv
      301 daslilhesw qawqavcvqn giagrlelps gplpvrsdgq rlrqvvdgll enalrvtteg
      361 spvvlaayps gsgltvevrd ggpglteada avafergalf arysgqrpvg sglglsiaar
      421 ivqrmggris vraapeggaa fvvelpgipa gsrqt
//
LOCUS       WP_284980559             267 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284980559
VERSION     WP_284980559.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..267
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27823
     Region          21..252
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mstssvssgn hdggpldgge lrrrlaagev tvgtfvgmas atavevcaaa gadwvlidle
       61 hgsggedavr dgvlaagsyg vptlvrvesa eririgrvld qgaagimvpr lnsveeasqt
      121 vkhmlyppyg drgvatynrs crwgmdkapl sadqqltvgi iqietldale hveeiaaqdg
      181 vdvlfvgpmd msfalgvpmq ldssafqdal qrvvaaaqlh nkaagilavd gmaaakyvrq
      241 gfrfvaigsd stimaaafrd afdtarn
//
LOCUS       WP_284980565             289 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. efr-133-TYG-118].
ACCESSION   WP_284980565
VERSION     WP_284980565.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..289
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31618
     Region          23..278
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtypstpeli atcwtsagni aplntpeisp vpigerleai astgwagfgl ayddlvaard
       61 aigfsglknl idqagfryve velltnwwdd slshewrpqf ellldaaeil garfikigta
      121 fseplddldf lveplrrlat easkrgtria lepmpfsmvg smpaaaeltr svdmpecglv
      181 vdywhvfrag tsleelsrsv tadqifgvel ndadaeikgt lfedtrdnrr lcgegdqdvt
      241 gfiktlqaig fkgpwgveil seqhrtrpir ealesarsta lacfppsvp
//
LOCUS       WP_284980579             448 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284980579
VERSION     WP_284980579.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..448
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=47977
     Region          24..329
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mgfsrqqkts vamaafgrsr dpvidlarff clilvvlshc mmvspvlhpd gtvttentlm
       61 eqhwfepvlw vfqvmplffv lggitglesw rrlrarggtg vdyaqlrllr lirpatalla
      121 smfvglwaat llgvdpevvq liatgagmpl wflaaylasq lsvpllarlh ghspwltlgg
      181 lvaavitlds lrgafpmlaf vnmlfvwcav qqfgffiadg ifagrsrgwf aglivgsnll
      241 lgfvtgigvy sgnmivdlnp pnfcmlllgl sqaatlqllr pglawaagvr wirwvvavag
      301 rrsmtvylwh lpllaamsgl llltdfpkpa agtaewwwar plvllgvlvl llpvlllcgr
      361 leerptaash arcrthvavv tagvvvfipv vdaafngltl tllgggaacf algvlllgrv
      421 pagvlsaavp dppvgplpep glranlds
//
LOCUS       WP_284980799             538 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284980799
VERSION     WP_284980799.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..538
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57545
     Region          <1..>160
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mslsvrifgl nswsillpqa lmgvlsvyll yrmvtkrtdp atgllaglff avtpvatvmf
       61 rynnpdallt llmigaafat lesidqgklr wllvagalvg agfltkqlqv alilpaiala
      121 yvvfarlpvy rrlvhlgtgl iaavvasgww fiiaqtadpa rrpfiggsrs nniweltlgy
      181 ngldrltged ashtlsspsa dlyqkldpgi trflqpqfsa qfawflplai agvgitiwfv
      241 irrhgtsqqr sflvlcaawf vcsatvlamm tgivhpyyai stvpslscla altathlarr
      301 lasglvrlas glvlatclil gfitvsrsvs efpwvppvll aagslavaia llppvkrqrq
      361 tvpvlligas illgptiwsv ntvlsphvga gvvagpstlg irsdhpdrtq lppgtpptft
      421 avmfgdvpsp kvleritasp psvrwaaavv gsetaanyql dssrailavg gfdgtdpfpt
      481 leqfqtmarq gsvglfviqn lppltvegrg esarivqwve nnfqpemidg asiyrltq
//
LOCUS       WP_284980868             201 aa            linear   BCT 25-DEC-2024
DEFINITION  YdeI/OmpD-associated family protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284980868
VERSION     WP_284980868.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Pilonieta,M.C., Erickson,K.D., Ernst,R.K. and Detweiler,C.S.
  TITLE     A protein important for antimicrobial peptide resistance,
            YdeI/OmdA, is in the periplasm and interacts with OmpD/NmpC
  JOURNAL   J Bacteriol 191 (23), 7243-7252 (2009)
   PUBMED   19767429
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..201
                     /product="YdeI/OmpD-associated family protein"
                     /calculated_mol_wt=22127
     Region          1..191
                     /region_name="YdeI"
                     /note="Uncharacterized conserved protein YdeI,
                     YjbR/CyaY-like superfamily, DUF1801 family [Function
                     unknown]; COG4430"
                     /db_xref="CDD:443542"
ORIGIN      
        1 maveleeliv kdaaewrswl emngadspgv wlvlhkkggn vteldyaaal dealcfgwid
       61 gqgrrrddes vfqrmtrrgp kspwskrnvg hvarleaegk mtpagwaavd sakadgrwes
      121 ayvgqadaev pedlaaaiaa vpeaqamfdv ltsvnryali yrtnsvkkpe trarkiagfv
      181 emlarqetpy pqkkkpapea e
//
LOCUS       WP_284980878             290 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. efr-133-TYG-118].
ACCESSION   WP_284980878
VERSION     WP_284980878.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..290
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31315
     Region          17..271
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 msnfsrlsdf srlslnrlsl ntattkkwtl aqavdgcvra gipaigpwrd ivadtgldka
       61 aklikdaglr vsslcrggfl taadaegqaa aladnraail eavtldtqel flvvggltpg
      121 ekdvvaarqr vadrledlvp favehgvrlv leplhpmyaa dralistlrq aldlaapyda
      181 ravgvavdtf hvwwdpeleq qiaragresr iasyqvcdfn lpiaadalls rgmmgdgvid
      241 fatigtwvrd agytgdieve ifnqdiwdad gdsvletmkq ryaelvlpya
//
LOCUS       WP_284980913             298 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284980913
VERSION     WP_284980913.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 298)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..298
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32181
     Region          19..291
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtqtsissaa alaemlaatg yladdglati gylalsmerp lllegepgtg ktslaealae
       61 gfglplirlq cyegidasqa lydwdftaqi lhlrsveasg gagmgaglsv aelesslydk
      121 rfllarpilk alqqspavll ideidradde feafllevls tyqvsipefg tvkadtppiv
      181 vltsnrtrdl hdalkrrcly hwidhpglar eveivrtrlp qvpallaeqv vrvvqqirst
      241 ddvlkppgva etldwaralh qlgrseldla saaasigalc kyredtervs aalsrmlg
//
LOCUS       WP_284980969             602 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284980969
VERSION     WP_284980969.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 602)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..602
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=63330
     Region          12..475
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          535..600
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(557,566..568,575)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            567
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 msanpaqpis spltkvlian rgeiavriir aardegiasv avyadpdrda lhvrladeay
       61 alggntaaes ylvmdkliev akqsgadaih pgygflaena efaakvidag itwigpspda
      121 isalgdkvqa rhiaekvgap lvpgtadpve sadeilafaq efglpiaika ayggggrgik
      181 vartieeipe lfesavreai aafgrgecfi erfldsprhv etqcladayg nvvvvstrdc
      241 slqrrnqklv eeapapflsp eqnerlyess kailkeagyl gagtceflvg qdgiisflev
      301 ntrlqvehcv seevtgldlv reqfriarge klgygdpevr ghsfefritg edpgrnfmpa
      361 pgtvstlknp tgpgvridsg ieqgdvisgn fdsmlskliv tgasreqalq rsrraleemv
      421 vegiptvipf dlavvtdpaf apaegpfkvh trwietefvn nipawtptgt gteaadager
      481 qrvvvevggk rlevvlpatl gsvssvasts tkgakvkkrs rsagataava ggnaltspmq
      541 gtivkvavaa gdvvaegdli vvleamkmeq pltahkagti hglvakaget vsagaviati
      601 ed
//
LOCUS       WP_284980976              85 aa            linear   BCT 25-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284980976
VERSION     WP_284980976.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..85
                     /product="type II toxin-antitoxin system RelE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0017148 - negative regulation of
                     translation [Evidence IEA]"
                     /calculated_mol_wt=9672
     Region          2..84
                     /region_name="RelE"
                     /note="mRNA-degrading endonuclease RelE, toxin component
                     of the RelBE toxin-antitoxin system [Defense mechanisms];
                     COG2026"
                     /db_xref="CDD:441629"
ORIGIN      
        1 msynitvlpa alrqlrklpp egrrrvqaai ellaetpqpp gakklagrve wrvrtgdyrv
       61 lyriddgrlv ivvvqaghrr eiyre
//
LOCUS       WP_284980996             812 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284980996
VERSION     WP_284980996.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..812
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=79643
     Region          <72..810
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 msiqprhhmp raaswlrtrt pwvligillv sgigsaayaf wqsisssnfa satgdavmpg
       61 nkpsvsatga disvnwtpgt taggravtgy tvarynaatg gsktpatgac agtvtvisca
      121 eqnvpggiwf ytvtpviglw tgaesarsda vssdstppva svasispspn asgfnnsspv
      181 ivnltaqdnt ggsgvasity avdsgspttv saanaavtvs gdgthvvtyf atdnagnasa
      241 pqnlaikidt vapgapsiiv ptyvnsanva avpingtaep gstltltitd pgaahtlart
      301 vtvngsgawt atgldltsln qgtvtyaaka tdaagntgst vtvtsikdtl apavptisap
      361 lyvnstnvan vpvsgtaeag savtlvvtda gaadsvtqta tangtgawst tglnlsalnq
      421 gavtytatat daagntgasv avaktkdtls atptvtvpty vnsanagnvp asgtsdagas
      481 vtltvtdags ahtvsqtvta tgsgtwsvtg lnlstftdgs isysatatda agnvsatktt
      541 tntkdtvsat pvvsapayvn ganvasvpvs gtsdagasvs ltvtdagtpv htvtqtvtan
      601 gsgtwsfngl nlgtlnpgai sysataadpa gnvsaagtas stkdvvaptv tgvaltnggt
      661 lgtadvldsv titysermda tkfctawnnt gtqilnsnnd vvvtlqdnga ndtltvssaa
      721 cpslnigtvs lggnyissat atfkgtqgnk stvqwdpltl kltivlgsyk tgtlasnvva
      781 gtpsytplsg lsdlaanpls ttpftspgts rf
//
LOCUS       WP_284981020             906 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284981020
VERSION     WP_284981020.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 906)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 906)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 906)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 906)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13203558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..906
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..906
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=98444
     Region          <91..887
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          <793..900
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
     Region          848..900
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mratpesete rhaterqalg aaerrkwssl vrqdlqntvi ealgdpslyg vvvvgapgvg
       61 katfarsvea rltprthvlh lhgstdvttp fgalahlvar lpadaanspg aiiygishli
      121 nsdaagrevl lvlselpald smstallvhl lisgtakvlv tvrqatdmpe dlvrllkdgl
      181 leevqlqvfs raevakllng vlgkrvtata asalhassgg nplvlqaivt eqlrsgnlhl
      241 agqvwamkge ihlssaevlt dlvrsrlare spavqealel lalirtapla vlldvlepev
      301 vaemewsgyl riepsgarrv alrdeymgev irgwmdlprr nelrrlaagv igsitwdlda
      361 eallgfasst lnvretlepg valaaataan rqfdpwfale carqigredk ewvaaaqqrc
      421 vshvilaehe aavaalkdvt peqlrrlpay dytdyvqelc sallwipggh lqipgliaea
      481 gedlsrrsqe igadateier acgmlrlasf elqvhqgeya evaealeqey rdgndlqqrl
      541 scgslltmaw avlgremeai elarelkhki qrakarprlh nwlseglfaa llcsgqweel
      601 armltatldq qpknihylgg aaelalgvsy tyagrasvai dtllgaqaql eirrnyygpa
      661 laysalafay aqagdvkesr tflelaekgq getawfpawm aefcvkmarr wlkdpgakqs
      721 liesanrdla kgrittasis lfgatvhgte eelllleqvs srrqgkmaav nrmvaegtrk
      781 kdpktlllaa svaqelklda vesrcavlal diareagdsg sarlaqqrld rlvgtvpvlp
      841 ltphtfgpel tererqvakm asqglsnkev anqlqvsvrt veghlyqift kmgissrsel
      901 egtaqs
//
LOCUS       WP_284981084             245 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsB family cell division protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284981084
VERSION     WP_284981084.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..245
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=25346
     Region          124..204
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 matrrpkvpr adalgrspqk npdgghvira dfgesrkasa gqqesqvhag srtssntrae
       61 ggtqskgqsg skagsaakpg gslpgrpgna pvagkasnkt pgagsahldk drstrpvpak
      121 afsgrmlala vvmiaitiml aptvkiwlek kaeisglead iaskqaeqas lqkqitrwqd
      181 pnyvkqqard rinmvmpgea gywvfggdvp agtpggstss gasgspsnlp wvdglwesir
      241 rsatd
//
LOCUS       WP_284981161             435 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284981161
VERSION     WP_284981161.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44168
     Region          33..381
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(43..44,47..48,51,85,135..136,138..140,143,163,
                     166..167,170,247,250..251,254..256,259,286,290,339..340,
                     344,348,364,367..368,371..372,375)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mnhtpsaaap ertqrhhspe asarfskrsa aavlvcwllv vfdgydlivy gtvqsslitn
       61 tgwgltkata gtvgsmaflg mmigaifagr msdswgrrrt iiacaalfsl ftilcafspn
      121 afvfgglrll agiglgglvp sanalvaelv pakwrstiat lmmsgvpigg siaalagipl
      181 ipvfgwpvmf lvaavallvv vplgmrflpe tlpetlppae kakqtvgfks llrspylgms
      241 llfaistlvt lfawyglgtw lpnlmqlagy nlgsaltfal alnlgavvgs vatawagtrf
      301 gpiptaiaaa avaavalavl vagppvglvy vmlvlagvgt hgtqcliiaa vashypahlr
      361 gtalgwalgv grigavaapq vgglllaagl gvnsnflafa gaaavaaill gaigtkikta
      421 kiqsksttsl gasnv
//
LOCUS       WP_284981210             328 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Arthrobacter
            sp. efr-133-TYG-118].
ACCESSION   WP_284981210
VERSION     WP_284981210.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..328
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=35458
     Region          2..313
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkviviggsg higsflvprl vraghevini srgthksyge apewqqvrqv vadrqqedrd
       61 gtfgdrvaal qadvvvdlvc ftfesasllv nrlrgeaghl lhcgsvwryg qslklpiaeg
      121 sgsaaapfge ygiqknriar mlkeetddgg lvttsvhpgh ivgpgwhpig plgnldpavw
      181 ytlsageplq ipgsgaelmh hvhaddvaqa fekaiqnrda aagedfniva ptaltvrgya
      241 diaagwfgqs atletvtweh frasttpeya esswghlyrs hcftiekaks llgyapryep
      301 eqavlesiiw liergqlrga nplsvlan
//
LOCUS       WP_284981280             345 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. efr-133-TYG-118].
ACCESSION   WP_284981280
VERSION     WP_284981280.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..345
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37936
     Region          34..305
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 maytaetwpi taallqfpgt datgqhinda dasswaevlq evkdagfana dltdswvrpg
       61 dlskerlaef kqtaehvgig ipvisairrs vihardwaen layshrtida aaelgcevvs
      121 fglhqaitae qqkqlwfwtv egykdpvgdk dawgnavtrl relgehaaea gillslemye
      181 dtylgtadss vqlvqdigla nvglnpdlgn lirlhrpied wremvaktlp ysnywhmkny
      241 irdedvards yitmpapmes glinyreafk lalsvgfqgi lctehyggdg lsvtasnqey
      301 lrrqvlpkte nyvlgqsqva qgrqqpsgrt esgstqpvas qlagv
//
LOCUS       WP_284981296             555 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284981296
VERSION     WP_284981296.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..555
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=61032
     Region          165..555
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mkrpfewdak ngrvmffqha fheyslkdrv alsqlpltvt vcltavlvai yfpatlgnpl
       61 fviflatqaa awvlcyavpw drlpfptfla iplldvvsig lgreggqdsp igislltvfp
      121 viwlcasgly rrsalvvsfl gplamiwmpq flhgtytpqd llrglllpim mlgigvsisv
      181 mtqsmvvqqk rleerdaall raledsqqke rllntvletv hlgvvaidad gremmanrkq
      241 renqvleasg dsdrhgepql lvfdadrvtp tepdrrpmrr aalrqeftdy lvwvgtgreq
      301 rafttsarsm kdsdgnylgs vlvfgdvtal vdalaakddf vsnvshefrt pltsitgyvd
      361 lvleeaenlp twvvqqleiv qrnadrllsl vsdllavrsg hlivqphavd vselvkssva
      421 sakpkandgr vrlhidaper leahvdanri sqvldnlisn aikyspdggd vrvtllreen
      481 alvchikdtg mgmdkqdqad aftryfragn vrntaiqgvg lglsickaiv dahggtigle
      541 svpgqgttft frvpa
//
LOCUS       WP_284981359             222 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284981359
VERSION     WP_284981359.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..222
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=24133
     Region          3..215
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 meafdvirwt trglisstcr ptviglenvp kegpfivapn hlsfldsviv qalmprpvgf
       61 fakaeyfttk gfkgramkaf fqavgsipve rgeqaasvqa lktlldilen grgigiypeg
      121 trsrdgllyr grtgvgwlal ttgapvvpvg ligtdqlqpv drntvrpqhf tmkvgeplyf
      181 ektgpdhslp arrevtdkim daiavlsgqe rstsynqsks ae
//
LOCUS       WP_284981345             263 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284981345
VERSION     WP_284981345.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..263
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27814
     Region          19..241
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mparhsavvp vpggaavgva daedrtrdrv lnavlehgpv saaelgdmlg ftpaavrrhl
       61 dhlqragvie vkrvakagag agrparryvl ssqgqsklgd dylniassal rrlrdlagee
      121 avrdyaverf aemeqryape vdragsdiaa ravalskals rdgyvasaas ietksplpas
      181 lssvqlcqgh cpiqqlaaef pvfcdtetel fsrlvgvdvr rlstlaqggh vctthiptgr
      241 paakealgfp klratphves nnq
//
LOCUS       WP_284981520             448 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Arthrobacter
            sp. efr-133-TYG-118].
ACCESSION   WP_284981520
VERSION     WP_284981520.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468626
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..448
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=51074
     Region          12..416
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
     Region          179..417
                     /region_name="RHO_alpha_C_NDO-like"
                     /note="C-terminal catalytic domain of the oxygenase alpha
                     subunit of naphthalene 1,2-dioxygenase (NDO) and related
                     aromatic ring hydroxylating dioxygenases; cd08881"
                     /db_xref="CDD:176890"
     Site            order(184..191,214..215,340,343..344,349,351,354..355,
                     357..358,361)
                     /site_type="other"
                     /note="beta subunit interface [polypeptide binding]"
                     /db_xref="CDD:176890"
     Site            order(200..201,205,207..208,212,358..360,362..363,
                     365..372,375..381,401,403)
                     /site_type="other"
                     /note="alpha subunit interface [polypeptide binding]"
                     /db_xref="CDD:176890"
     Site            order(201..202,205..206,208..209,213,289,291,301,346,352,
                     356)
                     /site_type="active"
                     /db_xref="CDD:176890"
     Site            order(201..202,205..206,208..209,213,289,291,301,346,352)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:176890"
     Site            order(208,213,356)
                     /site_type="other"
                     /note="Fe binding site [ion binding]"
                     /db_xref="CDD:176890"
ORIGIN      
        1 mvdlnelvds drgrvdpriy tdpgvyerel efvfgrswlf lahdsqlpkt gsfiqtymae
       61 dpvlvvrqrd gsvkaflnqc rhrgmricra dagvsktftc tyhgwaydle gnlinvpled
      121 raykgnldre awgalkvpri anyrgfyfgt wsdetpdfed ylgdmafyfd avadrfdsgl
      181 eftagttkwv idcnwkfaae qfggdmyhts ishasgpial tdqqvvrgdp nlvqgrqfgg
      241 dghgsggyiy pernmppnff rgqqehefte dhldeieari gdtrmkkvnn hntifpnfsw
      301 lgflwtmrvw hprgpnqiev wtwsfvpkda tealkreire kaqrtfspag vfetddgenw
      361 tevqqvlhgf karqntfhvg mglgheerna gglpgvtndv fsevasrgfy rrwhdllvgk
      421 swkqiqkeea arvsaipesq pelaegar
//
LOCUS       WP_284981548             416 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284981548
VERSION     WP_284981548.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..416
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44376
     Region          16..416
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mvsaddssak wnsecrpfeg vrildftqlv agpyatyqfa lmgadvikve rlegeamrsw
       61 dlsntllsge wierglapsw qainagkrsl aldlqrpqav eiakrlasta dvvvenfrpg
      121 vmdklglgya alselnplli ycalsafgqt gperlgagyd gkiqamsgim amsghqstgp
      181 trtgfslcdi vagataalgi ssalfqrtht grgqlvdvsm leatlaflsg piaehtiaeg
      241 qpsqlrgnka avptptadvf etgdgaills vvtdkqfeal mrslgradaa qdarfstepm
      301 rreneaalrr vietalttks arewetvlns agapcasiwk vedvidhqqi vardaiheld
      361 tshgklrlag lgfqlahggg hldrmaptls qhtdevlaea gyapheiaal rtaevi
//
LOCUS       WP_284981576             562 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284981576
VERSION     WP_284981576.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..562
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=60333
     Region          1..537
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtsvspvlsv rdlrvayrta rgelpavrgv tlslrhgeiv avvgesgsgk stlaqaiigl
       61 lapggvvtgg svllgdldls alsepemtki rgkgiglipq dpmlslnplr rvgdqvqeal
      121 lvhgtvpkse saahaiellr eaglrepeir anqyphelsg gmrqrvliai afscrprvvi
      181 adeptsaldv tvqkrildsi gkitqqfgta vlmithdlgv aadradriiv mcrgeiveqg
      241 ktadilsnpq haytqkliaa apgftdddll asdsnradie evpllrvtgl vkqfrvhepg
      301 hkpgsiravd rvsfdlhkgr tvgivgesgs gksttarlim rldtptegii eingqdisrl
      361 rgaglrqmrr hmqlvyqspy gslnprfsvg kvieeplref glgnarwrrn rvtelldlvs
      421 lpasyadhka gelsggqrqr iaiaralaie pelvvcdepv saldvsvqaq ilellvrlqr
      481 elglsyvfis hdlavvrqvc qdvivmqqgv avesgptgiv fddpqhpytk eliaaipgrv
      541 alghdagssl vpsleatmkg ts
//
LOCUS       WP_284981677             431 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284981677
VERSION     WP_284981677.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 431)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..431
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=45683
     Region          91..405
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mngqaedelq rsswrlalqt gallvlllva iagsvllivs tsqasaaqrl lttatehvds
       61 ivdapagtwl aisnqgtltv spgmpsglpd lkaieavaas gvaaqedvsi agrpytvrta
      121 dsgsrvvqav fdrhenleel nrlglalllt cggavvlasl lavwlarram rpmaealdrq
      181 rrfvadashe lrtpltllsm raqmlrrrva sfpaheppgn idaevdamie dsrsltrlle
      241 dllisadsrq veltdvdvva laddvvesfs vsaarrgitv ersgidgpmg itatptalrr
      301 lfvalldnav rfarsrvevg vskdprtlvi tvsddgpgfs dhvkprafer fataapagva
      361 pedgtgprhy glglalvaev aaqhggrvei gtqaagavii vrlpmirgkr gnspaagswl
      421 rafvsrvrrm f
//
LOCUS       WP_284981722             282 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284981722
VERSION     WP_284981722.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..282
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29548
     Region          48..156
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mrrfrltavl aaaaltiglf aapaaqadsi spdppgandw tckpssvhpy pvvlvpgtfe
       61 tmyknwalls pvlkdqgycv falnygvvng vpasgavrds aaelatfvks vlgatgaqkv
      121 dlvghsqggm mpryyigflg gakyvhqlvg iapsnhgtqg liapspagmv ldttatstlc
      181 qacadqhags afmaelnsig dtspgpfytv istrydevvt pyssqalvgp vkqvsnlvlq
      241 dycpldtfeh dqspndpnvw slvsnallqn gpadptyrpe cv
//
LOCUS       WP_284981780             292 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284981780
VERSION     WP_284981780.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..292
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31508
     Region          4..275
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mqipapfdye rasdvanala llerhgpesr iiagghsllp mmklrlarpe wlidindlte
       61 lefirregdq lrvgaltrht allesadvag lfpiirdaeq viadpvvrnr gtiggslcqa
      121 dpaedlstvc dvlraqavir gpdgermvam sdfhrgpyet avaqnellye vrftirprsg
      181 sayekverrv gdwaivaaga avglssdgtv eeaaigltav gldgtvpeae avlrgqqphe
      241 dlfveaaria aaachpvddq rgpvdykrhl adeltrrvlr racaraagaq eg
//
LOCUS       WP_284981879             281 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. efr-133-TYG-118].
ACCESSION   WP_284981879
VERSION     WP_284981879.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..281
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30219
     Region          18..256
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mstpavewel sgfgdeiddd pkiqiavmqa lgarhievrs awgtnivdld darlrelksl
       61 ldaadmkvsa iaspigkvdv slpvehever lrravnaaqv lesryirifs fyygedvave
      121 sirdavierm raladvaeet gvvllhenek diygdiperv ldivetvasp alkvawdaan
      181 fvqvgvkpfd dgyaklrphl eylqvkdalf snatvvpage gdgdvlrtve alkadgytgf
      241 aslephlaga hglggfsgpt afgiaarafa kvlheagvgt k
//
LOCUS       WP_284981911             186 aa            linear   BCT 25-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284981911
VERSION     WP_284981911.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..186
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=17994
     Region          52..169
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mkksnkifav aaagallltg gatavanavt paaaktataa vdvnpsaenv vpqnritvga
       61 ssqavnaala kcqadklpfv tvalvdrfgt vqallrgdna aehtieaakq kaytaaafga
      121 ptselakrin gngpsiadlp gtlflpggvp lkvngvsvag igvggapdga ldeacaaaga
      181 avleak
//
LOCUS       WP_284982041             536 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284982041
VERSION     WP_284982041.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 536)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 536)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 536)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..536
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56901
     Region          27..532
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mttdlsaris peipeasast ttagrgkrpr ppfgvsaisl lavlialfsl iplgyvaymt
       61 aatgwdtava livrprvgel llntvmlvvf tvpiclvlgv ggawlvertk lrghrwwava
      121 laaplaipaf vnsyawvtav pslegiwsgv liatlsyfpl vyipaaatlg rldpaieqsa
      181 aslglgpwai ffrvvlpqlr iamtggallv slhllaeyga famirfdtft taimtqfqst
      241 fngtagnmla svlvffclil llaevrsrgt aryarigsga qakptrlplh hyqipsqlal
      301 laltvlafgl pvffvlrwvv aggarvwsad eflpallqtl aygtvgaaat ivvgfpmayl
      361 avrhpswfsk mlelsnyvts slpgivvgla fvtvsirmvp gvyqtsgvli aayvllflpr
      421 alvnirsgla qapkeldeaa qslgkaplvs flkvtlrlta paaaggaalv flaivnelta
      481 tlllspngth tlatefwsks seidysgaap yallmillsa pmtyllfqqs kkvagq
//
LOCUS       WP_284982126             154 aa            linear   BCT 25-DEC-2024
DEFINITION  SRPBCC family protein [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284982126
VERSION     WP_284982126.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..154
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=16686
     Region          7..146
                     /region_name="SRPBCC_CalC_Aha1-like"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of Micromonospora echinospora CalC, human Aha1, and
                     related proteins; cd07814"
                     /db_xref="CDD:176856"
     Site            order(8,10,12,21..23,25..26,31,41,46,48,50,52,63,65..66,
                     68,71,77,79..80,93..94,96,98,108,110,112,114,124..132,
                     135..137,140)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mseqlttiev eeflphapak vwqaltdpal iarwlmendf kaivghqfqm rgipvpavgf
       61 sglvasevld ldagkrlris wrdansgnnl dstvtwsisp eddgtrlvlv hegfnpaept
      121 hiashcimsg gwrnhvlprl gqtlagldsa gpen
//
LOCUS       WP_284982131             319 aa            linear   BCT 25-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284982131
VERSION     WP_284982131.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..319
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=33429
     Region          3..311
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(8..9,11,51..53,74,102..103,106..107,109..110,113,
                     117,119,127,129,131,133..139,141..145,163..164,167..168,
                     267..268,275,281..287,289..292,294)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(52,75..77,100,238,285,288)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240626"
     Site            order(76..77,104,153..157,175..177,180,208..210,214..215,
                     236..238,262..263,285,287..288)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 msrvvvtgrv pdaaieklra ehevdawtgs esigreellr rvagadavvs llteridael
       61 ldaagprlkv vanvavgydn idvpacterr ivatntpgvl teatadiafg lilmatrrlg
      121 egerliragq pwkwgmffll gsslqsktlg vvgmggigqa tarrakafgm eivyqsrsei
      181 dpaiaaelga rrvdldella vsdvvslhcp ygpathhlig aeqlaamkss aylvntargp
      241 iideaalaaa lsdgviagag ldvferepqv hpalldlenv vlvphlgsat vetrtamaml
      301 aadnalavls geqppapin
//
LOCUS       WP_284982159            1008 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-mannosidase [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284982159
VERSION     WP_284982159.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..1008
                     /product="alpha-mannosidase"
                     /calculated_mol_wt=111390
     Region          250..1008
                     /region_name="MngB"
                     /note="Alpha-mannosidase [Carbohydrate transport and
                     metabolism]; COG0383"
                     /db_xref="CDD:440152"
ORIGIN      
        1 mhddrritek rlerfvreri apaiygralp lelsswdapg epvpvsealr qvfepqehga
       61 awgkawstkw lrlrgevpeg wgvadgttve ivvdlgfsnd apgfqcegia wrhdgtiika
      121 isprnqhvpl kllggglsvd fyveaaanpd lsqgwsfaat plgdkstsgd elryrfgria
      181 iaelnevvwe lhqdiwtlsg lmhelpfelp rrheilrafe rmldvmdpdd vagtagagre
      241 alaevlsrpa yasahellat ghahidsawl wpvretirkc artfsnvval mdenpdfvfs
      301 cssaqqlawm kefypelfir irekvkagqf vpvggmwves dtnmpggeam arqfvegksf
      361 flqefgvdcq eawlpdsfgy sgalpqivks agsrwfltqk iswnqvnkmp hhtfnwegid
      421 gtrlfthfpp vdtynselhg relahaqrny rehgrgtisl vpfgygdggg gptremvaaa
      481 hrtadlegsp kvrmgtaeef fkqaeaeyhn lpvwvgemyl elhrgtytsq antkqgnrrs
      541 ehllreaelw cstaavrtag sftypavdlk rlwrlvllqq fhdilpgsai awvhqdaern
      601 yaaiareleg iiadaasall gegdtiflln aaphersgvp alaaaeavhe dnpvnvtera
      661 ggyvldngii ravldangll tslsdyasgr eaiapgmfgn hlelhrdtpn ewdawdidef
      721 yrrnvvsvve arsvtlerag wdavvvvert vgsstitqri sleagaeslg isttvdwqeh
      781 ekllkigfpl dvradrsase tqfghvfrat htntsweaak fefcahrwih vaepgygvai
      841 snassyghdv trtiredggt ttnvrvsllr apkfpdprad lgvhvldlsi rpgasiggav
      901 eegyrtnlkp rllaganpve plftvfnqal vieavklaed gsgdvivrly eslgerstgl
      961 itanfesrmv qsvdllerpv eapgvtpgag aaeltlrpfq lvtlrfir
//
LOCUS       WP_284982209             373 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284982209
VERSION     WP_284982209.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..373
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39149
     Region          7..371
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 msstpptkhv vvigggilgv stavhllreg asvvlltekg laseasgrsl swlnsagers
       61 tpyhqlrltg vdryrtlfaa dpgrewlqfg gglmwnaage qavtearhay eksvgydskl
      121 ltpeeigfat pginasavpd caifnpgegw vslpdlidfl meefharggq lvlncgkasv
      181 avdggratgv etvagetyqa davlvacgaa tpavvaplgv dipndspvsm lvltkpvdhe
      241 vravmntpra airpnpgntf aldhdwyeeh itehedgsfs ipdgivqela degsrliagn
      301 pelkpaswki gykpipgdge pvlgelgqvp gcyvafthsg atlglivgel lageiltgsk
      361 hpmlstfrpg rfs
//
LOCUS       WP_284982293             165 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284982293
VERSION     WP_284982293.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..165
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=18151
     Region          <2..140
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mravpvaplv pdqpvmlpfa peavqcgfps paqdyfsgdl dlaehlirdr vstyiwraag
       61 dsminagihd gdlllvdrgi tpvaghivia vidaeyavkr ldlvqgrpvl rsenpaypdl
      121 tlhelselti wgvvtwvlhk tdvsrptyas hrddptrssd lhrtr
//
LOCUS       WP_284982494             256 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284982494
VERSION     WP_284982494.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..256
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28180
     Region          169..241
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mslglieelm drawpapdre dtegwvmraa ggvtqransv wpreqardee savraatywy
       61 rarrlplivq vfdderstgl navldaqrft rqsetlimvr pggslpgapr dgwpndveis
      121 depseewlrl wwsvdgrggd teleiarkil vscpsvyalv rdnegapaav grlalvdgkg
      181 giycmataag hrrqgfgrrv lralleaggh rgaaefwllv masntgaqal yegagfaehg
      241 rylyrqarpr ralsgc
//
LOCUS       WP_284982512             289 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284982512
VERSION     WP_284982512.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..289
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29581
     Region          52..277
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mnthrlktig alsaaamtva vsitacggpt sasnasctpk hsgiqtvtpg kltvgvidip
       61 pyssynsgnp tgvdisivsk iakdeclavs feqasyadai qsiggnsidl avgsiavtat
      121 rekvvdfsas iyvesmgvtt rigattvaev ekaggkvgtv egyneiadlk kifgdrlity
      181 pssvelkadf dngrlvasfd aygvsateyk gvdgvtvalg takpdprisa ltrppedgfp
      241 ltkdntslkq alddgitsqh qdgtigkllt gagltdalgn vsktqyvsp
//
LOCUS       WP_284982551             449 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284982551
VERSION     WP_284982551.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 449)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..449
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47552
     Region          1..>70
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Region          39..440
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(150,152,278,280,313..315,360)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrpkiraasl aagalcials asacsgaggs taagdqnsin vlmvnnpqme dlqkltadnf
       61 tketgikvny tvlpendvra kisqefssqa gqydvaslsn yeipfysang wlapldnvak
      121 dasfnqsdil paytasltgk dgklygepfy gessflmyrk difaakglam panptwdqva
      181 dlaakvdgaa qgmkgiclrg qpgwgqvfap lttvvntfgg twfdkdwnak vnapeftaat
      241 qfyvdlvrah geagaaqagf teclnnmsqs ktamwydats aagsleaads pvkgkigyvq
      301 apvketkssg wlwtwswgvq aaskkqdaag kfiswasskk yedlvaaklg wakvpsgkri
      361 styenadfqk aapffqaert aienadpknp gvqprpvvgi qfvgipefad lgttvsqgvs
      421 saiagqgsvs dalakgqdaa qkigdkykk
//
LOCUS       WP_284982577             404 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284982577
VERSION     WP_284982577.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..404
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43993
     Region          87..399
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mqqdvekive dvalklgrgl sledldgvll ayssnqshad rvrvnfllsk rvpvdvsawq
       61 lshgistavr pvvvpaneel gmvgrvcvpl lvrgfrvgyl wvqqdldeqt atailaelpg
      121 vrdeldllag llldsntaes efrrrreqef laacqgesna vaavagwkei qgrgpwqlvt
      181 vldaedsggv sdpiaatlth rsaalqatig vdsvlfsagt ethsvllfre tggravhaqv
      241 lvhyqlelak ragrkvdrvi lgisepfsvi rqlgrayrqs klaaqaaavd pplgelvdsr
      301 sagiyqlfer lqapggwdds isahfqeied adrngellpv lellydsdgs vqdvaaklhl
      361 hrssiynrla rvrqligadp lngatrlelh atlkarrwag rpri
//
LOCUS       WP_284982657             485 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284982657
VERSION     WP_284982657.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..485
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51750
     Region          5..473
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mstrsnpaav tevprledkt iqpiplnerh gkardlftiw fgsnimimti vtgglattvf
       61 glsfvpaivg iilgnviggi fmalhsaqgp qlgvaqmiqt rgqfgsfgal livvivvimy
      121 vgffaanlvf ggeamaavsp disvdagiii igvvsvvati fgyrlihaya rflsivagla
      181 lllafvwiml vhglpatfln qgnfnwvgfm atvsvsalwq layapyvsdy srympqgtgs
      241 gpafwasysg cvlgtlfpmi lgalvgtlav amgadagnve ivgsmgallq pwtlavvgvf
      301 clgvaasnam nlycgvlcsl tigqtfkpnw lpraktrsva aiilftfall islfardnfi
      361 lfytnflsfl myvlvpwtai nlvdyyllrh gdykvedffk rdggvygrfn wvaigsyvag
      421 alvqlpfsat aiytgpvaaa mggvdlswiv glivvaplyy vaarvfrkka eatpfqapvl
      481 asdlv
//
LOCUS       WP_284982796             120 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284982796
VERSION     WP_284982796.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 120)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 120)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..120
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12933
     Region          20..95
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(24..25,27,30,33..34,37..38,41,71,90..91,93..95,
                     97..99)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(25..26,30..32,45..47,56..59,61..62,65..66,68..69,
                     75..77,82..84)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(45,48,90)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mnadnrdcsl gvdsqyvela vevfamlada trvrivlalr ngemavgala elvgkspaav
       61 sqhlakmrla rmvstrqdgt rvmyrleneh arqlvadaif qaehalggtp ahhraeqepa
//
LOCUS       WP_284982798             231 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284982798
VERSION     WP_284982798.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..231
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=25206
     Region          13..229
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mssgwteplf pfelpdapda gpreiapgav hvpgwlglgq qqwiaarfee wtrgpvplra
       61 avlpgghpms vrtvclgwhw qpyrytreaf dvngrrvldf pdwmvrlgrk alfeaygdaa
      121 eaagytpdta lvnfydeaak mgmhqdkdek srapvvslsi gdscvfrfgn tetrtkpytd
      181 velssgdlfv fggasrfayh gitkvlpgta pegcglpggr initmrvtgm s
//
LOCUS       WP_284982809             463 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284982809
VERSION     WP_284982809.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..463
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50073
     Region          5..453
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mlnldrdvvi vgagpsglta arelkkagls vavleardrv ggrtwtdtid gamleiggqw
       61 vspdqtalmg llddlglkmy sryrdgesvy lapdgnrtry tgasfpvset taaemdklta
      121 ildglaaeig peepwahpka reldtisfhh wlrqnstdee acnniglfia ggmltkpaha
      181 fsalqavlma asagsfsnlt dedfildkrv iggmqqvsll iaaelgndvv lnspvrtinw
      241 dpageghrvt veseratvna rfvimavppn lysrvsfnpp lprrqhqmhq hqslglvikv
      301 havystpfwr edglsgtgfg adalvqevyd ntnhgdtrgt lvgfisdeka davfelsaed
      361 rkkkvlesia sflgekalda evyyesdwgs eewtrgayas sydlgglhry gkdqhanvgp
      421 iywsssdlaa egyqhvdgav rmgqaaaari vtannrvtav pva
//
LOCUS       WP_284982893             128 aa            linear   BCT 25-DEC-2024
DEFINITION  HesB/IscA family protein [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284982893
VERSION     WP_284982893.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Lu,H.M., Li,J.D., Zhang,Y.D., Lu,X.L., Xu,C., Huang,Y. and
            Gribskov,M.
  TITLE     The Evolution History of Fe-S Cluster A-Type Assembly Protein
            Reveals Multiple Gene Duplication Events and Essential Protein
            Motifs
  JOURNAL   Genome Biol Evol 12 (3), 160-173 (2020)
   PUBMED   32108236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..128
                     /product="HesB/IscA family protein"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=13571
     Region          24..128
                     /region_name="IscA"
                     /note="Fe-S cluster assembly iron-binding protein IscA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0316"
                     /db_xref="CDD:440085"
ORIGIN      
        1 mstatnenst eaqlaggelp ehevkltdva agkvrslleq egrtdlrlrv avqpggcsgl
       61 iyqlyfderl ldgdavrdyd gvevvvdkms vpylsgasid fedtiskqgf tidnpnaggs
      121 cacgdsfh
//
LOCUS       WP_284982907             937 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284982907
VERSION     WP_284982907.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 937)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 937)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 937)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19601452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..937
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=101894
     Region          <19..868
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          28..221
                     /region_name="ExeA"
                     /note="Type II secretory pathway ATPase component
                     GspA/ExeA/MshM [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG3267"
                     /db_xref="CDD:442498"
     Region          735..914
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          857..910
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mtsrtvvhpa lssddtpaav lkrtrqyrgg ivvltgiqgi gkttwclqfm dalrranvva
       61 csadtfessl plsfvdkllv alghreaepl sdpviaarql lsalasrpkn iscivvdnaq
      121 widersakal rfvlqrladd ritvvlagvs gpgtaaidrm vaddlswgfi krvnmeplsp
      181 eqvqdyvarv wdrtmsarta erlrwstggt pllinaameh aagpeysaqd pwpdalpyia
      241 pgnnpfaaml dalelgpvrs vvefvcvsrd pieqerlqri gfalneptdv aaalasglvr
      301 gtrvgqtvql rpfhdllavg vrdnlkshrl ssihraiage lddprlalqh rllvqepgtv
      361 alytdvtsgv dhaladgqpe lalqylrsam drfhgsrrdd ciieacvvas vhhriaevmd
      421 llpqvqsmrp gvvrdfallq llqmrpdldr vgqfaeelia kelnhpdeal lrahislaiv
      481 vsrmvsedks stavavaqah ryleqlsqsk gavhdprlrh lpsgtdlglq fdgfnligas
      541 gtqdpnlisk afaslsaria dandspalad altcragfls vtggieqatv dleramevsa
      601 stgaglaigh trvvlaycyf llgrvqemlt vvrtaqllsl dvsdvssrpl vfamsavlea
      661 vqgrsesyea alrraeevri seydtfgvel sglaklerar slaewqqqld aseaitlatp
      721 strsyridal aglgraeead rllqackdmn grgwwpvygs ldwlegrvse ayglssraak
      781 fyrlaakepr fplsqgiahl dlgrllismg ntkagaaalr gavriflalg aapylsramk
      841 lldgvsdrpg npylqafesl tgrereiafy aergmtnkqi aaqlfvspat vnfhirnvla
      901 kldlrsrrel gqlfsagleg stpsqartpl rhpltep
//
LOCUS       WP_284982916             117 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284982916
VERSION     WP_284982916.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 117)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..117
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13146
     Region          10..76
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mpeqrrigyr wnlralmakq nlwkttelmp llksrginls esqvyrlvts tperipartf
       61 aalcdildct pndlfepfve mraaatanap krsedlgiqp gnpiakrirl vppedge
//
LOCUS       WP_284982943             335 aa            linear   BCT 25-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284982943
VERSION     WP_284982943.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..335
                     /product="isopenicillin N synthase family dioxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36922
     Region          1..322
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 mtldtlpvid fsrldatpde asrfrdelrd amhevgflyl aghgipqelt daildvsrrf
       61 felpeeekla ienvhspqfr gytrvggelt dggidwreqi digverdave pglgvpeywr
      121 legpnlwpaa lpemreivse wtdrlstisl allralavsl gapedtfdaa faarafpvlk
      181 ivrypgesnp epkqgvgshr dggvltlllv epgkgglqve yqgkwidapq vpgtfvvnig
      241 emlelatngy lkatlhrvis plrgtdrisl pffynpalda tmpqlavspe fqakarglsv
      301 dptnspilet ygdnalryrl rahpnvvaeh hadll
//
LOCUS       WP_284983016             518 aa            linear   BCT 25-DEC-2024
DEFINITION  HNH endonuclease [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284983016
VERSION     WP_284983016.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..518
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54992
     Region          101..388
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          380..431
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mdgnrgtqli gagarsgsag pdvsvpgarl rdlidamnsl raataafela ggnelteltd
       61 yaelidqlra ledlksaaaa aqariavafd aaqrsaekdl gipaeeqgrg vgaqvalarr
      121 espargsrlh glakalvtem phtlaaletg rlnewratll vketaclsae drcavdeela
      181 adtgtfdgag dkaiitaart aayrrdprsv tqravraaee rhvslrpapd tmtyltallp
      241 vaqgvavhaa lsrhadtlrs ggetrtrgqi madtliertt gtpggisgve iqlvmtdrtl
      301 fqgdaeparl pgygivpagw artllaegpg csnepasqla qdqagqdqdl kvwlrrlyta
      361 pgtgdlvaad srarlfqagm rrfiqarddt crtpycdapi rhfdhivpwh qggpttlang
      421 aglceacnyt kelpgwtaqp startstaqt gtgtrhvldi rtptghtyqs tapplpgagi
      481 hgtepsdtap prsrhhrrrl rhqakalkya hltelqaa
//
LOCUS       WP_284983024             121 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284983024
VERSION     WP_284983024.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 121)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 121)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 121)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..121
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13392
     Region          20..95
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(24..25,27,30,33..34,37..38,41,71,90..91,93..95,
                     97..99)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(25..26,30..32,45..47,56..59,61..62,65..66,68..69,
                     75..77,82..84)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(45,48,90)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mdadnavcgr epdsqyvela vevfamlada trvriilalr dgelpvnqla elvhksqasv
       61 sqhlaklrlg rvvttrqagt rvyyrlaneh vrqlvtdaif qaehsldgtp rhhhadvmde
      121 v
//
LOCUS       WP_284983061             512 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284983061
VERSION     WP_284983061.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..512
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=55905
     Region          <8..510
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mtstesvedp rlqqlvdgvv rlaagdldar ikpsehrddi davitgvnll aeelghihse
       61 leqrvaarta mlrrtqvele qmaktdaltg lanrtllter iqeailsctd ggrapavlll
      121 dldsfkavnd ilghsagdav lvevakrlrs avrpqdtvar lggdefaili taateeeiir
      181 iahraseylq dsmcigietv wamasigvcv gkpgyraeal mrdadiamyq akargrnnvq
      241 lfhpemldav qersritael rtavaggela llyqpvvela sgrvigieal lrwhhpvrgt
      301 impgsfigia eetglifelg rwvlheglaq marwsqtdpd ltdfclhinl saaellrtdl
      361 ledisdtlat ygvdprrlvl eitetvlmsr gtgqeqvlsr lrelgvglqi ddfgtgyssi
      421 sylrslpadt vkvdqslikd mesdprqqnf vsailqlifa aglnatvegi etaeqaaqlr
      481 amgclygqgy ffgypvpaae ipsqlrqpar hl
//
LOCUS       WP_284983077             440 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284983077
VERSION     WP_284983077.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..440
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=48140
     Region          42..417
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mfsvispphr aptanptpgk pdtdsvpplg sgaenrlpks epkqsrpdla tltalrfvaa
       61 lwvvffhlqa mqhtflapvy elfrpviang dlgvdvffvl sgfiitytyl drlgprfrwr
      121 aaadfvwarf armwpafalv vgvvglwfvy gtaqetvrew slqtqapdls pwglakqllm
      181 mhlwfqpgtd gaswfgpgwt vsaewlayla fpllalvlfr lrrmhplaal aasvltllpt
      241 aiwgpdlpip tdghqpyewl lriaccfiag afaciaarna drmkfnpala gpgalltgta
      301 vviflatagk pgpgrlavla fplligllsl trgwlrsals agwlqyggrs syslylvhmf
      361 fiylfywlir dwpngagplv enllatacll gialathllf kyveeparlr lralvprvga
      421 arvarataav ghssrgggrp
//
LOCUS       WP_284983114             226 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284983114
VERSION     WP_284983114.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..226
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24354
     Region          <43..136
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mthqhdsgah lhnetgqdad paqfwdevyr ekpkrwsgnp npqliaeake lvpgtaldlg
       61 cgegadaiwl aqhgwtvtav dvsavalera eahaadvglq driswlqrnf gswhphegfd
      121 lvssqflhsp llpwrdslas aaaavapgga llmvghhpdg ltpwsghkdm kdkfftpedl
      181 vealtsgpgs wrinvadsre ravtgpegqh attidsvlra trshpa
//
LOCUS       WP_284983247             175 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284983247
VERSION     WP_284983247.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..175
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19014
     Region          4..109
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mplrsdwser tcslargldi lgdpwgslvl revffgngrf daiktrlhia dnvlskrlgw
       61 lveagllaqr pyldgartrq eyvltpkged alpvlnaiil wsekhldapa dnahmrvihn
      121 gcglptasad tcshcgsrlt aantswhslt rsehplalat aptsrdlpne sepsa
//
LOCUS       WP_284983127             585 aa            linear   BCT 25-DEC-2024
DEFINITION  sialidase family protein [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284983127
VERSION     WP_284983127.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 585)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 585)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 585)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 585)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468221
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..585
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=62089
     Region          11..385
                     /region_name="NanH"
                     /note="Neuraminidase (sialidase) NanH, contains C-terminal
                     autotransporter domain [Carbohydrate transport and
                     metabolism, Cell wall/membrane/envelope biogenesis];
                     COG4409"
                     /db_xref="CDD:443531"
ORIGIN      
        1 mtsylqrnga alpqarpdve hvlavrgtgg yrqyripala vstagtvlaa ydgrpnlddl
       61 pnpidlllrr stdngrswge qrvvrsgsgl ngygdpsllv dtmtarifmf haagthagff
      121 eavgglepdd dvqhcdvsfs dddgvtwhhr rltgqlkpgs vagaragard rgitgifaaa
      181 gqgiqmhtgp fagrlvqqfv vlvdgeimaa saysddhgen walgsligkg pdgvgpnenk
      241 vaclddgrll lhsratprrl aavsddgget wsrlepvedl pdpsdngsli rfdgqpgvps
      301 latpatnswl lasnnqdtsl rrntvlslsa dngaswpakl vlcegssays taarlpdgni
      361 gvlyerqgyr eivfvsvsvk qlteqlpvpa vgaarapetg prpearpdrl efhvelrsit
      421 pgrpavwqna gefhvispen dgdwdvqtwk evgqgysaeq aqilgtreaq dlnygpvipg
      481 ykagdilaft grarnlgtrp atgvvllgph anpgdfppad lapgaealyf tpvytvteed
      541 lardslelaf avaydggara versfsfdlr tgavtvnegg argas
//
LOCUS       WP_284983327             451 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284983327
VERSION     WP_284983327.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 451)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..451
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47606
     Region          39..437
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(150,152,301,303,334..336,380)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mkksigtvaa avtvavaaal slsacgggsa passeakgei nywlwdanql payqqcasdf
       61 tkanpnitvk itqrgwddyw ttltngfvsg tapdvftdhl skypefaskk qllalddava
      121 kdgvkldsyn kgladlwvgq dgkryglpkd wdtislfynk amtdsagita eqmakldwnp
      181 kdggsyekti ahltvdkngk rgdeagfdkn nvavyglgle ssgsgqgqtq wsflaattgw
      241 tatdknpwgt kfnyddpkfq etiawwagla dkgympklet tvgasvsdnf gagkaaints
      301 gswmigqytg ykgiqtaiap tpvgpsgkra smfngladsi wagtknpaaa tkwveylgss
      361 acqdvvanka vvfpaistsa dlaakafaak gvdvsaftqq vkdgttflfp iadkaakvdg
      421 imkpamdavl sgkkpassls dannqvnnlf k
//
LOCUS       WP_284983342             226 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284983342
VERSION     WP_284983342.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..226
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23999
     Region          37..206
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mtaledlvsl itridsglhp gpdpriaaat vdpdkarkaa vlmlfgvldd vpaqsgkpva
       61 padldvllle rahtlddhpg qvafpggsid pgdesavaaa lreaveetgl dsggvqvlgv
      121 mpelglirsn fvvtpvlaww tspspvrvvd yaesaqvfrv pvrdlldpdn rytgtltrlg
      181 rtfsspvfqv nglvvwgftg mvlsglfdal gwtvpwdadr lleiei
//
LOCUS       WP_284983365             200 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284983365
VERSION     WP_284983365.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 200)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..200
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20825
     Region          4..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mvtddvfavi aeatrrdilv slrsgdkavg elveelaasq ptiskhlkvl readlvsmra
       61 qgqkryyaln pkplagvasw letfdvgpae aeteaatptr sprarsvgqp gavgqqgqga
      121 akkqlkqpdg eplgtspast dverspetvp asgavasaag iddtrpqqig rtvgraatka
      181 adllanlpnl pnlpkfgrkk
//
LOCUS       WP_284983371             272 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284983371
VERSION     WP_284983371.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..272
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29620
     Region          22..241
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mpveknavva tapaatqqhg eaaffdvdnt lmkgaslfhv arkmyerkaf tlsqaagfaw
       61 kqfkfvlrge kmedvhsvrd salilaagiq vsdikelgee vydemiesri wpgtkalaeq
      121 hlrvgrkvwl vtatpievat vistrlgltg algtvgeved gaytgrlvge ilhgpakava
      181 vqriadeegl dlkrcwaysd shndiplltl vghpvcinpd aglrrharen nwpvydfrsg
      241 rraatlglka atvggavygl wrgfskfrsp ra
//
LOCUS       WP_284983417             551 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284983417
VERSION     WP_284983417.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..551
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=58365
     Region          202..550
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtndasspnr alvadpdpvr hsetvaalaa agfmvrsahd agslaaaves epsdvlvvdn
       61 dlreflprnd apvlllldpe deldvaalea wtiadfvyrg qppafrahra lvliaraaer
      121 trrrseaesl reslrkvsaa irstidpgri arhlvdgige algaehvwft tfpdtrvpqv
      181 saewnapglv pgvlpheltd diatfdlaer lwaeaevqpl pkrapagdad aalagrpgga
      241 dalggagaps asvvvpvgeg dlvlgviwia rpdtaqewtr aeigliqhvs gnlayglmqs
      301 hligaqqqvm yklqeldqak tdflttvnhe lrtpltsita yldmirtgag gplpagverm
      361 vdvisrnaer lrrliedmlt vshqdtsgdl qlsrvnvgtl lrlvvstlqp ladsrslslt
      421 vmhapgavtv qadeakleqv faniisnaik ftptgghvav ssgissdpgt vpsvvvrved
      481 tgvgipetei dqvftrffra snastaaipg sglglaiahd iverhsgrld vesalgvgtt
      541 vsvrlpldte s
//
LOCUS       WP_284983429             179 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284983429
VERSION     WP_284983429.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..179
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18750
     Region          36..179
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mglsacaqed alaqqakagd nknyvagdgs vtefakadrk aavgikgtlf dgtavtpqdl
       61 lgkvtvlnfw faacapcrve apileelhqe fkskgvqfyg vnlrdekata dafdktfnlt
      121 ypsfddkdga vllsvsgivp pgavpttlvl dkegkvaarv lgeiekstlk alittavae
//
LOCUS       WP_284983488             339 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. efr-133-TYG-118].
ACCESSION   WP_284983488
VERSION     WP_284983488.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..339
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36918
     Region          1..327
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mklgvynail hdrplpealk viadlgltgi eintggflpa vhvptfddil vsdaarddyl
       61 gifegtgvai aglncngnpl hpkreigekh aedirrsirl aerlgqnrvv tmsglpggep
      121 gatvtnwivn awnsaaldvl dyqwdiaakf wretdrlaad hgvkvalelh pqnivfntad
      181 vhklieltga thvgveldas hlfwqqmdpv avvrelgplv fqaaakdvrv ntanaalygv
      241 ldnsfrrlsp eenrtnlggd ewanewpkns awdfvalgrg hdtafwtefl ralheadpgm
      301 lvniehedts lgriegleva akvlrdadaa lseslnvta
//
LOCUS       WP_284983494             303 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. efr-133-TYG-118].
ACCESSION   WP_284983494
VERSION     WP_284983494.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..303
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33696
     Region          8..293
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtenkliigt apdswgvwfa ddpkqtpwer fldevaesgy kwielgpygy lpndparlae
       61 elkqrdlkvt agtvftafhr gldqwetawe parkvaelta amggehivvi pamwrddvtg
      121 eavesgelte kawsdlfagh nrlgktlled fglkqqfhsh adshvgaqed ietllaatds
      181 kylnlcldtg haeycgassl eliknypdri gylhlkqinp dvlrkvneen mtwaaanlag
      241 vmteppnglp dlravieave glnrpifgiv eqdmypvsfd vpmpiakrtr nyllscgsrt
      301 tvq
//
LOCUS       WP_284983526             142 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284983526
VERSION     WP_284983526.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..142
                     /product="YybH family protein"
                     /calculated_mol_wt=15713
     Region          4..128
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 msneqtpvtq aldsyaaavh akdvdaftal ydenvhiyds wgqwqytgie awrsmagewf
       61 sslgdervqv efndvqsvtg edvafghaav tfagisadge rlramtnrft iclekkddtw
      121 kishehsslp idmetgkgif ts
//
LOCUS       WP_284983624             296 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284983624
VERSION     WP_284983624.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..296
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32435
     Region          10..294
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mstgiltset flkaieltav paqihdeaye atsqyvpwpk ayggdmvaqa aaammrsvda
       61 drqlhsmhsy fmrpveigat vryeverlrd grgystrsvr ghqngktvya amgsfqvpeg
      121 gpefqplapt avepeslrsa aevlqgvegp aaeywsskrs fdmrhipgpv ylqvegdsvp
      181 hqaiwvkafe qlpdagdeha tadlhraala yvcdytilep llrvnglhws spglatasld
      241 hsmwfhrdgr vddwvlyaqe avsgqsnrgl atgrffdrqg rllatvaqeg mirags
//
LOCUS       WP_284983693             522 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA synthetase [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284983693
VERSION     WP_284983693.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..522
                     /product="acyl-CoA synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016405 - CoA-ligase activity [Evidence
                     IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0032787 - monocarboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=55535
     Region          10..513
                     /region_name="FACL_FadD13-like"
                     /note="fatty acyl-CoA synthetase, including FadD13;
                     cd17631"
                     /db_xref="CDD:341286"
     Site            order(180,183..188,190..191)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341286"
     Site            order(183,298..299,319..324,404,416,419,430,510)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341286"
     Site            order(183,223..224,271,273..274,277,298..299,319..324,404,
                     416,419,427..430,491)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341286"
     Site            order(223,273..274,277,298,427..429,485,491)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341286"
ORIGIN      
        1 menfgigswl qrrrpksgsk valisgdrrl syeefaersd rlanaltsgg vakgdrvayl
       61 genhpaflet lfacgqlgai fvplntrlap peinfqledc gavalihsas lnglaasgae
      121 gtrvgrrivv gdsfpgetta apggtgsetp taaedyedvv asgasrhlde evglddgami
      181 lytsgttgrp kgallthgni twncinvivd fdfsssdval mispmfhvas ldmgvlptll
      241 kggtvvlesr fdpqrtleli eqhrattisg vpttyqmlce hpawptsdlg slnkltcggs
      301 avpmrvleay earglrfsng ygmtetapga ttlpaarsrd kagssglphf fsdvriadia
      361 ggvagqgtvg eiqikgpnvi heywnrpdat aesyadggwf ksgdmgykda dgfvfvsdrl
      421 kdmiisggen iypaeveqai seldavgsva vigvpdekwg evpravvvlr egalltedel
      481 kehlagrlar ykipktvvfv ddmprtasgk irkselrrst vs
//
LOCUS       WP_284983823             220 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284983823
VERSION     WP_284983823.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..220
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23283
     Region          6..193
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mtearlparw tmiwsrpvgw mldhvlyrta itgrsnvpks gpvifagnhi sfldgpvmfg
       61 aaprpmhilv kkemfkgflg kvlrasgqis idrsgdraal qlgrqaldag rcvgilpegt
      121 rgsgtagnig ngvawlalms gatvipvail gtrigdehrd sipglrrrvh vsfgaplnvt
      181 rrngepgrvs mdraaaeira alaghvqdav kttgqslpgd
//
LOCUS       WP_284983837             271 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284983837
VERSION     WP_284983837.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..271
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29236
     Region          9..246
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mntlpdpspy asdftgsgps igvvmshgft gsphsmrpwa eylaaegyav rlpllpghgt
       61 twqdmatrhw qewhraldaa ylqlqaecdf vfaaglsmgg tlalriaatr pvagtvvvnp
      121 glviddpraa vvgilkhvmk stpaiandil kpgmdegayp rtpvaaahel kkmyrdtvtl
      181 lprisapvrv frssvdhvvs drsirqlker vkasmefstl ensyhvatld ndaleifrgs
      241 aefirktmag ltssstaasq saaelrdsph e
//
LOCUS       WP_284983847             598 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Arthrobacter
            sp. efr-133-TYG-118].
ACCESSION   WP_284983847
VERSION     WP_284983847.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 598)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 598)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..598
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=63757
     Region          8..584
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mvqktgkskn krtpaakkrl rlglgimltl llvvggklfl vqgldvggla eaaynnrltt
       61 tilpaergki ldangtvlas svirynivvd qtvntntdqf prfnsqtqai dtisrsqgia
      121 elssalgmdv gqvtqavtgv kkynivakev kpdvedrisq lhipgvvseg iskrvypngs
      181 vaggivgflk dgttgqagle qtqdellrgk dgkrvfeiga dglripvatd lltpavngkd
      241 vkltlntdiq yfaqqaiqtq vnqlnaewgs ivvediktgn liamadtnap dpndpgkvaa
      301 adrgvrsvta ayepgsvekm itasaaineg ksspldtvti ppaltidgqt ftdafdhgte
      361 qrtlagilgy smntgtvmig srlskqqryd yltrfgigqa pdiglpaets gilakpdqwd
      421 drqqytvlfg qgvsqstlqt vrayqsvand gvmlqprlid gyvgadgvee kvpakdsrqv
      481 vtkdtaqqvr dilesnvtmg evkdaaidgy rvgaktgtsq apredglpgf dgytasivgm
      541 apmdnprfiv evvlqrpkgs iygitqgpif rsvmgqvlrt ynvppstgtp arfpqyak
//
LOCUS       WP_284983928             950 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284983928
VERSION     WP_284983928.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..950
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..950
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=101184
     Region          <112..238
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          337..873
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 matrttsapr gssnsksggs gsgrtpaktg rsgtatargk qaavvepqqp wiqralagvw
       61 lgighvvgag irrighdvsd ldpldrrdga alfnlalgvf iatfawwgfk gwfpdvvfsi
      121 vngtfgwvsl llplmlfvca frlfrqpwds rgnnrvgigf limtfagtgl ahiiggqptv
      181 adgfeglrra ggmlgflaas plaaihpvvp vmvygalafv slliltatpf gaiprrirga
      241 yehlmgvdlv dpdaqrgdsh drsylyenev avepkkkrrk rffgkdhddd ptlegyvgde
      301 afehaivddd appakggpsv ppgvrrptqa eiavekikaa qglgspkaaa dnateaiplv
      361 aptaavppvi vpsapvgppp pptpipqrte qlslagdvty tlpssdnltp gsipkertea
      421 ndavvaaltd tlqqfnvdat vtgfsrgptv tryeielasg tkvervtals knisyavass
      481 dvrilspipg ksaigieipn tdretvslgd vlrsqnarrt dhpmvmgvgk dveggyvvan
      541 lakmphllva gatgagkssf vnsmitsilm ratpdevrmv mvdpkrvelt ayegvphlit
      601 piitnpkkaa ealqwvvrem daryddlaky gfkhiddfnk avragkvvpp vdskrvikpy
      661 pyllvivdel adlmmvaprd vedsivritq laraagihlv latqrpsvdv vtglikanvp
      721 srmafatssv tdsrvvldqp gaekligqgd alflpmgask amrvqgawvt eseihrvveh
      781 vkgqlkavyr ddvapeaqkk qidddigddl evllqatelv vttqfgstsm lqrklrvgfa
      841 kagrlmdlle srgvvgpseg skardvlvkp ddlapvlaam kgqeapaapd ahtaalsena
      901 naniavggya edlvaadler rkqvteyhdg adgiddedeg gedawsltgr
//
LOCUS       WP_284983896             362 aa            linear   BCT 25-DEC-2024
DEFINITION  fatty acid desaturase family protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284983896
VERSION     WP_284983896.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..362
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40226
     Region          11..347
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 msptstterp tksvrqpnav vlsysellkt vraegllkrr vgfyvsvfts lvllltgtwf
       61 gfaligpswy qlliaaalgi lctqlsflah eaghrqifas rrandwsari latsvagisy
      121 swweqkhgah hnnpnviskd pdiktgalaf hveaaagrqg rfafltrrqg wfffpllmll
      181 gislqweslm yicrpgaikh rwvetpilla rllalpvlaf tflplgmafa flgvqimvfg
      241 fymgasfapn hkgmpvlptd srvdflrrqi ltarnisggp fmnillggln hqaehhlfpd
      301 marphlrras eivrsycekh siaytettlm qsyaivvryl nevglaagrg fdcpvasahg
      361 rs
//
LOCUS       WP_284983964             265 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfite exporter TauE/SafE family protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284983964
VERSION     WP_284983964.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..265
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26980
     Region          10..259
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 misgfesvql ttlimivvag faagwidavv ggggliqlpa lllvpgitpv qalatnkmgs
       61 ifgtttsavt yyrrvgpdlk taipmavial agsfggavla anlpasvfkp iivvaliava
      121 lftalrpnag eltalrhdgh thyvvacaig avigfydgli gpgtgsflvi alvsamgyaf
      181 leasakakiv nmatnagalf fflphgsllw gvgavlglsn maggylgart avkqgsgfvr
      241 ivflivvgal iiklgmdvwn dyfak
//
LOCUS       WP_284983971             278 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284983971
VERSION     WP_284983971.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..278
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28792
     Region          1..276
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mtftmgpall fcpadrperf qkaaersdav ivdledavap aakkrargai laqlgsgget
       61 aeldpsrtiv rvnpvgtpdf ekdlhclaht pyrtvmlaka etgeqlkale gyhvialcet
      121 akgiinasei aqapnvvglm wgaedliasm ggtssrnddg gyravamhsr savllaakaa
      181 gkeaidsvyv dipdlaglav esadavasgf gakacihpsq vavvreayap speavagare
      241 lldaaaaagt gvfqhkgkmv dgpilkhaes tlrrarls
//
LOCUS       WP_284983986             239 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: LytR/AlgR family response regulator transcription
            factor [unclassified Arthrobacter].
ACCESSION   WP_284983986
VERSION     WP_284983986.1
KEYWORDS    RefSeq.
SOURCE      unclassified Arthrobacter
  ORGANISM  unclassified Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 239)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 239)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="unclassified Arthrobacter"
                     /db_xref="taxon:235627"
     Protein         1..239
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=25991
     Region          1..229
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 minvlvadde lpaveelafl lgrderigai hraasgaeal saletesvda vfldihmpal
       61 sgldiarais rsprppavvf vtadedcale afelaavdyl lkpvraerla rsisriseli
      121 kdgskvpemi tvdqggttrm irrddvsyvq aqgdyarlht aeasylirvp lsdleqqwag
      181 agfirihrsy lmslnhvghm klaaarpsvt vagaelpisr rhlpavrdkl eatrirpqg
//
LOCUS       WP_284984002             421 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284984002
VERSION     WP_284984002.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 421)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 421)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 421)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..421
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=44911
     Region          <64..417
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mgeqraqlyd vkeqarqaal sqyglpggil pragheydda lerrsgldkl aglaakicgv
       61 pygvvniita eeqhqiaaag lepavcsree smcartfldg vttvirdasa dprftanpfv
      121 tgeianvrfy asvplvaasg hvlgtlcvfs drkgslsgeq edaletlaaq tvdvlelrhr
      181 trlldeamke lrrsneslte fagrvshdlr npltaiigyv elseqdpavq pespavdylh
      241 siggsgrrml amlddllsys rlggaldrst islralvsdi ekdlhpaiee tgaiiecndi
      301 plsgdpaqlr tllqnlvsns lsyrspgktp kirisgelid dvavlrvidn grgippsdrh
      361 rvleplirlq rdsdgpgsgl glatcmrvvs ahegkltige tpgggttvtv slpsaaagqq
      421 k
//
LOCUS       WP_284984129             143 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284984129
VERSION     WP_284984129.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..143
                     /product="YybH family protein"
                     /calculated_mol_wt=15781
     Region          18..130
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mpdsdldlmv ekyhraldaf vkgdpeqqkk lfsksddvtl anplgppvrg ssaveatmdr
       61 assglregep irferisgyv gtelayivei ewarakvggs devspiplrv ttifrredge
      121 wkvlhrhadp ilsprpiesi vqa
//
LOCUS       WP_284984243             243 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284984243
VERSION     WP_284984243.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..243
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=25315
     Region          9..78
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(13,17,42)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(16,41)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(23..24,35,38,42..43)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mntlqtpegk llqdaqrrkg msarkaaela gmsdtrwrni vngyqaigqg qsihivapae
       61 tlarmarvvg vsgeefaaag redvqavlte lwpgeqagws wsadtgvmaa vpttgggpkg
      121 erglrrlies kragrtiasl sdacggdptp rrlqqiiadg idafpkanti qglarglgvs
      181 itevvmacav slglevedat sdalvlagag nlpassrail qnmakeliaa qheaqhhddp
      241 hva
//
LOCUS       WP_284984348             753 aa            linear   BCT 25-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284984348
VERSION     WP_284984348.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Shan,L., Mathews,I.I. and Khosla,C.
  TITLE     Structural and mechanistic analysis of two prolyl endopeptidases:
            role of interdomain dynamics in catalysis and specificity
  JOURNAL   Proc Natl Acad Sci U S A 102 (10), 3599-3604 (2005)
   PUBMED   15738423
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Polgar,L.
  TITLE     The prolyl oligopeptidase family
  JOURNAL   Cell Mol Life Sci 59 (2), 349-362 (2002)
   PUBMED   11915948
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Polgar,L.
  TITLE     A potential processing enzyme in prokaryotes: oligopeptidase B, a
            new type of serine peptidase
  JOURNAL   Proteins 28 (3), 375-379 (1997)
   PUBMED   9223183
REFERENCE   4  (residues 1 to 753)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 753)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..753
                     /product="prolyl oligopeptidase family serine peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=83057
     Region          15..745
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mtttaadqap apdnetaqgt aiapepvden iwledihgee qlawvreqna rtedllddad
       61 yaaleagile vldstdriam vnkrgehyyn fwkdqqnpkg lwrrttwesy lrdapewdvl
      121 ldidalaase geewvfhgan fmrpaegeph rlaiialspd ggdanrhref dvetrtfvdp
      181 aaggfdlpta kgnvswldad tllvattadg lpktsssysr tgvklrrgqs lveaerifei
      241 pedhmmalva hdstpgfert favdwidffn rttsvlrdda wlaidvptdv nlsshrewlm
      301 frprrdwnvd gttyaagsll aadfegylsg ardftvlftp dehtslqsws wtrnylllnl
      361 lhdvsseirv ldpahkdsag rwastlldac pplhdvnaya vddedeaegd dagndywlva
      421 tgfttpttlm rgtlspgias ytleaghdgg vssthavvks spsffnetdy evqqhfatsa
      481 dgtrvpyfqv askdldldge nptqlsgygg fevsrtpays gaigrawler rsesittedg
      541 saahsrggvy vvanirggge ygpawhraal qanrhrafed faavarhlis rgvtsprrlg
      601 cvggsnggll vgnmltqype lfgaiscgvp lldmrrytkl sagyswiaey gdpdvpeqwe
      661 yirtfspyhl lrdgveypet fiwtatsddr vgpvqarkma armqamgipn vwfhealegg
      721 hagasdnrqa aslqarsqhf lwralagkeg sgh
//
LOCUS       WP_284984405             492 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284984405
VERSION     WP_284984405.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..492
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53475
     Region          191..>443
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mitprfvvvs kdawpvktag tftlvvdmwd dlhyktsytl hygtgdstie igavkiaarg
       61 msegdphtkl prafkqlspe fyslgqdrey yvalanlpnd igrpalralr dvaenraifd
      121 dvqdepafet svlrsvpkqt vavqfnriie grapltpyrf sysrssvsta pplwlefgvh
      181 lgvmpptnvh vligtngvgk srllrdflka asgsigadgt fqdelgsdfs aggqdvpfan
      241 vvhvafsafd rdnleplgdd vdvhqvglss gagdpldaqf akslvvcskg prrdrwlaav
      301 ktlaaadgil adadldhlis sedakavfas mssghkivll tvtrlvelve erslilidep
      361 ethlhpplls altravsdlv idrngvaiia thspvvlqev prscvwmlqr sgddlrasrl
      421 stetfgesvs rltsevfhld anrtgynhvl rtlldqnnss avrvmdalgg hlgsegrfvl
      481 saleyhqded lv
//
LOCUS       WP_284984632             268 aa            linear   BCT 25-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284984632
VERSION     WP_284984632.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     BTLCP proteins: a novel family of bacterial transglutaminase-like
            cysteine proteinases
  JOURNAL   Trends Biochem Sci 29 (8), 392-395 (2004)
   PUBMED   15288868
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..268
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=29059
     Region          60..211
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mernvaaqlv fktvantkva maiavasnpg yeslteelsv tvegeavplt eltdhhggrf
       61 qymefaepse vtvdyrasve gfgvpdessr meliryvrps ryaesdrllp tsyaefgglh
      121 geellqavrn wvhdelryvs gssrgtdgav etllhrkgvc rdfahlaial lrskdiparl
      181 aavyapglsp mdfhavaeah idgtwyvidp tglapresml ritagrdssd taflstvggs
      241 lslkslkvta vvadelpded paklvvlr
//
LOCUS       WP_284984709             328 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284984709
VERSION     WP_284984709.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..328
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35438
     Region          18..317
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 miqtsarllq llsllqvrre wtgpalatrm gvtertvrrd idklrnlgyp ihaspgiagg
       61 yqlgagaqlp plllddneal avalglnsva agpvagigea svralakleq vlparlrpkf
      121 amlkaavttl psnaasvdpq qltvvsaaia dkrqlsfdyv kadggagrrl vepyrlvdtg
      181 rrwylvawdv dredwrtfra driaslpaer kkyvprplpa kdladyvqrs vtrspyrydv
      241 vvrlhapige vaavvgpqla slsddggnat llragwdsla qpaahlaald mdfeiispee
      301 fkeyartmag rlekaagnha mqgdappq
//
LOCUS       WP_284984720             204 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284984720
VERSION     WP_284984720.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..204
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23393
     Region          9..195
                     /region_name="HAD_sEH-N_like"
                     /note="N-terminal lipase phosphatase domain of human
                     soluble epoxide hydrolase, Escherichia coli YihX/HAD4
                     alpha-D-glucose 1-phosphate phosphatase, and related
                     domains, may be inactive; cd02603"
                     /db_xref="CDD:319790"
     Site            order(12..16,113..114,146,170..171,174..175)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            141
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mavqssdvli fdlfgviakd qnqegkaall atggvpekdf waaywdqrpp ydrgevtatq
       61 ywtavsdqla rsfdpdrirq lkehdiasws vvddrmiall edlsrtrrla llsnipkelg
      121 ehflrrhrwl dlfevrglsy qigyakpere tfewcirelg iepyqalfid dreenirsaq
      181 eaglrghlft ssealshile anvt
//
LOCUS       WP_284984768             362 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284984768
VERSION     WP_284984768.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 362)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..362
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35536
     Region          5..360
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 msdtprnlnr tallgsgvvv ffavavllgs ytvtipdffr iltahltgge kipgasfivm
       61 enklpravlg iligvafgls gglfqtmlrn plaspdvigi sygasaaavl aivvfgasga
      121 avsaaalaga tgvalliyai sqgssgggsg gggsggggsg gggsggrrgn aagnrlilag
      181 vgiaaalaav vnflmtradi rtasealiwl ngslnsanwe rvgvllatla vlvpalafla
      241 gplrmlelgd daaaglgirv navrfglvit avalaavata aagpvafvaf lagpiarriv
      301 grpslpasaf tgalivlaad yfaynvapli lggtvlpvgv itgalgapfl lwllvtsnrk
      361 ea
//
LOCUS       WP_284984845             356 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284984845
VERSION     WP_284984845.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..356
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39904
     Region          12..228
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mrprsarnta qvtvvvpcyn yaqylpavts svlsqagvda qvivvddast dnsaqvasdl
       61 alrdpritvv vhernmghia tyndglsrvv teyvallsad dllapgalsr atglmsanpr
      121 vgmvygrple fsdehqlpra dgsrwqswtv waghewinwa cwrgrcfils pevvmrtevl
      181 qhvgfyngll phsgdleywl rtaahwdvgr ingpiqafyr vhganmhlis fatmvvdlrh
      241 rleafrvllt sevlrglpqa drlldraqra lrrealilaa rtldsggsat dasalqdfal
      301 rvwpgqpasf rirgvrwrlv radegkpplp wqrtveifrt qvdrvrwraw rlvgis
//
LOCUS       WP_284984850             372 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284984850
VERSION     WP_284984850.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..372
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38246
     Region          8..372
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mdaslpanip lvdlaaqhae vesevlsgle gvfattafig gaavgqfeea yaawlgvdhc
       61 igvangtdal elalratgvg pgcevvlpvn tfiataeavv rigatpvfvd vdpvhllidp
      121 aqvaeavgkr tqaivpvhlf gqtapveqlr alaescgavi iedaaqaqga trhgspagsl
      181 gaaagtsfyp gknlgaagda gavttddpev arrvrmlaah gsatkyvhdv vgfnsrldti
      241 qavilnaklr rlsawndsrr eaaaryseml ddvpgasapi saegnddawh lyvirvadrd
      301 rvlallngag igagihyptp lhlsgafahl glgpgafpva ehaageilsl plhphitiaq
      361 qkfvvetlra al
//
LOCUS       WP_284984858             300 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284984858
VERSION     WP_284984858.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..300
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32570
     Region          26..300
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 msttstdlta rtprqeyasm islievpvln ekywskvpev aadgimldle dsatpenker
       61 vrervievla didyfggrri ivrsnnigsp wgrtdleala avdadivisy pkvetveeld
      121 evvaimrgag rvhplhvmie taralieldr iaahpavvgl hfgyvdlaad igsrpfdadg
      181 mlssltsgya rakiaaaaaa yglwatggsl ipeykdlekv rafiqtwsdl gftaciavsp
      241 ahlpiinevm rpsaadvdra rqvcdvyeet aargepaavl ngrvitlpdy rvarlvlera
//
LOCUS       WP_284984885             694 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Arthrobacter sp. efr-133-TYG-118].
ACCESSION   WP_284984885
VERSION     WP_284984885.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..694
                     /product="PhoX family protein"
                     /calculated_mol_wt=74012
     Region          62..693
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 msestarkfg llpmlghtkg krspvtcalk cdnacsgevc ntssnayfrd iasaavsrra
       61 algfgavgal avvlggslsg nvpggaglse aartgfdkak lkftpikpvd ymvdaftvpd
      121 gfawqpiirw gdplfadspa felngqtaaa qarqfgynnd ytdilpipds kdrravlftn
      181 heytnenimf patlaaaear aigraahglt vvelerknkn kpwsyvkgap lnrrfltdtt
      241 yeltgpaagt dlvktiddps graikgtlgn csggttpwgt ilsgeenfng yfvapgtsag
      301 dkryglsnkp tarkweldep rfntnnagys netnrfgwiv evdpfdpsst pkkhsamgrf
      361 kheganviva asgrvvaymg dderfdylyk fvskgkymag dsaaarrnnm nllsegdlyv
      421 akftgdspaa eidgtgalps dgafdgsgew lplvvdgvsa vpgmsvpevl vytrlaadkv
      481 gptkmdrced vepnlatgkv yvvctnnsdr gkpgkegate vnprtlnrdg hiveitetgd
      541 qtstrfnwtl lmvcgdpakn sstyfsgfpa dkvspiscpd nvafdsagym wiatdgapss
      601 igyadglfkv tldgsergkv eqflavprda etcgpivhdd ertvfvavqh pgeegsfdap
      661 hsyfpdyvga gaapaagqvr aprpsivqvf rkdg
//
LOCUS       WP_284984982             238 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284984982
VERSION     WP_284984982.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..238
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24523
     Region          19..>87
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mnetglhqll gayllgglep aearafeahl ascadcrlel geleslpall davpvpdava
       61 laggrpavep saavpsatag arslmgafse tlpqpilvkm aarrrksrrr waalvgavaa
      121 aclglgilag pvlnqppkpd asyslqtdng lqltvglvrk awgtelqleg rsmpaqgtmy
      181 lwvkgrdgte emacgwtats sghikvtgat pvqlagisgv elrddnqktv avisvpgs
//
LOCUS       WP_284984997             317 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Arthrobacter sp.
            efr-133-TYG-118].
ACCESSION   WP_284984997
VERSION     WP_284984997.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-118
  ORGANISM  Arthrobacter sp. efr-133-TYG-118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Arthrobacter sp. efr-133-TYG-118"
                     /db_xref="taxon:3040279"
     Protein         1..317
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33605
     Region          14..293
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(41,247,250)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(187,218,245,248..249,252)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mhsstvppcp ktdvvvvgea iidiidtgag pvefpggsgm nvafglgrlg vstafltalg
       61 rdersktiqr hldtagvrll pgaehldrts taralldssg saeyefdfew nlpqvspafl
      121 prvlhtgsla sfmepgatqv lsllglfsrr clitydpnir ptllrshtea lrtfertval
      181 atvvklssdd aqwlyprtsp hdvarrlldl gaelaviteg asgsylrsna aeievpappv
      241 lvkdtvgagd symssliagl iedpeddfgy gklsrlgtas slaaaitvgr hganpptrae
      301 lvrslelaqt srkssdd
//
LOCUS       WP_284985086             613 aa            linear   BCT 25-DEC-2024
DEFINITION  IucA/IucC family protein [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284985086
VERSION     WP_284985086.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..613
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=68025
     Region          19..611
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mtttadnvtt aaaasvshlt perwaianrh vvrkaiaefs herilvpefi redgagvgly
       61 kvvsdddtve yrfrarvlql ehwsvaadsi vrlrdgqevp vdaldfiaef healairqem
      121 lpvyleeiss tlashaykqg kpfssaqlaa gvtggadrav dfqaiehsmt eghpcfvann
      181 grlgfgiady hafapetgat vklqwiavhr skavftssag ldyrthfeae lgpatvawfn
      241 aelsasgldp edyllmpvhp wqwdnkltvt faaeiaqrhi vnlgtgedsy qaqqsirtff
      301 ntdhpekayv ktamsvlnmg fmrglspqym katpaindwl qeligndqel qnrglamire
      361 taaigyhnhy yeaasakgsp yrkmlsalwr esplpllkdg hqlatmasll hvdgtgqsmv
      421 saliarsgla ptewlrryfe aylvpllhcl yqyelafmph genvililed gvpvraimkd
      481 iaeeivvmgd rlelpeevsr ikaeipaeem vlaiftdvfd cifrflgail vedgtlgedg
      541 fwgtaatvvk eyqerhpela dqfamhdlfa pdfelsclnr lqlrnnqqml disdpsgglq
      601 magrlanpla kfa
//
LOCUS       WP_284985111             549 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284985111
VERSION     WP_284985111.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..549
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=58803
     Region          229..539
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mdtvaqsgiq qsavrlsdci qlmqadlvha nptpenlghl vsdvlmydpl dtwssvdnri
       61 ilavgctygs pdfdqllhra ansnaaaviv kahgaqmeql rsaavrhtls vlvapddadw
      121 tqlvalaras vvgaaadsvs gvrlgdlyaf anaaasitng aasivdplgr ilgystlpgq
      181 pidelrritt ltlqetiqpa fdqdfkavya apgavlvpap ddgmarlala vraggellgs
      241 iwiidpgeek ratalnaldr maplaglhml harsasdfge rrnadlirtl mddtphasfa
      301 aaqlgldtan glavaafsiv rpetgslesv reihrllhlv ttvcnvqfgs ghsaligsvv
      361 yallpgngps pralhariiq eieayshtis sfpviatvgg iaatidelpr srseamrtlh
      421 hllnlqarqg kspgnnkvpg valfedfqvp lnllrigefi ednglagade isriqardae
      481 qqteyletlr aylafngnis tmaaqlhvhn ntvryrvarl aedfnldlad pqkrlwlwlr
      541 vttmelaak
//
LOCUS       WP_284985109             244 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [Micrococcaceae].
ACCESSION   WP_284985109
VERSION     WP_284985109.1
KEYWORDS    RefSeq.
SOURCE      Micrococcaceae
  ORGANISM  Micrococcaceae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Micrococcaceae"
                     /db_xref="taxon:1268"
     Protein         1..244
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25695
     Region          16..243
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mthmtdlrna wsgasallfd ldgvltptav vhehawqelf ddylartghs qgyqesdyfd
       61 hidgkprfdg vrdflasrgi tlpegpvhdh pdnqtvqglg nrknaifnei vnsrgvepyp
      121 gsvkfinaav elglkvavvs ssrnapavlk aagldhhfev vvdgqvaagv glpgkpdpat
      181 yvyaagllgv pveecivved avsgvqagag adfyavigvd rgagrqtlld agatlvvddl
      241 ndll
//
LOCUS       WP_284985129             432 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284985129
VERSION     WP_284985129.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..432
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42997
     Region          37..385
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(47..48,51..52,55,89,139..140,142..144,147,167,
                     170..171,174,251,254..255,258..260,263,290,294,343..344,
                     348,352,368,371..372,375..376,379)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mnhtlpaaas hgptsgavta dapgaaprfs kgsalavlvc wllvvfdgyd livygtvqss
       61 lisetgwglt katagtigsm aflgmmigai fagrmadswg rrktiigcai vfsvftilca
      121 lapnaavfgi lrllagiglg glvpsanalv aelvptkwrs tiatlmmsgv piggsiaalv
      181 giplipafgw qamflvaala lvivvplglk fipetlapgk gastdankka gfgsllrapy
      241 lgvsllfala tiatlfawyg lgtwlpnlmq lagynlgsal tfalalnlga vagsvltawa
      301 gtrfgpipta iaaaavaavg laallasppv tvvylalvla gvgthgtqcl iiaavashyp
      361 dhlrgtalgw algtgrigav vapqvgglll aaglgvnsnf lafagaaava avllaavgln
      421 iknkisqgas na
//
LOCUS       WP_284985151             125 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284985151
VERSION     WP_284985151.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..125
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13514
     Region          16..120
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mkvsaipapl pdtladgvfp agcpsrtvld hitskwgvli llslsegeqr wselrrradg
       61 isekmlaqtl ktlekdglvr rdaqpvippr vdysltergr elaalliplv twafdnaeai
      121 iggeg
//
LOCUS       WP_284985173             191 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: GlcG/HbpS family heme-binding protein
            [Micrococcaceae].
ACCESSION   WP_284985173
VERSION     WP_284985173.1
KEYWORDS    RefSeq.
SOURCE      Micrococcaceae
  ORGANISM  Micrococcaceae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Micrococcaceae"
                     /db_xref="taxon:1268"
     Protein         1..191
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=18329
     Region          56..178
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mkksnkmiav aaagallltg gatavanava paaapaavea kapadvqpap envvaqnrit
       61 vgasskavna alakcqadkl pfvtvalvdr fgtvqailrg dnaaehtiea akqkaytaaa
      121 fgaptselak ringngpsia dlpgtlflsg gvplkvngvs vagigvggap dgaldeacat
      181 agadalaaaa k
//
LOCUS       WP_284985197             463 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284985197
VERSION     WP_284985197.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..463
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=51634
     Region          1..460
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mkpsvvwfrd dlrvadnpal raavddgeav alyvldeesp girphggaar wwlhhsltal
       61 kedlaalgip lllrrgaaae vvrktttaig agalywnrry gsaertvdag ikswageagl
      121 hvssfqasll hepwevttkt ggqykvftpf wrtisaqefr eplavpqkgh gfggelpayd
      181 dleswsllpk kpdwagglae mwtpgaaagh krlaafvdkg lsnysegrnr pdtdgsscls
      241 pylrwgelsp fqvwhalgsr rsesasiyas elgwrefcwh qyfhnphlat anlrtefdrf
      301 pwawpgsngs ggkhpghesa peefrawqkg rtgfpmvdag qrqlwhtgwm hnrvrmvaas
      361 flvknlgihw qlgeqwfwdt lvdadpasnp anwqwvagsg adaspffrif npeaqrvkfd
      421 pqgkyiahwi pefgtpdypd givdlkttra ealeaykgmk evh
//
LOCUS       WP_284985369             197 aa            linear   BCT 25-DEC-2024
DEFINITION  YdeI/OmpD-associated family protein [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284985369
VERSION     WP_284985369.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Pilonieta,M.C., Erickson,K.D., Ernst,R.K. and Detweiler,C.S.
  TITLE     A protein important for antimicrobial peptide resistance,
            YdeI/OmdA, is in the periplasm and interacts with OmpD/NmpC
  JOURNAL   J Bacteriol 191 (23), 7243-7252 (2009)
   PUBMED   19767429
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..197
                     /product="YdeI/OmpD-associated family protein"
                     /calculated_mol_wt=21711
     Region          1..191
                     /region_name="YdeI"
                     /note="Uncharacterized conserved protein YdeI,
                     YjbR/CyaY-like superfamily, DUF1801 family [Function
                     unknown]; COG4430"
                     /db_xref="CDD:443542"
ORIGIN      
        1 mpieleellv kdadawrawl tdhaeespgv wlilhkkggn vteldydaal dealcfgwid
       61 gqsrsrdaes yfqrmtprgr rsiwsarnvg hiarlesegk mtdagrsave aakadgrwaa
      121 ayagpadsvv padlaaaiaa vpeaqamfdv ltsqnrfali hrtnlvkrad trerkiagfv
      181 emlarheapy pqkkrps
//
LOCUS       WP_284985349             333 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. fls2-241-R2A-172].
ACCESSION   WP_284985349
VERSION     WP_284985349.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..333
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37468
     Region          4..316
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mprpytlftg qwadlpfeev arlasgwgyd gleiavsgdh ldawrwdepg yvesklavle
       61 kynlkvwais nhlkgqavcd dpidfrheai vgskvwgdgd pegvrqraae emkhtarlak
      121 algvdtvvgf tgssiwqyva mfppvpekvi dagyqdfadr wnpildvfde cgvrfahevh
      181 pseiaydywt tvrtleaigh reafglnwdp shfmwqgidp vsfiwdfkdr iyhvdckdtk
      241 lrptgrntvm gshlpwgdpr rgwdfvsagr gdvpwessfr altaigykgp isiewedagm
      301 drlhgapeal aalkkfdfpv sqtsfdaafs skd
//
LOCUS       WP_284985414             337 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284985414
VERSION     WP_284985414.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..337
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36821
     Region          65..330
                     /region_name="2-desacetyl-2-
                     hydroxyethyl_bacteriochlorophyllide_"
                     /note="2-desacetyl-2-hydroxyethyl bacteriochlorophyllide
                     and other MDR family members; cd08255"
                     /db_xref="CDD:176217"
     Site            order(76,78..79,139,143,163..168,187..188,192,202,
                     219..220,222,242..243,269..271)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176217"
ORIGIN      
        1 mtisreqehe pglqahaywv tktgdgemrt etiaapqege alvrtlytgv srgtervvhe
       61 grvpervadl mqaphqegdf pgpvkygyls vgtveqgpee wigktvfslh phqdlyvvpt
      121 snltvipedv pakravltgi vevainalwe agprlgdrva vvggglvggv latllrkypl
      181 grlqmvdadp kkqklaqtlg idfalpanak ddndivfhcs asneglklsl qlagddsdvi
      241 elswfadkev tlplgedfha rrlnirssqv gavalprrhr rtnaqrlqea anqlkdplfd
      301 tfltsecqfr nlpatlaklf eqpggfchvv aypnped
//
LOCUS       WP_284985422             136 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Escherichia coli].
ACCESSION   WP_284985422
VERSION     WP_284985422.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>136
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
     Region          1..>135
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 llvkttgary wrlkyriagk ekklalgvyp dislaearik rddarkiise ggdpgekkrk
       61 ekltqkisat ntfhalatew hqhkslswse syarsvleal dkdifpylgk rsvtdilple
      121 mleilrriek rgslek
//
LOCUS       WP_284985425             463 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284985425
VERSION     WP_284985425.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 463)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..463
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=48677
     Region          7..459
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 msampeayga algramvhag dwlasvptrp vrpssdadqv agsilprlpd gptdaaevvd
       61 elaalaepgl maiqsgrffg wvmggtlpaa maadwlvsaw dqntglrfat paaaaieesa
      121 aawlldllhl patadvgftt gattanfvgl aagrqylmde agwdlealgl nggprittfa
      181 grerhaavdl alrylglgac vpvdadregr iipdalaeam deqpgptlvc lqagnlhsga
      241 fdpmteaiav ahdrgawvhv dgafglwaai sptlrerlag veeadswatd ahktlnvpyd
      301 cglaivsrpe slrrafsvht syliateagl gdplekvpem srrargipvw aalrqlgrdg
      361 vismverlaa naralaegla aipgvevlnd vvftqvsvsf gsddrthrvt qrlmaegavw
      421 msgsswrgre ilrisvsnwt tdagdvaasi aavrraleae pea
//
LOCUS       WP_284985426             681 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284985426
VERSION     WP_284985426.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 681)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 681)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..681
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69787
     Region          39..>284
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mttyfkplte pagqastaqs srlapgsrag hrsnrgpvrh rleltavllg tavlyiwglg
       61 asgwanafys aaaqagsqdw tawffgssda ansitvdkpp aalwitglsv rmfglsswsv
      121 lvpqalmgva tawimylair raalpatdnl rlahraglla aavlaltpva tlmfrfnnpd
      181 allvllmtaa gyavlrsiqd rklrwlilag vflgfgflak qlqvllvvpg fglaylvcay
      241 prpgrrvlhl laaggamvas agwwiaavel vpadlrpyig gsqnnsilel tfgynglgrl
      301 ngdetgsvgg ggngwgtpgl lrmfgtefgg qiawlipsal ilggallwlg rraprtdvvr
      361 asvivwgswl lvtglvfsym qgiihpyysv alapgiaglv glggvllwqr rsrlpvalll
      421 gaslvaagft afallgqapa flpwlrwvvv lgavvlaaav vvtgrlrqvw vtrttaglav
      481 avalaaplay svataatpht gaivsagpat agfgpgfgrn tsaqgirrpg tqqgtgqapg
      541 gqgfggggtn gggfagggqg aamggllgat tpssdlvsal kadadnytwa aavvgsnnaa
      601 gyqlaaglpv mavggfngtd psptlaqfqq lvadgkihyf iggrlmqgng gsdasseiaa
      661 wvaanyqatt iggttvydlg g
//
LOCUS       WP_284985458             743 aa            linear   BCT 25-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284985458
VERSION     WP_284985458.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Shan,L., Mathews,I.I. and Khosla,C.
  TITLE     Structural and mechanistic analysis of two prolyl endopeptidases:
            role of interdomain dynamics in catalysis and specificity
  JOURNAL   Proc Natl Acad Sci U S A 102 (10), 3599-3604 (2005)
   PUBMED   15738423
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Polgar,L.
  TITLE     The prolyl oligopeptidase family
  JOURNAL   Cell Mol Life Sci 59 (2), 349-362 (2002)
   PUBMED   11915948
REFERENCE   3  (residues 1 to 743)
  AUTHORS   Polgar,L.
  TITLE     A potential processing enzyme in prokaryotes: oligopeptidase B, a
            new type of serine peptidase
  JOURNAL   Proteins 28 (3), 375-379 (1997)
   PUBMED   9223183
REFERENCE   4  (residues 1 to 743)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 743)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..743
                     /product="prolyl oligopeptidase family serine peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=81569
     Region          16..739
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mttteadqtp lpgneaapgr prhaaevape ptdeniwled ihgeeqlawv reqnarteel
       61 ledaeysave agilevldst driamvskrg gfyynfwkdq ehpkglwrrt twdsyltdap
      121 ewdvlldvda laaaegvewv fhgagflrpa dgneyrlamv slspdggdad rhrefdvesr
      181 tfveggfdlp takgsvswld adtllvssta dglpattssy artgvklrrg ealadaerlf
      241 eipedhmlam vshdstpgfe rtfavdyidf ynrstwvlrd gswvaidvpt dvnisahrdw
      301 llfrpqkdwd vdgtvypags llgaafedyl agtrsltvlf apdehtslqs wswtrdylll
      361 nllrdvssei rvlnpavlds hgawastpld acpplhdvna yavddedpgs agndfwlvat
      421 gfttpttltr gtlspassqg edggvvsehs vvkrspsffn eadyevqqhf avsadgtkvp
      481 yfqvaskdlv ldgqnptqls gyggfeisrt paysgtigra wlerrtfgap sddgaaahsr
      541 ggvyvvanir gggeygpswh raalqenrhr ayedfaavak dlisrgvtsr rrlgcvggsn
      601 ggllvgnmlt qypelfgavs cgvplldmrr ytklsagysw iaeygdpdvp gqwefirtfs
      661 pyhllhdgve ypetfiwtat sddrvgpvqa rkmaarmqam gipnvwfhea legghagasd
      721 nrqaaalqar snhflwrsla gsn
//
LOCUS       WP_284985536             418 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284985536
VERSION     WP_284985536.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..418
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=44629
     Region          1..368
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mligvvaglv glslgvfgml afklserqrs ivdldvtepl lpegaaevla vvgrafvvvd
       61 aidgvvrasp aayayglvrg htvvhkqlld mtakvrrdgv ileeqyelpr gplgkgtivv
      121 qvraamlgwe yivlladdrt eitrteeirn dfvanvshel ktpvgaisll aealeaspdd
      181 eeavrrfakr mhkesgrlaa lvqdiielsr lqganvaqqg havdintvin eavdrsqlpa
      241 eskniqivvg ghseslvfgd rdllvtalrn lidnairysp entrvgvgvr tregvvaisv
      301 tdqgegltpe dqervferfy rvdaarsrht ggtglglsiv khvvsnhgge vtvwsqpgqg
      361 stftvrlpem egqdddaglp ptahelpaav aavephhasq nasektgtsg aqeqgasa
//
LOCUS       WP_284985553             160 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284985553
VERSION     WP_284985553.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..160
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17244
     Region          13..111
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mnrsidkeld gpracfiaag ldvlgerwal lalremslgv hrfdqiarnt gasrdiltgr
       61 lrtlesrgvi ervqysehpp ryeyhlttsg aevapilial aawssawmrd etprasyqhs
      121 cgadlqpvvs cavcgeefaq gslmlgplvs aagaesased
//
LOCUS       WP_284985633             358 aa            linear   BCT 25-DEC-2024
DEFINITION  LolA family protein [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284985633
VERSION     WP_284985633.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Tajima,T., Yokota,N., Matsuyama,S. and Tokuda,H.
  TITLE     Genetic analyses of the in vivo function of LolA, a periplasmic
            chaperone involved in the outer membrane localization of
            Escherichia coli lipoproteins
  JOURNAL   FEBS Lett 439 (1-2), 51-54 (1998)
   PUBMED   9849875
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..358
                     /product="LolA family protein"
                     /calculated_mol_wt=36608
     Region          31..258
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mtrakrrwlp alliplalvl avltgsvqag atvslppkta devlamiart qvrafsgtlq
       61 qtaelglpdi pssapgitpa agtaleflag shtarvfvgd ptkarlqvmd amaerdlivn
      121 gkdawfynsa dnsathlqvp ksgaptetlp nkptlptpea lasrflaavd agtevtvgea
      181 ssvagrnayr lnlapkdpgt lvasvsidvd setgfplgvh vqaknqadpa yslaftdlsf
      241 sapdpglfqf tppagstvtt kilparptpv pdadasakap sphgtrvsge gwgsivvlpa
      301 aavpagltsn pqisqmlqsv sggraltssl vsvlilddgr vlaglvpler lqsaaaaq
//
LOCUS       WP_284985774             796 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: RelA/SpoT family protein [Micrococcaceae].
ACCESSION   WP_284985774
VERSION     WP_284985774.1
KEYWORDS    RefSeq.
SOURCE      Micrococcaceae
  ORGANISM  Micrococcaceae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 796)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 796)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Micrococcaceae"
                     /db_xref="taxon:1268"
     Protein         1..796
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=88663
     Region          71..791
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 meeratsapp aggedgrkav avpttgvaer tagavpidsg vrptfpgrre rtrsrlarlt
       61 grgvapyspi lepllrtvra nnpkedfdli qrafavaers hqgqkrksgd pyithpvava
      121 tilaelgmtg ttlaaallhd tvedtpytln dltrdfgpev amlvdgvtkl dkvsfgeaaq
      181 setvrkmvva makdirvlmi kladrlhnar twrfvsaess srkaretlei faplahrlgm
      241 ntikweledl sfaalypkvy eeivrmvgdr tperekslsv irnqiaddlr tsrikatitg
      301 rpkhyysiyq kmivrdkdfd dindlmgvrv lvdsvrdcya algtlhsrwn plpgrfkdyi
      361 ampkfnmyqs lhttvigpgg kpveiqirth emhrraeygv aahwkykdqp nrtaqgpgsp
      421 rdgdmgwlrs lvdwqqetsd pgefldslry einarevfvf tpkgevmalp agstpvdfay
      481 avhtevghrt igarvngklv plnselnhgd wveiftskae gagpsqdwqh fvksararnk
      541 irqwftkerr eeaidrgkdm ltramrkqnl plqrlmthda lsavaeafhy vdisglyagv
      601 gdghtsaqsv meklvehlgg qetpdedlee vsiptqvaks kfsdsgvivr gvgdvwvkla
      661 rcctpvppdp ilgfvtrgsg vsvhrtdctn vsglrdqpdr ivevewaptq ssvflveiqv
      721 ealdrkslls dvtrilsenh vnilaasvht ssdrvaiskf afemgdpkyl hhvlnavrri
      781 dgvfdvyrtt gnrrrs
//
LOCUS       WP_284985793             439 aa            linear   BCT 25-DEC-2024
DEFINITION  HNH endonuclease [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284985793
VERSION     WP_284985793.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..439
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46658
     Region          45..356
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          345..399
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 meqvreqqag gvaiaapvpa asatlaagld rgpegtvsgd liqqlrvled mksaisslqa
       61 kiavafdlaq rqeqarngvp asergkgvaa qvalarresp nkgsrllgla kalvtempht
      121 maalesgqln ewratllvke taclsvehra avdeeiapdt gtfdgagdka itaavkaaay
      181 rrdpctvter aahaaseryv slrpapdtmt yltallpvaq gvavfaaltr hagtarsdgd
      241 trskgqvmad tlverttgna agytgidlql vmtdrallag dseparltgy givpagware
      301 llsnsqgsdg pgayyqdfnv wvrrlytapr tgellatdsr arffppgirr fietrdntcr
      361 tpycdapirh ldhvipwhsg gtttvdngtg lceacnhtke npgwtatpea gsrhtlrvnt
      421 ptghsyqsqa pplpgyrrt
//
LOCUS       WP_284985796             333 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284985796
VERSION     WP_284985796.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..333
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=35259
     Region          4..248
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mtfepilpwp vlvvagigil vltawtlipr qgtrlhgkvr paalrsaavv llliaamrpg
       61 lmggqsvgas seidvffvvd tstsmaaedh hgtetrlagv kqdvtavare lagakfslit
      121 fdskatvrmp ltqdatalqt amatlqpqra ryasgssvti aanllkdrld aaqkqhpgrp
      181 alvfyagdge ntsaetptpm datnvaggav lgygtgeggr mresadggag yvkdkgsnea
      241 kdavsridet qlgriadqlh vpyahrtgae ptsdilrgvq lgklnttagd gpgrvelywl
      301 falaafllam heplrhffel anlrrtlrne pdl
//
LOCUS       WP_284985804             376 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284985804
VERSION     WP_284985804.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19687404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..376
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=39654
     Region          13..375
                     /region_name="PRK15001"
                     /note="23S rRNA (guanine(1835)-N(2))-methyltransferase
                     RlmG"
                     /db_xref="CDD:184963"
     Region          198..375
                     /region_name="RsmC"
                     /note="16S rRNA G1207 methylase RsmC [Translation,
                     ribosomal structure and biogenesis]; COG2813"
                     /db_xref="CDD:442062"
ORIGIN      
        1 mtawelealf grlsrlpdve adnlqaydat drllletaeg ylgpdsqvvv igdrygaltl
       61 galsgpgvgh vrvnqdlftg raalqrnaaa agldglytph elgrellqda dlvllqlpks
      121 laeleeiada varfagpdav llaggrvkhm svgmnavlek yfsavqpqla rqksrilvak
      181 gprpvpdepp fpvveanpel gitvcahgav fsgarldigt ryllgfldri paarqvvdlg
      241 cgtgilatmy arhqpgarvi atdqsaaava satataaang laerisvihd damssleags
      301 vdlillnppf hlgasvhaga glklfeaaar vlapggelwt vynshlqyrp aleryvgptv
      361 eegrnpkftv trsrka
//
LOCUS       WP_284985920             362 aa            linear   BCT 25-DEC-2024
DEFINITION  lipid II:glycine glycyltransferase FemX [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284985920
VERSION     WP_284985920.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Rohrer,S. and Berger-Bachi,B.
  TITLE     FemABX peptidyl transferases: a link between branched-chain cell
            wall peptide formation and beta-lactam resistance in gram-positive
            cocci
  JOURNAL   Antimicrob Agents Chemother 47 (3), 837-846 (2003)
   PUBMED   12604510
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Hegde,S.S. and Shrader,T.E.
  TITLE     FemABX family members are novel nonribosomal peptidyltransferases
            and important pathogen-specific drug targets
  JOURNAL   J Biol Chem 276 (10), 6998-7003 (2001)
   PUBMED   11083873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006395
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..362
                     /product="lipid II:glycine glycyltransferase FemX"
                     /EC_number="2.3.2.-"
                     /calculated_mol_wt=40167
     Region          12..352
                     /region_name="FmhB"
                     /note="Lipid II:glycine glycyltransferase (Peptidoglycan
                     interpeptide bridge formation enzyme) [Cell
                     wall/membrane/envelope biogenesis]; COG2348"
                     /db_xref="CDD:441916"
ORIGIN      
        1 mdtatlreft arfataeetd nwdkhvtanp nggnmlqsda yaavkdgngw lvrrvvveta
       61 gyasynllle kkfpvlgrlw ylikgpdaas adeiepmlra vaalakeqkl nvfsikiepd
      121 vvespevvak lkasglvkap niqsndstal ldisapanev lrsissrarn avrraeregc
      181 evveaepgqd sykklyalmq ntmnakgamp lrsyeyyatf weefcsrgqg hfffvyedga
      241 psvgafviny gskatykdgg stqnrkqygd shlvqwaaiq rmqelgcvey dfcgtppaar
      301 ikdkshplyg lgsfktsftk tvtdfvgcyd lvlgpvrykl wlkgaekvfr rletmrtggq
      361 fy
//
LOCUS       WP_284985961             305 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. fls2-241-R2A-172].
ACCESSION   WP_284985961
VERSION     WP_284985961.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..305
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33927
     Region          10..295
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtdvenklii gtapdswgvw fpddpqqtpw erfldevaes gykwielgpy gylpndptrl
       61 aeelkqrdlq vtagtvftaf hrgagqydea weparkvael taamggehiv vipamwrddv
      121 tgeavengel tdeqwadlfa ghnrmgkvll edfglhqqfh shadshvgaq kdietllaat
      181 dpqylnlcld tghaeycgas sleliknypd rigylhlkqi npqvlaevne knmtwaaanl
      241 agvmteppng lpdlraviea vealnrpifg iveqdmypva fdvpmpiakr trnyllscgs
      301 rtrvq
//
LOCUS       WP_284986033             101 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix domain-containing protein [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284986033
VERSION     WP_284986033.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..101
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10951
     Region          20..98
                     /region_name="HTH_34"
                     /note="Winged helix DNA-binding domain; pfam13601"
                     /db_xref="CDD:463932"
ORIGIN      
        1 msipaehprh klnelvhspv rfsimaalvk aesldfkdlr daiqvsdsvl skqlaileka
       61 efvkikksfa gkmprtsasl taaghevwaa hlhtlreiag g
//
LOCUS       WP_284986021             250 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284986021
VERSION     WP_284986021.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 250)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   6  (residues 1 to 250)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   7  (residues 1 to 250)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001941
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..250
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28211
     Region          1..78
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
     Region          104..237
                     /region_name="SRPBCC_CalC_Aha1-like_GntR-HTH"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of an uncharacterized subgroup of CalC- and Aha1-like
                     proteins; some contain an N-terminal GntR family winged
                     HTH DNA-binding domain; cd08893"
                     /db_xref="CDD:176902"
     Site            order(105,107,109,118..120,122..123,128,137,144,146,148,
                     150,158,160..161,163,166,172,174..175,191..192,194,196,
                     206,208,210,212,218..224,226..228,231)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176902"
ORIGIN      
        1 mdtvfkalad ptrrelldel fredgqsasa lgarfemtrf giakhlklle daglvvtrrr
       61 greklhflnp vpirlihdrw vskfaepwaa alsdlksrle spmekifeiy ikttperlwe
      121 aitnseirsk yqfgntltsd ltpgsrfemr npkadaplge genievdppr rlvqtmtalw
      181 gedvkaegts ritweiepvg dschltvthd qlregandql yggwpmilsg lktwletget
      241 lttpgslmya
//
LOCUS       WP_284986036             110 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284986036
VERSION     WP_284986036.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 110)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 110)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..110
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12132
     Region          2..83
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlpdvfgala npsrrtilds llggpltage ltgqlelsrs sasehlsvlk eaglireerq
       61 grhrlyhlqa aglqevsgwl khyeqywnhr ldaladlldg qsteqentdd
//
LOCUS       WP_284986138             362 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284986138
VERSION     WP_284986138.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 362)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..362
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39074
     Region          46..334
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 meskrqvtve psplhdqays erphdgaaln ghkpqvmdse rfhdaseril asigqvidgk
       61 adaaklaltv llaqghllle dvpgvgktll aktlartvdc tvsriqftpd llpsdvtgvs
      121 iynqssrqfe frpgavfani vigdeinras aktqsallec meehqvtvdg rsyqlglpfm
      181 vvatqnpiem egtyplpeaq rdrfmarism gypdkdaeie mlethqassp lvnvtpvvta
      241 nevaamiaav qqvyvstaik eytvaigrat rdsarlrlga sprsllqllr aakataaldg
      301 rdfvlpddvl dvaesvlahr iildrkaass gdtpqsilrg ilaslpvaqe tpgqgrrdrh
      361 ta
//
LOCUS       WP_284986251             446 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284986251
VERSION     WP_284986251.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 446)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..446
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47570
     Region          35..441
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(145,147,296,298,329..331,372)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mkktlgvaaa aaaialtlsa cggsspasse akgdinywlw danqlpayqq caddftkanp
       61 dikikitqrg wddywttltn gfvagtapdv ftnhlskype yaakkqllsl deavekdgik
      121 ldaytkglpe lwvgqdgkry glpkdwdtvg lfynkamtda agitaeqman lewnpkdggs
      181 yektiahltv dkngkrgdep gfdknnvaty glgltgsgag qgqtewsflt attgwtatdk
      241 npwgtkfnyd dprfqetiaw waglvdkgym pklettvgas mpdsfgagka aintngdwli
      301 gqyqtykgie tafaptpkgt dgkrasmfng ladsvwagtk npgasikwve ylgstacqdv
      361 vaskavvfpa iassaeiaak afadkgtdvs aftthvkdgt tflfpiadka akvdgimkpa
      421 mdavlagkkp asslteannq vnnlfk
//
LOCUS       WP_284986280             332 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Arthrobacter
            sp. fls2-241-R2A-172].
ACCESSION   WP_284986280
VERSION     WP_284986280.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..332
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=35011
     Region          3..294
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 msrifitggs grlgrsvvag lagaghtvis vdrdavpaeh lpagaeqyta dllapgeaer
       61 ligetapdav ihlaaiavpf sapedvifst ntrlayavis aatdagvpki vtassptalg
      121 ygspagwlpp sfpldeqtpp kpwnayalsk liaeqtvqmf aaaqgekiry aafrpcyvis
      181 peewegaltq qghtvrerld npafsapaqf nyvdardvad fldvlldkmd sipngevffv
      241 gakdalatap laelfprflp gsgpltehlt gtspafsidk arellgwepe rtwrteltpp
      301 yegpdtaase qaalndeiha glvpagatke tp
//
LOCUS       WP_284986282             369 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284986282
VERSION     WP_284986282.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..369
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39124
     Region          <129..348
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mttpiqsttp ttaltapgnv adravkrrrv ldildaagrd slllttntal twyldgsrmh
       61 islagdpvaa llvdrsgdhl vtfnneagri adeelpegvs lstvpwygql haaaaglaid
      121 gnplveaavt telraarqql lpaesaryaa lsadaaaamt evltaatpqt tefqlvsala
      181 arivaagaep lvllcngadr sdfrhplath spigrramav vcarrnglva nvtrwvafda
      241 gtaeeldaea riaaveadif ratvpgaqln evfaeiktay arhgfgddqw tlhhqggpag
      301 yagrdprvta dvtdtivlnq pftwnptgpg vkiedtvllt dsglrvltvd drwptaevdg
      361 rrrpltlrp
//
LOCUS       WP_284986314             408 aa            linear   BCT 25-DEC-2024
DEFINITION  thiolase family protein [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284986314
VERSION     WP_284986314.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 408)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..408
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41944
     Region          1..406
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mveaflvgga rtpvgrygga lssvrpddla alvvreavar agvdpdside vilgnangag
       61 eenrnvarma tilaglplhi pgitvnrlca sglsaiimas qmiksgaadi vvaggvesms
      121 rapwvqekpa tafakpgqif dtsigwrftn plftkgelsr dgkmtysmpe taeevarvdn
      181 isredadafa vrsheralaa iaggrfkdei vpvtvksrks etvvdtdegp rlgttmdvla
      241 glrpvvpggs vvtagnsstl ndgasaiiva seeaikkfgl tprarivdga sagcepeimg
      301 igpvpatqki lartgltvdk lgavelneaf atqslasmrr lglnpdivnn dggaislghp
      361 lgssgsriav tllgrmerel asatgpklgl atmcigvgqg tamllegv
//
LOCUS       WP_284986432             176 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284986432
VERSION     WP_284986432.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..176
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19283
     Region          4..109
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mplrsdwsar tcslargldv lgdpwgslvl reiffgngrf daikrrleva dnvlskrlaw
       61 lvesgllvqr pyqdgartrq eyvltpkged alpvlnaiii waekhldapn evshmrviht
      121 dcgqatssad tcahcgvalt aantswhsyk rsdhplplav aprenhapvl tseipa
//
LOCUS       WP_284986477             421 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Escherichia coli].
ACCESSION   WP_284986477
VERSION     WP_284986477.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 421)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 421)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 421)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 421)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..421
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48289
     Region          1..416
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 mlieftvqny ksisekqtls lvasklndlp nnlfsidepk slellksavi ygpnaagksn
       61 iinaittmae livrsatgyk sgdklditpf rldskkinqp sefeinfise giryqygfsa
      121 tedfihdewl fafpkgrpqk wflrlwdeek qthewelgps ltgekqtwlk strpnalfls
      181 tavqlnsvql kpvydwfyyk vkfteltgwd sdysakqcln dkkdeilnfl kaadvgiddi
      241 hvtkekfnpn alpddmpaai kelviknmqg keeyviktlh nnedgepipf dlkdeshgtr
      301 kifsfagpls hsletgnilf idelndnlhp klvefivglf hdkninknga qliftthets
      361 ilnqdvfrrd qiwfvekdns kqtnlfplmd fsprkgrenl easyldgryg alpligkwer
      421 y
//
LOCUS       WP_284986625             367 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284986625
VERSION     WP_284986625.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 367)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..367
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=36974
     Region          25..365
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mstlhkapae vapnankhph llplrrvlsp tfflglalvv mfavyvllgs ytvtipdfft
       61 ivinhltgge kipgasfivm ehklpravvg tmigiafgla galfqtmlrn plaspdiigi
      121 sygasaaavt aivifgasga vvswaalgga lgvaaiiyai srgtgsgagg gsrgnaagnr
      181 lilagvgiaa alhavvnflm tradirtaad aliwlngsln sstwdragvl avsllvlipa
      241 vialagplri lelgddaaag lgikvnatrl glvltavgfa avataaagpv afvaflagpi
      301 srrvvrkpsl pasaltgali vlladffasn iapvildgtv lpvgvitgal gapfllwllv
      361 tsnrkea
//
LOCUS       WP_284986704             404 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284986704
VERSION     WP_284986704.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..404
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44014
     Region          87..399
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mqqdveqive rvalklgrgl sledldgvll ayssnqshad rvrvnfllsk rvptdvsawq
       61 lshgistavr pvvvpandql gmlgrvcvpl lvrgfrvgyl wvqldveeqs atailaelpg
      121 vrdeldllag llldsntaes efrrrreqef lsacngesna vaavagwkei qgrgpwqlvt
      181 ildpdgagsa vdpiaatlth rsaalqstig vnaalfsagt ethsvvlfre sggradhaqv
      241 lvhyqlelak ragrtvdrvi lgisepfqvi rqissayrqs kvaaqaaavd lplgelvesr
      301 avgvyqlfdr llapggwddt gsvhyrtled qdrngellpv lellydndgs vqdvaaklhl
      361 hrssiynrlg rirqligadp lsgairlelh aalkahrwar rpri
//
LOCUS       WP_284986839             705 aa            linear   BCT 25-DEC-2024
DEFINITION  S9 family peptidase [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284986839
VERSION     WP_284986839.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18486225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..705
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=76099
     Region          270..>395
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          443..692
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mlnqimdsad ihapghqpet pfhdldhyls iprvgglsls pdgtrlvttv ttlngkgtef
       61 atalweidpt gqrparritr sskgeagavf astgdlyfts arpdpdnpda dpvsalwllp
      121 adggearvvh srsgginsvm aakdvdatfi taevlagssd eendearrka rkdnkvsail
      181 hsgypvrywd adlgpaeprl faveqgedke pgkpstvdaa pslklrnltp gvggslreak
      241 svvspdgkti ytsltkalak adsrevlaav dvatgnvkvl ldhegmsyfp gpvspdgrtl
      301 vvesesdttp tqapqvklhl lnvangette leplahhwdr watalawlpd asailakadd
      361 dgaspvfrig vadggvtrvt mdsaaysdvv vspdgataya lrssyefpae avridlatga
      421 vvrlpapaer pvyrgrlerv ettaedgarv paylalpega sadapaplll wihggplgsw
      481 nawtwrwnpw llvakgyavl lpdpalstgy gqefiqrgwg ewgkkpftdl maitdavver
      541 pdidesrtaa mggsfggyma nwvagqtdrf kaivthaslw aldqfgpttd aaqywlkemt
      601 aemaiqnsph lnvgniktpm llihgdkdyr vpigeglrlw yellsssqlp addngqsphr
      661 flyfpdenhw vlqpqhakvw ygvvehflak qllgedvelp eelgv
//
LOCUS       WP_284986851             375 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284986851
VERSION     WP_284986851.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..375
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40860
     Region          24..216
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 maaakgfsas krflrarvrt glvrsrsslt paiqmtvcav gayafaeyvl ghqgplfaat
       61 sslialgfsr dprlrrviev glgctlgivv gdlllhwlga giwqaavvll fsillarfld
      121 sgtifttqlg lqsllvvllp apaggpftrs idavvggvca llvtilvpkd prreprkdvq
      181 qilhelaevl recakamies dstmawhali rgrncqplvd rmrqtlrasg evatlapahr
      241 rhrdelasle hsleyidlal rnsrvfarrl tsainhaals deaidsisev lqetaaaide
      301 mtiglaeqse gtrrvhlrra rndlsdiaar lhpkmldvqr legetvvmlf rplmvdllea
      361 sgmepeeart vlppl
//
LOCUS       WP_284986864             325 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284986864
VERSION     WP_284986864.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..325
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34255
     Region          9..325
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mvktgasvew arqqvdlgrv plavlgiass ngiedvvafg sdggrqatvd dhfalfsvsk
       61 pisalavmrq velgklslgn alstavpgfg agrtdtvtle hllshrsgit dpelddgvpl
      121 rdaltsagqt fyagslvqyc niafegaaam aewadgrpfe eqvlslaadt gasgltfstd
      181 cnphtvhgte aeglnaeamf qqrhpgaglf gtatdllnlg tellrdsgka vqpatlaamr
      241 rprttelshi ttrpkplrht glgfqlpane seliargiyg hpgwsgteww mfpeqdrcvv
      301 fltnvldtpd lgvdttalfn avaas
//
LOCUS       WP_284986877             534 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284986877
VERSION     WP_284986877.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..534
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55884
     Region          6..507
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mndpvdvaii gsginslvaa aelaldgkrv cviersdrlg gfidssertl pgfihdtfss
       61 whplfvsgga yatlgkelqa rgleycnttg pvtasvatdp atgahrvvia hrdpaetaaa
      121 fkvasdqaay samlddlgsn agtvfgafga elrsfkevak iafgtlrrgr lagteaflrd
      181 svmsgrnyvr srfdgwetdq lwspwllhag lgpdqatggv mlpvmamsmh gfglpvvkgg
      241 asrfvaafes llkdngvqim lgteaeevlv gagsvkgvrt sngvvpagtv lanvspqaly
      301 tqllrrppaa aaaaaekyqn grgamqihla ldkpvewlda rlnkvplvhl sngsdstgia
      361 caqaeagllp aeptvvvgqq cvldpsrape gkatlwlqlq evpfspvgda agqlatadgw
      421 tdelkqayld rvldrlepfa pgtrdtvlas dilaptdlaa tnpnavkgdp yggsaelfqn
      481 llwrpfpaaa ghqtaveglw higasthpgp glsggsghlv aqklikkalk prkr
//
LOCUS       WP_284986893             453 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284986893
VERSION     WP_284986893.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..453
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=48987
     Region          20..359
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mdrarqthpa tglyeavrrd paidlvrftc lllvvaahcm mvspvlhkdg tvethnvlmd
       61 qswftpvlwl lmivplffvm ggvtglqswr rlvarggtgf dfaqlrllrl vrpamallal
      121 mwgglwvall mgvhpqviql mtagaamplw flaafltaql siplmarlhq kspfvvfgvl
      181 vaaiitvdsl rgaipvlaft nmifvwcavq qlgflmadgf fkrrsrtwlv gavvtsnlll
      241 glvtgvavyp gnmvvninpp nlcllllgis qtatlqllqp avrwvasarw vqtvmalagr
      301 rsmtiylwhl pllvgfsgll lltdlpipda stsdwwwari pvfaavvtll vpvvwlfgrl
      361 eerptaasha rgpsrvavvt aavvvfvpva daafngltls llgggaacfa lavlllgrvp
      421 tpqqaepean aterseaqap tlpapdlsan lep
//
LOCUS       WP_284987040             432 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284987040
VERSION     WP_284987040.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..432
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45877
     Region          170..429
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mdflsdvslv dgpfmwfcvg fgavgglyll wrrqrswpvv vvaclllsvg vvalvhwili
       61 dltasfsenl pfetlvwsvl avtalllsia rlprngaksr llgcvamlgv vllcvaqvnl
      121 yfglnktvad llgtavariq plepslqrsa gsvpgpslsa wkapdslpgg gvlrkahipg
      181 tasgfdarda yiylppayls sprpslpvfi lyagqpggpt dwlsggrlra lldrfaadhg
      241 glapvtvvvd pngsanantm cmdsniahad tylsqdvpaw isstldvstd hrqwavggfs
      301 fggtcalqmg tlhpnlfpsv vafsaerepa lakdrgktia dsfggdveaf esrtplvlma
      361 errfsgsgvy lvsgeadhef taymhelada arnsgfdthe qsiahaghsw daviegmpga
      421 lgflakrwgm pe
//
LOCUS       WP_284987102             257 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284987102
VERSION     WP_284987102.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..257
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27949
     Region          8..224
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mkesaksrat fillaglarp lmnilmnkkw egleklpqgg fiavpnhcte idpivvghmv
       61 ynqkrpphfl akaglfkvpv lgallqatkq ipverstaga nrslqiakev vdaggaiiiy
      121 pegtltrdpd lwpmkghtga arlalqtgap vvpiahwgah evfpryakrf hvfprktarv
      181 lvgapvdlsa fadrpldrat lseatdvimd aitslletlr getapkerwd pamhkqskhg
      241 rfvergstgt pepedge
//
LOCUS       WP_284987143             662 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-N-acetylhexosaminidase family protein [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284987143
VERSION     WP_284987143.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 662)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 662)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 662)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 662)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 662)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..662
                     /product="beta-N-acetylhexosaminidase family protein"
                     /calculated_mol_wt=71090
     Region          53..197
                     /region_name="Glyco_hydro_20b"
                     /note="Glycosyl hydrolase family 20, domain 2; cl03741"
                     /db_xref="CDD:446174"
     Region          203..514
                     /region_name="NAGidase"
                     /note="beta-N-acetylglucosaminidase; pfam07555"
                     /db_xref="CDD:429533"
ORIGIN      
        1 mnnapnsaga rrrrsllili aaaalaaamv msgwfviahd rpdgkggdvg avpdifpvpq
       61 hthvgtggsi plsghvyvva segtdqasid alvelvsgag gtaetvttls tpregssavr
      121 agtdsagalr alhldgdpei rtalerpegy aiatgqidgi ptavlagrda dgifhgvqsl
      181 rqllkdgsla avrisdwplm etrgviegfy gtpwshqarl dvikfagrqk mntyiyspkd
      241 dpllrerwrd lysnqelgel relidaaaas hirftyalsp gidvcysrts dlndaltkle
      301 slyslgvrsf viplddiatk vqcaedvkef gsgqanlaka qasfindvne kfivgkqgvq
      361 pletvptfyn gsdstaykre lgkalnpdiv vqwtgedvvs hritkesvdt arrsygtssa
      421 lrtlviwdny pvndfsqdhl fmapvlgrda dlytsirgiv tnpmiepyls lpaifnyadl
      481 swngpaydaa ksmnaalslv agpdpavqeg vrafvdlnqd wqddelspsa pelrrdidrf
      541 wtdydagrap sgglkarsal lqrlpellpr maqrgfaqda aawvaaaaey grgveaaldm
      601 leatkrgdte aaatarknve talasaeekr qptlelgvvt pvlggselks fleqalqrvp
      661 ag
//
LOCUS       WP_284987153             562 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284987153
VERSION     WP_284987153.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 562)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..562
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=59671
     Region          20..259
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mpapetpdgk dtpaerplim ryaarsdvgr irsknddsay vgrhlavvad gmgghaggdv
       61 asastvldmi hldhdnypeg adtvladeiq tansllselv hqnpklsgmg ttvtallled
      121 rklhfahigd srayrlrnkk feqvsvdhtf vqrlidegrl rpeeaethph knvlmrvlgd
      181 vdaspeldld vldvepgerw llcsdglnyv aghvvermvr etkdlrecad ilvdltleag
      241 apdnvtvvml eiaeetdddv staavdivpa aalassddea dsltaskspd gpaaskaaee
      301 shdssaakaa rdaepgssfs agdpttmdkd aessessdsg eppattdphl gehlsaevlr
      361 eelasrphel vgaaataaet gsiptvagrt varraatvlt hkaeqdrada eepprrrvrw
      421 lmpavaavvv lgvvvglwlg yawtqtryyv geydqrvaif ngisqrlgpi qlsrleavtd
      481 irvdslpeyg qqsvrqtvpa gdlhdaqgiv enlkntgsas ancptkgpkp tpsptisvpv
      541 pstaavatpt pspiptscea ak
//
LOCUS       WP_284987156             302 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284987156
VERSION     WP_284987156.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..302
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31319
     Region          12..290
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mrdrlsgtig glppwsmava ammavqlsna lsvavihqvg pagtawlrmc fgvvflwlvs
       61 rpairslrrr dlpalialgv vtgfmttffl aaveriplgt avaieflgpl tvaglmskrr
      121 kaliwpllaf mgvvlltepw hgtidmagvg falaagtcwg lynvltqhvg drfggisgls
      181 ltipvaalat lpiglpqvlg gslewwvlpv aagialitpv iafglemlal rrmthtafgt
      241 llsiepafgv ligvlvlaqa ptvlqlvgva lvvvagtaaq qggrrsptpa mttdvpaspa
      301 ap
//
LOCUS       WP_284987246             267 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284987246
VERSION     WP_284987246.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..267
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28700
     Region          18..249
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mnmlpdfspf ssqwngigpr vgvvmshgft gsphsvrpwa ehlaaagyav rlpllpghgt
       61 twqdmatrsw rewhravdda ylelaaecdy vfaaglsmgg tlalriaatr pvagtivvnp
      121 glvlddprav vvaalkyvvk stpaiandil kpdqdegayt rtpvaaahql kkmyrdtaal
      181 lprinapvrv ykstvdnvis kaslellrsr ssapvdihyl ansyhvatld ndapeifqgt
      241 vdfiqktvan laghgaspek dtaheqa
//
LOCUS       WP_284987269             536 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284987269
VERSION     WP_284987269.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..536
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=55837
     Region          15..492
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 metlnsadkp pnmpgyrvsr qlgtgasstv wlarrngdge rfaikcvkaa dhgpmeaqgi
       61 dggvsreagi lfgvkhkhlv gihdvvqfev dghgaqgivm dyaaggslan llsgrgrlrv
      121 gevvtvlgpl aqaldylhsq glvhgdvapg nvlftaegmp lladfgltsr vgdadaqhgl
      181 dvgtpgfidp vgvvsgghdq galrperdly slaavgwfcl tgsvpglapd rpplsfvadd
      241 vprsiagale aaldpdprmr psarefstai frsaapeavd lagavhasvi pelltrrqal
      301 drkphqravk fgklpslrpt akaatrrtpr trrtpkprkn mayvraavvl gigvlvgaaa
      361 wglwaqgkps ttpsgagnga rvssegpptd ipessslpeg lkqelrsddl avvvpalaav
      421 rdvalregpv ellavinapg spaeaadhqv adhlrtagtv faglattvta vtieqppqpd
      481 hamvglvaat sayeerrssg svvrsepagt pqhlrlhler sdgrwqivei lagttg
//
LOCUS       WP_284987314             132 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284987314
VERSION     WP_284987314.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..132
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14459
     Region          9..112
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 metnslpani ldpncpsrvi fqrigdkwas lviqvlgagp vrfselrkmv nvvtpkvltq
       61 tlralerdgl itrtvhaqvp prvdyeltam gesllqplsl lrewaeshvp tileareayd
      121 daqdsavlgt at
//
LOCUS       WP_284987432             134 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284987432
VERSION     WP_284987432.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..134
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14773
     Region          9..130
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 merfpeacve rtvewvdtda sghqhnsail rwveaaeael frlldlpeyf psaprvqqvi
       61 nykaklwfgq ritatvkisa lgrtsltmaf evtsdggdva afgtvttvhv peggtsaepw
      121 pehfvrrita rdgt
//
LOCUS       WP_284987526             241 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284987526
VERSION     WP_284987526.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 241)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 241)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..241
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26346
     Region          10..95
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 matdvlpage gfaslaalfa drtratfcla lldrrawtas elanyaqvpk ssatehlnkl
       61 igagilteir qgrhryvrle dariaeliet mashvepvps nrrsytsitr dqalrrartc
      121 ydhlagdlgv slmnalvarn iinldsgvql tpkgeqdlar agisierqgt rplirtcldw
      181 tgrqyhaagl vggaicrhal asgwvlptpq sralkitdlg vmemkrhfgl elargerrlq
      241 g
//
LOCUS       WP_284987583             121 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: DMT family transporter [Micrococcaceae].
ACCESSION   WP_284987583
VERSION     WP_284987583.1
KEYWORDS    RefSeq.
SOURCE      Micrococcaceae
  ORGANISM  Micrococcaceae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Micrococcaceae"
                     /db_xref="taxon:1268"
     Protein         1..121
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12224
     Region          11..109
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mtntkntgif wgillasail eavwatalgl sngftqlapt ivfavtalls mlglgfavkr
       61 iplgtayavw vgigaaltvg wamitgvesa splkllfiag ivgcaaglka lptekpvakp
      121 e
//
LOCUS       WP_284987676             198 aa            linear   BCT 25-DEC-2024
DEFINITION  dTMP kinase [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284987676
VERSION     WP_284987676.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Cui,Q., Shin,W.S., Luo,Y., Tian,J., Cui,H. and Yin,D.
  TITLE     Thymidylate kinase: an old topic brings new perspectives
  JOURNAL   Curr Med Chem 20 (10), 1286-1305 (2013)
   PUBMED   23394555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..198
                     /product="dTMP kinase"
                     /EC_number="2.7.4.9"
                     /GO_function="GO:0004798 - thymidylate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006233 - dTDP biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=21685
     Region          1..194
                     /region_name="Tmk"
                     /note="Thymidylate kinase [Nucleotide transport and
                     metabolism]; COG0125"
                     /db_xref="CDD:439895"
ORIGIN      
        1 mlivltgidg sgkttaaral vdsahaegrn alllsnhagr rhlsllsarl nwhlqpwfad
       61 fvetgirvfn vlvnharass aarrfdglvv mdrhlhcqla lrqanglgrg rlipwllgkl
      121 papdlmihfd vdprvahdrv margtdkeil adlvafraay rslpefddfv vvdangtped
      181 vlahlnrama avepawls
//
LOCUS       WP_284987692             538 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284987692
VERSION     WP_284987692.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..538
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57555
     Region          47..>281
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mltsstitpg hptnpqdqsg tpmlrvrirk eswtsklarr pvwiaglvgl lalvfrvtgv
       61 erandvfide vtyadlarql adgqvpstsg spfflhppgs yalnalviri mgldghpmdl
      121 alqlrwfnaf lgvatvvvcf mlvrrlvglg pafvagiila sdpfvlrmdg rlmmetptgl
      181 avlsgwllvl llikgergrt rlwleiaagl vfglaivmkd mtaiftvvpl lagvpwrrtv
      241 ptltalrivc csvvpyliyl slitaggllp qfleqksvgv lrmagvvqmt gfnavpgvgl
      301 ldrlmvllgr fgtsyvllgl sivagglaaa splverriig lfslitgmvg vysvffgaae
      361 eqfgycvvla alvstpvatv mvvawrprlr savtavvilm tglglflgvq arsvvddglv
      421 rarafmttel ppsaivglts vtgefallph egwevlpslq slhdrnaeyv ltqgrqlgeg
      481 ygyaspafld wleknaqpvf tfsgptsgnt vvwkldrdkl daavaggmtl ppvtggyp
//
LOCUS       WP_284987774             447 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284987774
VERSION     WP_284987774.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..447
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47840
     Region          27..443
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtvvplpleq tlpggelihg aeggsvvrrs vlpggvrvlt eampgqrsat igfwvavgsr
       61 deadgqhgst hflehllfkg tkrrtaleia safdevgges naatakestc yfarvldtdl
      121 pmaidviadm itgavldpae leqerdvile eiamdsddpt dvahekfvaa vlgshplarp
      181 iggtpdaika vardsvwehy qryyrpeelv itaaggldhd vvcelvldal kaagwqldsg
      241 aapverrgte ravitgnagl hvvkrpveqa niimgcptiv atddrrfvms vlnavlgggm
      301 ssrlfqeire krglvystys ftaayadagy fgmyagctps kvrqvlellg veldklakdg
      361 iteeelrkav gqlsggivla ledtgsrmsr lgraelvsge fqdidetlar iqavtvddvq
      421 elarelaaap rtitvvgpfe etetfgl
//
LOCUS       WP_284987805             288 aa            linear   BCT 25-DEC-2024
DEFINITION  trypsin-like serine peptidase [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284987805
VERSION     WP_284987805.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..288
                     /product="trypsin-like serine peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=29341
     Region          98..284
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mkkqnvavlv gaavmaltss lggsamasep tpqpasaevq pvshtvdksq tsgsaaspla
       61 dryslaaptk nggastdsvi gadgrvritn ttaapnrsiv qiefnggyic sgslisddtv
      121 ltaghcvhtg gtgstadysw gvkvapgrng stdpygtcga tqlltdqrwi dsantnadwg
      181 vikldctign ttgwlnytgt taslngttat vrgypgdkaf gtmwsmtgti dssatekvyy
      241 kmdtfggqsg apvynssnti vaihtnggst nsgtritptl anyltsvk
//
LOCUS       WP_284987858             140 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284987858
VERSION     WP_284987858.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 140)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..140
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15638
     Region          24..109
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtlysnqtys kttklyndkv mvlmvdelsa vfaaladptr railqrladg daqvsdlaap
       61 frisqpaisr hlkvlenagl isrnrvatar fshlepdrlk easeymeryk kfwgesfdkl
      121 dgalasfqrd tpptgkgrdv
//
LOCUS       WP_284987778             406 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Arthrobacter sp. fls2-241-R2A-172].
ACCESSION   WP_284987778
VERSION     WP_284987778.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..406
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42616
     Region          146..386
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mggselwtil awvllwavli gattlvllrl lrrasvltqi flvvvatvav lvagmvsafn
       61 amfisardle vmwyilatas avavalslml gagvsrnaar lvdaarrlgr getldntmea
      121 rrgrapavts elaelaqele assrslaesr ereaaietar relvswishd lrtplasmra
      181 mtealedgma advpgyyrki igqteqmtam vndllelski qagslqlrae pldlydlvsd
      241 alsdlaplaa krgikldggg drecmavadg pslarairni llnaiiysrp dsdvhvsvgr
      301 dngnavvavq dqcggipdad lphlfetgwq knpargttae lqgsysgagi glsmvagivk
      361 ahggtvgvtn ldggcrfals lpagstrdgs psastltsvd nrpgga
//
LOCUS       WP_284987945             290 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Arthrobacter
            sp. fls2-241-R2A-172].
ACCESSION   WP_284987945
VERSION     WP_284987945.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..290
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=31998
     Region          2..279
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mriavtggsg klgrsvvrrl tqdghqvlnl dragmrgqsy vnvdlrnygq vldvvlgldd
       61 rhdgfdaivh laaipapgla pdaaifennm vstynvfqaa rragikkvvy assetvlglp
      121 fdvdppyipv deeyaarpes tyslvkhlee qmaiqltrwd pdlsitalrf snvmdpedye
      181 afpsfdsdat lrkwnlwgyi dardgalavv ralehaqpgf etfiiaasdt vmsrssaela
      241 aevfpgvevv kelgehetml sidkarrllg fepvhswrdv hsnrttpted
//
LOCUS       WP_284987960             637 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FAD/NAD(P)-binding protein [Micrococcaceae].
ACCESSION   WP_284987960
VERSION     WP_284987960.1
KEYWORDS    RefSeq.
SOURCE      Micrococcaceae
  ORGANISM  Micrococcaceae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 637)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 637)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11816065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Micrococcaceae"
                     /db_xref="taxon:1268"
     Protein         1..637
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=68824
     Region          1..631
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
     Region          9..191
                     /region_name="NAD_binding_9"
                     /note="FAD-NAD(P)-binding; pfam13454"
                     /db_xref="CDD:433222"
ORIGIN      
        1 mpsrvpalaf igggprtagv lerlaanrpa lfdgpldihv iephqpgsgr iwrydqdpgl
       61 llnstaadvt mftdasvacd gpsvdgpgla twaagvldgt irdvpaleph llaqlrsltp
      121 ssfptrqlqs kylewffrra vsslgtevtv tvhqdtatav erasddgshh vklasgagva
      181 advvvyalgh tdslldpesa rlsdfaathg gfhappsytt dvdysaveag qdvivsgmgl
      241 afvdllvllf egrggrfeer pdgeldyvps gaeprvwags rrgvpyhski sselrgepia
      301 rpryftaeav qsllaehqel dfrtqlwpli akdagyayyr elftgypsrv lgtwesfeah
      361 fdavqwyssa reelvavsvp dpalrldlek ldhplsgcaf adhdavqrsv aayiqndlnl
      421 rtssdhsetl alftallfvy mdlgrlvpqe rlnarsqqai hgwwhgffsf vdsgppshrl
      481 remlalhrag llkflgpgmw vradeslgrf vagsfqspvv vdssayiear lpsasversa
      541 npallhlhda gwgteqrllt segthstgkl lvsgnhevls pvgipqkglf avgpwtsgwg
      601 agafarpntn aapfrendal arrilsavaa vpalqpn
//
LOCUS       WP_284987968             398 aa            linear   BCT 25-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Arthrobacter sp.
            fls2-241-R2A-172].
ACCESSION   WP_284987968
VERSION     WP_284987968.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. fls2-241-R2A-172
  ORGANISM  Arthrobacter sp. fls2-241-R2A-172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Pereira,J. and Lupas,A.N.
  TITLE     The VCBS superfamily forms a third supercluster of beta-propellers
            that includes tachylectin and integrins
  JOURNAL   Bioinformatics 36 (24), 5618-5622 (2021)
   PUBMED   33416871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Arthrobacter sp. fls2-241-R2A-172"
                     /db_xref="taxon:3040325"
     Protein         1..398
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=42217
     Region          200..261
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          250..310
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mgiirartvr fasaavlgla agllgtglse aasqptpsid gvpyvgaemr rqydysysgc
       61 rnpdgsgdgi tlewlrdgvp lpqerqgdvl kilpedrdgr islrvhpltp gqagcptgtq
      121 lsaetlpvka ssramgwtgr gnfeplartt dgrlvlyprt ytyykgmceg pcpayrgswd
      181 epqqvgqgwn vfdivfspgd fdgdgfndll grdaagklfl ypgdgeggwl prrqvgqgwg
      241 vfntivgpgd fngdgtndvl ardtggglfl ypgdgeggwl apeqvgwgwq imnkiitggd
      301 mnadgavdvf gldqygqlyq ypsdgeggwe qpsqvgvgwe sftvvaglgs sghskyneis
      361 avdadgnllg yttgastgal ygpygpigrg wnvfkell
//
LOCUS       WP_284988165             113 aa            linear   BCT 25-DEC-2024
DEFINITION  YegP family protein [Arthrobacter sp. efr-133-TYG-120].
ACCESSION   WP_284988165
VERSION     WP_284988165.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..113
                     /product="YegP family protein"
                     /calculated_mol_wt=12106
     Region          2..58
                     /region_name="YegP"
                     /note="Uncharacterized conserved protein YegP, UPF0339
                     family [Function unknown]; COG3422"
                     /db_xref="CDD:442648"
ORIGIN      
        1 magkfelfvd areryrfrlk aadgtvmavs kdfetkraav vgirevraca gmglitdlcp
       61 gqpaapgpas gisaqalpea rpprgrswlg rtsiarkrgn kaltskrwpn lvk
//
LOCUS       WP_284988176             247 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Arthrobacter sp. efr-133-TYG-120].
ACCESSION   WP_284988176
VERSION     WP_284988176.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..247
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26544
     Region          14..228
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mlasatqpfv kaelkaalwd mdgtlvdtep ywiaaertlv esyggawshe qamqlvgqsl
       61 mhsagilqka gvnlekreiv dslsaqvidr lrvevpwrpg akelldelyq sgvrcalvtm
      121 segpmvrevv anlpkpyfef litgdtvsqg kphpeaylaa verlrdtdpa ltvdhcvale
      181 dsvpgvasai asgvvtvgip hqmalpedar ratwdtlqgr rvsdlealvs arasatmpaa
      241 aflgqan
//
LOCUS       WP_284988292             259 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase
            [Arthrobacter].
ACCESSION   WP_284988292
VERSION     WP_284988292.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter
  ORGANISM  Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Arthrobacter"
                     /db_xref="taxon:1663"
     Protein         1..259
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26612
     Region          1..254
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mnisaktali tgastgigsv farrlaaega rlilvarsqd kldalaaelr ghgtevtvla
       61 mdlslpdsak elqlatdslg ltvdilvnna gfgthgqvvq adadryaeqi qlncstlvgt
      121 strylpgmae rgsgaiinia staafqpiph mavygatkaf vlsftqalwa etqgtgvkvl
      181 avcpgatdtp ffdiageaaa agslrtpeqv vdtamsairg nkpsvvdgrl nsfvarvavk
      241 llpeklviaa agravrpan
//
LOCUS       WP_284988352             258 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: lysophospholipid acyltransferase family protein
            [Arthrobacter].
ACCESSION   WP_284988352
VERSION     WP_284988352.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter
  ORGANISM  Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Arthrobacter"
                     /db_xref="taxon:1663"
     Protein         1..258
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27737
     Region          8..224
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mkesaqsram favlaglarp lmnvlmakkw egtdklpagg fiaapnhcte idpivvghml
       61 ynmkrpphfl akaglfkapv lgsllratnq ipversttga nrslqaaqev vdaggaiiiy
      121 pegtltrdpd lwpmkghtga arlaiqtgap vvpiahwgah evfpryakrl hvfprktsri
      181 lvgdpvdlsa fqgrpldrat lveatdiimv aitellatlr geeppkerwd paahnqskhg
      241 rfqategtag tdgtdglk
//
LOCUS       WP_284988623             303 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. efr-133-TYG-120].
ACCESSION   WP_284988623
VERSION     WP_284988623.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..303
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32469
     Region          1..288
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mkfsvftast pewspqeaat klaaqgwdgi ewrvtdqaea aepgfwagnr atwpmtgled
       61 svpeiarlta dsglefsglg gyarcdnhdd vdrvlaataa lgarqvrvnv lplgnsnmgg
      121 peptglpype lfaatrehye wvasraahhg vkalvelhhg tvtasassar rllegldprh
      181 vgvihdlgnl liegwesplp alqllgpyla hvhvknarwv rtdskddsga avwvnewapl
      241 aegqasvlay fraladvgyd swvtledfst elpleertas nlayvrkaaa lagfavvdpa
      301 sas
//
LOCUS       WP_284988665             299 aa            linear   BCT 25-DEC-2024
DEFINITION  TolB family protein [Arthrobacter sp. efr-133-TYG-120].
ACCESSION   WP_284988665
VERSION     WP_284988665.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..299
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=32096
     Region          48..202
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          133..290
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 mirtlqpgqr cevwiasvsg tselvfated llleapnwtr dgralilngd galwrldlfg
       61 eldtgglekv aitgvpdlnn dhvlapdgat iylsandghi yraaldggea tritdddgwf
      121 hflhgvspdg ktlayvgiea gdftqpgrli tipagggqtt aidvdghcdg peyspdgdwl
      181 yfnteaftdq pghaqlarvr tshasaperl lesdtvdwfp hlspdghlas yirfpggtvg
      241 hpadlpvdvv vvstsdwatp lhtwplfggq gtlnvnswsp dsdrfafvay pinlleeap
//
LOCUS       WP_284988700             212 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284988700
VERSION     WP_284988700.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 212)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 212)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..212
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22822
     Region          1..>87
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mldieviedp aaaeasldpi rtrilqelve pgsatqlavk vglprqkvny hlkalerhgl
       61 velveerkkg nvtervlrat aasylispva lasvapdprr fsdrfsafwl lalaartvqe
      121 mgkliagaaa akkklasfai dgeitfrsas draafaeela vavtrlvdky hdggtgaste
      181 tvsgarkhrl vvvlhpalka tqhspekeqd nd
//
LOCUS       WP_284988718             371 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Arthrobacter sp. efr-133-TYG-120].
ACCESSION   WP_284988718
VERSION     WP_284988718.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466432
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..371
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=41250
     Region          27..369
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 mptagqspeh saeeillafa aavraagvkv tadrslsfvd avgrlkldrr sdvfwagrat
       61 lcaspedlpa yqrtfeawfa vehsaaqrle nsatsvgaat lddddggpeg rreqlralas
      121 rrellrhrdv avlddeeral lhrmfeelpv rlptrqtrre hldrhgdvdr vrtlrdqlrr
      181 ggepgplrra raprknrrvv wlidvsgsma pyadsllrla hrvveaaprq vevftlgtrl
      241 trvtaalrvp dpdnalalag rtvpdwsggt rlgevlrafn drwgqrvmvr gavvviasdg
      301 wergdpallg rqaerlhhla rriiwsnphr gkagyeplqr giravlphvd ffigghsmqs
      361 feelldvvan a
//
LOCUS       WP_284988811             295 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284988811
VERSION     WP_284988811.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..295
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30640
     Region          173..285
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mqaiagflww aavflspvvr eatlgnldpv avavfdiplf vvasavasfg vkaaalvsag
       61 wtgavavala vyatvtteag wgvlgmgaas agslislclv llghvptawi iggpfafrpa
      121 iprataaahv astlgqivlf wgfflavipf avafleqrwa vvlpfpsfaa pvgvavlvla
      181 salgisaava mstlgngtpl psampnhlvi agpyrwirnp maaagilqga avgvilqswl
      241 vvayavvgsl vwnyvvrple esdleerfge efrqyrdavr cwvprmsgas ssqkr
//
LOCUS       WP_284988841             266 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase
            [Arthrobacter].
ACCESSION   WP_284988841
VERSION     WP_284988841.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter
  ORGANISM  Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 266)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Arthrobacter"
                     /db_xref="taxon:1663"
     Protein         1..266
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28609
     Region          6..256
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 metsksarsg lalitgassg igrelallaa rhgydlvvtg rsgalrdvae ecrrcgsdvw
       61 aveadlaqse gvenvwktvm atnrpldvai lnagrsiggs fldtdlndel dliglnvtsv
      121 vhlakhvsrh manqrqgkil itsslsatlp tpyetvygps rafvymfaqs lrqelrehnv
      181 tvtallpgat dtefhhragm dntafgkgaa knsrvevarq gfaamisgrd hvvggnlktk
      241 lvaikhrflp epykavrhae karprs
//
LOCUS       WP_284988849             286 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sugar phosphate isomerase/epimerase family protein
            [Arthrobacter].
ACCESSION   WP_284988849
VERSION     WP_284988849.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter
  ORGANISM  Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Arthrobacter"
                     /db_xref="taxon:1663"
     Protein         1..286
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30810
     Region          15..274
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mdvsadartq gpialacsti cfrnedlfda lertkqqgfd aidlgalqgl cehvplfgtp
       61 delkeasrtv vasglrvlsv nadpgsfndg tspfevldri eslavfcaet sapllllpcg
      121 aperddipyr hqleavasgi naaaasaary gvrvaveaph hyrlvntldr vrellplldp
      181 evglvydvsh vraagedaaa syaefasrvv hvhlrdaetg nirkvlgsgd vdfeafheas
      241 qragytgryv lelethdspf atkteevada lnrldhvfrs pakamk
//
LOCUS       WP_284988885             147 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [Arthrobacter].
ACCESSION   WP_284988885
VERSION     WP_284988885.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter
  ORGANISM  Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Arthrobacter"
                     /db_xref="taxon:1663"
     Protein         1..147
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15889
     Region          19..115
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mssvptplsa yegscletde grairdildr vgdkwsllii gtlsagrlrf gelqshipgi
       61 sqrmltltlr qlerdglltr tahaevpprv eyeltetgrt liepstalaa waitnqslia
      121 aareafdqta aarakrradg gqrshpg
//
LOCUS       WP_284988914             334 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sugar phosphate isomerase/epimerase family protein
            [Arthrobacter].
ACCESSION   WP_284988914
VERSION     WP_284988914.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter
  ORGANISM  Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Arthrobacter"
                     /db_xref="taxon:1663"
     Protein         1..334
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37195
     Region          4..317
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtrpitlftg qwadlpfeev arlagewgfd gleiacwgdh ldphrasvdd syvqerldil
       61 eknglkvfai anhltgqavc ddpiderhrd ilsdevwgng dpegvrqraa eamkdtaraa
      121 arlgvktvtg ftgssiwkav amfppaseam iergyqdfad rwnpildvfd evgvrfalev
      181 hpseiaydyw takraleavg hresfglnfd pshfiwqdld pvmflqdfap kifhvhvkes
      241 irqlngrngr lgshlpwadp rrgwdfvtag hgdvkwepif ralnaigyeg ptsvewedag
      301 mdrlvgapqs lamvrelaai appvaafdaa fssr
//
LOCUS       WP_284988936             278 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284988936
VERSION     WP_284988936.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..278
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28546
     Region          7..244
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mpvrvepdrt frqalaaadr plagmwvcsg spliaelcag agldwllida ehspnglesi
       61 laqlqavrgy pvqavvrppi ndtvllkqyl dlgvqdllip mvnsaaeaqa aiaavrypph
      121 gvrgvgsala rasrwnripd ylaraaetis vtvqietgaa vaaveeilav dgvdaiflgp
      181 sdlaasmgll geqehptvra avehclaaaq tagkpagvna fneataraym dagasfllvg
      241 advallargt ealadkfipt npdggaplgg tgdapssy
//
LOCUS       WP_284988961             374 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Arthrobacter sp. efr-133-TYG-120].
ACCESSION   WP_284988961
VERSION     WP_284988961.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..374
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39990
     Region          13..359
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mtsdtsggfa mdsneavntv ivgagqagla tgyhlkkhrq dflildsqar vgdvwrsrwd
       61 slrlftpaqh dslpglpfpa argtfpgkdt maeylenyat nwelpvrhga rvvgieredg
      121 rfrvqssags ilarnvvvat gpntqprvpa fardldpgih qlhgaeysnp dsippgdvlv
      181 vgsgtsgvei alelapthrt yiagnppfhi pgpvtryagg lwwlfihkvl nrstpvgrkv
      241 algftqhgap lirtstreld aagvtrlprl kgtrdgqplt deghaipvst viwatgyqpd
      301 fgwiqglptd edgwpltlrg aveqlpglff agmpfqyglt sglvggvgrd aehvagliag
      361 qagqkrvtap viqm
//
LOCUS       WP_284989049             419 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284989049
VERSION     WP_284989049.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..419
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45645
     Region          28..419
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mstdtlldef eetttaapag aaksngiplp legikivdft qvfmgpsctq llgdygadii
       61 kverpgagdi srnsfpdkdg qdnpiflsin rnkrsvsvdt rtdegkavlr rvmadadvvv
      121 snfrsgvmer mgfgyeelka enpgiiwasg tgfgpvgpys hkggqdaiaq aysgvmwrre
      181 sddqkpaiyp ttlcdyitgm hlmqgillal rtreasgvgq kvevtmydsm lhlqmqeacm
      241 qlnrgyevnw gamplsgvfe ttdgavcmvg gftpdplari sealgldedl tqrpefanle
      301 qqfkhkpalq aifreriatn tteywtnqle sqgllnapvh tleqaladaq teangmivea
      361 ehpgvgtvkm lnapirlsat ppsvrrvapr lgehnvevll engfdaetie rlqklgvlr
//
LOCUS       WP_284989123             428 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: vWA domain-containing protein [Arthrobacter].
ACCESSION   WP_284989123
VERSION     WP_284989123.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter
  ORGANISM  Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466432
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Arthrobacter"
                     /db_xref="taxon:1663"
     Protein         1..428
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=45572
     Region          16..391
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 mpeyapsdgl agvdaaalav gfsmalrrag lpsspdragw laqalrivpp tareplywtc
       61 rvalvssheq lpafdavfsa afdgmldpad trgdansppa igaaeharaa vserrlahad
      121 ghvpasrapl avagegndde snapgfeail amasadehlh aksfaeltpe esaqvrqlvr
      181 rivlatperr srrtrqwahn gakldlrrti raarrtggda sslvysrrra rprrlvflcd
      241 isgsmepytq vflsllqgav agaqaeafvf strltrltrq lsnrnadeal algaaaapdw
      301 aggtrlaesl rhfidghgrr glargavvvv lsdgwaqdap elveaqmarl rrlayrivwv
      361 nprkagtgyq plaggmaaal pycdafvsgh nyaalteaaa airaegprps rpsrvaasat
      421 rqhgqdka
//
LOCUS       WP_284989140             354 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Arthrobacter
            sp. efr-133-TYG-120].
ACCESSION   WP_284989140
VERSION     WP_284989140.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 354)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 354)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..354
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=36831
     Region          2..345
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrilvtggag figghiveaa margwevril dsldpavhpd pppgipgvsv lvgdagdpda
       61 vaqalagvdv vmhqsakvgl gvdffdapdy irnndlatav llagmaaagv dklvlassmv
      121 vygegaytds agrpvhpapr rvedlehgif dprdpatgel llpalvteda amdprnvyaa
      181 sklaqehlaa awarstgsta ialryhnvyg prmpkntpya gvasvfrsal argeavrvfe
      241 dggqrrsfvh vrdvaeanll svdalvggrv asgcarayni gasevhtvgq vaevlssvag
      301 apapvvtgef rlgdvrhita ssarawaelg wipkrgfedg mrefaiaplr gdqa
//
LOCUS       WP_284989155             369 aa            linear   BCT 25-DEC-2024
DEFINITION  fatty acid desaturase family protein [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284989155
VERSION     WP_284989155.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..369
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40876
     Region          60..356
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mtnqpspsvp altmpprpap prarinkvts syadllksvr eagllrrcrr yyllllttla
       61 vvgtgiwvvf filgdswlql avagasgvvf tqfaflghea ahqqvfasrs snewtarlia
      121 tlvvgmsfay wtdkhsrhha rpnmvnhdpd iaqgvvifhn evpssrgrlg ralgkhqgyl
      181 lfplllflgw tlhidslkyl lrrgpvkyrw leiallglhf gayvgllflv lspaiavtfi
      241 vvqvavfgly mggsfapnhk gmpilsensr vdfltrqvvt srniaggrfv tllmgglnhq
      301 iehhlfpdmp rphlrevrql vkahcdaegi aytetgllhs yaivvrylnt vglaaadpft
      361 cpvageyrr
//
LOCUS       WP_284989308             187 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284989308
VERSION     WP_284989308.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..187
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=19712
     Region          <6..152
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 maatlrlefl asrlaqqdfa atllgvpask lkaayecpdc gsgpdiahgr pgyvldggpa
       61 plalsasrss gwvlfaaiah pgpglrvgvd lenaagkefv gfddvaltar errhldalep
      121 grraqertrl warkeawlkm tgeglrvapd slevlerpgl wdlqlpasad grdlpaglla
      181 alavtsr
//
LOCUS       WP_284989348             447 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Arthrobacter sp. efr-133-TYG-120].
ACCESSION   WP_284989348
VERSION     WP_284989348.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..447
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47746
     Region          27..443
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtvvplplaq tvpggelihg aeggsvvrrs vlpggvrvlt eampgqrsat igfwvgvgsr
       61 deadgqhgst hflehllfkg tkkrtaleia safdevgges naatakestc yfarvldtdl
      121 pmaidviadm itgavldpae leqerdvile eiamdsddpt dvahenfvaa vlgvhplgrp
      181 iggtpaaika vsrdsvwahy qryyrpdeiv itaaggldhd ivcrlvldal rtagwelkdt
      241 aapverrste raditgtagl hvikrpveqa niimgcpsiv atddrrfvms vlnavlgggm
      301 ssrlfqeire krglvystys fasayadagy fgmyagctps kvkqvlellg aeldklaadg
      361 itdeelrkav gqlcggivla ledtgsrmsr lgraelvsge fqdidetldr ikavtaeqvq
      421 elarvlaeap rtvtvvgpfe esetfgl
//
LOCUS       WP_284989361             265 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfite exporter TauE/SafE family protein [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284989361
VERSION     WP_284989361.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..265
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26861
     Region          10..259
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 misgfesvql ttlvmivvag faagwidavv ggggliqlpa lllvpgitpv qalatnkmgs
       61 ifgtttsavt yyrrvgpdlk taipmavial agsfggavla anlpssvfkp iivvaliava
      121 lftalrpnag eltalrhdgh thyvvacaig svigfydgli gpgtgsflvi alvsamgyaf
      181 leasakakiv nmatnagall fflphgsllw gvgavlglsn maggylgart avkqgsgfvr
      241 ivflivvgal ivklgvdvwn dyfaa
//
LOCUS       WP_284989368             278 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284989368
VERSION     WP_284989368.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..278
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28903
     Region          1..276
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mtftmgpall fcpadrperf qkaaersdav ivdledavap adkkrargai laqlgsgget
       61 aeldpsrtiv rvnpvgtpdf ekdlhclaht pyrtimlaka etaeqlkald gyhvialcet
      121 akgivnaaei aqapnvvglm wgaedliasm ggtssrkddg gyravathsr stvllaakaa
      181 gkeaidsvyv dipdlaglav esadavasgf gakacihpnq vavvreayap speavavare
      241 lldaaaaagt gvfqhkgkmv dgpilkhaes tlrrarls
//
LOCUS       WP_284989427             159 aa            linear   BCT 25-DEC-2024
DEFINITION  SRPBCC family protein [Arthrobacter sp. efr-133-TYG-120].
ACCESSION   WP_284989427
VERSION     WP_284989427.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..159
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=17411
     Region          7..146
                     /region_name="SRPBCC_CalC_Aha1-like"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of Micromonospora echinospora CalC, human Aha1, and
                     related proteins; cd07814"
                     /db_xref="CDD:176856"
     Site            order(8,10,12,21..23,25..26,31,45,47,49,51,63,65..66,68,
                     71,77,79..80,93..94,96,98,108,110,112,114,124..132,
                     135..137,140)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mseqlttiev eeflphspak vwralteprl iarwlmendf qaivghqfqm rgipvpavgf
       61 sglvasevld vkaekllris wrdansgnsl nstvtwsiaa edtgtrlslv hdgfnpdept
      121 hvashrimsg gwrnhvlprl gqtlaelgst esdsaelds
//
LOCUS       WP_284989457              99 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_284989457
VERSION     WP_284989457.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>99
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          <6..99
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 vsqpgrnvra ksglnrsild qgwyemrrql eykqlwsggq vlavppayts qrcaccghta
       61 kenrlsqskf rcqvcgytan advngarnil aaghavlac
//
LOCUS       WP_284989575             498 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284989575
VERSION     WP_284989575.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..498
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52512
     Region          1..469
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mqatgkagtg gprverrsid fvpenerhgs pgqqftlwfg anmqitaivd galavlfgad
       61 alwaiiglli gnllggavma lhaaqgpklg lpqmissraq fgifgavipl vlvvvmylgf
      121 aatgtvlsgq avslilhtgt pavgmivfgv ltivvatlgy kyihmlgria tvvgilgfty
      181 lgirllasqd vgallgagsf efptfllais lgagwqltyg pyvadysryl psktparktf
      241 msayfgtvig sqwsmtlgal faalalpkga rfldgqvafl gnlsggglia vviylvivtg
      301 kltvntlnay ggymtmltsv taftrksava swtrfayvig figlsvliav laspdfianf
      361 knfvllllmv fipwssinlv dyylvskekv dipalydlng rygrwnktal lsyaigivvq
      421 ipflaqtlyt gpmtellgga diswlvglvv taivfyplak rnsnaraemv yptepdpaes
      481 dsgaiaplag sasnttav
//
LOCUS       WP_284989586             536 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Arthrobacter].
ACCESSION   WP_284989586
VERSION     WP_284989586.1
KEYWORDS    RefSeq.
SOURCE      unclassified Arthrobacter
  ORGANISM  unclassified Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 536)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 536)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 536)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="unclassified Arthrobacter"
                     /db_xref="taxon:235627"
     Protein         1..536
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56976
     Region          27..532
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mttdlsaris pevpeasasa ttagrgkrpr ppfgvsaisl lavlialfsl iplgyvaymt
       61 aatgwdtava lifrprvgel llntvmlvvf tvpiclvlgv ggawlvertr lrghrwwava
      121 laaplaipaf vnsyawvtav pslegiwsgv liatlsyfpl vyipaaatlg rldpaieqsa
      181 aslglgpwai ffrvvlpqlr iamtggallv slhllaeyga famirfdtft taimtqfqst
      241 fngtagnmla svlvffclil llaevrsrgn aryarigsga qakptrlplh hyqlpsqlal
      301 laltvlafgl piffvlrwvv aggarvwsad eflpallqtl aygtvgaaat ivvgfpmayl
      361 avrhpswfsk mlelsnyvts slpgivvgla fvtvsirmvp gvyqtsgvli aayvllflpr
      421 alvnirsgls qapkeldeaa qslgkaplvs flkvtlrlta paaaggaalv flaivnelta
      481 tlllspngth tlatefwsks seidysgaap yallmillsa pmtyllfqqs kkvagq
//
LOCUS       WP_284989615             493 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Arthrobacter sp. efr-133-TYG-120].
ACCESSION   WP_284989615
VERSION     WP_284989615.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..493
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52253
     Region          127..472
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mfnrwksasl rsqlvaiimg llllalaatg agtltlvksy lqgqvddklr aavqiaqqqq
       61 sfanlseasp avptdysltl yvqgqppypf ggsktdrpsi anitpveakn rnyapfqvng
      121 taggdwrvva vnvvdnrtgq navvivglpl spvdrvmeha tlvvvgvgll tlvlaffiat
      181 wtvarsfrpl arvektaaai aagdlsrrvd ienpvtevgr lgaslnamla hiessfaara
      241 asearmrrfa adashelrtp lvtirgfsel yrhgalatpe dvgtamgrie seakrmgsmv
      301 edllllarld eqrplqlkpv dlhllandav vdslatsger kisltgldgg aaapapvqgd
      361 eaklrqvlgn lvgnalrytp egtpielavg vrntpagpls vlevrdhgrg ipaeelprif
      421 erfyradtsr tretggsglg laivaaivgs hrgtvrveet dgggatlvvs lpfqdelsem
      481 pedagiaeae isd
//
LOCUS       WP_284989627            1008 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-mannosidase [Arthrobacter sp. efr-133-TYG-120].
ACCESSION   WP_284989627
VERSION     WP_284989627.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..1008
                     /product="alpha-mannosidase"
                     /calculated_mol_wt=111185
     Region          250..1008
                     /region_name="MngB"
                     /note="Alpha-mannosidase [Carbohydrate transport and
                     metabolism]; COG0383"
                     /db_xref="CDD:440152"
ORIGIN      
        1 mhddrritek rlerfvreri apaiygralp lelsgwdapg epvpvsealr qvfepqehga
       61 awgkawstkw lrlrgevpeg wgvadgttve ivvdlgfsid apgfqcegia wrpdgtiika
      121 isprnqhvpl kllggglsvd fyveaaanpd lsqswtfaat plgdkstsgd elryrlgria
      181 iaelnevvwe lhqdiwtlsg lmhelpfelp rrheilrafe rmldimdpdd vagtaaagre
      241 alaevlsrpa yasahellat ghahidsawl wpvretirkc artfsnvval mdenpdfvfs
      301 cssaqqlawm kefypelfir irekvkagqf vpvggmwves dtnmpggeam arqfvegksf
      361 flqefgidcq eawlpdsfgy sgalpqivks agsrwfltqk iswnqvnkmp hhtfnwegid
      421 gtrlfthfpp vdtynselhg relahaqrny rehgrgtisl vpfgygdggg gptremvaaa
      481 hrtadlegsp kvrmgtakef ftqaeaeyhn lpvwvgemyl elhrgtytsq antkqgnrrs
      541 ehllreaelw cstaavrtag sftypaadlk rlwrlvllqq fhdilpgssi awvhqdaern
      601 yaaiareleg iiagaasavl gegdttflln aapherngvp alaaaepvhs dspvsvtera
      661 ggyvldngii ravldangll tslsdyatgr eaiapgtfgn hlelhrdtpn ewdawdidef
      721 yrrnvvpvvd arsvtlerag wdvvvvvert vgsstitqri sleagaeslg isttvdwqeh
      781 ekllkigfpl dvradrsase tqfghvfrat htntsweaak fefcahrwih vaepgygvai
      841 snassyghdv trtirddggt ttnvrvsllr apkfpdpqad lgvhvldlsi rpgasiggav
      901 eegyrtnlkp rllaganpve plftvfnqal vieavklaed gsgdvivrly eslgerstgl
      961 itanfdsrmv qsvdllerpv eapgvkpgvg aaeltlrpfq lvtlrfsr
//
LOCUS       WP_284989713             343 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. efr-133-TYG-120].
ACCESSION   WP_284989713
VERSION     WP_284989713.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..343
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37733
     Region          35..305
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 maytaetwpi taallqfpgt datgqhinda etsawadvlq evkdagfana dltdswvrpg
       61 dlgkerlaef kqtaehvgig ipvisairrs iihtrdwaen layshrtida aaelgcevvs
      121 fglhqaitae qqkqlwfwtv egykdpagnk eawgnavarl relgehaaea gillslemye
      181 dtylgtadss vqlvqdigld nvglnpdlgn lirlhrpied wremvaktlp ysnywhmkny
      241 irdedvards yitmpapmes glinyreafk lalsvgfqgi lctehyggdg lsvtasnqey
      301 lrrqvlpkte nyvlgqsqva qgrqlpsgrt gstqpatsql agv
//
LOCUS       WP_284989756             370 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284989756
VERSION     WP_284989756.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..370
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38229
     Region          3..327
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 maahydvviv gggiaglsla salagqcsva lveaeqtlay htssrsarql ipsygpavvq
       61 eltvrtlelm aardaglpvp vleprsfmlv gdeatvkaea sghmhpitha ealelcpaln
      121 pgaftaagld tgsfacnapv lledhrqrae aggvdiitga rvhsaqrlgs gwqlgagleg
      181 fqsavvvnaa gawadelavl sgveklglqp frrtaaivdv erplrpgtpm vaaaddtyyf
      241 rregeqvlis psetvpsgpe darprpgdve elvarlnsit slgirsvaka wtglrteaad
      301 gvpvvgfdae apgffwlagq ggygfqtssa iaelaaaeil gsgtvgtapg ispasrtpre
      361 laaarwsirr
//
LOCUS       WP_284989909             274 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sugar phosphate isomerase/epimerase family protein
            [Arthrobacter].
ACCESSION   WP_284989909
VERSION     WP_284989909.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter
  ORGANISM  Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Arthrobacter"
                     /db_xref="taxon:1663"
     Protein         1..274
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28811
     Region          5..258
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mfnsrlgcss isfrhqdlpa alrtigglgf eeidlgalpg vcdhvpyeld sdavsavtae
       61 vvasglrvrs vngdigdlna vldagqraar eshldalltl tantgakalv lpcgalshdp
      121 vrgldedldt iaaqlvgagq raaefgvelw teslhflrfc wnldraeqla trlagsgvgi
      181 vmdfshivaa gedpleyier hrgriahvhl rdavpgninl signgqadfa aglsslaatg
      241 ysghfslele trdvthderp aaaakaasyi tdli
//
LOCUS       WP_284989968             137 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [Arthrobacter].
ACCESSION   WP_284989968
VERSION     WP_284989968.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter
  ORGANISM  Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 137)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 137)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Arthrobacter"
                     /db_xref="taxon:1663"
     Protein         1..137
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14747
     Region          28..118
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mavreavdec gvklvdpdkv elvraalpsd hdiaeladvf sllgdpgrlr lltsllegge
       61 lcvcdlaatt amsesavsha lrllrahrvv svsrrgrmay yrlddahvrm lldlglthtg
      121 htvavhpert akkdsgq
//
LOCUS       WP_284990086             272 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [Arthrobacter].
ACCESSION   WP_284990086
VERSION     WP_284990086.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter
  ORGANISM  Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Arthrobacter"
                     /db_xref="taxon:1663"
     Protein         1..272
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29634
     Region          22..241
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mpveknavva tapaatqqhg eaaffdvdnt lmkgaslfhv arkmyerraf tlsqaagfaw
       61 kqfkfvlrge kmedvhsvrd salilaagik vsdikelgee vydemiesri wpgtkalaeq
      121 hlrvgrkvwl vtatpievat vistrlgltg algtvgeved gaytgrlvge ilhgpakava
      181 vqrvadeegl dlkrcwaysd shndiplltl vghpvcinpd aglrrharen nwpvydfrsg
      241 rraatlglka atvggavygl wrgfskfrsp ra
//
LOCUS       WP_284990191             575 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Escherichia coli].
ACCESSION   WP_284990191
VERSION     WP_284990191.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13939702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..575
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=63413
     Region          110..430
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
     Region          392..569
                     /region_name="DUF3520"
                     /note="Domain of unknown function (DUF3520); pfam12034"
                     /db_xref="CDD:432277"
ORIGIN      
        1 mrnkniimll msslilsgcg pqpenkesqq qqpstpteqq vlaaqqaaik eaeqgaaaak
       61 alaqqevqqy sdkqalqgrl qeaptfaraa kakathianp gtarcqqfdd npvkqvaqnp
      121 latfsldvdt gsyanvrrfl nqgllpppda vrveeivnyf psdwdikdkq sipaskpipf
      181 amryelapap wneqrtllkv dilakdrkse elpasnlvfl idtsgsmisd erlpliqssl
      241 kllvkelreq dniaivtyag dsrialpsis gshkaeinaa idsldaegst nggaglelay
      301 qqatkgfikg ginrillatd gdfnvgiddp ksiesmvkkq resgvtlstf gvgnsnynea
      361 mmvriadvgn gnysyidtls eaqkvlnsem rqmlitvakd vkaqiefnpa wvteyrqigy
      421 ekrqlrvehf nndnvdagdi gagkhitllf eltlngqkas idklryapdn klaksdktke
      481 lawlkirwky pqgkesqlve fplgptinap sedmrfraav aaygqklrgs eylnntswqq
      541 ikqwaqqakg edpqgyraef irlieladgv tdisq
//
LOCUS       WP_284990215             348 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284990215
VERSION     WP_284990215.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..348
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=37571
     Region          48..347
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 msnwilyail aggvvfavss wwgvrrlrar htrsavheda hkpeaglqrv avvlnpvkak
       61 aedarriire achlagwdep rffettaddp ghsqtkaala ykpdvilvgg gdgtvrvvae
      121 alahtnvamg liplgtgnll arnvnldvnd lrgsvhtalf ghqryidtar maihneltgt
      181 ssehaflvia gmgldaevvg dtndglkkav gwlayteagv rhlpgrrkkv tiamddepeq
      241 srkirsvlfa ncglipggid fipgamiddg vldvvvmspr saigwlavya kilfkhnrnl
      301 pvmnyyrsgk vvisssepma tqldgdpsge atkvtvkvep rsllvrvq
//
LOCUS       WP_284990323             538 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284990323
VERSION     WP_284990323.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..538
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=58258
     Region          234..531
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 maplesaehv igamlsdile digvdngqll vppgmdngtv retvivdaed etavqrgslv
       61 lligvrgraa lpsirklipd ypaavavkgs eeeldavrem llptgiglia vspamswgtl
      121 esiakdriqe palstdasti ihrdlfaiaq ttatltnghv viedpanrvl ayspasndvd
      181 elrrlsilar rgperyqkll kesgvykhlq aaeapihmea npteglrerv aigihagnri
      241 lgyiwlqegk eplapntdkl mvgaarhaai elvrhrneqs qalrrdriss llsgtpqihs
      301 qaqsagidps kpaalvlisa kgddesaagl qlrrgelanv asihaaayrp gavvgaigle
      361 iamilpdldp vksppainrl inlivrdarv hlhcqvqaav gpvverldal hgtlehvrsv
      421 lkvlestpsi hvasyadvet tvltkellel lasrtdlrhg gitvlckryp efattlltyl
      481 effgdvnrca eelavhrntv hyrlrracev agidlqsaeq rllahlqlrl wthsegrn
//
LOCUS       WP_284990364             194 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284990364
VERSION     WP_284990364.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 194)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 194)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 194)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..194
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20149
     Region          4..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mvtddvfavi aeatrrdilv slrsgdkavg elveelaasq ptiskhlkvl readlvsmra
       61 qgqkryyaln pkplagvasw letfdvgpak paaeaatpsr tprprtagqg atgqpdaarn
      121 qtdgepivvs pastdversp eaapatgava aaagiddtrp qqigrtvgra atkaadllan
      181 lpnlpnlpkf grkk
//
LOCUS       WP_284990415             157 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NUDIX hydrolase [Arthrobacter].
ACCESSION   WP_284990415
VERSION     WP_284990415.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter
  ORGANISM  Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 157)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Arthrobacter"
                     /db_xref="taxon:1663"
     Protein         1..157
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17251
     Region          4..145
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18879"
                     /db_xref="CDD:467590"
ORIGIN      
        1 mpvpefirei rekigndplw lpgvrgvvld denrvllcqr adngrwtlit gmlepgehpa
       61 pgllreifee tavvaeteri lavgvigpvt ypngdvcdfl diafkcryvs gearvnddes
      121 iavgwfalde lpeisaghre tirlalepgs avafqrd
//
LOCUS       WP_284990422             729 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284990422
VERSION     WP_284990422.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 729)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 729)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 729)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444898
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..729
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=78129
     Region          75..471
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          349..614
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
     Region          648..717
                     /region_name="Fn3-like"
                     /note="Fibronectin type III-like domain; pfam14310"
                     /db_xref="CDD:433860"
ORIGIN      
        1 mtddevrimn qevtafeaav grirggshph aeatalyeel sgderlglld gdtpfwdgma
       61 eisrgynqrp yvhgevarlg vpgirfvdgp rgcvpgqgta fpvsmargat wdpaleekvg
      121 eaigrevraq ggnlfggvci nlprhpawgr aqetygddph hlgefgaalt rgvqkyamac
      181 vkhfavnsme narfhvdvtv deatlhemyl phfkrsikeg aaaimtayns vngdwcgqnt
      241 ylltdvlrdq wawdgitgsd fifglrdaaa slnagldvee pfsqvrgmhl rkaledghts
      301 weyveraglr lltvqlrsya qriehepplt vmasgehral arevaaramv llkndnigas
      361 avlpldpdav hslavigrla vrpnmgdlgs snvhppnstt plegiraafp garivfvdqd
      421 dpeaaekaar dadvaivvvg fderdegefi gagtltdpel lglfpprpag vempkpkkga
      481 gmtagegygg drtslrlrpv deeiiravsa anprtvvnvv aagavisenw rhdvpaivmm
      541 wypgmeggha ladvltgahn psgrlpysip tseehlpafd rdahamtydr whgqrllnkl
      601 gveaafphgf glsyttfgir egsvtlgtgg vsvyakvant gardghhvvq vygqrtdgih
      661 agewllagfl svfvpsggtv dvavpvslea lgswnpatkt ieapsvtslt frvgahaedp
      721 qalhlavta
//
LOCUS       WP_284990464             296 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Arthrobacter
            sp. efr-133-TYG-120].
ACCESSION   WP_284990464
VERSION     WP_284990464.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 296)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..296
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=32252
     Region          15..>215
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mnygnhaata prgtrvvmtg aggnigrgla prllaagyql tlsdlkpvdg latearfdaa
       61 dvrtgeglqa amvdadilvh lpalhgihva dhtetefwdl nvngtfrtlq aavaagvgkv
      121 vwlssqawhd ssdvygftkv igeqlldyhr mrhrisyvav rpaslvpwtd wardygrgll
      181 yervdrndvl daivlstdyv aandgglvld alhpdavpad elrdwehdpi gtvdrlfpga
      241 rsvvqrfgld istppvrpsk lgwtetgyap nrdfgrwide vtglsddqvk artsdy
//
LOCUS       WP_284990670             376 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284990670
VERSION     WP_284990670.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..376
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41931
     Region          69..366
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 masirkrtrk dgtssfmvcw rdpksreqqg itvateteae tlkrlldang qsfeiaqsal
       61 lsnaariptv aevvqehidl lirpssgttr tyqvmldlhi rniighipvd kldyrhlnhw
      121 aksmmakgka pktihnvhgl isaamntaem lqyisknpcr gvqlptidra edeamfltha
      181 eynmilevmg vryktftnfl vmtgtrfgea talkvadvdl lskpptvrin kawkrdgqsk
      241 yyigatktga gkrtiginpa lvdlliplva sragdellft tpkgdrivhk lfwhhywvpa
      301 vqtaqshglr ksprihdlrh thaswliqdg islftisrrl ghastrtteq vyghlmpeal
      361 qagadaters isgfar
//
LOCUS       WP_284990692             446 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Enterobacter hormaechei].
ACCESSION   WP_284990692
VERSION     WP_284990692.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..446
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47741
     Region          26..438
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,154,
                     157..158,161,267,270..271,274..276,279,306,310,360..361,
                     365,369,385,388..389,392..393,396)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 maysgkvdiq qvidespfsg fhwllivlgf lvlaidgfdt aamgyiaptl stewgihkqd
       61 lgpvlsaall glslgaliag pvsdrmgrkr vlvfsclffg laslgtawaq slntltlwrf
      121 ltglglgaam pnaitlisef apqrcramvi ntmycgfplg aagggaissw liphhgwrsv
      181 lltgaiapli ltvllalllp esvkflvqrg kdvaqvrria srfarstlds vtgfflaeek
      241 vaskkgsvsq lfsmpwlpgt lmlwvtyfmg lviyyvllsw mptlmqgmgy altesawlts
      301 lftfggtagi llagwmmdrw eahkvvacgf vltmglilll giehnhialf ggliflmgsa
      361 mngaqsgmqt laatfyptec ratgiawmqg igrfggvagt mtsaqllsmq wqadsilmil
      421 svpalvaaaa tvykmlysra qepgva
//
LOCUS       WP_284990705             427 aa            linear   BCT 25-DEC-2024
DEFINITION  thiolase family protein [Arthrobacter sp. efr-133-TYG-120].
ACCESSION   WP_284990705
VERSION     WP_284990705.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 427)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..427
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=44508
     Region          14..402
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 msqtgnsakp rtvrdvvfvd gvrtpfgkag dkgiyagtra ddlvvkcire lmrrnpglpa
       61 ervdevaiaa ttqtgdqglt igrtaallag lprsvpgfai drmcagamta vtttasgigf
      121 gaydvviagg vehmgnhpmg agadpnprfm serivdpaal nmgntaenlh drfpaitker
      181 tdayaaasqa klaaaygkgq iqpdlvpvat ikpgqgwtvn tvdepprpgt tvedlaelrt
      241 pfrahgrvta gnaaglndga taavlasaea aeelglsvkm rlvsyafagv epevmgigpv
      301 patekalkna glgigdidlf eineafavqv lsfldhfgia dddprvnryg gaiavghpla
      361 ssgvrlmnql arqfeedpsv rygittmcig lgmgatviwe nphhpdynsy nsetetavet
      421 eskgaaa
//
LOCUS       WP_284990714             243 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: potassium channel family protein [Arthrobacter].
ACCESSION   WP_284990714
VERSION     WP_284990714.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter
  ORGANISM  Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Arthrobacter"
                     /db_xref="taxon:1663"
     Protein         1..243
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=25666
     Region          <1..201
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mkvvivgags vgssiarell ahkheimlid lkpevigrsg lrgarwlvgd acelstlqea
       61 klegadvvvs atgddkvnlv vsllaktefg vgrtvgrvnn pkndwmfnds wgvdvavntp
      121 qlmtalveea veigdlvrll tlqtgvsslv eftvphdshi igstvggiew pedatlvail
      181 rdhapitpsr ddvidggdel ffvttiaaed glrgllspsa adhgsvdvee efsdqsdddg
      241 fdg
//
LOCUS       WP_284990738             452 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: MFS transporter [Arthrobacter].
ACCESSION   WP_284990738
VERSION     WP_284990738.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter
  ORGANISM  Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 452)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 452)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 452)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Arthrobacter"
                     /db_xref="taxon:1663"
     Protein         1..452
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47989
     Region          4..417
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mnaprawliw tigvlaylva vaqrtsfgvs gleaterfha saaaisfftv lqllvyaglq
       61 ipvgllvdrf gsramiasga vlmglgqlql ayadavpagv lgrvlvgagd amtfvsvirl
      121 vpiwfaparv plvtqltgms gqlgqlisvv pfalvlhsag wntaflalss lsalavvlvl
      181 allrdvppgh pprenaqglr atgvtlaraw kqpgtrlglw chftvqfsgn vfamswgypf
      241 lvsaqglnpa tvsalmglfv vtsilvgplf gtfvarhpmr rsamvllita atalawaavl
      301 llpsraplwl lallvialai ggpgsmigfd fartfnpshr igtatgivnv ggfvaallti
      361 ylvglildil htsgfsggel yglasfrial svqflfllvg tvlilmtrrk vrrqmaaqgv
      421 hvppllvsla nqrrrrvelr rerlakqrss tp
//
LOCUS       WP_284990783             455 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Arthrobacter sp. efr-133-TYG-120].
ACCESSION   WP_284990783
VERSION     WP_284990783.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..455
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=47206
     Region          220..446
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mrrwfgtlag rttaviaava tvavvlagll aaqlvnatav deakkylave adslskqssl
       61 gslqdlrtdl lthgarlaqi stdgrvtggg arlvdaktva evltgksvst svngpqntvv
      121 learplaagg gvvlaqpvse iraaaaplls rmlialavcl vfaivaggll aqwlsrplvr
      181 tahsahrlaa gersvavapg gpaevvevsq alaaldaalr tsedrqrefl lsisheirtp
      241 ltalrgyaea ladgvvsgdd vsgvgrtlva etnrldrfvr dllelarles ddfrvelqpv
      301 daslilresw qawqavcvqn giagrlelps gplpvrsdgq rlrqvvdgll enalrvtpes
      361 apvvlaayls gngltvevrd ggpglteada svafergalf arysgerpvg sglglsiaar
      421 ivqrmggris vraareggaa fvvelpgipa gprqt
//
LOCUS       WP_284990835             356 aa            linear   BCT 25-DEC-2024
DEFINITION  lactonase family protein [Arthrobacter sp. efr-133-TYG-120].
ACCESSION   WP_284990835
VERSION     WP_284990835.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..356
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=37143
     Region          1..355
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 maenidgtli wtgaytadsd gngwgigava aredgslswl gtaveapsps flavhptlpv
       61 vyavaeaaqt vrayrrtglf gleplgeawp agaaachvav dpsarfivvn cwgdgnvlmy
      121 gldddggits rfaappakdp hagveggidi atggprvsra haslmledgr imttdlgfdl
      181 vrvwnyfpdt gllkdheval pmgsgprhlv qhpsvdavfv vteysievvv llpgadgrfa
      241 lhrrgpatag gaadgdaaae ialspdhrfv ytgirgsnri svlavegsgt rlrpvadvps
      301 ggdwprhhlv rdgwlhvahe rsnqvttfal npatgipgdv leqvdvgspt vlviap
//
LOCUS       WP_284990854             143 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: LexA family protein [unclassified Arthrobacter].
ACCESSION   WP_284990854
VERSION     WP_284990854.1
KEYWORDS    RefSeq.
SOURCE      unclassified Arthrobacter
  ORGANISM  unclassified Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="unclassified Arthrobacter"
                     /db_xref="taxon:235627"
     Protein         1..143
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=15429
     Region          <8..143
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mslaldprmi kagaepghip vapvavpagy pspsqdyfss eldlnehlik dktstyivrv
       61 agnsmepagi sdgdelivnr alapkdgsvv vailddelti krlritragi ilqsdnpdyp
      121 pirvpelsdl riwgvvtwcl hhv
//
LOCUS       WP_284990941             425 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Arthrobacter sp. efr-133-TYG-120].
ACCESSION   WP_284990941
VERSION     WP_284990941.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..425
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=46462
     Region          42..421
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mfsviapphr aptanptpgn pakdgapslg sgaqnrlpks dakqsrpdla tltalrfvaa
       61 lwvvffhlqa mqhtflapvy elfrpiiang dlgvdvffvl sgfiitytyl drlgprfswr
      121 asadfvwarf armwpafalv vgvlglwlvy gsaqesvrew slqtespdls pwglakqllm
      181 mhlwfqpgtd gaswfgpgwt vsaewlayla fpllalvlfr lrrlhplaal aasvlvllpt
      241 avwgpdlpia tdehqpyewl lriaccfiag afaciaarna drmkfnaala gpgalltgta
      301 vvvflatagk pgpgrlavla fplliallsl trgwlrsals arwlqygghs syslylvhmf
      361 fiylfywlir dwpngagpva enelgvacll gialathlly kyveeparlr lralvpkvga
      421 arpga
//
LOCUS       WP_284990949             694 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Arthrobacter sp. efr-133-TYG-120].
ACCESSION   WP_284990949
VERSION     WP_284990949.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..694
                     /product="PhoX family protein"
                     /calculated_mol_wt=74048
     Region          62..693
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 msestkrkfd llpmlghtkg krspvtcalk cdnacsgevc ntssnayfrd iasaavsrra
       61 algfgavgal avvlggslsg nvpggadlsa aaktgfdkan lkfapikpvd ytvdaftvpd
      121 gfawqpiirw gdplfadspa felngqtaaa qarqfgynnd ytdilpipds kdrravlftn
      181 heytnenimf patlaaaear aigraahglt vvelerknkn kpwnyvkgap lnrrfltdtt
      241 yeltgpaagt dlvktiddps grkikgtlgn csggttpwgt ilsgeenfng yfvapgtsag
      301 dkryglsnka tarkweldep rfntnnagya nesnrfgwiv evdpfdpsst pkkhsamgrf
      361 kheganviva dsghvvaymg dderfdylyk fvskgkympg dsaaarrsnm dllsegdlyv
      421 akftgdspas eitgngalps dgafdgsgew lplvvggvsa vpgmsvpevl vytrlaadkv
      481 gptkmdrced vepnlatgkv yvvctnnsdr gkpgkegate vnprtlnrdg hiveitetgd
      541 qtstrfkwtl lmvcgdpakn sstyfsgfpv dkvspiscpd nvafdsagym wiatdgapss
      601 igyadglfkv tldgsergkv eqflavprda etcgpivhdd ertvfvavqh pgeegtfdap
      661 hsffpdyvga gaapaagqvr aprpsivqvf rads
//
LOCUS       WP_284991029             397 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284991029
VERSION     WP_284991029.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..397
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41463
     Region          5..385
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mnaqtdssap lagilvadfs rvlagplatm tladlgarvi kverpgtgdd trqwsppssk
       61 tgatyfesvn rnkesivldl nnpddqalar elacradvlv enfkpggiek lglgyealaq
      121 enpglvyasi sgfgsgggrn lpgydfivqa lgglmsitgd hqgdpfkvgv alvdvltakd
      181 atigilaals arttsgrgrr vevnllsslq galanqgqay lgagvlpkrm gndhpsivpy
      241 qllataddpl avaagndgqf arlceaigsp elavdprfat nsarvryrre lvplleagls
      301 vagaqtwqdk lvsagvpagr vasigegley aeklglapti avhdadgaiv ghqirhpitw
      361 tpplpqrtqa ppalgehthn vlswlrsprt gntddnl
//
LOCUS       WP_284991042              75 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284991042
VERSION     WP_284991042.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 75)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 75)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 75)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..75
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=8649
     Region          17..75
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 msnnnhsnvv tvdkaweltq siymdrrtta qfmgvsekfl athladgpkr lrvgskilyr
       61 lsdverwmqh qevtr
//
LOCUS       WP_284991075             525 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284991075
VERSION     WP_284991075.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19448763
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..525
                     /product="helix-turn-helix domain-containing protein"
                     /calculated_mol_wt=57138
     Region          11..120
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          246..516
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msdkppvtls dvvneghlgl spvvpgnpgt vitsahtsdi hnpaewlepn sillttglrf
       61 vnaerehlla vklvdelrea rvaavffgvg vyfdhvpaql vaackqagfp lytvakdvpf
      121 yrienfinqs qvapdayvqk ralwlsndll qsisaadpik sliarlatac rgtavlydes
      181 gtivessgdg pthlmwkeir sgkndsgtie igrwaamarp tvlkgvgytl avasmnhrvl
      241 tdlgdlllet tqrllaaiqg iaqfsdtrar hesmqlltml qdgipvaref rqwermralr
      301 ftpygpvrav vaanvddepl dpafpellqr raetsglgll laengrtpes ppgfhavvsd
      361 ssalnpwlel legsvvvgls epykdlvstp eafreaeaaa giarlqvkaa ghsehglsag
      421 ivrldevdpa twllarrlss kdksklqafv kdidvdvelk etliryladg fdvarvaadl
      481 fvhpntiryr lkkvesligg slsnarvitn lylayhddiv alsra
//
LOCUS       WP_284991357             286 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Arthrobacter
            sp. efr-133-TYG-120].
ACCESSION   WP_284991357
VERSION     WP_284991357.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..286
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31622
     Region          3..277
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 makigvqamm lkgsfaedga fetlrkvsai gynaveisqi pmtpenvael drsrselgmd
       61 iaalsvamet pkgmpgdslk dhfdkivdda krldthllri gmmpfpamks idavvdfakq
      121 aneyaenlre hgiglyyhnh hiefakfdgt ymldiiaens pamgmeidvh wvqrggldpv
      181 rtlakyagrt amvhlkdyri gelpesafgf lerrdlagfm aefknvvqfa evgegnldfp
      241 siihaaqaag aeyllveqde lygrtvweal qtsydnlvam ghgdlf
//
LOCUS       WP_284991377             221 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284991377
VERSION     WP_284991377.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 221)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..221
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24566
     Region          19..97
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mdkiqepefp vrkvdtaslk alahplrvqi lemlsrygpq tacslaelld essgatsyhl
       61 rqlakfdfvh evqgkgtare rwwerprgai qitspelahs patqeasrlv trefersrqa
      121 vladfmahgm dsldeewlda aivntanarm saeqlgryar smeafarnll eeirsepead
      181 darpvqihfn afpilgvpaw agdkksrdak shaagtegke s
//
LOCUS       WP_284991541             292 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284991541
VERSION     WP_284991541.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..292
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=30395
     Region          1..292
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mlavnptaaf grhalagdea arclreagld vvvlrrdsmd alregvdeal rtgaealvvv
       61 ggdgmvhlgv nslsgtglpl givpvgtgnd varmlglplq dvegscarvi saladggrvl
      121 dagritiggr tmwfagavsa gfdaavnera nswrwprgal rytlamlrel gsfrainytv
      181 tadgaetkeg amlisvanap sigggmrivp daapddglld lfivkplsrl allavfprvf
      241 sgrhtshpav eirrvrsvrl aaqnvvayad gerighlpld idvvpgalrv la
//
LOCUS       WP_284991585             598 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Arthrobacter
            sp. efr-133-TYG-120].
ACCESSION   WP_284991585
VERSION     WP_284991585.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 598)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 598)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..598
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=63853
     Region          8..584
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mvqktgkskn krtpaakkrl rlglgimltl llvvggklfl vqgldvggma eaaynnrlti
       61 tvlpaergki ldangtvlas svirynivvd qtvntntsef sryntqtqai dtisrtqgia
      121 elssalgmdv nqvtqavtgd kkynivakev kpdledrisq lhipgivseg iskrvypngs
      181 vaggiigflk dgttgqagle qtqddllrgk dgkrvfeiga dglripvatd lltpavngkd
      241 vkltlntdiq yfaqqaiqtq vnqlnaewgs ivvediktgn liamadtnap dpndpgkvaa
      301 adrgvrsvta ayepgsvekm itasaaineg ksspldtvti ppaltidgqt ftdafdhgte
      361 qrtlagilgy smntgtvmig srlskqqryd yltrfgigqa pdiglpaets gilakpdqwd
      421 drqqytvlfg qgvsqstlqt vrayqsiand gvmlqprlid gyvgadgaee kvpakdsqqv
      481 vtketaqqvr dilesnvtmg evkdaaidgy rvgaktgtsq apredglpgf dgytasivgm
      541 apmdnprfiv evvlqrpkgs iygitqgpif rsvmgqvlrt ynvppstgtp arfpqyak
//
LOCUS       WP_284991755             431 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Arthrobacter sp. efr-133-TYG-120].
ACCESSION   WP_284991755
VERSION     WP_284991755.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..431
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45983
     Region          22..429
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 metapptaaq qnraaqqnrp leidtlvvgg gqaglatsyf lsragvehlv lerryalgga
       61 wqdrwdafvl ntpnfsldlp gmpyagpepe afmarddvvd yfrdyakrig apvrtgtdvt
      121 wistsdgsfs vetsdggwra rnvvlatgay qipkipalsa glpksvlqlh thdyrnpeql
      181 pdgaalivgt gqsggqiaed llaagrevhl avstcpeapr ryrghdilyw llqagihgpe
      241 yginaltvgq lpspaarfac npllsgtdgg hdihlrelgr qgvqlhghle aaddgeltft
      301 ddlpqrlatv eagfgqrmgr aldayiaaag idapealpap addwlpvasp rvnlaaenit
      361 svlwatgyql dlsfvdipvl dawnyprhtr gvteqpglyv vglpwltghy ssivggvgvd
      421 aeyvagcvag r
//
LOCUS       WP_284991858             186 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: GlcG/HbpS family heme-binding protein [Arthrobacter].
ACCESSION   WP_284991858
VERSION     WP_284991858.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter
  ORGANISM  Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Arthrobacter"
                     /db_xref="taxon:1663"
     Protein         1..186
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=17909
     Region          52..169
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mkksnkifaa aavgallltg gatavanavt paaaktataa vdvspsaenv vpqnritvga
       61 ssqavnaala kcqadklpfv tvalvdrfgt vqallrgdna aehtieaakq kaytaaafga
      121 ptselakrin gngpsiadlp gtlflpggvp lkvngvsvag igvggapdga ldeacaaaga
      181 avlaak
//
LOCUS       WP_284991991             378 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284991991
VERSION     WP_284991991.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 378)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..378
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37959
     Region          73..374
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtqstttagp psaggtarel aahdphiast gqhllvraka gpdvggrgrg nraawllaav
       61 vvlalacaas laigarglsl etvwqaltqf spddgnhavv htriprtvlg lvagaalgla
      121 gaamqgvsrn pladpgimgv nagaalavva giylfgisga sgyiwfafvg aaaaavvvyl
      181 iasigrdgat pvklalagaa lsaglysimn vilvssqdtl drfrfwqvgg iagsdwsvvl
      241 tglpflliga livlgsgril nslalgddva rglgqnvtla rgvtalgivl lcgsatalag
      301 pigfvglvvp havrfftgpd yrwilpfsmv lapalllvsd vigrvvllpg evpagimtai
      361 vgapvfvwlv rrgkgasl
//
LOCUS       WP_284991992             345 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284991992
VERSION     WP_284991992.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..345
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=34315
     Region          7..343
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mnlrsrtall gtgvvvlfav tvllgsytvt ipdffrilta hltggekipg asfivmenkl
       61 pravlailig vafglsgglf qtmlrnplas pdvigisyga saaavlaivv fgasgaavsa
      121 aalagaigva lviyaisrgg sgsgggsggr rgnaagnrli lagvgvaaal gavvnflmtr
      181 adirtaseal iwlngslnsa nwervgvlma slavlvpala llavplrmle lgddaaaglg
      241 irvnavrfgl vitavalaam ataaagpvaf vaflagpiar rvvgrpslpa saftgalivl
      301 aadyfaynva plvlagtvlp vgvvtgalga pfllwllvts nrkea
//
LOCUS       WP_284992042             245 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family oxidoreductase [Arthrobacter sp. efr-133-TYG-120].
ACCESSION   WP_284992042
VERSION     WP_284992042.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..245
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=25439
     Region          12..235
                     /region_name="fabG"
                     /note="3-oxoacyl-ACP reductase FabG; PRK05653"
                     /db_xref="CDD:235546"
     Site            order(108,136,150,154)
                     /site_type="active"
                     /db_xref="CDD:187594"
ORIGIN      
        1 mpaaraesvw raprhlgath rllitatsdr iqrraqelns hgihtvsvta dltdpnqakg
       61 lvahaidvfg rldvlvnnag maavgeesas spvagttdaq wrrsiarnld ttfymtraal
      121 apmleagygr vvnmsslsgt vmafrhdagy haakaavagf tratalevag sgvtvnavap
      181 gwiatasste helimgaatp lgragypdev aatiaflasp sasyitgqvi iidggnsiae
      241 erlnh
//
LOCUS       WP_284992049             183 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein, partial [Arthrobacter sp.
            efr-133-TYG-120].
ACCESSION   WP_284992049
VERSION     WP_284992049.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. efr-133-TYG-120
  ORGANISM  Arthrobacter sp. efr-133-TYG-120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Arthrobacter sp. efr-133-TYG-120"
                     /db_xref="taxon:3040280"
     Protein         1..>183
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
     Region          6..>183
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mlnlnrdvvv vgagpsglta arelkkagls vavleardrv ggrtwtdtid gamleiggqw
       61 vspdqtvlle lldelglqty sryrdgesvy igadgvpvry agdsfpvdpa tavemdklig
      121 ildglaaeig atepwahpka reldtisfhh wlrqhsanee acnniglfia ggmltkpaha
      181 fsa
//
LOCUS       WP_284992097             431 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Enterobacter
            hormaechei].
ACCESSION   WP_284992097
VERSION     WP_284992097.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..431
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47451
     Region          101..400
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkiktnrtll aalvvsslls pavmaacngt dlttcpapfd arlpdahtml twsqadrvvg
       61 frndyrnyag dvfrhgnatp llpaekpltd aryqvkgksy tlqdylkrqn vsgmlvlkng
      121 kvaykylgeg ntdstlwtsr svgksvvsal vgvaikegki hslddlvtqy epdlkgtawe
      181 gvtlkqlith tsgvawnedy tnpqsdfarl teceakpgty ncvrtlvkgl hrehpagenw
      241 syssggawll gdvleratsm tlaaylekti wqpygmasdg vwhayskgqh dvgahgfnat
      301 ledwgrfgkf ilhngtlpdg kqilpegwvk qssawtqakg svsdahpkel ygyqwwnnev
      361 patathvepk venslkdslw algifgqmim vnqkenlviv qwstwpqaep sfsaqpleas
      421 lmfsaianal r
//
LOCUS       WP_284992121             107 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Enterobacter
            hormaechei].
ACCESSION   WP_284992121
VERSION     WP_284992121.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..107
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12198
     Region          1..91
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 miavlfeaka apahqarylq faaelkplla didgfidier fqslttdgki lslswwryee
       61 avrrwkqnvf hqaaqaegra sifsfyrirv aqlmreysse tgghahv
//
LOCUS       WP_284992131             654 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidase U32 family protein [Enterobacter hormaechei].
ACCESSION   WP_284992131
VERSION     WP_284992131.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..654
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=72685
     Region          6..307
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
     Region          444..505
                     /region_name="DUF3656"
                     /note="Collagenase; pfam12392"
                     /db_xref="CDD:463557"
ORIGIN      
        1 mrlhshhlel lspardaaia reailhgada vyiggpgfga rhnasnslrd iaelvpfahr
       61 fgakvfvtln tilhddelep aqrlitdlyq tgvdalivqd mgvleldipp ielhastqcd
      121 irtvekakfl sdvgftqivl arelnlnqir dihqatdati effihgalcv aysgqcnish
      181 aqtgrsanrg dcsqacrlpy tlkddqgrvv afekhllsmk dndqtanlga lidagvrsfk
      241 iegrykdmsy vknitahyrq mldaiiddrg elarasagrt ehffipstdk tfhrgstdyf
      301 vnarkgdiga fdspkfiglp vgevlkvakd hldvqvtepl angdglnvmi krevvgfran
      361 tvektgenry rvwpnempad lykarpnaal nrnldhnwqq allktsserr iavdialggw
      421 eeqliltmtc edgisvthtl dglfevanna ekalsnlkdg vaklgqtiyy arnievnlpd
      481 alfvpnslln qfrretaeml dearlanypr gsrkaetvpa pvypdthlsf lanvynhkar
      541 afyhrhgvql idaayeahee kgdvpvmitk hclrfafnlc pkqakgniks wkatpmqlvn
      601 gdevltlkfd crpcemhvig kmknhifkmp ppgsivasvs pddlmktlpk rkgs
//
LOCUS       WP_284992169             456 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Enterobacter
            hormaechei].
ACCESSION   WP_284992169
VERSION     WP_284992169.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..456
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=50566
     Region          12..392
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mttctpraaw gnllrrlhfy iglfvgpfif faaltgtlyv atpqlekaly hhalhtdavg
       61 eaqplaeqia maekavgsal rlhavrpgle ggettrvmfa dpalgtsehr aifidptsle
      121 irgdmtvygt sgilplrqti dylhtslmlg nigrlysela aswmwvaalg gialwfytrp
      181 krrinnrfqn rrrlhvilgw tllagmllfs vtgltwsqwa ggnvdklrae mnwltpqvnt
      241 tlsgapemrd ehaehrghhg gmtmpempvk lslfdnvlqv arqsgidann veirpasrvd
      301 qawtvteidr rwptqvdava vdphslkvld strfgdfplm akltrwgvdf hmgilfglan
      361 qllliafgva lcvliiwgyr mwwmrrpats aanpvqtlcq swlalplwgr gvsflislll
      421 glalpvmgvs lavfividwl rwravsgvsl agtsvk
//
LOCUS       WP_284992190             248 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Enterobacter
            hormaechei].
ACCESSION   WP_284992190
VERSION     WP_284992190.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..248
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=27178
     Region          1..156
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mathfargtl teghlvsarl ssachsealk lpehrrtrfl asrallaell fmlygtselp
       61 diltqpegrp vfadpalphf siaytgnivg valttegncg ldmelqrvtr sfhganalde
      121 yplssneklw irnqndpvea raqlitlrqs irklsgaasd dasllqllpg sgrlratkas
      181 lvealcdaed vliwsvavtp aierlkiwef dstrgwrslp dvperanepa arlmrltslp
      241 aekayths
//
LOCUS       WP_284992328             333 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Bacillus licheniformis].
ACCESSION   WP_284992328
VERSION     WP_284992328.1
KEYWORDS    RefSeq.
SOURCE      Bacillus licheniformis
  ORGANISM  Bacillus licheniformis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Bacillus licheniformis"
                     /db_xref="taxon:1402"
     Protein         1..333
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=39043
     Region          37..319
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 makeikqnmi rprakklpdv tnemwaqvdg ehrnlteefl dahsfrdktr kqytsslrqf
       61 fwwvhnslng kklykitkrd firyqsflkn rgmsssgial kkagvsslnn yienvvaedd
      121 dnyktfrnft rglpaipktv tyekvkitye dyqtmmkale edenylgmaw latafnvgar
      181 raeiiqfkte ildypipegq qyvlshkvfg kgsgegkvle ymintealky lklwhekrgy
      241 dheylfttty ggqpkqmset wadyfcsdvl sdilgrrinp hlfkascity llevkkikie
      301 lvskyiaqhe dvsttikhyd lrdfkeeknq ifm
//
LOCUS       WP_284992389             482 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein, partial [Bacillus pacificus].
ACCESSION   WP_284992389
VERSION     WP_284992389.1
KEYWORDS    RefSeq.
SOURCE      Bacillus pacificus
  ORGANISM  Bacillus pacificus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Bacillus pacificus"
                     /db_xref="taxon:2026187"
     Protein         1..>482
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          21..49
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(22,25..26,29..30,32,55,58..59,62..63,65..66,89,
                     92..93,96..97,100)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          24..317
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          53..83
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          88..116
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          152..178
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(154..155,158..159,161,185,188..189,192..193,
                     195..196,219,222..223,226..227,230)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          183..213
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mgknqriyke ngqvisfnql adffykkgmr aykgqklqda ikyfrraaqs ekepfilcql
       61 atvlseagey qesnqtffkl vrsnpeleqc yyfiannyay mglfqqakky adrylevaee
      121 kefvedtlel leimeeeamg aeeiededdl ivmqeeanry irngqleeai atleivtkdy
      181 pefwsghnnl aiahfqsgnv dkalkltemi leknpgniha lcntliflys igehkqveal
      241 aaqlvsvypi sfehrlklgt tlatighfep aykwfkllkr qgyegdvsfy ywfaysaymv
      301 kdqqvaekmw qhvvelhpdk kgkepwnaln lvdegqnvlf eelrksfqqs atleeqmlal
      361 ylmnelstpe kvgfffdvtq akngvpivsq lakyffllns hksipadlqq feqcariada
      421 lynytkkdde lieeclqfwf ctfirlytsg avftnvygws aaveyivrse qgnkmtqsel
      481 gd
//
LOCUS       WP_284992522             316 aa            linear   BCT 25-DEC-2024
DEFINITION  LolA family protein [Bacillus pacificus].
ACCESSION   WP_284992522
VERSION     WP_284992522.1
KEYWORDS    RefSeq.
SOURCE      Bacillus pacificus
  ORGANISM  Bacillus pacificus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Tajima,T., Yokota,N., Matsuyama,S. and Tokuda,H.
  TITLE     Genetic analyses of the in vivo function of LolA, a periplasmic
            chaperone involved in the outer membrane localization of
            Escherichia coli lipoproteins
  JOURNAL   FEBS Lett 439 (1-2), 51-54 (1998)
   PUBMED   9849875
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Bacillus pacificus"
                     /db_xref="taxon:2026187"
     Protein         1..316
                     /product="LolA family protein"
                     /calculated_mol_wt=35985
     Region          4..184
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mekkqddvvr dleakvkglk syqaeaklsi ktgnepqeyk veiwhkepsf yrvnlqnakk
       61 dqsqiilrne egvfvltpal nksfrfqsdw pqnssqayly eslvrdilqd kknltfektd
      121 kyyifktktn yqhqnmlpkq eitlkksdlt pvsvklmdnd qnvlvkvdfs kvkfdakfdk
      181 gafdtkqnms raqvdvqtta kedkpfaily prdtpqgmtl kdekelktds gkrailtytg
      241 skksftliqe kakvaeassa isvsgqlvdl gftigaltkd sltwshngve ymlvskglep
      301 kellmvarsv tekqvk
//
LOCUS       WP_284992908             219 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Bacillus
            paranthracis].
ACCESSION   WP_284992908
VERSION     WP_284992908.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..219
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=25232
     Region          4..199
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mdklhftidd ervkhlsevd ttlsklikvv gtvevplkkd yynslvkqii gqqlslkaah
       61 tiisrvekiw gnfdpyllnd irdeeirsag vstpklkyir nltekhlsne idfssihlln
      121 dkevieilts vkgignwtae mflifslgrl dvlsygdisi knaikwlyqi ekevplnldl
      181 nyekwkpynt ivslylwkai dlglvkkhpn elelikkid
//
LOCUS       WP_284992803             307 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Bacillus
            paranthracis].
ACCESSION   WP_284992803
VERSION     WP_284992803.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 307)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..307
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=34571
     Region          3..297
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkkilvtggs gwigkyvvhs liqkgyevha tyntnkpshl schwhkvnll cdeevkkliy
       61 dmkpshlihl aweavppacy vsinnyywlt ssisliqhft tcggkrvvva gtgaeyewfn
      121 gvlfedspll syktpyslck nalhswlqty akqtglsmcw grifhmygph eqgnrlvsni
      181 itsllkneea lcthgkqsrd flhvsdvada litvlehgvt dtiniasgqs vqikelasii
      241 akkigkehli klgaipfskd eplfvgvnve rlktelnwkp tydlntgiee tiswwesfiq
      301 khngthh
//
LOCUS       WP_284993259             187 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Escherichia coli].
ACCESSION   WP_284993259
VERSION     WP_284993259.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..187
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21157
     Region          53..148
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mhsqlrerir lmrarldnar pvieipaesq lfvtpapvcd rlvtlaeisn rdhileppag
       61 tgailraird tapgamcdav einsgllryl renfngvrvq ccdfmewqpv qyysriimnp
      121 pfshgqdirh ilrafsllrp ggvlvavcln gprqqekllp fsdvreelpr gtfaytrvpm
      181 miirlra
//
LOCUS       WP_284993323             556 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Bacillus cereus].
ACCESSION   WP_284993323
VERSION     WP_284993323.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 556)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 556)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 556)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 556)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 556)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..556
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=61611
     Region          1..552
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mvnrfvsvrq vgmtvalllv amliviplfl ilfssvyens swnflkpfev mqsgglagif
       61 lnsmllgvlv vigatifafp lafimsktdv gkyskldivf mipfmtppyi gsmgwilfmq
      121 pngyfeqffp mlktvsssff slggmvlims lhlfpflyfm lkntllqigs skeeaaavhg
      181 gsffyrlrki ilpllvssyv mgallifvkt iaefgtpatf grrigfhvlt seihkfissw
      241 pidfssatal sslllsacml mwyiqnvlnr kysyamvsgk gvkskrytls iftrvvawmy
      301 vigllivsig ipyfsilias fsklrggglh vnnfttshye alftmgspgl ealwnsflfs
      361 lvtaiiavmi gvflalmirk gkktsekwld mcgmlpnmvp givmvvglil fwnspympis
      421 iyntpimviv tyvvlflpyt vqyvksslgq iddslvqags ifsgnyiyif rkiilpliip
      481 gilagwamtf tisirelvas llvlppsvet satfifaqfe qgevsigmam avvsvglttm
      541 cllllqhmeq krkgva
//
LOCUS       WP_284993470             459 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Bacillus cereus].
ACCESSION   WP_284993470
VERSION     WP_284993470.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..459
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52016
     Region          114..437
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mdffetviii vnfsilgcil ffsekikqws vfiltvafcv vvvqlivegy rwqmipayls
       61 pfiltscylf aeskknvksc gaftvktall viyltiavml pslmpvvlfe ktsgpfkvgt
      121 tlyhwidynr eepymkdlng rrelmvqvwy pakekgemnr apyihnsdei akglekslsi
      181 pafafhhlgl mksnafmeaq lsdseerypv llfshglsgf rnqntfevee lasqgyivvg
      241 idhtydaaat vfpdgrtafv qsinltdfae rdrhiklwke dvvfvlnqie klnqsdkdnr
      301 ftgrmdtsri gmfghsygga taaqvlveds rvkaainmdg tlygenvtks rvgkpflimn
      361 aetsddstkd flegkvrsdh alagggmsmv iphtnhtsft dfhlfspllr sldedpryvh
      421 riinefslaf fdryvkqvdd ssalekldsk ypevkfkvn
//
LOCUS       WP_284993659             127 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Escherichia coli].
ACCESSION   WP_284993659
VERSION     WP_284993659.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..127
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14684
     Region          31..87
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mqnhyndlkp iaemmypdpa veelkaiadk mrlserlvdm nqvmelttls rrtllnlear
       61 gefpervqvt egrkawylse vidwinnipl aseycrvpvp kkpdaalclk iervrrnard
      121 gryklig
//
LOCUS       WP_284993661             585 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Bacillus
            cereus].
ACCESSION   WP_284993661
VERSION     WP_284993661.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 585)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..585
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=65486
     Region          30..570
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mlhtrrwrff avlsivglil lillkinfis itiatssaer gkifdkngvm latnkkvksl
       61 yctsndekls kqdtsntlaf fnqfssefqh disteniksq lqqsckkktm ndiplysdin
      121 enelafinkn kpnnviikde wiryypkhei gsqvigyven dlkskhmavg ksgielqyen
      181 dlkgklgktl ifklnnkkfl wniqkvqkgk dvrlaldsel qqkaeealks qikktpdaka
      241 gyaivsdakt gailtmansv afnpnilsth vssrkeniks lsqnkaiqkl kygesyvnma
      301 stikpltili glneklfqpe dtyldkgtfq ydnqnnitna pgtptgeitp rqaiinssnt
      361 fmtakvalpl fnqnngniek vahiwtdylm qfglrsktgi dlpfeedgqy efhpsnkfen
      421 gisallnasw ggnevhtplq laqyaatlas kgdkykpqiv saiigqdgke tkkfkpiles
      481 snrypmnfws vvqdgmsqni eeikklpfdv agktgitgfp neqarminhs lfiayapted
      541 pqiavsvvip gsnsekniaa lvtseileyw ntlqnenknk eegsl
//
LOCUS       WP_284993702             246 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Escherichia coli].
ACCESSION   WP_284993702
VERSION     WP_284993702.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..246
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=28035
     Region          <42..215
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mnnviplqns pervsllpia pgvdfatals lrrmatstga tpayllapev sallfympdq
       61 rhhmlfatlw ntgmrigear mltpesfdln gvrpfvrils ekvrarrgrp pkdevrlvpl
      121 tdisyvrqme swmittrprr replwavtde tmcnwlkqav rraeadgvhf sipvtphtfr
      181 hsyimhmlyh rqprkviqal vghrdprsme vytrvfaldm aatlavpftg dgrdaaeilr
      241 tlpplr
//
LOCUS       WP_284993752             529 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Bacillus cereus].
ACCESSION   WP_284993752
VERSION     WP_284993752.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..529
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57872
     Region          36..512
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mwkkiipava vlstitfssv faappsqnpa eqnryidvqm lgindfhgql dtvkkinnke
       61 aggadylaty lkerkkqnpn tllvhagdiv gasppvsall qdeptiefln dlkfdigtig
      121 nhefdegide mqrliyggyh ektgnfkgan fpyvaanfyn kstgrlflpp ftvkmvdgvp
      181 vgfigvvttd tpnvvmptml nnvqitdeve ainkstqqlk rlgvksivvl ahvggttdes
      241 gvtngdltri anetdpevdv ifgghshtyv ngtvnnkliv qansygtafs dvdvtidrkt
      301 kdivkkkaev vttyhegvep dkqvkkkldq ykekitplvn evvgkstapi drkqndages
      361 tlgnlvadaq rqtmqtqial mnpggirndl dagditwgel ygiqpfgnql ikvdltgqdi
      421 rdilnqqwqk gttrmlqisg iqytwdankp ngekvtnirl tngeelspsk mysvvanafl
      481 asggdgfvsf kngknaetgp ndfealvdyv kqlkepiqpv idgriqkvn
//
LOCUS       WP_284993812             406 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Escherichia coli].
ACCESSION   WP_284993812
VERSION     WP_284993812.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..406
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=46909
     Region          10..390
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mgkalnklsd stlkklvavq aekerfysdg ggleikhskg gkltwyfryr tggrevaaer
       61 lklgaypels lksarekrtq crawlaegkn pryelcatvq ealkpvtvke ainywleeya
      121 kdnrkdyikl vqrmdkhiic higaipldkc dtrqwiacfd rvrkkapvaa ghvmqtckqa
      181 lkfcrrrrya fsnalddliv tdvgkraeir ervhsnselk eilraidgdv fapyysalmr
      241 llivfgcrta eirlseikew dlkemlwtvp kehsktkvti frpipdgilp fiqklveqna
      301 htglllgelk kdttvaqygr nahkrlkqeh wtlhdfrhtf ttmlndlgvd phivehitah
      361 qmpgqqktyn hsrylqakrd alnlwverld mitgyneniv ilrgiq
//
LOCUS       WP_284994462             501 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Enterobacter
            hormaechei].
ACCESSION   WP_284994462
VERSION     WP_284994462.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..501
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=53627
     Region          1..454
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mnelvsaing viwspalifl clgvglyfsl rsrflqlrhi klmitlmfqg rpteagvssf
       61 qaltmtlagr vgtgniagva taitfggpga lfwmwivafl gassafvest lgqvykekin
      121 geyrggpafy iekgldvkwy awlfaivtif scglllpgvq ansigasldi afglspnvta
      181 allavllsfi ifggvkrias fssmvvpfma lgyiivacvi iainidqlps villiwksaf
      241 gleagfgail gqaimwgvkr gvysneaaqg tgphassaaa vshpvkqglv qafsvyidtl
      301 fvcsatgfml litglynvqg vdgaalytgi agvaagpgyv qtamesmmpg fgnyfvaial
      361 fffafttiia yyyiaetnia yinrkihrpw ltfllklclm astvygtvrt adlawglgdi
      421 gvglmawlni iaivllhkka faslkdyeiq naqgldphfd pvrlgiknad ywleerkdea
      481 gaqpeqvssp egkesvgkln s
//
LOCUS       WP_284994706             483 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein, partial [Bacillus pacificus].
ACCESSION   WP_284994706
VERSION     WP_284994706.1
KEYWORDS    RefSeq.
SOURCE      Bacillus pacificus
  ORGANISM  Bacillus pacificus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Bacillus pacificus"
                     /db_xref="taxon:2026187"
     Protein         1..>483
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          21..49
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(22,25..26,29..30,32,55,58..59,62..63,65..66,89,
                     92..93,96..97,100)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          24..317
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          53..83
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          88..116
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          152..178
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(154..155,158..159,161,185,188..189,192..193,
                     195..196,219,222..223,226..227,230)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          183..213
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mgknqriyke ngqvisfnql adffykkgmr aykgqklqda ikyfrraaqs ekepfilcql
       61 atvlseagey qesnqtffkl vrsnpeleqc yyfiannyay mglfqqakky adrylevaee
      121 kefvedtlel leimeeeamg aeeiededdl ivmqeeanry irngqleeai atleivtkdy
      181 pefwsghnnl aiahfqsgnv dkalkltemi leknpgniha lcntliflys igehkqveal
      241 aaqlvsvypi sfehrlklgt tlatighfep aykwfkllkr qgyegdvsfy ywfaysaymv
      301 kdqqvaekmw qhvvelhpdk kgkepwnaln lvdegqnvlf eelrksfqqs atleeqmlal
      361 ylmnelstpe kvgfffdvtq akngvpivsq lakyffllns hksipadlqq feqcariada
      421 lynytkkdde lieeclqfwf ctfirlytsg avftnvygws aaveyivrse qgnkmtqsel
      481 gdv
//
LOCUS       WP_284994761            1262 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Bacillus paranthracis].
ACCESSION   WP_284994761
VERSION     WP_284994761.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1262
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..1262
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=111013
     Region          <17..1259
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 msnkdkkfkn plnfddiisa isydpsvigp tfpnttivsp tgitgptgst gstgatgdtg
       61 atgdtgptgn tgptgntgpt gdtgatgdtg ptgntgptgi tgstgdtgpt gntgpagitg
      121 stgdtgptga tgpsgatgnt gptgvtgpsg atgntgstgv tgttgptgit gptgitgatg
      181 ntgptgntgp tgdtgstgst gptgntgptg vtgttgptgi tgatgdtgtt gptgitgptg
      241 itgatgdtgp tgntgstgdt gstgvtgttg atgptgatgn tgntgptgnt gptgitgatg
      301 atgptgntgs tgdsgptgnt gstgdsgptg ntgitgptga tgntgstgst gptgntgptg
      361 vtgttgitgp tgntgptgnt gptgntgptg vtgttgpsga tgntgstgnt gptgitgatg
      421 dtgptgitgp tgitgatgdt gptgntgptg itgptgdtgp tgntgptgnt gptgntgstg
      481 dtgptgntgp agntgaignt gptgitgptg dtgptgntgp tgatgntgst gvtgptgstg
      541 ptgntgptgv tgttgptgit gptgntgptg ntgptgntgp tgvtgttgps gatgntgptg
      601 ntgptgdtga tgdtgptgnt gptgitgatg dtgptgntgp tgatgntgpt gntgptgdtg
      661 stgstgptgn tgptgvtgtt gpsgntgptg vtgttgptgi tgptgitgpt gitgptgitg
      721 atgdtgptgn tgptgntgpt gntgptgdtg stgdtgptgn tgpagntgai gntgptgntg
      781 stgdtgptgs tgvtgttgpt gntgatgdtg atgdtgstgp tgntgstgpt gptgntgatg
      841 dtgstgptgn tgstgvtgtt gptgntgptg dtgstgvtgt tgptgntgpt gdtgstgptg
      901 vtgttgptgn tgptgatgpt gatgntgntg ptgvtgttgp tgitgptgdt gptgntgptg
      961 ntgptgdtga tgdtgptgnt gptgntgptg itgatgdtgp tgntgptgvt gttgptgitg
     1021 ptgitgptgd tgstgvtgtt gpsgntgptg atgptgntgp tgvtgttgps gntgptgatg
     1081 itgptgatgp sgstgptgrt gttgntgptg stgpttgstg ptgtlaqaya sltlgvnqtv
     1141 aangkvnfsg ggtnlngitf ngsdtltiqq ngdymitlnv spalgsvtpa afgvglnnnp
     1201 tpstnmvsnv sggmisstti isltagttls lfnnsgvavs lnngaggaag ggvarvtvir
     1261 vd
//
LOCUS       WP_284994393             454 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Bacillus paranthracis].
ACCESSION   WP_284994393
VERSION     WP_284994393.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..454
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52101
     Region          219..451
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mekvkkqvnl skiliqyifa fsigtialvt ffmilfqvgv naeiilpany yekqiesqrd
       61 aivkaeqedd qilkqykyal ydfsgnviqg sinkdyagqi wnnihndekg dstyyyaiie
      121 rdkdicvily tlhatfknpi lqkylpspev ceivlfillf vaeviflsrs fgkslskemm
      181 ilrkvtdkiq kedldfqveq skikevnevl tslvkmkdel ndslrtqwnm etnrreqiaa
      241 lahdiktplt ilrgnaelln esmldsnqkk cnehilksid emeiymksll ditkceegap
      301 lqfkqtdlrd fihniieesa icvlgkqlnl ienvqdipnf ipidetalkr aimnimmnai
      361 eysptkgdlm fsvemisekl qfivedsgrg fteeemhsat eqfyrgdksr nskdhhgmgl
      421 yiaksfakqh ggnlylsnsk klygakvvle isak
//
LOCUS       WP_284995164             387 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Escherichia coli].
ACCESSION   WP_284995164
VERSION     WP_284995164.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..387
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44782
     Region          57..365
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mslfrrseiw yasftlpngk rfkqslgtkd krqatelhdk lkaeawrvsk lgeipdmtfe
       61 eacvrwleek ahkksldddk srigfwlqhf agmqlrdite skiysaiqkm tnrrheenwn
      121 lraeacrkkg kpvpeytpkp asvatkathl sfikallraa erewkmldka piikvpqpkn
      181 krirwlephe aqrlidecpe plksvvefal atglrrsnii nlewqqidmq rrvawinpee
      241 sksnraigva lndtacrvlk kqignhhrwv fvykesctkp dgtkaptvrk mrydantawk
      301 aalrragidd frfhdlrhtw aswlvqagvp lsvlqemggw esiemvrrya hlapnhlteh
      361 arqidsilnp svpnlsqskn kegtndv
//
LOCUS       WP_284995188             223 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Escherichia coli].
ACCESSION   WP_284995188
VERSION     WP_284995188.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..223
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
     Region          <7..207
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 gfpgrfikav ftwagrqsmt svhparvvql lrennarqry ftedeirrif lsadndtspv
       61 aaryvkllll tglrrdelrl akwehvdpvk rtlwlpetkn gygrivhlns lamdvirtlp
      121 tqrgnpwlfi gkkpgmplsn pvkafqrivr ragifdkevc ihtcrhsvaa livsyggtly
      181 dvqaqlghrs sqssqryahl hpqrlqntsq llaeritaql psl
//
LOCUS       WP_284995386             401 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Enterobacter hormaechei].
ACCESSION   WP_284995386
VERSION     WP_284995386.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..401
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=45363
     Region          2..386
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mklnarqvda akprekaykl adgaglylev vpsgsrywrm kyrfngkekr mafgvypavs
       61 laqaralrde akkklaegid psfakkeekl vrdvqlnntf qavalewhgt kvsrwsegya
      121 sdiieafnkd ifpyigqqpv ndikplvlln vlrrmenrga tekakkvrqr csevfryaiv
      181 tgraeynpaa dltsamsghe skhypfltve elpdffkala gytgsplvvl aarlliltgv
      241 stgelrgafw sefdlekavw eipaermkmk rphlvplstq aleivqqlkv msgqyplvfp
      301 grndprksms easinqvfkr igytgkvtgh gfrhtmstil heegfntawi etqlahvdkn
      361 airgtynhal ylegrremmq wyadfigqvg kfqltpslcs y
//
LOCUS       WP_284995523             578 aa            linear   BCT 25-DEC-2024
DEFINITION  IucA/IucC family protein, partial [Enterobacter hormaechei].
ACCESSION   WP_284995523
VERSION     WP_284995523.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..>578
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
     Region          1..571
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mnalwqkvnr emvakilael eyertlraep vsadnwrism gnacwqfrat rgiwgwlhid
       61 pdtltttsga aveaenallq latvlemsda qtaehmedly atlrgdmqll qaretldada
      121 lihldpdelq clmrghpkfi fnkgrrgwgl dalrlyapey rgrfrlhwva vqrerlvwss
      181 dadcdinall ssamddaere rfdarwqeld lddswlpvpl hpwqwqqkia ihflaqlarg
      241 emvelgefgd eylaqqslrt ltnasrrapy diklpltiyn tscyrgipgk yiaagplasr
      301 wlqqqfasda tlihsgaqvl gepaagylsh pgyaalpeap yryqemlgvi wrenpscylq
      361 dgeqavlmaa lmetdnqgrp lidawikrsg ltadawlekl featvipfyh llcrygvali
      421 ahgqnvtlvm kdyvpqrill kdfqgdmrlv dedfpqaksl peqvkavtar lsadyiihdl
      481 qtgnfvtvlr fisrltlqcg vsetrfyqil alvlrryiaa hpdlaarfak fdlfkpqiir
      541 vilnpvkltf sehdggsrml pnyvcdldnp lflvsqes
//
LOCUS       WP_284995558             217 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha, partial
            [Enterobacter hormaechei].
ACCESSION   WP_284995558
VERSION     WP_284995558.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 217)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..>217
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
     Region          17..>210
                     /region_name="PobA"
                     /note="Chlorophyllide a oxygenase/letal leaf spot protein
                     [Coenzyme transport and metabolism]; COG5749"
                     /db_xref="CDD:444459"
ORIGIN      
        1 mtttvqhyld kglrglwypv laswevqsap vgitrlgeqi vvwrnkdgqv qaledrcphr
       61 garlsmgwnl gdriacwyhg vevagngevk dvpavdkcpl vgqqcvrsyn vqeahgaifl
      121 wfgvtadqqp deltfpdela dtenfsnflc taawkcnyqy alenvmdpmh gtylhssshs
      181 maegdrkadm vlqptktgfi fekkgqsgvn fdwvelg
//
LOCUS       WP_284995745             289 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase, partial [Enterobacter hormaechei].
ACCESSION   WP_284995745
VERSION     WP_284995745.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..>289
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
     Region          139..289
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mtnpvfalep diprnvrvar wllfrllngl hggsltlleg aqtfqfgdas aalhaevqvl
       61 apgvywrilt ggslaaaqaw mdgdwetphl tplleliarn sqilgklekg frllgkpver
      121 lrhwmrrnsr aqareniaah ydlgnafyah fldehllyss alfsgdeqdl taaqqakmar
      181 lcdqlaltan dhlleigtgw gamaeyaarh ygcrvttttl sqeqyhwata riaraglqdr
      241 vevllcdyrd ltgvydklvs vemieavgqr ylptffrtcq arlrpggrm
//
LOCUS       WP_284995825             460 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Enterobacter
            hormaechei].
ACCESSION   WP_284995825
VERSION     WP_284995825.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..460
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48990
     Region          1..432
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 myllsgagiw ftwrsgliqf ryirkfgrsl knsvtpqpgg ltsfqalcts laarvgsgnl
       61 agvalaigag gpgavfwmwv taiigmatsf aecslaqlyk ekdgkgqfrg gpawymargl
      121 gmrwmgvlfs iflliaygli fntvqansva halrfafncp ewltggalal ltlltivtgl
      181 kgvarlmqwl vplmallwvs tslmvcaihi devpnvivti fqsafgwrea asgalgytls
      241 qaltagfqrg mfsneagmgs tpnaaaaaas wpphpaaqgi vqmigvftdt ivicsasami
      301 mllagaaeqp sgstagihwv qqalvslvgs wgaglvalvv glfafssiav nyiyaennli
      361 flkvdsrlar nilragvlam vfvgcllsmp miwqiadvim almaitnlta illlspvval
      421 iardylrqrk lgvppvfdas rypeiesqia pgtwddlprq
//
LOCUS       WP_284995884             189 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein, partial
            [Enterobacter hormaechei].
ACCESSION   WP_284995884
VERSION     WP_284995884.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..>189
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
     Region          8..>189
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mrtmkgpgif lsqfiggeap fntldglagw aagkgykavq ipcnhphifd vekaaesqay
       61 cdditarlaa hglviselst hlegqlvavn pvyseafdhf apasvrgnea arqawatekl
      121 kqaavasarl glkahatfsg slawpffypw pphneqrfqd afgelaarwr pildtfdeqg
      181 vdvcfelhp
//
LOCUS       WP_284996062             275 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Bacillus cereus].
ACCESSION   WP_284996062
VERSION     WP_284996062.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..275
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31766
     Region          <78..270
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          184..267
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkldvnelae ylantpfrve gvyryaknpg vpfaestdsf pgfvfpitgk tqfqfngtpy
       61 tlspgkvihg gakmtlahkm lgeinweyil vlyrisnser edsgfthqhf elltgqsprl
      121 vellmrlwdv ynqrggismf qtemlfreal neallsvfnr esnyeshtlf erissyvhky
      181 yykdiaihtl teqnnvnrnr lsyvfrkhag mgaaeyllny rikmaqkmlc tsdvpvqqia
      241 qavgiadpfy fsrvfkkrvg isptkyrekf innpy
//
LOCUS       WP_284996216            2385 aa            linear   BCT 25-DEC-2024
DEFINITION  amino acid adenylation domain-containing protein [Bacillus cereus].
ACCESSION   WP_284996216
VERSION     WP_284996216.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 2385)
  AUTHORS   Konz,D. and Marahiel,M.A.
  TITLE     How do peptide synthetases generate structural diversity?
  JOURNAL   Chem Biol 6 (2), R39-R48 (1999)
   PUBMED   10021423
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01733.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2385
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..2385
                     /product="amino acid adenylation domain-containing
                     protein"
                     /calculated_mol_wt=267704
     Region          8..>2120
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
     Region          2133..>2287
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mpnsqkirhs lssaqsgmwf aqqldplnpi yntgeyvein gnihqdifel avrkvvmete
       61 alhvrfeede igpwqviees qfhmhfidvr keenpeeaak vwmkndlsmp vdlkkdtlft
      121 ealiqvennr ffwyqrihhi vmdgygfsll sqkvaneyts lieetnknek pfgslakvvq
      181 edieyreskq fqedrifwle kyadepevvs laeraprtsn gfsretayls ssstktlled
      241 inisltswpe fivaitsiym hkltgendiv lglpmmgrlg svsihtpsmv mnlvplritv
      301 tpnitlaell qqvskeirdv rrhykyrhee lrrdlkllge nqrlfgplvn vmpfdyglnf
      361 agnrgithnl sagpvddlsi nvykrfdqne lmihfdanpe vyngaelalh kerfmnlfel
      421 vvnnyeknes igkinitlpe enhkvllewn etkeddelis lpisfekqvq knpnklaitc
      481 dgvnltykel neranelahy lveegirpnq fvalvfprsi emvvsmlavl kagaaylpid
      541 peypadrvty ivndakpvci ithssvsskl viekdmkkiv lddeetklal htysrmniac
      601 kndvsllnpa ytiytsgstg npkgvivpmr glsnflmamq qkfslnendh llavttfafd
      661 isaleiylpl isgasltiaq kediqepsal ttllheervt imqatptlwq alvtdypekl
      721 qglsilvgge alpahlankl relgcsitnl ygptettiws tfmnidegek gippigkpic
      781 ntevyvldag lqpvppgvig elyiagegla sgylgkpelt aerfianpyg esgkrmyrtg
      841 dlvkwrsdga leyisradhq ikirgfriel aeietvlqrh kniqqaivmv redrpndkri
      901 iayivaeeke pinlseirsy vseslanymi psafvvleel pltpngkvdr kklpapdfng
      961 mhnervarnp keeilcdlfa evlgvsrisi ddnffemggh sllasrlmar iretlsvelg
     1021 igklfesptv aelakqlnda ksarpaiqka srpnevplsf aqrrlwflnc legpsptyni
     1081 plvirmngil nrealqgafy dvvekhetlr tifpnvlgss yqrildmenl nlemvitntc
     1141 kdelesvlse avrysfnldf epavrlqlft vsenehvlli llhhivgdgw slqpltrdft
     1201 vaykarcqgd rvqletlpvq yadyalwqqq llgdettpes listqldfwk eelkglpdqm
     1261 elptdfqrpi etsyrgetih fhidegmhsr lvelarkngv slfmvlqagl salftrlgag
     1321 tdipigspia grnddvlsdi vglfvntlvl rtntsgdpsf kellnrvkqv nlaayenqdv
     1381 pferlvevln pvrtrnshpl fqvmlafqnt peatfhvpgl easleiqsvg sakfdltfei
     1441 sesngvdgtp nglhgllefs tdlykretvq klierfilll ddaatnpdqs igrleiltva
     1501 ekntvlekwn ggfqiapemt lpqlfekqvy inpnsiavvf edkkltyeel nrkankiarf
     1561 liakgigpdq lvalamprsl nmvvsllavl kagagylpld pdypadrisf mlhdakptcv
     1621 ltnseveiec dealkvlvdd vkviaeveky seenidever ikplspshia yviytsgstg
     1681 rpkgvmiphq nvvrllgatd hwfqfdgndv wtmfhsyafd fsvweiwgsl lyggrlvvvp
     1741 htvsrspkef lqllvkekvt vlnqtpsafy qlmqadrene eigqklslry vvfggealel
     1801 srledwysrh phnapklinm ygitettvhv syieldetiv slransligc sipdlkvyvl
     1861 dnylqpvppg vvgemyvaga glargylgra gltaerfiad pfgkpgtrmy rtgdlarwrk
     1921 dgtldyigra dhqikirgfr ielgeieavi mkhpkveqva vivredqpgd krlvsyivas
     1981 nneaidtnem rqfasgslpd ymvpyafvvv nelpltpngk ldrkalpape fiassssrgp
     2041 rtpqeemlcd lftevlsvpq igiddgffdl gghsllavql msrmkealgv elnigtlfaa
     2101 ptvaglaerl emgngqsald vllplrasgd qlplfcvhpa gglswcyagl mkslgkdypi
     2161 ygvqargiak neelpkslee maadylkhvr evqpygpyrl lgwslggnvv hamaaqlqne
     2221 geevellvml dsypghflpn teapteeeal iallalggyd pdnmdgkplt mesaveilrk
     2281 dgsalaslee etilnlkety vnsvgllgky vpkvyngdil ffrstvipdw fdpispntwl
     2341 nyldgqivqh didcrhkdlc qpgplteigq vlakylqnkk gvsrv
//
LOCUS       WP_284996295             482 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Bacillus cereus].
ACCESSION   WP_284996295
VERSION     WP_284996295.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..482
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53552
     Region          32..365
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkktivfvlt ifilfsgfat qsyalsdsks vaiqalldda crtsgvpgms lsiladggvf
       61 yfssgyadle kglsasentl yelasvskaf tgmgilllee qgllsmtdpi qkylpwftlk
      121 yqgkpvdmqn ltlnnflhht sgltnirhtq nipqgntpdm lqktvetlvd aelafspgeq
      181 ynygtvnydv lglvieivsr qsyedfmkeq vflplglhqt yvykedaqat gqlaqgyrss
      241 ffittpfnap dyagnkpagy iisntkdmvr wmgiqmgivq dipeifhrai ekshrgdmsv
      301 savndmyyaa gwsvnaeqtf iehtgrnpnf stkvailpne rtaicllsng antninlvlq
      361 vndilngnlt qsyeisgtql ldiilsstti ilcllavllf flglrkrkmn eqqpmtkkrt
      421 ivtiifliat iaqcimffaf dwstiliwqt ysvltaliss tlltasitwf vythrlgasv
      481 rk
//
LOCUS       WP_284996277             691 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Bacillus cereus].
ACCESSION   WP_284996277
VERSION     WP_284996277.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 691)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 691)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 691)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..691
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=79832
     Region          5..689
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 msnifedelq kmkdtlhtmd eqldrlekip vyygedfkeq ilesmresnr qnlrigvqep
       61 yfgrldfqed gkeevmpiyi gkvgvsdmdt mkpiiidwra pvasmfysft ggeelafyqs
      121 pdglvegdvy lkrnisirkr elervvdtyv kgnedvshad dfllyrlgen kdnklkdivs
      181 tiqseqndii raernlplli qgvagsgktt ialhrlafli yeyreqleae rmivfapnsl
      241 fldyissvlp elgvgnisqt tfpdwalrtl ddsvklkqte kklkeafsin rdekkvmlgk
      301 lkgtlefktf ieermiqfen elvptkdfea wdraiipled vkkwmqveyk hyplqkrrer
      361 lvgrmkrwie ielkkfgetn ekkllkkeat krlnaymkfw pkmsalslys sivkskeile
      421 vlpeelvket ekscrkkevc vedlpaliyi hhritgieig qkfhhvvide aqdfspfqvy
      481 vlkeitlgns ftilgdlsqa iydyqgiedw nafkevfqet gyyeltrsyr stkeiiefan
      541 eiiknaeipv glatpvfrsg edvkvihaen qfteivktvk hlqnadvkti avigrteddc
      601 rdiyvkltna gltvnviean qskyeggisv vpvylakgle fdavllidvd eehykntkhd
      661 akllyvgctr slhdlwifhg geasplikgl k
//
LOCUS       WP_284996503             357 aa            linear   BCT 25-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Bacillus cereus].
ACCESSION   WP_284996503
VERSION     WP_284996503.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Rengstl,B., Oster,U., Stengel,A. and Nickelsen,J.
  TITLE     An intermediate membrane subfraction in cyanobacteria is involved
            in an assembly network for Photosystem II biogenesis
  JOURNAL   J Biol Chem 286 (24), 21944-21951 (2011)
   PUBMED   21531723
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Komenda,J., Nickelsen,J., Tichy,M., Prasil,O., Eichacker,L.A. and
            Nixon,P.J.
  TITLE     The cyanobacterial homologue of HCF136/YCF48 is a component of an
            early photosystem II assembly complex and is important for both the
            efficient assembly and repair of photosystem II in Synechocystis
            sp. PCC 6803
  JOURNAL   J Biol Chem 283 (33), 22390-22399 (2008)
   PUBMED   18550538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..357
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=40277
     Region          44..232
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          158..333
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
ORIGIN      
        1 mkrlflcmer elvvvkehnd nyettyhlqn mqptciavdp fqknrvycgt fgrglwfsdd
       61 sgdswrpigd syryfdfpke dgilhssits itissneqvn gygvvyvgte psalfrseng
      121 getwtelknm ksllssytwa fpprpfthhv rwitvdpnnp ntihvsieag aviqsndkgh
      181 twidkkfgap idahqllmhp eapnrlyasc gdgfmggpdr aylesynngn swiscsegle
      241 hhylysmaid padcntilvs aapsadlahh ripyesyiyr ktkdtpfqqv qqglpsaigt
      301 vismfatnkv ephtfytlnn ngvfqsndsg esweqlnisw kdeyktqhph allvtss
//
LOCUS       WP_284996538             405 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Bacillus cereus].
ACCESSION   WP_284996538
VERSION     WP_284996538.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..405
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46499
     Region          27..391
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mdlqkgklyw nttfsntpsy prldedikcd vliigagssg aqsayylses dlnivivdkr
       61 kvghgsnltn taliqylgdk mffelvntfg eeyavkhmkl ceqaindiey adqnlpycsd
      121 fkrrnslyya syeedikkle kelyylhkhd fkaawlseqq igqrypfkkr aaiytyndge
      181 inpykfthsl leqasnkgvh iyedteivgk klekecaify tkegnsitan kvivaagyeg
      241 lefkkeknat lissyaivtn pvedlsswyk rtliwetarp yiymrttadn riiigglded
      301 tniaqerdsk lihkkeklvn efnklfpnit vepefylsaf yggthdglpi igmyeefpnc
      361 hfiyaygdng lvysmvlski vrdiiingss pdlnlylqtr pklne
//
LOCUS       WP_284996540             476 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Bacillus cereus].
ACCESSION   WP_284996540
VERSION     WP_284996540.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..476
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=55778
     Region          2..473
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mqnkiivmfq kdfrlydnpa lfeavqsgev lpvyiqeetf sigsaskwwl hhavidvkkq
       61 lealgstlii rkgrteeeil slieqldita vywnicydpd rlqsnqkmkm mledkgiick
      121 efnshlllep wiikkkdnte ykvftpfyna fqkqvipkpi srvqsikwgs slpaslsvse
      181 lhllptipwt shmeaiwnpt eegayktfkk ffssklasys egrdfpgqnv hsmlapylsf
      241 gqisvklmfh ylinksterq cslfekqvns firqliwref syyllyhypf tvykplnksf
      301 ehfpwnkeee llrvwqkgkt gypfidagmr elwqtgfmhn rarmavasfl vkhllipwqe
      361 gakwfmdtll dadianntmg wqwvagsgad aspyfrifnp itqgekfdkn geyirrwvpe
      421 lkdipnkyih kpweapehil qksniklgdt ypypvvdhka areralcayk smkefv
//
LOCUS       WP_284996655             310 aa            linear   BCT 25-DEC-2024
DEFINITION  DHH family phosphoesterase [Bacillus cereus].
ACCESSION   WP_284996655
VERSION     WP_284996655.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..310
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=34690
     Region          3..305
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mheqilgaik efdtiiihrh vrpdpdalgs qgglgtilqe sfpekniytv gynepslayl
       61 rvmddiedsv yenalvivcd tanqervddq rytkgkmlik idhhpnedpy gditwvdtta
      121 sstsemiykf ynygkdkglk itkeaarlil agivgdtgrf lfpnttaktl ryvselvdmg
      181 vkftdlynem yktkekiarl ngyilqnftm veegaayikl tkevleefdv lpseasgvvg
      241 algnidglka wvlfleeddv irvrlrskgp vinklamqyn ggghpmasga kassweeadr
      301 lfadlreick
//
LOCUS       WP_284996728             345 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Bacillus cereus].
ACCESSION   WP_284996728
VERSION     WP_284996728.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..345
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38463
     Region          12..344
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mnntynekth tlikqllkkf spkapgfayi asfdsgvtyk gavglasiee nlpittksvf
       61 niasvskqft afsillleqe grlslddsiv kfvpsigtya epvtlrhlih htgglvdyme
      121 laqaenikft diltveqtlk hlnghqiarf pvgtkfeysn tgyfllslvv ekvsgkslrq
      181 fakerifdsl nmkdttivdc ypttisiarg yskneqgaym vyespwehtg dgavhatved
      241 lvkwgenltt gtvggkelvk rmseigleis ptgetiidne dyafglrlae gfncrylehs
      301 gswagyrsyf mrflkeyltv vvlsnydgfd skkyaneiag iilek
//
LOCUS       WP_284996766             344 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Bacillus cereus].
ACCESSION   WP_284996766
VERSION     WP_284996766.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..344
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36394
     Region          37..339
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mlhkpavyag nnrwlhikfi cfmsltilcl igsiflaisf gakdihlqtv waavlnydpk
       61 ltqhqiiyel rlprvigaav vgaafavaga vmqgvtrnpl adagvlgina gamfvvalsf
      121 affphmpysy lmivsfigav lstvlifvig satsggltpm rltiagavma allhslssgv
      181 aiyydlsqdl afwyaggvag vkwehlkflv piilitiifa ivlgksisli smgddvatnl
      241 gvktnrtril gmiivvilag vsvsavgsig fvglviphia rklvgvnyrl iipmaallga
      301 mllvvadlga rtvnppkela igimvalvgv pfflyiarkv grel
//
LOCUS       WP_284996857             321 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Bacillus cereus].
ACCESSION   WP_284996857
VERSION     WP_284996857.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..321
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=37641
     Region          6..321
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mettefhdti qafsifllnk grkpstikry vydvedfghw leknkklpss niwatlctkd
       61 yedyfsdlkt nrhysektmh rvfivlnrmh hflnipnplk nmeisiqpdr tlhnedfisp
      121 deekrlkyiv tsleglsekq lpvrpllmdr niailnllid yglslqelta ltmhhvhfet
      181 ntlsipatag vertitlake dkkqlynyyk sipepvrpky hsddplfvaf dfnrgtyrwv
      241 yendapkalt eiaiqkmirl evaranlrkg isgqhfrnty ilnlikketp eseiiklagf
      301 kskislkryy qyaenrknal l
//
LOCUS       WP_284996895             441 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Bacillus cereus].
ACCESSION   WP_284996895
VERSION     WP_284996895.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..441
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=49027
     Region          1..430
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mkitivgtgy vglitgvgla klghsvicfd idnekierik qgdlpiyevr lhelinyaye
       61 nnaltftsnk eeafddvefi fiavgtppll dgtadltyiq sacndiglya tndiivvtks
      121 tvpvgtndvm kgwieeklkg rhtvhivsnp eflregsgiy dffhgdrivi gadseevarr
      181 veslyselcl etyvtdiksa emikyasnaf latkisfine isnicekvga nvldvakgmg
      241 mdkrigasfl nagigyggsc fpkdtkalvq iagnvahdfr llkavievnn kqqlllieka
      301 kkvmnmskkr iavlgasfkp ntddireass liiieallni gaeivlydpk aiqyvknifg
      361 daiqysrcid esirdasavf ivtewediqt yplekyvqlm repilfdgrn cytdedvkkq
      421 kidyysvgrk sicnrkvsvm r
//
LOCUS       WP_284996953             476 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Bacillus cereus].
ACCESSION   WP_284996953
VERSION     WP_284996953.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..476
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51208
     Region          1..445
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mnileqfiss tntilwsyil iamliglgly fsiklkfvqi thlgemvrlm sdgltgktrk
       61 kgsvssfqaf cmssaarigi gnlagvalai smggpgavfw mwviaiigas ssfvestlaq
      121 iykvkdgsgf rggpayymek glnkrwmgiw fsilitvsyg lifnsvqant vtlafenafg
      181 leryivgivl aalvaviifg gvksiarmse mivppmalvy iavaifvvik nfylipdvft
      241 eifkgafgle savgggigaa mkygiqrglf aneagmgsap naaatadvth pakqgfiqti
      301 gvlvdtflvc tstafivlcs gaykatnleg ieltqnalss qigpwassfl aiiiflfafs
      361 sllgnyyyge tniefikqsk awltiyriav vgmvlfgsva tlqvvwnmad lfmglmvitn
      421 liaitllgrf ayaaltdyvr qkkqgkdpvf sadsipgltn tecwdkpvvt dkekav
//
LOCUS       WP_284996976             272 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Bacillus cereus].
ACCESSION   WP_284996976
VERSION     WP_284996976.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..272
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30341
     Region          37..159
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mnqkqlsiin ekswntaaye awtnrhgapa dyakkimedp trevahylpy iqspkgkrii
       61 nllgskgnka valallgsdv tvvdisasna kyaneladaa gvsiqyvvfd vlnvqlsesf
      121 divllelgvl hyfldlkplf qkiatllkrd gmlilrdyhp vytkllgvdh psfqangnyf
      181 deelieddva ysillteaqk eslpkttirr wtlgeiittl aeerfkiekl aeehgshqrw
      241 vfpstapegi eeripglyti iatackkgsl hg
//
LOCUS       WP_284997068             324 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Bacillus cereus].
ACCESSION   WP_284997068
VERSION     WP_284997068.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..324
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37237
     Region          13..323
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msclkrkkvi hlskakrlld ilifasakkt ftaqeiadef nisvrtvhry ildlsdmglp
       61 iyaeqgrngg ykvltnrvip pilfteeeav siffafqsls yyrdlpfnte insvthklys
      121 slqhdakvkv dkirsyiafw npkrtietpl lnevltaaie nknlhfqyes ksgiktkhvh
      181 pigvyahdgl wylpsydfgr kkvllyrvdr ilsilsmeen tdtfmnleew fasnsnvvhn
      241 ptqlhvlltt egvrqcksvp yleefvivne dgtgyinsti dkgeinfitp lfyrlgkdak
      301 vleptelidg lrmrakevls myed
//
LOCUS       WP_284997113             627 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Bacillus cereus].
ACCESSION   WP_284997113
VERSION     WP_284997113.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 627)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 627)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10106921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..627
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=73103
     Region          432..600
                     /region_name="vWA_norD_type"
                     /note="norD type: Denitrifying bacteria contain both
                     membrane bound and periplasmic nitrate reductases.
                     Denitrification plays a major role in completing the
                     nitrogen cycle by converting nitrate or nitrite to
                     nitrogen gas. The pathway for microbial...; cd01454"
                     /db_xref="CDD:238731"
     Site            order(439,441,443,517,545)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238731"
ORIGIN      
        1 mrqifsdkki daslflqmen lmyallkedd ayleygykay ydeiekkvvi shfwddrkee
       61 dtviglksev flkalgnkhy sdmtlirsyt ielqesplkk fltqlfvlle dlrveeivkn
      121 lrpgtkhvfk rrkemyrnyf ssqneinrvr nyhgdrlfcl cylsltsdky emfnneyfeq
      181 ieailhetfq arntedimyi vekiryrlee llesdmlnny fghaplylsv ladekncrve
      241 dlanddtqli dddenknkmd esfstwhren knnenenflr felesgtktn mmgdtarese
      301 dgdqalgsvq gtsqkstqsn fdgadteear ashassqhdg aygkynvgas htfkearkpn
      361 sdekkdyqai ksvvnkdvke lkkiiektie nktnansdky ygrlrkkflr iytekqprmf
      421 ykkgqesqel dvafqllvdc sgsmynkmee tkksvvlfhe alkslkipha isgfwedass
      481 akpedkpnvi hevvnyknst lpnvgpeimq lreeednrdg yiirivsekl akrpekhkfl
      541 lvftdgepsa ldyqqdgild theavklark sgmevigifi eegeakeaty qlmkniynhh
      601 flvanhaedl rlkikpllkk lllktie
//
LOCUS       WP_284997269            1474 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Bacillus cereus].
ACCESSION   WP_284997269
VERSION     WP_284997269.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..1474
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         <1..>1474
                     /product="beta strand repeat-containing protein"
     Region          1..1440
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 vttliqagga gsyttgavpg lvdpidasng tinsagwtli vayqngtlpa rnltiyvagn
       61 rvsaetgsad vsvsgfltps ggpvsgrlfl sstegdadlt gdqalfgpnf sslnalsgpn
      121 nainnffgsq vnnaagnldt tgtfgtrnqs aststnisag rqgwditsid ispyltnsqv
      181 saairlttng daymlntvgl qininspniq atksvnksva aigdiltytv tipntgllpa
      241 nnaifidslp ngtsfipgtv tvdnvpqtna npaagislgt inngasrivt fqatvvslps
      301 qnpisntani tfqytpiagg ttfnglatsn sagtqinlad ingtksvnkl ftdigetlty
      361 sialanigni aatnviytdp ipsgttfipg svtvngvtqa ganpangiti gsiaansttt
      421 isfqvlvpsi pqtnpilnsg tttyqyipvp nqpavsgtdt tnivstqvnn atvtmtkavd
      481 knfadigdtl tytvsftgtg ntnannvift diiptgttfv lnsltidgtt qvganpatsv
      541 nigsitsgtt knvafqvvvn tiptsnvvsn gssasyqytv npsqspvtkn issnlvstqi
      601 nnanvtltks tnkqfatige tisytilitn sgntaannvq ltdplpngti ltpgtvtlng
      661 vlqnidslva lpigtipgga tvtlsfqvtv inittqnpii nnafasylyt vnpslpptsk
      721 tansnsvtst irlanlhvnk svdktfaevg dvltytfalt ndgnvaanni llsdsiangt
      781 afvpnsvivn svtqpgvtpa sinigsinan ttitasfqvv itsipnpnpi snsasisynf
      841 ivypnaspvs knttstttft qvndanvisa ktvdrafatv gdiltytvtl tnagsvsads
      901 ptfvdtnpdg ttfipntfli ngvlqnnadp nigvplpsia angsltvsyq vtvtslptqn
      961 ptlnssstqy sfilnpgdpp tietsvsntv stqinlanvv ivkevdltia dvgqpityti
     1021 slanlgntta nnvivtdiip ngstivpnsi figgtlqqga dpstglqvgs ipsggfativ
     1081 fqisanglps pnpiqnsasl qysfiadpnl palvrnaasn ivttqintan ivatkltstn
     1141 fadvgdvily atiltnngni paanvtftdi ipagtlfipn tvtinnvpva nanpatgisi
     1201 gtiganssrt vafqvfvpti pavnpitnqs gttfqytydp skpavmqmva sntvqttinn
     1261 asiaatksad kqfanvndii mytttltnng ntlasnvift dvipngtsfi pnsvtvngnt
     1321 lpnvnpasgi aidpinqnan tiisfqvqvn sipnpnpipn qsnttyqyvi dpnlppasan
     1381 tlsnvittqi nnatiiatks vntpnaaigd ivtytiavtn tgntpasatv ltdglgagas
     1441 fiqnsvtinn vpqpgldpsl gvhladispg dtvf
//
LOCUS       WP_284997159             336 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Bacillus cereus].
ACCESSION   WP_284997159
VERSION     WP_284997159.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..336
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36031
     Region          27..335
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mmqsilrkqr liilalliii ittivvgmgl gsaslsydrl lptlmgqgtf keefvlyslr
       61 lprivitlla gmalalsgai lqgitrndla epgilginsg agvavaiffl yfpidvgsfl
      121 yllpvvgfig afltavliyv fsyskstglq pvrltltgig fafalsgtmi vlissadrmk
      181 vdfiskwiag niwgddwifv lamlpwlivf ipfifykanr lnilalnepv aigvgieiek
      241 erryllvaav alaaaavsvt ggisfiglma phiakslvgp prhqifmpia lliggwllll
      301 adtigrnivd pngipagivv aligapyfmy lllkka
//
LOCUS       WP_284997288             101 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase, partial [Bacillus cereus].
ACCESSION   WP_284997288
VERSION     WP_284997288.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..>101
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
     Region          21..>88
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mneqyydavl hiktvgeqkg fnksmhyhry eptpysglde llnqyeirss drivdfgcgk
       61 grlnfymhhk cgasavgiem neefykeamd nrdryarkar n
//
LOCUS       WP_284997708             400 aa            linear   BCT 25-DEC-2024
DEFINITION  alanyl-tRNA editing protein [Bacillus paranthracis].
ACCESSION   WP_284997708
VERSION     WP_284997708.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V.
  TITLE     Evolution of aminoacyl-tRNA synthetases--analysis of unique domain
            architectures and phylogenetic trees reveals a complex history of
            horizontal gene transfer events
  JOURNAL   Genome Res 9 (8), 689-710 (1999)
   PUBMED   10447505
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Cusack,S., Hartlein,M. and Leberman,R.
  TITLE     Sequence, structural and evolutionary relationships between class 2
            aminoacyl-tRNA synthetases
  JOURNAL   Nucleic Acids Res 19 (13), 3489-3498 (1991)
   PUBMED   1852601
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Schimmel,P.
  TITLE     Classes of aminoacyl-tRNA synthetases and the establishment of the
            genetic code
  JOURNAL   Trends Biochem Sci 16 (1), 1-3 (1991)
   PUBMED   2053131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..400
                     /product="alanyl-tRNA editing protein"
                     /GO_function="GO:0002161 - aminoacyl-tRNA editing activity
                     [Evidence IEA]"
                     /GO_function="GO:0002196 - Ser-tRNA(Ala) hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004813 - alanine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006419 - alanyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=45049
     Region          1..228
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
     Region          259..392
                     /region_name="DHHA1"
                     /note="DHHA1 domain; pfam02272"
                     /db_xref="CDD:396724"
ORIGIN      
        1 meqklyytda ykqdfttkvi kqdydkdgnl yvilnetafy ptgggqphdt gtlngiavfg
       61 veevneeirh fitkqlhtee vegkinwerr fdhmqqhaaq hilsasfwdh fniptigfhl
      121 gretvtidle tenlhtetve kavqianniv fenhpiriew mdleeaktlp lrkepnmten
      181 irvvmienfd yngcggthpk rtgevgpiqv lswernkggi rltfiagwrt lkligqqqqi
      241 mkdvskqlns sesdipakva qlltsqkene ktiqtmnekl lyaeanellq qpakihasil
      301 iskvftnrsm qeisklsaii teqqehaity fiienedklq cilacgktvt ldmnallkda
      361 lpaiegkggg nkksargggk aimtgdefln qlvsslqsav
//
LOCUS       WP_284997896             371 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Bacillus paranthracis].
ACCESSION   WP_284997896
VERSION     WP_284997896.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..371
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39791
     Region          1..367
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mksyivvgag ilgastayhl akaganviiv drqqvgqatd aaagivcpwl sqrrnkawyk
       61 ivkggaryys sliqqleedg etdtgynrvg aislhtdekk ldqmeerayk rredapeige
      121 itrlsaeetk klfpalseef ssvhisgaar vngrllrnal isaakkhgat fikgdavlvr
      181 egnhitgviv ndetilaekv ivtagawane ilnplginfl vtfqkgqivh lqmentaten
      241 mpvvmppndq yiltfdnghv vigathendt gfdhrvtagg lnevfhkalt vapglenatm
      301 letrvgfrpf tpgflpvigp lpnfegilva nglgasglta gpylgselak lalgqpield
      361 lndydvagai e
//
LOCUS       WP_284997913             708 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Bacillus
            paranthracis].
ACCESSION   WP_284997913
VERSION     WP_284997913.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 708)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 708)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..708
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=80060
     Region          1..693
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mkkqkkksdr avpmrlnilf lcvfilfsam iiqlgkvqii dgetykneve krenatvsls
       61 vprgkifdre gnpvvdnksl rtitytkmkg vkseeilkta rqlaeiieip qedidkltet
      121 dkkdfwmqln ptlteklvsk keinrfrdkd itgknldkki eelkrkrvtd knlqdltdkd
      181 ikvlaikskm tsgyqmapqi ikkdvsekef tiiseglanl pgvdvsvdwe rvyvndglfr
      241 svlgnvsnsd eglpserldy ylvrdysrnd rvgksyieqq yedvlhgtkk evrsvadkqg
      301 ttirtetise gksgknltlt idmelqkkve esiekilkay kgsesmldra fvvmmnpkng
      361 qvlsmagkrl vekdgkteie dyalgtmtss yelgstvkga tvltgfetka itpgtyfyda
      421 pmkfkgtrek kswkefgnid dlralqvssn vymfhtalki agvdyvknss lnikqeyfdk
      481 mryyfrqfgl gvptgidlpn etagqigkkd nqpgflldys igqydtytpl qlvqyistia
      541 nggyrmkpqi vqevreqtsq kdeigkvvha vepivlnkid mkeeyinqvk egfrkvfqeg
      601 dgtgvrafqk asykpagktg taqtvygges digrnekger recynltlag yapydnpeva
      661 fsvvvpwvmn dksginsdig kevldayfel knkrltgenl qidssqeg
//
LOCUS       WP_284997922             209 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Bacillus paranthracis].
ACCESSION   WP_284997922
VERSION     WP_284997922.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..209
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23965
     Region          36..135
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mefwessfie kqtmwgfept esailtkdff vennvkdilv pgigygrnak vfiensinvt
       61 gieisktaid larengiedv siyhgsvnem pfdnklydgi fshallhlln eqerekfikd
      121 cynqlkpggy mvfttvskka pmygkgkqld kdyyeimegv kmffydsesi kkdfnqyglv
      181 qvseidepnk nmankpsinf ltikckkel
//
LOCUS       WP_284997924             483 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Bacillus paranthracis].
ACCESSION   WP_284997924
VERSION     WP_284997924.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..483
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54040
     Region          35..373
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkntiyklsl icmlcnvlil citpskvyaq qnikatldny vekfikeqni pgasvaivhn
       61 kevfftktmg vtgesekkvt sktpfaigsi sksltalaiv kliedkkikl edpvqrylpw
      121 fklkdsqiss titiqhllth tsgintyegl alsdkqskss talkenvmel lnvkvtappg
      181 ekyqysnany ivlgalieev tneiyssyme kyifqplnmn gaaaskeiay ekgyltgyqs
      241 wfgiprksvv sydnagapyg yitanledmi qfimflnrqe npqflkqenm nlylsplyqt
      301 nseksygfgl rttnineset miwhsgstpd araeiftlnk sgwsgviltn knhvleetal
      361 selkkgiisi lngeepvdip knipltqiim livtlilfvi simlikkykh mktvkkviwl
      421 sigglsllls itfiplltys tsspwrtiki fapdvalvts iivtllavng lisirialrr
      481 kkv
//
LOCUS       WP_284997929             710 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Bacillus
            paranthracis].
ACCESSION   WP_284997929
VERSION     WP_284997929.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 710)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 710)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..710
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=79664
     Region          5..695
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mkeqkgkkqk tyisirlnim flcifllfsa iimqlgkvqi vegeayknqv ensqnattsi
       61 pvprgqildr egktvvnnks lrtitytrvk gitsddilkt aqdlakvlem peqdinkltd
      121 idkkdfwmql ntkradtkit kkdiekfkek giegkeldkk iedlrrnrvt evelgelteq
      181 dlkvlaiksk mssgyqltpq iikkdvtdee yarisenlan fpgvdatvdw ernyvngnlf
      241 rsvlgnitss eeglpkenld sylvrgynrn drvgksyieq ryedvlhgtk eevknvtdka
      301 gnivsteiis kgksgnsitl tidmelqkkv eesieknlra fksseplldr afvvmtnpnn
      361 gqvlsmagkk ivekegvlei edlalgnmtt syelgsavkg atlltgyetg aihpgdqfyd
      421 apmkfkgtqa kkswnvsgfg nindlralqv ssnvymfqta lkiagvnyvp ngsldikqga
      481 fdtmryyfkq fglgvptgid lpneiigqtr kvdsqpgfll dfsigqydty tplqlaqyis
      541 tianggyrmq pqivqeireq sikeevgkvi rsiepvvlnr idmkteyidr ikegfrwvfq
      601 egdgtgvkhf knapykpagk tgtaqtvygg ddpigrnakg ermecynltl vgyapydnpe
      661 vafsvvvpwl hndksginsi igkevldvyf dlkkqrmhde aastdnsnqn
//
LOCUS       WP_284997934             436 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Bacillus paranthracis].
ACCESSION   WP_284997934
VERSION     WP_284997934.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..436
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48120
     Region          1..425
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mkkfdvaivg gglagltasi ylakagrkvi vlekssrfgg rgmtinkngi cmnlgahaly
       61 rggaafltfn elgmnlpggi pstkahgiwk gdiftiptdf rsilstplls wsakvqfsrl
      121 mirlgnldvr kvqkvslttw aeneikdpmv rnifyalcrt ttytfaptiq lassvlkqiq
      181 lsikdgvfyv dggwetiitk lrdianhagv qfldkkhvle iehyedkqri ycfddeafev
      241 gtvivttppk eacniikgve gtslhrwskq svpvtvaald iglrrlpnpt hqfalgldqp
      301 ifftnqsraa klsddgsitv slikyhnpvl emkqthedke qlestmdllh pnwkreavaq
      361 qylpkitvvy dfphinrvek pgpnipempg iyvagdwtgh deiladaavg sgkraalhil
      421 kqlesegvhh gngaii
//
LOCUS       WP_284997985             238 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor [Bacillus
            paranthracis].
ACCESSION   WP_284997985
VERSION     WP_284997985.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 238)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 238)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 238)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..238
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28369
     Region          1..235
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mkillimeda eerrglvekf tenirnvecf eantgteslf mmkkhtpdfv flnsklldgt
       61 gfeyasllre vncymkfifm gedieesita frfqavyyll rpfreedlqf llyrmakeqg
      121 ekaksylrkl piegqegiry ifpedivyvs knkenktvsi yttnnqyist ytlqelenkl
      181 naydflrvhk sylinmsyvq elkpyyngty nlyldkydeq pipvsrnyvk rlrnkiel
//
LOCUS       WP_284998004             909 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Bacillus paranthracis].
ACCESSION   WP_284998004
VERSION     WP_284998004.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 909)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 909)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 909)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 909)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..909
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..909
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=104983
     Region          271..906
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mkkqthvsil isiillsimi hyvtmpflye ysfpfqilig mstlfidiia csyilyfsnl
       61 keglprlfwt ivcvgtlsyf igdivvayqr lilkdyytfv dpsdffyllf lisfafafly
      121 eiiynrdlle klfmicdici ivtaqftlsy ylliertihv sstsyidifv qltypmtdll
      181 ffliginllf kplsllpkkv gallgsalil yattdaiyay ikyftpeysm ftitplyqvt
      241 lvlvaiacil htkeperqeq vlltpklges irlslpyisv vmlivfilve yvfapivvig
      301 lmitfsfvli rhslvrkqnk illlaqmqfn selekqielr tedlveqkne lyhnqqmfks
      361 lyehhpdpif tldlygnflk vnnagttllg yqtnellnqp yysltyeedl eeiinafhrv
      421 kkgksislei rayhknrdiy ylhvtavpif lkdhisgvyl mikditeskq qqeqinflay
      481 hdtltelanr rafhqyveqa iarskiskmp favmfldldr fkvindtlgh rvgdllliav
      541 akrlesiatp nmklarlagd eftilienyk krpdvkkiad tivaamnepf eienqhlqis
      601 psigiaiype agedplsilq hadmamyeak nkgkngssly tkelykkmer kariekdlpl
      661 alvneefylv yqpqidittk kiigaeallr wkhpllgdip pcefipivee tpqviplghw
      721 vlnescrqlk iwhtfgykdl kisvnlsake fqqnnlieni lqiitdvkvd pkdvtlelte
      781 riamideket lsklkqlkey giqtsiddfg tgysslayls ifpidtlkvp reftqladhr
      841 peeraivsti lslantlnls vvaegietek qlkflqknnc kymqgyyfsk pltshqfikf
      901 lqktpsmnq
//
LOCUS       WP_284998060             330 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Bacillus paranthracis].
ACCESSION   WP_284998060
VERSION     WP_284998060.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..330
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=36042
     Region          14..311
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mnarkqlwia vicmtfvvil gtlgfmtiee islfqafwmt mitvltvgyg daipvtqagk
       61 vfalliipig vgivtyaigv vaamiiegnl fhavrrkkmd kqiaqlqnhi ivcgcgrvgl
      121 qvvhelqekk ipfvvvdkde silekeklly vhgdatedqv lhhagiskaa glvaivanda
      181 envfitltar glndaikiva raekpetedk lkragankvi npssmagihi akgianpltv
      241 hyidtvlygm eqsfvieeia vgkgsiltnk sllesdvrnq fdvtilailr ngnvihnptg
      301 qeklqehdmi ivfgsveklg qfekelqsmr
//
LOCUS       WP_284998243             341 aa            linear   BCT 25-DEC-2024
DEFINITION  trypsin-like serine peptidase [Bacillus paranthracis].
ACCESSION   WP_284998243
VERSION     WP_284998243.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..341
                     /product="trypsin-like serine peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37653
     Region          130..340
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mitsfipknv cifstilfsi ffsslssqqa maaedpetpv timnpdepsk penyiqskds
       61 lyeesgglyt eedlknaipk dktktpdnsi klnpsfkkpp mkekdkkqqf apptypsndp
      121 vptksivpkt tgklyfretp nsktsvcsas vvtsnednai ltaghcvhdg akgswytdfl
      181 fvpayfnger pygswiwekv hapygwtnsg kydydkaiir mrpnnsgtki anylgsngwm
      241 tnasqyqtdv ritgypsdap ydgqlpyscy gdtfkdglfs ndaymncgmt kgssggawfd
      301 rmsseslgyi faatsrssas gtkrlyavpl gdeftnmlna d
//
LOCUS       WP_284998286             376 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Bacillus
            paranthracis].
ACCESSION   WP_284998286
VERSION     WP_284998286.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..376
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=43811
     Region          1..375
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 milakkvrli ptpeqekllr nhagaarfay nyckrmsdry yklfgksvsq lalqkrftki
       61 kkrkryewlk einaqvpkqa skdfdtarkh sfkkykngyh tsykskkdli qgfyanyerl
      121 vigkkvvhiq sigevktsqq lprnkkpsnp rvtfdgrhww isvgfqedfe sqeltnesig
      181 vdvglkelfv asngmkerni nkdakvkkll krkksaqrdm srrfkkgvki qsagyekaka
      241 ehlrlsrkim nirnnhihqa taklvktkpm rivvedlsis nllknkklsk alsfqklnff
      301 fqclsykcek ygiayekadk wfasskicsc cgvkydhsvq pegqwslkir ewccvscnsh
      361 hdrdvnaain lsrwvk
//
LOCUS       WP_284998332             433 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Bacillus paranthracis].
ACCESSION   WP_284998332
VERSION     WP_284998332.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..433
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47330
     Region          25..432
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(35..36,39..40,43,77,127..128,130..132,135,155,
                     158..159,162,264,267..268,271..273,276,303,307,356..357,
                     361,365,381,384..385,388..389,392)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mqpsapphle stktifsnsi tklvvficwl ailadgydlg iygavlpkll ednswalspa
       61 hagtiasyal fgmfigailv gtitdligrk wtlicclalf sitmglaala pspelfglwr
      121 figgiglggv iptasaltve yspkkrqsfi yalmftgypl givlgailsm fmledfgwri
      181 mfgigmipll lipfiirylp esiqfllsrn rqeevdkiln rfqiefhake kthqppsnir
      241 kkngfltlfs keyikatllf wityimgmfl iyglntwlpq mmrqagyplg sslsfllmln
      301 itaaigalfa gaiadrigak ivisisylma avciglltik psvtiiylli glagigsvgi
      361 tqilnayvtq yfpshirats lgwglglgrv gaitgpilvg iimtmqydla wnfylfsfag
      421 llaaisvffi ptk
//
LOCUS       WP_284998339             202 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Bacillus paranthracis].
ACCESSION   WP_284998339
VERSION     WP_284998339.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..202
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23986
     Region          21..>111
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mneqyydavl hiktvgeqkg fnksmhyhry eptpysglde llnqyeirss drivdfgcgk
       61 grlnfymhhk cgasavgiem neefykeamd nrdryarkvr nskdkirfec claqeyeids
      121 rdnrfyffnp fsiqvfmnvv nnillsveet grevdiilyy psedyiffle nqtafelkke
      181 vrlpgayekn gnerfliytl rl
//
LOCUS       WP_284998459             627 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Bacillus paranthracis].
ACCESSION   WP_284998459
VERSION     WP_284998459.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 627)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 627)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10106921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..627
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=73062
     Region          432..600
                     /region_name="vWA_norD_type"
                     /note="norD type: Denitrifying bacteria contain both
                     membrane bound and periplasmic nitrate reductases.
                     Denitrification plays a major role in completing the
                     nitrogen cycle by converting nitrate or nitrite to
                     nitrogen gas. The pathway for microbial...; cd01454"
                     /db_xref="CDD:238731"
     Site            order(439,441,443,517,545)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238731"
ORIGIN      
        1 mrqifsdkki daslflqmen lmyallkedd ayleygykay ydeiekkvvi shfwddrkee
       61 dtviglksev flkalgnkhy sdmtlirsya ielqesplkk fltqlfvlle dlrveeivkn
      121 lrpgtkhvfk rrkemyrnyf ssqneinrvr nyhgdrlfcl cylsltsdky emfnneyfeq
      181 ieailhetfq arntedimyi vekiryrlee llesdmlnny fghaplylsv iadekncrve
      241 dlanddtqli dddenknkmd esfstwhren knnenenflr felesgtktn mmgdtarese
      301 dgdqalgsvq gtsqkstqsn fdgadtkear ashassqndg aygkyntgas htfkearkpn
      361 pdekkdyqai ksvvnkdvke lkkiiektie nktnansdky ygrlrkkflr iytekqprmf
      421 ykkgqesqel dvafqllvdc sgsmynkmee tkksvvlfhe alkslkipha isgfwedass
      481 akpedkpnvi hevvtyknst lpnigpeimq lreeednrdg yiirivsekl akrpekhkfl
      541 lvftdgepsa ldyqqdgild theavklark sgmevigifi eegeakeaty qlmkniynhh
      601 flvanhaedl rlkikpllkk lllktie
//
LOCUS       WP_284998426             580 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Bacillus paranthracis].
ACCESSION   WP_284998426
VERSION     WP_284998426.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..580
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=66618
     Region          343..577
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mnfnkrliip fimqhvfvlv tlliavvaaf tyliflvtst syepnipdae nfmiaryiss
       61 edgdislkae vkdlikeknd wiqvveengk vlyhfntpsd vptsytktsl fsyiqnhies
      121 pytfsyweie leeknvlviy ggmlksnall ktiqkthpsv stdsftltee ekqllskeka
      181 tlqifnsvge evfsypngkk ktfsviqaal sekepwnhke ntssfydtns nhllvitakn
      241 eyyypddeid dvfakkflig cglillivfv ylvilsiwyg nkfgkpllha mrwlkniagg
      301 kyeepvskkg kpirfrksgk ekwsfrlfsd vtnslehlsi tlkkndamrq vlqqtreewi
      361 tglthdlktp lssiygyall leskqynwtd rdiqqfgsvm keksqymttl iddlsltyql
      421 knnslpaqhv niemnqfvqk vllqfinnpt lqnqniefvp ssnkiqyfie ekwfqriien
      481 llvnavkhnn ettnvivkls qnatsftlsi sdngkgmddk trellferyy rgtnteesni
      541 gtglglaitk qlvhahngti sidselekgt tiilvfpfrs
//
LOCUS       WP_284998460             330 aa            linear   BCT 25-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Bacillus paranthracis].
ACCESSION   WP_284998460
VERSION     WP_284998460.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..330
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=36823
     Region          13..321
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(19..20,22,62..64,83,111..112,115..116,118..119,122,
                     126,128,136,138,140,142,144..149,150..154,172..173,
                     177..178,276..277,285,291..297,299..302,304)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(63,84..86,109,247,295,298)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240626"
     Site            order(85..86,113,185..187,190,217..219,223..224,245..247,
                     271..272,295,297..298)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 mrdkakgdgi vkpkvyiaep vptfvenyls ehcdyekweq nekvprdvll ekiqdkdgll
       61 nfgsainael leaapnlkvv snisvgydnf dlqamekrnv igtntpyvld dtvadlvfal
      121 mlsagrrvce ldsyvkngkw naeigkehfg ldvhhrtigi igmgrigeav akrakfgfdm
      181 dvlyynrrrk eeaeqkfdat ycdlqtllkq sdfivlltpl tdetyhlige kefslmketa
      241 ifinasrgkt vdeealiqal tekkifaagi dtftqepiqk dnpllslqnv vtlphigsat
      301 lktrqqmamt aaenlvaalq gktppnivrg
//
LOCUS       WP_284998472             482 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Bacillus paranthracis].
ACCESSION   WP_284998472
VERSION     WP_284998472.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..482
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53465
     Region          32..365
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkktivfvlt ifilfsgfat qsyalsdsks vaiqalldda crtsgvpgms lsiladgevf
       61 yfssgyadle kglsasentl yelasvskaf tgmgilllee qgllsmtdpi qkylpwftlk
      121 yqgkpvdmqn ltlnnflhht sgltnirhlq nipqgntpdm lqktvetlvd aelafspgeq
      181 ynygtinydv lglvieivsr qsyedfmkeq vflplglhqt yvykedaqat gqlaqgyrss
      241 ffittpfnap dyagnkpagy iisntkdmar wmgiqmgivq dipeifhrai ekshrgdmsv
      301 savndmyyaa gwsvnaeqtf iehtggnpnf stkvailpne rtaicllsng antninlvlq
      361 vknilngnlt qsyeisgtql ldiilsstti ilcllavllf flglrkgktn eqqpmtkkrt
      421 ivtiifliat iaqcimffaf dwstiliwqt ysvltaliss tlltasitwf vythrldasv
      481 rk
//
LOCUS       WP_284998485             487 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Bacillus paranthracis].
ACCESSION   WP_284998485
VERSION     WP_284998485.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..487
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55634
     Region          157..485
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 msklslkigt yflilalcie tiafvsfyks iskmrieeet lallekgnry ndkitqrakw
       61 safakekkhg eraeynknpk rpiypefdia deaehlvese siansdiaii itdnngkiis
      121 tsepvtkamq kqltcktepi panglvvekn wkkskfittv sslntaefqg klymllktsf
      181 lenmllklmn qfliisvltv ilttisvfvf srviteplik mkratekmsk lnkpiqlgik
      241 rndelgslak tiedlsselt ymkkernefl asvahelltp ltymkgyakv akrdtltkee
      301 reeylqiied etdsvtdlvq dlfmlvqleq hqfvikkqkv llrpflermv ektkttltnk
      361 qmqlhvyckd dlevciderr meqvmlnllh nayqhslent titirvltet nsftisvqde
      421 gegipeedip hifdrfyrvd ksrtratggk giglavakei velhngailv tsklgvgttf
      481 iielpfe
//
LOCUS       WP_284998704             927 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Escherichia coli].
ACCESSION   WP_284998704
VERSION     WP_284998704.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 927)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..927
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..927
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=104077
     Region          22..443
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          512..927
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mrnlcflltl vatlllpgrl iaaalpqdek litgqldngl rymiyphahp kdqvnlwlqi
       61 htgslheedn ergvahfveh mmfngtktwp gnkvietfes mglrfgrdvn aytsydetvy
      121 qvslpttqkq nlqqvmaifs ewsnaatfek levdaergvi teewrahqda kwrtsqarrp
      181 fllantrnld repiglmdtv atvtpaqlrq fyqrwyqpnn mtfivvgdid skealalikd
      241 nlsklpanka aenrvwptka enhlrfniin dkenrvngia lyyrlpmvqv ndeqsfveqa
      301 ewsmlvqlfn qrlqeriqsg elktisggta rsvkiapdyq slffrvnard dnmqdaanal
      361 maelatidqh gfsaeelddv kstrltwlkn avdqqaerdl rmltsrlass slnntpflsp
      421 eetyqlskrl wqqitvqsla ekwqqlrknq dafweqmvnn evaakkalsp aailalekey
      481 ankklaayvf pgrnlsltvd adpqaeissk etlaenltsl tlsngarvil aksageeqkl
      541 qiiavsnkgd lsfpaqqksl ialankavsg sgvgelssss lkrwsaensv tmsskvsgmn
      601 tllsvsartn npepgfqlin qrithstind niwaslqnaq iqalktldqr paekfaqqmy
      661 etryaddrtk llqenqiaqf taadalaadr qlfsspadit fvivgnvaed klvalitryl
      721 gsikhsdspl aagkpltrat dnasvtvkeq nepvaqvsqw krydsrtpvn lptrmaldaf
      781 nvalakdlrv nireqasgay svssrlsvdp qakdishlla ftcqperhde lltlanevmv
      841 krlakgiseq elneyqqnvq rsldiqqrsv qqlantivns liqyddpaaw teqeqllkqm
      901 tvenvntavk qylshpvnty tgvllpk
//
LOCUS       WP_284999050              95 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Bacillus paranthracis].
ACCESSION   WP_284999050
VERSION     WP_284999050.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 95)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 95)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 95)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..95
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=10879
     Region          14..87
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(17..18,22..24,38..40,49..52,54..55,58..59,61,67..69,
                     74..76)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mnytkinitd eniemlktls hpariqiiti lmqhnilnvs elvdilqipq atvsqhlskm
       61 kgkilgydrr glevyyyinn pkvpmiieif sptik
//
LOCUS       WP_284999347             417 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Escherichia coli].
ACCESSION   WP_284999347
VERSION     WP_284999347.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..417
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=46681
     Region          167..404
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 msfcwneins gikslililc ifslmtlslw ddvatkflha agiisalyfl vtpkktitnn
       61 ptllifislc llgivniiwy shykisgsvy tnayrgpmet gkialcsafi flvlfaknem
      121 itkikfgkli lfaslatqll ffahamwqhf ylnvdrvals ashattagyi ilfpsllasi
      181 lilksvfrhk ttlytinfml slcavivtet raailvfpff alilivmdsy inkrinykly
      241 cfitiallag vfsfkdtllm rmndlnndlv nyshdntrts vgarlamyev glktyspigq
      301 slekraekih eleekeprls galpyvdshl hndlidtlst rgipgvvlti lafsailiya
      361 lrtakepyil illfsllvvg lsdvilfskp vptavfitii llcayfkaqs dqcllek
//
LOCUS       WP_284999688             261 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Bacillus paranthracis].
ACCESSION   WP_284999688
VERSION     WP_284999688.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 261)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         <1..261
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <1..253
                     /region_name="KinB"
                     /note="Sporulation sensor histidine kinase B [Cell cycle
                     control, cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG5806"
                     /db_xref="CDD:444508"
ORIGIN      
        1 lyiiyfiilp tvlmlfvvyf nevlkdavcm rsklikmekm eivsqlaasi shevrnpltv
       61 vkgftqllkt pnltpesrde yikhileelh haqgiiddyl tfakpasekl deisveqeln
      121 rvinmilplc nmntihitkd fstativgnk qhfqqcflnl lkngieampn ggtlnisssi
      181 snnkviirie dsgigmsqeq inrfgepyfs tktkgtglgt mvavkiietm qgnlkirsvm
      241 nkgttltitf pkcntnasnn k
//
LOCUS       WP_284999909             437 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Bacillus paranthracis].
ACCESSION   WP_284999909
VERSION     WP_284999909.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..437
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49956
     Region          67..>249
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mnhiqtnfss ffnkitigam laffvyscwt afetskqffg gsttsvtiil aifvilillv
       61 atilqyrftd kqfliflisi sivvrlsmll fvdapiigdm kmmyesakei aignnigtit
      121 hlpfiiyesv iirifgdtlf alqlfnvlfc agtaffiyri aamvfgeecg riastfyvly
      181 ipnifmssvl tpeslaiflf yfacyillyk gldhpymwvf sailfacsnm ifpmglflpi
      241 fitiyvllie alqsatkqkv llktigilil fysahfsvny giktmglsqy tisnetyvqs
      301 vligkaqree kvsknqsvte hidqklkeie gerfkllepv inqfsdegin stlfkcekli
      361 yiavtlfmti allhflikkq qnegymlfll lisgyvllkl fqvdmayynl ivpalfilqs
      421 fgvymsyvyc qkiffrk
//
LOCUS       WP_284999919             372 aa            linear   BCT 25-DEC-2024
DEFINITION  MDR family MFS transporter [Bacillus paranthracis].
ACCESSION   WP_284999919
VERSION     WP_284999919.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023665
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..372
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41311
     Region          12..353
                     /region_name="MFS_MdtH_MDR_like"
                     /note="Multidrug resistance protein MdtH and similar
                     multidrug resistance (MDR) transporters of the Major
                     Facilitator Superfamily; cd17329"
                     /db_xref="CDD:340887"
     Site            order(32,82..83,85..87,90,109,112..113,116,185,188..189,
                     192..194,197,224,228,277..278,282,286,302,305..306,
                     309..310,313)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mfsylsinls pfsafqvgtv ltviiitsrv iplfsgliad kigyiimmia glflrgigfi
       61 algicsdfyt isissaligf gtafyepaar aifgsqpahl rknlftylnl sfncgaiigp
      121 iaggflllld piyafsltgs lmlifalify llknhfqvtt entsmtlgiq ailqnksfll
      181 fsfimiffyi mftqltvalp lhmknisnsn qlatlvitin aitgvifmvl frklfhkynt
      241 lsiikygvll msisfllipl fqhpywlfic vilftigetl vlpnadiaia nysnelytat
      301 ffgfyqlsla fgfiignytg tsftsnlsgv ytpwlifggi gligfislhi lntkkdflkk
      361 iyayckntnl qq
//
LOCUS       WP_284999972             353 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial [Bacillus
            paranthracis].
ACCESSION   WP_284999972
VERSION     WP_284999972.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         <1..353
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          1..352
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 gaarfaynyc krmsdryykl fgksvsqlal qkrftkikkr kryewlkein aqvpkqaskd
       61 fdtarkhsfk kykngyhtsy kskkdviqgf yanyerlvig kkvvhiqsig evktsqqlpr
      121 nkkpsnprvt fdgrhwwisv gfqedfesqe ltnesigvdv glkelfvasn gmkerninkd
      181 akvkkllkrk ksaqrdmsrr fkkgvkiqsa gyekakaehl rlsrkimnir nnhihqatak
      241 lvktkpmriv vedlsisnll knkklskals fqklnfffqc lsykcekygi ayekadkwfa
      301 sskicsccgv kydhsvqpeg qwslkirewr cascnsyhdr dvnaainlsr wvk
//
LOCUS       WP_285000059             574 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Bacillus paranthracis].
ACCESSION   WP_285000059
VERSION     WP_285000059.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 574)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..574
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=67037
     Region          522..>561
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mdqlkqlfqs tllvayplfq nvknnerifh kwkglctlin sdvnyiddpm ytsasfkkfa
       61 nwisykesqg vgimeivaqi eeyrpevfel landiekefe iplvkqkrek nyteeqqsfi
      121 ehssagfmyh ltdtiaknnf tedkelnahi aelpdksnsl vvvssrfndg dmklrgagel
      181 nrwntlvdst fvdrvmddlt adcldivtei wvksanaens svhigyeeil emcsmkqvrn
      241 gksyyrkedr lkimerlaal asifiyvned neivilndde npneslaykk qrvrrlfvmd
      301 eivfakdiet demlgiesmn vapgtflsky lfgsekltgl lskkaleyns kqqryhkrlt
      361 rylswrwriq qayqhlvhpy siggpkglls vmgvsmnqnp arirnvfekt lddlmrdevi
      421 kewqyqtpid egkcsgrnwl enywlnlkvt vtptdelvsl qqellqkkki apknklietl
      481 akepvievqd mrtediqplq lnqqqvnkdi nwyqqkilqy keenkcslrd iakeieisps
      541 nlsklltgkr krlseetrnk ldkwierqev vnll
//
LOCUS       WP_285000527             183 aa            linear   BCT 25-DEC-2024
DEFINITION  YagU family protein [Escherichia coli].
ACCESSION   WP_285000527
VERSION     WP_285000527.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..183
                     /product="YagU family protein"
                     /calculated_mol_wt=20676
     Region          6..180
                     /region_name="YagU"
                     /note="Uncharacterized membrane protein YagU, involved in
                     acid resistance, DUF1440 family [Function unknown];
                     COG3477"
                     /db_xref="CDD:442700"
ORIGIN      
        1 mainglfvrt dpqrrrygva llvgvlsgii safvkwgaev plpprtfsgg rdefnppyif
       61 lrdylgidpt qtvytfsehi inpvmvmhii fslvfaigyc vvaeifpkvk lwqgilagli
      121 vtvavhgifc palnltpplt qlpfdeyase ilghifwfwi ieimrrdlrn rithepdpev
      181 vir
//
LOCUS       WP_285000625             973 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Bacillus paranthracis].
ACCESSION   WP_285000625
VERSION     WP_285000625.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..973
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..973
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=83838
     Region          <50..930
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 megndenlki krsihsnfkl spdlvgptfp pvptgmtgtt gptgstgatg stgstgvtgp
       61 tgstgatgst gatgvtgptg ntgvtgstga tgntgatgdt gptgstgatg stgptgntgv
      121 tgdtgstgst gstgvtgptg stgvtgstga tgstgatgnt gatgdtgptg stgsagstgs
      181 tgvtgptgst gatgsagatg vtgptgstga igstgatgvt gptgstgatg sagatgvtgp
      241 tgstgatgst gatgstgatg stgstgstgp tgstgstgdt gptgstgstg ntgatgntgp
      301 tgstgptgsm gstgvtgptg ntgitgstga igntgatgdt gptgstgatg vtgptgntgv
      361 tgatgstgst gstgstgstg ptgstgatgv tgptgntgvt gatgstgatg ntgstgstgp
      421 tgstgatgsa gatgntgstg stgptgntga tgstgatgst gatgstgatg stgaigstgp
      481 tgstgatgst gptgntgvtg ntgatgdtgp tgstgstgst gvtgptgntg vtgstgatgn
      541 tgatgdtgpt gstgatgstg ptgntgvtgn tgvtgdtgst gstgptgstg ptgntgvtga
      601 tgstgatgdt gatgstgptg stgstgntgv tgvtgstgat gvtgptgntg aigstgptgs
      661 tgstgvtgpi gntgvtgstg ptgntgvtga tgstgatgnt gstgstgptg stgstgstgp
      721 tgntgvtgat gstgatgdtg stgstgptgs tgatgdtgpt gstgttgstg ptgntgatgs
      781 tgatgntglt gstgptgstg atgntgptgs tgttgstgpt gntgptgdtg atgatgvstt
      841 atyafannts gsvisvllgg tniplpnnqn igpgitvsgg ntvftvasag nyyiaytinl
      901 tagllvssri tvnssplagt inaptvatgs fsatiianlp agaavslqlf gvvalatlst
      961 atpgatltii rls
//
LOCUS       WP_285000658            2385 aa            linear   BCT 25-DEC-2024
DEFINITION  amino acid adenylation domain-containing protein [Bacillus
            paranthracis].
ACCESSION   WP_285000658
VERSION     WP_285000658.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 2385)
  AUTHORS   Konz,D. and Marahiel,M.A.
  TITLE     How do peptide synthetases generate structural diversity?
  JOURNAL   Chem Biol 6 (2), R39-R48 (1999)
   PUBMED   10021423
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01733.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2385
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..2385
                     /product="amino acid adenylation domain-containing
                     protein"
                     /calculated_mol_wt=267852
     Region          8..>2120
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
     Region          2133..>2287
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mpnsqkvrhs lssaqsgmwf aqkldplnpi yntgqyvein gnihqdifel avrkvvmeae
       61 alhvrfeede igpwqviees qfhmhfidvr keenpeeaak awmkndlsmp vdlkkdtlft
      121 ealiqvennr ffwyqrihhi vmdgygfsll sqkvaneyts lieetnknek tfgslakvvq
      181 edmeyreskq fqedrafwle kfadepdvvs laeraprtsn gflretacls ssstktlled
      241 inisliswpe fivavtsiym hkltgendiv lglpmmgrlg sasihtpsmv mnlvplrltv
      301 tpnitlvell qqvskeirdv rrhhkyrhee lrrdlkllge nqrlfgplvn vmpfdyglnf
      361 ggnrgithnl sagpvddlsi nvykrfdqne lmihfdanpe vyngaelalh kerfmqllel
      421 minayqkdes igkinitlpe enhkvllewn etkeddelis lpisfekqvq ktpnklaitc
      481 dgvnftykel neranelahy lveegirpnq fvalvfprsi emvtsmlavl kagaaylpid
      541 peypaeriny ivndakpvci ithssvsskl viendmkkii lddeetklal htysrmniec
      601 kndvsilnpa ytiytsgstg npkgvivpmr glsnflmamq qkfslhehdh llavttfafd
      661 isaleiylpl isgasltiaq kediqepsal ttllqeervt imqatptlwq alvtdypekl
      721 qglnilvgge alpahlankl kelgcsltnl ygptettiws tvmnideres gippigkpiw
      781 ntdvyvldag lqpvppgvig elyiagegla sgylgkpelt aerfvanpyg kpgqrmyrtg
      841 dlvkwrsdgv leymnradhq ikirgfriel aeiemviqry envkqavvmv redrpndkri
      901 iayivageke tihlseirsy vseslanymv psafvlleel pltpngkvnr kklpapdfng
      961 mnnervarnp keeilchlfa evlgvsrisi ddnffemggh sllasrlmar iretlsvelg
     1021 igklfesptv aelakqldra ktarpaikkv srpnevplsf aqrrlwflhc legpsptyni
     1081 plvirlsgkl negalqgafy dvvekhetlr tifpnvlgss yqkilhmenl nlemiitntc
     1141 knelesvlae avrysfnldv epavrlqlft vnenehvlli llhhivgdgw slqpltrdft
     1201 aaykarcqgn kvqletlpvq yadyalwqqq llgdettqes listqldfwk kelkglpdql
     1261 elptdyqrpm etsyrgetih fhidagmhsr lvelarkngv slfmvlqagl salftrlgag
     1321 tdipigspia grnddvlsdi vglfvntlvl rtntsgdpsf kellnrvkqa nlaayenqdv
     1381 pferlvevln pvrtrnshpl fqvmlafqnt peaifdvpdi etsleiqsvg sakfdltfei
     1441 seshgvdgtp nglhgllefs tdlykhetvq klierfilll ddaatnpdqs igrleiltla
     1501 ekntvlekwn ggfqiapemt lpqlfekqvh inpnaiavvf enkkltyeel nrkankiarf
     1561 liakgigpdq lvalamprsl nmvvsllavl kagagylpld pdypadrisf mlhdakpscv
     1621 ltnseveiec nealkvlvdn vkvieeiekh sednidemer vkpltpshia yviytsgstg
     1681 rpkgvmiphq nvvrllgatd hwfqfdgndv wtmfhsyafd fsvweiwgpl lyggrlvvvp
     1741 htvsrspkef lqllvkekvt vlnqtpsafy qlmqadrenk eigqqlslry vvfggealel
     1801 srledwysrh phnapklinm ygitettvhv syieldestv slransligc sipdlkvyvl
     1861 dhylqpvppg vvgemyvaga glargylgra gltaerfiad pfgkpgtrmy rtgdlarwrq
     1921 dgtldyigra dhqikirgfr ielgeieavi mkhptveqva vivredqpgd krlvsyivas
     1981 nneaidmnem rqfasgslpd ymvpyafvvv nefpltpngk ldrkalpape fiissssrgp
     2041 rtpqeemlcd lftevlsvpq igiddgffdl gghsllavql msrikealgi elnigtlfaa
     2101 ptvaglaerl evgngqsald vllplrasgn qlplfcvhpa gglswcyagl mkslgtdypi
     2161 ygvqargiak neelprslee maadylkhvr evqphgpyrl lgwslggnvv hamaaqlqne
     2221 geevellvml dsypghflpn teapteeeal iallalggyd pdnmdgkplt mesaveilrt
     2281 dgsalaslee etilnlkety vnsvgllgry vpkvyngdil ffrstvipdw fdpispntwl
     2341 nyldgkimqh didcrhkdlc qpgplteigq vlakylqnkk gvrrv
//
LOCUS       WP_285000704             287 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Bacillus paranthracis].
ACCESSION   WP_285000704
VERSION     WP_285000704.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..287
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33792
     Region          <134..286
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 miqqlktyyg edikineavl sedyswflve gnkvgirkir lhqkehqlls silipihadt
       61 fyktekeksw yealyrnnni pirsvrflhf fttqsivere efqdalqsmf sftttmlwet
      121 sqagvlilee nitesvlqta ldtletdffi slsffvgrry sqtteftyly qwertlfsvl
      181 spylskkity ieqllpyqlm islpkeerkk ytnqllenis ndkelidsvk vffqcnlnvs
      241 laakqlylhr ntlqyridkf iektginikt fegavavyma flsldis
//
LOCUS       WP_285000883             909 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Bacillus paranthracis].
ACCESSION   WP_285000883
VERSION     WP_285000883.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 909)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 909)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 909)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 909)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..909
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..909
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=104907
     Region          269..906
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mkkqthvsil isitllsivi hyvampflye ysfsfqilig mstlfidiia csyilyfsnm
       61 keglprlfwt ilcvgtlsyf igdivvayqr lilkdyytfv dpsdffyllf lisfafafly
      121 eiiynrdlle klfmicdici ivtaqftlsy ylliertihi sstsyidifv qltypmtdll
      181 ffliginllf kplsllskkv gallgsalll yattdaiyay ikyfipeysm ftvtplyqvt
      241 lvlvaiacii htkepekqeq vlltpkfgea irlslpyisv vmlivfilie yvfapiivig
      301 lmitfsfvli rhslvrkqnk illlaqmqfn selekqielr tedlveqkne lyhnqqmfks
      361 lyehhpdpif tldlygnfln vnnagttllg yqtnellnqp yysltyeedl eeiinafhrv
      421 kkgksislei rayhknrdiy ylhvtavpif lkdhisgvyl mikditeskq qqeqinflay
      481 hdtltelanr rafhqyveqa iarskiskmp favmfldldr fkvindtlgh rvgdllliav
      541 akrlesiatp nmklarlagd eftilienyk krpdvkkiad tivaamnepf eienqhlqis
      601 psigiaiype agedplsilq hadmamyeak nkgkngssly tkelykkter kariekdlpl
      661 alvneefylv yqpqidittk kiigaeallr wkhpllgdip pcefipivee tpqviplghw
      721 vlnescrqlk iwhtfgykdl kisvnlsake fqqnnlieni lqiitdvkvd pkdvtlelte
      781 riamideket lsklkqlkey giqtsiddfg tgysslayls ifpidtlkvp reftqladhr
      841 peeraivsti lslantlnls vvaegietek qlkflqknnc kymqgyyfsk pltshqfikf
      901 lqktpsmnq
//
LOCUS       WP_285000910             243 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Bacillus paranthracis].
ACCESSION   WP_285000910
VERSION     WP_285000910.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..243
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28018
     Region          <6..240
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mnqtigriee isfysaslqe dvtllvylpv nytplhkhtv viaqdgrdyf qlgkahrvie
       61 rlreteeidr tiivgipykn vhdrkekyfs nevknaayir flahelapyi denyptyqmg
      121 kgrvligdsl ggtvsfmtal myphtfgkvv mqspfvdetv mnlakdfknp ealelyhvig
      181 teetavkrtd gqvsdfvgpn relntlltdr nfithyeefe gnhtwkywqt dlpkafshml
      241 smk
//
LOCUS       WP_285000792             307 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Bacillus
            paranthracis].
ACCESSION   WP_285000792
VERSION     WP_285000792.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 307)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..307
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=34602
     Region          3..297
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkkilvtggs gwigkyvvhs liqkgyevha tyntnkpshl schwhkvnll cdeevkkliy
       61 dmkpshlihl aweavppacy vsinnyywlt ssisliqhft tcggkrvvva gtgaeyewfn
      121 gvlfedspll syktpyslck nalhswlqty akqtglsmcw grifhmygph eqgnrlvsni
      181 itsllkneea lcthgkqsrd flhvsdvaha lvtilehdvt gtiniasgqs vqikelasii
      241 akkigkehli klgaipfskd eplfvgvhve rlktevnwkp tydlntgiee tiswwesfiq
      301 khngthh
//
LOCUS       WP_285000943             364 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Bacillus paranthracis].
ACCESSION   WP_285000943
VERSION     WP_285000943.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..364
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=42908
     Region          <3..100
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnehiqqmid wievnlkkef sldelsrymg yspyycsfkf hqvtgfsirr yillrrlyls
       61 iedlkngrki idialdynys sqeaysralk svfgmnpref qlnqlpiqsf vklninkege
      121 fnmnisrkie veqlrnakse lfdkdvlnil ngqmmyeefk neklmgdsdy apfneamcvn
      181 qvttlvfdke fiktraaghn ssvesytkkv idplkklftk eykcivlwfg edmfcqmnll
      241 tilsyleqsr yegkvylnsf redefkvnqi elelgnyssv ynevlvnhkk tfykvppvmy
      301 qaidlylkml kednavmkfi sknkdlstqe lltklfqlfp tigygdsqyi evinkikkka
      361 tpki
//
LOCUS       WP_285001222             280 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Escherichia
            coli].
ACCESSION   WP_285001222
VERSION     WP_285001222.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..280
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30950
     Region          11..264
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mrdllqrpdl fsintatlgy ktplpaiida caargigaia pwrrelqged lqqiarqlaa
       61 snmsvsglcr styytaptla erklaiddnr ralddaavln aacymqvvgg lpqgtkdlye
      121 areqvkqgir qllphskdvg vpialeplhp mtaadrsclc tlrqaldwcd eldpddefgl
      181 gvavdvyhvw wdpelasqil ragkrilafh vsdwlvpttd lvndrgmpgd gvinipsirr
      241 lvenagfnga ieleifspyw wqkdinstld isvdriahyc
//
LOCUS       WP_285001248             790 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Escherichia
            coli].
ACCESSION   WP_285001248
VERSION     WP_285001248.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 790)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 790)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 790)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 790)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..790
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89122
     Region          31..610
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mkrvlipgvi lcgadvaqav ddknmymhff eemtvyapvp vpvngnthyt sesierlptg
       61 ngnisdllrt npavrmdstq stslnqgdir pekisihgas pyqnaylidg isatnnlnpa
      121 nesdassatn isgmsqgyyl dvslldnvtl ydsfvpvefg rfnggvidak ikrfnaddsk
      181 vklgyrttrs dwltshiden nksafnqgss gstyyspdfk knfytlsfnq eladnfgvta
      241 glsrrqsdit radyvsndgi vagraqyknv idtalskftw fasdrfthdl tlkytgssrd
      301 yntstfpqsd remgnksygl awdmdtqlaw aklrttvgwd hisdytrhdh diwytelsct
      361 ygditgrctr gglghisqav dnytfktrld wqkfavgnvs hqpyfgaeyi ysdawterhn
      421 qsesyvinaa gkktnhtiyh kgkgrlgidn ytlymadris wrnvslmpgv rydydnylsn
      481 hnisprfmte wdifanqtsm itagynryyg gnildmglrd irnswtesvs gnktltryqd
      541 lktpyndela mglqqkigkn viaranyvyr eahdqiskss rtdsatktti teynndgktk
      601 thsfslsfel aeplhirqvd inpqivfsyi kskgnlslnn gyeesntgdn qvvyngnlvs
      661 ydsvpvadfn nplkislnmd fthqpsglvw antlawqear kariilgktn aqyiseysdy
      721 kqyvdeklds sltwdtrlsw apqflkqqnl tisadilnvl dsktavdttn tgvatyasgr
      781 tfwldvsmkf
//
LOCUS       WP_285001363             110 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_285001363
VERSION     WP_285001363.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..110
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          <10..106
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 aagtvsqpgr nvraksglnr sildqgwyem rrqleykqlw rggqvlavpp aytsqrcacc
       61 ghtakenrls qskfrcqvcg ytanadvnga rnilaaghav lacggcqqtg
//
LOCUS       WP_285001384             847 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Bacillus paranthracis].
ACCESSION   WP_285001384
VERSION     WP_285001384.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..847
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=73693
     Region          <50..842
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 megndenlki krsihsnfkl spdlvgptfp pvptgmtgtt gptgstgatg stgstgvtgp
       61 tgstgatgst gstgvtgptg stgatgstgs tgvtgptgst gvtgstgatg stgatgntga
      121 tgdtgptgst gsagstgstg vtgptgstga tgstgstgvt gptgntgatg stgatgstga
      181 tgstgatgst gaigstgptg stgstgvtgp tgntgitgst gatgntgatg dtgptgstgs
      241 tgstgatgst gstgstgatg stgatgstgs tgstgstgst gptgstgstg dtgptgstgs
      301 tgstgatgnt gptgstgptg smgstgitgp tgntgatgst gatgntgatg stgstgstgp
      361 tgstgstgvt gptgntgvtg ptgstgatgd tgptgstgst gntgvtgatg stgstgstgs
      421 tgstgptgst gstgvtgptg ntgatgstgs tgstgstgst gvtgptgntg vtgstgptgn
      481 tgvtgatgst gatgdtgatg stgptgstgs tgvtgptgnt gvtgatgdtg ptgstgatge
      541 tgptgstgvt gnigptgstg ptgetgptgs tgvtgnigpt gstgatgetg ptgstgvtgn
      601 tgptgstgpt getgptgstg atgntgptgs tgatgstgpt gntgvtgntg ptgetgptgs
      661 tgvtgnigpt gstgatgetg ptgstgatgd tgltgstgpt getgatgatg vsttatyafa
      721 nntsgsvisv llggtniplp nnqnigpgit vsggntvftv anagnyyiay tinltagllv
      781 ssritvnssp lagtinaptv atgsfsatii anlpagaavs lqlfgvvala tlstatpgat
      841 ltiirls
//
LOCUS       WP_285001484             481 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein, partial [Bacillus paranthracis].
ACCESSION   WP_285001484
VERSION     WP_285001484.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..>481
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          21..49
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(22,25..26,29..30,32,55,58..59,62..63,65..66,89,
                     92..93,96..97,100)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          24..317
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          53..83
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          88..116
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          152..178
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(154..155,158..159,161,185,188..189,192..193,
                     195..196,219,222..223,226..227,230)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          183..213
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mgknqriyke ngqvisfnql adffykkgmr aykgqklqda ikyfrraaqs ekepfilcql
       61 atvlseagey qesnqtffkl vrsnpeleqc yyfiannyay mglfqqakky adrylevaee
      121 kefvedtlel leimeeeamg aeeiededdl ivmqeeanry irngqleeai atleivtkdy
      181 pefwsghnnl aiahfqsgnv dkalkltemi leknpgniha lcntliflys igehkqveal
      241 agqlvsvypi sfehrlklgt tlatighfep aykwfkllkr qgyegdvsfy ywfaysaymv
      301 kdqqvaekmw qhvvelhpdk kgkepwnaln ladegqnvlf eelrksfqqs atleeqmlal
      361 ylmnelstpe kvgfffdvtq akngvpivsq lakyffllns hksipadlqq feqcariada
      421 lynytkkdde lieeclqfwf ctfirlytsg avftnvygws aaveyivrse qgnkmtqsel
      481 g
//
LOCUS       WP_285001497              71 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family transcriptional regulator, partial [Bacillus
            paranthracis].
ACCESSION   WP_285001497
VERSION     WP_285001497.1
KEYWORDS    RefSeq.
SOURCE      Bacillus paranthracis
  ORGANISM  Bacillus paranthracis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 71)
  AUTHORS   Nazaret,F., Alloing,G., Mandon,K. and Frendo,P.
  TITLE     MarR Family Transcriptional Regulators and Their Roles in
            Plant-Interacting Bacteria
  JOURNAL   Microorganisms 11 (8), 1936 (2023)
   PUBMED   37630496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 71)
  AUTHORS   Will,W.R. and Fang,F.C.
  TITLE     The evolution of MarR family transcription factors as
            counter-silencers in regulatory networks
  JOURNAL   Curr Opin Microbiol 55, 1-8 (2020)
   PUBMED   32044654
REFERENCE   3  (residues 1 to 71)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   4  (residues 1 to 71)
  AUTHORS   Grove,A.
  TITLE     Regulation of Metabolic Pathways by MarR Family Transcription
            Factors
  JOURNAL   Comput Struct Biotechnol J 15, 366-371 (2017)
   PUBMED   28694934
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 71)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (residues 1 to 71)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   7  (residues 1 to 71)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   8  (residues 1 to 71)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10581578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Bacillus paranthracis"
                     /db_xref="taxon:2026186"
     Protein         1..>71
                     /product="MarR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          3..>65
                     /region_name="COG3355"
                     /note="Predicted transcriptional regulator
                     [Transcription]"
                     /db_xref="CDD:442583"
ORIGIN      
        1 mtvkqvfdik evtqteklvl iylyqrgcek khtevkhadi iekcnisqss vnralksles
       61 kslidvfyqs g
//
LOCUS       WP_285002039             184 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase, partial [Escherichia
            coli].
ACCESSION   WP_285002039
VERSION     WP_285002039.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..184
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
     Region          50..145
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 qlrerirlmr arldnaapva eiraesqlfv spapicdrlv tlaeisnrdh ilepsagtga
       61 ilrairdtap eamcdavein sglvrylren fngvrvqcgd fmewqpvqyy sriimnppfs
      121 hgqdirhilr afsllrpggv lvavclngpr qqekllpfsd vreelprgtf aytdvptmii
      181 rlra
//
LOCUS       WP_285002254            1504 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Escherichia coli].
ACCESSION   WP_285002254
VERSION     WP_285002254.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 1504)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1504)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1504)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1504)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1504
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..1504
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=166392
     Region          192..1504
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mgtglanadd slpssnyapp aggtffllad ssfssseeak vrleapgrdy rryqmeeygg
       61 vdvrlyripd pmaflrqqkn lhrivvqpqy lgdglnntlt wlwdnwygks rrvmqrtfss
      121 qsrqnvtqal pelqlgnaii kpsryvqnnq fsplkkyplv eqfryplwqa kpfepqqgvk
      181 legassnfis pqpgniyipl gqqepglylv eamvggyrat tvvfvsdtva lskvsgnell
      241 vwtagkkqge akpgseilwt dglgvmtrgv tddsgtlqlq hispersyil gkdaeggvfv
      301 senffyesei yntrlyiftd rplyragdrv dvkvmgrefh dplhsspivs apaklsvlda
      361 ngsllqtvdv tldarnggqg sfrlpenava ggyelrlayr nqvysssfrv anyikphfei
      421 glalakkefk tgkavsgklq llypdgepvk narvqlslra qqlsmvgndl ryagrfpvsl
      481 egsetvsdas ghvalnlpaa dkpsrylltv sasdgaayrv tttkeilier glahyslsta
      541 aqysnsgesv vfryaaless kqvpvtyewl rledrtshsg elpsggksft vnfakpgnyn
      601 ltlrdkdgli laglshavsg kgstahtgtv divadktlyq pgetakmlit fpepideall
      661 tlerdrveqq sllshpanwl tlqrlndtqy earvpvsnsf apnitfsvly trngqysfqn
      721 agikvavpql dirvktdkth yqpgelvnve ltsslkgkpv saqltvgvvd emiyalqpei
      781 apnigkffyp lgrnnvrtss slsfisydqa lssepvapga tnrserrvkm lerprreevd
      841 taawmpsltt dkqgkayftf lmpdsltrwr itargmngdg lvgqgraylr seknlymkws
      901 mptvyrvgdk paaglfifsq qdnepvalvt kfagaemrqt ltlhkganyi sltqniqqsg
      961 llsaelqqng qvqdsistkl sfvdnswpve qqknvmlggg dnalmlpeqa snirlqsset
     1021 pqeifrnnld alvdepwggv intgsrlipl slawrsladh qsaaandirq miqvnrlrlm
     1081 qlagpgarft wwgedgngda fltawawyad wqasqaigvt qqpeywqhml dsyaeqadnm
     1141 pllhralvla waqemnlpck tllkgldeai arrgtktedf seedtrdind slildtpesp
     1201 ladavanvlt mtllkkaqlk stvmpqvqqy awdkaansnq plahtvvlln sggdatqaaa
     1261 ilsgltaeqs tieralamnw lakymatmpp vvlpapagaw akhkltggge ywrwvgqgvp
     1321 dilsfgdels pqnvqvrwre paktaqqsni pvtverqlyr litgeeemsf tlqpvtsnei
     1381 dsdalyldei tltseqdavl rygqvevplp pgadverttw gisvnkpnaa kqqgqlleia
     1441 rnemgelaym vpvkeltgtv tfrhllrfsq kgqfvlppar ymrsyapaqq svaagsewtr
     1501 mqvk
//
LOCUS       WP_285002277             337 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_285002277
VERSION     WP_285002277.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>337
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          1..337
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkrlqafkfq lrpggqqere mrrfagacrf vfnralarqn enheagnkyi pygkmaswlv
       61 ewknatetqw lkdapsqplq qslkgleray knffqkraaf prfkkrgqnd afrypqgvkl
      121 dqensriflp klgwmryrns rqvtgvvknv tvsqscgkwy isiqtesevs tpvhpsasmv
      181 gldagvakla tlsdgtvfep vnsfqknqkt parlqrqlsr kvkfsnnwqk qkrkiqrlhs
      241 cianirrdyl hkvtttvskn hamiviedlk vsnmsksaag tvsqpgrnvr aksglnrsil
      301 dqgwyemrrr lennqiwrgg qvlavppayp sqrcayc
//
LOCUS       WP_285002971             188 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_285002971
VERSION     WP_285002971.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>188
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          1..>183
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkrlqafkfq lrpggqqere mrrfagacrf vfnralarqn enhevgnkyi pygkmafwlv
       61 ewknatetqw lkdapsqplq qslkdleray knffqnraaf prfkkrgqnd vfrypqgvkl
      121 dqensriflp klgwmryrns rqvtgvvknv tfsqssgkwy isiqtesevs tpdhpsatmi
      181 gldavvak
//
LOCUS       WP_285003072             216 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_285003072
VERSION     WP_285003072.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>216
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          1..>216
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkrlqafkfq lrpgdqqece mrrfagacrf vfnralalqn enheagnkyi pygkmaswlv
       61 ewknatetqw lkdspsqplq qslkdleray knffrkraaf prfkkrgqnd afrypqgvkl
      121 dqensriflp klgwmryrns rqvtgvvknv tvsqscgkwy isiqtesevs tpvhpsasmv
      181 gldagvakla tlsdgtvfep vnsfqknqkk larlqr
//
LOCUS       WP_285003364             517 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Escherichia coli].
ACCESSION   WP_285003364
VERSION     WP_285003364.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..517
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=58782
     Region          20..>502
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mqmitsrqnr llrfllprre yttivtiagy lnvsektiqr dlrlleqwlg qwrinvekra
       61 gagvmlsaen iadllhldhl lvaeceeidg vmnnarrvki asqllsetpn etsisklser
      121 yfisgasivn dlrvieswla plglslirsp sgthiegseg qvrqamalli ngiinhnepq
      181 gvvysrldpg sykalvhyfg eeevlfvqsl lldmenelsw slgepyyvni fthilimmyr
      241 nthgnalsre edqtrqyden ifnvasqmih tieqriahtl pddevwfiyq yiissgvaid
      301 gqkdvsiish mqasnearli twrlitvfsd ivdcdfseds alydgllvhi kplinrlnyr
      361 ihirnplled ikaeladvwr ltqyvvnqvf ktwgenavse devgyltvhf qaamerqiar
      421 krvllvcstg igtshllksr ilrafpewti vdvisaanls qvlpdnieli istinlptvt
      481 mpvayvtaff ndadikrvte mviteklhha tsrvvei
//
LOCUS       WP_285003849             468 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein, partial
            [Escherichia coli].
ACCESSION   WP_285003849
VERSION     WP_285003849.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..468
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          34..465
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 hisdnlrefs dyvrhistif vsklledqgp gdniskifat midnmdqgvl vvddesrvqf
       61 vnqtalktlg vvqnniigkp irfrpltfes nfthghmqhi vswddkseli igqlhniqgr
      121 qlflmafhqs htsfsvanap dephieqlvg ecrvmrqlkr lisriapsps svmvvgesgt
      181 gkevvaraih klsgrrnkpf iaincaaipe qlleselfgy vkgaftgasa ngktgliqaa
      241 ntgtlfldei gdmplmlqak llraiearei lpigasspiq vdiriisatn qnlaqfiaeg
      301 kfredlfyrl nvipitlppl rerqediell vhyflhlhtr rlgsvypgia pdvveilrkh
      361 rwpgnlrels nlmeylvnvv psgevidstl lppnllnngt teqsdvtevs eahlslddag
      421 gtaleemekq mirealsrhn skkqvadelg igiatlyrki kkyellnt
//
LOCUS       WP_285004581             645 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: BglG family transcription antiterminator
            [Lactococcus].
ACCESSION   WP_285004581
VERSION     WP_285004581.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus (lactic streptococci)
  ORGANISM  Lactococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 645)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 645)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Lactococcus"
                     /db_xref="taxon:1357"
     Protein         1..645
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=74578
     Region          34..627
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mlsynldill fserrfwkld kilevtglks hefqrqlvel nqilqdknqr pleftnnvla
       61 ipeklesfee irfnieeyel tlseekrqll iyllcfskrs vlaisdfqsl lnvsrntvls
      121 dikklrqqld nenisleysr klgfylqgas kelrkttwrf lqelheesdy yvlskhlnlk
      181 nplfihqvgq qisrliaels vqvihsrylp mliylallqs hlgetdlfqe dvlevealli
      241 gmsdgnfeks gfdflyrigf eimenvmkla avqfedftkt faalrahlvp ayfrlkyhfe
      301 ienvlldkik tdysslfelm dlalsplhea cgeiseaera yfvilfggei ykkkytqslr
      361 aivlcvngis sslimrkrle nmfpsmtfil stavsdldki pafsydiifs tvpvmtdkkl
      421 yvmsafpdse eetrlynrla qdfnlpgfyk pnarailrai epyvdiknna tkkqltriid
      481 rklnnkktes ealgvmlsdl ltkekihftd ekldwrsaie laaqpllnqg eiepsyisai
      541 ikrveefgpy idlgmgialp harpedgvkk lgmsflrceq pvylqddlkh eikifivlaa
      601 idnethlral stltqilsnk delnkmltve tvaeleqifa ekege
//
LOCUS       WP_285004437             186 aa            linear   BCT 25-DEC-2024
DEFINITION  phage tail protein, partial [Escherichia coli].
ACCESSION   WP_285004437
VERSION     WP_285004437.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10304845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..186
                     /product="phage tail protein"
     Region          <1..92
                     /region_name="Phage_TTP_12"
                     /note="Lambda phage tail tube protein, TTP; cl11463"
                     /db_xref="CDD:472191"
     Region          102..181
                     /region_name="Big_2"
                     /note="Bacterial Ig-like domain (group 2); pfam02368"
                     /db_xref="CDD:396788"
ORIGIN      
        1 ddedadwtat gqgqksagdt sftlawmpge qgqqallawf negdtrayki rfpngtvdvf
       61 rgwvssigka vtakdvitrt vkvtnvgrps maedrstvta atgmtvtpas asvvkgkstt
      121 ltvafqpega tdksfravsa dktkatvsvs gmtitvkgva agkvnipvvs gngelaavae
      181 invtas
//
LOCUS       WP_285004846             400 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lactococcus garvieae].
ACCESSION   WP_285004846
VERSION     WP_285004846.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..400
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46805
     Region          99..370
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mnikkmangk yrfrekyqdk dgiwrevsit mnsksreaqr eafnaierri qeklqkneka
       61 ialiqemtvn dvfaqstkkr kmelapssfy qencflnvfl ksfgtkkikd vkarnlqdyi
      121 vtnsksiktm halkrginsi fkyayiaeyi dsnpidrldl pkdtrtkesv aklkqkfftl
      181 defntlikqm rhdansdeth rkidlleflf wtglrigeal alkwsdvdll ngkisitksw
      241 dtkkhllgnv ktidsireid vntycieivq nfkkynsefi fvtdkgkqih yiglsqflky
      301 egakaqlfgk npdyfslhml rhshvtylvn mgvpekmime rlghkdprmm mgvythilpe
      361 nratlcqald ystswgqnfd kqkipkkspk iieyretrgk
//
LOCUS       WP_285005171             102 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lactococcus
            formosensis].
ACCESSION   WP_285005171
VERSION     WP_285005171.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..102
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11553
     Region          11..68
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(15,19,44)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(18,43)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(25..26,37,40,44..45)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mdtqehraii aanikkylqm sgikqkdfas kigivpstls dylnmrstps qgviqkmadi
       61 lgveksdidt tyknklslnl drlidealfy kkevleekdr ef
//
LOCUS       WP_285005175             542 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Lactococcus formosensis].
ACCESSION   WP_285005175
VERSION     WP_285005175.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 542)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..542
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=62508
     Region          8..461
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(22,24,26,30)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(61,64,101,104,146,165,169,201,243,403)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(201,243,318)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          468..538
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; pfam16657"
                     /db_xref="CDD:435493"
ORIGIN      
        1 mnkqnwwqea vmyqiyprsf qdsngdgigd ikgiisrldy leklgitgiw lspvykspnd
       61 dngydisdye aimaefgtms dmetlileae krgikiimdl vvnhtsdehp wfiearksee
      121 nkyrdyyiwr dapadgglpn dlksifggpa wqwdetagqy ylhlfskkqp dlnwenealr
      181 qavyemmnfw idkgiggfrm dvidligkqp degitgngpk lhdylkemhq atfggknllt
      241 vgetwgatpe iakqysnpan kelsmvfqfe higldeaegq tkwdliplei pklkevfskw
      301 qtelgdegwn slfwnnhdlp rivsrwgndk eyrvesakml aillhmmkgt pyiyqgeeig
      361 mtnnpvtdie qiddiesrnm yferleegys keailhsina kgrdnartpm qwsnaktagf
      421 stghpwlain pnyekinvda aledensify tyqklialrk enpiivwgef ellkdtaeev
      481 fayirsykge nwlivanfsa nenqfsssye vkeevihnys eviddvkeiv lkpyeafvak
      541 lk
//
LOCUS       WP_285005245             302 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Lactococcus garvieae].
ACCESSION   WP_285005245
VERSION     WP_285005245.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..302
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33536
     Region          1..302
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mkevkvfyne ksgkndenev lntikkffgk eenkashvey inpdspedav rlakkasqen
       61 tdlvvalggd gtinkvcggv feggsksilg ivpngtvnnl skplhipqdi eaalqnlneg
      121 klqkfdiakv nddymisslt lgiladiaqn vsssekkkfg pfaylkdayk virhnksyri
      181 elkyngktka lktklllitm tdtiggrqal sldakvddgl irvyslkein llkilfhlnk
      241 lrkgqledfm eityfdtdhl eisaqsnkkq dipysridgd kssplpldit vyrkglttvv
      301 pk
//
LOCUS       WP_285005234             563 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Lactococcus garvieae].
ACCESSION   WP_285005234
VERSION     WP_285005234.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 563)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 563)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..563
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64779
     Region          <112..367
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 miyiflsylr krksiffewl tlpkekktel hicleaeqye dvnrkkrikk vvkagplgae
       61 viiddiirql ltvtylkplr dantelsagn ksrisqvvqg lkeftgdins dkqeivdkfq
      121 lafedlgkqf eipvvkkier atkeffdsks ektarignkh msfseilkkl nltfdeigtg
      181 lgssnllfma lelilfeqee iglnlalvee ieahihpqaq lrvikffeqe srkeykdvqy
      241 iftthspila aslplesiim lhedvaysig rgktkleadd ydflerflda tksnlffakg
      301 vimvegdaen iflptfaevi glplykygis ivnvgslafk ryssiflrtd eqpmnfpvsi
      361 lsdldfkeyv lkdgdvltkf deylenksdk pflnfldeqs vvelkearld eagpefielf
      421 nrkklqelnk rlmnkktnlf dnnektsvyi sepwtfehtl lnsclrdeme ysiltanykq
      481 ssnienkkee wekivgdver ataayqfmld knvsksivaq nlakyvidnq kalkseilad
      541 pqlkylvemi nhvsqlggks dei
//
LOCUS       WP_285005262             694 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Lactococcus garvieae].
ACCESSION   WP_285005262
VERSION     WP_285005262.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..694
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79229
     Region          458..687
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 matkwknkfa vsiglalllf gvnslvftal naeqyifndy fqskyfkqei atleealint
       61 qvnpnlpiqv ttedieeyrm tqpdkysqvs aikedpvfle rlndakaagd ktaikkledq
      121 qnkklnevek lftddkyvte kvkeqkkeli aqqktdwmpq ykelssdihy qvteinsgky
      181 ldnlsdnktf ataktlfkgn vsqinvdehn qfegqiiilk nsnfnqrasv ksftemknlt
      241 igllctsils faaflfywkk kekgedille kvkscdkial dgqiflalil sllylaltre
      301 asvtwsflpf lqkfcwaflv lylfalvigg iyykvqehen wqqtylarsi rllkdaadnf
      361 srgskawfif wsmgaaafgf llammwggqg ivlylfvlvi ylllisiyll rrlamfnqtv
      421 kiieeiaqgk kaevlnvkpk gktvfrsvse nlktineevk tsksqqvkse rlktelitnv
      481 shdlrtplts iitsvdllrn adlsqdekek yvavidqksk rlkvliddlf evskmasgnm
      541 dlkksridlv qlldqslael sekiedsslk fvtqtdkell alvdgdkmwr vfenlihnil
      601 kysmentrvy isghksekgt ielvfknisr eelgensqel sqrfkrgdls rnttgsglgl
      661 aiaqsiveah eghflletdg dlfkitlsfp slev
//
LOCUS       WP_285005611              71 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Lactobacillus
            gasseri].
ACCESSION   WP_285005611
VERSION     WP_285005611.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus gasseri
  ORGANISM  Lactobacillus gasseri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 71)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 71)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 71)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Lactobacillus gasseri"
                     /db_xref="taxon:1596"
     Protein         1..>71
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          9..66
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(13,17,42)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(16,41)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(23..24,35,38,42..43)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mgmersnegl kikafreeag ltqseladyi gvaqvtvsaw ergvaspdaf sqrlvdqvlr
       61 yppsefkkpt e
//
LOCUS       WP_285005706             644 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Lactococcus formosensis].
ACCESSION   WP_285005706
VERSION     WP_285005706.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..644
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=74042
     Region          10..589
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mlvtqreqqi iqeflvketl tiadmmeatg asrrtiyrdl dkfqltlpnm giylrtsteg
       61 yylegdlarl eqlqelkefs pqerqkaeiv llvtkhhslk elaerfavsl ptvisdlkhl
      121 dkiceenelf lhqddeiwit gkeekirsvl vsilndsmsi sealngdfae gkiasfletq
      181 fletakaife knveikavdk skvlmqfflg itllrinqgk tissglwrkp skeaiafvre
      241 iiqelggtsf slaeivylas iydvlyfgfg revlfmekfd sqfsykvrql isevsqkmdi
      301 afikddklyg llyahlkete ilpdlsseke nkfikkiead nkkvfkvvqd vlpkvfsrkf
      361 sstdiafvtl hfvatlersd lvlpltaaiv tsrgriscef lishlkknfp flkridiiql
      421 seipdlehyd vvfttekeln yiyvsrildq kntddirhql rviqqearka nkedeprhtv
      481 dlsrlfsisn tlleqfslet lenpphlqav ielivqrlgf sekeglarll lerfeathla
      541 ipdtniallh glhgtvpypl fkiydleeri eviamnqeki svnrvlllla ppevdhyaty
      601 llgrisssii enklytkiyd sgnqevveel lktimtesiq kyge
//
LOCUS       WP_285005794             302 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Lactococcus
            formosensis].
ACCESSION   WP_285005794
VERSION     WP_285005794.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..302
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33512
     Region          1..302
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mkevkvfyne ksgkndenev lntiknflgk eenkashvey inpdspedav rlakkasqen
       61 tdlvvalggd gtinkvcggv feggsksilg ivpngtvnnl skslhipqdi eaalqnlneg
      121 klqkfdiakv nddymisslt lgiladiaqn vsssekkkfg pfaylkdayk virhnksyri
      181 elkydgktka lktklllitm tdtiggrqal sldakvddgl irvyslkein lfkilfhlnk
      241 lrkgqledfm eityfdtnhl eisaqsnkkq dipysridgd kssplpldit vyrkglttvv
      301 pk
//
LOCUS       WP_285005831             163 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Lactococcus formosensis].
ACCESSION   WP_285005831
VERSION     WP_285005831.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 163)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..163
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18169
     Region          <4..156
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mavhfgedfd kedaaklqke ffiykkssrf pieemlfpdv kvvlqrlset klkiglatss
       61 sheeiaevld thnlrkyfev issgedfpes kphpgvylsa mkqlnarasd vlviedspng
      121 iaagkaagat vwairdqrfd sdqsqadrrv ehltevlell gfs
//
LOCUS       WP_285005851             276 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Lactococcus
            formosensis].
ACCESSION   WP_285005851
VERSION     WP_285005851.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..276
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31196
     Region          16..276
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mwqftirghd lsditsvkel aqaaekvgih hlqlamgmsf pdlvdkptkl npglgrfvkd
       61 elgtydvdia vlscyinmih pdaeererll gkfesfvkna kafgaamvas etgcvlpqiq
      121 yteknfteea fedmlqviqr lvkkgeehgv migiepglnh plhslekiqr lidyvnsdyl
      181 giildptnli tsenyleqve mvkkafqmfg dkicafhlkd fiikdkkvlp vnvfegqmnv
      241 kavlkivady kpycyvvlee tkdlgikrai dqlvky
//
LOCUS       WP_285006093             327 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Lactococcus
            formosensis].
ACCESSION   WP_285006093
VERSION     WP_285006093.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..327
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36730
     Region          7..305
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mgilpmlsek asnifkmlea avvredtpgf aafymenqds qtiyggtidd veevtsssly
       61 dlasltkvvg tttrilqlid reeislsdsi ghffpvltel kitiedlllh ragfpadftd
      121 ktdfsqdffw nflkkidlpl pnerhmiysd igylllgeii ekidgcrlee sfythifepl
      181 gmvsttyfpd esfavpteit lsrgkikgiv hdgkaylwek eaghaglfst igdletfvra
      241 vfsgdilsde mlttlqtfev sgrtlgwlsr gagqlyhtgf tggvicldll qmralvvlsn
      301 rtypnrenks yicvrqdiie kffesei
//
LOCUS       WP_285006108             124 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lactococcus
            formosensis].
ACCESSION   WP_285006108
VERSION     WP_285006108.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..124
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14737
     Region          7..60
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(11,15,39)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(14,38)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(21..22,32,35,39..40)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 miykkygevf kklriqhkls lrdferigls kstissfeng ktlisfdkld lalqkmhttf
       61 rsymlmlnnd eedywlnqfk kieyayfnkn lyllehiyve nnaydleenk vialsakacy
      121 stfc
//
LOCUS       WP_285006161             182 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Lactococcus formosensis].
ACCESSION   WP_285006161
VERSION     WP_285006161.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..182
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20862
     Region          44..>180
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkipasllsl aknillvdvr gsykrrqhqk ilnqlktnny rshkisillp iyntehglek
       61 cldsilqqty sdfeiicvnd tsidntkqii gsysqkdtri sivdksqnqg fsfahrdala
      121 qakgsyvlci dsddwieptm ledlylfaqq sssydmvycd yyknnlvtyv ptileknfll
      181 se
//
LOCUS       WP_285006178             399 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lactococcus formosensis].
ACCESSION   WP_285006178
VERSION     WP_285006178.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..399
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46239
     Region          81..393
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mkvedikvgs lwsesrknkf lwrmryfniv tksedkvsvt ltsnsnqakt karkilltka
       61 krkieqseln ilnsslnins ltfssvanlw lndcskrlkp stlnnrrkqi krfadefgdq
      121 emsqfttfqi qvffnslnlk sgtvkgyflt cksifdfakr meiiskdptl nvklslskkt
      181 ledikkqnrk lftvedlakv lnrmrssenp rtyfialtie flfltglryc elaalkeeny
      241 drtrriikve tnldytkgvt khthtttktl ssyrevdlnd raieiieeyl kanhdntyvg
      301 yknhgyifct rsgqphnigh lnrsfkyygk atgldkqfsc hcmrhshisl laemginqkv
      361 vmqrvghats titnniythv tpnmskelnq kmnrinkis
//
LOCUS       WP_285006305             965 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Lactococcus garvieae].
ACCESSION   WP_285006305
VERSION     WP_285006305.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..965
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..965
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=100489
     Region          <42..877
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mskyykkrse kdkngksral hhyfklvlya fsffilspls pvfngipsfg tlsaeasitq
       61 qtdgsgitwn litagndint lattalpgat lyikaandlt lgvtavlpln ltlvfdmdgh
      121 alyntgaavi tpsvgntitf qnerivstgt tnsttvpspl gigtvtgvyn yyyglfsatn
      181 isgvsitykn viqdlgtitt wgaggqpfyn igssvnfsgt nyfnynsgqe fmegtginvl
      241 dgtttikhss ggnaplwaqs aasinvaaga tldftgsstg rgfiyldntp tftinnngtl
      301 klnmsgansn nfysntgmss itmnyganss ttiiapgffd ynatggafkt tigqgasfdy
      361 stgntsnafl gtlattdsft lnsakhvrln tnktsgssil gtdasampfv lnasspsaya
      421 ingynsagvs sllasptsga fgvtgtfhsn ladlskltgq kiptaseitt yqnsaqlefn
      481 lvspaqanfs yawaadvpgq nggagtllgq lparvseqgt vggaltaptl saapkgyyis
      541 gykapngtiy ttlaaalatv nnvfgttsnt tspdiympst ndfqvilsaq eqtfyinygy
      601 aftnfgnvpp fpanaytqkg ltgapltisg lgvaptgyhy savlnntasa widqsnpetg
      661 gantptpyya sislaltaai tqqnggmyfg tsslstppti nnqgafdnnv mvmltanaei
      721 anytygwani tpgyngnagq iygnlpsqat skggfgdtia rdtsginspg ntyqtfvapp
      781 tdnalsgysv avrapngity tsdpnavass tvvktttplt tatqantfke gaaatnfvit
      841 yaplanklsw hytydssisn ppsapadivq tgvltgaplt dpkatapngy fiegyqypgd
      901 tkiyrtiael qtahfsgtgd itinillakn fvlpytggsg qfgiilasat laflalafyi
      961 fkkkd
//
LOCUS       WP_285006471             483 aa            linear   BCT 25-DEC-2024
DEFINITION  FGGY-family carbohydrate kinase [Lactobacillus crispatus].
ACCESSION   WP_285006471
VERSION     WP_285006471.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..483
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=53806
     Region          5..476
                     /region_name="ASKHA_NBD_FGGY_GK"
                     /note="nucleotide-binding domain (NBD) of glycerol kinase
                     (GK) and similar proteins; cd07769"
                     /db_xref="CDD:466789"
ORIGIN      
        1 mpekyllaid qstqgtkail fdhqkqifwk talshkqlvn nqgwvshdld eiknnlkklf
       61 ksaleqvsad qieglaitnq resaaawskr tgeplcntiv wqdnrvqkli trisykelqe
      121 evknltglal spyftgakwg wmllneprvi qanqnndlcl gtmdswliyq ltngksfkte
      181 psnacrtqlm nihtgqwdek lseifgvdln slpqivdsna hfgdtdlfgl lphpipilsv
      241 lgdsqaalya hgcfntgdfk vtfgtgssvm lnignklpkd innklntsia wslngktsyv
      301 iegninyaga citwlkdnik liktpeetgd laltanpedh tilipafagl gapywkpdmk
      361 aafvgmtatt skkelvratl nslvyqiadi laefqklspq lnneihtdgg miynqylmqy
      421 lsnitqrtvk isniselsal gsamnafqdm sgskssasys prmkkdvaln yldewhnwie
      481 kms
//
LOCUS       WP_285006892             335 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Lactobacillus crispatus].
ACCESSION   WP_285006892
VERSION     WP_285006892.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..335
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=38643
     Region          1..271
                     /region_name="WecH"
                     /note="Surface polysaccharide O-acyltransferase WecH [Cell
                     wall/membrane/envelope biogenesis]; COG3274"
                     /db_xref="CDD:442505"
ORIGIN      
        1 mkkvrdskfe ilriismifi vishyslwgk wndankfkyl vyqplgqigv cvfvlisgyf
       61 lssrvlsakd gwrranklwl ktlvyswiif iavistmefk nisittilta ifpvvfgeyw
      121 fitefiilml fvpilnqmlv slnkkelkyy igiivfgsti lplfiknlrp fgdmnsaiai
      181 iavyliagyi kkyniklskl iswsmflggi viellsifil knydakmihf tygfiplisa
      241 iglfnvgism ksfhnkfiny iassvlaayl itenpllrmw lwnkflhisk lqnynyllfl
      301 lygmvisill vllcclidki yekieaivva kklgk
//
LOCUS       WP_285006944              73 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lactobacillus
            crispatus].
ACCESSION   WP_285006944
VERSION     WP_285006944.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 73)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 73)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 73)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..73
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8120
     Region          11..>55
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 meitnqqlet lrvergrknl tisslaqqlg msrytmgnii ngktnglrte tvhkinswlt
       61 anvhptkeva nne
//
LOCUS       WP_285007014             253 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Lactobacillus
            crispatus].
ACCESSION   WP_285007014
VERSION     WP_285007014.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..253
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29413
     Region          39..231
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mkriyyyqkt tddvvdshdq nfslpdnyvi lpnslgariw sttarhlaca fgwvvfrffd
       61 hvkvvgqekl kqvnggyfiy gnhtrpmgdv ftsltifpik nfyaianqan wgipfigkyl
      121 vrygglpvgk nmkqslklik aiqtvikdkk geiliypeah vwpyytkirp fdatsmhfpv
      181 klnapsfvmt ktyhkkwlsk rpsaviyidg pfysdtnlsr keaqnklhde iwqvmkqrak
      241 nsdyeycqyi qkk
//
LOCUS       WP_285007017             217 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Lactobacillus crispatus].
ACCESSION   WP_285007017
VERSION     WP_285007017.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..217
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24467
     Region          1..215
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(10..11,13..14,17..18,55,59..60,63..64,80,84,91,
                     94..95,100,116,120..121,123..125,127..128,131..132,
                     135..136,158..159,161..163,164..165,167..168,172,175..176,
                     182,184)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(119,123,126..127,129..130,167,170..171,173..178,
                     181..183,187,189)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(140..147,160,163)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mnpslkfila fiisleislk aslvtnllvi tfalvyliit rikikelill iilpfiaaft
       61 ifatlfwfsp tpnayyawnl strvyvytlt iacvtrnnta tdfarsleqn lhlpskfayg
      121 vlaainiipq mkmavkqirt sammrgiyls fwspvlyfka ilvalnsadn laqgmeshgy
      181 vegqrrstii aipltardwv ifftllilvn islflfk
//
LOCUS       WP_285007108             219 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Lactococcus garvieae].
ACCESSION   WP_285007108
VERSION     WP_285007108.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..219
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24574
     Region          3..209
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mnkfkavifd mdgvlvdteq fyaqrreeff snhnisiqhm kysdfiggnm reiwpqilgv
       61 dfdqdeaakl haaylklkdn nplpykdllf pdvktvleal endnfkigla sssamqdide
      121 mlnihglrpy fksilsgndl katkphpeiy qlsmkalnvk peetliieds ekgiaagkad
      181 gatvwaiedt rfgmnqsaad awfpnltavk ekleslsan
//
LOCUS       WP_285007158             302 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lactococcus garvieae].
ACCESSION   WP_285007158
VERSION     WP_285007158.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..302
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32563
     Region          3..72
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
ORIGIN      
        1 mvaiktigev lkdkrtelgl glseaekltn ipklyiiale tgdykalpgd fyikaylkqy
       61 aekldldadq imlayekdgs msveehediq eiyrfvkpse rveedeeeee snkpawrhyv
      121 piillsaval aivgsvtavv lltrppkpdl sdtsytykts etkktteepk kttessekpv
      181 eskpepqnqi tvtgsgaqln vkvenatspt qivfttaaga vttvsltnad watvrtlsda
      241 entatatlga gltnsvinls ntqgltmtin gstvdlsalt vgtpvqvqlt vtyasttapv
      301 tq
//
LOCUS       WP_285007203             396 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lactococcus garvieae].
ACCESSION   WP_285007203
VERSION     WP_285007203.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..396
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44673
     Region          69..389
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mkineitkkd gtvvyrtavy lgvdsltgkk vktyvtaktk kalkslsdlk iaefekngkt
       61 mlrkkvefen fealamawld dylltvkfns qtmmkshfkl yiipalgdyk vekitapllq
      121 sivngwakka ntapirkgkr pvgsnrgykl llntvkrild yafqlgiitn nparmvvapr
      181 lkvrgkpkik yldnaqlkkf ldyingleqt dqntfsvtly kllldtglri gealalnwsd
      241 idydsniihv nktvdragkv qdspksesgi rdisvsnrtm lmlkqwqnrq rvlyrknkip
      301 trivfasaig dylsrghiik sldtcyknag inltgfhafr hthaslllna gadykeiqhr
      361 lghakigmti dtyshlapdk aketasiyen alekls
//
LOCUS       WP_285007355             262 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family transcriptional regulator [Lactococcus garvieae].
ACCESSION   WP_285007355
VERSION     WP_285007355.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Nazaret,F., Alloing,G., Mandon,K. and Frendo,P.
  TITLE     MarR Family Transcriptional Regulators and Their Roles in
            Plant-Interacting Bacteria
  JOURNAL   Microorganisms 11 (8), 1936 (2023)
   PUBMED   37630496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Will,W.R. and Fang,F.C.
  TITLE     The evolution of MarR family transcription factors as
            counter-silencers in regulatory networks
  JOURNAL   Curr Opin Microbiol 55, 1-8 (2020)
   PUBMED   32044654
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Grove,A.
  TITLE     Regulation of Metabolic Pathways by MarR Family Transcription
            Factors
  JOURNAL   Comput Struct Biotechnol J 15, 366-371 (2017)
   PUBMED   28694934
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   7  (residues 1 to 262)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   8  (residues 1 to 262)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10581578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..262
                     /product="MarR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29281
     Region          <7..>29
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          <55..130
                     /region_name="COG4253"
                     /note="Uncharacterized conserved protein, DUF2345 family
                     [Function unknown]"
                     /db_xref="CDD:443395"
     Region          <111..256
                     /region_name="PRK12904"
                     /note="preprotein translocase subunit SecA; Reviewed;
                     cl46899"
                     /db_xref="CDD:481239"
ORIGIN      
        1 msenyktike ladelgvskq avqrrinnlp khlkpkking kfvltndlan eirkiyslkn
       61 ttanagdntt anagdnmtan agdnmtanag dnmtanagdn mtanagdntt anagdnmtan
      121 agdnmtanag dnmtanaeiy kkiisdlked kkksyeiife kdnqiknlie aqkqtqnlld
      181 qqqrlalqdk klleeyksei nelkalkmpk edmkedssir geaqeeierl kaqlklseee
      241 rnkakekepv kteskkwwql wk
//
LOCUS       WP_285007570             361 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Lactococcus formosensis].
ACCESSION   WP_285007570
VERSION     WP_285007570.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..361
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39976
     Region          5..360
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 msklerisnf lnenevdmtf itnpttlnyl tglaidpher iaglmvfpdk apslftpale
       61 vekakenttg fdifgyedsq npwavvkehl gskniqkiav efsdiplskt eglksqfsgv
      121 efvnltplve rmrliksade iekmkisgdy adkcfeigfe yansdrtetd vvakieyemk
      181 rmgvpqmsfe tivlsgaraa nphgmpedvk iqdnklllfd lgvmkngyas datrtisigk
      241 psdfdadihk ivleaqmaam dfvkpgvsal eidkvardvi tkagygeyfv hrlghgigmd
      301 vhefpsiggs ediiieegmc fsdepgiyip gkvgvriedc lyitetgcep ltktnkelmi
      361 f
//
LOCUS       WP_285007657             407 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Lactobacillus iners].
ACCESSION   WP_285007657
VERSION     WP_285007657.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..407
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46139
     Region          2..394
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mmeenliskt ydsgfvanii lkpgfaskfm givvdfggsd pqeisggahf lehklfakky
       61 gdialkferl gadsnaytgf netmyyaefa nhwpqilpll felvgepyft vdnidqerki
      121 icqelatakd dpewylihnl msnmfpqtmf thdivgseed lakidisfln kiykkyycsn
      181 nmrfiacgdf spsqvqkift lvnkmqkkyi ncapkpkiav qtidstatde qitnnnskni
      241 hvgvaiklpd lnkftsnall atdvlemlid ahfnsnniwl snmqlqniin dqpdvdiynt
      301 regsfviita isrypqklvs aikhelfrgh msaelielnk keflanylrl tddlnsyaqq
      361 magtllhgrs laqiieevvq mnnsdmvsly qdilakssiy scimsnr
//
LOCUS       WP_285007897             420 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Lactobacillus iners].
ACCESSION   WP_285007897
VERSION     WP_285007897.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..420
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47094
     Region          26..413
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mlsyeeiisg fsqkmlagdh nhvvflrnik krlgspeqaf ktihiagtng kgstgmmikg
       61 vlehagykvg yfnspalidd reqisinnil isrndfvaty yeilnklssd estkisvfew
      121 wtlimlvyfa nkkvdwavie cglggtddat niinapeyai fthialdhih ilgdtvekia
      181 kaksgiikyg tkatimaplq qkaavniike kcsqvqvpli lsddiakikv hnrkiniist
      241 dftlessfsl lgeyqrenlk tvialvkqlm rekvlislmp lkqmletiki parcekiasl
      301 pdvlidgahn pdaaynlaqt iislrhgrrv imilgflkdk nyqkmiqiyq eishdfilte
      361 pdhlqrklpv ailaqkfnnh vmqavnvrsa lkiarqnakp ddlivvtgsf ylvkdlindd
//
LOCUS       WP_285007864             797 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Lactobacillus iners].
ACCESSION   WP_285007864
VERSION     WP_285007864.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 797)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 797)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 797)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 797)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 797)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18767243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..797
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=91705
     Region          1..789
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          1..208
                     /region_name="AAA_27"
                     /note="AAA domain; pfam13514"
                     /db_xref="CDD:433272"
ORIGIN      
        1 mklikidvkn fgglsdsewk issqlhvfyg pneagkstia afikqimfgf hlksqkstff
       61 enymplkkvn qvggsltfkn ennqiitler tyttsdskkg nlavsldnek ipenifwnni
      121 knidgdfytd sfifnqdlla nvislnqgdl lehiyylgaa qsskllllrd kfvqsseklf
      181 ktngrkpein qilaqikeka etlskqqvef dqysslekqk ndvqneiell nsqvkklqqn
      241 qqnlaitkqe lnnyaqyqql keqyqlidfn qedytqaqal eltieqlttd iknyeseiia
      301 vsadnldeqa kilakkveiy qivneadrlq neikqlcqel eqiqtyqply fkleslsped
      361 klvmrskyeq clntqapksi iknisfglii fglvgvflkp lfyllilsgl iiyyldkikt
      421 dhirtnqiks fekeygfdpq kfdlelvmsq imqienkrni laekrknqak ileqvadfkq
      481 kisqfvsptn nltsdlekld ehyqqvqqkv ttqkllneki saikakladv kltlqkklsq
      541 nkvkdieefk akgnlyhqnq qiksqmmals anlkdrveil skldinslht teqslvsele
      601 qiqaklriky dalaqlklkl keltnsdslk rtqqelatan anlldytkey ladllvadwi
      661 qrgldlasnd rfpkmlastn qyfalltngr yikvaindql qvvkadgtrv aveylsrgta
      721 eqlyfalkla fveqiadeie lpiliddafv nfdlqridni vklvqnlsak tqvivftqnl
      781 qlakmltdni tkleirn
//
LOCUS       WP_285007901             539 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Lactobacillus iners].
ACCESSION   WP_285007901
VERSION     WP_285007901.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 539)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..539
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=62820
     Region          6..459
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(20,22,24,28)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(59,62,99,102,143,162,166,198,240,401)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(198,240,316)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          466..535
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; pfam16657"
                     /db_xref="CDD:435493"
ORIGIN      
        1 mtpwwkkavi yqiypksfqd sngdgigdlp giitrldyla klgidaiwls pvyqspgidn
       61 gydisdyqai dpqygtmddm dnlileakkr hikiimdlvv nhtsdqhawf vearknkenq
      121 yrdyyiwrdp vdghepnelq safsgsawqy dettkqyylh ffakqqpdln wsnsivrdki
      181 yqmmnywidk giggfrmdvi eligkepdkm vrengkmlhp ylqemnqktf gqsdlltvge
      241 twnatpkiae dysdparhel smvfqfenqt ldqkdgcskw dlkpidlvel kkilvkwqte
      301 ldfkhawnsl fwenhdiprv isrwgndqky rvvcakmfai vlhlmhgtpy ifngeeigmt
      361 nspvknidev ediesinmyn erldagydkd ellhainvkg rdnartpmqw sdalnagfts
      421 gkpwlrvnsn ytdinvkqcl adpdsifyty qklielrhhn qivvdgdfql ieetdaqila
      481 yyrilgdqkw lvvanltdke kpfncheqyq kvlvenyttp snlqniilkp yqafvvtia
//
LOCUS       WP_285007908             289 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Lactobacillus iners].
ACCESSION   WP_285007908
VERSION     WP_285007908.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..289
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=33776
     Region          <9..>93
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          9..34
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(10..11,14..15,17,40,43..44,47..48,50..51,74,77..78,
                     80..81,84)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          38..68
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msvsdlkkli elaqkaltig dlerakncyl qylslqhdik cvialgnifl qekrpdeayk
       61 llkdesdlfs ddmlfkfylk vlqerhfyie akqvsyllgk plaieivpiv gfdadkimsd
      121 fhklniitqe dyiklyslde etfiefsksl lldpttdfiv katlcndfik lgvskkinir
      181 ilgqmqsfvp adtsifyqns iyrylilflk hhyennpskl nllvneitif cevifpciel
      241 yiidadkfar cfidyinges dnineytkll ndvyaelyrf nynykiknn
//
LOCUS       WP_285008092             375 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Pedobacter faecalis].
ACCESSION   WP_285008092
VERSION     WP_285008092.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..375
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40701
     Region          6..373
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mtraeqfmqs rleqrtlags lrrleqpgal idfssndylg farsgalrer aegilnslgn
       61 ykhgatgsrl lsgnhaftee teayiaafhg aesglifnsg ydanvgllss lpqrgdtiis
      121 delvhasikd garlshanrf tfkhndvdql esrlrkasgn iyvvvesvys mdgdlapllt
      181 istlceryda alivdeahat glfgdhgrgl vsqlkleskv farimtfgka lgshgaavig
      241 sntlrnylin farsfiytta apvhgiamvs agyhllndtn yteaiantik lytarmqaem
      301 phiittesti qtlicpsnds crnaaaqlqs qgfdvrails ptvpvgyerl riclhlyntd
      361 peisglvnal sklnv
//
LOCUS       WP_285008034             405 aa            linear   BCT 25-DEC-2024
DEFINITION  thioredoxin family protein [Pedobacter faecalis].
ACCESSION   WP_285008034
VERSION     WP_285008034.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 405)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..405
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=45744
     Region          1..143
                     /region_name="SoxW"
                     /note="Thioredoxin-related protein SoxW [Posttranslational
                     modification, protein turnover, chaperones]; COG2143"
                     /db_xref="CDD:441746"
ORIGIN      
        1 mkkifllcil lpiiglaqek gvqfehglsw qqvkdkakke nkylfvdcyt twcapckqma
       61 tevftqekvg dflnknfvnv kiqfdktksd seeikswysd aqaindefki tayptflifs
      121 pegelvhriv gggkaddfia wvkvaldpet qyytllkqng sasgnpqrlk klalaaeiak
      181 deqnairfad dylatqsglf tmdnlefvtr fikntdskgf klvlgnrekv davlgkgkan
      241 eilsgvivre rinpafqnla ididsliavt kakypevdit kpadmirilf fqvnknwdrf
      301 qpalmaymdk ygdelipnal nyfartvfen ckdpdciaaa mawskrsven tqskepayld
      361 tyasllyklg nkqeailmqq ravdlvsgen ktgyqatldr mlkgq
//
LOCUS       WP_285008177             405 aa            linear   BCT 25-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Pedobacter faecalis].
ACCESSION   WP_285008177
VERSION     WP_285008177.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Pereira,J. and Lupas,A.N.
  TITLE     The VCBS superfamily forms a third supercluster of beta-propellers
            that includes tachylectin and integrins
  JOURNAL   Bioinformatics 36 (24), 5618-5622 (2021)
   PUBMED   33416871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..405
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=43619
     Region          56..114
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          106..167
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          156..222
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          211..273
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          262..333
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          322..391
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mkarvlthya afsllstlvy qsanaqttet ryfkdvtata lpadpeahil dvvladvnad
       61 ghldavlale gqpnrlyind gkgvfswkkg vfadknhdte hvrlgdfngd ghldgifvae
      121 ddhnheyylg nsdgtftdvs drlparsegn gldigdvngd glpdivvgnt gadaknflwl
      181 ndparpgyfk vhaggvlsel paqtqsvkla dldgngaldv vfgnevppnr lmfnngkgnf
      241 seregaldlp vplhtreviv fdangdkhpd ilfanltsna gkyekdpnar llindgkgrf
      301 kdetalrlpk qeystyagav vdfnrdghpd iifsavrips fapmqvqalq ndgkgkfnla
      361 taevipgsti grswgiavgd vngdgiadlf igqwgtqarl llgkr
//
LOCUS       WP_285008178             441 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Pedobacter faecalis].
ACCESSION   WP_285008178
VERSION     WP_285008178.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..441
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48128
     Region          15..346
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkkiiailll gvlfatqsha qtvntaklds ffnalaandk tmgsfavakd gkvvyqrsvg
       61 yqslgpdsvl asantqyrig sitkvftavm ifqlidegkl sldtklskfy palpnsdkit
      121 idhllshtsg lidyvsevsn rawitqahpk nelldtiakr kvnfepgskq qysnsgylll
      181 syileditgk sfnklletri vkklglkstv agvpnnskne ampyarissw tdikdiyfpn
      241 vigvgdilst psdllvfmna lasgkllsae ryadmrtftg qsrlarglmk vpfyeywglg
      301 hggdtygths ilyhfkeggi siafcvngln ypindisial lsaaynkplq ipsfksldlt
      361 paeldpltgt ygsaglpfti tvtrngnsii aqasgqsalp meavtksrfk fdgagivlef
      421 dtqkkemllk qhghsfvfsk q
//
LOCUS       WP_285008197             505 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Pedobacter faecalis].
ACCESSION   WP_285008197
VERSION     WP_285008197.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..505
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57489
     Region          388..505
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mkfikfdvlc litflflfsc rqaeatvidt paivsgtakl sgriitpega ikdgtkvkit
       61 vphqvsgefv kyeaavdrsg nfsidaevet svsyihfsts ldpsaplllk lrsdtlthle
      121 itytenldvl svgvspemnl qdvkrgfevi rdmieypprg ipeplydksi dyflttskse
      181 lsersevvkn dkliskelkq vlyddlrllf yrgavfnyga amkanyrrsg gdtskavviq
      241 kidrsyyrfl kdlelnspgy lyafsfwefq relleneily ippigdsdve swlstvkgvl
      301 sdlvgfeggl yydllaanay gkqlteglkp fnkkqeknir nywgdgeiak ilfrknqkvv
      361 qlakfkspvv vndvskmtpe evinnivaqh adkvilidlw atwcgpclea mqrfrptkae
      421 fydkdvvfvy ltnpsspvkl wkekiagigs ehyylsnaqw qyimnrykfd aipsyllfnr
      481 egklvrkfta fpenevvkdm lisll
//
LOCUS       WP_285008198             304 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pedobacter faecalis].
ACCESSION   WP_285008198
VERSION     WP_285008198.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..304
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34847
     Region          68..303
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkdemsnhrf nslsrlhkal dmpapmhplv tlinnadgti plknlptphi lsfykisykm
       61 nfqgkfkygq hyydfeeggm ffvspnqitg gheplsdqsg ytllfhpdfl lgyelakkik
      121 tygffsysin ealhlsekek ttiitvfesi eeelegridn fsqdvvisqi elllnyanrf
      181 ysrqfitrkt vssdllqkve dnlrgyfqsp qtqtqglptv qylsaqlnvs asylsdmlrs
      241 ltgqnaqqhi hnhliekake qlstteasis eiayelgfeh ppsfsklfkl ktnmspldfr
      301 rsfn
//
LOCUS       WP_285008206             251 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Pedobacter faecalis].
ACCESSION   WP_285008206
VERSION     WP_285008206.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 251)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..251
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=29597
     Region          1..245
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mkyliveder fayeelkrmm mklrpdylle mqtktvidti gflkesvvdl ilmdirladg
       61 ncfeifshvd vttpviftta ydehaiaafk lnsidyllkp fdeseletal nkfehifysr
      121 syksdpknfe qllslktknr fliskgenyh yietkdiahf ysedgviflh tfndrryiin
      181 ytldqldqql dgrlffrvsr ncignvkaie nvakyfnsrl klsfspecph evlvsrmrvp
      241 dflkwmdgil q
//
LOCUS       WP_285008275             197 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Pedobacter faecalis].
ACCESSION   WP_285008275
VERSION     WP_285008275.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..197
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21749
     Region          46..196
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mkaikilgca llvsfcinvn aqeqkvtspa nmdqmlaslv selqnklvgk kapnfitkdv
       61 ngrklslesf kgkyvildfw atwckpcrqs hphlislykk yhdkgleiig iadddprpea
      121 wreaiaadni tmfhhalags dpkkrmkgee npadimamys vpalptkfvi dkagkvvaay
      181 vgdsdkidgk lkelfgf
//
LOCUS       WP_285008302             175 aa            linear   BCT 25-DEC-2024
DEFINITION  D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase
            [Pedobacter faecalis].
ACCESSION   WP_285008302
VERSION     WP_285008302.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..175
                     /product="D-glycero-alpha-D-manno-heptose-1,7-bisphosphate
                     7-phosphatase"
                     /EC_number="3.1.3.83"
                     /GO_function="GO:0034200 - D-glycero-beta-D-manno-heptose
                     1,7-bisphosphate 7-phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19770
     Region          1..147
                     /region_name="HisB1/GmhB"
                     /note="Histidinol phosphatase/D-glycero-mannoheptose
                     bisphosphatephosphatase, HAD superfamily [Amino acid
                     transport and metabolism]; COG0241"
                     /db_xref="CDD:440011"
ORIGIN      
        1 mnkavfldrd gvlnrelydy icrpedfhvl eyqipplkkl ydegymliii tnqggiaqqr
       61 yseetlaemh qtlfgrfaqq gatithayyc phhptvsgec dcrkpkpgml keaiarynid
      121 pelsvmigdk prdveaanaa gvrgiliepd eqidyeivke vlagsefant skdfr
//
LOCUS       WP_285008306             264 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Pedobacter faecalis].
ACCESSION   WP_285008306
VERSION     WP_285008306.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..264
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29531
     Region          52..264
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mrlsfflflc lvlagcnhfe fspnqafdrn sfrdinnrnl kklgsgatdd tvrfvltgds
       61 qksrdetvaf ckavnalpgi dfvvlagdis efgvlkemew israledlnp pyvavvgnhd
      121 lvargkdvfl nmfgelnysf tyggikfvch dtngreyqfn gqtpdmqwlq hqlkpengvt
      181 gyiaishvpp nnpdfdpglv kpytdtmvqt pgllaslhgh thqfeeyfag drkvpfiits
      241 amadseflvi evvnnnltyk rvsf
//
LOCUS       WP_285008319             718 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Pedobacter faecalis].
ACCESSION   WP_285008319
VERSION     WP_285008319.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20140996
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..718
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81766
     Region          18..668
                     /region_name="YCCS_YHJK"
                     /note="integral membrane protein, YccS/YhfK family;
                     TIGR01667"
                     /db_xref="CDD:130728"
     Region          366..632
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mlnrpirsih dfllstyfad glrisfgvlc pplilaqfgm lqygitlslg alcvsitdsp
       61 gpivhrrnam lvttglitii svivgltnkn dyfigavltl csfvfsmffl yglraasvgt
      121 aalivmvlsi ddvrpwqdvl fyallvflgs iwytmlsylf yklrpyrlvq qslsecihei
      181 sdflrakakf yrentdydqa yaellklqvq vhekqdavre vlfktreivr estpegrfll
      241 lvfvdivdlf eqimstyyny krlheqfdps gilshyekvi ikiadelddi gfalvagntp
      301 hlpsdldkdv emlkaeivkl etdksganyt tlgiialkni evnienilsr lktingyfnk
      361 akkkslttrn invdkfvtrq sfdtdllwen ltfrsstfrh slrvaivmli gfvvakslnf
      421 shsywillti lviskpgfsl tkqrnyerlv gtiagsfagm giliyiqdkn alfaillicm
      481 igsysfqrkn yvvsvlfmtp yilvlfdflg igglsaarer iydtligsgi aliasyslfp
      541 nweheklkea lqetlqanmk yfeevvllys gplgdltnyk varkqvyvtt anlaslfqrm
      601 fsepkskqvi mkelhqftal nhqlssyiat lslyvkehnf tgidleelkp viqntqylfk
      661 qtieilqhnt gqvnnvplir rsskdgeiqt aqmviseqfd ltqkvaydiy klcerikl
//
LOCUS       WP_285008347             329 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Pedobacter
            faecalis].
ACCESSION   WP_285008347
VERSION     WP_285008347.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..329
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=37043
     Region          4..325
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mskkvlitga tgfvgyhlia qalqaglevv aavrpgtsra hlkafdisyv elnyasvadl
       61 rdtlekyqfh yiihaagitk aktreqyerv naeftrnlat aateakiple kfvfvsslaa
      121 lgpladlsac isdemtgqpv tqygasklka eqylselpel plivirptav ygprekdifi
      181 lfksikqgie pyigsfqqql sfiyvtdlae iiikslfaev rgrtynisdg qfydrytlgr
      241 lirkslgkrt lrfhlpvsiv galarimdfl yrnrkdtpal nkekmaelta vnwycdisra
      301 kadlnfqpry nlekgiaetv awyrenhwl
//
LOCUS       WP_285008476             242 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Pedobacter
            faecalis].
ACCESSION   WP_285008476
VERSION     WP_285008476.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..242
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28156
     Region          44..242
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mnkilrhthr yytlfvival slsfypfyya fsrnergygv lnrlrkinsm misvftgiff
       61 sfeyeepfnh rqtyiycanh tsnldimimc ilargrfhfm gkqellnnpv lriffetidv
      121 pvdrdskmss frafkrvgdn ldkgmsliif pegkiddhyp pvllpfkngp frlaieknva
      181 ivpvsligvw qkmwddgsrf gskpglcriy vhkpvatkdl niddsdtlkd rifetinskl
      241 lq
//
LOCUS       WP_285008462             251 aa            linear   BCT 25-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Pedobacter faecalis].
ACCESSION   WP_285008462
VERSION     WP_285008462.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..251
                     /product="MlaE family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26932
     Region          3..246
                     /region_name="MlaE"
                     /note="Permease subunit MlaE of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG0767"
                     /db_xref="CDD:440530"
ORIGIN      
        1 mnfrnifitl ydvfqfigrf fkeaflppye gkellkqcyd igykslalis ltgfitgivf
       61 tkqsrpslae fgatswlpsl vgiallrtla plltsliaag kvgssigael gsmrvteqid
      121 amevsatnpf kflvstrvla atitipiltf ytalvgmlga llnvslsegt saklffqasl
      181 esitfldita stikavifgf tigivgcyqg ynsakgtegv graanasvvi gmflifieev
      241 vsvqffglfr s
//
LOCUS       WP_285008509            1018 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            faecalis].
ACCESSION   WP_285008509
VERSION     WP_285008509.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1018)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1018)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1018)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1018)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1018
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..1018
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=112330
     Region          50..1017
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkeklpswre hhsrqtflll rnfvnyprqa mlllllilgs yanasaqnsi sgkvthngap
       61 lpgvgillkg talsavtnpe grftitvpdg stavliftyv gfaqqeipvn srtvvdvalv
      121 esdsnlsevv vvgygtqrkq dltgaisvvk aqdvqkrqat tvaeslqgla tgirvrgggq
      181 pgseaqiqir glknlsgtnp lyvvdglvtt anrdfnpadi esvqilkdas aaaiygsraa
      241 ngviiittkk gaegpmridf ngksslqtip rfnlagteef arlnymaydn sgtprqnldm
      301 sintdwqdva frtgnlqdys lsfsgggqgs syyvsggyfk nkgtvistdf drlsfrvntk
      361 gtkgiftvge nlaissanan emsgnpiidv vrllptipvy dpanpggygy gnearartfa
      421 tnpvaiadld drsnanlrir gnvfselqll pqlkyrinlg yetsrdhfqn lrkqgnwtln
      481 qpfdpsiyqe nraqsstglv entltftedl gkhrvnavag qsyqrnhyaq iwgrkrnila
      541 npaggyynvl dqgnepqtgg fkertdlisy fgrieynyad kyllngvirt dgtsrfgkdy
      601 kfgsypsvsa awriskedff nnswvsdlki ranygtlgss nigpydyiat intfstiamg
      661 pgqviipgst qvqlvnpdlr wekviqqnyg ldagflndri svsaeyfiak tkdvllrypl
      721 listgndggn pyvngvtlqn kgfeltatyr ensslfkydv tanltrlrnk vsdlgygknr
      781 tfvgntvter gqpigmwyvl etdglfqsne dvtnykneag mviqpnarpg dirfkdnngd
      841 gqinnsdkrv vgspwadyel glnmnfsykn fslsmdwfgs fgatvfngpr svmdmfsdnt
      901 nyragiqpwt petpntdvpr ayygstinsr gdtdrwledg sfvrlkyigl syeipsqimq
      961 rvgfrnaqlt isgqnlltft dytgldpefs nnsifekgyd fgafpnlrti slglqfgf
//
LOCUS       WP_285008577             287 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Pedobacter
            faecalis].
ACCESSION   WP_285008577
VERSION     WP_285008577.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..287
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31888
     Region          40..284
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mksihrnlcl lmfaalglta cksmnnkgki enhpeaklgw qlgsqaytfk nfsffeavrk
       61 idscnlryve afpgqtiggg iagkmdpkmd eatrkaildk mkttnvklva fgvygagsea
      121 eweqafrfck amgiqtitse pdekfiplls klcdeyqinl aihnhpdpsh ywnpetvlrv
      181 ikghskriga cadighwvrs gldpvaclkl ldghvlhshm kdlnekskkg hdvhwgegvs
      241 nipgviaelk rqdfkgtisa eyeynwnsns vdvaasvvnf rklvaqq
//
LOCUS       WP_285008579             381 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Lactobacillus gasseri].
ACCESSION   WP_285008579
VERSION     WP_285008579.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus gasseri
  ORGANISM  Lactobacillus gasseri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Lactobacillus gasseri"
                     /db_xref="taxon:1596"
     Protein         1..381
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42951
     Region          21..378
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mkkqkviltt kekselfgeg vitvilllll nlsiiillnl avlndprlen gifflkktit
       61 fangmhlwsw qrlfvgvmlv gdaivvywrl irryrqmqlr hvieelhyia dghfdhripf
      121 vvktdlqkvi dsinalvdst vasmeeerqi eqskddlitn vshdirtplt siigylgllk
      181 sselnedqak yikiaydkal qmkalaedlf eyttlrsstn nklvlaplhv nsmleqvaag
      241 feleaekkni afnvvarprd lvidadakmi vrmlnnlisn alkyghgate inliankvnn
      301 kfvelrvenn geqipkkslq kifdrfyrve ssrnlktggt glglaitksi vdlhggtikc
      361 qstseltsfi iqlplnspka k
//
LOCUS       WP_285008660             249 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Pedobacter faecalis].
ACCESSION   WP_285008660
VERSION     WP_285008660.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 249)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 249)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..249
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=27872
     Region          1..245
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mmravlidde ksnlenlrtl lskhcpqlti mataqnvada vsaieqskpd lvfldiqmgd
       61 qtgfdvlkll parnfevifv taydqygiqa vkfaaldyll kpvdidelln avnmaerkla
      121 ahfptsqldf llqqlkkpep svskialpmq neiryinlse iirceadnty thfflagnek
      181 ilvskplkey adllrpngfl rthqshlvnp kyvkswlked ggvlllisge kipvskpnkd
      241 avkqalqgl
//
LOCUS       WP_285008824             740 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Pedobacter faecalis].
ACCESSION   WP_285008824
VERSION     WP_285008824.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 740)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..740
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=80373
     Region          12..740
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 matdnsnekt ikrtfpvlgm tcascassae sitshqpgvv sasvnfatgn llveympkri
       61 gveqlqkamq sagydllied estqretldn lhaekfnklk nktiwavlls lpvvtigmlf
      121 mdmpyaneim wlfstpvvlw lgkdffanaw kharhrsanm dtlvalstgi ayvfsvfnmw
      181 vpefwhqrgl hahvyfeaas vviafillgk lleekakgnt staikrlmgl qpktimliqa
      241 dgtekqikid evkagdvilv kpgekiavdg lvtygssyvd esmlsgepip vlkkenekvf
      301 agtinqkgsf qfravkvgkd tmlaqiinmv qdaqgskapv qklvdkiagv fvpvvlgiai
      361 ltfllwvvlg gdngivhgll aavtvlviac pcalglatpt aimvgvgkga esgilikdae
      421 slelakkvna ivldktgtit egrprvtdiq wlnnddsakn illsiekqse hplaeavtkh
      481 lqgvqaisls mfesltgrgi kashhnenyy vgnqkllten qvqigeqlqa wadewsrqsk
      541 tviwfadsrq alsviaisdq iketsieair qlddmnidly mltgdneata kaialqtgir
      601 nysaevlpqq kadfirelqn rgktvamvgd gindstalat advsiamgkg sdiamdvakm
      661 tiissdltki aqaiklskrt vatikqnlfw afvynvigip laagilypin gfllnpmiag
      721 aamalssvsv vtnslrlkwk
//
LOCUS       WP_285008831             224 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Pedobacter faecalis].
ACCESSION   WP_285008831
VERSION     WP_285008831.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008387
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..224
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=24731
     Region          20..197
                     /region_name="TerY"
                     /note="Uncharacterized conserved protein YegL, contains
                     vWA domain of TerY type [Function unknown]; COG4245"
                     /db_xref="CDD:443387"
ORIGIN      
        1 mdeyisfeqi pfgsddfann pesrcpcmll ldtsgsmggr piqelnegiq ilknelvqds
       61 laskrvevam itfgpvsles dfqtvdhfyp ktlsangdtp igsavtlgie linkrkqlyr
      121 engvgyykpw iilitdggpt dnwshaakli qdgenenkfa ffaigvegan mdtlsklsvr
      181 spiklkglmf refflwlsss mkmvssknpg eqtkllpptg wanl
//
LOCUS       WP_285008840             851 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Pedobacter faecalis].
ACCESSION   WP_285008840
VERSION     WP_285008840.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..851
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..851
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=95260
     Region          47..222
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          280..837
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 mavrgnqfks nsfkneavdk qsvrsggtrr ttekrdilpt ldlqdgrlvk iiglvfiifs
       61 lyfliaftsy lftwqddhsy vidanggwgn lfktyeelqn vninpdvqnw lgklgallah
      121 qfiyewfgla sflfimiffv igyrllfkvk ifaiekmlay slfflifisl tlgflhafms
      181 ntphfvegef gywankllva qigtagvggl iiflaltvli iaynidfklp erklepkade
      241 ivpdvpehve leneirsepv eftlndrlgs qrkkeqnvvi aptrfepere pelepdavlp
      301 aavapavplp vevnlpvaet lvkaepeltv ekteeekkse elieqfghyd ptldlasyry
      361 phldllenyg snkisvnade leanknkive tlnhynieid kikatigptv tlyeiipapg
      421 vriskiknle ddialslaal giriiapmpg kgtigievpn lhpemvsmrs ilatekfqqt
      481 amdlpialgk tisnevyiad lskmphllva gatgqgksvg insilvslly kkhpsqlklv
      541 lvdpkkvelt lfnkierhfl aklpgeadai itdtkkvint lnslciemdq rydllkdaqv
      601 rnlkeyndkf ikrklnpnns hrflpyivli vdefadlmmt agkevetpia rlaqlaravg
      661 ihlvlatqrp svniitgtik anfparlafr vlskidsrti ldsggadqli grgdmllstg
      721 ndlirlqcaf vdtpevdris dfigvqrgyp eayqlpeyid eaaesakldf dpndrdgmfe
      781 daarlivmhq qgstsliqrk lklgynragr iidqleaagi vgpfegskar evlipdeyal
      841 eqflndldnn k
//
LOCUS       WP_285009065             246 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Pedobacter faecalis].
ACCESSION   WP_285009065
VERSION     WP_285009065.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 246)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 246)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 246)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..246
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=27808
     Region          1..243
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mfrtllidde slardivkhy lndfpdievv aeckdgfegi kaiaqhkpdf ifldiqmpki
       61 ngfemlelve qppaviftta fdeyaikafe vnavdyllkp iekarfdqam qkipgrlggm
      121 dplsaqqlld aaalspaqqn rvvvknngvi kiiavsdihy leadddyvkl stvegvfhkn
      181 ktmsffertl dpcqfirihr syiinlsqvt rielkekdsy ivllksdiwl pvsktgyvkl
      241 kaalgm
//
LOCUS       WP_285009087             334 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Pedobacter faecalis].
ACCESSION   WP_285009087
VERSION     WP_285009087.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10106971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..334
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=36627
     Region          92..280
                     /region_name="vWA_BatA_type"
                     /note="VWA BatA type: Von Willebrand factor type A (vWA)
                     domain was originally found in the blood coagulation
                     protein von Willebrand factor (vWF). Typically, the vWA
                     domain is made up of approximately 200 amino acid residues
                     folded into a classic a/b...; cd01467"
                     /db_xref="CDD:238744"
     Site            order(101,103,105,173,201)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238744"
ORIGIN      
        1 mswfegiefa dpvmfwllll vplmigwyiw knrqlqgtlr msafsgfaka gqgayrylrh
       61 ygivlralav aamvvalarp qspmswqdsv tegidiviat disgsmlsed lkpnrleagk
      121 qiaidfikdr psdriglvvf sgesftqcpl tidhevlvnl fqdvsngmie dgtaigmgla
      181 tavnrlkese akskvvillt dgsnttgsip plmaaeiakk mgvrvytvgv gtigyapypv
      241 ktpfgtqyqr vpvtideptm kkiagttggq yfratnneal kaiyaqidkl erakiavtqy
      301 hqkterflpw aliaavllla efllrntifk galt
//
LOCUS       WP_285009127             859 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Pedobacter faecalis].
ACCESSION   WP_285009127
VERSION     WP_285009127.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..859
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=99021
     Region          603..848
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mlkylisiii chcaipsala qkrplaidsf ksweslgdkk eisgdgryvg ysygsvtsgt
       61 ylilqgiken yrklfgafrg eiklsftdds ktlvfinesh lnlfdirsek lesigavqdf
      121 klfragkenw lvykttdqsl yvrnlntkql kkisaqtnty eideenlgil ictrssilsy
      181 hltkgkcdtv fkssnylavt shkkttqiaf lstganerdy svwyyrrgmk cstkivdstt
      241 cgvkskfcid ngniaftldg qaiifnakna vpssdnfkdt saggkiwnyk spfinrykqm
      301 stirliyrla nrkvfqlntd ttrltmeeks nymletsndm nedeyywnsq tyslnivsll
      361 dgskkliktf qkshklpran fspsgkyvvw adyaerayfa yeietretrk isgqvsealf
      421 deqteipark sffgrcgwlp nsdnilvydk ydiwsldlsg krepvnithg lgrlnnvqfr
      481 kleannlpss tllisaikid dkksaillwd vksefsfdtt rlnnvayytv ntsrsygvyy
      541 sldkpqksry hktylvsrms atespnlfvt edfkslrrvs nifpeknfnw mytelikwrl
      601 ptgeetsgil ykpedfdank kyptifnlye kksdeanvyk pprlsngdld iswyvsngyl
      661 vfapdfqykt grnseyitnt ivsavdyfrk ftwfdpgklg vqghsfggye tniliththl
      721 fraaqqsagv cnlinefsei wgdrtrqtfn qfnqlntgtk pwadpatfir nspiffadnv
      781 ttpllimhnp ndekvyfsqg velyaalrrl krptwllkyd neghelgsst nrwdftvrqq
      841 qffdhylknk ampnwmvgn
//
LOCUS       WP_285009123            1083 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            faecalis].
ACCESSION   WP_285009123
VERSION     WP_285009123.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=120708
     Region          27..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrilsllip allvfcynsf aqtqpkitit gtvtdsagva ipgasvvvek eskngamtgs
       61 ngkfvidvvp gsvlkvsyvg yldrlvpvta dtktltiilk enaiqvgevv vtafgkrerk
      121 ealvgsvtsi tpgdlkipas nltnalagqa agviayqrsg qpgqdnasff irgvttfgyk
      181 qdplilidnv elttndlarl qvddiasfvi lkdasataly gargangvil vstkegkegp
      241 akinfrseys msqstqtldl vdpiqymhmy neasltrdpt lplpftptki rnteatmaga
      301 pgsneyvypa vdwldmlfkk nastqrnnls vngggsvary yiagsynrdn gvlktdtrnn
      361 ndnnvkfqny qlrsnvnvnl tktteaivrl sgtfsdyngp itadgsfasd lysvamhasp
      421 vlfpayypad eanaranhil fgniggpdgt atnsirfptg npyaqllrgh knfsesrmsa
      481 qlelnqdfkf iteglkfrgi fntnrysyfd sqlayspyfy sysdydklnn sykltwlnpr
      541 nnvpnnvpte ylvysknepn ansfyylqga vdynrqfgsh nvstsligtm qqtlyssard
      601 prtntttlpy slpfrnmgla gratysyksr yfaefnfgyn gserfseehr fgffptfgvs
      661 wvasneefwn tngfinrlki rashglvgnd aigsqrffyl sdvnlnggnf aqfgvnnqnq
      721 lngvtirsya nsnitwetsr qtnlaaeitf lknfsmiaev yknhrydilr erfipstegf
      781 eaavstnlge vdsegidlsl dykqtfnntl waalrgnfty stnkytyiee pnyaeswrkf
      841 igqpisrgyg yiaerlfvdd eearnspsqi msttdaynnr ingilpqggd ikyrdvngdg
      901 kiddldqvfm gypttpeivy gfgfssgfkg fdlsaffqgq arvsffidpr kvspflernv
      961 pyidgntqvl qafadshwse enqdlyamhp rlgmsnamva nnlqnstwwl rdgsfmrlks
     1021 veigytlpar isnslklsnc rfylnglnli twspfkmwdp elggngfayp vqkvfnfgln
     1081 lnl
//
LOCUS       WP_285009218             445 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pedobacter faecalis].
ACCESSION   WP_285009218
VERSION     WP_285009218.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..445
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=49024
     Region          194..429
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mnrlrrlhdr ligspdqtil qarifhevsi ialllipaai ffnlfigvpy agyvlsaafi
       61 lvallfvnsr yfgnlkasva iftfsmasvl amnyyinsga qgptlllfvv lmvftislmp
      121 sdqykfwvvf naavvsalvi seysnpqlis esyegrasyf idilttyiav ivcigvvmay
      181 lirsheteka kvlkaskalk qandaktrll silshdlrsp lnsiqsflei lidynlseqe
      241 ekaikksllr etkntqvmlf nllnwtksqm eggvtvnlqk lnlnesvegc lkvqraaale
      301 kmitirnlta pdasivadpd mfsliirnlv nnaikfthtg gdisifsevg egftklmvrd
      361 ngigisedkq eklfsletqs aygtnkekgv glglllcwef temqggkisf ssrpgegtcf
      421 tlkfpsgqss visaayasge gktvy
//
LOCUS       WP_285009328             254 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Pedobacter faecalis].
ACCESSION   WP_285009328
VERSION     WP_285009328.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..254
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28086
     Region          5..>208
                     /region_name="Tdh"
                     /note="Threonine dehydrogenase or related Zn-dependent
                     dehydrogenase [Amino acid transport and metabolism,
                     General function prediction only]; COG1063"
                     /db_xref="CDD:440683"
ORIGIN      
        1 msesmkaalk taegkfevke vqrvqipapd wvlarvrvsg icgtdlrhwe khepelecki
       61 mghelagevv eigsevknvk pgdrvvietl lgdgtcdwcr vqqynlcpnl ynvrmetvsr
      121 afaeyligpa tkfhklpdhv sfeeatlldt fsvslhaqhl sglhindkvv vigagpiglg
      181 qlqlakasga dvliidvves slrvggadph rrqgshrrri rkrqdahgdr laksaderds
      241 ayserklffl ghls
//
LOCUS       WP_285009277             261 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Pedobacter faecalis].
ACCESSION   WP_285009277
VERSION     WP_285009277.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..261
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29291
     Region          88..261
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <199..261
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mvinnhsntd snlrqlldik llaqpfggae gqitleqakl iaevynridq ctcvlsdlks
       61 rksyiyysal aarlgieqrk leidsiweda llsrmhpkdv qakyrlelqy fqllsavpva
      121 ergnyevitg lrardeqgkf vklkhrllyi ssaddgsvsl alclyylvyd hpghgvpegv
      181 ivnrktglvi gydeeqfnrl lsprelqvlq likaglrske iadklllsin tvnrhrqnil
      241 kklnvtname acsvavvtgl v
//
LOCUS       WP_285009323             916 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Pedobacter faecalis].
ACCESSION   WP_285009323
VERSION     WP_285009323.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 916)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 916)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 916)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 916)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..916
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..916
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=103022
     Region          37..>542
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          555..>626
                     /region_name="LacZ_4"
                     /note="Beta-galactosidase, domain 4; pfam16353"
                     /db_xref="CDD:465101"
ORIGIN      
        1 mrrictailf ilacssavaq stivkylsgr dkdhtvnwdf fctdgrksgy wtkipvpsnw
       61 elqgfgsyny ghdkvksneq glykyefgtg kvdgkrvfiv fegsmtdtkv mingkmagpv
      121 hqgafyrfky ditdllkpsg knllevtvsk tsanasvnqa erksdfwilg gifrpvylei
      181 vpqkfidrva inakadgsfe mqvfpenlng tetieaqiqt legkaagasf sanagntads
      241 vvlrsqlnsp qlwsaefpnr yqvvvtikna gqiihqvkqk fgfrtvelrk ndglyvngek
      301 illkgsnrhs fwpesgrtls hsihlldvrl mkemnmnavr mshyppdqdf ldvcdsvgly
      361 videltgwqs kydtvagrkl vkelvvrdvn hpsilfwang neggfnrald ndyawydpqk
      421 rtvihpwekf ngtdtrhypd ydymvksaat gkevffptef mhglydggag aglddywnqm
      481 lkhphgaggf iwafvdeail rtdkngaydt dgnhgadgiv gphrekegsf ytikeiwspv
      541 yvglrkigad fsgrievenr ydftnlnqct fqwklvdfpa adkkgtepiv rasgypklan
      601 vkpgekgwle lnlpgswrny galyltayga dkkeiftwsw alkpaevmvq ktrsarsaql
      661 kaddqgdnlq iicdgttyvf dkvtgyisqv lrkgetvsls ggpvlasgaa elkmfshhev
      721 dgqyvveasy ggagalrvrw tfasgtpakl eyeygrqdaa dfsgitfnyp eekitgmrwr
      781 grgpfrvwkn rmkgqqlgvw kktynntvtg ehwqypefkg yhaevswvtv qtkespftvy
      841 sndedvffqm lrpakekdvl nnnvgpvfpe gsigfldain pignkfhaar stgpegqkne
      901 akaerikrtl wfdfgr
//
LOCUS       WP_285009350             396 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Pedobacter faecalis].
ACCESSION   WP_285009350
VERSION     WP_285009350.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616068
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..396
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=44709
     Region          160..296
                     /region_name="Methyltransf_32"
                     /note="Methyltransferase domain; pfam13679"
                     /db_xref="CDD:379330"
     Site            order(190..196,219..220,245..247,261)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
ORIGIN      
        1 midpeifeef ririhqvvas eafvkaslgn yhgiepelkk iyirpvlikg hkmlaftyry
       61 ktrdifknff vdegialleq fvvsgfrict vlstsgefvl evnkkgkvsl resqsdltre
      121 vslshdrfkk rliesgpnql yltqlgltdk sgkvlksgqd kyrqinryie ildslvcsvp
      181 sgsikhvcdm gsgkgyltfa lydylinvrk ldvsvtgvey radlvalcnn iaekasfdkl
      241 rfvegtiaef ssdsvdllia lhacdtatdd aiikgircga qlvvvapcch kqvrrqmekv
      301 kvrnhlsplt rhgvfmdrqs emltdairvl ileyfgyrvk viefisdvht pknvliagvk
      361 gnvsvarkaa iledltalkr yfgitehyle raflqq
//
LOCUS       WP_285009387             110 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Pedobacter faecalis].
ACCESSION   WP_285009387
VERSION     WP_285009387.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 110)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 110)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..110
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12024
     Region          10..99
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mgatktdlft keqnemaama kalahparia ilqylikknv citgtlveel glaqattsqh
       61 lkelknagii qgniegtsvc ycidakiwkq ykalfnsffg diqikeqncc
//
LOCUS       WP_285009455             268 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase [Lactococcus formosensis].
ACCESSION   WP_285009455
VERSION     WP_285009455.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..268
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=30640
     Region          23..251
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mkikcelynd nfqnrkkyni praqlviadi pynlgnnafa snpswyvggd nkngesskag
       61 kqffpsdknf nlveymhfcs kllikepker gkapamimfc sfeqmaplie vakrfgfkks
      121 yplvfikkss aqalkanmri vgateyavvf yrdklpkfnn awqqeetgkk mvlnwfewkr
      181 dsvkqvpkih ptqkpvnlle kliktftdpg dvvidpcags gttllaakkn grhsygfeiy
      241 kpfykaaveq llpsfnyeeq ldlfkdis
//
LOCUS       WP_285009482             204 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Pedobacter faecalis].
ACCESSION   WP_285009482
VERSION     WP_285009482.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..204
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22020
     Region          55..200
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mlaeiptkdk ktwfsfsnls tvlliglavs mfvfpdvksv llrglmavgl fqpempavkh
       61 saastqnvif kdasgrsist gdlkgkvvfi nfwatwcppc raempginkl ynnykskqdl
      121 vfimadadgk peaalaymkk kgfalpvhti asdipdtmfs gslpttviln ksgqivyrgv
      181 gaadygnqkv adfldhllsg gqpk
//
LOCUS       WP_285009557             289 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Pedobacter faecalis].
ACCESSION   WP_285009557
VERSION     WP_285009557.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..289
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=33015
     Region          143..>277
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(144..145,147,171,174..175,178..179,181..182,205,
                     208..209,212..213,216)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          169..199
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          204..232
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          241..267
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkfspfkclv llisiaplfl saqqkaatdl vfnknfydme nqwvvfpkkh tdsayaygvv
       61 yvdssagftf dfqgtfkvmd dgtfsarpfs nsgnakvrle tniaqvspls adrlkqlnlp
      121 qeaaflkhyk vnmeetrniv twgrhynhvg ayakaleyll nayakephaa glefelafny
      181 nankkfdkaa evlnvamrhd pknfwfyrel gytymnlgkl edaektysag idlagqspqk
      241 memaynmayg ffsvrnkgkf eewykkaeql ianpnsvmmr nlndmkqkl
//
LOCUS       WP_285009566             106 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Pedobacter faecalis].
ACCESSION   WP_285009566
VERSION     WP_285009566.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..106
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11132
     Region          2..104
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mawlflilag alevvwsyam kqsegfsrlt pslvtivamv asfgllsism rtlplgtayt
       61 iwtgigavga filgvvflge qftatrviaa clivaglilm kfssvd
//
LOCUS       WP_285009653             331 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Pedobacter faecalis].
ACCESSION   WP_285009653
VERSION     WP_285009653.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..331
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36906
     Region          193..331
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mnvlqaqqtf kirgnvnris gsktiqmgrl sapiqedgsf elagevtepk lealhldsss
       61 lsllwlepgd yllscreekh qghtstqlki vvkngpadas vfgrfnetag knflidasik
      121 gpeaqrkiae ayadslfkny pnakflpavv fssrsfvgld atkkyialls pelqkdrliq
      181 niqsdikrae rlaigatfdd falkttdgkd fklsslkgkk iivldfwakw capcraghpk
      241 lvelykkyad kgleivsvsl dnntedwlsa ikedqigswi nvsdlkawqt epvknnyiny
      301 ipfslmldgd rkilgvynfs kptekdildn l
//
LOCUS       WP_285009674             416 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pedobacter faecalis].
ACCESSION   WP_285009674
VERSION     WP_285009674.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 416)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 416)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..416
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=46786
     Region          <44..416
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mckitasrld giilaltefs rgnfavrldv sddgdplntv taglnrlgee lektnqlvtr
       61 litssdqvfy ivsidqtdpf kntftylsph vegvigfsvd dvrnepllwl nsihpedleg
      121 vkattkemft sksprtrvyr mkhkrtgkyv wledyvvpil detgriqefy asardftark
      181 eaelererli aelnrrhdel mqfshivshn lrspvanilg laqllhedvp saslaettgy
      241 ilkaaqsmdh vlrdlntvls vrssleekmq tfllseiisl vcinlkkeid esaarihvtv
      301 dpladeltsi ksyvqsalfn lisnamkyrs perppvidin vykegthtvi siqdnglgid
      361 ldlhqhrifa lygrlhsdrd gkglglymtk tqveslkgti avesevgrgt tftirl
//
LOCUS       WP_285009723             267 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Pedobacter faecalis].
ACCESSION   WP_285009723
VERSION     WP_285009723.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 267)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..267
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28915
     Region          1..246
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mktlnqfalv tgatsgigye laklfaadgy nlvivsrdqq eldrkaeefr aqgvqvhaia
       61 adlfnrdesf avhekvksmg ihidvlvnda gqgvyglfqd nelareldii elnvsslvil
      121 tklflkdmlq kdagkilnva siaskvpgpw qavyhgtkaf vlsfsegire elketgitvt
      181 allpgvtdtd ffnkadmqss tivqdkdams dpadvakdgy ealmsgkdkv tsglknkiqv
      241 amsnvlsdsa aahnmhqqqk pvdpeks
//
LOCUS       WP_285009754             421 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Pedobacter faecalis].
ACCESSION   WP_285009754
VERSION     WP_285009754.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..421
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47224
     Region          286..420
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mvitkimfvv vialpfclha qtdagkltpe qqasklkrny evidsvqari saekdvrkkd
       61 vlfcdffnsa agqekffavy rdgilkdlav gyaanndtta sdarigmirn drtreeavrl
      121 saaayatagn verglrmlrp kldafflpdg tlktenffny dyavkvlvsi lpegsevevi
      181 hylrpyyqfs ggffpsdvwe rlakpdlepr kqlfyryaea lrkespkeia avvakafeig
      241 avpkpmrpav ikdfsdvsgf erqfdavsaa gragfnrnvs allskpdmng kvwgaqglke
      301 kymlidfwgs wclpcrfghp hlkelyakyk drgfeivgia keapaapevi qqkwrkavae
      361 dkiewihlln nenestfdav kafgigsfpt killdkngne igryggkpde ldaklkeifg
      421 f
//
LOCUS       WP_285009804             173 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase [Pedobacter faecalis].
ACCESSION   WP_285009804
VERSION     WP_285009804.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..173
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=18794
     Region          1..143
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mnklillfak lgnstvkrvi ytkylgvrig dnvrftgspd fgsepylisi gsnvtitqnv
       61 tfhthdggls vlrkkyprin kygritigdn vfigsgvmim pnvdigdnvi iaagsivtks
      121 vssdsvvggv pakllktiqq yerdvisrnd hiimpegleg kakekfiids lkk
//
LOCUS       WP_285009815             209 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase [Pedobacter faecalis].
ACCESSION   WP_285009815
VERSION     WP_285009815.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..209
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=22835
     Region          41..190
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mikyiyrila elkrrklksk ctlkgsvyfs dssdirlyyg sdkgdvvign hvkmygkltt
       61 qnhakiickd nvtigsntiv havsgvtfet gatisynvti sdnnnhpvhp edrkliysnp
      121 spkylyrsvw eisdnapvvv genawigaha iilkgvtige nsivamasvv tkdvpansiv
      181 agnpakvvrt dihllprklv mkdgdisil
//
LOCUS       WP_285009833             389 aa            linear   BCT 25-DEC-2024
DEFINITION  trypsin-like serine peptidase [Pedobacter faecalis].
ACCESSION   WP_285009833
VERSION     WP_285009833.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..389
                     /product="trypsin-like serine peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43488
     Region          202..356
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mvrtagrlpe rarrpasldt vhiafeafpq lkdlyqeris etvsemvsdn ishemaelkt
       61 aametqqnqv sqqlvrqtsq ahrqqqmrqq qmrqrqqlrr iqraaesaak sltisksele
      121 lkkpllsgps qfdsrvephv ldlktpwqkk igdnassvgi vvekdklhav tdstfqldig
      181 itlgtryklc pgepfaeqpv agvgtafiva enkmataahv fsepvenyvv vfgfvmqsak
      241 gkynalisnr niyhpikvvh kdtdvdltvf evrerisrqp lqlalksdpa lkteiymvgh
      301 psgipqkial nadvqenkhp qyfyssldaf qgnsgspvfd mkthqvigvl vsgevdyiwn
      361 gscnklslcq fpyckgekvi kistlenvl
//
LOCUS       WP_285009861             225 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Lactobacillus iners].
ACCESSION   WP_285009861
VERSION     WP_285009861.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..225
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25800
     Region          8..220
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mktnlnktfk avifdldgll vdserlywra niqaaqelkt piprdaylei vgaspekvae
       61 fyhdffadas lkdkfisrtn elfsfwlaeg qlhlkkgvlq flqklkkdqk kciiassntk
      121 evieqilqkf hienyfdffi cyddvkqarl qakpapdiyl daikrldmqc delivfedtg
      181 igvaaaqkag lrcvmipdlk patiqdkkla ylicnnflef sknny
//
LOCUS       WP_285009895             379 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Pedobacter faecalis].
ACCESSION   WP_285009895
VERSION     WP_285009895.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..379
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42470
     Region          7..375
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 miktiqmvdl kgqylkikde idtsifdavm etayingpqv kqfadqlskf nnvdfavtca
       61 ngtdalqiam mglgfkpgde vivpaftyia tveviallgl vpkfaevred tfeidvryld
      121 glitertvgi vpvhlfgqcs nmellmafae kysisviedt aqamgaeyif ksgdrrfagt
      181 ighvgttsff psknlgcfgd ggailtdnae lgqrlhmian hgqrrkyhhe viginsrldt
      241 lqaavlnvki kylndyarar gkvasyydqq lgsiselvip krasysthvf nqytcrvlng
      301 rrdqlkeyln ekgiptmiyy pipvhlqeay lsygykkgdl pvserlceev islpihtemk
      361 devlkyiveh ikiffkdgk
//
LOCUS       WP_285009863             482 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pedobacter faecalis].
ACCESSION   WP_285009863
VERSION     WP_285009863.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 482)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 482)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..482
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55230
     Region          5..474
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          <124..>259
                     /region_name="PRK09776"
                     /note="putative diguanylate cyclase; Provisional"
                     /db_xref="CDD:182070"
ORIGIN      
        1 mptklelyer vtplaglgiw ernlvtgeay wnqiireife ieaaetpamd evimfykdpa
       61 riraildeam rsgqphtgtf eistasneqk wirlrvqsqi aggaceriyg tieditdnvr
      121 llnelqekek rfseafdhap igmalvspeg hwikvneslc qllgyneqef mnhtfqefty
      181 pkdldsdlrq mtlllngkiq rysmekryyr angvliwall svslvrdaag nplyfvsqvk
      241 ditqrkrnme tirdqnarll nfahiishnl rshtgnirmm tsmiseeqde eeriklveml
      301 dinannllet lnhlnevvki hdkgqadvae lhlrqqverv meilgpsfra arakvdlqid
      361 palvinyspa ylesilinll tnclkykhpe rkpeisicae ladsfiqlsi sdnglgidle
      421 lhghklfgmy ktfhkhedar gmglflvknh veamggriha eskpgegtkf tmeinthtyt
      481 he
//
LOCUS       WP_285010014            1073 aa            linear   BCT 25-DEC-2024
DEFINITION  UvrD-helicase domain-containing protein [Pedobacter faecalis].
ACCESSION   WP_285010014
VERSION     WP_285010014.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437585
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..1073
                     /product="UvrD-helicase domain-containing protein"
                     /EC_number="3.1.11.5"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=122058
     Region          7..1073
                     /region_name="RecB"
                     /note="3#-5# helicase subunit RecB of the DNA repair
                     enzyme RecBCD (exonuclease V) [Replication, recombination
                     and repair]; COG1074"
                     /db_xref="CDD:440692"
ORIGIN      
        1 mankplkilq asagsgktfs ltahyltlll sgenkyreil avtftnkate emktrildvl
       61 egfargepry dsyreivlka hpkldaaelr dradriyrki lhdysrfsvs tidgfvqkvi
      121 rgfafelgld tsynlemnye kvkeelvskl dealdhnkql lqwiidlaie risdnkswny
      181 ktelynlige ifkerfqsfe davsamgdne idalfkryid vnkeaiknfe geltnlaiea
      241 qdifnrfgve kehlnrksqs plakipmiig gdlskiealf nfvddpdiwf qkntrldevy
      301 aalnpvlkki qtyytthlpq ytlalafnkn lyylrlmqei avllklyree ndnllisdaq
      361 klisgitdda gdnpsfiwek vgtryrnflf defqdtstsq wnsfrslltn aiatptehli
      421 dhlivgdtkq siyrwrngdw nilhsqarld vgadrvlees leenyrsaen iitfnnflyv
      481 qvprllqedl natiqtrpsa icewwqqkgf eqiitsiyst avqqtakstp mggtirirki
      541 gkedadagqr fsesvfrdia ldelvkeish lktdlgyaak diailvrsnt eavltvkklm
      601 sqgievisge almvsansai qlivetlrvf tgvdtqtalh kancialyha lkaesldash
      661 ymglnnisls nlhhvlpaal ctnwqswiql plpelvemli eayglsemee hlpyllafrd
      721 ltcnagklge kgivafleww sqegitkslp spetadavqv itihkskgla fravfipfct
      781 weikgkansi fwvsstntay selrgiplry seslsnsvva qayyeellyn ymdalnmlyv
      841 attrakdyls igtmvkkdta klstvgdvln nifqqefden nvyeivdvvp erdtqthdtt
      901 kikldhypvs trlsnlyldt qerhlkhlln mdkssrrgsl lhdvlanatt aqqvedylsv
      961 lvldgivqet eseelkmaaq kvlsnpdlqa ilnrpsesit ekniidpqgk ihrpdlvlin
     1021 gdqvvildyk ftlteaaehl qqvlkykslf tqmgyskvdg ylfyavtgql rpi
//
LOCUS       WP_285010069             274 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Pedobacter faecalis].
ACCESSION   WP_285010069
VERSION     WP_285010069.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..274
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31846
     Region          6..272
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 megavisdeq vdllladtle qygydftgys raslkrrilr lftldkalsf aefryrinnd
       61 ssyfkrfveq itvnvtemfr dpmffktlre evlpklgtyp firvwvagcs tgeeaysiai
      121 ilkelnllek sliyatdinp avldraaqsi falsymkqys enyilsggnk efsgyytany
      181 slakfnddlk kkiifsthnl vsdrsfnefq lilcrnvliy fdrelqhkvf glfddsleel
      241 gylalgtket infspflkky krlgtekiwr kiqk
//
LOCUS       WP_285010169             409 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Pedobacter faecalis].
ACCESSION   WP_285010169
VERSION     WP_285010169.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..409
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45738
     Region          1..407
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 meynvhtlpn girllhvpsa spishacivi nsgsrdeadd ksglahfieh lifkrtekrt
       61 tnqilnrles vgadlnaytt keytcihasf lnpyldrtle lfndivfhst fpedemekek
      121 svildeiasy ldqpeeaiyd dfedlifagn algrnilgss esvmsitrad ifkflafkyr
      181 tseivvavlg nysfnrakav ftkhyadiae ntpsltrtpp kkvrpraive qkpiqqvhav
      241 lgaqayslhh eyktglllln nflggngmss vlnlqirekh giaytiessy splsdtglft
      301 iyfgtdkekv dkawmlinre lkkikdkpls piqlqkakqk ligqialgee nrigliisma
      361 kslldygfvd slqtvfnkie avssdaladi anevldeenl sslsffpis
//
LOCUS       WP_285010204             420 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Lactobacillus iners].
ACCESSION   WP_285010204
VERSION     WP_285010204.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..420
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47025
     Region          26..413
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mlsyeeiisg fsqkmlagdh nhvvflrnik krlgspeqaf ktihiagtng kgstgmmikg
       61 vlehagykvg yfnspalidd reqisinnil isrndfvaty yeilnklspd esakisvfew
      121 wtlimlvyfa nkkvdwavie cglggtddat niinapeyai fthialdhih ilgdtvekia
      181 kaksgiikyg tkatiiaplq qkaavniike kcsqaqvpli lsddiakikv hnrkiniiat
      241 dftlessfsl lgeyqrenlk tvialvkqlm rekvlislmp lkqmletiki parcekiasl
      301 pdvlidgahn pdaaynlaqt iinlrhgrrv imilgflkdk nyqkmiqiyq eishdfilte
      361 pdhlqrklpv ailaqnfnnh vmqavnvrsa lkiarqnakp ddlivvtgsf ylvkdlindd
//
LOCUS       WP_285010394             369 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Pedobacter faecalis].
ACCESSION   WP_285010394
VERSION     WP_285010394.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..369
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41126
     Region          19..369
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 metatltgqd iayedlhaln kpfmeayqqs ftdslnkgwf vlgdkvrafe qafaryngsa
       61 hcvsvasgld alvlglqyfd fpegsevivp sntyiatila iyhcrlvpvl vepdlatyni
      121 dpeqtaaavt srtraimvvh lygkpcnmea imaiaarhdl rviedcaqsh gaefmgrktg
      181 tfgdfgafsf yptknlgalg dggalltsdt sraekiralr nygchekyyn eyiginsrld
      241 eiqagflsvk laaldqinah kralasryde glkadfikpl kqegytdvyh iytvrhperd
      301 klrayllann ikteihypvp phhqnalrdk lkgafpvsel ihrstlslpi sfchareeid
      361 rvvevmnaf
//
LOCUS       WP_285010447             354 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Pedobacter faecalis].
ACCESSION   WP_285010447
VERSION     WP_285010447.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..354
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=39651
     Region          3..335
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mvpkserrfi rlnlitivit llvilaggvv rstgsgmgcp dwpkcfdqyv pptsasqlpa
       61 dykekyvngr iaknerfakt lerlgkghla dsirhdesir epeefnvakt wteyinrlvg
      121 altgimllav aiasftyrkt akrivvlsil nifvvayqaw lgsivvstnl mpwivtvhml
      181 lalvilaili ytyyyarkmr qqavlaagkt gtltmilfls ialsvvqivv gtevreaida
      241 iakslfyaqr etwvgkvgth flyhrdlaia vlvlniiiya imrrlykgsk eqmfvanavm
      301 ivlliqlltg vllanfalpp yaqamhilfs tmlfglqyyl yllvyktgsf nqtn
//
LOCUS       WP_285010474             555 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pedobacter faecalis].
ACCESSION   WP_285010474
VERSION     WP_285010474.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..555
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=63534
     Region          328..555
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mssdkksgyr knfsliitfi ilmmvlfils lflayrfstk iienefasek vnvleesika
       61 yndffqkklp evsyyngyld satashfvdt vlleypfvsk vifydsevrn tpvsdglntg
      121 rfsfgpkriy qfgslvpads vllfstdhtr nfiagddfnq lalklaayve sldttsmpsq
      181 eelfsnfsiv rankisylni prmedlkmyk rmmrrrlepq pvyqqdmlsf qldpykiria
      241 ntrphlyqhv riepltydpl dtsisyvste ialpgpfsdy klylissqsf idkeifnyfl
      301 piaigillfy givvlvafli yrnlninqkm fklqydfvnn lthefktpvs vikiagnnik
      361 saaalsqrel shygkildee adklnglmnk llaftqienr aiklnqdlin ieefisgtve
      421 shklkhpdfe ftyevsgfkt iitdpvllgs lfdnlaenay kysppnrkkl hvsamlvkgk
      481 avfrfadqgi gipaseinni fkkffriqnq ynqngsvglg lafckelvnf mggevsvksr
      541 vdkgtefkiv lpyhd
//
LOCUS       WP_285010647             222 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Pedobacter faecalis].
ACCESSION   WP_285010647
VERSION     WP_285010647.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..222
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=24373
     Site            order(102..103,106..107,109,135,138..139,142..143,
                     145..146,172,175..176,179..180,183)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          102..126
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          108..217
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Region          133..163
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          171..196
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msttekeinq pvhkgsfvqe nsksllfiag aivvligiyi wyqsvylknr aeeasakmyk
       61 aeqyigvdsl sakaingqgg ypgleqiade yentksanla nlylggiylr kgeykkaves
      121 lgkysetgsp vadplalgll gdayselkdy nkaatyykka adkssnkfts plflkklglv
      181 yenqkdfkka keayekirad fpasqeaaii dayiaraeaq vn
//
LOCUS       WP_285010690            1008 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            faecalis].
ACCESSION   WP_285010690
VERSION     WP_285010690.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=109665
     Region          27..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkriptklsv fvfllllfag tasaqnitit gtvidaadks plpgvgvlvk gtqigtttss
       61 sgaysinapa datlvftyig fttqevavgn rttinitlae saqdleavvv vgygtqrrrd
      121 vtgsistvsg etiarqpnvn plsslqgqva gltivnsgsp gasptvrirg insvngaapl
      181 yvvdgvhqsn idylnpadie sievlrdpss iaifglqagn gvivvttkra argetrvtlq
      241 ssagiqkvqk lidvtnasef rklydqllaa tpnatpfdys nytgdtdwqk eilqsafqsn
      301 nsltisnnge ktstlinlgy ntqegvikfg rfqrfvarvn eeinvtdkik vgaditgthw
      361 ilnassgnln nalwaapivg iresetayya mpsfqraqvg npvatiyqnd rnsinkgyra
      421 vgslfaeigf ldkfkwrsqv ytdlgfnnsr gytplpftmi ylgengepte yfnnpqsrts
      481 vrqaaneyrk fqqdhtltyd ntfneshkvt avagmtsive sstllsgsrt dvglnipddq
      541 sfwyvglpes tnptnldgsg teraslgffa rvnyaynnky linatfrrdg isrlapqnrw
      601 gnfggiglgw vvseenffki ngidflkirg awgtvgnaqg isdaiflpgl ttsnsgvfgd
      661 nvypgvapay ipdprlrwev vrgadigldi raldnrltse invydktskd iitditlpsa
      721 ngsyryrtnl gtitnrgvev nigwndklge nftygispnf synknkvvsi gnninyllig
      781 ngganrtitg esighfygyr qvgiyqstad ldrmprmnss lpgdiayadl dgdgritead
      841 renlgspfpa wnyginlnmg ykgfdlvlqg qgvagnhvyv qrrnvqftdi nfernrlnaw
      901 ngpgtsnvep alvkgrgnny lmstyflepg dyfrlrtvql gytmnadalk stglksvrfy
      961 lsgqnlqtws rttgytpeap iesilgggad ngtypvpavy tfginatf
//
LOCUS       WP_285010754             336 aa            linear   BCT 25-DEC-2024
DEFINITION  DHH family phosphoesterase [Pedobacter faecalis].
ACCESSION   WP_285010754
VERSION     WP_285010754.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..336
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=37559
     Region          5..327
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mlsvseiksl latpqkivit thhkpdgdam gsslglyayl iqkghhvkvi tptdypyflh
       61 wmpnnseviv ytenqelsar lveeaamifc ldfnslsrin elgelvrasg ayklmidhhl
      121 epedfdhyrh wninacaaaq lvyefivdem qdgasmtkdi atclytgimt dsgsfrfesa
      181 tssvyriaad lidmgaehwr ihqlvydnat enrlrflghc isnkleilre yntaiisvtk
      241 eelkafdimt gdtegivnya lsingirlaa fiiertdkvk lslrstgdfp aneickkyfg
      301 ggghrnaagg iseaglaetv eqfksiltey ktqllq
//
LOCUS       WP_285010809             270 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Pedobacter faecalis].
ACCESSION   WP_285010809
VERSION     WP_285010809.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..270
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30680
     Region          19..268
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mkrvfalfaf tfavlqlsaa tvdtvvtrsv smkkdikavv ikpdsygsgk ayptvyllhg
       61 agdkfsgwvn kvprikkyad dfdliivcpd gnvtswyfds pldptwkyet yvatelvnwi
      121 dnkyntiknr sgraitglsm gghgalylsi rhqdvfgaag smsggvdirp fpmnwdiakr
      181 lgpksqypqr weentvvnll hllepnklsl iidcgrddff yevniqlher laylniphdf
      241 tirpgahnwe ywtnavgyql myfnnffgrk
//
LOCUS       WP_285010814             288 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pedobacter faecalis].
ACCESSION   WP_285010814
VERSION     WP_285010814.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..288
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=32408
     Region          55..287
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mkksiiifyl lllyslvqli swgamvvrle rsrmamvmge gsvflfllcv gayflhraik
       61 kedrlreqqq nfllsvthel ksplaaikls lqtiikrdld rprqvsllnn slkdierldd
      121 lvenmllatk ienrsysfpk eefdfselvt kitdrlqihs cgceqvikqk iepgvklvgd
      181 qfalasvvtn lvenavkysg pcaevgvelt mrdghpfmsv sdrgpgvpda ekmlifdkfy
      241 rvgdenvrks kgtglglfiv kevlqnhgad isvkdntpqg aifeiifn
//
LOCUS       WP_285010815             171 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Pedobacter faecalis].
ACCESSION   WP_285010815
VERSION     WP_285010815.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..171
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=19779
     Region          56..150
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
ORIGIN      
        1 mynntgryai mallisvavv cffmeqmqla alaglflcyv iwshfkhssv vmaarfyqng
       61 dyeraarlld evpnpdrlar srrgyyefmr gnialkkely ddaeyhfqva srfpmggrnd
      121 kafvlihlan lslrkldrdk traylakare mvstpkakel idklerelnr l
//
LOCUS       WP_285010860             106 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Pedobacter faecalis].
ACCESSION   WP_285010860
VERSION     WP_285010860.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..106
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12591
     Region          4..83
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mrrdifqaia dptrrailll lavqsmtpng laehfdttrq avskhlrvlt eceivkqqqq
       61 greiyyhlea ekmneieqwl erfkqlwkar fdqlddvleq lkknri
//
LOCUS       WP_285010920             330 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Pedobacter faecalis].
ACCESSION   WP_285010920
VERSION     WP_285010920.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..330
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=37323
     Region          45..307
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          176..203
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          211..237
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(213..214,217..218,220,246,249..250,253..254,
                     256..257,279,282..283,286..287,291)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          244..273
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          278..307
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkkialflmt lmsaqfvlgq dtlavdsvqs vvksdsagfp eltklaedha srgymnkarf
       61 yylaaakads tsilpykrls elekgsptgr rltylelahk mdpvdadias elaalylenk
      121 dfkraaavla palnadaenl rlkrlmmpvd lenrkyrevi ktgqvllseg dstvmvldhl
      181 gkayyltldy rnavkhflmi petmssdkea lyydlarsyr girdyksait ylekainlgv
      241 spraasyygl lgdsyeqiqq nepatkaykr gldfendgsl lyniallyem kmgdkknaid
      301 yyerylktid ekkkvkqanf iknkiaelkr
//
LOCUS       WP_285010981             480 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Pedobacter faecalis].
ACCESSION   WP_285010981
VERSION     WP_285010981.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..480
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51925
     Region          3..471
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 msktaydaiv vgsgpnglaa aitlqqegls vlliegkdki ggglrsaelt lpgfmhdvcs
       61 aihplavgsp ffqtlplsdh gltylypela aahpfddgta avlssslrdt arclgaderr
      121 ylklmgpvve dwpdlaadvl gplrfpkhpl klasfglkal tsatylsrrf ktakarglwa
      181 gmaahsiqpl snlstsaigl vlmaaahlkg wpvpaggsge iaaalssyfl slggrietnw
      241 yvrsldelpt aktvlfdvtp rqmlqiaghr fstiykwqle ryrygmgvfk idwaldgpvp
      301 ftaaearrag tvhigntmee iefserecwq gkhadrpfvl laqqslfdds rapsgkhtaw
      361 aychvpygst kdmttaiegq verfapgfrd lilarhtmnt aqmqeynpny iggdinggvi
      421 dlaqlftrpa lrmspyrssa kglyicssst ppgggvhgmc gyhaakralk dvfsihlsdl
//
LOCUS       WP_285011004             291 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pedobacter faecalis].
ACCESSION   WP_285011004
VERSION     WP_285011004.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..291
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33862
     Region          40..291
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkneipiydi ssftgfrked iivsrfgpys kthqhlhyah rhsfyhvvlf tegsghhsid
       61 fenfevkpwq iyfmipgqvh swsftgavdg yvvnfssnyf qsfllltdyl qkfsffsgvv
      121 rdsvlevped crraiggife elliagnqsk rfsddyiril llkmfimlsd lvaekpdayv
      181 tsynytllkn fqqliernfa elrlpkayae llyitpnhln alcndllgmp agevirnrvv
      241 leakrllvnl dlpiseismq lnfndnsyft kffkkyvgqt peefrkhtlk k
//
LOCUS       WP_285011050             476 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Lactococcus garvieae].
ACCESSION   WP_285011050
VERSION     WP_285011050.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 476)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 476)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 476)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 476)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..476
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55033
     Region          29..468
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 mfhyvwkksk nrvkyiiwse kityggilml infrvenfls isnliefsmv sgktkrhmkn
       61 tiafgdksll kfsaiygana sgkssfikai sasrqliveg fdsigviqns ynknarened
      121 ketkfeydia igdriytygf svilskmefi newlydmthd etlvynidky nkaineeyls
      181 lkesiynrle iyaednqsnr iqlflsalne gkkefvlkdg raifseifdw fsnklevigp
      241 dditrdfnrd vsrksniylk nlanylrasg tgvtevitvs tnslvdippk lqdkikqdml
      301 eeesgkvvkr tgllrtpkhi yilnakngnf sieevkfkhl sgatynlyee sdgtvrliel
      361 fsilfnkrdk vfvideldrs lhplltlnfv esfldkkgkg qlvvtthedr lldldlirrd
      421 eiwfvekdsv gnstlyslee ykerfdrnvm kayldgryga ipklenlfss lnsevl
//
LOCUS       WP_285011051             471 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Pedobacter
            faecalis].
ACCESSION   WP_285011051
VERSION     WP_285011051.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..471
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=50621
     Region          1..453
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 meglltsind liwsnaliil cmgtgiyfsi vtrflqvryi kemwrllfdg kssdkgvssf
       61 qafaiaisgr igtgniagva taiamggpga vfwmwliafl gaasafieat lgqiykqvkn
      121 geyrggpsyy iekglglkwy avlfavatvl stafflpgvq snsialsmqn afdipvaytg
      181 aavvillali ifggvkrigk vaeiivpfma ggyilmaivi mlmniaeips viglifrsaf
      241 dlepafagif gmavawgvkr giysneagqg taphaaaaae vshpakqglv qafsvyidtl
      301 fvctatafmi lftgkynvln pdgnflvenl pgakigaeyt qqaisshfpa lgsgfvavsl
      361 lffafttima yyyiaetnls yldkkgnkwa inilrllllf stfygsvkta eaawtlgdig
      421 vgmmawlnvi ailllrkpal kalkdyqqqr kagkdpvfda raagientse w
//
LOCUS       WP_285011064             514 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Pedobacter faecalis].
ACCESSION   WP_285011064
VERSION     WP_285011064.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..514
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59540
     Region          390..486
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mkylstlall ffvftanaqt keqldtdvpa hiqkwlsekt afkkskarsk afflrdsiki
       61 vgyikgydrs sgyasgiiyh anniirqdfp ttvriypdgr fecamlgihp irssiylnnh
      121 tikfyaepgt ttglildfqn pkylgvnkvi neqlaaietp rpdynklndy vktqapedfk
      181 kvqlqewdka rrvadsamna krtsknvrrl iesqvdldya vylfdyesnr syyqkqepdn
      241 ailkmpmrad yfdylkkidm ndqsllvsnd fstfvnrfef spafqrqllh qankfgykql
      301 dsaylannkk tnlvydiakl raltsnfrfy qykertfade taalskamrd pfvlsemnaa
      361 yeryklgnva yelpntpaaa vfkkiigpsk gkvlivdfwa ewcgpcragi esslalrtky
      421 kdnpdfeyvf vtdsestaav fyedytkknl mtnthripad dylalrelfk fngipryvlv
      481 tadgkiqddn fashnmksef qkyfpekfpi dywk
//
LOCUS       WP_285011161             312 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Lactococcus garvieae].
ACCESSION   WP_285011161
VERSION     WP_285011161.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..312
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34072
     Region          20..311
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mkkkflflif lllafiiidl thfstdwdll silipqfrmp rtlvvliagt alamagfiiq
       61 tvvdnplada gtlgitsgas agavlflfls qwlklsgtwi fmyplfallg glfsfallyh
      121 lalkknvsni qvlliglgit alfqalitla qlsinrfdfq qvavwlsgdi wqtdktfigv
      181 afvlliigll ifsffrkeld lislgqemat slglnvkksk mqfyilallf asigvllvgg
      241 lafigliaph iarelvgfes kkrawatalv smiilllads lsqiiiapss lplgfvvali
      301 gapyyiyliq ki
//
LOCUS       WP_285011343             249 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Pedobacter faecalis].
ACCESSION   WP_285011343
VERSION     WP_285011343.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter faecalis
  ORGANISM  Pedobacter faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Pedobacter faecalis"
                     /db_xref="taxon:3041495"
     Protein         1..249
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27355
     Region          1..246
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mlsksqvsfi kslhqkkyrr englfiiegi ksiseflqsp yrvhsiyflp qfrsalpqla
       61 aniklfevnn aeldkistlq apqgimalvh mqhseelses elrntfslll dgiqdpgnlg
      121 tiirtadwfg fknvicspnt vevynpktiq atmgslcrvn vmyaelenlv rstdlpvfaa
      181 vlngtsiydt kwghegllil gnegqgiseg llnlvskpvt ipklggaesl nvaisaailc
      241 adisrnlhk
//
LOCUS       WP_285011377             501 aa            linear   BCT 25-DEC-2024
DEFINITION  TPM domain-containing protein [Lactococcus garvieae].
ACCESSION   WP_285011377
VERSION     WP_285011377.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Sirpio,S., Allahverdiyeva,Y., Suorsa,M., Paakkarinen,V.,
            Vainonen,J., Battchikova,N. and Aro,E.M.
  TITLE     TLP18.3, a novel thylakoid lumen protein regulating photosystem II
            repair cycle
  JOURNAL   Biochem J 406 (3), 415-425 (2007)
   PUBMED   17576201
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..501
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=56250
     Region          57..>188
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mkikswaeke lknqlklgki iliaitflst icvtsfhvka nssisqnfiy qsersevlsp
       61 sqikelntll nqfsastdkk tseklnsqfa vyitdslnga siedyaqnif ntkqigdvkh
      121 nkgvllvlav ndhkyriqlg egwkdtaltq ssikdyafgg sltsmlkaen yngaiqqivq
      181 rtigiagqdi slvqplqsys ksyaaakeda lkkseelyta gmkmiknliy lmssiisiyv
      241 ifkivkyllg ihresyvssg sqedfceitt nknyskkeka krifeakqll slefafddnl
      301 gnipytvqel aekfaksdye evseenlrkf iselaeeqek nklevarkqk ikslmherlr
      361 nemdlpvsyy eliraftktd ldateenidi fidnflknys llkkkekeqd lkpathalkl
      421 temkpttvfg ddivkqlilf nilttsyqsv hstshrtapt sdhsysstds sdfsssfdss
      481 swsdfggggg fsdgggasgg w
//
LOCUS       WP_285011532             793 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Oligella urethralis].
ACCESSION   WP_285011532
VERSION     WP_285011532.1
KEYWORDS    RefSeq.
SOURCE      Oligella urethralis
  ORGANISM  Oligella urethralis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Oligella.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 793)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 793)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 793)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 793)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Oligella urethralis"
                     /db_xref="taxon:90245"
     Protein         1..793
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=89211
     Region          22..792
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mikkvlaged dhhfseswls piyedlteed aaklrlaiew aekhltgksm fttepcvrha
       61 kgvlhslsll qmdvtsmiag ilaslpsepd pkqaheirqe ilalfglevl nlvqgtrtli
      121 rigaqatlae kkdseqvqdq qemlrkmlla lasdlrivil rlasrlqtlr wysdskrpcp
      181 lilaqqtrdi yaplanrlgi wqikweledl sfrflepaiy rdianklevr rtereelvqr
      241 fidklntnlq qlnihsevtg rakhiysiyn kmrnknlsfe eiydlqairi iteterdcyt
      301 vlslthslwt pvmdefddyi arpkpngyrs lhtvvqdesg rnfevqirtr emhqfaeygm
      361 aahwrykesg akggettass lydrqiswmr qllswrreeg iseqeatqlq eqvlaagdtd
      421 vmltlepaas attkakaatt dtpkskeakp vkaaldkgse apeaapariy vltpqarvie
      481 lpegstpvdf ayrlhtdlgh rcrgarvdgq lvslntplqt gqtveiiaak sggpsrdwln
      541 pqlaylaspr arakvrlwfn aielqkrivs gqelvekelq rlgktatnle hlaeklgfsq
      601 aedlfvavak deyslrnigl aftepeavgp ddevlarlqy shsqsdskng vlvvgvdsll
      661 tqlarcchpv ppdkihgfit rgrgvtihre gcpslkalql kyperiievd wgntadriyp
      721 vniavsasdr pglirditel fakhkmnvaa lntqsrqgvv nllftveikd geqvpkvvna
      781 iaempevhsv nrs
//
LOCUS       WP_285011752             461 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Lactococcus formosensis].
ACCESSION   WP_285011752
VERSION     WP_285011752.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..461
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=51425
     Region          109..449
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mirrkplsik trllltnigf vffaflwiil ifnilinsyi snsasrqlsq vriyqaqvtp
       61 psgsssadle daprgsfnth pvafnindny evqdlekvgn ferdtannia qalknqkvsl
      121 skvknyrldt sgstfyieti rqssglyqvl yvditgiinf tnsvnlflvs valavivils
      181 lavtfvtqrl ikplsilakf atrigqgdft eyqgtfqdse latlahnmnv aarqldnndk
      241 nqklffqnas helrtplmai ksyaegisye vmdpkkaset ilyetdrmse lvedlltlsr
      301 ldslsvhqel vyqdvrlimk diakeqeifa eqkgikittv fdkkavmltc dykalrrais
      361 nlvsnamryv eteivltctk kdgavvisva ndgsgidpet lphiferfyk gaggvhgigl
      421 aivqtiveqh qgqvsvtsde qqtiftmtfa ktpkkalekt a
//
LOCUS       WP_285011820             274 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Oligella urethralis].
ACCESSION   WP_285011820
VERSION     WP_285011820.1
KEYWORDS    RefSeq.
SOURCE      Oligella urethralis
  ORGANISM  Oligella urethralis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Oligella.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616068
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Oligella urethralis"
                     /db_xref="taxon:90245"
     Protein         1..274
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31576
     Region          34..176
                     /region_name="Methyltransf_32"
                     /note="Methyltransferase domain; pfam13679"
                     /db_xref="CDD:379330"
ORIGIN      
        1 mslipeikpq qslellkalh iltrdgkinq dsrrklkqvy hlyhfieplm lkvleeqkql
       61 vlvdhgagks ylgfilydll lknhpeahvy giefreqlvk sseelanklg fsdgmsfkam
      121 rveeamhstd ipakvditta lhacdtatdd airfalerqs kyivlvlccq aelaahlrqh
      181 knkaikhnsl aeiwrhpiht refgshltnv lrclqlearg yqvtvtelvg wehsmkneli
      241 varkvakykn sardrqleil kefgleemre rfay
//
LOCUS       WP_285011826             309 aa            linear   BCT 25-DEC-2024
DEFINITION  DHH family phosphoesterase [Lactococcus formosensis].
ACCESSION   WP_285011826
VERSION     WP_285011826.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..309
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=34689
     Region          2..296
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mkeiltkike ydtilihrhk npdpdalgsq cglrailran fpekkiyavg ydeptltyla
       61 kmdqvelesg tkylsiicdt antpridddr wmqadyviki dhhpnddayg dlrlvepdrs
      121 saseiitdfa lnhdlalnee asrllyggiv gdtgrflypa tsaqtlylas klaefdfdrp
      181 algremtsfd mkvarlqgyv yenleiseng agrvllskev lekfnlrdae tssivgtpgs
      241 irdvqswaif veqadghyrv rmrsktvpin eiakkhdggg halasgansy sleeneqiwq
      301 elqdnlekk
//
LOCUS       WP_285011876             217 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Lactococcus formosensis].
ACCESSION   WP_285011876
VERSION     WP_285011876.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..217
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24353
     Region          2..208
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mkfkaivfdm dgvlvdserf hskvldnffv esgidashlt pkdfvgsvlk dmwpkvlrde
       61 stearaaqvh qdfldydaqf pipykelllp gvtdalktfs ekgykmavas ssrrheiaev
      121 ldthdlrqyf efflsgqdef eqskpnpaiy laameklgve psetliieds hygimagkaa
      181 gatvwavkdn yfginqeqad rfietltdak nllaese
//
LOCUS       WP_285009359             312 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Lactococcus formosensis].
ACCESSION   WP_285009359
VERSION     WP_285009359.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..312
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34015
     Region          20..311
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mkkkflflvl lliafiiidl thfstdwnll silipqfrmp rtlvvliagt alamagfiiq
       61 tvvdnplada gtlgitsgas agavlflfis qwlklsgtwi fmyplfallg avfsfallyh
      121 lalrknvsni qvlliglgit alfqalitla qlsinrfdfq qvavwlsgdi wqtdkafigl
      181 tfvlliigll ffslirkeld llslgqkmat slglnvkksk mqfyilallf vsigvllvgg
      241 lafigliaph iarelvgfes kkralttalv smiilllads lsqiiiapss lplgfvvali
      301 gapyyiyliq ki
//
LOCUS       WP_285011959             372 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Lactococcus formosensis].
ACCESSION   WP_285011959
VERSION     WP_285011959.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..372
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41408
     Region          14..359
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mkkiaiiggg iigmtlanyl dtekfditvf dsgnnqatga sagiispwls krrnkqwyal
       61 akdgaaffeq lvkdlsldet iyekcgtlfv kspealqele qlalerrata peigevrhlt
      121 teettamlpl lkpveslyis ggarldgkay lqhlrkraqt rgvrvvseea hvkkenakwr
      181 vtsvqeevev evdelvltpg palktlldql gytakvspqk gqllsfetnf etekwpvafl
      241 egeadlipfq ngrlllgath eneagwdlep tqeafeqltk gvqtflkedy fadttysyrv
      301 gtraytddfa pffgpveqee glsvasglgs sglttgpyia yllaqhlnan hsewemshyq
      361 kemnlyvnkk ee
//
LOCUS       WP_285011970             616 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Lactococcus formosensis].
ACCESSION   WP_285011970
VERSION     WP_285011970.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..616
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=72526
     Region          7..613
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mkkrevlley lkknrkqnfi sskelskilg vtdrsiryyv kqlneeepkl ieasregyry
       61 sgqqevgdnt ndainsrrfs ilqlllknne kgvslfdlae klwvseatir qdigilqkmi
      121 sskglrisqh dfyyylkgsy dekrqlimsl irqqgnsiqs leeemqrflg eislsemtev
      181 crsifkshrf hvnnyffqnf ilhlifaihq qsvlkqqnfa spsfemieei sqwlfkhyni
      241 vittedkiel allcdgekgh pesqidayva qevseslqha lkeisevfli dftdkkfltr
      301 llihtqnlyn rikdrkvkrn lsaieikvry pilfdiavyl ssliardlei eiaedeiafl
      361 alhlgsflde qeeneykirt qlkisgyldr enrvlgclek rfgdellfvk ngfndeknve
      421 lilssdkiie snpqyetvqi heflmekdfi lireaidrvk nkryqyflrs flpeiiqena
      481 fihlkgeisk tvafekigqw ffkngfaeke faeklfereg lsstsfssgi alphsiryeg
      541 rktgilifkp ekplhwdnqi vqlilsftis pddskdfnki fphlieilte eyhveylrrs
      601 enrkeflerm iellsv
//
LOCUS       WP_285011976             372 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lactococcus formosensis].
ACCESSION   WP_285011976
VERSION     WP_285011976.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..372
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43330
     Region          66..368
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mwieelengk fkycerytdv kgkirkvtvt leknstraqn eaarllynki eakkekqaqe
       61 ndtssitfwe iqdqvleltk etvksrtnas resvkkkire hvtkdtllsd itstyildvl
      121 eklyykknys fpyiisikag fnlvleyava kgyiqtnpiq kvkikrkiet leqreakknk
      181 yleqdelkdi ikqmrvihkt taliiefmal tglrysecva iqeknikgni lhvngswdni
      241 tykkittknl ysdrkivltq rcldiideql diskdyykgm kenyifvnrn gtpvlistti
      301 drlkkldtnk kitthifrht hialltelgi plkaimervg hsnpnttlai yshvtekmsq
      361 niieklekid lq
//
LOCUS       WP_285012023             231 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lactobacillus iners].
ACCESSION   WP_285012023
VERSION     WP_285012023.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443800
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..231
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26426
     Region          1..69
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          118..230
                     /region_name="Peptidase_S24"
                     /note="Peptidase S24-like; pfam00717"
                     /db_xref="CDD:425835"
     Site            order(156,193)
                     /site_type="active"
                     /note="Catalytic site [active]"
                     /db_xref="CDD:119397"
ORIGIN      
        1 mkeskiifgq midyfrkqnn ltmeelgqkl gkatssisrw vsgerypkie eieqiaiffn
       61 tdiytlifgf nynensksni ltvynqltdi rkhkvysyaq qqldeqnsnl nekssiyvvg
      121 tsaagepiey gdfdsemiqt dvpakadkai hikgdsmepk iasnsiifyh eqptleigei
      181 gifeingsav tckkyyvdye skkiilksin pkyepmyfar dqvrilgkvv f
//
LOCUS       WP_285012143             440 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Lactococcus
            formosensis].
ACCESSION   WP_285012143
VERSION     WP_285012143.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..440
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48113
     Region          1..435
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mekydyiivg agpggnalay alkeqgaavl iaerdkwggt cpnygcdptk immalveaky
       61 raanlvsagl hgnlsidwqe mlarkraysd aipssteqgl knagietvyg sasfqteghl
      121 dvggkayfad nyilatgarp rvldipgney lltsndflel eelpkrlvfl gsgyvslela
      181 qianaagsev silthgalki rgfaddfats yikqlqkegi tftdnfsper leqtesgivi
      241 isednrkvta dgvisavgri pniedlnlda vgvkttpkgi lvneflqtnn pniyaigdal
      301 dkkqpkltpv sgfearylar yftqdgrieg iqypaiptvi fgssklaqig qtqildkene
      361 kkidmtdwyt ykriadplsk invivndkne ilgatllstv aeelvnilnf cinqainldk
      421 fqnmimaypt iasdlfylyd
//
LOCUS       WP_285012149             199 aa            linear   BCT 25-DEC-2024
DEFINITION  KdsC family phosphatase [Oligella urethralis].
ACCESSION   WP_285012149
VERSION     WP_285012149.1
KEYWORDS    RefSeq.
SOURCE      Oligella urethralis
  ORGANISM  Oligella urethralis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Oligella.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Oligella urethralis"
                     /db_xref="taxon:90245"
     Protein         1..199
                     /product="KdsC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=21405
     Region          22..189
                     /region_name="KdsC"
                     /note="3-deoxy-D-manno-octulosonate 8-phosphate
                     phosphatase KdsC and related HAD superfamily phosphatases
                     [Cell wall/membrane/envelope biogenesis, General function
                     prediction only]; COG1778"
                     /db_xref="CDD:441384"
ORIGIN      
        1 mkkphiphpv eslvlskipa avkeraslie lvifdvdgvl tdgglyytan genqkrfhal
       61 dghglkmlkq sgievalitg rqseittrrs aelgithllq nvrnkadalv elsktlaiel
      121 ervafigddv idlpamrrvg lalsvpnapv yvqqaadwvs qlagghgaar ehcdmilasq
      181 gllgpllthe hpiigeviq
//
LOCUS       WP_285012201             520 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Lactococcus formosensis].
ACCESSION   WP_285012201
VERSION     WP_285012201.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..520
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=58983
     Region          <296..520
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mkkiklkniv istiiylvat villvflniq ilktdtnrvl htidttkill aenpnsalpn
       61 kfqylpagth nqetakiedg adyaqsvsrh tieitspirv dgvitgylha edsrtspwft
      121 nlmvggfali vylactsyvf vharrnylft qdiiakikni erspltqsyl msenddkvtl
      181 alnslgeyiq nqilshsekk eniyefielf qfpifiynak gkirktnaaf knefadthnl
      241 difspyadfl sflvdkmlnp ttqeksfyfe ninayyqvri splpdldnrf lvtllditaf
      301 krtlnahnel ianvshelkt pltsikgfae llkddtlsea drhefshiis kessrlialv
      361 qdtllltkqn ihidkkkinl salveeilnt sqplldeknl slqtdivpis qvtnrqmvhs
      421 ifenlienai kytdehgkiy vglhqnkkkv vftvtdngpg lteieksrif erfyrvdesr
      481 tqvtgtglgl sivdknvrel qghievisvp gkgttfsvtl
//
LOCUS       WP_285012654             281 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Oligella urethralis].
ACCESSION   WP_285012654
VERSION     WP_285012654.1
KEYWORDS    RefSeq.
SOURCE      Oligella urethralis
  ORGANISM  Oligella urethralis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Oligella.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Oligella urethralis"
                     /db_xref="taxon:90245"
     Protein         1..281
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31884
     Region          7..239
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mklnqsfest eryiatddlr lavnaalsle rpllikgepg tgktmlaeev aaflqrpllq
       61 whiksttkaq qglyeydavs rlrdsqlgde rvkdianyir pgvlwqafes etpavvlide
      121 idkadiefpn dllreldqme fhvyetarti rakhrplvii tsnnekdlpd aflrrcffhy
      181 iefpdsetlr qivavhypnv dqdilnsamq sffelrempg lkkkpstsef ldwlallsas
      241 ninpqsveng nlplagalik neqdlslier lvamatgqgr r
//
LOCUS       WP_285012688              68 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lactococcus
            formosensis].
ACCESSION   WP_285012688
VERSION     WP_285012688.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 68)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..68
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7443
     Region          2..67
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 maikvhidrl lverqmsvte lsekvgitma nisilkngka kairfstleg lcrvlecqpg
       61 dlleyieg
//
LOCUS       WP_285012320             304 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Lactococcus formosensis].
ACCESSION   WP_285012320
VERSION     WP_285012320.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus formosensis
  ORGANISM  Lactococcus formosensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Lactococcus formosensis"
                     /db_xref="taxon:1281486"
     Protein         1..304
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35547
     Region          44..234
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkipapllsl akkillvdvr gnykrkqhqk llnqlkakny eshkisillp iynaehslek
       61 cldsilqqtf sdfeiicvnd astdntkqii esysqkdtri siidkaqnqg ssfarrdala
      121 qakgsyilci dsddwieptm ledlylfaqq nssydmvycd yyknnlvtya ptileknlpf
      181 erikkrsfsf gnmlwnrlik kdifekiifh qesmgedvyi stqlyyfsnk iaylckplyh
      241 ynqfsnpdsi scrpsldnil dmeanyhhmq vflkdrfgyq vafekafskk ekmitkakkh
      301 hltq
//
LOCUS       WP_285012874             220 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial [Oligella
            urethralis].
ACCESSION   WP_285012874
VERSION     WP_285012874.1
KEYWORDS    RefSeq.
SOURCE      Oligella urethralis
  ORGANISM  Oligella urethralis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Oligella.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Oligella urethralis"
                     /db_xref="taxon:90245"
     Protein         1..>220
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          3..>220
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mqlrkafkfe impngeqirr ikqfcgcsrf vfnralawqn eqyeqdnsvk fsytkianll
       61 pvwkkelpwl kdchsqvlqq slkdlesafk nffqkradfp kfkkkglkes frfpqgckle
      121 qqnnrlylpk igwvryrnsr avvgeiknvt vsqkcgrffi siqtefeyei pthrggeigi
      181 dmgvahfatl ssgeyfepln afktykgkla klqrrlknkv
//
LOCUS       WP_285012919             315 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Oligella urethralis].
ACCESSION   WP_285012919
VERSION     WP_285012919.1
KEYWORDS    RefSeq.
SOURCE      Oligella urethralis
  ORGANISM  Oligella urethralis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Oligella.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 315)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Oligella urethralis"
                     /db_xref="taxon:90245"
     Protein         1..315
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=35982
     Region          41..299
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mesgtdfsta napegvaevv avlvavtels arvltvdsgc alpygpftpv hrslqsgvra
       61 wvqeqtrqpm gyveqlytfv dttrsrasgh pviyisylgl vreaaesllq sqakwldwyl
      121 yfpwedhrqg rpamidelfi prfqtwieaa tdeqnrqqrq arvamcwgln gnawldeqvl
      181 sryelmyevg lipespyreq slaaasvgrf mkhdhrrvla taisrlraki kyrpvifelm
      241 preftllqlq ecietlagme lhkqnfrrli qhqelleatg qsivlgrgrp aqryrfkdtv
      301 llesilsgnk lplsr
//
LOCUS       WP_285013137             393 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lactococcus garvieae].
ACCESSION   WP_285013137
VERSION     WP_285013137.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..393
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=45141
     Region          70..386
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mnikeiikkd gtkvyrasvy lgvdtitgkq vrttataktr kmcetkanqa inkfnrngst
       61 vakekvefnn fkelsdywfd sykltvkens vrlaksvlkv yivpfigsyk ldkitsvllq
      121 sqvnkwakna ntakitngkr ergnckdfkl ilnfikrild yalqlgaiet npalqvrvpk
      181 lkdrtsqkik yfdndelkkf lkyldtlent eenkrkitly klllstglrv gealalswsd
      241 idfkecyvkv hktivqqsrn iqespktkds nrtvfldnat itmlkawrnr qnkgtillkd
      301 slifpykgkv siyenerhsl lqhfkkagvp nigfhgfrht hasllmnndv npkeiqhrlg
      361 hadyaitmnt yshlakhkek dtaekfgnil kal
//
LOCUS       WP_285013160             130 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Oligella urethralis].
ACCESSION   WP_285013160
VERSION     WP_285013160.1
KEYWORDS    RefSeq.
SOURCE      Oligella urethralis
  ORGANISM  Oligella urethralis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Oligella.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Oligella urethralis"
                     /db_xref="taxon:90245"
     Protein         <1..130
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <11..118
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 niyanikein lirvvgnlie narrygrsdn gelnisvkly pkgqsilidv adqgvgvnpk
       61 eiarlmrpfa rgntarsnvn gaglglaick rllqsaggti sllqnephgl lcrielpkps
      121 hrnilldkns
//
LOCUS       WP_285013186             143 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein, partial [Oligella
            urethralis].
ACCESSION   WP_285013186
VERSION     WP_285013186.1
KEYWORDS    RefSeq.
SOURCE      Oligella urethralis
  ORGANISM  Oligella urethralis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Oligella.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Oligella urethralis"
                     /db_xref="taxon:90245"
     Protein         <1..143
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
     Region          <2..126
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 slnnipinra kasealrqvl rmgtkrikeg rspvlfpegt rtpvgtrgry kpggvrlamh
       61 aqcdiipvah nagkvwprna fikkpgcvtl sfgpaispgd rsseeimaav eqwiesemir
      121 lnpedypsqd padtpyaqsk kkr
//
LOCUS       WP_285013258             433 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Lactobacillus crispatus].
ACCESSION   WP_285013258
VERSION     WP_285013258.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 433)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 433)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 433)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 433)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..433
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49669
     Region          1..409
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 mlieftvkny asfrerttls aetgnrlrkl ketntfsskn psllkslllf gpngsgksql
       61 iqalqtmegi vtrptqavtd klnyypflfd ekskiedtyf evklelknki ydysfsynre
      121 sitsealtli sgnkekeifs rngndiqvsn klledsipkl rdnslflyla qsendadcia
      181 iykwfvndli figsgypvni pdellnlmed eylkkemisf lsfadfnisd irirevptnp
      241 lnpqlqkive nlnidypktt kelytvhkiy hqngvinsge lpltqesvgt rrlfyivlam
      301 mlaqmngnek tividefdds lhvelaaalv rifnstenln qfiitthdiq lldsdlridq
      361 iylldkdfhg isdlksifdf edarnkgrhd isfakrylqg rfgavpvidv dglldvlqmi
      421 hekygdehgk nkk
//
LOCUS       WP_285013378             127 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase, partial [Oligella urethralis].
ACCESSION   WP_285013378
VERSION     WP_285013378.1
KEYWORDS    RefSeq.
SOURCE      Oligella urethralis
  ORGANISM  Oligella urethralis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Oligella.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Oligella urethralis"
                     /db_xref="taxon:90245"
     Protein         1..>127
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
     Region          4..>127
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 msilnrlisq laleqigerr flgrstdifr sgrvfggqvl gqalmaasyt tpvgrlahsm
       61 hgyfvrpada tkaieyavev irdggsfsvr rvtasqegkf iftlscsyqs velgfehqla
      121 mpaappp
//
LOCUS       WP_285013523             227 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein, partial [Oligella urethralis].
ACCESSION   WP_285013523
VERSION     WP_285013523.1
KEYWORDS    RefSeq.
SOURCE      Oligella urethralis
  ORGANISM  Oligella urethralis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Oligella.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Oligella urethralis"
                     /db_xref="taxon:90245"
     Protein         <1..227
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
     Region          1..213
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 itsalsgsrg gwlglpiilv vifvayyaif slrakllvll cvvlggffll snphigvkqr
       61 iaeayheial fqdgtvqtsv gyrlemwrga iklaqekplf gwgdegyqeg mqqlretnqi
      121 rgradlftha hnefidrlak qgitgliali llyqvplwtf asakrtahlp travamagil
      181 lslcyfdfgl tqaflrhnng vmvyvcymmv iaayfkvmrf eqakiss
//
LOCUS       WP_285014077             554 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Pauljensenia sp. UMB10120].
ACCESSION   WP_285014077
VERSION     WP_285014077.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB10120
  ORGANISM  Pauljensenia sp. UMB10120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Pauljensenia sp. UMB10120"
                     /db_xref="taxon:3046356"
     Protein         1..554
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=59889
     Region          111..544
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 msdhpaffgs deepsgipad llpyleaade pseadrqadq arqeaeeaad radreraeal
       61 ralvenslll gpdpsilaei esdededgtp sdeedherml ddaqqaaqer aevariyesi
      121 varapehkvq pslervsrvm dilddphtsy psvhitgtng ktttarmmda llgalglrtg
      181 rftsphlldv rericldgep ishrafiday hdvqpyidmv dhssieqggp tlsffevftv
      241 malaafadyp vdaavvevgm ggtwdstnvv dgqvgvimpi dvdhqkwlgk tvtdiaheka
      301 giikpgqitv vahqrdevle ilreradqvg arllvegtdf evvtreravg gqlmslrtph
      361 amytdiflpl hgehqaynaa aalagveafi geraldaqvv eqafgavtsp grlqvvrrsp
      421 miivdgahnp agartvraai ddlglahvvg vfaamadkdv dtmlgevepv mdelivtqmd
      481 seramelddv qaiaedvfdd trvsripdia eaiaeaatrv etraepgenv avivfgsivl
      541 agqatqivsq angr
//
LOCUS       WP_285014232             236 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Pauljensenia sp. UMB10120].
ACCESSION   WP_285014232
VERSION     WP_285014232.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB10120
  ORGANISM  Pauljensenia sp. UMB10120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Pauljensenia sp. UMB10120"
                     /db_xref="taxon:3046356"
     Protein         1..236
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=25061
     Region          <1..201
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mkiviagags vgrfvalell dhghevtlid hnpdqmrvat vadadwvlad acspdvlada
       61 gvretdvlva atgddkanlv isllaktefg vprvvarinh prnewlfnea wgvdvpvstp
      121 rimtalveea vsegapiplf tfnkanvamy aivlpedspl vgerigqvdf pagtvlaall
      181 rdqipmnpqp ddvfesgdel lmlvpekrgk hlehlgtlvn gvvpetgqad apttta
//
LOCUS       WP_285014246             265 aa            linear   BCT 25-DEC-2024
DEFINITION  TPM domain-containing protein [Lactococcus garvieae].
ACCESSION   WP_285014246
VERSION     WP_285014246.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Sirpio,S., Allahverdiyeva,Y., Suorsa,M., Paakkarinen,V.,
            Vainonen,J., Battchikova,N. and Aro,E.M.
  TITLE     TLP18.3, a novel thylakoid lumen protein regulating photosystem II
            repair cycle
  JOURNAL   Biochem J 406 (3), 415-425 (2007)
   PUBMED   17576201
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..265
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29001
     Region          1..>201
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mkkkrilltl lftvitlfal fafpkksfaq qvgiddqagl ltgptqsleq eaqllanqtk
       61 agifvvttmd ntespkdfav nylaqkvgqg nngivlminm sqrklyiwat gnlkhyitss
      121 riesildvvq pqlsdgnyqq aiesfyaqvt hyyeqgipgg rkytvdpqtg avtfhrsfrp
      181 ayiliavila lisagafvii lvsryqlkmg ahwnygyqen gklnlskqsd tlvnsfittr
      241 riprnnnssg ggfsggggsg ggrsf
//
LOCUS       WP_285014420             889 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Pauljensenia sp. UMB10120].
ACCESSION   WP_285014420
VERSION     WP_285014420.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB10120
  ORGANISM  Pauljensenia sp. UMB10120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 889)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 889)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..889
                     /organism="Pauljensenia sp. UMB10120"
                     /db_xref="taxon:3046356"
     Protein         1..889
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=98657
     Region          20..869
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 msaplnelld dledaghldd pdelvrafqs waastgrply phqeqsllei vmgnhviaat
       61 ptgsgksmia laahfvslah sgrsyytapl kalvsekffd lvelfgahnv gmvtgdvsln
      121 plapivccta eilanqslre gdaldadmii mdefhfyadp ergwawqvpl leltapqfia
      181 lsatlgdttr fqeqwkertg rdvalvdnaq rpvplefdyv vedvrtcver llkegrwpvy
      241 ivhfsqndav staaafdras lisddqkkqi srilrtvsfa rgfgqqlrgl laqgigvhha
      301 gmlpryrrlv erltqqglla ivcgtdtlgv ginvpirtvl itslvkfdgr rmrhlsaref
      361 hqiagragra gydtvgfvrv lapeheveaa rekarlsaaq eaarqardea aakkaakksa
      421 krstkapakg qiswtrstfe rlrdaeperl qshfaishsm vlnvlagqrh dpaahliela
      481 rtnddpprds nphmraladi yrslrqagvi dhvsteqaes dgmarvrlvr dlpddfalnq
      541 plspfalaal dlldaqspty aldvvsvves vledprplla aqqrmarska maamkaegle
      601 ydermealae vtwpqpladl ledafrtyvq tnpwvgdqhi spksvvrdmi ehamtftqlv
      661 srydvarseg vilryltday rslrqvlpdr vvteevaaim ewlshlirai dsslldewes
      721 lasgqrreeg eddasgqeva fgasedgtva fsanrhamrt avlralferv elmsrddvda
      781 larldswcgw deerwdhale rywaeydwig idqnarsgal vnlnenpsea ellavgvpde
      841 lvgsnlwlve qtlddpngdg dwrivavvdv datdeanrvv lhivdvgpr
//
LOCUS       WP_285014674             918 aa            linear   BCT 25-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Lactococcus garvieae].
ACCESSION   WP_285014674
VERSION     WP_285014674.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 918)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 918)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 918)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 918)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..918
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..918
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=100576
     Region          2..914
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mefykkakee viaeflvdpk tgltdeqvlk qrelygenkl peeeedshlk lflksfkepi
       61 vivllgavvl sfmssyhafh fqndskhgme amyeaiaili lilinaflgf yqemsarksl
      121 nalkemnnry vtvlrngqfe kifstelvag divkaslgdf veadlrwiet nelqvieshl
      181 tgeadaiskh tevihettel gdrhnmgfsg ssvsggqglg ivvavgehte lgkiakliqa
      241 venrtsplqn tvhkltktlm qvsagivvft lvvgiiqage lsiasitsvl stsialavas
      301 ipdalpavls ivltigaakm aknkgliksl nsvetlgsts yicsdktgtl tknemtvthf
      361 ytngqyyevs glgytpegei rslsegeqes sysafiagal lcnesalkev egkfvpfgnp
      421 teialtvlgq kagrtktqll eshelsrtlp ftsdrktmsv ivkkgdnyll yikgapdvlv
      481 eksrallidg elnteesekq kfittvndya nealrtlavg yrilskeeae hgqledlekd
      541 iiltgvagii dpareevkas vktlqdasve vvmitgdhen taraiaynlg ivkskeakvi
      601 kgieieemtd eelyavvktt nvyarvspeh kqrivkqlqq hgevvgmtgd gvndapalra
      661 adigiamgia gtevtkdsad lillddkftt iektvengrt iyaniknfir helttnvaev
      721 lslilgllff tvsignvdyt tptltalmvl wvnmvsdavp sfalgydvae sdimnekprd
      781 pkesvlanyt wsrvlirgti mglmvfvafv waakqgmssn eaqtvafltl vygqlwhvfd
      841 arssqtlfrr npfgnprlvl avafagissf lvtiipffnv vmgtaplsws vyllvffvpa
      901 lptfilsgik eifkvkiw
//
LOCUS       WP_285014747             326 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Pauljensenia sp. UMB10120].
ACCESSION   WP_285014747
VERSION     WP_285014747.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB10120
  ORGANISM  Pauljensenia sp. UMB10120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Pauljensenia sp. UMB10120"
                     /db_xref="taxon:3046356"
     Protein         1..326
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34810
     Region          <68..141
                     /region_name="PLN02217"
                     /note="probable pectinesterase/pectinesterase inhibitor"
                     /db_xref="CDD:215130"
     Region          136..237
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mnehenaaes vrqwplwhwf apaetlrqev pswvtippip qrlavaandl vgaarrrlql
       61 mtsvvcdtls aagdssgsqn gsddsaasps agpqspssit vtssalaqps tdagtptqpa
      121 asahtpatla astatpdcaa rpvaigipgi wesrhyldpw araladagwd arilegvram
      181 rrpidtiaqm aerylarenl thvllyshsk gglvakaima gpegwrirhl itfatpfdga
      241 piarllpips lrelspgspa irplasrtdl naritqieat wdenvppttl pgahrrvilp
      301 iyghgqmles rgaartlvql aepyrc
//
LOCUS       WP_285014759             957 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Lactococcus garvieae].
ACCESSION   WP_285014759
VERSION     WP_285014759.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..957
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..957
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=99678
     Region          <65..945
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 meriktgrve hyitilnwfy mllaslflvh chlfltgfll fgtlsaeasi tqqtdgsgit
       61 wnlitagndi ntlattalpg atlyikaand ltlgvtavlp lnltlvfdmg ghalyntgaa
      121 vitpsvgnti tfqnerivst gttnsttvps plgigtvtgv ynyyyglfsa tnisgvsity
      181 knviqdlgti ttwgaggqpf ynigssvnfs gtnyfnynsg qefmegtgin vldgtttikh
      241 ssggnaplwa qsaasinvaa gatldftgss tgrgfiyldn tptftinnng tlklnmsgas
      301 snnfysntgm ssitmnygan ssttitapgf fdynatggaf kttigqgasf dystgntsna
      361 flgtlaatds ftlnsakhvr lntnktsgss ilgtdasamp fvlnasspsa yaingynsag
      421 vssllaspts gafgvtgtfh snladlsklt gqkiptasei ttyqnsaqle fnlvspaqan
      481 fsyawaadvp gqnggagtll gqlparvseq gtvggaltap tlsaapkgyy isgykapngt
      541 iyttlaaala tvnnvfgtts ntttpdiymp stndfqvils aqeqtfyiny gyaftnfgnv
      601 ppfpanaytq kgltgaplti sglgaaptgy hysavlnnta sawidqtnpe tggantptpy
      661 yasislaltt aitqqnggmy fgtsslstpp tinnqgafdn nvmvmltana eianytygwa
      721 nitpgyngna gqiygnlpsq atskggfgdt iardtsgins pgntyqtfva pptdkalsgy
      781 svavrapngi tytsdpnava sstvvktttp lttatqantf kegaaannfv itytplankl
      841 swhytydssi snppsapadi vqtgvltgtp ltdpkatapn gyfiegyqyp gdtkiyrtia
      901 elqtahfsgt gditinilla knfvlpytgg sgqfgiilas atlaflalaf yifkkkd
//
LOCUS       WP_285014797             551 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 32 protein [Pauljensenia sp. UMB10120].
ACCESSION   WP_285014797
VERSION     WP_285014797.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB10120
  ORGANISM  Pauljensenia sp. UMB10120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Pauljensenia sp. UMB10120"
                     /db_xref="taxon:3046356"
     Protein         1..551
                     /product="glycoside hydrolase family 32 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=61193
     Region          68..537
                     /region_name="SacC"
                     /note="Sucrose-6-phosphate hydrolase SacC, GH32 family
                     [Carbohydrate transport and metabolism]; COG1621"
                     /db_xref="CDD:441228"
ORIGIN      
        1 mstptdshni eptnegaqip eqedhlnagn thalaheqhp lphapltlth eqaleraera
       61 sdqlerarnd rwyptfhiaa ragwindpng lcyfdgryha fyqhhpygsa wgpmhwghvs
      121 sadlvtwqre rialapsipa dqdgvfsgsa vegpdgllyv fytgnrwldg hadgrneqtq
      181 clavsedglt fhkegviida pglpnfrdpk vwrqgdtwcm vlgatseaar gqvhlytspd
      241 lrtwsfdrvl fedpdphvym lecpdlfplg dhwvlcygpm tnarasgyam rnghnagyvv
      301 gdwtlgsdfh pltdyalsdw gsnyyaqqtf eapdgrrial awmgafmlpl apqysdnwsg
      361 qftvpreltl tedlklaata lpelnrlecg rdtlgtfvld anrdrllvdd gdafaidmvv
      421 dlsattseqv glrvnetsdg sytwvayddl arrivvdrrt kagtdrgyrs apidmdegds
      481 hlrmtvlvdr gsvevfagrn tatlsacafp segkrrtsls sisgiisvee ltvrhfdsiy
      541 sdngsnprtm g
//
LOCUS       WP_285014846             268 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Pauljensenia sp. UMB10120].
ACCESSION   WP_285014846
VERSION     WP_285014846.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB10120
  ORGANISM  Pauljensenia sp. UMB10120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Pauljensenia sp. UMB10120"
                     /db_xref="taxon:3046356"
     Protein         1..268
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28887
     Region          94..250
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 maksessrdt rtkaremrea qlksekrtrv iiigvvvliv vavvaavaav mltyrpkgsa
       61 lpdeeaaall gpyadsspvv yshngiedpd pnlptltiyf dyschvcaqv dtaggeeivq
      121 aatdgkfnia yqpvttvgmd yakpattasl ivaqkdpehw vafhhalmgf fneqwtsgdt
      181 rvvksmdqsi dkvaelarsv gvpdevvstf danavqtyla nstkvwgekk fagrgdsygt
      241 peyvkdgtkv ipftlenfas diisgmae
//
LOCUS       WP_285015239             160 aa            linear   BCT 25-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Pauljensenia sp. UMB10120].
ACCESSION   WP_285015239
VERSION     WP_285015239.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB10120
  ORGANISM  Pauljensenia sp. UMB10120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Pauljensenia sp. UMB10120"
                     /db_xref="taxon:3046356"
     Protein         1..160
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=16258
     Region          25..>117
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 mefahtdsdd qshsrrtpal srarladiac vflggmigtl vrasldhiaa ahpassalvl
       61 awstiacnla galilgfcag sgrwlsarvn lligtgmcga lttystmmlg avtfvhsppl
      121 dtttgamgri lagsaitlgl lvlgvgvaaa gwwlgkkarp
//
LOCUS       WP_285015349             539 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Lactobacillus iners].
ACCESSION   WP_285015349
VERSION     WP_285015349.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 539)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..539
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=62726
     Region          6..459
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(20,22,24,28)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(59,62,99,102,143,162,166,198,240,401)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(198,240,316)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          466..535
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; pfam16657"
                     /db_xref="CDD:435493"
ORIGIN      
        1 mtpwwkkavi yqiypksfqd sngdgigdlp giitrldyls klgidaiwls pvyqspgidn
       61 gydisdyqai dpqygtmddm dnlileakkr nikiimdlvv nhtsdqhawf vearknkenq
      121 yrdyyiwrdp vdghepnglq safsgsawqy dettkqyylh ffakqqpdln wsnsivrdki
      181 yqmmnywidk giggfrmdvi eligkdpdkm vrengkmlhp ylqemnqktf gqsdlltvge
      241 twnatpkiae dysdparhel smvfqfenqt ldqkdgcskw dlkpidlvel kkilvkwqte
      301 ldfkhawnsl fwenhdiprv isrwgndqky rvvcakmfai vlhlmhgtpy ifngeeigmt
      361 nspvkninev ediesinmyn erldagydkd ellhainvkg rdnartpmqw sdalnagfts
      421 gkpwlrvnsn ytdinvkqcl adpdsifyty qklielrhhn qivvdgdfql ieetdaqila
      481 yyrilgdqkw lvvanltdke kpfncheqyq kvlvenyttp snlqniilkp yqafvvtia
//
LOCUS       WP_285015376             520 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Pauljensenia sp. UMB10120].
ACCESSION   WP_285015376
VERSION     WP_285015376.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB10120
  ORGANISM  Pauljensenia sp. UMB10120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Pauljensenia sp. UMB10120"
                     /db_xref="taxon:3046356"
     Protein         1..520
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54565
     Region          162..516
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mtrppshdmp hadtphpdaa hthtepnpvt ptsmskrlrg trkqaharqr prrsprpesg
       61 rpatltrskl vgriiaaaal vtflfvqlpg ldasgsrmfg ifiaaialwv teaiplaata
      121 vgvilmevll isnqavlsvs eeapaataif gslanpviil fmggfmladg aakynvdkal
      181 salmlkpflr narmtvmgvm mitalmsmfm sntattatmf avmmpvital pkgrartgla
      241 lsvpvaanvg gmgtpvgtpp naialgalqn hgihvtfidw mlaavplmlv vlviawlfiv
      301 wryipsdvkf dvdtsatfer tpkaimfyvv amitiglwmt eslhhissnt vgfipvaglm
      361 ilgvmggddv kkldwpvlwl vaggialgag vgatgldewl igsiswqaip malllltlaa
      421 vgwvtsnvis hsasanllip mgmglaatvs tspsqiavvl algcslgmcl pistppnaia
      481 ystgttptpe mvrvgivvgi sgvlllafva pltwrvlgvl
//
LOCUS       WP_285015542             231 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lactobacillus iners].
ACCESSION   WP_285015542
VERSION     WP_285015542.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443800
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..231
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26503
     Region          1..69
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          118..230
                     /region_name="Peptidase_S24"
                     /note="Peptidase S24-like; pfam00717"
                     /db_xref="CDD:425835"
     Site            order(156,193)
                     /site_type="active"
                     /note="Catalytic site [active]"
                     /db_xref="CDD:119397"
ORIGIN      
        1 mkeskiifgq midyfrkqnn ltmeelgqkl gkatssisrw vsgerypkie eieqiaiffn
       61 tdiytlifgf nynensksni ltvynqltdi rkhkvysyah qqldeqnsnl nkkrsiyvvg
      121 tsaagepiey gdfdsemiqt dvpakadkai hikgdsmepk iasnsiifyh eqptleigei
      181 gifeingsav tckkyyvdye skkiilksin pkyepmyfar dqvrilgkvv f
//
LOCUS       WP_285015849             282 aa            linear   BCT 25-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Pauljensenia sp.
            UMB10120].
ACCESSION   WP_285015849
VERSION     WP_285015849.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB10120
  ORGANISM  Pauljensenia sp. UMB10120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Pauljensenia sp. UMB10120"
                     /db_xref="taxon:3046356"
     Protein         1..282
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29991
     Region          11..278
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mprsssslph ldelvelctg krlaaltgag mstdsglpdy rgtgssgtpt vdidlflsdp
       61 kwqrwvwern qvtwralqdl patrgheala rmeragilhg vatqnvdgld ekagihqlal
      121 lhgsfltvdc mqcaarypre wldgelraan pnlvddpdpt hvailaqvdp egatasaitl
      181 vscpqcggil kpnvvffgem lpsdqmdkgl tfaaqcdvll vvgtsvkvst avwiahqais
      241 sgadlvvinr gpcdldhhpa vrlridgsas dylealadal ga
//
LOCUS       WP_285015895             468 aa            linear   BCT 25-DEC-2024
DEFINITION  rhamnulokinase [Pauljensenia sp. UMB10120].
ACCESSION   WP_285015895
VERSION     WP_285015895.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB10120
  ORGANISM  Pauljensenia sp. UMB10120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167330
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Pauljensenia sp. UMB10120"
                     /db_xref="taxon:3046356"
     Protein         1..468
                     /product="rhamnulokinase"
                     /EC_number="2.7.1.5"
                     /GO_function="GO:0004370 - glycerol kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008993 - rhamnulokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006071 - glycerol metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0019301 - rhamnose catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50945
     Region          3..447
                     /region_name="ASKHA_NBD_FGGY_RhaB-like"
                     /note="nucleotide-binding domain (NBD) of rhamnulokinase
                     (RhaB) and similar proteins; cd07771"
                     /db_xref="CDD:466791"
ORIGIN      
        1 mttalavdlg sssgrvvagr legdhieihe vhrfsheair rdgslvwdle hlwdqtvegl
       61 qkavqeypda qsvsvdtwgv dfvaldsddh pvgpprayrd ertartleqf rqriddeeff
      121 hltgiapati ntanqlvalt ceepelaehi dtilllpdyf awklsgvkgw srsicsssgl
      181 cepgsprwsd tvfsrlglpr swvddlnddl ttvgpctveg lesltvvrgg ahdtacavhg
      241 lpveegvkay flscgswsvl ggmldrpllt daafklgltn esrsdggvrp lfnitgmwil
      301 qelqrqwere gmptdtdelv aaartcapsa hlfdpddprf aepgemveki dtvireagge
      361 ppstkpeyvr lviesfaqry argidelaqi agsrpdqlnl vgggarnhll cdltaqaaql
      421 rvvagpieas ilgsliaqle tmgniasgdr pdiiattakt rvhepsar
//
LOCUS       WP_285016010             440 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Pauljensenia sp. UMB10120].
ACCESSION   WP_285016010
VERSION     WP_285016010.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB10120
  ORGANISM  Pauljensenia sp. UMB10120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Pauljensenia sp. UMB10120"
                     /db_xref="taxon:3046356"
     Protein         1..440
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46140
     Region          11..>271
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mliallcmvg vpahgddtir dqayedylgl dearsqgldg sgitigivdg ladtgvpela
       61 gadiaaheam csdaafepie vshatavtsv vaspdygvap gativnfavt slfnesrdgl
      121 sthcaaqdnv vsainaaina gadivvitig gsasllqyvs mraelhevll vaaagnkedf
      181 pidiaadngv lavgssdfeg nrstfsshge gldvvlpgeq itlrdpdpdg nltvitpdac
      241 gtsfsapmaa gmlalgmqkw peatpyevln afswstgred wdeqigfgvp qlheflnadp
      301 trfkdenpll hksdhgpddq lradyrdgli dpfftidvgd kdyvyrgrad dafarpeygd
      361 qwqpgtsprf tqsgqsgasq sdasqlpqsa psdgagqsng iplgiwiavg avvfvviivv
      421 vvlvararsp rtgtprqqpf
//
LOCUS       WP_285016011             315 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Pauljensenia sp.
            UMB10120].
ACCESSION   WP_285016011
VERSION     WP_285016011.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB10120
  ORGANISM  Pauljensenia sp. UMB10120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 315)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Pauljensenia sp. UMB10120"
                     /db_xref="taxon:3046356"
     Protein         1..315
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=33006
     Region          13..266
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mdlsrlgsvv rtrwgaatdq gprpdnedhw aaqpplyava dgmgghtggg rasevaiqaf
       61 tgalsgdaln greadvndld haisvaaqav malaspssms dedkdlaniv lagapgttlt
      121 gvliasheer pqwlvfnvgd srtylindgq iramtkdhsa rqeardaqws pdelpaanii
      181 tralgggmpg lpqadftvtt iapgdrvvic sdgvhsaidd aemvrivtqs ddaqraanal
      241 vdaalerqtr dnatvvtifv esvnppwpad dsvnpfertv giarpsstqt irrqpgsdaa
      301 eqagdevpss aeeti
//
LOCUS       WP_285016044             375 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pauljensenia sp. UMB10120].
ACCESSION   WP_285016044
VERSION     WP_285016044.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB10120
  ORGANISM  Pauljensenia sp. UMB10120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Pauljensenia sp. UMB10120"
                     /db_xref="taxon:3046356"
     Protein         1..375
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40154
     Region          7..368
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mnhrpgltfr flaaqvlvvv isllvaaava tmvgptlfhd hmlmagredp slelfhteqa
       61 yrdanlitla valptalisa llaslwlsrr lrtplqdltr aatslaagns rirvpageag
      121 pevatlahaf ntmadrleht eqvrrqmlsd lahemgtpls vltvyldglq dgvvdwnnan
      181 htimadqltr ltrlmedidd vsraqehrid ldlaeeglgd llhtaataag eayadkgvdl
      241 qvetitdtar vlvdrqrfgq vmsnllsnal rhtpaggqvr isvhrqgast alihvaddge
      301 gippdqlghi ferfyrgdaa rsrdnggsgi gltiskalie ahggtltats pgpgrgavfa
      361 lrlplsppds eeaar
//
LOCUS       WP_285016120             475 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Pauljensenia sp.
            UMB10120].
ACCESSION   WP_285016120
VERSION     WP_285016120.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB10120
  ORGANISM  Pauljensenia sp. UMB10120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Pauljensenia sp. UMB10120"
                     /db_xref="taxon:3046356"
     Protein         1..475
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49508
     Region          2..464
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 msdpaalets sgidqqgidl vppnrrhgka idlfflwagt ttniftvsyg allvilfgls
       61 fwqaiaaivi gnliayplla laslqgpktg ttnmtisrss lgprggrang lfswlmllgf
      121 eaaglvlvyy aiaallgifg vdisgvtqvv livvlgliqm llpligynfl maaqkfatii
      181 facafvilav lilpkvniat gevgadinam isaislvvvs gglswacsgs nfsrylpeet
      241 splsvstwaa lggfvpylll qslgaamatv avgpdvdlsd plavpailpa gfsvpflllv
      301 gfglmvqngt nlyssslnlq tagipakrpm vvvtdsiici litifavaqs sfyallsafv
      361 gslsvwlapw itiylvdwvm rrgnydlagl mndkggvywg vggvklpgfv sliagmigsa
      421 lfantgyfig piaaaispqh peyapdlaip agivvsgllf ialtitnkkk nlgia
//
LOCUS       WP_285016136             128 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Pauljensenia sp. UMB10120].
ACCESSION   WP_285016136
VERSION     WP_285016136.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB10120
  ORGANISM  Pauljensenia sp. UMB10120
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Pauljensenia sp. UMB10120"
                     /db_xref="taxon:3046356"
     Protein         1..128
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12877
     Region          2..105
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mhwlvlvlsg vfeavwatal sksegftkvv piivfilgaa ismgglgwal keipvstgya
       61 vwvgigagtt alwamlsgae pvrvvrilll cgiiacvigl klvsgddgva aatpsegarv
      121 tstaagdn
//
LOCUS       WP_285016181             453 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: bifunctional metallophosphatase/5'-nucleotidase
            [Lactococcus].
ACCESSION   WP_285016181
VERSION     WP_285016181.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus (lactic streptococci)
  ORGANISM  Lactococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Lactococcus"
                     /db_xref="taxon:1357"
     Protein         1..453
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51162
     Region          4..437
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mnslriihln dlhshlerfp vierffaeks vghpdvlrfd lgdnvdrvhp lteatggqin
       61 valmneldlt aatlgnnegl glthdmlsrl ynqadfdill snitnmpfah gpkiiksswg
      121 mrigilglta pylaylqagw divdpfvcld lllpldcdft illshlgkav dekiaknydi
      181 dliigshthh lfehgaelhg tllaaagryg ehvgeinltf dqnnkiiase istiatntlk
      241 keksdalhvn swelegrkml qgrtvaeipq sltnvypdye asyfiaella rygkvdacvf
      301 ntgllvteal psqltlddlh qflphsmrlv rltmrgkelk evlremldvs amlsgqnirg
      361 mgfrgkrfgq lifqgisfdr grfyyrntav rdaesysivv pdqylfawyf pllkkqekte
      421 ilfpyflrei vanelknekm nkkrkgeesa krs
//
LOCUS       WP_285016549             242 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Lactococcus garvieae].
ACCESSION   WP_285016549
VERSION     WP_285016549.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..242
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26217
     Region          4..240
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 meiitakdnk kikearkllt kkkyrknsyl iegfhlleea vnsgakilqi fveenkyqhv
       61 shlenilavs sevlkslsda gtpqgvvaev afeevkvefg hgkylvlenv qdpgnvgtmi
      121 rtadaagfsa vlcmgdtadi yapkvmrsmq gsnfhipvls vadftelqea riplyvttls
      181 nrsishkelv aeedfalvmg negagvsdqa vavadqlvhi empgraesln vavaagilmf
      241 sl
//
LOCUS       WP_285016605             216 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Lactococcus garvieae].
ACCESSION   WP_285016605
VERSION     WP_285016605.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..216
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=24561
     Region          12..212
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mliiffiigt ifgsflglvs drwgtgasii ygrsqcsscq tvlrwwqllp lisqfifksr
       61 cafcgekfsy hyfileflsg ilfgalwfdl dllhflilli slllskfdid thsdplnigl
      121 gftvcffiff ptgpisyfwl alacfsffin igigagdflw lffasfslsl vemllliqla
      181 cvfglcflli kkrkklpfip flslaylivi llpril
//
LOCUS       WP_285016646              71 aa            linear   BCT 25-DEC-2024
DEFINITION  thioredoxin family protein, partial [Lactobacillus jensenii].
ACCESSION   WP_285016646
VERSION     WP_285016646.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus jensenii
  ORGANISM  Lactobacillus jensenii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 71)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 71)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 71)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 71)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Lactobacillus jensenii"
                     /db_xref="taxon:109790"
     Protein         <1..71
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
     Region          <2..70
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 qapileklae evhedelkif kmdvdanpnt psefgimsip tlifkkygqv vkqvvgvhtk
       61 eqlkaiiael s
//
LOCUS       WP_285016754             200 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: TlpA family protein disulfide reductase
            [Novosphingobium].
ACCESSION   WP_285016754
VERSION     WP_285016754.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium
  ORGANISM  Novosphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Novosphingobium"
                     /db_xref="taxon:165696"
     Protein         1..200
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21474
     Region          63..198
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mlssrslksl vlcslagasa lviagcdskg nkdaqpapse eakqagpaqa peaggkldrs
       61 hkgepmptvs lvdntgesld lssfkgkpll vnlwatwcap ciaemptlnk lidregelgv
      121 tilpisqdmg qtdkvveilr rreleqiqpw vdeqgdlgfq yggnlpvtim fdrqgkevwr
      181 ytggndwtsp ealkliaeak
//
LOCUS       WP_285016821             243 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Lactococcus garvieae].
ACCESSION   WP_285016821
VERSION     WP_285016821.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..243
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28030
     Region          1..142
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mtasyeefar vydsvmdeel ydlwfdfsqr hfpektqnim elacgtgils irfsqagyev
       61 tgvdlseeml tiadqrarqm gekitfaagd mrelsgattf dvvtcysdsl cymsnasevq
      121 rvfdgvynsl nadgvfifdv hstyqvdsvf pgyayhende dfaflwdsfe gddphsvvhe
      181 ltffvkdsdg kfvrkdevhq ertypikeyl tglqkfskve vyadfedkkp eeeslrwffv
      241 ckk
//
LOCUS       WP_285016827             253 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285016827
VERSION     WP_285016827.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..253
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26951
     Region          72..250
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mtrtrfrtia lglvvaplal glaacgkkde ptagatsgap iakiaapagk swadtiekta
       61 eggyrmgnpn apiklveyga lscshcalfa qqsfeplrdd yvasgrvsye lryfmlnald
      121 ipasllaecg steaviplse qfwawqpkmf enmqaasker laqidalpke qqlaaiseva
      181 gmtdffasrg iardqaaacl adttkakala dqtqkaseqf nvtgtptfii ngnnvgsmew
      241 dklepklkea gar
//
LOCUS       WP_285017043             341 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285017043
VERSION     WP_285017043.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..341
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=36882
     Region          39..335
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mkkpklppkl akplkravdl pvwadlglrl ggafalvmlv vllhwidrdg lkdthdgtvs
       61 vldvfyftmi sitttgfgdi apvsdksrli eavivtpirf avififvgta ynyfikhswe
      121 swrmkriqer lsdhvvvlgf gvsgsqavqe liargtdpac ivvvdpsagr lrhaeqqgcn
      181 vlegdatrde tlaavridaa rtilvsagrd dtsilivlta rhlapgvpit vvvraddnel
      241 larqagadnv inpvrftgll lagsaegqhi aeymsdlasv dgrvqlverp vrpeevgksl
      301 dqlatgkgvr iyrgeqcigf wepgakvlea gdliveiavt p
//
LOCUS       WP_285017054             282 aa            linear   BCT 25-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285017054
VERSION     WP_285017054.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..282
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31303
     Region          1..278
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mairfedike figsrviwdd radlftpeaa aairakveer tvvvfpqanl tdqeqlaite
       61 amgekirlta rnnvqnndqd vyqvtldeki npqpeyvlgt ffwhmdgitv dmpppfatll
      121 scriapdkgg etefastyaa yeglpeeekq aleglkavhs vraslspiad aipekhrekv
      181 lgiglikehp lvwthesgrk smvigttadh ivgmevpagr amlirlqewa aqpafslrhk
      241 wtkgdfviwd ntgamhraip ydkstgrmmh rtsiagteav aa
//
LOCUS       WP_285017078             402 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285017078
VERSION     WP_285017078.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..402
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42577
     Region          1..401
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mgkplegikv vevamwafvp acggmladlg advikieppt gdplrglsig glgggkidys
       61 wesynrgkrs vtldlkqaag ravldrllkd advfltnllp parramride etirsgypdi
      121 iyasgsalgp ngpdhekggy daitfwargg isssltepea phpvgppgpa fgdtisgaml
      181 sgaicaaiak raltgeassv dvsllgtalw smqryvcqat adgvqkfpkp padkpnnvlv
      241 snyrtadgrf lalcmlqadk ywtpfceaag rpdlaadprf adaaarkani dacyaevkal
      301 fagktlaewk ailsrqsgqw dvvqdvgemk ddpqaqangy lkrvdygdgt qipmiglpmv
      361 fdgtplsstr spdlgahsda vleslgysed eiidlkvqgv vf
//
LOCUS       WP_285017247             315 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Lactococcus garvieae].
ACCESSION   WP_285017247
VERSION     WP_285017247.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..315
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35350
     Region          18..311
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mlliifsfls ltfemkkpla fflevlmdyd knnpehiifi shlarvlvsi sigaslalgg
       61 fimqlqyend ladptlmgvs dgsalaivig miflpnltmp eriafsvigs flayiiilyi
      121 ykilflsqsr ltfpligivi smllssmttf lvsyyniaqs vsswynsrly rvsfsdvvyf
      181 wpillllvil iillrkqmdi ysyghsitts igmkrrqwel fygvivvllt glsvaivgri
      241 afvglviphi iklsigkkya vsvffvpltg glfvlisdyf sryinypfet pigivialig
      301 vptflylikr gatih
//
LOCUS       WP_285017258             547 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285017258
VERSION     WP_285017258.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..547
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=60941
     Region          12..490
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mvevankgid gtydavvvga gigglyavyk lremglsvlg ieagdnvggv wywnrypgar
       61 cdlltidycy tfspevdaew swseqfaaqp eileyinfva drhelrkdyl fdtrvsraey
      121 dearqvwtfg tetgktfeat yavmatgpls vpkrpdfedf dsfkgelyys grwpkepvsy
      181 egkrvgvvgv gstgiqiipv vaqeakelfv fqrtpsftmp mrnhkhsdey taeikrnlpa
      241 mrvaaknspl ggvrpattrp yfslppeqrv kimesawqng ghtflgsfsd lmqneeaneq
      301 vaefvrgkis evvtdpatae tlkprgypif arracldtny yetyneehvs lvdcfkepiv
      361 gltekgvrta sreieldmli latgydgltg almafdvvgr dgktineewk ggahsylglm
      421 mkdfpnlfiv cgpngpsala niftineqnv nwlagaiehm rrsgltamep taeaehewme
      481 hvhelslntl vrkantwytg anvagkargl tmytggfkay retcqeaadd nwrgmvfeka
      541 gvpetva
//
LOCUS       WP_285017380             793 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-glucosidase [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285017380
VERSION     WP_285017380.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 793)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 793)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 793)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 793)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12807938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..793
                     /product="beta-glucosidase"
                     /EC_number="3.2.1.21"
                     /GO_function="GO:0008422 - beta-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0030245 - cellulose catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=83724
     Region          23..>327
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          56..758
                     /region_name="PRK15098"
                     /note="beta-glucosidase BglX"
                     /db_xref="CDD:185053"
ORIGIN      
        1 mtditltqas altaggamws svalpeadip aftmsdgplg iasgrvderd iallspcstl
       61 lgatwdrdlc rrvgelvghe avargvdavl apnlnlarsp lagrafeyfs edpvlagvlg
      121 aewavglqst gtgsvakhlv cndsetarde vdvrvddrtl revyllpfey avdagcvgll
      181 aaynrvngsw caeqaevltg ivkgewafgg limsdwfgth stegsinagl dlempgparf
      241 lgpkveaava agsvlrsrvd daaarvtava rrldapkaap apmdqaeall veaaaagftl
      301 lrnegamlpl epgtvkrlav igpnayapcf qggtfakisi spdaptplet lretygdsce
      361 lvfepgvdpq prlpgmpvvp aldigdgctr gmtleyfaqp gctgevlsre trdtnslvwf
      421 vgvheqaeft rpgslrasgr ftaesaglys fylgstgaar ilvdgrevlt aggevpasei
      481 mgvlkrgdad maaielaegq evtvtaefew lggrvqglwy gvrnpdsaea mlaraveaar
      541 gadavllmvg etsdssvesk drgdtrlpem qerliaqvca vnprtavivn vghafdcswe
      601 dgaaavlsvw ypgqgfaqal advlcgrrep rgrlpvtiaa deadypafdl apaadgtlty
      661 aegtrfgyrg lvaqgraarh pfgsglgyaq vlwsdaraed gavsvaltnp garetceivq
      721 vyrdepecal vgfarvilap getrrvtvpl etralriwge egwmpvadrl tlraarhced
      781 aglpvevtla afv
//
LOCUS       WP_285017458             499 aa            linear   BCT 25-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285017458
VERSION     WP_285017458.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..499
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=52336
     Region          21..499
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mtrpfdghtl spetvafldg dmrllidger vegeafhetr dpatgivlar fhvggkaqid
       61 savaaarraf egpwgsmaaa ertailqhla rvmeanatll teldvidngm prfiagltta
      121 ncvemvdyya gailriegtt ttpprhvsae aealtytlre pvgvvgqivp wnvplstail
      181 klapalaagc tvvvkpseet plsllaladm igeagfpagv vnivngfgat agqalaehpd
      241 vdkvsftgst atgrrivmaa mgnlkkvsle lggkspvivm pdadlalavp gvamatfflq
      301 gqncmagtri fahediydal ikglvqfasg mtlghgldpa tmqgplisea hcgkvmahid
      361 aakaagarlv tggeklarpg nfvqptiftd ctpdmavmre eifgpvmavq kvattdldel
      421 arlandtpyg lsgsvwtrdm aaahrlvkrv rsghvsinch gavgtnipfg gygqsgwgre
      481 fgqegldgyl etkavtarl
//
LOCUS       WP_285017470             454 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha
            [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285017470
VERSION     WP_285017470.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468627
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..454
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=52602
     Region          48..443
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
     Region          211..444
                     /region_name="RHO_alpha_C_MupW-like"
                     /note="C-terminal catalytic domain of Pseudomonas
                     fluorescens MupW and related aromatic ring hydroxylating
                     dioxygenases; cd08882"
                     /db_xref="CDD:176891"
     Site            order(218..219,223,226..227,230,232..233,235,237,362..363,
                     407..409,411..415,426..429,432,435,439)
                     /site_type="other"
                     /note="putative alpha subunit interface [polypeptide
                     binding]"
                     /db_xref="CDD:176891"
     Site            order(227..228,230..231,233..234,238,332..333,335,343,345,
                     352,354,393,396..397,401..402,405)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176891"
     Site            order(227..228,230..231,233..234,238,332..333,335,343,345,
                     352,354,393,396..397,401..402)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:176891"
     Site            order(233,238,405)
                     /site_type="other"
                     /note="Fe binding site [ion binding]"
                     /db_xref="CDD:176891"
ORIGIN      
        1 mkphvmgwdr asmdvkrvvd vfrvdpesvg ngtpterapd pelgtdiipa aryyspefmk
       61 lewervwtkv wllggrsddl kepgdyictd igkesvlivr qadgsirafp nlclhrgnrl
      121 rpegrgnaek fqcmyhhwty gldgklehip dlctfvqggp dgmkltplpc iewnsfvwfs
      181 ldpnvepfdd fidplkrhle pyhpermawm rditvewdcn wktsvdafse tyhvqgihpq
      241 lkwylddvnv qidcygkhnr ylipfaaisp rvampsqipp aiheimvhag mdpaeyegrv
      301 sdirrdvqlf krehgaaqgk dyselndeql tddyhytifp nvsvnvhadd vmlfrqrpha
      361 tdpnkmyydi wmfglvpege ewpervrhqr fkhgdktigq vldqdafnlp tvqtgmqsdf
      421 fpglhigdqe lrirhfhkvl ddyiythgkg pddl
//
LOCUS       WP_285017592             279 aa            linear   BCT 25-DEC-2024
DEFINITION  DODA-type extradiol aromatic ring-opening family dioxygenase
            [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285017592
VERSION     WP_285017592.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Vaillancourt,F.H., Bolin,J.T. and Eltis,L.D.
  TITLE     The ins and outs of ring-cleaving dioxygenases
  JOURNAL   Crit Rev Biochem Mol Biol 41 (4), 241-267 (2006)
   PUBMED   16849108
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Siegbahn,P.E. and Haeffner,F.
  TITLE     Mechanism for catechol ring-cleavage by non-heme iron extradiol
            dioxygenases
  JOURNAL   J Am Chem Soc 126 (29), 8919-8932 (2004)
   PUBMED   15264822
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..279
                     /product="DODA-type extradiol aromatic ring-opening family
                     dioxygenase"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016701 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29838
     Region          16..250
                     /region_name="45_DOPA_Dioxygenase"
                     /note="The Class III extradiol dioxygenase, 4,5-DOPA
                     Dioxygenase, catalyzes the incorporation of both atoms of
                     molecular oxygen into 4,5-dihydroxy-phenylalanine;
                     cd07363"
                     /db_xref="CDD:153375"
     Site            order(22,69,244)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:153375"
ORIGIN      
        1 mnaqtadmtv sstqmptffi phgggpcffm dwsvmggpad twdkteawlr alvstlpekp
       61 kgivvisghw eesaftasta vepgmiydyy gfpphtyelk ypapgspala ervvellkga
      121 glpartdpar gfdhgvfvpf llvdpdatip vvplslkadl dpaehiaagk aleplreegv
      181 livgsgmsyh nmrgfrtpaa trpsavfdqw ltgaveatpk eretllshwa eapagrqshp
      241 reehllplmv aagaggasag hkvfgdnvmm adisayrfg
//
LOCUS       WP_285017611             316 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Novosphingobium
            sp. fls2-241-R2A-195].
ACCESSION   WP_285017611
VERSION     WP_285017611.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..316
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34523
     Region          37..307
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mlsfgvdlit ffhpgfwgma neqevitfgr eqprafwdrm ldtlaqsgvt gieltfspfg
       61 pegliaaygs ieaardeldr rglaiasgff advaieggvg daqtearwld saeesvkala
      121 awgsdimvmg lpmrtswnae ppvfvdmefa rkaadfcnrl galtlrhgvr lalhteahst
      181 fcqprdidll lmltdpvyvg fcpdsahill sggdpvtvva rhiervvtah wkdaksampi
      241 nipidhgihh ahreyfcaig egtvdfdgwa klmlskadqk waileidavp dpltetrksl
      301 afagevldrl snetaa
//
LOCUS       WP_285017894             311 aa            linear   BCT 25-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285017894
VERSION     WP_285017894.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..311
                     /product="isopenicillin N synthase family dioxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34333
     Region          1..310
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 mdlaqipvls lvadradlpa rigesfrtfg famirdhgid qslidqawar teeffalpve
       61 tkqkyfipgq sgargytpfr tevakgakek dlkefwhvgr dvpadsplaa smppniwpte
      121 vegfeetfre lyaqfdeaga kvlsaiavdl gldagwfdag iedgnsvmrl lhyppvsaes
      181 ggairagahe dinlitlllg aqeaglells kdgrwlsvap pegaivvnig dmlqrltnhv
      241 lpstthrvrn pegaraghsr ysmpfflhlr sdfrfvtlpe cvsdenpdry pvsitaddyl
      301 qerlreiglk m
//
LOCUS       WP_285017936             239 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Lactobacillus paragasseri].
ACCESSION   WP_285017936
VERSION     WP_285017936.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus paragasseri
  ORGANISM  Lactobacillus paragasseri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Lactobacillus paragasseri"
                     /db_xref="taxon:2107999"
     Protein         1..239
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=26436
     Region          13..234
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mqdskdysls hyignkikqf riergytvee lanklgtsrp tvtryengtr kanqdvlfel
       61 anifnktldd ffppkdnaqs atyptqgddy sinddlssye ikpknmvett tkhipligei
      121 acgdpitaee nveeyithvf pkgqvpsgel idlrakghsm eptipdgsiv tirlqpeved
      181 geiaavqang dteatlkrik hidglvmlkp dndaydpiii tpnnpatiig kaiqftskl
//
LOCUS       WP_285017940              68 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lactobacillus
            paragasseri].
ACCESSION   WP_285017940
VERSION     WP_285017940.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus paragasseri
  ORGANISM  Lactobacillus paragasseri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 68)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Lactobacillus paragasseri"
                     /db_xref="taxon:2107999"
     Protein         1..68
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7986
     Region          6..60
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(7,11,36)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(10,35)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(17..18,29,32,36..37)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mwwrhidell rnkkislkel aiksnvnyet irsykyrgye psfknmckia dalgvsldkl
       61 rgdkkcnh
//
LOCUS       WP_285018063             367 aa            linear   BCT 25-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Lactobacillus
            paragasseri].
ACCESSION   WP_285018063
VERSION     WP_285018063.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus paragasseri
  ORGANISM  Lactobacillus paragasseri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Lactobacillus paragasseri"
                     /db_xref="taxon:2107999"
     Protein         1..367
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42309
     Region          20..241
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mkkiifviff ilvfpftcgf lniahrgdne qgkfaehswm aydralcaqv dyleldlqkt
       61 sdnvlvvshd dnlsrvfgvd kiiadypyqe llsyknqnge slhslgdvfk ryqnsnvkfm
      121 iepkdnseed iklllnlirq yhlenrvlle sfsktalmqi skinpqiptm qlagefnllp
      181 stqyyannfy skkvadylse hdkkyllwgv nkkvqmkqyl qldknvsgll tdypvelani
      241 lhssdifkrn yeagsfpsks isglmylkng ssvevdqvkm kdnqlfyhvr pdlwlsdhnl
      301 knsdhsapka qtgkirlqke tliytdpslk kysgkklpqn stwnyfavkk vhgktvynlg
      361 gaqwvkq
//
LOCUS       WP_285018196             158 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285018196
VERSION     WP_285018196.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 158)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 158)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008128
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..158
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15605
     Region          9..158
                     /region_name="CytC556"
                     /note="Cytochrome c556 [Energy production and conversion];
                     COG3909"
                     /db_xref="CDD:443115"
ORIGIN      
        1 mtfsnklsla vlgvsaavlt vsatvaiaas paetaiatrh anfkkmggam kvlkdqlasg
       61 sidkvqavaa aktlaatgra qvglfpngsg pssgvkteal paiwtnraaf dgamktyiaq
      121 adklvavagt gnaaaigaqf kavggacgsc hkqfradd
//
LOCUS       WP_285018199             511 aa            linear   BCT 25-DEC-2024
DEFINITION  adenosine deaminase family protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285018199
VERSION     WP_285018199.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Cristalli,G., Costanzi,S., Lambertucci,C., Lupidi,G., Vittori,S.,
            Volpini,R. and Camaioni,E.
  TITLE     Adenosine deaminase: functional implications and different classes
            of inhibitors
  JOURNAL   Med Res Rev 21 (2), 105-128 (2001)
   PUBMED   11223861
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004592
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..511
                     /product="adenosine deaminase family protein"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54524
     Region          50..449
                     /region_name="Add"
                     /note="Adenosine deaminase [Nucleotide transport and
                     metabolism]; COG1816"
                     /db_xref="CDD:441421"
ORIGIN      
        1 mrrlvstllt tlalplaapa ahadeaaasa lldemagnag rlrvflqamp kggdlhnhlg
       61 gsvyaedflk vaaakgmcad agitrivpgp cpaplqigpm aekdpftyak lidaistrgf
      121 qkgigpalvs ghnqffssfr kfgpaadged arwladafas agrnnlvyve lmhnpdsttp
      181 fmlsapdapl gvdgiaaayk rdlpaaqalv apaiaevdee eafakkrlgc stkaadpgcg
      241 vamhyiysam rglppqvvwr smlagfvlad kdprfvgvni vmpeddpval rdydlhmamf
      301 rfleakypkv nvtmhagela lglvppkdle dhigkavasg akrighgvdi ayevnapetl
      361 armardgigv einltsnavi lgveggvhpl hvyrsmgvpv mlstddegvl rsdmtnehvr
      421 avqqqglhya dlkelarnsl eysfapgasl wadrrygavv apcatdfaag scktflakne
      481 katlqarlem nfdrfersld rfkarqgaag d
//
LOCUS       WP_285018233             290 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285018233
VERSION     WP_285018233.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..290
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31058
     Region          7..283
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mtdpaaavae lralleveei dtdlfrggas eerpgrvfgg lvvaqalaaa ardlagsdrq
       61 ahslhayflr agdttrpiiy rvlrdfdggs fanrrvvamq ggkpilnlaa sfhrredgfa
      121 haaampqvpl peqcpdlvta laatgqkfpq amldrlaafe irpgppavqg sdtphqflwf
      181 klaapidsde vlrrvvltya sdfalvstai lphskaifsp gmqvasldha vwfhstppvd
      241 dwllyamdsp waghargfar galydragtl vasvaqeglc ravptqepta
//
LOCUS       WP_285018231             572 aa            linear   BCT 25-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285018231
VERSION     WP_285018231.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..572
                     /product="long-chain-fatty-acid--CoA ligase"
                     /EC_number="6.2.1.3"
                     /GO_function="GO:0004467 - long-chain fatty acid-CoA
                     ligase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=62224
     Region          30..551
                     /region_name="FC-FACS_FadD_like"
                     /note="Prokaryotic long-chain fatty acid CoA synthetases
                     similar to Escherichia coli FadD; cd05936"
                     /db_xref="CDD:341259"
     Site            order(213,216..221,223..224)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(216,331..332,353..358,438,450,453,464,544)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(216,258..259,306,308..309,312,331..332,353..358,438,
                     450,453,461..464,525)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(258,308..309,312,331,461..463,519,525)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 midaatiggv apatassttd emppiaprll tdlldhavda hgswsavdfm grkwtyseig
       61 alakraargl qdlgvtkgtr vglclpntpy yvvayfavlr igavvvnfnp lyteremahq
      121 vtdsgcevmi atdlalclpk leplvgktcl krvvvcpfad alpaikrraf llfkhrdiah
      181 ephdlryarw anliardaep dpverhpndl avlqytggtt gvpkgamlsh anlaansaqm
      241 iahvghmpeh qertlgvlpl fhvfalttvl nysvdtaaem illprfemks flatakrtrp
      301 tqffgvptly talnhqqlhg efdnvrvcis ggaplplevr refeektgvn vvegyglsea
      361 spiiacnple glvkdnacgp afpgtaleir dpsdptrlca pgekgevcar gpqimqgywg
      421 rpedtektfi ygalrtgdig yldedgylfl vdrikdvilc ggynvyprii eealyehpmv
      481 aeavvigipd ayrgqapkaf vvlhggdild qetlldflre rlnkiempas iefrdslpkt
      541 mvgklskkdl vaeeaakreg qnsgqgsggt aa
//
LOCUS       WP_285018522            1040 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285018522
VERSION     WP_285018522.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 1040)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..1040
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=109982
     Region          50..>576
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mrslplislv aslampmpaf aaeaaadaps vpvikdddtd pdnplevhgn eilvtaprvi
       61 gsidvpqqpi avfdendias ygvasieell daispqtgsg rgrggspvml lngqrissfr
      121 emrgippeai rrvevlpeev alrfgysanq rvvniilkdq fsavttsgey nrptrggydn
      181 yelegglfki tgprrfnvng kldntsmlte aergitqdes rvsqvagdpd paryrslaaq
      241 dheltlegtm tqglgekgla gaitatggyt rsntlslsgl dtvpltydgq tlrrtladpl
      301 rnrsitdtfe gglgystmlg ewqvsatana tytdtntrvd rrrtetqygd lqaevasgal
      361 sitgalpnvp gagvdvattr qltlsnlvtl sgkpfrmpag eanltvkggy dydrsmsedt
      421 rttvgnvtlr rgdllggvnl alpltskged flgavgditl nfsggldhls dfgtltdwsa
      481 gvtwsptetl mlqasyivdq aapkltqlaa pmvetynvav ydftnsrtal vttvtggnpd
      541 lkketqrdwk isaqwklpfl qrsnliveyf rnrssnvtqs fplltsaied afpdrvtrda
      601 dgnltridrr avtfdevkts smrwgfnisg slggsssagg gtpagqpapm saaptqsvtg
      661 pngpmaggqv lnggqatgea grpnfdpsrf aaireklcap gasdpdpasl peglrnrlvg
      721 adgkidpakl aefkqracsa egqgatpgeg ggrgpmeper ferirtalca ggsgppdvas
      781 lpdrmrerim gadgkvdpak laelrerfcn aptpapgttr aqgeqpmfpp pgafggqppm
      841 asnagergag gtraesggrg pgggpggppg ggfgppggrg gsrwnlsvyh twrftdtili
      901 apgvpvldql ngdsttaggt prhtieaegg lfkngyglrl kaewnaparv dgsgapgsqd
      961 lrfgstfdvs lrifadlgrn ealvakmpfl kgsrlslrad nlldsrqkvt dqngatpiay
     1021 qrayrepqgr vlgidfrkmf
//
LOCUS       WP_285018723             521 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Lactobacillus
            paragasseri].
ACCESSION   WP_285018723
VERSION     WP_285018723.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus paragasseri
  ORGANISM  Lactobacillus paragasseri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Lactobacillus paragasseri"
                     /db_xref="taxon:2107999"
     Protein         1..521
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58811
     Region          1..506
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mklvilhssd thgflmptdy qnkdnydapi slsrvssvvk sekekygadn vlvtdsgdcl
       61 qgsplasytq klpedeglrk fteaynevgy daralgnhdf nygldylsyy vdnnrapfin
      121 dnvldadtnv pffgkeytiv ekaglkigim gittqyishw esedhikglk fvsgyevlak
      181 lakklrpqvd ilcalyhggf esdpltgkat ephtgenegy kilteipeid vfltghqhrr
      241 lnlvtrntai vqpgyrgeav gkviidfdkd kngkvkindm ttelidskdy apdpaiekiv
      301 kgldeetqkw ldqpiahlse papiddaikg riegapfinl iqqmqlwftg advsataims
      361 esahgfsknv tmrevllnyp yanqlcivkl tgkelkeiie ysagflekdk dgkikfidrw
      421 itpkpmlyhf dlfypvkyea dlsrpvghrl tkvtlngkdl eddkvyklav nnyralgggf
      481 ypaysmdkie kifdqdyvqm fseylthgdi kvdtaknykf y
//
LOCUS       WP_285018891             157 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF2269 family protein [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285018891
VERSION     WP_285018891.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..157
                     /product="DUF2269 family protein"
                     /calculated_mol_wt=17536
     Region          2..153
                     /region_name="COG5528"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:444279"
ORIGIN      
        1 mdeylflkli hilsstllfg tglgtafhgw manragslaa rrvvnrnvvl adwlfttpav
       61 ivqpvtgvwl aqiagfplss gwlvaamlly vlvgacwvpv vfiqvemrri adrtpdgeal
      121 ppryfrlscw wfrlgwpafi gvliiywlmv akpeiaf
//
LOCUS       WP_285019002              96 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein
            [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285019002
VERSION     WP_285019002.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..96
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10442
     Region          1..91
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 miheiatiti dparaagfea avaaarphfe aargfvsfal ersiespery rlvvgwqsve
       61 ahmvdfrgsd gfqawrelas pffvgavave htirvs
//
LOCUS       WP_285019095             439 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285019095
VERSION     WP_285019095.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..439
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47514
     Region          37..398
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtkvtslpad drtcgwfhts svrqprpaht getrapwvvv gagyvglaaa rqlamnfpqd
       61 qvvlveaqev gfgtagrnag faidlphdig aadyigdlat anlvlklnkt gqnylkdlvd
      121 lhgiechmra sgkyqgavee rglavleayr ggldrlgqpy eviegsdlpd higtrfykka
      181 lftpgtmlvq psalvkglad tlpanvtlfe rtpitevsys pqiilthang rivadklila
      241 nngfgmafgf lknrmlpvft ygsltrqlte eeqarlggkd fwglipadpa gttlrrthdn
      301 rilvrnsfsy hpggisndhq revaakrhrr sferrfpmls gvpfdytwgg aivmsrnhes
      361 qfgelapnvy galccnglgi trgtatgvll adwlagrrge vidfllaspg psanpprpfl
      421 digvkanlaw aqakagpes
//
LOCUS       WP_285019137             292 aa            linear   BCT 25-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285019137
VERSION     WP_285019137.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..292
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32029
     Region          9..279
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mtlsatlarl dvirvagrig aevsglrlgg dldeaaiael raallrhkvv flrgqqhldd
       61 aahqafaarl gtpvghptlp gdggdfllel dshrggkans whtdvtfvpd ypaisilrav
      121 ivppvggdtt wancvaaydr lppalrtlae glrgvhsndy dytanqdtad daldayqatf
      181 tstiietehp lvrvhpetge ralvlgsffk rfaghgqees rrlydlfqth itrlentvrw
      241 rwqagdvaiw dnratqhyai ddyegahrvm rrvtlagdva rgidgqesrr vv
//
LOCUS       WP_285019168             265 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285019168
VERSION     WP_285019168.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 265)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..265
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26945
     Region          6..252
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mssfatltnp vtlvtgassg igaeiareaa rrghrvilta rrtdrieala aeigalaaip
       61 adlaapggva glvaelarra ievdilvnna gfgqqgsvat ipsglqtgqi dlnvraltel
      121 tvallpgiva rgaggvlnla siaafqagpn vavyfatkay vlsfsealhe evkaagvhvt
      181 alcpgptrse fadvahldtt aafrsaslva dpaavaragl dglehnravv vpglanrfaa
      241 fgtrlvpral srriagnmqk qpprs
//
LOCUS       WP_285019341             364 aa            linear   BCT 25-DEC-2024
DEFINITION  fatty acid desaturase family protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285019341
VERSION     WP_285019341.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..364
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39738
     Region          21..331
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mnaqnaidlp padarnsaqg stwhsqmpdd kamlraavel trdiaaarpg iywpdmlgsa
       61 algyaalaga ilagnpvvav llgvaaslal yrallfihel thihkdalpg frfgwnllvg
      121 vpmlipsfmy egvhtqhhar trygtvedpe ylplalmkpw slpvfaltai llppallirs
      181 avlvplgaiv pplrtlvwer vsalainpqy krrkpegdfa rmvfwqelac sawaiglvaa
      241 sfvwgwrpll ialcivsfta llnqvrtlva hlwendgeam tvtaqyldsv nvpppgfvaa
      301 mwapvglryh alhhllpsmp yhslaeahrr ltthledgst ygkanysgla pllgrlarst
      361 mkvr
//
LOCUS       WP_285019553             438 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285019553
VERSION     WP_285019553.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 438)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 438)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 438)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10605574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..438
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47914
     Region          50..249
                     /region_name="AAA_25"
                     /note="AAA domain; pfam13481"
                     /db_xref="CDD:463892"
ORIGIN      
        1 mnmpdnfdan dvetriglek vreafsqrks mlppfapdea yadefgatta pnaialkatp
       61 fqwrdpatip arkwlygrhl irkfvsldia pgglgkssvk ivealamasg lpllgkdlhe
      121 gplrvwlynl edpaeeserr ihaaaqhydl spgqfgdrly adsgreqpic iaeeteggar
      181 ivrpvsdavi aelqarkidv lsidpfvssh aisendnrai dmvakewsri advcdcainl
      241 vhhvrksnga evtaessrga vsligaarsv vvynrmtkee aeragidade rgfyfrtqnd
      301 kanlappega dwfrmnnvdl pngdsvgvac rwewpdafeg letrdlykvq laidgaewge
      361 svqakdwagn avatalgmda ekdkhrikal lrtwiaskal tvekrptakg rpkpfvivgs
      421 wvdsttlpts qsgvgkvg
//
LOCUS       WP_285019624             294 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285019624
VERSION     WP_285019624.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..294
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32829
     Region          13..254
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mhgktasmyn gplrlfhlsd ihfglvdqqa idwakacidr emphavaitg dltmrarhpe
       61 fqaacewiqg fdvpvtvevg nhdipyfnly qrffdpyrrf kaiermvetq ldlpnlaivp
      121 lrtttraqyq rfpwsngwvt dhalkqtlaq idalpegtrv lvtchhplpe rradgkllti
      181 ngtrtmkvla grkvmavlsg hihdpfdlte qtsagplrmi gagtlskrir stppsfneiv
      241 idgdqirvta rnlekvptpa mqidevpena lpprepgepv spvgkvppvd ppvh
//
LOCUS       WP_285019736             259 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285019736
VERSION     WP_285019736.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..259
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26860
     Region          1..234
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtkpavlitg astgigatya drfarrghdl vlvardvarm eamatglraq ngvsidilpa
       61 dltradeiaa vearlrdddr igillnnaga glngsfvdqp tdtitqlial nttsvtrlas
      121 avaprlaarg dgaiinigsv vglapelgms vygatkafvl flsqglalel gpkgvyvqav
      181 lpaatrtelw gragadeanl ppmmdvndlv daalvgfdkr egvtipplhd gtlwdafdga
      241 rkamlpgfgt tqpasryva
//
LOCUS       WP_285019767             942 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285019767
VERSION     WP_285019767.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 942)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..942
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=100668
     Region          17..942
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 masgqigivt efesqglger iafgrfcvhp gkrlltrdsq pleiggrafd llmalieqpg
       61 rvlskrellk rvwpdvvved gslrfhmagl rkllgegsdg gdarfiatqv gvgyafvapv
      121 erlglepplp draaaipapp eaqiggttni ppplphligr erdldlliar vadialftvv
      181 gpagvgktsl mieighrlta qfngratfvd fsmlenpalv ptmiagamgi svqsgdpaaa
      241 iighcgsdpf lllldncehv ideaariaer iveqaphvri vatsreplrv rgehvhrlda
      301 ldyppdtdal treqllaypa lqlfherara adsaweidgs earliadicq rldgmalpie
      361 laavraathg iaatarqige rfslawsgrr taqprqqtlr aaldwsydll ssqervvldr
      421 lavfvgpfsv daaldvvsda aigsdeaaia ldelaaksli sanrvrgagt yrllemtray
      481 areklaarga ddhrtatrrh alfflselea laaqdsaafq daralrpqlg nirsaldwsf
      541 gpagdiglav rlaaasmpvf lnlshlaecr twatraiaal epaqrgtvve lelqaslgia
      601 lmfahsnspe vgkaltrald vaaliedhrs rlgilarlhi fhehvgdyar tmacaeqaia
      661 vaqaladpea laiayslsgi shyqtgdqis arrdlelale nssasqggrs vvhgfdhrnr
      721 asialarvlc lsgepeaarr laertvaeaa aldhpvthci alicsmsidv wmgaftrare
      781 tlpvlrdcar ahalapyiav sqgfdgelal efgghaeavq lledslrqlh earyellttr
      841 fslalargla avgrltdarr vvdtsiarci dngervalae llrikaavas aagavdeala
      901 lldeaaaiar sqgarawemr vaadragmpa gaispggpaa ar
//
LOCUS       WP_285019800             332 aa            linear   BCT 25-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285019800
VERSION     WP_285019800.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..332
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=36204
     Region          11..320
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(17..18,20,60..62,83,111..112,115..116,118..119,122,
                     126,128,136,138,140,142..148,150..154,172..173,176..177,
                     276..277,284,290..296,298..301,303)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(61,84..86,109,248,294,297)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240626"
     Site            order(85..86,113,162..166,184..186,189,218..220,224..225,
                     246..248,271..272,294,296..297)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 mdtarplppr prvivtrrll pevearmael fdlvpnlddr pmtrvqleta mhdcdvlvpt
       61 vtdmidaami agageriami asfgagtdhi dlaaarahri lvtntpgvft ddtadltlal
      121 iilvsrrfse nartlregrw egwapssmlg hslsgktlgi vgmgrigqav ayrarafgle
      181 iryhnrhrlp pavenmvsar yepnldrlva eadiltlhcp agpetrhlid arrlglmkpg
      241 aclvntsrgr lvdedalvkv lsqeriaaal dvferepqvd prllampnlv alphlgsaty
      301 egrgaaghki vtnirswvdg hrppdmvlpa pa
//
LOCUS       WP_285019805             222 aa            linear   BCT 25-DEC-2024
DEFINITION  complex I 24 kDa subunit family protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285019805
VERSION     WP_285019805.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Parey,K., Brandt,U., Xie,H., Mills,D.J., Siegmund,K., Vonck,J.,
            Kuhlbrandt,W. and Zickermann,V.
  TITLE     Cryo-EM structure of respiratory complex I at work
  JOURNAL   Elife 7, e39213 (2018)
   PUBMED   30277212
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Hirst,J.
  TITLE     Energy transduction by respiratory complex I--an evaluation of
            current knowledge
  JOURNAL   Biochem Soc Trans 33 (Pt 3), 525-529 (2005)
   PUBMED   15916556
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11112961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..222
                     /product="complex I 24 kDa subunit family protein"
                     /EC_number="7.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=24670
     Region          30..182
                     /region_name="2Fe-2S_thioredx"
                     /note="Thioredoxin-like [2Fe-2S] ferredoxin; pfam01257"
                     /db_xref="CDD:460139"
ORIGIN      
        1 madryiepdt pelrarwgnf awteanaaka kevvarypeg rqrsavmpll dlaqrqvgae
       61 entqgwlpip vmeyiaeyla mpvirvveva sfytmyniap igrfhvqvcg ttpcmlrgsd
      121 dllatcksrg mkkghisedg lwsftevecm gncasapmvq inddnyedlt sdrlnavlda
      181 largetpkag tqdparhtve pvgeptnlva mmtenhdyrs ew
//
LOCUS       WP_285019833             540 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285019833
VERSION     WP_285019833.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..540
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58059
     Region          2..526
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mtdrydalii ggghngltca fylaraglkv rilerrdvvg gaavteefhp gfrnsvasyt
       61 vsllqpkvia dmrladhgyr vierpisnll pqeggylklg gglertqaef rrfsahdaev
      121 lpayydaleg vaevlrdlal rtppevgggw ralvdaavqg rklaglsmea qrdvldlftk
      181 sarslldswf eseavkaafg fdavvgnyas pdtpgsayvl lhhvfgevng kkgawghsvg
      241 gmgaitqima kvcrdlgvei sleapvaqvl vdsgkvagvr lesgeeiaap riianvgpkl
      301 lydrmiaaad ldadfrrrmk gfkagsgtfr mnvalselpr ftclpepgeh hqsgiiiapt
      361 ldymdrafid akqfgwsrkp ivemlipstv ddslappgqh vaslfcqqfa pelpdgrdwd
      421 meedkaadai idtveahapg frasilgrqv lspkglerkf glvggdimhg nltldqmwss
      481 rpvlghgayr gpikglymcg agthpgggvt gapghncahe viadsrgmal gfggmyrrfr
//
LOCUS       WP_285019883             330 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285019883
VERSION     WP_285019883.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..330
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=34826
     Region          12..316
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mglrtrftdl vgiehpivqg gmmwvgrael aaavsnaggl giltaltqpt pddlrreidr
       61 craltdkpfg vnltilpsvs pppyaeyrka iidsgvtive taghrpqehv edfkahgvtv
      121 ihkctavrha lsaermgvda isidgfecag hpgeddipgl ilipaaadkl tipmiasggf
      181 gdgrglaaal algadginmg trfcatveap ihervkqfiv dndergtnli frkfhntgrv
      241 aknsvsdqvv eisardgavf edirplvsga kgrtaletgd ldaglvwagq vqglihdipt
      301 caelvgrivr daesiivsrl agmvaekvta
//
LOCUS       WP_285019940             396 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285019940
VERSION     WP_285019940.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..396
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43131
     Region          4..393
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mtilkgirvl dcsiamagpf aaqrlgdmga dvvkveptsg ewqrhasagg atgnkinvsf
       61 lslnrnkrsl aidlkapegk avlldlvkda dvflqnyrpg vaerlgvdya tlsainprlv
      121 yvsmsgyged gpyrmlpgqd lllqgmsgam lsagsegtpp spagqylvda iaaysafega
      181 laalfhrert gegqlvqvnm ldaittiqmq elsvftvgnk pqarsaepha hsyirspygv
      241 fqtadgymtl amarfdtlar elddpffadm eeeregwtrr deifarlreh lirqptahwl
      301 dkfraadiwc gpvygyadlv ddpqikhngt fveydhpteg rvkvpgfpir fsrtpsaitr
      361 gaplvgehse ailreaglga kdiaqliesg vvrqha
//
LOCUS       WP_285019943             319 aa            linear   BCT 25-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285019943
VERSION     WP_285019943.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..319
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=33986
     Region          5..311
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(11..12,14,54..56,77,105..106,109..110,112..113,116,
                     120,122,130,132,134,136..142,144..148,166..167,170..171,
                     267..268,275,281..287,289..292,294)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(55,78..80,103,238,285,288)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240626"
     Site            order(79..80,107,156..160,178..180,183,208..210,214..215,
                     236..238,262..263,285,287..288)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 msdrprillt rrwpeavear lqarystaln gtdrplseae laqamrdyda vcptvtdkvt
       61 ravltvegrr aaiignygag fehidlaaar eqgiavtntp dvlteatadi altlllmasr
      121 ragegerelr sgawagwrpt hlvgqslsgk llglvgfgri aratakraea fgmriayhsr
      181 rpapdmpsea yfadlgdlaa qadmlslhap ggpethrmvd aallarmpah avlvntgrgt
      241 lideaalaea laarriaaag ldvyeaepnv hpalvelpnv vllphlgsat ieartamgmk
      301 vadnldrffa geplldpvl
//
LOCUS       WP_285019981             109 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285019981
VERSION     WP_285019981.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..109
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11182
     Region          2..106
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mnwlylvgai gfeiiatsal katdgftrvv ptavtvacyv aaffclsval rtipmgvaya
       61 iwsgvgivai sliglvvyrq qldapalagi alilagtlvi nlfskaagh
//
LOCUS       WP_285019988             375 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285019988
VERSION     WP_285019988.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..375
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40706
     Region          <38..375
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 malakhrsea lagrgsgrti lsldptnpai pairarafvf sdprsramvp liertapsea
       61 tvlvtgetgt gkelvaryvh alsdrrsgpf iavncgafse slieselfgh ergaftgamd
      121 arpgwfeaan ggtlfldevg dlpqslqvkl lrilqerevv rlgarkpval dvrliaatnl
      181 dlaravsggr fredlfyrln vvalpilplr erradilpla rhflelygtk igagrlelta
      241 gaeealfshp wpgnirelen ailratltci dgqitandla lhaldarpqt irpapeepsa
      301 elpaaaadqa imedrltplv arfleekqga lldrtienvv rtafsryegn qirtaaalgv
      361 trsvlrthlk nfgli
//
LOCUS       WP_285020062             819 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285020062
VERSION     WP_285020062.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..819
                     /product="PhoX family protein"
                     /calculated_mol_wt=86282
     Region          <74..158
                     /region_name="myxo_dep_M36"
                     /note="myxosortase-dependent M36 family metallopeptidase;
                     NF038112"
                     /db_xref="CDD:468355"
     Region          126..813
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mtemnpvtay tdgdvdtnes tqrslesmaa erysrrsamf rgagattmaf mgtsllaacg
       61 ddgeggsigg avsvsagssv atsagrvvtl tgtvsgngqd agwnqrtgpe valmgsgatv
      121 tfiapavaaa tdlvfqfsak pligdavtat ttvrvspavl gftavahsls dvamvpegys
      181 vtimtrlgdp iaagvsayan dgsdadfdkr igdhhdalhy fglsaagapd rnsstrglmv
      241 qnhenitety lhpagpsaap rplaealkei echgvsvvey vdggnrkwty kqdstfnrri
      301 tpntpmsfhg paagsaflvt ayskdgtagr gtinncangv tgwntnltce enyagyfrrd
      361 aaddakrtpa elaslrrngi tsrsgnysws tasstdtrft rwnatitgaa atddfryepn
      421 qygwvveidp ynptstprkr talgrfgheg afvriaagqk lgaymgddsr geylykfvsn
      481 etwaaadada tdrlavgdky ldagtlyvar fnadgtgtwl plvysptfpk rpasgtypey
      541 tftsqadicv ntrfaadavg atpmdrpewt vgnpvtgeiy ltltnsnnsf rpvtgtnaan
      601 prsyndpkgp snsaqtgnpn ghivrlredg dttsattfkw diylfgadst dadptnvnis
      661 glttandfss pdgayfsrst npsgqinplm wietddgalt drtncmllaa ipghvgdgga
      721 ytvnnagntq ntfvgakata anlrrflvgp veceitgidq tpdgrtlfvg iqhpgeggsy
      781 saptshwpys qdgstpaasv rprsaliait kndggvigl
//
LOCUS       WP_285020071             808 aa            linear   BCT 25-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Lactobacillus paragasseri].
ACCESSION   WP_285020071
VERSION     WP_285020071.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus paragasseri
  ORGANISM  Lactobacillus paragasseri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 808)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 808)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 808)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   4  (residues 1 to 808)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   5  (residues 1 to 808)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   6  (residues 1 to 808)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18941298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..808
                     /organism="Lactobacillus paragasseri"
                     /db_xref="taxon:2107999"
     Protein         1..808
                     /product="cation-translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0043169 - cation binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /calculated_mol_wt=88984
     Region          10..663
                     /region_name="P-type_ATPase"
                     /note="uncharacterized subfamily of P-type ATPase
                     transporter, similar to uncharacterized Streptococcus
                     pneumoniae exported protein 7, Exp7; cd02609"
                     /db_xref="CDD:319795"
     Site            order(301..303,365,383..385,412,466..468,511,514,517,536,
                     539)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319795"
     Site            order(596,600..601,603..604,629,632..633)
                     /site_type="other"
                     /note="putative cation binding site [ion binding]"
                     /db_xref="CDD:319795"
     Region          619..759
                     /region_name="Cation_ATPase_C"
                     /note="Cation transporting ATPase, C-terminus; pfam00689"
                     /db_xref="CDD:376368"
ORIGIN      
        1 mkdnfkqpig ltsaevdqrt kegkvnravn dqaktawqii kentftyfnl iflvlsillv
       61 ivgeykdltf lpviianmii givqelrakr vldklnvmnt tkiavirdgk eevipiehlv
      121 lgdvivlqtg dqipadgqvi sgtlrvneal ltgeadeiek dvgtelmsgs fvvsgkayar
      181 lekvgknsyv skltleakam nskegsemvr sinrlikwvg iiiipcgial fivaryvnhl
      241 nladsvvsme aavigmipeg lyllttiala laamrlarsq vmlhdmksve tlarvnvlcv
      301 dktgtitepk mevekiipvn tnkddlakni svfaqnmphd natikavana fnqkaniqvk
      361 kiipstsvnk ysgavvgest llmgapefvl rgqfkdyeke inkytsqgyr vlafakypea
      421 ledekqklsk evdllgyili snpirkearn tfkyferqgv nvkvisgdnp ltvarvakqa
      481 gikdadklid ateigegdye evvrkynvfg rvkpdqkkkl ikalqkngnt vamtgdgvnd
      541 ilamksadcs iamasgnsaa vqasqvvlld sdfarmpkvv degrkvvnni ersaslflvk
      601 nifsflmaif slvfamsypl rpaqialisa ftiglpsfll alennysrir gkfipnvlsr
      661 aipggitdml avsilvvadm vlalgrqeva ttatmllvav gmmvlyhisr plnkfrwtvl
      721 ggsflalvla viffhnlfal srisatavfl llvlffaeit ifrflskfad gvrevlvvyd
      781 qkgkdltlnd ikqayrkgrn lvnmpirk
//
LOCUS       WP_285020084             409 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285020084
VERSION     WP_285020084.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..409
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44232
     Region          1..404
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mfatqvfkgv rvlelaqfvf vpaagavmad lgadvikvem tegdpyrrlk itdgrqtasa
       61 nlamelnnrn krsvaidlkt aegrelllrl vetadvflts irpaalrrlg ltldvlrarn
      121 priiyahgng lgfrgeqadr agydascfwa rggfghmlsv pgqrptrprp algdhagamn
      181 vafgiasalf hrertgeats vevsllssam wilsadvtmg aalsdeqlak lanpgrhalt
      241 sayqtadgry lqlmfldper ywpelcrrld reillqdarf asvesrvehg eallealdea
      301 faartldewr gvfadwdapw evvqnlrelv tdpqgaands lfdvvvedgt pvtvvsgpvs
      361 fggsplppap rraptmgqdt aqilaelgls daqiegwaqs gvvagiarg
//
LOCUS       WP_285020105             591 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285020105
VERSION     WP_285020105.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 591)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 591)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..591
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=63790
     Region          26..558
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mnapafplgt ipttvsvgrr rlvnvrqrsl ltakarmlwi lavfmlvtvl aifrivylgf
       61 tgvgprqgdl admlipargd ivdrngvpla rdfrvyslwy npkamtegsa lihspeevta
      121 gllrifpdld rdeilaklra gkpaylrksl lpedankvha lgepalefpl eatrfypqgs
      181 maahvlgyvd sygkgkvgme eafndqlisp egrtghatls idfrvqsale delaramqls
      241 aakgaagvvl dvdsgeilal aslpsfdpnh vkptdmvisa eearngdvph gfnrvtnqvy
      301 elgstfkpit vaaaldagvv tdlskqwpat plhvgrftih dlhnygasln vpetlihssn
      361 tvtariadel ggvrlkktme algmnqrpyv elpakgfpiw asgewprlrt mtvayghgia
      421 vtplhlasay aalvnggiwr patlkklapa dvptgrrvft aatsarirql lrmivqygtg
      481 rkadapgfrv ggktgsaekp gvggyrhhsl iatfaaafpm dkpryvviam mdepqgtaat
      541 syqrtaawna apviqrvvpr igpllgvmpd etrdidttdl rplvpqgsdg e
//
LOCUS       WP_285020265             140 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285020265
VERSION     WP_285020265.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..140
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=14945
     Region          1..>80
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 misltprqqe lldfirayaa ehgglapslr vmqehmrlas kssvhklldl leqrgrirrc
       61 plsgwqvige papspaapvy mgidisgpgs dhtavvymrd rqivdraeva tcavcgeafc
      121 dhsdvafagl vgipaagapr
//
LOCUS       WP_285020267             217 aa            linear   BCT 25-DEC-2024
DEFINITION  XRE family transcriptional regulator [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285020267
VERSION     WP_285020267.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..217
                     /product="XRE family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23623
     Region          4..64
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          86..212
                     /region_name="COG2932"
                     /note="Phage repressor protein C, contains Cro/C1-type HTH
                     and peptisase s24 domains [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442176"
ORIGIN      
        1 madnniaafr krrglsqtel aeqigttlnm lgklergdrs ldqswlekig ralavaphel
       61 iapdvaveai aavsvlppta devvyiqkld lslsmgpgth iddwveaepv pfgldfirtv
      121 trtssdrlkl vtgigdsmyp tlnwgdvili dtterqlarq davywidlyg aaglkrlrtv
      181 gpgrvlvvsd npnvadqevd aadlriqgra iwlargi
//
LOCUS       WP_285020300             402 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285020300
VERSION     WP_285020300.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..402
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=43280
     Region          15..400
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mkrttgqdrs qtqnwrpatr airggtwrse mgetsealfl tsgysyddaa tvaarfqgde
       61 egmtysrlqn ptvamleeri allegaeacr tqatgmaamt aallcqlsag dhmvsaraaf
      121 gscrwlgdhl lprfgvdvtl vdagdtaqwe aairpntkvf ffetpanptm gvadlaaiae
      181 iakahgittv vdnafcspal qrplefgidv vaysatklmd gqgrvlagav cgseqfindv
      241 llpfqrntgp nlspfnawvv lkgletldlr akkqsenala lgkfmedrvp tilhpwldsh
      301 paqalamkqm dacgpifsfv ldggreqahg lldalklidi snnigdsrsl mchpastthh
      361 nmgpegream gigegmlrin vglediedlk edmdqalkav gl
//
LOCUS       WP_285020310             181 aa            linear   BCT 25-DEC-2024
DEFINITION  TPM domain-containing protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285020310
VERSION     WP_285020310.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Sirpio,S., Allahverdiyeva,Y., Suorsa,M., Paakkarinen,V.,
            Vainonen,J., Battchikova,N. and Aro,E.M.
  TITLE     TLP18.3, a novel thylakoid lumen protein regulating photosystem II
            repair cycle
  JOURNAL   Biochem J 406 (3), 415-425 (2007)
   PUBMED   17576201
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..181
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19060
     Region          51..>181
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mepvlkgmar skllialaap llavgcdgap agtpsdtaaa dvrqlgapiv qtgfvtdaag
       61 vlddaaeqrl tarlhaleqv thhqmvivtt pslggedilf ytvdlarrwg igrkghndgv
      121 vvlvapnerk vrisvgygle stltdprcke iieqdmlptf kqgdfaggle rgvdslvall
      181 r
//
LOCUS       WP_285020358             206 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Lactobacillus delbrueckii].
ACCESSION   WP_285020358
VERSION     WP_285020358.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus delbrueckii
  ORGANISM  Lactobacillus delbrueckii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Lactobacillus delbrueckii"
                     /db_xref="taxon:1584"
     Protein         1..206
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24346
     Region          18..202
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mrkiveyifc rdckkvyfyl hggplftlrn wqedpfatml yneqrnfilv nypivygngg
       61 isdyqflkey fweykrqnpn temvllgesy ggylaslfaa eyifrkiiai saftsiayqe
      121 lfsserswlk dylsenaldf ytlcrdnkvn trtifiigsr dsrvpyqqfl alpfmkkfkv
      181 nilpgfthre sgtrleyvvs likqel
//
LOCUS       WP_285020345             236 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285020345
VERSION     WP_285020345.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..236
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=24759
     Region          1..220
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtfkdqvalv tgasrgigea tavalaaega hvvltgrdtk alerveeriy eaggsatiap
       61 vdlvepdgia rlasavqdrw grldvlvina ailpeltsva didqrafnka lttnvlstqa
      121 lianfdpllk kspnarvvgl tttvaqapra ywgaygatka afevlldcya qetaktsnir
      181 iaivnpgatr tamraraypg eapasvkppe vvadrltall gesfatghre tvnqpq
//
LOCUS       WP_285020508              75 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285020508
VERSION     WP_285020508.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 75)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 75)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 75)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..75
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8011
     Region          10..72
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mgdetegtni vvklddllha rrmtltelae rigitlanls ilktgkakai rfstleaicr
       61 elgcqpgdll gydap
//
LOCUS       WP_285020600             338 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase family protein
            [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285020600
VERSION     WP_285020600.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..338
                     /product="zinc-dependent alcohol dehydrogenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=35237
     Region          5..337
                     /region_name="MDR7"
                     /note="Medium chain dehydrogenases/reductase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cd08276"
                     /db_xref="CDD:176237"
     Site            order(43..45,48,146,150,171..176,194..195,199,214,
                     239..240,242,261..262,284..286)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176237"
ORIGIN      
        1 mtenrryvit pgqgiaglrq ervamprpgr gqvllrmraf slnfrdllmi dghypggapd
       61 aivplsdgag evvelgegcs rfavgdrvcp ifmqswiggd mtdadgasal ggaidgvlae
      121 yvvvdeaglv aipahmdfaq aatlpcaavt twnalygrep itpgstvmal gtggvaiwtl
      181 qlakaagarv vitsssdakl eratamgadh vvnyaatpew gaaaraftgg rgidkivdsa
      241 gpgtmpqsls alrrggeiam vgviapgtid plailvggal vrgvmvgsrr hfedlgrale
      301 ahrieplidr sftfdetaea yehlraaqdm gkvviemt
//
LOCUS       WP_285020726             521 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285020726
VERSION     WP_285020726.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..521
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54993
     Region          8..331
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msqqaridva aldalfapyd rtdapgfavg valkgipgyr rgfgmanvel pvalspsirm
       61 rigsttkhfc vlavmllaee gklaitdspr dyipelpawa dpitieqlma htsgmrdsld
      121 lifstagpgv aadagfqldl lagldsvnap agttwnynng gyvllteiaa rvsgmpfadf
      181 lrtcildpig madtllrpld tdllpnsatq hlprsdggws rgifgawigg eggivstvnd
      241 mlawlrhmsh pivgnaetwa qmrtprmthg yglglnmtkh rgldtvhhag gvvggssqml
      301 kvlgheldii lmtngrsald lyslvdaiid cciqglppap qdaacrlveg tfhsartgqv
      361 lslvghagqq avvmggmslp tkrdadgrmt vailptdlri lpvetdgvta lettefgvad
      421 hlapvtvpeg ttaapligry esraarlaad iridetgtar ivlsgplggt dylleplgpd
      481 lwravsptfs ppggtlefga sgflftsgrt vrlafersaq a
//
LOCUS       WP_285020758             275 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285020758
VERSION     WP_285020758.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..275
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31719
     Region          4..275
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mdadkiedie irllleaiyr ryhydfrnya qasirrrlrq arermgfatf salqdkllhd
       61 palaaqvlrf ltvqvsdffr dpsyfkalre kvvphlrtyp slkvwiagcs ageelhslti
      121 lfreeglekr tlfyatdins ealeaaergi yplerikaft enhrlsggrs slsdyyttgy
      181 ggavfdkslr ervvfsdhsl vtdavfsemh liscrnvmiy fdralqdrav glfrdsltrn
      241 gflglgskes lrfsahsadf adfvreekiy qrrka
//
LOCUS       WP_285020798             503 aa            linear   BCT 25-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285020798
VERSION     WP_285020798.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 503)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..503
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=52732
     Region          23..503
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mtltaadfpv elspgtwdvl rgdfpllidg kfvssasgaa gvthdpatga aladfalgda
       61 vdvdlavraa hkafggpwsk lshferarll rkladlfean tqvlaelevi dngmpmwlag
      121 ltarnnaelf hyyagwaeri egttttppah vlaagealty tlrepvgvvg qivpwnvpls
      181 maclklapal aagctvvlkp aeetplsavv lgrlimeagf pegvvnivng dgatagaalv
      241 rhplvskisf tgstevgkli vrecaddlkk vslelggksp vivfpdadma kavpgvamat
      301 fflqgqncma gtrifvhadi ydellegmaa fagsmkighg lhadtmigpl isakqkarvm
      361 syvdearagp arivaggkap egpghfvept ivadttpdmr vvreeifgpv mavqrfegdd
      421 ldaiaamand sdfglsgsvw tqdlstahkm aarvrsghvs vnthgavgan ipfggfkqsg
      481 wgrefgregl dlyletkavt val
//
LOCUS       WP_285020810             485 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285020810
VERSION     WP_285020810.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..485
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51710
     Region          42..485
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mtmdrrsftl gmakgaigvg maamlpaaar gapakkaaag ldvlvlgagv sglqaawmle
       61 eqglkvavle grqrvggrvm tlldepgype mgfnsmgegy grgidaaqra gvtlediggr
      121 yrvgkppmlw mngqpltree warhpgnpfp damksvlpae mvnkllaert plkdwnawtd
      181 pasavldvpl hdflraqgls dtairlandv spyygtnswd vsalmlefnd gfvkaqfeag
      241 tksfgvkggn lhlpmgmakl lkgdvilgke vvaieatdsg stvycrdgst fsarrvicsl
      301 pfstlryvki lpglsgaqae avsqiayqpl smafltatap fwdedglspg mwtdglagtv
      361 ipqhygatpe evtgllvqar gglanywdrl grdkalamiv aqieamrpaa kgklvartyf
      421 swsqevfngg dwayfgpgqv srlvpemskp agrlhfcgeh tatgargleg alesaerval
      481 evlea
//
LOCUS       WP_285020849             318 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285020849
VERSION     WP_285020849.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..318
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33412
     Region          3..300
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 meiltgflgs gkttllnrml sdgafrdtav vvnelgeigl dhllvetapg qvalleggcl
       61 ccavvdslpe tlldlvrrra ggdlprfgri viettgladp gpimevvrrs pllahflslg
      121 vvvtaldmlg gqgqverhpe alrqlvladr lvltkldlrg plapeecvwi aganpladvv
      181 tasdvladpa lllapsrgar pavtddhaah shgvrawsfp lgepvtrsgl aafaaaldhr
      241 lgadllrckg lartrgrlll vqgvgarfsv teappsaaea gphltvivqr reageiaall
      301 pwlhvpegtm ppskedlq
//
LOCUS       WP_285020885             822 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285020885
VERSION     WP_285020885.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 822)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 822)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 822)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..822
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87415
     Region          10..776
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mrrilvtssi lalsiasgna ayaqaaddta apggsdivvt gsrgqartva tsptpidvis
       61 geqiaqlggs mqlrdvlsql vpsfqsqqvg ssswnsvtrp aglrglsgvh vlvlvngkrr
      121 hnsalidlns gstsmggnpv dldqipasai arievlrdga aaqygsdaia gvinvilksn
      181 pdagsgsiea gqrykdsvng sdgetvsaql skgfhlgdng sivvsaeakr qkatvrnsdy
      241 tgtiysking atnprdatgd krryqgglpd lksvnlaqns eiqagdltly snatfgyrea
      301 rvgqagrypy stsdiveiyp dgftpyytma etdwqatagm kqtvdgwnld lsttygrdyv
      361 rsgadntlna slgtssptsf dtfsaafdqw ttnfdvtkgf evlggrnlqv sagaefryes
      421 yvtksldtas wqnggyvypt gsalagqpga igaqgatvit padeasaqrt igaayidlal
      481 dltdrllvtg agrfetydds sgsvwsgkvs alwkatdwln frgafsngfr apslsqqaya
      541 qtatqvslvn gsyqlieski lqtgsaiaqa lggkdlkpek srnysfgvtl tplagftltv
      601 dayqiniddr itltgllssa gvrqilrdng fsgdqyvrff anaidtrtrg idavanysft
      661 lgdfgnvras aaynynktki thiadnpeel anlgltlfdr qtqgyftvft pkdkiilgln
      721 wskgpfsvna ketrygswka lanlvngqpt adqsygakwi tdvevgfqvt eklklsggay
      781 nvfntypdkn tvpntigssp ygsnspfgay ggyyygrlsf df
//
LOCUS       WP_285020948             116 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: c-type cytochrome [unclassified Novosphingobium].
ACCESSION   WP_285020948
VERSION     WP_285020948.1
KEYWORDS    RefSeq.
SOURCE      unclassified Novosphingobium
  ORGANISM  unclassified Novosphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 116)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 116)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 116)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007442
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="unclassified Novosphingobium"
                     /db_xref="taxon:2644732"
     Protein         1..116
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12226
     Region          15..113
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
ORIGIN      
        1 mslfvaiapa saqtanaqag krlfmrcqac hstaagqpnk vgpnlngfig kkaasrpgfr
       61 yspaltkssv kwddkslnaw lerpsklvpg ttmafpgiak pedraaliaw lktatk
//
LOCUS       WP_285020996             397 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285020996
VERSION     WP_285020996.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..397
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43375
     Region          8..382
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 malndsitap sgplaglrvi dltsvvfgpy atqimadmga evikveppeg dntrwittgp
       61 vpgmggiyvn vnrgkrgvml dlrqeedres lraliatadv fihsmrgkai aklgfdyesl
      121 rairpdivyt ncygysrrgp eadkpayddt iqaecgiphv qglmngepgy vatimadkva
      181 glhalyatmm alfhrertge gqevevtmfe amssfmlveh angamfappt tpahyhrave
      241 pnrrpyktkd ghvaalvynd khwnafvaav nppwaseefa tlaqrakqig rvygllgetf
      301 ltrttqewld tlqalhipca rlqstdelfd nehlnaigff eeveteqgpv rfpgvptwfs
      361 ktpgkvrgpa pmlgqdnael ltkvassvap aiagesq
//
LOCUS       WP_285021147             270 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Novosphingobium
            sp. fls2-241-R2A-195].
ACCESSION   WP_285021147
VERSION     WP_285021147.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..270
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28844
     Region          4..269
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mphplgiell tvlglgpveh vtlaadlgck avsmglsqlp erfnphgyap wslredpalr
       61 relkavladr giaisiaegl gvsaeldaae ragdmdifad lgalrvnavd mgaerarafd
      121 qlaalatmaa ergmefsief tpvftirslp ealeaveyig agkatvlidt mhffrsggtv
      181 rqvaqldpal ighvqlsdvp rkgdddymte amsgrmipgq gelplrefve alprgqvlgl
      241 evplmaaaas grdardyvge ivkrtrefla
//
LOCUS       WP_285021271             418 aa            linear   BCT 25-DEC-2024
DEFINITION  nitrate/nitrite transporter [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285021271
VERSION     WP_285021271.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 418)
  AUTHORS   Yan,H., Huang,W., Yan,C., Gong,X., Jiang,S., Zhao,Y., Wang,J. and
            Shi,Y.
  TITLE     Structure and mechanism of a nitrate transporter
  JOURNAL   Cell Rep 3 (3), 716-723 (2013)
   PUBMED   23523348
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   7  (residues 1 to 418)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..418
                     /product="nitrate/nitrite transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42978
     Region          34..403
                     /region_name="MFS_NRT2_like"
                     /note="Plant Nitrate transporter NRT2 family and Bacterial
                     Nitrate/Nitrite transporters of the Major Facilitator
                     Superfamily; cd17341"
                     /db_xref="CDD:340899"
     Site            order(44..45,48..49,52,84,136..137,139..141,144,162,
                     165..166,169,238,241..242,245..247,250,278,282,331..332,
                     336,340,355,358..359,362..363,366)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340899"
ORIGIN      
        1 mataffrpde dndvlapaqk pavgfwkagh tptliaafly fdlafmvwvl lgplapeisk
       61 tlgltpaqkg lmvalptlag allrvvngll vdrigpkrsg ainqvivitg lffawsmgvt
      121 sfggtlalgv ilgfagasfa ialplasrwy paehqgkamg lagmgnsgtv faalfaptla
      181 kmfgwnavlg lacipltvvl ciylalakda pnqpaprklv dyaallkqad awwlmafyav
      241 tfggfvglaa slpiyftdqf glstvaagyc tagcvfagsl vrpmggalad kiggvkalmm
      301 vyavaaialv gvsqapslia alglfvvaml algtgngsvf qlvpqrfqae igvmtglvgm
      361 aggvggfyla sslglakqft gsfapgflif aglavvalas vasvkgrwra twktgari
//
LOCUS       WP_285021313             409 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfotransferase family protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285021313
VERSION     WP_285021313.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..409
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=46581
     Region          110..356
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mkgrpigrre ednhtmatta tttehhlgya lveqamketg idsfdndswr egfdvftqsf
       61 negiakgwms eggiararnd tlhylrgrlk vsqylrenpe llqrpverpv fvmgvprtgt
      121 tlmsnllaad psrrspltwe iddpvppvts nallttdpra ttrlaqekaa leanpamgky
      181 yrgsavypne cvffmahdfk tlmieskgkl plykdfifsc dmtsayeyhk kflqvlqqht
      241 tgvwnvkkps hslwletifk vypdarviwt hrdpftatgs lcsvislshq ahmgridaew
      301 laedypwqaa ehanrimdfr dkygedkiid vhyadivedp vaatkkvyaa lgdewtaeae
      361 agvqkwvddn pqdkfgrhey klaqyglske aleplferyl srydvareg
//
LOCUS       WP_285021328             947 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285021328
VERSION     WP_285021328.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 947)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..947
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..947
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=103274
     Region          41..460
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          525..945
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mrvsliallv alapmplaak dkpapsaatg tvwafdrsdi pvdpdfrfgr lpngmryivr
       61 hnatpagtai vrmdveagsl despaeqgfa hflehmafng sqrvpegqmv pllereglaf
      121 gadtnastsf drtlykldlp rndpalidta lmlmretasn ltisqeavar ergvvlaemr
      181 drnswalrna idttrffypk slyaqrfpig tvetlnaada aslrafyere yvpahvtlvv
      241 vgdfdvaave agivrhfndw sakpaeqqps pgpvkakdka rtgvyldpal servtvqrng
      301 pyqdepdsia erretllrsi gydivnrrlq rlarsaeppf rgagfgtgdv fkaarstrii
      361 idtvdgkwra gleaagieyr ralaygfsaa evaeqvaqvr tgivnaaasa strsnamlta
      421 lalslvddem vpstpqsgle rferfapqit peavlaalkr ealtldapli rfqgrkapeg
      481 gatalrdawr evmrakidke aaadtaqfay tdfgpagqvl sdtrredlgi revrfangvm
      541 lnlrktdlek drvrvslaid ggdrlntren phatqlvpnl ddgglakhsr dsldtilagr
      601 svglglssaa asfdsrvttt prdleiqlql laalvtdpgy rpegevryrq ainnyfaqld
      661 atpasalaar iggilsnddp rfslgnvedy rhlsyaklkt dvsdrlarga ieiglvgdid
      721 edaaialvar tfgalparem afhgetgqpp rlfasdrsar ivrhtgpadq aliritwptr
      781 ddtdpveale lellervmrv eltdqlreal gkayspsass qlshewkgyg tfsvnasvdv
      841 aevpatraai rqvlddlrka pvsadillra rqpmieslan alksnagwma lvdhaqsqpd
      901 rierfqnare qllaltpadv qamaqryltp eaglevlalp kdvaepk
//
LOCUS       WP_285021333             288 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285021333
VERSION     WP_285021333.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..288
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32311
     Region          8..275
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mmvirsgdsl ndieldlive aiwrryqydf rdysrasllr rleraqahfg vahlsglldv
       61 ilhdsaslpv ligfltiqvs dmfrdpeyfr tiretviphl atwptikvwi agcangeefy
      121 slailfreag ledrtmfyct disrpalaka eagifdieri agfsrnyrea ggkgslsdyy
      181 tansnvarfd palrrravfa dhnlasdavf sevqlvssrn vliyfdralq dralglfaqs
      241 lppggflglg sketvafsae tecfsdfapa ekiwrrtthd vqeaafae
//
LOCUS       WP_285021402             460 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285021402
VERSION     WP_285021402.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..460
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=50061
     Region          17..378
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
     Region          365..>459
                     /region_name="DUF4175"
                     /note="Domain of unknown function (DUF4175); pfam13779"
                     /db_xref="CDD:463981"
ORIGIN      
        1 msntrkkrwr wpispetvrs vlsshsvlgl afaaiiylvc ltgtiavfap dlqrievpgt
       61 pvamhlseaa aaralteavr qtpsdssiyl tmpspakega tlvafkpgfe rnwavaedgt
      121 lspldaiwte fliylhiclh lprswggfiv gltgvallss lvsgilahpr vvrdafhlrl
      181 ggsrrlqead lhnrlgvwal pfhftlaltg allglstiiv aglslllyrg dmtrvyalfl
      241 dpppaidart vpmpdlaali aqararmaea aidsvmverp gradmrisvh grrprhlvvq
      301 devqfdaqga aiheehpkdm vvgtrvlsgi gqlhfgwfgg pvvrvaygll glalcvvtss
      361 gvtiwlarrr drgrpapqwe riwsavcwgq pvvlmltail afvypespla pawlilttia
      421 ivlcavmnrc sgeylarlwr rglvvasala avlylgraly
//
LOCUS       WP_285021407             775 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285021407
VERSION     WP_285021407.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 775)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 775)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 775)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 775)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..775
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..775
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=82214
     Region          37..722
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mkftnvlala avstvaiaqa qvaaaqetaa atgadseivv igsraqgrsk ldtaspvdvv
       61 tiqdlkqqgt telgtalans vpsisfprps atdgtdairp atlrgmspdq tlvlingvra
      121 htsaslnvng vvgrgsaavd lntipstalq sievlrdgas aqygsdaiag vvnlrlread
      181 hgggatvtyg iydtqidtar dsrhvtgest vtaagwqgik lgqdgfltvs geytkrnpts
      241 rgdvdprltt pvvdnrfgdp evesysvyvn sakplndtwe vyafggyqyr dsssaafprl
      301 dtaaavydld gflpkinths kdltvtgglr geiagwktdl nvsygrnrid ywtrdsanyt
      361 ygadsqtdfy dgasiydqwv agidfskqfd vfqslnvawg vegrresyei kagepasygy
      421 gtaypgatpg aqgfpgfstl nevnehrqng siyldleaqv tdkllvavag rgekysdfgs
      481 tatgklslry dfspafairs tastgfraps liqqyytsit sviqngnqiv tgtypstsae
      541 atslggkale aekstnlsag fvlrtggfsl tvdgyrihvr nqiglsenia vttipnvsaa
      601 rfflnglatt tkgidavany kivtevagtf dltvagnvnd ikvtkvpant alfarsrilt
      661 ieegtpgekv sgtvvwtgdt lgatarvtyy gdvlqpgtva tsdlhtgkha itdlelryqp
      721 kdapfnlalg asnlldvypk kvpatlnttg vtafpyyspf gfngrylyvr aglsw
//
LOCUS       WP_285021421             221 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285021421
VERSION     WP_285021421.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..221
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24254
     Region          34..217
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <153..218
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mrlsdflsqq gafdlsvmdn rpgrrrrtgi pgprrlpwet rkagelslva qaliveddvf
       61 wanrsrivta renplltrlw adtplklgvp almaiavrta fgriggvilt pksarhtdls
      121 aqyaafgpqf aslarefmle efdrdrqast aglqgvlspr evqcirliam grtdeeiadt
      181 mtiarttvry hfsnlceklg assranavyr aatlgllpsa a
//
LOCUS       WP_285021473             468 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha
            [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285021473
VERSION     WP_285021473.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 468)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..468
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=53812
     Region          40..>263
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
     Region          212..466
                     /region_name="SRPBCC"
                     /note="START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC)
                     ligand-binding domain superfamily; cl14643"
                     /db_xref="CDD:472699"
     Site            order(213,215,222..224,226..227,292,313,315,317,319,337,
                     339,341,343,345,355..356,358,360,368,370,372,374,402..406,
                     421..422,425..427,430)
                     /site_type="active"
                     /note="hydrophobic ligand binding site [active]"
                     /db_xref="CDD:176854"
ORIGIN      
        1 mnfqstprys hetgfvrypd aapgdpgaka pfidhggsvl saeryysrde aerewehmwt
       61 rtwqfaglth dlaevgdyfm idigresviv vrdgpgdegv nayfnvcphr gnrivsqrfg
      121 slgekgcfec dfhgwkfdrt gknveikdem lfrretiahr pglkrmrcgv wntlvfisma
      181 degislrdhl nvmiehmevf pldkfrvigd fettwdanwk taldafiefy hadevhpevi
      241 pfsathetqy dlydhglsrm ivpygfvsgr hedqdtvnpf lqmyvqffgg npddytdikg
      301 yeywkaladt krkwaarhgy tdffdqlddr rvtddwnyfv fpnitinyfa ealliqifrp
      361 hptdpeksfy raislnlpvp gtqecvvdia sigpeatstp gwdgserpdv repqtleefg
      421 avlaqdalrv plvqkgirsk afggillgds eirirhyhae idkylgrr
//
LOCUS       WP_285021502             292 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Novosphingobium
            sp. fls2-241-R2A-195].
ACCESSION   WP_285021502
VERSION     WP_285021502.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..292
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30653
     Region          1..292
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mtalrsflfi pgdsekklgk vdgcgadavi ldledavapa akplarrmva dflkarpree
       61 ravqlwvrvn pfdtgltead vaaiiagapd gimqpkidgp acvarlsall deaerahgia
      121 pgstrilpva tetpiapfrl gdfagagltr lagltwgaed lsaamgastn lgpdgawaft
      181 yrmvrsltlm aahaagvpay etlyvdfrdd aglrascrea raegwagria ihpaqvpgin
      241 asfapsaeel afarrvidaf aaqpdagtvg idgrmydiph lkaarrtldl aq
//
LOCUS       WP_285021504             188 aa            linear   BCT 25-DEC-2024
DEFINITION  HesA/MoeB/ThiF family protein [Lactobacillus delbrueckii].
ACCESSION   WP_285021504
VERSION     WP_285021504.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus delbrueckii
  ORGANISM  Lactobacillus delbrueckii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Lactobacillus delbrueckii"
                     /db_xref="taxon:1584"
     Protein         1..188
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21027
     Region          67..>179
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mnlatviesv gvravvqeln ekvikhlnge ldrkdlkisd qeliniiekf rslglittns
       61 ysdnskysrn isffewmdts dnvdpniyqe klqkakvavf gvggigsama eylvragvkn
      121 iklvdfdtve esnltrqtay vesdinkaki qacsdylkki dstvsvetvh cklqgqlilk
      181 rilmlkpi
//
LOCUS       WP_285021531             433 aa            linear   BCT 25-DEC-2024
DEFINITION  protoporphyrinogen/coproporphyrinogen oxidase [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285021531
VERSION     WP_285021531.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Pawelek,P.D., Cheah,J., Coulombe,R., Macheroux,P., Ghisla,S. and
            Vrielink,A.
  TITLE     The structure of L-amino acid oxidase reveals the substrate
            trajectory into an enantiomerically conserved active site
  JOURNAL   EMBO J 19 (16), 4204-4215 (2000)
   PUBMED   10944103
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440906
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..433
                     /product="protoporphyrinogen/coproporphyrinogen oxidase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006779 - porphyrin-containing compound
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=46929
     Region          13..431
                     /region_name="HemY"
                     /note="Protoporphyrinogen oxidase HemY/PPOX [Coenzyme
                     transport and metabolism]; COG1232"
                     /db_xref="CDD:440845"
ORIGIN      
        1 mkavvvgagl aglaaayrlq kagwevvvle aaaeiggrtr tfrkdgylle rgatqlstgy
       61 raylkladei glggqiaeca ntvmlmrggq lyeidgtrpi aalfskalsf rsklrmirgi
      121 rdylryrpkd vldvseawra dtetaeayce rrlnreifdv lvdplirtyt inrganvsal
      181 ewfsglanla gqrmlalrgg igsfpaalaa mldvrlstpv sqvrrdrggv lvtledgeti
      241 sadgcviatp lpqaaamape laeavgplda clkynravnv ylgyrrrtlt dalgvmvpta
      301 ehphiglvwf dhnklsetap dghslitcyf eegglndlqg cddavfgkma ddfvtrlfpe
      361 lagqldmvev vrwraaipnp apgiytqinr mkyllspsda iqlagdyftc tgqnsaihwg
      421 evaaanlign ipa
//
LOCUS       WP_285021633             313 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Novosphingobium
            sp. fls2-241-R2A-195].
ACCESSION   WP_285021633
VERSION     WP_285021633.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..313
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34418
     Region          41..313
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtdfalsrrg llggtallat glaagsmlgg agafarppkr plgiqlytlm tlldadfegt
       61 vakvakmgyr evetlgsfgr dpafvrdvfd rnglvspsqh imppglyevf ddgvagridr
      121 atferkfiea fdfdhvegli dacakqarpl gqkyivwqis wpsqlqsleq ikqliaalnr
      181 aaqaahdrgf qlayhnhdqe fkkvgpdvpy dliiegtdpd klkfeldlaw atkagvdpva
      241 yfkrhpgrfr mvhmkdvaad gsvrdpgtgl vdfrriipaa ekagiehffv eydvptdplr
      301 taadaqkyla plm
//
LOCUS       WP_285021639             127 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285021639
VERSION     WP_285021639.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 127)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007442
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..127
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12424
     Region          32..125
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
ORIGIN      
        1 mktfplaaaa laaagalaaa pafaapppag aqvfarscam chttntggan klgpnlagvs
       61 grkagsipgf ryspamakag vtwnaktlda flakpsgmvp gnrmgfagvk dpaqraalva
      121 ylaslpk
//
LOCUS       WP_285021653             440 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Lactobacillus
            delbrueckii].
ACCESSION   WP_285021653
VERSION     WP_285021653.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus delbrueckii
  ORGANISM  Lactobacillus delbrueckii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Lactobacillus delbrueckii"
                     /db_xref="taxon:1584"
     Protein         1..440
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47731
     Region          1..432
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mkkydyiiig sgpaanhllf klartdrtal viennlwggt cpntgcqpki flegavrpvl
       61 ntyyltgkgv kaaaqldwkt likrkkeiwa efraeerssi endqvdtvfg sgvitgphtv
      121 aaageeyegi niiiatgllp hhlevpgsey aisndeffdl delpkkavvi gggyvalela
      181 tilqaagsev tvlqkllrpf dqeyveklte imeergivih lntpvkaiak nsaayevtae
      241 ngqkfetdlv idasgrrpnv nglgleklgi kfdpvkgvav nehlqtnvps ifaagdvadn
      301 gqlnltpvaw vdsyhiydfv englkegvky pavatstfty pqiaqvgkre semsagdtvr
      361 rmklgstfas mgegdeeael kvifnqvgev vgaseisina gedinlfapl igrkdpaefa
      421 mnnlgfafpt lankldvlfr
//
LOCUS       WP_285021692             175 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285021692
VERSION     WP_285021692.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..175
                     /product="YceD family protein"
                     /calculated_mol_wt=18809
     Region          4..171
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mtpefsrlld vrqiegkhvr lspneaeraa lterfllvqi delvaeldls tsereggfrv
       61 eargtlkaei vqpcavsaed vpvsideplf frfvpmatdy apdeevelta deldeieyeg
      121 thvdigeava qslalaidpf ltgpeadtar kaaglgtped sgpfaalkgl klgge
//
LOCUS       WP_285021701             606 aa            linear   BCT 25-DEC-2024
DEFINITION  ABCB family ABC transporter ATP-binding protein/permease
            [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285021701
VERSION     WP_285021701.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 606)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..606
                     /product="ABCB family ABC transporter ATP-binding
                     protein/permease"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67325
     Region          2..594
                     /region_name="ATM1"
                     /note="ABC-type transport system involved in Fe-S cluster
                     assembly, permease and ATPase components
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5265"
                     /db_xref="CDD:444078"
ORIGIN      
        1 mppdtavrds narhdgwrtl lrflpylwpr dnpalrwriv wacvfivlst atqlvlpymm
       61 kwavdlmgtt gpkllqltml mvlgysagrl aqtgfdnlrn ivfekvgqda trqlaenvfg
      121 qlhrlslrfh larrtgevtk tiergtksid tmlyfmlfni aptvlqllvv avifwvnfgp
      181 glvaatalai aayiwvtrvi tewrtklreq mnrldgqals ravdsllnye tvkyfsaekr
      241 eeeryaqatr ayavaavkse nslgllnivq gvvinllmag alawtvygww rgnysagqlv
      301 fvqtyltqlf rpldmlgmvy rtirqglidm aemfrlldts vevpdapgap alvirkpsiv
      361 fddvvfgyep drtilhglsf evpagqafai vgpsgagkst iarllyrfyd plsgrilidg
      421 qdirevtqvs lrgaigivpq dsvlfndtig ynigygrdga evqeietaar gaalmglidr
      481 lpqgfetevg erglklsgge kqrvaiartl vknppilild eatsaldtrt eqdilttlhr
      541 vaehrtslsi ahrlstiada drilvlnegk laesgthsel lrhdglyaem warqaaeaea
      601 mieaae
//
LOCUS       WP_285021760             753 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Lactobacillus delbrueckii].
ACCESSION   WP_285021760
VERSION     WP_285021760.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus delbrueckii
  ORGANISM  Lactobacillus delbrueckii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 753)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 753)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Lactobacillus delbrueckii"
                     /db_xref="taxon:1584"
     Protein         1..753
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=84739
     Region          2..753
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mskyiemthe qvmaackkym tadqlafves ayqfaarahe gqtrasgqpy ivhptqvagt
       61 lanlgldpdt vaagflhdtv edtsvtnddi kekfgadvaf ivdgvtklnk yeykshkefl
      121 aenhrkmlia makdlrvilv kladrlhnmh tlehlrpdkq rriaaetldi yapladrlgi
      181 gtikweledm sfhymnpeay ykivsmmdak rseregyikd aidylrgtld slgikydisg
      241 rpkhiysiyk kmvnkhkdfn eiydllavrv ivptvkdcya vlgavhtkwk pmpgrfkdyi
      301 ampkangyqs lhttiigpgg kpleiqirte emhkvaeygv aahwaykrgn fqgvdekdgg
      361 aldigreile lqkdssdade fmeavhsdif adkvyvftpk gevyelpkgs vtldfayaih
      421 tqvgdhaiga kvndklvpld ykmkngdvvd iltqgnarps rdwaemvkts raknkirryf
      481 rdvdreesla rgkselvdll kenglsakdf ldkshidevl dhfsfktded myaaigfgnm
      541 savsiynrlt adlrrqqeee kqkqfeaqim sagqqaaass vvkkpapqkd daksktkgkk
      601 pdslvrvqgl edldmhfakc cnpvpgdpiv gyvtkgrgvt vhradcrnvv sadpavqgrm
      661 idvewnnide gkqasfnanf elfgynrqkl lgdvinrlna ltknitnvsa svneeniahf
      721 yitvevrnaa qlndimaklr dipdvydtkr tdn
//
LOCUS       WP_285021788             444 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Lactobacillus
            delbrueckii].
ACCESSION   WP_285021788
VERSION     WP_285021788.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus delbrueckii
  ORGANISM  Lactobacillus delbrueckii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Lactobacillus delbrueckii"
                     /db_xref="taxon:1584"
     Protein         1..444
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48315
     Region          5..433
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mknpydfdvl ylgsghgafd gagplaasgk kvavvegdmi ggtcpnygcn akitldtpvv
       61 lqrlaermqg vvsgnikinw salvahkqav ikplpnaigt gltqngvtii hgygkfqdah
      121 tvvvgektyt adkiviatgq rphridvpgt dlahdsrafm dldvlpkrig ilgsgyisme
      181 fatianaaga dvhvlmhhdr alrefhqpfv edvmadmtkr giqftpnaav talekttdgi
      241 lihygdkeql vvdwvldatg ripnveqlgl enigvkfnqh gilvddylrt nvaniyasgd
      301 vldklqpklt ptatfesyyl ykllsgqtta pidypaipst vytspriakv gvapeavkdd
      361 tnkvvhnhip ddwyhqtdqe tvgdsllvfd qehhlvgate ysaqaedain tllpaivyhl
      421 srdqmwqmah ifpaegaaaw hkir
//
LOCUS       WP_285021903             104 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285021903
VERSION     WP_285021903.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10648172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..104
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11610
     Region          9..62
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mtnnrgyngl trrqsqclal vnqgmtskei arqldlspst vdnhlreaiv rmgknnrqea
       61 ardfalahrq vdqserlpgd clpramslvr lddigpftvf ickn
//
LOCUS       WP_285022036             206 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Lactobacillus
            delbrueckii].
ACCESSION   WP_285022036
VERSION     WP_285022036.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus delbrueckii
  ORGANISM  Lactobacillus delbrueckii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Lactobacillus delbrueckii"
                     /db_xref="taxon:1584"
     Protein         1..206
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=22266
     Region          <52..200
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mltilrrihv knrkleqivt iveqvladyv alyrrigfsd qekqniinsi vailplivda
       61 adgkvpvvaa gglvdkrtvr aafdlgaegv yagtaflate esplaenikq dmlkydaddl
      121 lmfrapnsfy rslpgelpek llemdkqgks aaeiwaaagd yscllygmrd gdlsrgiasf
      181 glgissihsi dpvsvvvdrl nsgvia
//
LOCUS       WP_285022078             395 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Novosphingobium sp. fls2-241-R2A-195].
ACCESSION   WP_285022078
VERSION     WP_285022078.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..395
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42716
     Region          34..391
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 miggstaete larlspwddr apaiapaere armerarelt eklgadallv dagaslryft
       61 glpwgqterl vsmllapgrt pimicphfei gtleadlavp veirswqede dpvalvidal
      121 seigaktlai dpelpfhfae riraagtarl idampvvkqc rmvksaaela lmqqaksmtl
      181 mvqhaaaril rpgirqsevv rfidaahrrl gasgssfciv qfgeatayph glpgdralqe
      241 gqlvlvdtgc tvegyhsdit rtyafgavsg diqdiwaiek eaqqaafdav rpgepcesvd
      301 haaravlaka glgpdyalpg lphrtghgig lsihepayfv rgdrtllepg mcfsnepmiv
      361 vpgrfgvrle dhmyvadgga rwftepqari dklal
//
LOCUS       WP_285022079             406 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285022079
VERSION     WP_285022079.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..406
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43264
     Region          10..404
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 migivgggvv glcagldlle aghsvalidd dvrghaaswg naghiaveqv eplasmdmvr
       61 tlpsrlfmrg gplafppgam aqwvpfglsl laaarpsrfr agceamrplm aealpawagr
      121 verigvpell htqghfilwh gdeaartgqa awdaaetgta qvhpatsdei arlsalcrep
      181 iagavrfsgt aqisdlgdlr avlrcafveg ggtlmeakae validgrari agldadrvlv
      241 cagvrsraim eglghvvpmi aergyhiraq vresdwpadl pplvfedram ivtryrdtlq
      301 aasfvelghp dtpadprkwe rlerhvaqlg lpvsgpftrw mgcrptlpdy lpaigrstka
      361 nnlfyafghq hlgltlapit arlvaamigg tppviplapf diarfa
//
LOCUS       WP_285022156             216 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285022156
VERSION     WP_285022156.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..216
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=24355
     Region          <1..214
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mldwafasgf reseapmhpv tkslpkqpkn egrfaampyn kvpafvaslr trksfsrmal
       61 efailcasrs gevggarwee fdlenclwtv pkkrmkanre hvipltpsai riieraaalk
      121 lgdcplvfpg akrnmplsdm tlakllremk epytahgfrs afrdwvseet ehhgevaeaa
      181 lahvvkdkte aayrrgnlle krrllmngws afcepr
//
LOCUS       WP_285022264             114 aa            linear   BCT 25-DEC-2024
DEFINITION  Dps family protein, partial [Lactobacillus mulieris].
ACCESSION   WP_285022264
VERSION     WP_285022264.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus mulieris
  ORGANISM  Lactobacillus mulieris
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Choi,S.H., Baumler,D.J. and Kaspar,C.W.
  TITLE     Contribution of dps to acid stress tolerance and oxidative stress
            tolerance in Escherichia coli O157:H7
  JOURNAL   Appl Environ Microbiol 66 (9), 3911-3916 (2000)
   PUBMED   10966408
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 114)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   6  (residues 1 to 114)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Lactobacillus mulieris"
                     /db_xref="taxon:2508708"
     Protein         1..>114
                     /product="Dps family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          8..>114
                     /region_name="DPS"
                     /note="DPS protein, ferritin-like diiron-binding domain;
                     cd01043"
                     /db_xref="CDD:153102"
     Site            order(21..22,26,28..29,40,51,55,58..59)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:153102"
     Site            order(28,40,44,55,59)
                     /site_type="other"
                     /note="DPS ferroxidase diiron center [ion binding]"
                     /db_xref="CDD:153102"
ORIGIN      
        1 mkyqetkkvl nqlvadlnqm itvvhqthwy mrgrgfmklh plmdkfmddl neqmdvvser
       61 liaidgapfs tlrefadntk isdekgrwdr tmderleilv kdyryladly qkgi
//
LOCUS       WP_285022388             451 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285022388
VERSION     WP_285022388.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..451
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=48014
     Region          2..449
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 milladdepa fqrltagwlr slghevttvg dgdaarqafa qhgadvvlld lampphhdpe
       61 aglalipsfa papvvvmtgh adqplalkam eagawdflak pvdpdmlkvv veralerarl
      121 ardlaaakal ehsaedmglv gqsppmtslr dmirriapta lpvmvlgpsg tgkelvarai
      181 haaspragra lvpvhcgavp adlleselfg hlkgsftgah adrpglveta ahgtlfldei
      241 gempatmqvk llrfladgsy qpvgarevrr advrivaath rdlaaavadg sfredlyyrl
      301 kgvvlrvpal adrqgdiall arlflrrase gpasfvpgal dwleshgwpg nvrelrsvie
      361 caaalaprsa sgltigiadl afamgedrep vpntatlpps gqtlqdevta lerlriteal
      421 drtghnhtht arelglsrvg llkkmdrmgl r
//
LOCUS       WP_285022621             283 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lactococcus garvieae].
ACCESSION   WP_285022621
VERSION     WP_285022621.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443800
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..283
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32044
     Region          8..80
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          155..274
                     /region_name="Peptidase_S24"
                     /note="Peptidase S24-like; pfam00717"
                     /db_xref="CDD:425835"
     Site            order(197,235)
                     /site_type="active"
                     /note="Catalytic site [active]"
                     /db_xref="CDD:119397"
ORIGIN      
        1 msghlgnkei maenlqrymn kygldrndia eiagvsyftv rdwlvartyp ridkierlan
       61 hwniskadlv epeserpkpp tpiveeitki sskleeprqk ivldtakiql teqekviaea
      121 kkrerkilgl dskpiditkl pgympyepdk mgtapilgei aagynimaee nfdgmmpvsa
      181 eyagrddvfw lnirgqsmes lihdgsfglf ecsddiydgr igavmaedgd witvkriyhn
      241 ldengyllgl tlvpendecp tieineynpg riigtllevk qyf
//
LOCUS       WP_285022637             181 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Pauljensenia].
ACCESSION   WP_285022637
VERSION     WP_285022637.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pauljensenia
  ORGANISM  unclassified Pauljensenia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="unclassified Pauljensenia"
                     /db_xref="taxon:2908895"
     Protein         1..181
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20790
     Region          4..>47
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
ORIGIN      
        1 meigmelrar rralglspkd lslllavgeg vvadwesnhr qprdpdrlrg dlndirdlhd
       61 qlvseivdql eeteitnksl ietywtnday weidtyareh kipaslhnta aahaqqiiea
      121 kysttvsier altrkeilar ladildeqne ldlddpeesf tfdtldferi slehtlkerr
      181 a
//
LOCUS       WP_285022638             408 aa            linear   BCT 25-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Lactococcus garvieae].
ACCESSION   WP_285022638
VERSION     WP_285022638.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..408
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=42204
     Region          31..391
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mkkklitalm lstvvltaga pfaavkadst dskiaqqdsk ianakneaak aqsqvdsiqs
       61 qvstlkskqt smtkkvnelm aqqkeqsqqi qklsesiker ntaleaqars aqtdgsatny
      121 msavldsksl tdaiqkmtam atvaganksm ieqqqadqka iqtkladnqk kyaeatklqq
      181 eldaqanela tqeaalkvaq lnyqatvtta egkkqdllsq kaaaekaaek aaaaekaaaa
      241 ksvvaqqeka vaaapaasnp apstdntagn snpstptpip tpeptpdpep tpdpeptpdp
      301 gkpvnpghsg tnpypagqct afvwdyfggn mptymgnagd wvayansgpa agtiavfppg
      361 nqgaggvghv avvlsvsgsk mtviegnfng gwgttrecst agvsfirp
//
LOCUS       WP_285022774             108 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: type II toxin-antitoxin system RelE family toxin
            [unclassified Pauljensenia].
ACCESSION   WP_285022774
VERSION     WP_285022774.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pauljensenia
  ORGANISM  unclassified Pauljensenia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="unclassified Pauljensenia"
                     /db_xref="taxon:2908895"
     Protein         1..108
                     /product="type II toxin-antitoxin system RelE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0017148 - negative regulation of
                     translation [Evidence IEA]"
                     /calculated_mol_wt=12162
     Region          2..90
                     /region_name="RelE"
                     /note="mRNA-degrading endonuclease RelE, toxin component
                     of the RelBE toxin-antitoxin system [Defense mechanisms];
                     COG2026"
                     /db_xref="CDD:441629"
ORIGIN      
        1 mtytvvwtkn atkellkipk kqpllilswv qtnldgsesp ksvgdgkplq gtnnggrwrv
       61 gtyqilgkle devlelhivr vshrqdvykk lsiricrnys neaittvq
//
LOCUS       WP_285022780             421 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: phospholipase D-like domain-containing protein
            [unclassified Pauljensenia].
ACCESSION   WP_285022780
VERSION     WP_285022780.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pauljensenia
  ORGANISM  unclassified Pauljensenia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="unclassified Pauljensenia"
                     /db_xref="taxon:2908895"
     Protein         1..421
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=48287
     Region          68..420
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mrfprkrlis aetlglmkkt aigitiaqat aivtvhavdh mrkqrvpggr hgfptlepad
       61 iqiprgtvrt yteghslyad mlhaiqnatd hiyfesfiwr adewgqrfkd aliaaarrgv
      121 nvycvydgfg vlnqdprfyf fpdiphlwvr rfpairsgll tlnlrntgqd hrkilvvdst
      181 vgfvggynig npfanewrdt hvrvtgdavw elengfvdfw nhfkphrapq lpdtgakkwh
      241 aevtaafnap qrilypirgm yidaierats hilittayfi pdkeilqali aaakrgvkvk
      301 vlipeysnhi madwvarpyy gsllregiei wlyqhamvhs ktmsidgmws tigtanidrl
      361 smrgnhevnm qfhsrelaqh meeifdndlt tarqytigew egrnmltrit eyllhpfefm
      421 v
//
LOCUS       WP_285022802             741 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Lactococcus garvieae].
ACCESSION   WP_285022802
VERSION     WP_285022802.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 741)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 741)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 741)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 741)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..741
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=84152
     Region          2..741
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mpsepnltgd qvvklasaym nekdillvrk alqcasiaha eqyrasgepy iihpiqvagi
       61 laklqldaat vsagflhdvv edtnfiqsdl velfgeeian ivdgvtklgk veyksheeql
      121 aenhrkmlma mskdirvilv kladrlhnmr tlknlrpdkq krissetmai yaplahrlgi
      181 gsikweledl sfrylnetef yrirglmnek raarenlvee vieklnermk daqvdaeiyg
      241 rpkhiysiyr kmhdkkkrfd eiydliairc ltnstsdvyt tlgyihdlwk pmpgrfkdyi
      301 anpkangyqs vhttvygpkg pmefqirthe mhqiaeygva ahwaykqgrk akvdvheise
      361 tlnwinelve lqeqsgdsae efvkavqedi lgdkiyvftp tgavqelpag sgpidfayai
      421 htqvgdhatg akinermqpl nyvlktgdkv eiitsktsfg psrdwiklvk tnkarnkikq
      481 ffksqdkels ihkgremlqt elaengftpn qyldkkhlde vleklsyrds ealfaavgfg
      541 eisatsvfnr lteserrkve keklkgeseq lmkgevkren knknvmkirh dggvsvsgvd
      601 smlvhiskcc npvpgdkivg yitkgrgvsi hradcknvrs qedyekrlid vewddsqhlt
      661 keyvanihvy afnrpnllnd ivqvlsnttk slisinahpt kdkkmanihl sigiknlsdl
      721 tlivdkikmt pdvysvkrtn g
//
LOCUS       WP_285023041             316 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Lactococcus garvieae].
ACCESSION   WP_285023041
VERSION     WP_285023041.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..316
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33952
     Region          25..311
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mkiskfscqv alallvivvl sflylmlgdq nysfsqiwhe svvlhlrlpr llalvfvgil
       61 lsssgllvqs mtgnpiaeis tlgisggasf alalllvfnl stggwlgtvv aslgafiali
      121 tvavltvksk fqpmkvvlvg tsvglfatsl asiltfyskn mqsyflwivg sfsgitplkl
      181 eilmvvsvlf vsmvllfanq ikvlvfgeem atslgisvnr lrllimvmva lasgvtvssv
      241 gvisfvglma phlarrlvgg hflkrfcmsn llgvllllva dllarnlfkp yefpagsltl
      301 lfgaiffiyv msqeek
//
LOCUS       WP_285023071             236 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Pauljensenia].
ACCESSION   WP_285023071
VERSION     WP_285023071.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pauljensenia
  ORGANISM  unclassified Pauljensenia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="unclassified Pauljensenia"
                     /db_xref="taxon:2908895"
     Protein         1..236
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25296
     Region          1..224
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 migglvgeql dartreqvld livekgpvta tviarilklt taavrrhiti lldskeimem
       61 epaqlkkrgr grparhyvat pnahtklpdg yselavkalg ylgqvgggea idsfaasrsr
      121 eierryapiv reagsdpkvr aqaladaltq dgyaatvrdi gnghfaiqlc qghcpiqeva
      181 gdypqlceae tqafsrlldv hiqrlatlag gghvctthip vgapvlrsas ratlrk
//
LOCUS       WP_285023110             254 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: phage antirepressor [unclassified Pauljensenia].
ACCESSION   WP_285023110
VERSION     WP_285023110.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pauljensenia
  ORGANISM  unclassified Pauljensenia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="unclassified Pauljensenia"
                     /db_xref="taxon:2908895"
     Protein         1..254
                     /product="phage antirepressor"
                     /calculated_mol_wt=28670
     Region          1..106
                     /region_name="COG3617"
                     /note="Prophage antirepressor [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442835"
     Region          146..239
                     /region_name="ANT"
                     /note="Phage antirepressor protein KilAC domain;
                     pfam03374"
                     /db_xref="CDD:460903"
ORIGIN      
        1 mgnqiqtftn dvfgtirtit ndgqilfcgk dvavalgyqd ptnavklhck gvanyhplet
       61 aggiqqvrfi tegdlyrlii ssklpaaqkf eawvfdevlp tirrhglyay delladdefl
      121 ehaiatlrae rvkrlaaeqa lleaapkvsy ydvvlqsdsl ltttaiakdy glsakklnri
      181 lrdahvqfhq sgrwflyarf aeqgytqskt heygegqtrt hmywtqkgrl fiydllknkl
      241 gilpviereg qvqa
//
LOCUS       WP_285023156             516 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: protoporphyrinogen/coproporphyrinogen oxidase
            [unclassified Pauljensenia].
ACCESSION   WP_285023156
VERSION     WP_285023156.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pauljensenia
  ORGANISM  unclassified Pauljensenia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Pawelek,P.D., Cheah,J., Coulombe,R., Macheroux,P., Ghisla,S. and
            Vrielink,A.
  TITLE     The structure of L-amino acid oxidase reveals the substrate
            trajectory into an enantiomerically conserved active site
  JOURNAL   EMBO J 19 (16), 4204-4215 (2000)
   PUBMED   10944103
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440906
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="unclassified Pauljensenia"
                     /db_xref="taxon:2908895"
     Protein         1..516
                     /product="protoporphyrinogen/coproporphyrinogen oxidase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006779 - porphyrin-containing compound
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=54098
     Region          18..506
                     /region_name="HemY"
                     /note="Protoporphyrinogen oxidase HemY/PPOX [Coenzyme
                     transport and metabolism]; COG1232"
                     /db_xref="CDD:440845"
ORIGIN      
        1 msakdrtiss tselsrdhwd tivigggiag lvsawesvka gqatllvesr gyvggqvasm
       61 mvgaahvdig aesfaprgta vtsmaeelgl kvtapgggrs hyflppvpds vqttwglhrf
      121 psgsmmgips npasaevrai lgaqgamrac edltlpphvg aecadvasfi earmgratld
      181 rlvrplvagi hsqdpekldv drvlpgmrad llhhkslaka vgarlekssg prgdvsiegg
      241 mqvlidalta eilakggmia trcgaeaicr tqvsssdsst vqwqvdirnt tpagapsaep
      301 rrtpvgrllt asrvilacsh apalrvltpl fpeaqecafa pgapivrsfl avragaldsa
      361 pvgpgllvsp dissvaecpv gakalsqldv kwawiadelr eahgehvhll rlsygrpgde
      421 drtpslgell hdasvltgtd lgaedvidhr vihwngtlaq atpnlarris alrqkaeslp
      481 gllicgawvs gsgiagvvad trqrvrgerr sflfdr
//
LOCUS       WP_285023251             792 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: bifunctional metallophosphatase/5'-nucleotidase
            [unclassified Pauljensenia].
ACCESSION   WP_285023251
VERSION     WP_285023251.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pauljensenia
  ORGANISM  unclassified Pauljensenia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 792)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 792)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..792
                     /organism="unclassified Pauljensenia"
                     /db_xref="taxon:2908895"
     Protein         1..792
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=80913
     Region          90..601
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mnkrrtmlig gsaafllals pvaalavptt dgasdepqsg vaagvtgaqs gaattlvdsd
       61 aegasapsap dstpatgapa lapangggvv eldlytltdv hghieqvtkk gtvkeaglaa
      121 mncylksarn knpnssftll gdnigaspyt sgslkdnpti aalntldpla stignheldm
      181 gqavfkqrvd gsntaefvqa sfpylganvr gmgswedggi skpylgdykv waspsgvkva
      241 figaiaqdvp yklspgttag lvfddpiari delaaqikqs geaqvviaml dddvknnypl
      301 vgknvdgimg gdthvpyefd kvdsaeklds knpllagvas gsytdnlgli risydmtvga
      361 vvkadtqlvp aakvaecgea petkaivdka vadskeagkr vvgtgyteaf rrgvfttpgg
      421 qtdpgsnrgi esslgdfvad amretittke grpvdigiin agglredlvp nddgtityaq
      481 syavmpfsne lgyvsitgad fklaleqqwk tnlnsqnsrp llklglsenv rytydperpf
      541 geritsvtvn gqpldeakty tvgsvtflla ggdsfdaltk ggpfvnsgnl drdkfneflt
      601 ahsgatprsl kssigvtlpk dpvkdgasft vglrglsfse gpsrtagvrv aaggkageaa
      661 vdnslveeha sdessvittd gagratvsvt avgacegkaa gevvstpvti dtdfgrvvea
      721 saglsvnvac agpgsnppsd ggaassastt gtssgktgks glartgfdgg svlvlvglfl
      781 gagavalttk rr
//
LOCUS       WP_285023303             349 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: threonine aldolase family protein [unclassified
            Pauljensenia].
ACCESSION   WP_285023303
VERSION     WP_285023303.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pauljensenia
  ORGANISM  unclassified Pauljensenia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="unclassified Pauljensenia"
                     /db_xref="taxon:2908895"
     Protein         1..349
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37670
     Region          6..344
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 makavftndy satahpqila dltafgmqkf pgygmdaicd eaeklildqc gipggavrfl
       61 aggtlindla idlflrpwqs viattdghia theagaiens ghrvhtipsh dglmdpgele
      121 atllewrdgg lrehvsasgl vyisqptelg tlysrerlta iseichsfgv glyvdgarlg
      181 yamgspandv tfadlatltd vfsiggakcg mmmgealvlp daskadyslr ammkihggla
      241 skgwilgsqf rtmfadglyl ritreatqra qriarafkda gfemlvdspt nqlfpilsle
      301 maedarerfa iekwapvadr lavrfvisws ttdedeaall qwiatssac
//
LOCUS       WP_285023304             412 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: M50 family metallopeptidase [unclassified
            Pauljensenia].
ACCESSION   WP_285023304
VERSION     WP_285023304.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pauljensenia
  ORGANISM  unclassified Pauljensenia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="unclassified Pauljensenia"
                     /db_xref="taxon:2908895"
     Protein         1..412
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43495
     Region          1..406
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 msylvgilav vggfiitvgl helghlvpak kfgavvseya igfgpkilsr evkgtlvvfr
       61 aiplggyvri lgmfapgrpg rrplnskgql tlaeqarhqs aqempegcah rafwrltwwk
      121 kaivmaagpa mnfllaflfl viamvgigfr tasltladvs ptiqtsagnv aspayeaglt
      181 ggdtlialng rdlfdwsdlr dsiassngqp lqvtferdgd lheaslyprk tedgtyvvgv
      241 tagyeytaas msdvakeyry mftgtvgamt kipqslwnvt msmvtgserd ssglisivgv
      301 sriagevtsd sagtgvadvr sqiafllslm aslnmalavf nliplppldg ghiigalyeg
      361 vrggvarvgg kpnpgpvdta rllpltwvmg allavmsivl viadivdpls lr
//
LOCUS       WP_285023314             393 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lactococcus garvieae].
ACCESSION   WP_285023314
VERSION     WP_285023314.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..393
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=45160
     Region          69..386
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mnikeitkkd gtiayrasvy lgvdsltgkq vrttataktr kqceikanqa inkfnkngct
       61 varervvfrd feelalswfe nykltvkens irvannqlkv yilpalglyk ldkintvllq
      121 givnkwarna ntatitngrr ekgnskdykl llnyikrild yamqlgains npakqvippk
      181 lkvrttqkik yfdndelkkf lmyldnlett aenqriatly klllatglri gealvlswsd
      241 infkdrylvv sktliqknnt aqnsaktkes nrtifldidt lqmlkdwrik qndgtiplrd
      301 clvfsyrkim kyysteretl ikhfkkadvp nigfhgfrht hasllmnndv npkeiqhrlg
      361 hsdygitmnt yshlakhkek dtaekfgnil kal
//
LOCUS       WP_285023464             396 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lactococcus garvieae].
ACCESSION   WP_285023464
VERSION     WP_285023464.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..396
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44722
     Region          69..390
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mkineitkkd gtvvyrtavy lgvdsltgkk vktyvtaktk kalkslsdlk vsefekngkt
       61 mlrekvefen fealanawld dylltvksns qammksyfkn yiipalgdyk vdkitapllq
      121 sivngwakra ntaslnkgrr ptgscrdykl llntvkrild fafqmgviss nparmvvapr
      181 lktrakkkik hlndtelkkf ldyldnleqt dknvfsitly kllldtglri gealalnwsd
      241 idydthiirv dktvdragka qdspksesgi rdisvsnrtm lmlkqwqnrq rvlyrkhkip
      301 trivfassvg gyrartniak elnahyknag ialtgfhafr hthaslllna gadykeiqhr
      361 lghakigmti dtyshlapdk aketasiyek alekls
//
LOCUS       WP_285023544             673 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Lactococcus garvieae].
ACCESSION   WP_285023544
VERSION     WP_285023544.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..673
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76876
     Region          437..666
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mnslvftaln aeqyifndyf qskyfkqeia tleealintq vnpnlpiqvt tedieeyrmt
       61 qpdkysqvsa ikedpvfler lndakaagdk taikkledqq nkklnevekl ftddkyvtek
      121 vkeqkkelia qqktdwmpqy kelssdihyq vteinsgkyl dnlsdnktfa taktlfkgnv
      181 sqinvddhnq fegqiiilkn snfnqrasvk sftemknlti gllctsilsf aafifywkkt
      241 ekgedillek vkswdkiald gqiflalils llylaltrea svtwsflpfl qkfcwaflvl
      301 ylfalvsggi yhkaqehgnw qqtylarsir llkdaadnfs rgskawfifw smgaaafgfl
      361 lammwggqgi vlylfvlviy lllisiyllr rltmfnqtvk iieeiaqgkn aevlnvkpkg
      421 ktvfrsvsen lktineevkt sksqqvkser lktelitnvs hdlrtpltsi itsvdllrna
      481 dlsqdekeky vavidqkskr lkvliddlfe vskmasgnmd lkksridlvq lldqslaels
      541 ekiedsslkf vtqtdkella lvdgdkmwrv fenlihnilk ysmentrvyi sghksekgti
      601 elvfknisre elgensqels qrfkrgdlsr nttgsglgla iaqsiveahe ghflletdgd
      661 lfkitlsfps lev
//
LOCUS       WP_285023595             555 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: bifunctional folylpolyglutamate
            synthase/dihydrofolate synthase [unclassified Pauljensenia].
ACCESSION   WP_285023595
VERSION     WP_285023595.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pauljensenia
  ORGANISM  unclassified Pauljensenia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="unclassified Pauljensenia"
                     /db_xref="taxon:2908895"
     Protein         1..555
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=59225
     Region          110..552
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 msndhpaffg dseeeavags ipadlipyle aadepdelal tdvtdhghda eetelqtalr
       61 nlvesslllg pdpsilaele gdidedfadd aeaaraehee alakaadsve ldaavakiye
      121 siverapehd iepsldrirm lldilgdpqn tfptvhitgt ngktstarmi davltafgvr
      181 vgrftsphli dvrermsieg apisreafia awndiapyve mvdtksvang gvrlsffevf
      241 talalvafad hpvdagviev gmggtwdatn lieagvsvim pidldhtkwl gstireiaee
      301 kagiikpgqi vviaeqpeea levlldrare vdaivrlegr dfevidrqmg vggqlvtvrt
      361 psatytdvfv plfgehqahn aaaalvgvea fmggraldak ivengmmtvt spgrlqvvrt
      421 sptilvdaah npagarvlad alddsfafah vvgvysamgd kdiesvlaem ephldsivit
      481 empgeraani eqlreiaidv fgedrvevrd slgeavdraa tlaeattdpa dkcgvvvfgs
      541 vvlaghmldl agirp
//
LOCUS       WP_285023880             567 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: peptidoglycan D,D-transpeptidase FtsI family protein
            [Actinomycetaceae].
ACCESSION   WP_285023880
VERSION     WP_285023880.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetaceae
  ORGANISM  Actinomycetaceae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 567)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Actinomycetaceae"
                     /db_xref="taxon:2049"
     Protein         1..567
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=59594
     Region          4..552
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 macairlvdl qiikaptlat egeavrtsqt giaakrgsit datgtilads iltyniavnq
       61 inlrsyvhse ttkengvekt kvvgrgpvea arqlapllhm seaelgglfl gdstytyvkr
      121 nvdavtyrei raldiygiew eatyertfpn gnvaapvigt vnaegvgssg mesqfntllt
      181 gtpgsqqyei apngaiipga kkttvepvdg gslqltlhad lqhlvqdmld arvehhkaew
      241 gtvvvedvtt geilvmadse stipdnanpq pvasvqyave pgsvgkvvtf aaaldagtit
      301 ptsvfnvpys ldlldaggpi tdfhehdget ltatgilaes sntgtvlvgq tlsneqrydm
      361 mkaigfgelt gvelagettg ilrppsewag rdqyvsmfgq sysvsplqet sfmatiangg
      421 vhipprlvks wtnadgtvet peepkptqam kadtaqnlml mmesvvedhl gtagaakvdg
      481 yrvgvktgta divvngqhgi vsttagllpv eaprlaisvv lynptvayis sdssaplfge
      541 vaqasvrnlg ipasttpatl fpttptn
//
LOCUS       WP_285023884             277 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: TrmH family RNA methyltransferase [Actinomycetaceae].
ACCESSION   WP_285023884
VERSION     WP_285023884.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetaceae
  ORGANISM  Actinomycetaceae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Actinomycetaceae"
                     /db_xref="taxon:2049"
     Protein         1..277
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28592
     Region          4..273
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mlanphaerv kkvaalagrs arrktnlllv egpqavrell afsgqhvrdv yftegaaslh
       61 pdvhalascv trwchtvtde vasvmspdaq giiavatrda lmsklpdsap rqtyvvlaqg
      121 rdpgnvgtii rtadamgcas vivvagtvnv aspkvirssa gsvfhlplvg vasfdeaaql
      181 lkargvhllg tsggvgiedl gqamtqaiae gagplassha wvfgneakgm sqaeldacdt
      241 lvridmtgqa eslnvasaas mclfasqcar lsnealk
//
LOCUS       WP_285023948             186 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: HIT family protein [unclassified Pauljensenia].
ACCESSION   WP_285023948
VERSION     WP_285023948.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pauljensenia
  ORGANISM  unclassified Pauljensenia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="unclassified Pauljensenia"
                     /db_xref="taxon:2908895"
     Protein         1..186
                     /product="HIT family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20444
     Region          47..173
                     /region_name="FHIT"
                     /note="FHIT (fragile histidine family): FHIT proteins,
                     related to the HIT family carry a motif HxHxH/Qxx (x, is a
                     hydrophobic amino acid), On the basis of sequence,
                     substrate specificity, structure, evolution and mechanism,
                     HIT proteins are classified into...; cd01275"
                     /db_xref="CDD:238606"
     Site            order(72,74..75,82,84,130,138,140,144,146)
                     /site_type="active"
                     /note="nucleotide binding site/active site [active]"
                     /db_xref="CDD:238606"
     Site            order(142,144,146..148)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238606"
     Site            144
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238606"
ORIGIN      
        1 msdveplved sreiagtpda fkrfwtpyrm ayingegkps dstdhtcpfc vapsksdeda
       61 livyrgrraf vlmnlfpyns ghllvcpyrh vadytdltde erievgelaa tsmrvlrats
      121 gpqgfnlgmn qgdvagagia ahlhqhivpr wlgdanflpi iaqtkavpql lsdarqmlad
      181 awpkes
//
LOCUS       WP_285024004             329 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: AAA family ATPase [unclassified Pauljensenia].
ACCESSION   WP_285024004
VERSION     WP_285024004.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pauljensenia
  ORGANISM  unclassified Pauljensenia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="unclassified Pauljensenia"
                     /db_xref="taxon:2908895"
     Protein         1..329
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35764
     Region          25..316
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 maptisaeei ekagellgrv sdifsskvvg qhdlkralmv glltrghili esvpglaktt
       61 aaqtlasavs gsfrriqctp dlmpndivgm qiwnqataem ttqlgpvhan fvlmdeinrs
      121 saktqsamle amaeyqttig gvnyplpqpf mvmatqnpie eegtyvlpea qmdrfllkqv
      181 itypqpreef eiltriesgq makpatgdpi sieelvglqd tvqkvfihdt lkgyivdlmn
      241 ttrgsgpvpl pawanhvrvg asprggialm raaqaialle grhfvvpddv kvmryavlrh
      301 riirtfdala dnvsveglid avfnavpvp
//
LOCUS       WP_285024066             224 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: potassium channel family protein [unclassified
            Pauljensenia].
ACCESSION   WP_285024066
VERSION     WP_285024066.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pauljensenia
  ORGANISM  unclassified Pauljensenia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 224)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="unclassified Pauljensenia"
                     /db_xref="taxon:2908895"
     Protein         1..224
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=24267
     Region          <14..209
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 masddikdls sgtlviglgr fgsavavtld klgyeilave knptrvqafa grfplveada
       61 tsiealeqlg ardfraavvg vgssleasvl itanlvdmgm psiwakatsr ehgrilrrig
      121 ahhviypefd agqrtahlvg grmidyieme kdgfaimklr ppkevhgftl adldlrgryg
      181 vnmlgllrpg mpfeyadatt rinpedviiv sgdarlleyf anrp
//
LOCUS       WP_285024159             361 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase family protein [unclassified
            Pauljensenia].
ACCESSION   WP_285024159
VERSION     WP_285024159.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pauljensenia
  ORGANISM  unclassified Pauljensenia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="unclassified Pauljensenia"
                     /db_xref="taxon:2908895"
     Protein         1..361
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40565
     Region          29..348
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mhlpqpytrd lssrdnalnl lrlalaflvv fshaqilagv gdgvvwqgqh lgswavvgff
       61 gisgflitga rtrsngaqyl mnritriypg fllslvavaf ifapiayyve rhsfdgffgt
      121 pttplhyiys nifllinhyd vsgtlasvpy psawngslws lyyefwcyii igvflswtft
      181 knhvwptill flvsvaihak igwflpyvgn sgdfqllifm lpyflggaii fqlrdrlpmr
      241 weyafvslil alvciygsdg fgkqaaspfm aylilwlgav lpspkliqvh disygvyifh
      301 fpvlqllilf gvhtmgfwfl lmvstlitgi lataswlgve ratmrwvrgk spwgelslaa
      361 r
//
LOCUS       WP_285020275             365 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA polymerase III subunit beta [Novosphingobium sp.
            fls2-241-R2A-195].
ACCESSION   WP_285020275
VERSION     WP_285020275.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. fls2-241-R2A-195
  ORGANISM  Novosphingobium sp. fls2-241-R2A-195
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Fernandez-Leiro,R., Conrad,J., Yang,J.C., Freund,S.M., Scheres,S.H.
            and Lamers,M.H.
  TITLE     Self-correcting mismatches during high-fidelity DNA replication
  JOURNAL   Nat Struct Mol Biol 24 (2), 140-143 (2017)
   PUBMED   28067916
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Paschall,C.O., Thompson,J.A., Marzahn,M.R., Chiraniya,A.,
            Hayner,J.N., O'Donnell,M., Robbins,A.H., McKenna,R. and Bloom,L.B.
  TITLE     The Escherichia coli clamp loader can actively pry open the
            beta-sliding clamp
  JOURNAL   J Biol Chem 286 (49), 42704-42714 (2011)
   PUBMED   21971175
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Georgescu,R.E., Kim,S.S., Yurieva,O., Kuriyan,J., Kong,X.P. and
            O'Donnell,M.
  TITLE     Structure of a sliding clamp on DNA
  JOURNAL   Cell 132 (1), 43-54 (2008)
   PUBMED   18191219
REFERENCE   4  (residues 1 to 365)
  AUTHORS   O'Donnell,M., Jeruzalmi,D. and Kuriyan,J.
  TITLE     Clamp loader structure predicts the architecture of DNA polymerase
            III holoenzyme and RFC
  JOURNAL   Curr Biol 11 (22), R935-R946 (2001)
   PUBMED   11719243
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Herendeen,D.R. and Kelly,T.J.
  TITLE     DNA polymerase III: running rings around the fork
  JOURNAL   Cell 84 (1), 5-8 (1996)
   PUBMED   8548826
REFERENCE   6  (residues 1 to 365)
  AUTHORS   O'Donnell,M., Kuriyan,J., Kong,X.P., Stukenberg,P.T. and Onrust,R.
  TITLE     The sliding clamp of DNA polymerase III holoenzyme encircles DNA
  JOURNAL   Mol Biol Cell 3 (9), 953-957 (1992)
   PUBMED   1358275
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Novosphingobium sp. fls2-241-R2A-195"
                     /db_xref="taxon:3040296"
     Protein         1..365
                     /product="DNA polymerase III subunit beta"
                     /EC_number="2.7.7.7"
                     /GO_component="GO:0009360 - DNA polymerase III complex
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008408 - 3'-5' exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=38876
     Region          1..365
                     /region_name="DnaN"
                     /note="DNA polymerase III sliding clamp (beta) subunit,
                     PCNA homolog [Replication, recombination and repair];
                     COG0592"
                     /db_xref="CDD:440357"
ORIGIN      
        1 mpiviesgql aramksaatv vergtqpila nvrlrtvdgm veiattnldv efrqlvslav
       61 pgeidttiea qkllaianaa egaqvkltqe dgrviaqagr srwvlpsles qwftelpfdg
      121 qsapvnigga alarifsrvg wsicteetlw wlcgvyvdpe ptangavmrf ttatkatfas
      181 visdvpwpeg aapitiaskc vrlmeglvad hdevaiawdk skiritagda qltgklidgp
      241 fpayrnaynf ateepvlvdp ealrkaikri eivgldksrs iavdvqegal evrpagngag
      301 easehvpasc qprhrsgfdg rllsealrcv ggdtveihqa spttsallrr avddgvmcgl
      361 gpmsl
//
LOCUS       WP_285024273             231 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: Maf family protein [unclassified Pauljensenia].
ACCESSION   WP_285024273
VERSION     WP_285024273.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pauljensenia
  ORGANISM  unclassified Pauljensenia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="unclassified Pauljensenia"
                     /db_xref="taxon:2908895"
     Protein         1..231
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=24502
     Region          1..222
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mrfllasksp arratlisag itpivrisdv dedlvladfc arsagvpspg dqvttladak
       61 cgavisglvd gtivideahc erllvvacds mllqdgqmlg kphtaeiare rirafrgsea
      121 ilwtghsval verdpstpld syaliartha ststivrfgs msdaeidayv dsgeplhvag
      181 sftidglggp fiagvdgdhh nvvgislplv htmaeevgvf wpdlwdhrqp r
//
LOCUS       WP_285024277             213 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent DNA methyltransferase
            [unclassified Pauljensenia].
ACCESSION   WP_285024277
VERSION     WP_285024277.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pauljensenia
  ORGANISM  unclassified Pauljensenia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="unclassified Pauljensenia"
                     /db_xref="taxon:2908895"
     Protein         1..213
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23088
     Region          12..184
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mlssfptans pfdahaeqwd sspvrgerar tvaseimrrl psgghwldig sgtgllglal
       61 sshadhvslg dtsqgmleva hrniadagln drmdalfcda eqwvsevpsq eydvivslma
      121 lhhmkdqrsv iralvervrp ggwvaladmd addgsyhadg divpahhgte ralveqllhe
      181 rgcqnilvst vmtisksgrd ypvflataqv arr
//
LOCUS       WP_285024284             886 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [unclassified Pauljensenia].
ACCESSION   WP_285024284
VERSION     WP_285024284.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pauljensenia
  ORGANISM  unclassified Pauljensenia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 886)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 886)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..886
                     /organism="unclassified Pauljensenia"
                     /db_xref="taxon:2908895"
     Protein         1..886
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=97852
     Region          20..869
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtaslnelld qleddgllkd pdalyeafts waastgrply phqeesflel ldgkhiiaat
       61 ptgsgksmia laahfvsman ggrsyytapl kalvsekffd lvalfgaqnv gmvtgdvsln
      121 plapiiccta eilanqslre gpsldadmiv mdefhyygdp qrgsawqipl leltkpqfva
      181 msatlgdtaf frhtwqertg rkvalidnak rpvplefeyv vdrlddtver llnedrwpvy
      241 ivhfsqkdai staqsfdkrt lisddqkkki kaelasvnfa kgfgqalrsl ltqgigvhha
      301 gmlpryrrlv erltqqgllp ivcgtdtlgv ginvpirtvl ltslvkfdgn kmrhlsaref
      361 hqiagragra gfdtvgyvrv lapeheieaa reraklsaaq eaardarelk raqkkqakkr
      421 kgpgdgtisw tkatftrlte eqpeqlrsqf smthsmvlnv lagaelarrd pgahlvelav
      481 gnddrpqdsn phlrrlgdiy ssllqagvve hvstaqalke hrprlraatd lpddfalnqp
      541 lspfalaaie lldpespsya ldvlsvvesv lddprpllfa qrsvakgeal aamkaegmey
      601 dermealesv twpmpladll epafatyvka npwvgnleis pksvvremve namtftelvs
      661 rydvgrsegv llryltdayr gmkqiipdda mtdeveaiid wlatliravd sslldeweal
      721 aegtasnpat qtvgnevafg adedgtiaft tnkhafrtav rkamfhrvel msrdaveala
      781 redadsgwde erwdhvlery waeydwigid qearstslce lnehpssadl evagaeadgd
      841 htywlatqtl ldpngdgdwr lvalidlves drqgsvaltl lsvgph
//
LOCUS       WP_285024311             605 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: AMP-dependent synthetase/ligase [unclassified
            Pauljensenia].
ACCESSION   WP_285024311
VERSION     WP_285024311.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pauljensenia
  ORGANISM  unclassified Pauljensenia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 605)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="unclassified Pauljensenia"
                     /db_xref="taxon:2908895"
     Protein         1..605
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65183
     Region          17..601
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mkklrdgsft vkpkfkvgah esvsslliar akkypkqvav eqrtpvglpq pvtaeellaq
       61 indvarglig qgihpgdava ilsstsyewm lldyailsig aitvpiyesd saaqiehilt
      121 dakvvqvftq trqqaelves vrtpsvrfid sidrgamrni ataalgieas evearririk
      181 ssdlatiiyt sgttgmpkgv clthanfvgt ayatrqvlgs vidspdtrll lflpvahvla
      241 rfvmhvvisg qgtlgfspdi knllpdiasf kpsvllvvpr vlekvynsaa akagkgikgk
      301 ifswsakqar swatskektl gpsplkrvrh svadtlvlkk irevlgpnmk yivsggapla
      361 sdlaqffsgl glkvlqgygl settgpacvq llnnhpagyv gpvlpgnyvk iaddgeillk
      421 gvsvmsgyyn lpdatadsfi dgwfrtgdlg tvdknlgvsi tgrkkelivt aggknvspev
      481 leeqlithpl ianivvvgda rpyigalitl dsdmlptwlk nhglpvvdaa qaadmpevrd
      541 slekavtran kkvsraesir rlriidqtft vengymtpsl klrrravlkd fahevdalya
      601 egqkk
//
LOCUS       WP_285024439             302 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Lactobacillus
            johnsonii].
ACCESSION   WP_285024439
VERSION     WP_285024439.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus johnsonii
  ORGANISM  Lactobacillus johnsonii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Lactobacillus johnsonii"
                     /db_xref="taxon:33959"
     Protein         1..302
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33815
     Region          1..289
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 makihllvnl ksgsnrgeka lkkietvlkn ekmdydihis nypgqlvpla tkvaneinsg
       61 teyvivvggd gslnqalngv knsdhpntpl ayfpagtgnd faraakletd slklirhlkn
      121 npiitkvdcg kyhdlinget ryfvnnlgid fdayvvnktn hsklktkfnk inignltygi
      181 nivqalkgqd nfkvrvstng htsyyehayl vtttnhpyfg gsvpilpias iynhqldiai
      241 vekpnlakfi ylfsklling shmkskqfhy fessaievkt ddpeydqlde eelskrkfhl
      301 kf
//
LOCUS       WP_285024491             288 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285024491
VERSION     WP_285024491.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..288
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30797
     Region          29..285
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          198..281
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtltatppas tidtfdrala slewtiqgtd rdrlaagtpl rrphtasgfv ylssgrvrlt
       61 aadgtrdlda gdlvffprah attvvaleda elldvaftpp gqrqqvaetl pehlyvadfa
      121 gqepsmvali agmgcpqaag rprpgdnvic sriattivsa alrtwneagc apdrwlqrig
      181 dphigavlda lhaepgrpwt fetlariamm srsafaerfr evvghtpray lttvrmetak
      241 gliltgdatv aelagalgyv sedgfarafq rytgltparw raeaalaa
//
LOCUS       WP_285024586             294 aa            linear   BCT 25-DEC-2024
DEFINITION  TolB family protein [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285024586
VERSION     WP_285024586.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..294
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=31536
     Region          46..182
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          156..290
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 mtfralapgq rssvllggpn ddapallfet dellleapnw sldgrtllln gngrlwaltv
       61 ddptagltpi efhglpelnn dhvlepdgeh illsamdghi yrgalsggpv tkltadddrw
      121 hflhgvspdg triayveleg fehpgrlaia pavegggpvt vldtgdghld gpewspdgrw
      181 llcntehfgt apghaqlari pdgggeleql vvsdtvdwfp hlspdarlas yiafpagtig
      241 hpadldvevr lvstddwatp lrryplfggq gtlnvnswsp dssrfafvay pitr
//
LOCUS       WP_285024631             365 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285024631
VERSION     WP_285024631.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..365
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37241
     Region          33..364
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtatprstsr prrvwviaav stavalaigl afrpgpstlp aeatgdaela asvrdlagpd
       61 rkallavvvt pdgtrtatig aqpdtrfeig svskaftgll ladaiergev tpdtrlgell
      121 elgdapaadv tleqlathts glprlpidls tilssawfal ttanpygedl dqlleqarsa
      181 sldtptgtys nlgfellgaa lgsaagtsya dlleeritgp meldatgpvs daadlgdrdl
      241 lgetaggrta aawtgtaigp aggirsdted larfaerlad gsapgieald pqaafgdrei
      301 gwawitdrka idgedlvwhn gatggfasfv gvvpatgttv iivsatqesv daagvalleq
      361 igaar
//
LOCUS       WP_285024661             369 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285024661
VERSION     WP_285024661.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..369
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39235
     Region          16..367
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mredgsvtds lhdisirgfa sdnysgvhpe ildalaaang ghqiaygedd ytrrlhevfa
       61 dhfgrdvavf pvfngtganv vglqsmlprw gavisastah insdeggape rvggiklltv
      121 dapdgkltpd lidreawgwg dehraqplvv sitqttelgt lytpeeirai adhahghgmk
      181 lhldgarian aaaalgvplr aftadagvdv lsfggtkngl mfgeaivvle psaseglvyl
      241 rklnmqlask mrfgaaqlia llepaadggd glwlrsatha namaarlrts lealiaagea
      301 pglgfsqptq anavfatlpa gvpdrlrerf rfydwdaakg evrwmcsfdt teddidafva
      361 aireelara
//
LOCUS       WP_285024702             371 aa            linear   BCT 25-DEC-2024
DEFINITION  lactonase family protein [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285024702
VERSION     WP_285024702.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..371
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=38393
     Region          7..371
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 msddnpylll gsytseadgt gagisllrqd eagtlrlvqs seaqspsflt lhptlpivya
       61 asestgavea fkrsgefgla pfgkpieagd svchvatvpg advliascyg dgrvvtvpla
      121 enaafagdpr lgeasvdpwa sptalaaesa dagedaltll aleaavgeal psrpsrahas
      181 allpdgriat tdlghdtvri wqlrgsrlvl dhtvvfprgt gprhlvvhps ghlhviteys
      241 veaftlgvdg tdghwhilaa tvatsegvse gdtgaeisla asreqlhvgv rgsdriatlr
      301 vtgdgsrvea vadvecggtm prhhresgrf lhvanqlsns iasfrldert gvpttllgtl
      361 dagsptclil a
//
LOCUS       WP_285024812             554 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Lactobacillus johnsonii].
ACCESSION   WP_285024812
VERSION     WP_285024812.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus johnsonii
  ORGANISM  Lactobacillus johnsonii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 554)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Lactobacillus johnsonii"
                     /db_xref="taxon:33959"
     Protein         1..554
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=65410
     Region          5..473
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(19,21,23,27)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(58,61,98,101,143,162,166,198,253,415)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(198,253,329)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          480..551
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; cl02706"
                     /db_xref="CDD:445893"
ORIGIN      
        1 mkwwqnsviy eiypksfydt ngdgigdlkg vekkilyike lgidaiwltp iylspqidng
       61 ydvadyrkvd pmfgnnddlk eliqkahdln ikiildmvan htsdqcvwfk eskkskdnyf
      121 sdfyiwkdpk pdgsepnnwa asfggsawty vpernqyylh yyasqqpdln wenptvrqyi
      181 ydamrywksq gvdgwrldvi tqiskdltfk daprvvnkky vplkntsgph mhqfihelnq
      241 evlqpfdmms vgeapnssik eildltspkr qeldmafsfe hmridkatke ngaltlkqpn
      301 flqlkqvlsk mqndlnnkaw nalyfenhdr sripsrwgdd tryryesata fatilhglkg
      361 tpfifqgeei gmtnpkysvd eyedidlknk yqeqvkeqhl lstdeflave hkiardnart
      421 pmqwnnekna gftkgkpwyk vnpnfieinv esdklskksi fryyqqlitl rhkeevltkg
      481 dyqellendk nifvykrswk nknwlilvnm ternlslnrl hndlknykki ilhnyphkkl
      541 edtlrpyeay ilek
//
LOCUS       WP_285025001             676 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285025001
VERSION     WP_285025001.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 676)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 676)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..676
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72652
     Region          48..293
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mtgilerpaa pgrpelhles drlgwlasgp ptqrgpgvvr rwlsrhgrtl afllpvlaia
       61 avvqamnlgg spqriddegt ytaqawsvlk lgelahytyw ydhpplgwlq iaaytgltga
      121 fdrydiavva areamlvatl iavvlvwvla rrlhlsrama avaalvfais plavqfhrtv
      181 yldnvavpwl lgafilatsr khqlvgfags aaafgiavls ketfllalpf lawtmwraar
      241 ketrrytlpv aativvvigf tyvlfaaikg elvpgpdrvs llggvffqlg srvasgslfd
      301 peslsaktls mwwqldaall vagavaavag lfisrlrvia amtvflglfm lrpggylpvp
      361 yvimllpfmt ilimgvtgaa irrfrrrstv eagaprrrll ggraagavwv aavlaaavva
      421 vpntatqlrg flladldkpv rqaqqwvqtn vpkesrvivd damwvdlves gfdrdnviwy
      481 ykmdtdsavq aqspngwrda dyivttdsmr tfpttfpevk gaidnselva tfgsgtqave
      541 vrridadgld aaaeqaagrt aaraalgaql llnpslsvsa eaaqtvsdgq ldsrallalg
      601 qvlattpvrl estpvldget gdvrrtmvlr tgteagdsrl adsirsiqgd yaadrveeta
      661 agvrvtysvv epdvvr
//
LOCUS       WP_285025027             398 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285025027
VERSION     WP_285025027.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..398
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41154
     Region          1..382
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtrivivgag ivgaacaril arrgaevvvl drsaaaggts gsgegnllvs dkgpgpeldl
       61 aryasrlwpv vtaelaaelg ptfpsiefer kggivvatte agaqplldfa aaqraagvda
      121 rpltedella aepsitrsst aavhypedaq vqpviateal lasarlagai vrtgvtvtgg
      181 vrsatgrltg vrtsvgdvsg davlvsagpw saelgdllga pvpvrprrgm vlvttrmphr
      241 vhhkvydgdy fgatqssdas lqtssvvest aagtvligss rqqigfdarl dvdvlrevaa
      301 kslrlfpflr dasvmrsygg frpymldhlp vigpdhrvdg lwhatghega giglalatae
      361 liaarllggs tdlddapfql drpglaphlr vdrpaeva
//
LOCUS       WP_285025184             277 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Lactobacillus crispatus].
ACCESSION   WP_285025184
VERSION     WP_285025184.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..277
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31637
     Region          5..264
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(29..30,32..33,36..37,74,78..79,82..83,121,125,132,
                     135..136,141,156,160..161,163..165,167..168,171..172,
                     175..176,202..203,205..207,209..211,213..214,216..217,221,
                     224..225,231,233)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(159,163,166..167,169..170,216,219..220,222..227,
                     230..232,236,238)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(180..187,204,207..208,211)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mhnesqvlgy qpgdsfiyql nattklvfml lvsvacmaty dtrfliaici lsiflfkeak
       61 ikwsqisfiv kfivvfmlln lifvfifqps ygeniyhsks ilihagyftl tlqevfylfn
      121 lflkyvcsip ivllfllttn psqfaaslnk igisykisya vslalryipd iqnsywdisa
      181 aqqargnels kkaslgkrik gtlnivmpli fssldridti stamqlrrfg skkkrtwyvt
      241 qsfkkadylv miaavilvli vvglwqldhg rfynpfi
//
LOCUS       WP_285025200             549 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Lactobacillus crispatus].
ACCESSION   WP_285025200
VERSION     WP_285025200.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..549
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=63481
     Region          3..456
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mvyvkkliln nfkgyknnai ftfnqnknil vgdngigktt ivqalrlllk gsryeyngis
       61 ylanyindev vnnfisskny lytnlpsfdl tvifgieetd qrnlkllrfc gnyqdsngsi
      121 krngygitfr ysfdedfkde ynelirdkdy knnfiipygm yktdhrtlsg dvyssrmdpl
      181 ksifidndsf egnpfnifar qiystlppkk rvqveskfgf innnlfddin rndlaeynlr
      241 idtnslkfds iidvtsgris ikelgsglen llktqlslnq dntdsahliv ieepenhlta
      301 sntrkqidql nninnqiivt thnsyivtgl dienliwike englkkqati kselseetke
      361 ffkrrddvdf lrlltakkii lvegaaeyil mrtfikkvck edrldfeils iggrhyqpfi
      421 dlakyannkm aiftdndadv ekpadkrink idddnkktes vkifcdqqtk nytfevseyn
      481 snksiienkf pvnpyaktsk hgdndvaskq laymlnnkte sahamlpnye kevyqipeyi
      541 vkglkwlke
//
LOCUS       WP_285025226             312 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285025226
VERSION     WP_285025226.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 312)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18950610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..312
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=33218
     Region          6..136
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
     Region          148..301
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mtttaiyaag avcwrlidgk vhllvihrtv ygdvtipkgk vdpgetlaqt avreikeetg
       61 lsvhlgvplg vstyplssgr ekivhywsae vtdqavrest fipngevaal ewvsikrars
      121 ylsyerdvei leafaalvde gvtatfalia mrhgkatpps ewsgedatrp laprgvkqaa
      181 gnvptllafg prkivtstav rcvstvspia aaagiepkrs dlisqdayer gesdvrrvvg
      241 rrvralktai lcshgpvlpe ilheialatg strgsylgsa aaletgafsi vhlsrtnpss
      301 giiaiethep rv
//
LOCUS       WP_285025285             290 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285025285
VERSION     WP_285025285.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..290
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31868
     Region          4..287
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mkepihsllt aldlsapgvr tdediftgps qwmpqgrvfg gqvlaqsvva atrtvdaeri
       61 ihsmhgyflr pgdvdlpitf avdrihdgrs fatrrtqayq ngvpilsmia sfqtqdegpe
      121 hqielpdgip apetlpsaae llsgidhpaa eawatgrpfd lrhvgspvyl rvegerttqq
      181 avwfktiedl pddpalhraa layasdytil epvlrrhgvp watpgikias ldhamwwhrp
      241 arvdewllyl qdspsatggr glslgriydr aghlvasvaq egmvrfptpr
//
LOCUS       WP_285025340             385 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285025340
VERSION     WP_285025340.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..385
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=41471
     Region          1..376
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mtqvlviggg pvglvsaill aqagvdvtvw errwdsptgt raigihppsl dlferlgvld
       61 eirrdavrid qgeawnagrr lgtvvfrdlp vphpyvaale qwrterilra rleavapgsl
      121 rtgtsctrlt paedgvlvsg ndadgtvstr aavvvvaagg raavdgmqap gpvhqyrdry
      181 lmgdvadrsg agsiarvhlh hrgvvesfpl phgmrryvvh tgysveqdaa rpeptasdla
      241 slvadrtgdd vdpatntmls afgvlrrrrk rvvdgrvvyl gdaaheispi ggqgmnlgws
      301 darvfaplia rmttghlstq hdvaaavsrq qrairraswq aelnmrlgrp lpgplvgird
      361 lalrtalngp vmpiladayt mrwlr
//
LOCUS       WP_285025317             459 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285025317
VERSION     WP_285025317.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..459
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48095
     Region          21..448
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 msddlipgde lsaadaadav yrellerlge aqpqprlgat kralellgnp essfaiiqia
       61 gtngktstar miesilrahg lrtglftsph lvrfterigi dgerisdeav arnwddikpy
      121 lamvdaelta agepaltffe altvlgfacf gdapvdvavv evgmggawds tnaadaevav
      181 ftpidldhvq rlgktiaeia rtkagiikpg aqvvsaaqhp darqaivdaa vavddpavfe
      241 geefalvqda vavggqlitv rgragtypel ylplygdhqg rnatlaiaav eaflggatqp
      301 iaedvlaegl tevaspgrlq ligteptvlv daahnphgaa slvaalgsyf dvdeiafvvg
      361 ilqdkdaagi lttlapaasg ffftqseser aipaeelsrl avsldlpast fadtldeaae
      421 darrwaeeap rrlvvitgsi tlvgeaieva ddrewkata
//
LOCUS       WP_285025375             423 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285025375
VERSION     WP_285025375.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..423
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43637
     Region          95..419
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mfdwllairl drpellvwva gaavvlaiil ltgrrtvrgw ltmllvasgg allayvtawl
       61 lgdvfdvfgi eltpvtrawa avgfagaala iaaivrtraw rvvvaslaip aflligaigv
      121 nqdfgefatv raalgispyq sfsalsaarg ttaswqrpad lpsggrvehv dipattsgfa
      181 hrdalvylpp aaltahppal pvieafsgqp gepadlfasa giagildrfa ashaglapiv
      241 vvpdqlgapd rnpmcvdgpl gnsatyltvd vpawisahlp vsasrtdwfi agfsqggtcs
      301 iqlgaahper yggildisge vvpsigptti aqgfggsata yeaaapsail aahtpyadtv
      361 gvfgygsdds rygpgvrria amasaagmrt ttfvsdgtah dwhtvhtvfe ralpviaarf
      421 gla
//
LOCUS       WP_285025392             414 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285025392
VERSION     WP_285025392.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..414
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44793
     Region          116..399
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtktktkaet ldwlrrisge latatlkrle dtlpwyaemp pgrrsavglv aqagissfis
       61 wfddprstpw iaadvfgaap rellrsvslq qtlqlikvtv evveervasg svdlreaill
      121 ysrdiafasa dvyaraaear glwdarleal vvdsilsgea ddelpsriaa lgwhghgeac
      181 vlvgttprvl dvdmlrrtar hldadvligv qgnrlvlvlg raelpsteag dgepvdeaeq
      241 aaadarassq ltfldiaakl ehgfgpghlv lghavpslie asrsakaala gfavakswrh
      301 aprpvaaddl lperalagdn lakttlierv yrplkdysge lvttlwcyld ngrsleatar
      361 elfvhpntvr yrlkrvsevi gwdatgares lilqaalilg aiaepepsrr rlts
//
LOCUS       WP_285025495             313 aa            linear   BCT 25-DEC-2024
DEFINITION  amidohydrolase family protein [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285025495
VERSION     WP_285025495.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..313
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34280
     Region          10..308
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mtavdpheir ildahhhfwd fdgpgyypwl qgeyndrffl gdytgmlhtf lpaqyreata
       61 gyrvvgtvhv eaersraqev desrfleglh rtdprfpaaa vahaslarpd vgdvlaehae
      121 iglvrgirsk pvtsataaea asidgapgtm qdpvwlagla qlelhgfswd lrvpywhled
      181 aaavvrdlpg ipvivnhcgl pldrseagld vwrrgmrala alpnttvkvs elglprnrwe
      241 rasnerivae tvevfgvdrs mfasnlpvat ltapsfgevl dtvlsglpga tgdeldqlfa
      301 rtaarvyrvt ldd
//
LOCUS       WP_285025604             519 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285025604
VERSION     WP_285025604.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18527136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..519
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=56395
     Region          16..>71
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          84..515
                     /region_name="MurA"
                     /note="UDP-N-acetylglucosamine enolpyruvyl transferase
                     [Cell wall/membrane/envelope biogenesis]; COG0766"
                     /db_xref="CDD:440529"
ORIGIN      
        1 medtatfert dpaaplrqvg alirgarqgr kltqaqlaer vgtsqsainr ieqgsqnisi
       61 dllsristal eseivsfgeq kknshlrvqg grqlhgtiav rssknasval lcaalmnrgr
      121 ttlhgiariv evdriidvlr slgvsvvwsp dgqdveihvp dnlsleside dagrrtrsvl
      181 mflgpllgry dtfalpyagg cdlgtrtvep hlialrpfgl sieatagwyq atvapdvpee
      241 lsvvltergd tvtenaimaa avrdgvtiir naspnymvqd lcfylellgi tiegigsttl
      301 ritgrsvine dvdywpsedp veamslltag ivtdseitvt rvpiefmeie latlgemglr
      361 ytrspeyaaa ngrtrlvdvt vhpsklhapi dkihpmpfpg lnidnlpffa viaacaegdt
      421 lihdwvyegr aihltdltrl ganvrlrdph ridvsgpthw sgaevscppa lrpavvilla
      481 mlaakgtsvl rnvdiiargy eqlqerlitl gasietfrd
//
LOCUS       WP_285025661              81 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein, partial [Lactobacillus
            crispatus].
ACCESSION   WP_285025661
VERSION     WP_285025661.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         <1..>81
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
     Region          2..>71
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 hecivivggd gslnqalngv ksslhpdtpl ayfpagtgnd faraaklqkd pskfirklrn
       61 qptvtkvdcg ryqdlitgee k
//
LOCUS       WP_285025669             965 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285025669
VERSION     WP_285025669.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..965
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..965
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=102164
     Region          <100..216
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          312..893
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 maarsnstsr srsasspsga ssrttstktn tkpgpksgas ttkqqktvay paaeeqrsvl
       61 tsmwlglahg vggavralgp eriakedrrd gfpfllflla vvgavvewfg aadpvaqtfd
      121 awsfgglfgr lafvlpvimi vfavwlfrhp asvddngris iglglllisi salchihggq
      181 pnpsqglpal aqaggllgwi lgaplaaiit pigatvlisl lillslfivt ktppnrvgar
      241 vrqfstwmfg eqpeapeget aepkgartkr lddldeepde paalpwwrrn tsrreddptf
      301 edplmgdnmt ellglekpsg gfdsplepva vpaaspkaap vhdafgsell gdleaaesav
      361 krfntgeikp qtglhddsip gateviedld pallgapdqi dfsarpmaqq gqddtpyrlp
      421 sagtlaagep akthsaande avaaitsvld qfgvdakvtg fsrgptvtqy eielgpgvkv
      481 ervtalsknl syavasnevr ilspipgksa igieipntdr eivtlgdilr staatnsnhp
      541 mtigvgkdvg ggyvvanlak mphllvagst gsgksvfvns mitsllmrak psevrmvlid
      601 pkrvelapya gvphlitpii tnpkkaaeal qwvvkemdmr yddlasfgyr hiddfnkavv
      661 aneivlpags ervlkpypyl lvvvdeladl mmvaprdved sivritqlar asgihlvlat
      721 qrpsvdvvtg likanvpsrl afavtsvtds rvildqpgad kligqgdalf lpmganksir
      781 vqgawvgene iqrvvehvtn qarpeyrkdv qavaerkeid adigddlell laaaelvvst
      841 qfgstsmlqr klrvgfakag rlmdlmesre ivgpsegska rdvrvtaeql pgvlarlrge
      901 ddgsaapvpa aaaptaaaaa ppvvgaaggl epdpygadpv eaqfqdypev eggsdedaws
      961 ltgre
//
LOCUS       WP_285025752             332 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285025752
VERSION     WP_285025752.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..332
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=35981
     Region          <68..289
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 meliywwmpl vwllavaavv aavllvartg rrrkasaepl wvahserlta lpgyrralsr
       61 yrrliiatia algvlllagt algsrvvstt vfqpelrnrd ivlcldvsgs mteydaalvg
      121 vfeklvqrfd gerialvlfn asattyfplt sdydyvaaql dhlvedltsp esdyeywngt
      181 dlgngsslig dglgscvmrf dqvgeersrs ivlatdnyva gepiltlkea gayakaqdvt
      241 vyginpgdvs skdylddlaa emdevvtstg gdyyaladpg avggivqqit aeqtktlkga
      301 kqlvqvdepf vfvlaafggl aalmllawrl rr
//
LOCUS       WP_285025764             270 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285025764
VERSION     WP_285025764.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..270
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29054
     Region          34..249
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 madeeqtqrr aqepsdqttv epstddtava pskpgvvyyf gravlnttak llyrpkiigr
       61 knvpkrgpvi lasnhlsfid siaipisapr rvqflaksdy ftghglkgwv srtfftsiga
      121 vgvergvgqa aqealdqgrr ilesgeafai ypegtrsldg rlyrgrtgva wlalttgatv
      181 vpvgligtdd lmpvgttipk fkpvtvifge pidvshhgpa tsgrarrkat deimaaihal
      241 tgqelanayn esppadaver ikralrperl
//
LOCUS       WP_285025783             606 aa            linear   BCT 25-DEC-2024
DEFINITION  polysaccharide biosynthesis protein [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285025783
VERSION     WP_285025783.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 606)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18500220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..606
                     /product="polysaccharide biosynthesis protein"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=65526
     Region          133..251
                     /region_name="FlaA1"
                     /note="NDP-sugar epimerase, includes UDP-GlcNAc-inverting
                     4,6-dehydratase FlaA1 and capsular polysaccharide
                     biosynthesis protein EpsC [Cell wall/membrane/envelope
                     biogenesis, Posttranslational modification, protein
                     turnover, chaperones]; COG1086"
                     /db_xref="CDD:440703"
     Region          296..579
                     /region_name="Polysacc_synt_2"
                     /note="Polysaccharide biosynthesis protein; pfam02719"
                     /db_xref="CDD:426938"
     Site            order(300,302..305,325..326,352..354,375..377,379,394,417,
                     433,457..460,463..464)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(326,328,332,336,350..353,356,359,377..380,383,387,
                     390,393,464..465,470)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187548"
     Site            order(379,419..421,429,458..459,465..467,470..471,
                     482..484,488,490,525,548,551)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(395,419,429,433)
                     /site_type="active"
                     /db_xref="CDD:187548"
ORIGIN      
        1 mtstlpdapr rwtqapgprf aaktaldalc wvlaivvaql vrfeleyerv alvgtvllcv
       61 iavvaqlvva ylwsyyhglh sfgsfyeakq livvalivta iliavnavfg vawgvprstt
      121 viafpfaivf mgitryvkrl fvdsrsrpie aqrvlvygag algmsiiprl mrdpqspylp
      181 vgvidddpsk rnfriasvav vgtgadlvaa vkrtgaqali isiadvdndf irqvserade
      241 aklrvlvvpp idtmlapgta esapslrdln vedfigrntv dlqvesiagy ltgkrvlvtg
      301 aggsigseia rqvnqfgpae lvlldrdetg lhttqlsisg hglldtkevv ladirdlpsl
      361 meifedrrpd vvfhaaalkh apmleqypde awknnvlgtl nvlnaaravg vgtfvnistd
      421 kaanpttvlg yskriaeklt awmsaqetda rylsvrfgnv igsrgsaipa ftaqieaggp
      481 vtvthpdvtr ffmtipeask lviqagaigd pgevlildmg rpvrildvak rmiaasgkdv
      541 eivytglrhg eklhevlidt deiadrskhp kvshtriqpl dpalldidvw retiadegag
      601 thhlvq
//
LOCUS       WP_285025799             222 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285025799
VERSION     WP_285025799.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..222
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=23785
     Region          5..184
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mhradplpqp tvrllrwasa aeldlagtaa rldpsardrl dtfsasaahr flfgrallvr
       61 tvaetigtdp erievtavcp dcglahgrpr vrtgdrtvha svshtadasa vavsiehpvg
      121 vdverldaar fagvedvalt ptereewrrl pdrrrlrala erwtakeavt kalgtglttd
      181 patidlgsga arhvietagh rfvidrpepa pgfvvatall lp
//
LOCUS       WP_285025867             475 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285025867
VERSION     WP_285025867.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..475
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=51138
     Region          189..>390
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mlstepappr ppaalttral vvrhvavfat favlagtfwt nlltiwgyta valvsggaal
       61 aclmvvrpnw rrtrvpwslv gygvlsivsl awsaypsgta atllgaalct ilgvtlagcf
      121 twpevirvlg ravtwvlsls llfefvvaai irhpvlpnfy agdsadppll dywsrdllfs
      181 ggriqgisgn anllavvall giivfglrla arrdepgaat ltgperrwtl lirlglsvvm
      241 fllsfsttil laavvtavvl aaalairrap rpeartpvyl gflgigvvga vgavvfrtql
      301 lgllgkspdl tgrldiwatv wrlieqrpvf gwgfsspwap weplftdlvi rrgvrqlqah
      361 nawldvwfql gvvglvlfaa vvlsmltrtw flavdrprvd ldarrpytal slapvliavs
      421 lvvqsvaesr lliesgwvll vllvvktkqe pawpvpavaa ssdlapahrr dvvdg
//
LOCUS       WP_285026015             342 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285026015
VERSION     WP_285026015.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..342
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35035
     Region          1..342
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 msttrdreta rpitgrrpar rtllvcaavv vaivvaaiag lalgdypltt devigvltgr
       61 vdglartvvl dwrlprvlaa igfgaalgvs gaifqtltrn plaspdiigl angsftgmli
      121 allllggswp almagsligg laaavaifll alrqglsgfr fivvgigvsa mlaafnswll
      181 lradldvalf aaawgagtln tatatvvwpa laclvvlfav lpfaarplrq lelgddvaaa
      241 tgvrltrera iliglavalv savtavagpi afialaapqi arrltrspgi plvatglvgg
      301 vlllasdlva qhlipltvpv gvvtvvvggl yltqlllrer rr
//
LOCUS       WP_285026055             460 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285026055
VERSION     WP_285026055.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 460)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..460
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50540
     Region          40..433
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(156,158,306,308,339..341,382)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mvdlsrraal allglglagt aiswprltgg dipgrgddal tvalfgtaqd aaarqslvdg
       61 fqklhpdipv riiaiqgqdw gnffakiltm vaagtppdiv svategtqlf aerlahpide
      121 yvqrdaaelq eyfddvnpsl iesfmykgnl fqlpdnfnaa nmyyntsafe raglerprdd
      181 wsvddffavg rtmqasapgs flpyfwnnrl wggvvpwlyi ndtsflteek apggdwmwsr
      241 fypdetprgg gylwenadal sdrtvesfev lqrmvsegia anpaqgggne lvslfsrgsv
      301 gmtpaggfwv kglndaglgn deydvtyfpk mrgqrhqfga ggyammqtse rkdeawewmk
      361 ycisvegmsi ahsqpdsslp rrslnaelyg gdigpkhwev fydtldrfpt tgpmpappqq
      421 aavesalikn vvgtitngpn gvrrgletmq rdlelalkgr
//
LOCUS       WP_285026090             220 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285026090
VERSION     WP_285026090.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..220
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23241
     Region          99..181
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 msilvrlcas tdlaaaaeal avafadypwt rhvipdddyp arlralqhly lshahqhgvv
       61 avvddgsgvi allppdapgp ddnvldqvma lhgdrldrla hrrssgddwt letlgvhpnv
      121 qgrgaggall elglaeatrr garavrlets sednvrlyer hgfrvtgrsd lpqgptvwtm
      181 ravmagegva apsaqdaatg isvdaesrng dgdalrvrpg
//
LOCUS       WP_285026133             585 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 35 protein [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285026133
VERSION     WP_285026133.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 585)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 585)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12015514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..585
                     /product="glycoside hydrolase family 35 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=63720
     Region          10..323
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
     Region          <525..561
                     /region_name="BetaGal_dom4_5"
                     /note="Beta-galactosidase jelly roll domain; pfam13364"
                     /db_xref="CDD:463857"
ORIGIN      
        1 mptfsigadd flldgqpfri lsgalhyfrv hpeqwadria kaklmglnti etyvawnqhs
       61 pergvfdttg vndlerflgl vadagmyaiv rpgpyicaew dngglpgwll hdpelglrrs
      121 eprylaavre yfgallpiva plqidrggpv ilvqveneyg aygddhdylr tltawtrelg
      181 itvplttvdq ptaqmledgs ipelhktasf gsrslerlat lrehqptgpl mcsefwdgwf
      241 dhwgehhhtt piaetaadld allaagasvn iymfhggtnf gftggandkg qyrshvtsyd
      301 ydapldeagh ptekffafrd viakyaevpt eippaatdap aftvsfeqev pfadvadeia
      361 plqafdript mdelgafsgl aryraslggr ggvlrfaevr drvvvsvdgv pvgaltrefk
      421 ersivipage tlelllenqg rvnygkrlge pkgiigpvsl dgvdltswgi apvaldrida
      481 vvdaaaarts datisgagpv lltatvtlge ptdlfldtaa wgkglvwvng fllgrywsrg
      541 pqhtlyvpgg qlragenrft vfefhalttp elsflarpsl gptef
//
LOCUS       WP_285026230             339 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285026230
VERSION     WP_285026230.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..339
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36353
     Region          4..339
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mdtesvarvi eatdfsgvvl vkrgeetlfe aarglasrer depitldtrf dtasitklft
       61 aaavlqqvda ghidldesih eyvdldgtti rrdvqllhll thtsgiadda detagesydd
      121 lwaerpassi retadllplf adkeplaapg eeanyvnagy vllglalegv tglpyrqlie
      181 qqvfallgmd hsgfvdrrtg epglaeggdv dddgvwhsna dafpplggpd agaqstaadl
      241 itflraarda kiltaeltee ftspqievde eisygfgfef dvdedgqvrs myldgvnpga
      301 sgivrtyfgp taadaidvvv lsnsedgawd viraidael
//
LOCUS       WP_285026256             307 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Plantibacter
            sp. ME-Dv--P-122b].
ACCESSION   WP_285026256
VERSION     WP_285026256.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 307)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..307
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=32602
     Region          3..291
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 marvlvtgss grlgrsvvqa lvdagsevva vdsatspgsp aastervdlt digscyavia
       61 khrpdavvhl aaiavpfsap ehvilrtntl lafnvvraav dlgttrivta ssptvigygs
      121 pagwtperlp ldervtpkpw nayalsklfa eqltasvaae rgddiavaaf rpcyvispee
      181 wrgaltqqgh tvheriarpe laapslfnyl dardagafvv rlleamggve naqsyfvgas
      241 dalaerplae llpeffpatt glaaeltgdr pafsigkaer llgwrpthrw rteltsstpl
      301 ldrletv
//
LOCUS       WP_285026259             523 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Lactobacillus paragasseri].
ACCESSION   WP_285026259
VERSION     WP_285026259.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus paragasseri
  ORGANISM  Lactobacillus paragasseri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 523)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 523)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Lactobacillus paragasseri"
                     /db_xref="taxon:2107999"
     Protein         1..523
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58567
     Region          44..496
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 melmistftl aiaaaisiii aqaidkvsvn yismiigiii glipflnqqi asfdseifme
       61 livapllffe gqktrihnvg rrikeiiglt iimvllaliv sgfsihllad vslplafiig
      121 sistptdata seavtnglrm prrvtsalka eslfndasgi illnmsllwf angyinygqt
      181 iqdfcissig gailgfavaw viiifrqtlv rsrfnslnaq nliyiltpla lyalaehlhv
      241 sgiiavvvag llhnaesqqs lllnsrqvhm sqdlqnlisd ifnsmvfiil glmmvrisrn
      301 klfngdlakw iivgiivyla nllvrylygr liirydrres ivfslggihg avtlalalti
      361 svdflgsqsy nlvimseavl iilsmlvpti vfqfilphnv sdeeahivmd kirsemvkra
      421 lvavhkmylp qrvkrhviyt llnqkrvvkt reyirvllkt idqpnlskse qylqrlaffr
      481 afaiereyle migqkegkyr tyilnlynnv llaesliiep ede
//
LOCUS       WP_285026263             305 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Plantibacter
            sp. ME-Dv--P-122b].
ACCESSION   WP_285026263
VERSION     WP_285026263.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..305
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32268
     Region          53..273
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 msatartpvp epvegrttph prlsvnqati kyatlpeava avtaagvtsf gawrepvqey
       61 gvaasasllt dsglrvsslc rggfftmpeg ptrrasiddn rtaideaaal gapalvlvvg
      121 glpagsrdll garelvrdai geltdhales gvqlaieplh pmyasdravv stlgqaldia
      181 eqfapeavgv vvdtfhiwwd pqvleqiara gatgrissyq acdwatplaa dvllsrhypg
      241 dgvidfgslt raveaagytg dievelfnqe iwdspfqqvv drtvdafqat vvphldhedd
      301 aihqp
//
LOCUS       WP_285026304             285 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Plantibacter
            sp. ME-Dv--P-122b].
ACCESSION   WP_285026304
VERSION     WP_285026304.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..285
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30686
     Region          2..281
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mriavtggsg klgrtvvghl rehghlvvnl dqagergdgf vridlrdagq vfdaltgvde
       61 qapdgfdavv hlsaipapgl stntatfqnn ilstynvfna aikagitniv tassetvlgl
      121 pfdtpppyip vdeayaarpe styslskhle eqlaieltrw hpelkiialr fsnvmdeady
      181 aafpsfdada tlrkwnlwgy idgrdgaqav rlalehqatg fdrfiiaaad tvmsrdnvel
      241 vaevfpdvpv tgdiagngtl lsidharevl gydpkhswrd apsap
//
LOCUS       WP_285026305             344 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Plantibacter
            sp. ME-Dv--P-122b].
ACCESSION   WP_285026305
VERSION     WP_285026305.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..344
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38460
     Region          13..329
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtdttdktya srlpvtlftg qwadlpfeev arlaaswgyd gleiaasgdh ldlkradedd
       61 aylrsrldil drhglevfai snhltgqavc ddpidfrhqa ivrdytwgdg daegvrqraa
      121 edmkrsarva rklgvdtvvg ftgskiwqys amfppvpaav idagyedfat rwnpildvfd
      181 aegvrfahev hpseiaydyw tsvrtleaid hrpafgfnwd pshmmwqgvd pvgfivefan
      241 riyhvdckdt rirpatghag ivgshlpwgd prrgwdfvst ghgdvpweda fralssigya
      301 gpisieweda gmdrlhgaee avgyirnllw klpeqsfdaa fstq
//
LOCUS       WP_285026385             202 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285026385
VERSION     WP_285026385.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..202
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20912
     Region          55..198
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 marrsrtfav aavlavgall ltacgsdpla dqyregsskg yvagdgsvte vavdergepi
       61 sfsgvgedge qissadhagq vlvvnfwyaa capcraeakd lqalneaytd qgatfigvnv
      121 rdtadtakaf ngtfgityps ildvdsgeak laftgsvppn avpttivlda egrvaarilg
      181 qlqdrtildt lirdtiaesa pe
//
LOCUS       WP_285026574             457 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285026574
VERSION     WP_285026574.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 457)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..457
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48520
     Region          38..444
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(155,157,283,285,319..321,365)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 msqkrlrrla vpaavvilav vltgcqganp sgggdgkkiv iasvnngpmm tmqelapeft
       61 ketgievefv mltendirsk iqqdvavngg qfdvvtlgts dagtyldsgw tvpldpmfek
      121 mdadekaayd eddliagtvs afssekqgma aiplygestm tmyrkdlfda agltmpaqpt
      181 wdeiydfatq lndpatgqvg iairgkagyg enmyihntiq yaygaqiadd dwnagydspe
      241 maeawefyrk lqkdagapea ssngytetln lmssgkaaiy ydatvsadvf egadsavagk
      301 mgyalspagp gkgntqtvgg wgigltsssk nqdaafkfmt wvtskdyvkl vaekkgwlnv
      361 ltgarastyq apeyqavapy aslvleslen vdfthpavgd tpyvgnslps ipewsgmgek
      421 igqilaeyis gsgstkdala naqkvatdaf vdggrtk
//
LOCUS       WP_285026713             309 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285026713
VERSION     WP_285026713.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..309
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32353
     Region          189..302
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 msaerwgrwy favqalagaa wwvsvflvpp vgaatlgsld pvvtavldvp lfvvasalaa
       61 fgirwaaila tawtllvtvs lgifaavtqe agigallmvg aavgsvtala llltggipra
      121 witigpfafh padatastgs qlrrtaveii vfwgvflavi pavlrffelr wqvaialppg
      181 aeqiadvagv ivsvlgsvvg lwsaaamatt gggtplpaam pnrlviagpy rfvrnpmavg
      241 sivqgvgvgl llsswvvvvy avfgavvwnv lvrpveeadl earfgepyrr yredlrcwvp
      301 slrpvsars
//
LOCUS       WP_285026873             266 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Plantibacter
            sp. ME-Dv--P-122b].
ACCESSION   WP_285026873
VERSION     WP_285026873.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..266
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28183
     Region          5..263
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 msapsvqlyt vrdaiaedlq gavariaeig ftkvepyafv eraaefetaf taagvtapsg
       61 hapvidtadp avafdaasrl gigtvidpfi ptdrwqtadd aarlaervne lavqaaasgl
      121 kfgyhnhnwe fsthvdgrpi felfveqlsp evvleidtfw stvggadtpa flrslgdrvq
      181 flhikdgiis gdiatalpss esalvvpdal aqafanqqpa gqgqvdipai laaaphatrv
      241 vefdgyskei fggvaesyaw laendk
//
LOCUS       WP_285027040             198 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285027040
VERSION     WP_285027040.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..198
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=20760
     Region          1..196
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(47,51..52,55..56,92,96,103,106..107,112,135,
                     139..140,142..144,146..147,150..151,154..155,170..171,
                     173..175,177..179,181..182,184..185,189,192..193)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(159..166,172,175..176,179)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mitlyrpgsg wlhrapagpk algilvvvla isllptswwt agiattvtvl aylasglglg
       61 elgrqvllir wiititvagq llfldvesav sntsrivaai llaallvlst rvadlldafe
      121 ralkplgrfg vdpsrialml avaintvpvl arlassvrea qrargagsnl vtfvvpflvv
      181 slkhadelge altargvr
//
LOCUS       WP_285027060             490 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285027060
VERSION     WP_285027060.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..490
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52295
     Region          1..317
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mslqrstpsa qhvdaagiea fitalehtpn vephslmvlr hgnvvaegww apysadrvhl
       61 lyslsksfts tavglaveeg llglddtiis hfpeldaeit dprsramlvr hvlamasghr
      121 eetimraaai dptnlvrgfl llppdedpgt vfaynqpcty taativqrvt ggtltdylrp
      181 rlleplgigd fdwqrddegf elgysglhat teaiaalgql ylqggewegr qllpaawvae
      241 atrshiangd dpesdwaqgy gfqfwmarhg frgdgaygqy cvvlpehdvv laitgqsldm
      301 qavlnaaweh llpafgageg gdsgrgpnsd adqallarla glalppldas detgagaslr
      361 elvgrtfaaa adtglaqlta levtagegdd vvlvvhegdd rvelvpgvga wrthgpivas
      421 aawgtggeeg arvlrvdaif ietphrlhve idpaagtfda wwettplrts rlaevqrpsa
      481 vvegggkssw
//
LOCUS       WP_285027067             262 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285027067
VERSION     WP_285027067.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..262
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26250
     Region          5..242
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mttqrssrfr aaladpsgpa lgtwvklpam esmelvalag fdfavidleh spmsletaaq
       61 higvallagv spivripsld ggivqrvlda gaegimlphv dsveqaeaaa tavrfaplgt
      121 rgvgstsrag awgatsreey lrfgqeevvl iaqiesaaaa raagaiaava gvdallvgaa
      181 dlstsegrse sdpvvtalia davrdtvaag kpignaggas aasvqasvda gyrftlmsnd
      241 asllggaasa avqagrtvry ar
//
LOCUS       WP_285027242             234 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285027242
VERSION     WP_285027242.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..234
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24833
     Region          6..216
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mttllpaavl wdmdgtvvdt epywmeaete lvaahggtwt hedglllvgn glwdsaavlq
       61 grgvtldadt ivahltdhvr rliqergvpf rpgaqellre lreagvptal vtmsirsmae
      121 diasgipfda fdlivagdev erpkphpdpy lraaealgvd preciaieds atglasalaa
      181 gtiavsvphi vpipegprht twdtlagrsv adlaelrsta sgpthhpete aaqr
//
LOCUS       WP_285027252             267 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285027252
VERSION     WP_285027252.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..267
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28635
     Region          6..265
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mqviritdld dgrlddyarl tdvalrrvse pagglyiaes tkvmeralra ghrprsvllq
       61 ekwledvspl leehdipvfv gepalleqlt gfhlhrgala amhrppladp aelladarrv
      121 viledivdht nvgaifrsva glgadavlit prcadplyrr svrvsmgtvl qvpwtrlpgw
      181 dvasgvlrda gfetaalala ddavdldtya rtaperlaiv lgaegdglsa salaaadtiv
      241 tipmlhgvds lnvasasava lwelrvr
//
LOCUS       WP_285027337             310 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285027337
VERSION     WP_285027337.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..310
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=32951
     Region          1..291
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mdkrvrvvaw lsfafqlvli gtggavrlta sglgcptwpr ctddsfvntp emgihgfief
       61 gnrlltfvla aiviaaflav irmrrqrpdl frltllqgls ipaqavlggi tvltglnpyv
      121 vglhfvisiv lvalatmlvh rvyrgprgav kvmpgwylgv vhltslfvav tvvfgilttg
      181 sgphagdnsk evpaprngfd peflqhlhsw payatlagti vllvgaialg arrgsrgvra
      241 avstllavev vqiivgltqa rlglpevlvg lhmvlagllv aamtwvvlqq ripvrtasra
      301 edpaslsvsr
//
LOCUS       WP_285027390             265 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285027390
VERSION     WP_285027390.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 265)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..265
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27755
     Region          1..249
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 matalvtggt sgigaafata lagrgfdlvl vardverleh saerlratgr tvevisadls
       61 dradvarlaa riedqaspie vvvnnagfgv harltdpdts eldnaievmc rsvttlsgaa
      121 aramrergrg tiinvsstag yittggysav kafvttytea lavelagsgv rvtalcpgwv
      181 rtefhdragi strsipsglw idvdrlvada lrdagrgvvv sipslrfkal malvkfapra
      241 sirwisgrms ssrraanaaq sgarr
//
LOCUS       WP_285027392             234 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285027392
VERSION     WP_285027392.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..234
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25199
     Region          6..222
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mtaeprftss lhanarfvaq rlllkplvws ltrvtvtgre rlsgvtgpyi vvanhqshld
       61 aplvvgampr rlsrylaagv aadyffdvpa rrifaalffn afpvdrsgdr kragvsrell
      121 esgvpilifp eggrsrtgel grfkpgaaal atrqgipclp vavlgthsam pkgrnwpvpg
      181 rppvrvvfgq pihpqpnetp vqlmdrvvae ivalrasaep gthvsidtpr keag
//
LOCUS       WP_285027421              71 aa            linear   BCT 25-DEC-2024
DEFINITION  histone-like nucleoid-structuring protein Lsr2 [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285027421
VERSION     WP_285027421.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 71)
  AUTHORS   Gordon,B.R., Li,Y., Wang,L., Sintsova,A., van Bakel,H., Tian,S.,
            Navarre,W.W., Xia,B. and Liu,J.
  TITLE     Lsr2 is a nucleoid-associated protein that targets AT-rich
            sequences and virulence genes in Mycobacterium tuberculosis
  JOURNAL   Proc Natl Acad Sci U S A 107 (11), 5154-5159 (2010)
   PUBMED   20133735
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18741]
REFERENCE   2  (residues 1 to 71)
  AUTHORS   Gordon,B.R., Imperial,R., Wang,L., Navarre,W.W. and Liu,J.
  TITLE     Lsr2 of Mycobacterium represents a novel class of H-NS-like
            proteins
  JOURNAL   J Bacteriol 190 (21), 7052-7059 (2008)
   PUBMED   18776007
REFERENCE   3  (residues 1 to 71)
  AUTHORS   Oshima,T., Ishikawa,S., Kurokawa,K., Aiba,H. and Ogasawara,N.
  TITLE     Escherichia coli histone-like protein H-NS preferentially binds to
            horizontally acquired DNA in association with RNA polymerase
  JOURNAL   DNA Res 13 (4), 141-153 (2006)
   PUBMED   17046956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10570331
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..71
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7559
     Region          1..>69
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 matrtlttlv ddldgsdipr glgetvrfgi dgenyeidlt ddnaaalret lasyveaarp
       61 viasaslrrl h
//
LOCUS       WP_285027466             260 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285027466
VERSION     WP_285027466.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 260)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..260
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28956
     Region          58..224
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mqrsttpaeq aeqqvglavs tviftlradd gfgatdstpg iwlplvrrir epydglwalp
       61 ggplgaaesl vdaaastlea ttslrpryle qlyafgdldr spaervvsiv ywalvgsdea
      121 krtrlgqnvr wfpadalppl afdhrdivey alwrlrtkle yshiahaflg etftlselre
      181 vheavlqkql dpanfrrqve ssglvlqtde lrtggrhrpa rlyrwtqpvt rpeapspgrs
      241 tsrrpttstp ttrqqseepa
//
LOCUS       WP_285027520             335 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285027520
VERSION     WP_285027520.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..335
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34893
     Region          20..284
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
ORIGIN      
        1 mngirlqssg fldaitrpei gawveafvdf itdvfqpvfd virsvfqgly dgvdlvlsgp
       61 pfwviiivaa llaliargpv favgsavgll iivgveqwdn amdslslvlv agliaivigi
      121 plgilaarsk vassiirpll dfmqttpafv ylipalilfr igvvpgivat ivfalapavr
      181 ltelgirnvd revveagnaf gasswrilrq iqlplampni magvnqviml slsmvviagm
      241 vgagglggdv vkslsridiq lgseaglsvv ilaifldrlt aslgggrkqr gkrtkaapss
      301 pggirpapas sttttdstas gqeqhtpses ptavr
//
LOCUS       WP_285027557             406 aa            linear   BCT 25-DEC-2024
DEFINITION  MDR family MFS transporter [Lactobacillus iners].
ACCESSION   WP_285027557
VERSION     WP_285027557.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023665
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..406
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45794
     Region          25..392
                     /region_name="MFS_MdtH_MDR_like"
                     /note="Multidrug resistance protein MdtH and similar
                     multidrug resistance (MDR) transporters of the Major
                     Facilitator Superfamily; cd17329"
                     /db_xref="CDD:340887"
     Site            order(25..26,29..30,33,66,116..117,119..121,124,143,
                     146..147,150,228,231..232,235..237,240,267,271,321..322,
                     326,330,346,349..350,353..354,357)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mktahgtrpr deinlvwlll gelldwigas fiwpltsvyl nknlhvslai vgivilcncl
       61 anmvgsviag wvydrynpyy lliagasida tvlfcialnh swpiywfwmt ltgflagwng
      121 alinsiatsi hshpsryvfn mlffaqnlgv vlgtlfvgyl ydysitmlfv iaallfvgvs
      181 inailnyrps iqfhkerlaa kihnqqkiky ekmpmnnfkm tfglfitigi iwlmymnwes
      241 nlsvymvslg ipfhlysflw tinagiivvi qifmsrypni fktlfhqivf gismfaisfi
      301 tlifakdffh fvlsmitltl geatampaip ayindlspts skgkyqgltl stssigralg
      361 plfggividn wgyinffiva aigifltlvl igplhkqlkk rfviyk
//
LOCUS       WP_285028017             797 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Lactobacillus iners].
ACCESSION   WP_285028017
VERSION     WP_285028017.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 797)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 797)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 797)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 797)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 797)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18767243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..797
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=91666
     Region          1..789
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          1..208
                     /region_name="AAA_27"
                     /note="AAA domain; pfam13514"
                     /db_xref="CDD:433272"
ORIGIN      
        1 mklikidvkn fgglsdsewk issqlhvfyg pneagkstia afikqimfgf hlksqkstff
       61 enymplkkvn qvggsltfkn ennqiitler tyttsdskkg nlavsldnek ipenifwnni
      121 knidgdfytd sfifnqdlla nvislnqgdl lehiyylgaa qsskllllrd kfvqsseklf
      181 ktngrkpein qilaqikeka etlskqqvef dqysslekqk ndvqneiell nsqvkklqqn
      241 qqnlaitkqe lnnytqyqql keqyqlidfn qedytqaqal eltieqlttd iknyeselia
      301 vsadnldeqa kilakkveiy qivneadrlq neikqlcqel eqiqtyqply fkleslsped
      361 klvmrskyeq clktqapksi iknisfglii fglvgvflkp lfyllilsgl iiyyldkikt
      421 dhirtnqiks feqeygfdpq kfdlelvmsq imqienkrni laekrkkqak ileqvadfkq
      481 kisqfvsptn nltsdlekld ehyqqvqqkv ttqkllneki saikakladv kltlqkklsq
      541 nkvkdieefk akgnlyhqnq qiksqmmals anlkdrveil skldinslht teqslvsele
      601 qiqaklriky dalaqlklkl keltnsdslk rtqqelatan anlldytkey ladllaadwi
      661 qrgldlasnd rfpkmlastn qyfalltngr yikvaindqi qvvkadgtsv aveylsrgta
      721 eqlyfalkla fveqiadeie lpiliddafv nfdlqridni vklvqnlsak tqvivftqnl
      781 qlakmltdni tkleirn
//
LOCUS       WP_285028064             438 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285028064
VERSION     WP_285028064.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 438)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..438
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45650
     Region          32..432
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(138,140,286,288,318..320,361)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mlkrhaalai aaasalmlsg csagstertt vtvrvwdsav adayetsfaa ferenpdirv
       61 rvdvvewady wtklrtdvaa dtapdvfwln nsylagyads gsvldvgqtl gkdaskdwap
      121 svvsqftrnd klwavpqlsd agiavyynad lldaagvkpa dledatwspd atkdtflpla
      181 kkltkdaagv sadqpgfnpa apatygtglg ydlqavllpf igsnggkyqd gddfafndpk
      241 tsesvsylvn aingakvapp aastnadgdf ardaflqgkv amfqsglysl kavhdgadfr
      301 wgvaelpagp agkvsvtngi aaagnaatkh pdqvkkvlaw lgsaegnapv gasgsavpav
      361 taaqkqyfdy wkgqdvdvqp ffdviaddak tiapptgagy akglaaydpi fkeifagttp
      421 vadglkkaqe aanaaind
//
LOCUS       WP_285028096            1177 aa            linear   BCT 25-DEC-2024
DEFINITION  TM0106 family RecB-like putative nuclease [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285028096
VERSION     WP_285028096.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03491.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1177
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..1177
                     /product="TM0106 family RecB-like putative nuclease"
                     /calculated_mol_wt=128091
     Region          1..541
                     /region_name="COG2251"
                     /note="Predicted nuclease, RecB family [General function
                     prediction only]"
                     /db_xref="CDD:441852"
     Region          335..1175
                     /region_name="DNA2"
                     /note="Superfamily I DNA and/or RNA helicase [Replication,
                     recombination and repair]; COG1112"
                     /db_xref="CDD:440729"
ORIGIN      
        1 mflldgsait sasdlsnass cefaflrtvd aklgriepiv epedemlmrt sklgdqhelr
       61 vlesyraefg tgvveldrpd vrdavalaaa vestitafrd gapvvfqaaf fdgsfigfad
      121 fivrrpdgry rvqdtklars pkvtallqla ayveqletag ipvdddvdli lgdgtvstha
      181 vadilpvyrr rrarllriva erleadapva wgaqrysvcg rcawcdaeit asrdvllvag
      241 lrltqrdrll aagiatiddl asltltgste rpgphepsgg aggtvdgiae stlaalreqa
      301 hlqlepspaa gvpafrvhda talgllpqpd pgdvffdfeg dplytegepg darrgdrtrw
      361 gidylfglvd tdgrfrswwa hdfheertal idflayltar raefpgmhvy hyaayerthl
      421 lslaarhgvg edtiddllre avlfdlypfv rktvrvgsrs ysikkleply mgeehrdsdv
      481 tdaaasitay aearelsrsd dpelvaeger klaeiaeyna ydcestrrlr nwlldlgaer
      541 gvlpgtfvtd apeplvdept plhdaltala gdpldpersd datayalaaa aidyhrrehk
      601 sfwqehfsrl iaardewedt rnvftvtsgv verdwfregr qrsdrrhvrl rgrwapgssv
      661 kvgadpfavy dhpgpytlpr aepgsrpagq itvlevddds lliqetlktd repytelpva
      721 ltpsppprpg tqvdaiaewg qavldaspgw pddgvvdilr rrpprtssge plphrgdgrt
      781 iedvtaalld lddsalavqg ppgtgktyva shvitalvqq hgwrigvvaq shdvvenlle
      841 rvvkaglspa lvaktlrsga dpdaergytv lpanghgafm aeqtsgfvig gtawdfsnpn
      901 rfdrrsldll vvdeagqfsl aytiaasvaa rnllllgdpq qlpqvsqgth pepidtsalg
      961 fvadgrdvlp pelgyflhet wrmdaavtep vsrlsyggel rsaaattkrr ldgltpglhv
     1021 vevhhvgnat ssqeeadrva divraslglr wtdpdggrvd dslgqediiv vcpynahvaa
     1081 vratldaagf davrvgtvdk fqgqeaviai vslaasspad vprgmsfllm knrlnvgisr
     1141 aqwaaylvhs palteylpvt pegvaelsaf irlvdgf
//
LOCUS       WP_285028116             314 aa            linear   BCT 25-DEC-2024
DEFINITION  J domain-containing protein [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285028116
VERSION     WP_285028116.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Grynberg,M. and Godzik,A.
  TITLE     NERD: a DNA processing-related domain present in the anthrax
            virulence plasmid, pXO1
  JOURNAL   Trends Biochem Sci 29 (3), 106-110 (2004)
   PUBMED   15055202
REFERENCE   6  (residues 1 to 314)
  AUTHORS   Hahn,Y., Lee,J., Seong,C., Yoon,J. and Chung,J.H.
  TITLE     Structural analysis of phylogenetically conserved J domain protein
            gene
  JOURNAL   Biochim Biophys Acta 1447 (2-3), 325-333 (1999)
   PUBMED   10542335
REFERENCE   7  (residues 1 to 314)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   8  (residues 1 to 314)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..314
                     /product="J domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=34207
     Region          9..144
                     /region_name="DnaJ"
                     /note="DnaJ-class molecular chaperone with C-terminal Zn
                     finger domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0484"
                     /db_xref="CDD:440252"
     Region          155..253
                     /region_name="NERD"
                     /note="Nuclease-related domain; pfam08378"
                     /db_xref="CDD:462454"
ORIGIN      
        1 mpesplsasp yevlgvstta tqdelrrayr rlmrethpdl ggsarqfnav qlawervgte
       61 qdraaydrgr nvpssdagdd daptwsastt grsgtqrads rprarayghp ggdsreaylg
      121 lirewvgrgv plddpydpkl vrsapreirh qlanalaeeq tartvatlgi gytvwhdvla
      181 pgeakldhvv lgptglfavk sedwggpvrv hrgevvgetl dpreepvrsi vrsartvaka
      241 arvkftasvi vvpdgatpes vefigrkhpv tvlversrla dlvrtglpgv drmggnqlfd
      301 irtrlqqtir fvgv
//
LOCUS       WP_285028234             385 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285028234
VERSION     WP_285028234.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..385
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40949
     Region          37..378
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mpspenratg dprhtrrptp rvdhtafaga raiaawwvvf shsadwlfsv lpelswlapm
       61 ahtglavdvf fvlsgytiar ayldrrwtwp aygrylrnrv arlypahvav llafvllcvg
      121 gamagvqaed gafppigllt eltltrawfg dalwwnppaw slsaqflafi lfpvfalalr
      181 grmrgpvpai vlavalisst tiaaaiapsa mngmappalr vlccfvlgsc vaewtaalpv
      241 trraawvaag gavglvvaai alepgapraw aaitfagiiv gglavasprs tavlrcrpar
      301 ilgqlsfcty lvhvfvlill akaitpsavd gmplllrapi llawfgsila aswllhtlve
      361 vpwhrrlaap rtsrvvpadg saaga
//
LOCUS       WP_285028289             311 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285028289
VERSION     WP_285028289.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..311
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31669
     Region          1..308
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mkhsssttvg llvavlaava fgtsgafikp vlasgwspaa avtvraligg lvlapfalia
       61 lrgrwdavwr grwrllgmgl igvaatqlvy faalqtiavg tailveymap lllvvvawvl
      121 trrrpatvvl vgsvvslvgl vlvvapsggs tldpvgllfa ilamvgcaay yvisarpakg
      181 lppvafasig lligalslwl aglvgvpftt sdadvtvlgt dvvwwvpllf vgvvstavay
      241 aasitasqml gsrlasfagl levvaatgfa willgeqlsl aqllggvcil lgigfvrser
      301 apavpipvpv q
//
LOCUS       WP_285028317             143 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285028317
VERSION     WP_285028317.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 143)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..143
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=14943
     Region          15..136
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 msgapegsns plpdilvsav aiirgrrvlm vtargrdvly mpggkidage tpaeaavrea
       61 reevaveidp arvtplftvv tqahgepdgr lvrmhvfaaq tdetptpsae vsavhwagte
      121 sldrcppagr dvlerlaaag lid
//
LOCUS       WP_285028322             514 aa            linear   BCT 25-DEC-2024
DEFINITION  protoporphyrinogen/coproporphyrinogen oxidase [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285028322
VERSION     WP_285028322.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Pawelek,P.D., Cheah,J., Coulombe,R., Macheroux,P., Ghisla,S. and
            Vrielink,A.
  TITLE     The structure of L-amino acid oxidase reveals the substrate
            trajectory into an enantiomerically conserved active site
  JOURNAL   EMBO J 19 (16), 4204-4215 (2000)
   PUBMED   10944103
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440906
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..514
                     /product="protoporphyrinogen/coproporphyrinogen oxidase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006779 - porphyrin-containing compound
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=52575
     Region          25..510
                     /region_name="HemY"
                     /note="Protoporphyrinogen oxidase HemY/PPOX [Coenzyme
                     transport and metabolism]; COG1232"
                     /db_xref="CDD:440845"
ORIGIN      
        1 mslepkrlvv igggvaglvg avdcakvgis vtvvdaqesf ggalaaaeva glrvdvgaes
       61 fatrggsvae lieqlgltgr vvrpnragaw lhvakpgqpq rsvplpkagl lgiptnplad
      121 dvrrvigwkg alrayldrir ppltigtehn lgalvrkrmg aavhdllvap vtsgvysaap
      181 ddldvdraap glnaaltrtg alslavaalr enapagaavg gldggmtvlv dgltaelerw
      241 gstlitgvav taisrnpfdi dvdgpgvglg daglprmser paaagaskap wyvaltdgra
      301 leadlvliat peqparnlla dvgpalrdlp aagddagdpv lpapielvti vldepaldaa
      361 prgsgllvap gstlhakalt hatakwawla drarehgdhr hvirlsfgrq geadatsalt
      421 dgellstalh dasamlgvql dpgsvrgfhr iswtgtqpta argqrersta ireavaevpd
      481 lavtgawlsg tglasvvpda heaaarlrhq alqr
//
LOCUS       WP_285028341             274 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family oxidoreductase [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285028341
VERSION     WP_285028341.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Persson,B. and Kallberg,Y.
  TITLE     Classification and nomenclature of the superfamily of short-chain
            dehydrogenases/reductases (SDRs)
  JOURNAL   Chem Biol Interact 202 (1-3), 111-115 (2013)
   PUBMED   23200746
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 274)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10793067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..274
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28802
     Region          1..274
                     /region_name="PRK08278"
                     /note="SDR family oxidoreductase"
                     /db_xref="CDD:181349"
     Site            order(13,15..16,18,37..39,97..99,147..149,164,168,
                     194..197)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187535"
     Site            order(121,149,164,168)
                     /site_type="active"
                     /db_xref="CDD:187535"
ORIGIN      
        1 mttlagktil msggsrgigl aialraardg anvailaktd tpdprlegti htaadairea
       61 ggralpilgd vrnddditra vfetagefgg idivvnnasv islartldld akrydlmqdv
      121 nvrgtfmlsr aaipmlkdae nphilslspp lnldpkwlga htgytlakyg msmvtlglaa
      181 efgrdgiaan tlwpkttikt aavgnilgge allaksrtpe iyadaayevl tapsreltgr
      241 slivedvlae agvtdlakys pgvdeselyp difl
//
LOCUS       WP_285028474             497 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285028474
VERSION     WP_285028474.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..497
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52511
     Region          13..476
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 matpadptsp sgsaiggsdt qpslvesrsi dwvplaerhg rprslfslwf msnaqvttla
       61 tgmlgaalga nlatsllaiv lgvavgtvft afhsaqgpql glpqmiqsra qfgyrgvvli
      121 caivvfslvg fnmfnqmlga dvltmttgvd agagwyvlis gvavllaifg yswihrtqsw
      181 ltalflitfg lftvvvpfvv plpadalsla nfswtaflvq fggaaayalg wapyvsdysr
      241 ylppqtnpgr alaytyggvf vgavwlmglg afvasafqga dplegvreaa dailpgsgtw
      301 lliaalpgli svitvniyaa sietitiids irpvrptral rvitclaiaa aavigsllst
      361 geflanfssf lvvllyvlvp wtsinlvdyy lvrkghyvvr diftpngvyg awgwrgllay
      421 vigivamipf vvtvwftgpi aqalggadla lfiglaasai ayvllsrsld lgreraaaer
      481 dvtetghqav afssrrr
//
LOCUS       WP_285028488             325 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285028488
VERSION     WP_285028488.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 325)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 325)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 325)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..325
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35373
     Region          28..324
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mtqlqtrpar saardrrred aarrhrtplg trmrrewrmy alilpgllff vlfayvpilg
       61 nvvafqafsp flgiegspwv gfdnfvrivs dpevvravvn tiqiavlqiv fsfpapilla
      121 lllnsllssr vkrvvqsivy lphfiswviv isiwqqilgg agpvaglfes lgvdgvnims
      181 npdtfkllvt sqviwkdigw gtiiffaaia aipqelyeaa avdgakpwrq twhvtlpglv
      241 pvislllvlt vgnvltvgfe qlllqqpivg adaaqvidtf vyfrgvvggd wgisaaagli
      301 kgvigtllvl ganrlakrmg tegvl
//
LOCUS       WP_285028499             828 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285028499
VERSION     WP_285028499.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 828)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 828)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14311963
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..828
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=91564
     Region          20..>649
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          743..818
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; cl38983"
                     /db_xref="CDD:476840"
ORIGIN      
        1 msiidtttvr pltsrllheg wslravggav pdafvgtsvp atvpglvhtd lidaglipdp
       61 fldrnehlvt wigstdweyr safewapdgh drhdlvfegl dtvarvtlng svvattrnqh
      121 rtyridvgav llegenelvv hfaspvaaad lasleigyrp htyshpfnai rkaacnfgwd
      181 wgldaassgl wkpvslqsws tarlasvrpv vtvdgdegrv avhvdverag dgdtalalta
      241 tvaganadvv laagadtavv elsvadaelw wprgygeqpl ydldvvlhqd earlgewskr
      301 igfrtvavel epdaegtsfr fvvngeavwv rganwipdda fvtrvdrarl arrmdqaefa
      361 nlnllriwgg gyyesddfye lcdergimvw qdflfacaay aeeeplwsev eaeardnitr
      421 imphaslvlw ngnneniwgf eewgwekrvq grtwgmgyyl dllprlvael dpagnytags
      481 pwsgtpdipa ndpdhgsvhl welwnrvdyp ayrdvsprfv aefgwqgpat wstieraisd
      541 spltpespgm ihhqkatdgn dkltdglvah lplpddtedw hwamslnqan avtvaiehfr
      601 swsprcmgsi vwqlndcwpv tswaavdgde rakpllyalk hvyadrlvtv qprgeslvva
      661 vlndgpdawa ddlvirrlrf dgtelasarv pvdldrrsst lveipqsvav agtateellv
      721 atlgaergfw sfaeardsai papryradva rvddgyavtv taesflrdlt llvdkvdpaa
      781 vvddqlvtll pgervtfhvr tamelgedel lstrvvrtan qlvedwar
//
LOCUS       WP_285028566             183 aa            linear   BCT 25-DEC-2024
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285028566
VERSION     WP_285028566.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..183
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19271
     Region          4..170
                     /region_name="YdeN"
                     /note="Predicted esterase of the alpha/beta hydrolase fold
                     [General function prediction only]; COG3545"
                     /db_xref="CDD:442766"
ORIGIN      
        1 msiitmpgig gsddahwqsh weretpairr fapaswdepd lddwsaaldr avadqpailv
       61 ahslscllav rwaaanptrv aglflvaapd pdgprfprva aaftedldvr psvpallvts
      121 dddpycsear aaafaatwgv prisigrhgh vnstsglgaw pegrrlltaf sagtanaspp
      181 rgs
//
LOCUS       WP_285028601             274 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Plantibacter sp.
            ME-Dv--P-122b].
ACCESSION   WP_285028601
VERSION     WP_285028601.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14974002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..274
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30210
     Region          44..236
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          176..231
                     /region_name="LuxR_C_like"
                     /note="C-terminal DNA-binding domain of LuxR-like
                     proteins. This domain contains a helix-turn-helix motif
                     and binds DNA. Proteins belonging to this group are
                     response regulators; some act as transcriptional
                     activators, others as transcriptional repressors. Many...;
                     cd06170"
                     /db_xref="CDD:99777"
     Site            order(177..179,192..194,202..203,205..206,208..212,223)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:99777"
     Site            order(188,190,192,223..225,228,231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:99777"
ORIGIN      
        1 mgerrhlglh ldhrvhefsl llqdppfddi epetrawlra ryaeivpvvl paalraverg
       61 gpisprclae lrgvairsan epgatfstal rgsypalatf savmfelqha rpsqvvlamt
      121 ratwvahelg scwveswnqe rarldraqgs lvpvgevvae gvdespveli atgpeldete
      181 qhmltltayg lsnddiakqt nysrqavswh lgklmkawnv qnrtalvava fvrgvlaarf
      241 rrrsstpaql eaahrhpeia laqpgeredd dqla
//
LOCUS       WP_285028642             321 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Plantibacter sp. ME-Dv--P-122b].
ACCESSION   WP_285028642
VERSION     WP_285028642.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-122b
  ORGANISM  Plantibacter sp. ME-Dv--P-122b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Plantibacter sp. ME-Dv--P-122b"
                     /db_xref="taxon:3040300"
     Protein         1..321
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33292
     Region          126..296
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 msgagsqnrp tknerrdaar ekarvlreqq krrdrrnrvl lqggivlgal aivavvavii
       61 vtsikpagpv ptaakndgft vsaglqlvga pasastptpt atdpaapaep apaetpaate
      121 tpadgveisv yqdflcpycg qfettnaeqv kgwleagaat ytvhplatls nlslgtqysl
      181 rasnaaacva eyspndffsf ntalfenqpk entegltdae lksiakgvis ggekkinaci
      241 ddgtykswvk dstdrarsgp lpgtdvakve gtptilvngk qytgsltdae qfaafvlavs
      301 sesystgtpt pgasespvtn g
//
LOCUS       WP_285028919             380 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfotransferase family protein [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285028919
VERSION     WP_285028919.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..380
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=43012
     Region          90..337
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mtrtnvgtve dlhasavkac gledfggddd nylealgvll dsyqreadlt elgskmqrff
       61 trnalvarlv snaafkqypq hadvpierpi fvtglprtgt tvihrlltad pahqglqmwl
      121 aefpqprppr etwadnpvfs aldarfkqah eenpdytglh fmtadeveec wqllrqslhs
      181 vsyetlahvp syakwlaqqd wtksyqrhrk nlqliglnep ekrwvlknps hlfaldallk
      241 vypdalvvqc hrpaetimas mcslaqhtta gwsntftgkv igddsmetws rglelfnaer
      301 akhdpkqfcd vdyfefikdp vgavegiyrt fgieftdaar qamneshaqs qqgprapkht
      361 yslsdyglte eqvkerfanl
//
LOCUS       WP_285029133             422 aa            linear   BCT 25-DEC-2024
DEFINITION  CynX/NimT family MFS transporter [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285029133
VERSION     WP_285029133.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..422
                     /product="CynX/NimT family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43737
     Region          46..418
                     /region_name="MFS_NIMT_CynX_like"
                     /note="2-nitroimidazole and cyanate transporters and
                     similar proteins of the Major Facilitator Superfamily of
                     transporters; cd17339"
                     /db_xref="CDD:340897"
     Site            order(55..56,59..60,63,95,144..145,147..149,152,171,
                     174..175,178,250,253..254,257..259,262,289,293,342..343,
                     346,350,367,370..371,374..375,378)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340897"
ORIGIN      
        1 msaavngtkh tryedelale ldgaieiadv parpntrlas gvllalavvv talnlrpsvt
       61 svapllgemr talgvssvwa gilttlpvlc fsaagatapl lskriglgrt vtlallalav
      121 glavrpfgdg glmlgatlla ssgvalanvl ipvvikssfp arvglmtgvy tsalqaggaf
      181 gaavtpaveh svggwrpsla iwaalalaal llwvpaarrh rtdwaataaq atrrrsllrn
      241 plawtvtvym gsqsflayvm mgwlpqifid ngmdktsagv msgvmsligv piallispla
      301 arsthqslwn vglgvlgvsg tiglliapma apvlwstmig iglsafslal tiialrarna
      361 edtaqlsgma qgfgylfast gpflfgllhd vsgdwhvpfv lffsvyavql tagwfagrnr
      421 yv
//
LOCUS       WP_285029286             383 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Lactobacillus
            crispatus].
ACCESSION   WP_285029286
VERSION     WP_285029286.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..383
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=44715
     Region          1..380
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 miktqvaelk pnktmqreld rlcdyrrycw nlaletwqdm yeartlnkdn npspnecrvr
       61 delvnnkadw qftlsarclq lavkdlanaw ksffdkaqld wgkphfkskk aprqgfktdr
      121 akvingklrl dkprgikswf diptyealrm kqvkiasifr ervhyyaals yeekagikvk
      181 tgkktaidvn vghfsytegr inilparlqk lykrikhyqr ilakkrrvng klagrsnnyv
      241 qvrtklqrdy rravniqndl lqkfttelan nydqiviedl nvkqmmmthv askgiqrslf
      301 gkfrqilsyk cawydkelil adrsypstqr cascgyvkng adkitlqgnr khgtkhneyv
      361 cyecgysndr ddnavlnlla ltk
//
LOCUS       WP_285029361             424 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Lactobacillus paragasseri].
ACCESSION   WP_285029361
VERSION     WP_285029361.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus paragasseri
  ORGANISM  Lactobacillus paragasseri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Lactobacillus paragasseri"
                     /db_xref="taxon:2107999"
     Protein         1..424
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=47929
     Region          <206..424
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 miqkfrwkfi gmsitalfvv lvitlgtllg isytqshnev drvlttlvnn qgqltprnak
       61 pvfgnqkdpi nknflageyn peaifqyryf tvastknntp kiindanvyd vaqkkiints
      121 kqvfkdkvts gsvsignnqy ayrvgkdqkg nqfivylnes liyhrfsllf rvsvvlglia
      181 livfalilil vskkaigpii ttyhkqrefi tnaghelktp laiisantem eemlgnnsew
      241 nkstkeqvdr ltrlinrlia lartgetgev vlnkvnfsei vkknvtsfks vmqkndlkyn
      301 aiimpdlyvr aernilselt nilldnarky cdkdgevkvs ltkgklgtna ilrvantyke
      361 gkgkdyshff erfyredesh nskksgfgig lamaqeivqt fhgkihvshk demivftvil
      421 kltk
//
LOCUS       WP_285029661             518 aa            linear   BCT 25-DEC-2024
DEFINITION  purple acid phosphatase family protein [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285029661
VERSION     WP_285029661.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Klabunde,T., Strater,N., Frohlich,R., Witzel,H. and Krebs,B.
  TITLE     Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on
            crystal structures
  JOURNAL   J Mol Biol 259 (4), 737-748 (1996)
   PUBMED   8683579
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11244734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..518
                     /product="purple acid phosphatase family protein"
                     /EC_number="3.1.3.2"
                     /GO_function="GO:0003993 - acid phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=55648
     Region          54..136
                     /region_name="Pur_ac_phosph_N"
                     /note="Purple acid Phosphatase, N-terminal domain;
                     pfam16656"
                     /db_xref="CDD:465220"
     Region          198..478
                     /region_name="MPP_superfamily"
                     /note="metallophosphatase superfamily, metallophosphatase
                     domain; cl13995"
                     /db_xref="CDD:472684"
ORIGIN      
        1 mavvdvsrrt livggtaalv gaglgagatg yvatrrtgpm lwqradrsga ppvtglhtqf
       61 gsdaatevvv swhtavaven prvmvgtpdd gvgnavaaet vtyrdaqshs eirvhharlt
      121 glapdtdyvy aavhdgtdpe lgsvrtaprg rapirftsfg dqstpmldak vaasfgndhv
      181 gspaagditt averlaplfh lvngdlcyan lahdrvrtws ewfenntrsa rhrpwmpapg
      241 nhenergngp igygayqayf glpdsgsdpe lrglwyafta gsvrviilan ddicyqdggn
      301 syvrgysgga qkrwleqele rtrsnkdidw vvvcmhqtav stgnktngad lgirenwlpl
      361 fdrfnvdlvv cghehhyers haihgtlptd tltpnpvdaq sgsidtskgt vhlviggggt
      421 sipsntmlfp eprcrvlmsv gevnpgtgrk tpnyieeaap wsvfrdrdnp cgfvafdvdp
      481 grpggntsid atyyavsgpf gevravdrft ltrprtdg
//
LOCUS       WP_285029664             269 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Mycolicibacterium
            sp. lyk4-40-TYG-92].
ACCESSION   WP_285029664
VERSION     WP_285029664.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..269
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27896
     Region          4..264
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mkapdvasar sllfvpgdrp erfdkaagcg adgivldled aveparkcaa rrhvadwlas
       61 ggtglvring aetpwytddl amvaeygcpv mvpkaepetl rsarltapvi alietaagvl
      121 aasaicavrg vtraafgsid lsteigidah dydalsaars amvlasaaag rpapldgvtv
      181 nvrdtdvvrk daaaaarlgf ggklcvhpnq vsvvnemfsp tddqiewara vvtaagagga
      241 avldgrmldr pvlerarkil sqvesverq
//
LOCUS       WP_285029833             411 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285029833
VERSION     WP_285029833.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..411
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43207
     Region          3..401
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mteasslplt gitvvameqa vsapmctrvl adfgarvikv enpqggdfar dyddvvlgqa
       61 ahfvwanrgk qsitlnlksd kgiavlhrll dradafvsnl apgatarlgl spedlgrqhp
      121 qvipveidgy gpggplsqkr aydllvqaes gscaatgfpg mpakpgppva distglysal
      181 simalllgra rgvstgaaps vavslfdtmt dimgypltyt qhsgvnqqpl gmaspavapy
      241 gafatrdgqt vvlgttndre wqrlardiia rpdladdarf asnsdrcahr delhaaigsw
      301 caerelddiq riadaagign srynlpsevl ahphlkardr wrqvstpngp ieallpppvi
      361 sglelnmgai pglgehtdvi lgelgyradd iaglraagai gdvyesgsdh a
//
LOCUS       WP_285029878             268 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Mycolicibacterium
            sp. lyk4-40-TYG-92].
ACCESSION   WP_285029878
VERSION     WP_285029878.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..268
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28552
     Region          10..267
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mslnapgpgw lfcpadrper fekaaaaadv vildledgca akdrpaarqa lidtpldpar
       61 tvvrlnpsdt adhpldleal artpyttvml aktesaeqvr alapldvvvl vetplgalav
      121 tetarvdnty avmwgaedlf aatggtanrg pdgtyrdvak hvrsqsllaa kafgklalds
      181 vyldiknldg lraevddava vgfdakvaih ptqvavirdg yaptekeiaw aravldaatr
      241 ergvfqydgl mvdmpvlrra erivalap
//
LOCUS       WP_285029976             353 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285029976
VERSION     WP_285029976.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..353
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37727
     Region          <211..343
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <290..346
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mnyramvtrl nlidgqlrsv lglesvgkat tleeaivnsa atteqvtfgg tgfpavaspv
       61 aqrlliaslq aqvearllvg dasgamlrsi tdairrmkla qsaqalqrqm cielcravgf
      121 dsalisfvta dsfvpqtadq fggigmplpr vvcaaeqdcv rfsrlvragm gdspategyc
      181 ellgsteylv apvvaktkvv aivhvcrvgv ditdhdyeal gmllslysvl yermlnsarv
      241 eqlrvsiiga aaqlaeevdr iagaaislem ggehvggstt papdvftanl tnrerrvfer
      301 mvqgesnaqi arelvvsvet vkthvkrilr kvgaanrlea itlyvdgper pgh
//
LOCUS       WP_285030009             197 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285030009
VERSION     WP_285030009.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 197)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..197
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21007
     Region          32..195
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mggpiagqah aaaaapagdv isigdphalg qidlyldpic pfsgklirsd geelgrridn
       61 galrvnvrfv nflekysasg tydrraiyaa favageskss dvawrfiqqi fskenqpreg
      121 gdrdlsneql aelagragap qsaqdlirlg lpvgydskvi aannltllhe fpepgvplvv
      181 idgqvindee wlsrlps
//
LOCUS       WP_285030073             392 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285030073
VERSION     WP_285030073.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..392
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42525
     Region          136..390
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 magvdehmre lsrimltrve tlgeqladri ysridgyrat psardnvres cvanmtfvfh
       61 tlcndgeadl spaeatgrqr avegiplasv mtayrigfrs mwessvaaar eagiptesil
      121 easariflsq deftqamtga yreqltsqim dreeersalv eavllgritd nqslweaadl
      181 lglpttgpyv vaaaeipaig klglpeiask laardirsaw rllpdlqvgv vhlrqdatyg
      241 vlvevlrkia tarvglspaf aglaetgegl rlarlavagk psrdgfvcaf ddaplafaav
      301 sapevmnrie esvlgglral ppeeramlsq tfqawldagg saneaasaif chpntirhrl
      361 hrieertgrs lsrprdvael clafeisqrl pd
//
LOCUS       WP_285030075             500 aa            linear   BCT 25-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285030075
VERSION     WP_285030075.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..500
                     /product="long-chain-fatty-acid--CoA ligase"
                     /EC_number="6.2.1.3"
                     /GO_function="GO:0004467 - long-chain fatty acid-CoA
                     ligase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52869
     Region          4..490
                     /region_name="FC-FACS_FadD_like"
                     /note="Prokaryotic long-chain fatty acid CoA synthetases
                     similar to Escherichia coli FadD; cd05936"
                     /db_xref="CDD:341259"
     Site            order(156,159..164,166..167)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(159,273..274,295..300,379,391,394,405,485)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(159,200..201,248,250..251,254,273..274,295..300,379,
                     391,394,402..405,466)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(200,250..251,254,273,402..404,460,466)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mtnlsqnlva satrrpdgva lrcddqtyty aqfdnaaarv atllqqagie pgdrvgvmlp
       61 ngpafaaafy gilyagavav pmnpllkape iefylsntta ralfappafa geaqagaeaa
      121 gadcwvvdda glaalidglp aqpapverad ddtavvlhts gttgkpkgae lthgglrrna
      181 dvcvrtllni gpddvvmgcl plfhvfgltc glnsavlaga tlsllprfdp akalelverd
      241 gvtifegvpt mysallatpg aastttlrva vsggaaipvq vlqdfektfd cpilegygls
      301 etspvaafnh pnrtrkpgsi gtpvegvemr ivdndgvevt qgepgeiqir ghnvmkgywn
      361 lpeataeain adgwfatgdi artdedgyyy ivdrkkalii rggfnvypre ieevlythpa
      421 vaeaavvgip hdslgeevga avslkpgiev aadelrefvk sqvaaykypr riwflndlpk
      481 gptgkllrre itipttesdn
//
LOCUS       WP_285030131             452 aa            linear   BCT 25-DEC-2024
DEFINITION  WS/DGAT/MGAT family O-acyltransferase [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285030131
VERSION     WP_285030131.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Stoveken,T., Kalscheuer,R., Malkus,U., Reichelt,R. and
            Steinbuchel,A.
  TITLE     The wax ester synthase/acyl coenzyme A:diacylglycerol
            acyltransferase from Acinetobacter sp. strain ADP1:
            characterization of a novel type of acyltransferase
  JOURNAL   J Bacteriol 187 (4), 1369-1376 (2005)
   PUBMED   15687201
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Kalscheuer,R. and Steinbuchel,A.
  TITLE     A novel bifunctional wax ester synthase/acyl-CoA:diacylglycerol
            acyltransferase mediates wax ester and triacylglycerol biosynthesis
            in Acinetobacter calcoaceticus ADP1
  JOURNAL   J Biol Chem 278 (10), 8075-8082 (2003)
   PUBMED   12502715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496208
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..452
                     /product="WS/DGAT/MGAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0045017 - glycerolipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=48704
     Region          4..451
                     /region_name="acyl_WS_DGAT"
                     /note="acyltransferase, WS/DGAT/MGAT; TIGR02946"
                     /db_xref="CDD:274360"
ORIGIN      
        1 meimsptdam fllgesrehp mhvgglqlft ppegsgpefl pelyrdmlah tdfnptyrkr
       61 parilggias fgwaydddvd vdyhvrrsal prpgrirell eltsrlhtsl ldrhrplwet
      121 yfveglddgr favyskahha lldgvsalrm amrtlsedpa etevrvpwdl psrkrapkqg
      181 tsligsavga vgaaaglaps tfrvaravll eqnltrtfsa pktmfnvkig garrvaaqsw
      241 piarikavkq aaagvtvndv vlamcsgalr aylleqsalp dapliamvpv slrseadada
      301 ggnqvgailc nlatdvkdpa trlqtiadsm hgnkqvfagl skteslalsa lllspialst
      361 vpgfvdaapp pfnivisnvp gprvpmywkg arldgnypls ialdgqalni tlvnngdnld
      421 fglvgcrhsv phlqrllvhl edsltdleaa vr
//
LOCUS       WP_285030181             482 aa            linear   BCT 25-DEC-2024
DEFINITION  FGGY-family carbohydrate kinase [Lactobacillus jensenii].
ACCESSION   WP_285030181
VERSION     WP_285030181.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus jensenii
  ORGANISM  Lactobacillus jensenii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Lactobacillus jensenii"
                     /db_xref="taxon:109790"
     Protein         1..482
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=54038
     Region          5..477
                     /region_name="ASKHA_NBD_FGGY_GK"
                     /note="nucleotide-binding domain (NBD) of glycerol kinase
                     (GK) and similar proteins; cd07769"
                     /db_xref="CDD:466789"
ORIGIN      
        1 mpgkyilavd qstqgtkail vdhnnqifyk valphkqlvn nqgwvshdld eirhnlyqlf
       61 rnilkkvnpd qiealaitnq resaaawsrh tgeplchtiv wqdnrtekli nriaypelke
      121 tvknktglal spyftgakwg wmllneprvi qarenddlcl gtmdswllyq ltnkrsfkte
      181 psnacrtqlm nihtgkwdqq lceifgtnin elpeivdsna hfgktdlfgl lktpipiksi
      241 lgdsqaalfa hgcfnpgdfk vtfgtgssvm lnigsnlpsn innklntsia wslngkisyv
      301 legninyaga siswlkdkvq linkpeeten laltanpkdh tilipafagl gapywkaeak
      361 aafvnmtatt gknelvkatl nslvyqisdi lsqfqqlypk vnqgihtdgg mihnkylmqy
      421 lcnitqkvvk iadipelsal gsamnarnkk eqaqssksft pkmksesakf yltewhdwid
      481 rf
//
LOCUS       WP_285030194             413 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285030194
VERSION     WP_285030194.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..413
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43930
     Region          5..403
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mstqtkqsvf aglkvveias fiaapaaatm lsdfgadvik veppgigdpq rllssvppsp
       61 aapgnyswhl anrnkrgmsi nlkseggtqi lqrlvewadv litnfphgtr eglhlgyeev
      121 sgwnpriiya ditgygdsgp daklpgfdlt afwsrsglla atrdagappt spvwgsgdyt
      181 tataiyaait talyhrertg lganvgtsll atgvwatgtl vsaalaggtp yqlhdrnkpd
      241 namtnayvsa dgrwfmlaak rsawptlaaa mgrsdlltdp rfadaqaiaa nagelaktle
      301 defgsrplsh whdvldaari pygviqtpee aahdpqlraa givvpiegae dldytvnnpi
      361 alrglprtps rrapehgehn devlaqlgft adeiarlreq kvipaatqqe slk
//
LOCUS       WP_285030202             934 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285030202
VERSION     WP_285030202.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 934)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 934)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 934)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 934)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467590
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..934
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..934
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=100396
     Region          <13..868
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          876..930
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mssttvhslg nntatpplrg rademktala qldallkgrg galviegpvg sgksrllaem
       61 talaerrgvr tlygeaiehq qdlpfvpmft amlsggrpvg ngevlrklga sadagywvvq
      121 hlqaaiteaa ersplmvvle dihwadnrtl lalrslaaal anvrvlwvlt mrtgagsppv
      181 hetlatlhhs gaeflhlpam srgavvemva dlvrarvdes legmaakarg npylvteilr
      241 gvreegrlqi gggtasvtgq dlpgrltacm qrrldvlstd aselvrvaav lperfsagll
      301 aamlerqpas llpalaetar agllvddgeq lrfghrllre atreclpqsl rramerqsas
      361 lmmsmgappa dvaealvrsa epgdraaaaa lrgaaqslar tdvsaaadfs mralellptd
      421 dtdhgrlvae tvvllnrarr yqdaeelavt alaeatadse aeirlrlpaf trhgsrhrae
      481 enrralrlda vndvtrarhl allaynlmld dadgrhrala ddalaaadav ndleskvian
      541 vtmacfecvd gaagaaldrl kelcarcrts elpaayllsa ahyanalaav ghvdesvdli
      601 tsragrarqe hnamavdvws tyagmaqlaa geldaarlaa eavpipdvhd stqpdvteld
      661 vlraavlvev alrtddrkll qqmlfhvrsa yaegsamerr taahalamaa wyaddldeaa
      721 rwsdpevell rapltpqald qvilrarvaa asgerdcrag vlraveklss devplftavv
      781 lharglldad tdmlmratdl lrssqrpmlf aaatedvgrn ladaertdqa ldwfnaafdt
      841 ytrlgavada rrvgrrlrql gverritrhp kaksgwdslt dsehkvvtlv aqgatnrava
      901 dqlhlslhtv kthvhnafgk lgissraqlv qagr
//
LOCUS       WP_285030262             378 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein, partial
            [Lactobacillus jensenii].
ACCESSION   WP_285030262
VERSION     WP_285030262.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus jensenii
  ORGANISM  Lactobacillus jensenii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Lactobacillus jensenii"
                     /db_xref="taxon:109790"
     Protein         1..>378
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
     Region          23..>378
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mknssniktt ktnvhsnrfq vgrvlqviva lvfliflgrt lyisisktva genlstrtaa
       61 lykrnqvlka trgtiydrng ftiaedshvy tvyaildhss inyknkpeyv vdkdktaekl
      121 atvlplskeq ilkylnpktk afqvqfgsgg snltieqkkk ieqmklpgik fieapsrlyv
      181 ngvfashivg laqpiynkkt kstdlvgtmg ieayydkyla gkdgfkessv daseyqlpng
      241 tnayraakng ddiyltldsq lqnymenllt rvqnkyqska ltavvedlrt gkvlaasqrp
      301 tfdsqtkkgl tssytdlltq stfepgsvfk ilsfaaains ghynpnelyk sgsltvngst
      361 ihdwnvtgwg siplyeaf
//
LOCUS       WP_285030292             199 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Lactobacillus jensenii].
ACCESSION   WP_285030292
VERSION     WP_285030292.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus jensenii
  ORGANISM  Lactobacillus jensenii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Lactobacillus jensenii"
                     /db_xref="taxon:109790"
     Protein         1..199
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=21923
     Region          5..194
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mrnskeviay inelrkqqkm siselsekvg maksgvslyf ngkrefpinh aekfakalht
       61 nvfdllgvgd dsmikvpvlg eiacgqpila eqniegyryi ncrdqssnlf flkakgdsmv
      121 ptipensyvl idrddsvedn divavlidns atlkryhkng ntvtltgdnp nfppivltst
      181 edaiaqilgk aiqvsfdln
//
LOCUS       WP_285030374             398 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285030374
VERSION     WP_285030374.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..398
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42859
     Region          166..394
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mpdpaprytg lelgedvtsa lhsvlprtae rtvaavtvev psytdafsgp mgqnietavq
       61 malggflrla traedadagt qlapaldgay elgrgearsg rtidallaay rvgarvawre
      121 lastavnagl taetmarfae lvfafidels assvtghade lattgrvrer ylerlghsll
      181 agetteilea gaehadwtpp tsltavllpa sqihglavnf gpstlqlnqd lpgvdpteal
      241 tallvpdmdg phrrrllral agrrawvgpa rpwaqvrssy rralqardil lgsdvdvldt
      301 dehlvelvig adreaaddlr rrvlapladl rpntaaalte tlrswllhqg rrdavaadlv
      361 vhaqtvryrm tqlrelyger ltdprtilel tvalgies
//
LOCUS       WP_285030463             262 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285030463
VERSION     WP_285030463.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..262
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28678
     Region          9..259
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 msstapswia qlldfardgd tfiapqpteg pgrslfggli aaqalgaagr tvepgklpqs
       61 lhlyfvrggq ygvdvefhve rtrdgrsfdt rrvtakqngk tilemiasfh vpepgadwqr
      121 pevrglefdv svpkapslta adhfdirvrp edagafavpp fwirtkdeie ddaliraaal
      181 tfmsdfgpvp varpdgahlh dgfaasldha vwfhrpfvph dwhryevtrl nntdsrglvt
      241 galydtggvl iastsqealw rl
//
LOCUS       WP_285030404             454 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC1 kinase family protein [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285030404
VERSION     WP_285030404.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195515
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..454
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=50843
     Region          93..339
                     /region_name="ABC1_ADCK3"
                     /note="Activator of bc1 complex (ABC1) kinases, also
                     called aarF domain containing kinase 3; cd13970"
                     /db_xref="CDD:270872"
     Site            order(146..150,152,162,164,221,240..243,283,287..288,290,
                     300..301)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:270872"
ORIGIN      
        1 marrlpegrl arggklgala akqavrggrt rlsmvgrser arellaerat iqmaenlvtv
       61 lgsmkgaamk lgqmlsviel dlvpeshreq freklaalrd qapqapfgam revmetdlgp
      121 msgvfadfde sptaaasigq vyrarlrdgr dvavkvqypg vdraiqadmr nlallmklwr
      181 lwpsantaml deitrnfese ldylreadtq hmvaeqyrgh pfivvpdsvv efctprvllt
      241 eyldaagfdh mrtlpaadrn higeliyrfy igslftnhef cgdphpgnim laadgrlgfv
      301 dfglynrmdp anvafeldcf haaidgradd lhrlmlgrgi vdaesgvtaq dcleyiwaas
      361 ewhmidedlt itpelatgav vsaidprqte fagmkrqmlp pehvfsrrad fltfgtlghl
      421 qstnnwyrig qewffdrpae teigreiarw rasr
//
LOCUS       WP_285030497             489 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285030497
VERSION     WP_285030497.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..489
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=54569
     Region          1..419
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 miehfdvviv gagisgista whlqdrcptk syvilerren iggtwdlfky pgirsdsdmf
       61 tlgfrfkpwe saksiadgqs iwnyineaad engirqhirt gqhvtsvdws daenrwtini
      121 taggeekqit asflsvcsgy ynydegyspe fpgaadfkgq ivhpqhwped ldytgknvvv
      181 igsgatavtl ipslvnggvg hvtmlqrspt yigalpledp vakqtnkylp khlahfanrw
      241 kqigystaqy qlarkfpavf kkalrqmatr rlpegfdydk hfsprynpwd ervclapngd
      301 lfkairsgka gvvtdtietf tengikltsg eelqadiivt atglnmqlfg gatanrngep
      361 idlpscmtyk glmlsgvpnm aitfgytnas wtlkadlvse ficrvlnymd angfdrveaq
      421 hpgdsvdelp fmdftpgyfk ramdslpksg seapwklkqn yffdmrtiry gkvdeqalqf
      481 tkhrvavna
//
LOCUS       WP_285030541             329 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285030541
VERSION     WP_285030541.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..329
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33145
     Region          16..326
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mvmlgcavla lsiaaamiig padlgfgdvy avvaqhlwgr paqiapiddg ivwelrlpra
       61 llaaicgagl aicgailqsl mrnpladpfm lgissgastg avlvvvagig galtlsggaf
      121 vgaviafglv lalaavsggg qdrvllagva gtqlfsaata ivvfssadaq qtrgvlfwll
      181 gslagagwsq valcglvcaa claicwlqsd aldafafgrd aaaalgvsvr rvravllatt
      241 alltavlvsa agaigfvglv lphaarmivg pshrrllpvt avtgaiflvw vdaaartvfa
      301 pqelpvgvvt alvgvpifmw ilsrrrrir
//
LOCUS       WP_285030577             538 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285030577
VERSION     WP_285030577.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..538
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=57657
     Region          23..123
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          241..526
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mptvaeival pviqqgepei lcatgfdrpi rwvhvsdvpd lsevlqggel vlttgaalra
       61 apldylrsva aahavgvvve lgagavplpv nvgaiaeelg lalvavrrvi kfvevteqvh
      121 rvivadqyqe vdfarqthev ftdlsmrrat ptgiaeaaan llgapvvled lthqaiavat
      181 agrptpdvlr dwqrrsrqhe tgaertdgwv isevgrgeda wgrlialspa edvaarftmv
      241 lerasqalvl hrmaergrtd iehqaqagll edvarerirf edeatarafa lglrpaaqyq
      301 patlriagwa adtdpvseqr rgarlldvvt rsvkalghsg lfslrgpgei amvlslntra
      361 ggtleplgra lrrdaeravd ahglvlgvgt papglidaih ritdaahvad aalslpasqr
      421 vcfrvadirl rgllsmlrtd prvqrfaege lralilhdme sggerlldvl rgylelggnk
      481 salasrlhls rpslyaklnr ieqilgvdla dgesvtslhv alliletrna fggagapl
//
LOCUS       WP_285030584             586 aa            linear   BCT 25-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285030584
VERSION     WP_285030584.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..586
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=62833
     Region          1..584
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mfdlkitggt vvdgtgadrf tadvaikdgk ivevhrrgpn dpvlsgdsae tidaggkiva
       61 pgfvdihthy dgqvswdsvl epssnhgvtt vvagncgvgf apvrpgqeew lialmegved
      121 ipgtaltegi twgwetfgey ldivgqrela vdmgtqiahg avrayamger garnepadpd
      181 dikamarlvr eaieagalgf sssrtvahra mdgepvpgtf aaedelfalg raasaggaav
      241 felapqgaag edivaprkel ewmrrlgeei dcalsfaliq vdadpnlwre qldlsaaahq
      301 agsrlfpqva arpfgmllgf pghhafthrp tyrrlaaect reelaeklae pavraailae
      361 ddlpidptkl fdgmfmlaqn aanrlyhige ppdyeptver tvaaiaerrg vdqlaamydl
      421 mleagagaml mypmfnysng nhdairemlt hpagvlglsd ggahcsmicd asyptfllth
      481 wardrhrgek lpleyvirkq shdtaqlygm sdrgviavgk kadlnvidld altlhapkmv
      541 hdlpaggkrl vqdasgydat ivsgtvtrrh gadtgarpgr lvrgir
//
LOCUS       WP_285030623             151 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator
            [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285030623
VERSION     WP_285030623.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..151
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16779
     Region          7..107
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mssrlarstc pvsrtvdivg dkwtlmilrd afeglsrfsq fqrslgvakn ilsgrlqhlv
       61 eagvmesrpd sggssyreyv ltakgeklfh lmvalrewga dnaftddepr tsyldsrtgv
      121 plprlqyqsa dgdeikpeht rpvrpdgwva p
//
LOCUS       WP_285030729             333 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285030729
VERSION     WP_285030729.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..333
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36161
     Region          22..321
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtlprmqpgq sdiaeardiv gavasafshq vvgqqhlret mlvallgggh lliesvpgla
       61 kttaarvlaa svggsfrriq ctpdllpsdi igtqifeadt nsfttqlgpv hanivlldev
      121 nrssaktqsa mleameerqt tiagveyplp epflviatqn pvdqegtypl seaqtdrfml
      181 kelvhypsit deieiidrmd agrydrdrhp apvvslddvr raqeivrsvh ldralvayas
      241 rlvavtrdpa qhlpsnlarl ieygasprat iafcrsaral avihdrghvv pedisilahr
      301 vlrhrlilgf eaasaritpd avvdavlqtv pvp
//
LOCUS       WP_285030743             378 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285030743
VERSION     WP_285030743.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..378
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40581
     Region          10..375
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mtapaaepvs gtrgflpave glraaaalgv vlthvalqtg ytdgvvgrll arfdlsvavf
       61 falsgfllwr ghaaaahglr aepevapyyr srlvrimpay lltvvavltl lpdahradra
      121 vwianltltq vfvpktliag ltqmwslsve mafylvvpll allvaklslr mrvpviagva
      181 llsfgwgylp ipayyganpl nwlpayaswf avgmllaewm frpygwahrl arqrsllmav
      241 avvaflvgas plampgghqh atlgqfivrt algaviagal laplvlgtpd drhrvlasap
      301 mvtlgrwsyg lflwhlaald mvlamigqta fpgalpvvmv ltttfgfava avsyalleep
      361 crvalrrwea rrqaavtt
//
LOCUS       WP_285030736             204 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285030736
VERSION     WP_285030736.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..204
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21774
     Region          39..153
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mveqslwmqk veadpghsqw yierfralar agedlvgear lidamaarga rildagcgpg
       61 riggylaaag hdvvgvdvdp aliaaaeedh pgprwlvgdl aeldlpsrgi pepfdlivsa
      121 gnvmtfvaps trvqvlsrlr ahladngrvv igfgagrdye fgqffrdasq agltpdvlls
      181 twdlrvftdk sdflvavlip ipsg
//
LOCUS       WP_285030786             458 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285030786
VERSION     WP_285030786.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..458
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49039
     Region          171..434
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mtigattagl ygeqhvslth gwlpfsvqal aaavlilavg wrnqrwrtlw lpvaavsgvl
       61 vtaaarwvva sqgwsddpap arlwiwtavt gaavvllivg whatrwwrrg lavlsvplcv
      121 lstgltlntw vgyfpnldta weqansaplp nqtphetvva mqkarripsk gsvvevqtgs
      181 aasgfnhrde yvylppawfa snppprlpmv mmiggefntp adwlragnai ktvddfaaah
      241 qgnapvlvfv dpggsfnndt ecvngprgns adhlikdvlp fmtanygvsa drrhrgivgw
      301 smggtcavdl avmhpdlfsa fqdiagdiap nagdrpqtvq rlfggstaky adwdpmtvms
      361 rrtydditaw ydingpelsr gplpaqtiaa hslcgvgstr gircavverp gkhdwpfaaq
      421 aftaalpwla gqlgtpgvpr lplpgatapa mpveaarr
//
LOCUS       WP_285030897             328 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285030897
VERSION     WP_285030897.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..328
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34375
     Region          1..327
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mkafdfhrar dvddaltiad atggsyyagg tnlldlmklg vtqpsslvdv gglgldeita
       61 tdnggiligs gvtnsaianh hlvrtrypvl shailsgatt qlrnmatagg nlmqrtrcpy
      121 fmdvtfpacn krrpgsgcaa ldgfnrehal fgasrscvav hpsdmavala ildavvhirs
      181 regarsiavs effrlpgdhp eqdnallpge livgvelpps eyafhswylk vrdrhsyafa
      241 lvsvavgmai ddgiitsaav alggvaarpw rspdaeaalv gnvadittfg raaeaamaga
      301 valsqnafki elgkhgvvrt lqkaaarq
//
LOCUS       WP_285030905             375 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285030905
VERSION     WP_285030905.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 375)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..375
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=39467
     Region          <73..109
                     /region_name="LapA_dom"
                     /note="Lipopolysaccharide assembly protein A domain;
                     pfam06305"
                     /db_xref="CDD:428880"
     Region          144..373
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 milgamdlvi iavtalicts vatgaavlvm qlnrrgsigt qvsvligati vaivastvai
       61 siemylsshd lqvllavlai salmaglaag fmlrrlrrsv arlqraarqi gsgevvaadv
      121 dssrefaels sqlaqssaql aaaraeveql dasrrqlvaw vshdlrtpla gmramaeale
      181 egvvdepady irqirdqvda vngmvdglfe lskiqsgmlk lskepvvlld lvsdvvsdmr
      241 alaatrgiti thaemtdqvl fadpgelsrv vanllinsir hapedseiqv sahhldgdri
      301 vltvldqgpg vqshdlgrmf dmgwrgtqar tpeadgsgag iglaivrgiv eahggqvsaa
      361 hvpggfrldv tlptt
//
LOCUS       WP_285030952             427 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285030952
VERSION     WP_285030952.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..427
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46026
     Region          144..409
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msspsqlppi padaplrkvi edrideiatt llheavqsie wptpmpiehf dgevapyiig
       61 gflyglglit egrrvtraev atfvlpvaer haedgiplpf lftalhagir klweivlesa
      121 segdsetiaa lgmyladftg tisvlmtevy qdsdfalrat arrqlgalca glidgapdid
      181 vlakqvgikl sdrydvlair vdtdeprtth eilaarrrlr lanqvfygrg ageilntfdg
      241 hagvillpap vvehcddsav tghlgalvaa lsdrldiavy aayhpgaala aipaavsead
      301 eitrlarqln rgpgiyqlad vlfeyqstrp gpardllacr iaplrdhpgl lqalqahlqh
      361 gadrkaaaae lfihpntlty rlrriqditg ydptdphqsr llaaamtvht vdhadtpiav
      421 tepgnpg
//
LOCUS       WP_285030935             192 aa            linear   BCT 25-DEC-2024
DEFINITION  GTP-binding protein [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285030935
VERSION     WP_285030935.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Takai,Y., Sasaki,T. and Matozaki,T.
  TITLE     Small GTP-binding proteins
  JOURNAL   Physiol Rev 81 (1), 153-208 (2001)
   PUBMED   11152757
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006198
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..192
                     /product="GTP-binding protein"
                     /EC_number="3.6.5.-"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /calculated_mol_wt=20467
     Region          10..192
                     /region_name="Srp102"
                     /note="Signal recognition particle receptor subunit beta,
                     a GTPase [Intracellular trafficking, secretion, and
                     vesicular transport]; COG2229"
                     /db_xref="CDD:441830"
ORIGIN      
        1 mayglsnrha pastkivisg gfgvgkttfv gavseimplr teaivtnasv gvdalagtpd
       61 kntttvamdf gritladdlv lylfgtpgqr rfwfmwddlv rgaigaiilv dvrrlqdsfa
      121 avdffeargl pfiiavnefd gaprhpghav rkalalpdni pvvtvdarqr qsardalitv
      181 teyaltrlga pa
//
LOCUS       WP_285031040             374 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285031040
VERSION     WP_285031040.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..374
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=38960
     Region          31..371
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mssarfntdv yaarlrsaaa aaqaaglagl vitpgydlry lvgsraqtfe rltalvvpad
       61 gstptvvvpr lelaslkesa ilelglavrd wvdgddpyas vaaalpgklv avtdampalh
      121 llplasvlga vpvlatdvlr qlrmikdpse idaltkagaa idrvharvpe flvpgrtevd
      181 vaadiaeaiv aeghsevafi ivgsgpngad phhecsdrel qvgdivvvdi ggpvepgyns
      241 dctrtysige pdpvvvqqys vlqraqaaav aavrpgmtae qidaeardvl aaegladvfv
      301 hrtghgigls vheepyivag naltlepgma fsvepgvyfa gqwgariedi vvvtddgcvs
      361 mnnqphelvv vpvl
//
LOCUS       WP_285031361             378 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285031361
VERSION     WP_285031361.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..378
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39029
     Region          72..357
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mlvtapipta aaaapdwsgl darafadrvp rpgglirsvp lnpelsvaaa arayrilyst
       61 tdqhnspavs sgavfvppge appggwpvia wahgtvglgd dctpsaqprs ardnkylshw
      121 ltagyvvvgs dytglgtpgl msylnsvata haiidsviaa hhldlplspk walvgqsqgg
      181 aaavasarwa tefskgtgld yrgvvatgtp aniddvvita gpemvlppel gsiasaytay
      241 ilaafrelrp dvnsvltpag lsaadkaetl ctfplsdalt gstppqffsa plaslpdmrg
      301 aladfmgtpv agydrpiflg vglkdrdvpp sstlkfadql kangqdvtlh vypeddhsst
      361 vltsmadstp flqaqfag
//
LOCUS       WP_285031431             422 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285031431
VERSION     WP_285031431.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..422
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46597
     Region          167..411
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 marshdtgvl padtaamivd rlsdklpams qsllemlvqe raemagdgel kallydavqg
       61 nleaffpair hgipidriep ptaaleharr laqrgtsvde lvrayrlghh gvlkvildev
      121 raahldselg lqvfeeiaas sftyidrvsh qvvnayqaer drwlnsqnqm ralrvrevld
      181 ggdldidett dliryplhrv hlalivwcae qaegdeladm erfvadlaav lgarerplfv
      241 asdrttgwaw iplpagtddp vgqirefvrs rpdapwvttg taldglsgfr rshrqavaar
      301 tvtmapsapp rpvtaadepg livaaqfssd ldnarswvch vlgplatdsd sderlretlr
      361 gflrnsssfk ssadelhlhv nsvkyrvqra ierrgkpidt dridvevall lchwfgtavl
      421 ap
//
LOCUS       WP_285031491             325 aa            linear   BCT 25-DEC-2024
DEFINITION  AurF N-oxygenase family protein [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285031491
VERSION     WP_285031491.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Choi,Y.S., Zhang,H., Brunzelle,J.S., Nair,S.K. and Zhao,H.
  TITLE     In vitro reconstitution and crystal structure of p-aminobenzoate
            N-oxygenase (AurF) involved in aureothin biosynthesis
  JOURNAL   Proc Natl Acad Sci U S A 105 (19), 6858-6863 (2008)
   PUBMED   18458342
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10569062
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..325
                     /product="AurF N-oxygenase family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37198
     Region          9..291
                     /region_name="AurF"
                     /note="P-aminobenzoate N-oxygenase AurF; pfam11583"
                     /db_xref="CDD:431946"
ORIGIN      
        1 mtkamepgyq nlldvlsegs vrrrfdpyld iawgspdmai dlqdprwvls ptidplgate
       61 wyqsqplerq ieigrwrtln tvkvgaafes ilirglmafi mklpnnspef ryalhemtee
      121 cnhiqmfqel vnrsgtdvpg mrklffklsp yiglvgqysp tafmagilag eepidhfqkg
      181 mirdganlpp avlrtmqihi aeearhiswa neflkthmpe rswrfkafat vafpltlrwl
      241 aheimgssks fgkqfdiped vmrqafwrsp qsrkimasff detralaeei glmnrvgrwm
      301 wkrcgiagea aryrsapnre aqlia
//
LOCUS       WP_285031594             319 aa            linear   BCT 25-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285031594
VERSION     WP_285031594.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..319
                     /product="isopenicillin N synthase family dioxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34106
     Region          1..317
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 msaiatvdis rwyaggaead avaaevdqgl qragfivvtg hgvdqglaaa vrtasreffa
       61 ladevkrrys vpvgghgwig pgaeangyae gtetppdlke sfslgaetst gdpevdriwf
      121 apnvwpvevp alqtlvdeyt aqmrrlsddl lalfahalgl panpfaalad rptwtmninh
      181 yppvsvvgep epgqfrigph tdfgtvtvld repgagglqv ysdaggwqda pwepgaltvn
      241 igdlleywsg rrwpsgrhrv lppqphapee dlvsliyfye anhdalitpl rppigavsgl
      301 apvvssefik erldaitvg
//
LOCUS       WP_285031600             359 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285031600
VERSION     WP_285031600.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 359)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..359
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38699
     Region          61..350
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 marvrlsrrm aameqnltsr qnadlvdvlq ipeafvspvr rivrrviyal lvlaaavlvv
       61 yidrdgyrdv tenrmslldc iyyatvslst tgygditpyt psarlvnvlv itpmriafli
      121 vligttvetl ttqsrqalki qrwrstvrnh tivvgygtkg rtavqamvgd evapgdivvv
      181 denpaaldra raaglvtvvg datksevlrl agaqhaksiv vatdkdatav lvtltareva
      241 pkakivasar eaenqhllrq sgadstvvss etagrllgia tqtpsvvemv edlltpdagf
      301 aiserevetk elggsprhls divlgvvreg rllrvdapev dalaagdrll yirnaever
//
LOCUS       WP_285031621             641 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285031621
VERSION     WP_285031621.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 641)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..641
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=70733
     Region          136..597
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 miaatesssp aalapdsdvl rahllradpg vlvavlaqmt gdttvidrya pkidhvpdpp
       61 eragttdadt mralveevva algrarttda ppahdrdlfv rllpialgse vsdehvdlli
      121 eqggfrpsqp tlprttpips ttsvaiigag lagiavalaa aeenvqfqif ernsevggtw
      181 lttnypgigv dtpsayysls revnpdwssy ypqgaeyqay lvaladkhdl rrhtrfntev
      241 ealwwdeqrq qwqirsrngd gaetvdyarv vvtaagylnr prfpdlkgre sfggisihsa
      301 qwdpeldlag kkvaiigagc tavqivdacv edvdhltvfq rqphwvaprk rqsddvpehr
      361 rylghalpfy amwhrvksyw atadnnypvi lqdpewskth lsispandvl lqmcqeyidr
      421 mfgagtelak kvtpdfapyg kriirdpggy yaalardhvd veasepaevn angivtvdgr
      481 qidldviiya tgyhldflst vdirgrdgrt lsdewgespr ayrggtvpgf pnlfitsapn
      541 yspghgagan fsmevlahyi veclqlmalr gtstievtqr ahdeyvagid elmqgtvwch
      601 tpkahtyyrs gsgrvvvatp yrlvdlwqqh rapieedfil r
//
LOCUS       WP_285031659             418 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfotransferase family protein [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285031659
VERSION     WP_285031659.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..418
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=47755
     Region          116..357
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mssqsalaid dlvaprlepv qqqvldafsn qhigldpaal iadamadagl ddfgddgfrp
       61 rlnayvaaie adtgntnlnr filrnrivrl ltqrllltdl lrrypeihdv eieqpiivvg
      121 lprsgtthlv nliaadrgrr alpfwesqep fprrgeapdv ngldprflrs vaeheyakti
      181 tphlqamhdr fpaaieeeve lldidfasyv lewharvpqw rdfylalnqf dhyaylrtil
      241 kaltflrgpr rwvlkspqha eqlrplistf pdatiafthr dpvaviqsai tmlaygdrir
      301 rhdidpgglv dywvdrierl lracvrdrdl igqdrsidvl fhelngnema ivdklyelng
      361 ttlspesaad lqgyldanpr gkhgrmvydl ernfgrsakq mrarfdfyfe rfgvkeel
//
LOCUS       WP_285031676             354 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285031676
VERSION     WP_285031676.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..354
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38072
     Region          2..331
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mhahhevivi gagvagltam rtltaagvda vcleararvg grlltaqtdv gpldlgatwl
       61 waherritgl vrelglptfr qhadgavlld graverladt dfrpslrygs gaaaitehlf
      121 anlppdsvrl qtpvtalavd gtdtlqvrtp tatlhaeqvi vavppalava ridlppelpt
      181 rlvqvarstp vwmgrvtkvv vryrspfwrd dglsgtafsr rgplqeihdm sgpharpaal
      241 lgfvvggsnr pdlvadvttq lqrlfgwraa hpeevlvqdw stehwtspsh vyqltdftty
      301 ghpaytqptl ggrlhwaate tstehpghve galaaaeraa raaisrastt ltrk
//
LOCUS       WP_285031723             872 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285031723
VERSION     WP_285031723.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..872
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..872
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=92314
     Region          <2..829
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          <805..860
                     /region_name="PRK04841"
                     /note="HTH-type transcriptional regulator MalT"
                     /db_xref="CDD:235315"
ORIGIN      
        1 mrsphhlver dgvlgwldgr lqaaaagsgc vavvsgeagi gksavvtafv aalpvsvrvf
       61 ysacdplstp vplgpvlelr dalslsgavr vataldnphg paavpeavva aladsgpavw
      121 liedvhwada atldvlryli sriatiplll vlthrvegig rehqlsefla diaeshasgr
      181 telepltrdg vvtlaasrpg fdvdrlheat ggipllvves laagrygvvp qtisdhvigr
      241 larlgpsara vidsvavlgs datvdvlaam vdgaaselpa cvtagvlqrt ghvvgfrhel
      301 trqavletip tfgrrrlhas alaaltacgq ecslahlafh aeeagdadav lryatqaaer
      361 amrlgafaqa aeqyarairh shgqpadara awlesqarav ymsgqvvaaa eligkaialr
      421 retgdalreg ddhrwlshwl fagaplaqvs eaahtavril eplgptaela gayanaaqlc
      481 cvvfdhdsav dyatkaaaig qqldvvaeva waesfaalsa vlagngwdef darwavardd
      541 prtveaaavg gvvacwfata ryeldradsy ltvtaefcrd hnltglgyft rgigttqllh
      601 rgryadaaav ahavlartgl ppvfrlrplv vlalvyartg qhdavgplld ealdgldpsl
      661 vyltgtvlva rieaawlagd hrrareearr alaalpprad agtrgqvtaw aaiagvssap
      721 lprsedrqya lqidqqwaaa aaewrdrgca yeaaiaaihs dtpelaaaai aelhslgahg
      781 avdrarqhrr rrhqrrstqe hpfgltareq qvatllaerh tdkqiaeilv isrktvshhv
      841 asvltklgvt nrnavrdilk pdrgtgaits mr
//
LOCUS       WP_285031787             460 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285031787
VERSION     WP_285031787.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..460
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49895
     Region          6..339
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mlaqgfdvvi vgarcagspl atmlarqgvd vavveratfp rdtlsthife tdglafldrl
       61 gvtdqlratg apfmkrsnsr adsfqfnapw plrggdiggg asvrrtvldp ilvgaaeeag
      121 aevrmatevt glvwegrrvt gvrvkthgre delrarlvvg adgrnstign lvaarkynvv
      181 pgqrfaywaf fsgahmpaep snvfhrwddk fviaapcdeg lyqvivvpel sqlqryradl
      241 dgsfmadalt cepvaealvg aqrvskyfgm lhwtgffrep agpgwalvgd aghfkdpsag
      301 rgisdafsqv dalvpavvdg lagspekqda alarwgrwrd hefsdhywfa ndlgksgavp
      361 tvfaqmvadl hakgeigrfl dlfnhrekps qvlsatrlfg sagrllrhqh qgrrallnev
      421 rtlvgesahr qflnhrhayi taqeamkpag atevdagsva
//
LOCUS       WP_285031908             236 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family transcriptional regulator [Lactobacillus crispatus].
ACCESSION   WP_285031908
VERSION     WP_285031908.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Nazaret,F., Alloing,G., Mandon,K. and Frendo,P.
  TITLE     MarR Family Transcriptional Regulators and Their Roles in
            Plant-Interacting Bacteria
  JOURNAL   Microorganisms 11 (8), 1936 (2023)
   PUBMED   37630496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Will,W.R. and Fang,F.C.
  TITLE     The evolution of MarR family transcription factors as
            counter-silencers in regulatory networks
  JOURNAL   Curr Opin Microbiol 55, 1-8 (2020)
   PUBMED   32044654
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Grove,A.
  TITLE     Regulation of Metabolic Pathways by MarR Family Transcription
            Factors
  JOURNAL   Comput Struct Biotechnol J 15, 366-371 (2017)
   PUBMED   28694934
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   7  (residues 1 to 236)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   8  (residues 1 to 236)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10581578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..236
                     /product="MarR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26883
     Region          28..81
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
ORIGIN      
        1 mtkkrntsea nhkfkgvwip aeywldkdlt imevalitei dsldgengcf asnklfadfl
       61 gitpgrvsql vkslkekgyi ttiystknnv tqrtirvvsk lntpvkklnr gikntkgvfn
      121 klstsnissn tfnsntvsns ssakkeedpe rekiykefft iarmndklkn hstnptldel
      181 kqlrgllyqc nvdtlqavkd kfkermswdm vgkpysyllk mlrdglandr nyeswg
//
LOCUS       WP_285032189             134 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285032189
VERSION     WP_285032189.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 134)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..134
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=14336
     Region          5..125
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 mtvirivaav vaderghlll vrkrgttafm qpggklepge spadalarei reelgvgitd
       61 vrelghhtai aanepgytvd aelffvrldg tpqiaaeiee mawidphapg dielapltae
      121 avldwarsrp alep
//
LOCUS       WP_285032211             426 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285032211
VERSION     WP_285032211.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 426)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..426
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45311
     Region          23..405
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(129,131,276,278,308..310,353)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mavllaaavl lgrtqdsgkt vvtvrlwdaq vaaayrsafa eftrrhpdie vrvdvvayas
       61 yfdslrtdva gggaddifwl snaylagyad tgrlldigkl lgrgasdawd rsvnqqftrd
      121 gtlwavpqlt dggvavyyna dllaaagvep adldtlrwsp dgddtlrpll arltldrqgn
      181 qagtpgfdag qvrqwgynaa namqdiylny igsaggqfsd ddrftfdnpg areafeylvr
      241 linadhvsps aadtngngdf srnqflqgrm alfqsgtynl aaiadqarfr wgaallpsgp
      301 agrvsvtngi aaaansatrh pdavravlqw mgstdgnafl gtkgaavpav lgaqpvyfdy
      361 wkqrgidvlp ffqvldgpri papggagfpa gfqairplfd emflgraava atltaaqraa
      421 naaadr
//
LOCUS       WP_285032318             104 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285032318
VERSION     WP_285032318.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..104
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=10608
     Region          2..104
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mswlvlvlsg vleavwatam gksegfsrls psivfavalt asmaglayam rdlpigtaya
       61 vwvgigavlt vvyamatgde pasllkvvfl tviiggvvgl klvh
//
LOCUS       WP_285032356             114 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285032356
VERSION     WP_285032356.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 114)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 114)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..114
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12644
     Region          1..90
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mstavearap lfdalgdpnr lrivvrlcet gpcstsqvtq vipvtrqaat khlllleavg
       61 lvtssrhgre riwriqpdpl aeaseyltal skrwdraldr lrsyvedqpa epie
//
LOCUS       WP_285032451             410 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285032451
VERSION     WP_285032451.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..410
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44518
     Region          163..386
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtpdqlwpda sdpvrrlire laetmltrsg evvadltaas lrdsryraia ddpvlaeada
       61 sltvanlkhw ltsniaepgr rvapatgsam rtyardvvlr glttddvasw rsaqrvgwkw
      121 wlaacfeatn daeqlrelie itgnslatfi ddsieelaah vgrvreefag gsqlqryatv
      181 elllqgadia psraeaqlgy altgshigvv vwvdseqdvg lleraseqvm racdadrrlt
      241 vvagtaalwl wipakatpta adlaerlgrr pgvrvalgrp aagvsgfrrt hmdaaaaqrl
      301 larlgsalsi vryedvhlvd llstdlssad qfvadvlgel kdaspvlhqt vltyvdegln
      361 rtstaerlyt hrntidrrla rvdellpkpf arnpievaaa ltllgvrggh
//
LOCUS       WP_285032472             401 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285032472
VERSION     WP_285032472.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..401
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43645
     Region          151..387
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mardgvddms vdartlladv isdgqieria evaervedsi gglfaepdgm rlsevidcil
       61 rinadvvasl iegrppdlal arglgarcce arvaladaqt lrrmvfdsdw rhlfislrsr
      121 avsmetavdv taahwelmsq idealvgayr evetnrkmqr aernavlvda llagampdpd
      181 ttfarlgelm iataplycva vvivaklgea plpnvenllr rqsfdsawrl gseaqvgiia
      241 vqsksgarql kdalvrlgas stgisipvsa leipkgwrla qlaaettser eqvvifgdnv
      301 artatvatsp evlrllseqt lrevlrlpqa trehlletfe rwldcggsvr ltalaldrhp
      361 ntvrqrlnki qeltgksldn prdvadlvvl igferaasks t
//
LOCUS       WP_285032488             427 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285032488
VERSION     WP_285032488.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..427
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45903
     Region          153..411
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 maggadrtga gdaltdavag igtrldarlt eitrsvsell vadirelrde eqlqqvlads
       61 vsanidaffa aarhgisidl lhapaaaleh arrlaqrdis anvlvrsyrl ghqavlkevl
      121 eeiraaeldp glgldvfdvm stisfsyidr isqevvevyq qareswlenr nsvriteire
      181 llaggdvdid aatvairypl qrthlavvlw cddsadrlae merlvqqfaa sigaadsplf
      241 isvdratawa wvavpaaaig eavtwlgslv padgpyvavg tpqsgvagfr lshrqaedar
      301 avavasgprr rrftafghrg ialaallgsn vdalsawate vlgplacstd gdqrlretlq
      361 aflkaggsnk aaaeelhlht nsvkyrvqra ierrgrpied drldvevall lcslfgdrll
      421 dpvddgg
//
LOCUS       WP_285032573             419 aa            linear   BCT 25-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285032573
VERSION     WP_285032573.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..419
                     /product="metal-dependent hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43658
     Region          24..>66
                     /region_name="metallo-dependent_hydrolases"
                     /note="Superfamily of metallo-dependent hydrolases (also
                     called amidohydrolase superfamily) is a large group of
                     proteins that show conservation in their 3-dimensional
                     fold (TIM barrel) and in details of their active site. The
                     vast majority of the members have a...; cl00281"
                     /db_xref="CDD:469705"
     Region          46..397
                     /region_name="Met_dep_hydrolase_A"
                     /note="Metallo-dependent hydrolases, subgroup A is part of
                     the superfamily of metallo-dependent hydrolases, a large
                     group of proteins that show conservation in their
                     3-dimensional fold (TIM barrel) and in details of their
                     active site. The vast majority of the...; cd01299"
                     /db_xref="CDD:238624"
     Site            order(64,66,242,262,330)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mtaltvlraa rwadvdtgev rspavilveg drikavnpve pvpdsaevvd lgdvtllpgl
       61 mdmelnllig gpggpeglps pmhgvqddpa yrtlrgavna rttldagftt vrnlglmvkt
      121 ggylldvalm raieqgwhag priypaghav tpygghldpt vfqrlapgim plsvgegian
      181 gvdevracvr yqvrhgakli kvsasggvms hstapgaqqy sddefaaiad eahragvrva
      241 ahavgdsair aciragidci ehgflasddt iklmadtgtf lvsttyltea maidriapel
      301 rkkaevvfpr aqamlpkaia agvriacgtd apavphgqna kelcalvsrg mtpmqairaa
      361 tvtsaelida ddelgrlapg fladivavpg dvssdiastl dvrfvmkagq ifkqvdgga
//
LOCUS       WP_285032511             270 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285032511
VERSION     WP_285032511.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 270)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 270)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14398449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..270
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29639
     Region          28..110
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          175..256
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mserpvielr rggralggsy lyegdalitg whshevhqie yalhglveve tdvahyllpp
       61 qqaawipagl phqavmnpdv ktvavmfdpg liadrsdrar iiavsplire mmiyalrwpi
      121 drpagdavsd gffrtfahlv aealdheapl slptsehpiv aaamaytkah lasataeqvs
      181 ravsvsersl rrlfqesigl swrtyllnar mlramallte pgqsvqatat avgfeslsaf
      241 trcftqfsgq spsayrrqta ettrpphesr
//
LOCUS       WP_285032587             438 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha
            [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285032587
VERSION     WP_285032587.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..438
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=50321
     Region          21..414
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
ORIGIN      
        1 mahfpkpaag swtenwpelg tapvdytdsi dpeqwkleqq aifrktwlhv grverlpkkg
       61 syftrempsv gagtsiivvk dekdgaqtvr afynmcrhrg nklvwndypg eevsgscrqf
      121 tckyhawrya lngdltfiqq eqeffdvdka dyplkpvrce vwegfifvnf dddaaplney
      181 lgdfakgleg ypfhemtevy syrseikanw klfidafvef yhapilhmkq atkeeadkla
      241 kvgfealhyd ikgdhsmiss wggmsppkdl gmvkpieril hsglfgpwdr pdikgilpde
      301 lppavnparq ktwgqdsfef fpnftlllwv pgwyltynyw ptgvdshife anlyfvppkn
      361 trqrlsqela avtfkeyalq dantleatqt qigtravtef plcdqeillr hlhhtahkyv
      421 deyksaqsvt tngrvahv
//
LOCUS       WP_285032612             285 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285032612
VERSION     WP_285032612.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..285
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30280
     Region          11..272
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mttpssvtgm levfdvqpag pgrfrgfsdg geraivdgtq llaqsivava kqlpaktirs
       61 ahaifgravq vdlpvdfvvd vvndgrsfaa avvaveqdgr rcatvtvlad tptpdvirhh
      121 adlpaiappa esnpspmpmi grelrlvdvv dvnspdevgp pelhawlhyd piprrddlak
      181 allahftghl sisttmraha gvgtsqahlt vstapmtvtv sfhepvgwdg wllyshestq
      241 vgagmsyvrg qvhtedgrli asftqegmir plrttdvava atarl
//
LOCUS       WP_285032642             396 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285032642
VERSION     WP_285032642.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..396
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43708
     Region          40..391
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mttidspvkh dyeripylva yqnnsavrdv yggvaelvvl esyllkpkak psdtvlvfmh
       61 pigggaylpm inalaraghh viycnsrfrg tdsallmekv vedlgecikd aknrlgyskv
      121 vlagwsgggs lsvfyqqqaq rptvtaspsg dgpdltklgl ipadglmlla ahisrhgtmt
      181 ewmdasilde ndpskrdpel dlynpdnpnq ppytpeflqr yhdaqvarnr ritkwvkekl
      241 aelraagrpd defafvvhgt madprwldpt vdpnertpgq cylgdprvvn mspvglarfc
      301 tlrswlsqws yddangdavk agpdiavptl vignladdac tpshtrrlfe aighedkemh
      361 eipganhyys gpdqrgtlrq avgictdwlh rqgfsl
//
LOCUS       WP_285032678             284 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285032678
VERSION     WP_285032678.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..284
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29297
     Region          4..284
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mkrgplpsws vpfvfvtgaa sqylgaaigv flfsttqpat vawlraaaga lvlmawrrpw
       61 rmrltrrria iatlfglitv gmniafyeal ariplgtava vefigptlva tlgsrrprdl
      121 laaalaaggv allagiefts elagvawala aaalwagyil vgkrvadthg gldtlalgms
      181 taaailgpvi iglqahtnsa vffeprtwll glgvgllsta ipygldqvvl rqvgqarfai
      241 llallpvtat iigltvlhqv paigeiagig lvvaglllga rgar
//
LOCUS       WP_285032685             248 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285032685
VERSION     WP_285032685.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..248
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27161
     Region          11..134
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mpltgertvp dlaeenywfr rhevvyrrlv ercrdrdvle agagegygad liadvarrvi
       61 gldydessva hiraryprve mlhgnlaalp lpdasvdivv nfqviehlwd qgqfvaeclr
      121 vlrpggvllm stpnritftp gsdtplnpfh trelnaaemt ellteqgfvm eamlgvyhga
      181 glreldarhg gsiiqaqidr avadapwpad lladvaavti ddfdllnada agvdiddsld
      241 lvaiavrp
//
LOCUS       WP_285032694             486 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA synthetase [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285032694
VERSION     WP_285032694.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..486
                     /product="acyl-CoA synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016405 - CoA-ligase activity [Evidence
                     IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0032787 - monocarboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=52316
     Region          7..474
                     /region_name="FACL_FadD13-like"
                     /note="fatty acyl-CoA synthetase, including FadD13;
                     cd17631"
                     /db_xref="CDD:341286"
     Site            order(143,146..151,153..154)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341286"
     Site            order(146,259..260,281..286,369,381,384,395,471)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341286"
     Site            order(146,187..188,235,237..238,241,259..260,281..286,369,
                     381,384,392..395,452)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341286"
     Site            order(187,237..238,241,259,392..394,446,452)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341286"
ORIGIN      
        1 mnmfsvldta atrfgdrgav yrgrtqlhtw kalrerasrl aaglgppgsr iaiasenrpe
       61 ivellfaiwa aecvavpiny klharemaqi lddsgaslif asptiaarle rpaevigaeg
      121 ysqrlvappi dppdtdpaal awlfytsgtt grskgamlsh rnlmamtlah ladlddpden
      181 csllhgapms hgsglyippy vlrgarqvvp essafepgef ldlcehhpgs saflaptmva
      241 rlvgtgrarp rnlraliygg gpmyldglkk amaafgpvfa qlygqgeapm titglrradh
      301 esgddavlgs vgyarsgvev avlrqdgtra dageigeivc rgdvvmagyw nnptatadav
      361 rggwlytgdm gsfddrgylt lrdrskdvvi sggsniypre veevllthpd vaeaavvgap
      421 dpewgevvva fivgtapada ldahlleria rfkrpkryih idempknsyg kvlkrelrsr
      481 laefaq
//
LOCUS       WP_285032701             515 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285032701
VERSION     WP_285032701.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..515
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=54158
     Region          156..511
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mssslsdvvv aeppppsrrc rkyaprtwtl rsrlivvvsv lgaglctavg aatlialrhf
       61 ligqldtqvs daesrsvtff efgpppflrf sgpgpmflda pgqsagtvga iisqpgqsqg
      121 aviitsgdrr svspaaltql ervpqghkvs vdldglgryr ltaqqshdav vvaglpvsgv
      181 qqtlgsvtwm iggfsavala aaiaagsami rrelvplsrm seaaqhvagl plhegdvrlp
      241 sqiepvdada ahtevgrlgt alnrmvdrva dglatrhase trvrqfvada shelrtplas
      301 iqgytevarr lvigtpahrs deqgedlvya ltrvhaesrr msqlvedmll larldagrpl
      361 ehndvdlsqm vidavsdahm agpehrwald lpdqpvvvfg dhqrlqqvla nllsnarvht
      421 pagttvsttl aadsdgstrl rvadsgpgip sdllpeifer fargdesrsr aagstglgla
      481 iaqavvhahg gtiavdsgpd gsaftvtlpa rgaqs
//
LOCUS       WP_285032720             282 aa            linear   BCT 25-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285032720
VERSION     WP_285032720.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..282
                     /product="MlaE family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30081
     Region          16..272
                     /region_name="MlaE"
                     /note="Permease subunit MlaE of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG0767"
                     /db_xref="CDD:440530"
ORIGIN      
        1 maapsaflet rrsvvrtirq plieagqwal figttlwylp ltlrryyrqt lqamnslawg
       61 rgslivdggt isvllflgia vgasvaiegf ailnligfga msgiiggvgt vreigplvag
      121 iaftsqagcr mtaeigamri seeidalevl glrpipfvvg trliggllvv ipgylltmva
      181 afyvqstfik vfydqpggty dhylsmfltp tdlvysaika stfciavtli hcyygyftsg
      241 gpagvgqasg ravrtslvav mildfaltva lwglqpqfvf rg
//
LOCUS       WP_285032744             111 aa            linear   BCT 25-DEC-2024
DEFINITION  indolepyruvate ferredoxin oxidoreductase subunit alpha
            [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285032744
VERSION     WP_285032744.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..111
                     /product="indolepyruvate ferredoxin oxidoreductase subunit
                     alpha"
                     /calculated_mol_wt=11872
     Region          1..55
                     /region_name="IorA"
                     /note="TPP-dependent indolepyruvate ferredoxin
                     oxidoreductase, alpha subunit [Energy production and
                     conversion]; COG4231"
                     /db_xref="CDD:443375"
ORIGIN      
        1 mtyvindaci gemdgscvev cpvdciyegl tkryihprec vecgaclstc pvdailtpde
       61 fndapdvfed narffdeplp greqplgdpg gatplgpigv dtprvgprkd k
//
LOCUS       WP_285032800             412 aa            linear   BCT 25-DEC-2024
DEFINITION  HNH endonuclease [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285032800
VERSION     WP_285032800.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..412
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43877
     Region          39..325
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          308..365
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mgiasdlhpl ldhlrdvvlp demagddale varcllrmrn vvdhlaatla gvldrcgvaa
       61 gqgrtlrell mslgcapava erlvrvggal pllptlaaha cdgavsgehv daivkginhi
      121 rtrspgevde earfrqvadl lgqffsgatp atiadrarkl gnraaaaegg lpaaedrlvn
      181 tlehrvtsdg rlqvradlda evgaklvaav eelsaprpep dgspdtrsas rrradaleav
      241 ldmaarggdv asaprtqllv tvpaqvpdla elafmgsist mtlericcdt avttvvvdge
      301 qvpldmgrek rlfpphlrka lylrdqccik cgappgrtha hhivhwthgg etslgngcll
      361 cpachanvhh dgwdvvmgld rhpwlippat vdpqrnpvpa ynrrtmrldh aa
//
LOCUS       WP_285032801             172 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285032801
VERSION     WP_285032801.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..172
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18447
     Region          54..167
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mptsaslrrq slvrsavftv ivpgtmagli pysltsgwrr agdllgipga wvggvvlivl
       61 glpvllaaiy kfasdglgtp lpgaptqtlv vtgphryvrn pmylavaavi vgqalvlgqp
      121 vllwyaaffv lataafvyfy eqpallrqfg deyrrycasv pawlprvtpy rp
//
LOCUS       WP_285032803             713 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285032803
VERSION     WP_285032803.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 713)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 713)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 713)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..713
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73226
     Region          3..712
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mttsvtlsvg gmtcsscaar iekrlnridg vhasvnfate qaaithpdsv ttdelvaave
       61 atgytasink adapaetayl prllvslalt ipvialsmip alqfphwplw alalatpvvf
      121 wgawplhhaa wtnlrhgaat mdtlvslgvl tsylwsawml stgsdhlyle vaatvttlil
      181 agkffetrak rqsgaalral ldlgakdvav lrdghetrvp ieelavgdvf vvrpgekiat
      241 dgvvvsgtsa vdasmltges vpvevgpgdq lagatvnagg rleveatrvg adtqlaqmar
      301 lvadaqsgka evqrladrvs avfvpvvial alltlvgwli agsagaseva ggstvsaalt
      361 aavsvliiac pcalglatpt allvgtgrga qlgilikgpq vlestrkvdt vvldktgtvt
      421 tgkmtvaavh aesanvlrla galehasehp iaqaiatraa edgslpavtd fvnhdgrgvt
      481 gvvdghevav grrswltada spqlqtaaqk aeaegrtpvw vavdgaiagv ivvsdkvkdt
      541 aaeaiadlkk lglkpvllsg dnaraagava aevgietvia evlpadkvde ikrlqdqgrv
      601 vamvgdgvnd aaalaqadlg lamgtgtdva ieasdltlvs gdlraagdai rlsratlkti
      661 kgnlfwafay nvaaiplaam gmlnpmiasa amafsslfvv snslrlrrfk psr
//
LOCUS       WP_285032889             208 aa            linear   BCT 25-DEC-2024
DEFINITION  endonuclease III domain-containing protein [Lactobacillus iners].
ACCESSION   WP_285032889
VERSION     WP_285032889.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Kuo,C.F., McRee,D.E., Fisher,C.L., O'Handley,S.F., Cunningham,R.P.
            and Tainer,J.A.
  TITLE     Atomic structure of the DNA repair [4Fe-4S] enzyme endonuclease III
  JOURNAL   Science 258 (5081), 434-440 (1992)
   PUBMED   1411536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..208
                     /product="endonuclease III domain-containing protein"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=23124
     Region          22..192
                     /region_name="Nth"
                     /note="Endonuclease III [Replication, recombination and
                     repair]; COG0177"
                     /db_xref="CDD:439947"
ORIGIN      
        1 mtsnnlvgit earqilykii slfpdtkgel kwgtpfqllc avlmsaqttd kmvnkvtpil
       61 fekfpnsksl aaanisdiea cirniglyrt kakhlkatat lienkyqgiv pknkkalltl
      121 pgvgiktanv vlaeafgvps iavdthvmri akqfkivpks aepsqietil enimpekdwi
      181 klhhamiafg rykmpakyrn enpynflk
//
LOCUS       WP_285033048             754 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Lactobacillus iners].
ACCESSION   WP_285033048
VERSION     WP_285033048.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..754
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=83183
     Region          18..181
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <278..754
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 mprkntsisk vkkeklewvi tglilavlvl fscadfgllg nqatnlvrlf fgdahylasa
       61 iigvcalvmi iynqpphlgk krtwglivft ialtawcssl lfqklmlqhd ymsifltrig
      121 qeflhgrdsm svgggligtl fcqifnylfg sygskfiegl livtgllmff dvkfrtivkk
      181 fqtlskffia knkdagillk dkytdlieny hdqhkekqdf pnigdldapk neqlpesapv
      241 dvvvdkandl sndneisela hdlvkkddkn slgrldyvyp sldlldavpn tdqssdskli
      301 kqntltlent fssfgvsviv kkavlgptvt ryevqpavgv kvsrivnltd dlalalaakd
      361 irieapipgk pfigievpnk vastvsfrev mqkqenkakq evlsvplgkn vtgqivsadl
      421 rkmphlliag atgsgksvai ntiitgilmk ahpddvklil idpkmvelsv yggiphllip
      481 vvtdaklats alrkavreme rryqlfaagg vrnigeynek vtlnnqnkan svmellpyiv
      541 vivdelsdlm mvagreveds ivrlaqmara agihmilatq rpsvdvitgl ikanvpsris
      601 favssgidsr tildqvgaek llgrgdmlyl pigaskperi qgayinvdev ervvdwvkkq
      661 qateydqkmi psdsedaend nseqddtdde fyqqavdlvr qqqtasvsll qrrfrigynr
      721 aarivdamek ngivgpstga kprevllppl kdee
//
LOCUS       WP_285033382             427 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285033382
VERSION     WP_285033382.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..427
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=45933
     Region          21..328
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mttrvfpsaa eiaqrtpadr draidviriv slvgvvaght vmatsiidhe vfrwgnlltt
       61 svvfqaltwv fqimplfffa gvaasagsyr sgtswggwll krctrlyrpv fyyltfwaga
      121 llilkpllpi hvyepvagis iqllwflgay vmvlaavpll arittrgqlv aavagtyalv
      181 alvdairind hawsalgyln fvvwllpgml gvayrrgllt ttaalrvglg mlavnvalvw
      241 agpyelslvg ietqhiknmt ppslllagha immcafaiaa apaisrwaar pqvwrlavig
      301 ntgamtlylw hmpallgmhl afdlagmpry pgqphflvls vyqmtimaal vaglflllrp
      361 lennplplwd ggrvsapgwr satvgallvi agaatlasvg wglketglqc vsvmlaalva
      421 aralard
//
LOCUS       WP_285033386             501 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285033386
VERSION     WP_285033386.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..501
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=55083
     Region          4..452
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mehtdnttqv dvlivgagis gigaayylqq ehpgrsyail esrgatggtw dlfrypgirs
       61 dsdlhtfgye fkpwrdedai asadkilayl retvrehnid rnirfhhkvl gaawdsgtar
      121 wlvdvertdt gelvqisanw lfcaggyyry dqgftpqfpg rdryagqvvh pqhwpedldy
      181 tgkkvvvigs gatavtlvps maakaahvtm lqrsptyilp vpskdafanv aarvlgadrg
      241 yalarrknvi rqravytlcq kypaaarrvi rwtnarelpe gydvdthfsp gykpwdqrlc
      301 tvpdadlfka igsgkasvvt driatftetg ielesgehld adiivtatgl nvqlfggvsl
      361 tvdgqavnls dtvaykgiml sgvpnfafaf gytnsswtlk vgllcehfcr llshmdeggf
      421 dsvrpefdaa gmatkplldf aagyvqrvad tlprqgaegp wvmsmnynfd revlrhgava
      481 dpnlrfaats raevrafapv s
//
LOCUS       WP_285033454             335 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: DHH family phosphoesterase [Mycolicibacterium].
ACCESSION   WP_285033454
VERSION     WP_285033454.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium
  ORGANISM  Mycolicibacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Mycolicibacterium"
                     /db_xref="taxon:1866885"
     Protein         1..335
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=34663
     Region          24..334
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mqvtaieptt eirpqgarvd argaadllga vdsvsvvahv ypdadtigag lalalvlsea
       61 gkdvqvgfaa patvpdslqt lpgghllvpp dqmrpdadlv vtvdipsvnr lgslakladp
      121 grqvlvidhh asnrlfgtan yvdpsadstt mlvaelldaw gkpiklpvah clyaglttdt
      181 gsfrwasara yrlaarlldi gvdnaavsra lldthpyswl pmlsrvlsta clvpaaaggk
      241 glvyavvshq eyaaarseev esivdivrtt seaevaavlk eiepgqwsms lraktevdvs
      301 vlassfgggg hrfaagysst gtaddvvaal vaals
//
LOCUS       WP_285033509             467 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285033509
VERSION     WP_285033509.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..467
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50520
     Region          2..455
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 magaietrsi dwiptaerrg kvhhqapfwf tgnfvlttmv tgflgpangl sagwsvlaav
       61 agacfgtlfm cfhanqgptm glpqmiqsra qfgsrgalvp fvavifvyig fnvfntilat
      121 sgfktvfagp nwlwylglmv aaiviavvgf dlmmvvqrwl tyllivvfgv ltvyalstlh
      181 ldaaipdggk fsltvflmqf aaaagyqisy avyvsdysry lpentsakhv iwwtylgaag
      241 ssvwlmslga vlasalptpd aivsiqtvgn qllpgfgtft vvvasialvt imsvnaygas
      301 ltsmsaldaf rpitptvrlr vlgialtsfv afvvalslpe gylesfntfv llmlyflipw
      361 tavnlvdfyf vrrghysivd ifrpdgiygr wswrglaayf igmvsmvpfv slhfyagpia
      421 kmlggvdisf ivglavsgla yyvltrgvdl aperaavers rqeltta
//
LOCUS       WP_285033518             249 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Mycolicibacterium].
ACCESSION   WP_285033518
VERSION     WP_285033518.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium
  ORGANISM  Mycolicibacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Mycolicibacterium"
                     /db_xref="taxon:1866885"
     Protein         1..249
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25699
     Region          25..228
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mklpsgapea vgtatavasa tavsdghtrs aivqlllega vtatqigeql gisaagvrrh
       61 ldalieagda essaaaawqh ngrgrpakry rltaagrakl ghtyddlaaa amrqlreigg
      121 ddairtfarr ridsilsgva atdditdtad qvaaaltqag yattttpvtg piggvqicqh
      181 hcpvshvaee fpelcdaere afaevlgthv qrlativngd cactthvpvi pehavhsihp
      241 atqeegvsq
//
LOCUS       WP_285033635             852 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285033635
VERSION     WP_285033635.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 852)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 852)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   3  (residues 1 to 852)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   4  (residues 1 to 852)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
REFERENCE   5  (residues 1 to 852)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   6  (residues 1 to 852)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..852
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..852
                     /product="flavin-containing monooxygenase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=92068
     Region          1..477
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
     Region          618..816
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mtsdvdavvv gagfaglclv hrlrergfsv rvfeaaddig gtwywnrypg arvdipsldy
       61 mfsfdpdwhg dwqwsekyat qpeilrylnh vadkfdlrrd mtfgtrvtsa hwddgcwrvr
      121 tdrgddvacr hlvmatgcls ipkepdiagl etftgetfyt srwphepvyf tgkrvavigt
      181 gssgiqsipl iaaqaaqltv fqrtpcfsip ahngpvsqek qaaladetay raaarasfgg
      241 vpqertlipt favpeayrqq ryerawqige lletlnmfsd lmsnpaanaa fadfvrdkir
      301 tavhdpqtae llcpkdypvg akrlcldtdy hatfnqphvr lvdlrtqplv gvteggiatv
      361 gesfdfdtlv fatgfdaitg avtaidivgr dgltlkdkwa pgpstylglt ttgfpnlfli
      421 tgpgspsvls nmavsieqhv elvadtmayl rdhrfdtiep tptaeagwmq hvadagaitl
      481 fpqanswyvg anipgkprvf mpyaagvdfy aaacadvvaq gylgfqltgp agsqchdgvv
      541 rrlqpdvqmv ldmvamlnpp pleslpvdva raamveanaa rppgpdvgei idgrfpgtag
      601 eldfrlyrpa tprphpvvvy fhgggwvlgd arsddplcrd lcvradalvl smdyrhapeh
      661 pfpaavddgi aalrwvadna avlggipdrl avagwsaggn iaavvcqwar dhggphisgq
      721 lllspvtdaq pypsyqenae gygltaplmq wfaalydgpa ddprrsplrg dlaglppamv
      781 vtcefdplrd egnayaaala aagvptehvq arghthlstt mvdlvvsgep vraqmaaalr
      841 gflatqpssl qa
//
LOCUS       WP_285033829             210 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285033829
VERSION     WP_285033829.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..210
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23034
     Region          7..115
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mldwdhnayy qrlllqhlpp rcqrvldvgc gaggfavqla qrsdhvdavd rsaamiaear
       61 rrtpanvncv qadvltdgvp atgydaivsi salhhmpldt vlphladalr pggvlaaial
      121 prtdlrhewp helagalahr algvrfraer llkigtgfak tpdhdvmpvv ldpplttrev
      181 aaqtaellpg arvrrllfwr yllvwqkpdl
//
LOCUS       WP_285033844             369 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Lactobacillus iners].
ACCESSION   WP_285033844
VERSION     WP_285033844.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..369
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=40448
     Region          16..368
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mdaksklltl inariekvtk likeknadal iiinqanyry ltnftgeeae lilcangdri
       61 llsdsrfagq ikkqapgemk vimkhknsvs eiteqlrhls lkkvlvegea isaidyqnlv
      121 nsnsdiefem alelvevarn vkdeleldal kqaiaissqs fteilpmlqp gvtereigak
      181 ldylfkvngg dgpsfdtiia sgyrsswahg vasdkklqkg elvvidfgsf yhgytaditr
      241 tvalgqvpae lqkiykivye aqkqgiatav agktgadvdk aardyiceqg ygqyfghgig
      301 hgigleihel cmpalpfske vlkdnmaitv epgiylpdfg gvrieddili ngnspetmsk
      361 lpkeellvl
//
LOCUS       WP_285033881             400 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285033881
VERSION     WP_285033881.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..400
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43062
     Region          71..392
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mtknangegs iykrtrdgks lgyggaitye dgdgrtrrht vygrtraevr eklgkvrerl
       61 daggppkdas vtvgawmarw rattlavsdr kestrelyst lsrrhlepap fgdrrldklr
      121 ptdvealvle lrsrtkpgkv teadpkptpv raladstvrq iytvlragld gavrdgllak
      181 npaaavkrpg verreaqhld tgrvvavlqa aeqsryypal aliantglrr gevlalrwad
      241 vdldgaklkv vgtlgrvgkr gllitapktd rsrrtvplnp amvtllrkhr asqaaeqlra
      301 anqwstsglv fttelgtavd prnllrviee aakdvgvagi gvhtlrhsaa vawleagvhi
      361 kavadllghs svaitgdvyg htsdetaraa vdglatslgm
//
LOCUS       WP_285034080             421 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285034080
VERSION     WP_285034080.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..421
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45803
     Region          169..409
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mdpavseann aimtrliarq tevarsvgqr lasditelrg dpeiiellra svggnvetif
       61 halrydisle nieaptaale yarrlaqrgv pmnaltrayr ighalvldva geeinragfa
      121 pqtslaffer ltsvtfryid wisqqvvtvy ederdrwlan rnstqalrvr evlsgndsdp
      181 eaitaairyp mrrrhlgvvl wwpsgsghvt ghddalakle qflraaaehv gsqgsplfla
      241 adqrtgwgwl plsgatapaa saqlrqftds hpnapavaig iplpgvdgfr rshrqalrah
      301 svavtadltg vtaaddpgfa aaalmgenqd darefvhtvl gplagaggnd arlretlqvf
      361 lrhggsytaa adelvvhfnt vkyrvgrale rrgrplgddr ldiemalllc qwyaaavlld
      421 e
//
LOCUS       WP_285034192             374 aa            linear   BCT 25-DEC-2024
DEFINITION  saccharopine dehydrogenase family protein [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285034192
VERSION     WP_285034192.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..374
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40923
     Region          1..371
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 mseprpvviy gasgytgrlv aeylreysip fvaagrnkak lqeilksvpg ietadyeiae
       61 vdgsvdslta lfegrrvvcn mvgpflryap avleasvrtg chyldtageq khhlsllndw
      121 gpkfaaagaa vstavsiqya vpdiaarivl enpgidtlel geyvnavptv gstqsifdvi
      181 rtdafyledn vlkkydgiye qdivvpgtgy vvpglnwggt ampvffrddh rvrncrmlva
      241 mqnqardipt rvraaermfk vvfqwlpedk lfpvldrvaa gmtpvtppre nrqvhrsidw
      301 ctgrgnnvta ravihgtsgy qmtgliqayi amrllgnnfn gvgfrspael vghrellgal
      361 esyglarlte dsva
//
LOCUS       WP_285034253             459 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha
            [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285034253
VERSION     WP_285034253.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 459)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 459)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..459
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=50920
     Region          27..>228
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
     Region          192..444
                     /region_name="SRPBCC"
                     /note="START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC)
                     ligand-binding domain superfamily; cl14643"
                     /db_xref="CDD:472699"
     Site            order(200,202,204,211..213,215..216,255,258,260,295,299,
                     301,303,305,307,327..328,330,332,338,340,342,344,358..362,
                     371..372,375..377,380)
                     /site_type="active"
                     /note="hydrophobic ligand binding site [active]"
                     /db_xref="CDD:176854"
ORIGIN      
        1 mtvitptvas evtrildrve teieknrvpa eiwnndaifr aeldqvfgtc wvfvahesei
       61 pkpgdfvqrr igldpvivtr dgkgginvls nycrhrgtqv cqtdtgnsrf fkcpyhgwty
      121 snngdlvgtp hmreaygtrl dpkewglkra prvdvrsgfi faslaqegps ldeylggggw
      181 mldilanlap ggmkvagppe ryqvngdwka gaenfsgday hadtlhwsne eiqmiqglga
      241 naemmhayel gdghatlgfp wakiglplwg yspetvaqfd lsvlddaqry vletnpptig
      301 tifpnfsylr vasptlpggp ptvvttfrvw qpiapgkmel wnwqfvfecq sdqekldsyv
      361 tgqlifgsag nfetddtvaw egapraaksa wmqrenlsfn fdqagrttvd vtpdpdyhgp
      421 gikratgfge fvqlnfyrhw lavmrgdasa ttsegrhsr
//
LOCUS       WP_285034350             223 aa            linear   BCT 25-DEC-2024
DEFINITION  PaaI family thioesterase [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285034350
VERSION     WP_285034350.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Song,F., Zhuang,Z., Finci,L., Dunaway-Mariano,D., Kniewel,R.,
            Buglino,J.A., Solorzano,V., Wu,J. and Lima,C.D.
  TITLE     Structure, function, and mechanism of the phenylacetate pathway hot
            dog-fold thioesterase PaaI
  JOURNAL   J Biol Chem 281 (16), 11028-11038 (2006)
   PUBMED   16464851
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20171116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..223
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22748
     Region          <2..73
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
     Region          115..220
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 maadhilgev sfirrqpgew sltteltldf vgglvapgsv lqvkgsavrl esksgfvsga
       61 itdgagtpvv lattrivnvl gepemtppaq pqaliagsak idasleenls isyvagadgl
      121 tarlsepaaw tngfrilhgg vwacvaeava stavattndg lstahmhvsy lrpgvpaagi
      181 natadvvhvg grfalvsvrg yaddgtlctv asitfrriep sis
//
LOCUS       WP_285034478             520 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Mycolicibacterium sp.
            lyk4-40-TYG-92].
ACCESSION   WP_285034478
VERSION     WP_285034478.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..520
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55445
     Region          1..518
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 maqfdaivvg aghnglasav mlqkaglrtl clesklysgg mastvelfdg fkfeiagseq
       61 fptslkvsqe lgldevpsve qevmsvnmrg igdepllfys dpmkllthmn evhgaeavng
      121 maglmawsma paralgrfda glppktydem yacatnefer saitdmlfgs vtdvldrylp
      181 dkdkhgairg mlsvlacnst yrgpatpgsa aalafglavp tdgaslmrkl kggigalakh
      241 ledtfvahgg evrlrsavaa itvadgrvtg vrlddgteia apvvvsslap sltvdrllga
      301 avpddvrary arvdhrgsyl qmhfaldgip efaepyemln npelqgtigl fstpeelqqq
      361 wedsrrgivp adpsiawqip svldpelapp gkhassafal wfpvegdagg sakygsmkre
      421 mgqrvidkit rvapnfekli lrhttftprh mdrmfgapgg dychglihpe qmgpnrpgpr
      481 gyldqelpva glylggagch ggpavnfipg ynaahavlnt
//
LOCUS       WP_285034500             451 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Mycolicibacterium sp. lyk4-40-TYG-92].
ACCESSION   WP_285034500
VERSION     WP_285034500.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. lyk4-40-TYG-92
  ORGANISM  Mycolicibacterium sp. lyk4-40-TYG-92
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Mycolicibacterium sp. lyk4-40-TYG-92"
                     /db_xref="taxon:3040295"
     Protein         1..451
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47038
     Region          158..436
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mniglldgwl ptliqvvtvl alvvavgrrs prwlrlwlpv afgtgvvlal aaswfisdqg
       61 laggpaptsl wvwlvltgva lvvaiagwpg lhwwrravav avvplcavca glavntwtgy
      121 lptvealwqr atgaelrgei dlqtaltmrr sgerpdrgvl vsvqipttas gfrarpelvy
      181 lppawfakda pqlpavvmvg gefgwpadwp taggaqrtad efaaahggna pilvfvdtsg
      241 qfsndtecvn gprgmaadhl tkdvvpfvas tfsassdpsr wgivgwsagg tcavmttvmh
      301 pelfqtfvdm dgqvgpnags epqtiarlfg gdaaafahfd patvvrkrgp ytgiagwfav
      361 sengpvvyqp aqagapanvq ppdnpeshta vatymcalvs aagiecsvvp hggdhtfpsa
      421 aevfaaalpw lagrlhtpgv pavglpgstp r
//
LOCUS       WP_285034631             141 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein, partial [Lactobacillus crispatus].
ACCESSION   WP_285034631
VERSION     WP_285034631.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..>141
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          5..>141
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
ORIGIN      
        1 mskiivgryi pgdsliykmd prskllvtil filaiflann sityaivtif cflaviatgl
       61 nakvfwdgvk pligliffts llqlffmtgg hiywhwwifs lssyglinai yifirftlii
      121 listvmtvtt mpleiadame w
//
LOCUS       WP_285034661             149 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein, partial [Lactobacillus crispatus].
ACCESSION   WP_285034661
VERSION     WP_285034661.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         <1..149
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          <1..144
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(42,46,49..50,52..53,98,101..102,104..109,112..114,
                     118,120)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(63..70,86,89..90,93)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 tliilistvm tvttmpleia damewllkpl klfkvpvdki alvisialrf vptlfdetfk
       61 imnaqrsrga dfndggliqr akaitpilvp lfiqsletai dlstamesrg yrssegrtky
      121 rvlswskydl ialfyfvllv gllltfrty
//
LOCUS       WP_285034834             221 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285034834
VERSION     WP_285034834.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 221)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..221
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=22613
     Region          6..204
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mslitiigag pglgleiara fgrrgfdval vartqsklda laqtlagegi tahgfaadis
       61 rpdtvtaalr sitdtlgpid vlefspadps lapvdvlevt menlqpqldf ylggalaavg
      121 avlpdmiaag kgtvlittgg gsispmpflg nvniaaaglr nwalnlhnal qpkgvyvahl
      181 gitaligggh pdaepeviae alaqlhderq qaelhyvayn g
//
LOCUS       WP_285034849             115 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285034849
VERSION     WP_285034849.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..115
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12267
     Region          1..107
                     /region_name="ArsR_Rv2640c_fam"
                     /note="Rv2640c family ArsR-like transcriptional regulator;
                     NF041413"
                     /db_xref="CDD:469304"
ORIGIN      
        1 mqielpllea daaacctpvt ggvlaldeae riahtfkala dpnrvrllsf iaaseggeac
       61 icdltepvgl tqptvshhmk ilvdaglatr eqrgrwayfr vitdgleras qairp
//
LOCUS       WP_285034885             365 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285034885
VERSION     WP_285034885.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 365)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..365
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37111
     Region          56..361
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msrppaapat ldpadgsdvp tsgagkrssd sphrtavlat gllvatllla aatitslavg
       61 nraidpvtvl halfsydhen plhlmvvelr vprtllgvlv gaalavcggl iqaftrnpla
      121 dpgilgvnag asfavtfavg vlglttpgay vpfalagafv ltllvyvlgs vgssgatpmk
      181 ltlagvalga actgfttaiv lrdegtlqvm rfwsvgsigg rtldqlvwaa plivvgllig
      241 lacarslnal tlgddlaqal garvrstrvw vvvavtilag tgvaaagpia fvglmiphvv
      301 rwftgpdqrw vlstsmvvgp afllladvlg rivlpsgelr vgivtallga pilimlvrrk
      361 rvsgl
//
LOCUS       WP_285034892             799 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-glucosidase family protein [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285034892
VERSION     WP_285034892.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 799)
  AUTHORS   Varghese,J.N., Hrmova,M. and Fincher,G.B.
  TITLE     Three-dimensional structure of a barley beta-D-glucan exohydrolase,
            a family 3 glycosyl hydrolase
  JOURNAL   Structure 7 (2), 179-190 (1999)
   PUBMED   10368285
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444920
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..799
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..799
                     /product="beta-glucosidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0015926 - glucosidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=83226
     Region          38..523
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          411..645
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
     Region          683..751
                     /region_name="Fn3-like"
                     /note="Fibronectin type III-like domain; pfam14310"
                     /db_xref="CDD:433860"
ORIGIN      
        1 mtlqhegprs atrpvergrw nvrslspver aqalleamtl eekvaqlgsv wftdsggdfa
       61 psveatdsta aaetvssptd tgfdgglgql trifgtepvt vpdgvrrlse lqqqvvdgnr
      121 fgipaiahee cltgfaayga tafptplawa asfdedlver laesigadlr avgvhqglap
      181 vldvvrdyrw grveetlged pylvgqlgaa yvrglertgv vatlkhfagy aasrgaknhg
      241 pvsigrrela dvvlppfeta irlggarsvm naytdldgvp agasvelltg vlrdewgfdg
      301 tvvadywaip flatmhriad gaaeagalal tagidvelpe tvgfgaalvg svrdgtvsea
      361 lvdravlrhl rqkvelglld ggplvpedaa atdldgprnr aiatrlaees ivllrnsgvl
      421 pldarsriav igpaadqfrs lvgcyafpnh vlskhpghdl giaiptllda vrtefpgadl
      481 vseegcgitt tdrsgipaav raateadvvv lavgdiaglf gdgtsgegcd aedlrlpggq
      541 helvlavlat gtpvvlvvls grpyalgeyg aaeavvqaff pgqegaaava gvlsgrvaps
      601 grlpvqiprs pamsgtslqp plglasrgis vldptplypf ghgltggdvr yrsleaapel
      661 avdgellvev tvenvgdada vevvqlygsd lvasvvrpav eliafaridl aagttatvrf
      721 avsadrlsft gvdgrrvvep grsvlsagps agerpvtrti evtgtrrvlt grrslrvdwh
      781 rlgpddrgfd lavdptggr
//
LOCUS       WP_285034895             335 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285034895
VERSION     WP_285034895.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..335
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=35396
     Region          10..326
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mndapagpgp rraavvvnps kvdvaalraa vadaealhgl spstwhetsa dddgraaaea
       61 aiattpsvil vaggdgtlrv aagavastgi plalvpagtg nlfaralglp lndlrrsvei
      121 awsghdqpvd vgrvrlgrsd gthgeevflv magigldahm aghtnawlkr rigwlaysdp
      181 iarsifgnrq fdlhyrldel pettarahti ivgnsgtltg gvlllpeavv ddglldavml
      241 rpergpgwtn igyrltfnrm lhrtrfgrlv grfspkvrai syaqatsmrv rldepqeiql
      301 dgdshgavts valtnlhhal ivrvpegarp rplad
//
LOCUS       WP_285034998             623 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 35 protein [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285034998
VERSION     WP_285034998.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 623)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 623)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 623)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 623)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12015514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..623
                     /product="glycoside hydrolase family 35 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=67545
     Region          34..347
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
     Region          <560..596
                     /region_name="BetaGal_dom4_5"
                     /note="Beta-galactosidase jelly roll domain; pfam13364"
                     /db_xref="CDD:463857"
ORIGIN      
        1 mtkfadavgs alphvadepq pavpaalhwg dgklfrngvp hsirsgslhy frvvpehwrd
       61 rmlrfvdlgl nsidtyipwn fhqpqvdaap gftgwrdiga fmdtaadlgl dvllrpgpyi
      121 caewsngglp awltarditl rssdpgyqqp vetwfeelip rlapyqavhg gpvvavqven
      181 eygsygddar ypgwlasllr rlgvqellyt adgptdlmid ggsipgimma atlgskpdea
      241 rallrsrrpd epffvaefwn gwfdhwgqph hvrdadnaae vargiltdgg sisiymahgg
      301 tnfglwsgan lvdgelrpti tsydsdapia edgrltpkff alrealgmad qplrspelry
      361 lpersvplqh gaglldalgg lggplaerta spasfedldv dgglvvyead vllpdrpvel
      421 vfdgvadrgq ifldgehqat itaagtvtvi gtglvskltv vvenlgrvny gpqlgsrkgl
      481 lgpvlverrl vhgwrarpva ldrldalhlr svversvier sgdgatpggt gdgglssgtf
      541 hvdepldthl rlpgftkgfv wingallgry wnigpqqtly vpgpllrsgs nrivvlelhr
      601 sgsgvefvsr pelgpteeyv eef
//
LOCUS       WP_285034942             485 aa            linear   BCT 25-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285034942
VERSION     WP_285034942.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..485
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=51640
     Region          6..452
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mttlptptrt qlfiageftd gtssertevi spvtgdvvas ipvagtaeld eavrraheaq
       61 rewrklgvfk raeichrvgd ainarveela rlqtleqgkp laesiadiae aaqlfhlhae
      121 dalrlygetl pssdidkrmf twrapvgvwg iitpwnfpll mfsefvapgl vtgnacivkp
      181 psntplavla amdclveagv paglvsvlpg dgafgselvs hdgidaigfi gssatgakiv
      241 rtaglkrslm ecsgngpivv ledanieraa kaavdsafys ggqvccater livhqnvhdv
      301 fveaalayat anvrlgnpfd eginlgplnn egvaakmdrh ldearslgfd illgggraag
      361 hptdlyydft ivdgvsedsl lsreesfgpv lpiltakddd dilrianada lglqsavftd
      421 slskayrfme eletgqvivn dsngwwdinm pfggaggkgt gwgriggmyt lhdmtdlrtg
      481 aihir
//
LOCUS       WP_285035027             544 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285035027
VERSION     WP_285035027.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..544
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=56666
     Region          178..513
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mstgavptag vptfppkqrh pwtlqrrlvt giaaviaavl avsgvltivt veasvtavvd
       61 tqltgsmeaf ehsvvkfhdq qsrdgavadp datrgepgyv kpfvdyvghg pgtlialitd
      121 gqvvdsarft qsnakaldvr tqalieeaaa aggterqnig lgslggyrle fldhgdgetl
      181 vagvslatpr aavqqeaivi ailavlalav tivgaiivvr lalrplsrva aaaaevstlq
      241 lergdtgidv rvdqadtdpr teigkvgeal nglidhvdra lavraatdkr mrrfvtdash
      301 elrtplaaiq gyaeltrqds enlppmteha larieseatr msslvselll larldegqdl
      361 hlddvdlsdl vaaavsdaav sapghhwsvd vperaiivrg drerlhqlvv nllsnaavht
      421 pagtsvvtri aapknadepq raaltiaddg pgideaflpe lfdrfarads srsraagstg
      481 lglaialsia eghegaieva sspagttftv tlpwsgpsde hpavrssagg aaavhpdevp
      541 sars
//
LOCUS       WP_285035095             279 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Plantibacter
            sp. ME-Dv--P-095].
ACCESSION   WP_285035095
VERSION     WP_285035095.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..279
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30137
     Region          2..279
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mriavtggsg klgrtvvghl rehghlvinf dqagergdgf vridlrdagq vfdaltgvde
       61 qapdgfdavv hlsaipapgl stntatfqnn iigtynvfna aikagitniv tassetvlgl
      121 pfdtpppyip vdeayaarpe styslskhle eqlaieltrw hpelkiialr fsnvmdeady
      181 aafpsfdada tlrkwnlwgy idgrdgaqav rlalehqatg fdrfiiaaad tvmsrdntel
      241 vaevfpgvpv ngdiagngtl lsidharevl gyepkhswr
//
LOCUS       WP_285034897             320 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Plantibacter
            sp. ME-Dv--P-095].
ACCESSION   WP_285034897
VERSION     WP_285034897.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..320
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=34325
     Region          2..311
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrivviggtg higsflvprl vraghevvsv srgtrapyae atewehverl vvdreaedea
       61 gtfpariaal gcdvvidlvc ftlpsakalv eglrghvghl lhcgsiwryg psavvpiveg
      121 cgtppfgeyg vekdriarml qtetangglv ttslhpghiv gpgwapvnpl gnfdpdvwri
      181 ladgeplrvp glgaemlhhv haddvaqafe lavahrdrva gedfnvtsas aitvrgfaea
      241 aaswfgrsad ltpvtweefr sttseehadt swehlvrshc vsiekarsll gyapghtstd
      301 avrdalrwlv andeldvpsp
//
LOCUS       WP_285035357             546 aa            linear   BCT 25-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285035357
VERSION     WP_285035357.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..546
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=57256
     Region          12..546
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mssrptgdar avllrdariv dgtggpstlg svlidggriv aigadaatda padalvvdae
       61 glvaapgfid mhahsdlavl rdhdhlakvs qgvttevlgq dglsyaptdd htmaivrqqi
      121 agwngqpddv dfawrsvgey ldrvdrgaal nvaylvpqgs vrmlvvgten raatpdeivr
      181 mqelvaaglr agavgmssgl tyvpgmfadt eelvalcrtv aehggfyaph qrsygkgale
      241 ayaemidvsr rsgcalhlth atmnfgvnag raaelvalid daiadgvdlt ldtypylpgs
      301 ttlsallpsw aavggpeatl erlgdddvra rvrhelevlg tdgchgvvtd watieisgva
      361 npelagyvgr tvaaiaaedt ghawsgdpta lffelleadr latgilqhvg deanvrtmmv
      421 hpahtggsdg iligakphpr awgtfprylg hyvreagvlg ledavahlts rpaarlgltd
      481 rgvlrvgava dvvlfdpeti adratfaepr qqaagipwvf vngaaviadg rrtdavpgrs
      541 lrrrps
//
LOCUS       WP_285035383             378 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285035383
VERSION     WP_285035383.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..378
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39028
     Region          7..370
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mststqtsrr vvvigggilg tssavalarr gaevtlvtdr slasgasgrs lawlnsaarr
       61 sseyhalrvl gidrwrtfaa qvpsadflrf dgglmwapeg esyadtfaye rgigydarwl
      121 apediasvtp gvdpaavaae gaifnpgegw velpsvieil srefvarggr ivtdagaeia
      181 taggravgav langdridad avllatgpdv paqlaalgit igdqspaafv aftkpaasel
      241 vavlntpkva vrrtrdggfa ldsawseeei evrddgslhi adstverlla egsrvlagsp
      301 sleldhigag ykpipgdgep vfgavsqlpg lftafshsga tlgliagell adeivdgeps
      361 pllatfrper yadspvpa
//
LOCUS       WP_285035353             296 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Lactococcus petauri].
ACCESSION   WP_285035353
VERSION     WP_285035353.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 296)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 296)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 296)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..296
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=34201
     Region          14..291
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mpwskikrfl qtkiaqigvf lvmlfifvsn fllwhlpies linatilali vfviylvssy
       61 frwanreall cdlkhelldl eenlrakekh iketediikv wshqmkipla aidlmaqtei
      121 npielknqtf aldnylkmll eyqrianist dfhfekfsva allrellkky ssffiqknls
      181 vtisgdweit tdrkwfslai eqllnnaiky tnegrltisi eenkiilsdt gigilpedlp
      241 rifehgftgy ngrsyykasg lglyltklil drldfcikis selgegttve vkkneq
//
LOCUS       WP_285035264              63 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lactococcus petauri].
ACCESSION   WP_285035264
VERSION     WP_285035264.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 63)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 63)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 63)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..63
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..63
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7086
     Region          4..62
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mwdkieqllk eknittyrla qlsginkatl ahiksgkvkk plfetvckia daldadinef
       61 rek
//
LOCUS       WP_285035423             825 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-glucosidase family protein [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285035423
VERSION     WP_285035423.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Varghese,J.N., Hrmova,M. and Fincher,G.B.
  TITLE     Three-dimensional structure of a barley beta-D-glucan exohydrolase,
            a family 3 glycosyl hydrolase
  JOURNAL   Structure 7 (2), 179-190 (1999)
   PUBMED   10368285
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444920
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..825
                     /product="beta-glucosidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0015926 - glucosidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=86197
     Region          27..444
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          <518..686
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
     Region          742..807
                     /region_name="Fn3-like"
                     /note="Fibronectin type III-like domain; pfam14310"
                     /db_xref="CDD:433860"
ORIGIN      
        1 mtittprhaa atkpvdtdai dalvarldle ekvalvsgad fwttvpleki glramvlsdg
       61 pagvrgpvwd erspsinlps atalasswdp sfayrygava aaearrkgvd vvlgptinlh
      121 rsplggrhfe afsedpeltg slaaayvsgl qdngvaatpk hyvandsetd rftvdvrase
      181 ralrelylap fertvteagt waimsaynsv dgvtmsenel letplnsewg fdgvvvsdwt
      241 gvrslgsapa sqdlampgpa pawsdalvaa vrdgrveeaa vdrkvarlla lavrvgalge
      301 ealapapvdg vafsreaete gvvlltndgt lpldaaslnr vavighnard srtqgggsat
      361 vlpehtvspl egltlalpha tidyavgaiv qegvaelpld rltnprtgqp gllasfvdae
      421 gselfaedrr stalvwfggd apigtaaqlv ltttytpets eqlklgfatg lhgrlfvdgv
      481 llvdeqpviv gndlgaalla ppsatgafsa qaevpveira efdltpseng lgaisvtvgr
      541 apddsdpdal iaqaveaart advavvvvgt nakvesegwd rsdlslpgrq delvravaav
      601 nprtvvvvns gapvllpwsd dvaavvlgwf ggqemgnala dvllgvaepg grlsttwaas
      661 lddvpvldvt pvdgvlryee gihigyrawl rsgaqpafwf ghglgytnwt idegtvsgav
      721 dagtarlagt atntgeragk hvvqvyaera dsavdrpvrw lvgsavvrae agetvswevp
      781 lparvfahwa dgwqveagdv tlrigssvvd lvhetvvpia tgtvr
//
LOCUS       WP_285035707             264 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsB family cell division protein [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285035707
VERSION     WP_285035707.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..264
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=26979
     Region          16..>99
                     /region_name="kgd"
                     /note="multifunctional oxoglutarate
                     decarboxylase/oxoglutarate dehydrogenase thiamine
                     pyrophosphate-binding subunit/dihydrolipoyllysine-residue
                     succinyltransferase subunit; cl39092"
                     /db_xref="CDD:476867"
     Region          <131..201
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 mkkpsmpagg epkgtpptsg tssagtakqr ssasrrpsad kattprgaap skraagatak
       61 parsatkatr patkaarsaa agssgprtrn gstrtaparp seaggwlrsl rlsgfsvlll
      121 gilvlgvvvl apnlktfleq rqqiavlqas vadtqakvda qqaererwnd qsyvmtqard
      181 rlfyalpgev syiiindvdp aslpttetpv sdtlvdaksd wldgllaslv atgyspapta
      241 tdatdpaqtp apaqttpaap pagg
//
LOCUS       WP_285035735             174 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein, partial [Lactobacillus iners].
ACCESSION   WP_285035735
VERSION     WP_285035735.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..>174
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          12..>166
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mkecipyfik skrkiiiylh ggpffeiktp ledpfatffs kkenlillny piktgeggkk
       61 dfdwlystfk klksyfpnyk fyligesyga ylcslfsqfs ifekiicisg fssiqyqqlf
      121 ssekswlisy lspnaidlly lvqhnmiktk iylingdqdi ttpfqqittl ncln
//
LOCUS       WP_285035745             359 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein, partial [Lactobacillus
            iners].
ACCESSION   WP_285035745
VERSION     WP_285035745.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         <1..359
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          30..300
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 grrfiveehl definyvkny trtntnsini giitdthqkd vdsltsygrl gllhlkefny
       61 leergflklk vhlgdwidgs dpglvdeqel inlrncfssk ridyalikgn hdendkfdal
      121 hemlpsfper efedimwtnm yrqhnihyis rqhgvayfdy gdlriimint sdvpyildsn
      181 gkkkyntqht lairedqvqe iieileksvn kqiifmghav pidrkgmnsl kyngrslhel
      241 mvafnqrekg ylnshdvple ytltnkfdfs nvvkgkiiay faghahaedq yrinsiqyit
      301 fncsalvsls dsnkynqryn rqvdqrteya gyvvnvdldk kllqvfgyga askrrvyri
//
LOCUS       WP_285035836             194 aa            linear   BCT 25-DEC-2024
DEFINITION  tRNA dihydrouridine synthase, partial [Lactobacillus iners].
ACCESSION   WP_285035836
VERSION     WP_285035836.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Finet,O., Yague-Sanz,C., Kruger,L.K., Tran,P., Migeot,V.,
            Louski,M., Nevers,A., Rougemaille,M., Sun,J., Ernst,F.G.M.,
            Wacheul,L., Wery,M., Morillon,A., Dedon,P., Lafontaine,D.L.J. and
            Hermand,D.
  TITLE     Transcription-wide mapping of dihydrouridine reveals that mRNA
            dihydrouridylation is required for meiotic chromosome segregation
  JOURNAL   Mol Cell 82 (2), 404-419 (2022)
   PUBMED   34798057
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Bou-Nader,C., Bregeon,D., Pecqueur,L., Fontecave,M. and Hamdane,D.
  TITLE     Electrostatic Potential in the tRNA Binding Evolution of
            Dihydrouridine Synthases
  JOURNAL   Biochemistry 57 (37), 5407-5414 (2018)
   PUBMED   30149704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414563
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         <1..>194
                     /product="tRNA dihydrouridine synthase"
                     /EC_number="1.3.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0017150 - tRNA dihydrouridine synthase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
     Region          1..193
                     /region_name="DusA"
                     /note="tRNA-dihydrouridine synthase [Translation,
                     ribosomal structure and biogenesis]; COG0042"
                     /db_xref="CDD:439812"
ORIGIN      
        1 hpmslqifgg seetlveaar yvddnthadi ininmgcpvp kvtktdsgak wlldpdkiyq
       61 mvkavvnnvq kpvtvkmrtg wdedhiyave nalaaqeaga cavamhgrtr kqlytghadw
      121 gilkevsdal tipfvgngdv ttpqlakkml devgcsavmv gravlgnpwi lkeithyldt
      181 gellapqtve ervt
//
LOCUS       WP_285035862             431 aa            linear   BCT 25-DEC-2024
DEFINITION  HesA/MoeB/ThiF family protein [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285035862
VERSION     WP_285035862.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..431
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46432
     Region          165..>322
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mpfvvltada arliresdar gggvrlrrad aderfvadrv dvrdgtriav rvpseytaln
       61 wgdtsivgqw artvddrlal tflylgrrpg avipfntfhd lipgvrdpge llglviaqht
      121 qlpdtvralg apeftgwvva rdgvtpfevq vepdtfglsq lpnsqalqqn tvtvvgvgsi
      181 gstaatalah lgygriqlid pdrllwhnlv rhqlgpesvg rfkvdalkas lddtsrvfdd
      241 sivtqitahr ldvvehaekl hallmesdav lcaadgiapr rtvnhiarlt sipavfacvl
      301 edgaigeilr srpgtkfgcl lchraalrea gsldpeanqe raygtgdphk pmtatphdlr
      361 lvgdfaakvv tatvlesrhg dasqrlpgeh lvlglqptre lpapydvtma gearwdtvpa
      421 prtgcatcsa q
//
LOCUS       WP_285035886             277 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Plantibacter
            sp. ME-Dv--P-095].
ACCESSION   WP_285035886
VERSION     WP_285035886.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..277
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29772
     Region          1..256
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mstscvypsg trrafelaae agydgvevmv tedrvtqdav alrsladetg ldilsihapv
       61 ltrtafvwgr dhrvklrrsa eladavgast vvvhppfrwq rryavafvdl vaelseqygl
      121 eiavenmacf rsrglrvqpf afgydpgpla caaltldfsh aalagedsle iatrygdrlr
      181 hihlcdgtsp spraafldeh llpgdgdqpv aavlerlraa ewsgsivaev hlpsggddas
      241 rvaqlrssla fakrafastg rlpdespdag glpyrla
//
LOCUS       WP_285036026             346 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285036026
VERSION     WP_285036026.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..346
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36812
     Region          39..205
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 msvvpvlrtr srlpllqvlk talaaiaawi vaitiipgql pvfaaiaail vvqpsvnqsf
       61 gkalerslgv itgvvlatai gsvfghsawi vllaivvail lgwvlrlgpg sanqlpisam
      121 lvlsigaatp dyafariiet vlgagigllv nvvlvapvll apartavgal alacadtldh
      181 lataltrant daelaallte aralkplrer aiaavkegdd slllnprrsr hreeldrqrl
      241 llrrlepvvt rtlgmarsvh dhddptlhee ptvadiavel graahdlrll vndraasrep
      301 ptetaelpal taplvihrph pqhwiligsl medlrrvrde ivgept
//
LOCUS       WP_285036059             131 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285036059
VERSION     WP_285036059.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..131
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14212
     Region          9..101
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mgftaqawpa cgiarflsll egpwatlivr elldgshrfg qlkdalpgis ahtltdrlrr
       61 fetygivtrt sypeipprve yeltdlgqgl rpvldamnaw altvpaavde edavafpasc
      121 tgvvyqptth s
//
LOCUS       WP_285036128             365 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide)
            pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
            [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285036128
VERSION     WP_285036128.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Davies,G.J., Gloster,T.M. and Henrissat,B.
  TITLE     Recent structural insights into the expanding world of
            carbohydrate-active enzymes
  JOURNAL   Curr Opin Struct Biol 15 (6), 637-645 (2005)
   PUBMED   16263268
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   4  (residues 1 to 365)
  AUTHORS   van Heijenoort,J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit
  JOURNAL   Nat Prod Rep 18 (5), 503-519 (2001)
   PUBMED   11699883
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Ha,S., Gross,B. and Walker,S.
  TITLE     E. Coli MurG: a paradigm for a superfamily of glycosyltransferases
  JOURNAL   Curr Drug Targets Infect Disord 1 (2), 201-213 (2001)
   PUBMED   12455415
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..365
                     /product="UDP-N-acetylglucosamine--N-acetylmuramyl-
                     (pentapeptide) pyrophosphoryl-undecaprenol
                     N-acetylglucosamine transferase"
                     /EC_number="2.4.1.227"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0050511 -
                     undecaprenyldiphospho-muramoylpentapeptide
                     beta-N-acetylglucosaminyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051991 -
                     UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-
                     glutamyl-meso-2,
                     6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol
                     4-beta-N-acetylglucosaminlytransferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0030259 - lipid glycosylation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=38972
     Region          1..356
                     /region_name="MurG"
                     /note="UDP-N-acetylglucosamine:LPS N-acetylglucosamine
                     transferase [Cell wall/membrane/envelope biogenesis];
                     COG0707"
                     /db_xref="CDD:440471"
ORIGIN      
        1 mttyllaggg taghvnplla vadglrardp eatilvvgta eglearlvpe rgyelltipk
       61 lpfprrpnld alrfpgrlrr avadvvamir dhdvdvvigf ggyaaapayt aakragvplv
      121 iheanarpgl anrlgarytp yvgvafhrtp irharfvgmp lrreiedldr dtlrpsaiae
      181 fgldadrpll lvtggslgar rlnatmsesa edvvgagwqv lhitgaksei qdpgvehyhl
      241 leycsrmdla iaaadfavsr agsatvselc avglpavyvp ypvgngeqrf naadvvragg
      301 avmvddaqfv ptwvrehlvp llndrhrvdd laaqsksvgv sdgtarvval idealqpsvq
      361 rsrsr
//
LOCUS       WP_285036170             727 aa            linear   BCT 25-DEC-2024
DEFINITION  RecQ family ATP-dependent DNA helicase [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285036170
VERSION     WP_285036170.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Larsen,N.B. and Hickson,I.D.
  TITLE     RecQ Helicases: Conserved Guardians of Genomic Integrity
  JOURNAL   Adv Exp Med Biol 767, 161-184 (2013)
   PUBMED   23161011
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Rezazadeh,S.
  TITLE     RecQ helicases; at the crossroad of genome replication, repair, and
            recombination
  JOURNAL   Mol Biol Rep 39 (4), 4527-4543 (2012)
   PUBMED   21947842
REFERENCE   3  (residues 1 to 727)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 727)
  AUTHORS   Bernstein,K.A., Gangloff,S. and Rothstein,R.
  TITLE     The RecQ DNA helicases in DNA repair
  JOURNAL   Annu Rev Genet 44, 393-417 (2010)
   PUBMED   21047263
REFERENCE   5  (residues 1 to 727)
  AUTHORS   Chu,W.K. and Hickson,I.D.
  TITLE     RecQ helicases: multifunctional genome caretakers
  JOURNAL   Nat Rev Cancer 9 (9), 644-654 (2009)
   PUBMED   19657341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..727
                     /product="RecQ family ATP-dependent DNA helicase"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0043138 - 3'-5' DNA helicase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=77546
     Region          36..582
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
ORIGIN      
        1 msdvsapapt hheatttgsv aeataalaal tgvpgarfhd gqleailalv dehrrtlvvq
       61 rtgwgksavy fiatallrrr gagptllvsp llalmrdqva aaaragvrav ainsanahew
      121 ddvraqldad evdvllvspe rlnnprfrde qlptlvartg mlvvdeahci sdwghdfrpd
      181 yrrlaeligr lpvevpvlat tatanarvvr diaeqltapa asgstaaevl tirgslaras
      241 lrlgvlrlpe srdrltwlls hldgltgsgi iytltvsaae dtarllreag hevraytgrt
      301 dpdereeser llkenrlkal vatsalgmgf dkpdlgfvvh lgapsspvay yqqvgragra
      361 tehadvlllp gaedeeiwqy fatasmpdea ratavldald drprstpale alvnlrrtpl
      421 elllkvldvd gavqrvaggw vstgepwvyd reryrriaea rvaeqqamla yergeecrml
      481 vlqrelddat aepcgrcdrc agawfpteld saaaasasea lgrvgvelep raqwptgagk
      541 lgvttdgapv sgrisledrl epgralarlt dlgwggvlre lfaagaadap asravidasv
      601 rvladwpwar rpaavvsvps rsrpqlvdsv argiaslgrl pylgeldvvg dgprggpggn
      661 sayrlagvwd afsvgaelrt qlatlegapv llvddradsr wtltvagral rlagsgpvlp
      721 falgivg
//
LOCUS       WP_285036227             409 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285036227
VERSION     WP_285036227.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Erzberger,J.P. and Berger,J.M.
  TITLE     Evolutionary relationships and structural mechanisms of AAA+
            proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 35, 93-114 (2006)
   PUBMED   16689629
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..409
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42779
     Region          58..377
                     /region_name="RPT1"
                     /note="ATP-dependent 26S proteasome regulatory subunit
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1222"
                     /db_xref="CDD:440835"
ORIGIN      
        1 mtqdgdflev iaaevaqdpq naalredfvt lllqhdvdra aeevstferf ggdparvrll
       61 rarvmaarlr ggttggapae tpggdptass stpnrptavp nastpdqapv rigqpslwda
      121 erpaitladv agladvkqhl dstflaplrn pelaaafgqk pggsllmygp pgcgktfiak
      181 aiagdlgasf ihvtladlls kwlgdsekai qsvfhdaraa apcviffdef dalggrrtsg
      241 ggsqsmrtiv tqlleeldgv anendgvyfl aatnrpwdid palrrpgrid ktvlvlppda
      301 varaailqgd legkpaegvd viavaaatdg fsgadiaqvs rvalqrslsa smeagaivpv
      361 tteglleaaa glipstaswf dqvapvleyg vddgtfaqlr tyrvqhglr
//
LOCUS       WP_285036292             499 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285036292
VERSION     WP_285036292.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..499
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=52954
     Region          202..494
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 maqvtvadvi lqaehlgarc vagspadvlv tgveilalde lndatehaia vvttpdgavp
       61 rpyqvdiair raiaagcaal lfvgefpiae tsralagrgg lpvimsqgia sdlavlmdrt
      121 irggaeeams raefaiervi aasaaeteqa sgvgvreail evasttlgvp vtlvedagas
      181 wlepdavcig eipigrvhae rddpaaaial pviasvlsra lqrelhgrfg svrsraelii
      241 elifaessri dgfamdavra glplqlshav awltpkhvsd pdrraptvla psvelfalql
      301 vdqrdeqwhl amrrdeivvi aseelgaadh qrrlrdvmer ivahassvag pewtftvglg
      361 tpqsgaaglr qsatearvaa eaaiaggrfg tmeatdvtgl rrvlldfyas plsrtllddi
      421 lsplddlgpe raaiavrtll aylshrnslv ragaelnlhp navnyrirri eqsleldlad
      481 pdvrfaaela crvrligmp
//
LOCUS       WP_285036309             487 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285036309
VERSION     WP_285036309.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..487
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51280
     Region          5..473
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mrrsteefda vvvgagpngl aaavtlarag lhvqvvergd tigggartae ltlpgfhhdi
       61 csavhpmala sgffrsfkle rrielvvpei syahplddgr agiayrdidr tadalgrdga
      121 awralmgpla adadrvsqft ggkllqvprh pvtvakfglr aleqgspawn lrfredtapa
      181 mlsgvaahsi rpmpslatsa aalslgayah argwpipigg sqaivdalaa dllahggeiv
      241 tgtevrside lptaravlfd ttpkalaeia gsrlpdtylr rlsrfrygdg vakvdfalsg
      301 pvpwtnpela kagtlhlggs rpeiaaaerd vargrhsesp yvlvsqpavg dpgrapgdaq
      361 vlwaythvps gsaldqteai trqierfapg frdviltsas mtardmaryn pnyvlgdiaa
      421 gaasfaqlva rpvlsndpwr tptpgiflcs sstppgpgvh glagwhaars alrsvfgrdr
      481 mpslapd
//
LOCUS       WP_285036341             294 aa            linear   BCT 25-DEC-2024
DEFINITION  TolB family protein [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285036341
VERSION     WP_285036341.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..294
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=31245
     Region          46..182
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          156..290
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 mtfralapgq rsrillggls daepevlfet dellieapnw sldgstlvln gngrlwslsv
       61 edpgagltri efaglpelnn dhvldpdgeh illsamdghi yrgaltggsv tkltaddgsw
      121 hflhgvspdg ariayveleg fehpgrlava pavegggpvt vldtgdghld gpewspdgrw
      181 llcntehfgt epghaqlari pdgggtlehl vasdtvdwfp hlspdarlaa yiafpagtig
      241 hpadldvevr lvstddwatp lrrypvfggq gtinvnswap dstrfafvay ptap
//
LOCUS       WP_285036400             451 aa            linear   BCT 25-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285036400
VERSION     WP_285036400.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..451
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=47970
     Region          4..450
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mshtilnpan ehvvttvehl dvaetdaait raavaqrawa alapvdraqa lrrfadavda
       61 drehlaslev vnsghpitqa rweaghvrdv leyysgsper lfgqqipvag gidltfhepl
      121 gvigiitpwn fpmtiaawgf apalaagnav vlkpaewtpl tsirlgelal esglpeglfq
      181 vlpgrgsvvg erfvtnetvr kvvftgstav gkrimagase qvkrvtlelg gksanivfad
      241 adleraaata pygvfenagq dccarsrilv qrsvyerfme llepavqgvv vgdpndpate
      301 mgplvsaphl asvrsyvpdd apvaftgsap dgpgywfapt vltpergdrt vreeifgpvv
      361 tvlpfedead altlandtey glsgsiwtrd vgralraara veagnlsvns hssvrystpf
      421 ggfkqsglgr elgpdaplaf tetknvfiat d
//
LOCUS       WP_285036444             237 aa            linear   BCT 25-DEC-2024
DEFINITION  tRNA (adenine(22)-N(1))-methyltransferase [Lactobacillus
            paragasseri].
ACCESSION   WP_285036444
VERSION     WP_285036444.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus paragasseri
  ORGANISM  Lactobacillus paragasseri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Hori,H.
  TITLE     Methylated nucleosides in tRNA and tRNA methyltransferases
  JOURNAL   Front Genet 5, 144 (2014)
   PUBMED   24904644
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Roovers,M., Kaminska,K.H., Tkaczuk,K.L., Gigot,D., Droogmans,L. and
            Bujnicki,J.M.
  TITLE     The YqfN protein of Bacillus subtilis is the tRNA: m1A22
            methyltransferase (TrmK)
  JOURNAL   Nucleic Acids Res 36 (10), 3252-3262 (2008)
   PUBMED   18420655
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Lactobacillus paragasseri"
                     /db_xref="taxon:2107999"
     Protein         1..237
                     /product="tRNA (adenine(22)-N(1))-methyltransferase"
                     /EC_number="2.1.1.217"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0160105 - tRNA
                     (adenine(22)-N1)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26672
     Region          12..237
                     /region_name="TrmK"
                     /note="tRNA A22 N1-methylase [Translation, ribosomal
                     structure and biogenesis]; COG2384"
                     /db_xref="CDD:441950"
ORIGIN      
        1 mlkflvrges vleerlaqig kmvdpesrla digtdhaylp ialvkegkin faiasdvaag
       61 plnnakqdie qaglenkiet rlgsgletlk aedridtvvi agmggklmtn lletayqegk
      121 kyptlilean igeslvrkwl mdhqyeivae kiievaghiy eiikaeiktn khdlseqels
      181 fgpfllkekn pvfikkwtnq lryyqnlktn lnkaknkded kinkindlik mieevlk
//
LOCUS       WP_285036448             438 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285036448
VERSION     WP_285036448.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..438
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=47517
     Region          16..351
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; cl46764"
                     /db_xref="CDD:481104"
ORIGIN      
        1 msttardarp arrgesgsre twidsargia iilvvlfhav mylgvagitg pwslastpld
       61 tfrmplfffv sgllapsala rpfrdlfrkr lllllylyvv wstlqtayga vmppvgdaqd
      121 pvtwwsfasi lvqphpnlwf iyalpiyfvv awlirrwppl vqlalaaavs aafgtgmlss
      181 lgvpwekagr yffffllaah aaplvrrlap rlglvhllvl vgvyggivvf vlrtqarfvp
      241 fvllgaglma tatgialavv lsrfrscsfl avlgtrtlpi yllhtfpmia vagalhpiae
      301 tlplwwrivl ppaltaasil islgihrllr avpgvftapv kswtiasepr srnmdpsqil
      361 avpsvnstia ppdrnglsra esapsdaaep pphpprvdgs gapdpreepl ldfrpprsrs
      421 shdrpanapi dapsrptd
//
LOCUS       WP_285036723             286 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lactobacillus
            paragasseri].
ACCESSION   WP_285036723
VERSION     WP_285036723.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus paragasseri
  ORGANISM  Lactobacillus paragasseri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Lactobacillus paragasseri"
                     /db_xref="taxon:2107999"
     Protein         1..286
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33348
     Region          3..59
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(7,11,35)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(10,34)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(17..18,28,31,35..36)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 myghefkelr leqgitqkea csgicseskl srwendqvev efstamklln rihitshefm
       61 gwskfsprpe idpelseate kenipflkrv tqkqltkyhk nhnkfdlfma anlcnqlfii
      121 ehknylppid qkklfaifsk vnlwsqyyis afgasiflfn pkqiygssmq iirnidrlke
      181 aeisfnleii mgslsdgilr lislnelsya qklvkelkki elpqylmfft ltltylqkai
      241 dymkngddkp iltlisevld lgcsvqatty ldmfkylkaq rkkynf
//
LOCUS       WP_285036832            1008 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-mannosidase [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285036832
VERSION     WP_285036832.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..1008
                     /product="alpha-mannosidase"
                     /calculated_mol_wt=109747
     Region          253..1003
                     /region_name="MngB"
                     /note="Alpha-mannosidase [Carbohydrate transport and
                     metabolism]; COG0383"
                     /db_xref="CDD:440152"
ORIGIN      
        1 mhhddaltea rivrfmrerl tpallrrsap ldvtawevpg epvpfetava aehrpfavgd
       61 awgrpwgttw fhvtgtvptg wdepgtriel lidlgfsiaq pgfqaeglvy dpsgrivkal
      121 eplnmhvpvq vgaggvvdvw veaasnpdva gvwdfaptpl gdpatagtdp iyrlnrvdvv
      181 qldvtvwell qdcwtldglr relgpelprr aellrglgra vqevdpddva gtaqlgrdvl
      241 apllaapasa sahrivavgh ahidsawlwp vretirkcar tfsnvldlmd hdpdfvfacs
      301 saqqfawmrd hypelferir srvaegrfvp vggmwvesdt nlpggeamar qfvagkrffl
      361 eefgldltev wlpdsfgysa ampqivaaag atdfltqkvs wnetnrfphh tflwegidgt
      421 rvfthfppad tynsalaatd lhraqrqfqe kgesnvsllp fghgdggggp tremlaaavr
      481 trslegsptv eigtpsaffa aaradypspp vwsgelylef hrgtytsqar tkrgnrrseh
      541 llreaelwaa taairtgaey pydaldeawh tvllqqfhdi lpgssiawvh qvaeanyqav
      601 aerltalvde slraltapgd ggpagfanas pfvvdgvpal gvaatttagr avlsgradgg
      661 fvldndlvrv tvdadgrvts vldlaadrev vapgaatael qlfrdtpnqw dawdvdladr
      721 thwtvldrad vvevaletpg rvavlvrrsf gsssvtqtia ldagrptvdi ltavdwherq
      781 kllklafpld vradvassei qfghvdrpta vntswdaarf etaahrwvhv gepgyglava
      841 ndstyghdvt rttredggtt tlvrksllra prfpdptadq gehvlrstlt vgagildaaa
      901 egyrinlplr pvqgaavdpi vvvdrpgivv eavklaedrs gdlvvrlyea tggrsagrvs
      961 fgfpvrsvrr tdllerehge qprlapdgsv elrlrpfeil tlraarmq
//
LOCUS       WP_285037006             498 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285037006
VERSION     WP_285037006.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..498
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53089
     Region          12..369
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mhlvedgtet giarvfedri aggvapgsyv avfdrdrirf srgfgestrg gdvpdedtlf
       61 riasctksft aavllilrdt grldldtpvd afvpefapat pggtavrptv rmlltmsggl
      121 gtddpwadrq esitpaefrr llvrgvrcvt vpgtafaysn lgyallgqvi ervtggrfvd
      181 avtslllepl glgavferpd rehpedggav taighrvrrd ravdaddrfv evpfsgpgvf
      241 saigglfasa ttligwvrwl daawtgdesg plssasrrem qqlhrlappr psldglpprl
      301 algygfglfv eedatlgplv shsggypgys ahmrwhpasg fgvvafenag yaavakpaeq
      361 vlrlalaeaq asgelaepai rpwpetlvas mtatgllshw ddrvaaslfa envaldvpld
      421 errtaaeaav aavggiaeva sgrampvcds pdhlvwfveg eqgrlrlevr mtpvvplrvq
      481 tftvtvdheg pettdadd
//
LOCUS       WP_285037075             519 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285037075
VERSION     WP_285037075.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18527136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..519
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=56295
     Region          16..>71
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          84..515
                     /region_name="MurA"
                     /note="UDP-N-acetylglucosamine enolpyruvyl transferase
                     [Cell wall/membrane/envelope biogenesis]; COG0766"
                     /db_xref="CDD:440529"
ORIGIN      
        1 medtatsert dpaaplrqvg alirgarqgr kltqaqlaer vgtsqsainr ieqgsqnisi
       61 dllsristal eseivsfgeq kknshlrvqg grrlhgsiev rssknasval lcaalmnrgr
      121 ttlhgiariv evdriidvlr slgvsvvwsp dgqdveihvp ddlslaside dagrrtrsvl
      181 mflgpllgry dtfalpyagg cdlgtrtvep hlialrpfgl sieatagwyq atvapdvpee
      241 ltvvltergd tvtenaimaa avrdgvttir naspnymvqd lcfylellgi tidgigsttl
      301 ritgrsaine dvdywpsedp veamslltag ivtdsevtvt rvpiefmeie latlgemglr
      361 htrspeypaa ngrtrlvdvt vhpsklhapi dkihpmpfpg lnidnlpffa viaacaegdt
      421 lihdwvyegr aihltdltrl ganvrlrdph ridvsgpthw sgaevscppa lrpavvilla
      481 mlaakgtsvl rnvdiiargy eqlqerlitl gasietfrd
//
LOCUS       WP_285037132             332 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285037132
VERSION     WP_285037132.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..332
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=36033
     Region          37..289
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 meliywwmpl vwllvvaavv avavlatrag rrrkanqepl wvahsgrlta lpgyrraltr
       61 yrrlvvatia avavlllagt algsrvvstt vfqpelrnrd ivlcldvsgs mteydaalvg
      121 vfeslvqrfd gerialvlfn asattyfplt sdydyvtaql dhlvedltsp esdyeywngt
      181 dlgngsslig dglgscvmrf dqvgeqrsrs ivlatdnyva gepiltlkea geyakaqdvt
      241 vyginpgdvs skdylddlaa emdevvtstg gdyyaladpa avggivqqit aeqtktlkga
      301 kqlvqvdepl vfvlaafggl allmllawrl rr
//
LOCUS       WP_285037148             328 aa            linear   BCT 25-DEC-2024
DEFINITION  MraY family glycosyltransferase [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285037148
VERSION     WP_285037148.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Anderson,M.S., Eveland,S.S. and Price,N.P.
  TITLE     Conserved cytoplasmic motifs that distinguish sub-groups of the
            polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase
            family
  JOURNAL   FEMS Microbiol Lett 191 (2), 169-175 (2000)
   PUBMED   11024259
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Lehrman,M.A.
  TITLE     A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P
            transferases
  JOURNAL   Glycobiology 4 (6), 768-771 (1994)
   PUBMED   7734839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10160628
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..328
                     /product="MraY family glycosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=33547
     Region          31..273
                     /region_name="GT_WbpL_WbcO_like"
                     /note="The members of this subfamily catalyze the
                     formation of a phosphodiester bond between a
                     membrane-associated undecaprenyl-phosphate (Und-P)
                     molecule and N-acetylhexosamine 1-phosphate, which is
                     usually donated by a soluble UDP-N-acetylhexosamine
                     precursor; cd06854"
                     /db_xref="CDD:133464"
     Site            90..91
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133464"
     Site            198..201
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133464"
     Site            order(246,257..260)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:133464"
ORIGIN      
        1 mtaavlagvv alvvsllsql lirpilihrs vvdtpnhrsm hvtptirggg igvaiavavg
       61 lgtaavvfqs lplwivagis vlnaaigave dvrglpvrvr fglqvvlgll atwvlvvsms
      121 asfwwiplgi valvaytnia nfmdgvngis slhgtvvggf yaglgaaagl pgvtaaglvv
      181 aaaflgflpw nlakrrmflg dvgsyllggs lvavavyaaf sgvsfialig pvlvyvadtg
      241 ttiiarwrrg eplheahrsh vyqrlaaggl ghlgstavvs vatlatgllg vvvataafpf
      301 qvlavlgill vlaaylgspr llarrprl
//
LOCUS       WP_285037157             225 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285037157
VERSION     WP_285037157.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..225
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=23930
     Region          17..184
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 msrpsrhpqp tvrllpwara deldldgtad rldeaardrl easseaearr flfgrallvr
       61 tvaetvgada rrvtvtarcq dcglahgrpq vrvdggtvha svshtdgasa vvvsvdhpvg
      121 vdverldaar fggveavals paererwlrl perrrlrsla ehwtakeavt kalgtglttd
      181 patigltgqi graggtvaei agrrfvvdhp tlapdtvvat alllp
//
LOCUS       WP_285037186             567 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285037186
VERSION     WP_285037186.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 567)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 567)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..567
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=60397
     Region          19..564
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mdfaflavva vvtivavarf atklrvaapl ilvlvglals ylpfvpdvev kpewilagvl
       61 ppllysaavn vplvdfrrnl kaisglsvvl vvvssvligl ilstilpdls laagialgav
      121 vsptdavaat sigkrlgmpp rlvsvleges lvndasalvl lrsaiaatag svslwgvigd
      181 fayavalaia igivvgfvtv rirsrlgdpv lttvvsfavp fiaylpaehf hasgvlsvvv
      241 aglytghqsa kyftaqdris erinwrttqf llengvfllm gleleaivsq veqddlgiwp
      301 siglglltac tlivvrivfv gglvwslrrd erealsrrpk ldefsarled hpsenprsar
      361 rkaaftrsia rrsadldflq reglgwrgga vlawagmrgv vtiaaaqslp letpyraelv
      421 liaftvaivt lllqggslpl virlsrvggt dqeaataela glveeistvg vaalddpqlr
      481 tddgepfdpa vvdrvrttsl irvesaaert dagvgpheqy rqlrrrvlda erdalldara
      541 tgsypsevla raqrmldvee srldgag
//
LOCUS       WP_285037220             422 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285037220
VERSION     WP_285037220.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..422
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=45794
     Region          35..380
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mtsttnvpfd qpgrrsdrrg flrgdrvsls eglnghrnal gvlrlilasm vifshafptg
       61 gwgedpskgw tngqetiggf avigffaisg yliaksgasa dilqflwrrg lrifpafwav
      121 lcvgalivgp iawrmsgngl rdyigsgpim yifqnadlsi rqwgvydvfq tttpygrtvg
      181 ysvfngslwt lalewgcyll vaallvlgvl rhrrwvvpal agafwvlsiv nslapqivgm
      241 vapaladpnk ikltlvflig asfavyskri plndllgvaa gvvvvvtllt vgwvqigypa
      301 fayfvlwlaa rlpkrvqwig akndysygmy vygflvqqft aflgwntlgy wpwvgltilv
      361 tagcawlswh giekramalk dwgpgrgigw laprggsaav epgpgrpvas nvesptakdt
      421 ts
//
LOCUS       WP_285037208             183 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285037208
VERSION     WP_285037208.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..183
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=19125
     Region          34..167
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mlrkplgliv gsaevvvlrl asgvpnnavr laalrswgav igagcaihhg lqvrgarrls
       61 lgadcfiaed vtldargglt vgshvsinsg aqiwtaqhds aspvfayesa pvrigdrawi
      121 narsiilpgv sigegavvaa gavvtkdvpa wtmvggvpak pladrprvda yrldarrnkv
      181 www
//
LOCUS       WP_285037272             470 aa            linear   BCT 25-DEC-2024
DEFINITION  FGGY-family carbohydrate kinase [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285037272
VERSION     WP_285037272.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..470
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48903
     Region          20..456
                     /region_name="ASKHA_NBD_FGGY_FK"
                     /note="nucleotide-binding domain (NBD) of L-fuculokinase
                     (FK) and similar proteins; cd07773"
                     /db_xref="CDD:466793"
ORIGIN      
        1 mhpaanldpt tvasvapdgl vagldlgstg vkilvtdadg aevlihqlpt pwlagaggtt
       61 vmeaasliat vrelldhvaa altdrfgptv rvralavsgm gesgivldav grpvapaiaw
      121 fdprgaeqla alpatiaeqf agrtglplgv qvsvvkllhl rdagldlagt rwlnlpeylv
      181 aalggeeaae yslssrtgll dqdtgapwpe llehlgvdat flppfvdagt plgsasapwv
      241 pevfadaalt vaghdhlvsa vstgsfpaer yhvsmgtaev llrrldaplp faarerlaev
      301 fincvrhvvp gtwvlvagvk tgllmrrtlq lvgvtersgr drlddavmel paegrladgd
      361 ivvsgarndd gvlhltvrad gadpaevfaa vlrhgndelr vlieamdrev ppassalltg
      421 gwagmrsvqr araavlpgiq vsdrsqdtay gatvfarsll epavagrarp
//
LOCUS       WP_285037276             493 aa            linear   BCT 25-DEC-2024
DEFINITION  rhamnulokinase [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285037276
VERSION     WP_285037276.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167330
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..493
                     /product="rhamnulokinase"
                     /EC_number="2.7.1.5"
                     /GO_function="GO:0004370 - glycerol kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008993 - rhamnulokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006071 - glycerol metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0019301 - rhamnose catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50408
     Region          10..475
                     /region_name="ASKHA_NBD_FGGY_RhaB-like"
                     /note="nucleotide-binding domain (NBD) of rhamnulokinase
                     (RhaB) and similar proteins; cd07771"
                     /db_xref="CDD:466791"
ORIGIN      
        1 mtastvpsfh aavdlgassg rvilgrwdge hlrlvevhrf pngpvvrdgr lvwdaerlfe
       61 etltglaaav rhaeaaggal dgigidswgv dvglpvlgts rlassvpevr hhrgadehep
      121 eraaalvgpa aayavtgvie hpintafqlr slaagskagp ptteaptvll vpdlwvwllt
      181 gvvgaertia sttqlldqrs gdwaaalver wglggfrfpp vvapgtlags ttpeitarlg
      241 araaipvhrv aehdtasala farpdgaell vssgswslag vclaepvlse parlagftne
      301 agaagsslll rnlsgmwllt ecarawseed ghvvdpvalv aaatvaaasa dtvpptvfdv
      361 adprllvpgd mparitalcr aaggtppsgr vdlvrsvies laaayaatgr aaaaltgvpi
      421 rsvrivgggs rnrllcarta eltglpvtag paeasalgnl avqlvaagra psldavyrgh
      481 rddpaddqgq gpt
//
LOCUS       WP_285037329             305 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285037329
VERSION     WP_285037329.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..305
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31157
     Region          9..295
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(37,240,243)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(180,211,238,241..242,245)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mhttpttdvl iagetlidiv rrldgtqaes pggspanvgi tlgrlgrvpa lvthvgdder
       61 gaairawlda sgvslvsapt grtstaqatl dadgaatyef dlsldldatd apeasvvhtg
      121 siasvlepsa grlsalvear rasalitydp nirptlvdda ervrrtalvc iarahvvkas
      181 dedvaflhpd lalvdaakqw vasgpglvvv trggdgalvv ragsvfeiat prvtvadtvg
      241 agdtfmgali dglltagvsg peaeerlgai sdddlrrlle raaraasvtv srpganpptl
      301 aelda
//
LOCUS       WP_285037321             326 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285037321
VERSION     WP_285037321.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..326
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35572
     Region          17..313
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mssptsrllq llsllqarrd wpgalladrl svshrtirrd vdrlremgyr ieatmgpdgg
       61 yrldagselp pllfdddqvv altvalqtaa vagagigeaa lralttvrqv lpsrvrhrld
      121 alevanvart gaaptptvss evllsvsaai rdrhvlrfgr avdgpepprr vephhlvlsd
      181 erwylvawdl drddwrifrv drieprtptg prfrprevpg edvpafvaar fkgsehadrw
      241 pcvgtvllrl plssvepfvg dgaaeaagdd rtrytagaws wvalaaslnr fdteievvep
      301 pelaaafavl aernaatatr gaatpr
//
LOCUS       WP_285037347             322 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285037347
VERSION     WP_285037347.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 322)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 322)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 322)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..322
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36058
     Region          9..322
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mttaspprvs tkqrvarsrr gprehlkral rswqlyvlll patisvllfk ywpmygaqia
       61 frdynpadgf agsrwvgleh farfiesfqf erllantlti nglglliafp vpiilalivn
      121 qlqserfkkf tqtvlyspsf isvvvvvgmi hllfspragi vnnalvafgg epiffmgspd
      181 wfrplyigsd iwqnagfsmi vylaaltaid palheaarvd gankwqrirh idipgilpvi
      241 tilfilaign lfnlgfekvl lmqtdlnlpt seviqtyvyk aglqqaqfsy saaiglfnsl
      301 inlvllltfn wiarragqss lw
//
LOCUS       WP_285037365             828 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285037365
VERSION     WP_285037365.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 828)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 828)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14311963
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..828
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=91828
     Region          20..>649
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          743..818
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; cl38983"
                     /db_xref="CDD:476840"
ORIGIN      
        1 msiidtatvr plttrllheg wslravggai peafvgtsvp atvpglvhtd lldaglipdp
       61 fldrnehlvt wigstdweyr ttftwepdgh erhdlvfegl dtvatvtvng svvattrnqh
      121 rtyridvgav lregendlvv hfaspiaaad lasleigyrp htyshpfnai rkaacnfgwd
      181 wgldaassgl wkpvslqsws tarlasvrpv vtvhgsegrv avhvdverag dgdaalalta
      241 tiaevnadvv fpagadsvvl elavpdverw wprgygeqpl ydldvvlgqd earlgewskr
      301 igfrtvavel epdaegtsfr fvvngeavwv rganwipdda fvtrvdrarl arrmdqaefa
      361 nlnllriwgg gyyesddfye lcdergimvw qdflfacaay aeeeplwsev eaeardnitr
      421 imphaslvlw ngnneniwgf eewgwekrvq grtwgmgyyl dllprlvael dpagnytags
      481 pwsgtpdipa ndpdhgsvhl welwnrvdyp ayrdvlprfv aefgwqgpat wstidraisd
      541 spltpespgm ihhqkatdgn dkltdglvah lplpddtedw hwamslnqan avtvaiehfr
      601 swsprcmgsi vwqlndcwpv tswaavdgde rakpllyalr hvyadrlvtv qprgeslvva
      661 vlndgpdawa ddlvirrlrf dgtelasvrv pvaldrrsst lveipeavav agsasdevlv
      721 atlgaergfw sfaeardsti paprfsaeva rqddgyavti aaesflrdlt llvdkldpaa
      781 vvddqlvtll pgervtfhvr teveldedel lstrvvrtan qlvedwar
//
LOCUS       WP_285037393             339 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285037393
VERSION     WP_285037393.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..339
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36318
     Region          4..339
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mdtasvarvi eatdfsgvvl vkrgdetlfe varglasrer depitldtrf dtasitklft
       61 aaavlqqvda ghidldesih eyvdldgtti rrdvqlihll thtsgiadda detagesyee
      121 lwaersassi retadllplf ahkpplaapg eeanyvnagy vllglalegv tglpyrelie
      181 qqvfallgmd hsgfadrrtg epglaeggdv dddgvwhsnv dafpplggpd agaqstaadl
      241 itflraarda klltaeltee ftspqievde eisygfgfef dvdedgqvrs myldgvnpga
      301 sgivrtyfgp taadaidvvv lsnsedgawd viraidael
//
LOCUS       WP_285037410             200 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285037410
VERSION     WP_285037410.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..200
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21427
     Region          129..200
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mteirayrpt drsavatict rtgdsgadat ghfstdellp dvyalpyvdh epelallvda
       61 gagpigyilg tadtvafdrw fverwwptvv gkyetaassg aaseqergiv rsaterigla
      121 pellaqypah lhidllpetq gmglgrrlid afcgllaerg vpgvhlgvgv sntgaqrfye
      181 rtgftrvdgd pgahwyakal
//
LOCUS       WP_285037461             585 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 35 protein [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285037461
VERSION     WP_285037461.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 585)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 585)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12015514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..585
                     /product="glycoside hydrolase family 35 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=63876
     Region          10..323
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
     Region          <495..561
                     /region_name="BetaGal_dom4_5"
                     /note="Beta-galactosidase jelly roll domain; pfam13364"
                     /db_xref="CDD:463857"
ORIGIN      
        1 mptfsigadd flldgqpfri lsgalhyfrv hpeqwadria kaklmglnti etyvawnqhs
       61 pergvfdttg tndlkrfldl iaeagmyaiv rpgpyicaew dngglpgwll hdpelglrrs
      121 eprylaavre yfeallpiva arqidrggpv ilvqveneyg aygddhdylr tltawtrelg
      181 itvplttvdq ptaqmledgs ipelhktgsf gsrslerlat lrehqpigpl mcsefwdgwf
      241 dhwgehhhtt pvaetaadld allatgasvn iymfhggtnf gftggandkg qyrshvtsyd
      301 ydapldeagh ptekffafrd viakyaevpt dippaatdap aftaafesev pfadvadela
      361 pleafdript mdelgafsgl aryraslggr ggvlrfaevr drvvvsvdgv pvgtltrefq
      421 erslvipage tlelllenqg rvnygkrlge pkgiigpvsl dgveltawgi apialdrlde
      481 vvdaassrap gtpisgagpv lltatvtldt ptdlfldtad wgkglvwvng fllgrywsrg
      541 pqhtlyvpgg qlraganrft vfefhaltap elsflarpsl gpvef
//
LOCUS       WP_285037467             436 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285037467
VERSION     WP_285037467.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..436
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=45230
     Region          1..436
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mklsvigcgy lgavhaaama sighevvgid vdpakieala agrspifepg lpelllagve
       61 sgrlrfstdm adaagatmhf vavgtpqkag snaadlryvd aavtallphl sagdvvvgks
      121 tvpvgtaarl aelvaptgav lawnpeflre gfavqdtiap drlvyglppa pedaavaraa
      181 fdevyaqala tgtplvatgy staelvkvaa naflatkisf inamaeiaev tdadvtelad
      241 aigydarigr rflnagvgfg ggclpkdira ftaraeelgr gesvaflkev dainlrrrqr
      301 vvdlvveelg gsayqkrvav lglafkpdsd dvrdspaldv avglnglgak vlafdpeavp
      361 narrlhpqlm faasaeeavt dadivvvvte wkafraldpe avaaltagki vvdgrncldv
      421 dawrgagwry vglgrp
//
LOCUS       WP_285037524             329 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285037524
VERSION     WP_285037524.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..329
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=33870
     Region          1..329
                     /region_name="Tdh"
                     /note="Threonine dehydrogenase or related Zn-dependent
                     dehydrogenase [Amino acid transport and metabolism,
                     General function prediction only]; COG1063"
                     /db_xref="CDD:440683"
ORIGIN      
        1 mrivdagrvv vetvapvepg ageavvrves cglcgsdatm faghhpvirp pivpgheivg
       61 ivsavgdgad emlgrrvavl pqlgcgvcrq crrghqrlca dmrliggqvd ggaadevtvp
      121 aaslvivped vpasiapive plavarhavs rvdvadaevl vvgggpigll valciradga
      181 rsvtlvepvt srqeivthfg ipvvdatpdd gpaaaefdvv fdcvggalse rllglvaagg
      241 slvlvgvaap elsfdgmllq rqertilgsh mysrtdfeaa lrllaegllp tdaaslgllf
      301 drrplddava afddlvgrrs paikmllip
//
LOCUS       WP_285037562             332 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285037562
VERSION     WP_285037562.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..332
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=35954
     Region          42..313
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 msavapsiqq gprpsappla gvpsegatts tsvrtvyrpt gpldvhatlr lmsrggdgpc
       61 yrktpggvwl tartpqggat lyvsamrdge veatawgpga ewmidgvpel lgrdddwsgl
      121 dvsrspllte vlrrnpgmrl srnrlvfeml vpsimeqkvt aieawrawrq lvrrhgepap
      181 gpapegmiva paadtwrmip swewheagvg pqrsetvvrs srlasaiert vdehpddasr
      241 rlrslpgigv wtaaevtlra hgdpdavsvg dyhlaasvgq alagapvddd gmlellspwn
      301 gqrqrvlrli grsgihkprr gpkitiqdhr rh
//
LOCUS       WP_285037582             481 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285037582
VERSION     WP_285037582.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 481)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 481)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..481
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50412
     Region          129..473
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mtdglggrgr grrgrhhgir triaggslli avvvslfagl ainaqleriv rdgtvqalrs
       61 dgaqyvfalq arpddplqgp glgtriavia pdgsipvfsl pttlagqlsa laatrevtiv
      121 dagratyvll sqpvtvggdt wyviagrdea eettvlvqmr lllvgsfall vlgvaaggwi
      181 lttvslrpvt rlrvsaqsls grstaellpv graddeiaql aitlndlier lrasadrerq
      241 lvsdashelr tplailrtql elarledssr eqlladiega ersatrlsal vtsllelsri
      301 eadapvgrst adaldaetle averarfrva sddalagvev evvsaladra pdaaatyavr
      361 addfgrlvdn llgnalqafa drgtaprrls vmlddaadll tlrvsdtagg ldpafepral
      421 erfsrsdatr ssghgsglgl aivaaiarna ggairllnrp ghglevvvtl pvapvlpadp
      481 v
//
LOCUS       WP_285037594             287 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Plantibacter
            sp. ME-Dv--P-095].
ACCESSION   WP_285037594
VERSION     WP_285037594.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..287
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30611
     Region          2..281
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mriavtgssg klgsatverl rrdghtvhgl dlagaagpgf trvdltdygq tidsllgvta
       61 rffrldavvh laaipvnglv pdaatfhnnl tvsfnvlhga lragirtivt assitamgfp
      121 feeapeflpi detvsrannt yalgkvaeea maaqlvrwae gtsitalrft nvvapgeygt
      181 farasepgyr rdllfsyvda rdgaqavala laraepgfev ydvcasdtgt tvpsaelaat
      241 hfpgvplreg lgefetlmsi dkararlgye pehlwrdefe reeaarg
//
LOCUS       WP_285037801             470 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Plantibacter sp. ME-Dv--P-095].
ACCESSION   WP_285037801
VERSION     WP_285037801.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 470)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 470)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 470)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..470
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48681
     Region          135..461
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mattrrlidr lgirmriagg slliailiav aagivlnaqi erivrdgtss vlssdsapyv
       61 valqtepdds fdapgpsqlv avltpdgstp intlpaslad klpdvggsgq ahdvrvgdas
      121 fivlsttvav aggdwivvaa rdaqeettvl aqmrtllftg laviavgaag tawaltslsl
      181 gpvrrlrrsa dalsagssse llavgqarde isdlartlne lierlrdsar rerqlvsdas
      241 helrtpiall ntqlqiavae assveqmvrd vdgarrnvtr laalvtslle lsaieaaddg
      301 vrssigalgr eaddatdrar fraqdtevsi lydgpellas ddgtedtgsf pigaeafgri
      361 ldnllnnalr avghggvidv qlavgggfaw llvtdtgggm dpafepfald rftrqdasrt
      421 ggqgtglgla ivaalvrnag gsieldnrpg dgltiriglp avqaapshds
//
LOCUS       WP_285037839             124 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285037839
VERSION     WP_285037839.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..124
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14103
     Region          13..114
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mfryarlcsv rgdqgkairs lldriadkwa llliatlhdg pfrfteleqr ipgisrrmlt
       61 ltlrnlerdg lvtrttfaev pprveyeltd laesliphav alaewagehv ptieanrnay
      121 derf
//
LOCUS       WP_285037851             328 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Plantibacter sp.
            ME-Dv--P-095].
ACCESSION   WP_285037851
VERSION     WP_285037851.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. ME-Dv--P-095
  ORGANISM  Plantibacter sp. ME-Dv--P-095
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Plantibacter sp. ME-Dv--P-095"
                     /db_xref="taxon:3040299"
     Protein         1..328
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=33322
     Region          2..325
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mrrrglvmgv lgalivavfl vslmvgntly tpvdvvrvil gedvagagft vgrlrlprav
       61 lavlagasfg lagvtfqtml rnplaspdii gisagssaaa afaivtlslg atavsvfaiv
      121 vglavavlvy llsyrsgvag trliligigi aamldsvtay ilsraaqwdl qeatrwltgs
      181 lngtnwaqvw pvvaalfvlg pvllgqsrnl aatqlgddta aalgvrvdrt rlivivaavg
      241 liafataasg piafvaflsg piasrivgrg gsmlvpaalv gallvlvadl agqyllgtry
      301 pvgvvtgvlg apfliwliir tnrsggsl
//
LOCUS       WP_285038094             430 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Plantibacter].
ACCESSION   WP_285038094
VERSION     WP_285038094.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter
  ORGANISM  Plantibacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Plantibacter"
                     /db_xref="taxon:190323"
     Protein         1..430
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44789
     Region          10..386
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtdprpattv ivgaglfgla tavhlaragr rvtilesgta agattaagag fvglwaagya
       61 wywdeselal eqagldfyrg ldaagydigl rntgnvwlal teqavldhll pfaehplrpe
      121 darlltavet aelvpgldpe aivgafihpd giqisapdag ialaalarae gveiieqtpv
      181 vdllaeggra vgvltatrer vlgdevvlaa gswtnellaa tdrvlpfarv iasrlttapf
      241 glgevptlmi peldglwire hlggltygng vgyealavrd spadrrpdrp dlveamrehl
      301 spivselipa aapvvddaea vqgivsytad rrfiagsvpe ldglfvvagd nesgvthgpg
      361 lgrmlaeliv tgespfvdas ryapgrfpsr pfadeaavaa amparravda rgtaakrvtt
      421 esglpaesgr
//
LOCUS       WP_285038158             666 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ABC1 kinase family protein [Plantibacter].
ACCESSION   WP_285038158
VERSION     WP_285038158.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter
  ORGANISM  Plantibacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Plantibacter"
                     /db_xref="taxon:190323"
     Protein         1..666
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0004672 - protein kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=71705
     Region          125..578
                     /region_name="AarF"
                     /note="Predicted protein kinase regulating ubiquinone
                     biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport
                     and metabolism, Signal transduction mechanisms]; COG0661"
                     /db_xref="CDD:440425"
ORIGIN      
        1 mltdaltivl avvsalllgf aarrvldapv gwprsilvgl vvfvtgppfv nwllqqtglv
       61 qpgeagdara afaaiavall aigwifalgl gvlvaievii ptrplmnpid vvrsairrrr
      121 rtrrylqila iasrhgagwl vhgrsrvqle lttseqrana iiatindsgv tfvklgqvls
      181 trrdlvpepy lsalaslqse attlpwhevq vvietelgap idtvfasids eplaaasvaq
      241 vhtaelldgt pvvvkvqrpa arvqveadad ivvrlaerae thtkfgqdlr lasvarafts
      301 tlleeldyri earnvemirs tlkrreerde gvritvprvy paasgarllt mdlvdglpls
      361 rardriatip keeretlatg lmevvleqil vhgvfhadlh pgnvilredg slglidfgav
      421 gviersqrqr ltavmlatvs eddiaatdal llivdlpeda dldalrhdvg ivitterhrp
      481 ggdgsifsrl ldvirqhhia lpgdlaaafr sfatlegclk aldpdfdmfe qalpmvprll
      541 rrsqsirqta vtlqaqaavt aalarnlprr ldsllsgled gtvgvtlkgf adepakglve
      601 gvtaeivgtl isiaalviav vlvvtgagpv lpgglrvfdl iaafigflgf lgllrvlrqt
      661 vvrrgr
//
LOCUS       WP_285038130             487 aa            linear   BCT 25-DEC-2024
DEFINITION  rhamnulokinase [Plantibacter sp. lyk4-40-MEA-4].
ACCESSION   WP_285038130
VERSION     WP_285038130.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. lyk4-40-MEA-4
  ORGANISM  Plantibacter sp. lyk4-40-MEA-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167330
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Plantibacter sp. lyk4-40-MEA-4"
                     /db_xref="taxon:3040298"
     Protein         1..487
                     /product="rhamnulokinase"
                     /EC_number="2.7.1.5"
                     /GO_function="GO:0004370 - glycerol kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008993 - rhamnulokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006071 - glycerol metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0019301 - rhamnose catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50980
     Region          9..468
                     /region_name="ASKHA_NBD_FGGY_RhaB-like"
                     /note="nucleotide-binding domain (NBD) of rhamnulokinase
                     (RhaB) and similar proteins; cd07771"
                     /db_xref="CDD:466791"
ORIGIN      
        1 msaagrsgtv aavdlgatsg rvmlghvgpg elrlvpvarf pntpvrtpdg lhwnilelyr
       61 siiaglsgaa kqephlasig idswavdygl lrhgrllgap fhyrdertaa gveavhgtvp
      121 fadlyrvngl qflpfntvyq laterdagml dvadtallvp dliahwltga rvaeatnast
      181 tglvragept awdtellgrl hipatilppi vqpgdrigtl leavaaevgl asstpvtaig
      241 shdtasavva vpmttpdaay iscgtwglvg velerpvlte asraanftne ggvdgrtrfl
      301 hnvmglwlls esvrtwergg etidlpglia qaaavdapvs vfdandprfl apgdlparia
      361 gfltehgrav pqsraefvrc iieslaqafa davhtasels gvqvraihvv gggsqntllc
      421 qltadragip viagpveata lgnvlvqara vgiidgdles lralvarsfe ptryeprkpa
      481 gsttvsr
//
LOCUS       WP_285038180             486 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [Plantibacter].
ACCESSION   WP_285038180
VERSION     WP_285038180.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter
  ORGANISM  Plantibacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Plantibacter"
                     /db_xref="taxon:190323"
     Protein         1..486
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51903
     Region          6..363
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mhlvedstet ditrvfqdri ssgvapgsyv avfdrervrf eqgfggvtvg gpvpdadtlf
       61 riasctksft aavllilrda grldldapvd efvpefapvl pdgiavrptv rmlltmsggl
      121 gtddpwgdrq esitvdefrr llvrgvrcvt tpgtafsysn lgyallgqvi ervtggsyid
      181 avtslllepl glgavferpe gdgavtatgh rvrreravde dgrfvevpfs gpgvfssigg
      241 lfasastlig wvrwldgawt gdetgplssa srremqqlhr lapsrptldg vpprlalgyg
      301 fglfveedad lgtlvshsgg ypgysahmrw hptsgfgvva fenagyaava kpaeqalrla
      361 iagaqasgel lepairpwpe tlvasmtatg llshwddrva aslfaenval drplderrea
      421 vdaavtavgg iaevasgrat picdspdhlv wfvegtegrl rlevrmtpvl plrvqtftvt
      481 vddqge
//
LOCUS       WP_285038255             231 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: 5-oxoprolinase subunit B family protein
            [Plantibacter].
ACCESSION   WP_285038255
VERSION     WP_285038255.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter
  ORGANISM  Plantibacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Niehaus,T.D., Elbadawi-Sidhu,M., de Crecy-Lagard,V., Fiehn,O. and
            Hanson,A.D.
  TITLE     Discovery of a widespread prokaryotic 5-oxoprolinase that was
            hiding in plain sight
  JOURNAL   J Biol Chem 292 (39), 16360-16367 (2017)
   PUBMED   28830929
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Fan,C., Li,Z., Yin,H. and Xiang,S.
  TITLE     Structure and function of allophanate hydrolase
  JOURNAL   J Biol Chem 288 (29), 21422-21432 (2013)
   PUBMED   23754281
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Wang,L., Grau,R., Perego,M. and Hoch,J.A.
  TITLE     A novel histidine kinase inhibitor regulating development in
            Bacillus subtilis
  JOURNAL   Genes Dev 11 (19), 2569-2579 (1997)
   PUBMED   9334321
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005226
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Plantibacter"
                     /db_xref="taxon:190323"
     Protein         1..231
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=23922
     Region          10..229
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 mvntdtssgp vlramgeeav llelgsledv llvhralaas rpaglvdlvp aartvlavtg
       61 argpalaavg twllataera lapgaggstv aveeelarpd vvihvrydgp dlretaellg
      121 meladliawh tarawtvafs gfapgfaylv peredetigr pleiprlsvp rttvpagsva
      181 lagtfsgvyp raspggwrii gttdavlwdd aadppallvp ggrvrfvqvv a
//
LOCUS       WP_285038284             367 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [Plantibacter].
ACCESSION   WP_285038284
VERSION     WP_285038284.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter
  ORGANISM  Plantibacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Plantibacter"
                     /db_xref="taxon:190323"
     Protein         1..367
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41048
     Region          64..356
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mgtvksyetk tkgrlyevwy tkpdgsrghd rgfklkrdae ahlatvevsk lkgsyvdrad
       61 aratiaqlgt ewiarhktkv tpsshhsves awrvhvlpew ggyavgavtk rqveawltrl
      121 getrshttva rardllagif ddaiednrvt knpsrgitik kkpipdevfl thaqvealag
      181 asressivyf laytglrwge atafrvrnid qarrrvnire avaevnyqqi lgsvksherr
      241 tvaypdfldt evaaacknka pddlvwtadd gtflrpghah ngwfaravkr cmdddprfrr
      301 itphdlrhta aslaisagan vkvvqrmlgh ksakvtldty aalfpddldn vthalsrqrs
      361 eqvhrra
//
LOCUS       WP_285038360             126 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: fluoride efflux transporter FluC [Plantibacter].
ACCESSION   WP_285038360
VERSION     WP_285038360.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter
  ORGANISM  Plantibacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Plantibacter"
                     /db_xref="taxon:190323"
     Protein         1..126
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12410
     Region          20..126
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 mtpwlflaia aaggvgaaar fvvdglirsr vggaypwgtt vinvsgslll glvtalalgg
       61 vvdeawrlvl gggllggytt fstasietvr llhdgrsrag atnalgmlva svvaalvgyg
      121 vgslla
//
LOCUS       WP_285038388             123 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [Plantibacter].
ACCESSION   WP_285038388
VERSION     WP_285038388.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter
  ORGANISM  Plantibacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Plantibacter"
                     /db_xref="taxon:190323"
     Protein         1..123
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13642
     Region          15..120
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mtsvdtqlgr rpgftdgilp aacpsrtvld hvtskwgvlv llalsdgthr wgelrrvvqg
       61 isekmlvqtl rtleedglvi rvahpeippr veyslsdrgr dlnehlmplm awidhnasei
      121 lgr
//
LOCUS       WP_285038412             371 aa            linear   BCT 25-DEC-2024
DEFINITION  lactonase family protein [Plantibacter sp. lyk4-40-MEA-4].
ACCESSION   WP_285038412
VERSION     WP_285038412.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. lyk4-40-MEA-4
  ORGANISM  Plantibacter sp. lyk4-40-MEA-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Plantibacter sp. lyk4-40-MEA-4"
                     /db_xref="taxon:3040298"
     Protein         1..371
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=38449
     Region          7..371
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 msddnpylll gsytseadgt gagisllrqd eagtlrlvqs seaqspsflt lhptlpivya
       61 asestgavea fkrsgefgla pfgkpieagd svchvatvpg advliascyg dgrvvtvpla
      121 enaafagdpr lgeasvdpwv sptalaaesa dagedaltll aleaavgeal psrpsrahas
      181 allpdgriat tdlghdtvri wqlrgsrlvl dhtvvfprgt gprhlvvhps ghlhviteys
      241 vevftlgvdg tdghwhilaa tvatsegvse gdtgaeisla asreqlhvgv rgsdriatlr
      301 vtgdgsrvea vadvecggtm prhhresgrf lhvanqlsns iasfrldert gvpttllgtl
      361 dagsptclil a
//
LOCUS       WP_285038415             451 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: aldehyde dehydrogenase family protein [Plantibacter].
ACCESSION   WP_285038415
VERSION     WP_285038415.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter
  ORGANISM  Plantibacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Plantibacter"
                     /db_xref="taxon:190323"
     Protein         1..451
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=47852
     Region          4..446
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 msytilnpan ehvvttvehl dlaetdaaia raaiaqrswa avspadraqa lrrfaasvda
       61 drehlaslev vnsghpitqa rweaghvrdv leyysasper lfgqqipvag gidltfhepl
      121 gvvgiitpwn fpmtiaawgf apalaagnav vlkpaewtpl tsirlgelal esglpeglfq
      181 vlpgrgsvvg erfvtnetvr kvvftgstav gkrimagaae qvkrvtlelg gksanivfad
      241 adleraaaaa pygvfenagq dccarsrilv qrsvyerfme llepavqgvv vgdpndeate
      301 mgplvsaphl aavrsyvpeg apvaftgsap dgpgywfapt vltpgrddrt vreeifgpvv
      361 avlpfedead altlandtey glsgsiwtrd vgrairaara vesgnlsvns hssvrystpf
      421 ggfkqsglgr elgpdaplaf tetknvflav d
//
LOCUS       WP_285038444             573 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Plantibacter sp. lyk4-40-MEA-4].
ACCESSION   WP_285038444
VERSION     WP_285038444.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. lyk4-40-MEA-4
  ORGANISM  Plantibacter sp. lyk4-40-MEA-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Plantibacter sp. lyk4-40-MEA-4"
                     /db_xref="taxon:3040298"
     Protein         1..573
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=60028
     Region          183..565
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mqaghvqavp arpaparpaa aprpaspavg isvpaaaaap lprtnhlfag aqfafiasil
       61 mlglyiglts twtllepdfl iglsltaaat sllfavppsg alrgllvlvp tidilavgff
      121 rdtlpnlpts gllivipvlw laggfgvsal pvpvfgaifv slipvaraga wpttpggwga
      181 icilpalvli mtvtvhlaar qlrahegrar ialaaateaa aiattvsesv daavaffrpd
      241 gtaalrnaat yeqaelagfd rktragvhvy gpdrktrvsp ekqvinralr gesfrgelyw
      301 igepgdqrai ignarpvhtd dgafvgtitv ghdvtdlana valreaflid vshelrtplt
      361 siigyldllt eghdlrqlgl erevstiqrn aeqlyaiigd llaagdaemr vrialtdvad
      421 iarasaaail pqaseagvav raeipphvel egdggrlrqv ldnllsnavk ytprggrvav
      481 tvavdgetct vnvadtgigi spddqrqlfd rffrarevrd darpgvglgl sivksiteah
      541 hgwitvssrp grgstftvtl plrqpragap sas
//
LOCUS       WP_285038485             218 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: IMPACT family protein [Plantibacter].
ACCESSION   WP_285038485
VERSION     WP_285038485.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter
  ORGANISM  Plantibacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Park,F., Gajiwala,K., Eroshkina,G., Furlong,E., He,D.,
            Batiyenko,Y., Romero,R., Christopher,J., Badger,J., Hendle,J.,
            Lin,J., Peat,T. and Buchanan,S.
  TITLE     Crystal structure of YIGZ, a conserved hypothetical protein from
            Escherichia coli k12 with a novel fold
  JOURNAL   Proteins 55 (3), 775-777 (2004)
   PUBMED   15103642
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Okamura,K., Hagiwara-Takeuchi,Y., Li,T., Vu,T.H., Hirai,M.,
            Hattori,M., Sakaki,Y., Hoffman,A.R. and Ito,T.
  TITLE     Comparative genome analysis of the mouse imprinted gene impact and
            its nonimprinted human homolog IMPACT: toward the structural basis
            for species-specific imprinting
  JOURNAL   Genome Res 10 (12), 1878-1889 (2000)
   PUBMED   11116084
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Plantibacter"
                     /db_xref="taxon:190323"
     Protein         1..218
                     /product="IMPACT family protein"
                     /calculated_mol_wt=23051
     Region          10..203
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 mttarqypat iaapvehelv ikksrflgla hpvaspedae aviarvkkqa wdarhhcvam
       61 vtgllgdqar ssddgepsgt agmpilevir rreltdvvvv vtryfggvkl gagglvrays
      121 saasetldla slvrretltr atlvvphada grydnllrdw sathgatlge pvygaqaele
      181 lwvppaeler lqadvasasn gslavavgee rvvdvpdg
//
LOCUS       WP_285038528             289 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Plantibacter sp.
            lyk4-40-MEA-4].
ACCESSION   WP_285038528
VERSION     WP_285038528.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. lyk4-40-MEA-4
  ORGANISM  Plantibacter sp. lyk4-40-MEA-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Plantibacter sp. lyk4-40-MEA-4"
                     /db_xref="taxon:3040298"
     Protein         1..289
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30851
     Region          40..286
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          199..282
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtttltapag patdtfdral aslewtihgt drdrlaanvp lrrphaasgf vylssgrvrl
       61 saadgsrdld agdlvffpra hattvvaled aelldvaftp pgqrqqvaet lpehlyvadf
      121 agqepsmval legmgcpqaa grprpgdsvi csriattivs aalrtwneag caperwlqri
      181 gdphigavld alhaepgrpw tfetlartam msrsafaerf revvghtpra ylttvrmeta
      241 kgliltgdas vaelagalgy vsedgfaraf qrytgltpar wraeaalaa
//
LOCUS       WP_285038755             434 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Plantibacter].
ACCESSION   WP_285038755
VERSION     WP_285038755.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter
  ORGANISM  Plantibacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Plantibacter"
                     /db_xref="taxon:190323"
     Protein         1..434
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46176
     Region          105..381
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mdwlwnldvi dgplvwvldg lsiagllylv irrsgllwyl saaiallaga llalgtvwlv
       61 fdvlnlfggp lirsaepwli gvfagialav lticwrvswk rrviavacil vfgataalgv
      121 ngaygvqttl gsmfhvqnrk pitlvtptst ptgdparply etwkppadlp ktgrfgplpt
      181 gdripntnsg fdarpaqiyy ppaalvkdpp alpfvlmmmg qpgdpdakwi gealdaiaad
      241 hqglapialv vdqlgdpsvd plcidgrygk vetyvtqdvl pwakanlhil qspkdwtvag
      301 ysaggscaiy ygakypqtfg nvvsvsgeey pgaglpadnl rvmfdgdqna ydaikpstim
      361 akmnyadtea ffsagtadav ytammrraaa tatsagwkvq tfaipggdhg assltggldq
      421 tlralyprig lqrp
//
LOCUS       WP_285038780             277 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sugar phosphate isomerase/epimerase family protein
            [Plantibacter].
ACCESSION   WP_285038780
VERSION     WP_285038780.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter
  ORGANISM  Plantibacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Plantibacter"
                     /db_xref="taxon:190323"
     Protein         1..277
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29713
     Region          <116..276
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtippttern hmsdsnptaq rypltgygvi vpseripgaf asgadyaept ivgnlvvadg
       61 dgwtrhpdyd asirrgsfai lfpgdlslad pdfpaervta yldavmpiig svsepgakiv
      121 fgsgtartip agvdvtaara rfaevvvetr dtaernglqi vleplnrdet nllnsleetv
      181 afldefgidr vpvvadlfhi mleeeplavv kalgarigha hiadtgrrpp gqgdwpltef
      241 italrdggyd gpvtveclfe dfepeleaal ahlrqla
//
LOCUS       WP_285038787             293 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sugar phosphate isomerase/epimerase family protein
            [Plantibacter].
ACCESSION   WP_285038787
VERSION     WP_285038787.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter
  ORGANISM  Plantibacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Plantibacter"
                     /db_xref="taxon:190323"
     Protein         1..293
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31130
     Region          30..268
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtrtnakaea hvnaqhpvsw tlsgfgdeid adpttqiavl ealgashiev rsawgvnvid
       61 ldadqlarlg aqlersgmgv saigspigkv dvaldaelev arlaraiaaa halgtpniri
      121 fsffrgegvp veatrddvlv rmrlladlae regvvllhen ekdiygdvpe rildlvesvg
      181 spalrlawdn anfvqvgvap fddgyamlrp yldylqvkda vaasgqvvps gdgdgqlret
      241 ltalrddgyt gfaslephla dthalggfsg pasfgvaara frrltdelgi elr
//
LOCUS       WP_285038904             450 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Plantibacter sp.
            lyk4-40-MEA-4].
ACCESSION   WP_285038904
VERSION     WP_285038904.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. lyk4-40-MEA-4
  ORGANISM  Plantibacter sp. lyk4-40-MEA-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 450)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Plantibacter sp. lyk4-40-MEA-4"
                     /db_xref="taxon:3040298"
     Protein         1..450
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47540
     Region          55..436
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(161,163,283,285,319..321,365)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mkrispsrtv lrraataava samigaslva cssgggstas gdakdiesal eaggeityws
       61 wtpsaeaqva afekaypkvk vnlvnagtnt teytklqnai kagkgapdva qveyyaipqf
      121 alsdslvdln aygfgdlkdd yspgpwssvn igdglyalpq dsgpmamfyn ktvfdqygia
      181 vpttwdeyia aaaqlhtadp skyitndsgd sgfatsmiwq aggrpftadg tkvsvnlade
      241 gskkwadtwn qlvegdllsd vpgwsddwyk slgngsiatl itgawmpgvl essvaeasgq
      301 wrvapiptyd gkpanaengg ggqvvlkqsk npalaagflk wlnndedsvk vfldnggfpa
      361 ttadlnsdaf lsaapayfgg qkinevlvqg akdvstgwqy lpyqvyansi fadtvgqsya
      421 nkadlndgla dwqkqlveyg ntqgftvtek
//
LOCUS       WP_285038951             200 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Plantibacter sp. lyk4-40-MEA-4].
ACCESSION   WP_285038951
VERSION     WP_285038951.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. lyk4-40-MEA-4
  ORGANISM  Plantibacter sp. lyk4-40-MEA-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Plantibacter sp. lyk4-40-MEA-4"
                     /db_xref="taxon:3040298"
     Protein         1..200
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21108
     Region          129..>188
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mteirayrps draavaaict rtgdsgadat gqfstddllp diyalpyveh epelallvda
       61 gsgpigyilg tadttafdrw fierwwptve gkyaaaaasg aasegergiv rsatdrggla
      121 pellaqypah lhidllpetq gmgvgrrlid afcgllaarg vpgvhlgvgv sntgaqqfyq
      181 rtgftrvegg pgahwyaktf
//
LOCUS       WP_285039056             227 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Plantibacter sp. lyk4-40-MEA-4].
ACCESSION   WP_285039056
VERSION     WP_285039056.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. lyk4-40-MEA-4
  ORGANISM  Plantibacter sp. lyk4-40-MEA-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Plantibacter sp. lyk4-40-MEA-4"
                     /db_xref="taxon:3040298"
     Protein         1..227
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24662
     Region          40..138
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mirsalrtlg wwardyayal vwqarafvsr tdphdflsgd rspivvlpgv yetwrflepl
       61 irrlhddghp vhvidplgrn drsvpvaarl vadyleangl gdvvllahsk gglvgkyvms
      121 lggggarisg mlavaapfag sryarlmllp slriftpddp tilalsreat vnprivsvyg
      181 rfdphipggs rldgaknvel dtgghfrila hprvfaeaql ladgrda
//
LOCUS       WP_285039097             348 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Plantibacter sp.
            lyk4-40-MEA-4].
ACCESSION   WP_285039097
VERSION     WP_285039097.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. lyk4-40-MEA-4
  ORGANISM  Plantibacter sp. lyk4-40-MEA-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Plantibacter sp. lyk4-40-MEA-4"
                     /db_xref="taxon:3040298"
     Protein         1..348
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35763
     Region          1..347
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 msvidhgrrq irvetvhiat lvpvrsvlvc lglvvviiga glfattigay eigfdavira
       61 ivdpasdpdv rqvvtewrlp rvlfavlcga alalsggifq sltrnplgsp diigfgvgaq
      121 fgvtltmlvl glntylfkav galvggllta llvavlanrh tmssfrliiv gigvsaglgs
      181 ltswilisvs veqammaatw gagslaslgf dqllpaataf vvftllarpl rrslpvlemg
      241 ddaamalgvr pgrtrltamv vgvalvalvt aaagpisfia laapqiaqrl trsntpmgla
      301 pvmltgaalv vvsdavaqll avpvgvvtls vggiyltcll aaqfvrrt
//
LOCUS       WP_285039336             265 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Plantibacter sp.
            lyk4-40-MEA-4].
ACCESSION   WP_285039336
VERSION     WP_285039336.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. lyk4-40-MEA-4
  ORGANISM  Plantibacter sp. lyk4-40-MEA-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 265)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Plantibacter sp. lyk4-40-MEA-4"
                     /db_xref="taxon:3040298"
     Protein         1..265
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27822
     Region          1..249
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 matalvtggt sgigaafata lagrgfdlvl vardverler saerlratgr tvevisadls
       61 dradvarlaa riedqaspie vvvnnagfgv harltdpdts eldnaievmc rsvttlsgaa
      121 aramrergrg tiinvsstag yittggysav kafvttytea lavelagsgv rvtalcpgwv
      181 rtefhdragi strsipsglw idvdrlvada lrdagrgvvi sipsfrfkal malvkfapra
      241 sirwisgrms ssrraanaaq sgarr
//
LOCUS       WP_285039380             756 aa            linear   BCT 25-DEC-2024
DEFINITION  MMPL family transporter [Plantibacter sp. lyk4-40-MEA-4].
ACCESSION   WP_285039380
VERSION     WP_285039380.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. lyk4-40-MEA-4
  ORGANISM  Plantibacter sp. lyk4-40-MEA-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 756)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Plantibacter sp. lyk4-40-MEA-4"
                     /db_xref="taxon:3040298"
     Protein         1..756
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=78355
     Region          31..747
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 mthgrhggtr tdadtrtqrr nragaprwlr vvlpavlill wltaagvggp yfgkvsevat
       61 ndqtsflpas adatevqtal dgfregddip alvlfvrdgg itdedraaid delsalsste
      121 gvadgvspai psedgaavev fvpisgdaev gdvveairaq laeaapagld vfvtgpagft
      181 adltdafagi dgillltalg avflilivvy rspvlpflvl gtslfalcta lltvwwlaka
      241 gvvllngqvq gilfilviga atdysllyvs ryrealrdhe rrwdatwaal rgsfepivas
      301 ggtviagllc lllsdlnsnk algpvasigi vfsvlaaltf lpalllacgr tsfwplrpky
      361 gsehrvrass tdgtavpttg lwggiarlis rharvvwigs tllllvaslg vfqlkadgva
      421 qsdlilgtse ardgqaalge hfpagsaspv yvltqegdaa qvigileead gldsvqvlss
      481 daatgtadat vsdgeavfta paagppgtpv asaeptvddg rvvlqatlda apdsataees
      541 vrqlrstlda evgthtpvgg vtataidsnd asihdrnlii pvvlavilli lmlllrsvla
      601 pvllilsvvv sfaaalgvsa lvfdhvlgfp gadpsvplyg fvflvalgid yniflmtrvr
      661 eeslrvgtra gvlrglaitg gvitsaglvl aatfaalgvi pilflaqiaf ivafgvlldt
      721 iivrtllvpa lshdigsaiw wpsklakgrv ehrhaa
//
LOCUS       WP_285039430             475 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Plantibacter sp. lyk4-40-MEA-4].
ACCESSION   WP_285039430
VERSION     WP_285039430.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. lyk4-40-MEA-4
  ORGANISM  Plantibacter sp. lyk4-40-MEA-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Plantibacter sp. lyk4-40-MEA-4"
                     /db_xref="taxon:3040298"
     Protein         1..475
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=51028
     Region          189..>390
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mlstepappr ppaalttral vvrhvavfat favlagtfwt nlftiwgyta valvsggaal
       61 aclmvvrpnw rrtrvpwslv gygvlsivsi awsaypsgta atllgaalct ilgvtlagcf
      121 swpevirvlg ravtwvlsls llfefvvaai irhpvlpnfy agdsadppll dywsrdllfs
      181 ggrvqgisgn anllavvall giivfglrla arrdepgaag lagperrwtl lirlglsvvm
      241 fllsfsttil laavvtavvl aaalairrap rpeartpvyl gflgigvvga vgavvfrtql
      301 lgllgkspdl tgrldiwatv wrlieqrpvf gwgfsspwap weplftdlvi rrgvrqlqah
      361 nawldvwfql gvvglvlfaa vvlsmltrtw flavdrprvd ldaqrpytal slapvliavs
      421 lvvqsvaesr iliesgwvll vllvvktkqe pawpvptvaa ssdlapahrr dvigg
//
LOCUS       WP_285039488             428 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Plantibacter sp.
            lyk4-40-MEA-4].
ACCESSION   WP_285039488
VERSION     WP_285039488.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. lyk4-40-MEA-4
  ORGANISM  Plantibacter sp. lyk4-40-MEA-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Plantibacter sp. lyk4-40-MEA-4"
                     /db_xref="taxon:3040298"
     Protein         1..428
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45424
     Region          36..428
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 midedlrirl adlggfdtar gslagvvvvd vtrvvagpyc smvladlgat vikvehpdep
       61 dytrtfppll pgegdsdgqv gddplsgffa qynrnklgvt anlrhasgaa llerlvarad
      121 vlvenfrpgt mdrlglgyeq lrtinprlvy aalsgygqtg psrgrpaydn saqatgglws
      181 mngpaggppt rvgtiigdla aslygtigvl aalrhaettg tgqlvdisqq dsvltltena
      241 vvaytaegtv pgplgnahpf vrpyeafpcr dgfvffggyt dkfwriscel fggpgeyeah
      301 pglhamvdrf deevyehavr plverwfagr skaelealag dlvplsavkd igevvadpqi
      361 avremvveta ypgfgalrtf gspvkldatp prtngrapat gahtaavlre lldydeatid
      421 elraagti
//
LOCUS       WP_285039478             127 aa            linear   BCT 25-DEC-2024
DEFINITION  VOC family protein [Plantibacter sp. lyk4-40-MEA-4].
ACCESSION   WP_285039478
VERSION     WP_285039478.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. lyk4-40-MEA-4
  ORGANISM  Plantibacter sp. lyk4-40-MEA-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Plantibacter sp. lyk4-40-MEA-4"
                     /db_xref="taxon:3040298"
     Protein         1..127
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13540
     Region          8..121
                     /region_name="PhnB"
                     /note="Zn-dependent glyoxalase, PhnB family [Energy
                     production and conversion]; COG2764"
                     /db_xref="CDD:442048"
ORIGIN      
        1 mqlaatriit ddvdtlvafy ervtgataar lhplfaevrt dtgtlaiass atipllgeda
       61 aapranrsvi ldllvedvda vytrlqgvve tfvnepttmp wgnrsllfrd pdgnlvnvft
      121 pitvdag
//
LOCUS       WP_285039559             764 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: heavy metal translocating P-type ATPase
            [Plantibacter].
ACCESSION   WP_285039559
VERSION     WP_285039559.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter
  ORGANISM  Plantibacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Plantibacter"
                     /db_xref="taxon:190323"
     Protein         1..764
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=78373
     Region          7..763
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msapliqldl diegmtcasc varvekrlta ldgveaqvnl ateratvtap stvtadelia
       61 avskagytat vrppaderaa vnreqtptsg ttpdpsatvt tlrtrlvvsa vlalpvvlla
      121 mipawqfdhw qwlsltlatp vvfwggypfh ratfatlrhg svtmdtlitl gtgaaylwsv
      181 walffgmagm tgmrhefaff apdadpssal ylevaasvtv fllagrlieq rskraageal
      241 rdlmtlgase vsvlrhrapd ptdlmaptrt eeripieqll vgdhflvrpg esvatdgvvv
      301 egaasvdesl vtgesvpvel vagsrviggt iarggslvvr atavgagtql armaqaveaa
      361 qlgksrvqrl adrvssvfvp vvlvialgta ivwaltgstm eaaftaavav liiacpcalg
      421 latpvallvg tgrgaqlgil iagpealera sgidrilldk tgtvtsgrms vtevwaagat
      481 devlalgaal eaasehpiae aivaeatrrd aprpvvsdfa sleglgvtgt idggtvlagr
      541 pafaedqgfr igpdaasala aaaerastvv vvawdgevrg vvevadtvkp earaaigrav
      601 slgmtpvllt gdnaavaarv aaevgiaevi adaspadkva averlqaagh rvamvgdgvn
      661 daaaiatadl giamgtgtda akgaadlsiv sgslataida vrlsrrtlgi irgnlfwafa
      721 ynvaaiplaa lgllnpmiag aamafssvfv vlnslrlrrf rpaa
//
LOCUS       WP_285039576             703 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Plantibacter sp. lyk4-40-MEA-4].
ACCESSION   WP_285039576
VERSION     WP_285039576.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. lyk4-40-MEA-4
  ORGANISM  Plantibacter sp. lyk4-40-MEA-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Plantibacter sp. lyk4-40-MEA-4"
                     /db_xref="taxon:3040298"
     Protein         1..703
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73975
     Region          16..479
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          614..679
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(637,646..648,655)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            647
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mtiqtpnrpg qasarpfrsv lvanrgeiac riirtltamd iesiavfsda drdaphvrla
       61 dravrlgpap asdsyldvda vvraavttga eavhpgygfl seqpalaral aaagivfigp
      121 deralvlmgd kirakdhvaa rgvpiiegva dasldddalv ragvaigfpl ivkpaggggg
      181 kgmqvverte elpsaiasah rvaeaafgda tlllerfvtr prhievqvla dahgavvhlg
      241 erecslqrrh qkvveespsp liddrqrarl geaactvars vgyrgvgtve flvaddrpde
      301 faflemntrl qvehpvtelv tgldlvewqv rvaagepltm tqeevvlrgh avearlyaed
      361 pssgflpqtg vlervclpqg pgvrvdggiv agqfvgpwyd pmlakivswa edrgtalrrl
      421 daalaatvvf gvrtnlgflr rlladedvva grlhtgliae llddrpsdsm seriltaaal
      481 aetehrrcka eartaglgtp wsdpggwrlg aaaptrqhlr ledgrivrie vrgssddasv
      541 svddaaptra avlsrsdgtl rfehggvstl letvrvgder wialdgaisv vevvprealp
      601 aggdptaaga vdpevrtpmp gtvtavhvts gdavtagqpl vtveamkmeh lltattdgtv
      661 tlhvstggtv atrqsvatia adhvaahlna aptdaaptng asa
//
LOCUS       WP_285039577             455 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Plantibacter sp. lyk4-40-MEA-4].
ACCESSION   WP_285039577
VERSION     WP_285039577.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. lyk4-40-MEA-4
  ORGANISM  Plantibacter sp. lyk4-40-MEA-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Plantibacter sp. lyk4-40-MEA-4"
                     /db_xref="taxon:3040298"
     Protein         1..455
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48274
     Region          12..445
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mnaavdfplt rpelaftasg dalvrrtvlp nglrilsehm pgsrsatigy wvavgsrdeq
       61 patadrpatf gsthflehll fkgtpsrsal diavafdavg gehnaltake htcyyakvrd
      121 rdlpmavdvi tdmltsslld peefenergv ileelammdd dpgdvanerf fervlgehpl
      181 gppigghpqs iievgrdavv ahyranyran dvivtaagav dhdalvaqvs ealvqagwpa
      241 davaapvarr tlapaaivgg splsvvhrpt eqvhlqigga gliagderrf amsmlnsilg
      301 ggmssrlfqe irerrglays vysfagsysd agvfglaaac stakaatvae lmlaelhrla
      361 ehgvtdeels ralgqlsgas alaledsdsr msrlgraelt lgefidldes irrlqsvgqd
      421 dvqqlaqhla aqpitvsavg avdedtfapi iagvr
//
LOCUS       WP_285039792             208 aa            linear   BCT 25-DEC-2024
DEFINITION  endonuclease III domain-containing protein [Lactobacillus iners].
ACCESSION   WP_285039792
VERSION     WP_285039792.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Kuo,C.F., McRee,D.E., Fisher,C.L., O'Handley,S.F., Cunningham,R.P.
            and Tainer,J.A.
  TITLE     Atomic structure of the DNA repair [4Fe-4S] enzyme endonuclease III
  JOURNAL   Science 258 (5081), 434-440 (1992)
   PUBMED   1411536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..208
                     /product="endonuclease III domain-containing protein"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=23064
     Region          22..192
                     /region_name="Nth"
                     /note="Endonuclease III [Replication, recombination and
                     repair]; COG0177"
                     /db_xref="CDD:439947"
ORIGIN      
        1 mtsnnlvgit earqilykii slfpdakgel kwgtpfqllc avlmsaqttd kmvnkvtpil
       61 fekfpnsksl aaanisdiea cirniglyrt kakhlkatat lienkyqgiv pknkkalltl
      121 pgvgiktanv vlaeafgvps iavdthvmri akqfkivpks aepsqieail enimpqkdwi
      181 klhhamiafg rykmpakyrn enpydflk
//
LOCUS       WP_285039814             257 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Plantibacter sp.
            lyk4-40-MEA-4].
ACCESSION   WP_285039814
VERSION     WP_285039814.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. lyk4-40-MEA-4
  ORGANISM  Plantibacter sp. lyk4-40-MEA-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Plantibacter sp. lyk4-40-MEA-4"
                     /db_xref="taxon:3040298"
     Protein         1..257
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28184
     Region          8..215
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mrrriepvyd tavgvgrslf gfwrlrrhts giehlpdegg aviamthfgy lefalvewat
       61 vlhnrrrirf makqgafdqp ivgrllrsmr hiavdmraga aayadavaal rsgelvgvfp
      121 eagvsasftv relksgavrl aqeagvpiip vavwgghrll tknhrvgfre rfgvpvhfsf
      181 gepitvapga dvgasteqlr drlqgmidel qrdypvdgtg awwqpralgg taptpaeaaa
      241 adlererrre arrqtts
//
LOCUS       WP_285039823            1177 aa            linear   BCT 25-DEC-2024
DEFINITION  TM0106 family RecB-like putative nuclease [Plantibacter sp.
            lyk4-40-MEA-4].
ACCESSION   WP_285039823
VERSION     WP_285039823.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. lyk4-40-MEA-4
  ORGANISM  Plantibacter sp. lyk4-40-MEA-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03491.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1177
                     /organism="Plantibacter sp. lyk4-40-MEA-4"
                     /db_xref="taxon:3040298"
     Protein         1..1177
                     /product="TM0106 family RecB-like putative nuclease"
                     /calculated_mol_wt=128226
     Region          1..541
                     /region_name="COG2251"
                     /note="Predicted nuclease, RecB family [General function
                     prediction only]"
                     /db_xref="CDD:441852"
     Region          335..1177
                     /region_name="DNA2"
                     /note="Superfamily I DNA and/or RNA helicase [Replication,
                     recombination and repair]; COG1112"
                     /db_xref="CDD:440729"
ORIGIN      
        1 mflldgsait sasdlsnash cefaflrtvd aklgriepiv epedemlmrt sklgdqhelr
       61 vlesyraefg tgvveldrpd vrdtvalaaa vdstitafrd gapvvfqaaf fdgsfigfad
      121 fivrrpdgry rvqdtklars pkvtallqla ayveqletag ipvdddvdli lgdgtvstha
      181 vadilpvyrr rrarllriva erleadapva wgdqrysvcg rcawcdaeit asrdvllvag
      241 lrltqrdrll aagiatidnl asltltgste rpgphglsgg aggtvdgiae stlaalreqa
      301 hlqlepspaa gvpafrvhda talgllpqpd pgdvffdfeg dplytegepg darrgvrtrw
      361 gidylfglvd tdgrfrswwa hdfheertal idflayltar raefpgmhvy hyaayerthl
      421 lslaarhgvg edtiddllre avlfdlypfv rktvrvgsrs ysikkleply mgeehrdsdv
      481 tdaaasitay aearelsrsd dpelvaeger klseiaeyna ydcestrrlr nwlldlgaer
      541 gvlpgtfvtd apeplvdept plhdaltala gdpldpersd datayalaaa aidyhrrehk
      601 sfwqehfsrl iaardewedt rnvftvtsgv verdwfregr qrsdrrhmrl rgrwapgssv
      661 kvgadpfavy dhpgpytlpr aepgsrpagq itvlevddds lliqetlktd repytelpva
      721 ltpsppprpg tqvdaiaewg ravldaapgw pddgvvdilr rrpprtssge plphrgdgrt
      781 iedvtaalld lddsalavqg ppgtgktyva shvitalvqq hgwrigvvaq shdvvenlle
      841 rvvkaglspa lvaktlrsga dpdaergytv lpanghgafm aeqtggfvig gtawdfsnpn
      901 rfdrrsldll vvdeagqfsl aytiaasvaa rnllllgdpq qlpqvsqgth pepidtsalg
      961 fvadgrdvlp pelgyflhet wrmdaavtep vsrlsyggel rsaaattkrr legrapglhv
     1021 vpvhhvgnat ssqeeadrva elvrstiglr wtdpdagrid dpvseadiiv vcpynahvav
     1081 vratldaagf eavrvgtvdk fqgqeaviai vslaasspad vprgmsfllm knrlnvgisr
     1141 aqwaaylvhs palteylpvt pegvaelsaf irlvdgh
//
LOCUS       WP_285040023             100 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Plantibacter sp.
            lyk4-40-MEA-4].
ACCESSION   WP_285040023
VERSION     WP_285040023.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. lyk4-40-MEA-4
  ORGANISM  Plantibacter sp. lyk4-40-MEA-4
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 100)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 100)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 100)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Plantibacter sp. lyk4-40-MEA-4"
                     /db_xref="taxon:3040298"
     Protein         1..100
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=10695
     Region          15..81
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdtetdadta daatlfallg hpirlgvvra lldvdeltvr elnerlpgsd nslsqhlskl
       61 rlsklltarr egmtyayrit darlaaivaa alhpssepsa
//
LOCUS       WP_285040153             320 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Plantibacter
            sp. LMC-P-059a].
ACCESSION   WP_285040153
VERSION     WP_285040153.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..320
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=34298
     Region          2..311
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrivviggtg higsflvprl vraghevvsv srgtrapyae atewehverl vvdreaedea
       61 gtfpariaal gcdvvidlvc ftlpsaealv eglrghvghl lhcgsiwryg psavvpiveg
      121 ggtppfgeyg vekdriarml qqetadgglv ttslhpghiv gpgwapvnpl gnfdpdvwri
      181 laageplrvp glgaemlhhv haddvaqafe lavahrdrva gedlnvtsas aitvrgfaea
      241 aaswfgrsad lapvtweefr sttsrehadt swehlvrshc vsiekarsll gyapkhtstd
      301 avrdalrwlv andeldvpsp
//
LOCUS       WP_285040236             357 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285040236
VERSION     WP_285040236.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..357
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36360
     Region          32..339
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mlerpvpfat psrtrallva lvvcllllgv vsmavgsvai afpdvidvvl ahlggspets
       61 wsvdqivwev raprtilatv cgaglaiaga viqavvrnpl gdpsligvtp gaslgavvvi
      121 vlgggafggl plalaaflga latfavvfll grtagrmppt rlilagvaig ylvssmtyfl
      181 qtiatpnqvq rvlfwslgsv ggadwgvlpi pvivvvlgta willtsvsln alvggddlaa
      241 slgidvprlq vtllvlvaam tgslvavagg iafvglviph iarllvgadh rrmlpvaavl
      301 gsifllladl vartvrapae lpigvitaav gapfflwllt sgsrargrap vnrkvlr
//
LOCUS       WP_285040259             585 aa            linear   BCT 25-DEC-2024
DEFINITION  PhnE/PtxC family ABC transporter permease [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285040259
VERSION     WP_285040259.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 585)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 585)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..585
                     /product="PhnE/PtxC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=61253
     Region          57..285
                     /region_name="PhnE"
                     /note="ABC-type phosphate/phosphonate transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG3639"
                     /db_xref="CDD:442856"
     Region          341..585
                     /region_name="PhnE"
                     /note="ABC-type phosphate/phosphonate transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG3639"
                     /db_xref="CDD:442856"
ORIGIN      
        1 msadtrtrpg irtglrtatg tgdpvgrapr ravsperiaa vltllallaa sivalnsigi
       61 dparmaqsws naerffgrvg aisfpdpgel lyltgltlgl vicgtllaav isvpiaylaa
      121 snttpgtgwr afarffgvlt raipdvvfam vfvlvfslgt lpgilaigih sigmiskmfa
      181 daieqidegp rlairaaggs rmqeftagvl pqvmpswvat vlhrndinlr gsvilgyvgv
      241 vglgmqmsfa fksldyglgl gyavvifvlc vvmeivssav raamlgiapt grglgdrvlr
      301 girrgrdasr pgasrgwapv ataddalrrp wtatrvrntt wgwlavavvv gsvlicdiqw
      361 rdlltvwakv pavavqfwpp sfgsyelstm tdamvetiai alaatlltlv vsivvgslaa
      421 rnvapsrgvr ggmrfllvav rgipeiilai vlivisglgt qagtialaig gvgllgklia
      481 dsfeevkagp eraltaagas rlqvyagatv pqgvraligh tfymldtnir aatllgivga
      541 ggvgyyllna sqgsnygvvt aivlmilvtv lvvegiaiwm rrvfr
//
LOCUS       WP_285040277             263 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Plantibacter
            sp. LMC-P-059a].
ACCESSION   WP_285040277
VERSION     WP_285040277.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..263
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27939
     Region          8..263
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mtdiagtrwv itgaagnigs alrsalldre avlvstdvrs mtplspqevv tstdladlaa
       61 lvelfdgahg vihlggipde adfhdlaevn ivgtyhvlea arragvarvv yassnrltgf
      121 ypsgahiapd vpprpdgfyg vskvagealc rlyadkfgis tislrigsye qqpgslreqr
      181 twlspadavr afiaamttte htavfyavsa ntagwwdlda gtavgftpqd daaqwgepqh
      241 idphmpqggv yatpaystdr mrq
//
LOCUS       WP_285040401             558 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285040401
VERSION     WP_285040401.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..558
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=59077
     Region          3..546
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mnattpllrv dslsvafgtt epvvsgvsfd vergrcvaiv gesgsgksvt artllglaga
       61 sarvdaarld fdgadlrglg epawrrlrgr riglvlqdal vsldplrpig reiddalrlg
      121 tglsrgerae rvlevleavg mpepssrvgq rsgelsgglr qraliasaia ldpdlliade
      181 pttaldvtvq ariiglldri kqrgagllli shdlavvssi adhivvmrgg avveqgpaae
      241 vlttpkhpyt qalidavptd rprgtrlskg rattpdamag rtprtrieps avpaievrgv
      301 trafdrsgga spiravddvs lrlepgttlg vvgesgsgkt tlarlalglt tpqsgtvlfe
      361 ggpwseaper vrrsrrhrlg wvsqdplssf dprwrvgail adaargrgta dpdtakptva
      421 elltdvgldp alerarprtl sggqrqrvai aralagrpst lildepvsal dvtvqarild
      481 lldelqerhg lsyllishdl gvirhmsdrv avmqhgrvve ygdteqvfta prhpytarla
      541 adaprltrpp tgsgadav
//
LOCUS       WP_285040440             441 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285040440
VERSION     WP_285040440.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..441
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=46718
     Region          39..336
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mstptttgqa pavpdlsgrd laldlvrvac vvtvvivhll mvavavapdg tigisraleq
       61 qpwfdtgtwf gqimplffiv ggfatitgwr stvrrgggts dflrsrvfrl alptipvllf
      121 laaglwlaga lgvdpaiiea vaagvgsplw flaayllcqa vapflatrhd rhpfltcaal
      181 lagvilvdvv rystgllgig lvnlvfvwpl lqqfgfflad grlravprlv lvavvlaayg
      241 alvpittwlp ystsmlgnln pptlplvvlg vgqlallalv hplltaimrt rvaravvfli
      301 gsrlmtvylw hlpliiavag lqlalgipfa epltaawwwt rpvvllvvav llagvgallg
      361 rvehprrlrl dperkpaqaa vwialvsafi mpfaeishpl talmaaagaa gsiiavalln
      421 ptrrpvarvs sgsdqavdqr a
//
LOCUS       WP_285040485             246 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285040485
VERSION     WP_285040485.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..246
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27060
     Region          6..226
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mgversrpsi ywllssiaip pfsvlvklri rhgerlpqeg afilapnhds efdplimgaa
       61 vwrlgrqprf makgslfrvp vvgwllsrsg qipveregsa rgmdpvsaaa hlarrgqgvi
      121 vypegsltrd pglwpmrgrt gaarialthg lpiipaahwg tqevmprygk lrvfplrkrv
      181 dvaigepvdl safagrplds ktlneatevv mqaitalcee lrgaqapter wdpskhqqke
      241 tgrfes
//
LOCUS       WP_285040489             351 aa            linear   BCT 25-DEC-2024
DEFINITION  trypsin-like serine peptidase [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285040489
VERSION     WP_285040489.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..351
                     /product="trypsin-like serine peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=35804
     Region          132..329
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mivkqkrrap ataavlilaa lltgcsipvt gepvageagp vidvaggtdd tlrkdfdasp
       61 qevndywtdd kfggakapdl kpgedtltgd qatgvvvhps tgvgpdvdvk aiaptaagdp
      121 ypatglaaat qgrlyfsigg atyvcsasvv naptmdlvlt aghcvwdtyg kqlaeniifi
      181 padaangqtq pygqwagvst yvpdeftsea tsdasgatsg ngwaydfafi rlapnasgqk
      241 iqevtggqgi sfgtppegit vigypsaapf dgqsqrycas qaatkgysgy rvdclmtpgc
      301 sgggwltrld patgagyvts vtsrgdgswl egpvlgqral tlyndalaeg s
//
LOCUS       WP_285040557             333 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285040557
VERSION     WP_285040557.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..333
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34588
     Region          20..284
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
ORIGIN      
        1 mnglrlqssd lvdaitrpei gawveafvdf itdvfqpvfd viravfqgly dgvdtvlsgp
       61 pfwviilvaa ilaliargpv faigsavgll iivgveqwen amdslslvlv agliaivigi
      121 plgilaarsk vassiirpll dfmqttpafv ylipalilfr igvvpgivat ivfalapavr
      181 ltelgirnvd revveagnaf gasswrilrq iqlplampni magvnqviml slsmvviagm
      241 vgagglggdv vkslsridiq lgseaglsvv ilaifldrlt aslgagrkpg rrvkptpapg
      301 girpapasst tttdstshve psgkpapspa gsr
//
LOCUS       WP_285040591             260 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285040591
VERSION     WP_285040591.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 260)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..260
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28810
     Region          58..224
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mqrtttpaea datpvelavs tviftlrtdd gfgaddpapa iwlplvrrir epydgrwalp
       61 ggplgaaqsl adaaastlee ttslrpryle qlyafgdldr spaervvsiv ywalvgseea
      121 krthlgqnvr wfpadalppl afdhreivey alwrlrnkle yshiahaflg dtftltelre
      181 vheavlqkrl dpanfrrqve asglvlatde lrtggrhrpa rlyrwtqpia rpdtpaasrp
      241 asartsntpt tpratsqepa
//
LOCUS       WP_285040647             265 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285040647
VERSION     WP_285040647.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 265)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..265
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27519
     Region          1..249
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 matalvtggt sgigaafata laergfdlvl vardaqrlea saerlratgr tvevisadls
       61 dradvarlaa riedaaapid vvvnnagfgv harltdpdts eldnaievmc rsvavlsgaa
      121 aramrerggg tilnvsstag fittggysav kafvttytea lavelagtgv hvtalcpgwv
      181 rtefhdragi strsipsglw idvdrlvada lrdaargvvv sipslrfksl malvkfaprs
      241 sirwisgrms ssrraanaaq sgahr
//
LOCUS       WP_285040832             273 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285040832
VERSION     WP_285040832.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..273
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=28413
     Region          13..249
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mttietprst hvlrsegrtd tglvrrlned afyagapafv vadgmggher gevasrevaa
       61 alergipvgt pttteavvtt ivaanavirs iptpngvigt tvaglalval spqtdlhwmv
      121 fnvgdsrvyt wtdgvlrrit vdhsavqeli dagslteaea rehpdrnivt kaigveagid
      181 pdvwllpvag rqrfllcsdg ltgeltdagi aevlsqgfeg aadrlvelal aaggrdnvta
      241 lvvdvvstsl mssgpgydda gglgyleetm prg
//
LOCUS       WP_285040860             398 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285040860
VERSION     WP_285040860.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..398
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40960
     Region          1..382
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtrivvvgag ivgaacaril arrgaevvvl drsaaaggts gagegnllvs dkgpgpeldl
       61 aryasrlwpv itaeltdelg ptfpsvefer kggivvatte agaqplldfa asqrtagvda
      121 rplteaella aepsitrast aavhypedaq vqpviateal lasarlagav vrtgvtvtgg
      181 lrsatgrltg vrtsagdvsa dvvlvcagpw saevgavlga pvpvrprrgm vlvttrmphr
      241 vhhkvydgdy fgatqssdas lqtssvvest aagtvligss rqqigfdarl dvdvlrevag
      301 kslrlfpflr dasvmrsygg frpympdhlp vigpdhrvdg lwhatghega giglalatae
      361 liaarllgga aalddtpfql drqglvahlg vdraaeva
//
LOCUS       WP_285040926             202 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285040926
VERSION     WP_285040926.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12807001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..202
                     /product="helix-turn-helix domain-containing protein"
                     /calculated_mol_wt=21996
     Region          12..87
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          17..183
                     /region_name="PRK09943"
                     /note="HTH-type transcriptional regulator PuuR"
                     /db_xref="CDD:182158"
ORIGIN      
        1 mahgheeqrs idgvldavgp rlrairqhrg ttlaalsaet gisvstlsrl esgqrrpnle
       61 lllplakahq vplddlvgap qtgdprvhlk pvqrhgqtiv pltrrpgglh afksiihggp
      121 gpqtpgtqqv hegyewlyvl ngrlrlllgd qdlvltagev vefdtrvphw fgraeggave
      181 flslfgkqge rmhvrarste ar
//
LOCUS       WP_285040969             320 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285040969
VERSION     WP_285040969.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..320
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34493
     Region          61..317
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mpehddrqla rcpargritt trlsgaagmq easgairfvd vdpdrfsmti davalgdyvv
       61 hrnrvgpgtf dvldaagsee pvamivlltd gavslihgrq qldlhpggga lavseevyrt
      121 tvdehasylh vfvplralrr lgitptpfga lapspllrai aaffeevvsg fepiggaaql
      181 rlcrvidtml atlyaendlf qadadagrvp irlrimehia vsfaerelrp etlarrfnms
      241 trslqrvfeg sgtsaageia errlqlalal lsdpdhrtls iaevaarcgy hsqahlrrav
      301 vvhtgfsptq vreqstaggs
//
LOCUS       WP_285041014             124 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285041014
VERSION     WP_285041014.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..124
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13533
     Region          15..120
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mtsgtvqlgr rpgftdgilp aacpsrtvld hvtskwgvlv llalsdgthr wgelrrvvqg
       61 isekmlaqtl rtleedglvv rvahpeippr veyslsdrgr dlnehlmplm awidgnasei
      121 lgra
//
LOCUS       WP_285041044             322 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285041044
VERSION     WP_285041044.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..322
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33796
     Region          45..322
                     /region_name="COG4132"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443307"
ORIGIN      
        1 msasatrrsg agsaeadpav slpptttpga sadpvaarpr rrprwallgl tpfalytllf
       61 laiptvtala tgffdgegaf tldnltalge pavlgafass fwvsavtava gavigalvsy
      121 allavrpdgl irtfvdaass vlaqfggvml afafiatigi qglvtvflkd rlgidlfadg
      181 vwlyqvpgll lpylyfqvpl mvitfmpame glkrtwsean atlggtrlty wtriampila
      241 psflgsllll fanafssyat aaalisqgaq ivplqirgal isetvlgren lagslaigmi
      301 vvmvvmmtay salqarterw qr
//
LOCUS       WP_285041104             750 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-glucosidase [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285041104
VERSION     WP_285041104.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 750)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 750)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 750)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 750)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 750)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12807938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..750
                     /product="beta-glucosidase"
                     /EC_number="3.2.1.21"
                     /GO_function="GO:0008422 - beta-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0030245 - cellulose catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=80462
     Region          86..>378
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          89..694
                     /region_name="PRK15098"
                     /note="beta-glucosidase BglX"
                     /db_xref="CDD:185053"
ORIGIN      
        1 mgivtgrrna rpprqrragg spdpdaydev vrqirdgrid adtgaerlie rltdrellgl
       61 ldgdsprrll pliplllhrr pfvagavprl gipgirfsdg argvvigsst afpvtmaraa
      121 twdpeleeqv gtaigaetrv rganysasvc vnllrhpawg raqecygedp vltgrmgsam
      181 trgvrvhtma cvkhfalnsm ederfevdvs vddhalhevy lphfkavvda gadsvmsayn
      241 rvrgeymdvn rplltgvlre ewgftgfvts dwvfgthdav gslesgmdve mplrlrrahe
      301 lpaalregtl dratvlqsar rilrttllha atrapaeppa divagsahra lvrhvaeesi
      361 vllanapvdg tpllplpatt rwlavlgrla dqenlgdhgs srvrppstvs plqglrdalp
      421 qveittapsr dvraavaaaa aadtaivvvg fdqhdegesv vtggvdvgvl gaaldsgrlr
      481 gaitavahla srfvrggdrt slrlrpsder lilavtaanp rtvvvlvggs ailtetwrhr
      541 vpalvlawyg gmeggralad vltgvvepgg rlpfviptdp ahlppfdrta kavvyddrwg
      601 qrrlddegrt pafpfgfglg yttiehrllg hgfdasggta evrvtntggr egstvvqlya
      661 advararpvs qllgfrkvtl qageerivrv aldptptler dpfttrwsar pgdwmlqaaq
      721 hspddwsaav alrhdgavte ddvategaag
//
LOCUS       WP_285041157             126 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285041157
VERSION     WP_285041157.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 126)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 126)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 126)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..126
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13869
     Region          14..>76
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mvvqidagpe lstdevdrlf haladatrrd iltrvlareq svtalaeqye msfaavqkhv
       61 avleraalvm kerrgrqqiv hgdvttvqrs arlldayadv wnqralriga ilaedgpehg
      121 dtpntp
//
LOCUS       WP_285041241             342 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285041241
VERSION     WP_285041241.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..342
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=34247
     Region          2..338
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mfgrlwrgrv vvvtivclvv alafallgiv agsssltipd vittllgggt ggqelivfel
       61 rlprvvggll vgaalglaga ltqtfarnpl atpdilgvts gaalgavaai vlvggsysvg
      121 agalslglpa maaigalvts aavyalswrg gvdsfrlili gigatatlgg itsyliaraq
      181 iteaaaaaqw lvgslsgisw ssvwpvlval viltpiavlq tssldisqlg delstglgva
      241 vqrhriivia cavllvaaav saagpiefva fvapqlarri artgrpplla sallgavivt
      301 ggdalvrgvl pgeipvgiit aivgapyliw lltrrkeret sa
//
LOCUS       WP_285041258             288 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285041258
VERSION     WP_285041258.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..288
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30680
     Region          30..278
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          199..278
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtltlpavae sapdtldral aslewtihgt yrdrlaagsr ldrghpasgf lyvssgrarl
       61 ttpegaldld agdlvffpra httgllslgd aevlevglep srqrqavadt lpetltvrdf
      121 agqersmval iegmgcpgps grarpgdavi csriattivs aalrswneag caperwlqri
      181 gdphiaavld alhaepgrpw tfeslariam msrsafaerf rqvvghtpra ylttvrmeta
      241 kgliitggat iaelagelgy asedgfaraf qrytgltpar wraeaaaa
//
LOCUS       WP_285041289             309 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Lactobacillus crispatus].
ACCESSION   WP_285041289
VERSION     WP_285041289.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..309
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33721
     Region          1..296
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mvpaktrrlw tflaamaavm wgvsglfakg lfdispkitp mwltqirlii lgavlliasg
       61 flkqkpiatl knkhnvlvii aygifgllpv qlfyfmciqv anasiatilq figpffvlgy
      121 laithkqvmr rldiiaalca flgvfllsth gqfnhlaitp valfwgvlsa fgeaaytlip
      181 vnivkkvssm vvtgwgmifa gislliidpq fhavpnkpev wlytaavivi gtiipfqima
      241 nalryvipst vslldafepf satvgsvlff glvmmpmdwv gsvlvvvaam alnltpkqkk
      301 nkinqktkq
//
LOCUS       WP_285041294             344 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285041294
VERSION     WP_285041294.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..344
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37457
     Region          3..320
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mwdttsrtfr llellqrngf materladrl gvttrtvrrd varlrdlgyp vdtrlgvdgg
       61 ysiepgavlp pihltteeal acalalrrwq ddvdgtlaas sltkvvaslp prarwivdav
      121 aavtldtpvd alepidhptv ditllgdlar tclvrrrvgf aytgrdgtst prrvdphrlv
      181 ntarrwylva fdldadawrt frvdritgfa atelpvrerl lpnpdvegwv trqltvgwqq
      241 vtgtvrvhap ieavsrwvap awgsveavsp evtvvragad shdaiarwll lvqadvevie
      301 pdglraafgr vaeqagraae snpadppsdg paqetdpppv sgav
//
LOCUS       WP_285041324             405 aa            linear   BCT 25-DEC-2024
DEFINITION  fatty acid desaturase family protein [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285041324
VERSION     WP_285041324.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..405
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44443
     Region          50..391
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mprehhahap irlvlhapsa iidlddtarp pggagpvtve rssgfrktgp sstpraggts
       61 sysailaqvk sagllrrrya fywtlfavlv latagcwvaf allgaswwql lvaaalgvlf
      121 tqfaflshea ahrqvfesra wndlagrflg tflvglsysw wmnkhtrhhg npntvgkdpd
      181 iepdtirflp edvsavhnra aklfyrhqgw lffplltleg lnlhwlairs vvsgvgtrgg
      241 grdraiegal llarfglllg vvftflpfgm acaflgvqfa vfgvmmgasf apnhkgmpti
      301 ahdanvdffs rqvrtsrnvt gglwvsflmg glnyqvehhl fpsmprpalk earrlvrdhc
      361 aaldvpytet tllrscgivi rylnrvglga rdpfacplva elrih
//
LOCUS       WP_285041328             692 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285041328
VERSION     WP_285041328.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..692
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=72442
     Region          57..411
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mnvsrrgpag hptqtatrsr grtsvvlala aliaivcgpl aaagtaagme paaptgtgta
       61 aaplspedtt awldgllpaa leregitgav vsvvsggeiv akrgyglasa gsatseptpv
      121 dvdrtlfrig svsklmtata vmqqveagvi dldepvqsyl dvtlpvafdt pitlrhllth
      181 tagfedqlag liasapaepk plretvaidp peqifepgtt psysnysngl aayvvervtg
      241 tpfeqyateh vleasgmtga tyeqplsper rrdmsagyrf agspevpfev vspapagais
      301 atagdlanfm naqlghpsad grtlltpesl ermhapalde ehlgnlangp rmtlgfferd
      361 rnghrilsha gdltafhaql eiypnddagi fislnstgvn gdsstairda vttgfadryf
      421 peersaprve etaaahaaal agtyqlsrrg estfvrlfyv lssvevaaeq dgvvtisait
      481 dsagtplrfv evepwvwqev dgqrrvaast dgdtvtavgf dpaftmqpmp teralvptia
      541 agsllilvit llawplgalr ragtprpips drrdralrww trgsvlalva aapfwsvvaq
      601 alisdgpaps svvirvaqvl talavlgcip svwrairaar gtepepstsd grprrrvata
      661 arvtgsglta lafvglgfva vvgglllpdl sy
//
LOCUS       WP_285041353             409 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285041353
VERSION     WP_285041353.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Erzberger,J.P. and Berger,J.M.
  TITLE     Evolutionary relationships and structural mechanisms of AAA+
            proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 35, 93-114 (2006)
   PUBMED   16689629
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..409
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42797
     Region          58..377
                     /region_name="RPT1"
                     /note="ATP-dependent 26S proteasome regulatory subunit
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1222"
                     /db_xref="CDD:440835"
ORIGIN      
        1 mtqdgdflev iaaevaqdpq naalredfvt lllqhdvdra aeevstferf ggdparvrll
       61 rarvmaarlr ggttggapae tpggdptass stpnrptavp nastpdqapv rigqpslwda
      121 erpaitladv agladvkqhl dstflaplrn pelaaafgqk pggsllmygp pgcgktfiak
      181 aiagdlgasf ihvtladlls kwlgdsekai qsvfhdaraa apcviffdef dalggrrtsg
      241 ggsqsmrtiv tqlleeldgv anendgvyfl aatnrpwdid palrrpgrid ktvlvlppda
      301 varaailqgd legkpaegvd viavaaateg fsgadiaqvs rvalqrslta smeagaivsv
      361 tteglleaaa glipstaswf dqvapvleyg vddgtfaqlr tyrvqhglr
//
LOCUS       WP_285041411             335 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285041411
VERSION     WP_285041411.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..335
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33833
     Region          21..332
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 miagvlvlag vllllisvga aitlgpadil lvnvrdivtn hlgvtdipvk lskdaivwee
       61 rlprafvaaa cgaglglcgv imqsllrnpl adpfilgiss gastgavaig ilglggasig
      121 lsggafigal vafglvllla rlsgggtdrv vlagvastql fsaltslvif afadsdetrg
      181 vmfwllgsle gvrwddvilc aivvvagsll clryahalda fafgedvaas lgihvgrtra
      241 vllvatalit atlvsvagai gfvglvlpha arllvgprhg rlipataiig aifmvwvdag
      301 srvafsptpl pvgvgtalvg vpvfiallar rrkrg
//
LOCUS       WP_285041441             470 aa            linear   BCT 25-DEC-2024
DEFINITION  FGGY-family carbohydrate kinase [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285041441
VERSION     WP_285041441.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..470
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48943
     Region          20..456
                     /region_name="ASKHA_NBD_FGGY_FK"
                     /note="nucleotide-binding domain (NBD) of L-fuculokinase
                     (FK) and similar proteins; cd07773"
                     /db_xref="CDD:466793"
ORIGIN      
        1 mhpaanldpt avasvapdgl vagldlgstg vkilvtdtdg aevlihqlpt pwlagaggtt
       61 vmeaasliat vrelldhvaa eladrfgpav rvralavsgm gesgivldav grpvapaiaw
      121 fdprgaeqla alpatiaeqf agrtglplgv qvsvvkllhl rdagldlagt rwlnlpeylv
      181 aalggeeaae yslssrtgll dqdtgapwpe llehlgvdat flppfvdagt plgsaaapwv
      241 pevfadaalt vaghdhlvsa vstgsfpaer yhvsmgtaev llrrldaplp faarerlaev
      301 fincvrhvvp gtwvlvagvk tgllmrrtlq lvgvtersgr drlddavmel pvegrladgd
      361 ivvsgarndd gvlhltvrad gadpaeifaa vlrhgndelr vlieamdrev ppassalltg
      421 gwagmrsvqr araavlpgiq vsdrsqdtay gatvfarsll epavsgrarp
//
LOCUS       WP_285041589             395 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285041589
VERSION     WP_285041589.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..395
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42607
     Region          11..393
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mtddtfdsgf platsswdaa eyaaiqrvvd sgrftmgplv aqferdfasa fgagfgvmvn
       61 sgssanllai aaavldervd lqagdevlvp avswattyyp lqqyglipsf vdidvdtlnm
      121 dlalaeasit prtkaifavn llgnpndfaa ltalaerhgl lliedncesl gakddgrfag
      181 tvgsmgtfsa ffshhistme ggmiltddea taqmlislra hgwtrglpeh navhdksgde
      241 wddlfrfvlp gynvrplems gaigieqiqk vpsliagrre naaywterfa dldsvriqre
      301 qgesswfgfs lvlegslagr rselvrafaa agiesrpiva gnftknpvmk yldakvpael
      361 paadkihddg lfvgnhhfpv hagidrvydt vakls
//
LOCUS       WP_285041643             329 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285041643
VERSION     WP_285041643.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..329
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35349
     Region          22..316
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtdapaprtt tpspddlrra laqvrvevgk avvgqdaavt glviallakg hallegvpgv
       61 aktllvrsls halsldtkrv qftpdlmpgd vtgslvydak tgefefregp vftnillade
      121 inrtppktqs alleameerq vsvdgrslpl pdpfivaatq npieyegtyt lpeaqldrfl
      181 lklvldvper dvevevlrrh aagfsprdla aagvtpvmga aelraaqvev grvgasadvl
      241 ayvvdlarat rrspsvrlgv sprgttalla sakawawlsg yqsitpdhvq tmvlpvwrhr
      301 mqlrpeaele gvsvdailrs imqqvqvpi
//
LOCUS       WP_285041724             572 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285041724
VERSION     WP_285041724.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..572
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=61396
     Region          17..559
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mnqpilqhsa lhvvdtasap llvdglavgy rtrgsrlpad tvrqvsfqvg hgetvslvgq
       61 sgsgkstiar avagllpvng sitagrvava ghevadfsrk qwrplrgstl gfipqdplss
      121 ldplqrigvq iaqavqvtgd tprsavparv iellehvgir qaasrvrsyp helsggqlqr
      181 vliaiaiaar pklliadept saldvtvqrr ildlldglre elglgilfit hdlalaqers
      241 daivvlqdgn vresgpaeev lltprdpyti qllsdspass plryrerira aaeqvqaeqr
      301 gdtgtaapvv evshvskrfg reprtppald gaslvlrprs ihalvgesgs gkstlariva
      361 gltsfddgsv rvagrelpre havanpfard lqlvaqnpls avdprytvgq iieeplrihg
      421 vrsaverrrr vatildqvgl pasvlgrrar evsggqrqrv alartlilap svlvldepts
      481 aldvsvqaqi vellldlrde halsyvfish dlglirqiad evtvlsegrv vesgpssavl
      541 drpqhaytre lldavprfdv erldpsrfea vg
//
LOCUS       WP_285041758             222 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285041758
VERSION     WP_285041758.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..222
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=23632
     Region          4..184
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 msrpsrhpqp tvrlltwara deldldgtad rldarardrl easseaearr flfgrallvr
       61 tvaettgada pqitvtarcp dcglahgrpq vlvdggivha svshtdnasa vavsvthaag
      121 vdverldaar fagvenvals ptererwrrl parrrlrsla ehwtakeavt kalgtglttd
      181 patielagha gvtvaeiagr rfvvdhpvla pdtvmatall la
//
LOCUS       WP_285041840             265 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285041840
VERSION     WP_285041840.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..265
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28565
     Region          29..244
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 madeeqtqrr aressqgrpa vtpeptskpg lvyyvgravl nttakllyrp kiigrknvpk
       61 rgpvilasnh lsfidsiaip isaprrvqfl aksdyftgrg lkgwvsrtff tsigavgver
      121 gvgqaaqeal dqgrrilegg dafaiypegt rsldgrlyrg rtgvawlalt tgatvvpvgl
      181 igtdelmpvg ttipkfkpvt vifgepldls hhgaaesgra rrkatdeims aihaltgqel
      241 anaynesppa daverikral rperl
//
LOCUS       WP_285041864             332 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285041864
VERSION     WP_285041864.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..332
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=36107
     Region          37..289
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 meliywwmpl vwllavaavv avavlatrag rrrkanqepl wvahserlta lpgyrraltr
       61 yrrlvvatia avavlllagt algsrvvstt vfqpelrnrd ivlcldvsgs mteydaalvg
      121 vfeslvqrfd gerialvlfn asattyfplt sdydyvttql dhlvedltsp esdyeywngt
      181 dlgngsslig dglgscvmrf dqvgeqrsrs ivlatdnyva gepiltlkea geyakaqdvt
      241 vyginpgdvs skdylddlaa emdevvtstg gdyyaladpa avggivqqit aeqtktlkga
      301 kqlvqvdepl vfvlaafggl allmllawrl rr
//
LOCUS       WP_285041980             455 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285041980
VERSION     WP_285041980.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..455
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48287
     Region          12..445
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mnaavdfplt rpelaftasg dalvrrtvlp nglriltehm pgsrsatigf wvavgsrdeq
       61 patadrpatf gsthflehll fkgtakrsal diaiafdavg gehnaltake htcyyakvrd
      121 rdlpmavdvi tdmltsslld peefenergv ileelammdd dpgdvanerf fegvlgehpl
      181 grpiggrpqs iievgrdavl ahyranyran dvvvtaagav dhdalvaqvs aalveagwpa
      241 davaapvprr tlaaasvlgg pplsvvhrpt eqvhlqiggp gliagderrf amsmlnsvlg
      301 ggmssrlfqe irerrglays vysfagsysd agvfglaaac stakaatvae lmlaelhrla
      361 ehgvtddels ralgqlsgas alaledsdsr msrlgraelt lgefidldes irrlqlvgqd
      421 evqqlaqhla aqpitvsavg avdedtfapi iagvr
//
LOCUS       WP_285042051             501 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285042051
VERSION     WP_285042051.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..501
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53875
     Region          1..317
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mslqrstpsa qhvdasgiea fidalehlpn vephsfmllr sgqvvaegww apysaervhl
       61 lyslsksfts tavgfaveeg llslddtvis hfpeldaevt dprsramlvr hvlamasghr
      121 eetimraaai dptnlvrgfl llppdedpgt vfaynqpcty taaaiiqrit ggtltdylrp
      181 rlldplgigd fdwqrddqgf elgysglhar teaiaslgql ylqrgvwegq qllpeawvae
      241 atrshiangd dpesdwaqgy gfqfwiarhg frgdgaygqy cvvlpehdvv lavtgqsldm
      301 qavlnaaweh llpafgrgde tssedgasad adqallerla glalppvgvs gdqgvpdaep
      361 gaseasfrel vgwtfaadpg salpqltale vvsgdgdqvl lvvhegddrv eivpgfgewr
      421 thgpvvasaa wgaddesgag gvgvlrvevi fvetphrmhl vvdpaagtfd awwettplrt
      481 srlaevrrps evvdgsgssa w
//
LOCUS       WP_285042062             198 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285042062
VERSION     WP_285042062.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..198
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=20885
     Region          1..196
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(25..26,28..29,32..33,71,75..76,79..80,92,96,103,
                     106..107,112,135,139..140,142..144,146..147,150..151,
                     154..155,171,173..175,177..179,181..182,184..185,189,
                     192..193)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(159..166,172,175..176,179)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mitlyrpgtg wlhrapagpk algillvvla isllptswwt agiaaavtvl aylvsglglp
       61 elgrqlvlir wiititvvgq llfvdlesal sntarivaai llaallvlst rvadlldafe
      121 ralrplgrfg vdparialml avaintipvl arlaagvrda qrargvrsnp vtfvvpflvv
      181 slkhadelgd altargvr
//
LOCUS       WP_285042127             104 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285042127
VERSION     WP_285042127.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 104)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 104)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..104
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11395
     Region          11..>77
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mpaaadlahp dreaielpav lfalsdpdrl emvrqlrdgp mdaanctald ptipkstksh
       61 lmkvlreagi irnepngrrr tltlrrddld trfpglldav ldad
//
LOCUS       WP_285042142             266 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Plantibacter
            sp. LMC-P-059a].
ACCESSION   WP_285042142
VERSION     WP_285042142.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..266
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28144
     Region          5..264
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 msapsvqlyt vrdaiaedlq gavariaeig ftkvepyafv eraaefetaf aavgvsapsg
       61 hapvidaadp avafdaasrl gigtvidpfi ptdrwqtadd aarlaervne lavqaaasgl
      121 kfgyhnhnwe fsthvdgrpi felfveqlsp evvleidtfw stvggadtpa flrslgdrvq
      181 flhikdgiis gdiatalpss esalvvpdal aqafanqqpa gqgqvdipai laaaphatrv
      241 vefdgyskei fggvaesfaw laehdk
//
LOCUS       WP_285042176             450 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285042176
VERSION     WP_285042176.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..450
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46995
     Region          3..426
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 marmahaddf alsrvrpdaq kpwfgiavqr fgqvsalsqf llgatlgysm tfgeaflall
       61 lgsiilevim civgiigqke glntallarw tgfgevgasl vglaigisli gwfgiqsais
      121 aesldallpg fmpvwawsli fglavtaiva ygfkgmqwla nitvplflil vgwsiiselt
      181 khdfmelvtg papgptmsvw agtgivaggl ivgaiitadm trfnrsradv ikqtvvgvsl
      241 gefviglsgv llahaaasgn vvaivtssvg ligliivitg tlkindwnly sstlglvnfi
      301 stafgknlnr vtttivlgvv gsilaavgil gqfsgfliil gvafppiagi mvaeyfivkr
      361 wrgeldetra sgrlpttapr ivpatiiiwa vsaitgyfvt wgipavlsli lsmvlyiaag
      421 klgwvrgvgv ahtsqiaadv ptdspanasn
//
LOCUS       WP_285042210             214 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285042210
VERSION     WP_285042210.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..214
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22527
     Region          <31..145
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mtsahepalt dpaefwedry rsrgqvwsgr pnaalereva dlhpgtalel gsgegadavw
       61 laqqgwsvta vdisptalal grstaeaagv adriawiead laawepsggf dlvtatflhs
      121 pvafpreevl rraaaavapg gtllvvghag pppwatehia hahfptpdev rtsleleagd
      181 wevviaalvp raaagpdgep aelddsvlhl rrrp
//
LOCUS       WP_285042275             416 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285042275
VERSION     WP_285042275.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..416
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=44072
     Region          37..374
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mtstadrepp pdpslevatp radltafaga ralaawwvvf shsadwlfsv lpelswlapl
       61 ahtglavdvf fvlsgysiaq aygarrwtwr sygrylrnrl arlypahvav lltflalclg
      121 galvgidsep gafppvgila eltltrawfg dalwwnppaw slsaqflafl lfpvmalair
      181 grsrrrstta llvlagatia vstlmaglap samngmappv vrvlcgfalg vcvaqltsrl
      241 patvhaawva aggglgllia avvlepgapr awaaitfaai vvgglavasp rttaalrsrp
      301 aqvlgrlsfs tylvhvfvli llaktitpaa vgafplllra ivllvwfgsi lgaswllhtl
      361 veapahrkla aprrdhdgnl erpsggqrsv rrsdegadas qpgrhrrlae gdgarh
//
LOCUS       WP_285042182             336 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285042182
VERSION     WP_285042182.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..336
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=35706
     Region          15..334
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mttpdstttp sdttatktaa viynpvkvdl dalresvdrs aadagwgesl wfetsvddvg
       61 qgvtaeaiaa kvdlviaagg dgtvravsea lrgsgiplal lpsgtgnlla rnldltlndl
      121 pgsvitaftg ddkpidlgvi dieradhsrd rhvfvvmagm gidakmiknt dddlkakagw
      181 aayvdaivks lrdpdelhlr friddepqir atvhtviign cgslpanill lpdavvddgl
      241 fdlmfmrpgg vlgwiriwak vawvngvlrr tktgralagk qkddgelryg takrfvarms
      301 kpeeieldgd gfgkavaint wiepgaltvr vpaaae
//
LOCUS       WP_285042559             141 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285042559
VERSION     WP_285042559.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..141
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15480
     Region          13..112
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mtsnppvwnv mldtcpsrts lariankwta mivialsegp arfgtvrqav ggisgkvlas
       61 tlrdlerdgi ltrtaydemp prveyeltpl gqtlreplma lglwaeqhie evlgardafd
      121 drradetgst peseklprrg f
//
LOCUS       WP_285042594             305 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285042594
VERSION     WP_285042594.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..305
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31334
     Region          9..295
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(37,240,243)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(180,211,238,241..242,245)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mhttpttdvl iagetlidiv rrldgtqaes pggspanvgi tlgrlgripa lvthvgdder
       61 gaairswlda sgvslvsapt grtstaqatl dadgaatyef dlsldldatd apdapvvhtg
      121 siatvlepsa srlralvear rdaalitydp nirptlvdda ervrrtalec iarahvvkas
      181 dedvaflhpd lalvdaakqw vssgpglvvv trggdgalvv ragsvfeiat prvtvadtvg
      241 agdtfmgali dglltagvsg paaeerlgai sdhdlrrlle raaraasvtv srpganpptl
      301 aelda
//
LOCUS       WP_285042629             342 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285042629
VERSION     WP_285042629.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..342
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35007
     Region          1..342
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mtaireraad alrtrnrpap rllivcgaal llivvaaiag lalgdyplsa eevlgvlsgr
       61 vdglartvvl ewrlprvlaa igfgaalals gaifqtltrn plaspdiigl angsftgmlv
      121 allllgggwp almagsligg laaavaifll alrqglsgfr fivvgigvsa mlaafnswll
      181 lradldvalf aaawgagtln tatatvvwpa lgcllvlfal lplvarplrq lelgddvaaa
      241 tgvrltrera iligmavalv savtavagpi afialaapqi arrltrspgi plvatalvgg
      301 vlllgsdlva qhlipltvpv gvvtvviggl yltqlllrer rr
//
LOCUS       WP_285042630             361 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285042630
VERSION     WP_285042630.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..361
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35797
     Region          57..356
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtddvvsgai ataepagrap vdarpgvrsp hrrhralpll aglgalalav vlsllvganp
       61 ispdavwsal tgagssearf vvwdqrvprt vaalavgasl gvagalmqaf trnpladpgi
      121 lgvnagagfa vaaglaflgv tapgeiawla cggalvvtlv vytigsggre rssaarltvt
      181 gvafgavlag lttgiaithp dafdrmrgwn agsllerdlg vvvpvlpfla aglvlaaast
      241 rslnaialgp dvaraqgvsv grsrvlvlaa vtllaggata iagpiafvgl vvphlvrwtv
      301 gsdqrrilag svvvgcvlvl csdvvgriav lpgempvglv tafvgapali alarrrtasg
      361 l
//
LOCUS       WP_285042653             351 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285042653
VERSION     WP_285042653.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..351
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37234
     Region          18..336
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 msdarpgpde ddrrrkharl velldaqaar aivlrsaaav swyldgarvh vslaadpiva
       61 vvvshddawl vatsneaerl qaeelpdirv ttvpwhtpid tvlpsgagvl resdvpaelr
      121 aarasllpae lerfrslgre ttaeletlig rldpswtera vaadlasrlv aagidplvll
      181 vagtdrlahr hplptdgplg sramvvacgr rdglivnltr wfdeggaape pfatdmrrir
      241 averayldat vpgatladvf ragtaayaaq gfgpeewtrh hqggaagyag rdpratpdtt
      301 dvvqpwqafa wnptapgvkv edtvvvtpdg vevltdagag stavepplva g
//
LOCUS       WP_285042665             326 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Plantibacter
            sp. LMC-P-059a].
ACCESSION   WP_285042665
VERSION     WP_285042665.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..326
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34048
     Region          43..312
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 msstalrqaq gpegqaqgpe gqaqepegqa qgavggstap hprlsinqat ikyatlpeav
       61 savaaagvts fgawrepvqe fgvaasarll aeaglrvssl crggfftmpe gphrrasidd
      121 nrtavdeaaa lgapalvlvv gglpegsrdi vgarelvrda igeladhale sgvqlaiepl
      181 hpmyasdrav istlgqaldi aeqfapeavg vvvdtfhlww dplvleqiar agatgrissy
      241 qacdwatplp advllarhyp gdgvvdfasl traveaagyt gdvevelfnq eiwdapfdav
      301 vrrtvetfqs avvphldptd aadlhp
//
LOCUS       WP_285042695             248 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Plantibacter
            sp. LMC-P-059a].
ACCESSION   WP_285042695
VERSION     WP_285042695.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..248
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26053
     Region          6..241
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mstshlsvql ysvreplsad raaalqrlte igfrqaepfg fgpgvslqdi hdaglvtpsa
       61 hgkviddgid lsavfgaaae qqvgvlidpa iaverfatad svasiaddln aaaqvaaghg
      121 vqvgyhnhww elegdvagts plehlaaitd pavvfevdty wvevggrrav dvlasigdrv
      181 rfihvkdgda srdtmkqlpa gagvvpvldi idaapqalrv vefdafdgdi fqgleqsfty
      241 lttngvqa
//
LOCUS       WP_285042700             177 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285042700
VERSION     WP_285042700.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..177
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18878
     Region          86..174
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mvstrpatad daatlatlaa atfglacppg ttqadidafi aehftlehfe eylrspdrav
       61 rllladdgta vgytmlvfge ptdpdviavi thrptvelsk lyvladghgg gvarvlmeat
      121 lddalqhgas svwlgvnqqn arairfyeks gftvagrktf lvgserhddf vmervsg
//
LOCUS       WP_285042750             202 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285042750
VERSION     WP_285042750.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..202
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20902
     Region          56..198
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mvrrsrtfav aavlavgall ltacgsdpla dqyregsskg yvagdgsvte vavddrgeai
       61 tfsgvgedge qiassdyagq vivvnfwyaa capcraeakd leslnadytg kgatfigvnv
      121 rdtadtakaf ngtfgityps ildvdsgeak laftgnvppn avpttivlda egrvaarilg
      181 qlqdrtildt lirdtiaess ae
//
LOCUS       WP_285042837             268 aa            linear   BCT 25-DEC-2024
DEFINITION  MerR family transcriptional regulator [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285042837
VERSION     WP_285042837.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10248988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..268
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29167
     Region          11..113
                     /region_name="HTH_MerR-SF"
                     /note="Helix-Turn-Helix DNA binding domain of
                     transcription regulators from the MerR superfamily;
                     cl02600"
                     /db_xref="CDD:470628"
     Site            order(12..14,28,45..47)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133381"
     Region          140..254
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 mdergategg mtvgrvsaei gvsvrtlhhw dglgvaqpsg rtssgyrsyl pvdvarlrrv
       61 lllrdlgvpl ariptlltap aaerraeltq rrrdladtia rledvarsvd rlleadevgv
      121 lvpedqhhav fgddwnptma esararwgds aqwaeyaers aertpedwra vvgplrdlvd
      181 elaeakragv dagsvaanal aerhraalse yfhctpamhv itgrlaltep gmadtydrve
      241 pglaawlssl idanarthgv dpetavwe
//
LOCUS       WP_285042937             744 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285042937
VERSION     WP_285042937.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 744)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 744)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 744)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..744
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=82229
     Region          2..742
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mqndaiaeeq dhldrlhdvi rtqsdleerr selalrafdg dddssfserd alvahhrqrm
       61 velrsssygl lfgllerete erhhigrigl rdpesgdqll ldwrapasrp fytatplrpe
      121 glrlrrrigt agrrvtevhd evldttllse depsgigesg allaalgrar tkhmadivdt
      181 iqaeqdaiir aplpgtllvq ggpgtgktav alhraaylly ehrerlmrsv vlivgpnstf
      241 ldyisrvlps lgetavvlvt patlvpglda haedsldvae lkgqlrmadv varavrerqv
      301 pldeavtiri agdgplrvtp gvlrrikagi ersgtphnea klrfdravlt hligleakrd
      361 gfeprtgeda derrqelsee peveelldtm wpilepaeiv drlftdaell arvtpdhtde
      421 errlllrapa dpsaagetaw adrltpgdia lvdeaaelig edqrpelerq rraayerrhd
      481 veyarsvlem igdisiddea qdddylrsaq dladrqtied drspadraas drtwvyghvi
      541 ideaqeltpm llrailrrgp nrsmtlvgdi nqqstsatrs swqellgpql prwtqelltv
      601 nyrtpeqime ladpvrleld pespapvsir rgeeepvqlt vgpdelaata vraaieaita
      661 hvgiagviap rplladidal ladagadrsr vwsgtaresk glefdsvvlv qpeqlggsgr
      721 salslryval tratqrltvv dtps
//
LOCUS       WP_285042945             322 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285042945
VERSION     WP_285042945.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..322
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34142
     Region          3..322
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mptpphaalv ynpvkvdatr lrsalearsq eagwaaphly etsvedpgvg qarravldga
       61 rvvlvaggdg tvravaeglr gsgvpltlip sgtgnllarn lklplgdqaa aiataftget
      121 raidigvami trpdgseeeh afvvmagmgi dammistanp dlkkslgwla yvesglrsii
      181 taapfrihyq lrghrqhaat vssvlvgncg tlqggvqlmp daelddgfld vavlqpkgaf
      241 gwllvwrkvt wenrvlrrta vgrrmirfte grgantvtnl raealtlrve eaqdleldgd
      301 afgmatmvaf dahrggllvt lp
//
LOCUS       WP_285042963             289 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285042963
VERSION     WP_285042963.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..289
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=32398
     Region          22..289
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mslaaaapdg pplwtpdgpd lvlegdnldv vaqlpdeaft liyldppfnt grvqrrhsst
       61 svrtaetgvn rfagfkgqay erirgdlrrf ddafddywgf leprlveawr vlaadgtlyl
      121 hldyreahya kvlldalfgr ecflneiiwa ydygakaqsr wptkhdtilv yvkdpkgyhf
      181 dnatvdrepy mapglvtaek aargklptdv wwhtivsptg rektgyptqk pegilrrivq
      241 assregdwvl dffagsgttg avakalgrry vlvdenpqal eiirarlar
//
LOCUS       WP_285042997             287 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Plantibacter
            sp. LMC-P-059a].
ACCESSION   WP_285042997
VERSION     WP_285042997.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..287
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30377
     Region          2..281
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mriavtgssg klgsatverl rrdghtvhgl dlagaagpgf trvdltdygq tidsllgvta
       61 rfsgldavvh laaipvnglv pdaatfhnnl tvsfnvlhga lragirtivt assitamgfp
      121 feeapellpi detvsrannt yalgkvaeea maaqlvrwae gtsitalrft nvvapgeygt
      181 farasepgyr rdllfsyvda rdgaqavala lagaepgfev ydvcasdtgt tvpsaelaat
      241 hfpgvplreg lgefetlmsi dkararlgye pehlwrdefe reqmarg
//
LOCUS       WP_285043012             486 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285043012
VERSION     WP_285043012.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 486)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 486)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 486)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..486
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50803
     Region          134..478
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mtggpggder ggrarggrgr hhgirtriag gslliavvvs lfaglainaq lerivrdgtv
       61 qalrsdgaqy vfalqarpdd plqgpglgtr iaviapdgsi pvfslpttla gqlpalaatr
      121 evtivdagra tyvllsqpvt vggdtwyvia grdeaeettv lvqmrlllvg sfallvlgva
      181 aggwilttvs lrpvtrlrvs aqrlsgrsta ellpvgradd eiaqlaitln dlierlrasa
      241 drerqlvsda shelrtplai lrtqlelarl edssreqlla diegaersat rlsalvtsll
      301 elsrieadap vgrstaaald aealeavera rfrvasddtl agvevevvsa ladrapdtaa
      361 ayavraddfg rlvdnllgna lqafadrgta prrvsvlldd agdlltlrvs dtaggldpaf
      421 epralerfsr sdatrssghg sglglaivaa iarnaggaiq llnrpghgle vvvtlpiaqv
      481 lptdpv
//
LOCUS       WP_285043040             332 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285043040
VERSION     WP_285043040.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..332
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=36086
     Region          42..313
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 msavapsiqq aprpsappla vvpsegatts tsvrtvyrpt gpldvhatlr lisrggdgpc
       61 yrktpggvwl tartpqggat lyvstmrdge veatawgpgs ewmidgvpel lgrdddwsgl
      121 dvsrspllte vlrrnpgmrl srnrlvfeml vpsimeqkvt ameawrawrq lvrrhgepap
      181 gpapegmiva paadtwrmip swewheagvg pqrsetvvrs srlasaiert vdehpddasr
      241 rlrslpgigv wtaaevtlra hgdpdavsvg dyhlaasvgq altgapvddd gmlellspwn
      301 gqrqrvlrli grsgihkprr gpkitiqdhr rh
//
LOCUS       WP_285043067             143 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285043067
VERSION     WP_285043067.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 143)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..143
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15013
     Region          15..136
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 msdptgggrg pladilvsav aivrdrrvlm vtargrdvly mpggkidage tpaeaavrea
       61 reeiaveldp asvtplftvl tqahgepdgr lvrmhvfaae tdavpqpsae vsavhwvgte
      121 sldrcppagr evlerlaalg rid
//
LOCUS       WP_285043099             432 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285043099
VERSION     WP_285043099.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..432
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44453
     Region          37..389
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtatasrrrr laafftaatl atvlvgcsgp svsdtdfpdq vsgalagdtt daitaavesa
       61 vaqsgssgai vgvwapwags ytagvgttep ggktkmdpsm vyriadttrp mtctvllelv
      121 degkikltdq vkktlpqiqg idgitfqqlc qgtsglgtyt palnaqfvtn ptrnwsmaei
      181 langlasgsr tapgalfgss dtgyillgma leeltgqswq slydhyvfsp lgmskssfpd
      241 aatvtlpgsh pkgyltpria dgtfqcdtpt detelspsmv wtaggvvssv ddlrkftqsf
      301 asgsllndst ykkqwkdpva lgddqptwkt fgvggvqlgp lrgqagsmpg slsaafadpt
      361 sgltvvvmln nstlgagfvq alamqlasig akaapasgqk apeialpwse qqmaeqlaas
      421 amvcappvap ag
//
LOCUS       WP_285043136             727 aa            linear   BCT 25-DEC-2024
DEFINITION  RecQ family ATP-dependent DNA helicase [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285043136
VERSION     WP_285043136.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Larsen,N.B. and Hickson,I.D.
  TITLE     RecQ Helicases: Conserved Guardians of Genomic Integrity
  JOURNAL   Adv Exp Med Biol 767, 161-184 (2013)
   PUBMED   23161011
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Rezazadeh,S.
  TITLE     RecQ helicases; at the crossroad of genome replication, repair, and
            recombination
  JOURNAL   Mol Biol Rep 39 (4), 4527-4543 (2012)
   PUBMED   21947842
REFERENCE   3  (residues 1 to 727)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 727)
  AUTHORS   Bernstein,K.A., Gangloff,S. and Rothstein,R.
  TITLE     The RecQ DNA helicases in DNA repair
  JOURNAL   Annu Rev Genet 44, 393-417 (2010)
   PUBMED   21047263
REFERENCE   5  (residues 1 to 727)
  AUTHORS   Chu,W.K. and Hickson,I.D.
  TITLE     RecQ helicases: multifunctional genome caretakers
  JOURNAL   Nat Rev Cancer 9 (9), 644-654 (2009)
   PUBMED   19657341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..727
                     /product="RecQ family ATP-dependent DNA helicase"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0043138 - 3'-5' DNA helicase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=77503
     Region          36..584
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
ORIGIN      
        1 msdvsapalt hheaattgsv aeataalaal tgvpgarfhd gqleailalv dehrrtlvvq
       61 rtgwgksavy fiatallrrr gagptllvsp llalmrdqva aaaragvrav ainsanahew
      121 ddvraqldad evdvllvspe rlnnprfrde qlptlvartg mlvvdeahci sdwghdfrpd
      181 yrrlaeligr lpvevpvlat tatanarvvr diaeqltapa asgstaaevl tirgslaras
      241 lrlgvlrlpe srdrltwlls hldgltgsgi iytltvsaae dtarllreag hevraytgrt
      301 dpdereeser llkenrlkal vatsalgmgf dkpdlgfvvh lgapsspvay yqqvgragra
      361 tehadvlllp gaedeeiwqy fatasmpdea ratavldald drprstpale alvnlrrtpl
      421 elllkvldvd gavqrvaggw vstgepwvyd reryrriaea rvaeqqamla yergeecrml
      481 vlqrelddat aepcgrcdrc agawfpteld saaaasasea lgrvgvelep raqwptgagk
      541 lgvtsdgapv sgrisledrl epgralarlt dlgwggvlre lfaagatdap asravidasv
      601 rvlanwpwak rpaavvsvps rsrpqlvdsv argiaslgrl pylgeldlvg dgprggpggn
      661 sayrlagvwd afsvgaelra qlatlegapv llvddradsr wtltvagral rlagsgpvlp
      721 falgivg
//
LOCUS       WP_285043289             419 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285043289
VERSION     WP_285043289.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..419
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45288
     Region          164..414
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mngqrhagrr rgpgsrtggl gstisevrrr rspvtdavli aggataavga lglaivatia
       61 rkvvvpardr psearilald reagtlelva tpdtvvpgry gswvtrraay vqlgdivemr
      121 qhtvvrtllg gdvdalrvgq eaefsgwffr rpdelglaae dvlvptplgp apawaihpee
      181 gpstrwavlv hgrgttrsea lravpsfrna gyscllvsyr ndgdappald fryalgdeew
      241 rdvdaaigwv reqgaadvvl mgwsmggaiv lqasrrtthp eliravalds pvidwvdvlq
      301 hqarenrips vvgrvallai srrwgrfltg qatsidlarl dyvanaadla lpillmhsdd
      361 dgyvpagpsr alalarpdiv tfvpftvarh tklwnydper wtaavsdwld eivplppgh
//
LOCUS       WP_285043156             590 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Plantibacter
            sp. LMC-P-059a].
ACCESSION   WP_285043156
VERSION     WP_285043156.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 590)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 590)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..590
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=62276
     Region          3..575
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mvrhtkttrr rlaftivavs ivmtlfvlrl vdiqvvrasa lsaeslekte tgdtilatrg
       61 silasdgsvl aeavmrysma aspkdagpfe rdvdgteqti tleqatneig aiigkpgpev
      121 lalitdalaa dkdslyalia kkldldqlra lkaleipwtt ftedpyrvyp ngavagnvvg
      181 fvgeegepqa gvelmedscl agangrttye kgsgglplpg ttvtkpakdg gdvvltidkd
      241 iqwfsqqsla aqaeavgasw givtvmevkt gkllavaeyp svdpgnvsat paedrgsraf
      301 aapfepgsty ksltaaalid qgvaspnsqv iapfrykpsn gadindsefh admrltlsgv
      361 mvqssntgis qfgekmsadt ryayfqkfgq lqktevgfps esgglmadpe dwdnqtdyat
      421 mfgqgfstta vqgaslyqti anggvrmpvq lvegcrnadg tmtdvpdakg tqvvspdaak
      481 qvsemlemvd qqswvaenvd vpgyrvamkt gtaqqpdgdg gysssylvsm agfapaeapq
      541 fvvsvnladp vkmnssaava pifrdvttqv lksrgvqpst epapnlpldf
//
LOCUS       WP_285043307             435 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285043307
VERSION     WP_285043307.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46365
     Region          4..411
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mgsrrvwwvf gvgvfaylit vmqrstlgva avdatgrfhi daaalstlav aqlivyaamq
       61 vpvgvlidrl gpriliaagl svvmigqiwl glttelggai vgrmlvglgd aavftsvlrl
      121 vnswfpthrv pivsqwvgni gqigqvlsav pfsfvlhalg wspaflgaag lvllalvgvl
      181 ivvrdrptgs deaprpeswg hvvrevvvsl rrpgtrlgfw shfvtqssgt vltllwgfpf
      241 mvyalgysqp laaslliviv vsgmiagpii gvltarfpyr rsnlvlcivt vmglawaall
      301 lwpgvppmwl vivlfvvvgv ggpgsligfd fartfnpira lggangivnv ggflasfvim
      361 fligliidav sggsradysm dsfriafsvq ylvigfgvam llvarsrtrk rfveeegiav
      421 gplwiavrar lgrrr
//
LOCUS       WP_285043378             452 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Plantibacter sp. LMC-P-059a].
ACCESSION   WP_285043378
VERSION     WP_285043378.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..452
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=47108
     Region          114..451
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 madggrrepv tarrapwrsv raraalgsvl avalflgvgs ivfvglfsat lrsgveqsaa
       61 aeadsvsaql taadattlpa ddgrllvlle dgrvvdrtdd evdlptpvpd gdsfvavvdd
      121 esvlfasedv evdgrdlvvl agrsleetdd avglvgvlll vavpvlvvli galtwllvgr
      181 alapverirr evselgagel hrridvpttg deigrlagtm nallgrleda qtaqrrfvsd
      241 ashelrspla virqyaevas lhpdrvdtae lsatvldega rmqtlvesll llakldegas
      301 gagrraldvd dlllaeagrl rsvgglrves savaaarvdg deallarvvr nlvdnaarha
      361 rsvvrlgcss dgrsvriave ddgpgvpvel rarvferfvr ldesrsrdag gsglglaiva
      421 dvvrlhggsv elvdsglgga acvvvlpast as
//
LOCUS       WP_285043400             955 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Plantibacter sp.
            LMC-P-059a].
ACCESSION   WP_285043400
VERSION     WP_285043400.1
KEYWORDS    RefSeq.
SOURCE      Plantibacter sp. LMC-P-059a
  ORGANISM  Plantibacter sp. LMC-P-059a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Plantibacter.
REFERENCE   1  (residues 1 to 955)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 955)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 955)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 955)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20012755
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..955
                     /organism="Plantibacter sp. LMC-P-059a"
                     /db_xref="taxon:3040297"
     Protein         1..955
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=102632
     Region          39..>114
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            60..67
                     /site_type="other"
                     /note="Walker A motif"
                     /db_xref="CDD:99707"
     Site            order(61..68,113)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:99707"
     Site            109..114
                     /site_type="other"
                     /note="Walker B motif"
                     /db_xref="CDD:99707"
     Region          <130..660
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          777..950
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          890..947
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 msagghhfgg gsrsagaalr rsgefrqaat rapaaqssra aaiarvttli ddrastllvg
       61 phgygkthva ehigrrmheq grsvirlsds slnasnalgg wreapsgavf iiddgadlhp
      121 sslsdlvdla rsrdqvalvt leqertglqg rpdeaahrll avwrsgaltr idlpaldgfe
      181 asaladaaad davlddmaka aivrlsngsp rlvheltkda letggefylp rsilslgvag
      241 vsprvhdlte pqlarledee ryalvmlakl gtvpyaravr llgehplhal mrlglarndg
      301 tgqdrivade lhawsalaew rhsgrlhrhd rvqrtlisdl rsgsrltpne sfilgrywlt
      361 taadhndegl tslitarvfl eaahvanvag laedarslae rsaalhpsva aalqgsrala
      421 mlgdvvgaqr vlevdpsaat ddemqsevls wratldrwsd rtcaqhltdq eedsrvlsqr
      481 ilmietwrdq hqqgptdsda vfwkvlrdte aaqssrlyaa aalltrlgmr stpselrdlf
      541 qlgdavyrav pysssrplsh airdasamyv lsagtirlfa glswagfary vdefaeraer
      601 gtgrlatidq svvgilgaql alfdgrpera ladlriverm ldstvppevh tqlgllmvsa
      661 laqtghvdea merratedqq lidsstalsy ladsadfsll msngrvdaar vhlhrmaqsc
      721 tkplteriya aclasvvgae paeafewvad aradeltplq gallllleag aagdasraee
      781 aacsleqlga rhraigahql aerlhtaqgr pqharrcaer aakltdaapk ppvdvalgqa
      841 svaspsplfv sfrndtaavp sipatppsha playlatdtg ssegedpadl ssltrrelev
      901 glliaeglsn qeiatrlfls vrtveshvlq artkvgagrr rdlgrivaqs vqrea
//
LOCUS       WP_285043520             443 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Lactobacillus
            crispatus].
ACCESSION   WP_285043520
VERSION     WP_285043520.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..443
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=51416
     Region          13..433
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkrmsslayh fgiklcfyps skqkkiikln cdaqrfvyns yvgrnrtnyh akrylavrqy
       61 kampfafsal nsyearlaee vvtnsellak prnirdtysf lrvkeidsla lanaiqnyqk
      121 awnnyrkigh giptfhkkrs dwsyqtncqy pkqkeafldn gtarfidakh iklpklgivr
      181 iagfrrlike rllnhiptri gtvtikktad dqfylsmqlg sdiafvkela ktqsqisidl
      241 nldnfltesn gamvanprfy ckakkklaha qrvlsrrqrr akkegrnlrl aknyqkqrlv
      301 vaklhdkirr qrndflqvls taliknhdlv vaeelrsrnl lknhalsqai sdvgwrsfln
      361 mlaykanlyg kefktidpky ttqrchqcgs imgqngykkl tlkdrewtcp icrthhirdw
      421 naavnilekg lgkwqnpkik kaa
//
LOCUS       WP_285043532             425 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Lactobacillus crispatus].
ACCESSION   WP_285043532
VERSION     WP_285043532.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..425
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=47673
     Region          82..425
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 miqkfrwkfi gtsvaalfvv llltlgglvw vthvqsqnev drvltalvkn eghlspknak
       61 pafgdqrdpi nrnflgeqyn peavyqyryf avmideshrv hvindnnvyk vnnskiqnit
      121 raalengdks gvvalgqnqy afrvaknstg etmivflnet lifnrfwllf rvalvlglga
      181 livfalvlil vsgkaikptv dayhkqqefi tnaghelktp lavisantem eemlgnnsew
      241 nesnkeqvak ltklinrlis lartgemgel tlskidfski veettkdfks vmkkndlvyq
      301 vsvreglnvl aekhtlaeiv nilldnaqky cdphgkiqvk ltkggtlsky avlrventyr
      361 egkgkdyshf fdrfyrddks hnskkggfgi glamaqelve afhgkisahh kgedivftvs
      421 lkiak
//
LOCUS       WP_285043561             280 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsB family cell division protein [Pauljensenia sp. UMB1235].
ACCESSION   WP_285043561
VERSION     WP_285043561.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB1235
  ORGANISM  Pauljensenia sp. UMB1235
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Pauljensenia sp. UMB1235"
                     /db_xref="taxon:3046329"
     Protein         1..280
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=31145
     Region          <152..221
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 mprnprserp qaprrpdpnr gllrgtapkk dqkasekssl fkrskksdsa kgqadtqapr
       61 spaerlerar eirsahrana aastrqlrpa rvplsreerr rakarerrqe kkarqerrla
      121 egktflvggl elstrllsvv vlvgvlgall vpnlyawwkq eqelrditak veqtkqqnaq
      181 mreqldlwsd pefiasqare rlgyvkpgev qyavvdpgee yldkaqinaa spegparpwi
      241 qvvgkliqea deaevgqska vpsqsgdqsa pgdaqsaqsq
//
LOCUS       WP_285043576             449 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Lactobacillus
            crispatus].
ACCESSION   WP_285043576
VERSION     WP_285043576.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..449
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=52342
     Region          13..433
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkrmsslayh fgiklcfyps skqkkiikln ydaqrfvyns yvgrnrtsyh akhylavrqy
       61 rampfafsil nnyetrlaee vvtnsellak pknirdtysf lrvkeidsla lanaiqnyqk
      121 awnnyrkigh giptfhkkrs dwsyqtncqy pkqkeafldn gtarfidaqh vklpklgivr
      181 ivgfrklike rllnhiptri gtvtikktad dqfylsmqlg sdiafvkela ktqnqigidl
      241 nldnfltesn gsmvanprfy rkakkklara qrvlsrrqrr akkegrnlrl aknyqkqrlv
      301 vaklhdkirr qrndflqvls taliknhdlv vaeelrsrnl lknnalsqai sdvgwrsfln
      361 mlaykanlyg kefktidpky ttqrchqcgs imgqngykkl tlkdrewtcp icrthhirdw
      421 naavnilekg lgkwqnpkik kqprkaavr
//
LOCUS       WP_285043733             130 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Peptoniphilus harei].
ACCESSION   WP_285043733
VERSION     WP_285043733.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..130
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14420
     Region          <1..>119
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mitefdsipy snagrglqcl lktelalnni ntnkdkiili eepenhlsys nmnnlidilq
       61 ensnkessqi iisthssfvl nklnlenlil lsnkksskit nlssdtekyf kvisgydtcg
      121 dggiivkkik
//
LOCUS       WP_285044076             283 aa            linear   BCT 25-DEC-2024
DEFINITION  TPM domain-containing protein [Peptoniphilus harei].
ACCESSION   WP_285044076
VERSION     WP_285044076.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Sirpio,S., Allahverdiyeva,Y., Suorsa,M., Paakkarinen,V.,
            Vainonen,J., Battchikova,N. and Aro,E.M.
  TITLE     TLP18.3, a novel thylakoid lumen protein regulating photosystem II
            repair cycle
  JOURNAL   Biochem J 406 (3), 415-425 (2007)
   PUBMED   17576201
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..283
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30278
     Region          1..>175
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mkkllatilf vftlvfnvya fdknqmsynv ydetntlsqe tidylnktty dlkkktggei
       61 gvvlvknleg qtleeyatni fndikigdkd knngvlilla llddenklvk ietgygaegf
      121 vpdayasrii ramgrvvaen endrpfekav legyaqiikl yegeygvdiv arepqeaidy
      181 sdddddyree dpflaifkli viiaiislif rnksddgpgg gsgpgsrrrq rpvifwgpgs
      241 fggyggfggs ggfggssggf ggggfggfgg ggssggggas grl
//
LOCUS       WP_285044239              93 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Peptoniphilus harei].
ACCESSION   WP_285044239
VERSION     WP_285044239.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 93)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 93)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 93)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..93
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=10417
     Region          1..83
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mkkkidklen taellkvmah pirlriiknl idngpanvgs mqakfhipqp tvsshlgklr
       61 ragilianrn gteiyykven efilkpaktl fkn
//
LOCUS       WP_285044259             243 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Peptoniphilus harei].
ACCESSION   WP_285044259
VERSION     WP_285044259.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..243
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=27931
     Region          7..241
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mkinfyflfi sflvflfggs lgsfyqvfie rrergedfif srsscdscnk nlkfyemipv
       61 fsyiflrgsc sscgekigre nfyievltsl lallvfmryr isletliiif ilivasfigv
      121 ldyktgyiyn ldlfillffv ivykifisgg ilvsikfsla mgliffllyy ftgmmglgdv
      181 yyafimglva nnlfeafllf rdsfiiagiv smilillkkk tlkdsisfgp fmtmaliilf
      241 icr
//
LOCUS       WP_285044402            1039 aa            linear   BCT 25-DEC-2024
DEFINITION  CD1108 family mobile element protein [Peptoniphilus harei].
ACCESSION   WP_285044402
VERSION     WP_285044402.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Brouwer,M.S., Warburton,P.J., Roberts,A.P., Mullany,P. and Allan,E.
  TITLE     Genetic organisation, mobility and predicted functions of genes on
            integrated, mobile genetic elements in sequenced strains of
            Clostridium difficile
  JOURNAL   PLoS One 6 (8), e23014 (2011)
   PUBMED   21876735
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF045974.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..1039
                     /product="CD1108 family mobile element protein"
                     /calculated_mol_wt=120302
     Region          <19..534
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          <914..1038
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mkkrnpinpr dmpekvrgkn sklknenrik vieelpkstr fkdnsqaldn qgvkednlkk
       61 dsfkdplkke nyretkeenk tsdsfnikek tpkekrqrkm aerifeenri denqniesne
      121 ektyveeenp lsnkedwvee ytesstqayi pqvqqedslp vfslpklglg mrpskkkked
      181 qriegkntfk rgtnqqtqep sirdkkdflp iekmsksqrq kkqaertfrs yeeenkeaiq
      241 eknypikpvn nfdgaksfqg knfkqpnesk enkevledgs igssyrnfre kssrqrvgnv
      301 kentlktdsi kkkrttkfqk evrspqegns qssseiydpl gkdmdndgvi drydvdfrds
      361 dvsyrhkerv dvkenqainl qsikekrnyr nkplgkenil anekiknkkl kktlvekqsp
      421 klrktkgkev flkgesqnfy rkenqdklkn ktdfnrklpi gkekkediek trsnfigeee
      481 ltrkkktsvk eietskeskk skveekgqkd inkdlaknkk skkfqlekev reskfhnkek
      541 kisklykkke ktekkllkde kkagskldsp ailatsltan ylysgkedna gidaaykltr
      601 gselslrkmr rdrrkkpfkt rkklgkldkk ihkreekllf qknfedlkkt sayqkinpln
      661 rffmkkrfqr rfrnktkesl skrikksfss gakkvtdfik nggykkvfla lgilglffvl
      721 lqigsnmatm tagfasnitt ttylsdegvl sdvnneflsy enalqdeids lssyhpgyde
      781 yrvkgdtvgh dvhelfsylt arfgeiksvd kikgelktlf nqmykkdysv ktitkydseg
      841 kpysyriftl tlskktidev areafkdyet nlahyealls aqgnmasifg sgngdlseil
      901 dnpnfgnpgi afdnasvktl fneaekhigk kyvfgasgpk nfdcsgfvcw sftksgvrnm
      961 prttawliyk nycnpispse akagdiiffq gtyksgtpis hvgiyagngm mihagdpiqy
     1021 tsinskywkn hfyafgrpr
//
LOCUS       WP_285044541             409 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidase U32 family protein [Peptoniphilus harei].
ACCESSION   WP_285044541
VERSION     WP_285044541.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787090
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..409
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=46860
     Region          1..305
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
     Region          325..404
                     /region_name="Peptidase_U32_C"
                     /note="Peptidase family U32 C-terminal domain; pfam16325"
                     /db_xref="CDD:465094"
ORIGIN      
        1 mkkiellapa gdinklktav eygadavylg gesfglrkas knfsmedikw atdylhergk
       61 kihvtlniip hnhdmegved yikelyeigv dalivadpgm fmkvkevapd fpihistqgs
      121 vtnvetvkfw qklgaervvm arelslkeva diikevgdsi evetfahgam cmsysgrcll
      181 snymtgrdan mgdcaqpcry kyhlveekrp geyfpieehd egtfimnskd lcmiehidem
      241 ieagiaslki egrvkseyyl atvirsyrma idayyrdpen ykydpsllee ikkvshrdft
      301 tgfffgqane nsqvykdnsy irgydfvgiv ldydedtkia tieqrnrvfv geeieifgpg
      361 vkhfdykiek mlddkdreid vankakqifk ikidqpikkg filrrenee
//
LOCUS       WP_285044585             236 aa            linear   BCT 25-DEC-2024
DEFINITION  MarR family transcriptional regulator [Lactobacillus crispatus].
ACCESSION   WP_285044585
VERSION     WP_285044585.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Nazaret,F., Alloing,G., Mandon,K. and Frendo,P.
  TITLE     MarR Family Transcriptional Regulators and Their Roles in
            Plant-Interacting Bacteria
  JOURNAL   Microorganisms 11 (8), 1936 (2023)
   PUBMED   37630496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Will,W.R. and Fang,F.C.
  TITLE     The evolution of MarR family transcription factors as
            counter-silencers in regulatory networks
  JOURNAL   Curr Opin Microbiol 55, 1-8 (2020)
   PUBMED   32044654
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Grove,A.
  TITLE     Regulation of Metabolic Pathways by MarR Family Transcription
            Factors
  JOURNAL   Comput Struct Biotechnol J 15, 366-371 (2017)
   PUBMED   28694934
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   7  (residues 1 to 236)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   8  (residues 1 to 236)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10581578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..236
                     /product="MarR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26923
     Region          28..81
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
ORIGIN      
        1 mtkkrktsea nhkfkgvwip aeywldkdlt imevalitei dsldgengcf asnklfadfl
       61 gitpgrvsql vkslkekgyi ttiystknnv tqrtirvvsk lntpvkklnr gikntkgvfn
      121 klltsnissn tfnsntvsns ssakkeedpe rekiykefft iarmndklkn hstnptldel
      181 kqlrgllyqc nvdtlqavkd kfkermswdm vgkpysyllk mlrdglandr nyeswg
//
LOCUS       WP_285044624             313 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lactobacillus
            crispatus].
ACCESSION   WP_285044624
VERSION     WP_285044624.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..313
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35889
     Region          <214..308
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 maavaldqyl asvlksnstd kneikleagn pdfdlftiyl enhntgihry rmdvstilyi
       61 akgtvtiksg ekiiqmksgn vllltegcky eilsqkpdtv liklkfkrgf lyrkyfkdfs
      121 ckgerevkvi eqivdslene hvlwlknnqi trasqvmqhi iggylnndlf tkaliqaelt
      181 tmliisirtq rmatptsldk tkfekktldn yidlhfadvs lsdaakyfgf npnyfsnmvk
      241 aktgksfvah vddrrmqear ellaqpdisl reiigrvgys sksffykkfn qyyhitpaam
      301 raelfrqani nlk
//
LOCUS       WP_285045076             118 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Neisseria mucosa].
ACCESSION   WP_285045076
VERSION     WP_285045076.1
KEYWORDS    RefSeq.
SOURCE      Neisseria mucosa
  ORGANISM  Neisseria mucosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Neisseria mucosa"
                     /db_xref="taxon:488"
     Protein         1..118
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12720
     Region          1..116
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mnygghland avlrlchevr mrwlaglgws etdaggagli madaavqyla qgfygdelsa
       61 emgvedigkg vfallfrltr iadgkvlara rtgmvcfdya rqkvcrlpea lktvlevv
//
LOCUS       WP_285045088             310 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Neisseria mucosa].
ACCESSION   WP_285045088
VERSION     WP_285045088.1
KEYWORDS    RefSeq.
SOURCE      Neisseria mucosa
  ORGANISM  Neisseria mucosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Neisseria mucosa"
                     /db_xref="taxon:488"
     Protein         1..310
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31631
     Region          26..306
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mkkwlpalpv lslfliwfca gvgeggwsnp laadpvlmei rlprifvall vgaalsasga
       61 alqalfenpl adpsligtsg gaamgvvlai amgwsiavpl aafagafavc ilillghrlv
      121 gggklgllvm gfvvsalcga lvslilflsd dmalrsamtw lsgsfseagf vspayaggvm
      181 laglvvlaav grrldylllg detahtmgis vaatrvatii gaalmtgaav slggiigfvg
      241 mmipnvlaqv vggsrtrlii lsaavgsifm lladtfarwv vypidlpvgi viailggpff
      301 lwlivkdqrs
//
LOCUS       WP_285045156             265 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Lactobacillus gasseri].
ACCESSION   WP_285045156
VERSION     WP_285045156.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus gasseri
  ORGANISM  Lactobacillus gasseri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Lactobacillus gasseri"
                     /db_xref="taxon:1596"
     Protein         1..265
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30163
     Region          5..247
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(28..29,31..32,35..36,74,78..79,82..83,112,116,123,
                     126..127,139,155,159..160,162..164,166..167,170..171,
                     174..175,200..201,203..205,207..209,211..212,214..215,219,
                     222..223,229,231)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(158,162,165..166,168..169,214,217..218,220..225,
                     228..230,234,236)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(179..186,202,205..206,209)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mskiiigryi pgnsiiykmd prgkiiatfl fiviiflann wlsylflsff tllavgatkl
       61 kpkvfwdgvk pliwlilfts vlqlffttgg kvywhwgifn iseygiqnsi fifirfvmii
      121 listvltltt tsleiadgme wllrplgylk vpvaqialvm sialrfvptl ldqavrimna
      181 qrargadfns gglikrihai ipiliplfis sltiaidlat ameargyreg akrtryrilr
      241 wskydwvnlg yfalltlill ltrty
//
LOCUS       WP_285045454             385 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Neisseria mucosa].
ACCESSION   WP_285045454
VERSION     WP_285045454.1
KEYWORDS    RefSeq.
SOURCE      Neisseria mucosa
  ORGANISM  Neisseria mucosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Neisseria mucosa"
                     /db_xref="taxon:488"
     Protein         1..385
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=42147
     Region          1..383
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mkfatkvihs sydcdehnra lmppiyqnsm falheigeqv pyrysrlsnp trqvledtva
       61 dlergaagfa fssgmagida vwrtflrpgd tivavadiyg gaydllvdvy kewgvnvvfa
      121 dlgnpdrlde llavhnvklv wletpsnpll rlvdikalaa kahaagalvg idntfatpyl
      181 qqplemgcdi vfhsatkylc ghsdvlmgiv avktkelakp lhdmmvhtga iagpmdcwlv
      241 lrgiktlalr meahcknald iarrleahpa vekvfypglp shehyelakn qmpkgiggvv
      301 tvylkndtre aansviknmk lvkmasslgg veslvnhcys qshsgvphdv kmemgikvgl
      361 lrfsigieda ddiwndiska ldstl
//
LOCUS       WP_285045480             470 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Lactobacillus
            crispatus].
ACCESSION   WP_285045480
VERSION     WP_285045480.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..470
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=54646
     Region          28..365
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mtkktknvpr nstqythlcs eyiipasnil dkisykahdl ynralydlrq glfhkqyvkg
       61 yeqldsmfkk rykarecily helgyvqsaq qtlkevntiw qawfkankay qknpgkftgk
      121 prmpkylrkk erhtlfvtnq nakvkdgylt ipklkikvel alqvkkiqrv afkpvyggyk
      181 livqykinke inylpdngry igidpgvdna facvsntenm pllingrnlk svnqyynker
      241 arlkklqaqy hqlesiintk qgpkpvyqet kamkrltvwr ndkirqfahk askrivnyal
      301 sceantivig nnkswkrssn mgkknnqnfi giphkvmiem iqykanlagi svirtnesyt
      361 sqtsaldnek pcwengnknr qrqgkspliq qyfvgsvrka lskkyswdds iskakirsds
      421 vrlpvvsntk nldfnymeky iraiekltia eavkykdrei ltteslinkm
//
LOCUS       WP_285045484             336 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Lactobacillus
            crispatus].
ACCESSION   WP_285045484
VERSION     WP_285045484.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..336
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38090
     Region          3..331
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 midfnktqhl iesmvfervv pgvnytfikn kqiftsttgf asiypevtql spfaeydlas
       61 ltkvlatenv llklydqgkl nfteplqqfi pefkdprvrl yhllthtsgi rgwiphrdkl
      121 dhdallqaii nlpvtdefeh kmryadtnfi llglvikkif gkpvqevvte qvlnqmplen
      181 ttfspqkddc vptalvdghv lqgiphdpka rqlgidcgsa glfstlqdlv tfaqgylglk
      241 dvlpysqktv sqlfdnknpq gikprswgwd lrfdpkqnyp iilhtgftgt liildrikrs
      301 glilltnrvh ptghntvfla mrekiihsfi nenaki
//
LOCUS       WP_285045545             702 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Neisseria mucosa].
ACCESSION   WP_285045545
VERSION     WP_285045545.1
KEYWORDS    RefSeq.
SOURCE      Neisseria mucosa
  ORGANISM  Neisseria mucosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 702)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 702)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Neisseria mucosa"
                     /db_xref="taxon:488"
     Protein         1..702
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=78492
     Region          67..702
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mqysarlsll paliasafpl yaadtadseh ytatlptvtv vgqsdtsvlk gyinydeaav
       61 trngqliket pqtvdtlniq knknygtndl ssilegnagi daaydmrges iflrgfqada
      121 sdiyrdgvre sgqvrrstan ierveilkgp ssvlygrtng ggvinmvsky anfkqsrnig
      181 avygswanrs lnmdinevln knvairltge vgransfrsg idsknvmvsp sitvkldngl
      241 kwtgqytydn vertpdrspt ksvydrfglp yrmgfahpnd fvkdklqvwr sdleyafndk
      301 wraqwqlahr taaqdfdhfy agsengslik rnyawqqtdn ktlssnftln gdyhigrfen
      361 hltvgldysr ehrnptlgfs raftasinpy draswpasgr lqpvltqnrh kadsygifvq
      421 nifsatpdlk fvlggrydky tfnsenkltg ssrqysghsf spnigavwna tpahtlyasy
      481 nkgfapyggr ggylsidtss aavfnadpey trqyetgvks swlddrlstt lsayqierfn
      541 iryrpdaqnd pytwavggkh rsrgvelsai gqiipkklyl rgslgvmqak vvedkenpdr
      601 vgihldntsn vtgnlffryt ptenlygeig vtgtgkrygy dssqkvtttl pgfvrtdamf
      661 gwnrknlnlt favgnlfnqk ywrsdampga prtytarvny sf
//
LOCUS       WP_285045567             383 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Lactobacillus
            crispatus].
ACCESSION   WP_285045567
VERSION     WP_285045567.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..383
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=44864
     Region          1..382
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mikaqvvelk pnktmqqkld klcdyrrycw nqalatwqdm yeartldkdn npspnerrir
       61 delvdnkadw qfalsarclq lavkdlanaw knffdkaqpd wgkphfkskk aprqgfktdr
      121 akvvndklrl dkhrgiktwf diptyealkm kqikvasvfr erghyyaals yeeetlvkpr
      181 tgrktavdvn vghfnytggk invlpsrlqk lykrikhyqr mlakkrrang klagqsnnyv
      241 qvrtklqrdy rkvaniqndl lqkfttklvn nydqiviedl avkqmmmthv askgmqrslf
      301 skfrqiltyk cewygkelil adktypstqr ctncgyvkkg dekitlqgnq khhtkhneyi
      361 cyecgytndr ddnavlnlla lak
//
LOCUS       WP_285045743             319 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Neisseria mucosa].
ACCESSION   WP_285045743
VERSION     WP_285045743.1
KEYWORDS    RefSeq.
SOURCE      Neisseria mucosa
  ORGANISM  Neisseria mucosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Neisseria mucosa"
                     /db_xref="taxon:488"
     Protein         1..319
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35321
     Region          47..300
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          215..298
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdtldkliel aqitgsvdiq clfrdkwyap herrrahgia hlvvagesyi kiegepearl
       61 lqtgdliffp rsaehiisse adcnncgdti higndgafti essgsvgekg ldlfcarfey
      121 dehadimhdl petvlikmdh pslqclisml qyesahtlsg sraivnalss vllvlivrah
      181 leqggeaplg gilnglrdkr lrqliqtvvs rpedewniek mtelanlsra qlmrlfkqqt
      241 gisphafvnl irlrqaavll rqtadsvlsv alnvgfqset hfgkafkkqy gispgqyrkn
      301 etaddatmaf epersseng
//
LOCUS       WP_285045866             384 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Lactobacillus crispatus].
ACCESSION   WP_285045866
VERSION     WP_285045866.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..384
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=43462
     Region          44..378
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mkkervkltg aekselfaeg vvtvvllfll nlsiiilihl ailqdeslvn giyflkktit
       61 faggyhlwsw qnvfivlmgv gdlvvlywrl irryhqmqlr hiilelhyia nghfdhrinf
      121 rvrpelqrvv dsinslvdst vnsineerai eqskdelitn vshdirtplt siigylgllk
      181 agvtspedqk kyaniaytka eqmkalandl feyttlkstn tklnlndlhi ysmleqvaag
      241 feleaekngi eieiearpkn ltikadaekl vrvynnlisn afkygtgatk iklvanlvnk
      301 revelrvenn gapipkksln kiferfyrve tsrntktggt glglsitkgv vdlhhgtirc
      361 esnekwtsfi irlpldpkka spth
//
LOCUS       WP_285045798             419 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Neisseria mucosa].
ACCESSION   WP_285045798
VERSION     WP_285045798.1
KEYWORDS    RefSeq.
SOURCE      Neisseria mucosa
  ORGANISM  Neisseria mucosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 419)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Neisseria mucosa"
                     /db_xref="taxon:488"
     Protein         1..419
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46017
     Region          7..407
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 masetykrys vlfsstlsft vcfmiwmmla vvgikvqeem gfnqtqygil ialpvlsgal
       61 irvplgiltd kfggrivlft lmilsvptif lmryanqywh flviglvmgl aggsfsvgtp
      121 yvarwfpkhq qgvamgifga gnagsainkf laawlivtfg twqivptvys aimlatailf
      181 wftsyhdpkh lvssnvtlke qlallkdpgv lrysqyysvv fggyvalalw mtkyyvgeyg
      241 mplqtaafla acfslpggvl rafggylsdk fgaykvtwav mwliwicffi lsypqtdlsi
      301 rttdggsltm hlglnvtvft ilmftvgvat avgkasvfkf vaddypdnig avsgivglag
      361 glggfllpim fgaledwtgi rstsfmllyg tvcvsliwmh fsfkakresd mkalkehqt
//
LOCUS       WP_285045934             401 aa            linear   BCT 25-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Lactobacillus crispatus].
ACCESSION   WP_285045934
VERSION     WP_285045934.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..401
                     /product="metal-dependent hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43797
     Region          15..>70
                     /region_name="metallo-dependent_hydrolases"
                     /note="Superfamily of metallo-dependent hydrolases (also
                     called amidohydrolase superfamily) is a large group of
                     proteins that show conservation in their 3-dimensional
                     fold (TIM barrel) and in details of their active site. The
                     vast majority of the members have a...; cl00281"
                     /db_xref="CDD:469705"
     Region          50..386
                     /region_name="Met_dep_hydrolase_A"
                     /note="Metallo-dependent hydrolases, subgroup A is part of
                     the superfamily of metallo-dependent hydrolases, a large
                     group of proteins that show conservation in their
                     3-dimensional fold (TIM barrel) and in details of their
                     active site. The vast majority of the...; cd01299"
                     /db_xref="CDD:238624"
     Site            order(65,67,224,244,315)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mtktafvncn lfvgnednlv dnawfvvdde tgkltdqgkg kctadfdkqv dlkgkyvmsg
       61 llnshthmgl dsdlkkkfpt teasttyaal rdlrealqtg vtyvrscgts fdvdcklvqm
      121 rkqypfegpq vmptgmamai vgghgdfkvg lngeqnashl vngpedmrra vreqfakgak
      181 nvklmatggi mslgdevddt elsleemkma veeahskhmt vcahaegrrg ihyavvagvd
      241 svehgfyldd ndlalmkkqg tflsptltag rtivvhgkdv vpefsyrkmc avvddfynhv
      301 ghaikegvrl amgtdagtyf nrfsdtpnel velvragatn ypalragglg saellkvdqe
      361 ygslevgkya dflvlrdnpl edvaavgqkd kqvyqhglrk f
//
LOCUS       WP_285046021             203 aa            linear   BCT 25-DEC-2024
DEFINITION  IMPACT family protein [Neisseria mucosa].
ACCESSION   WP_285046021
VERSION     WP_285046021.1
KEYWORDS    RefSeq.
SOURCE      Neisseria mucosa
  ORGANISM  Neisseria mucosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Park,F., Gajiwala,K., Eroshkina,G., Furlong,E., He,D.,
            Batiyenko,Y., Romero,R., Christopher,J., Badger,J., Hendle,J.,
            Lin,J., Peat,T. and Buchanan,S.
  TITLE     Crystal structure of YIGZ, a conserved hypothetical protein from
            Escherichia coli k12 with a novel fold
  JOURNAL   Proteins 55 (3), 775-777 (2004)
   PUBMED   15103642
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Okamura,K., Hagiwara-Takeuchi,Y., Li,T., Vu,T.H., Hirai,M.,
            Hattori,M., Sakaki,Y., Hoffman,A.R. and Ito,T.
  TITLE     Comparative genome analysis of the mouse imprinted gene impact and
            its nonimprinted human homolog IMPACT: toward the structural basis
            for species-specific imprinting
  JOURNAL   Genome Res 10 (12), 1878-1889 (2000)
   PUBMED   11116084
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Neisseria mucosa"
                     /db_xref="taxon:488"
     Protein         1..203
                     /product="IMPACT family protein"
                     /calculated_mol_wt=22727
     Region          3..190
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 mittyktits ptqaefkdkg srfiafvypi rtladvkkyl dplkeehhka rhwcyayrlg
       61 vdgtqfrand dgepsgsagr pilgqidsvg vtdvlvvvvr yfggtllgvp glihaykeat
      121 aqalavaevv ekniektvwl kceypflnea iriakqyqad ileqdlqldc rltvnlslan
      181 yeacvsawkn trqievntek pfe
//
LOCUS       WP_285046327              63 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lactococcus petauri].
ACCESSION   WP_285046327
VERSION     WP_285046327.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 63)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 63)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 63)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..63
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..63
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7112
     Region          3..58
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mwnkieqllk eknmtpyrla klsglnkatl ahiksgkvkk plfetvckia dalevdinvf
       61 rek
//
LOCUS       WP_285046580             449 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lactococcus petauri].
ACCESSION   WP_285046580
VERSION     WP_285046580.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..449
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=51784
     Region          95..436
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mnnvkisnit qksirdsskk gskevkfrss fnhpltnkrr eflsewylik ekyddkgnik
       61 issqfksiiq rdmqnlansi yqdiskvqlt sknnitieki wyewhndriv kkkvapktla
      121 geagrfnnhi trfiprdsll qnirseliqs llddlyplgn hkrvaqsiks dlssiyifav
      181 kknyilpeqn pmlyvtveek glseqleqla nnsienhyle kdelnevlti vrkynqqyar
      241 ilefqvltgm rigevlglki seisfdthsa tikrsrsthr gaskedyegd vknkqsyrti
      301 klsdkallll eeeieinqhh iignpeykdn gwiftskstn ktefngiplh ysvinnflns
      361 setgkitktg hvkkvginid nrlsfnkhis thifrhtfvs hmaeqgvpli avqryighks
      421 gskiteeiyt hitkkmsdti tesidtlid
//
LOCUS       WP_285046559             325 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Lactococcus petauri].
ACCESSION   WP_285046559
VERSION     WP_285046559.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 325)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 325)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401372
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..325
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38311
     Region          46..129
                     /region_name="cupin_Lmo2851-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to Listeria monocytogenes Lmo2851 protein, N-terminal
                     cupin domain; cd06996"
                     /db_xref="CDD:380400"
     Region          241..324
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mellndiake ylftlnnkei sqrkngnfvf dyptkatnde kellsfskef fiknnqvfls
       61 khnrfadype hdheffefny mlsgschqkl ngkeiilnkg dlilldpncr hsikalgqnd
      121 iliniifphk sfdinwinnl glenntlfnf lmnelsahsk gnyikfetsc nenveviihq
      181 linkfytgsy fsneimkfmi pilfmelign tpyelnhpqk draenhiiak tlqliseeyf
      241 eitleqlanr lhynknylsn likkktghtf tehlvdermk rallfiqtss dsisdiceqv
      301 ginnksyfyr lfkehyghlp tyyrk
//
LOCUS       WP_285046798             470 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Neisseria
            mucosa].
ACCESSION   WP_285046798
VERSION     WP_285046798.1
KEYWORDS    RefSeq.
SOURCE      Neisseria mucosa
  ORGANISM  Neisseria mucosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Neisseria mucosa"
                     /db_xref="taxon:488"
     Protein         1..470
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=52169
     Region          15..430
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mdtsqpaprs dqqanrrylt vwrwhfyfgl lvapfltlla vtglgmllfa nitgkegeri
       61 hvtpqaqvqp lsaqaeaarq svnpetasvv qyiapraddm vavfrvnndd katmvavdpy
      121 takvvnsmpr negwyhtmdg ihgdmmlgtt gdylietaas ltilmmitgi ylwwakqrsl
      181 ksmlvpqtgk grswwrsmhg afgtwvslil llfclsgvaw agiwggkfvq swsqfpagkw
      241 gvepnpvsvv pthgdvlndg ktkevpwile ltpmpvsgtt kgenginpse pmtletvdrf
      301 areigfkgry qlnlpkgetg vwtlsqdsms ydmvsptadr tvhidqysgk iladirfddy
      361 nffgkfmaas ialhmgtlgw wsvlanvlfc lavificvsg cvmwwkrrps kagglvppaq
      421 kielpvwwam avpllivavl fptaiaaivv iwlldtvlls ripvlsrwfk
//
LOCUS       WP_285046857             405 aa            linear   BCT 25-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Lactococcus petauri].
ACCESSION   WP_285046857
VERSION     WP_285046857.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..405
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=41701
     Region          31..376
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mkkklitalm lstvvltaga pfaavkadst dskiaqqdsk ianakneaak aqsqvdsiqs
       61 qvstlkskqt smtkkvnelm aqqkeqsqqi qklsesiker ntaleaqars aqtdgsatny
      121 msavldsksl tdaiqkmtam atvaganksm ieqqqadqka iqtkladnqk kyaeatklqq
      181 eldaqanela tqeaalkvaq ldyqatvtta egkkqdllsq kaaaekaaqk aaaaekaaaa
      241 ksvvaqqeka vaaapaasnp apaanntadn snsstpstgn ntggngnssk ptpeptptpt
      301 pdpghsgtnp ypagqctafv wdyfggnmpt ymgnagdwva yansgpaagt iavfppgnqg
      361 aggvghvavv lsvsgskmtv iegnfnggwg ttrecstagv sfirp
//
LOCUS       WP_285046901             739 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Neisseria mucosa].
ACCESSION   WP_285046901
VERSION     WP_285046901.1
KEYWORDS    RefSeq.
SOURCE      Neisseria mucosa
  ORGANISM  Neisseria mucosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 739)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 739)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 739)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Neisseria mucosa"
                     /db_xref="taxon:488"
     Protein         1..739
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=79914
     Region          69..739
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mikpasrlsi lslsllavsa afasdepqar eiaeletitv tasadaskgg lipafkggqv
       61 argsrvgilg nkknlespfs ntaytnrliq dkharsvgdv lqndptvrva rgygnfqeay
      121 firgfaaesd dtmynglygi lprqyiatel fervevqrga saflngmapg gnniggtvsv
      181 lpkrasnegl nrltanygag krgglaadva rrfgqnqefg vrvnaahhng ktaiddeksk
      241 lslvnvgldw rnenarlsad lgwqdnklka trtnvtlsgl tavpaapdas snwaqpwtys
      301 nerdwfgtmr geydfndnlt ayvaygfrrs kennslanlt vrnvngdgsi yrfdnarkdk
      361 idtgeiglrg kfntgavghe wtaaanrfqs srknayimdw gnqyttnlyn psrypqpaaa
      421 dplysgndmg npavtgktrl tsfalgdtfs lwdkrlqfml garwqqvhnk ayayntgaqt
      481 enykksrlsp avgavyritp nwsvygnyie slgqgatags tasingraya vsnageslkp
      541 yvskqkeigt kyeaggfgag ltlfhtdkpr slyvvennta rltsegkdrh qgaeitvyge
      601 vapgvkllgg vtlldakqks tgssstdgkr tigaaktqan iglewevpkv qglafdgrmv
      661 ytgssyadaa ntlkvggwtr fdigaryrtq igrheatfra rldnvankky wasvggypgs
      721 gylnagaprs fslsasvdf
//
LOCUS       WP_285047029             109 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Lactococcus petauri].
ACCESSION   WP_285047029
VERSION     WP_285047029.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..109
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11489
     Region          4..108
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mnlgyfflav aivsevtgss likytegftk igpsmlclal fgtaifmlsk tvryvplyia
       61 yglwgalgiv lvtaisvvfl kesintptii gialivvgvl lvnlygash
//
LOCUS       WP_285047116             228 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator, partial [Neisseria
            mucosa].
ACCESSION   WP_285047116
VERSION     WP_285047116.1
KEYWORDS    RefSeq.
SOURCE      Neisseria mucosa
  ORGANISM  Neisseria mucosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12820769
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Neisseria mucosa"
                     /db_xref="taxon:488"
     Protein         <1..>228
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          13..227
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          178..>228
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 gsltarktfq strlsepyia fvlllegsld fginreryri eaegghvlli acdeeilfsr
       61 ylyegghtak ltlkgidrwl arpqyagllq avyrekvrhw pldgslrrla lsslkgaeqg
      121 gladdlqrea dvlqllaglw tdflnrypyt etaaepphps esfirllnqa fdagahqvsa
      181 ladalyiser tlqrrlkesf gttasewlrh khmqyalyal gtdsvsig
//
LOCUS       WP_285047207              73 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Fusobacterium
            necrophorum].
ACCESSION   WP_285047207
VERSION     WP_285047207.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 73)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 73)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 73)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..73
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8370
     Region          1..69
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mlkfkihilm aehrmtqkdv meatgitttv mkkyyygtia ripthhieal cklfqcnvqd
       61 lveyipddep sae
//
LOCUS       WP_285047397             662 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Fusobacterium necrophorum].
ACCESSION   WP_285047397
VERSION     WP_285047397.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..662
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=77216
     Region          412..657
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mkkieiktfl eysflsnvrf skngkyisyt ktkanleknd yehyvyvydt qskenkeyts
       61 lgkeknivwl ddtrllfqts rdsnikekkk egeewteyys idvrggeaka flqlpysvtd
      121 iqacssgfvf tanysnadis lhgltgeera kaiekkkeea dyevldeipf wsnglgftnk
      181 qrnrlyryet asqkiealtp efmnveyfkv senrvlfiae eyhdkleqtn alyeydllen
      241 rcscliedgn ynfsfadymg rdivcaasdm ktfginenhk lyfvknrtle lfyendtwll
      301 stvgsdckfg ggktfhttdn alyflstled fsvinclhrd grlelltard gsvdffdiyk
      361 dtlvygamkd yglqelylke nteeieitkh nrtvfeeysv skpekifmes ygesieiyvi
      421 kpvgfeegke ypaildihgg pktvygnvfy hemqvwanlg yfvfftnphg sdgrgnrfmd
      481 irgkygsidy edlmkatdiv lesypidrkr mgvtggsygg fmtnwiight drfacavsqr
      541 sisnwiskfg ttdigyyfna dqnqstpwnk veklwshspl kyanqvktpt lfihseedyr
      601 cwlaeglqmf talkyhgvea rlcmfrgenh elsrsgkpkh rvrrleeitn wferylkkqe
      661 re
//
LOCUS       WP_285047532             399 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Paracoccus sp. SSJ].
ACCESSION   WP_285047532
VERSION     WP_285047532.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..399
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42327
     Region          1..380
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 minpgslanl rvidasrvlg gpyagqilad hgadvvklep pagdetrgwg ppflgdaasy
       61 flglnrnkrg iavdlsqemg relllalled advlienfkt gtmerwglgq delarrfprl
      121 vhcrvsgfga dgpmgglpgy daaiqalcgi msvngeaggq plrvglpvvd mvtglnatig
      181 ilmalnerat sgkgqfvets lydcgvsllh phlpnyylsg rvagpsgnah pnicpydtfa
      241 tgtepiflav gnnrqfatlc amigrpdlpq darfasnsqr nihrdalkaa leaalsafdc
      301 aglsdrlika gvpcgavrsi dqviadphti hremvvdige yrgtgspikl srtpasyrra
      361 ppgfaqhtge vmaeraldpd syrevlpgld peqnaarka
//
LOCUS       WP_285047602            1007 aa            linear   BCT 25-DEC-2024
DEFINITION  UvrD-helicase domain-containing protein [Fusobacterium
            necrophorum].
ACCESSION   WP_285047602
VERSION     WP_285047602.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 1007)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437585
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1007
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..1007
                     /product="UvrD-helicase domain-containing protein"
                     /EC_number="3.1.11.5"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=121478
     Region          4..990
                     /region_name="RecB"
                     /note="3#-5# helicase subunit RecB of the DNA repair
                     enzyme RecBCD (exonuclease V) [Replication, recombination
                     and repair]; COG1074"
                     /db_xref="CDD:440692"
ORIGIN      
        1 mkrlvlkasa gtgktyrlsl eyllslyrgi pyseifvmtf trkataeire rilefsaeil
       61 shsekgkelv ehlqaldstl flkeevlkaa ydsmlknkdk iriytidsff qmlfhklvcp
      121 yyqiysmkmi eteeenkeyy kkilkhifsk eelfekmkvf fdlspeknie nyllliqnil
      181 qerwkflllq geqkkrtpln fektreehik afqalfqave etkkkergyf thpfyqnffe
      241 qteeereetl tkererffdt nvfdgrrlsn rgkdekilsl reelleetds frrdlakevy
      301 nqdmiafees lfsifeelyq lydeykrker sfnyddiaiy tyltlfqeel hliennkita
      361 lleeildvki hsifldefqd tsilqwkils vflekaeavi cvgdekqsiy gwrggekklf
      421 edlpkilgae vehldtsyrs lesivefcne ffksypalyq eeaiewkfle skshkqkrge
      481 vlsyflseee slqtllstik ekysgnygsl silarknktl lqladfleeh klpyqlsivk
      541 eqqdeeivss flslfryfcs neylylleff rspvikasnr ilknllthqe nmiqyicfgk
      601 ewkekpkgse eifelyrefq eneakigdlw lhciekfslp erfskdshll ayysfqesls
      661 yydtwfeyle dldrnrlpkl direeenkna iqlmsihksk glefenviyf epkekrkgrk
      721 eqnilfyfqm addycslehy fltkgkyrky meylpkpfpn ylkdlerkek eeeintlyva
      781 ltrakhnlyl ffnetfqgre lleklsfvss emfteskeet klkeekqgiv ltfqkekksf
      841 eedrkqrpqk ytlqtelhrm eglathffle hiryateeei rfakqrvfqe yasyfgmekm
      901 eqlfseerir kiltldsdif srdwdyiype fsiispmdqk kyvldrlmir kakkgkkglv
      961 yivdyktggk dpkqlenyeq ilrelfkree geyefqtkfl elgrege
//
LOCUS       WP_285047682             275 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paracoccus sp. SSJ].
ACCESSION   WP_285047682
VERSION     WP_285047682.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..275
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29042
     Region          1..272
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
ORIGIN      
        1 menfvtafdt tvdnalfwlt dhaafifdga ravleglydg vlwllmlppf ylaavlvgll
       61 awrvlnlwag iatavaliac aamglwpetm etlalviaas iialaislpl gvlaglmprl
      121 dralvpvldl iqtmppyiyl lpaiallgfg patalvatvi vamppairlt slgirqtpne
      181 fielghasgv tpaqmfwkir lpfampsima gvnqslmmaf gmvviagivg sgglgetiyg
      241 airtldiats inasiaivvl tmvldrvtqs lartk
//
LOCUS       WP_285047969             342 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Fusobacterium necrophorum].
ACCESSION   WP_285047969
VERSION     WP_285047969.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..342
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38302
     Region          1..323
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mlsflndyse gghprvmedl mrsnqestvg ygfdryceea rsliarkikq egaetwflag
       61 gtltnltvia halkphqavi tactghinvh etgaieatgh kvlglpseng kltskmiedc
      121 layhedfffv epkmvyisnt tevgtiyskk elmdlkacce knnlylfmdg arlayalgae
      181 enditwedlg rytdvlfigg tkcgamfgea vtiihedlkk dfkysikqrg glfakgrlig
      241 vqfisllqen lyeeigkran eaarilrdgl kelgfispyd spsnqqfvlm teeefqkiss
      301 vvlcgvegkw kdgrcrvrfv tgwknteeea keaiekiqei ls
//
LOCUS       WP_285048010             371 aa            linear   BCT 25-DEC-2024
DEFINITION  3-hydroxyacyl-CoA dehydrogenase [Paracoccus sp. SSJ].
ACCESSION   WP_285048010
VERSION     WP_285048010.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12804107
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..371
                     /product="3-hydroxyacyl-CoA dehydrogenase"
                     /calculated_mol_wt=38597
     Region          1..276
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
     Region          292..>336
                     /region_name="3HCDH"
                     /note="3-hydroxyacyl-CoA dehydrogenase, C-terminal domain;
                     pfam00725"
                     /db_xref="CDD:395588"
ORIGIN      
        1 mttiaviglg tmglgiaqty aaagfallat davpeareta ldrlraglap rvragklaqa
       61 dldailarit vvdgpkamga tdlaieavve rmpvkqslfa aleavvapda vlasntssls
      121 vaamaeglar perllglhff npapvmklve lvahpgtgaa aldrarrlte aagktvipcp
      181 drpgfivnrc arpfygeala mleegrstae idaamqaagy plgpfglidl vgadinlaat
      241 eslaaamegh pryhvfdalr rqvasgdlgr ktgrgflypd epgpapkdae aivrrieaal
      301 vneagwllae ggttqqgidt alklglnfpr gpfevlaaqg hervlarldh laaaapahld
      361 gryqpapvlt r
//
LOCUS       WP_285048122             347 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Fusobacterium necrophorum].
ACCESSION   WP_285048122
VERSION     WP_285048122.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..347
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38246
     Region          32..345
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mnpvknihqy nskkilkivi alfillfvsy isvftgiani nlkrvlatif egffyetepl
       61 sqremvvfld lriarvvlgs iagfllaicg tvmqaitenk msspfttgis saasmgaals
      121 ilffngkyvy fdfitiffaf sfgiicsllv ygisnlkamn kstliltgia fnylfssgna
      181 alqfianedv lssivnwtfg nlsgvswnki lilflillif fpyffinrys ynilltgeds
      241 aislgihvrk frfisgiivt litsavvsfi giiafvgiia phisrmligd dhkysiilsg
      301 iigaflvifs dyigrnllsp iiipigivis fvgipifiyl iinskrg
//
LOCUS       WP_285048205             483 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Fusobacterium
            necrophorum].
ACCESSION   WP_285048205
VERSION     WP_285048205.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..483
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=52361
     Region          1..462
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mlkyfeafvn flwglpiivi ilgtgfyftf ktgffqvfhl khifsetick iikkgnkaee
       61 ngeglitpfd avataiggsv gvgniggvat aiavggpgal fwlwiaafvg milkmaevtl
      121 gvyyrekden geiyggptyy mekglgkekg ykwwiipavi fgggifstff itvqnytvse
      181 avsaafgiki iyasilyiii nyililggik slgklagkiv pfmcifyvga afyiilvnig
      241 nlpeaivsvl qgaftgtaav ggfagaafnq vmrvgmarsv fsneagwgss pmihssaqtd
      301 hpvkqglwga fevfvdtmiv ctltalviii tgvwqggatg atltlsafet gmgaaskifi
      361 acgiflfgvt tssgwyayye iilrhlmkss pklkagilkf yrifypipgf imvvmattig
      421 mpggtvwlfa dfttaiptfv niavvlalsg tflrlfhdyk rryilkedms qvkdplffse
      481 eke
//
LOCUS       WP_285048344             350 aa            linear   BCT 25-DEC-2024
DEFINITION  HesA/MoeB/ThiF family protein [Paracoccus sp. SSJ].
ACCESSION   WP_285048344
VERSION     WP_285048344.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..350
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36234
     Region          99..344
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mlilaimlav lvaarllgwp awrgwagvaa lwlaavaalv lapgsgvarl vggdarvwvl
       61 gggvvalllg yrlllrqlhr ravpvpeapq psaqsgplsd peldryarhi vlrelggpgq
      121 aalrrarvlv vgagglgapv clylaaagvg ritvadddhv glsnlqrqvi frsaddgrpk
      181 aeaardamla lnphvevaal nrritdadaa liaehdlvld gtdsfaarra vnaacvaagv
      241 plvagaiaqw egqvtiwdph hgapcmtcif peapapglap acaeagvvgp lpgvigslma
      301 leaikliart geplrgrmli fdglygenrl mkisrradcp tcgsghfrag
//
LOCUS       WP_285048427             213 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Paracoccus sp. SSJ].
ACCESSION   WP_285048427
VERSION     WP_285048427.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..213
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=22431
     Region          24..209
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mpnvardagn gpepraaaae tdtpalilgs asprrlella qigivpdmil paeidetprr
       61 gesprdyvrr marekaaala gsahgailca dtavvagrri lgkplddaea rrflqllsgr
      121 rhrvltsval ahdgrlrerl vettirfrpl taaqidayla tgewqgkaga yaiqghasaf
      181 aiwmqgsysg vvglplaeta sllaaigiqg kat
//
LOCUS       WP_285048539             409 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Fusobacterium necrophorum].
ACCESSION   WP_285048539
VERSION     WP_285048539.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..409
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47103
     Region          4..395
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mmkiyshsmf giklglqnme rlcerldhpe raykiihiag tngkgstatt lekilleagy
       61 rvgkytsphi lkfnerivan gvqiseeeie yyyyqvekim keekidatff eittammfsy
      121 frdkgldyvv letgmggrld atnvseailc iitnvsldht eylgdsiyki akekagiikn
      181 cpkvivadqq eeflqailee kaelinvlnk yadahytldf enffthidie gkqyrfslfg
      241 dyqyhnflca yeaakqlgis ediiqkaaek vrwecrfevv skeplvildg ahnpdgvrel
      301 vkivkqhyqk revailtsil rdkdvktmle mmteisddil ltslddnprg staeelfhiv
      361 nqpaifsiee nmkraydkli kknrklniic gsfytlikwk eevqtdein
//
LOCUS       WP_285048575             471 aa            linear   BCT 25-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Paracoccus sp. SSJ].
ACCESSION   WP_285048575
VERSION     WP_285048575.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..471
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51572
     Region          2..471
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mirfdnsyar lpegfftrtr ptpvrdpklv alnrplaerl gfdavwlagp egvamlagnt
       61 lpegaepiaq ayaghqfggf vpqlgdgrav llgevvapdg arfdiqlkga gptpfsrrgd
      121 grawlgpvlr eylvsefmaa fgipttrala avttgetvir etllpgavlt rvaashirvg
      181 tfefyaargd rqrlqlladh viarhypeas gaadllqrvv erqaatiagw malgfihgvm
      241 ntdnmsvsge tidygpcafm dgyrpdkvfs sidahgryaw neqpniavwn laqfasclvp
      301 lmgnddaava eatrivhsfp elyqaewlrr faaklgiaap rpedralier lltlmaadea
      361 dftrsfagla dgrardefka peqfdawaeg wqarirdlsd aaqvmaranp criprnhrie
      421 eviaagregd yapfhaldaa lrtpfedrpe wdgyalapqp deivrrtfcg t
//
LOCUS       WP_285048726             279 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Paracoccus sp.
            SSJ].
ACCESSION   WP_285048726
VERSION     WP_285048726.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..279
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29597
     Region          1..262
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mtrpyrsvly ipaanarame kaqtlaadai ifdledavap aekvgarell aralqadygg
       61 rarivringm dtewgegdar afavgadavl vpkvsrgadl drvaalvpdt plwammetae
      121 gmlnaaeiaa hprlqgmvmg tndlakelns rfradrlpmm aglglcllaa rahgrvivdg
      181 vfnafkdeeg lraeceqgrd mgfdgktlih paqlavanev fapseaevdl arrqieafde
      241 aqaqgkgvav vdgrivenlh vetaratlak aaaiaelag
//
LOCUS       WP_285048763             545 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Paracoccus sp. SSJ].
ACCESSION   WP_285048763
VERSION     WP_285048763.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..545
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=59698
     Region          19..538
                     /region_name="COG4425"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:443540"
ORIGIN      
        1 mfsvlpllag llflaasltp sliprdwlmq gvlagvsmaa gyvmtqflla lwralelpvm
       61 kgrpariaha vlavpvlvll grgvilsgtw qnsirarmgm pdlevnntak mlalalavfl
      121 vlfvigkaiq alfdllrlrl aryipvrsan vlglllaali vitltrdgvv nwamriadss
      181 yaaaqhltdp nvappgepwq sgsvasgidw elmgkpgrdf mlggprarai sgftgrpare
      241 plriyvglaq dkdpdtrakv aldemlrvga fdrkvlvlas ptgtgwmdpa sydaleymhg
      301 gdvatvavqy sylqsplali feteagldqt talmravydh wrhlppdrrp rlylhgislg
      361 awssmyafnp fqmmnepvag afwvgppfps tlwrqandar qpgsrfvlpe ldedevirya
      421 sqyappdrsg rewgrlrilf lqygsdpivf ydpaslwrap ewmreapapd vsprlrftpv
      481 vtqlqlavdm lvstsappgf ghtyhardyi dgwvavtape gwtaadterl kaicgqdgkl
      541 gcang
//
LOCUS       WP_285048807             390 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal-phosphate-dependent aminotransferase family protein
            [Paracoccus sp. SSJ].
ACCESSION   WP_285048807
VERSION     WP_285048807.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Koper,K., Han,S.W., Kothadia,R., Salamon,H., Yoshikuni,Y. and
            Maeda,H.A.
  TITLE     Multisubstrate specificity shaped the complex evolution of the
            aminotransferase family across the tree of life
  JOURNAL   Proc Natl Acad Sci U S A 121 (26), e2405524121 (2024)
   PUBMED   38885378
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Koper,K., Han,S.W., Pastor,D.C., Yoshikuni,Y. and Maeda,H.A.
  TITLE     Evolutionary origin and functional diversification of
            aminotransferases
  JOURNAL   J Biol Chem 298 (8), 102122 (2022)
   PUBMED   35697072
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..390
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40910
     Region          10..377
                     /region_name="PucG"
                     /note="Archaeal aspartate aminotransferase or a related
                     aminotransferase, includes purine catabolism protein PucG
                     [Amino acid transport and metabolism, Nucleotide transport
                     and metabolism]; COG0075"
                     /db_xref="CDD:439845"
ORIGIN      
        1 msfaqgravl aipgpspvpd rvlramhras pdiygpelaa enramiaglk rlagtaghva
       61 pyignghagw eaanvnlldr geralalvsg hfgrswaasa ralgieveel dfglappdpq
      121 rladrlaqdr egriravlvc qvdtassara dipalraamg ehpaflavda iaslgcepmr
      181 mdewgvdllv sasqkglmvp pgltfvwfsd rvkarahsgl atpywdwtpr aeaeelwqfw
      241 ggtppvqhif glnealhill deetlpaawa rheglaqatw aaldhwgagg hgigpliadp
      301 agrarsvtaa rlpnaaalre wtaakagvtl giglgapdpd nalriahmgh anahqllgvl
      361 avieagmaal siphgkgale aaaaeiarla
//
LOCUS       WP_285048838             198 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: LolA family protein [Paracoccus].
ACCESSION   WP_285048838
VERSION     WP_285048838.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Tajima,T., Yokota,N., Matsuyama,S. and Tokuda,H.
  TITLE     Genetic analyses of the in vivo function of LolA, a periplasmic
            chaperone involved in the outer membrane localization of
            Escherichia coli lipoproteins
  JOURNAL   FEBS Lett 439 (1-2), 51-54 (1998)
   PUBMED   9849875
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..198
                     /product="LolA family protein"
                     /calculated_mol_wt=21692
     Region          1..191
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mklktlalap vlclamafpa laekiplnei srylnslkta kadftqvnad gsistgivyi
       61 qrpqrvrfey kgdrtlvmas agnvavfdgk trgapqqypl sktplslila pnidlsrarm
      121 vtgytekknt tvvtaqdpqh peygniqmvf tanptqlrqw vvtddtgkrt tvilgdmqtg
      181 msfpastfai qneiarrk
//
LOCUS       WP_285049082             448 aa            linear   BCT 25-DEC-2024
DEFINITION  SufB/SufD family protein [Paracoccus sp. SSJ].
ACCESSION   WP_285049082
VERSION     WP_285049082.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Hirabayashi,K., Yuda,E., Tanaka,N., Katayama,S., Iwasaki,K.,
            Matsumoto,T., Kurisu,G., Outten,F.W., Fukuyama,K., Takahashi,Y. and
            Wada,K.
  TITLE     Functional Dynamics Revealed by the Structure of the SufBCD
            Complex, a Novel ATP-binding Cassette (ABC) Protein That Serves as
            a Scaffold for Iron-Sulfur Cluster Biogenesis
  JOURNAL   J Biol Chem 290 (50), 29717-29731 (2015)
   PUBMED   26472926
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Sendra,M., Ollagnier de Choudens,S., Lascoux,D., Sanakis,Y. and
            Fontecave,M.
  TITLE     The SUF iron-sulfur cluster biosynthetic machinery: sulfur transfer
            from the SUFS-SUFE complex to SUFA
  JOURNAL   FEBS Lett 581 (7), 1362-1368 (2007)
   PUBMED   17350000
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Fontecave,M., Choudens,S.O., Py,B. and Barras,F.
  TITLE     Mechanisms of iron-sulfur cluster assembly: the SUF machinery
  JOURNAL   J Biol Inorg Chem 10 (7), 713-721 (2005)
   PUBMED   16211402
  REMARK    Erratum:[J Biol Inorg Chem. 2006 Jan;11(1):128]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..448
                     /product="SufB/SufD family protein"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=47840
     Region          53..442
                     /region_name="SufB"
                     /note="Fe-S cluster assembly scaffold protein SufB
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0719"
                     /db_xref="CDD:440483"
ORIGIN      
        1 madtavlaaq vpavegkvrp gdaalaarld aldlprggft raaredaaqr lqamglpgar
       61 deywrytdpa pfnaarpepv efgadastlf tgierlnlvf vdgrfdaaas dvldvegvei
      121 eslaaaeaaa dhwaaglygr letagqvpvk rpfavlntla aaegvlirvt gkverpvhit
      181 yrrsapdadv ylhhvvklee gaeltllesg aigarsnvvi eadlgrgarf hhisakrand
      241 pklglghifa hvaaealfks fslsvngsmm rneavieiag ddavahiaaa vlgdgdtgrf
      301 hhddtvfvth aaercesrqv fkkvlkngae gifqgkilvk pgaqktdgyq isqgllldeg
      361 sqflakpele iyaddvkcsh gsttgaldet alfylrsrgv pkeraivllv lsfladalde
      421 iedqrlrddi lgrledwlta ragnsata
//
LOCUS       WP_285049016             200 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Paracoccus sp. SSJ].
ACCESSION   WP_285049016
VERSION     WP_285049016.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..200
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21328
     Region          1..195
                     /region_name="HAD_sEH-N_like"
                     /note="N-terminal lipase phosphatase domain of human
                     soluble epoxide hydrolase, Escherichia coli YihX/HAD4
                     alpha-D-glucose 1-phosphate phosphatase, and related
                     domains, may be inactive; cd02603"
                     /db_xref="CDD:319790"
     Site            order(7..11,107..108,141,165..166,169..170)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            136
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mksvifdlgg vlidwdpala fadvftsrae aeawmkrigf adwnriqdgg rsfaegvaaa
       61 ravhgdearh lagyplafpv aiektvpgtw aiaeallarg vplyaltnws aetwphalel
      121 hprlgglfad ilvsgqvgvl kpepaiyrll mdrnglvaed cifiddsaan aegaralgid
      181 aihftgaeal geelarrgvi
//
LOCUS       WP_285049280             347 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Paracoccus sp. SSJ].
ACCESSION   WP_285049280
VERSION     WP_285049280.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..347
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36395
     Region          1..347
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mnfasdnagg vhprimaala aaneghvtsy ggdaitraaq drlrelfdap eaavhfvasg
       61 taanalslsl lspgwgkvfc hadahvqtse tgapefftgg aklvpipgag gkitpealae
      121 allangrdsv hagrnaaltl tnatewgtvy spdeveslaa iacdaglglh mdgarfanal
      181 agldvapadl twragvdals lggtkngcmg veavlifdpa rseefefrrk ragalvskhr
      241 ylsaqilawl egdlwlqlar hanamahela lglarlpgvr idqrvesnav fatipselhr
      301 rayeagighh lwphtqdaae depvsirlvc gwdtriedvt galqala
//
LOCUS       WP_285049427             291 aa            linear   BCT 25-DEC-2024
DEFINITION  TPM domain-containing protein [Paracoccus sp. SSJ].
ACCESSION   WP_285049427
VERSION     WP_285049427.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Sirpio,S., Allahverdiyeva,Y., Suorsa,M., Paakkarinen,V.,
            Vainonen,J., Battchikova,N. and Aro,E.M.
  TITLE     TLP18.3, a novel thylakoid lumen protein regulating photosystem II
            repair cycle
  JOURNAL   Biochem J 406 (3), 415-425 (2007)
   PUBMED   17576201
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..291
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31539
     Region          26..>197
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mlftllwlal lapahaqtlp dwqdlrvndf aglltpedaq aldtalstld aqtgiegtvv
       61 tltdrarygg tdgleafatr lfdhwgvgdg arndgfmvlv laddrearie lgrgyendad
      121 ilaqkimrnt mlpafrdgrm srgirdgtqa vieliarpva agqplraper gmmdrivpfl
      181 fggawllilg aiarqlwhrn rcpqcgrrgl etrvapletp lpegghmvsh ddvtrrcpac
      241 gwsetrqrlr rqtvwygpng avlrskanrg aggasgfggg ssrgggasgr w
//
LOCUS       WP_285049477             550 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paracoccus sp. SSJ].
ACCESSION   WP_285049477
VERSION     WP_285049477.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 550)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 550)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 550)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..550
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58126
     Region          42..550
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mtpelaqrpr vragvgwqaa alavaalvll pvlalglfal qgspglwahl vsnvlpvaar
       61 qtvillvgvg iivatlgtat awlvaacdfp grrffgwall lplavptyiv ayayldllhp
      121 vgpvqgairg wlgysspref rlpdirsmpg cilllglvly pyvylpvral famqagnlld
      181 agrtlgagpv atflrvaipl arpavaigta lalmeamndi gaaeflgvrt ltvsvystwi
      241 nrsdlpgaaq ialamlaitm alvmlerrgr rrqryaagaq rsqplrrtrl rgwrawgaml
      301 vcalpvtfgf aapawylaga awaryrfagl sprileeagn taffaglatl valllglvvt
      361 gaarmrpgtl trtmvrlstl gyavpgtila igllpviala drqiaavsqa llgvgpglll
      421 lgsgaaliya yvarflaias ggieaglsrv prsldhvart lgrspgqvfr evhvpisrpa
      481 laasgllifv dcvkelpatl llrplnfetl sthlygeaar gtyedaaiaa liivligilp
      541 vivlartirr
//
LOCUS       WP_285049515             448 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Paracoccus sp. SSJ].
ACCESSION   WP_285049515
VERSION     WP_285049515.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..448
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=48611
     Region          1..433
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mtprvllved deqmrsstaq alelagftve alasgeeala lagsgfagav vsdirmpgmd
       61 gmtllgrlhe vdpeipvilv tghaevplav eairggaydf iekpfvvqel atvirraidh
      121 rglvlenrrl ravagkrddv earlpgrtqv mvdlryrlra igasdadalv igptgagkev
      181 vartlhdisa ragrpfiain caalpealie selfghepga fpgalrpryg kfeharggtv
      241 lldeigsmpl elqakllrvl qertitrlgs ndsvpldvrf iavskvdlee lvaqglfred
      301 llwrlnvavl hvpplsarre dipllflqll reaaarhnlp ereapaafls glaakewpgn
      361 vrelrnlaer fvlglegael gpeqgarlae rvaefersli agaiaahggk lrpvyetlgi
      421 srktlyekmq kygldrrlil daaeddag
//
LOCUS       WP_285049586             446 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paracoccus sp. SSJ].
ACCESSION   WP_285049586
VERSION     WP_285049586.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 446)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..446
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=46676
     Region          126..438
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 milprdsira rlialaallt gvalvggyla iaailedfit grfdaeteav adaliagati
       61 daegrlaagp gpadprfqmp lsgwfwqltq dgqvmaksps lfdnvlnppe adfqggpglg
      121 paeeplrvar haftlpdsas alavtvtapr aeidaamarl rrplavslav lglalaaasv
      181 lqvvaglqsl drlgrdlrri rsgqaealpl pavaelrpva teinalleqn ravlarareh
      241 vgnlahslkt plaaldnalp sehpghglia rmdrqigwhl rrarssaapr llgqrtpvap
      301 viqdillvlg gpirdsglra eiradadpaf agerqdleem ignlvenavk waknrvritv
      361 llqgdqlril ieddgpgmsd edharaltrg arldetgppg tglglaivad laalhggalv
      421 legsdlgglc aglrlpaaap pvawrg
//
LOCUS       WP_285049616             436 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Paracoccus sp. SSJ].
ACCESSION   WP_285049616
VERSION     WP_285049616.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..436
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46861
     Region          35..400
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mnllfsndrl geyppslyaa trdplpafpq qrgeeradvv vvgagytgls aalhlaeagr
       61 dvvvleahrv gfgasgrngg qlgsgqrlev ddlesmagve tahrlwdmae eakrltrdla
      121 aragvpvadg iahafrkpve fdharamidr lsrdygydri ealdrdafra lvpsdayaag
      181 eldhgaghlh plnlvigmar ladaagarir elshvhhirh arkpgeksvv qtgkgrvicd
      241 hvilaangyl gnldthvaar vmpinnfiva teplgaraae vltrpigvhd tkfvvnywrl
      301 dpetrlifgg genvsyrfpt diaakvrkpl leiypnladv althawggtl aitmnrmpcf
      361 arpspnclsa sgysghglal atlagklmaq avqgqsegfd tmaalpspsf pggaalrwpl
      421 lvagmswysl rdrlgf
//
LOCUS       WP_285049683             597 aa            linear   BCT 25-DEC-2024
DEFINITION  relaxase/mobilization nuclease domain-containing protein
            [Paracoccus sp. SSJ].
ACCESSION   WP_285049683
VERSION     WP_285049683.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..597
                     /product="relaxase/mobilization nuclease domain-containing
                     protein"
                     /calculated_mol_wt=66199
     Region          3..597
                     /region_name="VirD2"
                     /note="Type IV secretory pathway, VirD2 component
                     (relaxase) [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3843"
                     /db_xref="CDD:443053"
ORIGIN      
        1 mssddrefri rpgrprstra prsgsfvnqv lratrkagpv rkagpdggss ssgrpvrtgh
       61 stfgrgrasf grsrlfspqr rvvvkarvvr hkgrsfrsap mtahlaylkr egvrrddsdg
      121 lmfdatsdda ddsgfaercq ddrhhfrfiv spedasdmtd lraftrdlvk qmqadlgtkl
      181 dwiaadhwnt dnphvhllvr gadetgkdlv isrdyigygl rsraedlvsl elgprqehei
      241 rfalerevta erwtrldati rrqademgfi dlrldapirg eptgrspepr rlmigrlqhl
      301 ekmglatsag pgewmlglev ertlrdlgrr gdivsrmhra fagrgeergv ldfvtdsgrd
      361 gppvigrlvd lglhdeltge ayavvdgvdg rahhirlrgi eafdqapplg givelrrfgg
      421 pedpnptlwl ahrsdldlqs qiaapgatwl dhrlverrpm plamggfgke vreamdarae
      481 hlvgeglarr eggrilvrrh llatlrrrel davgaelark tglrhvqara gdnvagtcgr
      541 qlslssgrfa viddglsfql vpwsrdlegq igrhvsgvak pgdgidwslg rrrdlgl
//
LOCUS       WP_285049881             411 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Paracoccus sp.
            SSJ].
ACCESSION   WP_285049881
VERSION     WP_285049881.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..411
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43476
     Region          1..387
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mkprlllpvl vafaigsmap aqpaapaqdd sslgqaaqea araadmlrea vgqldealte
       61 ddqvasltrm irayeqgmaa lreglrragi reqeiraefd arrerlgrvl gvmtsmqksp
      121 etmlllhpsg pessaragmi lssvapglet earemqqkle eirtvraiql saantlaqgl
      181 dqvqearrll asavtdrssl pvrfgedpke ltalvqsadt ldafasgivg meqdvgppma
      241 dfegaqgsla lpvlgrvlrr ydepdaagvr rpgmviatsp aalvttpwpa tiryrgplld
      301 ygnvmivepa rgylmifagl aqvfgetgdv lalgepvglm ggqeppaqef gaefvanaaa
      361 gggagqtetl yvelrkgket ldpaewfvmn pivgeatdgt grnatgqdgt e
//
LOCUS       WP_285049940             487 aa            linear   BCT 25-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Paracoccus sp. SSJ].
ACCESSION   WP_285049940
VERSION     WP_285049940.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..487
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=51152
     Region          11..487
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mtrsfdpdtl dlprghfiag ehvadrgrla mhrpsdgaaf gespvadadm vdravaagra
       61 alaasgwgcg vprdrtrall kwadlieaea etlarfeaac strpvvqlpa gdiavtaeqi
      121 rffaemadke gsdlvptrda slgmtvdepy gvvgaitpwn fplsmagwkl apalaagnav
      181 vlkpsemtpf stlymaelsv ragipaglvn vvlgdgpvtg naitghpgig kvsftgstga
      241 gqaimgniar ngvkpmtlel ggkspqivfa dadldlaadc iarsitfnag qacvagsrvl
      301 vaaeiaeala erlivrmadh rpgttwdaet qyspiiserq iaridgivqa avaqgaevla
      361 gaarldhpgw fyaptllagv apdspavtee ifgpvltlep fadeeqavam adhptyglca
      421 giftrdlsra lrvmrrieag tvwinrygrs rdhilptggy kssgigkdlg raayhanrrq
      481 ksvlidl
//
LOCUS       WP_285049989             339 aa            linear   BCT 25-DEC-2024
DEFINITION  FGGY family carbohydrate kinase, partial [Paracoccus sp. SSJ].
ACCESSION   WP_285049989
VERSION     WP_285049989.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Yeh,J.I., Kettering,R., Saxl,R., Bourand,A., Darbon,E., Joly,N.,
            Briozzo,P. and Deutscher,J.
  TITLE     Structural characterizations of glycerol kinase: unraveling
            phosphorylation-induced long-range activation
  JOURNAL   Biochemistry 48 (2), 346-356 (2009)
   PUBMED   19102629
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426119
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         <1..339
                     /product="FGGY family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
     Region          <1..338
                     /region_name="GlpK"
                     /note="Glycerol kinase [Energy production and conversion];
                     COG0554"
                     /db_xref="CDD:440320"
ORIGIN      
        1 lafgtvdswl iwnltggrvh atdatnaart llyniaenrw daeicalfdi pmpllpevrd
       61 caadfgmara dlfgreipil gvagdqqaat vgqacfqpgm mkstygtgcf allntgeemv
      121 asknrllsti ayrlegrtty alegsiliag avvqwlrdgl glirsaaetq glaeaadpgq
      181 elvlvpaftg lgapywrpdc rgavfgltrn sgpaelaraa lesvgfqtrd lweamradwp
      241 gaaagvlrvd ggmaasgwtm qfladilgap vdrprvtett algagylagl qaglcpppgd
      301 fardwalerr fepamaeger earygrwkqa vkatmgvag
//
LOCUS       WP_285049993             635 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Paracoccus
            sp. SSJ].
ACCESSION   WP_285049993
VERSION     WP_285049993.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 635)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 635)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..635
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=68759
     Region          28..603
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mlfrtpasll aatalllpaa atgqegqapv mldpvvlsgg lspvaesayg raysiltaed
       61 lrqrgfvtvq dalrdlpgla vtstgetltk vrirggeanh vlvlidgvea nspgngdyvf
      121 sglltedver ievlrgpqst iyganaaagv iaittrrasv pglsygggie igglgtraas
      181 ahlramgerg qisfsaatrr tdgedasrtp ggdtefnnre tltlggsydi aeavtagftl
      241 rrtwqeygyd raidpvdspd dhvidtphta drnetygslw ieaealggrl lnrfavsgsn
      301 qatdhfndsv pdyddasrlr dfrytgtwal dggnarnsaq klnfavqkkr eiyessyapg
      361 gryerdtrsl aleyqgqfdn gigiqaglrr dfnddfrnat twniagawql pdrdlrlraa
      421 agkaivnptm felygyapgs ysgnpdltpe tsrsyeigad wsfaagraal gatlftskve
      481 dmivgagtts qniagtstrk gfeadlhyea tdwlrlgaty tytdartedd dpiprqprhq
      541 lglratgdfa ggrgsatadl ryvagnydee wfrswtpptt elpdfvtvnl aaqydltenl
      601 rltgrvvnlf drdyseawgy ygqgrtfyag ltaqw
//
LOCUS       WP_285050099             506 aa            linear   BCT 25-DEC-2024
DEFINITION  Y-family DNA polymerase [Paracoccus sp. SSJ].
ACCESSION   WP_285050099
VERSION     WP_285050099.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..506
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=54910
     Region          7..344
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(10..11,14..15,53,56,110..111,163)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(108,111,183..189,218,247..252,280,306..310,312)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mtgrrivsis lprlaieswq sratrrgdaw pediplalaa pgphgpviha anraaeraga
       61 rigaravdsr aicpalhiep aepkrdaarl arlafwarrw gpystpdgdd giildttgaa
      121 hlfggeaaml aeiqagfara gltarpalap trgaawalar fgperaictd plpalaplpv
      181 aglrlsgetl lllrrlglkt igdlaaiprl slmrrfarae pqdnplvrld qalgraaepl
      241 dapepapefa aearlaepvm dpsdwlpgll adlcaqmaaa drgcrrlcls vfrvdgerrd
      301 irvamaaptr dpghllrlfd grlerldpgy gfdlirlaae aveplaqsqp gldgaaptgl
      361 alarlvdrla arfgaqaisr plpreshvpe raeapgppla atpaplarpd rpirllnppe
      421 eirvlyaipe gppaqfvwrr qtlrvarhtg periapewwh drpgtrlrdy frieddsglr
      481 lwiyreglvh dgrggaprwf lhgifa
//
LOCUS       WP_285050111             965 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Lactococcus garvieae].
ACCESSION   WP_285050111
VERSION     WP_285050111.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus garvieae
  ORGANISM  Lactococcus garvieae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..965
                     /organism="Lactococcus garvieae"
                     /db_xref="taxon:1363"
     Protein         1..965
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=100549
     Region          <42..877
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mskyykkrse kdkngksral hhyfklvlya fsffilspls pvfngipsfg tlsaeasitq
       61 qtdgsgitwn litagndint lattalpgat lyikaandlt lgvtavlpln ltlvfdmdgh
      121 alyntgaavi tpsvgntitf qnerivstgt tnsttvpspl gigtvtgvyn yyyglfsatn
      181 isgvsitykn viqdlgtitt wgaggqpfyn igssvnfsgt nyfnynsgqe fmegtginvl
      241 dgtttikhss ggnaplwaqs aasinvaaga tldftgsstg rgfiyldntp tftinnngtl
      301 klnmsgansn nfysntgmss itmnyganss ttitapgffd ynatggafkt tigqgasfdy
      361 stgntsnafl gtlattdsft lnsakhvrln tnktsgssil gtdasampfv lnasspsaya
      421 ingynsagvs sllasptsga fgvtetfhsn ladlskltgq kiptaseitt yqnsaqlefn
      481 lvspaqanfs yawaadvpgq nggagtllgq lparvseqgt vggaltaptl saapkgyyis
      541 gykapngtiy ttlaaalatv nnvfgttsnt tspdiympst ndfqvilsaq eqtfyinygy
      601 aftnfgnvpp fpanaytqkg ltgapltisg lgvaptgyhy savlnntasa widqsnpetg
      661 gantptpyya sislaltaai tqqnggmyfg tsslstppti nnqgafdnnv mvmltanaei
      721 anytygwani tpgyngnagq iygnlpsqat skggfgdtia rdtsginspg ntyqtfvapp
      781 tdnalsgysv avrapngity tsdpnavass tvvktttplt tatqantfke gaaatnfvit
      841 yaplanklsw hytydssisn ppsapadivq tgvltgaplt dpkatapngy fiegyqypgd
      901 tkiyrtiael qtahfsgtgd itinillakn fvlpytggsg qfgiilasat laflalafyi
      961 fkkkd
//
LOCUS       WP_285050150             316 aa            linear   BCT 25-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Paracoccus sp. SSJ].
ACCESSION   WP_285050150
VERSION     WP_285050150.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..316
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=33781
     Region          1..308
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(7..8,10,50..52,72,100..101,104..105,107..108,111,
                     115,117,125,127,129,131..137,139..143,161..162,166..167,
                     264..265,272,278..284,286..289,291)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(51,73..75,98,235,282,285)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240626"
     Site            order(74..75,102,151..155,174..176,179,205..207,211..212,
                     233..235,259..260,282,284..285)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 mkllvtrrmt qaaehalsar feteildrkd glgvdeaaka ladydaimpt lgdrftaeaf
       61 qgqprcrlla nfgagynhid vaaaaaagia vtntpdavte atadialtli lmtarrageg
      121 erllrrgewt gweptqllgr hvtgctvgii gmgrigkaia rrchfgfgme vlfhnrsvvs
      181 slnfparqva dldellvqsd faiiavpgga etrhmigahe lerlgprsyl iniargdvve
      241 eaalaealaq griagagldv yefeprvspa lcamenvtll phlgtaaeev rtamamramn
      301 nlvafaegqa lpdrvn
//
LOCUS       WP_285050332             338 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Paracoccus].
ACCESSION   WP_285050332
VERSION     WP_285050332.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..338
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34549
     Region          1..333
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 maseitvagg gifglacawe ltrrgrkvrl feavrigaga sgghvgalap hapenwnakk
       61 qvqldaliaa agwwaevgaa ggvdpgyart griqpvpega qarmaervea arahwpawag
      121 meltdaplgp lvpasasglw lvdrltaris prragaalaa airaqggeiv egqaapdtpa
      181 iwatgvagla pfggngvkgq sallamdlpd apqafadglh vvphadgtva igstserdva
      241 dlgtdgqlea lidkaralcp vlrdapvvdr wagirpraas raplvgpwpg rpghyvangg
      301 fkiglamapa cagmladlil egrdtiprdf rpelragg
//
LOCUS       WP_285050463              96 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Paracoccus sp. SSJ].
ACCESSION   WP_285050463
VERSION     WP_285050463.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 96)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..96
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10578
     Region          31..90
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
ORIGIN      
        1 msdafksiet glqealahar gekvglvhei elpepdvqai rartglsqsd farsigirkg
       61 tllnweqrrr spegparvll alidkdpqiv qrtlvr
//
LOCUS       WP_285050507             313 aa            linear   BCT 25-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Paracoccus sp. SSJ].
ACCESSION   WP_285050507
VERSION     WP_285050507.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..313
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=32168
     Region          23..311
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mkqfvlaslf aaatalpama dytiiapanp gggwdqtart mqtvmqeegi sksvqvqnvp
       61 gaggtiglaq fasqnkgnpd alivggyvmv gailtnnspv slkdvtpiar ltgeyeaivv
      121 paaspiqdva gliealkadp gavswaggsa ggtdhiavgl iakaagvdpt kinyiaysgg
      181 gealaailgn qvtagisslg efeaqiqagt lrllavtape rlegvdaptl qeagldvvle
      241 nwrmvaaapg lsdeqkakvi adiekmakse nwqkqlsdkg wmdtylagpe feaqleqdvt
      301 steailkdig lvk
//
LOCUS       WP_285050689             642 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Paracoccus
            sp. SSJ].
ACCESSION   WP_285050689
VERSION     WP_285050689.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 642)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..642
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=69663
     Region          3..610
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mtsassiats iqdapasitv idqsdiqakg arhlqdvlrt vpglnltrgn dgnsqvsfrg
       61 lsssrtltli dgkrvssrnt farhyqgdlq ivpldaieri evvrgpmstl ygsdamggvi
      121 niitkkatdt wsgslttdfg fadenstads rsisgyvsgp lgenlslsaw gklaeidape
      181 epyayspgqg gslsplyasn gtrtktlgar ltwtpqegme wgaeaqtsvd nylsdagahd
      241 tnevtkksig ltnewqlgqg hlssylryet sgnetwnstd evwndpidyd tttfesryts
      301 qtnlagrqld ytigglvahe klsdpqttsg aliegsvnta aiyaegrlqa tnalslttgl
      361 rvdhherfgt hvtpriyany dfgnglmlkg gysqafvapd lrnlnpnyqm gsrgngckpy
      421 qgpctiignp dlqpetsdnf eiglnyqgeh sswevtafyn dvedmisarr irpatptesa
      481 lfqrdnfdyg ktagiefgld hqinddltwt tsgtyiakse fkygdfdtay pmattpkwni
      541 ttglawqand rlnlsgevty vgkqagyvve dglvvgegeq asvpagqnsk ayylvnvaaa
      601 ydlndmatln vgidnlfngq pesdvsyren grlftlgitt rf
//
LOCUS       WP_285050826              88 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Paracoccus sp. SSJ].
ACCESSION   WP_285050826
VERSION     WP_285050826.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..88
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9074
     Region          1..50
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(3,7,32)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(6,31)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(13..14,25,28,32..33)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mlteaiksmg lkravvaenl gigraylsgl esgkkkpsle lavkiarltg gavpveswvd
       61 pevsaipqpa ataaqpqehp hvpdlqsp
//
LOCUS       WP_285051095             147 aa            linear   BCT 25-DEC-2024
DEFINITION  thioredoxin family protein [Paracoccus sp. SSJ].
ACCESSION   WP_285051095
VERSION     WP_285051095.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..147
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15437
     Region          8..>46
                     /region_name="PqiA"
                     /note="Intermembrane transporter PqiABC subunit PqiA [Cell
                     wall/membrane/envelope biogenesis]; COG2995"
                     /db_xref="CDD:442234"
     Region          44..140
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 msgtdiqiac tacgatnrlp pgrdprearc gkcraalfsg qpadvdgamf qrqvgrnsip
       61 vlvdvwapwc gpcqmmapef araaamlepg mrliklnsea epqaaatlgi rgiptlllyr
      121 ggreigrqsg amdaasiagw araqlrg
//
LOCUS       WP_285051145             663 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Paracoccus sp. SSJ].
ACCESSION   WP_285051145
VERSION     WP_285051145.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..663
                     /product="PhoX family protein"
                     /calculated_mol_wt=72182
     Region          29..658
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mteqhpsrhv frtsqleead gpghnptdnr tmgeiiaarf srrgflkgsm aataisatvs
       61 pfallaadea raqdavegsa fsfpeveagv dadhhvaqgy dadillrwgd kvfadapdfd
      121 pknqseaaqe rqfgynndfv gfipldgadd rgllvvnhey tnehlmfpgi vtvedgkiav
      181 aeatearvdi emaahggtii eirkvdgkwq pvldgalnrr itaktpmeir gpatgharmq
      241 taadptgtrv lgtinncagg vtpwgtyima eenihgyftg alpeghreae nykrmgiped
      301 syawgrfhdr fdigkepnep nrfgwivevd vmdpnsvpkk rtalgrfkhe gaasalakdg
      361 rvvfylgdde rfdyvykfvt agrynpddra anldlldegt lyvarfdedg sfvwlplvhg
      421 qgpltaengf esqadvliet rraadllgat pmdrpediep naetgrayvm ltnntkreea
      481 naanprvena fghiieiled ggdlaatqgt weillqcgdp svaevgatfs tattangwfg
      541 mpdncaidsd grlwvstdgn spkdtgrtdg lwavdvegaa rgtsrlfyrv pvgaemcgpc
      601 ptpdlttffv avqhpgdgge dweghgrpsy yedlstrwpd frddmpvrpa vvaitkqggg
      661 rig
//
LOCUS       WP_285051358             109 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: DMT family transporter [Alphaproteobacteria].
ACCESSION   WP_285051358
VERSION     WP_285051358.1
KEYWORDS    RefSeq.
SOURCE      Alphaproteobacteria (a-proteobacteria)
  ORGANISM  Alphaproteobacteria
            Bacteria; Pseudomonadati; Pseudomonadota.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Alphaproteobacteria"
                     /db_xref="taxon:28211"
     Protein         1..109
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11285
     Region          6..107
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 msqglawlll iiagfldvaw aismkyaegy trpgwtilsl allaafvyll grvlevlpvg
       61 tayaiwtgig aagtvllgit lfgetinlmr lggvalivvg ivalklapa
//
LOCUS       WP_285051463             196 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II [Paracoccus sp. SSJ].
ACCESSION   WP_285051463
VERSION     WP_285051463.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..196
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=20791
     Region          2..189
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 millidnyds ftwnlvhymg eagadvvvrr ndalsvdeal emgaqgivis pgpcdpahag
       61 iivpliraaa erglplfgvc lghqaigeaf ggkvvrasri vhgktdaish dgtgvfadlp
      121 spltatryhs ltvepeslpd clrvtataad gtimglahrt lpvegvqfhp esiaseyghd
      181 mirnflrrcs nldraa
//
LOCUS       WP_285051473             423 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Paracoccus sp. SSJ].
ACCESSION   WP_285051473
VERSION     WP_285051473.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         1..423
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45979
     Region          1..408
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 msvekidtlv vgggqagvam sehlgkagvp hlvlergria erwrserwds lvangpawhd
       61 rfpgmefpgd pdafvakeqv adyfaayaek lgapircgve vrevrrnagr pgfavttsqg
      121 vieanrvvaa tgpfqkplvp alipadagvt qlhssgyrnp dqlppgavlv igagssgvqi
      181 adelmragrk vylsvgphdr pprsyrgrdf cwwlgvlgkw dmaapapgte hvtiavsgar
      241 ggetvdfrrl gnrgmvllgr tegygdgsln fspdlrrnld rgdenylsll deadahiasn
      301 gldlpqepea rkrepdpdcv tdpilelnla gagiatviwa tgfavdfgwi radafdergr
      361 plhqrgvsvq pglyflglpw qsrrgssfiw gvwhdarhia eqiviqrkys dyqgkaqrtl
      421 qea
//
LOCUS       WP_285051536             233 aa            linear   BCT 25-DEC-2024
DEFINITION  FGGY family carbohydrate kinase, partial [Paracoccus sp. SSJ].
ACCESSION   WP_285051536
VERSION     WP_285051536.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. SSJ
  ORGANISM  Paracoccus sp. SSJ
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Yeh,J.I., Kettering,R., Saxl,R., Bourand,A., Darbon,E., Joly,N.,
            Briozzo,P. and Deutscher,J.
  TITLE     Structural characterizations of glycerol kinase: unraveling
            phosphorylation-induced long-range activation
  JOURNAL   Biochemistry 48 (2), 346-356 (2009)
   PUBMED   19102629
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426119
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Paracoccus sp. SSJ"
                     /db_xref="taxon:3050636"
     Protein         <1..233
                     /product="FGGY family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
     Region          <1..233
                     /region_name="GlpK"
                     /note="Glycerol kinase [Energy production and conversion];
                     COG0554"
                     /db_xref="CDD:440320"
ORIGIN      
        1 gtgcfallnt geemvasknr llstiayrle grttyalegs ifiagavvqw lrdglglirs
       61 aaetqglaea adpgqelvlv paftglgapy wrpdcrgavf gltrnsgpae laraalesvg
      121 fqtrdlweam radwpgaaag vlrvdggmaa sgwtmqflad ilgapvdrpr vtettalgag
      181 ylaglqaglc pppgdfardw alerrfepam aegdretryg rwkqavkatm gva
//
LOCUS       WP_285051916            1431 aa            linear   BCT 25-DEC-2024
DEFINITION  autotransporter outer membrane beta-barrel domain-containing
            protein [Fusobacterium necrophorum].
ACCESSION   WP_285051916
VERSION     WP_285051916.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10657847
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1431
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..1431
                     /product="autotransporter outer membrane beta-barrel
                     domain-containing protein"
                     /calculated_mol_wt=165497
     Region          1162..1412
                     /region_name="Autotransporter"
                     /note="Autotransporter beta-domain; smart00869"
                     /db_xref="CDD:214872"
ORIGIN      
        1 mrlkkrtlil aliiaanssy akeyyfeket egeeknteik kileewkdks flakelkeki
       61 kemkpdssme vitegdklyi rtkekpeeki lvgkrsetyq lekgeapdyr vahdaehqdd
      121 pierggyega lrivdqenrq ngisnryfna edkmektfdn vnfvpvaqyv nngeqgmfss
      181 dsiktnknpm sgyhsfeewe kltknpekmk kfieenrdkf ssvrksnqkr fffgngntvk
      241 diimtgkenf dkkmqekenm qytftgtyqn idntkknqld ismkdfkeki egksreevak
      301 flktkleekq ksdtgnekik dkkfeikdgd lytvegdksw kvywtlepvt vlaetmsekl
      361 kdevfskiyv yhekkegkds agrilytkdg silvedtldy nkdmidvgkl swgtvskdkg
      421 leeylkekke kkveeksslq eemkkfseem kealdkkskl eeekekcekk ceakimpepk
      481 dnggqdidws klddtmseek idqeypnlnq egkdylkayv akkkvekelt tleekitkrk
      541 nemkdkyeks giddkliivn nlgknvefrg rgtilgtvdl gegynelsig gnltgrygtn
      601 iimgadssfk gikkvslgqd idddkfnega vsgtasltld idptiknsqg hltkhllhnt
      661 qdknilflky gsyglepnsy pddfnmqmml srigengvid mgrklshqvl dtkngvhrtl
      721 hinmtsdsia hhlyqektee nsenkdkntl lkvevkdkik rlseeendvy gsivnskrlg
      781 ilhptltntn kkisfsykyg mnyedknlkl vqaikdgknl eeilehnsef hlneeqkeka
      841 kkylediqdk knkdlkyvhe kmetnkkevq qtkeelekkq keekeisdki qkmeeelkkl
      901 pemrsseeyk klnpnqklek alqemdfsdm hkqldsvsnh knfnqekenh pcyqklktfk
      961 ealdnsalee wkkkypdspl ikeldekikg fnfdfgqytn cteskwtrny cakylkqgea
     1021 kaeeidailk qltneekyke kiekekketl epkqkevaek ktllenkekt meeetetaly
     1081 akkylkrnkd yqklrnllyy tlreeealse lkemisqmkd tniyskvnki aknelstytn
     1141 lpfdknrsls kktqyarggf isartvqnnf kgniytaygl yekqldknsy lgvmfggant
     1201 nhtlthnkrs akttptnstv kgvslytgay ygkklyeeld wisgmgvqyg nykverhlkn
     1261 nyqgldsngk vkvgawttys glvlhyplqe dvevqlkgil sysylnqgki kesnglnldi
     1321 qskdyhylds elgvslnktl ydfgvksnls agisaisgla gyknkdlkak ihgstssfni
     1381 kgdktkkdav klfmdynvqm dagfnygleg tyisnqdesn vkigikagys f
//
LOCUS       WP_285052030             128 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Fusobacterium necrophorum].
ACCESSION   WP_285052030
VERSION     WP_285052030.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..128
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=14529
     Region          2..124
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mgrknrrgal kpdltplidv iflliiffmi sttfnnygtf pielpsstve skkenkavei
       61 ivdkhgrfyv ntegknqevt ledipnhlqg veevtisadr dmkyqtvmnv mtkvkeqnia
      121 nmgltfye
//
LOCUS       WP_285052061              74 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Pectobacterium
            carotovorum].
ACCESSION   WP_285052061
VERSION     WP_285052061.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium carotovorum (Erwinia carotovora)
  ORGANISM  Pectobacterium carotovorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 74)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Pectobacterium carotovorum"
                     /db_xref="taxon:554"
     Protein         1..74
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=8658
     Region          8..70
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mnqfkhyqqp aervireaec rqltgicrtt rymmekegvf parrklggrs vgwmlseile
       61 wqrqqpkvtt hpia
//
LOCUS       WP_285052119             341 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Fusobacterium necrophorum].
ACCESSION   WP_285052119
VERSION     WP_285052119.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..341
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=39845
     Region          73..341
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 makykrrang cgtvvklsgk rrkpwaalsp akmsyetekv krevigtfet rqeadkalll
       61 ydpketerrk llfktiyekw weghvkkvee ntiktyhsiy nkylskldnv sfkelnalfl
      121 qdfidkvdsa ssqklvkail agifkyamkh eivdkdfskl ldmkkqvavl erknftkeem
      181 ailfeyserk iakaililsy tglrisefln lnkevinngy mkiiksktea grnrivpihs
      241 kiqgpidell aenrkylytq dedkkvtyar frkefedfmk evkmnhtihd trhtfsnmad
      301 dtkmnkkila qlvghknvkt tintyvhkdl ealrkaidli n
//
LOCUS       WP_285052161             552 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Kingella kingae].
ACCESSION   WP_285052161
VERSION     WP_285052161.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 552)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..552
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=60987
     Region          10..550
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mtkhslnrpv livddesdir dlmemtlmkm glavdtaegv vaakkkldan ryslvltdmr
       61 mpdgsglsvv ehivaqnndt pvavitaygn adqavqalki gafdylqkpi tlaqlrtlvk
      121 saikvqdesk qpapisqpkt vtpepepakv qaalsheaav sdwgdsadwq aaadsltedy
      181 tqtakrstta raptrrknas sknitpddvv pavastnsgv tlqsdadlpr llgssqqiet
      241 vrqmirklas avvpvyisge sgsgkeqaar sihelsprkd apfiavncga ipenlmesef
      301 fgykkgsftg adqdrlgffq hahggtlfld evadlplamq vkllraiqek avrrigdaqe
      361 vkvdvrivsa thknlsalve sgafrqdlfy rlnvvtlnmp alrdmhedlw gliqhilrrh
      421 qgdsevamte dareallryn ypgnfrelen ileravalcs nrlidvddlq invdplnqid
      481 peslegnqhq vvnglpnfqm gntqiqdyld dierqilqya lrltqnnrtq aakmlgisfr
      541 smryrlerln ie
//
LOCUS       WP_285052230             199 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Fusobacterium
            necrophorum].
ACCESSION   WP_285052230
VERSION     WP_285052230.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..>199
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
     Region          13..>189
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mlekwqgvte knrkiyekyl nscrsnneet wdttyktyvs rmykflkwln keknryllsq
       61 dtlenaveii eeyknycrec gnskrtiana ivtissfydw tvrrkmikyh pfkdrlekqk
      121 itdrdstrds yyltteqilt arlymkvehk kfdlqdrilw elfidsacri saiqaltleq
      181 leleggyfkn viekegyvv
//
LOCUS       WP_285052248             476 aa            linear   BCT 25-DEC-2024
DEFINITION  MBOAT family O-acyltransferase [Kingella kingae].
ACCESSION   WP_285052248
VERSION     WP_285052248.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Hofmann,K.
  TITLE     A superfamily of membrane-bound O-acyltransferases with
            implications for wnt signaling
  JOURNAL   Trends Biochem Sci 25 (3), 111-112 (2000)
   PUBMED   10694878
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004295
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..476
                     /product="MBOAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53892
     Region          1..476
                     /region_name="DltB"
                     /note="D-alanyl-lipoteichoic acid acyltransferase DltB,
                     MBOAT superfamily [Cell wall/membrane/envelope
                     biogenesis]; COG1696"
                     /db_xref="CDD:441302"
ORIGIN      
        1 mpllsieftl fillflpiyw laspsvktqn wlllaaglgw lysvgawlla pvvvlttvvh
       61 glasslqsnr yrktklwagi afavgglcff kyydffrpai qshlgqnnii divmplgisy
      121 yvfqsiayll hsyrfpdaer fswhelllhl sffptitsgp iirshafksi ngehmgaleq
      181 irsssprsmi rpslaiglil lgiakkwwla gcladgwvsp vfanptqfdg lsvlaaiygy
      241 tfqlffdfsg ysdlvigmam llgfklpynf aaplrahnlr nfwdkwhitl stwirdyiyi
      301 plggsrggwv rtqinlllam vlsgiwhgyg wnfllwgalh gvalvllnlg dkiigrnwls
      361 hskwtrwlai iitfhfvcft fvifntrtlg daqmvftalf anqqgwvind waniallagf
      421 glmialypll lrlfhiavrg leklpmwlwf ipislililv ivfaptgipn fiyanf
//
LOCUS       WP_285052330             133 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Fusobacterium necrophorum].
ACCESSION   WP_285052330
VERSION     WP_285052330.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..133
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15460
     Region          2..130
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mfqviykiqk edmnvgnhvg nekslvffek vrkqwleshg ytelclgegv glmqksasve
       61 ykkqlfledt itigiskiev erlfftffyq icnetgelcm egstkmlayd yqsqrvkkip
      121 edflntikey nrg
//
LOCUS       WP_285047794              91 aa            linear   BCT 25-DEC-2024
DEFINITION  large ribosomal subunit protein uL3, partial [Lactobacillus
            jensenii].
ACCESSION   WP_285047794
VERSION     WP_285047794.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus jensenii
  ORGANISM  Lactobacillus jensenii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Ban,N., Beckmann,R., Cate,J.H., Dinman,J.D., Dragon,F., Ellis,S.R.,
            Lafontaine,D.L., Lindahl,L., Liljas,A., Lipton,J.M., McAlear,M.A.,
            Moore,P.B., Noller,H.F., Ortega,J., Panse,V.G., Ramakrishnan,V.,
            Spahn,C.M., Steitz,T.A., Tchorzewski,M., Tollervey,D., Warren,A.J.,
            Williamson,J.R., Wilson,D., Yonath,A. and Yusupov,M.
  TITLE     A new system for naming ribosomal proteins
  JOURNAL   Curr Opin Struct Biol 24, 165-169 (2014)
   PUBMED   24524803
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Meskauskas,A. and Dinman,J.D.
  TITLE     Ribosomal protein L3: gatekeeper to the A site
  JOURNAL   Mol Cell 25 (6), 877-888 (2007)
   PUBMED   17386264
REFERENCE   3  (residues 1 to 91)
  AUTHORS   Wilson,D.N. and Nierhaus,K.H.
  TITLE     Ribosomal proteins in the spotlight
  JOURNAL   Crit Rev Biochem Mol Biol 40 (5), 243-267 (2005)
   PUBMED   16257826
REFERENCE   4  (residues 1 to 91)
  AUTHORS   Petrov,A., Meskauskas,A. and Dinman,J.D.
  TITLE     Ribosomal protein L3: influence on ribosome structure and function
  JOURNAL   RNA Biol 1 (1), 59-65 (2004)
   PUBMED   17194937
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Lactobacillus jensenii"
                     /db_xref="taxon:109790"
     Protein         <1..>91
                     /product="large ribosomal subunit protein uL3"
                     /GO_component="GO:0005840 - ribosome [Evidence IEA]"
                     /GO_function="GO:0003735 - structural constituent of
                     ribosome [Evidence IEA]"
                     /GO_function="GO:0019843 - rRNA binding [Evidence IEA]"
                     /GO_process="GO:0000027 - ribosomal large subunit assembly
                     [Evidence IEA]"
                     /GO_process="GO:0006412 - translation [Evidence IEA]"
     Region          <1..91
                     /region_name="RplC"
                     /note="Ribosomal protein L3 [Translation, ribosomal
                     structure and biogenesis]; COG0087"
                     /db_xref="CDD:439857"
ORIGIN      
        1 kgkgfqgvik rhgqsrgpma hgsryhrrpg smgpvapnrv fknkhlagrm ggnrvtiqnl
       61 eiaqvvpekn vilikgnvpg akkslitiks a
//
LOCUS       WP_285052477             462 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Fusobacterium
            necrophorum].
ACCESSION   WP_285052477
VERSION     WP_285052477.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..462
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=52506
     Region          27..460
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 milfgfrlda elkeelsnnf ennlsfadni vdfmdcvktk kyeaivieeq nlkddnlmnl
       61 iakvsefqkk gviivlgets nlkvvagsik agaydyilkp eenstivksi ekavkdykim
      121 aeridknrki gdkligrske mmelykmigk vagndvpvlv vgergtgkts vakaihqlsn
      181 vseegflsin cnsfrgelie rklfgyeiga fqganfnqkg ileqeemkil hlgnveslsl
      241 dmqskilyll eeqkffrlgg qdsiqskvri iastsedlel riqqgkfiee lyrklrvvei
      301 hipplrnrkn dipfiadhyi tecnlelntn irgmsrpalk kimrydwpgn vnelknaiks
      361 amtlcrgnsi lledlpstvl gekvmtkagi gelslkewir qeiqyyknen sqdyygqiis
      421 kvekelihqi lemtngkkve taeilgitrn tlrtkmnnyg le
//
LOCUS       WP_285052723             396 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Pectobacterium carotovorum].
ACCESSION   WP_285052723
VERSION     WP_285052723.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium carotovorum (Erwinia carotovora)
  ORGANISM  Pectobacterium carotovorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Pectobacterium carotovorum"
                     /db_xref="taxon:554"
     Protein         1..396
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=45572
     Region          35..333
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mdhirtntfm fdngerychv insltgeplf dpnlyittnv rsksvsintm evvagslvll
       61 yrflhmrkid ivdritrmef lssyeidala dfasenfknr kktsgsrsvk aptkyfrltf
      121 ichyldwlyh hhlphsvdvn ldaritrmva elknkrpdsd gyrdyipeks ltkaqqdilf
      181 nvvsvgsaln pfspavqtrn rliilllfsy giragellnl risdidfacs sitiqrrand
      241 ksdprvkqpl vktrgrvlls ekavmselyn yiqqdrlkir nakkndflfi tykkgdtegn
      301 plsmsayrki ihtisqcspe lygvtghqlr htwndhfssm sdahglsevr egqcrvycmg
      361 wvpgsemami ynkrhltkka netslavqqe iireml
//
LOCUS       WP_285052790             347 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Kingella kingae].
ACCESSION   WP_285052790
VERSION     WP_285052790.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..347
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=36598
     Region          8..347
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mqtllsslrh rfiqapmaga qdaqlaiavc qagglgslpa amyspeqlda qlstfrqavg
       61 napvnvnffa hetpnpsaeq vvrwqsalqp ycaelgvdls qvalqdtrrp fdetmlpvla
      121 khrpavvsfh fglpssplld avwvtgakil ssattvrear ylaeqgvdgi iaqgweaggh
      181 rgwfldkddv atqsgtfall pnivravdll viaaggiadc atvqaafalg aaavqsgtaf
      241 lladealtap ihraylqseq aactavsnif tgggargivt rwmrelgymh pnalpfplag
      301 vyfaalrqaa qnagchefns fwagqnaplc qtgsaaqiir nlmgeta
//
LOCUS       WP_285052825             157 aa            linear   BCT 25-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Kingella kingae].
ACCESSION   WP_285052825
VERSION     WP_285052825.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Bagautdinov,B. and Kunishima,N.
  TITLE     Crystal structures of shikimate dehydrogenase AroE from Thermus
            thermophilus HB8 and its cofactor and substrate complexes: insights
            into the enzymatic mechanism
  JOURNAL   J Mol Biol 373 (2), 424-438 (2007)
   PUBMED   17825835
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..157
                     /product="shikimate dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16727
     Region          <4..153
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 msqkgksamv vgnggvgsai aaslaaagia rlalfdvnee ssrklgarlq ehypnlqley
       61 asndptgfdl lvnatpmgmk egdpmpvdld kvssqtfvgd vvlkseltaf lqacqakgct
      121 iqvgvdmlfe qipvyleyfn lptttaqrlr eladirc
//
LOCUS       WP_285052830             450 aa            linear   BCT 25-DEC-2024
DEFINITION  cytochrome b [Kingella kingae].
ACCESSION   WP_285052830
VERSION     WP_285052830.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Tolkatchev,D., Yu,L. and Yu,C.A.
  TITLE     Potential induced redox reactions in mitochondrial and bacterial
            cytochrome b-c1 complexes
  JOURNAL   J Biol Chem 271 (21), 12356-12363 (1996)
   PUBMED   8647838
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Howell,N.
  TITLE     Evolutionary conservation of protein regions in the protonmotive
            cytochrome b and their possible roles in redox catalysis
  JOURNAL   J Mol Evol 29 (2), 157-169 (1989)
   PUBMED   2509716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..450
                     /product="cytochrome b"
                     /GO_function="GO:0008121 - ubiquinol-cytochrome-c
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=50398
     Region          9..418
                     /region_name="QcrB/PetB"
                     /note="Cytochrome b subunit of the bc complex [Energy
                     production and conversion]; COG1290"
                     /db_xref="CDD:440901"
ORIGIN      
        1 menqkscnka kalldwvdar fplskmyneh vgqyyapknf nfwyffgsla llvlviqivs
       61 gifltmnfkp dgttnaqnlp vafaaveyim rdvsggwiir ymhstgasff fivvylhmfr
      121 gliygsykkp relvwvfgsl iflalmaeaf mgyllpwgqm sfwgaqviin lfgaipvigp
      181 dlstwirgdf nvsdatlnrf falhviavpl vllglvvahl ialhevgsnn pdgieikklk
      241 dsngipldgi pfhpyytvkd ilgvvvflif fcgvmffape gggyflekpn fdpanplvtp
      301 ahiapvwyft pfyailraip sflgtqvwgv igmgaavvli allpwldrge vksvryrgpi
      361 fktalvlfii sfiglgilga mvatdvrtwv arvlsiiyfa ffllmpiytk mdknkpvper
      421 vtmgttkqki mffvyvvitl igsylfvtni
//
LOCUS       WP_285052965             662 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Fusobacterium necrophorum].
ACCESSION   WP_285052965
VERSION     WP_285052965.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..662
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=77087
     Region          412..657
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mkkieiktfl eysflsnvrf skngkyisyt ktkanleknd yehyvyvydt qskenkeyts
       61 lgkeknivwl ddtrllfqts rdsnikekkk egeewteyys idvrggeaka flqlpysvtd
      121 iqacssgfvf tanysnadis lhgltgeera kaiekkkeea dyevldeipf wsnglgftnk
      181 qrnrlyryet asqkiealtp efmnveyfkv senrvlfiae eyhdkleqtn alyeydllen
      241 rcscliedgn ynfsfadymg rdivcaasdm ksfginenhk lyfvkngtle lfyendtwll
      301 stvgsdckfg ggktfhttdn alyflstled fsvinclhrd grlelltard gsvdffdiyk
      361 dtlvygamkd yglqelylke nteeieitkh nrtvfeeysv skpekifmes ygesieiyvi
      421 kpvgfeegke ypaildihgg pktvygnvfy hemqvwanlg yfvfftnlhg sdgrgnrfmd
      481 irgkygsidy edlmkatdiv lesypidrkr vgvtggsygg fmtnwiight drfacavsqr
      541 sisnwiskfg ttdigyyfna dqnqstpwnk veklwshspl kyanqvktpt lfihseedyr
      601 cwlaeglqmf talkyhgvea rlcmfrgenh elsrsgkpkh rvrrleeitn wferylkkqe
      661 re
//
LOCUS       WP_285053153             261 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Fusobacterium
            necrophorum].
ACCESSION   WP_285053153
VERSION     WP_285053153.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..261
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30659
     Region          5..259
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mkrnkvhisd lilyknsaee ilnflkkysv knlelfiepl deeymkkmly vlehytfksv
       61 sfhgpfrkcn ismlteldwk kvvysyeesf kiaqkyspsf mvlhtneama knsiteelkl
      121 eikkridyiv tlaeqyeini vvenvgigan mifsqeeyen lilnssyqcl idighaflnh
      181 wnietliktl qnhilgfhfh nndgvydkhd pmflgkipyg sllpiirkyt peavivleyd
      241 flnpkevvie dwkrleslls t
//
LOCUS       WP_285053783             467 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Kingella
            kingae].
ACCESSION   WP_285053783
VERSION     WP_285053783.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..467
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51611
     Region          14..435
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mvesantssn sqryltlwrw hfytgiliap flmllaatgl amilfahtsg rdgeritvpv
       61 lqtvkplseq aqtaldtvdk nsgmvvqyia praadmvavf rvnngegkat mvaidpytaq
      121 vvktyprnqd wyhlmdeihg dillgktgdy lletaaaltv lmilsgwylw wcsrqrsvpk
      181 mlgigklgqg rsvwrglhgv fgsyisvmll lfclsgmawa giwggkvvqa wsaqfpagkw
      241 gvepipksap lhgelndgkt keipwvlelt pmpvsgttlg kdgiapdvpm tletvdrfar
      301 esgfvgryql yfpkgetgvw tlnqdsmsyd spsptadrtm hidkysgkvl adikfddypw
      361 fgqfmaasia fhmgtmgwws valnvvfcll vifmcvsgyi mwwkrrptga alcppaqgrd
      421 lptwktaaiv llivaaifpt alvaiavial ldwllisrvg alkkwfk
//
LOCUS       WP_285053802             235 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Kingella kingae].
ACCESSION   WP_285053802
VERSION     WP_285053802.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..235
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=27172
     Region          1..>217
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mkrnisldff rgimsiaval ghffhwngqt skmplsfila vdfflvlsgf visasvfnke
       61 nfntykfiks ryfrlipvyl fcviitlipq yffaenfvkp nsldvirils igemlpmnnl
      121 rfiyleplgi sytisaefwv gillfplifv irkyasqlll pvliifslfa flkivndtsd
      181 flnihyalay pfitygvirc lldyslgvia ytifeqrttn neqrttgqpc fklly
//
LOCUS       WP_285053836             179 aa            linear   BCT 25-DEC-2024
DEFINITION  KdsC family phosphatase [Kingella kingae].
ACCESSION   WP_285053836
VERSION     WP_285053836.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..179
                     /product="KdsC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=19209
     Region          9..178
                     /region_name="KdsC"
                     /note="3-deoxy-D-manno-octulosonate 8-phosphate
                     phosphatase KdsC and related HAD superfamily phosphatases
                     [Cell wall/membrane/envelope biogenesis, General function
                     prediction only]; COG1778"
                     /db_xref="CDD:441384"
ORIGIN      
        1 mfnhvapdil praqavklli mdvdgvlttg qlfiastgei ikpfntldgh gikmlqktgv
       61 qtaiitarnd pavaaraqsl gishylcgid dkrmayeqlr dqlglsakqc amvgddvidl
      121 pvmvrcglpi avanahvfvq qraayttqkh ggmgaireca dlimhaqntl qaalneytq
//
LOCUS       WP_285053875             669 aa            linear   BCT 25-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Kingella kingae].
ACCESSION   WP_285053875
VERSION     WP_285053875.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Shan,L., Mathews,I.I. and Khosla,C.
  TITLE     Structural and mechanistic analysis of two prolyl endopeptidases:
            role of interdomain dynamics in catalysis and specificity
  JOURNAL   Proc Natl Acad Sci U S A 102 (10), 3599-3604 (2005)
   PUBMED   15738423
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Polgar,L.
  TITLE     The prolyl oligopeptidase family
  JOURNAL   Cell Mol Life Sci 59 (2), 349-362 (2002)
   PUBMED   11915948
REFERENCE   3  (residues 1 to 669)
  AUTHORS   Polgar,L.
  TITLE     A potential processing enzyme in prokaryotes: oligopeptidase B, a
            new type of serine peptidase
  JOURNAL   Proteins 28 (3), 375-379 (1997)
   PUBMED   9223183
REFERENCE   4  (residues 1 to 669)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 669)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..669
                     /product="prolyl oligopeptidase family serine peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=74671
     Region          3..667
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mftdpyqyle nlhasetqkf hqsahaktla qfcqsenfhk tkqqiteqlq derqipfcqe
       61 hrarmyhfhq sadlpkgvyr vcsaasyrag ipdweilfsv adfdeilgdd vyldgvshyv
      121 erpelalisl ssqgsdsvyt iefnlktgei vsggfhfplg knhvawrden svwvcpawde
      181 rqlttsgypr qvwlmqrgqs fdeatpvyem dadgvmvsaw ryldaqgapl dlieantsff
      241 qkdyfyvnad laavklslpr dcevvcylag qlflhlksdw qrskqkyvsg sliavklnkg
      301 elgeafclfa ptssqaleli ettrkfvias lldnvsgslk awkwengawv eqalprfpng
      361 aieladqpwg gdtvylaasd fvtpltlfal dlnvmeltvl rrqpkqfdaq givvtqnfat
      421 sadgtripyy hvgkaqspdt ptlvyvyggf avpelphymg aigrhwlerg gafvlanvrg
      481 ggefthwhta aqrenkhksv ddllsvindl vergyssakk iaiqggsngg lvvasafcrl
      541 penlgamice vpltdmlryt elyagaswid eygdpadpkm reylaafspy hqlsgslnyp
      601 pafittslsd drvhpahalk fyaklrdnpn akawlfapek gghtgngtqa etaeelavvf
      661 eflnwaivs
//
LOCUS       WP_285053907             418 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Pectobacterium carotovorum].
ACCESSION   WP_285053907
VERSION     WP_285053907.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium carotovorum (Erwinia carotovora)
  ORGANISM  Pectobacterium carotovorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Pectobacterium carotovorum"
                     /db_xref="taxon:554"
     Protein         1..418
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=47958
     Region          2..407
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 maltdvvart akprdkaykl adahglyllv spngskrwyl kyrfegkesr iafgayplvs
       61 lakarekrde irllllegih ptekreeeke qaqealntfa kvaqdwhrni sqnrwsetha
      121 grvwrdmern llpaighrhi adlktkdlle plkvveqngh ldlasrlrqr vtdimrfavq
      181 ndliernpaq dlsgaiaapk athrpalkln klpdflarie rhkgraltrl alkltlcvfi
      241 rsselrfarw peidfkramw tipaeraaip gvkhsqrgak mrsehlvpls rqalalleei
      301 kaisgaheli fpgdrrptkp msentvnnal rtmgydttte vcghgfrtma csalvesgqw
      361 srdaverqms hqerngvraa yihkaehlde rrlmlqwwad yldanlkeyv vpyefknv
//
LOCUS       WP_285053920             238 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase, partial [Fusobacterium necrophorum].
ACCESSION   WP_285053920
VERSION     WP_285053920.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..>238
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          1..208
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mkqiaaffdi dgtiyrnslm iehfkkliky elldvesyqe hveeafklwd trvgdydeyl
       61 dklveayvka meglpvsynd fisdqvvylk gnrvysytrd qikwhkeqgh kvifisgspd
      121 flvsrmaekw gaddfrasvy kldeqgkqys geiipmwdsk hkikaleefq keynidlsks
      181 yaygdtngdf smlmsvgfpr ainpsrelvf kiketpylqe kakiiierkd vvyeldan
//
LOCUS       WP_285053978             231 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Fusobacterium
            necrophorum].
ACCESSION   WP_285053978
VERSION     WP_285053978.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..231
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27795
     Region          20..140
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mktdiydrww ieekenedsm ekqhhhfwnk lisyidkenw ednyvldfgc nqgaflrhly
       61 lkkkffkcig vdlasnsikv ansrknnlpl eyfntaypnk ldikfdiais ssvlfliedl
      121 eehskiiwds lknngvyyat ytdyvknpnl pylyktisky amlkmqlhsl ndiaeafwkq
      181 gfiveiqrma pksyvrlnke etwisrieek meyeyehmyi fkfikstens f
//
LOCUS       WP_285054019             123 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase, partial [Fusobacterium necrophorum].
ACCESSION   WP_285054019
VERSION     WP_285054019.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 123)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 123)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 123)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 123)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..>123
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          2..>123
                     /region_name="COG1672"
                     /note="Predicted ATPase, archaeal AAA+ ATPase superfamily
                     [General function prediction only]"
                     /db_xref="CDD:441278"
ORIGIN      
        1 mkfvnrkqel nilqeeyeke nsfvvlygrr rvgkttliqk fiegkkafyf fadkqnermq
       61 irrfqqqmaq yfqddllrkl eiydwesifd yflqkigdek iifvidefpy lcmgnkgfss
      121 ifq
//
LOCUS       WP_285054195             263 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Kingella kingae].
ACCESSION   WP_285054195
VERSION     WP_285054195.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..263
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=29265
     Region          150..252
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
ORIGIN      
        1 mnqhkkcrll llewekqpal nylnkqkiyf thmtkplsli isllglaaca tspqsappiv
       61 qaasvptsip ypeptqaeqi nqlaiqvarl eqqiavlteq lnqhetkhhs cntsrnqtkq
      121 papkrvtapa vsqskpeast splsqaqtwy kqgqyqkvld llrlhdsggn gdanaqqsmi
      181 lllqsnqklg ycqsviqigq rfatlfaqhd fapealyavg qcqwqiqqrd iaketwrnlv
      241 lrypntpaar ragssnpvkk dtp
//
LOCUS       WP_285054184             194 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Kingella kingae].
ACCESSION   WP_285054184
VERSION     WP_285054184.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..194
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=20880
     Region          4..193
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mslpiilast svfrqqqlrt lgvdfvaakp mfdetplage spsdtalrla igkaqslaqh
       61 ypqhliigad qvawcnnrql gkpmsvekaa amlaelsgqr iefysavcvl dtsagclrhh
      121 vdktvvqmrv lspeqirhyl arepdaiyca gaakseglga alleridssd pnaliglpif
      181 wlvsclnelg vdvi
//
LOCUS       WP_285054206              91 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase, partial [Kingella kingae].
ACCESSION   WP_285054206
VERSION     WP_285054206.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         <1..91
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
     Region          <9..90
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 lpdlrlaqlv vsradiryrk aaclgdvlhi hsqisslqsr qivlsqrief adtqqicata
       61 ditlmptsan gkmcrlpdal llyltnlmes s
//
LOCUS       WP_285054250             342 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease, partial [Kingella kingae].
ACCESSION   WP_285054250
VERSION     WP_285054250.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 342)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 342)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 342)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         <1..342
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          <1..337
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 whvelpvlrp wlasagclif lycfsgfgla lllggqqyat aeveiyrlia heldlehasv
       61 lvwlvlfata aagllnawfs rqthaadirp iaaqspsslh hkillgytlf llttccalpl
      121 laivvqatqa gnawrvlwhe dtlaalwntl rfsaialfgt avlgilhaaa araiplfrsi
      181 tflpfmispv clsfgallay pqhagslhll lalyvllayp fvtkdvlatw dtlphryfqa
      241 aqvfgaspiq tlwhitlpll rpalrrgltf aaatsigefa atlflsrpew qtlttliyyy
      301 lskvgsnnyg kamvltlllm tlatlvfvll dtqesrkksv ad
//
LOCUS       WP_285054353             301 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285054353
VERSION     WP_285054353.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..301
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34826
     Region          49..299
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 minrteslae fyqhklnwlp egwsdgshfn vfkledcadi ggnvpvkysr rdfykismir
       61 gksiyhyadk sietsgtalm ffnpqvpytw qpasaeatgy fcifkeafft enlrsnikdl
      121 pmfmpsgkps ysldteqegl ivqifekvit einsdyrfkf dlirnhvtel ihvalkmqpt
      181 eriyqhtdan tritavfnel lerqfpietp sqqfsmrspk dyaeklavhv nhlnraiket
      241 tgkttsqhis erltteakal lkhtswnise isyclgfeep ahfnhffkkh taitptafre
      301 v
//
LOCUS       WP_285054394             123 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA recognition motif domain-containing protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285054394
VERSION     WP_285054394.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Muto,Y. and Yokoyama,S.
  TITLE     Structural insight into RNA recognition motifs: versatile molecular
            Lego building blocks for biological systems
  JOURNAL   Wiley Interdiscip Rev RNA 3 (2), 229-246 (2012)
   PUBMED   22278943
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Clery,A., Blatter,M. and Allain,F.H.
  TITLE     RNA recognition motifs: boring? Not quite
  JOURNAL   Curr Opin Struct Biol 18 (3), 290-298 (2008)
   PUBMED   18515081
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Maris,C., Dominguez,C. and Allain,F.H.
  TITLE     The RNA recognition motif, a plastic RNA-binding platform to
            regulate post-transcriptional gene expression
  JOURNAL   FEBS J 272 (9), 2118-2131 (2005)
   PUBMED   15853797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..123
                     /product="RNA recognition motif domain-containing protein"
                     /GO_function="GO:0003729 - mRNA binding [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=13238
     Region          1..83
                     /region_name="RRM"
                     /note="RNA recognition motif (RRM) domain [Translation,
                     ribosomal structure and biogenesis]; COG0724"
                     /db_xref="CDD:440488"
ORIGIN      
        1 mvklfvagip dnlqeiglie mfslyalvss itvvtdkqtg kslgygfiev qdmaaagrai
       61 ealnglkvga rklevkiaee rnkpfskrpq erpaqknssg lsksnarqpv qgkskrprvk
      121 sgl
//
LOCUS       WP_285054408            1069 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285054408
VERSION     WP_285054408.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=117499
     Region          47..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtikqlliag ipmlcltskq slaftassdm rvtssmgsas ffqaqkilit gtvvdensqp
       61 vpgvgikslk tgkaavtnaa gkfsievesa teqltftyig yaaqtraagp gtaplniklv
      121 paagvdladv vvigygtsrk sdltgsvgsv regelqerpa sslnqalagr isgvqvntns
      181 grpggranvr vrgfssinss nnplyvvdgv qlpmgnqlqa sqaidyinpn divsvevlkd
      241 asstaiygsr gangvilitt krgktgesri dynvdfsvpt vgpnfpkvln akeflavedl
      301 ayknmekydp vnwaagkyag rnpalarkdp rlfdangnpy ydtdwlkeat qnklsqnhel
      361 gfsggndrtv ysfsighrnd qglvktsflk rysgrfsidd qmkkwlkvgg tlsytnqnen
      421 lvdqsdqvar sivedfpflp vkypdnglya dnrdypnaeg rfnvvhrlnd tkfllgtqtt
      481 lgslysnitf teglemktii ganiitqenn eyssrtlnis dqgyaavrtr keafwsienf
      541 ltynkkfnen hsinallgis wqksgfnnss aevrgfatdy llynnlsags lnpqvgsnry
      601 fqqlnsyfgr lnynlkdkyl ftvtgradgt srvgesnkys ffpsaavawr vseenflkdn
      661 ntisnlklrt sigvagnsei paysslallg tnypavindt rvvgtglnrl anrelrwekt
      721 tqsdigvelg lfdgrislel dayyrkttdm lldapvprts gyerirknig smenkgiele
      781 lnttnfnsed ftwktafnis lnknkvlsla tpadifgigg pnftnptnii rvgeaagsfw
      841 gltrlgvwte aeraeaakyv syrngltmlp gdikyldvng dyaindadrs iigngspdaw
      901 gafsntfryk kvdltvelqy sygadvmdmt thssedrqsl ansyatvlda wtpqnqnsqi
      961 aeirdtragy vtnvdthwik dasfirgrnl llgytfgnet vqkmrlnklr vyvsaqnlfl
     1021 itskelqgdp ettptggyan dannvfsqgm nwhsyprpti fmlglnigl
//
LOCUS       WP_285054437            1071 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285054437
VERSION     WP_285054437.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=119350
     Region          48..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkklriags cqgllltcci ciaglvvhak kptpktirin lqsvllkkev rglvsdsaga
       61 lpgvsvlvkd ksnigtttdi ngryflevpd ensvlvfkmv gfetqevtvg aksvinvvlk
      121 paqnmldeav vvafgkqkke svigsittin pkelkvpssn lttalagrva gmiayqrsge
      181 pgqdnanffi rgittfgtnr nplilidgve ltttdlarln pddiasfsim kdatatalyg
      241 argangvvli ttkegkegka eislrlensl saatknvela dpvtymrlhn eailtrdplr
      301 elpysddkid ntvpgsgsli ypstdwrkel fkdytmnqra nlsvsgggai akyrvtgafn
      361 qdngvlkvdq rnnfnsnikl knyslrtnvn vnltkstemi irlsgnfddy tgpvdggeam
      421 frrvmrtnpv lfpatypkda dhqfvkhimf gnavdgnyln pyadmvsgyk dysrssmvaq
      481 lelkqnlsal aqglsfrtml nttrgaffdv grvyspfyys mgqydrrent yrvnvinpds
      541 gtdfltyspg dktinstfym esavnymrdf nkhtlsgllv aimrqsltan aptlqeslpf
      601 rnlgisgrat yaydnryfae fnfgyngter fykdhrfgff psagvawsis neefwkplkn
      661 tvnnfrirgt yglvgndnig sgrflylsev nmnnasyaai fgrdngytrn gitvsrysdq
      721 ditwetakkm nmavelslfn kldviaeyyt ekrenilqqr vstpasmglw vqpyanigka
      781 kgkgvdvqla ynhsfnnafw mqgranftya tsqytvfeey dylnepwksr igypisqvwg
      841 yigeslfvdd aevanspqqs fggvvmggdi kyrdvngdgk itvldqvpig fptepeivyg
      901 fglsagfkgf dmsaffqglt resfwidpqa tapfvsfyyq serdagaril gsitqnqllk
      961 ayaddhwsee nrnvyalwpr lsapevsqnn sqtstwfmrn gaflrlkqve igytlpkria
     1021 drlrmkapri yvsgtnlltf skfklwdvem agnglgypvq kvfnlginva f
//
LOCUS       WP_285054482             317 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285054482
VERSION     WP_285054482.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..317
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34776
     Region          45..315
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mnrrnfinlg aaaalisgts slalgnpvsk terkdkryqk gvspwpicld tatirpaslk
       61 dkvkiaakag ydaiepwdge lqefeakggn lkdlgkeikd lglfvpsvig lwnalpptre
      121 lfdaslkdtr nrmrmaseig aqhiqtipnt agdnynqkwv aaryrdiiei glkeyniqpa
      181 lvfvkyqpvk tmgqamgiam danhpkamii pdtyhmyise ggfeglkmid gksiaifqfg
      241 dvpsspsaie dlgdqhrvyp gdgilplpqi lkdlkatgfk gcvslelynp nywkedlqqv
      301 astglkktle vikkagv
//
LOCUS       WP_285054682             301 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family oxidoreductase [Pedobacter ginsengisoli].
ACCESSION   WP_285054682
VERSION     WP_285054682.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Blankenfeldt,W., Kerr,I.D., Giraud,M.F., McMiken,H.J., Leonard,G.,
            Whitfield,C., Messner,P., Graninger,M. and Naismith,J.H.
  TITLE     Variation on a theme of SDR. dTDP-6-deoxy-L- lyxo-4-hexulose
            reductase (RmlD) shows a new Mg2+-dependent dimerization mode
  JOURNAL   Structure 10 (6), 773-786 (2002)
   PUBMED   12057193
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437758
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..301
                     /product="SDR family oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009226 - nucleotide-sugar biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0019305 - dTDP-rhamnose biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=33244
     Region          3..299
                     /region_name="RfbD"
                     /note="dTDP-4-dehydrorhamnose reductase [Cell
                     wall/membrane/envelope biogenesis]; COG1091"
                     /db_xref="CDD:440708"
ORIGIN      
        1 mkkilvtgsn gllgqkiteq ilqtrqfdli atsrganrfp vqegytyaem dildplnvrn
       61 vvhhyqpdai ihtaamtnvd tceaqqdlan rlnvdavktl isvceknqiq lvhlstdfif
      121 dgasgpydea aepspvshyg ltkvraeeai aasscdwvii rtilvygivs dmsrsnivlw
      181 aknalekgdp invvndqwrm ptlaedlaia cllavekkaq giyhisgkdm msvaelvtrv
      241 adywqlnqsg vteissasln qkarrpvktg fvldkaikdl gyvphsfeeg lelfdkqiks
      301 r
//
LOCUS       WP_285054684             324 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Fusobacterium
            necrophorum].
ACCESSION   WP_285054684
VERSION     WP_285054684.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..324
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=37781
     Region          <179..314
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkpyyefvqt ylgatdcknn qkycsightf cfnkeeiegi ywfyetkdfi vdihdffikk
       61 dftqnnfpnm syfmsfcssy litangesfn pyqtlssnll yimdidnldt nyhfllhgny
      121 pylsvginfk kqmieeylns lknkgninys diffntksiv sksleslakd ilnckmsspa
      181 aeiffeakak ewlsitidaf lsrknihlsl dddkalenva nylddhyait vsqkvlekia
      241 mmsgtklkkl fkqkyqmsit eysqrrrmni aeilllnsnl kikeiaeavg ysshskfstc
      301 ykkykgvypr eikkfnlnlr akni
//
LOCUS       WP_285054850             163 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Pedobacter ginsengisoli].
ACCESSION   WP_285054850
VERSION     WP_285054850.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469162
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..163
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18430
     Region          46..161
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          53..78
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          83..109
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
ORIGIN      
        1 mtknkkilag ivaaavvigt iiwspwssgr yekysfskqm paiaqgadnr aellkaaely
       61 nkgdyaeark ilgkeymfnp qnpvltyyfa vtlietkqty eartllkhlf egqsvfkyda
      121 afyaglsfvk edngkeaimw lqkiprenar yakaqelise lkk
//
LOCUS       WP_285054910             229 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NUDIX hydrolase [Pedobacter].
ACCESSION   WP_285054910
VERSION     WP_285054910.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 229)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19271407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..229
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26714
     Region          12..>70
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cl00447"
                     /db_xref="CDD:469772"
     Region          43..217
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mkevlpkfds tfsidcvvfg fdegelkill ierneepfkd wwalpgnivg edesldqsas
       61 rilneltglt niymeqyytf gdvnrhpqgr vvsiayyall rlggeksvkp lstyakqayw
      121 rnvkdlpkla fdhqkifekg lekikrrikh qpiafellpe kftltqlqnv yevilnkkld
      181 krnfrkkmls fgvlrdldek qqgvsfraat lykfdkrkya klfgkeisf
//
LOCUS       WP_285054946             233 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Pedobacter
            ginsengisoli].
ACCESSION   WP_285054946
VERSION     WP_285054946.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 233)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 233)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..233
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=24962
     Region          2..202
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mniiltgass gigfeaalef tlskenkvvc iarsadklrk lleiarginp dcilfpvefd
       61 ivnddyaalv pflkehlgnv dilinnagal inkpfletsa admyqmfesn vighfnmiqn
      121 ilplmgtggh ivnigsmggf qgsvkfpgls aysssksalh tlteclayel adtgikvncl
      181 algsaqteml eqafpgyesp vmafemgkyi adfartghkf fngktlpvav ttp
//
LOCUS       WP_285055020             159 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein, partial
            [Kingella kingae].
ACCESSION   WP_285055020
VERSION     WP_285055020.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..>159
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
     Region          14..>158
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mvesantssn sqryltlwrw hfytgiliap flmllaatgl amilfahtsg rdgeriivpv
       61 lqtvkplseq aqtaldtvdk nsgmvvqyia praadmvavf rvnngegkat mvaidpytaq
      121 vvktyprnqd wyhlmdeihg dillgktgdy lletaaalt
//
LOCUS       WP_285055091             679 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Pedobacter ginsengisoli].
ACCESSION   WP_285055091
VERSION     WP_285055091.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 679)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 679)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10541096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..679
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=75614
     Region          1..76
                     /region_name="BatA"
                     /note="Aerotolerance regulator N-terminal; pfam07584"
                     /db_xref="CDD:429551"
     Region          48..>192
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mnflypgflf allaiaipiv ihlfnfrrfk kvyfsnvqfl keakeqnssr eklknllvll
       61 srilaivflv lafarpflps dssdspalrn avsiyidnsy smetvnkegs lldeakrkak
      121 eiaaayslnd qfqlitndfe grhqrlvske efvqlldeik isgtsrnlqq vinrmqsdan
      181 agrnqicyll sdfqksfagl skieggkair ynfvklnans lpnisvdsvw slspvhkpgq
      241 termvvqlkn ygeedakgip lkltvnlqqk aisnvavgag ktvadtlsfs glkpgwqkas
      301 isikdfpltf ddelnfsfnv snelrvlnis gnpsdkfiaa lfgadsyfkl tempesniky
      361 stfpdygliv lsglrepssg laqelksyvq nggsvvifpd ldvsaavynp fltglslpai
      421 qqlqtgvpia ttidlkseif kdvfdqipkn mdlpvvsryf syadgsrtsr esilqlplnr
      481 slfakytvga gkiylsassl slkdgnlprh pvfvplmykv afsgarerpl fhtigqdnli
      541 gmekisllan qslklvsadf evipeirqtp grtllyvadq vkksgfyelk kadstlavva
      601 fndnrtesdm hyatereleg lfgkqkisvf nsrkdamsln iaaknnstel wklciilsvv
      661 flameillir ffnkniqtt
//
LOCUS       WP_285055241             252 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Pedobacter ginsengisoli].
ACCESSION   WP_285055241
VERSION     WP_285055241.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 252)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 252)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..252
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28373
     Region          2..245
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mkikaliidd epnnienlql iidkysadvf iagtadnaea gaklirehep dlvfldiqmp
       61 eksgfdllsa lpgvnfevif itaydkygiq aikfsaldyl lkpinieefk laiekakqri
      121 qlskqsrnid nlleylkvgq kgspkialpt lketmyvris dvirceatnn yttfhlqnqe
      181 qvlvcktlkd fadllkphdf irthqshlvn pqyvksylke dggtlllenl qkvpisrqnr
      241 etvkaslsgp gs
//
LOCUS       WP_285055242             166 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Pedobacter ginsengisoli].
ACCESSION   WP_285055242
VERSION     WP_285055242.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..166
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=18519
     Region          1..137
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 maelslsrts rsvpkvdlta mvdlaffmlt tslskpvamd vakpdepind kqlpwpasrt
       61 mtillgandk iawymgepgk stptiedfsq irksiianqe mvakanhndr kkplyiiikp
      121 tsganyknfv dimdelklvd lktapaiddd hilkeeldfm kqkgir
//
LOCUS       WP_285055249             236 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Pedobacter ginsengisoli].
ACCESSION   WP_285055249
VERSION     WP_285055249.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 236)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..236
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=26771
     Region          7..231
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mksskalrci vlddeihavk lladyvirtn glelvlhttd paaaislihe gnidlifldi
       61 qmpdltgiev maiirqtqtk vilttaypey alsgfeydai dyllkpvtfe rflvavnkak
      121 erisvkasea pepdhifvkv ehrlqkilfs sifyieglgd yicfhvlagk ilslermkhi
      181 elilpqplfl rihksyiint shidfvergr iiinkeylpi gesykekvrq qlglgs
//
LOCUS       WP_285055395             662 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Fusobacterium necrophorum].
ACCESSION   WP_285055395
VERSION     WP_285055395.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..662
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=77129
     Region          412..657
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mkkieiktfl eysflsnvrf skngkyisyt ktkanleknd yehyvyvydt qskenkeyts
       61 lgkeknvvwl ddtrllfqts rdsnikekkk egeewteyys idvrggeaka flqlpysvtd
      121 iqacssgfvf tanysnteis lhgltgeera kaiekkkeea dyevldeipf wsnglgftnk
      181 qrnrlyryet asqkievltp efmnveyfkv senrvlfiae eyhdkleqtn alyeydllen
      241 rcscliedgn ynfsfadymg rdivcaasdm ksfginenhk lyfvkngtle lfyendtwll
      301 stvgsdckfg ggktfhttdn alyflstled fsvinclhrd grlelltard gsvdffdiyk
      361 dtlvygamkd yglqelylke nteeieitkh nrtvfeeysv skpekifmes ygesieiyvi
      421 kpvgfeegke ypaildihgg pktvygnvfy hemqvwanlg yfvfftnphg sdgrgnrfmd
      481 irgkygsidy edlmkatdiv lesypidrkr vgvtggsygg fmtnwiight drfacavsqr
      541 sisnwiskfg ttdigyyfna dqnqstpwnk veklwshspl kyanqvktpt lfihseedyr
      601 cwlaeglqmf talkyhgvea rlcmfrgenh elsrsgkpkh rvrrleeitn wferylkkqe
      661 re
//
LOCUS       WP_285055422             370 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Pedobacter ginsengisoli].
ACCESSION   WP_285055422
VERSION     WP_285055422.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..370
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41882
     Region          9..367
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mrndlnelas kphypildgl rgvaaiivvt fhlaepfsts nvdklinhgy lavdffflls
       61 gfvmsyaydd rwhkmtfgsf fkrriirlqp mvilgmtlga igfyftdstl wplihtvplw
      121 kmllvllvgy tilpvplsld irgwqemhpl nsvgwslffe yianilyavw irrfsktals
      181 vlvgiaavvl ahlaisngdv sggwtfnaeh lrigftrvmf pffagvllsr iakptrikna
      241 llwcsllvav vlympriggt eqgwmngiyd avciiivfpl ivylgasgvm qsqeenrick
      301 flgdisyply lvhypivyfy vawisdnkgi tiatawpygl liflgsiila yasskwydep
      361 vrkwlrknls
//
LOCUS       WP_285055488             482 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Pedobacter ginsengisoli].
ACCESSION   WP_285055488
VERSION     WP_285055488.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..482
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55424
     Region          47..172
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mkfikrsmta illllslntn aqknesiysn rlyvgdkvdl esiefnnvrn ypggkmklsd
       61 fkgkfiildf wtkgcsvcia sfpkmeelqn kfkhdiqvll itknskeeil pllknspnvk
      121 ntklpiiigd qiltkrlfph gpvpyhvwlg rdgkvlatis mgetnvenlt kltsggslnl
      181 lmrnesfdne tyeelkdekk sllkigngaf rkvlkyyaqi pipkgvntlp rseitmlelp
      241 yysafmnflp gyfpqgstkf lrdqrgkekg lrfynetida lyrfaydapr ekvvledkak
      301 slyeeitdst nldrykasnw ycyesslney sidnarnllk qdlsrffgmv gsveyrpikc
      361 liltrlgtin dsklwakdqn trkedyqnqr tpeglkiknk pfqsfltnli nanrasddpl
      421 ilnetgyrhg efinkkidil lrgslhctdd nipllrnelv ryglglkeei rgvkvlvlrt
      481 iq
//
LOCUS       WP_285055523             802 aa            linear   BCT 25-DEC-2024
DEFINITION  peroxiredoxin family protein [Pedobacter ginsengisoli].
ACCESSION   WP_285055523
VERSION     WP_285055523.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 802)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 802)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 802)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 802)
  AUTHORS   Schroder,E. and Ponting,C.P.
  TITLE     Evidence that peroxiredoxins are novel members of the thioredoxin
            fold superfamily
  JOURNAL   Protein Sci 7 (11), 2465-2468 (1998)
   PUBMED   9828014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003123
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..802
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..802
                     /product="peroxiredoxin family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=89875
     Region          644..800
                     /region_name="Bcp"
                     /note="Peroxiredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG1225"
                     /db_xref="CDD:440838"
ORIGIN      
        1 mrriskivli vllfcsvavr gqvfdstgis rarleyylkr avtmaeflav dpyandgpyp
       61 ykkddvrlih ntgakfigra iyrwgneatl anpdflnkam alirevhskd pevifqaavf
      121 eavtgqvnql ripdwafial grkpevrnfr yedmldvkgk finhwgkgss vpditrpeaq
      181 lwlmylcgvy mnlgcealhl gqvalmgmnd pglkvwngfv qkvrnyarah tphhwvllda
      241 htpqggmvvd gksildfnsf plrikeipek pmegvlqigy ldaifrrsmg cvtpsgwkcd
      301 alpylvefdn fgisrkpgva dtashfiwgy deitwfyllp ekkrnawlry ahdwvaandp
      361 vgwlqmpisr ivslgrgnqp arhrgnirse dcpaglnveq tvkeiwrqps lpasaqvdle
      421 pgkwratllr edgfqipfgl dfkregadla cyilngterm kterivvsgd smlirmpvfe
      481 syfsvkavtk dslsgfwikg gaakdiiipf tatagkgrfp nvkqgaagra ggkwsmeftr
      541 anqtkrpavg efvqnghfvt gsvltpagdy ryldgivkgd slflstfdgi hallfaaeis
      601 getingyfys sasvperfta rkdagaklta pvtavkegsd gklnfsfkdl dgnmvslqse
      661 ryrnkvvvvq lmgswcpncm demaflseyy rrnkdrgvev ialayelttd eersrkslrk
      721 fqqqfnvqyp mlitgvavgd partektlpq lteikvfptt viidkngvvn einasfygpa
      781 tgqyhldyka dferkisall gr
//
LOCUS       WP_285055573            1087 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285055573
VERSION     WP_285055573.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1087)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..1087
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=120504
     Region          31..1086
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrilntsal llicfftlvg nkaysqgsak itvvgtvtdt lknkitgvni mvegnpkigt
       61 rtddngkfvl dvdagavlki syvgykeqhv tisasnktln iqlkednlva deivitamgq
      121 rqrkeamvgs vttikpgalk ipssnltasl agqaagiiay qrsgqpgqdn asffirgvtt
      181 fgykreplil idnveltand larlqvddie sfsilkdasa talygargan gvilvstkeg
      241 kegkakinfr seysmsqstq tlqladpiqy mqlyneaslt rdpklplpfp vskientkat
      301 lagapgsnpy vfpavdwldm lfkdrattqr nnlsvsgggs takyyiagsy nidngvlktd
      361 vrnnnnnnvn fknyqlrsnv nvnltkttev virlsgtfse yngpitadgs fasdlynvav
      421 haspvlfpay ypaegenaka nhilfgnvgg pdgtannsir ypngnpyaql lrghknsses
      481 rmsaqlelnq dfgfiteglk frsifntnry syfdsqlays pyfysaggyd klnnsysltw
      541 lnprnnvsnn vpteylvysr nepnansfyy fqgaldynkl lgnhgisatl igtaqqtlys
      601 sakdpvlhvt tlpyslpfrn lglagratyn ykskyyaevn fglngserfs eehrygffpt
      661 fglswvasne sfwkaggivd rlkirgsygl vgndaignqr ffylsdvnln ggnfaqfgin
      721 ngtqlngvti rsyansnitw etsrqtnvaa eitmlknlni vaefyknhry dilrerqvpv
      781 tegfeaavlt nlgvvdskgi dlsadykqnf nnglwtsfrg nftystnkyt yieepnypet
      841 wrhfigqpis rgygyiaerl fvddnearns ptqimsinda ygnkingilp qggdikykdv
      901 nadgkiddld qvflgypetp eivygfgfss gfkgfdlsaf fqgqarvsff idprkvspfv
      961 ernvayidgn tqvlkefadn hwseenqnly alyprlgtss aaiannlqps twwlrdasfi
     1021 rlksleigyt lpssiskslr isncrlyfng lnlitwspfk mwdpelggng fsypiqkvfn
     1081 vglnlnl
//
LOCUS       WP_285055655             511 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Fusobacterium necrophorum].
ACCESSION   WP_285055655
VERSION     WP_285055655.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 511)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 511)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 511)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..511
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58857
     Region          16..452
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mkekrvqkii insiylllwi lplfwfirdf wivediqnsf dgalwktilf twkqslyssf
       61 lafflaiipa rylayhnnll skmlesllfi pfffpvlsti gifsilfnlp gvqnfsvlys
      121 mkailiahvf ynspifvkyl gealrripke ieesmildga gswtifwkgq lplilpqifk
      181 afilcftycf lsfaillslg giqyqsleve iaaslqgdfn fskamlygll qffmllgins
      241 lgtflpdyel kgrayekkms ghsmlfsify vifeygivla sivasfynyf tgefsvkayr
      301 ilfsaafqee ypiwrslgns flvagiasig tvivvyfllq nysrivelli fsnlgisgaf
      361 faitlyyvyv lyevpfavll vfaylmtgip lvysflyqnv kmfprdfkem afldgaspwq
      421 yfwsiqfpil rplfllsflq sfaiflgeft laytmqlgdm fpvvslvnys llvdkkyles
      481 salsaillal illlfflgec lktrgeryen t
//
LOCUS       WP_285055658             314 aa            linear   BCT 25-DEC-2024
DEFINITION  DHH family phosphoesterase [Fusobacterium necrophorum].
ACCESSION   WP_285055658
VERSION     WP_285055658.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..314
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=34718
     Region          3..314
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mknkirelll qhnsilitah knpdgdavga glaltlslle lgkkarfvlq dkvpdttlfl
       61 egsqlieqyq aeesfeevel vifvdcatrd ragcmddltk gkltvnldhh msnphygdya
      121 fvepkisats elltqllqdw nfpmnaaias alylgivndt gnfahdnvtv ntlkaaqflv
      181 eqgadnaliv rnflkthsya slkllgeals qfqffpekkl syfyltqevm nkygakkeht
      241 egivetllsy ekasislflr eekdgsikgs mrskdsidvn riaslfgggg hikaagfscl
      301 ekadsilhki leqi
//
LOCUS       WP_285055720             342 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Pedobacter ginsengisoli].
ACCESSION   WP_285055720
VERSION     WP_285055720.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..342
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38566
     Region          32..329
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 meeaniiten ssygtdiral nemiqkesaf idllflemdk vivgqrymve rlmigllang
       61 hillegvpgl aktlaintls kcvdagfsri qftpdllpad llgtmiynqk keefivrkgp
      121 lfsnfilade inrapakvqs alleamqerq vtlgdetykl pepflvlatq npieqegtyp
      181 lpeaqvdrfm lkvvigypqr edekkimran iapqgmpkpn tilhtddiir arkvvkdvym
      241 dekieqyiid ivfatrfpeq ykladyknli sfgasprasi nlalaakaya firrrgyvip
      301 edvravchdv lrhriglsye aeaedyttek iitgilnaie vp
//
LOCUS       WP_285055919             372 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285055919
VERSION     WP_285055919.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..372
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=42710
     Region          3..351
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mrkrfkdiir qihlwlglgt glivfvvsit gctyvfeeei reatqkerly vpvqqkpfig
       61 ldkvitafqk aapnekisvi rmtnstpnat veiaskknty yfnpydgqlv ykgrhdwldt
      121 veeihmtllm getgkfiqrw avvvfvlmli tgiilwfpnq mrllkqslri kwkgsfkrvn
      181 ydlhnvlgfy aswiliiisl tglffafkev ktaasfftgs kltegkkqpp vetpviesla
      241 lrydyiyktt alkypgaist sisirkggel rlrmiypykw arnqntfffn easgqllrak
      301 rykefngadl ieatnydlht grlfglpgki iaciaalisa slpitgfiiw lkkgkkrkrr
      361 irkrrspahs fa
//
LOCUS       WP_285055984            1029 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285055984
VERSION     WP_285055984.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1029)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..1029
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=113267
     Region          50..1028
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqnfkkgryv fgagslfkka lllssctlvl lalpfisnaq vttplinspl kgqivdsltk
       61 qgipgvsvhi vgtthsvqtn segrfefvtg qkfpytleig hvtyekktiv vdnspvvikl
      121 keitaqlndv vivgygtqqr knligsvski dpsgtrsipe agfdsqlqgk aagvqinsnt
      181 gvpgsdifir vrgatsinat ndplyiidgv wvnnsslqni aqergtspls dinpsdiesi
      241 eilkdataia iygsrgangv vlvttkrgny gqktkidfng seglgwaped rvwktttgee
      301 hailvneysr nigkpepfrp ateiingvtg rglpstqpty drmsylnrta alrnydlsiq
      361 ggsdktrfyl gggyaeqesi wkpmgfdras lkvnldhkln srisigtsnt iarshrdqar
      421 pangangtll qaslniptyl pifdangtpl kwvnfdnidv ltstvnlwsn syhyignlyf
      481 dyaitpklkf rstfgvdydn yeeneywdtr tilgnsggrg tqsitqssaa ineqtlsynd
      541 qigkhsfgll igntlqgaei knvaatgtnf pnnsytqiss aatqiasqfk tnstlasffs
      601 ranynyggky yaeftiradg sskfgknnkw gyfpsvgaaw rikeenflkd vsqisnlkyr
      661 isygvtgnqa gindfasqgl wtggfgyadv aggaelpgta plqlanpdlk westaqfstg
      721 ldiglfedkl niefnyynky tsdallqvav pgasgfsayl tnfgeisnkg felginstnl
      781 rttgftwktd fniarnknti ekipadipfa grdlirlqqg kelysywlyk qlsvnpdnge
      841 avfddynkdg kitaddrqiv gstwpeffgg ltnnftyrgl dlsifftfsy gnyiwnhnrm
      901 lgetggtlda grvllksqld rwttpgqitn tpklndanya rqensrffed asylrlralt
      961 lgytlpkvft ekisiekirf yvtgsnlllf trytgadpes nlgtqniqgy dygtppqprt
     1021 vqlglnltl
//
LOCUS       WP_285056060             423 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Pedobacter ginsengisoli].
ACCESSION   WP_285056060
VERSION     WP_285056060.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..423
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44081
     Region          3..422
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 mhnrvvitgl gvvapngvgl plftealkng hsgikhdpel erllfscqia gkpsvsaela
       61 aqyfselelk slnstgilyg viagmdawkd aglpvsagee pdwdsgtvfg agtsgidkfr
      121 esvykiddlq irklgstavv qtmasgisaf lggklglgnq vttnssactt gaesilmaye
      181 rikcgralrm lcgstsdggp yvwggfdamk vctykhnadp ekgsrpmsat asgfvpasga
      241 galilesles alrrgaviya evlgghinsg gqkgvgtmta pnpsavqrci knaladagis
      301 aaevnaingh ltatskdave irnwcealgr sgidfpyins lksavghcls aagsiesvas
      361 vlqlhhgfif pnvncedlna eimtmvdevr ipqkmistdl nivakasfgf gdvnacvifk
      421 kys
//
LOCUS       WP_285056073             287 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285056073
VERSION     WP_285056073.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..287
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31677
     Region          7..285
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mplnvtygvs twlwtspfqt ssieelfpki aamgfdavei avedpglidg eavkagleky
       61 glkavicgaf gptrdltned tsvhencfry ieacldfcvl wdikifagpm ysavgkarmv
      121 ppeqrkkewn lavsnlrvvc dmaaqrgvkl aieplnrfes dlvntakdav rlvndinhpa
      181 agilldgfhm sveerdleaa vklagdklfh vqvsenyrgs pgtgqtrwdr lkagleavny
      241 qgivaiesft peikelaeav ciwypfaddq defaadglkf lksyfnt
//
LOCUS       WP_285056170             150 aa            linear   BCT 25-DEC-2024
DEFINITION  SRPBCC family protein [Pedobacter ginsengisoli].
ACCESSION   WP_285056170
VERSION     WP_285056170.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..150
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=17229
     Region          5..131
                     /region_name="SRPBCC_CalC_Aha1-like"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of Micromonospora echinospora CalC, human Aha1, and
                     related proteins; cd07814"
                     /db_xref="CDD:176856"
     Site            order(6,8,10,19..21,23..24,41,47,49,54,56..57,59,62,68,
                     70..71,90..91,93,95,105,107,109,111,117..125,127..129)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mkindfttti lvdqtpkevf davnhpenww sgeikgstek lndeftyryk efhfskqriv
       61 dmipdqkvvw lviesqinyt ednsewtgtt isfeiseegk ktrlrfshlg lvpeiecfes
      121 csnswsqliq qslfslittg kgqqlllags
//
LOCUS       WP_285056274             444 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Pedobacter
            ginsengisoli].
ACCESSION   WP_285056274
VERSION     WP_285056274.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..444
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=49610
     Region          1..440
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mqnsvliidd ekkicsllar iielegfkvf qansgkeglk ilkaedilvv vsdvklpdfn
       61 gvelvneikk irpvaevinl tafgtiadgv mamrngafdy itkgddndki ipliykamdk
      121 aklnarvyel enqisrkfnf dsilgksktl keavalarrv agtnttvlll getgtgkevf
      181 aqaihhespr rakpfvavnc sgfnpelles elfgykagaf tgaakdkrgl ldeanegtif
      241 ldeigelnld lqakllrvle nqtyikigdt qttqvnvrii aatnrdlkae aeagkfrldl
      301 fyrlsvfsie lpplshrred ilpiamhyla eftakvnkpe fsvdkefirl ltnhnwkgni
      361 relknvmerv viladnglit snllpfefht earaadpmnm qdvekqhiik vlkytggnkt
      421 etsrllgigl ttlyrkieey kiea
//
LOCUS       WP_285056344             378 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Pedobacter ginsengisoli].
ACCESSION   WP_285056344
VERSION     WP_285056344.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..378
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41238
     Region          6..374
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mntaeqfmkd rlqsrtdngs lrnlssshlp vdfcsndylg farstmlkeq idqelnkhsl
       61 yqngsggsrl lsgnteytee tesfiavfhq aqaalifnsg ydanlgllsc laqrgdtiis
      121 delihaslvd garltyasry tfrhndlndl etklknakgn syvvtesvys mdgdtaplpe
      181 isalcdryna nlivdeahal giigdhgkgl vqhlglqdkv farvvtfgka lgchgaavlg
      241 slalrqylin farsfiytta apihtiaavk cayqmllttd fsliirekik hyadlanttg
      301 lnhpaptpsa iqtlihpgnt aartaaallq nkgidvrail sptvhagqer lriclhtynt
      361 deeikqlate laqlksne
//
LOCUS       WP_285056371             752 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Pedobacter ginsengisoli].
ACCESSION   WP_285056371
VERSION     WP_285056371.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 752)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..752
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=79668
     Region          9..733
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 masvknintl slpvlgmsca acavsvesmi saqegvtqae vnyatqkvkv sydpavtgpa
       61 kfqkavqsig ydlitdtdte kgnekqaeaq ahhykalkkr tiaaailtip vvvtgmflmd
      121 lpyanyimli ltapvvfyfg ksffvnawkq agygkanmdt lvalstgiaf ifsvfntvyp
      181 efwhsrglhp hvyfeaaavv ivfimlgkll eenaksntsg aikkliglqp kmvllitekg
      241 eqeipvadvq kgdkllvrsg ekipvdgtly egssyvdesm lsgepvavlk eqgskvfagt
      301 inqkgsfrfv adkvgsetml aqiiqmvqda qgskapvqkl vdkvagifvp vvifiavctl
      361 gvwtlaggsh aftqgllamv tvlviacpca lglatptaim vgigkgaesg ilikdaeale
      421 lgykvnaivl dktgtitagk pvvtaiywnk nlsdgkgsle qifaaleqss ehplaeaiyn
      481 elkakgvtpv disnfdsltg mgvsgihngk kyiagshkav knqlrasglq geakglleqa
      541 kvlqeqaqtv iyfadesevl avvaiadqvk dgsaaavtel kklgitvyml tgdneqtaaa
      601 vakqagidhy qaevlpsdka afikklqqag kvvamvgdgi ndsqalaqad vsiamgkgsd
      661 iaidvakitl issdlrqvpk alqlsrltvk tirqnlfwaf iynligipia agvlypfngf
      721 llnpmiagaa malssvsvvs nslrlklakl ns
//
LOCUS       WP_285056446             284 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Pedobacter ginsengisoli].
ACCESSION   WP_285056446
VERSION     WP_285056446.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..284
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32531
     Region          43..227
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mnifkvpewi sqfnfgyqsf deipeqtfnt irrdlehivs nepvvsilis ayneevnvlk
       61 claslsktks shpleiivtn nnsndntqlt ldklnvknvf qgiqgwgpar qmglehakgt
      121 yvlladadci ypgtwvdemm kvltkpgivc vygrysfipe pgfpryklyi leqlkniiae
      181 yrqlkrpyln tygismgfvk ayalkigfim ekvrgedgrl sfdlmkygki aqvrskratv
      241 wtgprtlerd gsfskvltkr itkelkrfft llspekphdt kklk
//
LOCUS       WP_285056506             491 aa            linear   BCT 25-DEC-2024
DEFINITION  TPM domain-containing protein [Pedobacter ginsengisoli].
ACCESSION   WP_285056506
VERSION     WP_285056506.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Sirpio,S., Allahverdiyeva,Y., Suorsa,M., Paakkarinen,V.,
            Vainonen,J., Battchikova,N. and Aro,E.M.
  TITLE     TLP18.3, a novel thylakoid lumen protein regulating photosystem II
            repair cycle
  JOURNAL   Biochem J 406 (3), 415-425 (2007)
   PUBMED   17576201
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..491
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54527
     Region          26..>188
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mkkstlflff silffmagcs qqshketisg ipdpktlnet yvsnpdqlld petvsdlnak
       61 lstldqagia hidvvfvkti gelvpkevah elfntwkigs ketnngllil ivqdqkrief
      121 etgyglegvl pdiicyriqq qymipyarln dfnsavtrgv navvshltsn papnltdtag
      181 mgsteltitp peslqsltdm dsmysskepg diyslilaii yfiisiitgi alskkaslri
      241 liilfiftap vlsvvqlnld hpvswhnira llvaytflli ythihiflls wisassfkvg
      301 tqheqylkrr ntfaamewlt kvfafpflwl fwkkhqatle alryenince hcgtlmtlts
      361 edkddeflsk gqakeeeifs idydvwvckd celnkildys nlkskareck fchfttslfs
      421 rretieqatt snpgygydyf vcancgketk kqfiiakist sgsssssgss sgssssssgg
      481 ssggggagss w
//
LOCUS       WP_285056589             389 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Pedobacter ginsengisoli].
ACCESSION   WP_285056589
VERSION     WP_285056589.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..389
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=43269
     Region          4..380
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mklknkqvav igggpggltl akllqlkavs vkvyerdfnk darvqgspld lheesglaal
       61 rkaglleafk qnfmpgadrm iianelaevf lsdhenkpea dfgneyfrpe idrgslrkil
      121 leslqtdtvv wdshfitmda qnegwllhfk nqpsayadlv iaadganski rpfitdlkpf
      181 ysgitmlegn iynaektaph inallnggki mafgnaknll lgqkgngeig fyasfktged
      241 wavtnglnyh dhtqllnwfk ttyaewssiw yelfentevp fiprpiycas pdqdwdtlpn
      301 ltmlgdaahv mppfagegvn mamldalels efltdnqyss iqhaishyet amrkraataa
      361 keslengerm hsenslrdml nmfgghmvt
//
LOCUS       WP_285056599             377 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285056599
VERSION     WP_285056599.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..377
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=43528
     Region          <256..352
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkfdvfsliv llgasqalff siylffapah nkiqkcslaf fifilsyngf etlnwsself
       61 syfpffelcs filifglgps iylyvrsfrt vsatlknwph fsilwlalfc riwilvtwil
      121 qvngkkgfvd vrvlndwfcl iaeplsvlvf tvylilaire yrnlasehaq qdnreagekt
      181 mimrwlktll fvlvifnllw iatvspflav lgdkkyymie iaavifvywi gyagyhrsri
      241 iyvsqqkkta syfdnleage iersvaalel amekdqlyld pelnlnslaa hlnmhpkmls
      301 avlnqvlqkg fseyvnawrv eavkrmildp dkqhltitgi afdcgstlsq lfsgllklrl
      361 vkhpviiyem pfksrie
//
LOCUS       WP_285056629             366 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285056629
VERSION     WP_285056629.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..366
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40222
     Region          31..366
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mlpmrkmlfl acavaflcpl fclsqytqre araiarfene lkasvaddgi dgsisaaivk
       61 ndkviwakaf gyanrdtkkl adtgtiyrmg sitktftstl lmmlvedktv llddpaekyv
      121 pevariigyg edtkftlrql ashtsglyry aahesvavgg envwqrllla dlptasfasr
      181 pgkqwlysdl ghailqlalq raahisyvtm vkeriiyplh mthtfisidp nrenlaqgld
      241 nrngtadagl prrmhvgrgp aaangslyst padlakffst fmvqpgllsk asirkmqqip
      301 rggkdyglgm fvipgsdvig hdgwvpgyta qfsieldkky gviimrnyna sgvnlsetag
      361 rlwegi
//
LOCUS       WP_285056666             909 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Pedobacter ginsengisoli].
ACCESSION   WP_285056666
VERSION     WP_285056666.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 909)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..909
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..909
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=103371
     Region          599..852
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mkllkshytf iltllfvcsa taqkkvidet ayrnwpsvgy aaitnngkyv cytienktss
       61 knalvlksid nrweknisgv igfssiskdg kyavclnqkd slvivtlgkd qirslpnvas
      121 frmfkseggd wifykltnsn kelgiynlit akeqihhgii eyilgddght lvlqierkin
      181 ktisqeikwl dlntgkcdli wqgleansii ldsehnqlaf iskdslfhyn rnterttcli
      241 nqenieiksd ltlggidrfs ingdklfikl reeskpkpvs daveiwsyld yklqsqqkee
      301 lglksyaavv dlskrkilrl eqqfenaqfn dhpnqsdtig ivtyqksdgr sgevewnlag
      361 risyslvsvk tgkrtkieys ptispkgkfa vyfdikrkcf vsyniktgvp knismqmmef
      421 lkrtsihkgi ecgivgwlan eeavllndgy diwnldllgl rppinltngv grksnivfsi
      481 vydhyndrtf erknrlilsa fdlgskkngf yyikqldkqn dpeiltmepr ifitnsayvp
      541 snvdmapika knaniyivrr msafeapnff stmdfksfkr lsilhpekey nwyttelhsw
      601 ksldgrtlqg ilykpedfnp nkkypvifhy yerksdglna fikpeplcdg ctinipsyvs
      661 ngylvftpdi yyntgnpmkg tfdavvsaae yvrampfvnp rqlglqgcsf gaiqtnylia
      721 hsnlfaaacs ssgiadwvsn ygrigiggss lqgftetgql rmgttlwesp dryiktspif
      781 ylnrietpll imhtkndnic afddaielfs glrrlgkkaw mlaysqgnhg lrgeeardfs
      841 vrmmqffdhy lrnkaapvwm ldgipasrrg lddglslddr qrvpgpglli peeqrkmdsi
      901 vvknnhdnf
//
LOCUS       WP_285056658             233 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Pedobacter ginsengisoli].
ACCESSION   WP_285056658
VERSION     WP_285056658.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 233)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 233)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 233)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..233
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=26239
     Region          1..225
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mlraiaidde pialeiiknl aaevpfidlr ecftnalsav sllhqqqvdl lfldikmpgi
       61 sgldfiqtvs qpplviftta ysehavqsfe lnaidyllkp fsaerflkac nkaaeqfefr
      121 rsypqangpe paifiksgye hvrvelsaih yaeslgnyvr fqvdgppils rltmnetesl
      181 lpktsfirih rsyivarqli tridktsvwv gqtelplgsa yrqeldnlik nks
//
LOCUS       WP_285056711             524 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pedobacter ginsengisoli].
ACCESSION   WP_285056711
VERSION     WP_285056711.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 524)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 524)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 524)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..524
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=59885
     Region          73..520
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mshpilqrli sehlgssfvp epykrlfddl dialrqlsad tffnsmaevf ysvsmqnnrn
       61 sellqmspac ksvygynaee fftdpdlwfk vildedkhlv tsgmpllaag qttdseyril
      121 hkdgsirwve skitpmldeh kklvridgii fdittrkeae larmqadlkf raliensmda
      181 itvsndklvf tfasssmsvi tgvspdefvg tsilkyihpe drermgdllg lllkepgkaf
      241 lfqmrikrsd gqwrwtegyv snlldepavn gyianfrdvt errqyeaale asnaqlaktn
      301 qeldrfvysv shdlraplas ilglilltqh eatdqnllen lsmmkqsvek ldvfildild
      361 yarnarmeik srkidfpeml eqiktdlkfi naadnskfdi rieiedndaf ysdrkrihvi
      421 lnnlisnair ysnpqeenpf vevkiyfdsc gawllvkdng igigeahhek ifdmfyrvsk
      481 ksngsglgly lvketveklk gtiefssepn vgtrfliflp nmmp
//
LOCUS       WP_285056760             558 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF4091 domain-containing protein [Pedobacter ginsengisoli].
ACCESSION   WP_285056760
VERSION     WP_285056760.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10594704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..558
                     /product="DUF4091 domain-containing protein"
                     /calculated_mol_wt=63682
     Region          <125..>159
                     /region_name="DUF6067"
                     /note="Family of unknown function (DUF6067); pfam19543"
                     /db_xref="CDD:437375"
     Region          445..517
                     /region_name="DUF4091"
                     /note="Domain of unknown function (DUF4091); pfam13320"
                     /db_xref="CDD:463843"
ORIGIN      
        1 mkiflllfml pgllfaqnnl riyqldplek vlkdrtyfid epdtirvakg etatlqlvik
       61 skvdlqkvsi qaanaitken sqplkpsqmg fvgyvglgrt vpspgrnqli spsgyfpdpi
      121 ftdstfnlpa gepqsiwiti pvpieasqgi yrgsvkisal ssgksiiqnr nfvmrvypvt
      181 iaetslwvtn wihhtpesls flnngkpvef yterywelig liaqrikgtg qnvvmlpvqt
      241 lvqykidgdk ysfdftyldr mvsiyqkagv lkrmagshvg yrmgdwtsqf gvdvpllene
      301 kismhrmpis dsraknyldq ffpalmahlk lkgldknymq hvsdepvaen igsykaiaay
      361 vkklipgtki idanigsdli gsidvwvpvl dqlakeydfy kkrqkagdev wfytclgpqg
      421 nyanrfieqp limprllhwl nykygvtgyl hwgltawhmp yrkdlyndvt gmfddgnvvp
      481 ggdsyivypa ynklyssirl eamrdgindy ellrqlekkd pdlvkkiina tvfkfdhydi
      541 dikafrdkrk qilerlsr
//
LOCUS       WP_285056816             226 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Fusobacterium
            necrophorum].
ACCESSION   WP_285056816
VERSION     WP_285056816.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..226
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=26661
     Region          <59..187
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mkmlkiikit rlselningi vqllnddyiv vviiattnsf minectqymn knqikimfky
       61 kkendrinya atkaivnllf skieklkyqe irwqygkynk pyienkskik fnishtiecs
      121 ivtfsrnnig vdienlkrni dyseiknnff mnskniltln dfykhwvske aylkykgvgl
      181 tqslesvevi dendnavkvi drknniqkei lifdkekenf ifaicy
//
LOCUS       WP_285056843             302 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285056843
VERSION     WP_285056843.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..302
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33100
     Region          54..298
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mnfktqtitt pksmnltrki fsglclllil gacksmnsnk sgssaknpes klgwelgsqa
       61 ytfrmftfae aikkidscnl ryveafpgqk igggiegtmg pdmddakrka vlemlkannv
      121 kvvafgvtga nseadwvklf efckamgiht itsepnekdi pllskladqy qinvaihnhp
      181 dpshywnpdi vlnaikgqsk rigacadigh wvrsgldpve clkkleghvl hshmkdlhek
      241 gkgghdvhwg egvsdipavi aelkrqnfkg aisaeyeynw lsnsadvaas vvnfrnlvtk
      301 tn
//
LOCUS       WP_285056667             417 aa            linear   BCT 25-DEC-2024
DEFINITION  thioredoxin family protein [Pedobacter ginsengisoli].
ACCESSION   WP_285056667
VERSION     WP_285056667.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..417
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=48293
     Region          1..145
                     /region_name="SoxW"
                     /note="Thioredoxin-related protein SoxW [Posttranslational
                     modification, protein turnover, chaperones]; COG2143"
                     /db_xref="CDD:441746"
     Region          <304..399
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
ORIGIN      
        1 mkktvlslal igltslafaq ekgiafekgl nwdqtkakar tenkyifvdv fatwcapckw
       61 mdknvfdseg lgkyindrfi sfkvqgdtsi edseqtkkyy seakqlisnf kvrsyptflf
      121 fspkgelvhq fsgavddtaf itivkealtp ekqystllrk fnkgqlryeq mpllaktakq
      181 lldtnivhrv adcyisefll klketelfta dhltfindfi vdtksegfkf fmkytkkina
      241 vlgdnkaeya irstiarecl pspstwkttk pdwdslqkvm eenfgplgke vmfgnrmmyc
      301 rdvkdwqnfg kcfvlyfeka lkrpeylinn iawtvfeqvt dqdvleyaik vmrydietwd
      361 qqaadaydty anllyktgrk slavdweeka vklkkgapde siykdtlqkm lkgektw
//
LOCUS       WP_285056928             133 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Pedobacter ginsengisoli].
ACCESSION   WP_285056928
VERSION     WP_285056928.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..133
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=14542
     Region          1..133
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mnlrkrnkgt vevhtsalnd imfflllffl lasavvnpqv vklllpkses gqqsnaqktv
       61 tvsiddklny tinkkpttle nlpaeieayq kaapdltivl yaagsvsidn tmlvydvank
      121 lklkvvlave pkk
//
LOCUS       WP_285057026             406 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Pedobacter ginsengisoli].
ACCESSION   WP_285057026
VERSION     WP_285057026.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 406)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..406
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45961
     Region          26..241
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          147..404
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnteyfiagr ialksertfs klivriaiag vmlslavmml svaiikgfkt eiqekvrgyi
       61 gdvrifkfdl nnsfelspfv papetinnlk knpeveyfqp yatkpaiisa nneveginfk
      121 gidktfnwdy irkhlvsgtv idfsdstkat rqimisqfta srmnlkigdn fimyfvqdpp
      181 rkrpfkivgi ynigveeidk nfvigdlnli rrlnnwkade iggieirikd fsrlkqtsad
      241 iykgleiklk sesvqeyfpa iftwlslldv nttvllvlmm vvgvinmita llimilertn
      301 migllksmgm tdvsimkifl ynaiylvgig lllgnilglg lgfiqqythv fkldqssyyl
      361 syvpieihfl dvlllniatv vicflvliip smlvskispl kairfk
//
LOCUS       WP_285057029             447 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285057029
VERSION     WP_285057029.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..447
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=50276
     Region          19..391
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mvtvnrqtav kkkgrgplfn rinkwlhlwl glssgiivli vcltgciwvf hdeiegllep
       61 etkvekqdkp vltpsqltai afqnypdkvp ayanyqqgra inltlkgptd egrrgggtlm
      121 kinpytgevi skvvrqkdev dffrfilngh rflwlpleig rpvvnygtlv fvvllitgli
      181 wwypkkwnks trdksfkikw gasfkrvnld lhnvlgfysl lfllaialtg mvygikwyse
      241 glywvtsgge klaeykrles dslqagkhys pkqamdlawn kvigkhpesm gfyynfpdis
      301 kakssinitv ypsagqfyns egytfdqhtl kelkredays vayanasfgq klrkmnydih
      361 vgsilgfpgk vlaflvtlig aslpvtgfli wfgrkfkkkk gkkgddtgtg aadevadkpa
      421 vkprpgvitk eqepvlaana ridrsyn
//
LOCUS       WP_285057343             167 aa            linear   BCT 25-DEC-2024
DEFINITION  SixA phosphatase family protein [Pedobacter ginsengisoli].
ACCESSION   WP_285057343
VERSION     WP_285057343.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..167
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18760
     Region          5..161
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mtkqlllirh gksewgnahl adfdrplnpr ghrnapemaa rlaykqfipe livsspalra
       61 ittarhfsqv wkipaeqire easvyeadtk allkvvnhfd nkynkialfg hnpgftdfan
      121 yltdagiyni ptcgavlief mtddwqeash stgslvlfdy pksqdtd
//
LOCUS       WP_285057364             339 aa            linear   BCT 25-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285057364
VERSION     WP_285057364.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Rengstl,B., Oster,U., Stengel,A. and Nickelsen,J.
  TITLE     An intermediate membrane subfraction in cyanobacteria is involved
            in an assembly network for Photosystem II biogenesis
  JOURNAL   J Biol Chem 286 (24), 21944-21951 (2011)
   PUBMED   21531723
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Komenda,J., Nickelsen,J., Tichy,M., Prasil,O., Eichacker,L.A. and
            Nixon,P.J.
  TITLE     The cyanobacterial homologue of HCF136/YCF48 is a component of an
            early photosystem II assembly complex and is important for both the
            efficient assembly and repair of photosystem II in Synechocystis
            sp. PCC 6803
  JOURNAL   J Biol Chem 283 (33), 22390-22399 (2008)
   PUBMED   18550538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..339
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=36405
     Region          39..206
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          145..303
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
ORIGIN      
        1 mktllisalf fpvlclaqsy nlkpvttgen tsirgmsvvs dkvawvsgsn gsigktldgg
       61 mtwiwtkpag yekldfrdie afdenkaviv nagspafill tsdggknwre cyknldsaif
      121 ldgmgfwdaq ngmifgdpir nkmqllktrd ggmnwqdvsg nlktemkvge agfaasgtti
      181 ttygkgnvwi atggsvsniy fsdnfgyswk vykcpiiqge sstgpfsmaf fdakngvvvg
      241 gnylkdtent nnvlltgdgg kswkkparpv tgyrsgvtyi nkkvllatgs sgtdvsndgg
      301 mtwhnisgls fnviqksktg glillagnkg eiyqliigr
//
LOCUS       WP_285057449             163 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Pedobacter ginsengisoli].
ACCESSION   WP_285057449
VERSION     WP_285057449.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..163
                     /product="metallophosphoesterase family protein"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18009
     Region          4..153
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mvtigllsdt hgflddavfk hfadcdeiwh agdfgpevad klaafkplrg vygnidgkei
       61 raefpehirf siegldvwit higgypgkys lqvkgeiytk ppklficghs hilkvmydkk
      121 idclhinpga agnsgwhrvk tlikfsvtdg kihnlaaiei gnr
//
LOCUS       WP_285057464             475 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Pedobacter ginsengisoli].
ACCESSION   WP_285057464
VERSION     WP_285057464.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..475
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=54876
     Region          203..452
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          337..>454
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Site            order(351..352,355..356,358,386,389..390,393..394,
                     396..397,420,428..429,432..433,436)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          351..379
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          384..414
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          419..452
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkanfvfdpn saaaykaifd lrlndarryi aeekskypqn giaillenyv dyfqlltsds
       61 kadydkfktr rseridalee ndenspyylf aqaevylqwg likakfgdyt sstldlrkaq
      121 gllkknnekf rdflpnqksl alievvfgai psnlkgiadf igvrgniskg vrqleafksn
      181 iagtkynfyd deaifllcfm didllhnrgn ytklnsylse msdksmlkty lqgyvafktg
      241 hndtaityfe nisesnqytp mptvqyllgn aklcrmdsda hvyltnylks yrgtnyikdt
      301 ylklayhyll kgdmlgysny lklvrskgya idekdkqalk eandakpdtd llrarfyfdg
      361 gyypkalaql qnkrqnelkl lrdqielyyr lgriydrmns fneaitnyqk ainlgrneaf
      421 yyaansalfs gmlyehkkdh akaaayynmt lkmkgheyqn sidtqakegl srikq
//
LOCUS       WP_285057643             238 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Fusobacterium
            necrophorum].
ACCESSION   WP_285057643
VERSION     WP_285057643.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..238
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27929
     Region          1..139
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mykhfskiyd nfmqhadytk wkeeiekliv lgqpkgkell elgcgtgell krfqkeyhch
       61 gldisehmlk vaqeklgapk vplflgdmvd fdtgerydii lsifdtvnhi idmidlkwhf
      121 rsvfanlnpg giyifdmvdr afmdemfpng vfvdvrddlt viwehevedg idyidatyft
      181 hlvgsryrrv eetytkkiyh kreiehairr snlkiqklva ntgiagnryl yllkkeel
//
LOCUS       WP_285057721             365 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Pedobacter ginsengisoli].
ACCESSION   WP_285057721
VERSION     WP_285057721.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..365
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41248
     Region          13..364
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mqekvpgpei leskqhfeil dglrgiaafa ivifhfmemv yppgdnfiah gflavdfffc
       61 lsgfviayay ddrlqkmgia tfftsrlirl hplvilgsvl gllafiydpf ggnpevysag
      121 kvalificsi llipfpvite rsfnlfglna pswslfweyv anilyafvls rlhrryllal
      181 alisvfvlcy asyhaggsll ggwagenfwd ggarifysfl agmliyrfnw iiktklgfag
      241 lsillslafv mpyttwnwlt eplvvlvyfp vlialgagar isqrlkkicv ffgkisyply
      301 mthyaviwmf lnyytghkpg tsqlvliiit gtglllliay lvmifydtpi rryltsrrti
      361 nrpsk
//
LOCUS       WP_285057832             102 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285057832
VERSION     WP_285057832.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..102
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=11761
     Region          1..92
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mvlevailyi rtgladqfea dfkvagqyis sidgyirhtl qkcvevdhky illvewetme
       61 ahtvgfresa vykdwkallh nyydpfpive hylevplssp ar
//
LOCUS       WP_285057891             249 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Fusobacterium necrophorum].
ACCESSION   WP_285057891
VERSION     WP_285057891.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..249
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=28919
     Region          <2..228
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mlkrcfayak hhrkieknit eqllcisyks krvayitpkq fyalveemkt fttledleek
       61 ilfletlflt girhsecral qvfkfnften tvlisnaiys dqvgvweltd pktetsfrvi
      121 svpeyhmrki kcfvektgkk padflfaypd gtpriftfak wplekagkrl gikisthglr
      181 hshatflrqs gldlekiqkr lghsnvlitl hyshaklnee dvvdviektc yplsrgeene
      241 rkennesdi
//
LOCUS       WP_285057972             140 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Pedobacter ginsengisoli].
ACCESSION   WP_285057972
VERSION     WP_285057972.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 140)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..140
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15708
     Region          <36..122
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mrktlltflt lsviasiiys cqnsdelkqq iyytngrdly ikhcqnchga ngeglgklvp
       61 pltdtvylkq nkqklaclik ngsdttvtih nqdyegkmpd naqlfdidia qlivyitnsy
      121 gnkqgmykpe qiaedlknck
//
LOCUS       WP_285058140             211 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Pedobacter ginsengisoli].
ACCESSION   WP_285058140
VERSION     WP_285058140.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..211
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23919
     Region          43..141
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mvnenekpef wetafgekre mwgfepansa vltkdfflqk svknilipgi gygrnaqifk
       61 esgmtvtgie isktaiemar rhygsdmvih hgsvndmpfd knkydgifcy alihlldsnd
      121 reklirdcyd qlsdngymvf taiskaarty gqgnfisedl yeifpgvnmf fydrasiese
      181 fgsaglfeit einesqpffl ikckkgngqs q
//
LOCUS       WP_285058202             276 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Pedobacter ginsengisoli].
ACCESSION   WP_285058202
VERSION     WP_285058202.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 276)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 276)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..276
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=32392
     Region          <139..260
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 msfldrqfip pfsrrhvtvk hallhtlywv liaaffayek rylihkanlp yflfcvigrv
       61 imlvaiayln iqyflpkyll rkqylryfll vllsvagymv aqslfdyfly gyvigpmrns
      121 nlmetmsynf fstiwylalm vavklsidwy elqnkpaett eplpeftfvk sgtqkikiiy
      181 sevthieglk dyaiahttan qkivikgsik ymneifpeal firvhksfiv akdkirqiek
      241 nkiiinehqi pigrsykqel gkhllnnnfs itklte
//
LOCUS       WP_285058246             365 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Pedobacter ginsengisoli].
ACCESSION   WP_285058246
VERSION     WP_285058246.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..365
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=41603
     Region          34..61
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <44..212
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(71..72,75..76,78,101,105..106,109..110,112..113,136,
                     139..140,143..144,147)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          71..94
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          99..130
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          135..163
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mnkrllnkcl yasliailff sapvfsqtdt dpnrakliea vklmdkgevd asitilkdlq
       61 kvdpnnynyn yelayafflk kdypaaievl eklktnkdvs dlvyqllgnt ydmsekaeka
      121 vqtyaeglqr fpnsgklyle sgvmnlkknd laaatkvfqk gtevdpkfps nyywlskvwa
      181 ttpeklwtlm ygeifmnles ntkrtaeisk llfdtyknei kvtspghfsv sfsnnnvvnp
      241 neknpdkllp ygvavyerll misalglkev nintldsira nfageyfkgk tavtypnvlf
      301 syqkkiadag hinsynhwvl qkgdeelfkt wvaanadkwq dflkwfaanr lildsgnrfi
      361 isdyq
//
LOCUS       WP_285058252             353 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285058252
VERSION     WP_285058252.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..353
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38891
     Region          77..324
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 msanisrkqf irntaiaaaa lplglstlna apatslstaa atslndappa qntglpeaep
       61 sqkpdpaaap addklsisif skhlhwlnyk dmaalaaqlg ydgvdltvrd kghvlpenva
      121 kdlpkaveai rnaglevyti ttdirtadep htqailktaa svgiknyrmg wygytgkgiq
      181 adletfkkdl kglatlneky qihgdyenht erfggpiwdl wlslkdldpk wtgiqfdirh
      241 atvdgaeawp rnlelihnhl gsitikdfhw ekkdgkwttq nvalgqgmid fkkyfrllkq
      301 ygfkkpisqh feypiggaes ggrklsipkd evishmqkdl qtlkgwlkea elg
//
LOCUS       WP_285058269             329 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285058269
VERSION     WP_285058269.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..329
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=36552
     Region          4..325
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mnkkvlitga tgfvgyhlie kavgagldvy aavrpnsnrs hlsefkiryi dlnytavgdl
       61 vktleehqfn yiihaagttk aktsadynki naeytknlal aavtakisle kfvfvsslaa
      121 lgplidlser iqddtpahpv tnygasklla erylleiagl pliiirptav ygprekdifi
      181 lfksisrgle phigsfkqhl sfvyvkdlad vivnalfatv ngkqynvsdg yvynryvlad
      241 tvkkalnkkt fkfhipvgvv slmasfmdll yryskntpal nkekmaelta vnwacnidsa
      301 kkdlgyapqf dlgrgiqdti kwykenswl
//
LOCUS       WP_285058278            1874 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Pedobacter ginsengisoli].
ACCESSION   WP_285058278
VERSION     WP_285058278.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1874)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1874)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1874)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1874)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1874
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..1874
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=207253
     Region          518..1874
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mesqqssppd nflkknkial tavlvvgiii avaaffffkk ekhhdynqky skyiesytsg
       61 tvskksfirv hlanqvktls dvgvadnrdl fsfspsvkgk tywidaqtve frpdeplksg
      121 eaydatfnln kvteteegle efdfnfrvik pglsltqngl vsqnntsldy mklsgeists
      181 dqedpkaiek aleldfgqpl kikwahnpek nsyvfnidsi kktktdtelt lkwsgdpiya
      241 dnegemkvqv palgvfkvld ikavqgqedy alvqfsepvg vaqdlsgmls lsgisdlrft
      301 idasqvkiya pvnlegaytv tvnpgvenin gkklgvektg aisfenklps vtisgsgtil
      361 pnsgklvmpf eavnlkavdv tiikiyenni pqffqnnnyk dgnelrrvgk pvvektirld
      421 edkalnlhkk nrfvldldkl lktepgamyr itigfrqsyh vyqcgtedgn tassglseee
      481 deyhgyseni dedddfwsry sgyypdnyrw edrenpckps yyttdkwasr nvmasnigli
      541 akrgndnsmm ivatdlltaq pmsgvtlell dyqrqlittv ktggdgmvsf dlkrkpflli
      601 akngeergyl kmddgsslpl srfdvsgdvv qnglkgfiyg ergvwrpgds lylsfiledk
      661 lkklpggypv tfelynpqgq lirrsingkp lngfyafktv testaptgnw lakvkaggsv
      721 fsktikietv mpnrlkinfn tgdvgylgig gasyatlsan wlfgspgknl kakvdvnlnt
      781 mktmfkgfea yefdnptvvf qsqvktifdg klndngvaqv stslnenkta pgmlkanftt
      841 kvfeaggnfs idnfsipyhv yenyygiktp egerlsgmlv tgkdhtvniv nvdrngklvk
      901 ggktvdvely kvqwrwwweq ddensfanft qnsynklvkk enitlqdgkg nwnlrinepe
      961 wgrylilvrd lngghvtgks vyidwpgwaq reqannptea smlsftsnkp kynvgedvvl
     1021 tipsgkggra lisiengsrv lktfwtdtkp gqtqftfkae aamapnvfan vtllqphaqt
     1081 vndlpirmyg aiplliedpq tilkpvikma dkikpetent itiaeqngka mtytiaivde
     1141 glldltrfkt pdphgifyar eglgvktwdl fdyvlgawgg nlerilsigg dgsinrnlnp
     1201 akanrfvpvv kylgpfalgk geskvhkfkl pqyigavram vvagqdgayg faeksvqvkk
     1261 plmllatlpr vigpgesftl patifatepn lknvsvqlka tnlqviggas kqlafkqpge
     1321 qlayfqikvp eligiakvqi taqsgtekav ydvemdirnp npyvtnvvsa viqpgsnwsv
     1381 gyspigmngt nsgsvelsai ppidlkkrls ylmqyphgcv eqttssvfpq lfldkltaln
     1441 esqkaktemn ikaginrlrg fqtpdgglsy wpgegnsdew gtnyaghfli eaqnvgytlp
     1501 vgmadellry lktkasawvp nstnfyggdl sqayrlyvla lakrpdiaam nrlrgfqyls
     1561 vtakwrlaaa yklagqndaa gnlikglste iqpynqlggt ygsdlrdeam iletltllgr
     1621 tssaaqilqt vaaemgkdsw ystqttaysl laiakfcgqt sssaslkysy tvdgkkgnvn
     1681 saqyiistpl tfkggssagq gavsvtntgk gvlfarlilq gqpsagqntf lpnnpdaldm
     1741 sisykllngk pldpgilrqg tdfyaevtik npgrmgyyeq maltqifpsg weiintrvnd
     1801 nesiiasspy tyrdirddrv ftyfnlrene tvvykvllna syigryylsa tqceamynnn
     1861 isateagkwv qvvk
//
LOCUS       WP_285058313             382 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Pedobacter ginsengisoli].
ACCESSION   WP_285058313
VERSION     WP_285058313.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..382
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=42960
     Region          137..160
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          138..381
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          170..194
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          200..228
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          267..297
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mskisflnit llvlmtsnla fsqrsqvqia rnsigklhva inakaepakq lgilgegika
       61 seaaqsdrkt kkwpetwaik aylssyisii dadegnadky ytlaidaids arrldkfqan
      121 srlidaaiyn vnirkqnkan tafnnndfan aykllkdvsd ffpkdtvlai ntalaaqnvq
      181 aydnalvyfk rakdngvknp vlfqnlsniy vskfenelai ktledgikln pydanltnsy
      241 inllldneky etaikiient lkvdsknkll yflygylhqn nsnystaela ynkalsiden
      301 yfdalyqmgl ayvgsantal kssgqdksqk fisfinraei allqaheinq ndkstvqlli
      361 diytrknrld kvqelkskle ef
//
LOCUS       WP_285058395             319 aa            linear   BCT 25-DEC-2024
DEFINITION  formylglycine-generating enzyme family protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285058395
VERSION     WP_285058395.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..319
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=36299
     Region          30..299
                     /region_name="YfmG"
                     /note="Formylglycine-generating enzyme, required for
                     sulfatase activity, contains SUMF1/FGE domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1262"
                     /db_xref="CDD:440874"
ORIGIN      
        1 mklsfslfvp lvlfytqtan aqtkaesykq qidgttlsfe mqaipageft mgskkgkkde
       61 lplhkvklaa fwmgkhevtw diyepflyrd yekthsvspv penvdavtrp tkpyldmtfg
      121 mgkagqpala mthynaiqyc kwlyartgvf yrlpteaewe yasragtste yffgddeskl
      181 seygwfkdns ggkthpvglk kpnpwglfdi ygnvaewtyd qyipdfyagn vsdnpvavpd
      241 klypqvvrgg syddlakdsr saarlasdpv wkqldpqmpk snwwfpeapf vglrlvrpvk
      301 tpskedieay ynkkpipdy
//
LOCUS       WP_285058434             429 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Pedobacter ginsengisoli].
ACCESSION   WP_285058434
VERSION     WP_285058434.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..429
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49711
     Region          277..421
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mktltlimtf llsalmgtna qnspvksead lywdtmpkkt fiagsislaa gpeeiqipds
       61 iqvdlqingd kqgllakrre slickniyde ifrrmlrdwg iefwrrfpdd prrfqwlvnt
      121 clmepayfvn lrngalatie erylialdti akkqwkelsq kyfqevslst elqepakknt
      181 lrfqfnqirn qrwrdsenek fnidefferi iafvtrygds gtsqsfkeil rfkadlglns
      241 kdikhlidll katsfesfqk eadylekivr leeeplslna ksikgdevdl nqfrdnlvli
      301 dfwniycaac ilkmpeiktv yekykdqgfr visaclydng kfqknelgki kaiygkigad
      361 wplvllggdk gqqgrqifdt ydffgvpqll lldekgkllh yngdlenkgg leklvkehla
      421 krnniqksk
//
LOCUS       WP_285058285             344 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Pedobacter
            ginsengisoli].
ACCESSION   WP_285058285
VERSION     WP_285058285.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..344
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37555
     Region          70..>340
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 meelqrikrr gfitksglla gsaalslssf dalgafsadh rkrntlnage kdalnrlgad
       61 qqalvngevv klcilhtndv hsriepfamd gskyqglggt arraaligki radeanvlll
      121 dagdifqgtp yfnlyggeie mklmtlmayd gatmgnhdfd nglegfhkql phakfpvics
      181 nydfsntvls kstvpfkvfh kgglkigvfg vgielkgivd dknygdtvyi dpvskanema
      241 lllkeelkcn lviclshlgy sykndkvsdk vlaaqtrnid liigghthtf mdvpedvmnl
      301 dglvttinqv gfaginlgrv dyyferykgk hvntgspyli snqv
//
LOCUS       WP_285058453             384 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285058453
VERSION     WP_285058453.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..384
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43432
     Region          18..376
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mktwklftla ltfiitkvaa qdashqidsl lkartetagi vglsaaiisd kgvlwskgyg
       61 yadkekqipy tpetimnigs vsksitgicv mravqenkls ldedinkylp fkvqnpyfpg
      121 dkitmrqlvv htsgiqdrep vysdtsyyyg gdakiplgef lkdylvpkgr fyqdsnfvka
      181 kpgtesyysn igaalagyiv ervtgmklne yskkflfdpl nlkntgwlls didtgkhsrl
      241 yerkgdtlsl vrwyglvtyp dggvrtsvsd lskillsiig sgkqilsaks raelwrpnft
      301 atdkpinyny dainynegvf wsmndlmrki ghigrdpgin tymyydkslk rgliifynts
      361 ipykdrqqfe tvydqlwhla sllk
//
LOCUS       WP_285058455             242 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Pedobacter ginsengisoli].
ACCESSION   WP_285058455
VERSION     WP_285058455.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..242
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27285
     Region          26..>151
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mliwvltgli ppgaiarqtv vsspdsltlf dkirnrqipv aiykprsgka kivifshgyg
       61 qnrpgtylay sylneylask gyfvisiqhe lstdslipss gipqvvrrpf wergaenilf
      121 vinelkrtnp eldfkhitli ghsngadmta lfpqtypgii dkiitldnrr mplprtaspk
      181 vyslrssdqp adegvlpnea eqqkygikii klpntihndm ddhannrqrn eireyvlsfl
      241 nd
//
LOCUS       WP_285058462             109 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Pedobacter ginsengisoli].
ACCESSION   WP_285058462
VERSION     WP_285058462.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 109)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 109)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 109)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 109)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..109
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12544
     Region          6..86
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 memrrdvfqa iadptrraii gllseqslnl nevaghfevs rpaiskhiki ltecglvmvl
       61 qkgrerfcsa dmdklkevdq wlshyrkfws rkldalgtfl erddaedrp
//
LOCUS       WP_285058474             303 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Pedobacter
            ginsengisoli].
ACCESSION   WP_285058474
VERSION     WP_285058474.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..303
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34750
     Region          41..293
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          205..287
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mlsnyfryls ptvfdqnwgi yvttsgyskv apfeeypngt hpeshhltwn rgrilndyyv
       61 vfiskgrgty asaltsptpv tagncfllyp gvwhrykpdp khgweeywvg fngsyisqll
      121 qntfarnrpv vnlgfntdml ilftrlidei rlsnvgypqq iagitlqilg lvnnavrnde
      181 raddpvgkli akarylires fensldmerl asdlpmgyss frkafkqvtg qspnqyhmei
      241 rmerarnlll mtllnineis dqlgfesvay fsklfkkkhg ispmnfrmer grnlnngled
      301 fav
//
LOCUS       WP_285058478            1027 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285058478
VERSION     WP_285058478.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=112660
     Region          35..1024
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkklllfrs lryysalfll lafylpsaaq tqlavtgtli dsvdaspipg atislegttv
       61 rvqtdangkf sinvpsggil svsyvgysnk kvtvqqagal tirlgaslqn lkevvvvsyg
      121 tqnrrevtga isqikasevk dmpvpnigqk lqgklagvqi nhnsgtpgse mtfrirgaas
      181 inagnnpliv idgfpsqsgl qslspdeiet itvlkdassa alygsraang vilvttkqak
      241 agqksldfsa yygaqsvpdr gkpdlmnaqe faqykkewye daaryegrtd gvpavyqnps
      301 qyasdpgtnw fdvllrnavs qnynlsysng mkdlksfmnl nynkqegvil nssderftar
      361 snntynpser ltlnanlels ygsnqvvpgl dngrniiena ylmdptlkyk npdgsypisf
      421 sqpgmfpnpn yyllvtqrvn ksraarvian gfaeyklidg lkfkstinvn tdntvnrrft
      481 pstaqgglgs appqpatgsy stsnfitwls entlnyeksl gkhnfealag ytyqkysaen
      541 sgingtqfpd dhiqwisaat trlgnvgade wsliryigrl kynydgkyla efalgrdgss
      601 kfgpnnkygn fpsvsigwva sdesfiqdlk avnflkfrgg ygrvgnnnig nysylaslat
      661 tnyvfdgkvv pgkslsgian ngltwettag ynfgfdlelf nsriaitydy ynkktdglly
      721 aidipmqagf snitsnigef nfwgnelsis trnltggftw ntsfnisfdr nkviklgtnn
      781 apiggyneyw ddnrtavgqp igmfygyind gvymtqqeyd tqphrsdsmv gtvrfkdvsg
      841 pngapdgkid tydrtfignp npkftygitn sfsykkfdls mvfagsvgnd iaddafqste
      901 nldgvfnvrk gvagrwrsee npgngeyprt rtgttepfrl ftsrqvfrad ylavknitlg
      961 ytlpvkdkqf fkslrayasa qnaviltkyp gmnpeagmsg lnglnqgrdf tgypiprvfs
     1021 iglnagf
//
LOCUS       WP_285058489            1058 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285058489
VERSION     WP_285058489.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=118033
     Region          48..1056
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkilillvy silgsayyvs aanagktgvf ngennlykin nnsslfqrvl tgtvndesgl
       61 pipnvtvkve ssvpvraatt nqegkysiqv ssdsevlafs yvgyktqkvt vgsnktldik
      121 lisdnsleev avvafgtqkk tdlvgsvvsv kvsdlkipss nlttalagri pgmiafqrga
      181 epgndnanff irgvttfgyk ndplilidnm evgttelarl qpddiasfsv mkdatstaly
      241 gargangvil ittkqgavgk aqislrvens lsssvrdiel adpvtfmkqa neavltrnpl
      301 gqvlysdeki antaagvnpy iypandwrel vfkdytanqr ynlnvsgggq varyfvsgal
      361 nkdngllkvd prnnfnnnid ltsyslrsnv ninltkttem vvrlsgsfde ytgprdggad
      421 mykkvvrsnp vlfpqyypld eqhqfvkhim fgnsdvggkn ylnpyadlvs gykdssrslm
      481 laqlelkqdl sfvtqglnfq mmantnraaf fdvsraynpy yynligynpe dntysidgmn
      541 edtgteyldy rpgervlnsv fyaqsqlnys rtfnkhgvsa llvtmlqnnl sangrdlqes
      601 lpsrnmglsg ratynydsry yleynfgyng serfaekrrf gyfpsagvaw tvsnekffsk
      661 mksvvnslrl ratyglignd aigtdrdrff ylsnvnmnaf eraayfgngl gaghslpgvn
      721 isryanedis wekstktnla levgffdklk itaevyseqr knilmtraai pvtmgltaev
      781 ranvgeasgk gtdlsfeytq nvgqdfwitg tgnftyarsk ftvyeepvyn ekyrsrighp
      841 ifqeygfiae rlfvddvear nsprqnfgpy gggdikytdv nrdgqitgad mvpignptlp
      901 eivygfgfss gfksfdfsaf fqglsnesfw idsrktspfd netqlikaya dshwsedsrd
      961 vyalwprlsp tinennnqrs twfmrdggfl rlkqveigyk lpesiqrrlh trnfriyana
     1021 tnlfniskfd lwdvemggeg lgypiqrvfn fginlsfk
//
LOCUS       WP_285058560             425 aa            linear   BCT 25-DEC-2024
DEFINITION  serine/threonine protein kinase [Pedobacter ginsengisoli].
ACCESSION   WP_285058560
VERSION     WP_285058560.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..425
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=46762
     Region          17..>295
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 makiftiteg lenmgalrtg gqgsvykgkr mgaiitavkl lptpihkent ddknfrdfqs
       61 eveklkkvne rpspnvvkil ssgltesgsl pfiemeyieg pdledllkap hnpvfsirea
      121 lklaeqlaaa lahchevgvr hgdiksnnvk fntatgnyil ldfglaimsd eqrrsslrna
      181 gavefmapeq ydgkmlfetd vysygvvlye llagnvpfpl vnkhesarnl vmvahiekpv
      241 pdllelrrth lpadwpedkk maemqvpgwl levigrclek lpekrykdgp elyeavcngm
      301 lskeevsgqf malqnenavl rnkikdherl aksrlliiaa lllgvfigaf aigssfnrkd
      361 pgdtagksgm pgpggkdtln nakpaavvqr petkladssa qkkksatpkk kkktkdglvd
      421 dvpyf
//
LOCUS       WP_285058618             379 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pedobacter ginsengisoli].
ACCESSION   WP_285058618
VERSION     WP_285058618.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..379
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41293
     Region          17..376
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtpaisywek lhffnfdlli igsgivglsa aialkekqps lniavlergl tpsgastkna
       61 gfacfgsvse lieqenncgt dglhqliknr wkgllklrnl lgdeaiaykn yggyelfrpa
      121 ekelssvcls kigyfnalik divnrpdtfk pvnhqiadfg fngvdtliln eceaqidsgr
      181 mmramlrkag eagilvfnnc kvtsfeqsdd gykvytadgn fncrklmlct nafakelape
      241 ldivpgrgqv iitrpvpglk vkgtfhynkg yyyfrnvdnr vllgggrnld faaeqttefg
      301 stavvqnall nlldevilpg agfeieqsws gimafgssit pivkeldngv fcalrcngmg
      361 iaignqtgcd aaelllkki
//
LOCUS       WP_285058717             204 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Kingella
            kingae].
ACCESSION   WP_285058717
VERSION     WP_285058717.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..204
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=23434
     Region          <60..129
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mqteftlyya andyaqhyap eklspndrlr vqqnpaleqr tswkmsraik avvpcsngvl
       61 shcryravwl tsksslhfgi diepiqsrdf sawrdwilsd decrwlqqqs cqiaahlilw
      121 tlkeslvkas ngqwadlaqv gllqheqqwq lhtqgqtgwf grvwqceqfl vacvayqsdl
      181 avqwqglgdc anrlphlrat flsv
//
LOCUS       WP_285058800             230 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease, partial [Fusobacterium
            necrophorum].
ACCESSION   WP_285058800
VERSION     WP_285058800.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..>230
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          32..>209
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mnpvknihqy nskkifkivi alfillfvsy isvftgiani nlkrvlatif egffyetepl
       61 sqremvvfld lrlarvvlgs iagfllavcg tvmqaitenk msspfttgis saasmgaals
      121 ilfftgkyvy fdfitiffaf sfgiicsllv ygisnlkamn kstliltgia fnylfssgna
      181 alqfianedv lssivnwtfg nlsgvswnki lilflillif fpyffinrys
//
LOCUS       WP_285058811             378 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Kingella kingae].
ACCESSION   WP_285058811
VERSION     WP_285058811.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..378
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=43405
     Region          4..378
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkilkaykfe lipngeqirk lkqfcgcsrf vfnralayqn eqyeanksfk fsytkltall
       61 pkwkrelvwl kdchsqvlqq slkdlesafk nffakrgdfp kfkrkgekds frfpqgckle
      121 qhnnriylpk igfiryrnsr aisgslknvt vsqkcgkwyv siqtefetet pkpnsgeigi
      181 dmgivrfatl sngeyfepin afkalkgkla klqkqfkhkt kfsknwqklk akiaklhhki
      241 snirknylhq isnqisqnha ivyvedlqva nmsksakgdv eqhgknvkqk sglnraildq
      301 swaefrrqla yklawnggfl favppqntsr ccpncghttk dnrqtqanfe cvecgyqnna
      361 dvvgainvlk rgqaiqaa
//
LOCUS       WP_285058846             179 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase, partial [Kingella kingae].
ACCESSION   WP_285058846
VERSION     WP_285058846.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         <1..179
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <1..178
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mlnlihdlmm lsaledpqqq tapkaacnis dlvkqivqda qclsagkhqi iadieadisl
       61 larerelyqa lsnlvfnavr hagegcqihi glqrianpnp ykpplvqfsv rdtgkgiape
      121 hlphltdrfy radsgrsren ggtglglaia khalanhqas lhirselgvg sefmtqlpt
//
LOCUS       WP_285058955             231 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Kingella kingae].
ACCESSION   WP_285058955
VERSION     WP_285058955.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..231
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=25351
     Region          118..220
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
ORIGIN      
        1 mtkllsliis llglaacats pqsappivqa asvptsipyp eptqaeqinq laiqvarleq
       61 qivvlteqln qhetkhhsrn tsrnqtkqpa pkrvtapavs qskpeastsp lsqaqtwykq
      121 gqyqkvldll rlhdsggngd anaqqsmill lqsnqklgyc qsviqigqrf atlfaqhdfa
      181 pealyavgqc qwqiqqrdia ketwrnlvlr ypntpaarra gssnpvkkdt p
//
LOCUS       WP_285059071             385 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Kingella kingae].
ACCESSION   WP_285059071
VERSION     WP_285059071.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..385
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=42681
     Region          1..381
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mqfstktiha aydadehqra impplyqnsm famheleeni pfrysrlanp trkiledtva
       61 elengthgfa fgsgmaaidc ifrtflqpnd tivavsdiyg gsydllhnvy akwgvnvifa
      121 dltkpenldk ilteqkvkmi wletpsnpll rvvdiellaq kakahgalvg idntfatpyl
      181 qnpldlgcdi vfhsatkylc ghsdvlmgva vvkdeklakp lqnmmvmtgg iagpmdcwlv
      241 lrgiktlsvr mkqhianaqi laerleqhpa iervfylglp shehhelakr qmrgfggvvt
      301 vylkndtrea vnsviknlhm lqlasslggv eslvnhcysq shsgmahdvk malgirvgll
      361 rfsvgiedie diyadidqal nttls
//
LOCUS       WP_285059090             275 aa            linear   BCT 25-DEC-2024
DEFINITION  CheR family methyltransferase [Pedobacter ginsengisoli].
ACCESSION   WP_285059090
VERSION     WP_285059090.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Crystal structure of the chemotaxis receptor methyltransferase CheR
            suggests a conserved structural motif for binding
            S-adenosylmethionine
  JOURNAL   Structure 5 (4), 545-558 (1997)
   PUBMED   9115443
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..275
                     /product="CheR family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32065
     Region          7..275
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mnsshpetit yeqlsdlinl irhthgfdfs dysaaslkrr vtrimqlqkl dlldlrtllt
       61 nnadyfesfl ievtvnvtem frdpsfyqsl tshvipylrs yqrikiwnag cstgeelysf
      121 ailfseenly drtffygtdi nndvleyakn giyalekmkq ysenyhktgt hhtlsdyyta
      181 kydaakinrs lkknvlfsvh nlasdgvfne fqviscrnvl iyfntdlqnr vidlfynsla
      241 nfgflclgsk etlryneigr fkivdkknni yqkia
//
LOCUS       WP_285059119             471 aa            linear   BCT 25-DEC-2024
DEFINITION  MBL fold metallo-hydrolase [Pedobacter ginsengisoli].
ACCESSION   WP_285059119
VERSION     WP_285059119.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..471
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51714
     Region          2..183
                     /region_name="POD-like_MBL-fold"
                     /note="ETHE1 (PDO type I), persulfide dioxygenase A (PDOA,
                     PDO type II) and related proteins; MBL-fold
                     metallo-hydrolase domain; cd07724"
                     /db_xref="CDD:293810"
     Site            order(54,58,110,133,136,140..142,183)
                     /site_type="active"
                     /db_xref="CDD:293810"
     Region          254..353
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
     Region          357..457
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 miieqiytgc laeaayyies ngeaaiidpl revspylrra eragarikyi fethfhadfv
       61 sghidlseks gakiiygpta ktsfesyiaa dgeefkigel tvialhtpgh tpesttyllk
      121 dgdgrpycif tgdtlfigdv grpdlaqqgd ltaedmastl ydslqdkili lpddvlvypa
      181 hgagsacgmn msretfdtlg hqkavnyalk aqtkeqfike vtdgilpppq yfaknadmnk
      241 ngyerfeevh ekglnpltpe efellanqtg avildtrpar vfaksfipss vnigldgqfa
      301 pwvgalitdl kqplllvgde gneeetitrl srvgydntig yleggiaawq aagkdtdtis
      361 sisaeafedi yrkdpdvhvl dvrkpgeyes ehlemtlarp ldyindwthd inpketyyih
      421 caggyrsmia asilkargvd qvvdiaggyg alkatnlkrt dfscpskamk i
//
LOCUS       WP_285059158             437 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Pedobacter ginsengisoli].
ACCESSION   WP_285059158
VERSION     WP_285059158.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..437
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50575
     Region          297..437
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mekratllpi iillnknahm kmkclliisl iifghysnan dtvnyqmqys nadrdwkvle
       61 ellkpanksg kqklyldesl gleyrnkgle fwykypndpr rydwfyftsg fpsdsagpky
      121 wsnietgatl ssekawyygq iipvnhnair rweliypkll kefmvsdisi kkkntiksiq
      181 lysylyhrin psyqasakld lkhvqrifks vaemfygdgf eivtgrsrni nfenaggisd
      241 pfriidgtli skyeiygltt keiiyflkpf ldssnphiqn wasektklls lknkffdfqa
      301 vsmngesysl segkgkvill dfwstscgac ikamprlkev yekykddgfe vfsisinpkg
      361 dkkdvekihn kigakwptfl iggeswkdke slgykiwnty nfqsvpqlfl ldkegklvay
      421 ngtlhsdleq ivkkllk
//
LOCUS       WP_285059176             638 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Pedobacter ginsengisoli].
ACCESSION   WP_285059176
VERSION     WP_285059176.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 638)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..638
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71624
     Region          1..539
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mrisklhien frsinaidle ldettvfiga nnsgksaiie avrialsrrw gqrgtgften
       61 dvhlvdentd prtappvkis fefiepvvns wpadmvadle eimiinevgl nkvafsityt
      121 wnidketfep aweflnqngv plppkrrsin lsgfydyilf lwlgalrdvd sefnsrsrnw
      181 ggllksvkvp qdleasiket ldlldaqlle vdpkltdiak tiglateiam edtpgaaklr
      241 mlpldvwdml sragvilrne eirpwlplgh hgqglqslsv mflfqaaaaq qlaeelhegt
      301 epifaieepe ahlhpqaart lwsrisalpg qklvtthspy fvqnvplhnl rivrfknget
      361 rvsaiprlip srlpwtekvn nlvagrgike fvknqtteti dilchfnkal sddlaacwst
      421 eadadavkge ietlrrigrv liskddendl sflgrrirge iffarrwilv egiseyllln
      481 algqvlgydl dqhgiaiidf qnngnagiya alaesfeipw hmitdgdaes eqfkkqllnr
      541 gfndqdladh fstltlpnsl edqlladghe mllreilrdi gvnqamtcti eefskklkgk
      601 ktaymsrlah iiakdtglaa qmpvqfvsli edlkakri
//
LOCUS       WP_285059217             237 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Pedobacter ginsengisoli].
ACCESSION   WP_285059217
VERSION     WP_285059217.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 237)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 237)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 237)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..237
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=26970
     Region          3..232
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mmtmrcivvd deplvrelle dhmsevpfle lvkscksale aleilqeeqi dlifldiqmp
       61 rlnglqflqs ldrpplvimv tayekyaves fnlqvadyit kpfsferflk acnraadlfr
      121 mmnsamsaat eknhdffvnv eythvkivaa didyieslkd yikiylssgt kpvltrmslk
      181 sieaklpagt fvrthksflv amskitavkr dfvcigatei pvsetfreni nkvlksh
//
LOCUS       WP_285059239             320 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Pedobacter ginsengisoli].
ACCESSION   WP_285059239
VERSION     WP_285059239.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..320
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35417
     Region          20..314
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mqfendikav dalhlaynni kseigkivig qeevvksvli sifsnghcll vgvpglaktl
       61 lvqtvadvmd lqfnriqftp dlmpsdiiga eilgddrnfk fihgpvfsni vladeinrtp
      121 pktqaallea mqekavtaag qrhvlpnpff vlatqnpieq egtyplpeaq ldrfmfnihl
      181 dypsfaeelt ivksttsnad vklkkiidak qiqyfqklir nipvtdnvve yavklasktr
      241 pntalatedv nkyinwgagp rasqflviga kchaaisgky spdiedvqav aepilrhriv
      301 rnyraeaegl sveqiiknlf
//
LOCUS       WP_285059257             320 aa            linear   BCT 25-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Pedobacter
            ginsengisoli].
ACCESSION   WP_285059257
VERSION     WP_285059257.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..320
                     /product="isopenicillin N synthase family dioxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36233
     Region          1..319
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 msapyipsld lgsyingnde qrrkfsdelg rafndsgfvt itnhgldqal idklykniqa
       61 mfslppeqkk qyekielagq rgytspgket akgaktadlk efwqigqevt dndpvkyeyp
      121 dneyleeipe fnevtreiyq rleangkhll raiatyldlp vnyfdeyvhn gnsilrgihy
      181 fpiedpdslp adavragahe dinlitllig asadglqvlt rsnewlpika ghtdivvnvg
      241 dmlqrltnnr lrstthrvvn pprelmktsr fsvpfflhpr atmdltclds cidgehpkay
      301 edmtageyld erlreiglkk
//
LOCUS       WP_285059384            1026 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285059384
VERSION     WP_285059384.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=112751
     Region          23..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkifllfcl llmaasesfg qarvisgkvt dnesvpleav tvvvqgtqrs vltdqngnfk
       61 isaengqvlk fgyigadpys ytvtsdsqdi avklnvatts lnqvvvtgyq kerkkditga
      121 vsvvdvksik dipvgnplka lqgrvpgvfi ttdgspsgga tvrirgigtl gdndvlyvid
      181 gvptkrglqe lnpndiesiq vlkdassati ygsraaagvi ivttkkgkag lakvdvnasa
      241 siqnyaskln tldadgrgra ywqaavndkq dpnlhqiyqf dwnkdfnnps lsniiypefi
      301 daaktmrpan tywydlisqn sliqsydvav sngtdkgssl fslgyyqnkg ivksskndkl
      361 tarlnsdynl lnsklkigen ltasyiknal tpvsdilfts lvqqpvvpvy tvdggwggpa
      421 sgmtdrqnpl rliednrqny snfyrllgnv faeyniipgl nlrtsvgldy ngtyqrvlrk
      481 sytsgflsdk tnqvsntqny sgnivwqntl nykftekkhq vevlvgheqi rnviqgfsas
      541 rqglalenid yayldagssn tlnsgsgtgn sllsffgkan yvfndryias ltlrrdgssr
      601 fgqnnkygtf pafsagwris qeefmkkipf isdlklrygw grsgnqeipd nankflyrai
      661 ygidptwefd sgsayeiggt gsgqlpsgft llqrgndnlk wesleehnig ldfglldnkl
      721 tgsfdyfike tsdilinpay lavlgeggsf wmngatlknk gfdallsydt klsadfsmnl
      781 tgnfsmyrnk vvdlpeevlt sypgngtdkn ilgrpvnsff gfvtdglfqs qqevdahaaq
      841 pgkgigriry kdldangvin drdrdyigdg gpkftaglna sftyrnfdls ffiqaiqvkv
      901 vndfktytdf sslwtgtnwg srtldawtps nasstipalt lvdnnnegrf styfiengsy
      961 vklrnlqigy nlknlfkskv qnarifvqgs nlltiksksf tgpdpeipny gfpvpvigti
     1021 glnltl
//
LOCUS       WP_285059404             924 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Pedobacter ginsengisoli].
ACCESSION   WP_285059404
VERSION     WP_285059404.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 924)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 924)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 924)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 924)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..924
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=103774
     Region          37..>547
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          555..>626
                     /region_name="LacZ_4"
                     /note="Beta-galactosidase, domain 4; pfam16353"
                     /db_xref="CDD:465101"
ORIGIN      
        1 mkkillqlll slicfssfsq qtmikylsgt dkdhtvqwdf yctagrksgq wtkiavpsnw
       61 elqgfgayny ghdkdkaseq glykyeflsg nwankrvsiv fegsmtdtkv lingkeagpv
      121 hqgsfyrfky ditdlikpnd knllevtvsk mstntsvnta erksdfwvfg gifrpvylei
      181 vppvfierta vnakadgsfq ldvyaknltg delievqvqk lngenvgkpf svkadpgpdh
      241 lelknnfasp llwsaefpnl yqtvvsiknq qgvvhqmkhk fgfrtvelri ndgfyingtk
      301 vimkgsnrhs fwpesgrtls heihvmdvrl mkemnmnavr mshyppdadf ldvcdslgly
      361 vldeltgwqa kydsevghkl vkelvvrdvn hpsvvfwdng neggwnteld ndyalydpqk
      421 rivihpwekf ngtdtkhyqd ykaiektvaa gkevyfptef mhglydggag aalddfwslm
      481 mkhphaaggf iwafideavi rtdkngayds dgnhgadgiv gphrekeasf ytikeiwspv
      541 yidpkpidgn fkggilvenr ysftnlnqct fkwklvkfps ahakttaati vatgtpaapg
      601 lkpgekgmiq lslpsswskn dalyltaygp dkreiftwsw aistpavvak kigsisgktg
      661 ksgikteqtd eslivkndgi hyyfdkatgy iqkvvkpsgt islsggpvla gisstlkeft
      721 hkslkgqyvi eaeyqgtgsl hvkwtftsgq pvkleyqhsq qgdadftgit fnypeekitg
      781 mkwlgrgpyr vwqnrlkgqq fgvwhkaynn sitgetfeyp efkgyhaevn wavienkegp
      841 fmvytpdkam ylqmlrpare kdamrnnnve pafpegsigf lntisaignk fqsasqmgpq
      901 sqkgrhngek vngtlwfdfs gnyk
//
LOCUS       WP_285059424             364 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Pedobacter ginsengisoli].
ACCESSION   WP_285059424
VERSION     WP_285059424.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469209
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..364
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=41122
     Region          1..364
                     /region_name="COG4867"
                     /note="Uncharacterized conserved protein, contains von
                     Willebrand factor type A (vWFA) domain [Function unknown]"
                     /db_xref="CDD:443895"
ORIGIN      
        1 mrgfhfsdft pddlpkggfd ellklftqll nytagdaaea lswmneldkk ykftnneygm
       61 gdfidelkek gylnedgsgn lkitakteqt irksaleeif gklkkagkgn hnsnisgige
      121 eknadrrefa fgdsldqidm tasiqnaqin hgignftlte rdleveekdy ktltstvlmi
      181 dishsmilyg edritpakkt amalaelikt qypkdtldiv vfgndawpit ikdlpylqvg
      241 pyhtntfagl elaadllrrr kthnkqifmi tdgkptclke ngryyknsmg ldrkvisktl
      301 nmaaqckrlg ipittfmiak dpylqafvre ftqvnggraf yssltglgey ifedyiknrr
      361 ktvr
//
LOCUS       WP_285059429             555 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pedobacter ginsengisoli].
ACCESSION   WP_285059429
VERSION     WP_285059429.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..555
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=63522
     Region          332..552
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mssdkksgyr knfsliitfi ilmsalfils lvlayrfstk fienefvsek vnvleqsikp
       61 yndffqkklp evsfyngyld satasnfvdt vlleypfvsk vifydsevrn tpvsdglnig
      121 kfsfgpksiy qfgtlvpsds vslfsrndtr nfiagddfnt lalklvtfie sldtsrvpaq
      181 delfsnfsvv rsnkitylni priedlkmyk ammrktlksq pvyqqdmmsf hldpykirii
      241 nsrplmyqyi kiepltydpl dtssayltte itlpgpfsdy klyfissksf idkeilsyfl
      301 pialgifgfy sivvlvafli yrnlninhkm fklqydfmnn lthefktpvs vikiagnnik
      361 sattlsqkel nlygkildee adklnglmnk llaftqienk aielnrdevn iddfmvstie
      421 shklkhpdfd ftyevsgfts fvtdpvllgs lfdnlaenay kysppdrkkl hisarlikgk
      481 vvfrftdqgi gipaseinni fkkffriqnq ynqngsvglg lafckelvnf mngeitvksk
      541 vdkgtefkiv lphnd
//
LOCUS       WP_285059600             252 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285059600
VERSION     WP_285059600.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..252
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28618
     Region          46..248
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mnkflgyifs plfyfsfflt liifqpiqwl cyrlggykah kisvdilnff ltycdfflgs
       61 svtfinhqsl penrsiifia nhqsmydipa liwflrkyhv kfiskieltr gipsisfnlk
      121 yggganidrk dskqavseii klgrrmkeht wstmifpegt rskdgrlkpf qvggiatllk
      181 vvpdalivpv aienswkivq ygsfplsfge qlkwtvldpi epagrnaeev taaaenairt
      241 qlkqipadlq da
//
LOCUS       WP_285059604             513 aa            linear   BCT 25-DEC-2024
DEFINITION  M28 family metallopeptidase [Pedobacter ginsengisoli].
ACCESSION   WP_285059604
VERSION     WP_285059604.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Turner,A.J.
  TITLE     Exploring the structure and function of zinc metallopeptidases: old
            enzymes and new discoveries
  JOURNAL   Biochem Soc Trans 31 (Pt 3), 723-727 (2003)
   PUBMED   12773192
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10168791
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..513
                     /product="M28 family metallopeptidase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=57051
     Region          293..508
                     /region_name="M28_like"
                     /note="M28 Zn-peptidase-like; uncharacterized subfamily;
                     cd08015"
                     /db_xref="CDD:349937"
ORIGIN      
        1 mikiytiiaf lfglvlplta qdkadlqaiq rirkeglehs rvmdiafqit dvagprltns
       61 pglkraqdwa mkqfsewglk nvqleswgkf gkgwqidkyy aattvpyyhp viaspkawtp
      121 gtnglirsev ilikadtvtd ldkykgklag kivmfdqmtl qplqntykpd avrhtdsvln
      181 kmeqasagtq rprpagdnnm raqmmkirav rtaisamlte ekvglvltya rgsygtffts
      241 ngasyaldag pvspelevsa edflhilrll ragqkvemea eiktsfydqd pngynviaei
      301 pgtdkklrde vvmigghyds whsatgatdn aagaavmmev mrilktidfk pkrtirialw
      361 sgeeqgiygs rgyvtkhfgd pktgenekvs ayynldngtg tirgiylqgn eaarpifkew
      421 lapfndlgag titinntggt dhlsfdaagi pgfqfiqdpm dyntrthhsn qdtydrlved
      481 dlrksatiia sfvyhtsere kqiprkalvk ksd
//
LOCUS       WP_285059626             341 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pedobacter ginsengisoli].
ACCESSION   WP_285059626
VERSION     WP_285059626.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..341
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=38985
     Region          5..337
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mklsilvlia alavgiaigl vnfyfqqswy dlaisfgvsf visylvfyyl lekyiyskiv
       61 liyklihnlk lgkdlkdalg eyvsadpind veqevkewag akkreidilk kqeqfrrefl
      121 snvshefktp lfavqgyidt lqdciaddpe tatkflkkaa dnverlsyli ndldsiskle
      181 sgeipinyqk fdfvglarev mealedkaka rniklsfkek ytypayvnad rekirqvmmn
      241 lienslkygk pdgstaikif elhdqyliev tdngigidek hlprlferfy ridthrsrqe
      301 ggtglglaiv khileahqqi isvrstqqig ttfaftlqkl g
//
LOCUS       WP_285059760             203 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Pedobacter ginsengisoli].
ACCESSION   WP_285059760
VERSION     WP_285059760.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..203
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=23359
     Region          3..203
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mtdlfskgta seinllpydg evnyygrlfs sqqasdyynt lfhhiewrnd eaiifgkriv
       61 tkrkvawygd tefeytysnv tklalpwtke llelkkiaee qtgetfnscl lnlyhtgeeg
      121 mawhsdgekd lkkngaigsm sfgaerkfsf khkqnkqivs vilengsllv mkdttqthwl
      181 hrlpptklvt kprvnltfrt iil
//
LOCUS       WP_285059786             279 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Pedobacter ginsengisoli].
ACCESSION   WP_285059786
VERSION     WP_285059786.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..279
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30758
     Region          <34..276
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mkrficllvp lltqlfsvsa qqpgppsegf dvmrsgiahg rldtityask tvgtnrkavv
       61 ylppgftdkn kypvlyllhg iggdelewlr ngnpqhildn lyaakkivpm ivvlpngram
      121 pddraagnim aadkvaafsn fegdllndli pyieqrypvl adrksrgiag lsmgggqaln
      181 fglgnldkfa wiggfssapn tkqpkellad pasarskisl lwiscgdqdr llpitertrd
      241 ylsanqvpht flkepgqhdf kvwkndlyqf sqllfksek
//
LOCUS       WP_285059790             216 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pedobacter ginsengisoli].
ACCESSION   WP_285059790
VERSION     WP_285059790.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 216)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 216)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 216)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..216
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=24184
     Region          <7..216
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mlesniaafr qqkeftenas helqtplaiv qskldlllqd galssaqsqi ieetnnalsr
       61 vsrinknlll lakienqqfl dkqqinisep lqevldllsd llegrtiean inpicivegn
      121 rilieimltn llmnslrhte pgvkimvyls vaelvisnpg nypldavklf rrfstasgqt
      181 pgsglglsiv eqiysrygwa veykfteqqh qfsvrf
//
LOCUS       WP_285059941             352 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285059941
VERSION     WP_285059941.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..352
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39365
     Region          8..323
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mttlkgpgvf laqfigdeap fnsldaickw aadlgfkgiq mptldarfid lqkaaeskty
       61 adelkgrias ygleitelst hlqgqliavh paydlafdaf apdsvknnpk artewavqqm
      121 kyaaqasqnl glnahatfsg sllwhmfhpw pqrpaglvda gftelakrwm pilnefdkcg
      181 vdvcyeihpg edlfdgitye mflekvnnhp racllydpsh fvlqqldyiq yidfyherir
      241 afhvkdsefn ptgrqgtfgg yqswanragr yrspgdgqvd fgkifsklaq ydykgwavme
      301 weccikdaqv gaaegaefik khiikvtkka fddfaasggg dddfnnkilg ls
//
LOCUS       WP_285060027             591 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Pedobacter ginsengisoli].
ACCESSION   WP_285060027
VERSION     WP_285060027.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..591
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66961
     Region          2..584
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 maetitrvfd llkynlerfp keefisgkvn gewkkystad fcrivddlsr gltsigvakg
       61 srvavmshnk pewnitdfai mqlgayqvpl yptlaehdik filenaevnl ifvddeaiya
      121 kvkpvceelk rdikiysfsq tkdiphweel lkagkgltvd ldsyrtqvkp ddiltliyts
      181 gttgtpkgvm lthdnlvrnf ensavllpeg ikkglsflpl shifermvvy lymycdvavy
      241 yaesmdtiva diqyvkpnvf stvprllekv yekimekgka ltgikrglff wavslaekfe
      301 fkkgwfykfd lgiarklifk kwqqalggnv vviisggaal nprlarifwa agmpvfegyg
      361 ltetspvitv nhfgntmfgt vgpviegvev kiaadgevla rghnimkgyy lrddltaeti
      421 dkdgwfhtgd igqlvdgkfl kitdrkkeif ktaggkyiap qmlenkfket plvdqvmvlg
      481 enrkfpaalf vpnfpalklw aqkkginytt dqemtkdeqv lvkfdqivkn tckdfgkweq
      541 vkrfalldkp wsidggeltp klslkrkvil eknkslieki yadaenykvp e
//
LOCUS       WP_285060046             442 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Pedobacter
            ginsengisoli].
ACCESSION   WP_285060046
VERSION     WP_285060046.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..442
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=49445
     Region          1..439
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mikiliiedd ltfsqilegf lnkhgyktml sndvkkslai vesqhpdlll vdyrlpdgtg
       61 ldvlsylren glpqpmiimt sfndvrtavk siqmgafdyi tkpvnpdell miikeatdkr
      121 kpvnnsktie nsdaikgksa iadklyehin lvaptdmsvi iqgesgtgke yaartlhmqs
      181 krksmpfvai dcgalskela aselfghvkg aftgaltdkk gqfevagggt lfldevgnls
      241 yevqvkllra lqektiqpvg stksikadvr iitatnddlk tnvsngtfre dlyhrlnefk
      301 iqlpalrnrg kdldlfikhf vslsnkelqk nvqhisqsam elllqydwpg nlrelknvik
      361 rmvllttgdt adietlpdem iiavhkesrp lgsdlkaine inekalilet llkvrynksk
      421 aakllnidrk tlyskmerye ie
//
LOCUS       WP_285060077             424 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Pedobacter ginsengisoli].
ACCESSION   WP_285060077
VERSION     WP_285060077.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..424
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48783
     Region          26..171
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mkvkliylva ivatslqsfa qnslkigqql pdleinkily hksekvklsd fkgklilldf
       61 wstvcgpcia gmpkmdslqk hfgdkiailp iypdlkggmd nklvtdldsf whsndilskt
      121 slpsilddef arhfparvay qvwidskrvv raitsseyvn kkeiqkmldg iypdweteiy
      181 tfyddkhpif ketrnylnkd qfhsefsgyi ggindnkdri ngyqgivddk vssslrfsal
      241 nmdivylyrs liskltgnis lsnskvivet sdsskyfint ymnewcrknt ycyeavfpks
      301 eskdkvqqkm ikdlnsrlgl narfekrlvn cwtlkknsaf gkrqyqekgs syekmkdlvs
      361 dvqyitglkv fdetsikdki dvklndtttd qiisqlkqqg ldlvkeqrll evfvitdksf
      421 ksti
//
LOCUS       WP_285060090            1099 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Gardnerella vaginalis].
ACCESSION   WP_285060090
VERSION     WP_285060090.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 1099)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 1099)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1099
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..1099
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=123837
     Region          <833..1018
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(899,902..903,906..907,909,933,936..937,940..941,
                     943..944,970,973..974,977..978,981)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          899..926
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          931..961
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          969..995
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mqdevqsskk idsaessekn rsdiaddsmq ivqetiktlw enresipvri fskkhifkdf
       61 pmmpknvklg wiklsgkkhg iaiglfnddc krfrqlavad fegrvytghd isiedtmeri
      121 pelsfveqns mtlkdslrfy gvddrkitha sharkkvnsi nknnresdlv virgdvvvql
      181 sqdegmqwvs swirkvndkk eaytleetrv llpdrlrcnl sycdaistsf fasffipdit
      241 rafsgfgsgn ifrrltkeap lgairrsimd skvaekaglr vssmekyfay lmldsgaleh
      301 sgpleavhga erlhlqksqv sdanflvwdd sleakaalkv lriegainrf qsisscleen
      361 canggnlten svnfgqisei dlsfiedpaf cangeldmns fgnplqddni rplmhlwnta
      421 kksndlyiyk sdgssncews yrqrlsglir slylpfrfdt dfrsnledgn valafmatgs
      481 smmptrrfds anqkwitltn agksrmttdy nlrlgiimat lafgaseevq nvsirldsig
      541 leemvaaqdd amskilnqti nalnnmnrea arskgdpkdg dihgdvnngl anvqdlqnft
      601 nhtilhedev tvpdssnkat ssksinssds ysdteisdsn tndigsdpie pnpmdafsky
      661 ptvkslltvt fnresfikhi ranglnnplg aykkfnanmk ideegalnpi epsfdlrdsc
      721 fsphgaqeep efsdvifdik sqktlgttns kglsiqredl lqqavadfhh issevmisna
      781 ekarmamdiv esiddpelne kanlitsali dekeipeisf kvskdiynmr lhaheqfmsg
      841 dlenaieeye navkhfdsmf sfndvvpryf nsyaervvyn rifatqnerm ilipdglfya
      901 hmeladlltq lsrhedalkh lntmvsyapt yvishlklas qltekedwts veavclnalp
      961 vcfdredaaf iyyrlayaew mqdnfplava sykmadnlss gkiesieiel dellsrmqsq
     1021 cipapndmsq veevlkinnv pkwpdveaye iideaakitv negmfviart lsvararmlf
     1081 snnssdnvvq mqflrslns
//
LOCUS       WP_285060107             178 aa            linear   BCT 25-DEC-2024
DEFINITION  YceD family protein [Pedobacter ginsengisoli].
ACCESSION   WP_285060107
VERSION     WP_285060107.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..178
                     /product="YceD family protein"
                     /calculated_mol_wt=20328
     Region          1..178
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mkplkqfsip ftglkigkhq fdfeidnsff dafeyslvkk gtlkaeveld kqetmlilqf
       61 ridgtivldc dkclaefnsp vsiqerqivk faedelqsdd leiiilskke seidisgliy
      121 efitvsvpyi kiceengngq rcdqemiarl eslavgaqke eeqqqdedpr waalkklk
//
LOCUS       WP_285060143             316 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Pedobacter ginsengisoli].
ACCESSION   WP_285060143
VERSION     WP_285060143.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..316
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=33861
     Region          9..303
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 msnritelfn ikypivqagm vwcsgwrlas avsnagglgi igagsmypav lrqhiqkckq
       61 atdrpfavnv pllypevqei meiiteekvs ivftsagnpa twteylkrng iivvhvians
      121 kfalkaeasg adaivaegfe agghngreet ttmclvpmic arvkipviaa ggigsgraml
      181 aamalgadav qigsafavae essahpdfkh riisagegdt klrmkklvpv rllknefada
      241 vaqaeaqgad aevlvrllgr araklgmfeg dmeqgeleig qvsamlkqvr paeeilneiw
      301 kefliekerv sglsfk
//
LOCUS       WP_285060183             159 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase [Pedobacter ginsengisoli].
ACCESSION   WP_285060183
VERSION     WP_285060183.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..159
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=16720
     Region          20..159
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mkigkgtkve nivvnwphqv vvgdncvler gvtikfpgvw rpgpmigign ntlvakdcei
       61 niteslsign dcliaagcrl idhdhgtgig elmrkqecpg spivvgddvw igsdtivlka
      121 vmigdgavia agsvvtksvp smeiwagipa rkigerkke
//
LOCUS       WP_285060193             364 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Pedobacter ginsengisoli].
ACCESSION   WP_285060193
VERSION     WP_285060193.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..364
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=42549
     Region          1..363
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 msgqnriksl dgirgtfiim vliahafqtt pefaanhkif vyyisgfghl gvriffvmsg
       61 ylitrlllke qekngkvnir dfyirrmfri fptfflyifa illlkwtilp diftdyslil
      121 faafylwnyk hlfihdvgae adkgnwfmgh fwslsmeeqf yllwpvtfvk fkrltlikii
      181 lvivaimpfl rivtflflpn srphvsemlh tggdaimigc laalleqapq frekyfkyve
      241 nqklivvvmf flfvispvlt wylqaaynlt vgitlnnisi mfllfwamyi pskasdflnk
      301 kfishlgias yslyvwqqlf ltdkndlwvn kfpqnilvai tvgmashlla ekpilklknr
      361 fkri
//
LOCUS       WP_285060262             240 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Pedobacter ginsengisoli].
ACCESSION   WP_285060262
VERSION     WP_285060262.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 240)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 240)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..240
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=27763
     Region          3..231
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 miytcviitd hneevkflkn qiavhnelel tasypniynv pasvyshiaf inindsvmng
       61 qdqfnlmrsn fefiiftgdr decariaydm dgldylskpi epsrfnqafy kvtrsalnaq
      121 kpkitmnslf aikdvhdern wvintyndvv avesdknylk iyttasfhit ylslskfefn
      181 vlnlpnfikv hrsfivsknh lqkitnhniy mkgvtvkipi ginyrknlqe fidgvslnrk
//
LOCUS       WP_285060291             181 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase [Pedobacter ginsengisoli].
ACCESSION   WP_285060291
VERSION     WP_285060291.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..181
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=19928
     Region          <28..144
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mlrrlifklv gmlvlhtkgr rgfaifvgvt lgsnnriytt dwgsepflit ignfvtiang
       61 vkfithdgaa glmkdqkgrr yyfnritign nvflgldsii mpgvkiennv ivaagsvvtk
      121 sipegsivag vpakiigsfd elkekmlmqy iseadmdfsi dfksritkvt stdykpflek
      181 l
//
LOCUS       WP_285060312             267 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Pedobacter ginsengisoli].
ACCESSION   WP_285060312
VERSION     WP_285060312.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..267
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30291
     Region          5..>172
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mqnnrplvsv vipmynsekt iqntlrsvsi qtythleviv vddgstdgsa glveqfagqn
       61 pqmniqlirk anggvstarn agmkqskgdy ialldsddew lpkkleiqie ifknnphidf
      121 lgstrngehf srflfkkfsy lthissrlll yktflitptt lfkrtildtv gyfdetqkya
      181 eegnywirvc kdnhcvlqne slvitgggkp dfgfsglssn lkqmelgelk nlrdglnlki
      241 igrieyvflv lyslvkyvrr ilivklr
//
LOCUS       WP_285060315             197 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase [Pedobacter ginsengisoli].
ACCESSION   WP_285060315
VERSION     WP_285060315.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..197
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=21372
     Region          68..197
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mrtairlpvl vssnvllkct egqiriegpi ftgvvrlgyg dmalfdrrrs kgiwevkglv
       61 vfkgkawigq gtkisvgqtg riifgpdfev tansaivsys eiefgkkcll swdvlimdtd
      121 fhailnaega vinapkciki ddnvwigcrs tilkgshvgp gnviaagtvv tkklegqqti
      181 yggpeakilr enitwkq
//
LOCUS       WP_285060325             315 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285060325
VERSION     WP_285060325.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..315
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=36477
     Region          68..315
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mndkelntsi fdnltehcev qytdeigtss fmrvseirid gadifaansk qereitlrer
       61 hetptlamyf slqgqssawe lnskdkyvln dnehvlsfvp gfdgyyalss peirnfgisl
      121 yepffrrlys adldclkrfw ekvhsgkaad lsehalpvtp rqqslinemq ncvytgsmkq
      181 lffeskiiel fllqaeqaen lngqrplkme rhnieklhaa rqfikqrmfd plslngiare
      241 tglnefmlkk gfkelfgltv fgylnelkmd yarqmlldsg ctiyevaytm gynepynfsk
      301 afkkhfgylp gelkr
//
LOCUS       WP_285060367             272 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Pedobacter ginsengisoli].
ACCESSION   WP_285060367
VERSION     WP_285060367.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..272
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30468
     Region          <93..269
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 myitmslpei irtrhslksd hlkrevefei fipdnlmgne qlnllllndg qdadalglqq
       61 mltglygqrr isavaavaik asaarleeyg vagvpdfggr ggkahaytnf itkelipclk
      121 etvatpingk rvfagfslgg lsafdiawnn dnyfdaagvf sgsfwwrkkd lkdgytdndr
      181 imherirtts nkpglkfwlm tgtedelsdr nrnliidsid dtidvikell kkgyrrpddi
      241 vyyekvggkh dlstwaealp aflgwafgrk ni
//
LOCUS       WP_285060408             179 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Pedobacter ginsengisoli].
ACCESSION   WP_285060408
VERSION     WP_285060408.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..179
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=19620
     Region          19..151
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 maeldtssgg gkkgggkvrt kkantkvdlt amvdlaflli tffmlttsls kpiamdiakp
       61 dqednevrne lrasqtmtil lgeknkvawy mgeakdakpv iesfaevrrs llknkeevkn
      121 ktgrqivvvv kptdgatykn fvdimdelni aaiktapaid dvnildnekq fmreggilk
//
LOCUS       WP_285060421             287 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285060421
VERSION     WP_285060421.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..287
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33743
     Region          <194..283
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkqhyidpis agelhltqqe atfdrlffqr drkdkfltia wnngpaqmvm idgiqyaypa
       61 qtilplmvnq tftfekpeqi iawqynrnfy civdhdkevs cvgflfygsa eimfiqldeq
      121 qqkkfnlllq vfidefedkd tiqrdmlqmm lkrliiiitr lakkqylneq tltddkldvl
      181 rkynllvenn yrkqhtvqfy adqlnkspkt lanyfalynh ksplaviqer iileakrllm
      241 ytdksakeig yelgyddaay fsnlfkkhtg yapsdfrnak ssllsgq
//
LOCUS       WP_285060479             284 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_285060479
VERSION     WP_285060479.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..284
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=31069
     Region          1..284
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mkilfivnpg agseglnfse liteyfesse heaeiyklpq dctlkqlkit iagsradrvi
       61 avggdgtlkl vsecllqsgt pigiipagsa ngmakelkip ltlnealdta vngtpkkiha
      121 vmvnnelcih ladigfnayl vkkfdallhr gmwgytkaaw kalwnhnkmt veikikdqti
      181 rseaamvvva natmygtgvk inpdgklddd vfevvlvkky svmeilklkf tnialnpdni
      241 elfqvsslhi ktkykahfqv dgeylgkvns ldariipdai siiv
//
LOCUS       WP_285060486             196 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II [Pedobacter ginsengisoli].
ACCESSION   WP_285060486
VERSION     WP_285060486.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..196
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21827
     Region          11..195
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 mksnnntqkk vlvidnydsf tynlvhlvne ldrdvevwrn dkfaledvdq fdkillspgp
       61 gipeeaglll dvirtyasak sifgvclgqq aiaeafggsl lnlgrpmhgi atpidvldqd
      121 elifkdcpav ikvgryhswv vnsaglpdcf tvtatdntne imalrhnkfd vrgvqfhpes
      181 vlteygkqmm knwles
//
LOCUS       WP_285060544             400 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pedobacter ginsengisoli].
ACCESSION   WP_285060544
VERSION     WP_285060544.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..400
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44998
     Region          28..374
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mdirsnepfw lvrnglmhsy pslrnnlecd vvivgsgitg almahackek gydtvlidkr
       61 eiahgstsat tsmlqyevdv plyqlkemig qqgaiasyka crdaiyklek lveeigstcd
      121 fekkesvyfa gnpkdlkwlr kefearfeag fdvkwldrpa lrstygivae gaiasadgas
      181 idafrlahdl lhfnssrglq vfdktelqkv ryetgyvlle ldtgasikak niiyctgyea
      241 qqmlpdkivs lkstyamise kggqdadvwk dtlfwntdlp ylylrstedg rmlvggeden
      301 frnatrrdll igrkrdkllk tlkrylpevn fiedfcwagt fgetkdglpy igshpkfpns
      361 yfvlgfggng itfsvtgmdm imgmmdgspd llshyfrfgr
//
LOCUS       WP_285060561             309 aa            linear   BCT 25-DEC-2024
DEFINITION  GDP-L-fucose synthase family protein [Pedobacter ginsengisoli].
ACCESSION   WP_285060561
VERSION     WP_285060561.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..309
                     /product="GDP-L-fucose synthase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34388
     Region          6..305
                     /region_name="GDP_FS_SDR_e"
                     /note="GDP-fucose synthetase, extended (e) SDRs; cd05239"
                     /db_xref="CDD:187550"
     Site            order(11,13..16,37,40..43,63..65,67,87,106..108,137,141,
                     164..165,167)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187550"
     Site            order(84,108,137,141)
                     /site_type="active"
                     /db_xref="CDD:187550"
     Site            order(108,137,166,185,202,210)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187550"
ORIGIN      
        1 meknakiyva ghrgmvgsai yrklvkegyt nlvtktstel dlrdqqatan ffaaenpeyv
       61 flaaakvggi vanntyradf lyenlciqnn vihqayltgv kklmflgssc iypklapqpl
      121 keeylltgll eetnepyaia kiagikmada yrdqygcnfi svmptnlygy ndnyhpqnsh
      181 vlpalirkfh eakvngtaev tiwgsgspmr eflfaddlag acyflmqeyn epgfvnigtg
      241 kdltikdlal likkvigfeg tlafdsskpd gtprklmdvs klhslgwqht veleegiela
      301 yrdflakhi
//
LOCUS       WP_285060588             543 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pedobacter ginsengisoli].
ACCESSION   WP_285060588
VERSION     WP_285060588.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 543)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 543)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 543)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 543)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..543
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=61886
     Region          36..541
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mltativlal lflvvtycla rnmaavrrmk nevaglrkqn etlsaraell glaerisnlg
       61 twelfpgskt vrwseelyni ygfkdkciel saelneqvia peyrdkvake lrsaisnqtt
      121 faveyqiiqp dgtrryvlgq gfyiekddkl vgtiqditqq kdaifklkin etllreaemv
      181 shsgswewvd gkefvlwsde mynihgflph svfvnfafyq glvheedlhe flknffkare
      241 nkapfkinyr ivrpsgevrh vlstaeykki glnnfayign tqdvtelrka qvqleekvte
      301 lnrsnqdleq fayvashdlq eplrkiqafg dklkdkylah lppealdyle rmrnaaermr
      361 alindlltfs ratrdhknfi atdlaeling tireldfsig israairvtv dldadaipsq
      421 lqqlfqnlia nalkftdaei ppeieitgya kyghelsiae arpnqlysvi eikdngigfe
      481 eeeakkifdi fhrlhsrney sgtgiglaic kkivenhsgf ilansepgng avftvilpkr
      541 qik
//
LOCUS       WP_285060627             347 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Kingella kingae].
ACCESSION   WP_285060627
VERSION     WP_285060627.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..347
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=36533
     Region          8..347
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mqtllsslrh rfiqapmaga qdaqlaiavc qagglgslpa amyspeqlda qlstfrqavg
       61 napvnvnffa hktpnpsaeq varwqsalqp ycaelgvdls qvalqdtrrp fdetllpvlv
      121 khrpavvsfh fglpraplld avratgakil ssattvreak ylaaqsidgi iaqgweaggh
      181 rgwfldkddv atqsgtfall pnivravdlp viaaggiadc atvqaafalg aaavqsgtaf
      241 lladealtap ihraylqseq aaftavsnif tgggargivt rwmrelgymh snalpfplag
      301 vyfaalrqaa qnagnhefns fwagqnaplc qtgsaaqiiq nlmgeta
//
LOCUS       WP_285060625             107 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Pedobacter ginsengisoli].
ACCESSION   WP_285060625
VERSION     WP_285060625.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..107
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11708
     Region          2..106
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mswiiliiag lfevgfttcl klsnnftnlk wsiafalcis lsfyflnkat qtlpmgtaya
       61 vwtgigavgt vlvgiiyfqe panfwriffi vtligsilgl kffagsh
//
LOCUS       WP_285060611             407 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pedobacter ginsengisoli].
ACCESSION   WP_285060611
VERSION     WP_285060611.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 407)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..407
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=46735
     Region          131..395
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mnpyekkrrw kffllvfaiv igtasvfysd ffvkkmeree qlqfqlyvrv teqslimydn
       61 diytplieli rtktklpvim tdskgeiigt qgldstktny niekkegvty dpayfrrelr
      121 kmkkqhpptp itglgadgsr wliyykdspt ltqlryfpyi qlavialfll tayvafssar
      181 kaeqdqvwvg maketahqlg tpisslmawv eliksrfdae ddpliaemen dikrlevitd
      241 rfskigskpv vedhvvytvi ynfveyfklr tsdktrfsit gddqvramln vplfdwvien
      301 llknavnaid negkitinii enltkeevfi dvtdtgtgia rskfdavfqp gyttrkrgwg
      361 lglsltkrii enyhsgqifv kdselgkgtt frivlkssit yepttnt
//
LOCUS       WP_285060636             103 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: thioredoxin family protein [Pedobacter].
ACCESSION   WP_285060636
VERSION     WP_285060636.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 103)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     Protein         1..103
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11504
     Region          1..97
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 mfleltednl qqyvaennkv mvqyaaswcg ncrimkpkfk klaaenedvt flivdaeklp
       61 gsrklanvdn lptfaafegg alvhqvqtnk aellnelfdr iks
//
LOCUS       WP_285060738             377 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein, partial
            [Pedobacter ginsengisoli].
ACCESSION   WP_285060738
VERSION     WP_285060738.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Porat,A., Cho,S.H. and Beckwith,J.
  TITLE     The unusual transmembrane electron transporter DsbD and its
            homologues: a bacterial family of disulfide reductases
  JOURNAL   Res Microbiol 155 (8), 617-622 (2004)
   PUBMED   15380548
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Kimball,R.A., Martin,L. and Saier,M.H. Jr.
  TITLE     Reversing transmembrane electron flow: the DsbD and DsbB protein
            families
  JOURNAL   J Mol Microbiol Biotechnol 5 (3), 133-149 (2003)
   PUBMED   12766342
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   8  (residues 1 to 377)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   9  (residues 1 to 377)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         <1..>377
                     /product="protein-disulfide reductase DsbD family protein"
                     /EC_number="1.8.-.-"
                     /EC_number="1.8.1.8"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
     Region          <1..373
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 sffgafeitl psalvnkidn kadsskglgg iffmaaslal vsfsctgpii gtllvdassk
       61 gellapavgm fgfslalalp ftlsavfpgf lnsmprsggw lnsvkvclgf lelalalkfl
      121 saadlvwhwe wfdrevflsl wivifvlmgv yllgklkfsh dsdlayvsvp rlflavlsfs
      181 favymvpglw gapvsvlsgl appmntqdfl lsgsgsgtsa sepgfparvk ydevfkkpvg
      241 ftpffdleeg layakkvnrp vmldftgwac vncrkmednv wvkpevgnli reyvliqlyv
      301 derkikmpag kvhyseilrr ktddlgywng dfqasrygsn sqpfyvltgh dlvplvkpqg
      361 avfdakeyaa ylqtgld
//
LOCUS       WP_285060803             543 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Kingella kingae].
ACCESSION   WP_285060803
VERSION     WP_285060803.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..543
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60233
     Region          25..316
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mltytsrpkr peptheypwl llllafcwlw pgvfshdlwt psepnmmlai ddaaqrgawl
       61 ptvfgaayfd vsplyvqtaa wfkmllspwa adafsaarft svlftslgll gsgmagyrfl
      121 grhhgrsvvl iligsvgilp iahflgaysp vfagvglamw gfsiaqrqvm fsailvalgt
      181 mllaqslgll aalamllvas llpfsphwrn qrytvalvam waisspllav ypialaivep
      241 aafavywqqh ifgsfgginq vqaafslhyy lqhllwfafp alplaiwtrt rqsfratpag
      301 mlvatwlavf ggflllnpeq hqdllvlllp plalsgaaql dnlrrgmaaf lnwfgialfg
      361 caavflwigf vamnygfpak laeraayfsp yytrdldimp ilvallftpm wliaitrkri
      421 rgrqavtnwa agttlvwall mtlflpwida akshrpiiqq liqavpdvah anclyidprd
      481 ktarlawqqy gtgaytiqnt scrytlaqyn prnevapagn ivwqgkrprs ktelfvlihn
      541 gge
//
LOCUS       WP_285060821             260 aa            linear   BCT 25-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Gardnerella
            vaginalis].
ACCESSION   WP_285060821
VERSION     WP_285060821.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..260
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28317
     Region          12..255
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mrnseknskn nshnhivalt gagistsagi pdfrgpdgvw tkhpeqmsvy didaflssee
       61 ervyswrwqk espvwnaqpg tahkslvkle kagmldliat qnfdalheka gnspdivvnl
      121 hgsigtshcm schasyntad imrnldahpd phcrralpyr gnmpcnglik tdvvyfgeal
      181 pegamersaq aimhaselwv igstlevfpa aslvplaara gvpitimnlg atqydylaec
      241 iirediakal pklvdetiak
//
LOCUS       WP_285060824             467 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Kingella
            kingae].
ACCESSION   WP_285060824
VERSION     WP_285060824.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..467
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51763
     Region          14..435
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mvesantssn sqryltlwrw hfytgiliap flmllaatgl amilfahtsg rdgeriivpv
       61 lqtvkplseq aqtaldtvdk nsgmvvqyia praadmvavf rvnngegkat mvaidpytaq
      121 vvktyprnqd wyhlmdeihg dillgktgdy lletaaaltv lmilsgwylw wcsrqrsvpk
      181 mlgtgklgqg rsvwrglhgv fgsyislmll lfclsgmawa giwggkvvqa wsaqfpagkw
      241 giepipksap lhselndgkt keipwvlelt pmpvsgttlg kdgiapdvpm tletvdrfar
      301 esgfvgryql yfpkgetgvw tlnqdsmsyd spsptadrtm hidkysgkvl adikfddypw
      361 fgqfmaasia fhmgtmgwws valnvvfcll vifmcvsgyi mwwkrrptga alcppaqgrd
      421 lptwktaaiv llivaaifpt alvaiavial ldwllisrfs tlknwfk
//
LOCUS       WP_285060845             154 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase, partial [Kingella kingae].
ACCESSION   WP_285060845
VERSION     WP_285060845.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 154)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 154)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 154)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         <1..154
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          <5..148
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 lwhclvlqht fqdttqkinl reesdgtqki fefsglilkv ltkgdtliid elnkslhpdl
       61 arflvklfns elntknaqli ftthetsilr kdllrrdqiw fceknndkss yfysltefkp
      121 hvsredieey ylhgrygakp mltdfhmldh fvee
//
LOCUS       WP_285061282              90 aa            linear   BCT 25-DEC-2024
DEFINITION  dTMP kinase, partial [Fusobacterium necrophorum].
ACCESSION   WP_285061282
VERSION     WP_285061282.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Cui,Q., Shin,W.S., Luo,Y., Tian,J., Cui,H. and Yin,D.
  TITLE     Thymidylate kinase: an old topic brings new perspectives
  JOURNAL   Curr Med Chem 20 (10), 1286-1305 (2013)
   PUBMED   23394555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         <1..90
                     /product="dTMP kinase"
                     /EC_number="2.7.4.9"
                     /GO_function="GO:0004798 - thymidylate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006233 - dTDP biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
     Region          <1..83
                     /region_name="Tmk"
                     /note="Thymidylate kinase [Nucleotide transport and
                     metabolism]; COG0125"
                     /db_xref="CDD:439895"
ORIGIN      
        1 lntfatqsla pdltlvfdvs pevgqarraa grddriesrg tefharvrqa frdlarlepe
       61 rvevlsalas paeihrevle tlrvrhmidl
//
LOCUS       WP_285061331             178 aa            linear   BCT 25-DEC-2024
DEFINITION  GAF domain-containing protein [Fusobacterium necrophorum].
ACCESSION   WP_285061331
VERSION     WP_285061331.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Ho,Y.S., Burden,L.M. and Hurley,J.H.
  TITLE     Structure of the GAF domain, a ubiquitous signaling motif and a new
            class of cyclic GMP receptor
  JOURNAL   EMBO J 19 (20), 5288-5299 (2000)
   PUBMED   11032796
  REMARK    Erratum:[EMBO J 2001 Mar 15;20(6):1483]
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005630
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..178
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=20814
     Region          <16..>178
                     /region_name="GAF"
                     /note="GAF domain [Signal transduction mechanisms];
                     COG2203"
                     /db_xref="CDD:441805"
ORIGIN      
        1 mnflnfildd vkkyseivsk vigmdvevmd ssftriagtg slkekvgldm keeshiyhqv
       61 lesketiiil eprkdmhclt cekkflckee leistpimyq ddvigvigli cfekykknef
      121 igkkdlyiqf lkqisefisy kvyeyfhslq lkrdneilsn iidrvqdiii ltnrknqi
//
LOCUS       WP_285061474             358 aa            linear   BCT 25-DEC-2024
DEFINITION  GGDEF domain-containing protein [Paenibacillus polymyxa].
ACCESSION   WP_285061474
VERSION     WP_285061474.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus polymyxa
  ORGANISM  Paenibacillus polymyxa
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 358)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 358)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Paenibacillus polymyxa"
                     /db_xref="taxon:1406"
     Protein         1..358
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40121
     Region          89..356
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mlkelinnfa lltsflffgn lffrkyeryl kkhvfiyrvm nglmlglfgi llmmtglwir
       61 ghfvvdlrhl aiiisvymgg svsgllttli islyriyitg gwtdvsltat vncfmtlgis
      121 lifirekslt lrkwmsavig aavvsllstf yvvnppdnes miiittvkll gglftyfmms
      181 hikkteravh lleeaanrdh ltglyspraf dalfeevfht skttkqpfgl mmldidhfkn
      241 indtyghlng dtvlsqlgml ltresttray psrkggeefa iligncdsqk aasfaekirk
      301 avenerflln dgtmisltis igagsspvia srhllektde alyeakrsgr nqvklakp
//
LOCUS       WP_285061475             319 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus
            polymyxa].
ACCESSION   WP_285061475
VERSION     WP_285061475.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus polymyxa
  ORGANISM  Paenibacillus polymyxa
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Paenibacillus polymyxa"
                     /db_xref="taxon:1406"
     Protein         1..319
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36297
     Region          1..319
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrlhrliail lciesrgrmk akelalalet svrsiyrdid llaeagvpiv tasgpkggiy
       61 lmegytanlk qlnggdviql yltgmgiytg gptesglklk nallkleqtm pdpyqsdikk
      121 akarfyfddt pwwteriaip cleavraavw gshkitiqye kadgicssrh vhpyglvvkk
      181 gdwyliafce vvqeirtfkc erikevqpsa evfevpvdfs lehhwmrqet afkqlcteke
      241 yypvlirtnk kqagiiakrm diihsvqegs hftltvnmys yeaachdamn wigrvevvep
      301 vplrqfvkee inrlqrlyg
//
LOCUS       WP_285061538             716 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Kingella negevensis].
ACCESSION   WP_285061538
VERSION     WP_285061538.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 716)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 716)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 716)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..716
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=80310
     Region          1..716
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mptpqpqapy dsltadyreq llrearylsa deqqqlekac afafhahdgq irksgepyit
       61 hpiavatela rwrmdiqals aglmhdvled tsvtkeqmta efgdtiaemv dglsklenlk
      121 ydskeehqae sfrklilamt kdvrviivkl sdrlhnmrtl gakkpasrrr iatetlevya
      181 pianrlglnh vyrelqdlaf famhparygv lqramttfkk nrhdviervl remslrlvgq
      241 nieaqirgre rnlysihqkm ltkkvkfeel qdiygfrviv nsvsqcytal galhglyqpk
      301 pgkfkdfiai pksngykslh ttlsgpyglp ievqirtrem nmiaevglas hwrdsgsqed
      361 ettrrtnqwl knildlqars enaieflehv kidlfpnesy mltpkgkiit lprgatpidf
      421 ayavhtdvgn hcvgarvnki pvplrtrlkt gdtveiitse yakpnpawln faassrarsa
      481 irsyiknadr sdaialgerl latalgsllp kkvaesdelk ekyfqqladk qlsfedvlyn
      541 vgigrtmpva vameiatmag ehfgdevkls piqvnsheta rvhlgkcclp vagdsiravv
      601 vpeqglmihr dicpvllktd vehqldadwa alpegmekiy qtalvvssed shgllanmas
      661 aisetgcdiv svdtlskaqe gfiefkftlt vrdllhvqav marlhkivqv rkvarv
//
LOCUS       WP_285061540             668 aa            linear   BCT 25-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Kingella
            negevensis].
ACCESSION   WP_285061540
VERSION     WP_285061540.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Shan,L., Mathews,I.I. and Khosla,C.
  TITLE     Structural and mechanistic analysis of two prolyl endopeptidases:
            role of interdomain dynamics in catalysis and specificity
  JOURNAL   Proc Natl Acad Sci U S A 102 (10), 3599-3604 (2005)
   PUBMED   15738423
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Polgar,L.
  TITLE     The prolyl oligopeptidase family
  JOURNAL   Cell Mol Life Sci 59 (2), 349-362 (2002)
   PUBMED   11915948
REFERENCE   3  (residues 1 to 668)
  AUTHORS   Polgar,L.
  TITLE     A potential processing enzyme in prokaryotes: oligopeptidase B, a
            new type of serine peptidase
  JOURNAL   Proteins 28 (3), 375-379 (1997)
   PUBMED   9223183
REFERENCE   4  (residues 1 to 668)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 668)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..668
                     /product="prolyl oligopeptidase family serine peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=74489
     Region          2..666
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mqdtyqylen lhspetqkfh qsahaetlaq fcqsenfhkt kqqiteqlqd erqipfcqeh
       61 rarmyhfhqs adlpkgvyrv csaasyragi pdweilfsva dfdeilgddv yldgvshyve
      121 rpelalisls sqgsdsayti efnlkageiv sggfhfplgk nhvawrdens vwvcpawder
      181 qlttsgyprq vwlmqrgqsf deatpvyemd adgvmvsawr yldaqgapld lieantsffq
      241 kdyfyvnadl aavklalprd cevvgylagq lflhlksdwq rskqkyvsgs liavklnkge
      301 lgeafclfap tssqalelie ttrkfviasl ldnvsgslka wkwengawve qalprfpnga
      361 ieladqpwgg dtvylaasdf vtpltlfald lnvmeltvlr rqpkqfnaqd ivvtqnfats
      421 adgtripyyh vgktqspdtp tlvyvyggfa vpelphymga igrhwlergg afvlanvrgg
      481 gefthwhtaa qrenkhksvd dllsvindlv ergyssakki aiqggsnggl vvasafcrlp
      541 enlgamicev pltdmlryte lyagaswide ygdpaypkmr eylaafspyh qlsgslnypp
      601 afittslsdd rvhpahalkf yaklrdnpna kawlfapekg ghtgngtqae taeelaavla
      661 flqqtivl
//
LOCUS       WP_285061676             744 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Kingella negevensis].
ACCESSION   WP_285061676
VERSION     WP_285061676.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 744)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 744)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 744)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 744)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..744
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=78332
     Region          4..743
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 matqhinfni qgmtcqacan riekvlnkke fvseavvnfa getaqitfdd tqtnpdelik
       61 iiektgfqaa vqtsllpetd sheshwrvwt llalslpfwv gmlgmlgssh almpplwlqi
      121 aiatvaqtyf alpfykgava svrgglanmd vlvsvgtlsi ylyslgmvla ghahhvyfea
      181 gvmvlafvsl gkyleaktkr gslnalgsll qltprdvqil qnnqwqtvki dqvkqgdilr
      241 cvqggriaad gevvsgegwv deshltgesq pvyktignkv lagsilsgsl dyraeslgsd
      301 tllgdmvaav adaqgskapi arladkvaav fvpsvlaial ltlvanwliv gdftaalvra
      361 vavlvvacpc alglatpaai magigqavqh gvwfknaaal emagavdtvi ldktgtltqg
      421 kpdiaaiwta dnftenqlfe iaaaveqhaa hplanaivqa afvreiapln aenvntvage
      481 giganiddlg dvkvgkldfc gfrlpeslip sprrrgqtvs dsnnvianpn nplpqgegav
      541 gsvwqiaslv avslnnqpvg afaladplkp dslaaiqrlr ehniavhils gdnaatvahi
      601 aqqlglpenh ahgnqsprqk aefiqqlqqq gakvamagdg indapalala dvgfavrgst
      661 diaeqsadav lvqqsvnqla sglivaratl raikqnlffa fvynalgipf aavglltpvl
      721 agammamssv svlgnalrlk rmkf
//
LOCUS       WP_285061552             378 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Kingella
            negevensis].
ACCESSION   WP_285061552
VERSION     WP_285061552.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..378
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=43577
     Region          4..378
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mlilkafkfe lipngeqirk lkqfcgcsrf vfnralayqn eqyqkdnsfk fsyakianll
       61 pewkrelvwl kdchsqvlqq alkdlesafk nffakrsdfp kfkrkgekds frfpqgckle
      121 qhnnriylpk mgwvryrnsr aisgslknvt vsqkcgkwfv aiqtefeqei plpkggevgi
      181 dmgivrfatl sngeyfepin afknlkgkla klqkrfknkt kfsknwqklk akiaklhhki
      241 snirknylhq issqisqnha ivyvedlqva nmsksakgdv eqhgknikqk sglnraildq
      301 swyefrrqla yklawnsgfl favppqntsr ccpncghttk dnrqtqanfe cvdcgyqnna
      361 dvvgainilk rgqaiqaa
//
LOCUS       WP_285061813             273 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Kingella negevensis].
ACCESSION   WP_285061813
VERSION     WP_285061813.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..273
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=30104
     Region          55..269
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mklktvlvfl aigfqaacsg sdgkkqaese aaaskpkvev yvdngpkpqy wamsnvsypp
       61 fsfrnkdgfl tgldidllna iaekerieik impqemdslf rrldedatdi ilgginitpa
      121 rqqkyiftqp ylnlfsaalv dkkvsgklts fsqlngktag vvassaydml akqaqfgavk
      181 yfpniyqgit amasgkvaav ydnervldly aannphlyil kntsskvyfg fvlskkndvl
      241 kqrldkglea irkdgtydki lakwgteqvr gki
//
LOCUS       WP_285061683             385 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Kingella negevensis].
ACCESSION   WP_285061683
VERSION     WP_285061683.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..385
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=44011
     Region          2..379
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mkltdkqcan agvpekgtkq lsdgggmyle irangckywk mkytspitkr qtilhlgtyp
       61 emnlkaarta hmkarfeies gndpkdqkqa akkkaasnre ntfehiartw htdrskqadk
      121 wsedhaarvl rslelhifpy igslpiaeim pmqvleqlkr ieyagkndta hkvydvvnqv
      181 fsyavrlric lfnptaelrt elaavkqksf phitdpiqig ellrkidgyl glpqtrtllk
      241 ispylftrpv eirtmkwsei dfqaalweks gedmkngldf ivplpkqaie lleslkpftg
      301 hyeyvfynia knqplseaaa skamqrlgys gimtphgfrh mastrlnemn fnkdwieaql
      361 ahkdpntara tynkaqyldt lrhqp
//
LOCUS       WP_285062258             276 aa            linear   BCT 25-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Frigoribacterium
            sp. ME-P-080].
ACCESSION   WP_285062258
VERSION     WP_285062258.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium sp. ME-P-080
  ORGANISM  Frigoribacterium sp. ME-P-080
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     BTLCP proteins: a novel family of bacterial transglutaminase-like
            cysteine proteinases
  JOURNAL   Trends Biochem Sci 29 (8), 392-395 (2004)
   PUBMED   15288868
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Frigoribacterium sp. ME-P-080"
                     /db_xref="taxon:3040289"
     Protein         1..276
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=29154
     Region          76..220
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mkrtasarle fdvdgpaefv lsiaasraya apdavaqvgt ariteealav tqhgapleir
       61 elhdhhgtll hlcevgagrv tvdyrvvvdg rldepavddl dlvryrrpsr ycesdtlspt
      121 araefggleg rellaavatw vgshlayvpg asaptdgavq tlldrqgvcr dyahlviall
      181 rgldvparlv svyapglspm dfhavaeafv dgawhvvdat glaprqtllr iatgrdasdt
      241 aflsshggrv tvagmqvgav adelprddvs tfvslg
//
LOCUS       WP_285062186             707 aa            linear   BCT 25-DEC-2024
DEFINITION  transketolase family protein [Frigoribacterium sp. ME-P-080].
ACCESSION   WP_285062186
VERSION     WP_285062186.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium sp. ME-P-080
  ORGANISM  Frigoribacterium sp. ME-P-080
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Schenk,G., Duggleby,R.G. and Nixon,P.F.
  TITLE     Properties and functions of the thiamin diphosphate dependent
            enzyme transketolase
  JOURNAL   Int J Biochem Cell Biol 30 (12), 1297-1318 (1998)
   PUBMED   9924800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Frigoribacterium sp. ME-P-080"
                     /db_xref="taxon:3040289"
     Protein         1..707
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016744 - transketolase or transaldolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=73098
     Region          3..688
                     /region_name="TktA"
                     /note="Transketolase [Carbohydrate transport and
                     metabolism]; COG0021"
                     /db_xref="CDD:439792"
ORIGIN      
        1 mihdldaaav ttarllalda veragsghpg taaalapvah llfqkhlrhd pqapdwagrd
       61 rfvlscghas vllytqlflt gydvslddlk afrsfgsrtp ghpelghtpg vetttgplgq
      121 glatavgmam amlheravnd pdaapgesvf drrvfvlasd gdlqeglsye agalagrhrl
      181 gnltvvyddn diqiegdtsl tssenvgarf aaqgwrvdhv glapdgdvdv ealdevlstt
      241 drrgdrphlv vlksqiawpa pnarntsash gaplgaaeva atrvelgvds epftvddavl
      301 ahtrsvlerg raareawqva ahaweaahpa aaaelhrsrs rtlpadlgsr lpvfspgdtl
      361 atrdasgkvi qalaealpel wggsadlaep nrtaiaggas ylpeeapgtg ragrnvhwgv
      421 regamasamn gialiegsrf fagtflvfsd yqrpairlaa lmqlpvtylw shdsvalgad
      481 gpthqpiehl aslrampgfs vvrpadgaet aaawlailek dgpaglvlar qplpvaptpa
      541 dvvragvrrg ayvvqdggaa aaaaaaaaga aagtgttgag tteagapdvv vvatgseval
      601 vleavaridd lavrvvsmpc rewfdaqpae yreqvlprav tarvvveaaa sfgwegvagp
      661 dgvvvgidef glsapaadal rergmttdrv vaavraaaar aatsvas
//
LOCUS       WP_285062329             403 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Frigoribacterium sp. ME-P-080].
ACCESSION   WP_285062329
VERSION     WP_285062329.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium sp. ME-P-080
  ORGANISM  Frigoribacterium sp. ME-P-080
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Frigoribacterium sp. ME-P-080"
                     /db_xref="taxon:3040289"
     Protein         1..403
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43118
     Region          325..395
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mpddqpaeta tltsgvaata aaatadtadt avgapatppp vvvgrgeaae gvgigtadrp
       61 vrervtapdv vaspepvagv twrpltlddl vplhalcarm gsvdhpdrgh alevvrddlt
      121 spgidlvrds ivgvdaegrf vawglshlgp trvslvrvgv pggvdpgrrg eglgrrlldw
      181 qrvrgeqhla tcdevlpagl vtdveedala traafrragf desrwwtelr rdltepierv
      241 aldpavrlvt mtdewveatr qarndafrdh wgsqptseer wgrmvgagtf rqdlsllava
      301 rplddpeaae qvvafvlsdv dpedwaalgr rcayveyvgv rrswrgrhla qsllastlea
      361 hvaeglevtv ldvdsvsptg alglydragf vaarrsatvv ray
//
LOCUS       WP_285062373             220 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Kingella
            negevensis].
ACCESSION   WP_285062373
VERSION     WP_285062373.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..220
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=24972
     Region          <4..216
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mviiyllkig wvryrnsrai sgslknvtvs qkcgkwyvsi qtefeqeipl pkggevgidm
       61 givhfatlsn gqyfepinaf kalkgklakl qkqfkhktkf sknwqklkak iaklhhkisn
      121 irknylyqis hqisqnhaiv yvedlqvanm sksakgdaeq hgknvkqksg lnraildqsw
      181 yefrrqlayk lawnggflfa vppqntsrcc pscgytallp
//
LOCUS       WP_285062505             113 aa            linear   BCT 25-DEC-2024
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Kingella
            negevensis].
ACCESSION   WP_285062505
VERSION     WP_285062505.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..113
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=12535
     Region          1..>56
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 mrilsyniqa aiasdsyfsy vsrlhrqvmp spakeqvlan iakyisdfdv vclqeidlgg
       61 frngfqnqvq qllaqtpfsh hmcqtnrvvg klkpaetaln aplrtksrnl gvt
//
LOCUS       WP_285062525             183 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Frigoribacterium sp.
            ME-P-080].
ACCESSION   WP_285062525
VERSION     WP_285062525.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium sp. ME-P-080
  ORGANISM  Frigoribacterium sp. ME-P-080
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Frigoribacterium sp. ME-P-080"
                     /db_xref="taxon:3040289"
     Protein         1..183
                     /product="metallophosphoesterase family protein"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19961
     Region          5..166
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mptsvlvvsd thvpqkakav pgavwtaver advvvhagdw tgeplldefe ararllvgvw
       61 gnndgdalra rlpevartti egvslavvhe tgakearerr mdrdfpetdl llfghshipw
      121 dtttpaglrl lnpgsptdrr rqphatyltl tldagevrdv vlhelpvaar drtgvlphpr
      181 mtt
//
LOCUS       WP_285062586             227 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Frigoribacterium
            sp. ME-P-080].
ACCESSION   WP_285062586
VERSION     WP_285062586.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium sp. ME-P-080
  ORGANISM  Frigoribacterium sp. ME-P-080
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Frigoribacterium sp. ME-P-080"
                     /db_xref="taxon:3040289"
     Protein         1..227
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=23523
     Region          33..174
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mtgarvwlvd ldldlglgre gdagappase vcdayerara aafvdatdar rylashralr
       61 lllssvtgre agsiefgrea crscggphgr pvpvpsddlh vslsrsgrwa avavragapv
      121 gvdvegarpa galehlrpdv spedvdvdvl rawvrkeall kstgegltta msalrlgpgp
      181 ggtttdgrrg lvhdrrsmtg vllavagpal daveftdvtp gvptvrp
//
LOCUS       WP_285062629              68 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: YegP family protein [unclassified Frigoribacterium].
ACCESSION   WP_285062629
VERSION     WP_285062629.1
KEYWORDS    RefSeq.
SOURCE      unclassified Frigoribacterium
  ORGANISM  unclassified Frigoribacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="unclassified Frigoribacterium"
                     /db_xref="taxon:2627005"
     Protein         1..68
                     /product="YegP family protein"
                     /calculated_mol_wt=6946
     Region          2..59
                     /region_name="YegP"
                     /note="Uncharacterized conserved protein YegP, UPF0339
                     family [Function unknown]; COG3422"
                     /db_xref="CDD:442648"
ORIGIN      
        1 magtfvvtqd asgeyrfalt tgsgvviass eghrqkgaam naiddlrrta vdavvddrts
       61 vpepghad
//
LOCUS       WP_285062694             365 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein
            [Frigoribacterium sp. ME-P-080].
ACCESSION   WP_285062694
VERSION     WP_285062694.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium sp. ME-P-080
  ORGANISM  Frigoribacterium sp. ME-P-080
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Frigoribacterium sp. ME-P-080"
                     /db_xref="taxon:3040289"
     Protein         1..365
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=38467
     Region          17..357
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 msatgassst dgpglllvtg gagfigsaiv dlaldrgwrv rvldslrpdv hggeptvdpr
       61 vdfvhgdvrd aetvdralag vdavchqaak vglgvdfqda pdyvssnelg tavvlaamdr
      121 agvdrlvvas smvvygegsy rtstgaterp aprriadlda gvfdprdeag ellepqlige
      181 eapldprnvy aitkltqehl stswarstgg raaalryhnv ygpgmpqntp yagvaslfrs
      241 alergeaprv fedgaqrrdf vhvrdiasan laalewtanq padtfrafnv gsgtvhtige
      301 maealareag gptpvvtgey ragdvrhvta ssarlqgelg wrpsvtfeqg mhefasaplr
      361 aavvr
//
LOCUS       WP_285062708             185 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsB family cell division protein [Frigoribacterium sp. ME-P-080].
ACCESSION   WP_285062708
VERSION     WP_285062708.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium sp. ME-P-080
  ORGANISM  Frigoribacterium sp. ME-P-080
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Frigoribacterium sp. ME-P-080"
                     /db_xref="taxon:3040289"
     Protein         1..185
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=19824
     Region          28..119
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 mpretanrrv pvtlptgetp tghwlrsirf sgfsvlmlvi lvmfvvilap slrtlvqqqq
       61 qiaalqddvr qqeqsvdelk edvarwsdpa yieaqardrl lyvypgeysy lvmgddaaqa
      121 pgtapgtgts isdslqtpqv dwvaamtasv ldaglsdepa telvapdisg sqvpaptseq
      181 tggtp
//
LOCUS       WP_285063082             257 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Kingella kingae].
ACCESSION   WP_285063082
VERSION     WP_285063082.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..257
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=28241
     Region          144..246
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
ORIGIN      
        1 mqaafagmgk qpalnylnkq kfyfthmtkp lsliisllgl aacatspqsa ppivqaasvp
       61 tsipypeptq aeqinqlaiq varleqqiav lteqlnqhet khhscntsrn qtkqpapkrv
      121 tapavsqskp eastsplsqa qtwykqgqyq kvldllrlhd sggngdanaq qsmilllqsn
      181 qklgycqsvi qigqrfatlf aqhdfapeal yavgqcqwqi qqrdiaketw rnlvlrypnt
      241 paarragssn pvkkdtp
//
LOCUS       WP_285063094             177 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix domain-containing protein [Frigoribacterium
            sp. ME-P-080].
ACCESSION   WP_285063094
VERSION     WP_285063094.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium sp. ME-P-080
  ORGANISM  Frigoribacterium sp. ME-P-080
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10582168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Frigoribacterium sp. ME-P-080"
                     /db_xref="taxon:3040289"
     Protein         1..177
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19295
     Region          2..73
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 msaldelrat ahpirlrlls lltgvamsaa eagrelglsq atasyhlrvl ervglvevve
       61 vvtirggeak ryrhlssaqp fpvvppsvdg tdddtdvera ryvdaladel rrrsprradg
      121 pqistdaelw vdpetwqrvv rhvghasall haaaqrprtp gtnpvsmtaa lfpmrrp
//
LOCUS       WP_285063168             266 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Frigoribacterium sp. ME-P-080].
ACCESSION   WP_285063168
VERSION     WP_285063168.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium sp. ME-P-080
  ORGANISM  Frigoribacterium sp. ME-P-080
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Frigoribacterium sp. ME-P-080"
                     /db_xref="taxon:3040289"
     Protein         1..266
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27145
     Region          4..238
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mstasdfart irrreravgy witldappat eriarlgydy vcldaqhglf gyqgmmtgll
       61 aidagqtsag lvrveandit pigkaldaga agvivplvdt aedaasavrs akypphgrrs
      121 ygpmrsslri gpvpadandt tivlamietp dglsnveaia atpgldglyv gpsdlciavg
      181 gaypgdpavq eafdaalvrv aaaaeaagia agihtphgdv arqrlaagyt fatvagdlnh
      241 leaaardhlq ratatddpdt taggaa
//
LOCUS       WP_285063324             553 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Frigoribacterium sp. ME-P-080].
ACCESSION   WP_285063324
VERSION     WP_285063324.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium sp. ME-P-080
  ORGANISM  Frigoribacterium sp. ME-P-080
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Frigoribacterium sp. ME-P-080"
                     /db_xref="taxon:3040289"
     Protein         1..553
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=60188
     Region          44..495
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 msdatrassv pgegddrpag gddrpaggdd rpaggddrpv vggvehvdll vvgaglsgvg
       61 vaaqlrrdfp rrslavvear aaiggtwdlf rypgvrsdsd mftlgygfrp wrdaraiapg
      121 eaireyvrdt adetgvagli rfghrvvaad wvsaearwtv tievastsaa dassaagees
      181 saggtgavpt srrvtitcsf lfvcsgyyry degwspafpg qdsfagrvvh pqhwpedldv
      241 sgkrvvvigs gatavtlvpa laesaeqvtm lqrsptyvls lpsrrkepra wrrllpqavd
      301 drlirwrsig mallsfqtsr rspekmkafl raqvaqrlpd dfdvdrhfqp sydpwdqrlc
      361 itpdgalfra lrsgsasivt ddidsftagg vrvkgrdgqr ahelpadvvv tatglnlllf
      421 ggmrlsvdgv evdpatrlty kgfmlsgvpn lafaigytna swtlkidlvv hyvarllrha
      481 drhgyrsavp iaperpgpts plidltsgyv srgvhlmprq gsrspwrmhq nyprdvwlmr
      541 hstltrdgvr fer
//
LOCUS       WP_285063393             363 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Kingella kingae].
ACCESSION   WP_285063393
VERSION     WP_285063393.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..363
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=42799
     Region          1..348
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mkrnisldff rgimsiaval ghffhwngqt skmplsfila vdfflvlsgf visvsvfnke
       61 nfntykfiks ryfrlipvyl fcviitlipq yffaenfvkp nsldvirils igemlpmnnl
      121 rfiyfeplgi sytisaefsv gillfplifv irkyasqlll pvliifslfa flkivndtsy
      181 flnihyalay pfitygvirc lldyslgvia ytifeqrttn neqrttnneq rttnnwatvf
      241 qiivlvlcfl lyrkisynrv nefvfpficm vfiislahrr gvifhwfnng igqffgdisy
      301 pmylihpffi nifqwthqef nylnslfyil lcvvsaffih kfiekpciiy fskqynivif
      361 kly
//
LOCUS       WP_285063543             466 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Frigoribacterium sp.
            ME-P-080].
ACCESSION   WP_285063543
VERSION     WP_285063543.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium sp. ME-P-080
  ORGANISM  Frigoribacterium sp. ME-P-080
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 466)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Frigoribacterium sp. ME-P-080"
                     /db_xref="taxon:3040289"
     Protein         1..466
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48908
     Region          28..462
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mgisekdydv avigagpagt aaalraaelg arvvvleagr eggtcvntgc vptrvlakta
       61 rliretrhad vygvgvappt idwattvarv rervdavrsi kreaerfeaa gvelvhegra
      121 rfvddstlvl dsgrtisaas ilicvgghsr rlpipggela tvpehvldlp slphrvavig
      181 agntgaqlvt vfdafgsdvt lldvaprvlt tsdasiseav svafteqgid vrtgidgves
      241 laraddgsit ltwrqddaha radfdvvvma tgwpadvedl glenagieve rssvpvdryf
      301 rtvvphvfav gdangrdmlv qaaqfegeaa aenavlganr rtphhllpag gftdpdyagv
      361 gltedearea descvvvtip ystvdravid dretgflkli adrrrelvlg ahavgenave
      421 vvqavttama ggvdvatlae vrfayptysa vigmaaravl adrtpr
//
LOCUS       WP_285063561             443 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Frigoribacterium sp. ME-P-080].
ACCESSION   WP_285063561
VERSION     WP_285063561.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium sp. ME-P-080
  ORGANISM  Frigoribacterium sp. ME-P-080
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Frigoribacterium sp. ME-P-080"
                     /db_xref="taxon:3040289"
     Protein         1..443
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46159
     Region          98..426
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mdwllsvpll sttmlltvdv vaalvavgll vrprtrrtww rwialavllg aglgalatww
       61 lgdvrdvlgl sptwvdrlwv aavvagvavv vvnlfrtrww rklvavlavl vfalagglal
      121 nrdgsvyqnl sqalgrdevp alpataaapp saapgstefd ptlwstwkap adlpavgryg
      181 svaipgavsh fpardavvyl ppaalvadap alpvmimlsg qpaepssvit aghlvetlda
      241 faaknhglap ivvvpdqlsa dahnpmcvdg algnsatyit tdvvdymtsh fhvatgpraw
      301 aiggfsqggt csiqfasarp dlfstfidvs gelgpsigde kttidqgfag nraayeaarp
      361 qaimaahgpy edtaaffavg atdgrygqim tansaaaaka gmtvtryvsp gsghdwttat
      421 ngfahgigqf yprlglsatv qtp
//
LOCUS       WP_285063746             330 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Pantoea anthophila].
ACCESSION   WP_285063746
VERSION     WP_285063746.1
KEYWORDS    RefSeq.
SOURCE      Pantoea anthophila
  ORGANISM  Pantoea anthophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Pantoea anthophila"
                     /db_xref="taxon:470931"
     Protein         1..330
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35551
     Region          1..330
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mnefswkvaq spedaaamkq qaggqllagg ttqldlmkcg vftppqligi tglttlktlq
       61 fdenritaga lvtmsqladh pecqqrapai ysslwqaasp qirnmatlgg nlrqrtrcay
      121 yrdpatfsac nkrnpgsgca ardgvnsnha ilgasdscia vypgdlaval vafdaivvvq
      181 nqqgetrria iddffllpgd spdrehdlre deiivaievp qttslrhshy lkvrdrssye
      241 faaasaaagf tlengvmrqv hialggvatk pwrvrsveqa legqpfneet vfqaaelitq
      301 etqalahnay kvklaprvia ralmaageta
//
LOCUS       WP_285063790             709 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Frigoribacterium sp.
            ME-P-080].
ACCESSION   WP_285063790
VERSION     WP_285063790.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium sp. ME-P-080
  ORGANISM  Frigoribacterium sp. ME-P-080
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Frigoribacterium sp. ME-P-080"
                     /db_xref="taxon:3040289"
     Protein         1..709
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=73244
     Region          74..421
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mittptreap psrrrhprll vrttrttrla aaaavvalgv tlagcasgat gatadpappa
       61 ppqhqpgghs ltkddvdtwl dgavgsalqt tgipgatvsv vadgkvltar gygmadtgtg
      121 etpaeavdpe rtlfrvgsvs kvvsataimq lvekgdldld advqqyldfd ldtpkgavtl
      181 rhllthtagf eeviagligt pgsektlrea vseappaqvf tpgttpaysn ygatlagyva
      241 ervsgvpfad llqqdvfdra gmtsssfaqp lpadldarla hgypddskpa vatevvnaap
      301 agamsatatd marfmlaqlg dlpddqallq pdtlaemhrp algaddlgtl vagqrmdlaf
      361 fddstpglaa fghdgdtqvf hsamrmfpeh dtgiflsmng sgrsatasld lrttvlqgfa
      421 drylrdaatv gtadtdsrgg agtvdgdasd gpvaadlagt ylssrspvtn pgallalsgq
      481 ttivprsdgt vavtpkplgv ttgvyekvgt dlwrevggda llatrttdtd gdstveaisw
      541 gasftmlraq pwqaasavlp svvlavvvll asmivwpata lagvgrrrrd lraglstgsa
      601 tttprrrdrt lllsrlgqas tllalvgwav vavqamsfae vsavtlrvlq glqllgvvai
      661 vpaalvawra vrdrrgwavv tgrvlvlasl vvlagfafgf rliapsvsf
//
LOCUS       WP_285063764             295 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein
            [Frigoribacterium sp. ME-P-080].
ACCESSION   WP_285063764
VERSION     WP_285063764.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium sp. ME-P-080
  ORGANISM  Frigoribacterium sp. ME-P-080
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 295)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Frigoribacterium sp. ME-P-080"
                     /db_xref="taxon:3040289"
     Protein         1..295
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=31759
     Region          2..287
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkvvitgsrg kvgraavrrf veaghdvlgv dlvrpvfdtg vdepgryvmg dltdpgtafs
       61 vvagadvvvh vaaipqptan pahvvfhtnl mstfnlveaa vrfgvprfvn vssesivgnf
      121 fperpflpdy vpvdeehplh pqdpyalska fgeqlmdaav rrsdlraisi rpstvhdddn
      181 yeanlgpqvr eadpdsanfg syvdaddlad alllaaesdl pghevfyiaa adnagghdfa
      241 atlrqhhgdr ielreltrad asgistakaa rmlgwratrs wrdhldaegh alpka
//
LOCUS       WP_285063812             196 aa            linear   BCT 25-DEC-2024
DEFINITION  CGNR zinc finger domain-containing protein [Pantoea anthophila].
ACCESSION   WP_285063812
VERSION     WP_285063812.1
KEYWORDS    RefSeq.
SOURCE      Pantoea anthophila
  ORGANISM  Pantoea anthophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Pantoea anthophila"
                     /db_xref="taxon:470931"
     Protein         1..196
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21737
     Region          6..190
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 maetqsstaq gpwfladhpa ldfintvaiv dgqphdfwqt dedvdawlqq aglatdgpaa
       61 hseagtllqa arqlrdnird mvqqqkagea idlrvlnawl geaishmqlv teqgtlqirr
      121 iypaqsamqr lgrvaeqaas llaqadfsrv racehpacnl wfydrtkahr rrwcsmalcg
      181 nrakvarfrq gvkseg
//
LOCUS       WP_285063860             361 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Pantoea anthophila].
ACCESSION   WP_285063860
VERSION     WP_285063860.1
KEYWORDS    RefSeq.
SOURCE      Pantoea anthophila
  ORGANISM  Pantoea anthophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Pantoea anthophila"
                     /db_xref="taxon:470931"
     Protein         1..361
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38372
     Region          18..345
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mvrtrlials llffcaggqa apgfrqvels dsagsplsva iwypaiqqgk retvgenaaf
       61 vgvsvipdas pipgrhllvv ishgyngswr nlswlaaala aqgyivaapd hpgtttfdqn
      121 pdaakklwrr prelsrvidf islhsdlaga adttriaaig hslggwtvls lagarfdpsl
      181 flsscqrfpr rgdcrltnkl gmnevaaqdr fsdlrdsrig avvsldagla pgftsqsltr
      241 mtlpililaa gndslgelpa aqesayiadn lpaslhhyri vkgathfsfm qlckpggekl
      301 ideaspgdgi vcqddrgadr galhqqltsq itlflqsaln ypapaddtpp atfrkaagih
      361 d
//
LOCUS       WP_285063916             952 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Frigoribacterium sp.
            ME-P-080].
ACCESSION   WP_285063916
VERSION     WP_285063916.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium sp. ME-P-080
  ORGANISM  Frigoribacterium sp. ME-P-080
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..952
                     /organism="Frigoribacterium sp. ME-P-080"
                     /db_xref="taxon:3040289"
     Protein         1..952
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=100127
     Region          <113..228
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          384..889
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 matptkstar arsssrasqt sgvtkatkkl pasrqpdpvp dgpgpfvaaw mglahltgga
       61 frllgkesla kderrdgvpf llvllaiaga vvewlnptsp lavgfdaytf gglvgrvaya
      121 lpvimilfag wlfrhpasvh dntrigiglg lsivsisalc hifggqpeaa aglralatgg
      181 gvlgwvvasw lvalatewva vplvvillaf slliitktpp nrihrrlgel ysylfgetts
      241 aadgadadpd lvdlaesesl pwwrrnkdqr eedpaydtpl vkadessate psgrrrrkkp
      301 vfepsvddag saaaagaags aapttaptdv fsadllgdld raedavraqg fdvpsvqpta
      361 sttvlpvvpv vpvvpaepvg esdaaadfla vdpdeaapps ldevddgaes apyrlpaass
      421 lsvgepakar seandaivaa isqvldqfnv dakvtglkrg ptvtryeiel gpgvkvervt
      481 altknlayav asnevrilsp ipgksaigve ipntdkeiva lgdvlrssaa sksvhpltig
      541 vgkdveggyv vanlakmphl lvagatgsgk ssfinsmits llmrakptdv rmvlidpkrv
      601 elsiyagvph litpiitnpk kaaealqwvv kemdmryddl asfgfrhidd fnravvggei
      661 vlpvgsqrkl kpypyllvvv deladlmmva prdvedsivr itqlarasgi hlvlatqrps
      721 vdvvtglika nvpsrfafav ssvtdsrvil dqpgadklig qgdglflpmg askamrvqga
      781 wvqeneiaqv vahvtrqarp dyrpdvaavv ekreidgdig ddlelllaaa elvvstqfgs
      841 tsmlqrklrv gfakagrlmd lmesrdivgp segskardvl vtteqlpgvl aklrggdaas
      901 dagagrassg sssaaradag dydgdpveam trgyaeddda gsedawhltg re
//
LOCUS       WP_285063962             615 aa            linear   BCT 25-DEC-2024
DEFINITION  PT domain-containing protein, partial [Kingella kingae].
ACCESSION   WP_285063962
VERSION     WP_285063962.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10522371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         <1..615
                     /product="PT domain-containing protein"
     Region          1..>19
                     /region_name="PT"
                     /note="PT repeat; pfam04886"
                     /db_xref="CDD:282710"
     Region          477..>540
                     /region_name="PRK12704"
                     /note="phosphodiesterase; Provisional"
                     /db_xref="CDD:237177"
ORIGIN      
        1 tnqptnqptn qptnqptnqr klnypsdyip yeiraqitqi dpnldvfwqq nlndifttls
       61 pqdrknvaqq ilapkhifwn adkkafeyke svqtlaqaan avpasfkklk vlanqvaqsl
      121 sllqndyhea tqiadylenm lekiqlfdcd ndleqhickq nvyrafiyaa advirnkqnl
      181 elppnarklh vnavkvfine vylkqqllgy afktvrnrql lahphplmsq flaheqktrq
      241 levvrasgyl faiapmleys snpfgirrfl eeerlfggsl llhgasynaa ylsgsrppte
      301 lffqkqiefi itiqgnirkv vmdfmeqldv yheerlltll fapfgtssgs lqqevhkrla
      361 dyeklltvgi leplanslrr lpnhqdefdf iyvsmrqllg kmiaalqdfq mqpalllddq
      421 vksllgrlta yatflekrrs dvfaeleqnq waenhkrtll pmkhvrsvak dhldeyrkrk
      481 yavdkqqrll eqteslldkl fkrkaaqere leelkkdlrk vqyeahkqlc yppesvlqlt
      541 vrmefetqln vrpeernlaf pdgdngvsrl pmvltlpenr lqfdvnafak avnvgehede
      601 ekmlheaekv llkrt
//
LOCUS       WP_285063929             582 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Frigoribacterium sp. ME-P-080].
ACCESSION   WP_285063929
VERSION     WP_285063929.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium sp. ME-P-080
  ORGANISM  Frigoribacterium sp. ME-P-080
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 582)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 582)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Frigoribacterium sp. ME-P-080"
                     /db_xref="taxon:3040289"
     Protein         1..582
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=62390
     Region          3..554
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 melgelliil tgslvvtafa rwrglpapll tvgvallvsl ipgvpdieid sevvltvvlp
       61 pllysaaldv sllnfresrv qiarlgvgav ivtafavggv ayvmipdmtl paallvgavv
      121 appdavsaaa igrklglprk vmtvlsgesl indaasltlv kvflaivgga sltlwddlgi
      181 fglaigvgva vglvlgfvah rvrmriddpv venviglllp fiayiaaeel sgsgvlavva
      241 aglyvgfnsp rtgyatrlqe rpfwsaadvl legfvfalig lqlravvldv seserglgqs
      301 vgvalavlav vvlvrpvfvf gtyhaaragr ylflstvlrk lrrvpalrrl rrapalrtvr
      361 yhpqprmdwr qlsviswtgm rgvvtlaaav sipavtessi pvpardtmfl iafivtvgtl
      421 llqgltlpvv irvlgvrddt qrdrdlaael avfatstdet mayvaerrad wekrwgpelt
      481 eravllattr llrqnealqr tavddaderd vsgataaqra rrraapqalg sirrellakr
      541 revvlrerda galdeevmrr vllgldaeel amdtsaftst rs
//
LOCUS       WP_285063965             307 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Frigoribacterium sp. ME-P-080].
ACCESSION   WP_285063965
VERSION     WP_285063965.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium sp. ME-P-080
  ORGANISM  Frigoribacterium sp. ME-P-080
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 307)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Frigoribacterium sp. ME-P-080"
                     /db_xref="taxon:3040289"
     Protein         1..307
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31617
     Region          114..284
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mtpptdspas kkerreaare karvtreaea rrrrrnkwll qgglvvgvva vlaivalvit
       61 qsikpagpgp anmasdglvl egsngavtav psgalaadat ptpapsasgd vpsivvyldy
      121 mcpfcgqfdt tnaqqldeav ssgaatlaih pigfldnasq gsrystraan afacvanhep
      181 dkaldvntal faqqpeentr gltndelvtl vqgagatddq ipscikagdf edwvasatqr
      241 alndpipnss ldklastplv lvngqqyqgs ltdastfaqf vaevqngapt gdtstgdteg
      301 statpap
//
LOCUS       WP_285063967             468 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Frigoribacterium sp. ME-P-080].
ACCESSION   WP_285063967
VERSION     WP_285063967.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium sp. ME-P-080
  ORGANISM  Frigoribacterium sp. ME-P-080
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Frigoribacterium sp. ME-P-080"
                     /db_xref="taxon:3040289"
     Protein         1..468
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48689
     Region          29..460
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mtpkkndrqg dpadeqggef sagaqrvhde llarigeqap qprleptrra vellgdpqra
       61 ypvihltgtn gktstsrmie silrahglrt glmtsphlvh lnerivvdge pisderlvan
      121 wddiqpyltm vdtdleasge ptltffealt vlafacfada padvvvlevg mggewdstnv
      181 adgqvavftp ialdhqnrlg stvaeiartk agivkptaav vsasqtpeal veleravels
      241 egslavegta fgvesttvav ggqvvtirgl agryddlllp qfgdhqaqna avavaavesf
      301 lgggsqpldh evlaeglasa tspgrlqiva neptilvdaa hnphgarala kalddyfqfg
      361 gvvavlsvla dkdaagivra laptvtqfvv tssksdraid adelaaiavg vvgadrvvve
      421 tdlvaalrta rdladevegd epggvvvtgs itlvgdvial sqqpegls
//
LOCUS       WP_285063990             703 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Frigoribacterium sp. ME-P-080].
ACCESSION   WP_285063990
VERSION     WP_285063990.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium sp. ME-P-080
  ORGANISM  Frigoribacterium sp. ME-P-080
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 703)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Frigoribacterium sp. ME-P-080"
                     /db_xref="taxon:3040289"
     Protein         1..703
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=71024
     Region          38..>264
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 msagttpvpl tdrrspsgsa gprlrplarr lvrgredaar werpaflall vatgalylvn
       61 lsangwansf ysaavqagsq nweaflygss daansitvdk ppaslwvmal svrvfglssf
      121 sillpealmg vatvglvwat vrrhfsgvaa fvaggvlalt pvaalmfrfn npdallvlll
      181 tlatyltlrg vetgrvrwvv wagvaigfgf ltkqlqafvi lpvlagvylv aapvllrkrl
      241 lhllaalgav vvsagwwval velvpagmrp yvggsqtnsf leltfgyngl grltgdetgs
      301 vtgggggtga attgmwgetg itrlftgefg gqitwllpaa lvigvsalvl lgwrhrtsar
      361 ratlllfggw tvltalvfsf msgifhayyt valapaiavt lgaaadvlwr rrarswvriv
      421 laasalltgv wawvllgrae swqpwlryvv valavvgavl vllprrgral taatlavllt
      481 ggllapaays vetvstahtg sivtagptvs ggtggfgggg aggaggfggr ggavgggpgg
      541 aaggtppqlp ggtgggagtg tgtgagtagg agtatrghpg ggggagsllg sgsvsdelaa
      601 vvgadadryt wvaaavgsns aagyqlatdd pvmavggfng sdpsptlaqf eqyvadgqih
      661 wfvggtvgqs nggsssssei aawveanfss tevdgvtlyd lss
//
LOCUS       WP_285064006             423 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Frigoribacterium
            sp. ME-P-080].
ACCESSION   WP_285064006
VERSION     WP_285064006.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium sp. ME-P-080
  ORGANISM  Frigoribacterium sp. ME-P-080
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Frigoribacterium sp. ME-P-080"
                     /db_xref="taxon:3040289"
     Protein         1..423
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42425
     Region          24..420
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mshsvrpvpl ssplrrrtsa ttvalvlavl atflvpdrai aaaptwqavl aarddesakk
       61 kaladlqtal daasaraeaa rtsadeagrv lgeaqaavde atarherlet rraearetad
      121 ssrrvvgqaa allarpgsgg mvgdllaagd gaqevlkgls lssklgenvg rlreraqaad
      181 nlatsladqa avalaerdrl aadaqtalde aaaasvtaea dlaavddeka tlaaqvalle
      241 ddrmtleqay aqaqaaaaaa aaaaarpapa agggtgpvap gtggpgpgtg wvaairafgs
      301 yqaygyrihp itgeyklhag adfgascgtp iysvsagrvs yagpssgygn livvdhgggv
      361 ssayahmern giyvsvgqqv aagqniagvg tsggstgchl hlevrqggvp tdpvvflask
      421 gvr
//
LOCUS       WP_285064208             925 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Kingella kingae].
ACCESSION   WP_285064208
VERSION     WP_285064208.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..925
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..925
                     /product="class I SAM-dependent DNA methyltransferase"
                     /calculated_mol_wt=104657
     Region          87..925
                     /region_name="YeeA"
                     /note="Type II restriction/modification system,
                     endonuclease and methylase domains [Defense mechanisms];
                     COG1002"
                     /db_xref="CDD:440626"
ORIGIN      
        1 mltsaqilin aqtfatrwqh esdeksesqt fwneffaifr ldrkaiaile krlksakstk
       61 fadvfvpkkl lceqktkgkn lddaaaqare yleqiraqep enlppyfivc dfvtmrfyet
      121 igtacvefpl eklpeniglf nflldletei hhaqslvnlq asammrelyn gikadydtdt
      181 dtvrkfliri lfclfaedtg ifrpdqfnrl idkhtkadgs dtgaliself qtlntakrsp
      241 klpeylqefd yingglfaet lptiyfdsem rqklihigre inwgfispei fgslfqeald
      301 vnerrelgah ytekdniekv inslflddlk aelaqisslk rdkkkrlief qqkiaklkfl
      361 dpacgtgnfl vaayralrel eiqviheyqk ldkthlqsav sieqffgiei dglaaeiavl
      421 smwlidhlcn lqegaalgkg ygslniplrk sahithgnsl rldwenvdfi fgnppfigst
      481 yqtkeqkadt qavsgslkna gildyvanwy vkaaqimrdn pqvqaafvst nsicqgqqve
      541 alwgalldwg veihfahrtf qwtsqahgka avhcvivgfr qpekhsgaky lfdypdikgq
      601 pekrevanin pylidapnvi iskcskpisg epemiygskp tdggnlilst eekneliaae
      661 plaeqyirrf lgaeeflnnk erwclwfhgm semrlftdlq kmplvakrie lvkqmrless
      721 dkqtnkaaat phlfqairqp esgnyllips assetrefip igyldsntin gnanfslpna
      781 tlyhfgllss tmhnafmrtv agrlksdyry sntivynnfp fpfaafrqpe teispaeqkh
      841 rtaiataaqa vldarahyia qaqqenlpep sladlyrrga pftrlhaaha aldkavdnay
      901 gytggnddad rveflfgvye kmkga
//
LOCUS       WP_285064233             102 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Kingella kingae].
ACCESSION   WP_285064233
VERSION     WP_285064233.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..102
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=12118
     Region          <9..86
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mgfsnlswrk lvntgvyryt khpayvaknl ywwlhtlpfc gvawfsanww hnmlalfgts
       61 lvyygracse erhlmkfpey rayaehiskh glfrklklpf ik
//
LOCUS       WP_285064320             137 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Pantoea anthophila].
ACCESSION   WP_285064320
VERSION     WP_285064320.1
KEYWORDS    RefSeq.
SOURCE      Pantoea anthophila
  ORGANISM  Pantoea anthophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Pantoea anthophila"
                     /db_xref="taxon:470931"
     Protein         1..137
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15749
     Region          <9..125
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          69..115
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mvfvnqtddi mteqlpvcyr slvvisrlds vrtisqkvic swlafqdrmh aflpadclhc
       61 efaritvvql qvlsllkkgy svrqtakrld lsektiyahk ynvmrkfalr gdmefnafin
      121 dlsllelyrg vinsvev
//
LOCUS       WP_285064362            1099 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Gardnerella vaginalis].
ACCESSION   WP_285064362
VERSION     WP_285064362.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 1099)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 1099)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1099
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..1099
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=123893
     Region          <833..1018
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(899,902..903,906..907,909,933,936..937,940..941,
                     943..944,970,973..974,977..978,981)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          899..926
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          931..961
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          969..995
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mqdevqsskk idsaessekn rsdiaddsmq ivqetiktlw enresipvri fskkhifkdf
       61 pmmpknvklg wiklsgkkhg iaiglfnddc krfrqlavad fegrvytghd isiedtmeri
      121 pelsfveqns mtlkdslrfy gvddrkitha sharkkvnsi nknnresdlv virgdvvvql
      181 sqdegmqwvs swirkvndkk eaytleetrv llpdrlrcnl sycdaistsf fasffipdit
      241 rafsgfgsgn ifrrltkeap lgairrsimd skvaekaglr vssmekyfay lmldsgaleh
      301 sgpleavhga erlhlqksqv sdanflvwdd sleakaalkv lriegainrf qsisscleen
      361 canggnlten svnfgqisei dlsfiedpaf cangeldmns fgnplqddni rplmhlwnta
      421 kksndlyiyk sdgssncews yrqrlsglir slylpfrfdt dfrsnledgn valafmstgs
      481 smmptrrfds anqkwitltn adksrmttdy nlrlgiimat lafgaseevq nvsirldsig
      541 leemvaaqdd amskilnqti nalnnmnrea arskgdpkdg dihgdvnngl anvqdlqnft
      601 nhtilhedev tvpdssnkat gsksinssds ysdteisdsn tndigsdpie pdpmdafsky
      661 ptvkslltvt fnresfikhi ranglnnplg aykkfnanmk ideegalnpi epsfdlrdsc
      721 fsphgaqeep efsdvifdik sqktlgttns kglsiqredl lqqavadfhh issevmisna
      781 ekarmamdiv esiddpelne kanlitsali dekeipeisf kvskdiynmr lhaheqfmsg
      841 dlenaieeye navkhfdsmf sfndvvpryf nsyaervvyn rifatqnerm ilipdglfya
      901 hmeladlltq lnrhedalkh lntmvsyapt yvishlklas qltekedwts veavclnalp
      961 vcfdredaaf iyyrlayaew mqdnfplava aykmadnlss gkiesieiel dellsrmqsq
     1021 cipapndmsq veevlkinnv pkwpdveaye iideaakitv negmfviart lsvararmlf
     1081 snnssdnvvq mqflrslns
//
LOCUS       WP_285064364             879 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Gardnerella vaginalis].
ACCESSION   WP_285064364
VERSION     WP_285064364.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 879)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 879)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..879
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..879
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=99083
     Region          25..876
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 msktsyrkkk kndilvdsnd ykndseipls paerfnlfkq tiehsrtmaa kfeqslsfdl
       61 ddfqaeaida lengdnvlva aptgagktvv adfavflgvn rgvktfyttp ikalsnqkyh
      121 dfcevygidr vglltgdtsv npeadivvmt tevlrnmlye rsitlkslgf vvldevhyla
      181 dkfrgavwee viihlpqsvk iiglsatvsn vedfsawiss vrgethlvvd ehrpvplerh
      241 viiqkdgrte pellnlydvd kngnstnhvn laltrkitqw enaslrrkas yrnvnkrfsk
      301 gkfsknkfsn ssksnrgeva vrhtpkrwav ideldyldml pgiyfifsrs gcdqavqqcl
      361 naglsltsde emyeirrivd smiaenklsk sdlkalrfer fryaleqgfa ahhagmiaif
      421 rhivetlfer glikvifate tlalglnmpa rsvvveklvk fdgtghvplt pgeftqltgr
      481 agrrgiddig havlidnpdf dpskaaslss krvyplhssf vptfnmavnl lnnsdvktar
      541 itlsssfaqw eanasaqrll sriedlkeai ngyeqafhct qgdfsefmtl rmrlkdaqhd
      601 qrrklkhtif asevelakaf keldktidtl rneernhpca gcpdiqehlh wgyywaremr
      661 elnqvkdryn srtgsvarcf dsicevlcrl dylkntndal vltdkgqllr rlyneldvvf
      721 aqsicegifn nltpiqllsc lsalvyesrg paggeprryp gglnapvfnt vlkmkelfir
      781 isdmclnnhl dalrpldfga idmiydwaqg adlldilqnt ditggdfvrf akrlidllnq
      841 lavaseylki lpnvddslah nayeaaklin rgvvaycdv
//
LOCUS       WP_285064374             469 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Gardnerella vaginalis].
ACCESSION   WP_285064374
VERSION     WP_285064374.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..469
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=51902
     Region          227..463
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mksipkliqr fisifllstv livlmniiaf vvligsyapd kemspyniak etgealqlsa
       61 sgdyvlsknm sskltnsgaw ailidnntlr vvwktkdvpa tipndytlsd vanlsvgyid
      121 gyptytgdnk ngvvvvgfph ksfwkhtqps wnyslisnfp qivlsvffin illilgiyli
      181 anikllksin pitkgiqrls sgesvhipet galseissni nsasdilqiq keqlrkketa
      241 ranwiagvsh dirtplsmvm gyagqlensl hisqedrkka tmiikqsarm knlindlnla
      301 skleynmqpi mkkeenivav vrqvvvdfmn mgmqdefsik wetdakltvc ninvdkdllk
      361 raisnliqns ishnengcti yvsvaannnn ciicvedngi gvsdekiekl nhaphymicd
      421 tstseqrhgl gllivqqiig ahngtvdisr skyggfkvel tvpskkfgl
//
LOCUS       WP_285064549             375 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Gardnerella vaginalis].
ACCESSION   WP_285064549
VERSION     WP_285064549.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..375
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42287
     Region          9..258
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 menyaknenp lvsiivpvyn sakylsgcvn silaqtykni elilvddgsk ddsgkicdsy
       61 askdsrvkvi hqqnggisra qnagldavsg efiafadndd ildcknieil lnailqsgas
      121 mskakwrqfg lssleqikke aglgarglga eksqatarle natqikivkn plkayqtvfc
      181 kifriignkl gknsearyfn eanwcrlykr eiwqgvrfpe gkfaqdtama svlysrmncv
      241 ahvdevlyyw lqredsvthk mrdagfyhdh idavranwdl clkhnvvpar syytmvgnlr
      301 yercalksge nklnggkssd aeiqkiyekn yvkdvefaks avkkltilqr aqcftmacvr
      361 nlekiiydyk iknmk
//
LOCUS       WP_285065022             370 aa            linear   BCT 25-DEC-2024
DEFINITION  CMD domain-containing protein [Pantoea anthophila].
ACCESSION   WP_285065022
VERSION     WP_285065022.1
KEYWORDS    RefSeq.
SOURCE      Pantoea anthophila
  ORGANISM  Pantoea anthophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Pantoea anthophila"
                     /db_xref="taxon:470931"
     Protein         1..370
                     /product="CMD domain-containing protein"
                     /calculated_mol_wt=40440
     Region          31..201
                     /region_name="YciW1"
                     /note="N-terminal domain of uncharacterized protein YciW
                     (function unknown) [Function unknown]; COG4950"
                     /db_xref="CDD:443977"
     Region          215..368
                     /region_name="ahpD_dom"
                     /note="alkylhydroperoxidase AhpD family core domain;
                     cl00460"
                     /db_xref="CDD:469777"
ORIGIN      
        1 meqrrypghn hwfyesqtsp rtsqaaplvp eaahiddrfl lgchadhagm hsllrsqqpa
       61 llaardlaql lfpdrvitsl thtltlydrl staltvaqva giqrlcnhys arlnplpgpd
      121 ssresnnrlt qitqyarqla mqpelingsa italdgvglt epdivtlnqv igfvsyqarv
      181 vaglqalqaq pvrwlpgsta ppdaeatgfd qparwqpvlk plelryasae qlaaitrcqs
      241 lpgmqeavwv lahdpaalyg waqlrqhlsd dpalpeavaa rilgsrwlfr lldgqaglie
      301 gvddagsrga eqqiialaaq ltrsperfsa ahlqplmeag wendalfalv qrvaignwns
      361 rlfyalgeaq
//
LOCUS       WP_285065040             728 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pantoea anthophila].
ACCESSION   WP_285065040
VERSION     WP_285065040.1
KEYWORDS    RefSeq.
SOURCE      Pantoea anthophila
  ORGANISM  Pantoea anthophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 728)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 728)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 728)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Pantoea anthophila"
                     /db_xref="taxon:470931"
     Protein         1..728
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=79748
     Region          49..722
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 minsiklsad frrsflrevl vplvailllt fagagaalfi gtsltnaear hqqqrmieas
       61 fsqslnehlr qlhslsrwap leqhlaasns drwldenige wlyemfghql imvldqqnqi
      121 vrvwregqpv aapdsdplaa evlqstlvtd parpdradya rvtnraaala vgniqqesrt
      181 lprfrlvslk flddgylasl aernqlqdlh ftdgtaqpgs aaryllvaqa gdpvgylewi
      241 psrpgaqmlr tigpstglav laisllclym vwrlwhslvs lsqsmlrlga seaqaqhlaf
      301 hdvltglpnr alveermtqa lalatrhdqr valllidldr fktindtygh hagdeliiav
      361 aqrlsrivra sdtvgriggd efivvmpdve nlsqaqslaq rivdelalpv tlfgsevwsg
      421 asiglslapr dgidrlelmr kadialyeak sggrgkyrqf eramdesvrt rqaiaadlrs
      481 alqsrqglev wyqplmdigg qqmvgieall rwhhptrgli apgefiaiae etglimplge
      541 wvlaeacatq qrfptllvav nvspvqfrsa gfverimaiv sqhggdpkrl eleitegvli
      601 ederearaii valreagfri alddfgtgys slnylstfpv dkikidrsft qslgvaensv
      661 aivesvvklg hamglmvtae gvetpgqmsa ladagcnqlq gylfsqavpa dqlaalmtsa
      721 apettpqa
//
LOCUS       WP_285065054             425 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Pantoea anthophila].
ACCESSION   WP_285065054
VERSION     WP_285065054.1
KEYWORDS    RefSeq.
SOURCE      Pantoea anthophila
  ORGANISM  Pantoea anthophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Pantoea anthophila"
                     /db_xref="taxon:470931"
     Protein         1..425
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47163
     Region          25..396
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mnyvesyyaa tanahepwpt lqesiqcdvc iigggftgls aalhltevgy dvvvleaari
       61 gfgasgrngg qvvnsysrdv dvieqrygke sarmlgsmmf egaaiirdri dryaidcdyr
      121 pggifaalnt rqmahlqkqk tlwqqygnhd lelldergir revateryvg glldrrgghl
      181 hplnlalgea eairrhggri yeqsaalkvv ygspnrvkta hgevsatfvi fagnaylspq
      241 leprlsrksm pcgsqivvte plspdqalsl lpnnycvedc nylldyfrlt adnrllyggg
      301 vvygarepad iealirpklr rtfpqlqnvr ldfswsgnfl ltlsrmpqfg rlennvyfmq
      361 gdsghgvtct hlsgklisev lrgdaerfda farlphlpfp ggrrfkvplt amgavwyalr
      421 drlgv
//
LOCUS       WP_285065086             403 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Facklamia hominis].
ACCESSION   WP_285065086
VERSION     WP_285065086.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..403
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44959
     Region          5..396
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mkkmnipfsp pdisqkeidy vvdalksgwi ttgpkckele qklsefcgta ktvavnssta
       61 amemtlrvlg vgpgdevits aytytasasv idhvgakivl vdtamdsfem dydqleaait
      121 ektkviipvd lggvmcdydr lyqiveakkh lfhpkkdslq ekfdrvilla dsahalgaky
      181 hgkpagsvad fttfsfhavk nfttaeggav twlpingvdd ewlykqfmll ilhgqnkdal
      241 aktkagawey dimapyfkan ltdihaaigl gqlerypsml errhevikry deickelavs
      301 plnhfkency ssghlyllri dgygeeernq liqkmaevgi acnvhykplp mmtayknlgf
      361 nigdfpnayn qyqnevtlpl htllsdeeve yitsnlvslm nnd
//
LOCUS       WP_285065150             251 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Facklamia hominis].
ACCESSION   WP_285065150
VERSION     WP_285065150.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..251
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=28967
     Region          13..250
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 mtgfkqdshr shemeinlta fqgpfdlllh likkmeidiy dipvaeitdq ylefihqssa
       61 idldqisdyl vtaatlieik srllipiedk sldmeleedp rktlvdhlll yqqfqevadd
      121 ldrrqsnral tfsrassdlt ayqlsvplee gelelgdlqe amlrllqrql dqqvpakeik
      181 ydqvsvsdki nairkkfrql vqgqslslrd lmdketrpei iacflailel vrkqelifeq
      241 ksqygpihir g
//
LOCUS       WP_285065187              68 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Facklamia hominis].
ACCESSION   WP_285065187
VERSION     WP_285065187.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 68)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..68
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7871
     Region          5..68
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mkanykklwh illdrdmkkk elaqiaevst ytinklnkne nvtvevlgki cralnctldd
       61 imefeede
//
LOCUS       WP_285065223             230 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Pantoea anthophila].
ACCESSION   WP_285065223
VERSION     WP_285065223.1
KEYWORDS    RefSeq.
SOURCE      Pantoea anthophila
  ORGANISM  Pantoea anthophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Pantoea anthophila"
                     /db_xref="taxon:470931"
     Protein         1..230
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26108
     Region          1..208
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mkmkicffdm egtllvknsy ldngkvapsa wtvlakeige scyieeektk dlwldnkyis
       61 ytqwmmetis ihikygmrkn hlaavlsqak iqegaeelik ylkkegyitv lisggfkela
      121 dltqrklkid haysaceyff deegivehfn llptdeegkl vfmthlasey nvgledcifi
      181 gdgkndvfia rnvgtsiafn aqrelievst hvvnqsepdl sriidilsle
//
LOCUS       WP_285065249             283 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD-IIB family hydrolase [Facklamia hominis].
ACCESSION   WP_285065249
VERSION     WP_285065249.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01484.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..283
                     /product="HAD-IIB family hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=32495
     Region          7..261
                     /region_name="Haloacid Dehalogenase-like Hydrolases"
                     /note="The haloacid dehalogenase (HAD) superfamily
                     includes carbon and phosphorus hydrolases such as
                     2-haloalkonoate dehalogenase, epoxide hydrolase,
                     phosphoserine phosphatase, phosphomannomutase,
                     phosphoglycolate phosphatase, P-type ATPase, among others.
                     These...; cl21460"
                     /db_xref="CDD:473868"
     Site            order(10..14,45..46,196,218..219,222..223)
                     /site_type="active"
                     /db_xref="CDD:319763"
ORIGIN      
        1 maplkliaid ldetllrrdk tyevarfnqv lkelrsqsvi vaivtgnsyd kvkdyfdasi
       61 rpflyfacdn gnylvqnevt lkkigipyer fieiidfide fkgyypalcl gdatyeresk
      121 gvgheilsqf nprvqrvdsf rdlpedslvt kiailsqddl drnkalvrii neryddvtav
      181 tsaenwvdiy ncqggkgsai rflkdryqlk aedclamgds lndesmmkev hysvamenad
      241 kdltmqcryq ignnndqavv qlmedyqqtg sldfmqkyrt iki
//
LOCUS       WP_285065259             122 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Facklamia hominis].
ACCESSION   WP_285065259
VERSION     WP_285065259.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 122)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 122)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..122
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14131
     Region          37..112
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(41..42,44,47,50..51,54..55,58,88,107..108,110..112)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(42..43,47..49,62..64,73..76,78..79,82..83,85..86,
                     92..94,99..101)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(62,65,107)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mtekltsier ceynaihedi inqvrdkmpq ekslsdlael fkvfgdltri rilwalheae
       61 mcvcdiavll nmtqsaishq lrvlkqtnlv knrkegkvvy yslvddhvre ifdqgfihts
      121 er
//
LOCUS       WP_285065316             404 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Facklamia hominis].
ACCESSION   WP_285065316
VERSION     WP_285065316.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..404
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43198
     Region          18..365
                     /region_name="FucP"
                     /note="Fucose permease [Carbohydrate transport and
                     metabolism]; COG0738"
                     /db_xref="CDD:440501"
ORIGIN      
        1 mgrgrvviks sirlkesafv asygamffeg alnviinasl iqlaqsldrs lgevaqlisa
       61 kslgtllfly lagkwsdqyg rkplvllgsl cflifllgfs wttsftglll lallggvghg
      121 lmdapsmsil fdlladkags alilvqfffs lggmfvsfvv shtvaaglsy rwiyalmlgf
      181 glvyflhval splpalrrse gsaplpqkas qilatpammt vlagiclfai yqyimltwtp
      241 hflqqtkgyq aatalrtvai yqmggalgsv afslvlrrir aaqlalmntg ltlglslall
      301 flqqaltlql clflmgaims vyfslcisig gelypqatgl vsgaiasfnv vttllaslli
      361 sflmegkmpv talflllvli lgilmgvswk mgqieqglkd sips
//
LOCUS       WP_285065373             312 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Facklamia hominis].
ACCESSION   WP_285065373
VERSION     WP_285065373.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..312
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=35978
     Region          1..293
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 miekiyiiay pmagfgkgqq vlnqvrqelq alriphltye teyaqhavsi tkqlvtqqfd
       61 pnkhrlavig gdgtlsevin tllslrlkip ityfaagtgn dfyrarfnea svpdmidkml
      121 yqrqakhipi gyyqnksqhk vgyfinsygf gfdaevihsm thynlkekld rfklshlsyf
      181 favflalkdi ktfsldvnhe gsqqhfdncg lvlmmnhpfv gggiqiapqf dphqkdfsly
      241 ifhhlnfkvi lnlvwnilfs hkpinsnnlt hlrgnqfelw spqiirseyd gelntsspih
      301 cqfkknsypf fi
//
LOCUS       WP_285065471             251 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Facklamia hominis].
ACCESSION   WP_285065471
VERSION     WP_285065471.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443800
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..251
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28364
     Region          1..70
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          136..250
                     /region_name="Peptidase_S24"
                     /note="Peptidase S24-like; pfam00717"
                     /db_xref="CDD:425835"
     Site            order(178,214)
                     /site_type="active"
                     /note="Catalytic site [active]"
                     /db_xref="CDD:119397"
ORIGIN      
        1 malgkiikdy rsrnslsmdd fakksqlska yisvlekned prtgkpispt ittikkvadg
       61 mdisfdelfs mlndedvvaf dgysvpekif diskkishdr qlkvynfaqy qlveqnrtnt
      121 leeikeepae yiteglygrl sagtgqqifd npvedvkvps aiipdepydi mlkivgdsmq
      181 pafedgeyvf ikltkeirsg qfaaiivdde aflkkvyvee dqmrlvslnk nyediivney
      241 snvevvgtvv l
//
LOCUS       WP_285065526             300 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Facklamia hominis].
ACCESSION   WP_285065526
VERSION     WP_285065526.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 300)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 300)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..300
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=34698
     Region          9..293
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mkaffktcla elclmvitll vvgfifylsp lepaygrlcl iwllfidgcy liirfwlfnh
       61 qvqlkaqldk rgqelydlks qmlrqqkdld dyfihwihqi ktpiaairlm ldsqvelskn
      121 dleqqmlaid nytrtalayl kiqnpatdlm iqpivlddli apllqryrws fiynhtrley
      181 hpikdqvitd gnwtqlmieq ilnnalkygk gtlitiryns qdqvllisdq glgipdsdlk
      241 kifdkgysgf ngqlhcessg lglylvdqis qrlhqkvtvr sepgqgtcft itfnnqltkl
//
LOCUS       WP_285065588             727 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Facklamia
            hominis].
ACCESSION   WP_285065588
VERSION     WP_285065588.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 727)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 727)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..727
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=80298
     Region          15..687
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 minsnyklkr kkkkshiprr lnilftvsfl afvalfvrlg ylqlykgqsl tqmvertdst
       61 istgsvprgm iydslgrivv gnqperaily trgrdsqvss keiltvakql aslielptqs
      121 ltevdlknyf latrrdevls rmtaeektlk gtkgyqaqld kikpedlnfs dveleiamiy
      181 nrmssayals tvpiknknvt qeeiarisen msvlpgiqlg tdwqrtypqg dmlrsilgqv
      241 steergipsd takelltrgy amndrvgmsy leeqyetvlr gtksvnnivt dsqddilkne
      301 qvypgnkgan lvltinsdfq kkldqvveen lknigpnqyl ndriyvvain pqngdilgis
      361 gkkfaydqat dsynydqiqd dvlgainssy smgssvkpam vatgyqegai sltdnvlvde
      421 pmkfqasqvk ssvfnrngqv pvdditaiqk ssniymikla mkiggqlnye kegrlninpd
      481 tiniirrhfs efglgtstgi dlpnesqgfs pksnqlvsal dlsygqfdly tplqlgqyaa
      541 tianggkrfs prlvkeirst dsngelggvl atvppkllnd inidpaamdr ihqgmyqvsh
      601 tneggasryf lnypiklgsk tgtaeafysg piqyaknnpv tnasfigfap ydkpeiavav
      661 vvpylkegil gvdvlnlakq imdiyfesqs etnqlikgqe gvdtnavsts teadsessve
      721 qtttsvq
//
LOCUS       WP_285065613             449 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Facklamia hominis].
ACCESSION   WP_285065613
VERSION     WP_285065613.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..449
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51142
     Region          4..444
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 meftrieeat dwllnqvnpi prpdmtkmyq aleymgnphl glpvlhitgt ngkgsvvayl
       61 rdlfqsqgln vgsftsphie rfnerisynh eqisdeavir wtnrlkelnt ymethseygr
      121 liyfelftil aclyfqekkp dvclieagig gmhdcsnvld gqvsvitsig ldhaemlgdt
      181 kekiayekag iikpghsavt gymeegplav idqwaqdhha kayhydkeyq vsqvkdlgph
      241 gaefifkspl clneslavki amigehqvhn aatalqafil wmqdhhleid wskalhalsq
      301 thwigrleai sedpliyldg ahnmegltal kevvshqfkd yqieliyagl rkknqhdqvp
      361 llltfevdqv nftafdhfea meladfqail eqtdkpikqt yhlvedwptw idqychdhsg
      421 sdrslllitg slyfvsqvre yilsqklng
//
LOCUS       WP_285065733             226 aa            linear   BCT 25-DEC-2024
DEFINITION  RluA family pseudouridine synthase [Facklamia hominis].
ACCESSION   WP_285065733
VERSION     WP_285065733.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426207
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..226
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=25585
     Region          5..226
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 maieilyedn hvlvvnkpvn clsqgdrsgd ldlltqlkqm ikvrdhkpgq vylglvhrld
       61 rpvggvmvfa ktskaagrla kqlqsqqfdr vywavvegdp gssgqldhyl ykdqrknqvy
      121 avdakhpkgk karltyqrla qsqgrslvqv rlhtgrshqi rvqfktaghp lwgdqkynpk
      181 aqpgqqialw ayqlqfehpt rkepvsitcr ppsssiwqdf qalisq
//
LOCUS       WP_285065807             390 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Kingella kingae].
ACCESSION   WP_285065807
VERSION     WP_285065807.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..390
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=45501
     Region          48..314
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mdirtpsger irrsldtqdk qkaqelrakl ehefwqqsrl gikpkklwde aalkwleekq
       61 hdkksieddi srlrnlpqlr gifldeltrd iimaaiepkk ckpstknryi alvrailyka
      121 rdewgwidea pklkqykeps grirwlkpne aqrlidalpd nfwrqmvifs lctglrqgnv
      181 fglkweqvdl arriawiypd eakadkaigv plnqtaiqvl serlgrhsvf vftnsvnnri
      241 keldervwer slkkaqiknf rwhdlrhtwa swlvqkgvpl lvlkemggwe klemvmryah
      301 laaehlqsha dildtlngfg hnlgtspnel qkenrlndcl dglnlaprag lepatcgltv
      361 rnrpllkiql ndfyrlfilw clhipshkvs
//
LOCUS       WP_285065844             163 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Facklamia hominis].
ACCESSION   WP_285065844
VERSION     WP_285065844.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 163)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..163
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18912
     Region          4..155
                     /region_name="NUDIX_MutT_Nudt1"
                     /note="MutT homolog-1 and similar proteins; cd18886"
                     /db_xref="CDD:467596"
ORIGIN      
        1 mqqlsticyi dngsqlllly rnkkkndihh gkwisvggkf eaeedpksca ireikeetgl
       61 eakkldllgf itfpnfthdg rdwysfvyrv keytgelidd cdegqlewvd ydqvltkptw
      121 tgdalilkwv leakgffmak fkynelgelv dyevdflyeg dqs
//
LOCUS       WP_285065919             277 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nosocomiicoccus
            ampullae].
ACCESSION   WP_285065919
VERSION     WP_285065919.1
KEYWORDS    RefSeq.
SOURCE      Nosocomiicoccus ampullae
  ORGANISM  Nosocomiicoccus ampullae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Nosocomiicoccus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Nosocomiicoccus ampullae"
                     /db_xref="taxon:489910"
     Protein         1..277
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32258
     Region          4..54
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(7,11,35)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(10,34)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(17..18,28,31,35..36)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mlnesikkrr telgisrkkl csdlcsestl yrfemglsdi nahllieick rlklgevvit
       61 dvnftekeya qflliqhyiy qrniteleki iesaeskskv wtkiitwcqa viyfykgeyk
      121 rceniiskdl siskpknsld llilntlils hlsqnsykea levattciny iethrvgste
      181 lnfkirysya hslhqngnkk eaetiileli dalihektff llgkcyffly alhkdekvql
      241 snkylkmsym tfiienspip nqvleeikkl pdsslfl
//
LOCUS       WP_285066018             384 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Nosocomiicoccus ampullae].
ACCESSION   WP_285066018
VERSION     WP_285066018.1
KEYWORDS    RefSeq.
SOURCE      Nosocomiicoccus ampullae
  ORGANISM  Nosocomiicoccus ampullae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Nosocomiicoccus.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Nosocomiicoccus ampullae"
                     /db_xref="taxon:489910"
     Protein         1..384
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44154
     Region          <216..319
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mdnyfkqgnf esfvykrlne vidtykndtd syvvfdydnt siimdiednl nvylmehlay
       61 rltpevlyet ltnpdyreel sqtfdsrfkn atgfnlaedi ykeyqwlydn yislenrsed
      121 llkkiketdh yktfraklrl fhthvnskls rrpsngwmty lfaghtidsf kelcrscike
      181 slekpfekvt yessenipgk sgvvistfks glsvpeelln lyraftnngi ttyivsaspr
      241 vyvevaaeml ghsvkvdniv amefeedngv itpvmkadsp itkgpgktea iqklimpkhn
      301 gkqpvamfgd sigdydmmqt ftetplcvif nrhmtddfkq lidlaieqyn qkdarfvlqg
      361 rdentgvlip sqssisfget epkl
//
LOCUS       WP_285066027             471 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Nosocomiicoccus ampullae].
ACCESSION   WP_285066027
VERSION     WP_285066027.1
KEYWORDS    RefSeq.
SOURCE      Nosocomiicoccus ampullae
  ORGANISM  Nosocomiicoccus ampullae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Nosocomiicoccus.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 471)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Nosocomiicoccus ampullae"
                     /db_xref="taxon:489910"
     Protein         1..471
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=53101
     Region          14..461
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mtfnennidl etiirdevnk ylnrdvsqlp atvqapkelt qkyekmevpk vgrdiyevls
       61 elnnevltyl yrpnhkrafs fipgpasrls wlgdilttan nihasnfkna tlpisiernl
      121 inylaekvgy evkpsggvfv sggsmanlta vvtardakvt ldkltqatvy ltsqthhsgr
      181 kalhvagfpa dniriidhne dftmnvthlk rtieedvkng fipalvista gttntgavdd
      241 fdaianicee yniwqhvdga ygashllstk gkalfkgier sdsvtwdahk llfqtyscam
      301 iivkdkdnli nsygekaeyl dditsdddvi dpemlgielt rparavklwl tlqvvgedef
      361 rrridygqel aeytkdyves lenfeiisqp slsilsfryy ndsftdeend hlnnlaakkl
      421 adsgygvayt ttlnnkkvfr mctihpette ddiketidrl rlyileeien l
//
LOCUS       WP_285066064             305 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Facklamia hominis].
ACCESSION   WP_285066064
VERSION     WP_285066064.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..305
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33123
     Region          1..304
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mkkiliianp gsgkgdapdy aknlekvllt nyqveleirl tekegdanhw akaakqegyd
       61 tviclggdgt vnevvsgiae lddkplfsfv plgtvndlgr vvgfsmdpde avqqfahlee
      121 tkvdiarvnd qyfinvlalg diptavletd sdqknklgff aylidgvkaf fggknknlri
      181 ydsqgrhydl dsnlilvalt ssvggmegli qgatyndgma hlyaikdsmt lssiqtlvqe
      241 kglpdeavnn dhllalrdsa friesveghs tnklksnvdg degpalplei eilkecipml
      301 iprka
//
LOCUS       WP_285066079             265 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Nosocomiicoccus ampullae].
ACCESSION   WP_285066079
VERSION     WP_285066079.1
KEYWORDS    RefSeq.
SOURCE      Nosocomiicoccus ampullae
  ORGANISM  Nosocomiicoccus ampullae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Nosocomiicoccus.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Nosocomiicoccus ampullae"
                     /db_xref="taxon:489910"
     Protein         1..265
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29647
     Region          7..263
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(29..30,32..33,36..37,74,78..79,82..83,113,117,124,
                     127..128,133,156,160..161,163..165,167..168,171..172,
                     175..176,201..202,204..206,208..210,212..213,215..216,220,
                     223..224,230,232)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(159,163,166..167,169..170,215,218..219,221..226,
                     229..231,235,237)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(180..187,203,206..207,210)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mfdsmllgry ipgdsiihrl darakliata lfmvivffan nlvtylllig fvlvilklak
       61 lgvmfvlngl kiilvllvft flmhlfltkg gpvlvdakif tielegvikg lyistrliml
      121 vvittimtlt tspisltdal eklasplkvf kvpvheiamm tsislrfipt lmdetdkiik
      181 aqssrgstfm tgpvknrika lipiviplfi safqraedma vamevrgykg degrthyrll
      241 iwhrrdtitl iilvifgvll wmlrt
//
LOCUS       WP_285066203             481 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Facklamia hominis].
ACCESSION   WP_285066203
VERSION     WP_285066203.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 481)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 481)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..481
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=54621
     Region          2..466
                     /region_name="his_kin_PieS"
                     /note="two component system sensor histidine kinase PieS;
                     NF041210"
                     /db_xref="CDD:469114"
ORIGIN      
        1 mkflwqqiiv ffvvlltals isaygishym ekhiyneren qlllygeniv nnafsrndlv
       61 iasqllasek imiqvylsdg riiyptydqr fssklsqsdl dqiangrsig lrfsqrlvnp
      121 stqeqmatvy ipleenqvag fpsgfislga pledlevqvs tmqrqifisy lvasfvgvli
      181 sivyslyqtk klkhlqkatq eiaaghyqve vntegkdefa dlardfqlma dslveyqaei
      241 krqeslrrqf mmdaahemrt plttmsglle glqydmipes qkarsleliq setkrltrlv
      301 nenldyekir srqivlkkta ikgktlfehl ktqmqtkadd kndriviqas ddliiwadyd
      361 rllqilinlv nnaiqfssds dieiigsmed egsmiqvkdh gigieaekik liwerfykvd
      421 vsrkstkfge sgiglavvqs lveahegkie veseegegtt ftiglphqns tseekesnnd
      481 d
//
LOCUS       WP_285066234             573 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Facklamia hominis].
ACCESSION   WP_285066234
VERSION     WP_285066234.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 573)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 573)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 573)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 573)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 573)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..573
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=63562
     Region          29..572
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mknqfqknek gttatlfpfl qlttkfsrlg iillififfa lpvirlmwms fsgenglsfe
       61 fyneilsdsr twevlgntli vvlgsmtiat ilgvtiawli aytnlhlkgi iqlliflpfv
      121 ipsyvsslaw vqffrskglf skivgllgin igkidlynfg giifvmgitm yplvymftvn
      181 afrqiprdae iaakasgass wtafsritvp malpgiaggm fiaflgcldn fgipaflgtp
      241 anidvlttyi yqqiigfgpt afnrasvlsm lltlialivm afqwmvtrks raletgkidl
      301 kpryilgrsg wliemllwlf littsilpli slvvaplika vgldfslenl slknyefvln
      361 npqtqsaift slklagissv vilcfasvfa yfrvrfnngf lrvieafiti pyalpgtvfa
      421 lsmifawmqp fhgwnpgiyg siwilyiayi trfmivqvrs aitafgqvde sieeaseisg
      481 srgrgkwlkv mlplilpsil sgtvlvflqa lteltvssll yssssktigv qvlsyqqagy
      541 tlnatafssv ivgliiltyl viliiqkfve rkr
//
LOCUS       WP_285066281             238 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Nosocomiicoccus ampullae].
ACCESSION   WP_285066281
VERSION     WP_285066281.1
KEYWORDS    RefSeq.
SOURCE      Nosocomiicoccus ampullae
  ORGANISM  Nosocomiicoccus ampullae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Nosocomiicoccus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 238)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Nosocomiicoccus ampullae"
                     /db_xref="taxon:489910"
     Protein         1..238
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26130
     Region          3..234
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mvitskdnkr ikeirklltk kgrtkaqqfl iegehlieea iqfgahieei fvletdtfnf
       61 dlkttvvtkd imsslsklvt ppgiiavvrm etksiesdrv laidgiqdpg nlgtlirtad
      121 afnfkrilig kntvdpysdk vlrssqgshf hvsledvdli evmqnfngti lttdlsgesl
      181 tdkitdekim ivlgnegqgv sqevlavany kvkidmpgda eslnvavagg ilmhqysl
//
LOCUS       WP_285066395             218 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Facklamia hominis].
ACCESSION   WP_285066395
VERSION     WP_285066395.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443800
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..218
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=24220
     Region          4..63
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          108..217
                     /region_name="Peptidase_S24"
                     /note="Peptidase S24-like; pfam00717"
                     /db_xref="CDD:425835"
     Site            order(146,183)
                     /site_type="active"
                     /note="Catalytic site [active]"
                     /db_xref="CDD:119397"
ORIGIN      
        1 midlksrrle lgltledvgd mvgvgkstvr kwengmidnm krdkiallah alqisplqil
       61 sddyqptnni isiynqlnkp rqnkvytfaq hqldeqnngv eessaiylvg qtaagepley
      121 gqlqpeqisv dvpkgadral nvkgdsmepl ikdgsivfyk dqptvengei aiveidgsev
      181 tckkfyfdgd kitlksinek yedmvfsngv riigkvii
//
LOCUS       WP_285066398             358 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Facklamia hominis].
ACCESSION   WP_285066398
VERSION     WP_285066398.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..358
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41975
     Region          61..355
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mwveelangk fkyceryldh ktgknkrasi tldkntpqak nyaikmlnkk iestktetkk
       61 irlgelteey iafkkkhwal stynknlgfy krhiqpypeh dfyvckltln diqciidrvq
      121 ydkglarnti iniksligsv lnygydeydi efvksfdrvf ikeelpkelp iinsdeipkl
      181 iedvrsnine lyadavevqi ltgmrigelr alteedwfdn kirinksier ktnafskpkn
      241 iqsirtidss drineiferr iklnhllfgd eanlifaskl ngpltytyfq elikrvnpel
      301 sshvfrhthv sllaekgfpl kyimervght npettmkvyt hvtekmqkea rdklnnli
//
LOCUS       WP_285066579             313 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nosocomiicoccus ampullae].
ACCESSION   WP_285066579
VERSION     WP_285066579.1
KEYWORDS    RefSeq.
SOURCE      Nosocomiicoccus ampullae
  ORGANISM  Nosocomiicoccus ampullae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Nosocomiicoccus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Nosocomiicoccus ampullae"
                     /db_xref="taxon:489910"
     Protein         1..313
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34177
     Region          33..307
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mnkqyvalas iligvilasl vigtinvfeg hfnivysirl prilfavlgg avlsicgavf
       61 qillnnrmad sftlgmanga vigaaiaiyi sasfyfiplf gvvaglislf lvlfiakqid
      121 smlrpetlvi tgvlfstlls gvlyiiimld ptktksivqf mfgsfsgsry eyitivficf
      181 iislivlfks srdldlltlg elrafslgve vsklrlklli vmaipslvll sftgiigfig
      241 iivpqmiqyi rprkakelfi lsgfygaill givdtiarti lspiqlptgv llsifsvpli
      301 lflmykrflq kti
//
LOCUS       WP_285066588             463 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Nosocomiicoccus
            ampullae].
ACCESSION   WP_285066588
VERSION     WP_285066588.1
KEYWORDS    RefSeq.
SOURCE      Nosocomiicoccus ampullae
  ORGANISM  Nosocomiicoccus ampullae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Nosocomiicoccus.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Nosocomiicoccus ampullae"
                     /db_xref="taxon:489910"
     Protein         1..463
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49162
     Region          2..445
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mldqflafvd kvngviwgpa alvflglvgi yltvgtkfvh iknffkiikq sfsglnddkd
       61 ekqdgdltsl qsmfvslssv igmgsvvgva salisggpga llwmwiaafi gmvikyseii
      121 livmfreqks dgtyvggpal yvrkglglky lgevivvlmv lvclasamiq snvtvsnmtn
      181 iaphlsnyly ilaavnvviv givivggvkr igsvaeklip fmslfyiiva tiviiihykd
      241 iipavqlvfs safspaeaga gfagygimka mqygiargff vsgagqavft vshaparvkn
      301 pveqavfgvt evflvtvvct ftalalltsg velegkdagi ivaqvfgdis pilgiavgia
      361 tilfaystvi glgyvgesql stitstkkar iyryiflvav yiggigglka iwdltdvflg
      421 lvmfvnlivm lllskkifka sndywgdegq ssgltagcsk nkk
//
LOCUS       WP_285066675             981 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Nosocomiicoccus ampullae].
ACCESSION   WP_285066675
VERSION     WP_285066675.1
KEYWORDS    RefSeq.
SOURCE      Nosocomiicoccus ampullae
  ORGANISM  Nosocomiicoccus ampullae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Nosocomiicoccus.
REFERENCE   1  (residues 1 to 981)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 981)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 981)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 981)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 981)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 981)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 981)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18767243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..981
                     /organism="Nosocomiicoccus ampullae"
                     /db_xref="taxon:489910"
     Protein         1..981
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=115838
     Region          1..960
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          1..184
                     /region_name="AAA_27"
                     /note="AAA domain; pfam13514"
                     /db_xref="CDD:433272"
ORIGIN      
        1 mkikgldiyg ygkiidksfk iehdfvqvfg eneagkstmm sfihsilfgf prrnegeprr
       61 eprlgnaygg rlivqfvdev gpvtierikg nksagdvrit madgtersed wlkrklnyid
      121 kemyrsifsf dvlglqdink nltekdlqdy llragalgsn kyedmlnain tkldelykrn
      181 gtkpdinvki dsisnmteki aelesyeety eslvsekhki iesierkrhs vnstkqqlkn
      241 kmkeimyhpe ikewqslank idvepalfpe kgieryealk nhlttgqkdk llrqekleal
      301 ireenrvvlp eedtlnyler lskeepnikh ellelerlqs evatieekih rsmndigwqe
      361 ehldvddsni vrenvqslls rhdeiemese fynnsiaqlk deiketdkkl esfsdtqisn
      421 qriraklevq dlehelkeke rvyhliedky feeekkrear nktqgtviis msvilmligl
      481 syifisnqni ygiifivvgl lsllllklnk teeeddhlkd eyeqdleklk qqikekkeah
      541 dlnfdyydar emmnevdrhm nkklsdeikl esleekrsil dstndqlkrd larvkeklyv
      601 sdelenaqiv dtiytirnik qmrrnideln trieaidsni tqfsnsvree vskygidfhi
      661 nsiffetnkl lekllkdkst yhnlreqinl feneidvidn rnyvaekemk elfnyvgadd
      721 edeyyyygrm ftefkenear fkelnnklte enfdlerrqq lsefntadlr deetalntmi
      781 enyendidee ttmlakieqd ikhlekngql svlrhqyele knsietsavd ymslmyiktl
      841 ieahikaikd krlpivveea rkifeyitke ryidvmyedn iikvkhsngq ifdpseisqs
      901 tkellyialr islikalkny ynlpiiidda fvhfdqtrtr tildyfkkqs eehqvlfftc
      961 nleksipstn tivlqdgknr r
//
LOCUS       WP_285066835             709 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Kingella kingae].
ACCESSION   WP_285066835
VERSION     WP_285066835.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20158983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..709
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=78933
     Region          <228..>344
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          293..701
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mrrflifcgi asfavlyllt fstdsdsrfa pyfwwiavaa allasmlftv ivryiwlils
       61 dknnqvfgsv iarklsgmft lvaalpaifl lgvaaqfiay sidswfgndt kealerslkl
      121 sqsalnnaaq hsmvqaasvr ahvltavmqq ndvapalntt earefahlav wnldtrqplv
      181 ernpnqftpp eldesslqki rqadthhsie sinhtlytng wlllpkhnhq qyalffrqav
      241 pqqvaqdael ieaarskyae lafaqkglqt fflvtlliaa llaillaiaa alyfarrfve
      301 pivqladgar evaqgnfqrr lhiirqdelg kltllfnhms eqlaiakqad eqhrqeqeaa
      361 rhylervlds lsagvitlds agclntynrs aetildcsls ailgqnpqdw aqqspqyhal
      421 nqaltplies enankaielt ylaqdesril lgkavrlpae ngnglvlvfd nittlvqaqk
      481 eaawgevakr laheirnplt piqlsaerla wklrdklsdl dvqtldkstn tiikqvaalk
      541 emveafrnya rapsirlkpv dlnvligevl vlyesvpctf haelsnipmw lnadttamrq
      601 vlhnlfknaa eaaesdakpq vwvstqiqne qihisvsnng ksfshemlqa afepyktdks
      661 ngtglglavv kkivedhngr itlhnraegg aclnlyfpfv anltepsek
//
LOCUS       WP_285066847             164 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase [Nosocomiicoccus ampullae].
ACCESSION   WP_285066847
VERSION     WP_285066847.1
KEYWORDS    RefSeq.
SOURCE      Nosocomiicoccus ampullae
  ORGANISM  Nosocomiicoccus ampullae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Nosocomiicoccus.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Nosocomiicoccus ampullae"
                     /db_xref="taxon:489910"
     Protein         1..164
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=18325
     Region          43..164
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mrklerfpsk kenplwrmyr tisffrvvkn fiiveagrys pstrmkhtly ktglnmklgd
       61 kvsfaykamp dlfypenitv gensiigyna tlltheylvd eyrigsvtig kntmiganvt
      121 vlpgvtigdn vlvgagsvvs kdipdnsiay gnplvirers diee
//
LOCUS       WP_285067358             475 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Pauljensenia sp. UMB6358].
ACCESSION   WP_285067358
VERSION     WP_285067358.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB6358
  ORGANISM  Pauljensenia sp. UMB6358
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Pauljensenia sp. UMB6358"
                     /db_xref="taxon:3046335"
     Protein         1..475
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49415
     Region          2..464
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 msdpaalets sgidqqgidl vpphrrhgka idlfflwagt ttniftvsyg allvilfgls
       61 fwqaiaaivv gnliayplla laslqgpktg ttnmtisrss lgprggrang lfswlmllgf
      121 eaaglvlvyy aiaallgifg vdisgvtqva givvlgliqm llpligynfl maaqkfatii
      181 facafvilav lilpkvniat gevgadinam isaislvvvs gglswacsgs nfsrylpeet
      241 splsvgtwaa lggfvpylll qslgaamatv tvgpdvdlsd plavpailpa gfsvpflllv
      301 gfglmvqngt nlyssslnlq tagipakrpv vvvtdsiici litifavaqs sfyallsafv
      361 gslsvwlapw itiylvdwvm rrgnydlagl mndkggvywg iggvklpgfv sliagmiasa
      421 lfantgyfig piaaaispqh peyapdlaip agivvsgvlf ialtitnkkk nlgia
//
LOCUS       WP_285067574             109 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Kingella kingae].
ACCESSION   WP_285067574
VERSION     WP_285067574.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 109)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..109
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12550
     Region          1..58
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mgnqfkkvlr kiridnditq aqmakvlnvs lsflssvane ksalpktmlg kllknydlad
       61 cekrvifkry vrdnfrlpen micenriddf iesvaarlld eysyqkttv
//
LOCUS       WP_285067587             444 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Kingella kingae].
ACCESSION   WP_285067587
VERSION     WP_285067587.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..444
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47439
     Region          25..439
                     /region_name="MFS_PcaK_like"
                     /note="4-hydroxybenzoate transporter PcaK and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17365"
                     /db_xref="CDD:340923"
     Site            order(35..36,39..40,43,75,125..126,128..130,133,153,
                     156..157,160,269,272..273,276..278,281,308,312,362..363,
                     367,371,387,390..391,394..395,398)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 msgnnidvre lldsrdvsay qkfivfisfl ivvmdgfdvv imgfvgpalk eawnwtnsdl
       61 apvlsaalfg ltfgaltagp lgdkfgrrkv ltasvfifgl ftllvatass ktefivyrfi
      121 agfamggimp mvatlvkeys pvkrasllvt ivfagftvga agggflaawm vphfswasvf
      181 vlggvlpiit avvmfftlpe sltflvlkgg qceeickive rcapgvttad ttftvptppn
      241 tstdvkespi qialnshyrl gsillwssyf lhlflvyllg swmptmikes gmttsqaaii
      301 samfqlggpl gsvmlgwfmd kfephrvits ayvlgaimlv vmsnigggyl lmcivafvig
      361 agfngggtam nalssnffpl paratgnswm hgigrtgaii safagawmln agwnfstval
      421 altvpavfig illtvkflry rtls
//
LOCUS       WP_285067656             446 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Pauljensenia sp.
            UMB6358].
ACCESSION   WP_285067656
VERSION     WP_285067656.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB6358
  ORGANISM  Pauljensenia sp. UMB6358
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Pauljensenia sp. UMB6358"
                     /db_xref="taxon:3046335"
     Protein         1..446
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47242
     Region          53..442
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mtiwivvgil tlafvlfggl wlwrwyqtrq arlqlrkdam ltpssafdpe rgrprpwviv
       61 npvkhddvda fkaevnqaah qmgidhvhwr ettaedpgtg qaidalaqga sviiasggdg
      121 tvravaagva gsgvrmgiip agtgnilarn lgipiddsaq amrialgenh raldcgwlrv
      181 dnvdtpseip aegmlvraal tknrvdtdtp psldqadssl ahraqnlpgt deysfvviag
      241 lgfdgetmaa tdselkkkvg wvayviaalg aiakegtrlr lmlrnpkpid dpvgdapgdd
      301 ehsrvvdesa tisgvsvpdq pesvltwvhs rtvmfancge lpfitlapga rvddglidvi
      361 avnteagvlg wadlslkimg qglgvktmnl pvstgkiqfr qaegasvaaq spqviqvdgd
      421 aigtartvhv rldpqaldia vpglen
//
LOCUS       WP_285068198             295 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Kingella kingae].
ACCESSION   WP_285068198
VERSION     WP_285068198.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..295
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=31674
     Region          68..293
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mqlstkkill ssalclmlsa cggesqtaap aapadtkpta aassvpaten knlvddyvsp
       61 lpanapvinv attsktlpfs fsatnggvvg mdadvirkig eaegfkvqfh krnwqtlftd
      121 vdegtydlai sgisysddra aryalsdsya tnasvmmfkd ealvsklktl gdtaglrvgt
      181 ldgskhatqi keagvakeil pykttfllfg glmknevdvi lqdrlllqqy vknnpneklh
      241 ivayeadnlp eaqlvmvmkk gntelqarvn kglatikqng eldkirdkwl gtnsk
//
LOCUS       WP_285067864             277 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Pauljensenia sp. UMB6358].
ACCESSION   WP_285067864
VERSION     WP_285067864.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB6358
  ORGANISM  Pauljensenia sp. UMB6358
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Pauljensenia sp. UMB6358"
                     /db_xref="taxon:3046335"
     Protein         1..277
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28557
     Region          4..273
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mlanphaerv kkvaalagrs arrktnlllv egpqavrell afsgqhvrdv yftdgaaslh
       61 pdvhalassv trwchmvtde vasamssdaq giiavatrda vvstlrdtap rqtyvvlaqg
      121 rdpgnvgtii rtadamgcag vivvagtvnv aspkvirssa gsvfhlplvg vpsfdeaarl
      181 lktrgarllg tsggvgtedl gqlmtqaiag gagplassha wvfgneakgm sqaeldacdt
      241 lvridmtgqa eslnvasaas mclfasqcar lsnealk
//
LOCUS       WP_285068209             709 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Kingella kingae].
ACCESSION   WP_285068209
VERSION     WP_285068209.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20158983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..709
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=78963
     Region          <228..>344
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          293..701
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mrrflifcgi asfavlyllt fstdsdsrfa pyfwwiavaa allasmlftv ivryiwlils
       61 dknnqvfgsv iarklsgmft lvaalpaifl lsvaaqfiay sidswfgndt kealerslkl
      121 sqsalnnaaq hsmvqaasvr ahvltavmqq ndvapalntt earefahlav wnldtrqplv
      181 ernpnqftpp eldesslqki rqadthhsie sinhtlytng wlllpkhnhq qyalffrqav
      241 pqqvaqdael ieaarskyae lafaqkglqt fflvtlliaa llaillaiaa alyfarrfve
      301 pivqladgar evaqgnfqrr lhiirqdelg kltllfnhms eqlaiakqad eqhrqeqeaa
      361 rhylervlds lsagvitlds agclntynrs aetildcsls ailgqnpqdw aqqspqyhal
      421 nqaltplies enankaielt ylaqdesril lgkavrlpae ngnglvlvfd nittlvqaqk
      481 eaawgevakr laheirnplt piqlsaerla wklrdklsdp dvqtldkstn tiikqvaalk
      541 emveafrnya rapsirlkpv dlnvligevl vlyesvpctf haelsnipmw lnadttamrq
      601 vlhnlfknaa eaaesdakpq vwvstqiqne qihisvsnng ksfshemlqa afepyktdks
      661 ngtglglavv kkivedhngr itlhnraegg aclnlyfpfv anltelsek
//
LOCUS       WP_285068233             279 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Kingella kingae].
ACCESSION   WP_285068233
VERSION     WP_285068233.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..279
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=30308
     Region          58..278
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mnkllktkli vmtmtmtmtm tmtmalaacs gketappapa papaasapta aaksasvvkv
       61 gvsaeyrpya faennnaqgl eidilqkiad kqgftvefvp tlwnvaykev qdkkidivam
      121 gtaqdeadan ivvptdsymr sgdclvhike ttlpdwtkgk igvlndegme eelmsannvk
      181 esqimkeqtn flilsslvkk stdvavgdct alkfyakspt lkdysfdiae yvhssqqeas
      241 msmvlmvskd kpellqkint glaelkksge lnqiiqkym
//
LOCUS       WP_285068364             901 aa            linear   BCT 25-DEC-2024
DEFINITION  sialidase family protein [Gardnerella vaginalis].
ACCESSION   WP_285068364
VERSION     WP_285068364.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 901)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 901)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 901)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 901)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 901)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 901)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 901)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468221
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..901
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..901
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=98760
     Region          363..849
                     /region_name="NanH"
                     /note="Neuraminidase (sialidase) NanH, contains C-terminal
                     autotransporter domain [Carbohydrate transport and
                     metabolism, Cell wall/membrane/envelope biogenesis];
                     COG4409"
                     /db_xref="CDD:443531"
ORIGIN      
        1 merrstktts liediayieg skqtrfshat ikitpssena sclnrkdkne eknqnegiig
       61 fkfvansdcd lldikpaqks easaqqehtt piikisiked apllsaqnll edsadangak
      121 eialhmedav nisngrehdf aitygsfgsr fyldgyqcfa satnlgpqrv stkeaeasts
      181 lekssriydf yysshlpnpe eiansatqaq pdiwfagpti cardikrvsc kssgtlhiqf
      241 rlrgpgqhgv lfaagtvgak tnlessekis vyagpegiki tlidsetcvk svieaaasvd
      301 dgewhdliir anrgatdiyv dgyseshnig qfwfanipel davsigedlr gvrlmgeart
      361 ggiyfsalte gqiqriskik plvttalfdt gyagsrsyri pslvktrmgt liagadqrts
      421 vsndapnhin fvirrsadgg ktwgplqtvi dmpgknlgkl gasaidscpv ldpegkseri
      481 nvlidinpgg igltncktav gvdacgrikl idrlggnyaa amdasaavkl pcdssekeca
      541 tkwlvfpdgs ikncdshndl rnnshsnqtc dsstwniwks qeiasesqpl faektcyiaq
      601 iysdddgktw saprlidhmv kepwmsfagv cpgngivirq sekhygrilv pfycsgqsks
      661 hyssgalisd ddgktwsrgk minegrling kivdpitmqd ddatssetvf verkngdila
      721 ffrnqnrsgc vgkaishdcg etwselifdt slpeifsqps atcfnsenae nadciafana
      781 sqmmpyrgrg vvrfsydggk twaknvcinp fhhvyqclss snkrtlqllw erettgiyit
      841 aidsnlwkqd nlqidfksna kslnntdldc iknkintsek mkdleegslt rtersqhgrd
      901 i
//
LOCUS       WP_285068665             467 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Kingella
            kingae].
ACCESSION   WP_285068665
VERSION     WP_285068665.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..467
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51568
     Region          14..435
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 maesantssn sqryltlwrw hfytgiliap flmllaatgl amilfahtsg rdgeritvpv
       61 lqtvkplseq aqtaldtvdk dsgvvvqyia praadmvavf rvnngegkat mvaidpytaq
      121 vvktyprnqd wyhlmdeihg dillgktgdy lletaaaltv lmilsgwylw wcsrqrsvpk
      181 mlgigklgqg rsvwrglhgv fgsyisvmll lfclsgmawa giwggkvvqa wsaqfpagkw
      241 gvepipksal lhgelndgkt keipwvlelt pmpvsgttlg kdgiapdvpm tletvdrfar
      301 esgfvgryql yfpkgetgvw tlnqdsmsyd spsptadrtm hidkysgkvl adikfddypw
      361 fgqfmaasia fhmgtmgwws valnvvfcll vifmcvsgyi mwwkrrptga alcppaqgrd
      421 lptwktaaiv llivaaifpt alvaiavial ldwllisrvg alkkwfk
//
LOCUS       WP_285068719             280 aa            linear   BCT 25-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Kingella kingae].
ACCESSION   WP_285068719
VERSION     WP_285068719.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Bagautdinov,B. and Kunishima,N.
  TITLE     Crystal structures of shikimate dehydrogenase AroE from Thermus
            thermophilus HB8 and its cofactor and substrate complexes: insights
            into the enzymatic mechanism
  JOURNAL   J Mol Biol 373 (2), 424-438 (2007)
   PUBMED   17825835
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..280
                     /product="shikimate dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30019
     Region          4..276
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 mlingrteii ahigypthtf tspmiynpyf adaginalvv pmgskaedya eflpavfkls
       61 niigalvtmp hkvttaqmlg vdritqtaqi agavnavrlg kdgklegdlf dgegfvrgik
      121 nkgfepkgks amvvgnggvg saiaaslaaa giarlalfdv neessrklga rlqehypnlq
      181 leyasndptg fdllvnatpm dmkegdpmpv dldkvssqtf vgdvvlksep taflqacqak
      241 gctiqvgvdm lfeqipvyle yfnlptttaq rlreladiry
//
LOCUS       WP_285069532             484 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: peptidoglycan D,D-transpeptidase FtsI family protein
            [unclassified Pauljensenia].
ACCESSION   WP_285069532
VERSION     WP_285069532.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pauljensenia
  ORGANISM  unclassified Pauljensenia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 484)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="unclassified Pauljensenia"
                     /db_xref="taxon:2908895"
     Protein         1..484
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=49922
     Region          <73..481
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mnhqirrlsi vifamfallg laatnnqflq apslnadgrn ertilhaaet drgpiivags
       61 aiasstkieg shrfqrsysq gplyasvtgy fssafsqatg lesaaestld gqsqallgqr
      121 lhnlftgasr qggglvltld ptlqqiaadq lgnrkgavva lnaktgaila mysspsydpn
      181 slaafdseav sdaykalted pneplsnrai agnryepgst fkiltsiali engvaspstn
      241 vespvstvlp gtqttvsnie sstcgdgnpt laeafarscn tsfilaaqsl shnqladvas
      301 rfgfgasqsi plavtpsvfp ettdaaqlam saigqysvqv tplemaeiaq tianggqmmt
      361 pylvsqvvda dlavqsetnp tvlrtpisad iatqltemmk gvvnqpygtg tsmaidgisv
      421 aaktgtaetg tnghanawav gfapaddpqi afavlvegdd tdpaphggtv agpiaralle
      481 agiq
//
LOCUS       WP_285069733             922 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Pauljensenia sp. UMB1177].
ACCESSION   WP_285069733
VERSION     WP_285069733.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB1177
  ORGANISM  Pauljensenia sp. UMB1177
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 922)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 922)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Pauljensenia sp. UMB1177"
                     /db_xref="taxon:3046323"
     Protein         1..922
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=101807
     Region          28..920
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mspkrrrqas kasgepqpve qlspaqrmqa fkkdqhiqrt mryawcetld fqaddfqiea
       61 mdaleagqsv lvaaptgagk tvvgefatyl alqkgkrsfy ttpikalsnq kfsdlrrrfg
      121 edtvglltgd tsinshapiv vmttevlrnm iyagadlsdl dsvvldevhy ladrfrgpvw
      181 eeviihlpae qkivalsatv snaeefgtwi ghvrggcrvv vsehrpvply qhmlvgrhly
      241 dlyspskkge strinpelrs aigpsnpgrm grggrnwhet arvrppresr pstlieldra
      301 gllptitfvf sragcedavt qvvragiwlt nkeeqkqiat avdevktqvg aqdchvlgin
      361 awgealergi aahhagllpi qketveklft rglikmvyat etlalginmp arsvvieslr
      421 kwngaahvql tpgeytqlsg ragrrgidte ghaivlhrgq vtpeevnala skrtyplisa
      481 ftptynmvvn llhhssraat rdvletsfaq fqadggvvel aqharalarq rakfeqdmec
      541 drgdareyfa lrddlvlaqk sesklraaek rsanrvalat cqpgtiiryg sgrrslyavv
      601 afhsdtaigh vsttligtdg kfhslsakdv sssfavvgsm kiaggsavrr nkermkiade
      661 lkrrirvksi eipldtpdfd atksaqiekq lkahpvhqcp erehharagh qwarinrelr
      721 tvneridsrt hsvahkfdrv cqvleelgfl dgdtvtdqge rlrhifgerd iivmeclrsg
      781 awsglddael aaivstcvfe srredgarpa lpvglsknlt ralkatfqas akvaevekra
      841 glepttepds gmmeaclawa hgaslgtsld geemlggdfv rwirqvmdll dqlrhdtdea
      901 masqakrarh qlvhgvvaws vl
//
LOCUS       WP_285069820              81 aa            linear   BCT 25-DEC-2024
DEFINITION  pyrroline-5-carboxylate reductase family protein, partial
            [Pauljensenia sp. UMB1177].
ACCESSION   WP_285069820
VERSION     WP_285069820.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB1177
  ORGANISM  Pauljensenia sp. UMB1177
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Pauljensenia sp. UMB1177"
                     /db_xref="taxon:3046323"
     Protein         <1..>81
                     /product="pyrroline-5-carboxylate reductase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004735 - pyrroline-5-carboxylate
                     reductase activity [Evidence IEA]"
                     /GO_process="GO:0055129 - L-proline biosynthetic process
                     [Evidence IEA]"
     Region          <1..80
                     /region_name="ProC"
                     /note="Pyrroline-5-carboxylate reductase [Amino acid
                     transport and metabolism]; COG0345"
                     /db_xref="CDD:440114"
ORIGIN      
        1 sgssptivym lieamadagc qqglqrsqaq slaaqtvlga aamvvetgqh pgqlkdavcs
       61 pagtsiecvr kaedkglrsa a
//
LOCUS       WP_285069832             617 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Neisseria
            subflava].
ACCESSION   WP_285069832
VERSION     WP_285069832.1
KEYWORDS    RefSeq.
SOURCE      Neisseria subflava
  ORGANISM  Neisseria subflava
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Neisseria subflava"
                     /db_xref="taxon:28449"
     Protein         1..617
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=67901
     Region          <43..295
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          208..616
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mrykplilal llsfslptha akdapkekaa avkkaapvkk ekeatkadvk ketskkqavk
       61 ekeedkkavk akaskeketa dknerasakn ktaktaeaaa dnkkanrkae epketakdkk
      121 avaaksgkak eqdkkpvedk kdskakepak kvaedkkdgk ktkepvkkva edkkaeakep
      181 akkavddkkd tkakehnkka epkvepkats saendfkaav taaandmetk ksfakrnegf
      241 iihvnatlkq lqqtrnnlsg inrkqrdawe kfqklnadan qlkaevsnth aqisrfvsgn
      301 yknsqpnava lflknadagq ktrflrytry innandqvmr dlekqqkela aqeqkinnel
      361 aylkklqani qaslrqqgvt ntaeqaesrr qnaqmakeaq kkinhreneq rlnnllkdle
      421 krkaeqrkae aearkkaaea rlaaaekark eqaaaqqkae aeraamstlt dedmklqapn
      481 tqgftvsnsn sfsrmqgrlk kpvngtlagl fgqdrgdgev wkgvfyntvp apvssiasgt
      541 vtfagelegy gkvvvldhgd gyvsiysgln eidtaqnyav nagskigtsg tlpsgetgly
      601 levryngqvm nplswin
//
LOCUS       WP_285069858             199 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: Maf family protein [Neisseria].
ACCESSION   WP_285069858
VERSION     WP_285069858.1
KEYWORDS    RefSeq.
SOURCE      Neisseria
  ORGANISM  Neisseria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Neisseria"
                     /db_xref="taxon:482"
     Protein         1..199
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=21439
     Region          4..196
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mnaiylasgs prrreilenl gftvrrlpad idetpkegea aveyvrrmac eknqaavaqw
       61 faahdqepef avltadttva dgeailgkpe sdadaldmle rlsgrthqvl tavcvywqgv
      121 rhdvvqtsev rfktltaeei aayvasgepm dkagaygiqg lggvfvehlq gsftgvmglp
      181 vyetaqllks lgleappfa
//
LOCUS       WP_285069910             720 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Neisseria subflava].
ACCESSION   WP_285069910
VERSION     WP_285069910.1
KEYWORDS    RefSeq.
SOURCE      Neisseria subflava
  ORGANISM  Neisseria subflava
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 720)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 720)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 720)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 720)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..720
                     /organism="Neisseria subflava"
                     /db_xref="taxon:28449"
     Protein         1..720
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76141
     Region          3..717
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mqqkvrfqie gmtcqacasr iekvlnkkdf vesagvnfas eeaqvvfdds ktsaadiaki
       61 iektgygake ktedtlpqpe aehhigwrlw lllainipfl igmagmmigr hdwmippvwq
      121 fvlasvvqlw laipfyksaw asikgglanm dvlvtigtvs iylysvymlf fsphaahgma
      181 hvyfevgvmv igfvslgkfl ehrtkkssln slglllkltp tqvnvqrdge wkqlpidqvq
      241 igdliranhg eriaadgiie sgsgwadesh ltgesnpeek kaggkvlaga litegsvvyr
      301 atqlgsqtll gdmmnalsea qgskapiarv adkaaavfvp tvvgialltf ivtwlikgdw
      361 tvalmhavav lviacpcalg latpaaimvg mgkavkhgiw fkdaaameea ahvdavvldk
      421 tgtltegrpq vaavycvpds gfdegalyci aaaveqnaah plaraivsaa qergleipaa
      481 qnaqtvvgag itaevegvgl vkagkaefae ltlpkfsdgv wdiasivavs vdnkpiggfa
      541 ladalkadta eaigrlkkhn idvyimsgdn qgtveyvakq lgiahafgnm sprdkaaevq
      601 rlkaagktva mvgdgindap alaaanvsfa mkggadvaeh tasatlmqhs vnqladallv
      661 sqatlknikq nlffaffyni lgiplaalgf lnpviagaam aassvsvlsn alrlkrvnie
//
LOCUS       WP_285069912             188 aa            linear   BCT 25-DEC-2024
DEFINITION  SGNH/GDSL hydrolase family protein [Neisseria subflava].
ACCESSION   WP_285069912
VERSION     WP_285069912.1
KEYWORDS    RefSeq.
SOURCE      Neisseria subflava
  ORGANISM  Neisseria subflava
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Neisseria subflava"
                     /db_xref="taxon:28449"
     Protein         1..188
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=21031
     Region          1..183
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 mtvyligdsv rlasdpytra alpeedivsp sencrsshdv lehigqwteg atvgdiihin
       61 cglhdirynq gcnepvadie tyrsnltrif dylkqtgaki iwasstpfle svhnivkpsr
      121 ryladlkayn rvaedlarqy gfavndlysl mfeqdltdvm lcdglhfnef gskiigkava
      181 eailkqmd
//
LOCUS       WP_285070026             842 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Gardnerella vaginalis].
ACCESSION   WP_285070026
VERSION     WP_285070026.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 842)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 842)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..842
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..842
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=93548
     Region          14..834
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 madlgelald lhhasedeif qafvdwvkdn khvdlwphqe esvmdllagd hvilntptgs
       61 gkslvalgmh faalatgrrs yytapikalv sekffdlvai fgrdnvgmit gdshinadap
      121 iicctaeila nqalregana evdcvamdef hyygdpergw awqvplltlp ntqfllmsat
      181 lgdvtdiaer lekstkrsvd iianaprpip leyeytdkpl attvellfnk gltpiyvvhf
      241 sqdaaletaq alastgvssk eqrekiaqai kgtkfttgfg kilqrllrtg vgvhhagmlp
      301 ryrrlveqla qqgllpvicg tdtlgvginv pihsvvltal tkfdgnrsrk lrarefhqia
      361 gragrmgfdt eglvvaeape feienarava kagndpkklk kvkrkkapeg fvvwgeptft
      421 kliesapetl nphmvithsm ilnevtqggd ararveklie dsaqkpqdke kllercndif
      481 qtlldtqvie crelsdgscd ydldvampeg faldqplspf llaalelldp espsyaldvi
      541 smveatlddp kpvlraqerk ardaamagmk ddgidyeerm erlvevsypk pledllepaf
      601 aqyrkdvpwa ndywikpksv lrdmvetasd ftgyisrygi arsegtllry lsdayrslar
      661 tvpedmlnee lcdiiswlrl vvrsidsslv dewesaggsd aeasavtmaa pgtsesvved
      721 rrglivlirn amfrrvqlmd ledadtlgel dkawgygvhe wndvlddyyd eheyvgidak
      781 arsgdlfild dsleksehsw kvrqiiddsd gdhnwaitgv vdldstqdtg evvffdyrvs
      841 hv
//
LOCUS       WP_285069996             647 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-N-acetylhexosaminidase [Gardnerella vaginalis].
ACCESSION   WP_285069996
VERSION     WP_285069996.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 647)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 647)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 647)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261889
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..647
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.52"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=74199
     Region          7..136
                     /region_name="Glyco_hydro_20b"
                     /note="Glycosyl hydrolase family 20, domain 2; cl03741"
                     /db_xref="CDD:446174"
     Region          142..448
                     /region_name="GH20_GcnA-like"
                     /note="Glycosyl hydrolase family 20 (GH20) catalytic
                     domain of N-acetyl-beta-D-glucosaminidase (GcnA, also
                     known as BhsA) and related proteins. GcnA is an
                     exoglucosidase which cleaves N-acetyl-beta-D-galactosamine
                     (NAG) and N-acetyl-beta-D-galactosamine...; cd06565"
                     /db_xref="CDD:119335"
     Site            order(151,226,293..294,337,360,424,426)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:119335"
ORIGIN      
        1 mkidnsntei ipspqnisiy akdtitlpqs shisfinikp dlrittaakq lcedlknnhn
       61 cnwsisyseg yksaisatin knlriqeyki sskistnqtl vnieagsias icfaiqtirq
      121 limqyglilp slqiqdfpei pvraysydvs rgrvpklswl ktlvdqlsly kynqlqlyve
      181 hvidlddtie swighspltc seiidldeyc yargielvpt latfghmyei lrsnsykqlg
      241 efpeqserpf sfvermmhht lnptnpntip fiskrikdya slfksnkfni gadetfdlgc
      301 gesknvaeki gvanlylsyi krlceklhel dlqpimyadi aikhpellad ipknvifanw
      361 dysanvnenn ikliksqnrd qyvcpgtqsw nrlipdfdsa isnisktcey ghknhvlgfl
      421 ltdwgdyghi ndpilslpyv iisseyawks nniakkdlin kvsnvfanrt nsnllniikq
      481 ashaqafsws davqfkeley nnenianedv lfslgypknt sleqarrrfl nereaqilna
      541 keynrtlsec sksiydinac senincenin kdfistsiln iqgqqllnql glyilnqrft
      601 laeaksfktn lnewftqyqn rwesigktad lyrirevldw yikilgm
//
LOCUS       WP_285070065             544 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Gardnerella vaginalis].
ACCESSION   WP_285070065
VERSION     WP_285070065.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 544)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 544)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..544
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62458
     Region          2..449
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mikkviikgy rkfkdfkfep eggmnivvgd nesgkstlfe aiimaltgri dgvraseain
       61 pymfnkdnve nffknkelkn lpeflievyl nagdgdiqrl rgannslhed svglsihayf
      121 dldyekeikd yfeqhdcpni ipteyyrvdw idfsgrsifk kpkdlgvmli dssniisnky
      181 anyntrniin shidakdnnk itseyrsrcs nlaaqqisei nekleeyyke ekewtiglqp
      241 dqsnssswwn iftpcvdnip lnfigqgyqa csktvltfsq ksdksnyifm eepenhlsys
      301 tlrkllyfie dnysekqifi sthssyvlnr mgldkislin ngkiskfsnl nldtveyfkk
      361 lsgfntlril lskkaviveg psdeivfnkf fkntygkepl dcgidviain gvafrrclel
      421 adilskdivv lrdndnknpe ewkeklcknm hndyknkifi gevndgntle tqivtansnn
      481 ketlkrilny sesddndnia efminnktds alliaesdek lnqpayikna irslkeianq
      541 snnk
//
LOCUS       WP_285070329             385 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Neisseria subflava].
ACCESSION   WP_285070329
VERSION     WP_285070329.1
KEYWORDS    RefSeq.
SOURCE      Neisseria subflava
  ORGANISM  Neisseria subflava
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Neisseria subflava"
                     /db_xref="taxon:28449"
     Protein         1..385
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=42055
     Region          1..382
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mkfstkaihs sydcdehnra lmppiyqnsm falheigenv pyrysrlsnp trqvledtva
       61 dlehgaagfa fssgmagida vwrtflrpgd tivavtdiyg gaydllvdvy qkwgvnvvfa
      121 dlgnpdnlda llkahnvklv wletpsnpll rlvdikalaa kakaagalvg idntfatpyl
      181 qqpldmgcdf vfhsatkylc ghsdvlmgvv vaktkelaqp lhdmmvhtga iagpmdcwlv
      241 lrgiktlalr mnahcqnale iarrleahpa iekvfypglp shehyelaqa qmpkgiggvv
      301 tvylkndtre aansviknmk lvkmasslgg veslvnhcys qshsgvphdv kmemgikvgl
      361 lrfsvgiedv ddiwndiska ldttl
//
LOCUS       WP_285070473             237 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Gardnerella vaginalis].
ACCESSION   WP_285070473
VERSION     WP_285070473.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..237
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25446
     Region          15..198
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mainttaaqn ttnhklsavf wdmdgtlids epywhdaeiq iakehggews eelawqysgg
       61 slkdvaeami argtkmgvee ignamvdyva qkeqievpwv pdvlnllqkl adagipsilv
      121 snsprrlven ivnhapkgaf agyicgddgy atkpspepyl aagkllgisa qnmkyciaie
      181 dsfaglksaa asgattlaqt aysnldvsng pqfadihgye dvtpqtlery iiariaq
//
LOCUS       WP_285070593             293 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Neisseria subflava].
ACCESSION   WP_285070593
VERSION     WP_285070593.1
KEYWORDS    RefSeq.
SOURCE      Neisseria subflava
  ORGANISM  Neisseria subflava
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Neisseria subflava"
                     /db_xref="taxon:28449"
     Protein         1..293
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31798
     Region          2..277
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(26,238,241)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(172,209,236,239..240,243)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mkvtsfgevl wddfpngkvl ggaplnvavr lqslgidaai isrrgddadg eelllqiqsk
       61 nvntdylqvc hecatslvkv hldksgsasy eivypcawdr iavddaaikr vgesdafvfg
      121 slatrdevsr kslavllkea kfkifdvnlr kphydidrll etmkqsdmvk lnddelyela
      181 aaygspyhsi eqnisylvel tgvkilcvtl gshgavlykd gelyrhcgfr vkvvdtvgsg
      241 dsflggltyk llnnappqea iafacalgal vashhgatad islekieafm npa
//
LOCUS       WP_285070785             130 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein, partial [Kingella
            kingae].
ACCESSION   WP_285070785
VERSION     WP_285070785.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         <1..130
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
     Region          <12..130
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 vgsemcirds nlpmptsghv agsygstrat ggtwnglfie tassgvqsva agtvayaanl
       61 rgfgntviid hgdgymstya glsqiavsng srvgarqnig tsgtlpageq glyfelryrg
      121 rainprswvr
//
LOCUS       WP_285070781             313 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein, partial [Kingella
            kingae].
ACCESSION   WP_285070781
VERSION     WP_285070781.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..>313
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
     Region          10..>256
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mkitawigav fllmgtvvqa atdtapeass sklqnirqai datqkdlavk qeahrkaqqt
       61 laqakaalaa aqreliamnr rrevawqrlq klqgdlsklq aeianskaqi arllvanyrn
      121 rqphavalfl knadsnqksr fltytrlinq sndqviqkla vqekelavqe kavndqvakl
      181 qalvneqqqk mqqlgqtrsq aqatsqklnq emassrsrla qlredeqrln svvagimsrq
      241 saqrraeaea rtqaarqrve qaakaqnels eaelaavppv ikpepkpepk pvesnvgnrq
      301 gnlpmptsgh vag
//
LOCUS       WP_285070897             613 aa            linear   BCT 25-DEC-2024
DEFINITION  autotransporter assembly complex protein TamA [Neisseria subflava].
ACCESSION   WP_285070897
VERSION     WP_285070897.1
KEYWORDS    RefSeq.
SOURCE      Neisseria subflava
  ORGANISM  Neisseria subflava
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Neisseria subflava"
                     /db_xref="taxon:28449"
     Protein         1..613
                     /product="autotransporter assembly complex protein TamA"
                     /GO_component="GO:0097347 - TAM protein secretion complex
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=68491
     Region          59..613
                     /region_name="TamA"
                     /note="Outer membrane translocation and assembly module
                     TamA [Cell wall/membrane/envelope biogenesis]; COG0729"
                     /db_xref="CDD:440493"
ORIGIN      
        1 mtkltypvlf aslalaygha lavdtsvpka edyeavpese mpkqpkddqt gklkpkfpvk
       61 idtqdsevke mleeylplit qqqdeeldke qvgflaeeap dnvktmlrtk gyfnsnvsiq
      121 dhgesytvnv tpgprtkvdn vsvailgdvl nddnlaeyyq namenwqqpv genfdqdgws
      181 asktsvlsav trkkyplakl tttqatinpn tqkadlnviv esnrpiyfge fqitgtrryp
      241 esvvsgmarf qpgspydldk ildlqqaleq nghysgasvq adfdqlqgdr vpvkinvtev
      301 krhkletgir ydseygiggr iaydyynlfn kgyigsivwd mdkyettlaa gisqprnnrg
      361 nywtsnvsyn rsttqnlekr altsgiwyvr drnnidarfg lefitedrkv pdtsydlgrs
      421 hatmltaswk rqsietelhp qngyyldgki gttlgkflss tqmaratara gyfftpenkk
      481 lgtfivrgqa gyvyahegee vpsslmfrtg gatsvrgyel dsiglagpng svlpqralvv
      541 gsleyqfpvt ksfsgaifhd vgdaasnfkh mtlkhgtglg vrwfspvapf sfdiaygyhd
      601 kkirwhislg trf
//
LOCUS       WP_285071077             173 aa            linear   BCT 25-DEC-2024
DEFINITION  rhodanese-like domain-containing protein [Neisseria subflava].
ACCESSION   WP_285071077
VERSION     WP_285071077.1
KEYWORDS    RefSeq.
SOURCE      Neisseria subflava
  ORGANISM  Neisseria subflava
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Neisseria subflava"
                     /db_xref="taxon:28449"
     Protein         1..173
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=18308
     Region          5..109
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
     Region          116..166
                     /region_name="DUF2892"
                     /note="Protein of unknown function (DUF2892); pfam11127"
                     /db_xref="CDD:463227"
ORIGIN      
        1 mstvgqlpri tpseamakir dgalavdirs qaeyrgghig galslppkqh rdklpddiap
       61 clifyclsgk rtagaetils vlgqgrecyi legglqawka aglpivadra tpdimrqvqt
      121 iagslillgv lagwlvspwf ylidvmvgag lltagltgfc gmarllakmp wnh
//
LOCUS       WP_285071110             235 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Neisseria
            subflava].
ACCESSION   WP_285071110
VERSION     WP_285071110.1
KEYWORDS    RefSeq.
SOURCE      Neisseria subflava
  ORGANISM  Neisseria subflava
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Neisseria subflava"
                     /db_xref="taxon:28449"
     Protein         1..235
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26743
     Region          4..217
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mknflkkqla wltdqalcls vsfltgvrpk spreltfnqh qkvyyanhgs hgdfvlvwis
       61 lprrwrlstr pvagsdywla sklkrfiiqn vfnalliprh sdnpqaiteq mrdalnagds
      121 liifpegtrn tddntillpf ksgiyhlaks kpntefvpiw idnisrvlpk gkilpipllc
      181 evhigqpltl qenedkdsfl trsreallal rpsendrnel rqnepevqqn kggqa
//
LOCUS       WP_285071181             409 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Neisseria subflava].
ACCESSION   WP_285071181
VERSION     WP_285071181.1
KEYWORDS    RefSeq.
SOURCE      Neisseria subflava
  ORGANISM  Neisseria subflava
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Neisseria subflava"
                     /db_xref="taxon:28449"
     Protein         1..409
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=46386
     Site            order(15..16,18,42,45..46,49..50,52..53,76,79..80,83..84,
                     87)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          <17..>93
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          40..70
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msnekiqqkf eqayhsfiee enyeealkra eilclltpqs aefhhkvaya ylkqlkweka
       61 ieaemktlel dstyipaldl lahaygaldn wektgfyghq alvlkdkaip dleheiiptp
      121 apkngkriis fslfgnnsky iepavlntql apvlfpgwtc rfyvddsvsa eaiqrfrnng
      181 aevikvgtpl dnwpgtmwrf laindpevey vifrdadsii cyrdaaavse wiksgtlfht
      241 irdsgshtal ilagmwgaka gavpdmqeri qnfvdegyps rhfadqdfle kelwayirqn
      301 lfahdrlfdf cnaheipgef ysnyqiafse gvtsfnattd yedgslarwt lyssasplvn
      361 pdyslnvvpe fkvcsyvtev kngvvsaflp krygnaikak larinieqi
//
LOCUS       WP_285071205              48 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Kingella kingae].
ACCESSION   WP_285071205
VERSION     WP_285071205.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 48)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 48)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 48)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..48
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..48
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=5289
     Region          <1..45
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mstngyakie rgvrrldipk leqiaevfgm dllalinfda ervvnlis
//
LOCUS       WP_285071234             542 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Neisseria subflava].
ACCESSION   WP_285071234
VERSION     WP_285071234.1
KEYWORDS    RefSeq.
SOURCE      Neisseria subflava
  ORGANISM  Neisseria subflava
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 542)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Neisseria subflava"
                     /db_xref="taxon:28449"
     Protein         1..542
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=60413
     Region          8..540
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mnklqepvlv vddeadirdl memtlmkmgl rvdtaagvee akdkldnndy slvltdmrmp
       61 dgsglevvqy idelmldtpv avitafgnad qavealkaga fdylqkpitl sqlrslvksa
      121 vsvsdntaep tpsekvksqp apvsaalykp epqpakpvvt ppksvqsefn rpltvpegln
      181 slkerfsags inpalqqdap vlegeddmpr llgtspqmve vrhlirrlar slvpvyisge
      241 sgtgkeqaar tihelsdrad kpfiavncga ipenlmesef fgykkgsftg adqdrlgffq
      301 hadggtlfld evadlplamq vkllraiqek avrrigdare ttvdvriica thknlealve
      361 sgafrqdlyy rlnvvslhmp plremredlg alilyllykh rhgnqtykls pkaqeallhy
      421 sypgnfrele nileravalt vgqviqvddl qiqnapqvka ersgfsfddi aepdarettl
      481 nhspippfdp rtmqiqdyld qversiieqa lrqtrynrtq aakllgisfr smryrmerld
      541 in
//
LOCUS       WP_285071303             740 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Neisseria subflava].
ACCESSION   WP_285071303
VERSION     WP_285071303.1
KEYWORDS    RefSeq.
SOURCE      Neisseria subflava
  ORGANISM  Neisseria subflava
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 740)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Neisseria subflava"
                     /db_xref="taxon:28449"
     Protein         1..740
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=80204
     Region          69..740
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mtkpasrlsi lslsllavsa afasdepqdr eiaeletitv tasadaskgg lipafkggqv
       61 argsrvgilg nkknlespfs ntaytnrliq dkharsvgdv lqndptvrva rgygnfqeay
      121 firgfaaesd dtmynglygi lprqyiatel fervevqrga saflngmapg gnniggtvsv
      181 lpkrasnegl nrltanygag krgglaadva rrfgqnqefg vrvnaahhng ktaiddeksk
      241 lslvnvgldw rnenarlsad lgwqdnklka trtnvtlsgl tavpaapdts snwaqpwtys
      301 nerdwfgtmr geydfndnlt ayaaygfrrs kennslanlt vrnvngdgsi yrfdnarkdk
      361 idtgeiglrg kfntgavehe wtaaanrfqs srknayimdw gnqyttnlyn psrypqpaaa
      421 nplysgndmg npavtgktrl tsfalgdtfs lwdkrlqfml garwqqvhnk ayayntgaqt
      481 enykksrlsp svgavyritp nwsvygnyie slgqgatags tasingraya vsnageslkp
      541 yvskqkeigt kfeangfgag lalfhtdkpr slyvaesgnt arftsegkdr hrgaeitvyg
      601 evaqgvrllg gitlldakqk stgssstdgk rtigaaktqa niglewevpk vqglafdgrm
      661 vytgssyada antlkvggwt rfdigaryht pigrheatfr arldnvankk ywasvggypn
      721 sgylnagapr sftlsasvdf
//
LOCUS       WP_285071272              92 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Neisseria subflava].
ACCESSION   WP_285071272
VERSION     WP_285071272.1
KEYWORDS    RefSeq.
SOURCE      Neisseria subflava
  ORGANISM  Neisseria subflava
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 92)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 92)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 92)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Neisseria subflava"
                     /db_xref="taxon:28449"
     Protein         1..92
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=10434
     Region          2..87
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 meikrlstil klianperma ilfllldgdr sitelaqald ssptdianhl arlrtegiid
       61 ftryhriiey rliseeatti lntlrtlkdq ae
//
LOCUS       WP_285071482             391 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Neisseria subflava].
ACCESSION   WP_285071482
VERSION     WP_285071482.1
KEYWORDS    RefSeq.
SOURCE      Neisseria subflava
  ORGANISM  Neisseria subflava
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Neisseria subflava"
                     /db_xref="taxon:28449"
     Protein         1..391
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43424
     Region          9..386
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mlntslspwp sftqeeadav skvllsnkvn ywtgtecref ekefaafvgt qyavalsngt
       61 laldvalkam gigqgddviv tsrtflasas civtaganpv fadvdlnsqn isaetikaal
      121 tpntkaiivv hlagmpaemd dimalakehn lwviedcaqa hgakykgksv gsighvgaws
      181 fcqdkimttg geggmvttnd kelwskmwsy kdhgksydav yhrehapgfr wlhesfgtnw
      241 rmmemqavig riqlkrmpew tarrqahaak laeslgkfas irlvevadyi ehaqykfyvf
      301 vkpehlkdgw trdrivneln arkvpcyqgs csevylekaf dntpwrpker lknavelgnt
      361 slmflvhptl tdeeiafcke nieavlteat a
//
LOCUS       WP_285071339             463 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Neisseria
            subflava].
ACCESSION   WP_285071339
VERSION     WP_285071339.1
KEYWORDS    RefSeq.
SOURCE      Neisseria subflava
  ORGANISM  Neisseria subflava
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Neisseria subflava"
                     /db_xref="taxon:28449"
     Protein         1..463
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48572
     Region          5..459
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mqlfldnlka ffetisgwvw gpimlmllvg tgilltvllk glqftmlgya lkqafvpskk
       61 hedsedhegd ishfaalmta lsatigtgni agvatavvtg gpgavfwmwm taifgmatky
      121 gegvlavkyr vtnskgemsg gpmyyiekgl gknwkwmava falfgtfasf gigssvqsns
      181 vaqavqtsfg vepaytgval tvltaivllg gikgiakaas fivpamavfy vvggiaiivi
      241 nsdvlmpavk lifsdafsaq avaggaigtv irygvargvf sneagmgsap iaaaaaktdh
      301 pvrqalvsmt gtfldtivvc sitgivlvmg llgaggefvk pelsgaaltt vtfqkmlpgi
      361 ggwivtigli ffaystilgw cyygekcavy vfgekfagly rvgyvssvml gtvlsldlvw
      421 lasdtfnglm alpnlialll mikvivnetr dfkqkvkdga lph
//
LOCUS       WP_285071779             267 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Kingella kingae].
ACCESSION   WP_285071779
VERSION     WP_285071779.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..267
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29451
     Region          1..169
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkldiiipcy naastlnrav esslqqaelh qlwlvddast ddtwahiqaw qarypsriqa
       61 crlpdnggva rarnwgalqs qaeiiaflda ddayqahalq aalycfeqld ylglirlrlq
      121 avgldsryan hpniaqawhs lqmtvggntv frrafflacg gfpqdalfre lggedgalgi
      181 attqssvvgt lfadsepavl hycragmhae rlldaylfqq hdsrvtpeny aqaqavtcqi
      241 hqqlqqlrpi lnqaqngsmp ltvsrae
//
LOCUS       WP_285071797             297 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Peptoniphilus harei].
ACCESSION   WP_285071797
VERSION     WP_285071797.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..297
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32590
     Region          1..297
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mnrvkiianp nsgrgaalgk ilelielmse dryeiellft heegdgtrfa ydysgedfii
       61 csggdgtvne vvngmylsgr diplgilqsg tvndfanaqg lptspnafyk miknyktkti
      121 dlglageraf invaaggmlt eiaytvsaek katlgdmayy legarvllee kifkykksln
      181 fyieseeftg tiegllflit nstsvggfkk mapladisdg fldvlifkei risdvpelfa
      241 slmggrhvdh nkvmylktkn ikissdenlt idvdgekast lpmtfkvlen klkiivp
//
LOCUS       WP_285071909              82 aa            linear   BCT 25-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Peptoniphilus
            harei].
ACCESSION   WP_285071909
VERSION     WP_285071909.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..82
                     /product="type II toxin-antitoxin system RelE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0017148 - negative regulation of
                     translation [Evidence IEA]"
                     /calculated_mol_wt=9794
     Region          2..79
                     /region_name="RelE"
                     /note="mRNA-degrading endonuclease RelE, toxin component
                     of the RelBE toxin-antitoxin system [Defense mechanisms];
                     COG2026"
                     /db_xref="CDD:441629"
ORIGIN      
        1 mtykvrttkk fdksfkkldr qsqkliknwm egnlidcqdp rfygkaltgn fkvvwryrig
       61 acrllskidd dkliiffidr rn
//
LOCUS       WP_285071918             302 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Peptoniphilus harei].
ACCESSION   WP_285071918
VERSION     WP_285071918.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..302
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34777
     Region          6..201
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mtiknkidyk yrigmrtlkt slavviglyi sylldldsai fvsiaavstm kpsmsesled
       61 fkkrlftcvf gvmvgyffsk isvveylepl iaglgillti yilvvvkmkd mtqlscivfv
      121 asfcsnsdkf yyatnriigt vigiivgvlv nyfisspnvw edfilsarsc yrssslvlkq
      181 ilfgekvdls efnrelasat klykllekea dtpfqyrykk isrekrimsl iesisvrlev
      241 venmnadhfs fevsqealkr ydleeeyssd ldvedrvyny hieyilkymd qlkeeienik
      301 vk
//
LOCUS       WP_285071921             106 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Peptoniphilus harei].
ACCESSION   WP_285071921
VERSION     WP_285071921.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..106
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12469
     Region          4..93
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlnekmdkyi efskkikilc epkrlqiidl lscrdlcace ileyfhisqp tlsshmkkle
       61 eanfvesrrd gkniyyrlke dslkdvknfi deistntedc icktqe
//
LOCUS       WP_285071951             332 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Peptoniphilus harei].
ACCESSION   WP_285071951
VERSION     WP_285071951.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..332
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37384
     Region          31..330
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mnnfrndysd fgskeiykei erifdkkvsg ygtdeisnea rdlilreigr eadiefvsgg
       61 tatnilattf glrpyeavls astghithhe tgsieatghk vvtlktadgk lradeirkfi
      121 ddqpgeidvk ikvvyisqtt evgtvytide ikeiyevcqe knlylyidga riahamaans
      181 sslsdyakys hifslggtkn gaifgealvi ldenlkkdfr yylkqrgamm aksfliglsf
      241 kvlfqdglyy enakraydms rmlveglkdl grdpvfaesn qvfiksspee ieklkkenif
      301 eienakesii rlvtnyrtse eevrgflnsi sn
//
LOCUS       WP_285071980             467 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Peptoniphilus
            harei].
ACCESSION   WP_285071980
VERSION     WP_285071980.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..467
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49905
     Region          1..446
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mrellsavng vlyypiliiv llacgfyfti rtkfiqfgll geafkvitek pegkddvssf
       61 qalmvstasr vgtgnivgva naiclggpga vfwmwiiali ggasafiest laqiykkrgs
      121 dgvsyggpsy yienalgsrg igvlfavali atyavgfnml asfnlqdsfr vydfyvpgkt
      181 swmigavlav lagycilggg kriikytsll vpvmgvifvi malimilina knipamfgmi
      241 fedafnfkai fggvagsalv qgikrglysn eagmgsapna aasasvshpv kqglvqmisv
      301 fldtivicsa tafmslasgi apteelagap fvqaslatvf grygnlfitv slalfafttl
      361 lgnlyyvdsc ltylnkktps kifmlcyrii atilifvgag memslawdia dflmgvmcli
      421 niptiiilgg talkalddyk kqreegknpv fkaetigidt skldywk
//
LOCUS       WP_285072201             229 aa            linear   BCT 25-DEC-2024
DEFINITION  RsmE family RNA methyltransferase [Peptoniphilus harei].
ACCESSION   WP_285072201
VERSION     WP_285072201.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Basturea,G.N., Rudd,K.E. and Deutscher,M.P.
  TITLE     Identification and characterization of RsmE, the founding member of
            a new RNA base methyltransferase family
  JOURNAL   RNA 12 (3), 426-434 (2006)
   PUBMED   16431987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..229
                     /product="RsmE family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=26049
     Region          1..218
                     /region_name="RsmE"
                     /note="16S rRNA U1498 N3-methylase RsmE [Translation,
                     ribosomal structure and biogenesis]; COG1385"
                     /db_xref="CDD:440995"
ORIGIN      
        1 myrffedref qgntnlkeet lhhlknviri kdgeafqvvf edgifsfaye gekiknlgev
       61 lesneskvrl slffgilknn ksedvlrhat eigvsdfypv imdrsisdif kkkekklerf
      121 qkivesaakq skrdiipmvh diiktddiln fsgdlvlcye dedktqlgev tkdlsnnigl
      181 iigpeggise relellseak kvglgrrilr aetaaitasf yiihakece
//
LOCUS       WP_285072425             384 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Peptoniphilus harei].
ACCESSION   WP_285072425
VERSION     WP_285072425.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..384
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=44129
     Region          1..381
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mkriknvknt ivfklilsii lifivmtats nyiigkyqen riqdigekiv meetnkgnkd
       61 yfivledskl kstkeiknfs livigstial gslvyyflvs rslkplkelk ekvqeididk
      121 vnseekiyme gqsqeieels lafqksldki ygsyarekal sssiahelnt pvavmkssle
      181 iylmknkled qelkelldnf denidriski iesllflnrr enaisrkfdi kdlveeivfd
      241 ledlaeeknv nliskmgsre ihtsdiller vlynlgknai aynkegglvv fdfaedeeny
      301 fiyvrdtglg ideeekekvf dlfyrvdesr nkktggygig lnlvknivek lggqvlirdn
      361 lnenneirgs vfevrlpksk eeil
//
LOCUS       WP_285072653             975 aa            linear   BCT 25-DEC-2024
DEFINITION  UvrD-helicase domain-containing protein [Peptoniphilus harei].
ACCESSION   WP_285072653
VERSION     WP_285072653.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 975)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437585
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..975
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..975
                     /product="UvrD-helicase domain-containing protein"
                     /EC_number="3.1.11.5"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=114364
     Region          1..934
                     /region_name="RecB"
                     /note="3#-5# helicase subunit RecB of the DNA repair
                     enzyme RecBCD (exonuclease V) [Replication, recombination
                     and repair]; COG1074"
                     /db_xref="CDD:440692"
ORIGIN      
        1 melsevqkka vytldkdlsl magagtgktr vltsrfiniv knnispkhil aitftkkaaq
       61 emlgriskel vlnnidfeer dlnvmtihsf aheivenysf ilginprfki leegegdyll
      121 eeavkesfnn federfknyl ldfksspfee knnfinlyrd fknnnldfdd ilnkslnfig
      181 aeksfddlii lldafrslsg nkfktfydnn ideikslntf dneilnmiee nlgtstkhnd
      241 kiieikdliq elkkdleekn kdyyeiiiei lkeidknykk skedisgldy ediisyaell
      301 lknplvkgel varysyilvd eyqdtneiqn eiirafsssn ifivgdpkqs iyafrgtdls
      361 syfsfsgdie argtslimnk nyrsdgeiin finekfkdli dsydemefsh kegggvylyn
      421 sseisniadl aedflkkyka kdiailsrsn sqideigevl sargikynkg errleeieil
      481 rliknilsai yspkeflefl slfnskllnf efkdlvsiln eginnsedll nynstqdnik
      541 nflrflketr ekasylmide vldeimdyfy klgtlresdw eyiyrfkeea rdfvenysnd
      601 fraferqiss mtfedledgi nlltihkskg lefdgliish mdkgkklgsn nriivdrdlg
      661 lginsdlsny sykeisnklr eideeeeirv lyvamtrakk elvlfgdhek aragsyfsll
      721 gdvfslqeyk lsnveerqve ekfipldidi kfenrireyy tvtdfinfkr skkdfyykyf
      781 lgidkytrgq gtnqvmdpkt lgnivhmfay kygkndlknk kiediikdif lyyeeeinpe
      841 klnlskelvl nylemeeeci idkellfyyd lkgflvkgyi dqvikingdy yildlktshg
      901 svedlkktye nqlilysaiy enlykvkvka ayifdlrgkn kivvetseek ykevmeefln
      961 yikfirshkl lrdyl
//
LOCUS       WP_285072695             245 aa            linear   BCT 25-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Peptoniphilus harei].
ACCESSION   WP_285072695
VERSION     WP_285072695.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..245
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27009
     Region          1..239
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mdkireaadl ilkskkvfal tgagistdsg ipdfrsssgy yskmdpalal skdrllnhpe
       61 ifykegyqil edlndqepng ghkalakmee egflagiitq nidnlhakag skniyevhge
      121 trgthcmkcg keypfalmrk kveageippk cdacggvirp nvvmfgdmmp ddfergarel
      181 dstdtlivvg ssltvspvnf lpnyvdhlii inndptpmdr radvvihens trvleeilke
      241 lears
//
LOCUS       WP_285072732             137 aa            linear   BCT 25-DEC-2024
DEFINITION  SixA phosphatase family protein [Peptoniphilus harei].
ACCESSION   WP_285072732
VERSION     WP_285072732.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..137
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15885
     Region          3..>116
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mkiyfirhge aeiyaeddfk rklttigrvk lensfkafan kledkrsyki yssplerake
       61 taeilakyld sdfevkdyla ggrirdilkt ldqdgnyifv shepfisnwi yqltgemkiv
      121 srgsinfvei npqdfae
//
LOCUS       WP_285072757             310 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Peptoniphilus harei].
ACCESSION   WP_285072757
VERSION     WP_285072757.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..310
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=36618
     Region          <217..305
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mknnnylasw dfevvddndd fieyqgishp knkmknyklf pglmlmyidl reryqvqasd
       61 skgmkgyris ysyegnyfty indtkilitr eifigkalpy aresyttkdr vqafnfiife
      121 nqidkdsfyg kilgeflkki nsikdmgfvy rnerliqran eliqvlksed ilgisikald
      181 liyditmekt seirksyqkq ekseeiilie efikenlekd itldlltkkf kisksnlnkk
      241 firkfqytpi kylnnlrmmk aeeilmktdk niteismelg ltspsnftrs fkkftglsps
      301 eyrkkealse
//
LOCUS       WP_285072784             473 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Peptoniphilus harei].
ACCESSION   WP_285072784
VERSION     WP_285072784.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..473
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=53482
     Region          132..463
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mknkigkrlv rsfliiilit isiidifllf afssyyynni skeliqrmev sleiyrrdys
       61 dksiedliye dsdiflsntn aevqildkdk nllsdsigrl asnpietsdv laaergeikt
      121 wkgeesqtge simsvagpik nnedetigyl rfissmeevk aaifktiisl liftlfvall
      181 tttvsllisk sivrpilelt evaktmlkgn yeekakvfed deigelaktl namsdeiink
      241 drikndfiss ishelrtplt sikgwavvlk dakedekdlm edglniiene adrlakmvee
      301 lldfsryisg ritldkeiid isqtcldisk qmrpraksnn ielitdlpke silinadenr
      361 ikqllinlld naikftsdkg wvkfqmlked dkvqimisdn gmgmtkeela hvkekfykgk
      421 hskshsgigl sisdeitklh qgsleifsee nigttvkvsl pievdkevge nnd
//
LOCUS       WP_285072973             325 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Peptoniphilus harei].
ACCESSION   WP_285072973
VERSION     WP_285072973.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..325
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=37948
     Region          <234..317
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mgkelmchly grnlekiien skgricefhn lengkyivsk yeifkgvtvf yndihtsvik
       61 kklsknlnqs yeinhcregr fecvlsdgti tymesgdfai nassnssees ffpishyhgv
      121 tfyinpkefd seiyfleeml gikfevvlrk lcnkdkifvq ratrhiehif yevykvpdei
      181 lieylrvkfq elflyissld tsnkisdrky fiktnvdivk kidefiknny eknitydkls
      241 eifkintttm kscyksvfgq tikeaitskr levaadflnn tsisiteiai rvgftdhakf
      301 sntfknkfnl tpseyrkisk tahlv
//
LOCUS       WP_285073015             263 aa            linear   BCT 25-DEC-2024
DEFINITION  NACHT domain-containing protein [Kingella kingae].
ACCESSION   WP_285073015
VERSION     WP_285073015.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..263
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30301
     Region          22..>249
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mearlveikk krfnkqahsl frpatqitls silknekfii ieggmgtgks tlfrkyiksl
       61 ainesfhkek ilpallnvke iidniekiee tiisleqfvn dtivekyifi dgideiqnis
      121 tfinalplia ellskytnvr iilgsrpmwd iedeeilfky lkrysivpls teqlykviqn
      181 tcavldksis erlmrdlnrs entllrtlpk tpmsaillar vlssdikelp qtlpelysky
      241 ielslgrwdi vcgqwqkeni lll
//
LOCUS       WP_285073049             859 aa            linear   BCT 25-DEC-2024
DEFINITION  CD1108 family mobile element protein [Peptoniphilus harei].
ACCESSION   WP_285073049
VERSION     WP_285073049.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Brouwer,M.S., Warburton,P.J., Roberts,A.P., Mullany,P. and Allan,E.
  TITLE     Genetic organisation, mobility and predicted functions of genes on
            integrated, mobile genetic elements in sequenced strains of
            Clostridium difficile
  JOURNAL   PLoS One 6 (8), e23014 (2011)
   PUBMED   21876735
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF045974.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..859
                     /product="CD1108 family mobile element protein"
                     /calculated_mol_wt=98697
     Region          <36..>490
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          <734..858
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mdkklkkdfq kkiirnrdap eknlesklvh sddytnkiik tkdrfgdkis ekesklihen
       61 vlakdqkqdk lkdfqkaknk erirkevldn kdkanevkqt nleiradesf kldedldvdy
      121 kkvnfdsens rnvnfnkltt ddisakaqpi snkkesskrq vlknyedkli hskdkfqdki
      181 nekeskriqt sedkpieakk skrvyrkdkl vkdevsknes ntnidkkqkq klyqekkfrd
      241 kekiskeidk esklsevdtd ktfdnpefkd nnqefikdek etslkaseqk kvnkkktyyk
      301 rknyesdkft rkkiddlkde skkvtrkdsk kaqdvkdfis dkkigeleks ksnlkdnilk
      361 nktkgslssg vllsgaksse lvrdylssgs dntgvesgek vanvssklqh girkykldkk
      421 kkslkklskl dkkirkrksk lefksgledl kksdayikkn rfkkfyqrkq mksmiakkhe
      481 trlvdrvkka ilslgkaske livrkskmvl flviglglml simigggsvg msglsnsvns
      541 vmtttylsqd tvlsevnqef ssmeydlqsq iesvktshpg ydeyiinkeg eighnthell
      601 syitsrcgev ksasevkgil kelfdkmykl dfkeeieirt rtvartryds rgnpytsyek
      661 eeyeykkliv tlkkkemdev vreifkdypd nvvhyealle akgnmgdvfg sgngdlgeiv
      721 dnpnfgnpgl afdsatakal fneaekhigk ryvfgasgps nfdcsgfvcw sftksgvksm
      781 prttawriyk dycnpvssse aqpgdiiffh stynsgtpis hvgiyagngm mihagdpiqy
      841 tsinskywks hfygfgrpr
//
LOCUS       WP_285073479             324 aa            linear   BCT 25-DEC-2024
DEFINITION  DHH family phosphoesterase [Peptoniphilus harei].
ACCESSION   WP_285073479
VERSION     WP_285073479.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..324
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=35791
     Region          9..319
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 minlkevsse lknlidssqt iavashlnpd gdnlgsatam igmlnklgkk pifvlddlip
       61 ssfkflsnls fakspdnidt tfdlfialds sdedrmgdrv keifnkskkt vnidhhfsnk
      121 nyadlnivde kspatceila rifkslglgl nneiatslft glstdtgsfk yssvtsqtfe
      181 iasdlfkyni ninevtqnvy qsrsrqktdl likamnsiey fyedriavvl vtkddmentk
      241 aaksdadgiv efvrdidsve lavllkekdd cirlslrsks yvdctkiask fnggghiras
      301 ggtinhtdli kakkdlikva eeel
//
LOCUS       WP_285073532             297 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Peptoniphilus harei].
ACCESSION   WP_285073532
VERSION     WP_285073532.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..297
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32618
     Region          1..297
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mkrvkiianp nsgrgaalgk ilelielmse dryeiellft heegdgtrfa ydysgedfii
       61 csggdgtvne vvngmylsgr diplgilqsg tvndfanaqg lptspnafyk miknyktkti
      121 dlglageraf invaaggmlt eiaytvsaek katlgdmayy legarvllee kifkykksln
      181 fyieseeftg tiegllflit nstsvggfkk mapladisdg fldvlifkei risdvpelfa
      241 slmggrhvdh nkvmylktkk ikissdenlt idvdgekast lpmtfkvlen klkiivp
//
LOCUS       WP_285073537             405 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Peptoniphilus harei].
ACCESSION   WP_285073537
VERSION     WP_285073537.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..405
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=47078
     Region          167..400
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mlsdfkvfmr dlfldlmdrv flenifvssv iifelfnink hfilawtvtl ifallkikrk
       61 klldtiftyn lykyrrfknf rlfgtlnvtl iimyiifysl iksdivllnv llfmilravi
      121 ivevqfaqna lsieliesil ygyefeipsp feneyldkit vlmedfkvrd rlrleenfrs
      181 erfkvdlitn ishdlktplt siinyadlls kkevlddeak nfvailkrns trlkdlivdl
      241 vfasktstgn lsiekslvel nemilqiygd ydslfekmdl efsyksasde iliytdvnlf
      301 vrivenlfsn aakharpgtr vlagvieres tiefyvkniv deklnmnsde lfeellkadr
      361 srhsegsglg lnivknlael lggevkvsih gqwfevhvll lrdsd
//
LOCUS       WP_285074096             310 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Peptoniphilus harei].
ACCESSION   WP_285074096
VERSION     WP_285074096.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..310
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=36801
     Region          <217..305
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkntnylasw dfeiiddndd fieyqgishp knkmkkyklf pglmlmhidl rekyqvqasd
       61 skgkkgyris ysyegnyfty indtkilitr eifigkslpy aresyttkdr vqafnffiye
      121 nqidkdsfyg kilveflkkv nsikdmgfvy rnerliqran eliqvlksed vlwisikald
      181 liyditmekt seirksyqke erseeiilie efikenldkd itldlltkkf kisksnlnkk
      241 firkfqytpi kylnnlrmmk aeeilmntdk niteismelg ltspsnftrs fkkftglsps
      301 eyrkkealse
//
LOCUS       WP_285074242             478 aa            linear   BCT 25-DEC-2024
DEFINITION  MBOAT family O-acyltransferase [Peptoniphilus harei].
ACCESSION   WP_285074242
VERSION     WP_285074242.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Hofmann,K.
  TITLE     A superfamily of membrane-bound O-acyltransferases with
            implications for wnt signaling
  JOURNAL   Trends Biochem Sci 25 (3), 111-112 (2000)
   PUBMED   10694878
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004295
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     Protein         1..478
                     /product="MBOAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55565
     Region          1..478
                     /region_name="DltB"
                     /note="D-alanyl-lipoteichoic acid acyltransferase DltB,
                     MBOAT superfamily [Cell wall/membrane/envelope
                     biogenesis]; COG1696"
                     /db_xref="CDD:441302"
ORIGIN      
        1 mlfnsfeyli flpivvifyn llrgkfknif lllasltfys fwnvkytflm vlsilitymt
       61 gifiennrds karmklavfl cffinlgilf ifkyfnffmd laskisggnf nialdlllpv
      121 gisfytfqal gytidvyrkd leaerslidy alfvcffpql vagpiersrn llpqiknpkk
      181 fsyenlvrgl qlffygmflk liladraaif vndafsnyqt yskeflligg flftlqiycd
      241 fysysimakg sakilgidlm dnfkepllsk sitefwrrwh islstwfkdy lyiplggnrh
      301 gelrkcinll ivflvsglwh gaelsfvlwg lihgvfnile sllginkskk snfllnffrr
      361 iltlvivvfa fiyfraenih qgnayilgil nnpssnnlle eianskfgia nlyplgigif
      421 illifdiiky nkidlsekif klflpirwiv yftfllaiii fgiygpdfse safiyfqf
//
LOCUS       WP_285074264             179 aa            linear   BCT 25-DEC-2024
DEFINITION  KdsC family phosphatase [Kingella kingae].
ACCESSION   WP_285074264
VERSION     WP_285074264.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..179
                     /product="KdsC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=19243
     Region          9..178
                     /region_name="KdsC"
                     /note="3-deoxy-D-manno-octulosonate 8-phosphate
                     phosphatase KdsC and related HAD superfamily phosphatases
                     [Cell wall/membrane/envelope biogenesis, General function
                     prediction only]; COG1778"
                     /db_xref="CDD:441384"
ORIGIN      
        1 mfnhvapdil sraqavklli mdvdgvlttg qlfiastgei ikpfntldgh gikmlqktgv
       61 qtaiitarnd pavaaraqsl gishylcgid dkrmayeqlr dqlglsakqc amvgddvidl
      121 pvmvrcglpi avanahifvq qraayttqkh ggmgairect dlimhaqntl qaalneytq
//
LOCUS       WP_285074291              68 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Kingella kingae].
ACCESSION   WP_285074291
VERSION     WP_285074291.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 68)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..68
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7656
     Region          1..>42
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
ORIGIN      
        1 mshfpdvgyt pdnlrhllge lnltqrevae klgvqlravq rwaaavdlpt hadmplkkwn
       61 ellnllnk
//
LOCUS       WP_285074585             476 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285074585
VERSION     WP_285074585.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..476
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51910
     Region          5..461
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mstrktqtlt ilhtndihsh fgsmssiaam igqekeeage flvvdigdhm drmavetegt
       61 lgaanvdvln ltgydaitig nnegltftpe qlaqsysgll cpvvcgnvvd qatglppvwm
      121 ksslilekgp frigllgata pftafyellg wdvlepveal reqvealrsq vdvivilshl
      181 glstdrrlae qipgidvilg ghthhvleep lvigqtvlga agkfgqwlgk vvlereygan
      241 elalvssgcv pvqnmmleer valaidthrt eaeralgqta vitdrtlaid ydhespfasl
      301 laqavrqftg aqlslvnagq lladlpqgni tkgmlhslcp spinacticl ngiqireale
      361 qsllsefsrk piigfgfrgh ilgtlcmdgm dveydphapl yekiraiyie gepirdehey
      421 vvgtldmftf nvgypslslg tdttyrlpef irdlletelk rpgalddslr srwhei
//
LOCUS       WP_285074592              54 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285074592
VERSION     WP_285074592.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 54)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 54)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 54)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..54
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..54
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=6335
     Region          <1..46
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(3..4,15,18,22..23)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mtqaefsrrt gwskrmisff atsqrpmnve amylaamild iqmeqlyewe vltk
//
LOCUS       WP_285074702             422 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfotransferase family protein [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285074702
VERSION     WP_285074702.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..422
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=47611
     Region          10..212
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mvdvhgnglv lllcvprsgs slstvmlqnh srvfatqemw flmnlvdlqk adsrpyggsa
       61 iirqfysamv sdegfekacr sfaleiyngf legsgadflv dkspryyyml ewldrlfpqs
      121 krihlqrnpl avaasykkvn rhtgegfeli rslqspnlnm kavdltlgmf rlndyfadkh
      181 tnayevqyeq lvsnprdeme klcgflgigy eegieqygrf adstksnmfy smgvgdpfls
      241 shqeahkdsv nnwknildpq evefycrvmg adlfhqmgys eqleeaeqwt gvryeagpde
      301 eviakldrqf seatgcswqh gyrmqpvdva ggtqdgnnnn lgtsepkaid ptlaalatir
      361 qleaalraad nrlergyner erlkaqlasa hskiqriksl ipfgnqlsaw asqrkilrgg
      421 ks
//
LOCUS       WP_285074795              60 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285074795
VERSION     WP_285074795.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 60)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 60)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 60)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..60
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..60
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=6824
     Region          11..59
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(11,34)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(16..17,28,31,35..36)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 myekfqvlld reqktayrva kdtgvttatl tswkkgkytp kvnklkvlad yfgvsvdyfl
//
LOCUS       WP_285074983             128 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Paenibacillus
            sp. UMB7766-LJ446].
ACCESSION   WP_285074983
VERSION     WP_285074983.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..128
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14767
     Region          16..112
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mteqgqtgsp kkyrvgveva levmggkwkp liiyhlmtgr krtselrrli pditqkmltt
       61 qlrglekdei vqrkvysevp pkveyeltdy gwglkpaldh lcywgeehle kvhgdkskvl
      121 eefdsper
//
LOCUS       WP_285075174             856 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-mannosidase [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285075174
VERSION     WP_285075174.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 856)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 856)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 856)
  AUTHORS   Nascimento,A.S., Muniz,J.R., Aparicio,R., Golubev,A.M. and
            Polikarpov,I.
  TITLE     Insights into the structure and function of fungal
            beta-mannosidases from glycoside hydrolase family 2 based on
            multiple crystal structures of the Trichoderma harzianum enzyme
  JOURNAL   FEBS J 281 (18), 4165-4178 (2014)
   PUBMED   24975648
REFERENCE   4  (residues 1 to 856)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 856)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14312054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..856
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..856
                     /product="beta-mannosidase"
                     /EC_number="3.2.1.25"
                     /GO_function="GO:0004567 - beta-mannosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005537 - D-mannose binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=97979
     Region          10..>680
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          687..774
                     /region_name="Mannosidase_ig"
                     /note="Mannosidase Ig/CBM-like domain; pfam17786"
                     /db_xref="CDD:465505"
     Region          779..852
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; pfam17753"
                     /db_xref="CDD:465483"
ORIGIN      
        1 mnnlsqdlsg qwkiqhfevg ekramdvaaa alddrfwiga evpgdvhtal versiidppy
       61 yghndaksrw ieqkewwyrt nfnlvkdgea eeyfelvfdg ldtfatvyvn ghevgktanm
      121 lmshtfnvtt lvrngwnaia vkfdplylhh rdketfdwss ytkerpwlrk aamnfgwdwg
      181 prmvtvgiwg rvrlerrtia klenvfarte svskqlaavh vtadvksvls frsrhkreka
      241 vvlscdiril dasgqevars aevvvkngla dtiltldspq lwwthdlgep ylyrlavtll
      301 adgvevdqyn epygvrtiel alhneqgeda ftfilngvrv yakganwipa dhligaipas
      361 ryrelieltv eghmnmlrvw aggiyekdif ydecdrqgil vwqdfafana lfpdfnrefm
      421 nnvrdevenn vlrlrnrasl alwcgnneid wlydmksasg ditspfygel iyhelipevl
      481 erldssrpyw psspygdshg ndandpdvgd rhnwqvwhgs vyprkhgepp lldysiegvt
      541 fknykkdnal fssefgmhas anrytleknm pagqfywgsp emayrnkdtn hqkgillmeg
      601 ytgipqniee ymnysmltqa eglrygiehf rrinhrnsga lvwqlndswp gtswsmidye
      661 llpkasfyyg kvffhpills lehepgeplt lwvvndtret lrgqlrlnvy glngekvyss
      721 shhvetgsqc striaemsea evlggrlaee vlvelvaegf taplnryflr dpknvnllpa
      781 qlnvhvneee qsvsvtaiga iarlvklelp lgrvrfsdny fdllpgesrt vrlrhpekls
      841 lpmtelrvsa mngrea
//
LOCUS       WP_285075235             244 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285075235
VERSION     WP_285075235.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..244
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27915
     Region          <8..243
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mtdsrylkrt ivkeeiesry lgekrtlriy lppgynells ypvvycqdge effnfgriat
       61 tanriildeg aepfiivgvq vdvsvrtqey apfgdrfkay tscfaeeiip yveekypvrs
      121 spqervlagd slggsvslhl allypnlftr vismsgayys asqeiyaaae dlswlsiwmi
      181 vglqetafea dtgtynfvql nrdtrdllek rgaivsyqek dgrhqwgfwq nelpeallyf
      241 lqen
//
LOCUS       WP_285075300             429 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285075300
VERSION     WP_285075300.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 429)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..429
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46827
     Region          45..419
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(152,154,277,279,311..313,354)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mnirkkwaag laslllvslm agcnnsndgg gaadsgaqkk vtisytiwdk nqqpameaia
       61 dafteqhpni kvkvdaipwg eywtkmsaaa pagmlpdvfw mhggqfmkya egqflepitd
      121 kvqageidld nyasnltsiy tvdgqnygip kdfdtiglay nkelfdqani aypddtwdya
      181 klaevakqls qpdkgiygfg akldtqagyw ndmlanggfi lnddmtksgy deqasiealk
      241 aryqmildka spthqqmtdt dsvemfksgk lamifdgswd ngnlasseii kgkydwaplp
      301 kgkvkrgnii ngignvmstk gkhkdeawqf lkflgskeaa eitaemgaai pafnntqdaw
      361 vknnpdlnlq vfidqaadat pypsgsksyp vwfskeaeim sqawggaisi eegakkvaem
      421 mnqaigdak
//
LOCUS       WP_285075349             366 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285075349
VERSION     WP_285075349.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..366
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=39442
     Region          20..365
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mneenismsi qlnsklcesf nirypivlag magianmapl vaavsnaggl gtlgaaymsp
       61 eelrdaihei kkrtqapfav nifahvgpdq ytnfdavnee ltsiqeslgv krrtkdeihs
      121 pnhfeeqfgi lldekvpiis ttfgllsehh mqrakslgik imskvttvee aiqaekrgcd
      181 vivaqgseag ghrgtfdvss qpgganigtm alvpqivdhv hipvvaaggi mdgrglvasl
      241 algaqgvqmg trfltsaesg ahevykrall dsteestvit nafsgrparg ikndfiqhwe
      301 asrtkplpfp tqntltreir nasarqnnse ymalwagqgt rmltdnqsag diinqiveea
      361 rtiiql
//
LOCUS       WP_285075351             294 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285075351
VERSION     WP_285075351.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 294)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 294)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 294)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..294
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32770
     Region          1..294
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mrknwplyvl cipafvfvcl fsygpmvgll mafqdykpwl giggsrwigl dnferifqyk
       61 eatqaivntl iiavskiivg iivpivmail lseirnvgik ksvqtlvylp hflswvtvag
      121 lmidilgldg gvnqvltwmf gndpiyflgd pdlfrftvvv sdvwksfgfg mivylatiag
      181 inpsyyeaae idgatrrqqi ryvtlpsmlp miivistlsl gnildagfdq vfnlynplvy
      241 stgdiidtyv yrssllsgqy gfgtavglfk sgislilivv syrlaykyan ykif
//
LOCUS       WP_285075372             302 aa            linear   BCT 25-DEC-2024
DEFINITION  RCC1 domain-containing protein [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285075372
VERSION     WP_285075372.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Hadjebi,O., Casas-Terradellas,E., Garcia-Gonzalo,F.R. and Rosa,J.L.
  TITLE     The RCC1 superfamily: from genes, to function, to disease
  JOURNAL   Biochim Biophys Acta 1783 (8), 1467-1479 (2008)
   PUBMED   18442486
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Renault,L., Nassar,N., Vetter,I., Becker,J., Klebe,C., Roth,M. and
            Wittinghofer,A.
  TITLE     The 1.7 A crystal structure of the regulator of chromosome
            condensation (RCC1) reveals a seven-bladed propeller
  JOURNAL   Nature 392 (6671), 97-101 (1998)
   PUBMED   9510255
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..302
                     /product="RCC1 domain-containing protein"
                     /GO_function="GO:0003682 - chromatin binding [Evidence
                     IEA]"
                     /GO_function="GO:0005085 - guanyl-nucleotide exchange
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31267
     Region          19..284
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
ORIGIN      
        1 mdynspneta lkvkrpkytt iaagrrhsig lksdgtvmav gdnkvgqcdv sdwrdivava
       61 agnvhmatnt gnshtiglts hgtvvavgwn kheqcnvkdw rdimaiaagw rrtvglksdg
      121 tvvavgrnne gecdvgswrd maalaagdwh tvglksdgtv ttvgnnqygq cdvsvwtdiv
      181 avaagylhtv glksdgtava vgrnthgqcd vsdwggivai aagsnhtlgl ksdgtvvavg
      241 lnkheqcnvg dwsdivavaa gcayslglks dgkvvavgdn eygqcnvigl qvptsspavk
      301 kv
//
LOCUS       WP_285075454             255 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285075454
VERSION     WP_285075454.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..255
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28624
     Region          <11..254
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 miaapkgydq yregiprgii etveypsttv gnsrkvmvyt ppgfssdnty nvlyllhgig
       61 gdetewynhg tpqvildnly degklepmiv vfpngrampn draegdlfap dkiqaferfe
      121 sdllddlipy ieenypvwin renrgiagls mgggqslnig wgnldrfawi gafsaapntr
      181 apevlipnps eitglvrklw lscgdqdnlk hisdqmhayl aqhgishiwn eeqgghdwpv
      241 wknglyqfsq llfki
//
LOCUS       WP_285075456             106 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285075456
VERSION     WP_285075456.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..106
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11866
     Region          11..98
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mslytpafds sdlkqfdepa nllkalshpi rlcivrglmr kkkcnvsymq ecldlpqstv
       61 sqhlqklrsa givaterngl evnyvladqr ieqiipilfg eddces
//
LOCUS       WP_285075621             302 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285075621
VERSION     WP_285075621.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 302)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 302)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 302)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..302
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33903
     Region          5..302
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mgamkrrlwk erqiwiiaip mlvwvlvfcy yplygliiaf qnyvpghsll sgpwvgldnf
       61 irffhvpefk hiirntvais lltmllslpa piilavlfne vksklfkrsi qtlsyipyfi
      121 swvvvasiin tilgsdgivn dillrlglid railfmgegk yfwgilasan lwkevgfsti
      181 iylsaiagid geqyeagrvd glgrfgliwh itlpsirtti vllwilglgn ilnagfeqql
      241 llgtpmtqdy yevidtyvyr ygvqlgnysf gtavglmkai igivlvvtvn kiskktldts
      301 if
//
LOCUS       WP_285075650             323 aa            linear   BCT 25-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285075650
VERSION     WP_285075650.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Rengstl,B., Oster,U., Stengel,A. and Nickelsen,J.
  TITLE     An intermediate membrane subfraction in cyanobacteria is involved
            in an assembly network for Photosystem II biogenesis
  JOURNAL   J Biol Chem 286 (24), 21944-21951 (2011)
   PUBMED   21531723
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Komenda,J., Nickelsen,J., Tichy,M., Prasil,O., Eichacker,L.A. and
            Nixon,P.J.
  TITLE     The cyanobacterial homologue of HCF136/YCF48 is a component of an
            early photosystem II assembly complex and is important for both the
            efficient assembly and repair of photosystem II in Synechocystis
            sp. PCC 6803
  JOURNAL   J Biol Chem 283 (33), 22390-22399 (2008)
   PUBMED   18550538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..323
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=35709
     Region          70..217
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
ORIGIN      
        1 mrrsrliagi lcltlvlsvl gfntkamale eykeidsitl qesphsigdg wtedftfssn
       61 apyaltqgkn neylavgpyg tvikskdgvs wralskfgny hltaiawdgk ryvmfgtntt
      121 ydmdiykqps eafisqdgls wtkvdfapge tieqlkwggn gfvalgtkhv ftskdgtnwa
      181 tsytlksqrg snglhavnnt ffvssydnky vlvskdgvtw saktynasaa irdfiwsgkq
      241 yigvgngiyt stdgvnwkkq skspngvqlk tvlygnntyi vtgssnldgg gelqyrlfie
      301 rrgyleedkp vlssneylyh vsg
//
LOCUS       WP_285075670             307 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285075670
VERSION     WP_285075670.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 307)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 307)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 307)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..307
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35573
     Region          2..307
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 msnrqsfrsr fvrdfmmnky lyimmipvig yylifhygpm ygaiiafkdy spmkgimgsd
       61 wvglkhfeef fnsyyflrvl kntllislyt llfefpapii lallinevrk rtfkrvvqti
      121 tympyfislv vicgiitdft nadglinrli mmlgydgqam lqkpelfrpi yvlseiwqri
      181 gwesiiyiaa lmsidleqye aakidgasrl kqmfhitlpg llpiitimfi lrmgnmlnvg
      241 fekiillynp vtyetadvis sfvyrkglle fgwsyssavg lfnsvinlal lisanyisrr
      301 vsqnslw
//
LOCUS       WP_285075878             318 aa            linear   BCT 25-DEC-2024
DEFINITION  GGDEF domain-containing protein [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285075878
VERSION     WP_285075878.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 318)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..318
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35573
     Region          89..>290
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mlstffvnvc vmitfmyvsg iiakfyrirv pfpsmrvqmi ggllfgiygt vlmnysfpln
       61 ettivdlrhl aivtaavylg gfasvisglv isilrilmfg mssaaidaaf vmtiiglsgv
      121 yfayapwsrl tkiitmnllg mtlifvilml ntssmnslmk vyplqitisf vggifiyfia
      181 efinksneml fllerkastd hltnlsnrrq fekslelele rarenkqkls llvididrfk
      241 kvndtfghss gdavlkqlgq llikharsad ivsrnggeef aillldcgha trlwrllsrs
      301 gkrwrstssp crmairsg
//
LOCUS       WP_285075986             674 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285075986
VERSION     WP_285075986.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 674)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 674)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..674
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=77104
     Region          11..630
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mkalsareyq ilhfllerrd fvpvkeianh mnwsektiyr elnalehnld trgirlerkp
       61 gtgialaltq eqtmelrstq wipgkkvvtt lsvearriki ltnllydspe etsinklsee
      121 yfigkasivn dlkaieerie pfhlrleksq lgtrligsei dirkamasli helvsedrke
      181 qehqsridgn tlgeliehfg sdsvegiqri leeteqhlgy tigdpyyinm lthllicirr
      241 lksgkvirla dgisdhpvtd pnvhsiakam anrikeqygl elpseeiyfi yqylissgms
      301 ipslnlelsg lmdkacpesk amvkeliqnv sgmirrdltr deqlykglii hfkpmlnrlk
      361 ynisinnpll edirkeyaei fslvslgmlp iaqacglnsf sddeisylvl yfqasiekss
      421 kkkrvilvcs tgigtshllk nrinrtfpew evvdvistsw fkrmedwtei dliistvkle
      481 hqdlpvvyvs allndtdvsl ikakfneekl nqhpnkvfsf pligayfhps clqietntke
      541 pfaegkasrl klftsilkhv ganmenrtfa eaklnnhlsi flirsdvnvn pvvgfnvvqg
      601 ksanskleiv iaffegepit ellieiqsll mcrrmfeqim rvttplelve ilqskhgqee
      661 dhygynqdyq rtvd
//
LOCUS       WP_285076004             427 aa            linear   BCT 25-DEC-2024
DEFINITION  Leu/Phe/Val dehydrogenase [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285076004
VERSION     WP_285076004.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Brunhuber,N.M. and Blanchard,J.S.
  TITLE     The biochemistry and enzymology of amino acid dehydrogenases
  JOURNAL   Crit Rev Biochem Mol Biol 29 (6), 415-467 (1994)
   PUBMED   7705101
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10500541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..427
                     /product="Leu/Phe/Val dehydrogenase"
                     /EC_number="1.4.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44863
     Region          13..>96
                     /region_name="ELFV_dehydrog_N"
                     /note="Glu/Leu/Phe/Val dehydrogenase, dimerization domain;
                     pfam02812"
                     /db_xref="CDD:460706"
     Region          226..420
                     /region_name="NAD_bind_Leu_Phe_Val_DH"
                     /note="NAD(P) binding domain of leucine dehydrogenase,
                     phenylalanine dehydrogenase, and valine dehydrogenase;
                     cd01075"
                     /db_xref="CDD:133444"
     Site            order(255,257..259,278..279,283,313..314,335,337)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133444"
     Site            368
                     /site_type="active"
                     /note="Phe binding site [active]"
                     /db_xref="CDD:133444"
ORIGIN      
        1 mqlwhemere ameelifchd prsglkavia ihstvlgpal ggcrcwtyas eedavrdaik
       61 lakgmtyksa vsglpygggk avvwdvptel rgitggnspg seilkknnek tkgqthgdre
      121 aagieaetkk dignnindgp lntsvirtnr dpepsdsial slqaskraai fralgrsler
      181 lngryvtgld lgttaadmdq irletahvtd ttgslgakdd ftaemtaygv ytgivtslch
      241 qgigalqgis vavqglgkvg yalcrylhaa garlivadvv pervqralvq fsgaisadpa
      301 hihaadckvf apcalggvlt patveelrcs ivagaannql serelvvrrm qargilyapd
      361 yvlnaggiis tacelegagp dlirqkvagi agtlskvyar akqstmstad aadqlaeavl
      421 qsgksha
//
LOCUS       WP_285076132             191 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Paenibacillus
            sp. UMB7766-LJ446].
ACCESSION   WP_285076132
VERSION     WP_285076132.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..191
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=20907
     Region          <2..136
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mhladayrsv lgevltrvtl skltglnpge lsftrnqygk pslsndadvq fnvshsgdwi
       61 alisggdtdl gvdvekispt dmkiaerffs mtesqflaae paeiqletfy rlwtlkesyi
      121 kavgmglsmp ldsfsmirna dghwhspeaa sypflsmrld pghmlaacsa geglpaqpdf
      181 itieelyqal l
//
LOCUS       WP_285076170             511 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Kingella kingae].
ACCESSION   WP_285076170
VERSION     WP_285076170.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 511)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 511)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 511)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..511
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56307
     Region          6..506
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mphllralll atipaaflcl ltaiplwkml dyggsplwle mlhdsyyrqr ilwtatqaac
       61 tvlltlllgl pcawalarlq fsgkalilrl lmlpfimptl vagmgvlalf gekgllwrgw
      121 qdtavlllyg niffnlpvli rsayqgllav panriaaakt lganawqqfw hvelpvlrpw
      181 lasagclifl ycfsgfglal llggqqyata eveiyrliah eldlerasvl vwlvlfatat
      241 agllnawfsr qthaadirpi aaqspsslyh killgytlfl lttccalpll aivvqatqag
      301 sawhvlwhed tlsalwntlr fstialfgta vlgilhaaaa raiplfrsit flpfmispvc
      361 lsfgallayp qhagslhlll alyvllaypf vtkdvlatwd alphryfqaa qvfgaspiqt
      421 lwhitlpllr palrrgltfa aatsigefaa tlflsrpewq tlttliyyyl skvgsnnygk
      481 amvltlllmt latlvfvlld tqesrkksva d
//
LOCUS       WP_285076172             270 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285076172
VERSION     WP_285076172.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..270
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30826
     Region          32..147
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mersrvidyy srfdewgrld replefiinm hyiraslpat glvldngagp gkyamelakl
       61 gyrvtlsdlt pgsvdiaqqk akeldltkqf dgfhvldath lngiadeayd aslmlgplyh
      121 lqveeervaa vkelhrvtkr ggivfvamqs rtrmgitslq fpqqwkphdh meairsfvek
      181 gtfdhpdqgr ftgayyfniq dinpfmeqng fetvdligss slramlteeq qqywkeraey
      241 deliqymiea akdpsilgis shllyigrrk
//
LOCUS       WP_285076187             255 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285076187
VERSION     WP_285076187.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..255
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28089
     Region          12..248
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mpelnlgsls tpieailfdk dgtlldftam wgfwthcvmd nfreelaarg lqfnaadiph
       61 iwgtfhdeqg rmngydvrgp lamgtmeevy avltwhgyra glswaeakii vrecllqaey
      121 amnkerpaqp lpgvlafleq crnkglkmgv vtadetenal shlkwmgies ffsvvvgtdq
      181 vgrgkpfpdm lllacerlgv paarvvvigd tdgdmemara agaawkiavg dpahikladl
      241 tvrsfhelle vevtr
//
LOCUS       WP_285076253             302 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285076253
VERSION     WP_285076253.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..302
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35208
     Region          6..300
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mnnrklalmr lmdsrkkfta relaerfqvs irtiqrdlnd lqelgfplyt evgvnggyrv
       61 lpnrilpplq ltqhealglf mmieylenvp dfpygsireh laeeyystlp qdvqdlitrm
      121 rqhitflqhh avqaealtte ilgaavdkke iefiyhsrqg hkkvqavpig iyydhgywym
      181 paqrkdrvll yradrmqelv ilnaidesvp slqewlnfke nresvevvlq ftdfgarlag
      241 sdvlfksveg newrglvppe efpftarkll sygpevkvie plelqqqvre mlerslkqyn
      301 il
//
LOCUS       WP_285076396             421 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Kingella kingae].
ACCESSION   WP_285076396
VERSION     WP_285076396.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..421
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=45700
     Region          9..421
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mkitawigav fllmgtvvqa apdtapeass sklqnirqai datqkdlavk qeahrkaqqt
       61 laqakaalaa aqreltamnr rrevawqrlq klqgdlsklq aeianskaqi arllvanyrn
      121 rqphavalfl knadsnqksr fltytrlinq sndqviqkla vqekelavqe kavndqvakl
      181 qalvneqqqk mqqlgqtrsq aqatsqklnq emassrsrla qlredeqrln svvagimsrq
      241 saqrraeaea rtqaarqrve qaakaqnels eaelaaalpv ikpepkpepk pvesnvgnrq
      301 gnlpmptsgr vagsygstra tggtwnglfi etassgvqsv aagtvayaan lrgfgntvii
      361 dhgdgymsty aglsqiavsn gsrvgarqni gtsgtlpage qglyfelryr grainprswv
      421 r
//
LOCUS       WP_285076461             217 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-L-isoaspartate O-methyltransferase family protein [Kingella
            kingae].
ACCESSION   WP_285076461
VERSION     WP_285076461.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Edwin,R.K., Challa,N., Sharma,R., Satyamoorthy,K., Parsa,K. and
            Misra,P.
  TITLE     PIMT/TGS1: An evolving metabolic molecular switch with conserved
            methyl transferase activity
  JOURNAL   Drug Discov Today 27 (8), 2386-2393 (2022)
   PUBMED   35462043
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Furuchi,T., Sakurako,K., Katane,M., Sekine,M. and Homma,H.
  TITLE     The role of protein L-isoaspartyl/D-aspartyl O-methyltransferase
            (PIMT) in intracellular signal transduction
  JOURNAL   Chem Biodivers 7 (6), 1337-1348 (2010)
   PUBMED   20564550
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Kagan,R.M., McFadden,H.J., McFadden,P.N., O'Connor,C. and Clarke,S.
  TITLE     Molecular phylogenetics of a protein repair methyltransferase
  JOURNAL   Comp Biochem Physiol B Biochem Mol Biol 117 (3), 379-385 (1997)
   PUBMED   9253175
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..217
                     /product="protein-L-isoaspartate O-methyltransferase
                     family protein"
                     /EC_number="2.1.1.77"
                     /GO_function="GO:0004719 - protein-L-isoaspartate
                     (D-aspartate) O-methyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0030091 - protein repair [Evidence IEA]"
                     /GO_process="GO:0036211 - protein modification process
                     [Evidence IEA]"
                     /calculated_mol_wt=24056
     Region          12..206
                     /region_name="Pcm"
                     /note="Protein-L-isoaspartate O-methyltransferase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2518"
                     /db_xref="CDD:442008"
ORIGIN      
        1 mdfnkarfnm veqqirpwdv ldfdlldale siprelfvsq eqqgyayadl plkldngsmm
       61 lepkivarmv qgltlsktdr vmeigtgsgy atavlatlvd svqtydvdeq qlsraqavlq
      121 slnfdniqfv aedgfansqp eakydaiyvg gslpevpeql kqqladdgrl vvvvggepvq
      181 rclqitrngn efsqktlfdt lvtpltakak kpskfqf
//
LOCUS       WP_285076472             270 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A [Kingella kingae].
ACCESSION   WP_285076472
VERSION     WP_285076472.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..270
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=30070
     Region          25..257
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 mstpavayif gqavtdvphd lfippdalqv vlhsfegpld lllylirkqn idvldipmvt
       61 itqqylgyia qidaqqfdla aeyllmaavl ieiksrlllp tpaldatede adpraelvrr
      121 llayeqmkla aqdldtlpra grnfawvylp lelavptrlp evqiadltqa wltilsraqq
      181 nrshavvqev vsvrermtai lrklnagslh fsqlfnpelg aahvvvnfia llelvkeglv
      241 rvlqdthfge ievqaashia dveiierese
//
LOCUS       WP_285076527             425 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Kingella kingae].
ACCESSION   WP_285076527
VERSION     WP_285076527.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..425
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=47788
     Region          6..414
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mkstdilivd deigirevlq etledegytv avaenaeear klrikmrpsl vlldiwmpds
       61 dgitllkewa tnglltmpvv mmsghgsidt aveatkigal dflekpiplq kllqtveral
      121 kygesqtqap mtannlgssa vikelnkqle layrhnnavl llgeagcpfe tvartfhknn
      181 tpwveahkpe hissmpldll ekasggilyl gdisqydkci lqsmgvilgk aerfnvrivc
      241 csstpvnewl nvqsdtrlsn llsgavislp plrhqiedip flagqilrel ssslqeethv
      301 kftsaaynrl rqydwpgnle qfrnviksla lncegnevhd gavtrvlsqf nqnetaqevk
      361 ggfnfnlplr elreelerry fefhiqqenh nmsrvaqkvg lerthlyrkl kqlgisftrr
      421 ggeke
//
LOCUS       WP_285076642              78 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285076642
VERSION     WP_285076642.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..78
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9028
     Region          10..74
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mdfdkvtlhc kldeilkkhn nmsvlklsee ighrrttime llhntnmdkk kisaslivkl
       61 cvyfditpnd lfeirnvd
//
LOCUS       WP_285076878             508 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285076878
VERSION     WP_285076878.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..508
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=56740
     Region          <220..505
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mgslplkdkl pwawlhrwvs prslrsqlla rslfilaall lligilqfwi mesflyrnqa
       61 ktmeeqlmsm ppvwlgtssr sgatnnpfgg qsgsdprgsg nrflyipdrs lalfdnqsgf
      121 edifgedglt aprltsveye nitdqindkh hvpyrivtdn qgneqlivfs spgprnrglp
      181 mvqmgtptkp lkdlivkqll iflmlsllam vaglilytka lrrtliplss mvdtvqrida
      241 gslaerlpav qgqqevdqla lsfngmlerl edsfeaeres keqmqrflsd ashelrtplt
      301 sihgfievlk rgaasnseql ynalnsmyge svrinklved llmltkldqa pqqeqeviql
      361 dslllemqsq lvmmaqqrqv hldltaevhv madahklkqv vlnlfhnavq htdsdrgais
      421 itlyavqhka eltikdngsg iepehlphif erfyrtsssr srkqggaglg laitrsives
      481 yggkitvrsq igegteftil lplveget
//
LOCUS       WP_285076936             221 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Kingella kingae].
ACCESSION   WP_285076936
VERSION     WP_285076936.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..221
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25022
     Region          1..213
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mpiflqrffa wlidqvlyff vsfitgvrpk fegdiafspe kkvyfanhas hgdfvmvwis
       61 lpkpwrklvr pvagadywlk gkirrfviqq vfngllimrn gndpkaitaq mtaalqegss
      121 liifpegtrn tdddvvllpf ksgiyhlare npdvqfvpiw idninrvlpk gklipvpiic
      181 svnigqemql fpgeskdefl qrardamlal apegkrlpap k
//
LOCUS       WP_285076946             221 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285076946
VERSION     WP_285076946.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..221
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=23985
     Region          <1..202
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mkkqfivlgl grfgssltrt linnghevla vdknenlvqe istiathvvq adctdksvlk
       61 elgasnfsha ivaigedlqa silttlllke lnvpkvtaka kndnhgsvls kigadqivyp
      121 erdmatrlgn qlssdniids ielspdynlv eikapesmnq ktlqelnira gygctviaik
      181 tgsnlnispr aedtvrtgdm llligsnedi rilesdyeqk k
//
LOCUS       WP_285076988             449 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 30 protein [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285076988
VERSION     WP_285076988.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..449
                     /product="glycoside hydrolase family 30 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004348 - glucosylceramidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006665 - sphingolipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49883
     Region          3..447
                     /region_name="XynC"
                     /note="O-Glycosyl hydrolase [Cell wall/membrane/envelope
                     biogenesis]; COG5520"
                     /db_xref="CDD:444271"
ORIGIN      
        1 mtklkmykst gedalfvsvs pdqlqpqdsg setttilldd qqtyqemdgf gasftdssay
       61 linqilseeq raevmtrlfh peegiglsvi rnpmgasdya rtvysyndlp anqtdpecsg
      121 fsiahdeadv ipltqkalel npdlklfasp wsapgwmkts gsmitgqlkn ewypayaeyf
      181 vkyiqayash glpihavtpq nealyepghy pgmlmpaeaq adfiknhlkp aldrndiqsk
      241 ilcydhnwdr pdypltvlee ageevdgvaw hwyggeasaq tkvyeafagk evhftegsgg
      301 ewippfeqaf snvirtgiei lrnysksfvl wnmaldenng ptvpgfgkst crgivkvnqq
      361 tkeltytldy yalahfsali rpkavridss sneasirsva fkntdgsiav vlfndgeetg
      421 nvqvqlkeed llsfqlesks alsilinqe
//
LOCUS       WP_285077056             280 aa            linear   BCT 25-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Kingella kingae].
ACCESSION   WP_285077056
VERSION     WP_285077056.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Bagautdinov,B. and Kunishima,N.
  TITLE     Crystal structures of shikimate dehydrogenase AroE from Thermus
            thermophilus HB8 and its cofactor and substrate complexes: insights
            into the enzymatic mechanism
  JOURNAL   J Mol Biol 373 (2), 424-438 (2007)
   PUBMED   17825835
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..280
                     /product="shikimate dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29961
     Region          4..276
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 mlingrteii ahigypthtf tspmiynpyf adaginalvv pmgskaedya eflpavfkls
       61 niigalvtmp hkvttaqmlg vdritktaqi agavnavrlg kdgklegdlf dgegfvrgik
      121 nkgfepkgks amvvgnggvg saiaaslaaa giarlalfdv neessrklga rlqehypnlq
      181 leyasndptg fdllvnatpm gmkegdpmpv dldkvssqtf vgdvvlksep taflqacqak
      241 gctiqvgvdm lfeqipvyle yfnlptttaq rlreladiry
//
LOCUS       WP_285077089             453 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285077089
VERSION     WP_285077089.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..453
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50680
     Region          <163..448
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtgslytrvv ltflvsvigg tilsflattw ifqdklnenl qgslldfgqd ivriyetlpl
       61 reaemfisem kqlnsyhiri ykatgqfqsy gelkgqhpfl vtteqvkkvl dggrvqvngi
      121 dtiflglpik temgsiamfv epltssstsf likfvvtfli csllagslli liaaiflvrp
      181 ikklteatrl iaagdfsvkl nikqkgeigt larsfeemmh dlqqleqmrr efvanvshev
      241 qspltsisgf aialkqvdip dderssyldi iitetarmsk isdsllklsl lesqslqmrl
      301 atlsldeqir rvivaiqpqw sarniqfdld lqpakitadh dqlnqvwini fgnaikfsee
      361 garisirikq niknvticis dsgigilped qkrifdrffk adrshsqkye gsgmglaivk
      421 qivslhqgdi rveseygrgt tfivilpitt pte
//
LOCUS       WP_285077114             416 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285077114
VERSION     WP_285077114.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 416)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..416
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45005
     Region          40..409
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mvkkwsliil sllvvialsa csgnggnsse sqsgtkdkgk itfafwgaqs eadaikqaid
       61 nfetnypdiq vesqwiqkdy ltklqtmiag gttpdvmlis ggdlpgfana fqelkmdksl
      121 fsspslvdsm svdgityaap fiikpkvmai nvdlfeknni plpsktepmt ieqfndiakn
      181 ltsgegaaki fgseplwlgn wiyafggqfy sddlsksald speaiaaaey ivsskqagiv
      241 pndsekqgqs mmnwylggri gmftdfgpwy lpqmadvqkf kwdivpfpgn ggskevngla
      301 lskdsknaea aktfinhltq neevqkiigg nknaygvpvi ssatsafeav spdknlkafv
      361 laaekqhtqe aqkgtneinn vmkaiddttp igignkdvke vfpqvaekin qilqqn
//
LOCUS       WP_285077157             309 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285077157
VERSION     WP_285077157.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 309)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..309
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34823
     Region          8..92
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mlelsfdnpd elvtvthals trsrvdilrl lisqnlnive iaealklpvs tvasnikvle
       61 aarlintell pasrgamkvc srnyddihia lnlekaipkg diqvyevdmp ighysdcevs
      121 ptcgmangeg miiredepas ffhpkhvgaq imwfrkgyve ylmpleipge avieslelsm
      181 emcseapnyd hnwpsdisvw ingveigmwt cpgdfgdrrg klnpawwfew stqygllktw
      241 rvdknkttld mekisavdld qlnlqnshkl rvrigikpda vhqggvnlfg rqfgdydqni
      301 kmtvhyaih
//
LOCUS       WP_285077213             106 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285077213
VERSION     WP_285077213.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..106
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11065
     Region          3..106
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mgayfllgla ivsevfgssm mklsngfqkk lpiiglilgm staffclsla lkiiplgtay
       61 atwsgvgtal talvgivfyk esvnirkisa liliiagvvi mklahs
//
LOCUS       WP_285077215             116 aa            linear   BCT 25-DEC-2024
DEFINITION  DMT family transporter [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285077215
VERSION     WP_285077215.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..116
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11998
     Region          3..107
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mkgyfalgia iitevfgttm lklsegftnl lpsiglvvgm slsfyfltmc lktiplstay
       61 aiwagagtal tallgvilwn dpfnilsgig lilviggvvl lnlskspvks snasqs
//
LOCUS       WP_285077375             197 aa            linear   BCT 25-DEC-2024
DEFINITION  YdeI/OmpD-associated family protein [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285077375
VERSION     WP_285077375.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Pilonieta,M.C., Erickson,K.D., Ernst,R.K. and Detweiler,C.S.
  TITLE     A protein important for antimicrobial peptide resistance,
            YdeI/OmdA, is in the periplasm and interacts with OmpD/NmpC
  JOURNAL   J Bacteriol 191 (23), 7243-7252 (2009)
   PUBMED   19767429
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..197
                     /product="YdeI/OmpD-associated family protein"
                     /calculated_mol_wt=22907
     Region          7..197
                     /region_name="YdeI"
                     /note="Uncharacterized conserved protein YdeI,
                     YjbR/CyaY-like superfamily, DUF1801 family [Function
                     unknown]; COG4430"
                     /db_xref="CDD:443542"
ORIGIN      
        1 mttnktnpkv dgylnkakkw keesvklrei ildcgltedf kwmhpcytle nknvviihgf
       61 keycallfhk gallkdkqgi lvqqtenvqs arqirftniq qivemenilk eyiqeaieve
      121 ktglkvtlkq htdydvpeef qhqldenpal keafealtpg rqraylfyfs qpkqsktrvs
      181 rvekytqqil dgkglnd
//
LOCUS       WP_285077414             543 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Kingella kingae].
ACCESSION   WP_285077414
VERSION     WP_285077414.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..543
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60200
     Region          25..316
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mltytsrpkr peptheypwl llllafcwlw pgvfshdlwt psepnmmlai ddaaqrgawl
       61 ptvfgaayfd vsplyvqtaa wfkmllspwa adafsaarft svlftslgll gsgmagyrfl
      121 grhhgrsvvl iligsvgilp iahflgaysp vfagvglamw gfsiaqrqvm fsailvalgt
      181 mllaqslgll aalamllvas llpfsphwhn qrytvalvam waisspllav ypialaivep
      241 aafavywqqh ifgsfgginq vqaafslhyy lqhllwfafp alplaiwtrt rqsfratpag
      301 vlmatwlavf ggflllnpeq hqdllvlllp plalsgaaql dnlrrgmaaf lnwfgialfg
      361 caavflwigf vamnygfpak laeraayfsp yytrdldimp ilvallftpm wliaitrkri
      421 rgrqavtnwa agttlvwall mtlflpwida akshrpviqq liqavpdvah anclyidprd
      481 ktarlawqqy gtgaytiqnt scrytlaqyn prnevapagn ivwqgkrprs ktelfvlihn
      541 gge
//
LOCUS       WP_285077465             276 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Kingella kingae].
ACCESSION   WP_285077465
VERSION     WP_285077465.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..276
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=30118
     Region          54..275
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mirrilpilv lailisacgs etpssqnsnn saapvasaan vatsptanpn metllvgsev
       61 lyepfefkde hgqpqgfeie mmteiakaad mniqvidvpr ntaettlnsn kyqvfisams
      121 rsperlekld mgepyleyeh alyvldtpen anlrtiedfk gkniavhkgs sgniakikew
      181 eanpvlsdsf flslkntsad kadatlgdsr vmqyyltknp gvkarlimir dgktgisfav
      241 kkgnttllnk lndglakika ngtfdaliik wfgske
//
LOCUS       WP_285077472             709 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285077472
VERSION     WP_285077472.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..709
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=77142
     Region          68..400
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkprevtklk msvrrarkrn tiaavtlmlt ilapmsamaa paamnnsinl tyettkktvi
       61 ekaklltety gttslqyali dggeitvsgq tgkndlndkv pltsntiygi gstskmmlta
      121 avmklvdegk idldvpvvny mpdftmkdkr ykqitprmll nhsaglfgts vgsailygdn
      181 dtyahdtfld qlatqnlmak pgaysvysnd gftlaeilve rvtgmsftaf ihknfteplk
      241 mnhtktpqdi vntgemagiy spvykgqlpr enyniiasgg lystakdlvk fsqiftgevk
      301 gilsnksvea meqkeyrrgm wpedsdssms yglgwdsvdl fpfsdygika vtkggdtlsy
      361 hsslvvlpey nmaaavissg gasitnqfia selllsalee kgiikerkpe ksfgvpvkad
      421 mpkeiskfag nyggnnsvtk ikinkagqmt lssltapsnp vqeytytsdg tfvsddgtek
      481 lkfvvekngn tylwsrsyis vpglgqvals eynaeklkan tlpkeinaaw akrdgkkyyl
      541 vnakytsmly lnatsilpiq lnkenpgyms nnkiigagea anqlqipgsa grepmdihfs
      601 kknggeyltf sgyvfasegl vkpiysgkqs attiqadgya kwfsvpatak gkvmtvklpa
      661 kgafaiydqn gicinhsvvs gknfvvlpen grivfageag sqfeitlkk
//
LOCUS       WP_285077524             264 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285077524
VERSION     WP_285077524.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..264
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30293
     Region          7..250
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(24..25,27..28,31..32,69,73..74,77..78,108,112,119,
                     122..123,128,144,148..149,151..153,155..156,159..160,
                     163..164,188..189,191..193,195..197,199..200,202..203,207,
                     210..211,217,219)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(147,151,154..155,157..158,202,205..206,208..213,
                     216..218,222,224)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(168..175,190,193..194,197)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mqlsfphret wlhavnpglk mtfltllfvf vilihnlnvm anvavvmlll lvwtghpwpr
       61 lllyaspfil vfiststgmi mfgkgettwf qwglihitee nfyrglhlgf rslsmaaagl
      121 lfglttkpvr lfyslmqqwr lppkyaysfl aamrmipill defqtllyai rirgtrqrgs
      181 rwnvygilkr yaipllaqsi rraqrmavam eakgfkeggs rtfyvqigys qadvwfvgyf
      241 iimltaayll gitfpynstv vdvr
//
LOCUS       WP_285077577             255 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285077577
VERSION     WP_285077577.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..255
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29690
     Region          26..247
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          161..244
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mhkplehylc gkfisegnws hmkrsmpvhe vilmlegely iaeedeqyvv randllflra
       61 grthygyqfs dapvsfywvh ydsnekefdq ypthatiqvp smanqlfkql lhsssfspee
      121 avaalllllk elerntqagy rphnaivdhi ckwvdihlht ditvgkiaet fnfnkdyisk
      181 mvkrekgigl ktyilterir rakqmllntn asvkeiagqc gfsdyklflr mfkqyegntp
      241 teyrnnlyst qlnrl
//
LOCUS       WP_285077626             179 aa            linear   BCT 25-DEC-2024
DEFINITION  KdsC family phosphatase [Kingella kingae].
ACCESSION   WP_285077626
VERSION     WP_285077626.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..179
                     /product="KdsC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=19328
     Region          9..178
                     /region_name="KdsC"
                     /note="3-deoxy-D-manno-octulosonate 8-phosphate
                     phosphatase KdsC and related HAD superfamily phosphatases
                     [Cell wall/membrane/envelope biogenesis, General function
                     prediction only]; COG1778"
                     /db_xref="CDD:441384"
ORIGIN      
        1 mfnhvapdil praqavklli mdvdgvlttg qlfiastgei ikpfntldgh gikmlqktgv
       61 qtaiitarnd pavaaraqsl gishylcgid dkrmayeqlr yqlglsakqc amvgddvidl
      121 pvmvrcglpi avanahifvq qraayttqky ggmgairect dlimhaqntl qaalneytq
//
LOCUS       WP_285077729             557 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285077729
VERSION     WP_285077729.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..557
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=61347
     Region          10..541
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mtsitttssf dimvtsdlhg airpihyntn ayrpaglall aslirrqrer spelllvdng
       61 dllqgsplas yaasfvsdhe vhpfinvlne lgydaavmgn hefnygqqll rkavedshfs
      121 wlsanivveh qddtimnhln egkhdqeirp vapsgtgipa fgppyliktl ssgvkiallg
      181 atthyipnwe hpknieglhf ldaletiraw vgyireheqp dvlvvsyhgg fesdletgep
      241 aerltgenqa yaicrdiegi dvlltghqhr qltadihgvt viqpgfsgng vghvsvqleq
      301 langkwwiag kqarllllde nsdvqpdaav mkltdeleak aqawldqpig evagdlsiad
      361 paalrlaahp fiafvhqvqm eatgaqisnt allseeargf gslitvrdvl snfiypntlt
      421 vlelrgqdir daleqtaryf evessgeviv npaymqpkpq hynydmwagi eyeldiskpa
      481 gsrvvklere gipiamdaty svvmnsyraa gggdyamypg kkvlhegatd maalvedyir
      541 rhqpltveqa nnwrvve
//
LOCUS       WP_285077712             447 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285077712
VERSION     WP_285077712.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 447)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..447
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48482
     Region          48..446
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(159,161,307,309,337..339,379)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrakskrlfn vwalvlatmv visgcgnggs senadstdsg ssqnepvtit ysqwgtaeel
       61 hrtqelldqf mkantdikvk legkdwgsyw dgltanaagg tlpdvfktsy ayvekyaelg
      121 ifkeldglla enqfdlnnvd ksllglhqye gkqvslpida nvivwyynka ifeneatnph
      181 kapvpslept wdeitdiatk ltldkngksa deagfdagni vqwglsispg stmdwflepe
      241 lwsngaklvn ddgslaletp eamevlnyfi dmtknkkint tpaqieglgg qvnlaittsk
      301 vamnpggswn ttnyqeagvd ygisylpkfk tnqtvvqpag laissntkhe eaaykllawl
      361 agpegqtela kqgysipank aaadayiatv gednkiflda qqygivspft tkktdlvwty
      421 geqslklpla gdgdlnaalk dlaskmq
//
LOCUS       WP_285077874             295 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285077874
VERSION     WP_285077874.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..295
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33654
     Region          40..291
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          212..291
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mldlkalhen tridhkshpf qlfqnrcqgm kteecilylh whehfelifm rkgsalfhid
       61 srpyvaqage viiipggalh vgyaleegdi nydsvvlnsa lfhdfthdpv hlkyvapyle
      121 gkvrfpvkpa eqnivcqgyy slldeaieem asqppayqlv vksklhalft llartfmphq
      181 lsdktaqsyf pnrerfkhli eqieaeptgk msvteaagqv glntyhfckm fkkltgrtfv
      241 eyvngcrmtk aeqllqessm titeiaaqvg cenanyftkl ykqykgmtps qgrlk
//
LOCUS       WP_285077927             119 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Paenibacillus
            sp. UMB7766-LJ446].
ACCESSION   WP_285077927
VERSION     WP_285077927.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..119
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13432
     Region          19..110
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msetcvptgv alkdtgfgyt lslvsgkykm vilywlaenk vmrhnelkrs igtisfksls
       61 vmlkemeedg lvirqeypqi ppkveyslse rgrslmpllh mmcdwgeanm vsdpesvqr
//
LOCUS       WP_285077883             564 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285077883
VERSION     WP_285077883.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..564
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=63211
     Region          67..564
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mkhllpdlms llrtdmsild sglcmpvips ttgladaipl fntspylliq ddgpslgyia
       61 vsdvlqemmh ahrlmeayfe ttletagsal tlinedakvt ywtsgaehvf sinkkdiigk
      121 paadffppdr lqslktlytg etvyrkqhqp rpdlfalina rpvqldgriv gavaaevdit
      181 teirlhqell hmtskvqhle kavarlrpds dpfarikgss pvinqcleti rkisttsatv
      241 lilgesgtgk elfakaihdl repqtapfia incgaipgsl feselfgyek gafsgadpkg
      301 kkgkielaeg gtlfldeige mplelqvkll rvlqeksyfp vggtrmkqan criiaatnqn
      361 llgmiarnqf redlyyrlnv inlvipplrm rkediyeltq tflqefslly nrhielvppe
      421 vfkllfhydw pgnvrelrnv ieritilttd gevkpeylpd tfmspmeqeq silqetvqlh
      481 sqtelessls pisrstdtfa psdkseides tdssnlsyqq rldiyesell lhylkaaggn
      541 krtlarqlgi sratlynrmk rlgl
//
LOCUS       WP_285078008             443 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285078008
VERSION     WP_285078008.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..443
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=47941
     Region          1..430
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mniavigtgy vglvsgvcfs eignqvicvd nneakvemln egnvpiyepg lkelmasnmq
       61 agnlsftsni aeaisqsdii fiavgtpslp sgeanlsyve qvaieigshi esykiivtks
      121 tvpvgtndrv relississq pfdvasvpef lregsavkdt lnpdrivigt dsdraiktlk
      181 klhrpltenl iitdirsaem ikyasnafla tkisfineis nicekvgadv trvaegmgyd
      241 krigssflra gigyggscfp kdtqaliqia gmvdydfkil ksvvkvnqeq rfhvihklee
      301 algslkgkti avwglafkpd tddvrdapai diiqqlseag amikaydpia tdnfckevna
      361 vsitweenpl eaakgadalc vltewkefvh idlaeladlm ndpvmidgrn lyspeqiras
      421 rlqyysvgrp gltsakgkta aii
//
LOCUS       WP_285078123             252 aa            linear   BCT 25-DEC-2024
DEFINITION  tRNA (adenine(22)-N(1))-methyltransferase [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285078123
VERSION     WP_285078123.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Hori,H.
  TITLE     Methylated nucleosides in tRNA and tRNA methyltransferases
  JOURNAL   Front Genet 5, 144 (2014)
   PUBMED   24904644
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Roovers,M., Kaminska,K.H., Tkaczuk,K.L., Gigot,D., Droogmans,L. and
            Bujnicki,J.M.
  TITLE     The YqfN protein of Bacillus subtilis is the tRNA: m1A22
            methyltransferase (TrmK)
  JOURNAL   Nucleic Acids Res 36 (10), 3252-3262 (2008)
   PUBMED   18420655
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..252
                     /product="tRNA (adenine(22)-N(1))-methyltransferase"
                     /EC_number="2.1.1.217"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0160105 - tRNA
                     (adenine(22)-N1)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27498
     Region          2..246
                     /region_name="TrmK"
                     /note="tRNA A22 N1-methylase [Translation, ribosomal
                     structure and biogenesis]; COG2384"
                     /db_xref="CDD:441950"
ORIGIN      
        1 mklsnrlqri hdqipegsrl adigsdhall pvaavrsgka asavagevnp gpyeaarkqv
       61 sdaglkerit vrrgdgldvi sagevdvvti agmggalias ildrglskld evkllilqpn
      121 vgedilrrwl lehnwvvvae qlleedgkvy eiitampqel spianeevyr arpleggvel
      181 tsdlllrmgp yltdrptdvf fakweseivk lqsvvqsisk sdqessreka aevehlivnl
      241 kevlsclpkv kr
//
LOCUS       WP_285078209             239 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285078209
VERSION     WP_285078209.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 239)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..239
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25870
     Region          1..>181
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mktylvfgas kglgdafvrg vpdqgdkvwv vsrtepdnlk lndgveriwi qadlsdlnaa
       61 tlvvdklqne aldvliynvg iwekegfedh ytfdkdtpad isnlihvnit saivciqall
      121 phlrqstagk iiligstagl snanssqvsf vaskfairgv tealrehtrh driavtcinp
      181 gelaaevpyk dgidralsey ngtriplqdm vsivkcivsl skaacvkein ipaitdina
//
LOCUS       WP_285078295             706 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD-IIIC family phosphatase [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285078295
VERSION     WP_285078295.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 706)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 706)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..706
                     /product="HAD-IIIC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=82570
     Region          187..545
                     /region_name="FkbH"
                     /note="Predicted enzyme involved in methoxymalonyl-ACP
                     biosynthesis [Lipid transport and metabolism]; COG3882"
                     /db_xref="CDD:443090"
ORIGIN      
        1 mtiaeentrk lvitstfesd pivphmewwa ermlpfklnv tlhkqrmlpd llyprsqfmn
       61 sfdyrvvfnr fedwirdddh mmepqkcekl eyafketlna iesasqkeal ivaifpiste
      121 aglsntlfsy itelnqrwrd alsgisgvhl vdfersqkly vienpfdyvk dnlaqmpfsq
      181 sfdavmgayl irqlhalnnq kfkvivldcd ntlwegicge nqlnvgidmp fqslqqtmis
      241 kmeegmllci tsknnesdvw nvfenhkdml lqkkhfvswr inwkskaeni reiaqelnlg
      301 mdsiifidds pheclevmnq lpevltlklp kdkmqipafl shvwaldkll itnedrkrtq
      361 mqltnvqrkt letkspedyl nelglqlymd vadssmiprl aqltqrtnqf nstiirrsek
      421 emyelmqdrn yvcwaievtd rfgsygltgl iitkmmheal iidtfllscr vlgrgvevav
      481 fsllkkfcle rqltkielvl ingdknkaih qfirdndwme hevvhegerv itipvsripd
      541 evshivcvyg qglddeylen vepaketesk seciesvgew difinnekel thaeqyipll
      601 hsqptelkfl pmesrrvehv qqeglselek fvenamynvw genavswndr lnlnseevwh
      661 kfaflseiyq kfgvvlpeek weefitrgdi idflklelrg mdpyyv
//
LOCUS       WP_285078343             410 aa            linear   BCT 25-DEC-2024
DEFINITION  CynX/NimT family MFS transporter [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285078343
VERSION     WP_285078343.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..410
                     /product="CynX/NimT family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42915
     Region          29..405
                     /region_name="MFS_NIMT_CynX_like"
                     /note="2-nitroimidazole and cyanate transporters and
                     similar proteins of the Major Facilitator Superfamily of
                     transporters; cd17339"
                     /db_xref="CDD:340897"
     Site            order(39..40,43..44,47,79,128..129,131..133,136,155,
                     158..159,162,236,239..240,243..245,248,275,279,328..329,
                     333,337,354,357..358,361..362,365)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340897"
ORIGIN      
        1 mpsslqqnsp nqsavdnsss asmklgllla giiviaatmr spitatgpiv dlirtdtgis
       61 htmaglltsl pllafaaisp fapklarrfg letalltaii lvtvgvalrf ipsvpvlfag
      121 tailgcgial snvllpslik rdfplrvglv tglysvsmni wgaiasgisv paagltsmgw
      181 haslgmwail silalilwlp hvrsgrrgev yvasrketkp vrlissslaw hvtlfmglqs
      241 lifyttitwl pevlsdqgfs sssagwmlsl mqmvsvpvtf ivpilagrmk dqrgltaitg
      301 sclilgyafl lsgisslvtv gvtlagvgag asfglvtmff vlrtadarqa aglsgmaqsf
      361 gymlaafgpl lfgvlhdwtk gwtlpllvqv ilaivlliag ikasknrvig
//
LOCUS       WP_285078452             244 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285078452
VERSION     WP_285078452.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..244
                     /product="metallophosphoesterase family protein"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27457
     Region          3..218
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 meriaivsdi hgnmtaweav lndirsrglk rifclgdlvg kgpdpvqvvd lvretceqvi
       61 rgnwdelvav nsdnenftwq akrlgkerlt ylkslpfshq lelsgrkirl vhaspqsvyh
      121 rvqpwdeigk rlamfdppad epelgvadvv gygdvhnafl qflngkmlfn agsvgnpldl
      181 tqasycileg enssdrntpf nlqfvrvpyd ieqevqtaqq aqvpsldfyi relrtgvyrg
      241 lqtd
//
LOCUS       WP_285078449             257 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285078449
VERSION     WP_285078449.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 257)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 257)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..257
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28128
     Region          2..254
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mlkdqvvfit gassgigalc aqmlieegai pilaarsrdk leeigaslkg qhelltldvt
       61 ndeqvqtavn amlqkygrid illnnagygk faamtdmsvq efdemmdvny mgivrctkav
      121 lpqmlqrgrg qivnvasmag kigtaksasy tatkhavlgf snalrqelrk sgvtvttinp
      181 gpidtpffqr adpsgnyvnn vrwmmlkpee vaghmiramk krkeevnlpr lasagvwlyq
      241 lfprladrls hgvmnqk
//
LOCUS       WP_285078786             183 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285078786
VERSION     WP_285078786.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..183
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21300
     Region          82..160
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mkqipaawns drlfmsdlke seifdiqyiv gtssyvqewd grdhepdyvr tcfekgdlpp
       61 ggrlenyriq tirtskenks igvlslyhgy pkedsvylef lyihsetqkq gygqemmhal
      121 tqlfselgym eirinvalkn wpalrfwtks gfdqisriyg dlehsdktfa nmelikalkt
      181 hdi
//
LOCUS       WP_285078763             275 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paenibacillus
            sp. UMB7766-LJ446].
ACCESSION   WP_285078763
VERSION     WP_285078763.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..275
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30371
     Region          17..266
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mirgltragl gniesneqyi tnaakygfqs vdlnplsliq evgqeqakhl lesnqviigs
       61 sdltvdwrtt deqfreglqs lvqmaeaaas lncyscctyi lpstdqpaas fmaaatrrlr
      121 lcadildayg irlglefvgc hhlrtqwknp fiwsvgdtld wietihapnv gllvdsyhwh
      181 tnglaieevl nlkkeqvvhv hindaydlpi eelldyerly pgegvidlpg flknlqaigy
      241 tgvvsqevla pastldtsel fakskagfds vfaki
//
LOCUS       WP_285078792             300 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285078792
VERSION     WP_285078792.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 300)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..300
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33828
     Region          2..97
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mikangeakf iplyealase vrwrimdlia dsemnvkdia aalelspsiv tmhirkleqa
       61 glidsrrirl nggthklcfl kqnnieielp sanrtarire qtisvghyta fevhptcglg
      121 thekeigvwd dpryfldpel vhaailwfgr gyveyktpny mlpdetasti eisveiasea
      181 pglrdhwpsd ilftfngisl gtwtspadfg raargkytpt wwhrnvnqyg llktirvdds
      241 gtymdgerms dvtiedikle epfwtlrftv deeganvggl tlygsgfgnh dqdivirvqr
//
LOCUS       WP_285078867             442 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidase U32 family protein [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285078867
VERSION     WP_285078867.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787090
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..442
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=49947
     Region          19..342
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
     Region          360..439
                     /region_name="Peptidase_U32_C"
                     /note="Peptidase family U32 C-terminal domain; pfam16325"
                     /db_xref="CDD:465094"
ORIGIN      
        1 metvavkrkf sgkrnrldkp ellapagnle klkfaihyga davyiggqay glrsnadnft
       61 feemregvef akkygakvfv atniyahned iegiqaylqn lydagiaaii vadpaiieva
      121 qravpglevh lstqqstlnw qavkfwkdeg lprvvlgret sfeeieeika nvdieieafi
      181 hgamcssysg rcvlsnhftd rdsnrggccq scrwkydlfe daregtvwvs eeemqmqapa
      241 pfklgenqlp lfqeqdnsfs mgskdlcmig hipelidvgv dsfkiegrmk sihyvatvvn
      301 vyrqaidsym adpenyvlkp ewveemnkaa nrplntgffy dtpdhedhiy epeekavpyd
      361 faglvidyda ttgmatiqqr nhfkpgqeie ffgpgghffk qvvgelqdee gnvldaarhp
      421 lqrvkmkvdq pvsyfdmmrk kk
//
LOCUS       WP_285078864             602 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Paenibacillus
            sp. UMB7766-LJ446].
ACCESSION   WP_285078864
VERSION     WP_285078864.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 602)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 602)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 602)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..602
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=66142
     Region          4..598
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mhvqlkrriy itcilltivf gllmfrlawv qmvqvnrtmp gfqrtvrems vlqrergvml
       61 dtgrgqftdy kgvpltgele wgvvlfphtd qsnhsypsst ahskikelaa llhtdvkslq
      121 kewnqgnaph fwtggtdqpi tlteaqltrl relkadgasv ypimtrygqg atgmqwlgyl
      181 aeqpgsihgh prhknevkqp famksgaagl ektlepllmg igptlvsrmv tgsgevipsi
      241 qprviapsnt hyplraetti nidlqqgieq ivkksgmkeg avvvldaana dvramvsapf
      301 ynpqhvdpqq tawanravqg avpgsifkiv taaaaleyqa vskgetfhcg gewgkyglsc
      361 wkehghgtln leqgfaescn ivfaetarrl smgqlertad alglarpigw egkqvagmpv
      421 lhhfdhedag rvrlpsvspq degakvqtai gqrdvlvtpl qaanlivtll hegkvtaprl
      481 vqriryadgd mmldmpmhds pssagrispa tahqllswmk kvvsdgtgks lqharwqvag
      541 ksgtaqvqqh rekrnhqwfi gygptekpqy avavlvqnvv pssrhqatai frkvmdylae
      601 ss
//
LOCUS       WP_285078897             728 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285078897
VERSION     WP_285078897.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 728)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 728)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..728
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=82600
     Region          1..703
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 msdsfqsayq eeeyrlertm kevdsqlerl hnipvytghd fteqvleagr eerrtalsks
       61 aqqpyfgrld feeegsgark plyigkigvd reevgehplv idwrapvasl fysftggeas
      121 atyeapegli eglvylkrnv virqrilerv adtynrdsdq pavsdeflvy rlgenkdnkl
      181 rdivstiqae qdqiiraarn taliiqgvag sgkttvalhr lafllyqyke qvsaekmvif
      241 apnhmfldyi sdvlpelgvg diqqrtfpdw amnllgldqp ladtsetlnt wfetpdarpe
      301 lnddvpgryk gsirfmelir ewlsgmeees vpdmdfspwd gavlrkaeie nwfgeeykhy
      361 plakrkervm arihrwieme lkkpspeavr kerkkkaatr ekayakkwpq yepltlykql
      421 fkvvkggsvp aslsalipkl vmkqtaadlk qdiireedlp alvyihtlvh diegserfdh
      481 ivideaqdfs pfhvalldqf vkghsftilg dlsqgiheyr gvhawdemss lfpeeqnayf
      541 altrsyrstm eiidyantil ergvksgita ipvfrsgdpv rtlsygekgr tasleqalkl
      601 ltvkdyrtvs iltrtlheak elhhelqaag welnlidggk kqytgghsvl pvylskglef
      661 davivadade khylpnagda kllyvgctra lhelwlfhag plpdyaaath nsegesvaiq
      721 gwpdsese
//
LOCUS       WP_285078964             356 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285078964
VERSION     WP_285078964.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..356
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39835
     Region          20..322
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkdlqscvsd ytkdkkhlql vigivregdv eyysfdnnkk krlippenkl feigsitkvf
       61 tsilllemer ekllssddvv gkfvqnvend ylnkitlrsl athtsglpil atnhnlakkr
      121 snpysmyteq dltaflsnad ytdsmgsfgy snigvgllgy ilckvsgsty ddllkkyits
      181 plrmnetavm lnseqngrfl nghastgkrv phwdlaiheg aggikssvrd lslfvqanlk
      241 ddspiaatlq kshlpiwigd snryfgwged qlldkgilwh nggsagfnsy lafnkelrvg
      301 vvllsnysff snslidnyvd qlkkwitkke psqgtmidft gkkileeimq seaslk
//
LOCUS       WP_285078932             725 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285078932
VERSION     WP_285078932.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 725)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 725)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 725)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 725)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..725
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=82733
     Region          1..725
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mgieqlleka gayikepdlv rireayefad qahhgqtrks gepyilhpla vadivvnmqm
       61 dtisiiaall hdvvedttvs leeirnhfgn tcamlvdglt kleriqfrsk eeqqnenyrk
      121 mfiamaqdir vivikladrl hnmrtlkfqs eesqrrisye tleifcpian rlgisaikwe
      181 medialryln pqqyyrianl mhkkraereq yidtvmdgit skldemgiqa dlsgrpkhiy
      241 svfkkmttkn kqfneiydll airiivdnik dcyatlgiih tlwkpmpgrf kdyiampkan
      301 myqslhttvv gpngeptevq irtwdmhrta efgiaahway kegaangnnf edkitffrei
      361 lelqneaqda sefveslkmd ffsdlvfvft pkgevielpt gsvpldfayr ihtevgnrti
      421 gakvngrivp ldyhlktgdi ieiltskhsy gpsqdwlkia kssharakik qwfkkerree
      481 nvekgrdsce relkrmgldp sawmtddklq eaakkyafnd iedmlaavgf ggitaaqivt
      541 kateklrkeq eessllelns emrelkpape rknrptngir vkgidnllvr farccnpvpg
      601 daiigyvtrg rgvsvhrsdc pnipsstdgd eaarvievew eenieanysv dieitghdrn
      661 gllnevlqav sesktnisav tgrtdknkla lvhvtilirn tehlhsvver ikrvkdvysv
      721 hrimq
//
LOCUS       WP_285079013             411 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285079013
VERSION     WP_285079013.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..411
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44188
     Region          1..404
                     /region_name="FucP"
                     /note="Fucose permease [Carbohydrate transport and
                     metabolism]; COG0738"
                     /db_xref="CDD:440501"
ORIGIN      
        1 mkkllwigcl syfliglahv vlgsilpval ehygkdysqg gtlifaqfag flggvllspw
       61 lnnrfgkrgg lliaaallci aelsymllpp wgwmfviapa agfgfgmiea vigtiiiaai
      121 kdntavamsr levlfgigam vmpliasgli sagywrmsfl vvaacaamtf ifwakssfge
      181 ldselsrrss gqtsghapva espdgtnppd mkptrstyqg cnlallslfv lffflyvgte
      241 mslanfmpai liekmnmkea gaalsvtcfw iamsvgrlfa gyiaerfqyr vyvlysclaa
      301 vvllmifpft nqiwsaflii lllglalsgv fsialvfask mlpgteestp siliasggvg
      361 gailplvtgw sldhlevnqs awmlaifavg llmisviayq wqrrhtvssa s
//
LOCUS       WP_285079151             257 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285079151
VERSION     WP_285079151.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..257
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29707
     Region          <27..82
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mggekqstil tellkyitrn nllpshlaek aginsgafsr imsgsqtisv kildkvsvim
       61 glnpgelyeq yvdeliides tdwrrlkpfl ircselgkls cieriigfim ekqqyipllf
      121 evaeslenke aaiflfqkva daeryqhser laiaqyrifk lmlsddqdnn lecaiqfepf
      181 iarlneseql dafkdlanly lslrrwekak ylvgemkrls sylyeqkhlr ikknkqftep
      241 qkplfgyily anvrgtc
//
LOCUS       WP_285079371             124 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285079371
VERSION     WP_285079371.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 124)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 124)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..124
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14024
     Region          32..108
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(36..37,39,42,45..46,49..50,53,84,103..104,106..108,
                     110..111)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(37..38,42..44,58..60,69..72,74..75,78..79,81..82,
                     88..90,95..97)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(58,61,103)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mfmkdsceiy cydepkvrkv qkaleqqdik smskmfkvla detrmkiafa lceedelcvc
       61 dvanitgasl atashhlrsl kqlgvakyrk egklafysle ddyvrqlvhl asthseelmt
      121 hatt
//
LOCUS       WP_285079426             304 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paenibacillus
            sp. UMB7766-LJ446].
ACCESSION   WP_285079426
VERSION     WP_285079426.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..304
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33885
     Region          1..294
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mklsvftvat pdltadelas aaaaagiegi ewryrgipad alseepsywr hnrcsidpdq
       61 weeqvpafre aakkhgrqsi alvpylncgd llateqafqs aqalgastmr vgvpgydrkt
      121 sypelykqav qylsevqema qqykvkavve thhqtiapta slayrlvqsl dsqhvgvlyd
      181 pgnmvhegye nhrmglellg pylahvhvkn agwfkdasnm dsnssvneqn teisiasawh
      241 cqwtpltegv vnwlqvfrdl ksvgydgyyg iedfsgvles kamlqhfadv faeierrvde
      301 evqv
//
LOCUS       WP_285079374             124 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285079374
VERSION     WP_285079374.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 124)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 124)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..124
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14007
     Region          32..108
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(36..37,39,42,45..46,49..50,53,84,103..104,106..108,
                     110..111)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(37..38,42..44,58..60,69..72,74..75,78..79,81..82,
                     88..90,95..97)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(58,61,103)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mfmkdsceiy cydepkvrkv qkaleqqdik gmakmfklla detrmkiafa lceedelcvc
       61 dvanitgssl atashhlrsl kqlgvakyrk egklafysle ddyvrqlvhl asthskelmt
      121 hatt
//
LOCUS       WP_285079483             908 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285079483
VERSION     WP_285079483.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..908
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..908
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=99252
     Region          18..195
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <441..903
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 marrkkrkkk aaafsgvlky eiygivlitl avialsgeat vgrslskmfg lmlgkfyfai
       61 pligiyyglm vmihrkwpsg wttrktglvl lvfaltlmst vsamhqklip vgalepgavl
      121 tqihndmqte lltpaapger dsmlnkdisg gyigaaqfal flwlfgslga rlimivmfii
      181 sfmlitnlsy vdlirifrtk iwdagsamyk rlearpatra asssagkksg nirkvvpvpv
      241 vddeedddde mhdqqlpkrk spiffqlfgk wgsdrermka ereldqddss dtehvvyrae
      301 qenladawqd gpiiasdtta paavavqsrt ssapiirdff ehvraedask dddlddaypf
      361 pddltvnmqg eelpikvsde ildtnewaet anagadvmda vdgisdvest lsnaaqgsdt
      421 egqevqpvkp ppppkpyklp sfrllskpnn ggksgdqkdy mqtarkleat lesfgvrakv
      481 levvrgpavt ryeiqpdigv kvsrivsltd dialalaakd irmeapipgk saigievpng
      541 evsvvtmrev metatfqdae skvtiafgrd isgqtiignl armphllvag atgsgksvci
      601 ngiitsilyk akpdevkflm vdpkmvelnv yngiphlmap vvtdpkrasl alkkivveme
      661 kryelfsksg trnvegynnl mkdnpaavlp yivvivdela dlmmvaagdv edaiarlaqm
      721 araagihlii atqrpsvdvi tgvikanips riafgvssqv dsrtildmgg aekllgrgdm
      781 lfmpmgaskp vrvqgafmsd eevenivnyv rgqgeaqyde sivpevddsv qaadevqdel
      841 yeqavqiile akqasvsllq rrmrvgytra arlidsmear gvigpyegsk prevlisleq
      901 yqqnkiss
//
LOCUS       WP_285079502             325 aa            linear   BCT 25-DEC-2024
DEFINITION  DHH family phosphoesterase [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285079502
VERSION     WP_285079502.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..325
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=35503
     Region          12..321
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mhtyeqalqd gkqfllehdd ylvvshvqpd gdavsstvtv gwllsclgkt ftminegeip
       61 qlmhflweag kivnmteqpp erkykaiicv dcadfsrvgl trhyfeedav ilnidhhptn
      121 daygtvniik pdaaataeil fdflnlfpvk wnkdvatavy tglltdtggf ryantspnvm
      181 ttaskllehg vdgpylaqil leqvtlpqvr ilnqalsslq mtddgkiawv vitpedmiac
      241 gaanedlegv vnyprniqgv evgiffkvin dnavkvslrs agkvdvasla qnfgggghvl
      301 aagcrvegkl edivalvlkq vntqw
//
LOCUS       WP_285079554             543 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Kingella kingae].
ACCESSION   WP_285079554
VERSION     WP_285079554.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..543
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60215
     Region          13..316
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mltytsrpkr peptheypwl llllafcwlw pgvfshdlwt psepnmmlai ddaaqrgawl
       61 ptvfgaayfd vsplyvqtaa wfkmllspwa adafsaarft svlftslgll gsgmagyrfl
      121 grhhgrsvvl iligsvgilp iahflgaysp vfagvglamw gfsiaqrqvm fsailvalgt
      181 mllaqslgll aalamllvas llpfsphwrn qrytvalvam waislpllav ypialaivep
      241 aafavywqqh ifgsfgginq vqaafslhyy lqhllwfafp alplaiwtrt rqsfratpag
      301 vlmatwlavf ggflllnpeq hqdllvlllp plalsgaaql dnlrrgmaaf lnwfgialfg
      361 caavflwigf vamnygfpak laeraayfsp yytrdldimp ilvallftpm wliaitrkri
      421 rgrqavtnwa agttlvwall mtlflpwida akshrpviqq liqavpdvah anclyidprd
      481 ktarlawqqy gtgaytiqna scrytlaqyn prnevapagn ivwqgkrprs ktelfvlihn
      541 gge
//
LOCUS       WP_285079615             377 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285079615
VERSION     WP_285079615.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..377
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42425
     Region          11..371
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mselkvness ipvyilsgfl gsgkttllvq liehwqqqgl rpavvmnelg evnldgqmvd
       61 ssvpmtemlg gcicctvrgd lglqladlvq eespdviiie atgaanpmei ldavtetsly
      121 mrlelkslit vvdaahlsgl yqeqkgqtfk lmqeqircas vlllnktdrl neqqladlrd
      181 lltrwngfap viptvrcevd mdvllrsgdn vhayqsvdet skdakkeqhv hseacaehgc
      241 shehehehhk hmdqeahqhs vvnvqghphd hdhshvhpha shehvmvyth yftqpvnsea
      301 ferliaelpr dvyrakgils fsdtssrfwf qyayresdym kitpqgdvpn vavfigehfd
      361 qtvirnqlle leaines
//
LOCUS       WP_285079662             107 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285079662
VERSION     WP_285079662.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 107)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 107)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 107)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..107
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11868
     Region          8..93
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mkilhhpqve dielssvlya lsdpirlgiv teaarsgeqp cshfrapvvk stmshhirtl
       61 reagvirvrv qgtqhfltlr sedlevrfpg llqpllqaat qseihds
//
LOCUS       WP_285079693             585 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285079693
VERSION     WP_285079693.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..585
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=65782
     Region          203..585
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrrngvtmkl flvmagflll lygttviaql vwfpdfyqhq kissikknla kfeqqysagr
       61 wndvqlaket gnfmrqnqsh lviltntgkl vndpfhitll redgtqvkvs lslfinsena
      121 gwiashlkyg qqltvtgpas gltepmvypf kikdasssvw gtesfqelae pvqewsgvlt
      181 dvvlpnlatw sqrqgllvqa ldsrfplake dqqslangkm ineewtdsws gvrnvltiap
      241 vhssgpqqql ifsltslqem reaskatqlf yayfgiaafv livflsllls rivtkpllal
      301 nhvakkmstl dftvkspirr ndeigslses lnalsttlgq tleelrqans qmrtdmemkq
      361 qieqrqrkff adashelktp isiikgyseg lkdgvsegkr eryieiiade avkmetmvee
      421 mldlvrlesq avrlntdava lgdmiediag rlgpqlkdkg levvlvstte qsvegdrskl
      481 eqviynmmmn airhavphtd ilieisrpeg qvrisienkg eriseaerqy iwerfyrver
      541 srnrkmggtg lglaiakqil dlhgcsygve ntpdgvrfyi ifpna
//
LOCUS       WP_285079856             362 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285079856
VERSION     WP_285079856.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..362
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=41040
     Region          118..351
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 msypiarfli lalsfplill fmlkqikkir inisvfvafi ffvfsslisv lvnadsgsii
       61 nvmaiaylyi flailfnsie enqqlnlmrs silsshitil iislvffggi svpfkgmfln
      121 pnsmgqllit isvvvsaify qliynkmfln lkikksklfw sfvlalivly lsiltksrts
      181 nlvviivyil plvyiffksl rnlknvtnli vlfpfaafav walirytgif nlfnnlilsk
      241 fviksndltd grsyvwkyti dntglfgngh yffdntvgah ntfidilgey gwasliffii
      301 ftlltlinsl kylkgnhdnr fvpflmvvaf iatsmtegqm fkplmiglfl vsgiptlkpn
      361 sh
//
LOCUS       WP_285079868              76 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285079868
VERSION     WP_285079868.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..76
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=8584
     Region          1..>70
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mkkltrreee algvikdyfr dhgyppttre lgdmmgvtss staygylkrl ekkgcikrtt
       61 stprgikile gdrygr
//
LOCUS       WP_285079910             450 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285079910
VERSION     WP_285079910.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..450
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50612
     Region          <169..448
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 miktlyvrii ctflvviifs lltsfflglf lfkkevnhig qndmiaagee mihlyeqtqp
       61 edrdafiksm vkvstypihl ydasgnatyy dldntdtvhi apevvqmvlq ghvyrspaev
      121 dqtfigipfp fqgeshavfm qyspqnenii nrmvflilll alligslcil iaarylvkpi
      181 qvltratkrl akgdfdveiq tkrvdeigal thsfnemase lkqleqmrqd fvssvsheiq
      241 tpltsisgfa mamknsslva eadrnyyldi iitesgrlsr lsdnllelas ldsdhhpfea
      301 ttyhldeqir qiivtcepqw sakniqvhle ltdtiqvtad rdqlnqvwmn llgnsmkftp
      361 agghihirtd qltneilfti tdtgigiaqe qldyvfdrfy ktdlsrnrsi sgnglglaiv
      421 kkivtlhqgn veinsqvgeg ttvmvhlpsg
//
LOCUS       WP_285079914             284 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285079914
VERSION     WP_285079914.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..284
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32265
     Region          1..240
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mrliimgdlh ypallvdadd qmieardafy taylaefldf sadyhisigd lthagealef
       61 dfimskvqkv lpqgrflyal gnhdthacsk aeleattgqk rylaieeeea vllvldtare
      121 npdhwggmmd eeqmdwlrgq mnkygqktll vfahhpvydt tarstepmms ldpeldlwsv
      181 lkehqgqgiy fnghnhvqsv iqrdqwhfvq iaavpdipav vlvnlqdqqm sihtfelqga
      241 hyqelartfv kglydyephp dakgdhdste liftlssgkk emtp
//
LOCUS       WP_285079915             402 aa            linear   BCT 25-DEC-2024
DEFINITION  Gfo/Idh/MocA family oxidoreductase [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285079915
VERSION     WP_285079915.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..402
                     /product="Gfo/Idh/MocA family oxidoreductase"
                     /calculated_mol_wt=45079
     Region          4..285
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
     Region          <242..369
                     /region_name="GFO_IDH_MocA_C"
                     /note="Oxidoreductase family, C-terminal alpha/beta
                     domain; cl21649"
                     /db_xref="CDD:451345"
ORIGIN      
        1 msrkrvrlai vggnrgasfl nalhsladri dltatcdlne lvleqwkgif pgirtysdys
       61 emlqdasida vfvispmhmh arhsidalna gkhvlsevia vqsleeawel vetvertglk
      121 ymmsenycfs rsnltvnhma qqglfgeith veggyihdlr hlihhpngsl twrgqlhqny
      181 ngvnypthsi gpaaqwialn kpggdrlksi saqvsepral qnyfseqfgk dhpaaregyw
      241 sqgdsavaal ktekgvlitl rvdwvsvrph nkthymlqgt kgaylsarhp yeedlvwlqd
      301 rspvngedgs emweemsryq peydhpkwkq wghlaagtkh gggdflvlee fisaiqedrs
      361 plvdvydavt wssvfflsme svklggntvt fpdfrgkags ee
//
LOCUS       WP_285079928              69 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285079928
VERSION     WP_285079928.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 69)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..69
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7886
     Region          1..69
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mikihlsrim gekriniadl srqtglhrng iaklyneetd gvkfdtlnri cealdceiqd
       61 iiefikdek
//
LOCUS       WP_285079974             309 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285079974
VERSION     WP_285079974.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..309
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35729
     Region          1..305
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mkidrllali millerevvs arelaerlev srrtiyrdid tltfaglpif thqgamggvg
       61 lmkaykmdkl lftphdiqtl ltslksykql fdhneivfvl eklnaihrgs adikagrfav
      121 dlslnqgnes lrnllsyiet amneqrylvf eygdrdgkis srtvepyqiv fkesswylqs
      181 ycvdredfri fklarmnrlq vsedafvprd ftplpmdgag wmnqdwvevt irvhrsvidk
      241 vierfgeahi lhmgeetcla typiikntfg ydkllafgdk ceviepievr ngfqdyvrri
      301 lgkyehqge
//
LOCUS       WP_285079993             290 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paenibacillus
            sp. UMB7766-LJ446].
ACCESSION   WP_285079993
VERSION     WP_285079993.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..290
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32717
     Region          1..287
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mkvglstysl lndlnsgemt vldmidwiaa nggehmemvp ygytvednye ladaireraa
       61 sagielsnys mpanfvqete eafeeemarv krhvdvvhrm gvkhmrhdvt aftlpkekmt
      121 iawfeenlpl mvkgsqiiad yaaqfgittt ienhgfsvqa sdrvqrvlha vdrpnfkttl
      181 dignfmcvde npiigvmknl pyaslvhfkd fyfrsydehp gegewfttan gnflrgaivg
      241 hgdipirkiv klikdsgydg nitvefegme ecksaskiam nnlrrfwkea
//
LOCUS       WP_285080219             326 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285080219
VERSION     WP_285080219.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..326
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36526
     Region          21..326
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mnpssipsml qqtippldlr sclvsvrgei iyehyrnqea athiakvnsc tksvlsalic
       61 iamdhgwlpe astpistffp qlgsdpdprk peitleqllt mtagfnwdef ggqnsfprmt
      121 rtdhwvnfal eqslshvpgt ymeynsgvsq ilsailmqst gmsvaefaer ylfgplgiqe
      181 yewesdpqgv htggfglkml prdllkfgql flqqgvwndq slisndlvsr stkpaitvtp
      241 pnhgsyawhw wvdaytrets eaeagirekp tsilhyyyar gfggqfvyiv palelvavlt
      301 ndkrkkekpp ldvfpkriap ellecl
//
LOCUS       WP_285080143             244 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Paenibacillus sp. UMB7766-LJ446].
ACCESSION   WP_285080143
VERSION     WP_285080143.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..244
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26937
     Region          18..225
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mvankefggl geandgiiqa vifdmdgvli dsepiyfeie rnsfahfgam mteaehhtyv
       61 gvtlesmwrq vldkhqltat veealayhqh nvmqtmlahp kltampfver wlswlheqhi
      121 piavassspr alidlimdkt glgkyfevrm tgeevahgkp apdiflttae migvspsncl
      181 viedsrngvq aaksagmhci gyhnpgsgnq dlskadlqis sydelwtlkd tlpfegrspi
      241 ltkn
//
LOCUS       WP_285080271             244 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285080271
VERSION     WP_285080271.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..244
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27900
     Region          26..142
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mkqnkydeae ffgnysqmar stqgleaage whelqtmlpe lkgknvldlg cgfgwhcrya
       61 reqqarsvvg vdlsenmlqr aremtddphi eyqrmaiedi dfapgqfdvv isslalhyie
      121 rldqvyakin eclvqggtfv lsaehpifta raeqdwhyga qgeilhwpvd hyheegqrva
      181 nflnqdvvky hrtlathlne liqagfviqq vaeskpstem meqvpgmrde srrpmflmia
      241 avkv
//
LOCUS       WP_285080316             271 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285080316
VERSION     WP_285080316.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..271
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30001
     Region          6..265
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mstafelpag gdavirgnif tarqpaqgim ilahgykgfk dwgmfpyaas qlsenhhvlt
       61 fnfshngvge dleqfselek favntysrel sdlaalldyv stqpelnelp vflighsrga
      121 gvslvyaldh peqiagvlsw ngvtnldlft peqkeemrtf grshvtngrt gqqmpldvsi
      181 ledldkhkdr yaiidrlsas plrvaliqgt edgqrlrdgs aalvqarpdv pwhqipggnh
      241 tfntvhpfke ltpqleqait etlrqieaws k
//
LOCUS       WP_285080339             316 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285080339
VERSION     WP_285080339.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..316
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36198
     Region          1..311
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mkldrllaiv vllinrgrvq akdladtfev sirtiyrdid tlgqagipvv tyqgasggig
       61 laegyrldrn vltdkdlasi vtalrsvsts htnvardllm eklssivpea knedfqants
      121 rfivdysmwt hpealqiklq lieqgmdqlr pitftycsae gtqthrttdp htlvlkkhsw
      181 ylyafchern efrmfklvrm rdvalaqgnf erkpinlqdr pwqqdwatpd nkvpltlrfh
      241 arirhiavew fgiesvipnd egyyisqvaf pednwlygfi lgfgadvevl eplhireeir
      301 riaeqivqny sapprt
//
LOCUS       WP_285080445              89 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein, partial [Kingella
            kingae].
ACCESSION   WP_285080445
VERSION     WP_285080445.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         <1..89
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
     Region          <5..89
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 assgvqsvaa gtvayaanlr gfgntviidh gdgymstyag lsqiavsngs rvgarqnigt
       61 sgtlpageqg lyfelryrgr ainprswvr
//
LOCUS       WP_285080520             279 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Paenibacillus sp.
            UMB7766-LJ446].
ACCESSION   WP_285080520
VERSION     WP_285080520.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB7766-LJ446
  ORGANISM  Paenibacillus sp. UMB7766-LJ446
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13303788
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Paenibacillus sp. UMB7766-LJ446"
                     /db_xref="taxon:3046313"
     Protein         1..279
                     /product="AraC family transcriptional regulator"
                     /calculated_mol_wt=32683
     Region          27..276
                     /region_name="PRK13503"
                     /note="HTH-type transcriptional activator RhaS"
                     /db_xref="CDD:184094"
     Region          <192..279
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkpifyestl fdisrkkqiy tsmpsshyhd ayeilylisg dfyyfigdrt yqvaggtllf
       61 mdiherhklv nsgcnmyerv tllfkkeflq hlctggqcee llelfksdyr alkmtgkdqy
      121 fieqlfqkmi qeeqkqargy eqyqqillve llinlnrklf dslaaplves nrahkkvldi
      181 vnyvnqhyme plklceisrq fdisssylcr tfkestgfsf ieyinnirik eardllvgss
      241 fnvteiagmv gfdntshfgr tfklmmgisp lcfrkqfks
//
LOCUS       WP_285080886             257 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Kingella kingae].
ACCESSION   WP_285080886
VERSION     WP_285080886.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..257
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29389
     Region          47..255
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 matytinqwy rlfatalgfv ifgvfgvlfk lylgpgkrfq sslhtqflar krvtqswyvf
       61 tqylikmgiv eahfhgfdkl grqgqmilan hpslldvvfi lsrvpqanci vkadllhnpa
      121 mssqiracgy vlnqenldfv eetdrilqqq cllvfpegtr tgwdgevkfh rgavsmalrs
      181 akvitpiavk msppnykkgq pwyriplqkp vyhfvvgddi dpqtwlaekp lpiaarrlnd
      241 ylqdyfnqqt rekqpap
//
LOCUS       WP_285080877             301 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Kingella kingae].
ACCESSION   WP_285080877
VERSION     WP_285080877.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 301)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..301
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32879
     Region          1..294
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mnaeftslfq qlntvilgke tvlkqliasi lagghvlled vpgvgkttla tslaavlglk
       61 yqrvqftndm lpadllgvnv fmpsdgsfkf hpgpvfnqfm ladeinrasp kvqsalleam
      121 eegqvsvdgt thrlpkpflv vatqnpseql gtfplpesql drfmmrlsmg ypveeaekml
      181 yhmsdrrqlv hkieavgtpe kllqwqaqvq qvtvseavaa yiyrlvaatr ragvfalgls
      241 praglavana akawaflegr dfvlpedvka vwvsvgnhrl qslqqqnssk vlaeileqva
      301 v
//
LOCUS       WP_285080969              94 aa            linear   BCT 25-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Kingella kingae].
ACCESSION   WP_285080969
VERSION     WP_285080969.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 94)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..94
                     /product="type II toxin-antitoxin system RelE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0017148 - negative regulation of
                     translation [Evidence IEA]"
                     /calculated_mol_wt=10839
     Region          2..88
                     /region_name="RelE"
                     /note="mRNA-degrading endonuclease RelE, toxin component
                     of the RelBE toxin-antitoxin system [Defense mechanisms];
                     COG2026"
                     /db_xref="CDD:441629"
ORIGIN      
        1 msyklrfvve aedewrkldn sikqqfksal akrlenprip saalhnmpdc ykiklrkigy
       61 rlvyrvddnv itvtviaigk rdksvvydva nsrl
//
LOCUS       WP_285080985             394 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Escherichia coli].
ACCESSION   WP_285080985
VERSION     WP_285080985.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..394
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=45673
     Region          1..389
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mitdtklrka lgkkrddiei isdshglnar isqagkisff yryrwagkav klnvgdyptm
       61 sitqarerrq qfrnwltegl dpreqvkldk qtrqeamsva eafnywierh cianglvkvd
      121 yyrqvfekhi aepmknvkvd ntakmhwinv fdsiesrvma hymlslckra frfcvnrsvi
      181 asnplegllp sdvgqkptrr mddddlrkiy qwlkshmsie svflvkfiml tgcrtaeirl
      241 serswfrldd newvvpagsy ktrvhirrgl sdaavnlvrn hlkkintnhl vtsqrkidgg
      301 ikdspvhspv asnyarsiwn gtgmaewslh dmrrtiatnl selgcpphvi ekllghqmvg
      361 vmahynlhdy iddqkhwlrv wqshleeiig epfs
//
LOCUS       WP_285081270             235 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Peptoniphilus
            duerdenii].
ACCESSION   WP_285081270
VERSION     WP_285081270.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus duerdenii
  ORGANISM  Peptoniphilus duerdenii
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Peptoniphilus duerdenii"
                     /db_xref="taxon:507750"
     Protein         1..235
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27585
     Region          1..132
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mykgfayiyd elmydldykg feefikeklk gkesvldmgc gtgtmmklle ddfeidgfdl
       61 spdmlamarn kvkgnlycld mrsfdmhksy daiissgdsl syildteelk difknvannl
      121 neggififdl ntfykfqnme evyidetenv fyiwenffde eerlnyydin ffvkeengty
      181 rrfienhvec ahdiktvkny legcgfrvel ynnysdeggi dtakrvtfvc ygenl
//
LOCUS       WP_285081311             392 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Peptoniphilus
            duerdenii].
ACCESSION   WP_285081311
VERSION     WP_285081311.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus duerdenii
  ORGANISM  Peptoniphilus duerdenii
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Peptoniphilus duerdenii"
                     /db_xref="taxon:507750"
     Protein         1..392
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43815
     Region          10..391
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mkfkrfavff lsfsllvtsv fastkelkkk rdskidqktk ieqklketke kvkkknaeas
       61 nvekeiekld aeiskydnsi fdlnqkmdvl nveiaanekk ldeanknlda vqdefgermr
      121 asymngrvgy levvmnsksi edllnniema kriaesdkkm idyvdfqitq ikevkeklvv
      181 ahqeldnskr alevqrgkla iasenksrym ksllkdveky kqeyeaseal wasldkeian
      241 lkkeiqsaea restsqrmni ttragaslgw pvpghtrlsr gfgmmkhpil gytkmhtgid
      301 ipaptgtpal saakgtvlma rtlgsygnvv mvdhgstvtv yahlsvikvr qgdrvdkgqv
      361 vglvgstgls tgphlhfevr vngtpqnpln fv
//
LOCUS       WP_285081388             543 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Kingella kingae].
ACCESSION   WP_285081388
VERSION     WP_285081388.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..543
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60171
     Region          13..316
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mltytsrpkr peptheypwl llllafcwlw pgvfshdlwt psepkmmlai ddaaqrgawl
       61 ptvfgaayfd vsplyvqtaa wfkmllspwa adafsaarfa svlftslgll gsgmagyrfl
      121 grhhgrsvvl iligsvgilp iahflgaysp vfagvglamw gfsiaqrqvm fsailvalgt
      181 mllaqslgll aalamllvas llpfsphwrn qrytvalvam waislpllav ypialaivep
      241 aafavywqqh ifgsfgginq vqaafslhyy lqhllwfafp alplaiwtrt rqsfratpag
      301 vlmatwlavf ggflllnpeq hqdllvlllp plalsgaaql dnlrrgmaaf lnwfgialfg
      361 caavflwigf vamnygfpak laeraayfsp yytrdldimp ilvallftpm wliaitrkri
      421 rgrqavtnwa agttlvwall mtlflpwida akshrpviqq liqavpdvah anclyidprd
      481 ktarlawqqy gtgaytiqnt scrytlaqyn prnevapagn ivwqgkrprs ktelfvlihn
      541 gga
//
LOCUS       WP_285081408             228 aa            linear   BCT 25-DEC-2024
DEFINITION  tRNA (adenine(22)-N(1))-methyltransferase [Peptoniphilus
            duerdenii].
ACCESSION   WP_285081408
VERSION     WP_285081408.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus duerdenii
  ORGANISM  Peptoniphilus duerdenii
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Hori,H.
  TITLE     Methylated nucleosides in tRNA and tRNA methyltransferases
  JOURNAL   Front Genet 5, 144 (2014)
   PUBMED   24904644
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Roovers,M., Kaminska,K.H., Tkaczuk,K.L., Gigot,D., Droogmans,L. and
            Bujnicki,J.M.
  TITLE     The YqfN protein of Bacillus subtilis is the tRNA: m1A22
            methyltransferase (TrmK)
  JOURNAL   Nucleic Acids Res 36 (10), 3252-3262 (2008)
   PUBMED   18420655
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   4  (residues 1 to 228)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Peptoniphilus duerdenii"
                     /db_xref="taxon:507750"
     Protein         1..228
                     /product="tRNA (adenine(22)-N(1))-methyltransferase"
                     /EC_number="2.1.1.217"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0160105 - tRNA
                     (adenine(22)-N1)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25929
     Region          1..220
                     /region_name="TrmK"
                     /note="tRNA A22 N1-methylase [Translation, ribosomal
                     structure and biogenesis]; COG2384"
                     /db_xref="CDD:441950"
ORIGIN      
        1 miskrlnkis shikgnrmad igtdhglvpi fliehkivdy aiaadiskps lqkaidlake
       61 knleldarlg dgmevlnped gietvviagm ggvligeils aseisknvrl ilqpmqgare
      121 lrkylfengy eiidedvvfe ddryfeiiva eydgkirevp neielkipik afrknqeeaf
      181 lyveylkgan lsimkglkqg kralkryiel kkevnyyeki ndkyrknn
//
LOCUS       WP_285081466             101 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_285081466
VERSION     WP_285081466.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..101
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          <1..97
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 rnvraksgln rsildqgwye mrrqleykql wrggqvlavp paytsqrcac cghtakencl
       61 sqskfrcqvc gytanadvng arnilaagha vlacggcqqt g
//
LOCUS       WP_285081539             373 aa            linear   BCT 25-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Peptoniphilus duerdenii].
ACCESSION   WP_285081539
VERSION     WP_285081539.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus duerdenii
  ORGANISM  Peptoniphilus duerdenii
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Peptoniphilus duerdenii"
                     /db_xref="taxon:507750"
     Protein         1..373
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=44252
     Region          230..>371
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mnnfyedlfk kqsemlekmg lsfftnenqf ldgnfmksym entkkfqedf vnkyfdkekv
       61 kenlkainpm lgdyydryve nllnmnafdf neylkspeef skmyrdsfds ymraydlykd
      121 iykapelake nfekslekyk dlsisylken vfklmpealk kefeksldda dttgaafkei
      181 lspwefsgad mkdyyleamk srpalvvkfl edmdsrmnls lnavenldss estkeivklq
      241 rkylkeyvdy akklgdynda iykilkeate stiedmkkdf nelkekksfe dfykylsniy
      301 kknmnklkdq eqvnklvekt letvstfked aekmmkeyre ltevsrksev dslkaevqal
      361 kdkiaaleak ldk
//
LOCUS       WP_285081577             923 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Kingella kingae].
ACCESSION   WP_285081577
VERSION     WP_285081577.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..923
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..923
                     /product="class I SAM-dependent DNA methyltransferase"
                     /calculated_mol_wt=104477
     Region          56..923
                     /region_name="YeeA"
                     /note="Type II restriction/modification system,
                     endonuclease and methylase domains [Defense mechanisms];
                     COG1002"
                     /db_xref="CDD:440626"
ORIGIN      
        1 mltsaqilin aqtfatrwqn esdeksesqt fwneffaifg ldrkaiaile krlksakstk
       61 fadvfvpkkl lceqkskgkn lddaaaqare yleqiraqep enlppyfivc dfatmrfyet
      121 igtacvefpl eklpeniglf nflldletei hhaqsqvnlq asammrelyn gikadydtdt
      181 vrkflirilf clfaedtgif rpdqfnrlid khtkadgsdt gamltelfqt lntakrspkl
      241 peylqefdyi ngglfaetlp tiyfdsemrq klihigrein wgyispeifg slfqealdvn
      301 errelgahyt ekdniekvin slfldnlkae faqigslkrd kkkrliefqq kiaklkfldp
      361 acgtgnflva ayralrelei qviheyqkld kthlqsavsi eqffgieidg laaeiavlsm
      421 wlidhlcnlq egaalgkgyg slniplrksa hithgnslrl dwenvdfilg nppfigstyq
      481 tkeqkadtqa vsgslknagi ldyvanwyvk aaqimrdnpq vqaafvstns icqgqqveal
      541 wgalldwgve ihfahrtfqw tsqahdkaav hcvivgfrqp ekhssakylf dypdikgqpe
      601 krevaninpy lidapnvvie krskpisgep emiygskptd ggnlilstee kneliaaepl
      661 aeqyirrflg aeeflnnker wclwfhgmse mrlftdlqkm plvakrielv kqmrlessdk
      721 qtnkaaatph lfqairqpes gnyllipsas setrefipig yldsntingn anfslpnatl
      781 yhfgllsstm hnafmrtvag rlksdyrysn tivynnfpfp faafrqpete ispaeqkhrt
      841 aiataaqavl darahyiaqa qqenlpepsl adlyrrgapf trlhaahaal dkavdnaygy
      901 tggnddadrv eflfgvyekm kga
//
LOCUS       WP_285081789             472 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Peptoniphilus
            duerdenii].
ACCESSION   WP_285081789
VERSION     WP_285081789.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus duerdenii
  ORGANISM  Peptoniphilus duerdenii
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 472)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Peptoniphilus duerdenii"
                     /db_xref="taxon:507750"
     Protein         1..472
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=51542
     Region          43..470
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mfkdnkrilv vlvsvivlyl slilylsyft vfvgqniidn panrretiie qniergsild
       61 regnilayse gdkakavrky nfpisyshii gysdkvmgka gieksydnyl lglevprsik
      121 vlksvynkkv eldkgnnvyl ttntniqnys reilsktgaa gaivamdpkt gdilamvslp
      181 dfnsesiakd nkalseqnkg alynraiwtk yppgstfkii taasilenhi dqnyidegsq
      241 eidgrvfkna lektygkldl ksafvnsvnt yfvkkttdlg aealgktadr fmfnqnfkfd
      301 lpyhgslfky ndisktelas sgighgtvsa tplemcmvas aiandgklmq pnlvgsvisp
      361 kgeivlkkep evlsealtpe vaaeikdyml avvgsgsgrn ayrrgygiag ktgtaqksqe
      421 gqenfawfvg fapakdpkia iavvledvnd yggsiaapia gdimkysidl gi
//
LOCUS       WP_285081843             348 aa            linear   BCT 25-DEC-2024
DEFINITION  SufB/SufD family protein [Peptoniphilus duerdenii].
ACCESSION   WP_285081843
VERSION     WP_285081843.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus duerdenii
  ORGANISM  Peptoniphilus duerdenii
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Hirabayashi,K., Yuda,E., Tanaka,N., Katayama,S., Iwasaki,K.,
            Matsumoto,T., Kurisu,G., Outten,F.W., Fukuyama,K., Takahashi,Y. and
            Wada,K.
  TITLE     Functional Dynamics Revealed by the Structure of the SufBCD
            Complex, a Novel ATP-binding Cassette (ABC) Protein That Serves as
            a Scaffold for Iron-Sulfur Cluster Biogenesis
  JOURNAL   J Biol Chem 290 (50), 29717-29731 (2015)
   PUBMED   26472926
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Sendra,M., Ollagnier de Choudens,S., Lascoux,D., Sanakis,Y. and
            Fontecave,M.
  TITLE     The SUF iron-sulfur cluster biosynthetic machinery: sulfur transfer
            from the SUFS-SUFE complex to SUFA
  JOURNAL   FEBS Lett 581 (7), 1362-1368 (2007)
   PUBMED   17350000
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Fontecave,M., Choudens,S.O., Py,B. and Barras,F.
  TITLE     Mechanisms of iron-sulfur cluster assembly: the SUF machinery
  JOURNAL   J Biol Inorg Chem 10 (7), 713-721 (2005)
   PUBMED   16211402
  REMARK    Erratum:[J Biol Inorg Chem. 2006 Jan;11(1):128]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10477762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Peptoniphilus duerdenii"
                     /db_xref="taxon:507750"
     Protein         1..348
                     /product="SufB/SufD family protein"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=39400
     Region          97..315
                     /region_name="SUFBD"
                     /note="SUF system FeS cluster assembly, SufBD; pfam01458"
                     /db_xref="CDD:460219"
ORIGIN      
        1 mstiqanelk fktfdylkvn ettvkipaif tqdfslpsdk fveinefkdd eygvskeale
       61 mneefgnyyr ylnskdnnke iirlatddlh telfdtidiv tekdesqsii idyaskghkd
      121 kfrnsiiril ghensktnvf iiqregeest vlesilvhae eganifvnqy evgssklisn
      181 ykanligeas haevnsiyfg yndheidliy niihkgkqst sniiingalk dnarkvfksn
      241 ldflegstgs vgneeefcml ldstvksisv plllcheddv lgnhaasagr idenilfyim
      301 srgfsmaeae kliieskfas aideledekl keeiwnrvlv ysgkdlhe
//
LOCUS       WP_285081846             287 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Peptoniphilus duerdenii].
ACCESSION   WP_285081846
VERSION     WP_285081846.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus duerdenii
  ORGANISM  Peptoniphilus duerdenii
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Peptoniphilus duerdenii"
                     /db_xref="taxon:507750"
     Protein         1..287
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=33666
     Region          65..281
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 miyligilll islhlnykli gerkrfkkdf nirtminsts kmksdygvel nevasrleel
       61 llknkdqrvq lrnlddfhke nladmshdlr tpltsilgyi kllekenlne kersyldiik
      121 nkslylknmi dmfyeaslae mgshlniein dvisitnecv leyyddftkk fdstevdlnn
      181 kleleideni frqvvsnils nmlkyslgkn kiiyrdgkly fknltdledg nydrlfeksy
      241 vldpsrqnst glglyivktr ldsmnisski yvqekiftie idfkkll
//
LOCUS       WP_285081876              93 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Peptoniphilus duerdenii].
ACCESSION   WP_285081876
VERSION     WP_285081876.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus duerdenii
  ORGANISM  Peptoniphilus duerdenii
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 93)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 93)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 93)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Peptoniphilus duerdenii"
                     /db_xref="taxon:507750"
     Protein         1..93
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=10577
     Region          2..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mklldvaaif kvlgdptrlk iikilsddke rcacellatf ditqptlshh mkilnnfklv
       61 ktkkagvwny ytlnrktmee lksymdvlfn tga
//
LOCUS       WP_285082059             455 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Peptoniphilus
            duerdenii].
ACCESSION   WP_285082059
VERSION     WP_285082059.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus duerdenii
  ORGANISM  Peptoniphilus duerdenii
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Peptoniphilus duerdenii"
                     /db_xref="taxon:507750"
     Protein         1..455
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47909
     Region          3..446
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 medkllaivk singvlwgvp mmvilvgcgi fytlalrgiq vrdfglafkk afsgfslkgk
       61 kagadgmssf qslataiagq vgtgnltgsa taiisggpga ifwmwisaff gmatifaeav
      121 lgqkykvvkd gqvtggpayy lrngihskvl aalfaifiti alglvgnlvq ansigqafss
      181 vinvptwvvg lvivvisgfi figgvgrias vtekivpvma ffyilgglii liknggatad
      241 afrqifvgaf npqavlggaa gvtvrqavry gvarglfsne agmgstphah aiakvnhpcd
      301 qglvaivgvf idtfvvltin alviiatgan qidglkgikv tqkafelgig higvafiava
      361 lfffafstii gwyfygeanv rylfgqkgig ayrilalvfi ylgtmfevdl vweladmfna
      421 mmvipnvigv iglykvvqst lneyqslkld vnpna
//
LOCUS       WP_285082232             181 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Peptoniphilus duerdenii].
ACCESSION   WP_285082232
VERSION     WP_285082232.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus duerdenii
  ORGANISM  Peptoniphilus duerdenii
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Peptoniphilus duerdenii"
                     /db_xref="taxon:507750"
     Protein         1..181
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=20998
     Region          75..181
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mkyvpisafi lylimlfair keigedlkrt gelvdikrnk lyfilifian inllvvdlvr
       61 pvpgylnrni mkypgiflyv ygllltiyvv atikdsmrgp nadkmkefdg edaytinrnp
      121 lykalmlita ghlvtttrls fvflfivtvl lvisqtlkee ralqtrygkk ylryknkikr
      181 f
//
LOCUS       WP_285082512             330 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Peptoniphilus
            duerdenii].
ACCESSION   WP_285082512
VERSION     WP_285082512.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus duerdenii
  ORGANISM  Peptoniphilus duerdenii
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Peptoniphilus duerdenii"
                     /db_xref="taxon:507750"
     Protein         1..330
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=37908
     Region          64..315
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 myadkfysgl fsqlnlipgk sgikpgdgft mvpkdstgeg ylwtypvnaf csiniyhlcf
       61 ynemhyryyh pkmlvlsqss yyvakaiknn scnqknqlig yylangehey tipagiwlds
      121 vgvsifpeyy ekylpkifhq dfsslseivp qigtdlfipk isiilddiat ytptseisev
      181 yyeakimeii atllswktna ihnfintdds ealhrlghyl eqnfsyptdi qmyarmcnms
      241 ksklselfhs iygytivefi kncridkakr lllendlsik qiasavgysh qssftyifkq
      301 hvgctpreyr kansnfhsfs stistsknyl
//
LOCUS       WP_285082604             364 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Peptoniphilus duerdenii].
ACCESSION   WP_285082604
VERSION     WP_285082604.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus duerdenii
  ORGANISM  Peptoniphilus duerdenii
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469162
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Peptoniphilus duerdenii"
                     /db_xref="taxon:507750"
     Protein         1..364
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=42592
     Region          224..355
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          224..248
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(258..259,262..263,265,289,292..293,296..297,
                     299..300,323,326..327,330..331,334)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          258..282
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          287..317
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          322..350
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 miekeikkrl nnigfvelke dttvegfkfl kevplpimvd dikrlaiekn digvradlis
       61 rgiiyvlgcd tefkykdnyk eileaiikdi ksfvitnalk aednldkyiy lnsfigldis
      121 ddeieynkli ylenyldehr knlkeedqse iiknllvnye kiedkkiipy snyrlgiink
      181 aignylkskm yfekslesgd lvedeelknt lrreiedisd ysnieiaety inysdfdkae
      241 ealknvsiyy vdqsylnfli gfvyqstgri elaieeykka islnknredy ynslaiclvn
      301 lnkykeasyi leegiennst synlkynlgv iyvnlnklee arellkeaya ikpseelyky
      361 iesl
//
LOCUS       WP_285082624             299 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Peptoniphilus
            duerdenii].
ACCESSION   WP_285082624
VERSION     WP_285082624.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus duerdenii
  ORGANISM  Peptoniphilus duerdenii
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Peptoniphilus duerdenii"
                     /db_xref="taxon:507750"
     Protein         1..299
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33243
     Region          6..299
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 menrfkkiki ianplsgree aldkvlefir llsldqwdin llfthkrgdg mrfaesddge
       61 diivacggdg tlnevvngiv kskrdtplai lqagtvndfa nyfklpqdps kfyklikegr
      121 tkkidvglag drvfanvaag gmlteiaytv pedqkavlgr mayylegarq mvklnfqeek
      181 aykvkidcee ykgeenlfff litntssvgg fkkmapaatv tdgyldvlli kecslvdfmq
      241 iaplvltgnh idhekviylk tkdislssdi eldidvdgeq sgklpmnfkv leealtiii
//
LOCUS       WP_285082734             117 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein, partial [Kingella kingae].
ACCESSION   WP_285082734
VERSION     WP_285082734.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         <1..117
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
     Region          <1..117
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 swvqagswqp velfddddle yivcrtklgk dgyalrvrgd smqpeftegd iividphgep
       61 ragsfvialh dnettfkqlv fdgsrpmlrp lnsnypylqi kendrilgvv kekvkly
//
LOCUS       WP_285082787             319 aa            linear   BCT 25-DEC-2024
DEFINITION  ribose-phosphate diphosphokinase [Peptoniphilus lacrimalis].
ACCESSION   WP_285082787
VERSION     WP_285082787.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus lacrimalis
  ORGANISM  Peptoniphilus lacrimalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Sinha,S.C. and Smith,J.L.
  TITLE     The PRT protein family
  JOURNAL   Curr Opin Struct Biol 11 (6), 733-739 (2001)
   PUBMED   11751055
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Becker,M.A., Smith,P.R., Taylor,W., Mustafi,R. and Switzer,R.L.
  TITLE     The genetic and functional basis of purine nucleotide
            feedback-resistant phosphoribosylpyrophosphate synthetase
            superactivity
  JOURNAL   J Clin Invest 96 (5), 2133-2141 (1995)
   PUBMED   7593598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Peptoniphilus lacrimalis"
                     /db_xref="taxon:33031"
     Protein         1..319
                     /product="ribose-phosphate diphosphokinase"
                     /EC_number="2.7.6.1"
                     /GO_component="GO:0002189 - ribose phosphate
                     diphosphokinase complex [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004749 - ribose phosphate
                     diphosphokinase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0006015 - 5-phosphoribose 1-diphosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009156 - ribonucleoside monophosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009165 - nucleotide biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34960
     Region          5..316
                     /region_name="PrsA"
                     /note="Phosphoribosylpyrophosphate synthetase [Nucleotide
                     transport and metabolism]; COG0462"
                     /db_xref="CDD:440230"
ORIGIN      
        1 mnqkmgdivv ftgnsnnelv dnickeigie kgkckvstfs dgeiaididi svrgrdvyii
       61 qstsspvnnn lmellilmda irrasagrin vvipyygyar qdrktkarep itsklvanli
      121 sntgadrvva mdlhagqiqg yfdipvdhlt aipylaryfk siikeedfvv vspdlggvtr
      181 arafanelnl piaiiekrrp kpnvsevmni igdikgknai lvddiidtag tickacdsli
      241 ekgakkvygc athgvlsgpa idrinnsnle kfvitdtihl pkekqidrid ivsvapifas
      301 aikrintnss vsemfekkr
//
LOCUS       WP_285082818             204 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Peptoniphilus lacrimalis].
ACCESSION   WP_285082818
VERSION     WP_285082818.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus lacrimalis
  ORGANISM  Peptoniphilus lacrimalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Peptoniphilus lacrimalis"
                     /db_xref="taxon:33031"
     Protein         1..204
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23692
     Region          26..199
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mdrelftike kfrhkkprai dvknaysvli plikrdnevh ilfekralsl knqpgeisfp
       61 gggiergens rdaairetce ellinkrdls iigkgdflvn pysaiiysyv gilniefdai
      121 spskeevesi ftipldffki nkpnsyktki nliredsfpy elipngrnyk wkraegemdf
      181 yvykdiviwg ftakmlrnfi knvy
//
LOCUS       WP_285082991             283 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Kingella kingae].
ACCESSION   WP_285082991
VERSION     WP_285082991.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..283
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32823
     Region          6..204
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mmithspvvs iitpcynstk yvhetlssls aqtftdfeii amddgssddt lailqayaqh
       61 eprlkiytqs nqgqagarqn aiahatgeyl lcvdsddkls pnalekfvqa arthqvdivs
      121 snhqlfgrkg tsiihmsfnl krllwvncil mtallrrdkf iaaggfdanl rcfedwelwi
      181 nlikhgakvh hipevlffyr qredltsvtd tttqyeneat ayiynkhrqf yseqginlyy
      241 vfhdayscye kkrshyanpl rrwfyktfkp kkyqqiyary dll
//
LOCUS       WP_285082945             348 aa            linear   BCT 25-DEC-2024
DEFINITION  SufB/SufD family protein [Peptoniphilus lacrimalis].
ACCESSION   WP_285082945
VERSION     WP_285082945.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus lacrimalis
  ORGANISM  Peptoniphilus lacrimalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Hirabayashi,K., Yuda,E., Tanaka,N., Katayama,S., Iwasaki,K.,
            Matsumoto,T., Kurisu,G., Outten,F.W., Fukuyama,K., Takahashi,Y. and
            Wada,K.
  TITLE     Functional Dynamics Revealed by the Structure of the SufBCD
            Complex, a Novel ATP-binding Cassette (ABC) Protein That Serves as
            a Scaffold for Iron-Sulfur Cluster Biogenesis
  JOURNAL   J Biol Chem 290 (50), 29717-29731 (2015)
   PUBMED   26472926
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Sendra,M., Ollagnier de Choudens,S., Lascoux,D., Sanakis,Y. and
            Fontecave,M.
  TITLE     The SUF iron-sulfur cluster biosynthetic machinery: sulfur transfer
            from the SUFS-SUFE complex to SUFA
  JOURNAL   FEBS Lett 581 (7), 1362-1368 (2007)
   PUBMED   17350000
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Fontecave,M., Choudens,S.O., Py,B. and Barras,F.
  TITLE     Mechanisms of iron-sulfur cluster assembly: the SUF machinery
  JOURNAL   J Biol Inorg Chem 10 (7), 713-721 (2005)
   PUBMED   16211402
  REMARK    Erratum:[J Biol Inorg Chem. 2006 Jan;11(1):128]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10477762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Peptoniphilus lacrimalis"
                     /db_xref="taxon:33031"
     Protein         1..348
                     /product="SufB/SufD family protein"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=39570
     Region          102..319
                     /region_name="SUFBD"
                     /note="SUF system FeS cluster assembly, SufBD; pfam01458"
                     /db_xref="CDD:460219"
ORIGIN      
        1 mkikgnelsf ktfswmkvnd ceiqvpkigk dlipmessek yvrhlkefdn lkygisqeal
       61 dlvkedmnly riyetikged ivynpcyfkt dddnpnlvdv qdiiahegsk ikvfldyyse
      121 gkkekfrntl irilaekdte vslfviqreg seakslesig ifahenakvn lcqyqlgcgk
      181 lytnykclld gkkseahvns vyfgqgeeel nlfyemthkg ekttssilvn galkdkaykn
      241 fksnldfleg cndavgsege favllsddvh sisvplmlch eddvegnhas ssgkidpqil
      301 fyimsrgfsy deaealiies kfsqaidlld neeleeevwk svrkilvk
//
LOCUS       WP_285083174             210 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Peptoniphilus lacrimalis].
ACCESSION   WP_285083174
VERSION     WP_285083174.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus lacrimalis
  ORGANISM  Peptoniphilus lacrimalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Peptoniphilus lacrimalis"
                     /db_xref="taxon:33031"
     Protein         1..210
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24974
     Region          1..194
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mtrkiaffdf ddtlvdcqsi tilwkfaikk qpyliiylfi qlligiikyi ftfnfshikt
       61 smvsllkfls eedlkffann ilnpkyfyrd gikeiekfgd dylkflvsas plnymkyfke
      121 ilsfdyiiat eldenfqvks knnsghqkvl ninkylyeln ikidyensyc ytdnykadrf
      181 maslvankfl insklkvsgf knlywketlr
//
LOCUS       WP_285083202             238 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Peptoniphilus
            lacrimalis].
ACCESSION   WP_285083202
VERSION     WP_285083202.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus lacrimalis
  ORGANISM  Peptoniphilus lacrimalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Peptoniphilus lacrimalis"
                     /db_xref="taxon:33031"
     Protein         1..238
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28296
     Region          2..137
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 miynefaqvy dklmydfpyk enseflfnil gdgkikvlem aagtgnftki lgekyhlhaf
       61 disenmlsia qnkvknvfff kadmvnfktl dkydailclc dsynyllkee dllssfkcvy
      121 qaledngifi fdmntkekfl nidrayvdei ddifysweny fdenksinhy cvnffveeke
      181 dlyrrfyeeh leraypspkv kslleqvgfk sieiykdykn skqiekadrl vyvvkkrg
//
LOCUS       WP_285083479             455 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Peptoniphilus
            lacrimalis].
ACCESSION   WP_285083479
VERSION     WP_285083479.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus lacrimalis
  ORGANISM  Peptoniphilus lacrimalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Peptoniphilus lacrimalis"
                     /db_xref="taxon:33031"
     Protein         1..455
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52649
     Region          3..337
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkdklekilk tyahefnlqg vnlgilkngk keivsiglrd iknnlpmekd tiyaigsqtk
       61 aftavalgkl lyengysfdt pikqlyedfk meddyltkdl rikdgfshrt gfpphlaawy
      121 nnnfkkpqef lkilaylpat mplrytfcyq syffilggli ieklsgksyg dylkenifgp
      181 lqmnntyvlg sfapdenkar pydfvdgtyk eisynyeftk fpngsgtiys tmedmmkwld
      241 fclhgnkkiv drkiqeelys pqtiigsdtn mpelsysknk tygmgwylen yrgrklishg
      301 givdgfrafh ilvpeedmav sivtnlneaq gtelitlsvi dealgikkdw qekyikdlka
      361 inekkspked klkdlkdedf skylgiyrdk aygefefiee dgklyvkafs hklevkeskg
      421 kkviafkpyn lfipiefedc nlilyiddrk iiikk
//
LOCUS       WP_285083591             217 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-L-isoaspartate O-methyltransferase family protein [Kingella
            kingae].
ACCESSION   WP_285083591
VERSION     WP_285083591.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Edwin,R.K., Challa,N., Sharma,R., Satyamoorthy,K., Parsa,K. and
            Misra,P.
  TITLE     PIMT/TGS1: An evolving metabolic molecular switch with conserved
            methyl transferase activity
  JOURNAL   Drug Discov Today 27 (8), 2386-2393 (2022)
   PUBMED   35462043
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Furuchi,T., Sakurako,K., Katane,M., Sekine,M. and Homma,H.
  TITLE     The role of protein L-isoaspartyl/D-aspartyl O-methyltransferase
            (PIMT) in intracellular signal transduction
  JOURNAL   Chem Biodivers 7 (6), 1337-1348 (2010)
   PUBMED   20564550
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Kagan,R.M., McFadden,H.J., McFadden,P.N., O'Connor,C. and Clarke,S.
  TITLE     Molecular phylogenetics of a protein repair methyltransferase
  JOURNAL   Comp Biochem Physiol B Biochem Mol Biol 117 (3), 379-385 (1997)
   PUBMED   9253175
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..217
                     /product="protein-L-isoaspartate O-methyltransferase
                     family protein"
                     /EC_number="2.1.1.77"
                     /GO_function="GO:0004719 - protein-L-isoaspartate
                     (D-aspartate) O-methyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0030091 - protein repair [Evidence IEA]"
                     /GO_process="GO:0036211 - protein modification process
                     [Evidence IEA]"
                     /calculated_mol_wt=23939
     Region          12..206
                     /region_name="Pcm"
                     /note="Protein-L-isoaspartate O-methyltransferase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2518"
                     /db_xref="CDD:442008"
ORIGIN      
        1 mdfnkarfnm veqqirpwdv ldfdlldale siprelfvsk eqqgyayadl plkldngstm
       61 lepkivarmv qgltlsktdr vmeigtgsgy atavlatlag svqtydvdeq qlsraqavlq
      121 slnfdniqfv aedgfansqp eakydaiyvg gslpevpeql kqqladggrl vvvvggkpvq
      181 rclqitrngn efsqktlfdt lvtplttkak kpskfrf
//
LOCUS       WP_285083824             330 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Peptoniphilus
            lacrimalis].
ACCESSION   WP_285083824
VERSION     WP_285083824.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus lacrimalis
  ORGANISM  Peptoniphilus lacrimalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Peptoniphilus lacrimalis"
                     /db_xref="taxon:33031"
     Protein         1..330
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=38445
     Region          <217..316
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msyydfvkdy mkvdecknnk kyssaghtfc wnkedltyae glywfyegdg fiidvhdfyi
       61 reeivqnnty smadyvsiys syivsangdr fspyqtltan slctldfdni kddfvfllhe
      121 nsyylavsig fkrellekhl lsinidpesf yrallqtnqi iltkalekva leilnckmda
      181 paadfffkak anewisivid tylnrkkykf esddnkaled varflddhfa mninqgtlek
      241 iskmsgtklk nlfkekygqs iteytqrkrm nvaetlllnt elpikeiaes vgytshskfs
      301 iyykrykgkl psavrnlsck hhklkcdysd
//
LOCUS       WP_285083856             286 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Peptoniphilus lacrimalis].
ACCESSION   WP_285083856
VERSION     WP_285083856.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus lacrimalis
  ORGANISM  Peptoniphilus lacrimalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 286)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Peptoniphilus lacrimalis"
                     /db_xref="taxon:33031"
     Protein         1..286
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=33022
     Region          <50..282
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 miyvfwiisl lllyyflekr kknrinelid lienmknqny kipmkqddfs iledkiyklf
       61 ieiveakets rknsekqiey lediahqikt pitsmlfsie nlemdfpang dieilkrqti
      121 rlnslsdill klssldankd lmkkeeirld elvayaldsl dlrrstnvev aeslkknsiy
      181 gdfywlaeal iniiknadnr ptcekivvss yknplytsli iedngggiek enikkifkrf
      241 yktpdsngfg iglamaktiv eknngeisvs nidggarfei kfynvt
//
LOCUS       WP_285084127             345 aa            linear   BCT 25-DEC-2024
DEFINITION  single-stranded-DNA-specific exonuclease RecJ, partial [Kingella
            kingae].
ACCESSION   WP_285084127
VERSION     WP_285084127.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Cheng,K., Xu,H., Chen,X., Wang,L., Tian,B., Zhao,Y. and Hua,Y.
  TITLE     Structural basis for DNA 5 -end resection by RecJ
  JOURNAL   Elife 5, e14294 (2016)
   PUBMED   27058167
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Lovett,S.T. and Kolodner,R.D.
  TITLE     Identification and purification of a single-stranded-DNA-specific
            exonuclease encoded by the recJ gene of Escherichia coli
  JOURNAL   Proc Natl Acad Sci U S A 86 (8), 2627-2631 (1989)
   PUBMED   2649886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         <1..345
                     /product="single-stranded-DNA-specific exonuclease RecJ"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
     Region          <1..325
                     /region_name="RecJ"
                     /note="ssDNA-specific exonuclease RecJ, DHH superfamily,
                     may be involved in archaeal DNA replication intiation
                     [Replication, recombination and repair]; COG0608"
                     /db_xref="CDD:440373"
ORIGIN      
        1 lldlvalgti advvpldhnn rilvsqglkr iragkmshgi ralfeiarrd trkaqpfdmg
       61 falgprinaa grlddmsigi scllsdnlpy aqqvaselnq lnqtrqeieq gmlqevlalc
      121 pdvlpssqtt lsvyheqfhq gvvgivasrl kdrfyrpvfv fapsddgelr gsgrsiaglh
      181 lrdaldmvak rcpdmivkfg ghamaagltl rkhrfdefcq vfedvvqglv nedilsqtyl
      241 tdgslhgsdi tleqanlisr qvwgqnfppp sfsdefdvvr qqfmgkeqkh kkawlqkdgy
      301 efeamfwrce delpnkiriv ylltvnewng nqelqlyvdy werav
//
LOCUS       WP_285084946            1099 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Gardnerella vaginalis].
ACCESSION   WP_285084946
VERSION     WP_285084946.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 1099)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 1099)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1099
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..1099
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=123810
     Region          <833..1018
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(899,902..903,906..907,909,933,936..937,940..941,
                     943..944,970,973..974,977..978,981)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          899..926
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          931..961
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          969..995
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mqdevqsskk idsaessekn rsdiaddsmq ivqetiktlw enresipvri fskkhifkdf
       61 pmmpknvklg wiklsgkkhg iaiglfnddc krfrqlavad fegrvytghd isiedtmeri
      121 pelsfveqns mtlkdslrfy gvddrkitha sharkkvnsi nknnresdlv virgdvvvql
      181 sqdegmqwvs swirkvndkk eaytleetrv llpdrlrcnl sycdaistsf fasffmpdit
      241 rafsgfgsgn ifrrltkeap lgairrsimd skvaekaglr vssmekyfay lmldsgaleh
      301 sgpleavhga erlhlqksqv sdanflvwdd sleakaalkv lriegainrf qsisscleen
      361 canggnlten svnfgqisei dlsfiedpaf cangeldmns fgnplqddni rplmhlwnta
      421 kksndlyiyk sdgssncews yrqrlsglir slylpfrfdt dfrsnledgn valafmatgs
      481 smmptrrfds anqkwitltn adksrmttdy nlrlgiimat lafgaseevq nvsirldsig
      541 leemvaaqdd amskilnqti nalnnmnrea arskgdpkdg dihgdvnngl anvqdlqnft
      601 nhpilhedev tvsdssnkat agksinssds ysdteisnsn tndiesdsie pdpmdafsky
      661 ptvkslltvt fnrgsfikhi ranglnnpld aykkfnanmk idgegalnpi epsfdlrdsc
      721 fsphgaqeep efsdvifdik sqkalgttns kglsiqredl lqqavadfhh issevmisna
      781 ekarmamdiv esiddpelne kanlitsali dekeipeisf kvskdiynmr lhaheqfmsg
      841 dlenaieeye navkhfdsmf sfndvvpryf nsyaervvyn rifatqnerm ilipdglfya
      901 hmeladlltq lnrhedalkh lntmvsyapt yvishlklas qltekedwts veavclnalp
      961 vcfdredaaf iyyrlayaew mqdnfplava aykmadnlss gkiesieiel dellsrmqsq
     1021 cipapndmsq veevlkinnv pkwpdveaye iideaakitv negmfviart lsvararmlf
     1081 snnssdnvvq mqflrslns
//
LOCUS       WP_285084953             641 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Gardnerella vaginalis].
ACCESSION   WP_285084953
VERSION     WP_285084953.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 641)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 641)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 641)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 641)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..641
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=71028
     Region          288..627
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 maegsngrrr fsdkwgkhel dvlavlssaf pqwltsrqia qrvkayadsy geladqaaka
       61 afakqfqrdr aklaamgiai esrqpeyssk segqdfasyr lqlgdeprvr irfeqeelpv
      121 laaanylars msisssesrk veqqhssasr taprvpqtpi pglgldsiap glgtqtipda
      181 lvkvidsrrf aatvdvdgeh lnvaytdsdd lamfvlehpg scvvspqeav dafhrrlnaa
      241 tefvscdedy veqddlsqns sddnqdlsds epdksrqkka sfqtgsevdr rlrlmlflsa
      301 hlgeefplde lavrfigkpk sedelrrfva ilhkdintlt tvsddgemag sqffdidwsl
      361 leaegivsat nslglerlag vsqqymsmlt asvnylahsp llpveqrdqa kalymrlrrh
      421 vrpgetpwls ltgyeveprn csivrsaina galidmeytd gagrtrrkvv apskifvdeg
      481 vyyvavwtdv enqapedkrs lvakdtsink anglpriwqv lrvariehae vitpvcpvei
      541 pdvpiielrk wsfdngtqtc fitdepdlnf lkslsgatve pcgsgvkvhl tvcsdswfva
      601 fciaharhik avspetlrtm iiaraqrels vdhsdspive n
//
LOCUS       WP_285084957             686 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Gardnerella vaginalis].
ACCESSION   WP_285084957
VERSION     WP_285084957.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..686
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=75200
     Region          10..606
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mlrefavevi hptndgdtiy sllanramrd pqgviaqwqd ddtrqwhdvt asemllkvra
       61 takglialgv ergskvviys ptcyewgvad facacigavt ipiyetdsai qaaeiisevk
      121 pviafagdde haqclervrq dnkrmslkti fnfkaagida vidfgksisd delnksicqv
      181 kaddlativy tsgstgkpkg amlsnrnfth ivyaaydvln dmlykpsrll lflplahcfa
      241 ryiqyvaigs hgvigyvpna khlladlrsf kptyllgvpr vfekvynaas qkagagirgr
      301 ifakavqhfi ewskdevegr thsiyaklqh dfymktvgss irsalgpnls wlacggapin
      361 aelahffngl dgitfiqgyg mtetaapcvv nfehanqvgs vgrpgpgiti riaddgevlv
      421 kgpnvfigyy dkpdltsdvi dedgwlhsgd lgeiddegfl sitgrkkdii itaggknisp
      481 aplesiiskc plvshavvvg dgkpfvsali evepdmvrsw lksqgmdenl smsavaenda
      541 irsvvqqfid qanstvsrae sirkfiilde efsqetgtlt psmkvvrpkv lkrycdlien
      601 qlyapkpnsk plpatvkild kttetvkqaq etvkqaqeav tprvkqaidq aathlkrfge
      661 dlptqvnvkd qhteyaeknn nsndke
//
LOCUS       WP_285084999             556 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Gardnerella vaginalis].
ACCESSION   WP_285084999
VERSION     WP_285084999.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 556)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 556)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..556
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=61534
     Region          <327..395
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mpwrvkstit ggktisvada seyktksakl qelsndfhsl stswmqaamq iesqkssvfs
       61 ennknfngyf nddslqplld paecrikssq ceslsnklde lssliirann lyanaeyknr
      121 enldnlvsig tsifpitavp ffasvgfsil ldmtqksgmk nfskwsheta piqqgfirgf
      181 skhflinpvt gipirlfssi qekndvkhsk apvstfasal slfsakinda nqgnslkvtk
      241 irlphreysk ilhyrgsnis qalanltdls ngnlgvkppk inadaatiai qrfkkkdgsi
      301 swlvtipgtd gkpkspfgwp qnaevmsssk nvrqnadsir mvieamrksg ikakdsvilv
      361 ghsqggivaa siasdyskqy nirhivtags pianhpipnk twvtsiemed elvptldgas
      421 npnrnnwvti hgtakksaia rngtiapkta hnaiynslvv ngiksqnknk ennkknnkqy
      481 rtksyknekl fekdgilvkn vpeegtlthd lnyhkaayed shqlgskeir mqeehfrktl
      541 gdeleettlw qgimsh
//
LOCUS       WP_285085311             234 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase, partial [Kingella kingae].
ACCESSION   WP_285085311
VERSION     WP_285085311.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..>234
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
     Region          8..>234
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mqtllsslrh rfiqapmaga qdaqlaiavc qagglgslpa amyspeqlda qlstfrqavg
       61 napvnvnffa hetpnpsaeq vvrwqsalqp ycaelgvdls qvalqdtrrp fdetmlpvla
      121 khrpavvsfh fglpssplld avrvtgakil ssattvrear ylaeqgvdgi iaqgweaggh
      181 rgwfldkddv atqsgtfall pnivravdll viaaggiadc atvqtafalg aaav
//
LOCUS       WP_285085493             713 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Kingella kingae].
ACCESSION   WP_285085493
VERSION     WP_285085493.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 713)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 713)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 713)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..713
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=75233
     Region          4..712
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 matqhinfni qgmtcqacan riekvlnkkk fvseavvnfa getaqitfdd tqtnpdelik
       61 iiektgfqaa vqtsllpetd sheshwrvwt llalslpfwv gmigmigssh almpplwlqi
      121 aistvaqtyf alpfykgaia svrgglanmd vlvsvgtlsi ylyslgmvla gqahhvyfea
      181 gvmvlafvsl gkyleaktkr gslnalgsll qltprdvqil qnnqwqtvki dqvkqgdilr
      241 cvqggriaad gevvsgegwa deshltgesq pvyktignkv lagsilsgsl dyraeslgsd
      301 tllgdmvaal adaqgskapi arladkvatv fvpsvlaisl ltlvanwliv gdftaalvra
      361 vavlvvacpc alglatpaai magmgqavqh gvwfknaaal emagavdtvi ldktgtltqg
      421 kpdiaaiwta dsftenqlfe iaaaveqyaa hplanaivqa afareiapln aenvntvage
      481 gisanidglg dvkvgkldfc gfrlpenlad nvwniaslva vslnnqpvga faladplkpd
      541 slaaiqrlre hniavhilsg dnaatvahia qqlglpenha hgnqsprqka efiqqlqqqg
      601 akmamagdgi ndapalalad vgfavrgstd iveqsadavl vqqsvnqlas glivaratlr
      661 aikqnlffaf iynalgipfa avglltpvla gammalssvs vlgnalrlkr mkf
//
LOCUS       WP_285085644             227 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease, partial [Kingella kingae].
ACCESSION   WP_285085644
VERSION     WP_285085644.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..>227
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          32..>227
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mftkyilpil aigllalfcl gigegtwqnp ftiddvmrei rlpriivsll vgaalsasga
       61 alqalfenpl adpsligtsg gaaigvvvvi amgwgsigvp laaflgafgv cmlillvhrw
      121 igggkygllv lgfvlsalcs slvslilfms ddmalrsamt wlagsfseag fislsyaasi
      181 mligwlilla igrqldclll gdeaaqtmgi siaktrtlti igaammt
//
LOCUS       WP_285086056             408 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Kingella kingae].
ACCESSION   WP_285086056
VERSION     WP_285086056.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..408
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=46742
     Region          295..392
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mnisskfsvh nsawaasfvl lisfllgwan akwlsgwidn qdyiiriwfl iclvplvgia
       61 frqnqaklsp tlnafnkqri igkmkafvlq lvcvvcmafl amqvaseyaa tfmtfvgdmi
      121 fivpviills pfyitfvdrr lanpedeyak igamfvdknk idveiiksfm lktlvksifi
      181 pymyggfign lalllstpva anpvtlslll fnigisidml igvfgylvts slinnqvkdt
      241 drnflgwafa lvcypplfdl lhnlhqqtdn liwsdilpnn sivywimfga invlwiiywl
      301 atiefgmgfs nlswrklvnt gvyrytkhpa yvaknlywwl htlpfcgvaw fsanwwhnml
      361 alfgtslvyy gracseerhl mkfpeyraya ehiskhglfr klklpfik
//
LOCUS       WP_285086180             365 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Gemella morbillorum].
ACCESSION   WP_285086180
VERSION     WP_285086180.1
KEYWORDS    RefSeq.
SOURCE      Gemella morbillorum
  ORGANISM  Gemella morbillorum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Gemellaceae;
            Gemella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Gemella morbillorum"
                     /db_xref="taxon:29391"
     Protein         1..365
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40027
     Region          1..358
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mkvaiigggi vgatcayyls knkdieltvf dygvgqatka sagiispwfs krrnkpwykm
       61 arlgadfylk lvqdleaegi ntnfysqcgv yllkkdeakl pelkelaesr melspmigel
      121 kllskedvqk vipsfdnngd vlyasgggrv egerfvktll easraqvvnk kvslelagdk
      181 ylvdnkefdv vvlatgawlk dvleplgfav dvrpqkgqlr dykikdnntg aypvimpege
      241 ldiipfengv vsvgathend mgfdlgidrt qldvfgneaq qflkeladaq iinervgira
      301 ytsdfspfyg evptlknvfa vsglgssglt tgpiigysva niilgrenel dsqdydinsy
      361 islkd
//
LOCUS       WP_285086184             320 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Gemella morbillorum].
ACCESSION   WP_285086184
VERSION     WP_285086184.1
KEYWORDS    RefSeq.
SOURCE      Gemella morbillorum
  ORGANISM  Gemella morbillorum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Gemellaceae;
            Gemella.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Gemella morbillorum"
                     /db_xref="taxon:29391"
     Protein         1..320
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36956
     Region          4..217
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mgekisvivp vynveqylek cvesiinqty knleiilvnd gstdnsgklc delakkderi
       61 kvihkenggl sdarnrgiee atakvigfid sddyidkdmy kilfenlnkt gadlsmcghy
      121 dvfngvipnq venievklls siqainmvme akvmsvtavn klykkdlfnd lkfeigkiae
      181 dafimiklld kcqtivatne kkyyyihren sittqkfslk flnvieayeq nyklieqkyp
      241 ellsvaqmrm nwayfyvldk lllddnykdi dlenklinyl kknkknilsn tsftvgrklg
      301 fisllfnrni ykkiiekrgy
//
LOCUS       WP_285086203             287 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Gemella morbillorum].
ACCESSION   WP_285086203
VERSION     WP_285086203.1
KEYWORDS    RefSeq.
SOURCE      Gemella morbillorum
  ORGANISM  Gemella morbillorum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Gemellaceae;
            Gemella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Gemella morbillorum"
                     /db_xref="taxon:29391"
     Protein         1..287
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32805
     Region          4..277
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mieiivnskh kkslleleki enilnrekie yrvlktsetk naqklmdevs snqiiviggd
       61 gtinevinny heediiylgq gsgndlarsl qlerssscii klinssdfna ydvgdvngkk
      121 fcsgfdigfn advierveks rlkkyfgsyi ylvegvitil klkkyyakiq vgdsiletdk
      181 lrllnvmiqp yegggirfsn tatgrdgqfh imimtdmswf rfvynyicll lnkhnklkgi
      241 kvlkadslsv etsqshyqid gelvakdkkm qlkcikefyk ikkeerk
//
LOCUS       WP_285086330             410 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Gemella morbillorum].
ACCESSION   WP_285086330
VERSION     WP_285086330.1
KEYWORDS    RefSeq.
SOURCE      Gemella morbillorum
  ORGANISM  Gemella morbillorum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Gemellaceae;
            Gemella.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 410)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Gemella morbillorum"
                     /db_xref="taxon:29391"
     Protein         1..410
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=46522
     Region          <181..384
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mfkslrrkfv asavvsvavv itlmavtlnf inyykleqri detlhetaks qtlvalfkeg
       61 aendlvitkn tssatdstgf saakvnsegk iersyrddal issqkdlqsy idkiytngqe
      121 sgfigsyryl kaetktgnvi lflncqrdle syysfvrnti iissivilsv liiivmvskk
      181 viapiqqsyv kqkqfitdas helktplaii ssntdvlele hgnskwtkni qnqverltsl
      241 vnslvafsrm eekdtvervk fdltntlksr indfnelanf qkkfiatdid nnlyyngdqq
      301 aiiqlmdill enaikyapqn sdinislkkn rryatmkisn kanvkkgdlr kvfdrfyrld
      361 esrnshvkgy giglsmaqvi aekhkevika yapkdgifsi etrftldekk
//
LOCUS       WP_285086399             713 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Gemella morbillorum].
ACCESSION   WP_285086399
VERSION     WP_285086399.1
KEYWORDS    RefSeq.
SOURCE      Gemella morbillorum
  ORGANISM  Gemella morbillorum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Gemellaceae;
            Gemella.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 713)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 713)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 713)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 713)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Gemella morbillorum"
                     /db_xref="taxon:29391"
     Protein         1..713
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80899
     Region          1..>432
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 meilftiaif ivlvitgsfi nryipripaa lfqvmlgffi tylpiplhfe feseafmalv
       61 iapllftday kasrselwly krpivymsvg lviatvlvvg sfinfiipsi slgasfalaa
      121 ilsptdavav ksitkgmklp kglmailege sllndaagiv sfkialaaii tgtfsfanas
      181 keffiaaigg mflgiilglv tislkslnrk flnseptilv itqvilpilv yfaaekfhls
      241 giiavvftgi llnfekylfq geslnnqgvv sinynqdtvs yilngfvfvf lgyllpdifs
      301 nmvkfpdldi ktgllyvali tialivsrfi fvylfylsfq phtfntsnki ieflktkkld
      361 vgnysrfeya lisslcgihg tvtlatalmi pltlestgqp fplrdailfi asgvvllsmi
      421 igtiflpiti kkeeneeifl nnarskilge videlqtkyy nnldttpdrm gyaiaikklq
      481 eqqiyfcnde krlvhyskkl valiekeeqk kineilieye nnrhlrhile vrkwrlkkll
      541 tysvfkqlfi tlklsilegk frrllvllnl atddmsssta nqhriekhlr nrlktnvelr
      601 qqikefrhsi pdiidsltyn ainiienqkt kentliidfl kniydnfdyt lynapsnsyv
      661 eesrkfetea iaiqkekinn lkiqkkishh eadtllrdln yneallyann iee
//
LOCUS       WP_285086567             239 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Gemella morbillorum].
ACCESSION   WP_285086567
VERSION     WP_285086567.1
KEYWORDS    RefSeq.
SOURCE      Gemella morbillorum
  ORGANISM  Gemella morbillorum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Gemellaceae;
            Gemella.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Gemella morbillorum"
                     /db_xref="taxon:29391"
     Protein         1..239
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27758
     Region          1..155
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 myenlsivyd klmdvdyday aniiaqelgd kkdllildlg cgsgtmipyl kkygqvfavd
       61 nseqmlsias skspdnnffa mdlleisnlg yefdfilsaf dvfnylpdft sfkdglkevy
      121 cslksggkfi fdihtpkkmk nmidnqvfay etdeisylwf tygteqelev eseltffikq
      181 knglyrrleq fhtqrtyeie dissaakeig fkinkyfcdf eldnkdyena driifilek
//
LOCUS       WP_285086630             164 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator, partial [Gemella
            morbillorum].
ACCESSION   WP_285086630
VERSION     WP_285086630.1
KEYWORDS    RefSeq.
SOURCE      Gemella morbillorum
  ORGANISM  Gemella morbillorum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Gemellaceae;
            Gemella.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 164)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Gemella morbillorum"
                     /db_xref="taxon:29391"
     Protein         <1..164
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          <10..164
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 wnykkemidr kngevynvsp falvwndeny ymvaydnkkd likhyrvdkm rhvvidendr
       61 vghenflked issyskkifg myggilekvt lefkesligv vvdrfgkdii ihrkndvyqt
      121 svevisshfl gwifslgsdi eiiapqnvrn lyvkeiegll knyr
//
LOCUS       WP_285086634             226 aa            linear   BCT 25-DEC-2024
DEFINITION  tRNA (adenine(22)-N(1))-methyltransferase [Gemella morbillorum].
ACCESSION   WP_285086634
VERSION     WP_285086634.1
KEYWORDS    RefSeq.
SOURCE      Gemella morbillorum
  ORGANISM  Gemella morbillorum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Gemellaceae;
            Gemella.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Hori,H.
  TITLE     Methylated nucleosides in tRNA and tRNA methyltransferases
  JOURNAL   Front Genet 5, 144 (2014)
   PUBMED   24904644
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Roovers,M., Kaminska,K.H., Tkaczuk,K.L., Gigot,D., Droogmans,L. and
            Bujnicki,J.M.
  TITLE     The YqfN protein of Bacillus subtilis is the tRNA: m1A22
            methyltransferase (TrmK)
  JOURNAL   Nucleic Acids Res 36 (10), 3252-3262 (2008)
   PUBMED   18420655
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Gemella morbillorum"
                     /db_xref="taxon:29391"
     Protein         1..226
                     /product="tRNA (adenine(22)-N(1))-methyltransferase"
                     /EC_number="2.1.1.217"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0160105 - tRNA
                     (adenine(22)-N1)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25253
     Region          4..226
                     /region_name="TrmK"
                     /note="tRNA A22 N1-methylase [Translation, ribosomal
                     structure and biogenesis]; COG2384"
                     /db_xref="CDD:441950"
ORIGIN      
        1 mlainkrlkl vasyvedkrl adigsdhayl piylakenki nfaiageive gphkvsiknv
       61 keeglsgvie crkaagleai eladnievit icgmggklia dilekgkdkl inrpnlilqp
      121 nlgerfvrkk lqdlgytiia ediieedghi yeiivatdgh msltedeknf gkflskeknd
      181 lfikkqkqel dkvnyilsql ekakeeksek vlelqakakk ieevis
//
LOCUS       WP_285086717             266 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Gemella morbillorum].
ACCESSION   WP_285086717
VERSION     WP_285086717.1
KEYWORDS    RefSeq.
SOURCE      Gemella morbillorum
  ORGANISM  Gemella morbillorum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Gemellaceae;
            Gemella.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Gemella morbillorum"
                     /db_xref="taxon:29391"
     Protein         1..266
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31679
     Region          24..131
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 menynndknt yikrmnktal skfdvlkpyl kkktkvldyg sgispdfirs vqqtgakyya
       61 ydisptvqne lanlnievit denlakskek ydiifmssvf heiisymsrp ertkvlkqih
      121 rnlkkdgkli irdwanknsd ipytlhvkne kvskevdrwv kklkensiiq nvekfdnkey
      181 qttekeayel vfhvvwglqs lereskeeyn ihdylekwll kplnfkissi ieekdesylq
      241 ylqkyfklke vpfytkcili lekeei
//
LOCUS       WP_285087312             155 aa            linear   BCT 25-DEC-2024
DEFINITION  segregation and condensation protein A, partial [Kingella kingae].
ACCESSION   WP_285087312
VERSION     WP_285087312.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         <1..155
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
     Region          <7..142
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 mcirdrlaye qmklaaqdld alpragrdfa wvylplelav ptrlpevqia dltqawltil
       61 sraqqnrsha vvqevvsvre rmtailrkln agslhfsqlf nselgaahvv vnfiallelv
      121 keglvrvlqd thfgeievqa ashiadveii erese
//
LOCUS       WP_285086878             447 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Gemella morbillorum].
ACCESSION   WP_285086878
VERSION     WP_285086878.1
KEYWORDS    RefSeq.
SOURCE      Gemella morbillorum
  ORGANISM  Gemella morbillorum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Gemellaceae;
            Gemella.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Gemella morbillorum"
                     /db_xref="taxon:29391"
     Protein         1..447
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50609
     Region          <154..447
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mlkkikeiif kpfrritltf kitlwytifi villtsiilg tffvsdsive ssgkkkliee
       61 vteisngken ftafedgvtl slydkdgnli egsipknfdv rdfslgvvty ytdsknnkym
      121 yydietnsek fangkyvrgi vqissgqtsw ylpfaiiags piiiliityg gyliissslk
      181 pvremietae tisnsadlsk ritiedgkde vhklalvfne mleslerasm rerqfssdvs
      241 helrtpisvi vaeseygtky idtvgeakes favikrqskr mtiminqile marldnrlei
      301 pkeffdlssc leetledykk lfetkdiqli tniddnitlf gnqvllirli dnlvsnalky
      361 anskiwisia krnniiievs ddgrgiadde kayiwdrfyk vdksrsised nssglglpis
      421 kkivelhgge iaaldnkpqg akfvinl
//
LOCUS       WP_285087470             715 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase, partial [Kingella kingae].
ACCESSION   WP_285087470
VERSION     WP_285087470.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 715)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 715)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 715)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         <1..>715
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          48..694
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 glgsyyknrt anaekaalpp deilaqlkly dlpevqaefv evlpqnekea mlmlsgitca
       61 actwlieqql lrqsgivkve lnystqrarv rwdnsrvqls qilhliqqtg ytaspydtqk
      121 veaqaqrerk kmlirlavag lvsmqtmmfa lptylygdie pqyltilhwg gflmvlpalf
      181 ysaqpfyqga wrdfrnkrtg mdtpialait mtfiaglgal wkgaseglyf esiamlvffl
      241 ligrfmeqsa rrkagdaaer lvrlvpafch kiinlyaeqt eeaavvtlks gdvllvrage
      301 ivpvdgvvlr geseineaml tgesvpiqkk sgsqvtagtl ntaspliiqa qqvgnqtrla
      361 hivklldral sqkprlamla ekyasvftla qivlaiptfi awwwyadvvq avwivvallv
      421 itcpcalsla tptalaasmg rlanagvlva rghaletlaq vsdavfdktg tltegklsvt
      481 qfhnfsgslh dtdliaiakl leqhsehpia railnlsltl pplvregwgg gshsatqmde
      541 stenhihiaq klnkighgvs aqitlhnhtq iwaigkpdfv aeisgslpek lselaqqgsv
      601 ivlgnqhgfq aafllrdtvk adaadvlaal rsqsiavhil sgdiaaavnq laddlaierr
      661 qaaampedkl ryvqqlqaqg krvlmlgdgi ndapvlaaad vsvavagsad vardg
//
LOCUS       WP_285087619              51 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsB family cell division protein, partial [Kingella kingae].
ACCESSION   WP_285087619
VERSION     WP_285087619.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 51)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 51)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..51
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         <1..51
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
     Region          <1..51
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 kqqndmlrre nemlraevqd lengfdtkae iarsemgyig dgeifynlkp d
//
LOCUS       WP_285087970             198 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Kingella
            kingae].
ACCESSION   WP_285087970
VERSION     WP_285087970.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..>198
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          41..102
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
ORIGIN      
        1 mserewvifq vavgvipapa fsdfeialkk vpsyakpefi pptpteikqf lkengltqaq
       61 aaaclgiger sfrryvsgek pytmsetnwk lleqlskeka ilpenpdssd fpqpepiska
      121 deiqkafddl ahaadvvkkr nnkreadflp ifemqfvvie ksknqsalff rlpdyvnmcw
      181 smwhgfllpk demhnlla
//
LOCUS       WP_285087987             120 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Kingella
            kingae].
ACCESSION   WP_285087987
VERSION     WP_285087987.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..>120
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          11..61
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(13,17,42)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(16,41)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(23..24,35,38,42..43)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mfypdiptpd eikafrvshg lanyqaanli nvnlsswtry ekgtmkptvf nwalllnald
       61 vlelpendpl tpfarralsf vpptalkagn erqgyippkp eqitklreka gltrvqcndl
//
LOCUS       WP_285088480             226 aa            linear   BCT 25-DEC-2024
DEFINITION  tRNA (adenine(22)-N(1))-methyltransferase [Gemella morbillorum].
ACCESSION   WP_285088480
VERSION     WP_285088480.1
KEYWORDS    RefSeq.
SOURCE      Gemella morbillorum
  ORGANISM  Gemella morbillorum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Gemellaceae;
            Gemella.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Hori,H.
  TITLE     Methylated nucleosides in tRNA and tRNA methyltransferases
  JOURNAL   Front Genet 5, 144 (2014)
   PUBMED   24904644
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Roovers,M., Kaminska,K.H., Tkaczuk,K.L., Gigot,D., Droogmans,L. and
            Bujnicki,J.M.
  TITLE     The YqfN protein of Bacillus subtilis is the tRNA: m1A22
            methyltransferase (TrmK)
  JOURNAL   Nucleic Acids Res 36 (10), 3252-3262 (2008)
   PUBMED   18420655
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Gemella morbillorum"
                     /db_xref="taxon:29391"
     Protein         1..226
                     /product="tRNA (adenine(22)-N(1))-methyltransferase"
                     /EC_number="2.1.1.217"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0160105 - tRNA
                     (adenine(22)-N1)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25241
     Region          4..226
                     /region_name="TrmK"
                     /note="tRNA A22 N1-methylase [Translation, ribosomal
                     structure and biogenesis]; COG2384"
                     /db_xref="CDD:441950"
ORIGIN      
        1 mlainkrlkl vasyvedkrl adigsdhayl piylakenki nfaiageive gphkvsiknv
       61 keeglsgvie crkaagleai eladnievit icgmggklia dilekgkdkl inrpnlilqp
      121 nlgerfvrkk lqdlgytiia edtieedghi yeiivatdgh msltedeknf gkflskeknd
      181 lfikkqkqel dkvnyilsql ekakeeksek vlelqakakk ieevis
//
LOCUS       WP_285088721             636 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Gemella morbillorum].
ACCESSION   WP_285088721
VERSION     WP_285088721.1
KEYWORDS    RefSeq.
SOURCE      Gemella morbillorum
  ORGANISM  Gemella morbillorum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Gemellaceae;
            Gemella.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Gemella morbillorum"
                     /db_xref="taxon:29391"
     Protein         1..636
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=74637
     Region          26..630
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 meifnydnrs lrllnilesn flvqdkylid vlkvssktin neikslneif gscayieskn
       61 snyslyiikl eeylkkkrsi yeagenfdss kvrlvyifkk lvstsdgqli ddlafemivs
      121 rttlntdlkk lneiindynl vikgkpnigi kivglekdir ifileniyny mykedifdke
      181 dnkffdemfv kykideqakg eflkyltvsi drfangfrln lvenqyeell dsyakdfike
      241 vceyttlkyg itlnqdemkf laicfatmrv ptkinkiren lkyteeykkl vqeileivvy
      301 eyglkfdtsd iieefiyhiy flmerlkygv ryhnnmkeki kkdfpvsyki artasevite
      361 kyqysvsede isylaiyfet flkkikiqpd nlkillvtna gpaykklmik elenisqsse
      421 itvvttyenv kyddfdiiis tvnknfetai piiyqneild ivylkkeinf lryvnkmnnp
      481 airgmesivl ssmsestffi cdnrktyeen letmikglea kgfvdkefll rirereqkss
      541 mifadsvafp htqnekensl lialgvckdg fkdnkelkli flacvpkdgd qglllaktyd
      601 elisiikdkk liddiskveg ynslvnyfik htnlyr
//
LOCUS       WP_285089335             221 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Pediococcus acidilactici].
ACCESSION   WP_285089335
VERSION     WP_285089335.1
KEYWORDS    RefSeq.
SOURCE      Pediococcus acidilactici
  ORGANISM  Pediococcus acidilactici
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Pediococcus; Pediococcus acidilactici group.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Pediococcus acidilactici"
                     /db_xref="taxon:1254"
     Protein         1..221
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=24418
     Region          12..221
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mstdpkifgs klkelrekhr ftvrqvakqa dissaywsql engkrnvpkp vtlnkiadgl
       61 reprdlifni agylpeknkl pdniqpaspe nfvglpvvgv ikagpngvam eehlgtefti
      121 kdnldmsfdy fwlkvsgdsm igdgindgdy amikktldfn ngdicavivd geegtlkhit
      181 ksadtivlta snpayeprvf igkemnkimi agklvqtmrk y
//
LOCUS       WP_285089684             214 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial [Kingella
            kingae].
ACCESSION   WP_285089684
VERSION     WP_285089684.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..>214
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          4..>214
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mqilkafkfe lipngaqvrk mkqfcgcsrf vfnralayqn kqyqkdnsfk fsyakianll
       61 pewkrelvwl kdchsqvlqq slkdleasfk nffakrsdfp kfkrkgekds frfpqgckle
      121 qqnnriylpk mgwvryrnsr aisgslknvt vsqkcgkwyv siqtefetet pkpnggeigi
      181 dmgivrfatl sngeyfepin afknlkgkla klqk
//
LOCUS       WP_285089622             127 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl-CoA carboxylase biotin carboxyl carrier protein [Pediococcus
            acidilactici].
ACCESSION   WP_285089622
VERSION     WP_285089622.1
KEYWORDS    RefSeq.
SOURCE      Pediococcus acidilactici
  ORGANISM  Pediococcus acidilactici
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Pediococcus; Pediococcus acidilactici group.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Li,S.J. and Cronan,J.E. Jr.
  TITLE     The gene encoding the biotin carboxylase subunit of Escherichia
            coli acetyl-CoA carboxylase
  JOURNAL   J Biol Chem 267 (2), 855-863 (1992)
   PUBMED   1370469
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423502
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Pediococcus acidilactici"
                     /db_xref="taxon:1254"
     Protein         1..127
                     /product="acetyl-CoA carboxylase biotin carboxyl carrier
                     protein"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=13891
     Region          20..124
                     /region_name="AccB"
                     /note="Biotin carboxyl carrier protein [Lipid transport
                     and metabolism]; COG0511"
                     /db_xref="CDD:440277"
ORIGIN      
        1 mkidkvydil nrlkdypyqe isiemeglkl hvkkadsapt apptpaqvtd pqpagmvvks
       61 pmvgivhfnq dltprqlvek gqviaqiesm klfndikapq agtvqrllve dgegvaydqp
      121 lvelvgk
//
LOCUS       WP_285089773             130 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Kingella
            kingae].
ACCESSION   WP_285089773
VERSION     WP_285089773.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..>130
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          12..70
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(16,20,46)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(19,45)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(27..28,39,42,46..47)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mskskiqdsa fsermkllle tkfgnnnsef arsvgvavts lnrwldgdad psrtnlirla
       61 qaadaniewl algigepfpq apkiqaatts emdeqaamqs sldktaqfia qqqaakrkak
      121 latqranglc
//
LOCUS       WP_285089946             167 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Peptoniphilus lacrimalis].
ACCESSION   WP_285089946
VERSION     WP_285089946.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus lacrimalis
  ORGANISM  Peptoniphilus lacrimalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Peptoniphilus lacrimalis"
                     /db_xref="taxon:33031"
     Protein         1..167
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=19731
     Region          55..162
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mknknnlpif gvgpfyvitc liitlfslll iknghfkfat ikkemilhsi fnllayffii
       61 fgiylwvrav iiqkvnkkvq qgillkdgiy sivrnpiysa flfiftgvlf lsmnyillvl
      121 pfffwifltv lmknteekwl rekfgkeyid yckdvnrvip wfaknky
//
LOCUS       WP_285089953             431 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Peptoniphilus lacrimalis].
ACCESSION   WP_285089953
VERSION     WP_285089953.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus lacrimalis
  ORGANISM  Peptoniphilus lacrimalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Peptoniphilus lacrimalis"
                     /db_xref="taxon:33031"
     Protein         1..431
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50891
     Region          212..427
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mfnyiikrfk kivirilflm fllifllmtf lylnyrlynk ypkpddvysy vennksdlyl
       61 seknkeflkr eniwairldr egkiiesfnk pkvvkdkfel rdvagftryy lndypvftyi
      121 vgdgllvfay pknsldkfpf nyynyenfif ninlivfsll lflvfvyviy kidikeifkn
      181 ilpfqraidt lyeddyekld eygelkelaf sinranekyn nlkesqskwi rglshdvrtp
      241 lakiswelsk enkedidtqn ikdqvlkisn ileglnltls lsnidkenfk lesplkvirk
      301 livdklnenp greiifeskv kdqnikinmd anlfyrmlen ilknaliyte gkiqvrisdd
      361 nnnllisild egggisensi ekikkddltn itrhglgifi skqiaelhdg tftiknkdkg
      421 levsfifkft n
//
LOCUS       WP_285089970             135 aa            linear   BCT 25-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Peptoniphilus lacrimalis].
ACCESSION   WP_285089970
VERSION     WP_285089970.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus lacrimalis
  ORGANISM  Peptoniphilus lacrimalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Schwartz,C.J., Giel,J.L., Patschkowski,T., Luther,C., Ruzicka,F.J.,
            Beinert,H. and Kiley,P.J.
  TITLE     IscR, an Fe-S cluster-containing transcription factor, represses
            expression of Escherichia coli genes encoding Fe-S cluster assembly
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 98 (26), 14895-14900 (2001)
   PUBMED   11742080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Peptoniphilus lacrimalis"
                     /db_xref="taxon:33031"
     Protein         1..135
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=15371
     Region          2..131
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mkitqetdya fritsflash eneiigapii aqecsvterf tlrilrklnl agityakrga
       61 kggyglkrpk eeitlyqiic aiegptvinr clahdhycnr ktiegvkhck fhnklfhiqk
      121 siinmfnset idnyi
//
LOCUS       WP_285089973             336 aa            linear   BCT 25-DEC-2024
DEFINITION  threonine aldolase family protein [Peptoniphilus lacrimalis].
ACCESSION   WP_285089973
VERSION     WP_285089973.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus lacrimalis
  ORGANISM  Peptoniphilus lacrimalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Peptoniphilus lacrimalis"
                     /db_xref="taxon:33031"
     Protein         1..336
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38452
     Region          31..332
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mnnflndykd fgckeiyenm qkifdnnycg ygldeisnna rqllkneikk dsqiefisgg
       61 taanilattf alrpyeavla ldsghishhe tgsieatghk vinitspdgk mkvhqikdll
      121 nnmseeidvk ikvvyisqtt ekgtvyside ikkiydfcld nglylyidga rlahamaann
      181 skledygkys hifsiggtkn gaifgeaivi ldenlrknfr yyikqrgamm aksflislsf
      241 qtlftdglyy knayhawems rlmvdelkkl drepifcesn qiflksnpee ieflkkenif
      301 evddkkesii rlvtdyrtnk edirgfissl kkwgtd
//
LOCUS       WP_285090151             468 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Peptoniphilus lacrimalis].
ACCESSION   WP_285090151
VERSION     WP_285090151.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus lacrimalis
  ORGANISM  Peptoniphilus lacrimalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Peptoniphilus lacrimalis"
                     /db_xref="taxon:33031"
     Protein         1..468
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52620
     Region          131..459
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mknrigkrlv ksyllliitt ivildiflli gfktfyytsv enelksrlsf slnfynrnys
       61 dknlediile dndilwtytn aevqvltpkg niiidsigai skepinsqdf llaksgtmka
      121 wvgkcpttkg lvmaitgpii nnsgktigyl rfiasmeean lailktmltl vvfsivlsii
      181 taivsilisr sivrpitdlt evarkmadgq ykikarnwed deigelaktl ntmseeilkk
      241 eqikndfiss ishelrtplt sikgwavvlk dskgqedims egltiienes drlskmveel
      301 ldfsrfisgr mslekelfdi gqtvrdvckq mkpransnki dfqtelletp cvtigdenri
      361 kqllinivdn aikftsengw vkvqsfdenn nfvilvsdng cgmnkkdleh vkekfykgkh
      421 skshsglgls isdeivklhn gsldifseln igttvkitil iikeekae
//
LOCUS       WP_285090162             328 aa            linear   BCT 25-DEC-2024
DEFINITION  DHH family phosphoesterase [Peptoniphilus lacrimalis].
ACCESSION   WP_285090162
VERSION     WP_285090162.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus lacrimalis
  ORGANISM  Peptoniphilus lacrimalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Peptoniphilus lacrimalis"
                     /db_xref="taxon:33031"
     Protein         1..328
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=37000
     Region          10..323
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mvknfneyik ileekinkan tiaiashmnp dgdnlgsklc lyklfknlnk evyviendqv
       61 ptaekflpgv ehlvdsdtle dkkidlmivt dcgdierigr aesifkkadf tvnidhhetn
      121 vefadlnlvd mkapavcefl ylilkqmnfs idkdmatcly tgistdtgsf kydsirpltf
      181 evaiellkig idinkitvnl yqrrskekte lliralnnis yyennkiglv sinekdifet
      241 garksdsdgi vefvrdidgi elsiflnekk dcyklstrsk tyvdctkiak vfgggghira
      301 agatlykkdy pnlcdainri idlssnei
//
LOCUS       WP_285090207             181 aa            linear   BCT 25-DEC-2024
DEFINITION  SGNH/GDSL hydrolase family protein [Peptoniphilus lacrimalis].
ACCESSION   WP_285090207
VERSION     WP_285090207.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus lacrimalis
  ORGANISM  Peptoniphilus lacrimalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Peptoniphilus lacrimalis"
                     /db_xref="taxon:33031"
     Protein         1..181
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=20771
     Region          4..180
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 mknkylalgd sivegyklqg ksfvyylskd fdianrglng lssnllkyyr gdlkpfthvi
       61 vhigindflq gydnaqveks imelvdifks edlkiiflkp viiaqeacdy nwcskthypl
      121 ikerlinyre fldklgqenn fkiidlmdtt gidiydnlmd gihpnlklsk amgkyistkl
      181 l
//
LOCUS       WP_285090334             210 aa            linear   BCT 25-DEC-2024
DEFINITION  IMPACT family protein [Peptoniphilus lacrimalis].
ACCESSION   WP_285090334
VERSION     WP_285090334.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus lacrimalis
  ORGANISM  Peptoniphilus lacrimalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Park,F., Gajiwala,K., Eroshkina,G., Furlong,E., He,D.,
            Batiyenko,Y., Romero,R., Christopher,J., Badger,J., Hendle,J.,
            Lin,J., Peat,T. and Buchanan,S.
  TITLE     Crystal structure of YIGZ, a conserved hypothetical protein from
            Escherichia coli k12 with a novel fold
  JOURNAL   Proteins 55 (3), 775-777 (2004)
   PUBMED   15103642
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Okamura,K., Hagiwara-Takeuchi,Y., Li,T., Vu,T.H., Hirai,M.,
            Hattori,M., Sakaki,Y., Hoffman,A.R. and Ito,T.
  TITLE     Comparative genome analysis of the mouse imprinted gene impact and
            its nonimprinted human homolog IMPACT: toward the structural basis
            for species-specific imprinting
  JOURNAL   Genome Res 10 (12), 1878-1889 (2000)
   PUBMED   11116084
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Peptoniphilus lacrimalis"
                     /db_xref="taxon:33031"
     Protein         1..210
                     /product="IMPACT family protein"
                     /calculated_mol_wt=23494
     Region          1..194
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 mynsvlsgge gdfvekksrf igggyfvkse eealnkisqi keiykdathn tyayiigkda
       61 kiqrysddge pqgtagipml evlkkeemrn vlvtgtryfg gillgsggll raytkcarlg
      121 llaakkvvre nfnrtkfsyd ytyhgkilny lkingykilq eeftdiaslt lyvkenasii
      181 kdlkdmtgak ikievkacee lptidgkimr
//
LOCUS       WP_285090356             380 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Peptoniphilus lacrimalis].
ACCESSION   WP_285090356
VERSION     WP_285090356.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus lacrimalis
  ORGANISM  Peptoniphilus lacrimalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Peptoniphilus lacrimalis"
                     /db_xref="taxon:33031"
     Protein         1..380
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=44944
     Region          155..360
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(265..266,269..270,272,296,298..299,302..303,
                     305..306,329,332..333,336..337,340)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          265..289
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          294..323
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          328..356
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtieekleke inekierigf ielkenikik ddiylkkgid yplkfsylkk glrdksfyag
       61 idlekfidsm iyligikkdi nnsqiyikni kdilkdpfey iiskayeslk ndsasaiiyl
      121 qayenlygfd krilfskyqv ieyytdknrd efdykeleqa esniinnyld mieedekfap
      181 pylrlayiye nrghfikakl yfekylfysk eestkeevrq elvkiedyvs ieaaqtyiiy
      241 gdnfkalqal ekisldykdk mllnllkgkv nyalgkfeea skflelsyle kitdenasll
      301 amayaqegqi nkakkileea ieiekesnil yydlatinln enkleealen fkksyrlhsd
      361 eniekiikkl ketidkknks
//
LOCUS       WP_285090730             278 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Gallibacterium
            anatis].
ACCESSION   WP_285090730
VERSION     WP_285090730.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..278
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31850
     Region          5..232
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mnnnfklavn tsiydgydld tifnsikkcg fdyfelaynq gyvgnlnqdl fskenanyin
       61 qlkskysldt falgctmdls vdnlydifsp ritfanliga kyinvctttl enrenlilnl
      121 kslrsllemn kcilcienag dynfnafvdl sdgikilnel esdlysinfd pgnmvtydrk
      181 ldvvnqslns inycnhfhik dvkinndkfe fvpigegiid ysniirklke ndivsgleip
      241 lriyreldst pkrcsdkvdi nlieetliks rkyidnii
//
LOCUS       WP_285090904             192 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Gallibacterium anatis].
ACCESSION   WP_285090904
VERSION     WP_285090904.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..192
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=20888
     Region          2..192
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mkkiylgsns prrfqllqql glsvevlkge idetvgenet asdyvlrmai sknqqirylf
       61 pqksdypllt adtciafnhq ilgkphsaed afamlsmlsg nthqvltaic istpikqhsc
      121 lqasevsfks lsaeeihayi asgepfdkag ayaiqglaag fikhlsgsys gvmglplfet
      181 sellkkfstn il
//
LOCUS       WP_285091063             328 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Gallibacterium anatis].
ACCESSION   WP_285091063
VERSION     WP_285091063.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..328
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38087
     Region          17..327
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 matrskdida tllqieilri iprlpasiea ktiheklkdl gfnrdlrsiq rtlqalclhf
       61 ddlecnndik pytyywkers agfalpvlne qqslllklae kqlkyllpan imssmkpffe
      121 qadrmvsgty sndkekpthq wldkvcitpt slplipakie ddifsavsqa lyqnkllkie
      181 yqnssgkryv atimplaiaq qgasiylicr fdgfsdnril amhrickadi stfsferpkd
      241 fnlqvyqdeg ylgftryqti rkirltfsia kwagfhltet plsndqqile esdqhyrfra
      301 tlpendmldw wllkfgediw diereplt
//
LOCUS       WP_285091065             630 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF262 domain-containing protein [Gallibacterium anatis].
ACCESSION   WP_285091065
VERSION     WP_285091065.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..630
                     /product="DUF262 domain-containing protein"
                     /calculated_mol_wt=73897
     Region          5..528
                     /region_name="GmrSD"
                     /note="DNAse/DNA nickase specific for phosphorothioated or
                     glycosylated phage DNA, GmrSD/DndB/SspE family, contains
                     DUF262 and HNH nuclease domains [Defense mechanisms];
                     COG1479"
                     /db_xref="CDD:441088"
     Region          491..617
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mennqvrtlt iselcngdny iipiyqrnya wgrdeielli qdisealknk edkennyyig
       61 slvvakrkdg yevidgqqrl ttlklllsyf nknpninlnf eyrdesnqsl nnlgdnkygn
      121 sieigykfil difskkivke nkendfieef sgflldkvvi lrtevpedtd lnhyfeimnn
      181 rgeqlekhev lkarlmeklt gdddkklfal iwdacsdmsv yaikrfpysn denknirtsd
      241 affgelvnki penfdkmkdi lnkieytdke tnkesilnll eqtdnkinqd kgsdedgnfq
      301 siidfpnflm ivykifrggd vplndkylln kfeeigdepa tikefiilll kvrlifdryi
      361 ikskeeedsw ilngikkykd gsfrevntfg taleqlnkds dkdgdtddls knhiqivqll
      421 smfhtsfrqn kswlfdilek lsksselent yslsaveyie ileqlaydyy knskrqelfk
      481 sggqnipnyi fnyldyllwk dwdnrgkdnk flkksdfvfs lsrnsiehyl aqskrdsllp
      541 rneteenknr llnslgnlcl ishyqnssln devpsekrkr yesgslkcis pkqalmlsye
      601 iwgkeeiekh nedmieilds etkkyinnis
//
LOCUS       WP_285090459             713 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Kingella kingae].
ACCESSION   WP_285090459
VERSION     WP_285090459.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 713)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 713)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 713)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..713
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=75134
     Region          4..712
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 matqhinfni qgmtcqacan riekvlnkke fvseavvnfa getaqitfdd tqtnpdelik
       61 iiektgfqaa vqtsllpetd sheshwrvwt llalslpfwv gmigmiggsh almpplwlqi
      121 aiatvaqtyf alpfykgaia svrgglanmd vlvsvgtlsi ylyslgivla gqahhvyfea
      181 gvmvlafvsl gkyleaktkr gslnalgsll qltprdvqil qnnqwqtvki dqvrqgdilr
      241 cvqggriaad gevvsgegwa deshltgesq pvyktignkv lagsilsgsl dyraeslgsd
      301 tllgdmvaal adaqgskapi arladkvaav fvpsvlaial ltlvanwliv gdftaalvra
      361 vavlvvacpc alglatpaai magmgqavqh gvwfknaaal emagavdtvi ldktgtltlg
      421 kpdiaaiwta dnftenqlfe iaaaveqyaa hplanaivqa afareiapln aenvntvage
      481 gisanidgls dvkvgkldfc gfrlpenlad nvwniaslva vslnnqpvga faladplkpd
      541 slaaiqrlre hniavhilsg dnaatvahia qqlglpenha hgnqsprqka efiqqlqqqg
      601 akvamagdgi ndapalalad vgfavrgstd iaeqsadavl vqqsvnqlas glivaratlr
      661 aikqnlffaf iynalgipfa avglltpvla gammalssvs vlgnalrlkr mkf
//
LOCUS       WP_285091090             403 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Peptostreptococcus
            anaerobius].
ACCESSION   WP_285091090
VERSION     WP_285091090.1
KEYWORDS    RefSeq.
SOURCE      Peptostreptococcus anaerobius
  ORGANISM  Peptostreptococcus anaerobius
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Peptostreptococcus.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Peptostreptococcus anaerobius"
                     /db_xref="taxon:1261"
     Protein         1..403
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45021
     Region          2..402
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mskkglpleg irvieyanfv aapvcgrila dwgaevikie psfgdsmriv giqwcfpake
       61 denpmfeien agkkdividt ntkegveiiy kllenadvfl tntrqkaldk sglnykevkk
      121 raphiiyahl lgygekgpak dnpafdytay yarggvaasl mekgtspanp vaglgdhyag
      181 lglaggvaaa lykrketgkg ervtvslfht avfgmgimvs aahygyrmpi srknppnpln
      241 ttfkcsddrw iqiaffqydk wfpkfcdevi erpdlkdtky stlrsavnyv eefvemmeve
      301 fakrpvdewc drlqsagipy eklatteevl edpqcwengy lhrhtfesgh egvifntpvm
      361 fteapkpeyv rapklgehtk evlaeagigd aeleelkekk vil
//
LOCUS       WP_285091094             470 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Gallibacterium
            anatis].
ACCESSION   WP_285091094
VERSION     WP_285091094.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..470
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51263
     Region          1..445
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 meifhqlikd indplwnivt imllgaglyf tlsmffvqir llpqsireml garnvdrkha
       61 ispfqafvtg lasrvgvgni agvslaityg gpgavfwmwv tallgmssaf aesslaqlfk
      121 vkdlaghfrg gpayyitsgl kqrwfgwlfa icliitygfv fnavqsntia eagngawgwt
      181 peatgvalvi ltapmifggi rriskiaevl vplmallyia mavfilcknv sllpttihli
      241 issafnfdaa asgffgaifs qammygikrg lysneagmgs apnaaatadv dhpvsqgliq
      301 mlgvfvdtiv ictatavivl lsgesissgi tgaqltqlai ehqvgawgkd flalilfmfa
      361 fstiignyay aegnikfikn nptmimlfrm lvlvmvyfga vqkmqlvwdm adtfmglmam
      421 inliaillls pivwlllrdy qqqlkttksp ifkvekyphl asrvkaniwr
//
LOCUS       WP_285091280             378 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Gallibacterium
            anatis].
ACCESSION   WP_285091280
VERSION     WP_285091280.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..378
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=43900
     Region          3..378
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mqlrkafkfe impngsqirr ikqfcgcsrf vfnralawqn eqyeqdnsfk fsytkianll
       61 pqwkkellwl kdchsqvlqq slkdlesafk nffqqradfp kfkkkglker frfpqgckle
      121 qqnnrlylpk igwvryrnsr dvigeiknvt vshkcgrffv siqtefeyei pthkggeigi
      181 dmgvarfatl sngeyfepln afkiykgkla klqrqlknkv kfsqnwqklk akiaklhhki
      241 ancrkdflhq tsskisknha miyvedlqvs nmsrsakgtv eehgknvkqk sglnrsildq
      301 swfefrrqld yktiwnggfl vavppqntsr ccpncghtak enrqtqadfe cvecgytena
      361 dvvgalnvla rgrvivqa
//
LOCUS       WP_285091409             415 aa            linear   BCT 25-DEC-2024
DEFINITION  site-specific DNA-methyltransferase [Peptostreptococcus
            anaerobius].
ACCESSION   WP_285091409
VERSION     WP_285091409.1
KEYWORDS    RefSeq.
SOURCE      Peptostreptococcus anaerobius
  ORGANISM  Peptostreptococcus anaerobius
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Peptostreptococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Peptostreptococcus anaerobius"
                     /db_xref="taxon:1261"
     Protein         1..415
                     /product="site-specific DNA-methyltransferase"
                     /calculated_mol_wt=47168
     Region          11..98
                     /region_name="ParB_N_like_MT"
                     /note="ParB N-terminal-like domain, some attached to
                     C-terminal S-adenosylmethionine-dependent
                     methyltransferase; cd16403"
                     /db_xref="CDD:319260"
     Site            order(57,59..60,62..63)
                     /site_type="other"
                     /note="putative ParB Box II like motif [polypeptide
                     binding]"
                     /db_xref="CDD:319260"
     Region          169..396
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mittkemkli dieklvpyvn narthsqdqi nklrssiref gfinpviidk nygviaghgr
       61 imaakeegik evpcvfadhl neaqkkayil adnrmaldag wdeellrvei esledygfnv
      121 eltgfspdel sslfdlgvea eeddfdveee lkkptfsktg diwtlgshkv icgdstqwet
      181 fekllndtkv nlvctdapyf vdlknksgti kndnlndeea yeflmkvftn fkeamakdas
      241 iyefyatmka rvfydafeda gfkvgagliw kkprapfmrt dwkfnmepii fgwrkdgkhn
      301 wygdqkqtav fefdgikdse kegcghpssk pvpliaylik qstqtnglvl dgflgsastl
      361 iaceelnric ygieiepkfv dvavkrylnl vgsdeeikll rngkeykyle vvkde
//
LOCUS       WP_285092006             603 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Peptostreptococcus
            anaerobius].
ACCESSION   WP_285092006
VERSION     WP_285092006.1
KEYWORDS    RefSeq.
SOURCE      Peptostreptococcus anaerobius
  ORGANISM  Peptostreptococcus anaerobius
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Peptostreptococcus.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Peptostreptococcus anaerobius"
                     /db_xref="taxon:1261"
     Protein         1..603
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=68161
     Region          158..601
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mpierinidc iqdeiekvaq aislvldidv tivnddmvri agtgvykdkl gqkiegmsaf
       61 kksyrekktl iidnpkvsdl crdcyrlgnc meeaevccpi ilddqcygvi gliafdqvqk
      121 tkllssrdel iqfiekmadl isgniraeik sseynierek iaqvlnsidr pvvsldemar
      181 idsfnykfsk mfsigpdvqg rsikealeff dletlfdfkk sdrnsdkfyy eykayrgiys
      241 iakiryggvv sgyvidfidn keaiqtynrm nvdhrmtidd iigksraimd vkrdalnaak
      301 ststilitgq sgtgkemfar athshsdrsd gpfvtincaa ipgellesel fgydegaftg
      361 akkggklglf eiankgtifl deigdmglhl qakllrvlqe keihkvgggk nikvdvriis
      421 atnknladmv aegmfredly yrlnvipisi psleerkddi pllvdrmidv yshnlgkevr
      481 svsdrvisal keyswpgnir elqnvieysi nmtngsiidd vnlvysrfrk igpqvmektr
      541 vasqgegqdi eirtieslee dqirkalrky kdykkdkdla akalgisrat lyrkmdkysi
      601 evd
//
LOCUS       WP_285091481             266 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Peptostreptococcus
            anaerobius].
ACCESSION   WP_285091481
VERSION     WP_285091481.1
KEYWORDS    RefSeq.
SOURCE      Peptostreptococcus anaerobius
  ORGANISM  Peptostreptococcus anaerobius
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Peptostreptococcus.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 266)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Peptostreptococcus anaerobius"
                     /db_xref="taxon:1261"
     Protein         1..266
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29262
     Region          1..246
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 medskkwaiv tgassgigse fakilaqkgy slillarrld rlrdleadlr tnpskgidik
       61 imsmdirnts diarlveets dldvevvinn agfgdlgdfd qtdiekemam idtnikglhm
      121 ltkeylkvfl ekdkgyilnv sssaglmpag pymatyyatk ayvtsltsai agelraknsk
      181 vyigqlcpgp vdtefndvan csfslkgipa kycakyaies mfkykevivp tskmksavff
      241 skflprkiiv dicgrqqkkk ngsptd
//
LOCUS       WP_285091864             217 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Serratia nevei].
ACCESSION   WP_285091864
VERSION     WP_285091864.1
KEYWORDS    RefSeq.
SOURCE      Serratia nevei
  ORGANISM  Serratia nevei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Serratia nevei"
                     /db_xref="taxon:2703794"
     Protein         1..217
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23991
     Region          13..216
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 msrinlensd staqsvsdrl ltllktrgpq qasdagkvlg tageaarqqf vklakeglve
       61 avaetrgvgr pvqlwhltsa gnarfpdtha dltvqllrtv rdklgeqald vlietreqen
      121 rinykqamig aadlqervar lteircregy maewrqeedg tyllvenhcp icaaatvcqg
      181 fcraelsift evlqaqvera ehilagsrrc ayrisll
//
LOCUS       WP_285092088             716 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Gallibacterium anatis].
ACCESSION   WP_285092088
VERSION     WP_285092088.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 716)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 716)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..716
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=80555
     Region          68..716
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mkakkiffyi sislsfslyv nansdfsddd tleqvevite lerykatnkl ksdvnlsllg
       61 qqtaftapis vvnynqqaie qtearnivda iakmdasvmn fggetntlsg iyvrglqlda
      121 rqfsvnglag lyssynspls avasaqlikg astatvgmdp egssgasvni qtkratdapi
      181 nilgmrwysq draqpyfdfg rrfgnnnqwg irisglyrdg dtareqfser nkeiaigady
      241 rgdklraaid ymytkratkg grariqdiqd ldfalasapn gainliphws gqttedqtvm
      301 atfeydlpyq mmlsggighm askyygafgq irmtdpqtyn iqsmramdyk inttsanlkl
      361 hgdfnthsis hnwnigwdsv irtrdfkqsp vidykkvttf rniniyhpil psaptykali
      421 qstdekiqah svafadtvgl fedvlrltlg gryqwikqtd yqsnihansh rfspmitlay
      481 qptsdliwya nyledlkpga vdedgvmskp lvskqielgv rknwgeqytt tfslyqlsrp
      541 gtitskaann yprkageqqg kernrgiefn lyanllnghl rpnlgisynk gelidyanya
      601 gqiingvqva spriiakagi ewdtpfiqgl tlnsaiqyyg ssyqdyakky kfpsyttvdi
      661 gakytfklqq qqftlklgve nlfnknywqv qrgrydrsfa vlgmprtywa nvefsf
//
LOCUS       WP_285092220             238 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase, partial [Serratia nevei].
ACCESSION   WP_285092220
VERSION     WP_285092220.1
KEYWORDS    RefSeq.
SOURCE      Serratia nevei
  ORGANISM  Serratia nevei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Serratia nevei"
                     /db_xref="taxon:2703794"
     Protein         1..>238
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
     Region          11..>238
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mtapsafvre lglrypivqg pmngasppal avavsnagal gscaaalfsp avilervqqi
       61 raqtaapfni nlflldeqhp dlaelkraqh llrpfrealg lseppiptqf aennrdqiaa
      121 lleaappvas ftfgvlprat vtqfkkagsr vigtattvae araweeagad fvcvsgseag
      181 ghrptflgdi eqscvglmal lpqvvaavki pviaaggimn grgiaaarll gaqaaqlg
//
LOCUS       WP_285092227              96 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator, partial [Serratia
            nevei].
ACCESSION   WP_285092227
VERSION     WP_285092227.1
KEYWORDS    RefSeq.
SOURCE      Serratia nevei
  ORGANISM  Serratia nevei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 96)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 96)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 96)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Serratia nevei"
                     /db_xref="taxon:2703794"
     Protein         1..>96
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          1..>96
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msraqrlldl mqllrshryp vaghalaqtl gismrtlyrd iatlqqqgae ivgeagvgyv
       61 lrpgfmlppl mfsqaeteal vlgmrwvsrr gdsqla
//
LOCUS       WP_285092298             258 aa            linear   BCT 25-DEC-2024
DEFINITION  RsmE family RNA methyltransferase [Peptostreptococcus anaerobius].
ACCESSION   WP_285092298
VERSION     WP_285092298.1
KEYWORDS    RefSeq.
SOURCE      Peptostreptococcus anaerobius
  ORGANISM  Peptostreptococcus anaerobius
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Peptostreptococcus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Basturea,G.N., Rudd,K.E. and Deutscher,M.P.
  TITLE     Identification and characterization of RsmE, the founding member of
            a new RNA base methyltransferase family
  JOURNAL   RNA 12 (3), 426-434 (2006)
   PUBMED   16431987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Peptostreptococcus anaerobius"
                     /db_xref="taxon:1261"
     Protein         1..258
                     /product="RsmE family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=28929
     Region          1..256
                     /region_name="RsmE"
                     /note="16S rRNA U1498 N3-methylase RsmE [Translation,
                     ribosomal structure and biogenesis]; COG1385"
                     /db_xref="CDD:440995"
ORIGIN      
        1 mdrffvdren idtqarnlvi lgddvkhisk vlrysvgdel evcdgqnkey icrinsmdkt
       61 eiglsiieek dvdrespiri klyqglpkst kmeiilqklt ecgvaeiilv ntarsvvnid
      121 dkksekkldr wqrivyeaak qskrgiipdl kgiysfkeal rdmeindini mpyeeegslg
      181 ikdllrsegi qqiikenksa tigifigpeg gftedenakv keagghsvkm gprifrteta
      241 sivatsicly elgdiggm
//
LOCUS       WP_285092537             221 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Gallibacterium anatis].
ACCESSION   WP_285092537
VERSION     WP_285092537.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..221
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=24827
     Region          33..216
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 miteeeirkg fadrlalack lkefpdkgkg kiladhlnlt pkavskwfna etmpspaniy
       61 aiakfldvsk ewltygdkna sletikpqra ypllssiqag lwkgintldn eqgyemipst
      121 ilasedsfyl riegksmlpr fnegdlvlid ptlypspgdf vaavnhdnea tfkqykelge
      181 ldeygrphfe lvplnpmfpr lnsqshqiri igvavqriet l
//
LOCUS       WP_285092717             442 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Gallibacterium anatis].
ACCESSION   WP_285092717
VERSION     WP_285092717.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..442
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48579
     Region          1..>426
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mgiytyicfl saisillgfv tskisdkvqs tiaitaaami gslllltlgy lgwfqidsia
       61 tevmqeidfk sfllngilgf llfagalgik ipvlrdqkwe itifalfstl astfivgali
      121 ylianliglp idfiycllfg alisptdpia vlaiiknlra pkrlsmqveg eslfndgvgl
      181 vifvtiftva fsgeqmsase ilhlflheai ggiifgfvlg lvahllisat ddgsleillt
      241 ltiptagfml anllevsgal amvvsgimvg nwtrhrgfse qsqryldhfw emidhflnsl
      301 lffligfall lidftfqgfl mmllaipvcl aaryislwlp ysllrffrty npytlkimtw
      361 gglrgglala malsipakav fvngtdvkdi ilimtyavvv fsilvqgvti ekvikksklv
      421 dpnreeyltp sshfehhssv qe
//
LOCUS       WP_285092810             370 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Gallibacterium anatis].
ACCESSION   WP_285092810
VERSION     WP_285092810.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10191051
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..370
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40272
     Region          25..368
                     /region_name="Esterase_713_like-3"
                     /note="Uncharacterized enzymes similar to novel bacterial
                     esterase that cleaves esters on halogenated cyclic
                     compounds; cd12810"
                     /db_xref="CDD:214009"
     Site            order(224,247,344)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:214009"
ORIGIN      
        1 mlsirqkftv laavsllasq tfaspltiek qgsfavggtv ktsagqytpv peaikgkssn
       61 pfwdvyqasi aaggqtlhgd hasvfyqipv nakpyplvfl hgygqsarmw qttpdgregf
      121 dtiflrkgyp iylidqprrg qagqstvaan lpavpddqfw yaqfrigvyp nmnkgvafpk
      181 daasqdqffr qmtpdtgafd vgvitdsmvk lfdkvgqgvf vthsaggvig wttamqsdkv
      241 kgiiavepgs fpfpegevpp tqtsqfgdva pmtvskaqfe rltklpiviy fgdfipdhld
      301 gtqggeqwya rlqlakqwak vvnqhggkvs vvelpkvgih gnthflmsdt nnqqvaehla
      361 ewlkengldk
//
LOCUS       WP_285093119             371 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Niallia taxi].
ACCESSION   WP_285093119
VERSION     WP_285093119.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     Protein         1..371
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=43157
     Region          1..371
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 milskkirlk ptpeqetllw ksvgtarfiy nwtlnqqdin yssggkflsd nvlrkeltql
       61 kkgeliwlne vsnnvakqav kdacnsfkrf fkgqskfpry ksrkrskpsf yndtsklkik
      121 vgqvliekig wiqtseqvpm dckytnprvs ydgkywylsv gveqifeeve lkdfslgidv
      181 gikdlaicsd gsvfkninkt rtvkklekrl rrlqrkvsrk yennkegnrf aktcniikie
      241 kqirllhrrl tnirknhlhq ttsaivktkp srivmedlnv sgmmknkhls kaiaqqglye
      301 fgrqiqykce kygiefiead rwypssktcs scgsikkdlk lsdrkyichc gfeldrdlna
      361 sinlsryqla m
//
LOCUS       WP_285093251             168 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Niallia
            taxi].
ACCESSION   WP_285093251
VERSION     WP_285093251.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     Protein         1..168
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=19104
     Region          69..>131
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mniylasgty dflvkkyakq idqqsliamq vygdenavll hetsgpsifa aprkyetvfd
       61 kgdftdkkya vmnhipvtde hkplfeqnik rsleqidsqi styrfirplk gdtyiilsvw
      121 aerkdfiiwk qknstldspi tgdptnggif qhamfngkay lleltiss
//
LOCUS       WP_285093437             150 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Gallibacterium anatis].
ACCESSION   WP_285093437
VERSION     WP_285093437.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..150
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=17445
     Region          <35..144
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mqpqtktaac veqkysylpl plyddkpqlp yfnkqsdihy kmdlnrycir kpqqtfflrv
       61 tnenllawgi evgdiliieq reqinegdlv vieqddglql yeyfamkdqq yvffsldsnh
      121 snltikqltq lniqgvvast ihqlknrkaa
//
LOCUS       WP_285093447             731 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Niallia taxi].
ACCESSION   WP_285093447
VERSION     WP_285093447.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 731)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 731)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 731)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     Protein         1..731
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=83662
     Region          8..731
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mandqvltae qvidktrgyl neehtefiqk ayefaqnahr eqyrksgepy iihpiqvagi
       61 ladlqmdpat vaagflhdvv edtditlddi sdsfsnevam lvdgvtklgk ikyksheeqq
      121 aenhrkmfva maqdirvili kladrlhnmr tlkhlpaekq rrisnetlei faplahrlgi
      181 stikweledt alrymnpqqy yrivnlmkkk raereqylee vvseiregtg evkiqsdisg
      241 rpkhiysiyr kmvlqnkqfn eiydllavri vvssikdcya vlgiihtrwk pmpgrfkdyi
      301 ampkanmyqs lhttvigpkg dplevqirtt emhriaefgi aahwaykegk tvdegssfee
      361 klswfreild fqedsinaee fmeslkidlf sdmvfvftpk gdvfelpsgs vpidfayrih
      421 seignktiga kvngkmvtld yklktgdive ihtskhsygp sqdwikiaqt sqaknkirqf
      481 fkkqrkeenv ekgkelveke irnmefdlke iltpeniktv lekfnfvgee dmyaavgyng
      541 italqvanrl tekwrrkrda eqsatisnav aelksfpstk krasgvrvtg idnllirlsr
      601 ccnpvpgdei vgfitkgrgv svhrsdctni dtedakarli pvewetalnd rkeynveiei
      661 sgydrrglln evlqavnesq tnisavsgks drnkmatitm sililnvnhl hkvverikqi
      721 pdvysvrrim n
//
LOCUS       WP_285093461             212 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Niallia taxi].
ACCESSION   WP_285093461
VERSION     WP_285093461.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     Protein         1..212
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23645
     Region          7..166
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mgkefieife kwadtydssl tkdieykevf rgydqildsv ankafgevve fgpgtgnltv
       61 kllelglsvt giepspamrk lsdeklkgka vvkdgdflsf tvekkpdvfv styafhhltd
      121 kekaeaitly snllsssgki vfadtmfrse eeyekakaaa sqsgfhnlaa dlareyysti
      181 pklkgmleen gftatftrln efvwimegik lq
//
LOCUS       WP_285093493             239 aa            linear   BCT 25-DEC-2024
DEFINITION  tRNA (adenine(22)-N(1))-methyltransferase [Niallia taxi].
ACCESSION   WP_285093493
VERSION     WP_285093493.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Hori,H.
  TITLE     Methylated nucleosides in tRNA and tRNA methyltransferases
  JOURNAL   Front Genet 5, 144 (2014)
   PUBMED   24904644
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Roovers,M., Kaminska,K.H., Tkaczuk,K.L., Gigot,D., Droogmans,L. and
            Bujnicki,J.M.
  TITLE     The YqfN protein of Bacillus subtilis is the tRNA: m1A22
            methyltransferase (TrmK)
  JOURNAL   Nucleic Acids Res 36 (10), 3252-3262 (2008)
   PUBMED   18420655
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     Protein         1..239
                     /product="tRNA (adenine(22)-N(1))-methyltransferase"
                     /EC_number="2.1.1.217"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0160105 - tRNA
                     (adenine(22)-N1)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26446
     Region          5..236
                     /region_name="TrmK"
                     /note="tRNA A22 N1-methylase [Translation, ribosomal
                     structure and biogenesis]; COG2384"
                     /db_xref="CDD:441950"
ORIGIN      
        1 mntdrlsnrl etvakyipag akfadigsdh aylpcymlkk qkasfaiage vvdgpflsaq
       61 kqvvneglsd visvrkgngl evisdgevdc itiagmggsl iaailddgkd klrsvkrlvl
      121 qpnvsaysir iwlmendwsl vteeiieedd kiyevlvaer gegkkpyssh idaelllgpy
      181 lskeknqafq kkwsmekanw eriigrleta neteetaakr qelswkialv qevlgnesn
//
LOCUS       WP_285093602             420 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Niallia taxi].
ACCESSION   WP_285093602
VERSION     WP_285093602.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     Protein         1..420
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=47633
     Region          5..28
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          8..267
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(40..41,43,67,70..71,74..75,77..78,101,104..105,
                     108..109,112)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          65..95
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          100..128
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          134..158
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          138..403
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          168..198
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(207..208,211..212,214,238,241..242,245..246,
                     248..249,272,275..276,279..280,283)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          207..231
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          236..266
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          271..299
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          305..329
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          339..367
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          372..402
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mekvneilsl lengqqakal syyekilnqg sneerfvlge elfqlgflee akalfqille
       61 aypeegellv mlaeaemeig neeeaisqle kinpedasyp qslllladly qmdglyevse
      121 qkllqakkll pneviidfal gelyseqgri tdaikaykvv aaeqstvagv nvngriadnl
      181 saggafeeai qyyelaieek veintvfnlg ltalqagqlt iainrfeevk tldpsfqsly
      241 lylarsyeqe emlqeayetv leglkhdefn kelfllggkl alkngieega ekhfrealai
      301 dpefaeavll lnklfltqer fediieliel mdsqdieepq llwdaakayq gnenysvaln
      361 kyqeaytffk elpdflydyg yflleegkrq eaaevfnsll ekdpsneefi eivqrltsgq
//
LOCUS       WP_285094005             369 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF4097 family beta strand repeat-containing protein [Niallia
            taxi].
ACCESSION   WP_285094005
VERSION     WP_285094005.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     Protein         1..369
                     /product="DUF4097 family beta strand repeat-containing
                     protein"
                     /calculated_mol_wt=41798
     Region          <191..366
                     /region_name="YvlB"
                     /note="Uncharacterized conserved protein YvlB, contains
                     DUF4097 and DUF4098 domains [Function unknown]; COG3595"
                     /db_xref="CDD:442814"
ORIGIN      
        1 madekrrilq lleegkltie ealsliekad eadlakklns eetladdsvf qekkkdpyqq
       61 safkfqsake klfdfvdnav kkvkevdfdq lnitrheevs hifqftevfp knidvdipng
      121 evelipwdqd eirieckaki yrvdsteqak elflkevqvk akedilelkv nhkwmklqtk
      181 fyipknayhl akvrlftgsi ktydlladql yaktangkit inagqsekle adaangsivi
      241 ensviekldg etlngaikae gffqkvdlqs fngnilcinh sedidvleln gttgsievqv
      301 pdqiavtgnl ktnfggfnve legiqiieek ndvlqkvmqf qsiqsldkrt kieantktgs
      361 ikikkreqq
//
LOCUS       WP_285094012             766 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Gallibacterium anatis].
ACCESSION   WP_285094012
VERSION     WP_285094012.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 766)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 766)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 766)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..766
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=82587
     Region          46..766
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mrgasrlfgk vtsqrvessq pqhveaettt advqspatpq qdeqlflisg mscaacvakv
       61 ekairnvaqv eqvrvnladn taavvggdsd qisqavtaag yqaelledei traqkieqky
      121 qqdiqhkirq atvalvvgfg lmiamwlkll psyeqfgqah pvgyqafyll lsllviaaiy
      181 ysgkhffvra wtnllhktts mdtlvtlgal tslllsllii lfphqftqhh lyldsglmvi
      241 gfvnigkile srgkksasta lsalmdllpq qstviengqt ktiptkqvqp qmllqlqtgd
      301 kipvdgklns gelwvneail tgesqpikkn igdivtagtl vsngggqmla tqtgrnttla
      361 qmirtidqaq tskpqlatlv dkiaaifvpt vlliatltfc lwlfngadis aatlaaisvl
      421 viscpcalgl aipmsiivgt gqaaklgilv keanglqhls qvkhiffdkt gtltsgntqv
      481 tavwqqnses vaiaaaieqn mvhplaqaii qfaqqqsavl ptikqvnaia gqglqatikq
      541 qqwllgslsf mqeqqvdlqp cqtfiqqqlq laaslvflan gkkvinvfai sdqikqdasi
      601 alqqlkqqqi dctmltgdnr qtaeafakql gitqviaqat pqqkaeqisq srqngitsmv
      661 gdgvndaqaf vmadvsiamg ngakvsmeta dltllnanlm tlvnairiak aifnniklsl
      721 ffafiynvil ipvaafglln pmwaalamac ssitvvinan rlrywk
//
LOCUS       WP_285094106             118 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF4870 family protein [Gallibacterium anatis].
ACCESSION   WP_285094106
VERSION     WP_285094106.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007819
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..118
                     /product="DUF4870 family protein"
                     /calculated_mol_wt=13846
     Region          1..112
                     /region_name="COG3671"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:442888"
ORIGIN      
        1 mmeptiykmn dtkkwamigy wlyiasflit flsivaivia yvfrddvrgt yleshfnyqi
       61 rtfwigllya iictvlclvm igyilfigwa iwllvrsikg lrllncdqai inektwlf
//
LOCUS       WP_285094034              88 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Niallia taxi].
ACCESSION   WP_285094034
VERSION     WP_285094034.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     Protein         1..88
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=10035
     Region          <4..71
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 makmsvssfh hyfkqvtsls plkyqkkirl qearkllmse pieaaeaafq vgyespsqfs
       61 reysrmfgyp pvsdvkrlrd sltnsaek
//
LOCUS       WP_285094118             934 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-glucosidase [Niallia taxi].
ACCESSION   WP_285094118
VERSION     WP_285094118.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 934)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 934)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 934)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 934)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 934)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12807938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..934
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     Protein         1..934
                     /product="beta-glucosidase"
                     /EC_number="3.2.1.21"
                     /GO_function="GO:0008422 - beta-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0030245 - cellulose catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=101397
     Region          56..454
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          108..878
                     /region_name="PRK15098"
                     /note="beta-glucosidase BglX"
                     /db_xref="CDD:185053"
ORIGIN      
        1 mtvlsegkrk ltilgilfmm vlsfavapls tsaeafpwmn kdlsakeraq llveamtled
       61 kidfitgnvn nyygfynegl dkygipalqm adgpvgvria npevqnkqst alpsaiglaa
      121 twntetaeky gdligneahn tthnvmlgpg ldiarnafga rnfeslgedp ylqgqmatsy
      181 vnalqsnnvl vtakhyllnn qekdrftsds qaserainei yarpfasvie nadlgsvmcs
      241 fnqvnstyac enpdlltdll rdnlnfegfv msdyganvst ansinagldl etpgepyglw
      301 gdqlqqavad gqvkeetidq sayrilyqmf dkglfdnpaq nnpidiaahg eiarqiaaet
      361 mvllqndnkt lplntdklds iavigpdadt asaagggssl vnptytvspl egiesragad
      421 iqvdyapgtd sisagdilpg pnavpssfll pqagsnengl qatywsnknm egdpvfehta
      481 kqvnlnlgfy nyegfnaqss kldslptsln gmmsarytgv invpksgdyt lsttsygssk
      541 vyidgnlvid nageklgtve ktvsleagkn ydvkieyktd ykdatgndng gqlrfgweas
      601 dnvvdkkmad avelakksda avivtrtyds egyvdrsdme lpnnqeqlik evakvnknvv
      661 vvnesgiavk mgdwkdkvds ivqawypgqe qgnaiadvlf gdvnpsgklp vtfpvdedst
      721 pvnseeqypg vdevtkyted ifvgyrgfeq dgikpafsfg hglsytefgy kklktkvtrs
      781 nkakdqavev tlnlkntgdv tgsevvqvyt gklptnteta pkqlagfekv elkpgktkkv
      841 tikldpkafs yydeaknewv tptgnvpiyv gssssdirlk gkvqisknts nyfnkennsg
      901 stneniissn gsnkntakhe kaskknkkdd qarr
//
LOCUS       WP_285094248             217 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Niallia taxi].
ACCESSION   WP_285094248
VERSION     WP_285094248.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     Protein         1..217
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24885
     Region          1..204
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mikgiifdfd glifdtethq yhllqelfte hscelplelw qkeigthtdf spfvyleeqa
       61 krkldlkile tafqenflrk lelekerpgv kdyldtaksl rlkiglasss nydwvskhlk
      121 rlglfnyfdc iktsddvekv kpdpalyiea arcleiqpne ciafedsahg aqaaktagln
      181 vvifpnevtn amqfcdvdyr fdsmmampla dlvskyk
//
LOCUS       WP_285094387             386 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Gallibacterium anatis].
ACCESSION   WP_285094387
VERSION     WP_285094387.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..386
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43503
     Region          1..386
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mtsffseklq qlaqigqrra fpqiehqskw iqqrgqnlln lssndylgia aepqflsqfl
       61 aemsqqplpl tssssrlltg nfpiyetleq riaqdyqrqa cllfnsgyha nigilpavtd
      121 rhtlivadkl vhasiidgir lseckwvryr hndyqhlsdi lqkqaadyqr iiivtesvfs
      181 mdgdivdlaa ltalkqqydn vllyvdeaha vgvfgekglg iaeqqgyidq idflvgtfgk
      241 alasmgafvv cdqavkdyli ntmrplifst alpplnvaws yfiwqqlanf herrqhlani
      301 sqqlrtfiqq tlglpmpsat nvvpyivgen qralevaqrl qqrhfyalpi rpptvpkgta
      361 rirfsltaai neaeiaelmq tlkela
//
LOCUS       WP_285094806             727 aa            linear   BCT 25-DEC-2024
DEFINITION  acid phosphatase [Niallia taxi].
ACCESSION   WP_285094806
VERSION     WP_285094806.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130290
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     Protein         1..727
                     /product="acid phosphatase"
                     /EC_number="3.1.3.2"
                     /GO_function="GO:0003993 - acid phosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=78000
     Region          <114..320
                     /region_name="PAP2_acid_phosphatase"
                     /note="PAP2, bacterial acid phosphatase or class A
                     non-specific acid phosphatases. These enzymes catalyze
                     phosphomonoester hydrolysis, with optimal activity in low
                     pH conditions. They are secreted into the periplasmic
                     space, and their physiological role remains...; cd03397"
                     /db_xref="CDD:239491"
     Site            order(207,214,244..246,279,285,289)
                     /site_type="active"
                     /db_xref="CDD:239491"
     Region          <445..>582
                     /region_name="PRK15319"
                     /note="fibronectin-binding autotransporter adhesin ShdA"
                     /db_xref="CDD:185219"
ORIGIN      
        1 msnkrvqkkn kknqkstipi lllttllttq gaytasaaad nsaiepkpgs ygyyvdvygs
       61 nessnmtpet nssigvlskf ldiwqpgdsw dngkvlnesv hnhnintsia itknrteaea
      121 kdaylsdrrn qnysvitglg pyadnfktga nagttipdei pqdatsvkye dggnsngnwa
      181 etnsslgnmv nlintirwtg astssakayy sykrpfrwse dvsilptlvp akkddpssdg
      241 gfpsghtnaa ylasyglaya vperfeemmt raselgnsri vagmhspldv iggrvmatav
      301 aaaalndpan kavkdaayke ahevlltqeg tsydaysdye tnkqnytkrl tygfqqigdt
      361 tkpmvvpkga evlletrfpy lddmqrrwvl yttglpsgyp vlddaegwgr lnlfaaaggy
      421 edfetdvnvt mdsslggfna adswkndiag sgkltkagtg vltltgdnty tggtvieegs
      481 liasssaafg sgdvinnggt vnenvssslt ieqdfiqtda gtlelhigsk eevlnidgea
      541 tfggtlkldf tdgyvpaeda nvisysslan dskfaeveit glpenyqvay vdnavrivpa
      601 dqeetdnnnp enpsnpdepa dneeenntdn ptpvnpddht neetannent nqannnagnd
      661 tneentaetg sksenvstgs ktvdtdsvkn phtgddtnif lyvgtllasa aaaaivfwkr
      721 klkkadq
//
LOCUS       WP_285094809             183 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Niallia taxi].
ACCESSION   WP_285094809
VERSION     WP_285094809.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     Protein         1..183
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20930
     Region          59..155
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 meiktvakwd eelwqdantl yneafgekga kpvkiiknml akgiaelhvg ysdkkpvvma
       61 ltgkltndka mlidylavse ternhgigkq fvalmrqkai aegyemliie aesemtpdnr
      121 rrmafwqtcg fqltayihty iwvpetyqam ylpltdkvte khgeelfvyi ntfhrlsfsg
      181 vkk
//
LOCUS       WP_285094945             302 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Niallia taxi].
ACCESSION   WP_285094945
VERSION     WP_285094945.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     Protein         1..302
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32077
     Region          7..285
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mknwhyvliv flggcsygil stfvklayat gfsvqeitgg qylfgtaiiw llvaltkkqk
       61 isrnqavkll lsgvpfgltg ifyyhslqsl haslaiiflf qyiwigsile lvflkkkpsl
      121 eklvaivill agsllaagil sdtgvtvslq gamwgmlsav tfatfiflsg svgkdtapll
      181 ksallssggl iivfivfppf ylvdlpvlig vtkfglilgf fgavlppllf sigmpkigpg
      241 lgtiltasel pvavlmsafv lkehvsgvqw igvviilegi aasnlkysks smntkannsl
      301 an
//
LOCUS       WP_285095067             466 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Niallia taxi].
ACCESSION   WP_285095067
VERSION     WP_285095067.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     Protein         1..466
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=51691
     Region          37..405
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mtttrktiey tkvpepttpa anepvdlndd tleqhkqkil krmqekqldv ivvyadrehg
       61 vnfgyltgfe prfeeaalvl hkdgkaymml gneslrmqqy srikaeavht pyfslpnqpm
      121 etsktlaglm edagikqgmk vgiagwklft saledneqif dvpyfivtav keavgeqgsl
      181 inatslfihp gegarvimna neiahyefga slasdrmlrl lnklqtgmte melagelaaw
      241 gqqtnvqtiv atgdrftnav vaprakkvsi gdkfsatlgf rgglssrsgy avtsqedlpe
      301 evrdyleava kpyyaasvaw yeniaiglrg nemyelieev ipkaeygwrl npghltagee
      361 wmsspiysgs eipvesgmlf qmdiipsipg yggasaedgv aiadeklrde laalypdvwe
      421 riqarrdymi ntlginlkpe vlplstingy mrpyllnkqy afkvks
//
LOCUS       WP_285095070             196 aa            linear   BCT 25-DEC-2024
DEFINITION  YdeI/OmpD-associated family protein [Niallia taxi].
ACCESSION   WP_285095070
VERSION     WP_285095070.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Pilonieta,M.C., Erickson,K.D., Ernst,R.K. and Detweiler,C.S.
  TITLE     A protein important for antimicrobial peptide resistance,
            YdeI/OmdA, is in the periplasm and interacts with OmpD/NmpC
  JOURNAL   J Bacteriol 191 (23), 7243-7252 (2009)
   PUBMED   19767429
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     Protein         1..196
                     /product="YdeI/OmpD-associated family protein"
                     /calculated_mol_wt=22610
     Region          5..195
                     /region_name="YdeI"
                     /note="Uncharacterized conserved protein YdeI,
                     YjbR/CyaY-like superfamily, DUF1801 family [Function
                     unknown]; COG4430"
                     /db_xref="CDD:443542"
ORIGIN      
        1 mttlnpkvde finnakswqe eyvklrsiil dcelteefkw mhpcytlnnk nivlihgfke
       61 yvallfhkga llkdpkgilv qqtenvqaar qirftnlqei vekeavlkay iheaiaveea
      121 glevelkkne eysvpeelqq kfaenpafke afealtpgrq rayllhfsqa kqaktreari
      181 ekylphileg kglndk
//
LOCUS       WP_285095234             331 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Niallia taxi].
ACCESSION   WP_285095234
VERSION     WP_285095234.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     Protein         1..331
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35836
     Region          17..330
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mivfvllali laagyysitn gvypitfkqf fesifrmqqq edidlvifel rlprvvlall
       61 igfglgigga vlqgitkngl adpailgins gagafivaym llfqgtfsgd qllmkllmpl
      121 igmvgglfaa tiifllawnr ingldsqrll ltgiaistgf gslsmflslk mkaqdfemat
      181 vwlngtiyna twtyvvsilp wfllvvpfii ikaykldlfr lqenvmkglg iqvekekwll
      241 magsvilvss cvsvsgsigf iglicphiar llvglkhrhs llvcglvgml lltvadfigr
      301 svvapaeisv giilsiigap yfifllvkak v
//
LOCUS       WP_285095133             321 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Niallia taxi].
ACCESSION   WP_285095133
VERSION     WP_285095133.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 321)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     Protein         1..321
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36289
     Region          4..321
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 msnnlainnn lptenkpkis fysklnkdfq lnkikylmvl pviiyflifa ykpmygllmv
       61 fqdfsprlgi sgstwvglen fqrffadpsa wrivkntfni sfwslvfgfp apiilallin
      121 eirnkffrrv vqtvsympyf isivvlcsli kfftqsdgli pevfsyfgle ktnllaepsa
      181 fvpiyvisdi wqtigwdsii ylaalagidq eqyeaaridg asklqqifhi tlpglkttii
      241 illilrmgtl lnmgfekill lyspstysva dvistyvyrm gilnadysya aaigllntlv
      301 nvtlllitnr lakkfagsgl f
//
LOCUS       WP_285095329             320 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Niallia taxi].
ACCESSION   WP_285095329
VERSION     WP_285095329.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     Protein         1..320
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37316
     Region          1..315
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mkkverinti mryinnraqf tiseimqefd isrstavrdi keietmgmpl vaevgrdggy
       61 yvmsnsvlpn vqftdteika lfiafmatrn qqlpylksrq slaekllgll senqqddlvl
      121 lnqillfegt npnnpdlldl sdlphpilek lirillidsy llitlkeere iksfpifllh
      181 lyrekslwfi ggfdlneekr rifpvdnlrn vepystkyrv skkkileklk nqqevfnvvi
      241 elgpkaitqf kkyhplkaai sytnpyqtta ilktfihvnn seelteltnw llflgkdikv
      301 mevpeevlee wrervclfdi
//
LOCUS       WP_285095358             256 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Niallia taxi].
ACCESSION   WP_285095358
VERSION     WP_285095358.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     Protein         1..256
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28504
     Region          36..133
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mktfkqdpwn aslydgkhsf vsnfgeglvs llspspgeki ldlgcgtgdl asslakydce
       61 vigidnspnm ialaqkkyph ipffvedata lpyesrftav fsnaalhwik spkqalasiy
      121 sslqqggrfv aefggkgnvq iitdaiieef aeqgisfnwa nfpwyfpsia eytqlmeeag
      181 frvvfaqhyd rptsldgeng lnnwiemfgd sffkgvsesk kemlirnvad klhadvfkdg
      241 swlidykrlr vigike
//
LOCUS       WP_285095654             230 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Niallia taxi].
ACCESSION   WP_285095654
VERSION     WP_285095654.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 230)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     Protein         1..230
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25884
     Region          65..228
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 maktknlkqk ksqstgnkps kfiywiigiv vvciaglvil anlpekgfdf dyenqpvlge
       61 esasvsivef gdyrcpvckn fnesffpvvk enlidtgkak fyymnypfih adsttsalfa
      121 etvyselgnd ifwkfhdsif anqpdnetee tyteeflker lkdagatded itkvteafqt
      181 qtakdslqkd ldyvnqlnit gtptiyvngv kfegssynel ldmvneaaek
//
LOCUS       WP_285095811             335 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Serratia nevei].
ACCESSION   WP_285095811
VERSION     WP_285095811.1
KEYWORDS    RefSeq.
SOURCE      Serratia nevei
  ORGANISM  Serratia nevei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Serratia nevei"
                     /db_xref="taxon:2703794"
     Protein         1..335
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34882
     Region          26..332
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mnsptrrfml laplalsvlc glmvwslqlg svvlswrqtm aalglssapl sgmldtivvq
       61 lrvprallaa ltgaglamtg allqtttrne ladpflfgls sgasagavlv itrfgdalga
      121 ltlplsafag gvlsalavmi lfrvgrvrra eqlivcglav sflfsaltsy lvfsgdqraa
      181 gsvlfwslgg lglarwdnls iplasfvlla gftalrwral dallageqta hsmggnvarl
      241 rtetflccal staflvsltg vigfvglmvp ylarrlvgvr hrlavpmcgl lgatlltggd
      301 mlsrslipnq elpigiitag lggafivsll lraer
//
LOCUS       WP_285095821             664 aa            linear   BCT 25-DEC-2024
DEFINITION  T6SS phospholipase effector Tle1-like catalytic domain-containing
            protein [Pectobacterium atrosepticum].
ACCESSION   WP_285095821
VERSION     WP_285095821.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium atrosepticum
  ORGANISM  Pectobacterium atrosepticum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10561933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Pectobacterium atrosepticum"
                     /db_xref="taxon:29471"
     Protein         1..664
                     /product="T6SS phospholipase effector Tle1-like catalytic
                     domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=73311
     Region          156..439
                     /region_name="DUF2235"
                     /note="Uncharacterized alpha/beta hydrolase domain
                     (DUF2235); pfam09994"
                     /db_xref="CDD:462937"
ORIGIN      
        1 maadpycipc ehydcwieid vrdehnrsfk glkatltddt gksetvtlnd gptlvhgfav
       61 gpitvkletq pwlkaaqsre vlkegqsivp ayvvekmgne etprehvkat tgdlcltape
      121 qplpeahqag kagsvrlltk hsyvievkgy qinvlrigvf fdgtgnntyn aesglkkveq
      181 wlaetcsdpa qrekelrgcq mgqlpvsdsa anditnvgkl ydqylfgpkt lsahsyisgi
      241 gtrdpvagkd gteyqtddml tkavdidfgg entsivgkvn laceqeivaa vmrdledilp
      301 niecihrivf dvfgfsrgaa aarhfvnvid qkadhplvqa vansgsirlk agfdwanrdd
      361 vriafvgifd tvassyhpsv nirlrddcae rvvhltalde vrkhfpltri tptaigtsip
      421 phftelalpg ahsdlgggyy srwslrnpng dpalteclel erfmseeaas tpdtesrayr
      481 qarayaeeki vqgwvgrlhp rllraaippl gaislipysf irqhgkddsw pkkavyvevv
      541 msrvvegeys riplhmmlea gravgvpfka wrsedkmlql eplsvrrpsv nlaklderws
      601 laaieqgvvk nlsqqispev yralrrdyvh rsasnqgias pantskqeat vgkerrhiig
      661 nqea
//
LOCUS       WP_285095851             684 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Gallibacterium anatis].
ACCESSION   WP_285095851
VERSION     WP_285095851.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 684)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 684)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 684)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 684)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 684)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..684
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75235
     Region          138..671
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mdstkfsint tttwillsfl afailpsfal dygllestad eflaamgwhs fnlswfwffs
       61 laifwlfprl gfsqekeaki elvavcaial ftfisadsyh lslgyavilq iialtaiatn
      121 alaklkimqg dkfiiaslla iillifffiv yptlaifism fydgnefnps qfiqiitqsy
      181 ilrvilnsvw lsafvgflst vfglafalyt triakrtafi gkifsilpiv tppfvvglgv
      241 tlmlgrsgyl teflvqhfgf tntnwlygfn giaiaqilaf tplafmileg slksvhpsie
      301 easytlranr yqtffqvifp llkpalanaf llvfiqslad fsnplvlggs fdviatqiyf
      361 yiagsqldya sastlgtill lfslgifivq yiwignrsyv tvsgksyrgd vqdlptglkn
      421 aiiallavwi ifnatlygsi fygsftvnwg vdytltleny aslfgqgfsd gawpslinti
      481 iyagiaaplt alfglliayi vvrkeftgkk tlefltmlcf avpgtvagvs yilafndapl
      541 yitgtgviii ismvmrdlpi gmraaiaglg qldksldeas lslkgnswkt liyvtlpllk
      601 pallsalits fvramttvsa ivflvtadtr vatayilnrv edgeygiaia ygsllivvmm
      661 aiilffdwmv gdtrisrska kqmn
//
LOCUS       WP_285095947             378 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Gallibacterium
            anatis].
ACCESSION   WP_285095947
VERSION     WP_285095947.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..378
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=43554
     Region          3..378
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mllrkafkfe impngeqsrk ikqfcgccrf vfnralawqn eqyqqdnnqk fsyskianll
       61 pqwkkelswl kechsqvlqq slkdlekafk nffqqradfp kfkkkgvkes frfpqgckle
      121 qqnsriwlpk igwvryrnsr evigeiknvt vsqkcgrffv siqtefesqi pvhkggeigi
      181 dmgiarfatl sngkffvpln afktfkgkla klqrqlknkv kfsqnwrklk akigklhhki
      241 ancrkdflhk istqisknha miyiedlqva nmsksakgta aqhgknvatk sglnraildq
      301 swfefrrqld yktqwqggfl vavppqnssr tcpccghisk enrqtqahfe cvecgytena
      361 dvvgamnvla rgraivqa
//
LOCUS       WP_285096023             204 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Gallibacterium
            anatis].
ACCESSION   WP_285096023
VERSION     WP_285096023.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..204
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=23794
     Region          <5..129
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 masnkqrqrk igyfllwkll qqlgqeqvfa qgiekdqqgr phfnapqfdf nlshsgdwva
       61 vilvqrvhne svaidiehpl rirnferllh yyaskteiaw wqsqqkqdea fyltwcarea
      121 ilkakgrgig aiskvrfepe nscfftqeap ngqlffaqel pfylacfvqg sgtishcfcw
      181 qeknasllqq kvklkryrvi nrkl
//
LOCUS       WP_285096257             370 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Gallibacterium anatis].
ACCESSION   WP_285096257
VERSION     WP_285096257.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10191051
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..370
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40138
     Region          25..368
                     /region_name="Esterase_713_like-3"
                     /note="Uncharacterized enzymes similar to novel bacterial
                     esterase that cleaves esters on halogenated cyclic
                     compounds; cd12810"
                     /db_xref="CDD:214009"
     Site            order(224,247,344)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:214009"
ORIGIN      
        1 mlsirqklta laavsllagq tfaspitiek qgsfavggtv ktsagqytpv peaikgkssn
       61 pfwdvykasi aaggqtlhgd hasvfyqipv nakpyplvfl hgygqsartw qttpdgregf
      121 dtiflrkgyp iylidqprrg qagqstvaan lpavpddqfw yaqfrigvyp nmnkgvafpk
      181 daasqdqffr qmtpdtgafd vgvitdsmvk lfdktgqgvf vthsaggvig wttamqsdkv
      241 kgiiavepgs fpfpegevpp tqtsqfgdva pmtvskaqfe rltklpiviy fgdfipdhld
      301 gtqggeqwya rlqlakqwan vvnqhggkvs vvelpkvgih gnthflmsdt nnqqvaehla
      361 ewlkengldk
//
LOCUS       WP_285096343             465 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Gallibacterium
            anatis].
ACCESSION   WP_285096343
VERSION     WP_285096343.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..465
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49642
     Region          3..443
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mnfnqilaei dsfiwgppll illagtgiyf slrlgflqik slpralrylf qrgnsgegdv
       61 safaalctal satigtgniv gvataiqagg pgaifwmwiv affgmatkya ecllavkyrv
      121 kdkngfmagg pmyyierglg ikwlaklfav fgvlvaffgi gtfpqinait hamqdtfgvs
      181 tvitavvmtl lvamiilggv nriavvssfi vpfmavlyvg tslfillinw nvvpqalali
      241 iesafnpqaa lggavgftvl kaiqsgmarg ifsnesglgs apiaaaaaqt qepvrqglis
      301 mtgtffdtii vctmtglviv isgvwqseva gaavtnlafa qglgnsigat ivtigllffa
      361 fttilgwcyy gercfvyltg irgikifrsc filliacgaf ikldiiwsla divnglmaip
      421 nlialiglrk viiaetrdyf arlqisakdr deeiaengel resyn
//
LOCUS       WP_285096382             119 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Gallibacterium
            anatis].
ACCESSION   WP_285096382
VERSION     WP_285096382.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..119
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13982
     Region          5..107
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mqatdknite hqqcpvnttl eiiggkwkvi ilyhlfqgtq rfnelrrlip nitqrmltlq
       61 lremenagil hrevypeipp kveysltefg qtllpvikam hkwgnkyekt cqqrhqqen
//
LOCUS       WP_285096390             305 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Gallibacterium anatis].
ACCESSION   WP_285096390
VERSION     WP_285096390.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..305
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33540
     Region          3..289
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 miskfvskgf ifgcigasfy glnplftlpl yelglspdsv lfyrfsvasl ilafimqqqk
       61 isfsltktel vavifvgvmf aisslalfms yqlieagias tilfiypllv avmmimffke
      121 rinlitmlai tlvifgvsml yqgddgtsln pfgvllvfis altyaiyiia veksplhnlp
      181 iikltfygll fsalvfflrl dfgthlqvnn ssqfiiniig laivptvlsl vlmnqsiqmi
      241 gsttasiiga lepitallvg vlvfheqmtv rilfgiiail saivltvsgk eilrffggrh
      301 hhfrh
//
LOCUS       WP_285096930             200 aa            linear   BCT 25-DEC-2024
DEFINITION  YagU family protein [Gallibacterium anatis].
ACCESSION   WP_285096930
VERSION     WP_285096930.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..200
                     /product="YagU family protein"
                     /calculated_mol_wt=22583
     Region          4..195
                     /region_name="YagU"
                     /note="Uncharacterized membrane protein YagU, involved in
                     acid resistance, DUF1440 family [Function unknown];
                     COG3477"
                     /db_xref="CDD:442700"
ORIGIN      
        1 minlfqqtdp srrrygvaif vgiiagvisa fvkwgaehpf pprspldlfv aacqdpsqal
       61 evcsraflnp phvflrdylg idptaaaftf adqafnwigv thiifslvfa iaycvvaerf
      121 pkvklwqgvl agiicdicvh yitfpllglt ppvaewpfye hvsefvghif wfwtieiirr
      181 dlrnrithep daevplgenr
//
LOCUS       WP_285097110             358 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase family protein [Serratia].
ACCESSION   WP_285097110
VERSION     WP_285097110.1
KEYWORDS    RefSeq.
SOURCE      Serratia
  ORGANISM  Serratia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Serratia"
                     /db_xref="taxon:613"
     Protein         1..358
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40031
     Region          1..350
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mnngrldsvq ilrgfaalsv mlfhfrwnin lsypnlgdql fgwgavgvdi ffiisgfvit
       61 lsakkltpgl saagvflkhr arrilpayfi illitfllsg amstfhypek vsnlisaitf
      121 spidanhapf yvddsgfygi rwtlnyevlf ylvmavclis kyrwpllfgm fslslvvlpm
      181 lsghsptldv sgyqfnsayl nlmtnpiiwm flvgvafglv ypytkklngq lrisilivsi
      241 ivigycilfa pswghgmtms gwylsilfia vvlndelitk cipgffvtlg eisfslylih
      301 tlmnggigkr fedigvadgm prfalscvvs vvlaylsyrf ierpvsrrkk etvrheav
//
LOCUS       WP_285097178             306 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Serratia nevei].
ACCESSION   WP_285097178
VERSION     WP_285097178.1
KEYWORDS    RefSeq.
SOURCE      Serratia nevei
  ORGANISM  Serratia nevei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Serratia nevei"
                     /db_xref="taxon:2703794"
     Protein         1..306
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34661
     Region          2..191
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mnpkvsvvia syntekyive cvnsvfnqdy pnvelvvvnd gstdatgall aevvrnhsnv
       61 kvvnqenqgq svarnngvnv atgefivfld sddifdvsli skcvmalmst hsdivffdae
      121 kfyddecave fsstyvrdns lygktmdskt ffkeswrlns yivspcmyms rtqlvrdnpf
      181 ypgiihednl fttsillaqk stivclkesl ykrrlrrdsv mtskknhrhv igyltvarkl
      241 pvlrsrtdre lnnylnsfis rcvsfsinda kscygrvpka lrkeylsafk eigimnikkk
      301 vlnsca
//
LOCUS       WP_285097246             605 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Paenibacillus sp. PK4536].
ACCESSION   WP_285097246
VERSION     WP_285097246.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 605)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 605)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 605)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 605)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 605)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 605)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15747384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..605
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=70930
     Region          <93..156
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          254..336
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          350..589
                     /region_name="TroA-like"
                     /note="Helical backbone metal receptor (TroA-like domain).
                     These proteins have been shown to function in the ABC
                     transport of ferric siderophores and metal ions such as
                     Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is
                     formed in the interface between...; cl00262"
                     /db_xref="CDD:469696"
     Site            order(413..414,419,442)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238347"
ORIGIN      
        1 mflkkqkvhk qghvytyyri vesyrdeqgk nkhrtvkylg klsdeevsai teqlkenryp
       61 fsnpndvsip ehkqhthils rkvwiplslt iitylhhhpk ewtvaeydtl mmikegqadv
      121 qlqgshftik adqilfcpag sgvflynnss qpvqllklmf qnvdkhasss wssdglatii
      181 pvhsplemqr lgkellatvd qpkelsveke lysqllfyql lhliwnhqsp gteatnlnmi
      241 qqatdevrmy yreeirrtvi aarlgitpeh fsrifrkhkg isftdyvyrw rmnaakkdlq
      301 yssasiseia rrngypnehy fsrrfkslfg lspkqyqsse kqyatwnypf tamllqlgmv
      361 pqagyleqwk wekyhqhldl stmivlhdsl eqsiqtmndv qpdlvfayed nlgrfileey
      421 vpvqtlsieh hnwqqqwlwl aeqvgrleqa hqwlndwdrq iqqareqlss figmdetvgi
      481 ykivsekiyv ygdrrsmggp liyqqlhhhp paivqediid qnliskevtl aelsryaadh
      541 miviyypveg tsevalepvm eslewqqlaa vqnrqcytmd rnifygfdpc sqeaqlklwl
      601 qqfis
//
LOCUS       WP_285097523             310 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [Paenibacillus].
ACCESSION   WP_285097523
VERSION     WP_285097523.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 310)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 310)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 310)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..310
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34302
     Region          2..310
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mkarkgetah rktlkkrhnh yflyallapa liltiifkyv pmygaviafk dfsplkgimr
       61 sdwvgfkyfe kflnspnftd iftntislsl fglicsfpip ivlalmlnqv rqakikknvq
      121 lilyapnfis vvvivgmlfi flspvgpinq lvsaifgqpl mfmsepgyfr siyilsgiwq
      181 gagwssiiyv aalagvdpel hnaasldgan ifqrilhidl ptirpimaiv filaaggims
      241 igfekaylmq tsmnlpssei istyvykvgl qagdysysaa vglfnsvinv fllvavnfvv
      301 kklnegegly
//
LOCUS       WP_285097665             510 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Gallibacterium anatis].
ACCESSION   WP_285097665
VERSION     WP_285097665.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 510)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..510
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=56487
     Region          21..495
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 msmlsqhkqa lfcrdeqsiq dyqramnkav eavcqwlqnd kmytggsirr lrstiefapt
       61 kegaglentl qrlvtiflnp slkvhhphsl ahlhcptmvs sqiaevlina tnqsmdswdq
      121 spagsimeeq linwlrqkvg ygegtagvft sggtqsnlmg vllardacia khwqnedgse
      181 wlvqqnglpp dalqkvkvvc senahfsvqk nmammgmgfq svvtvptnkn aqmdiaalek
      241 tlaelqaqgk lvacvvatag ttdagaiddi eairtisdqy gawlhidaaw ggalllskdf
      301 rhwlngleka dsvtldfhkh ffqtiscgaf llkdernfrf idykadylns eydeeygvpn
      361 lvakslqttr rfdalklwft mealgedlya smidhgvyla reirdyinat ddlemlvepq
      421 fasilfrvnp qgypaeyvdl lnqnvadelf argeanigvt kvgeqqalkm ttlspiatld
      481 dvkslldqvl seaarikdai vagnyvppia
//
LOCUS       WP_285097905             716 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Gallibacterium anatis].
ACCESSION   WP_285097905
VERSION     WP_285097905.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 716)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 716)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..716
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=80728
     Region          68..716
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mkakkiffyi sislsfshhv nansdfsddd tleqvevite lerykatnkl ksdvnlsllg
       61 qqtaftapis vvnynqqaie qtearnivda iakmdasvmn fggetntlsg iyvrglqlda
      121 rqfsvnglag lyssynspls avasaqlikg astatvgmdp egssgasvni qtkratdapi
      181 nivgmrwysq drtqpyfdfg rrfgnnnqwg irisglyrdg dtareqfser nkeiaigady
      241 rgdklraaid ymytkratkg grariqdiqd ldfalatapd gainliphws gqttedqtvm
      301 atfeydlpyq imlsggighm askyygafgq irmtdpqtyn iqsmramdyk inttsanlkl
      361 hgdfntrsis hnwnigwdsv irtrdfkqsp vidykkvttf rniniyhpil psaptykpli
      421 qstdekvqah svafadtlgf fedelrltvg gryqwikqtd yqsdtkadnh rfspmitlay
      481 qptsdliwya nyledlepga vdedgvmskp lvskqielgv rknweeqytt tfslyqlsrp
      541 gtitskaann yprkageqqg kernrgiefn lyanllnghl rpnlgisynk gelidyanya
      601 gqiingvqva spriiakagi ewdtpfiqgl tlnsaiqyyg ssyqdyakky kfpsyttvdi
      661 gakytfklqq qqftvklgve nlfnknywqv qrgrydrsfa vlgmprtywa nvefsf
//
LOCUS       WP_285098230             579 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Serratia nevei].
ACCESSION   WP_285098230
VERSION     WP_285098230.1
KEYWORDS    RefSeq.
SOURCE      Serratia nevei
  ORGANISM  Serratia nevei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 579)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 579)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 579)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Serratia nevei"
                     /db_xref="taxon:2703794"
     Protein         1..579
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64278
     Region          1..579
                     /region_name="COG4986"
                     /note="ABC-type anion transport system, duplicated
                     permease component [Inorganic ion transport and
                     metabolism]"
                     /db_xref="CDD:444010"
ORIGIN      
        1 mnvrlnthvs arrllpngwd viafpliigl iammaiglhq tlqpivtlkt qaisldpanl
       61 peyalrttlr mlvamvaala fslvygtlaa ksrraekvlv pildilqsvp vlgyisftvt
      121 ffialfpgrv lgvelaamfa iftsqawnmt fsfyqslrtv prdlqevarg fhlspwqrfw
      181 kldapfampg liwnmmmsms ggwffivase aitvgnntft lpgigaylaq ailsqdlpai
      241 gwvlltmtvv ilaydqllfr plvawadkfr mettrsasap tswllnlmrr trlihllltp
      301 lgallaktar lklslparpl rrgnsaqrqr rsrtidrcws aivilltlai awrvilyvqt
      361 gvtlndvghv malglitllr vavlialssl iwvplgvlig lrptlagkiq piaqflaafp
      421 anllfpvfvi tivhfrlnpd iwlsplivlg tqwyilfnvv agatalpndy reaaanfhir
      481 gwqwwrqvml pgifpyyitg aitasggawn asivaefvqw gstqvkahgl gayiaettaa
      541 gdfpkiilgi avmslfvtlf nrllwrplya yaesrfrid
//
LOCUS       WP_285098289             270 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Pauljensenia sp. UMB3104].
ACCESSION   WP_285098289
VERSION     WP_285098289.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB3104
  ORGANISM  Pauljensenia sp. UMB3104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Pauljensenia sp. UMB3104"
                     /db_xref="taxon:3046331"
     Protein         1..270
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28626
     Region          107..266
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mtdndnkasq nkaedaptnl yktlffvtap itailagacv wmgvqlssts pagqatptat
       61 ptaaaqmpqn tetaapsqtn asnleimksf vrhqaddpqa kgdinapvtm vlfsdfacpy
      121 ctkyaqeidp aladlvadgt lrvewydlaq itetsplaaq agiaageqgk fwefhdvvya
      181 aadptghpqy seqalvdfaa qagvpdldkf ratmladhtv skvkaakeqa hqagisgtpt
      241 mfinkafvsg yrdasyirnt ileqaaqsas
//
LOCUS       WP_285098370              88 aa            linear   BCT 25-DEC-2024
DEFINITION  integrase core domain-containing protein, partial [Serratia nevei].
ACCESSION   WP_285098370
VERSION     WP_285098370.1
KEYWORDS    RefSeq.
SOURCE      Serratia nevei
  ORGANISM  Serratia nevei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Ballandras-Colas,A., Maskell,D.P., Serrao,E., Locke,J., Swuec,P.,
            Jonsson,S.R., Kotecha,A., Cook,N.J., Pye,V.E., Taylor,I.A.,
            Andresdottir,V., Engelman,A.N., Costa,A. and Cherepanov,P.
  TITLE     A supramolecular assembly mediates lentiviral DNA integration
  JOURNAL   Science 355 (6320), 93-95 (2017)
   PUBMED   28059770
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (5), 302-307 (2001)
   PUBMED   11774877
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Dyda,F., Hickman,A.B., Jenkins,T.M., Engelman,A., Craigie,R. and
            Davies,D.R.
  TITLE     Crystal structure of the catalytic domain of HIV-1 integrase:
            similarity to other polynucleotidyl transferases
  JOURNAL   Science 266 (5193), 1981-1986 (1994)
   PUBMED   7801124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Serratia nevei"
                     /db_xref="taxon:2703794"
     Protein         <1..88
                     /product="integrase core domain-containing protein"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016893 - endonuclease activity, active
                     with either ribo- or deoxyribonucleic acids and producing
                     5'-phosphomonoesters [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          1..67
                     /region_name="rve_3"
                     /note="Integrase core domain; pfam13683"
                     /db_xref="CDD:433402"
ORIGIN      
        1 hgvelrliqp gkptqngfie sfngrfrdec lnehwfsdiv harkiinnwr qdynecrphs
       61 alnyqtpsef aarwrngkce gkqtditn
//
LOCUS       WP_285098401             313 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein, partial [Serratia nevei].
ACCESSION   WP_285098401
VERSION     WP_285098401.1
KEYWORDS    RefSeq.
SOURCE      Serratia nevei
  ORGANISM  Serratia nevei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Serratia nevei"
                     /db_xref="taxon:2703794"
     Protein         <1..313
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
     Region          30..313
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 llchgtvcvv gkmrdlilql skssiystkp lffiisgfim ayithgksvn fisfmkkrfv
       61 riipiywvlt svalavfiis pssvnstmap pgvinsyllf pvegksmlle vawtlryefi
      121 fyiifslsll tpnryvtvsv llggiwacsk fsyenyyigf ffthymgefl lgilsflfyt
      181 kgksltlvvl ssiaalvgyf ygthdgvlty glystvlfnv fvmledkikr nasmvrpisy
      241 lgdasysiyl ahlfiiaaag ilykhtefmn dpilfnistl vasvffsvlf yefveriitr
      301 kltaikhaap svg
//
LOCUS       WP_285098440             305 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Gallibacterium anatis].
ACCESSION   WP_285098440
VERSION     WP_285098440.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..305
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33668
     Region          3..289
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 miskfvskgf ifgcigasfy elnplftlpl yelglspdsv lfyrfsvasl ilafimqqqk
       61 isfsltktel vavtfvgvmf aisslalfms yqlieagias tilfiypllv avmmimffke
      121 rinlitmlai tlvifgvsml yqgydgssln pfgvllvfis altyaiyiia veksplhnlp
      181 iikltfygll fsalvfflrl dfgthlqvnn ssqffiniig laivptvlsl vlmnqsiqmi
      241 gsttasiiga lepitallvg vlvfheqmtv rilfgiiail saivltvsgk eilrffggrh
      301 hhfrh
//
LOCUS       WP_285098488             417 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Pauljensenia sp.
            UMB3104].
ACCESSION   WP_285098488
VERSION     WP_285098488.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB3104
  ORGANISM  Pauljensenia sp. UMB3104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 417)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Pauljensenia sp. UMB3104"
                     /db_xref="taxon:3046331"
     Protein         1..417
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44033
     Region          47..335
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrptiskfla lgatasafal lagacgsgsa sssggsgsdq vhqmytwvst dndraqwqsf
       61 idaakekdpn ftltfdgpaf ndywtkvktr mvasdapcil ttqaaraqel sgllepldsy
      121 meaagikasd ynaammqgmt vdgkvlalpy daepdvlyyn remfekaglq apstsyatdq
      181 flkdakaltg dgkygmavkp lllgnapgdf gisfggqvsk dgkntltdpk fvegvqfafd
      241 lvhkeqvava pnaadndgpa qtaftsgtaa mivdgpwmyg sfekelgdkl gvavlptptg
      301 qpraviqgsg fgiskscpdk qaafnvlkel vtpevigtva dkqgtvpsve samdkwaank
      361 pedsaeavrv llengtplvt tttwnqints fqqyspegfr gtktaldilt dlqnsag
//
LOCUS       WP_285098469             442 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Gallibacterium anatis].
ACCESSION   WP_285098469
VERSION     WP_285098469.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..442
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48599
     Region          1..>426
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mgiytyicfl saisillgfv tgkisdkvqs tiaitaaami gslllltlgy lgwfqidsia
       61 tevmqeidfk sfllngilgf llfagalgik ipvlrdqkwe itifalfstl astfivgali
      121 ylianliglp idfiycllfg alisptdpia vlaiiknlra pkrlsmqveg eslfndgvgl
      181 vifvtiftva fsgeqmsase ilhlflheai ggiifgfvlg lvahllisat ddgsleillt
      241 ltiptagfml anllevsgal amvvsgimvg nwtrhrgfse qsqryldhfw emidhflnsl
      301 lffligfall lidftfqgfl mmllaipvcl aaryislwlp ysmlrffrty npytlkimtw
      361 gglrgglala malsipakav fvngtdvkdi ilimtyavvv fsilvqgvti ekmikksklv
      421 dpnreeyltp sshfehhssv qe
//
LOCUS       WP_285098579             335 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Pauljensenia sp. UMB3104].
ACCESSION   WP_285098579
VERSION     WP_285098579.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB3104
  ORGANISM  Pauljensenia sp. UMB3104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Pauljensenia sp. UMB3104"
                     /db_xref="taxon:3046331"
     Protein         1..335
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37206
     Region          <70..294
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mttrlvrktn rfritaital cllallgvts falnrsgnrq kdptaiayee dedplpegva
       61 slmdtakslh gtidtityeq syegttytkq ayvyvpasya sdtpanilyl thgwwgnaag
      121 ladgvspvvd elesdgkaap tlvvfatyyp drsfatddye edytlnrffa tseidtlidt
      181 vesryttfar gdtsdqslra srkhrafggf smgatttwdv falrpqyfyg ympmageswi
      241 greeeadspr iaelvtagve rahygprdfl ilasvgsedp alwdmtpqid elhedypdlm
      301 tedslqlwid dgethsmtsi anqvehnlpl lfpak
//
LOCUS       WP_285098763             412 aa            linear   BCT 25-DEC-2024
DEFINITION  nucleobase:cation symporter-2 family protein [Gallibacterium
            anatis].
ACCESSION   WP_285098763
VERSION     WP_285098763.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10795438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..412
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=43135
     Region          12..403
                     /region_name="ncs2"
                     /note="uracil-xanthine permease; TIGR00801"
                     /db_xref="CDD:273276"
ORIGIN      
        1 msqdtqsqia eskvkqafvg lqmlfvafga lvlvplitgl dsntalltag vgtllfqlct
       61 krqvpiflas sfafiapiqy giatwglpvt lggltcaglv yvalsalvkm kgvealqkvf
      121 ppivvgpvii iigmglapva vdmalgknsn ysydqailvs mitllttlcv avfakgimkl
      181 ipimfgiaag yivcafmgli nlqsvydapw fslptittpe fkleailyll piaiapaveh
      241 vggimaissv tgkdflqkpg lhrtllgdgv atsvasflgg ppnttyaevt gavmltknfn
      301 ptimtwaavw aiaisfcgkv gaflstipti vmggimmlvf gsiavvgmst lirgkvdvte
      361 srnlciisvv mtfgiggmfv nfgevslkgi slcaivaill nlilpkaqkt en
//
LOCUS       WP_285098808             366 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Pauljensenia sp.
            UMB3104].
ACCESSION   WP_285098808
VERSION     WP_285098808.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB3104
  ORGANISM  Pauljensenia sp. UMB3104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Pauljensenia sp. UMB3104"
                     /db_xref="taxon:3046331"
     Protein         1..366
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38228
     Region          5..360
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mtqpfippar pligeeeida vaavmrtgmi aqgpqvaafe defvaalvpg travavnsgt
       61 salhlgllaa gigpgdeviv psftfaatan svaitgatpv fadidpltft lspaaveasi
      121 tprtraimpv hlyghpapmd alqaiatehg lmifedaaqa hgatlhgtav gsfgsfaafs
      181 fyptknmtsg eggmvtsadp giirgvrlar nqgmetryan eivglnnrmt dihaaigrvq
      241 ltkvgawtak rrenaaflna hlrgvtvphv apgathvyhq ytirvpedrd gfadalrdey
      301 gigsgvyypi pnhelpslar fapdaelpat reaaaqvlsl piypsltpge leriaqgina
      361 laeaga
//
LOCUS       WP_285098811             119 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Gallibacterium anatis].
ACCESSION   WP_285098811
VERSION     WP_285098811.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..119
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12749
     Region          61..114
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
ORIGIN      
        1 msdiqekial amknididat vaaviaddpd akqikaslts alkqaksgky ariskvqvsp
       61 ivetrlktgl sqnkfaetlg isvntlrswe qgnrqpsgaa atllhllnkr pelvlelra
//
LOCUS       WP_285098865             434 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Pauljensenia sp. UMB3104].
ACCESSION   WP_285098865
VERSION     WP_285098865.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB3104
  ORGANISM  Pauljensenia sp. UMB3104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 434)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 434)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Pauljensenia sp. UMB3104"
                     /db_xref="taxon:3046331"
     Protein         1..434
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48297
     Region          2..416
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 mhllrftfen hrsfrdeatl dltrptlktl rpskgtewtd hihhvdgiyg anasgktnvl
       61 dalhymlgvi gssatswlde pqfprapfal ipeqmtapat felefiysgq rydyrfatds
      121 dgiteeslhv vstrwkevys rntdgrvkgl kgitrvarre lalsraaqfn hasvtpiwea
      181 lmrgfdlyhv gdgevnarid riarqlkers lnlsalvtla qiadtgithv eveehaippr
      241 faqlvaqmla pasddsqeqa sdsssdeved isnyiarnll frhgessgrl rssdestgtm
      301 awlalgtavv nalrkgcvlv vdelgsslhp qlsrliidwf ddpevnttga qliftshdmt
      361 lldagrgsra kreqvwfvek gsngaselfn lddftlqkgs nivkqylegq fggvpytaps
      421 lihnllnrnt eeir
//
LOCUS       WP_285098868             431 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Pauljensenia sp.
            UMB3104].
ACCESSION   WP_285098868
VERSION     WP_285098868.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB3104
  ORGANISM  Pauljensenia sp. UMB3104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Pauljensenia sp. UMB3104"
                     /db_xref="taxon:3046331"
     Protein         1..431
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=45225
     Region          49..422
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mdatpwvlaa vagagaigva rlatalsrrr rrrqalevpa svddptrgrp rpwiimnpsk
       61 hedpqafkdr inrkakelgi dhvhwrettr edpgtgqavr aleegatvvi aaggdgtvra
      121 vaagmagsgv rmgiipvgtg nvlagnlsip dnpaqalava ldrnhravdl awvrvedttq
      181 esdqpaeggl rlaahaalhp edtlqdeaap assneprade yaclvvagmg ydgetmadtd
      241 pelkkrigwi ayvwaglgam gaprmkarlt lrspaaaapd plgigdqisg sivheagdva
      301 devtkiears vmfanagemk mlilapdanl sdglidviav daqagllgwa dvtwkmlgql
      361 iglrpvnlpv atgtvafrqa kgasvtskea qvcqvdgdai gvartmhvrm qagaldiavp
      421 aertwmellp s
//
LOCUS       WP_285098886             507 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Pauljensenia sp.
            UMB3104].
ACCESSION   WP_285098886
VERSION     WP_285098886.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB3104
  ORGANISM  Pauljensenia sp. UMB3104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Pauljensenia sp. UMB3104"
                     /db_xref="taxon:3046331"
     Protein         1..507
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=56344
     Region          123..507
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mlppppeppl wawllvgaid fvirvvalgv vpkhrrasts tawllliflw pllgvplyii
       61 fgswwamgrr ldddpearal vdaivadsta lqpesyevpt gpdglpfgsd gdtasimrls
      121 gnlsgfpasa grvgrlyndt aetflamaas idaathhvna lyyqtswdey tapfyealqr
      181 avargvtvrl lvdhhgmrti pghrdfrrrl namgvqwhem lpfaplrgqi rrpdlrnhrk
      241 ilvidgreay igshnlvapd ydtpsyqkag mhyddtsvsv tgpivaqiqa vfavdwyyac
      301 kevltpevla ppaaqetger eeeqasamqi ipsgpaykge pnlrafvhmi ssarthvsit
      361 spyfipdeal mtaltnaals gvtvelfvse qfdqflvgha qrsyygpllk agvrihlyhk
      421 prmlhskymi vdgslciigs snmdvrsfgl nyeivlvads arlvemlhgn dertrgqsre
      481 ltyeewkgqp whvhyvdnvc rlgssll
//
LOCUS       WP_285098948              78 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pauljensenia sp.
            UMB3104].
ACCESSION   WP_285098948
VERSION     WP_285098948.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB3104
  ORGANISM  Pauljensenia sp. UMB3104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Pauljensenia sp. UMB3104"
                     /db_xref="taxon:3046331"
     Protein         1..78
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8466
     Region          9..73
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mtinrafsyk plwkllidrd mnktqlqera gispatlskl grggnvttdv laricealdc
       61 niadicevvp tdtkgetd
//
LOCUS       WP_285099154             319 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Gallibacterium anatis].
ACCESSION   WP_285099154
VERSION     WP_285099154.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Higgins,C.F., Hyde,S.C., Mimmack,M.M., Gileadi,U., Gill,D.R. and
            Gallagher,M.P.
  TITLE     Binding protein-dependent transport systems
  JOURNAL   J Bioenerg Biomembr 22 (4), 571-592 (1990)
   PUBMED   2229036
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467926
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..319
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35777
     Region          1..318
                     /region_name="SapB"
                     /note="ABC-type antimicrobial peptide export system,
                     permease component SapB [Defense mechanisms]; COG4168"
                     /db_xref="CDD:443329"
ORIGIN      
        1 mivalirrll lifislvils ilayaimlkd plnqvlfegs tfqgylqyie klanadfgit
       61 yiggellrdq ilsvlpstle lciaamilal lfgiplgfig alsnrsvskf irgfssvgls
      121 ipvywiglil lylaaiynwe issvgqynal yeikpvtgfa iidvwfveep ykikivqsvl
      181 qhlvlptlvl mimpmmeiir ltqhraeqvi sanytktalt rgwskfkilr vyllrntlap
      241 ispyiirtft ltlaacmlie nifnwsgigq wliaalseqd ynavasgviv igiivlfinl
      301 ladlseflld pfkkkawyd
//
LOCUS       WP_285099219             597 aa            linear   BCT 25-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Pauljensenia sp. UMB3104].
ACCESSION   WP_285099219
VERSION     WP_285099219.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB3104
  ORGANISM  Pauljensenia sp. UMB3104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Pauljensenia sp. UMB3104"
                     /db_xref="taxon:3046331"
     Protein         1..597
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=63908
     Region          4..460
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          525..590
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(547,556..558,565)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            557
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mrtinrilva nrgeialrvc rtatdmgist iavyadqdma aphtreadea lslggddaas
       61 tylngekila ialetgadai hpgygflsen sdfaraveda giawlgpasd vidalgdkik
      121 arrvaeacgv spvpgvsepv tsreeveafi asagypvvlk radggggrgi siirsqadld
      181 lffarhtdad dlgahfverf vevarhvetq sardslgnfh vistrdcsvq rrnqklveea
      241 papflpegah etlvnasral fehvnyvgvg tvefllepdg niwflevnpr lqvehpvsee
      301 vtgidlvreq iriaqglplt tppeprghsf efrvtsedps kdltptagrl devhwplgpg
      361 irlelgideg dsvqtafdsm iakiivtgad reqalarsrr alaefsvqgv atpvpvyqdi
      421 indpdfcgvg gfnvstrwfe ttfmpqhdys dlavpaeass tadlprqtyi ieldgrrvsl
      481 tlpagmfnap aaraprppqp lrssprrasa savqagphqg apgdivapmq aivvalavse
      541 gdqveegqlv avleamkmek pllapragtv tslsikqgdt vtagtriahi ateeear
//
LOCUS       WP_285099288             386 aa            linear   BCT 25-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Gallibacterium anatis].
ACCESSION   WP_285099288
VERSION     WP_285099288.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..386
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43539
     Region          1..386
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mtsffseklq qlaqigqrra fpqiehqskw iqqrgqnlln lssndylgia aepqflsqfl
       61 aemsqqllpl tssssrlltg nfpiyetleq riaqdyqrqa cllfnsgyha nigilpavtd
      121 rhtlivadkl vhasiidgir lseckwvryr hndyqhlsdi lqkqaadyqr iiivtesvfs
      181 mdgdivdlaa ltalkqqydn vllyvdeaha vgvfgekglg iaeqqgyidq idflvgtfgk
      241 alasmgafvv cdqavkdyli ntmrplifst alpplnvaws yfiwqqlanf herrqhlani
      301 sqqlrtfiqq tlgfpmpsat nvvpyivgen qralevaqrl qqrhfyalpi rpptvpkgta
      361 rirfsltaai ndaeiaelmq tlkela
//
LOCUS       WP_285099312             154 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase [Gallibacterium anatis].
ACCESSION   WP_285099312
VERSION     WP_285099312.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..154
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=17145
     Region          35..153
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 midriilkir vlvhfmlhff iykkakvilr gvprilyghr ikfgnlirln dnvfihavng
       61 veigdnttls ygvvlltesy dissknkyll rkhkgapiki gknvwicans tilpgvsiad
      121 niivgagsvv tkdldransl yagnparfik eldf
//
LOCUS       WP_285099314             398 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Gallibacterium
            anatis].
ACCESSION   WP_285099314
VERSION     WP_285099314.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..398
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44687
     Region          2..396
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mkisfsppdi tdleinevie alksgwittg prtktleqrl asymgtkrgv clnsataale
       61 lilrvldike ddeiitcayt ytasaspvvh igaklvlvdt apnsyqmdye alekaitekt
      121 kviipidiag vpcdydkifd iverkkslfk ssndlqakig riavvadcah slgsiwrdqm
      181 tgaiadfssf sfhavknltt aeggyatwrs idgvddeaiy hqfqllslhg qnkdalaktk
      241 lgaweydiqg cyykcnmtdi caaiglaqfe ryplllarrk eiigryiegl kgcnveilph
      301 ftknymscgh lflvrligkd ehyrnrfiek maeagiatnv hykplpmhta yknmgfsind
      361 ypnsynqycn eitlplhtql tneevdyiie kfkkilsd
//
LOCUS       WP_285099345             684 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Gallibacterium anatis].
ACCESSION   WP_285099345
VERSION     WP_285099345.1
KEYWORDS    RefSeq.
SOURCE      Gallibacterium anatis
  ORGANISM  Gallibacterium anatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Gallibacterium.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 684)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 684)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 684)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 684)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 684)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Gallibacterium anatis"
                     /db_xref="taxon:750"
     Protein         1..684
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75175
     Region          138..671
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mdstkfsint tttwillsfl afailpsfal dygllestad eflaamgwhs fnlswfwffs
       61 laifwlfprl gfsqekeaki elvavcaial ftfisadsyh lslgyavilq iialtaiatn
      121 alaklkimqg dkfiiaslla iillifffiv yptlaifism fydgnefnps qfiqiitqsy
      181 ilrvilnsvw lsafvgflst vfglafalyt triakrtafi gkifsilpiv tppfvvglgv
      241 tlmlgrsgyl teflaqhfgf tntnwlygfn giaiaqilaf tplafmileg slksvhpsie
      301 easytlranr yqtffqvifp llkpalanaf llvfiqslad fsnplvlggs fdviatqiyf
      361 yiagsqldya sastlgtill lfslgifivq yiwignrsyv tvsgksyrgd vqdlptglkn
      421 aiiallavwi ifnatlygsi fygsftvnwg vdytltleny aslfgqgfsd gawpslinti
      481 iyagiaaplt alfglliayi vvrkeftgkk tlefltmlcf avpgtvagvs yilafndapl
      541 yitgtgviii ismvmrdlpi gmraaiaglg qldksldeas lslkgnswkt liyvtlpllk
      601 pallsalits fvramttvsa ivflvtadtr vatayilnrv edgeygiaia ygsllivvmm
      661 aiilffdwvv gdtrisrska kqmn
//
LOCUS       WP_285099382             519 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Pauljensenia sp. UMB3104].
ACCESSION   WP_285099382
VERSION     WP_285099382.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB3104
  ORGANISM  Pauljensenia sp. UMB3104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Pauljensenia sp. UMB3104"
                     /db_xref="taxon:3046331"
     Protein         1..519
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=54025
     Region          158..519
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtrrpslagr lsralaacva lalivmvaas tlvmrswmlg nmdselhrls qragehldve
       61 dapddgvgah ddadddsdeg gravpqsggr aprpggpvvp ggpkgpgfgg sgiaegtlqy
      121 vsedgeaaga vvsnfsvtyl nepalailaa vptdgaprtv rlkelgafrv tsqvvgdktv
      181 lvgvqmdsvd dvvlmlvave vglslvvaia agfagrawvr celrplgvvr aaaadiasrd
      241 laddaedltr vgeeatsgpv evadvagaln smidavedgm errarseakl rqfvadashe
      301 lrtplasvqg yaqlarrdid easrtqaler issegarmas lveemltlar ldgnralkrd
      361 nvdviplild alsdahvvap dhawelgeas diqvlgdeaa lrqiltnlla narvhtpagt
      421 rvtvslsrap qgvepakdap assmvrirva ddgpgipaei rdrvfdrfvr gdssrtrdgh
      481 gssglgmsiv eslaramggs vrladadkgt vidvtlpaa
//
LOCUS       WP_285099446             890 aa            linear   BCT 25-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Pauljensenia sp.
            UMB3104].
ACCESSION   WP_285099446
VERSION     WP_285099446.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB3104
  ORGANISM  Pauljensenia sp. UMB3104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 890)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     BTLCP proteins: a novel family of bacterial transglutaminase-like
            cysteine proteinases
  JOURNAL   Trends Biochem Sci 29 (8), 392-395 (2004)
   PUBMED   15288868
REFERENCE   2  (residues 1 to 890)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..890
                     /organism="Pauljensenia sp. UMB3104"
                     /db_xref="taxon:3046331"
     Protein         1..890
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=95596
     Region          475..627
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mssnvntkpr aqriesqaqp eanethvrav geipdaterr drgageqssd apkpkttrnr
       61 lltitqrfat yrtrlpiwsl lilgflfvgp vaafepvfgg gvgaiaagag vicglalsaa
      121 strwrwdgvt svlsvvvtyf llgsaaalrs ealfgvlptg ktlqvmvlgs frawkdlltl
      181 tapvsvysgp alvpwmsglv laflagiita rfgravlgsi plvlmgvisv ffglshhtlp
      241 lwavltwwal laawwaataq yqritlgqdv lvgrssapga dntlgrqsrs tvyvwtrvmg
      301 alavlavsvg ialpaasylg ssgtrivgrd lvqppldiqa ypspmasfrh yttdlkdqtl
      361 ltvsdlpenq rvriaamdvy dgttfgmtnk rddehtgyip vettipgrpe gtsiatvett
      421 gmsgpwvpvl gepsqitfsg asataqkegl fvdtwsnaal ttgpagtmsy svtttftapv
      481 rdedvatlav apftmadtnv peavatkaae itqnastala aaraiehyls tngfylnent
      541 qfsrpgvrad rlermlsddn nligddqqyt almalmlhql ginarvvmga ypeggsqgga
      601 atlrgsdira wvevefaggh wvvfdptppr dhtpqtqvpk prsvprpqvl qppeppeapa
      661 elppttrdqn adpmappadp fpwgvvagia ggfllvllpp llvllykagr rrrrrraaaa
      721 qalvgswdev vdlaadsglr idvgrtrqet awslasqwdl gedpgdpftl vtgevrhgdd
      781 gstdsveide aeagkgryvi dgwsrfgddv papvviarya dvanfasnga srdrardawe
      841 qvgalraqvs kragffarir ralslrslrm rrklrlsasi artmneeedr
//
LOCUS       WP_285099497             637 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Pauljensenia sp.
            UMB3104].
ACCESSION   WP_285099497
VERSION     WP_285099497.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB3104
  ORGANISM  Pauljensenia sp. UMB3104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Pauljensenia sp. UMB3104"
                     /db_xref="taxon:3046331"
     Protein         1..637
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=69109
     Region          37..629
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msetntpqls ekemeeiver avapsaapas sdihpddaqp llkitdlevt ftsstgvvpa
       61 vrganltiyp gqtvaivges gsgksttaaa vigllpgtgk vaggtiefdg rdithlstkq
      121 wvelrgsgig lvpqdpmsnl npvlrvgtqv keallannvv prseagqrvt qlleeaglpd
      181 aerrakqyph efsggmrqra liaigmaahp klliadepts aldvtvqrri ldhlgkltae
      241 mgtavlfith dlglaaerae qlvvmhrgri vesgpaleil qhpqhpytkr lvsaapslas
      301 ariesahkqg isvteeelvg agkgatstda iiraehltke fdirgakkgq dtflavddvs
      361 felrrgttla vvgesgsgks taanmvlqll kptkgkvyfd gedtsqmseg elfrlrrrlq
      421 avfqnpygsl dpmfsiyrli eeplkihgyg tleyaraeik raeatgrepe ewmrvlveaa
      481 dakrsltaae krefnpkklr iaraselldm valprsamrr ypnelsggqr qrvavarala
      541 lnpevivlde avsaldvlvq nqilyllndl qaqlglsylf ithdlavvrq iaddvivmek
      601 gklveanstd elfnnpvqdy trelieavpg rniqlnl
//
LOCUS       WP_285099536             401 aa            linear   BCT 25-DEC-2024
DEFINITION  cysteine desulfurase family protein [Pauljensenia sp. UMB3104].
ACCESSION   WP_285099536
VERSION     WP_285099536.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB3104
  ORGANISM  Pauljensenia sp. UMB3104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Pauljensenia sp. UMB3104"
                     /db_xref="taxon:3046331"
     Protein         1..401
                     /product="cysteine desulfurase family protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41130
     Region          1..378
                     /region_name="NifS"
                     /note="Cysteine desulfurase/Cysteine sulfinate desulfinase
                     IscS or related enzyme, NifS family [Amino acid transport
                     and metabolism]; COG1104"
                     /db_xref="CDD:440721"
ORIGIN      
        1 msvyldqaat tplrecalea wtraqrdlaa tpgnpaalhf ggrrarrmld dareqvacal
       61 gadihevift sgatesdalg vmaaargmrg rdggrslivv sglehdavah qrevasrecf
      121 dwevlpvdag gvsvlpavsg deapaawdgr lalgsmtlvs seigtiqpva nfaalvhasg
      181 glahsdaaqa iptldvsfle lgldlmsvgg hkvgapagtg vlvvrrgipm ttdrpggghe
      241 rsirsgtpdv agacalaaal aevvaeravf atraadlrah llshlpdgvs atvgesasss
      301 aiihlslpta rpeavlmafd magiavsags achagvtrps divmamgrse eqalgvlrvs
      361 lghettrddi daflaalpma iragaaldgv ahvrnernee r
//
LOCUS       WP_285099579             339 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Pauljensenia sp. UMB3104].
ACCESSION   WP_285099579
VERSION     WP_285099579.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB3104
  ORGANISM  Pauljensenia sp. UMB3104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Pauljensenia sp. UMB3104"
                     /db_xref="taxon:3046331"
     Protein         1..339
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=36955
     Region          <90..296
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mrfgwlipvv llvvvaatvi gwmlarrage rsgkkgwvan tgflrdlpky qalvrrtrss
       61 lamavvcfii aviatsvsag apvdrytkyd ksasrdivlc ldasgsmlpy dseigdafkq
      121 iiahfngeri slqlwntysm tmfpltddye maddvltema qqidrgfsqi gnkiyftkel
      181 eaylkptlgn pdekrgslvg dglascvlgf dhtdkkrsrt illatdnevf gegiynlsea
      241 iefaksqgvt vsvlypgsky gmkdegvelq dqvkstggdf ydasspsavd dvvrqieseq
      301 keeldsagkl vetdrpgaal gwtivgvlsl lgllafgrl
//
LOCUS       WP_285099686             465 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Pauljensenia sp.
            UMB3104].
ACCESSION   WP_285099686
VERSION     WP_285099686.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB3104
  ORGANISM  Pauljensenia sp. UMB3104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Pauljensenia sp. UMB3104"
                     /db_xref="taxon:3046331"
     Protein         1..465
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48791
     Region          7..464
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mstnaietvd llvvgggkag kslameraka gwkvamverr fvggtcinva ciptkslvns
       61 arrlsdartd eafgivgteg ahvdlaklra hkegivgamv gahekmfaap gldfirgear
      121 ftgertvtia ledggertir gervlinlgs rparpaipgl wesgawtnee ilrleelpss
      181 laiigasyig vefasmmatf gvdvtlissg dhvlpreded aarvveaglt sagvrivpgr
      241 aesasregnt ttltlsdgst vsaeavlvav grvpntdgig ldeagveltd rgfiavdehl
      301 rtsaqgvwaa gdcagtpmft haswsdfrii raqltgasld dpttttkgrt ipyavfatpe
      361 lariglsege areagldvri akiptaaipr aktmryageg fwkaivdant hqilgatlig
      421 pnvsevitav hvamagglty eqlrflpiah ptmgeglqvl fdslg
//
LOCUS       WP_285099890             342 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Pauljensenia sp. UMB3104].
ACCESSION   WP_285099890
VERSION     WP_285099890.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB3104
  ORGANISM  Pauljensenia sp. UMB3104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Pauljensenia sp. UMB3104"
                     /db_xref="taxon:3046331"
     Protein         1..342
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35328
     Region          30..339
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mksvltrngr lrawvvptlv vlivacaaaa mligrfsvsl edvvaalrar fwggpavppr
       61 vnsvvfdlra priivailig gglsvagasf qslfsnplat pdtlgvaagt cvgavialll
      121 dwnligvqaa alvaglatma fttaisrtrt gsfnvitlvl ggvivsalan avlsllklta
      181 dptsqlpeit ywlmgslaav tyhqialgap fiiagvvviv alrwqlnils lsedearsag
      241 vnvslmrail ivastvitas vismcgqvgw vgllvphcar mlcgqnnrav ipvslllgsa
      301 lmiiidtlar slsaseipis iltaiigapf fivllrrtgg ar
//
LOCUS       WP_285099923             404 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Pauljensenia sp. UMB3104].
ACCESSION   WP_285099923
VERSION     WP_285099923.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB3104
  ORGANISM  Pauljensenia sp. UMB3104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Pauljensenia sp. UMB3104"
                     /db_xref="taxon:3046331"
     Protein         1..404
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42223
     Region          7..400
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mtptpdvprr prmfvgvvgr aarvlataac alalsvgava vspssaradd tittqdyfsy
       61 ykldqarakg ytgqgvtiam idgpvdtsap elaganitvk tpceyeaaks tkthatavas
      121 vlvskdygva pdatliayst asvddkesea ckkdsfgikg safaaiemam ndgaqiisis
      181 rsekdhdvef lnwaitrama rgviivgpmg ndardendas ygwwsgtvgv saidasgqla
      241 sysswgqgvv aagiggpvka rdyetgaikd vqgtsistpi vagqialars rwpqatpnqi
      301 lqlvirsgsn ngvwnqytgy galsldgllg sdpsqypden pladkgggst ptpaevqqyl
      361 dglvpfmdvv fddsyvyrgl dedaagneya pnahigtspa yhrk
//
LOCUS       WP_285099947             917 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Pauljensenia sp. UMB3104].
ACCESSION   WP_285099947
VERSION     WP_285099947.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB3104
  ORGANISM  Pauljensenia sp. UMB3104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 917)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 917)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..917
                     /organism="Pauljensenia sp. UMB3104"
                     /db_xref="taxon:3046331"
     Protein         1..917
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=100464
     Region          19..808
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 msatlneild dledegrlgd ddalyeafvs waegtgrply phqeealvei lagnhviaat
       61 ptgsgksmia laahftsmah ggrsyytapl kalvsekffd lvslfgadnv gmvtgdvsln
      121 adapiiccta eilanqslre gptldadmiv mdefhfygdr qrgwawqvpl lelrapqvva
      181 msatlgdttr ferawkertg rdvsliddae rpvplefeyv vdrlpntver llgegrwpvy
      241 ivhfsqrdav ataqsfdrss lispeqkkai aaqlagvsft kgfgqtlksl laqgigvhha
      301 gmlpryrrlv erltqagllp ivcgtdtlgv ginvpirtvl mtslvkydgr rmrhvsaref
      361 hqiagragra gfdtvgfvrv lapehevdaa rerarlsaaq eaardareak raakksakkr
      421 kgpgegeisw trstferlvd aapeqltsrf emthamvlnv lagapaagrd pgehlvwlar
      481 nnddpptdrn phlrrlgeiy tsmkqagvve hvssaeasas geprlraatd lpddfalnqp
      541 lspfalaale lldpesptfa ldvvsviesv ledprpllfa qekaaraeav aamkaqgmey
      601 dermaaledv twprpladll gdafavylha npwiedqeis pksvvremie naltftgivg
      661 rydvgrsegi vlryltdayr alrqivpdel mtdelrsiia wlsaliravd sslldeweam
      721 stgqafspea egvgtegael afgaredgtv pfsanrhafr ttirgalfer veamsrdnve
      781 alarldeasr tpvvapwgkd ewdaaleryw aehewigidq raralslcsl neaptredvl
      841 elapavvssd feraqvarie aiadaldqaa pgtfwlatqt lfdseedmdw rivalvdvpa
      901 sdeanrvala titvgvr
//
LOCUS       WP_285099952             481 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Pauljensenia sp. UMB3104].
ACCESSION   WP_285099952
VERSION     WP_285099952.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB3104
  ORGANISM  Pauljensenia sp. UMB3104
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Pauljensenia sp. UMB3104"
                     /db_xref="taxon:3046331"
     Protein         1..481
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49812
     Region          3..466
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 magldvipes drkgkpsdlf mpwfaanisv lgiswgswvl gfglsltqai vvsvvgvals
       61 fvvcgliaia gkrgsaptlv lsraafgfng nrisaaiswi ltvgwetfla imavqatatv
      121 mgalgftnhv vaqiialilv vvlaagsgil gfeaimkvqt witwataalt ivylvlvapt
      181 idfavlssrp sapltavlga gcmllvgfgf gwinaaadys rylpraastr gvvgwttlga
      241 alptvvlvff gillvgsade slseaigndp igalttllpt wflipfalva ilgliggivm
      301 diyssglsll atgvpvsrpv ataidgtimt vgtiivvffa dsfltpftaf lttlgvviaa
      361 wggvmladia lrhkdydeps lftpsgrygs vnlgavasli vgslvgwglv vnanaswlsw
      421 qgyllgplgg regdwagani gillamvvgf vgywltsagr vraqeklpsr tyaqgveege
      481 q
//
LOCUS       WP_285100468             101 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [unclassified
            Promicromonospora].
ACCESSION   WP_285100468
VERSION     WP_285100468.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 101)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 101)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 101)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..101
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11118
     Region          13..95
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mgdypspdma evelvdvlka lgdpvrlqiv hkladgepkp ktldgwgldl tkstmshhfr
       61 tlreagltrt ivhgrthaiq lrrdelddkf pgliaavlae r
//
LOCUS       WP_285100661             950 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Promicromonospora sp. MEB111].
ACCESSION   WP_285100661
VERSION     WP_285100661.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..950
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..950
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=100535
     Region          <2..949
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mgrtaelesl vrkvlqtpsl vvidgeagvg ksrlvrelat dpalagrpvl ighcehlqep
       61 lplapvldvl shhadlvpag dhnpivgala plvpelgdrl pppppeladq gasrhrvfra
      121 aaelldrigp avlvledvhw aesstfdflt flaahqpagl civltlrsgg aplpvresfa
      181 raasgpplal tlrpldpagv gelagrilgt qvsdafaasl hertggipfv aeevlgtlhe
      241 tplpddgahq ddvltdlavp talrdvvlgr ldgvaegtre vlgvasvldh pvdvdliaev
      301 tglppadvva alvdaitagl lheqdgqvrf rhvlaeqivy dalptptrrl lhrtvaraie
      361 dregprpvar lahhyqragd tirfvryaed aadlavshgd dahaarllvq ametdlptdh
      421 rlrlavklgr aavdglahie avpllqqlla tellpsdvrg elrfalgrll rqqgladagy
      481 reieqalpdl ganpallara lavlaapetv adrpmtvhaa rgeqardaar rsgaadvela
      541 vriadaslli eqgrpegwsv veelladeal adfprehara cvnwaqaalh vghvrraerl
      601 laegrrvvaa aeylrvtdvi elvaaavdcs agrwadlagr ahelvvrrpg ydaatlddhl
      661 lhgimlaasg gtqeavahft alvedaarvg avwpllagrs alarllltld dvegsahqag
      721 lavstarqkg nwvwaaepml clvdalvaqg rtaqarahve elaaglgvvd aplalaalhs
      781 cravvahadg nhaaavgllr eartivadag lrheesrvve rlgvwlaedg daegaallee
      841 alrgyggraa sndvarvtrt lrrlglpvpy pwrggrrsng lglsgrerev allaaqgrtn
      901 rqiaadlfls prtveshvrn alrklgcssr adlavhlldd agedraavag
//
LOCUS       WP_285100669             340 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285100669
VERSION     WP_285100669.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..340
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=34245
     Region          39..338
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mttpnllgsd lpivaapmag gatttalaaa atragafafl pggyltperl aadiaaaraw
       61 dspfgvnlfv pgtgsldraa faayarrlap eadalgvels adpvddddrw pdklallldd
      121 pvpvvsftfg lpgpadihal rragtvvlas vttadeaaaa sdggvdglva qgpaagghsa
      181 twdparrvad aptasvvrav aaavdlplva aggvggpeav relltagaqa vavgtlllrt
      241 desgasatyr dalaasdrgt vvtrsftgrp aravrnrfvd rhdavapvgy paihhltrdl
      301 rrraaaagda erlhlwagtg yrhattgaaa evvrglaaal
//
LOCUS       WP_285100759             534 aa            linear   BCT 25-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285100759
VERSION     WP_285100759.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..534
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=56093
     Region          6..534
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mstradlllr gglvvdgsga epvtgdvlvr sgriaavggr idapgarvvd adglavapgf
       61 idmhahsdla vladgdhlak vtqgvttevv gqdgisyapv tdetmalvre qiagwngipd
      121 gvdfswrsva eylaevdrrg satnvaylvp qgtvrmnvvg tgdrratpae iaemraqvdq
      181 glregafgls sgltyvpgmf adtdelvalc evvaerggfy aphqrsygag aigayaemvd
      241 varrsrcalh lthatmnfpe nrgragella lvdravadgv ditldtypyl pgsttlsall
      301 psraavggpe rtlarlgdpa erawitheve vvgsdgchgv pvdwdtieia gvrdaalgdr
      361 vgrtvarial degrppaevf ldllvadrlg tsilqhvgde qnvreimrhp rhtggsdgil
      421 vgakphprgs gtfprylgry vreegvlsla emivhlsarp aarlglhdrg riaeghvadv
      481 vlfdpaavad raapdeprlt aagipwvlvg gvpvieegar taarpggalr hapr
//
LOCUS       WP_285100760             417 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase 5 family protein [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285100760
VERSION     WP_285100760.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Sharma,K., Dhillon,A. and Goyal,A.
  TITLE     Insights into Structure and Reaction Mechanism of &#946;-Mannanases
  JOURNAL   Curr Protein Pept Sci 19 (1), 34-47 (2018)
   PUBMED   27739373
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Ketudat Cairns,J.R. and Esen,A.
  TITLE     beta-Glucosidases
  JOURNAL   Cell Mol Life Sci 67 (20), 3389-3405 (2010)
   PUBMED   20490603
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467628
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..417
                     /product="glycoside hydrolase 5 family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46013
     Region          7..330
                     /region_name="COG3934"
                     /note="Endo-1,4-beta-mannosidase [Carbohydrate transport
                     and metabolism]"
                     /db_xref="CDD:443135"
ORIGIN      
        1 mttttprfgv nytpskdwmf qwmaidpdvv radfeaiaal gvdhvrvfpl wpvlqpnrtl
       61 irqralddia lvadlaaeqg ldiavdviqg hmsgfdfvpa wlvnwhdgnm ftdqpaieaq
      121 aalvaavyda vrdkpnflgl tlgnelnqfq rpnpaampak rdevthwlts lleaprdrdp
      181 rhlvthsend hlwyrdehpf vpvhasrlgd vttvhswifn gtaatygals pqsvrhaewm
      241 ielskafaae prrpvwlqev gapsmnlaea empefcarti eaalttddly avtwwcshdv
      301 trelgdykdl eyslglldte nrvkplgrrf aevvaearaa garpagpgra tavvvdvded
      361 dlplsrpslg pggavferwh alreegvevt vvtsaaaadp aaleargire lvrvdag
//
LOCUS       WP_285100909              67 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285100909
VERSION     WP_285100909.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 67)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..67
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=7515
     Region          1..62
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mesdpllrtr evaellgvpe ntlrwwryvg ygpesfrlgp rrvvyrrskv lawlaaqeaa
       61 gakttav
//
LOCUS       WP_285100917             403 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285100917
VERSION     WP_285100917.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18528417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..403
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43077
     Region          1..79
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          164..>368
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
ORIGIN      
        1 mtdlaenlar lrkakdlsqe slaeragvgv dtvariergt rttcrpatlh rlaaalsvsa
       61 qtlltgednr qsalatnaem vrlrqaitsg glvpglsdfa entetvslte aerqttavwr
      121 lyvdgrhtel lallpavlad arrlvetnhg ddaaagrrll attyriaagi agrlgqddla
      181 wtaaeraldv arssddpelq qavalrylaw tlvrqgrede aeqvatnaae aiqptmldad
      241 pvrtavfgnl lfnaataavk agavqraadl laearsaaar tmtsvvteaa ifspravalq
      301 evdhwsrsnd petalhqaat lqsvpgqlpa fweagsalhi asaslktrry ddalhhldqa
      361 hrlapdwats qplgvttmra lldratrrrg prfaglaqaf gva
//
LOCUS       WP_285101127             302 aa            linear   BCT 25-DEC-2024
DEFINITION  type I methionyl aminopeptidase [Pauljensenia sp. UMB0895].
ACCESSION   WP_285101127
VERSION     WP_285101127.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB0895
  ORGANISM  Pauljensenia sp. UMB0895
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Pauljensenia sp. UMB0895"
                     /db_xref="taxon:3046319"
     Protein         1..302
                     /product="type I methionyl aminopeptidase"
                     /EC_number="3.4.11.18"
                     /GO_function="GO:0004239 - initiator methionyl
                     aminopeptidase activity [Evidence IEA]"
                     /GO_function="GO:0046914 - transition metal ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32777
     Region          4..288
                     /region_name="Map"
                     /note="Methionine aminopeptidase [Translation, ribosomal
                     structure and biogenesis]; COG0024"
                     /db_xref="CDD:439795"
ORIGIN      
        1 mqrielktrd qirwmreagl ivadihaslr qavragvtta eldevsadai rrggatsnfl
       61 nyygypatvc isvndvvvhg ipgkqklkdg divsfdcgaw vshggkqwhg daafsiivgd
      121 ewvddesfma gkrgsgahpq gvdeammkrr reldvvtres lwaalaslek grrissvgra
      181 veevvakydd efgweagiie eytghgigta mhqdpevlny dargifprvk pgmvlavepm
      241 ltsgsietlt esdewtvrtv dgsdaahweh tvailddgis vltapdygka glapfgvepi
      301 el
//
LOCUS       WP_285101128             208 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Promicromonospora sp. MEB111].
ACCESSION   WP_285101128
VERSION     WP_285101128.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..208
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21669
     Region          <40..202
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mspsepapts pvehfavrhy rrartevapw arssgvvali aavwavwasg pgwltpaylv
       61 lavvgaalgv idahthrlpd alvfpltwat avllavaalg tgswgdlgra alggiaffal
      121 yqvlylvspr ggigygdvkl slslgafltw hswgtllvgv faahlvagvv aivlllgrra
      181 gwksgiafgp ylllgtaigl twarltaw
//
LOCUS       WP_285101149             286 aa            linear   BCT 25-DEC-2024
DEFINITION  arylamine N-acetyltransferase family protein [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285101149
VERSION     WP_285101149.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Zhou,X., Ma,Z., Dong,D. and Wu,B.
  TITLE     Arylamine N-acetyltransferases: a structural perspective
  JOURNAL   Br J Pharmacol 169 (4), 748-760 (2013)
   PUBMED   23517104
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Sim,E., Walters,K. and Boukouvala,S.
  TITLE     Arylamine N-acetyltransferases: from structure to function
  JOURNAL   Drug Metab Rev 40 (3), 479-510 (2008)
   PUBMED   18642144
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Sim,E., Westwood,I. and Fullam,E.
  TITLE     Arylamine N-acetyltransferases
  JOURNAL   Expert Opin Drug Metab Toxicol 3 (2), 169-184 (2007)
   PUBMED   17428149
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Sinclair,J.C., Sandy,J., Delgoda,R., Sim,E. and Noble,M.E.
  TITLE     Structure of arylamine N-acetyltransferase reveals a catalytic
            triad
  JOURNAL   Nat Struct Biol 7 (7), 560-564 (2000)
   PUBMED   10876241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..286
                     /product="arylamine N-acetyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31352
     Region          14..260
                     /region_name="NhoA"
                     /note="Arylamine N-acetyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2162"
                     /db_xref="CDD:441765"
ORIGIN      
        1 mdillamehe aagylarlgl earppatvgt lfeihrrhae ripyenlhtm lgdppaigaa
       61 atlarvatgg nagycfhhng vmttalralg ydvvpawghn wddeaerrdl hvghlalsvr
      121 glptdenpag vwwpdvgcgd glheplplaa geyrqgpfty rldvrddgwt fhhdaqgsfg
      181 avdlfdealt peqadaahrr ltapdggaya rklvvqrrlp daaetlrgcq ftrtgsraeq
      241 velttyddwr dglrtlgitl rginddalrg lfdrslaahr dwvatr
//
LOCUS       WP_285101274             446 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Pauljensenia sp.
            UMB0895].
ACCESSION   WP_285101274
VERSION     WP_285101274.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB0895
  ORGANISM  Pauljensenia sp. UMB0895
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Pauljensenia sp. UMB0895"
                     /db_xref="taxon:3046319"
     Protein         1..446
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47272
     Region          53..442
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mmiwivvgil tlafvlfggl wlwrwyqtrq arlqlrkdam ltpssafdpe rgrprpwviv
       61 npvkhddvda fkaevnqaah qmgidhvhwr ettaedpgtg qaidalaqga sviiasggdg
      121 tvravaagva gsgvrmgiip agtgnilarn lgipiddsaq amrialgenh raldcgwlrv
      181 dnvdtpseip aegmlvraal tknrvdtdtp psldqadssl ahraqnlpgt deysfvviag
      241 lgfdgetmaa tdselkkkvg wvayviaalg aiakegtrlr lmlrnpkpid dpvgdapgdd
      301 ehsrvvdesa tisgvsvpdq pesvltwvhs rtvmfancge lpfitlapga rvddglidvi
      361 avnteagvlg wadlslkimg qglgvktmnl pvstgkiqfr qaegasvaaq spqviqvdgd
      421 aigtartvhv rldpqaldia vpglen
//
LOCUS       WP_285101300             271 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285101300
VERSION     WP_285101300.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..271
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27305
     Region          1..263
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mstsptllvl gagpglgmsv arrfgkegyq vglvsrsadr hpgylddlrs agaravavaa
       61 dvrrpgdlrr aineveaelg pvevvyhgpg adnpaaapig ildtsaddvr gaaaqvvdpa
      121 velaglvlpg mrergsgaiv yvsglsavvp lpflgpfapa saalrtyalt laeaaapdgv
      181 hvgslvvggl iergdihrml tagqmdvggt dapqatldpa pdlasdltsd papgsapipv
      241 ldpddladav wriatgaere vvfnalvpna v
//
LOCUS       WP_285101355              69 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pauljensenia sp.
            UMB0895].
ACCESSION   WP_285101355
VERSION     WP_285101355.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB0895
  ORGANISM  Pauljensenia sp. UMB0895
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 69)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Pauljensenia sp. UMB0895"
                     /db_xref="taxon:3046319"
     Protein         1..69
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7605
     Region          10..65
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(13,17,42)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(16,41)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(23..24,35,38,42..43)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 msisqvvttr kvrqfleeth tsqeslakal hltqstlsar lrnetrwsln dldaladagi
       61 vaplwegde
//
LOCUS       WP_285101368             324 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285101368
VERSION     WP_285101368.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18123688
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..324
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35472
     Region          7..208
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          <251..306
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 miryrlgaga asvrwamspv hevvslarll teprrhpvfq pwlrrrrqrl tgldlsaltv
       61 fmadgayrpd fldpspmsse ptfddglaal laapldqvha elvdatarhd ddvrrrlldd
      121 pertrtqaaa avrrlwkaav epewpsmrqa lraemldrav qvnreglrav vprlhssasa
      181 egdtitiesa vdvgvdcpdg lilvpslfit drvqcttsdh wspaicypat grylwsapvi
      241 prsldrplgv trsrilaalv tplqtsvvad lvsvtkptas ehltilrdag lidssragrt
      301 vtheltvagr alleaapprp rpgr
//
LOCUS       WP_285101425             772 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Promicromonospora sp. MEB111].
ACCESSION   WP_285101425
VERSION     WP_285101425.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 772)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..772
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..772
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=83627
     Region          8..767
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 massfgpllr glrqstglti eelshasgvs vraigdmerg vsrgpqrrtv ealadalgld
       61 deqraeladt aragrpraad papeqpgsna lprslgdfvg rtaelellde rartasadgp
      121 tpvvvvhgaa glgktacavr aaellherfp dgglyvdlrg vdpepmatte alrrlllasg
      181 ldaraiaedq heragqlrai ladrrslvll dnaadeaqvr pllpahgagm vivtsrrtla
      241 glegvtrvpl apfspqesae llealanrta dgnavtetaa etarvselcg rlplalriag
      301 trlasqpewt mrhlaerlsd edrrlanlav gdvgveaafa lsyvalpeqa kecfrrlalv
      361 pavdfgapia avltetdryd aedqldelve lgllqhegtd ryrfhdlirl yanqrlheee
      421 sdaarataer rmtdwlleta taagrwfdge sppagdeghv rftspeearv wllvekeswl
      481 aalrlaavag rdaqvarfge amnwianetq vwatdwlevf gltrsaaarl pdrrgelwht
      541 iryvwarltv aaqrrddkal reaaeqamea yqlaeglgav reqaeavcna aeawrlahdd
      601 drslwaytrg relaetagdq styfwasggl vvglaqagry ddalkafrsm lrtieelpap
      661 taaaentrwf alarlstlla dagrygdvve iartsaaall eegnnwaplt hravgraylg
      721 lgandkareh ltlaigrgea rgrwqprpaf vdevnaliaa lddeagapee ig
//
LOCUS       WP_285101494             313 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Pauljensenia sp.
            UMB0895].
ACCESSION   WP_285101494
VERSION     WP_285101494.1
KEYWORDS    RefSeq.
SOURCE      Pauljensenia sp. UMB0895
  ORGANISM  Pauljensenia sp. UMB0895
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Pauljensenia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Pauljensenia sp. UMB0895"
                     /db_xref="taxon:3046319"
     Protein         1..313
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32485
     Region          8..313
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mtahttakrr sihllissms aggrsvnvgp evvrilrggg wavrvsvtra sddpcqiasa
       61 ttedvigalg gdgfisaiar gahetgtlfa pipggrgndl cralgispda sarakqlael
      121 gfvneesdel fasrirpmdg mwvttpdgtv hslvlglvsl gldakanlla nesmftsgpi
      181 aygygafaal athrpstitl kidgqerelt gwitsvsnsg rlgggvrlvp qsdmtdgime
      241 lchvedipll kalpilakvv ggrsqghevi hvepassiei tqpvgmvama dgdkvaeipf
      301 tvtsaphivd vlv
//
LOCUS       WP_285101517             174 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Promicromonospora sp. MEB111].
ACCESSION   WP_285101517
VERSION     WP_285101517.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 174)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..174
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19093
     Region          27..156
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04683"
                     /db_xref="CDD:467566"
ORIGIN      
        1 mteaagtapv gsdryderdh erftlvpaay lyfrregqvl lqlrqgtgyr dgfwacaaag
       61 hveegesvvd tavreareel gvevapadvr pltvlhrgep ggpaieqrvd fmfevtrwtg
      121 tpsiqepdka adlawfpfvg lpdpvvphel avlravhdag rhgtemprll tfgf
//
LOCUS       WP_285101598             555 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Promicromonospora
            sp. MEB111].
ACCESSION   WP_285101598
VERSION     WP_285101598.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..555
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=58878
     Region          20..550
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtvtaaapag vaaapassal lrvegltvay grthvvsdvs ftlgrgesla ligesgsgks
       61 tiarsllrll pdagaahgrv efegrdvlsl perqfrplrg rslgfvpqdp gsslnavrti
      121 gaqaqeaaal tgerdagtrr rlildtfaqv glddpgrvyd syphqlsggm lqrvliglav
      181 lprpallvad eptsaldvti qkrildllse lradlgisll lithdlaiaa eradslvvlr
      241 dgvvqeagpt aqvfaaprsa yarelqadvp alnpdryral retragsagd pgsaeateaa
      301 prielrgvtk aftvegrrlt alddvsfavr hgtthalvge sgsgkttavr lllgldqadd
      361 geilvagepv hgrsaaglra vrrhlqlvyq npftsldptw rverlvrepl drfgigdrae
      421 rtvrvreala avglaeella rrpgalsggq rqrvaiaral vlrpdvlvld eptsaldvtv
      481 qadlvevlvr lqaelgltyv fvshdlalvr qladtvtvlh rgrvveggev ekifatpaap
      541 ytrrlldsip hpsgg
//
LOCUS       WP_285101620             292 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase
            [unclassified Promicromonospora].
ACCESSION   WP_285101620
VERSION     WP_285101620.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..292
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29771
     Region          19..247
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 madtaapnps eaaapgpart alvtgasrgi greialglar agldvallar daarleavaa
       61 evraagataa vltadvsdpa avraavgqae dalgsidllv nnagaieseh plweadpdew
      121 wsvfetnvra pflfsrftvp gmiargggrv vdlasgassh emagghsayn asktalvrmg
      181 anlhedgfph girvfelapg vvktdmstgm tlhenrtewt paervtdvvn aiaageldac
      241 sgwflrvsdd tpeslkalaa dvaeqgagat arrlrvlpag sgdplaaalt gr
//
LOCUS       WP_285101878             254 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase family protein [unclassified
            Promicromonospora].
ACCESSION   WP_285101878
VERSION     WP_285101878.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..254
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27115
     Region          8..252
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mvvaervtfe sttgprlagi idrpdgevrg wgvfshgftl gkdspaaari ckqlaiegig
       61 mlrfdnlglg dsegdwgdgs fthkvadtvr aaefmadhdm pvhllvghsf ggaaviaaga
      121 dvpgvqavat igapvqprha ehnydavlgr vfddghaqwm vggraltlkr hfvedvrrae
      181 lrskirelgs pllvmhsptd stvdisnage ifrearhprs fvslegadhl ltapgqakra
      241 ariisawadq ylta
//
LOCUS       WP_285101861             259 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase
            [unclassified Promicromonospora].
ACCESSION   WP_285101861
VERSION     WP_285101861.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..259
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26839
     Region          1..256
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mgtalitggs aglglefarq lgaaghdlvl varddrrlad vaaqlhaatg vavevlpadl
       61 svpddvarva rrlavvggrp edgdlrpvgl lvnnagfats spfstgritt errgidvmvk
      121 avvelshaav gqmlerrrga ilnvgsvaal taggsyaaak ayvrtfsesl aaelkgtgvt
      181 vtvvapgfth tefharagia esaivpewgw leaedvvrta ladvrrgvvl stpsvrykva
      241 saalrimprw avravgsyr
//
LOCUS       WP_285101952             307 aa            linear   BCT 25-DEC-2024
DEFINITION  COX15/CtaA family protein [Promicromonospora sp. MEB111].
ACCESSION   WP_285101952
VERSION     WP_285101952.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..307
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=32416
     Region          45..305
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mtapaapvsw ldalpgrvdr frhwtravli anligqigii gtggavrltd sglgcstwpq
       61 cepgsftpqf heattlhpyi efgnrtltgv lgvvavllav lvctdlkrta syrmlglapi
      121 vgvmmqalig givvllhlhp gwvslhfavs galvavslyl lhrhgegdga prlvvpprvr
      181 tlawalaglt avvvvlgvlt tgagphsgds evgyrfaidp alltrwhaaa vwvflaalaa
      241 flvavrrgpa evrraavill vitlaqglig yvqyftdlpe llvglhmiga aaliagttrv
      301 wlttrvr
//
LOCUS       WP_285102132             166 aa            linear   BCT 25-DEC-2024
DEFINITION  flavodoxin family protein [Promicromonospora sp. MEB111].
ACCESSION   WP_285102132
VERSION     WP_285102132.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..166
                     /product="flavodoxin family protein"
                     /calculated_mol_wt=17770
     Region          3..161
                     /region_name="FldA"
                     /note="Flavodoxin [Energy production and conversion];
                     COG0716"
                     /db_xref="CDD:440480"
ORIGIN      
        1 mlyesmfgnt rqiaqaigdg lsdltdvrve pasagpdlav dlvvigapth ahtlpqassr
       61 edaarwaadp dqhlvlepga akpgvrewie slstppaawa afgtrvdipr ifagdasagi
      121 errirrlhsr pvadsecflv ttknvlvdge ldrarewgrs lgqavr
//
LOCUS       WP_285102206             342 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285102206
VERSION     WP_285102206.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..342
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36389
     Region          21..334
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mptaastmts arllsllsll qvrrdwpagq larrlgvsdr tvrrdvdrlr elgypvrtar
       61 gpdggyrlea gselppllfd deqavalava lrlavvtgag ieeaaaralt tvrqvlparl
      121 rqrvdalelt aaepagpgdg dqvdtdvlla lgaalrahee vrfdyaspgr pdagtpprrv
      181 qphhlvvrar rwylvgwape pgewrtyrvd rmtprvpngp rftprqvpgg dvgaflaarf
      241 rgstdlegst gagawpcigd vvlalpvarv apfagdglve elgpdrtrlr tgswswaala
      301 aalarfgaei evvgppalrd afadlagrag raadlpsadp vs
//
LOCUS       WP_285102370             234 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Promicromonospora sp. MEB111].
ACCESSION   WP_285102370
VERSION     WP_285102370.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..234
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24217
     Region          9..198
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mpressalpa avlfdmdgtl vdseaywmra eheivvahga mwthedalga vgqallttgg
       61 mlhdagvple paeivtwlva rvneqlreav pwragvlell edlraadvpc aivtmsyrsq
      121 aqvvadgapa gtfthlvtgd evthgkphpe pylvaaglfg vraedcvaie dsgpgitsal
      181 asgartlgvp aevpvpprpg lsraaslkqv dldllgrias gevvdllgag dlag
//
LOCUS       WP_285102215             537 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Promicromonospora sp. MEB111].
ACCESSION   WP_285102215
VERSION     WP_285102215.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..537
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=56291
     Region          165..533
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mpdvvaptdr apstrrptal rrrlvlvlaa vvlvvtagla vastavlrsq llnqvdsele
       61 qasqrltqgp vqirfrdaap gddasgtqpg qeipalpmpa pgeasdttrp afppglgpgs
      121 avvryvdgep vladhvttsl erealdddqv aelldvpadg rphdvrldgl gafravhvtt
      181 dddeplvvat statvdatvh gyvlvevalg vaallaavgv gawlvrrslr pldgvadaas
      241 rvselelsrg aidaiprvpa tltdertevg qvgaalnrml envevslqar hdsetqvrsf
      301 vadashelrt plasirgyae lvhrapeelp ptaarsldri eseavrmtgl vedllllarl
      361 dagrgldrap vdlvalavdg vmdahaaspg hawklelpsg adddahaggd radelvvtgd
      421 easlrqvvan llanarthtp agtqvrvrll regdavvlhv tddgpgipag lrpslfhrft
      481 rgdvarnrng gstglglsia daivtehggs iavrsrtade gpatgttftv rlphrmr
//
LOCUS       WP_285102455             190 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: HIT family protein [unclassified Promicromonospora].
ACCESSION   WP_285102455
VERSION     WP_285102455.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..190
                     /product="HIT family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20573
     Region          46..172
                     /region_name="FHIT"
                     /note="FHIT (fragile histidine family): FHIT proteins,
                     related to the HIT family carry a motif HxHxH/Qxx (x, is a
                     hydrophobic amino acid), On the basis of sequence,
                     substrate specificity, structure, evolution and mechanism,
                     HIT proteins are classified into...; cd01275"
                     /db_xref="CDD:238606"
     Site            order(71,73..74,81,83,129,137,139,143,145)
                     /site_type="active"
                     /note="nucleotide binding site/active site [active]"
                     /db_xref="CDD:238606"
     Site            order(141,143,145..147)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238606"
     Site            143
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238606"
ORIGIN      
        1 mnseptpesp tafgpsddgl qrlwtphrmv yiggqdkpad gttqqcpfcr ipagddeqgl
       61 vvargercyv vlnlypynsg hmmvlpyrhv sdytdldaae tvelarmtqq amrvsravha
      121 pagfnlginq gevagagiaa hlhqhvvprw lgdanflpvv gqtkalpell adtrrrlaea
      181 wetagggeen
//
LOCUS       WP_285102604             414 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified
            Promicromonospora].
ACCESSION   WP_285102604
VERSION     WP_285102604.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..414
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=43640
     Region          7..403
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrphvprvpd vrpldplrsl kiklgvlvaa tvtaavlitw lglqaslgps rtfplaiils
       61 llvtqilarg mtsplreite avqamadgdy trrvratssd evgqlahafn rmaedlasve
      121 qtrrdlianv shelrtpvaa lqaqlenmvd gvvqptpaal eqahaqterl trlvtylldl
      181 srieagasal nvgeiavgdf lehcaedlqm vdaakdlhyv idvtpedlti egdaerlhqv
      241 vinllqnair hspqggvvrl daypvdgteg sdivlevsde gpgiaaadre rifqrfvrgt
      301 gstgaqrgdg grdgggrgvs rrggrnrgdk gdkgragtvd eslvdtmsga dgtvgsgtvg
      361 ssggtgigla ivrwavelhg ghvevvdsdr gatmrvtlpa rahpapgvtt thtv
//
LOCUS       WP_285102644             255 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: GOLPH3/VPS74 family protein [unclassified
            Promicromonospora].
ACCESSION   WP_285102644
VERSION     WP_285102644.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..255
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=26016
     Region          3..200
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mliaedflll avddetgkta nvdnlgvrla galladlsda rktllrgape agatkeerek
       61 agdatiivtd nspvghvald aalqsvlatp daparkvvea iskdaeenll aalvergile
      121 keesklfrml pvtrwpaads shetalranl tkvlvegaep dertatlisl lhgsglisgl
      181 vgkeqrkaaq draeeiagse wgvatvatqv aiaasvaava tvgaavaaav iisatkenae
      241 aeaaaipaae gtpva
//
LOCUS       WP_285102676             912 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285102676
VERSION     WP_285102676.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 912)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 912)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 912)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 912)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11971133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..912
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..912
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=96270
     Region          <3..874
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          851..907
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mtttssgllg redeqdrlaa lvggarngrs gtlvilgepg mgktsllgev atraeharvl
       61 ridgyeseat ipyaglhrlt lslrefmael pphhrdaldv avgrtagapp drflvglgal
      121 ellgaaatdr ptlcvvddah lvdaesldvl afvarrlmve rltllcagrd egdlvtrmrg
      181 idlftlsgla tdsavnlftr avrgtidpvv atqvahatgg nplalielar slspaqltdl
      241 glsatpvpvg qrlerhyigr vdelddhart wlllaaadst rktglvmaaa dtwgldpgap
      301 draeaaglve igdvvrfrhp ligsavyrsv dgaarrrahr slaraaaalq iteleawhas
      361 ratvgiddav aaqlervadm aarrggmasr armlgraael tspgplrdar qvsaaeaala
      421 vgagnaaata ldavdvaeae pvtqgrvtma ratlaaftgs gpdyvrasad lvraadlfhg
      481 rdavleqral vsaaelcmna drlmegittt dlghrlhrgt avadgpaavv laglgalirl
      541 pyaeavphar taldtiralp daelmhsgis vaalstflwd tsgrelllra mraardagal
      601 qvvdlllkvm slnelscgtv rlatryaell revrlamgyd tapvlnpvvl awtgsprgev
      661 lalaaaaqaa grggvsalte aavavrdlag gsyhdaydrl rplvtssflq vtptqwadyv
      721 eaaarsghpd eassyaaalr eravvngspw crgvadratg laasgpeaek yfrsaldale
      781 ptavltdrar ahlvygewlr rsrrradavv qlreairlfe eagaqifvpr ataeleaags
      841 raettpaspr qplttqelti aekaaagrtn aeiasnmfis antvdyhlrk vfqklgissr
      901 rqladrlgat rs
//
LOCUS       WP_285102687             283 aa            linear   BCT 25-DEC-2024
DEFINITION  amidohydrolase family protein [Promicromonospora sp. MEB111].
ACCESSION   WP_285102687
VERSION     WP_285102687.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..283
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30747
     Region          3..283
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mfvdthvhlw drrehdlgyg wldgddfpfg dlvavrtarf svpelraegr lagltkvvhm
       61 naastagdpv aetawlqrls detgwpdaav vtcdlaapdv aaqlarhrah pvfrgvremg
      121 pvarfadpaf rrgyaelgrv gglffhtvgl agtaaaldlv rscpetvfvl dqagmppdrg
      181 vdtfeawrgm lrglaaepnt lckvsslgma dpvwtpasrr pwvlapieaf gadrvflgsn
      241 wpverlyssy tdvveafrha vrdltpaern avlagtaerv fgi
//
LOCUS       WP_285102986             209 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285102986
VERSION     WP_285102986.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 209)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 209)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..209
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23250
     Region          26..93
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mpeqmqpetq gftrptpped avisqadaik amthplrirl lglfrpgvel tatqcaertg
       61 esvascsfhl rqlekyghve raeahgkerp wravsrgfsv rpdladpesw paaqafgsmf
      121 vaeqfaalqr wladagrddp awvfastqta qefwatrdel ddlsrrleei tapfrgravd
      181 pgkrpecarr ahlfgavwae ipepegeda
//
LOCUS       WP_285103006             572 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Promicromonospora
            sp. MEB111].
ACCESSION   WP_285103006
VERSION     WP_285103006.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..572
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=59998
     Region          19..570
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msrvegtsat pgeavpdrpv ldvrdlvvsf sgrrvvdgvs lqvaagecva ivgesgsgks
       61 vtarsvvgla gegarvsaar lsvagqdvls lsgrrlrklr ggtvgliaqd alvsldplrp
      121 vgreiadtla lhtdldaaar rartvaller vglpdaelra gqrpgqlsgg qrqraliaag
      181 iaadprlvva depttaldqp vqagvlrllg qlrdegtgvl lishdlsvvl giadrvlvmt
      241 dgvvveegtp aevferpghp ytrklvdavp agrprgesls vsagalppsa gpgvgersdg
      301 rsksadtatd stfdgtdage rvlveargls rvfhvggrei vatddvsftl ragrtlglvg
      361 esgsgkstta rlllglehpd agevallgep wnplpearrr prrhligavf qdalssfdpr
      421 wtvgavlada itrgrslrpg pvraqiadll ntvgldpala trrplhlsgg qrqrvsvara
      481 laaeprvlvl depvsaldvs vqaqvldlld rlqrerdlay llithdlgva lhmsddlavm
      541 qegriieqgp astvfedaeh pyarqlrdav rl
//
LOCUS       WP_285103085             345 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family oxidoreductase [Promicromonospora sp. MEB111].
ACCESSION   WP_285103085
VERSION     WP_285103085.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142552
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..345
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37326
     Region          3..289
                     /region_name="AR_SDR_e"
                     /note="aldehyde reductase, extended (e) SDRs; cd05227"
                     /db_xref="CDD:187538"
     Site            order(8,10..13,33,81..85,122..124,154,158,182..185,
                     196..197)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187538"
     Site            order(85,87,124..126,129,154,182..184,200,218,286)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187538"
     Site            order(124,154,158)
                     /site_type="active"
                     /db_xref="CDD:187538"
ORIGIN      
        1 msrvlvtgat gfiaghaiee llrnghevrg tvrslrdpar vahlhrvada vggrldlvea
       61 dlarddgwde avagqeyvlh maspfpaapp rdeselvgpa vdgtlrvlga saragvrrvv
      121 mtsslaavsa arsragdrrc teedwsdpdr iapyaksktl aeraawsfaa dhpglelavi
      181 npglvlgpvq haasgtsvsl vrrllgreip avpelgfapv dvrdvarahr lameapdaag
      241 qryicagdnm wfgdiarild eefepqgyrv prrrmpywll waigrfdrev rlgldfvgsa
      301 elvsaekahr elgwsmrpvr etlvdtgrsl aelglvrprg avraa
//
LOCUS       WP_285103273             325 aa            linear   BCT 25-DEC-2024
DEFINITION  saccharopine dehydrogenase family protein [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285103273
VERSION     WP_285103273.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..325
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33898
     Region          1..317
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 msgrlliyga tgytgrlvae ravqtgldvt vagrdtgkvr elagtlgves rvfdvddada
       61 vrkalqdvdc vlnvagpfrh tarqlmdaai eagvhyldtt aefdifalae skgsealrag
      121 vmimsgtgwd vvpsdslalh tarrvpdaek ltialrvtgg fsrgslassa gigdlgtlvr
      181 rsgeltrlde vatrsfdfgn gpedcvpvpm gdlitglrst gignievflg tdagfpdvdp
      241 adagptaqer sqgrylaiae vtgrdgqvar slidtptgyt ftqlssveia rrvldgqfsa
      301 gfqspasayg pelatgiadt tivdl
//
LOCUS       WP_285103302             367 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285103302
VERSION     WP_285103302.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..367
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39610
     Region          7..359
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtttvsnqta drlqlaieki vdpgiiglsv rvnneqgewv gtagaggnvk ppadghirig
       61 sntktftatl vlqlvaedri glddpvsdhl pefgidqrit vrmllqqtsg lfnftgevye
      121 dgsivfgipi pygpngkewl dnrfktyrpq elvelalskp arfepgagws ysntnyvlar
      181 llvekvtgrt vteemqrlil tplgmshtvv pddaeiaeph ahayyryded geprtvditr
      241 qnpswvsagg dmisttedlh tfiaaltggk llpdelreem ftpratgipn mdyglgvfvl
      301 ttddgatvis hngaavghaa lmyatpdgsk tltaalncvd danltvaaaf qgaqqrllne
      361 vfgsrpa
//
LOCUS       WP_285103513             886 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Promicromonospora sp. MEB111].
ACCESSION   WP_285103513
VERSION     WP_285103513.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..886
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..886
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=93713
     Region          <2..885
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 marlsargar ealrgrtrhc ealdevlttv qgglgavlvl rgeagvgkta lldhlvgraa
       61 rcrvtdvagm esemelafag lhhlclpfld rldhlpvpqr dalttafgls agpppdrflv
      121 alaalsllad vgadlplvcv vddapwldev slqtlafvar rlgadpvamv favrepdlph
      181 elrglpeitv dglaeadara lldsafpsrl dtqvrdriva etggnplall elpralttae
      241 laggferpdt rplagqleng flriirslpa ttrqllvlaa aepvgdpsvl graadllgvs
      301 ldaaapaeaa glieigasvr frhplvrsav yraadararr ethqalgaat aqdtdpdrra
      361 whlaqaadgf ddavadeler aahrargrgg vtaaaafler ateltrpggg gvrralaaaq
      421 eklragapda arslletaaa ghpddlqraq iarmrahlaf vsqgagaslp llldagrkle
      481 rldppaarea yleavaaamf tgrlgdpndl qaaaaaaraa ppgplphrpt dllltgvatr
      541 itaghaagql plvealesfr vesgaagese mswmwlacpv apepiapdlw ddeawyllat
      601 ravrlartag alsilpfamg yqagvsvhtg elaaaaalld eaasiaaata aapplytsll
      661 llahqgdelt arraissavh qattrgegra lglaeyaaav lhnglghyda alesarsace
      721 yedlgfygss laelvesavr cgarsdaeta lrqldertrs sdtgwaqgvl arsqallseg
      781 readrlyrks iehlsrsraa vqlarahlty gewlrrenrr tqardqlrga ydrftrmggp
      841 glrrpgpaga pgdrregtee tragrqrahg pgeqdrsprr rrshqp
//
LOCUS       WP_285103446             137 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator
            [Promicromonospora sp. MEB111].
ACCESSION   WP_285103446
VERSION     WP_285103446.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..137
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15222
     Region          19..125
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mpnatpatrs gtstwcpqpd ddpatacpis pvvdlvfsrw ttpilwvlqa hgtqrfvele
       61 rrigvtpkvl tqrlrqlerd glvqrriyae vpprveyeit elgsslqavf aalgewgdah
      121 madversrad ytgplpr
//
LOCUS       WP_285103447             497 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285103447
VERSION     WP_285103447.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..497
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=55805
     Region          111..476
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mrlyeillvl sslslllcvc lprlipqrfv vmisgastvv lamhlfmegy rwqlyavyvi
       61 vvlllllqla kylfkikrin iwspvkwvvc glliiligls tvvsaylpvf qlprpdgpya
      121 vgtqtfhftd snreeifter kddkrelivq fwypaaeveq qkteyllass knmskqvara
      181 yaeqmglpgf vleywkyvrt nsyenakvqp tntpypvili shgmgtgrml htsqaehlas
      241 qgyivvaanh tysstatelk dgtiagsktn ftvdqfyapn nlvgqvwtkd vefiirqlgq
      301 lnggqikstl ngkldlnkig vmghsfggat afnafynnpn ikaginmdgs lynvdnktkf
      361 tkpfmfmesg eyltkkheme tkkltdaela diqltrpqye nmvrsvkkey givdkvaqhg
      421 gtmvvvdgag hynftdlqly ssfttfmgmt gdikgergad ivnkyvldff nkqlkgvgge
      481 likgpnpqfp evefpld
//
LOCUS       WP_285103558             320 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285103558
VERSION     WP_285103558.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 320)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..320
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35752
     Region          14..319
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mksaalegpg gngkgrsklg slfiemwkhr mvytlllpgl iwlvlfaylp mgglslafke
       61 ykanlgiwgs pwvglenfky vfrdpaflds lwrtlyiniv klviqfpfpi llalmlnelr
      121 mrrakkwfqt vltfphflsw iivsgvvinv laydgllnst ltmlglptin flgsesmfvp
      181 miiftdiwks tgwgaiiyla aisgidqdqy esaeidgasr mqqmfritlp nilptvtimf
      241 ilsvgglmss gfdqifnlan aatknvsevl dvyiyritfq satdfsfsta vslfrslvnm
      301 alllladrva kmmggdglfr
//
LOCUS       WP_285103613             228 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Promicromonospora sp. MEB111].
ACCESSION   WP_285103613
VERSION     WP_285103613.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..228
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=24252
     Region          35..207
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 msssasarkq lvalaeqgfe gpwryargdf tggarpasvl vlfgvlddla tdrddhdlav
       61 padldvllla raatlrshag qvafpggrad dgedavaaal reaveetgld asgvevlgaf
      121 gelpmpvsnh vvtpvlgwwa rptpvrvvdv aesahvfrap vadlldpanr fttvlrrgnq
      181 twrgpgfhvh dgdlthlvwg ftagildamf dqlgwtegwd rgrelgis
//
LOCUS       WP_285103621             691 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Promicromonospora sp. MEB111].
ACCESSION   WP_285103621
VERSION     WP_285103621.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 691)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 691)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 691)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..691
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72738
     Region          1..690
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mqprqteqsa eqqyvdalya rldretervr adlddavras stdpaeaytr evrvamlgrr
       61 artlgaaehh lcfgridgad grtlhigrtg lsdgddqllv dwraeaarpf yaataahpmg
      121 lrrrrhlgld grkvarvsde ildgtqpgph dvvgdgplle aisarrtgrm rdvvatlqae
      181 qdaiirsahr gvtvveggpg tgktvvalhr aayvlagfde artdgvlvlg pgtrfldyia
      241 evlpslgend vamstadrlv aealgltgvp aaghelrraa gdvrradela eivrdyqaps
      301 gtltvlvdgd pvtldehala earetaggtg lphnqaralf kdlvvefvad evqararvfl
      361 akldedievl tggvnvdkaa agdlarlgfa pdeggafgha aavaeldpga lqaeladdva
      421 leraveaawp hlvaqdvvld lldahpelth aglalddaaa dgdtaawtsa hlplldeaeh
      481 llngppariy ghvvvdeaqe ltamqwrsvl rrcpgrsmtv vgdlaqagpa tgaaswadal
      541 gadlarradv rtltvcyrtt aevlevaapl lariapdqap travrhgdvp rrvaavpgel
      601 vaavvreaga lasaapddlv avvaadarap evaaaldgtr vrvvpvsqvr glefdavvva
      661 dpdgitaarp ggerdlyvav trptrrlvvv g
//
LOCUS       WP_285103698             474 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285103698
VERSION     WP_285103698.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..474
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=54005
     Region          121..469
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mkrrgitfki fivttillvv salilyltly fllppyyyht kkakleagvh tlvsqieask
       61 wdkakdilke fehqynasvm vqseknqiif pnvvflkdtd nakitgstlp pvvrddtfnk
      121 mmpvsfvgdr eryrlmvmas lqpvdeaatv iltflpymvi villlsfvga yvysrliarp
      181 llglnvmakk mamldfstdf afksndeige lasslnklsr nlqrsmeelh lansqltddi
      241 kkkeeqeiqr refvamishe lktpitavsg qleamihnig pyrnrdkyll qshqitqeme
      301 klvheildis slesqefrpq irtlnatlll tniienyqyf cdtrkiklvs diaenvtlqa
      361 derllskavs nvlsnavkyt pkgevvsvhl fktldgiqld vmnsgthiea nelphlfkpf
      421 yrleksrsrt tggsglglyi vqkvleahha qykltneang vkfsmsfprt wndt
//
LOCUS       WP_285103732             287 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Promicromonospora].
ACCESSION   WP_285103732
VERSION     WP_285103732.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..287
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=30116
     Region          <120..262
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mahvpgsgvp evlapyvsav vpydldlgap gvhrgmpgtg vtfelplgdp ldvswagsdg
       61 trrqawscvs glhtrpaaih hggrqrglsv sltlrgarvl lgvppgelag eltslpevap
      121 hlahlpella aasdggspdg atvvralveh larageprpr advgralagi arggqvreva
      181 aeqgwsrrrl qdlvraecgl tprdlrrvar larsrralvv aarsgragla dvaawagyad
      241 hahmtrewva lggctpstwl reefpfvqdv adppraswet peqggsr
//
LOCUS       WP_285103745             217 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: potassium channel family protein [unclassified
            Promicromonospora].
ACCESSION   WP_285103745
VERSION     WP_285103745.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 217)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..217
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=23708
     Region          <1..192
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mgcgrvgssl aqeiegrghs vavidqnpda frrlpadfsg kkvtgvgfdr dtlvqagied
       61 tyafaavsdg dnsnilsarv vretygvdnv variydphra eiyqrlgipt vatvrwtadq
      121 vlrrmlplgf tdeyrdpsgt vrlaqidyhr rwvgrpvlnv eaatgarvaf vtryssailp
      181 tpdivlqend vlhllmaadr saeierilta aptaeed
//
LOCUS       WP_285103767             295 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Promicromonospora].
ACCESSION   WP_285103767
VERSION     WP_285103767.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..295
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32144
     Region          57..294
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrirdgfpgq rlrvlpttvv ratskagpts rllvtdagyf phatnhgrvr rqgavgtivi
       61 vssagrgwcr tpgglhriga aqalvipagv pheywadddd pwtiwwmhvr gddaaeferh
      121 laghagpddv avvevhdlvr vvadlervvd aletdetyps llrcagaaws vlaqigadaa
      181 agspvrgepv raaqeylrth ldavvevaal arrfglstsh fsarfraatg ggvveyvkrl
      241 rmaracelli ttelpvadia rsvgypdpfy fsrqfrsvhs csptdfrrgi hdrer
//
LOCUS       WP_285103821             402 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [unclassified Promicromonospora].
ACCESSION   WP_285103821
VERSION     WP_285103821.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..402
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42836
     Region          10..402
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 msvsrdpavg alaglrvvda stlfagpmaa mhlgdlgasv ikvehpvkad psrthgaakd
       61 gvnlwwktlg rnkrtvtanl gsdggrevfl alaeradvvi enfrpgtler wglgyeelsa
      121 rnprlvlarv sgfgqtgpyr trpgfgtlae amsgfaamtg eadgpptlpp fgladgvasl
      181 atafaimtal sardrtgrgq vvdtaivepi lamlgpqitr wdqlgtvqar tgnrssnnap
      241 rntyrtsdgh wvavstsaqs iaervmrlvg rpelvdepwf argvdrarha deldaavggw
      301 iaertrdevv kafeeaqaav apvydardiv adpqfqalgt iheiedpelg pmlmqgplfr
      361 lsendgviqf tgrphgadtd evlgelgfsa ervaelreeg av
//
LOCUS       WP_285103823             273 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Promicromonospora
            sp. MEB111].
ACCESSION   WP_285103823
VERSION     WP_285103823.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..273
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28378
     Region          5..271
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mtpltllyvp gdrpdrvaka lasdadvvlv dledavapsh kaeardnaar llaglpdglv
       61 qvrinhgssr whaddvamla alplavgarv pkvesaaevr dlaaalpgra lhllvesalg
      121 verafelata spqvrsiglg eadlrsdlrv dgeegllwar srvvvaaraa glvppvmsaf
      181 tnvrdldgla ascragralg fcgrtaihpg qlhtiraafl psaeevaaar evlarvgaaa
      241 tegvgavalt dgtfldvamv erarwvvelg ekr
//
LOCUS       WP_285103837             482 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285103837
VERSION     WP_285103837.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..482
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55169
     Region          94..482
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtkwlnmlkm krityklfvt tslillsfav liyvslyffl ptfyqqyktt qlqtgieeii
       61 tkskeldlqy gvllldafsk knnaivylqn kegaiiyspf fssvrkgysl paevrverak
      121 pilntnsfdv avpiqfidan lvlvvsatfq pideasqvlv lflpylsiiv ivigigsayf
      181 ysrfitkpll yinqgaqkma nldfseqiev hstdelgels tslnelsvnl qqtmqelhna
      241 nrqlksdiek eravetkrre ffaiaahelk tpltvmkgyl egmiyhigpy rdrdqylqkn
      301 hqivegmeql vreilsmskl erdafklqle evnlsqlvdk itadleyfaa qreiqlmkhi
      361 asnimvhtdr lmlvkackni ihnaimyspq gekvciqltr dmqegsiqfq vintgvnike
      421 edmqqifepf yrveksrnrn tggsglglyl vkqifealgi sysinnieqg vefeaaipip
      481 eq
//
LOCUS       WP_285103856             900 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285103856
VERSION     WP_285103856.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 900)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 900)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 900)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 900)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11970831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..900
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..900
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=94895
     Region          <2..867
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          <843..900
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mrsetvlrgr rretdaldel lrevraghsr vlvlrgeagi gktalldhls tragsarvvr
       61 tvgvepesei aysalqqlca plldhldrlp apqrdtlata fglspgrppe allvglavlg
      121 lfaeaaaeqp lvclvddvqw vdrmsevilt fvarrlqaes valvlavrsp gdeqvlpglp
      181 elrvgglpda daaalldsal pgpvddhvra rilaetrgnp lallelprgl tpaelafgfg
      241 apsptpvtdq vedgfqrrva dlpadtrtll ltaavepvgd vpllwraldr lgvapdaaaa
      301 aeaaglvrig arvrfhhplv rsaswrsatp aelraahral advtdpgqdp drrawhraha
      361 algpddevag dlertadral arggrsaaaa fleraaeltq dpklraervl aaararfasg
      421 aldgipglls aaelgplepl qragaerlra qvafaldrgr gavgplleaa rrldqldpaa
      481 areaylwalg aavhagrlgd ddlrraaeaa ravpsgldvt glfltglavr ytagygpavp
      541 hlrgalaapa dddaallwls apvahelwda tawfrlteqa lasarsagar tvlptaltfr
      601 agalvaegrf aeasdllrea esfanlpphp saaltlaahq gveepamrlv datvreaear
      661 gegrwlglag yaeavlhngl grypaaleaa rravayddla ltgwslgelv eaaarageag
      721 aaaearerla ertaaagtpw algaqalada lagppaaaed ryreaidllg gtrltlltar
      781 arlvygewlr renrraaare hlraahevfa aagaegfagr asrelaatge tvrrrsagpa
      841 dgltaqeaqi arlavtgrtn peigaelfls prtvewhlrk vfgklgigsr relaaalrer
//
LOCUS       WP_285103994             126 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Paenibacillus
            sp. UMB4589-SE434].
ACCESSION   WP_285103994
VERSION     WP_285103994.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..126
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14655
     Region          6..111
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mmkqtestek qnsltpfdyt ltmiggkwkm kimyqlinqe virygelkrc ipyithkvls
       61 sqlkeleenn iinrreyrqt ppkveysltp rgrtlmpile amckwglhnl psnlsiepte
      121 nssygt
//
LOCUS       WP_285104066             337 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285104066
VERSION     WP_285104066.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 337)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..337
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=38913
     Region          11..330
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mklfikdnts yiilhiiqfi flystfrwld vnmvasnivy lflvsifmll iylifryvag
       61 rggykwlsni pdlkdakvfl qmdvtapllh tfkrglarqy qllqsekers iqekqeqidf
      121 mnrfvhllkt plsalhlivq dredsegaee mqmeiarmey qlnmiltlsr mssfrqdfyi
      181 qtvpigplvf evindlkshf ihqhifpsad vqgdatvlsd rkwlkfvltq lvtnsirysd
      241 ggnrqiriwv rrqgafitlt vndegvgisp qdlprvfdly ftgangrkyg estgiglylv
      301 rkicdelghk vsiqsslgvg tevkidfplp yhpdstr
//
LOCUS       WP_285104107             270 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein
            [Promicromonospora sp. MEB111].
ACCESSION   WP_285104107
VERSION     WP_285104107.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..270
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28661
     Region          9..>214
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 msndapqvva itgaagrigr aitpllrrpg relrlldral paerdardrw ftgditdptt
       61 lddavrgadl vvhlaahpwe rpwpeilavn idgtqkvlda ahrggvprvl mastihavgy
      121 atpdeagatd vlvprpdtfy gvskaageal gsvyadrfgm tvvsaricaf sddvregrsv
      181 aewlspadaa rlveavaald rpghhivwgv sdnapgwfpl gpghaigfhp qddgvrrate
      241 rdgvappipe rdgalagifa dddhplggew
//
LOCUS       WP_285104263             132 aa            linear   BCT 25-DEC-2024
DEFINITION  SRPBCC family protein [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285104263
VERSION     WP_285104263.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..132
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=14944
     Region          2..132
                     /region_name="SRPBCC_CalC_Aha1-like"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of Micromonospora echinospora CalC, human Aha1, and
                     related proteins; cd07814"
                     /db_xref="CDD:176856"
     Site            order(3,5,7,18..20,22..23,28,34,42,44,46,48,58,60..61,63,
                     66,72,74..75,84..85,87,89,100,102,104,106,112..119,
                     121..123,126)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 msltlsldfq yltsieklws altdpsklak wvmendfkpv vgyrfqfrte pnewwdgvie
       61 geviivdepn clsytwasag eqhtvvwtlq aledgkvnlh leqtgfsnaq glegakygws
      121 gwcaklekvl eq
//
LOCUS       WP_285104240             210 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285104240
VERSION     WP_285104240.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..210
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23847
     Region          109..>185
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtaagitvep mqakynlqvg rlfvygfrgk fqhltnlndd dlaqffasll elfpsamttr
       61 rviavyegev igtlsvkwnv gsiikqeeka saswrnfsrf gkwnvvklfi glwllghepk
      121 vgecyisdva vhpghrskgi gsmllewarq haqaepslkl lslhvsgknp rarqlyeqms
      181 frrhshkisv mshvllkegk wyymvqtltk
//
LOCUS       WP_285104297            2691 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285104297
VERSION     WP_285104297.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2691
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..2691
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=283255
     Region          <8..1204
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          1011..2669
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mtlitrytti dkaiiaatgn slvtcgsstn vdvntadlmt ldgngtrgwa saastasisv
       61 qanstilyae liwystvfst asgaldvrsl adqaitlttp sgnysitpiy tdsitnvsgs
      121 idrfrsadvt sivtqslsga ytvskvpisi pptglsntka gwtlvviyrn dafapelisf
      181 ssgianvndn nllqtsitgf tvgqspqsgg iyvaaangss ltsnsqlkvg psfarltnig
      241 ntvgvphtnp atapnnpwnn ifagqinvsn plssnvglin iegtngtnnh dpfvptqvin
      301 arnkwdlswl disstlednq slialqssaa gttdgiqiva lgsavkvisp nisavltgys
      361 sesnllypye vgqeiiyeii vqnsgaanad nvifnaavda ncsfvpnsvi vngvvktgas
      421 iasgvnlgti paagivhlqy glhidrlpvn qqisqtanys yqfssgansp iytnnattnt
      481 vahavvaaql navksastnt asigdlvtyn inltnsgtel lsnlffqdpv spyctyiags
      541 vtingtaqss ydptvgfqla nlqpgqttkv qftvkiqslp psdyvdnaay vtysyqynds
      601 tapttltits nhtairvqyv eivakrvinn eypnigdtvt ytlsltnign ipdvnvnvve
      661 ppvagatfvs gsltlngvsr pelnpftgft iasiqpqqty iityqvlinq vnpgqtveni
      721 aqvpfkyqit pggpiisdeq dsnkvvtrtn fvtltiqesv dksyavlgdt lyytvnvsnt
      781 gnidalntif laaiqagtqf vpnsvaingi vvpgadpnig fslgsidpsn tvmvtfqaiv
      841 tnipvpnivy nqskliydfy pdpsgnhvts tafsntvqti lnnvqfshik svdkayaqlg
      901 etlvyrttiq ntgtvvltnv fffdhlneal tfqagtvqin ginypaynpl tgfslsnisp
      961 adtvtidfqa tvssippvgi iynsssftys yqtapdaptf tatsssnqvr ttitngslsi
     1021 tkstskiyat vgdsysysll lsntgnvtlt nivlqdqlan gilfipgsvt ingtskpdyn
     1081 pntgfplgtl nagqvasisf rvtvdhvptp ntvlnyataa fsytvdpsqp pitgtstsnt
     1141 vttiinqags slvktvnkaf atigdtltyt itanntgtvp lanvgfkdii psgaalvagt
     1201 vsidginypd ynpnvgfsla nipaggrtvv ifqatvvsvp fpprldntat inyqyqlspa
     1261 gavlsgsqts nvattfvslv nivntktvdh tyatigdtlt ytsviqnkgn inisdvffvd
     1321 sipvstafva gsvtidgaas plldpnigfs lgtiapdenv avsfkvtvad lplsgyvqna
     1381 snvtyqyqid ptapplvgsq tsnivttyir vgslivqkss nrnytrvgdv ityslvlant
     1441 gstllqqlff qdtiqtesaf vtgtviidgv nqpgldpnvg fmlsdlgvgs nieiqfqvlv
     1501 naipsteqll ntatvhyayy idpngvihta taasnqtivq vddtplsvnk fvdksvakig
     1561 dqllftvsls ngstnltaqq iqfvdvldsn lsfdqgsvti nsvqqpalnp ntgftltdip
     1621 gettttvtfs atvisrpsnn ivsnlasihy qyildpqlpp vvvdtitntt qtliavgelt
     1681 vvksatasya tigdvftysi lvnnsgsvla tsvslqdivp salafvpgsv tidgsaqpal
     1741 dpnvgislsn lapghtafis fevkvisvpl sgevyntasv tfsyqltpsd pvetktaisn
     1801 tvviniwlgq ltvtkavdks yatigdklhy tvtvrntgnt ictsvqfkdv vqanadfvpg
     1861 svqingitqp sydpnvgfsl iditpdstvt itfdvnvtsl pdnyllanta tvrylyssnp
     1921 skppvnaatv sntvtttinv glvavtksvs qsyatigdvl tysvqisntg ntnatavnfr
     1981 dvipngllfv pdsvtingvl kpgydpyqsf slgtltpgss sivqfqatvv svpvpslvsn
     2041 iaqvtftyri qpegpditde vnsntastqi nnavlafskq asqsyaavgd tytysfvlnn
     2101 tgnvdlfnvs fldnlqsdla fvtgsvvvng qsqptfdptv gfiigtiptl sqlnlsfnvt
     2161 vrslpanhiv snfatanyty kidpngnsyt kttasnavft tiilgsltat kavdlayatl
     2221 ssilnytitv kntgstivsn lfftdtlsvg anvvsgsvvi dgvpqptfnp isgfpippln
     2281 agttttikfq aqvssipaag titnyavvtg vyrvnpsgpd iqvsattntv ttqvnvgrle
     2341 svksvdksya nvgdsltfts vvtntgnvta snvwfydtlq leagfisgtv ringtvqptl
     2401 dptlgftlgs ltpnqsvsid ftvkinslpt ppqitnksqv efsyyvdpng tiitstifsn
     2461 tvttavvqgq lsavksvnkt iatlqdvlty tivltnagnt palqvqfkdt psagaafksg
     2521 svlingtarp dfdptagfil gdigvgntlt vqfqaivtsv pasnivtnqa alnfsilvdp
     2581 kqppisqtay snttttsivl ghlsvvksvd kqfatigdtl tytivitnng nidvtnvifi
     2641 dptpqhavfi vgsvvvngin qptynpaagf plhtmtpgqi itvvyqvqii s
//
LOCUS       WP_285104340             250 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285104340
VERSION     WP_285104340.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..250
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28212
     Region          31..143
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mmiehnnlee yldpinydle fggeinkyhf yielaksnpg evlelacgtg lttiplsqsg
       61 initgvdisp tmleyarika kglpaifldg dartfksekr fsmiyltgna fqaflsdedq
      121 tcllktvyth lkpngifvfe trnplgtdls sqeestwgqf idkdghhvkv sgtqsyddtn
      181 himhwvtfrd wghkkstsri acrftdndtl ksmltsngfc iesqysdwdk tpfstfsssi
      241 itvcrkvshk
//
LOCUS       WP_285104376             610 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Promicromonospora sp. MEB111].
ACCESSION   WP_285104376
VERSION     WP_285104376.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..610
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64641
     Region          11..601
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mdeifspili elpptsnlnd vlaervgaga dkpmmevpag kgepwrvvsa gefdaqvvav
       61 akglvargie pgdrvgimcr tryewavldf aawaagavpv pvyetssaeq vewilsdaev
      121 kvvfaetpan aatvaevrda vplvtdvlvi ddgaldavaa egadvpddei arrrglsgld
      181 dlatiiytsg ttgrpkgael thrnfaslav naveavpevf akeggrtllf ipmahvfary
      241 ihvlavaggv vtghwgdtst lvdalgefkp tfilavprvf ekvyntaeqt aaaggkakif
      301 hwatatgiaw sraldtpsgp glglrlqhav asalvfsklr aklggraefa vsgggplger
      361 lghfyrglgl kvlegyglte staptsvnrp tatkigsvgl qlpgcgvkia edseillkgh
      421 hifrayhkne aataeafted gwfrtgdlgv ldddgfltit grkkeiivta ggknvapsml
      481 edrirahalv sqcvvvgdgk pfigalftld aeglpgwlkm hgkpvmsvde arkdpdvlaa
      541 ldgavqrank avskaesirk ytvlagdlti engyltpkqs vkravflkdf dadverlyad
      601 knkdslhlln
//
LOCUS       WP_285104393             377 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: PucR family transcriptional regulator [unclassified
            Promicromonospora].
ACCESSION   WP_285104393
VERSION     WP_285104393.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..377
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=40363
     Region          113..374
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mnlqrvreas gvltaaamrr ldedlswyre lpaedrsyvg lvaqaginaf tswftdpnrp
       61 phgvseifaa apteltrsis lqhtlqlvrv vvdvvethsd riaapggerd lreavlrysr
      121 evafsaaevy araaewrgaw darlealvvd alvrgdgdds lrsrisalgw sgrgnalvvv
      181 glateeldei rtaeirrvar raagdalvgi hgdrlvlvlg gegdlvaaat almsrfgtgp
      241 vvigtqvpsl tdaprsarsa lagltaapaw pqaprpvmad dllpervltg dytaratlia
      301 qaftplqdag gavletlsay lgtgrsleaa arhlyvhpnt vryrlrkvse itgwdpldar
      361 esfvlqvala lgqlgrg
//
LOCUS       WP_285104600             246 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285104600
VERSION     WP_285104600.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 246)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 246)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 246)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..246
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28191
     Region          1..235
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 myrvaicdde dkqrelvksi litlsiktni dfeiesfgsg eqlvsyyech etpfhilild
       61 iemggingiq tahkirglnn ldeqiiflts ypqymvesfd vmtfqylikp iapsileeki
      121 iklhqyfqal nkkymviksg yeevvlkyde lisieaaksl tiksklhftt tnqtyeskgt
      181 isdyavalkd cnflqihrsi iinllhvrkf asgvvlmsng lelpigrski kevkdvytkf
      241 mimkvd
//
LOCUS       WP_285104759             317 aa            linear   BCT 25-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Paenibacillus
            sp. UMB4589-SE434].
ACCESSION   WP_285104759
VERSION     WP_285104759.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..317
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=36421
     Region          33..227
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mvaysdqtag ikqvnaecqh gkylpvsgkk pivwfirvqp dryelqqgeq ankwksrlpl
       61 seycrvlsyr ihadrvrclv gylavrllta kmteikpvdq pwsrtpygkl swgfnkagqq
      121 qinldsaeee edtldpddvk hswhvnlshs gdwigvighi epvgidieer grisydiaer
      181 wfhpaeaeri qqaldqqaal gdwwtlkesy vkwdgrglsy glnqfailpq qqvhavplel
      241 qtrmdvepfl wreagcfkgd qleqdervkl qygsiaanys asicmssnsp spfvcmltde
      301 mliemweeym tqergrl
//
LOCUS       WP_285104819             997 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Promicromonospora sp. MEB111].
ACCESSION   WP_285104819
VERSION     WP_285104819.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 997)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 997)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..997
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..997
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=107347
     Region          29..995
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mndlspaery safrsqrrle aegrsvagpe ltlfrevigf elddfqvaac ealeqgrgvl
       61 vaaptgagkt vvgefavhla lasgrkafyt tpikalsnqk yadlvrrhgp envglltgds
      121 tingeapvvv mttevlrnml yagsatldgl ayvvmdevhy ladrfrgpvw eeviihlsdd
      181 vqlvslsatv snaeefgdwl emvrgdtavv vserrpvplw qhvlmsspep rgkprlldly
      241 aghvdptdpg tsppinpdlt aafrsgrggn rpgdhaggpg ggrgrgrgrg drgyrgngrr
      301 addrpggavg pgrrtpprfi vidalnadal lpaiyfvfsr agceaavdqc lkaglrlttp
      361 qeeatirsvv eertaaippe dldvlgywaw sqalargiaa hhagmlpvfk etvedlferg
      421 lvkvvfatet lalginmpar svvldklvkw dgsshvpvtp geftqltgra grrgidvegh
      481 avvvdhpald pvalaglask rlyplkssfr ptynmavnlv aqvgrdrare vletsfaqfq
      541 adrgvvglak qaqahaeald gyakamscdv gdfaeymdlr raikdrerel sraatgarra
      601 evvaslenlr rgdvvevpsg rrrgyvlvld pgepggfdgp rptvltqerq vkkltladap
      661 dgletvttvk ipkafnprkp darrdlvstm rnalgvladd vpsahsttsp srsaasraar
      721 ggrpvvsrrs daatdaelar lrkalkahpc hacperddha rwaerwnklk rehdqlvrrv
      781 egrtgsiart fdrtldvllt lgylqrtggd tsagtgagts gstggrirvt ddgrwlrrly
      841 aendlllaec lrrgvwdgld aaglaavvst vvyqgrrdda pdpyipggpt grlagvlddt
      901 qrvwsevddl eeahgidatg pldlglvgam yrwasgkgld svlrgsdlaa gdfvrwckqv
      961 vdvldqlgga apsdrlrata rkaqdavlrg vvayssl
//
LOCUS       WP_285104827             329 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Promicromonospora sp. MEB111].
ACCESSION   WP_285104827
VERSION     WP_285104827.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..329
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34811
     Region          21..310
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mpdlneatep lavadvaalg eqvlaevgta vvgmrdalqi alatilaggh vlfedvpglg
       61 ktlaarslaa algldfarlq ctpdllpadi tgssvfdpat rtfefrpgpv ftglfladei
      121 nrtapktqsa lleamaerqv siegtsrplp spfhvlatsn pveyegtypl peaqldrfmv
      181 rlavgypdag qeaevltrrl arrqeaahvr kvvepatvla mqagteavpv dpdvvrycvd
      241 laastrghta levgasprgs qnlvllarai avldgrdyvl pedvkrvavp vlahritltp
      301 tawasatrpe tvvadllrav ptpttvrsr
//
LOCUS       WP_285104983             870 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FtsK/SpoIIIE family DNA translocase [unclassified
            Promicromonospora].
ACCESSION   WP_285104983
VERSION     WP_285104983.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..870
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..870
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=92038
     Region          42..181
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          247..810
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 mahavggatr aagprtapeg sgtgsqnaeg qggqelepdh rrdgvgfall avavivaare
       61 wwgidgpfgd gvhavvagtl gvagvalpvl lmwlafrvmr hpertqqngr vaiglsflvv
      121 atcslvhisa glpspadgft pvqdaggvig flfatpvvtg ltqwfaiply vlagffgili
      181 vtatpvhrip arlrglydrl tgnhreaddt gedglaladg vsahdgtpep krrkrrtkqe
      241 iaaekerlag fvgdeafeka aeveqragka gkattqript gqsagkvtga paigpgvlgp
      301 dgepasakkd gprpprdaep mprgvqpmle gdtvyllpde dvlvqgpphk arsaandrvv
      361 esltgvfeqf gvdakvtgfs rgptvtryev evgaktkver itslsnniay avasadvril
      421 spipgksaig ieipnsdret vvlgdvlrsg aarrtehpmv mgvgkdvegg yvvanlakmp
      481 hilvagatga gkssfinsmi tsilmrstpe qvrlilvdpk rveltiyegi phlitpiits
      541 pkkaaealdw vvremdaryd dlatfgykhv ddfnvavrag kvkplpgser kiapypyllv
      601 vvdeladlmm vaprdveasi qritqlaraa gihlvlatqr psvdvvtgli kanvpsrlaf
      661 atssladsrv vldqpgaekl igqgdalflp mgaakpmrvq gawvtesevh qvvehvkgql
      721 kpiyredvaa paaakkqvde digddldlll qatelvvttq fgstsmlqrk lrvgfakagr
      781 lmdllesrei vgpsegskar dvlvaaddlp salalirgeq paqvfdqass ddaepddggs
      841 ygsadqyadg tdghmppvar dyhddaepvr
//
LOCUS       WP_285105018             641 aa            linear   BCT 25-DEC-2024
DEFINITION  peroxidase family protein [Promicromonospora sp. MEB111].
ACCESSION   WP_285105018
VERSION     WP_285105018.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Zamocky,M., Janecek,S. and Koller,F.
  TITLE     Common phylogeny of catalase-peroxidases and ascorbate peroxidases
  JOURNAL   Gene 256 (1-2), 169-182 (2000)
   PUBMED   11054546
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..641
                     /product="peroxidase family protein"
                     /EC_number="1.11.-.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=70077
     Region          91..615
                     /region_name="An_peroxidase_bacterial_1"
                     /note="Uncharacterized bacterial family of heme
                     peroxidases; cd09819"
                     /db_xref="CDD:188651"
     Site            order(288..289,379,382..384,386,389,414,467,484,491,495)
                     /site_type="other"
                     /note="putative heme binding site [chemical binding]"
                     /db_xref="CDD:188651"
     Site            order(350,353..354,358,378,382,384,558,562,566..567,
                     570..571,574)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:188651"
ORIGIN      
        1 mvqptqappq gdpnhsphea vdlaqtpagr tvrrighggv fvpadpdape dprdstatlm
       61 prteaavrrd lrehrfdatt sfdyllrdla refpdahlpv gdrvagtrda lmrlgagmie
      121 apapapapap gappapaapp rdstipsiyt ywgqfidhdi tlntngpddd sgprgdqalg
      181 divndpfrvf tpdvvrrslh ngrvplldld slygsgprfa gekdrgttrs eaayvpdsak
      241 lrlgrigtep fgpfslvapg ddpqrdlprs teagsermpl ipdsrndenl ivaqfhvami
      301 rfhnavvdwv aehepwsatt qrelfdraqq lvrfhyqwlv vndylrtltk pgvldsvlat
      361 gptlfrparr vsmplefava afrfghsmvr gaydfnvnft gngpggvarl dqlfqftgng
      421 glspnpanps pvlpsnwpve wprltdkgdp lafrmarkid pfladglghl lnegntaaep
      481 ikallkqlaq rnllrgymla iptgeavake lrarpltptq lrqnaspevv aaldaldgtp
      541 lwyyvlkeae vqgngnflge vgsrilaetf vyllrlddes flrrpgrdwt paygvrfedr
      601 rlittisdll afagvfpigq ddaglplfrr ngdgyaghdg a
//
LOCUS       WP_285105257             610 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Promicromonospora sp. MEB111].
ACCESSION   WP_285105257
VERSION     WP_285105257.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..610
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64855
     Region          11..600
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mtlatspawv evpagtsint iladrvarsg dealierrda pdgpwikvsa sqfedevlav
       61 arglvargik agdrvaimsr tryewtlldf aiwaagavav pvyetssaeq vqwilsdadv
      121 rlivvesaah aetvkqvrps lpgledilli degavldlrk agtnlsagiv aerrdavrrd
      181 dlatiiytsg stgrpkgvel thgnfahltl naaagipell saenartllf lplahvfarf
      241 vevatiagqa vlghapdikn lvadlgsfrp tyllavprvf ekvynsaeqk assglkakif
      301 awsarvaedf sraldvpegp grtlkvkhai adrlvfsklk atmggqlswa vsggaplger
      361 lghffrgacv tilegyglte staptavnlp gkivmgsvgp affgtgiria ddgevllsgp
      421 hifrgyrnqp eltaealvdg wfrtgdlgrl dehghlhitg rkkeiivtag gknvapavle
      481 drmrahpivs qvvvvgdqrp figalvtlda emlpgwcaan glpklsvada rvhpkvlael
      541 dkvvaqanea vskaesirki tvldldftea ngyltpsikv krakvladfa gtvdalygap
      601 vpnaqpaatr
//
LOCUS       WP_285105268             377 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Promicromonospora sp. MEB111].
ACCESSION   WP_285105268
VERSION     WP_285105268.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..377
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39883
     Region          7..377
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mvltvsviga gpaglsaaaa lkargadvtv leksehvgna wrhhydrlhl httrglsrlp
       61 glaipreygr wvarddvvry leayathhdl rvehgvevth ldrpvadaga drrwtitttd
      121 gtrtadavvv atgynhtphv pdwpgqdaft gevvhasryr nsapyagrhv lvagvgntga
      181 eiaqdlaeng aasvhlavrt pphivprnqg pwaaqytgvl vrhlpdrlvd avgvavrrag
      241 vpdlsdlglp ipdvgiatrv aqgsvplqdi givaavqagt vrvvraverf dggevvladg
      301 arltpdvvla atgyrralep vvghlgvlgd rgkplatngr paapglyftg ftnpisgmfl
      361 emaadarria rhatrgr
//
LOCUS       WP_285105361             742 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF4129 domain-containing transglutaminase family protein
            [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285105361
VERSION     WP_285105361.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..742
                     /product="DUF4129 domain-containing transglutaminase
                     family protein"
                     /calculated_mol_wt=84401
     Region          378..573
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
     Region          677..735
                     /region_name="DUF4129"
                     /note="Domain of unknown function (DUF4129); pfam13559"
                     /db_xref="CDD:433308"
ORIGIN      
        1 mkrdstftqr ifglfwedrl iwlclyvmly qwaialvpyw ydetiamtkl mlntvvfagl
       61 lfprsllvri piglgvvlws vyeelqqfql wvstdaglsi lesllqyhpy lwlvgliwlt
      121 yelfmsrvkt swhivmllvl qfivlgalds ftpeilwdqv awvmsaslvw lialhfrtmk
      181 hkfpaqsght kryavqmtls aivlvsaiic sglsmpglap ivtdpytawi snerfpvaga
      241 gngsgggigs gvssgysthd ydlgggfemd fksvmtvtad yrgywrgesk avyigngwad
      301 lesedlqtak pgtelqalnq lephvptrtv kqtftmqdsk typilfgvat isafdqvkgk
      361 hsgsmkwnsh dgeliykpga dkaypesyti lsevsvatpe emrkgtvtrn fptegikgal
      421 myqylklpne ypgrvkslae qitkgatndy drakfiesyl rtefkytnkp dirkkvsedf
      481 vesflfeiee gycdyfsstm avmlrsvgip trwvkgyapg trdlmidnrm peamlermsd
      541 pneggtfrvt nadahswvev ylgeygwvaf eptpgftmpr lqapsaaeep elgtdlnqee
      601 pdqqtaksee vslpawigtl aqavlmlaaa fafvmmllrw rsigytmrwi rfigrrltpr
      661 ehiiadtelw lsychlhgmr kekhetvrea verwsherta kkqsaeqivc lfeqakyghe
      721 elkvedwqql kavirefkrt gs
//
LOCUS       WP_285105480             504 aa            linear   BCT 25-DEC-2024
DEFINITION  FGGY-family carbohydrate kinase [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285105480
VERSION     WP_285105480.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..504
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=54217
     Region          12..454
                     /region_name="ASKHA_NBD_FGGY_FK"
                     /note="nucleotide-binding domain (NBD) of L-fuculokinase
                     (FK) and similar proteins; cd07773"
                     /db_xref="CDD:466793"
ORIGIN      
        1 mkrrswqvvh mmgidlgtsn rkvglfdeeg rvlaissrpt tvietgqgys vydpeqlwnd
       61 vaamikevla qtgvsqvaai giasmaesgl lvnrstgkvq spclpwfetc stpqaerirq
      121 sdaplalfqr sglhlsfkhg lpklmwlhdq dasmftdavw ltmsgfiayr lsgvmacdpt
      181 latrtfaydi rhecwdmewl kefglpeglf pqvlpsgspl gtvttelanv lglgegttva
      241 igghdhvcas lavgavhpgd vfasmgtaet lvglmkprhl gqaefdtgls ygfhvvpgyq
      301 fwmggnaasg galewirkql addaltydqm kalmadvpdg pgqalffpyl sgsgapypns
      361 ktraafigls yasgkaelvr avcegtayql emirrsaeqv sgetireira vgggtrirtw
      421 lqmkadvgna tlivppvdea tllgaayaal igtghigsat elqglieqrg varidpdaar
      481 hmlyaaryeq vyapmaaalr qmel
//
LOCUS       WP_285105687             336 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285105687
VERSION     WP_285105687.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..336
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35790
     Region          28..335
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mkkrfalarp igvililsvl vilvavismn vgrlnlslle vlqviigkgt ekqnlivfel
       61 rlprialavl vgmgmaisgc vmqsllrndl aspgtlgiss gsglfvmlyi tvfaangfls
      121 pmflpllafv ggitaamlif vlayrkgkel sptgliltgv algsgygalt lmitlgleqk
      181 qydfalrwqi gnlwgddwky imvllpwvii igfyvlfksn tlntlnlgnq tatglgvavk
      241 refigltiaa valssgsval ggnfffvgli aphlarrivg pnhkfmipta alvgaliila
      301 adtftrtvsm gadiptgvii tifvtpyfly llsksn
//
LOCUS       WP_285105819             458 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285105819
VERSION     WP_285105819.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19687404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..458
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=47840
     Region          27..447
                     /region_name="PRK15001"
                     /note="23S rRNA (guanine(1835)-N(2))-methyltransferase
                     RlmG"
                     /db_xref="CDD:184963"
     Region          245..447
                     /region_name="RsmC"
                     /note="16S rRNA G1207 methylase RsmC [Translation,
                     ribosomal structure and biogenesis]; COG2813"
                     /db_xref="CDD:442062"
ORIGIN      
        1 mnpeveavla rlqpypedgs radgpvaada tdrllldeaa alvqehpdgv vvlgdrfgal
       61 tlgalasgah qvrtqmdavt aeaalsansr rvskvlwdgr artaasapap hepaglgftq
      121 ydrleprlfe garlvllrlp tslaelteia ehvaryadpa vtllaggrvk hmthamndvl
      181 gasfaqvgas larqksrlli argpradvgp ltypvtarlt dreildaivp pgtapgsadp
      241 depagltvva hgaafagatl dhgtrfllaq ahrwphlsdl qvtpatstsd tsgpsdtpip
      301 gmdahpvavd lgcgtgilaa vlglryptah vlasdrsraa cdsaaatlaa ngvrgrvvrd
      361 dagallpipd gsadlvllnp pfhdraalst daahrmfata grvlrdggel wtvfntglhy
      421 rraleravgp tehvaqdrrf svtrsvrkll tdmsvtgg
//
LOCUS       WP_285105833             199 aa            linear   BCT 25-DEC-2024
DEFINITION  YdeI/OmpD-associated family protein [Promicromonospora sp. MEB111].
ACCESSION   WP_285105833
VERSION     WP_285105833.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Pilonieta,M.C., Erickson,K.D., Ernst,R.K. and Detweiler,C.S.
  TITLE     A protein important for antimicrobial peptide resistance,
            YdeI/OmdA, is in the periplasm and interacts with OmpD/NmpC
  JOURNAL   J Bacteriol 191 (23), 7243-7252 (2009)
   PUBMED   19767429
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..199
                     /product="YdeI/OmpD-associated family protein"
                     /calculated_mol_wt=22429
     Region          1..192
                     /region_name="YdeI"
                     /note="Uncharacterized conserved protein YdeI,
                     YjbR/CyaY-like superfamily, DUF1801 family [Function
                     unknown]; COG4430"
                     /db_xref="CDD:443542"
ORIGIN      
        1 madtdtevlf tdvaawrawl deneetsdgv wlilarkgkd aptnltydla ldealcsgwi
       61 daqgrsrddt tslqrfcprr srsrwsarnv rivdrltteg rmrprgrqev dkakadgrwd
      121 vayegsksie vppdlaeala aspratamfg iltaqnrfai llritgvkra etrerniakf
      181 vgmlergetv ypqkrkled
//
LOCUS       WP_285105835             182 aa            linear   BCT 25-DEC-2024
DEFINITION  peroxiredoxin family protein [Promicromonospora sp. MEB111].
ACCESSION   WP_285105835
VERSION     WP_285105835.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Schroder,E. and Ponting,C.P.
  TITLE     Evidence that peroxiredoxins are novel members of the thioredoxin
            fold superfamily
  JOURNAL   Protein Sci 7 (11), 2465-2468 (1998)
   PUBMED   9828014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003123
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..182
                     /product="peroxiredoxin family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18723
     Region          52..171
                     /region_name="Bcp"
                     /note="Peroxiredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG1225"
                     /db_xref="CDD:440838"
ORIGIN      
        1 mrrtlaalla aglaigalag cagtprgqlp gpvpsgvefr aapdgappap pltleltdgt
       61 tldlagqwae rpvvlvffes wctrcagqqg pindvvdeye drvlflgvan lsdpddvaay
      121 veenditypv avdptgdawl myavaeaplv alvgkdgsll rgwpegvtgr elgatiadla
      181 vg
//
LOCUS       WP_285105953             290 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Paenibacillus
            sp. UMB4589-SE434].
ACCESSION   WP_285105953
VERSION     WP_285105953.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..290
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=31378
     Region          2..283
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkifvagstg vigrllihrl vhaghevvgm thrldrkahi qamgaksivv dvferdavla
       61 avgdvrpdvi ihqltslsnw siednariri egtrnlvdaa qaagvtrmia qsiswayepg
      121 dhpageqvpl dihapfprkt tidgisaler ivaeipehvi lrygalygph twydhkglia
      181 ekviqgqlpa tdgitsflhv edaanaalla ldwppgpvhv vddepaagte wlpvyatalq
      241 apvpahqsgr qrgergasna rarneygwtp lyptwrtgfa qslnpapgqh
//
LOCUS       WP_285106065             327 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285106065
VERSION     WP_285106065.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..327
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37520
     Region          1..321
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mnrtdrlmai vlelrqrrvy raedlaalye vgvrtiyrdm qalsemgvpi asipgigysl
       61 megyflppvl lhpeeallll tgvehiggrl deswtayaqg arakmkelln eaglhrmrdi
      121 egqirflped ygvtplhrnk tnpllhkmqq avkqqrvlsi ryeapvgisg svetertihp
      181 ygivhtgavw vviaycslrl sirhfrldri qellemeehf erpaqfslse ymptddrtdr
      241 gyhvtvsfpi slsqrvkesr yfyiesveer ehelivklta rkeqdvlswl lswgaqatvm
      301 epaslaqaik aeaermvrly ssdatyy
//
LOCUS       WP_285106125             358 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285106125
VERSION     WP_285106125.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 358)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..358
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41301
     Region          260..341
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mipiapsiya hispvfewfa amyrvvnhem ltpsvpnaaa faskdidrfv kearqaigae
       61 glkdlqlffn pessmgiyll kdfyikgllh diqaaihele hlpakdllna flrcvkwedt
      121 dvidehsewd alsllshikq stlseeeqwk vfyfahdeeg tkrkflaivt qfyetvyaaf
      181 smpfetiheq tvqqlrhvfe eerahnlnal lgldldekmn meletifips yffhtssmll
      241 lndkqmlcil ganrqaylqa krnqsqqisd ifklladekr ikiiqllnqa prygyelake
      301 ieltnstvsh hvnalsqagl vkatrhenrv myqvqpeqie rlleelssll lphsrfgh
//
LOCUS       WP_285106423             531 aa            linear   BCT 25-DEC-2024
DEFINITION  RecQ family ATP-dependent DNA helicase [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285106423
VERSION     WP_285106423.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Larsen,N.B. and Hickson,I.D.
  TITLE     RecQ Helicases: Conserved Guardians of Genomic Integrity
  JOURNAL   Adv Exp Med Biol 767, 161-184 (2013)
   PUBMED   23161011
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Rezazadeh,S.
  TITLE     RecQ helicases; at the crossroad of genome replication, repair, and
            recombination
  JOURNAL   Mol Biol Rep 39 (4), 4527-4543 (2012)
   PUBMED   21947842
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Bernstein,K.A., Gangloff,S. and Rothstein,R.
  TITLE     The RecQ DNA helicases in DNA repair
  JOURNAL   Annu Rev Genet 44, 393-417 (2010)
   PUBMED   21047263
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Chu,W.K. and Hickson,I.D.
  TITLE     RecQ helicases: multifunctional genome caretakers
  JOURNAL   Nat Rev Cancer 9 (9), 644-654 (2009)
   PUBMED   19657341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..531
                     /product="RecQ family ATP-dependent DNA helicase"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0043138 - 3'-5' DNA helicase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=57455
     Region          1..496
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
ORIGIN      
        1 mqdiaalare rlgydalrpg qaeavgavld gqdtlavlat gtgktaiyql aglalggltv
       61 vvsplvalqr dqvrvlstgg leatelnsgd ragqhqarem lverrpgfvl mspeqlthad
      121 vlelladsrp hlvavdeahl vsewgqdfrp dylrlpaaiq amgrppllal tataappvrd
      181 eivhrlqmrs pavvvggfdr pnlnlavhtf adeetknrrl lshvrssrgp gvvyvathrh
      241 aeelaaelrl aevsaqayha glsakerrev qdgfladrhr vvvatvafgm gidkpgirwv
      301 shaeapgsvd ayyqeigrag rdgepahiel fyrhanlgin rffasggvrd edlhavasai
      361 dehhpadvae laavsllspa tveralgrlt daravtathr fqltartdvd kavaaasave
      421 hdrrevarsr vemvaayaeh ggcrreflls yfgeryegpc gncdndlsgr tavpvadqpf
      481 pvgsrvkhrt fgpgvveryd gttvtvlfdr vgykelrtal mthnhllepe g
//
LOCUS       WP_285106433             950 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Promicromonospora sp. MEB111].
ACCESSION   WP_285106433
VERSION     WP_285106433.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..950
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..950
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=102237
     Region          <21..940
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mladggrarr ighdalsgnw agryrvpirg rrheadgieh gfeaavsgkr avtvlsgdpg
       61 igktrllqha leladgrgwp tvvvapdids amtplgalie avsrtdpplv atsdlasvmq
      121 gvapqywltr miaeklevaa spsgvlvvvd dlqwldagsl galtalirdl qgvpicwlla
      181 trtgvystah qrfmsqiadv gsivelqpld paavdamard algrvpgpgv enamkraagf
      241 pllvlellqg lqeegllrsg rgmvdvddet iparfgtsir drlrhlshda lrvaqvgsly
      301 grdfplsgvl eilgrtatea apavqelldl gfivdrgssf afrhdtvqsa ardslsptlr
      361 ramarevlhs rlragegvat lattivsvve agdddsidll faaarqlssi dmrgaadlvi
      421 lgarltsgnr shaeqvanll plvlagglve dameiirtlr pllsadarar vglalarqlt
      481 essfeqaive tsaaleipgl sdetkvqlla vralnfanka dcggtrtsle qgravadddr
      541 dglalatida tesvlvfyen hfdraeklqr halariartg tlaglwlpeg lwlpfmrnst
      601 ghceealrlt edglaetrta knviaeaywm mlrtrilhdl grleeartqa etvvdlaarl
      661 glgdftnata gvvlhrislr tgdvelrdti rpliqqladg agltktgrws laleamdrgr
      721 phdayqhagl alaslreasp smttpadfad dimlalichr vderpsldlv aavaqeradl
      781 npesslvrav atatrgirdr ssadlraaad llgtvrrplv taqvleaagm fsldreaatn
      841 alteamrlfd dhgatrdasr ilhslrsrgv hrrlrstsrd asglssrehq vaqriyaglt
      901 tqqiaddlll sphtvvtyir hiyakwgvkt rgrralspal gsfrprprsg
//
LOCUS       WP_285106470             306 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285106470
VERSION     WP_285106470.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..306
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33595
     Region          1..299
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mkksamywls vifvligass ygfvssivkl afaegystaq vtisqisvga avlwimvllr
       61 phtwrnpfah ggwkllfvgi fglslttify nsalqqldas laiillfqft witlvmecvt
      121 hrtwpnryqw lsifivllgt vlavgitsdn lerftfagvv lglasaitys lflyltgkiq
      181 thhdpvmrsa mmmtgtlpvi ygiyvpfiag gmelppdvgh lllwglllgs lshiiptvtf
      241 nigiprigss lasmicamel pvvtvvayvl lheqvtllqw lgillilagi viaeqkakri
      301 tvdheq
//
LOCUS       WP_285106479             332 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285106479
VERSION     WP_285106479.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..332
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33365
     Region          11..325
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mvalsvlavv sagsgqlhvp paevvgsllh hagldvgptp ahpngdaalw tirfprvama
       61 alvgaalata gavmqgvfgn plaepgvvgv ssgsavaasv tivlgltalg pwttaaaafa
      121 gglaatflvy glarsagrte vvtlvltgva vnavcgagla lttflgdtqa reqivfwqlg
      181 sfngtrwayv avvaplvavg vigalllarr ldllslgers arhlgvdver lrvlsivvva
      241 vltaagvafc giiafvglvv phlirmavgp ahrvlvplsa lggavlllaa dlvartavgy
      301 adlpigmlta lvggpfffwl irrtrrtagg wa
//
LOCUS       WP_285106592             239 aa            linear   BCT 25-DEC-2024
DEFINITION  GTP-binding protein [Promicromonospora sp. MEB111].
ACCESSION   WP_285106592
VERSION     WP_285106592.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Takai,Y., Sasaki,T. and Matozaki,T.
  TITLE     Small GTP-binding proteins
  JOURNAL   Physiol Rev 81 (1), 153-208 (2001)
   PUBMED   11152757
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006198
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..239
                     /product="GTP-binding protein"
                     /EC_number="3.6.5.-"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /calculated_mol_wt=24943
     Region          49..237
                     /region_name="Srp102"
                     /note="Signal recognition particle receptor subunit beta,
                     a GTPase [Intracellular trafficking, secretion, and
                     vesicular transport]; COG2229"
                     /db_xref="CDD:441830"
ORIGIN      
        1 mlgggggasa ptaqasrpaq aqpappvmqq apaanagaqa apgaqpaaer taptvvkivv
       61 aggfavgktt figsisdvep lnteaamteh svgvddaggv tdrkttttva mdfgrvelpg
      121 nlwlylfgtp gqdrflfmwd dlvrgaigav vlvdtdrleq cfpaidyfes rnipfvvgvn
      181 cfdgvakhrl edvrealqip shvpmlytda rsraatkqtl ialvqlamrq lrsgaqaqg
//
LOCUS       WP_285106624             575 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase [Promicromonospora sp. MEB111].
ACCESSION   WP_285106624
VERSION     WP_285106624.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..575
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=60321
     Region          59..191
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mdhsaaqgvr rvdflpweyd pasaegaaqa arqrelvdag aqlgagvfva pnaavycdrl
       61 algdrtyvaa laylsgdlti gadcsvnpfa vvrgeirmgd gvrigahtsi lgfnhqmand
      121 rpvfqqgtws kgitigddvw igsnatildg vtvgdhvvva agavvtknvp dwavvagnpa
      181 rvlrdrraet kgatagdlaa rlaafgdrar eqagdvlarc fedgrfvdrp saaagplppa
      241 vrpwadavei adlllgtppp gfdaadlvrr ltarqdpatg lipegdladr glsagtaerp
      301 daadeplspt dgdaayhvls vgyavrllga rlphpvravh algdrdvvaa leardwgaqa
      361 wgsgaavdsl atacalnmad fseelpdggv gplhgllgwl taranpatgl wgapqpaprw
      421 lqavngfyrl trgsyaqfgl plpypeavvd tvlehaadpv latpdgytac nvldivhplw
      481 laakqtahrr aegeawardq ldralenwad gagiafaprg dgpdgvpglq gtemwlsivw
      541 yladhlgvad slgyrprgvh npdplvrltp vdead
//
LOCUS       WP_285106638             317 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Promicromonospora].
ACCESSION   WP_285106638
VERSION     WP_285106638.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..317
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34371
     Region          5..313
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mpsetsptar alraleilqt rpgttadelg drlgvteraa rryveilrea gipvtsargp
       61 hggyrlgrgt rlppvtftqt ealglvmavl dshpeaddlv stalgkvira lpedvgrqaa
      121 tlrehasaap dryaarpdta vtselvaava arrrvlvtyr gesgsewvae vdpwavvvry
      181 grwyllchsh radavrtyrv drviavehtd rpfeppadld pvaaleehlg tgwqfttrvv
      241 fdapladvap wvgaqmgrle avgedrcvlt gttrnpamya qewlasvpfa frvedgpelr
      301 aavatlaerl aaavrds
//
LOCUS       WP_285106626             231 aa            linear   BCT 25-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Promicromonospora sp. MEB111].
ACCESSION   WP_285106626
VERSION     WP_285106626.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..231
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=24055
     Region          12..209
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mtapttpdta liaedlllll fdprsgtiag entlfytlag avltelavgd hveidgkpgl
       61 tgpritanag sppadpllre rwellvekpr gaqtflaevg prlreplldr lverghvgre
      121 krkalgfipt taltdggtpr raelvaavrp vladgadpdp rtavlaalls asgslptlhr
      181 dipwsgavyt rgkeleqgdw gaaaageavl rttiavttts aaiaiaavqn t
//
LOCUS       WP_285106722             119 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [unclassified
            Promicromonospora].
ACCESSION   WP_285106722
VERSION     WP_285106722.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 119)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 119)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..119
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13003
     Region          3..88
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 maraatttda fnavaeprrr eildalagge lavgdlvell glaqpqvskh lrvlrevglv
       61 dvrddgrrrl yrvngaplqa vhdwvaryer lwnerfdlvd dvlgeledaa deagtgqgd
//
LOCUS       WP_285106826             280 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Promicromonospora sp. MEB111].
ACCESSION   WP_285106826
VERSION     WP_285106826.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..280
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29620
     Region          9..261
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mttldvvrid dpaderlady nsltdvvlrs khepakglyi aesstvirra laaghrprsf
       61 lmapkwldsm seviarsgap vyvaeepllk eitgfhlhrg alaamhrppl agvdellaga
      121 rggagarrvv iledivdhtn vgaamracaa lgvdavlftp scadplyrra vrvsmgtvfq
      181 ipwtridpwp ggietlhdrg ftvaalaled dsislddlva nppeklalvl gtegdglkas
      241 tiancdltvr ipmsggvdsl nvasavavaa watrvpddgh
//
LOCUS       WP_285106854             326 aa            linear   BCT 25-DEC-2024
DEFINITION  Kelch repeat-containing protein [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285106854
VERSION     WP_285106854.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Shi,X., Xiang,S., Cao,J., Zhu,H., Yang,B., He,Q. and Ying,M.
  TITLE     Kelch-like proteins: Physiological functions and relationships with
            diseases
  JOURNAL   Pharmacol Res 148, 104404 (2019)
   PUBMED   31442578
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Gupta,V.A. and Beggs,A.H.
  TITLE     Kelch proteins: emerging roles in skeletal muscle development and
            diseases
  JOURNAL   Skelet Muscle 4, 11 (2014)
   PUBMED   24959344
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Adams,J., Kelso,R. and Cooley,L.
  TITLE     The kelch repeat superfamily of proteins: propellers of cell
            function
  JOURNAL   Trends Cell Biol 10 (1), 17-24 (2000)
   PUBMED   10603472
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..326
                     /product="Kelch repeat-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=36142
     Region          46..324
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          58..105
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          201..246
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          249..290
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
ORIGIN      
        1 mpinvkesgt wkagklvyak vggawqqakr iftkiggiwv giwsaaywtq ksnfqyarkq
       61 gqavgvngyl yyiggrynnd ysgsgtytne rwdpntntwt yladclykkt dgwvaargqy
      121 ihvgsgtdhy ythvmydtns nkwfsknhit daqgpcaaya gdgntiymag gwnggsyyns
      181 fykwqdsvdy atsltsmpmq rawaaggfin nkfyviggei slgqltnqch vynpdtnawt
      241 qaadlpeqvs qsphwvlnsk myviqnstss ktfcydpatn awilgptcps nvyyakgasl
      301 ngkgyvvggi qqgtgnitqt lyeltm
//
LOCUS       WP_285106886             377 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285106886
VERSION     WP_285106886.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..377
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=39408
     Region          8..373
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 msmhswttra vhagkddlaa lglhappidl sttypsydvv geatrldefa egrddggppv
       61 ygrvanptvr rfenalaele gaeaavafas gmaalsacll tqvaagrphv vgvrplygtt
      121 dhlldsgllg tsvtwaaped aasaitgrtg lvvvespanp tldevdlral tdacapvpvl
      181 vdstfatpvl qrpleqgaam vlhsatkylg ghgdvmggvv acdeelarsl rqvrfvtgam
      241 lhpmagyell rglatlpvrv rgaaataael arrlgehprv trvhypsigg amvsfetsad
      301 pvalvsavrl itpavslgsv dsliqhpasl thrimdevsr keagispdlv rlsvgledve
      361 dlwtdldqai ahaarlp
//
LOCUS       WP_285107032             322 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Promicromonospora].
ACCESSION   WP_285107032
VERSION     WP_285107032.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..322
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34686
     Region          1..322
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mgsaqrligl lgalqarrht taealaeefg vstrtvlrdi qklvdadipv ltergryggi
       61 sllpgqqvdl trlttseadv lravgvdler aralgaetaa raavgkfatr pgapparpga
      121 aplsladvvt venrawfapq epreapdvaa lardlrqarr lhvtyrrsgq saaadlvvdp
      181 yglllrvdrw ylvadvdaap rlfaltrldg wtlldeprrv rdvaledvar glgqaletrr
      241 gmtveavlda gavdlayril gsrlrtvgpp dasgrvpiti gyaqveaarq llqfadhiev
      301 tgppearall hrlaeetarr ha
//
LOCUS       WP_285107157             303 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sugar phosphate isomerase/epimerase family protein
            [unclassified Promicromonospora].
ACCESSION   WP_285107157
VERSION     WP_285107157.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..303
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32123
     Region          7..281
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtppfllgyg tngfgdhplr valdvlddvg yaavavtlgf phldpfapla gddvralrah
       61 lrrmrggtga aavvetgtry lldplhkhrp tlvdrdaalr mryleravei aadldarcvs
      121 ffsgilpdda saadgwarlh ervgalveya gergvhlsle pepgmlvetv gdalrlladl
      181 gtppelgitv dvghclvvep dgvegalraa apylsnvqld dmpgthhehr pfgqgdldlp
      241 lvlatladig ytgvaavelp rhshdaprla rdsraalmra wadvtgarar artattsseg
      301 als
//
LOCUS       WP_285107163             402 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285107163
VERSION     WP_285107163.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..402
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42776
     Region          5..398
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 mdksvvitgl gvitpfgkgi dvirshtfag rhgftdiesf stalnhakrg gelkdkdrtf
       61 rafsrycide alamagldrm kdrellkdav vaignvgegv slesyysaqy grktgddsgl
      121 qaavddslir qrdpfraaee aaayigstnv hiafsnacva sanaigygyd qirkgrasca
      181 lvggihilnp fvfnnfdsnr amasgvvrpf slerdgllis dgaamllles reharqrqak
      241 plaellgwgi sadgfhvtqp hpegnglara mqaalrsanl spadidyina hgtgtplndr
      301 setkavkqvf gkeayqipvs stksttghml eatgaveavi gilalmdqri pptanygtpd
      361 ptldldyvte gvraaplqiv msnssafggn ncslilgkgk de
//
LOCUS       WP_285107169             282 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paenibacillus
            sp. UMB4589-SE434].
ACCESSION   WP_285107169
VERSION     WP_285107169.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..282
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32679
     Region          1..273
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mkwtmttvsf ryhlhsfael mkfgadagfq gielwephwt rhadaildyl qsnqqdalpi
       61 rvlsgyqdlt dlaqpthqwq qqlrhklevc qqlnipvlrl ftgqmssaea ndsvwqawld
      121 rldtlehmaa erkvqvvfet hpgtlldqpd avdrfvkait trswkqigln fdvyhvwefg
      181 vdpldyiqrw fpvikhihlk naskrtsqfv fanvyhpagd ysdltelhqg qidilpimqy
      241 asdsgyngav tlewfglpsr eqyqrelayl eqvqvpakqv ll
//
LOCUS       WP_285107209             225 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285107209
VERSION     WP_285107209.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..225
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=26399
     Region          <52..221
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          70..94
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          100..128
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(101,104..105,108..109,111,137,140..141,144..145,
                     147..148,170,173..174,177..178,181)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          135..164
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          169..197
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mskllgfgll ywlfgnpfia iialliiaym lerryvglsp sfirpikrmq rigklkqels
       61 anphnvslkh elgrlllerk ryrearevle piqdrmehsa eywddlgtsy vhtddeekgi
      121 qailqaldin prvkygqpyl rlaalyartd kdkalealqe lhilhsssce ayyrmgllye
      181 emgrkdeakr swneaisiyr alpkymrrke rawmlrsryk amsss
//
LOCUS       WP_285107185             397 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285107185
VERSION     WP_285107185.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..397
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42709
     Region          3..396
                     /region_name="FucP"
                     /note="Fucose permease [Carbohydrate transport and
                     metabolism]; COG0738"
                     /db_xref="CDD:440501"
ORIGIN      
        1 matlflviiy lafislglpd sllgaawpvm rmdygapiet agmlymiiag gtivsslasg
       61 tvlkrfgtgk vtfvscvlta galfgfsiap sliwlflcai plglgagavd aglnnyvath
      121 ykahhmswlh cfwgvgatig pmimsfyisr gqswrdgytt ifiiqlalvv llfctlplwk
      181 rvspesrder tddggdtdpe ganeqkartn plkikgvklt ltsfllycgv estvglwggs
      241 flvntkqlta ataaqwvsly yagitvgrli tgfvtfkvsn rvliragqmi alagtvllvl
      301 plptsfslvg fimiglgcap iypcllhetp trfgkeqstg imgyqmavay tgstflppll
      361 gwvigysttg vlpyfvityi vlmfigseqv nrlmkah
//
LOCUS       WP_285107211             497 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285107211
VERSION     WP_285107211.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..497
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51643
     Region          46..366
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrndrtgarr vrlraaqgva lltaavvafa paasaaadda dvdrhlaeyv rvhrapglal
       61 vtladgdahv rvhgttgsga pvgedtpmri gsmskaftal avlqqvdagr felddpvvev
      121 lpefrladdr yrsitvehll thrsglaatg leyssdpasa paetvgrlap eklaadpgtt
      181 tlysnagyav larlvertad adfgpyldqn vfeplgmsst tvtercdaep agldrgfsll
      241 gpvrvavpel placagsggi vstardmtaw lrfqvgdgts atgerllree tfrafhdvpa
      301 sgaeygygwh gttadgddap lvghggtlat fasgiefspv tgtgavvlan aagdpmaltr
      361 davvavdggt plpmtnpfdp fnavlvgvaa lvllagvlvv vrshrwaerr aagsrratvl
      421 rlvplalvtl lgaalpwlga tlmglsepva ayrvvlwlyp avvllgvalv laaggglaar
      481 lvrlrgeqvr rapgprr
//
LOCUS       WP_285107245             972 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285107245
VERSION     WP_285107245.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 972)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 972)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 972)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 972)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18732943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..972
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..972
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=103109
     Region          <6..936
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          904..972
                     /region_name="GerE"
                     /note="Spore transcriptional regulator GerE (stand-alone
                     HTH domain) [Cell cycle control, cell division, chromosome
                     partitioning, Transcription]; COG5905"
                     /db_xref="CDD:444607"
ORIGIN      
        1 magwsaqeqp hrgeaargrf vgrraeraql qeawaaarag srqvrfvgge pgagksrllt
       61 qlaaelprdg vtvltgacps tlaspyepfv apaaamraai adgalplarp spdeqavagt
      121 vallgtvvge rpagrasrrd lldavvtsvr saaaveplvl llddvhwage tawellsylv
      181 eqtadlrlll vathrvtatd rtdhlvnhva rlyrldgvrr vdlpplaaad veeylqkean
      241 vpaalartaa vdlrertggn ayfvrelvqt laaegpagfv qpggrmppsv qdavearlga
      301 ldaeargtve raavigdvvd vdllvaaget qpeaalghld aavdayllep vddaptavrf
      361 rhaitrdvvl gampsarrtv lhlrvarale arggrgaaha aqvahhfeaa yvlghraeav
      421 rylrlaavla aeglahdeaa dlyeraaaid ddraraddat llasrermlt gafvrsrala
      481 epvaddaasa hrlraavqye danwrtnvag grsvallraa ldssddqdee lrirakaglg
      541 ralafdgede pgrvlfersi trarelggdd llgdvlvasl vlgsavtdad vklgraiels
      601 elclrthdll rlgpaasyrt llgyqrgdta vvragltdlr lavesthqry fgylagcvdf
      661 sdhlaagrla raaqvseall eighavelde hvgpdgqygv qqfvlrrerg eldevrglvs
      721 gdddfggrwv pgllalytel gmhdaarral wwliesgtae sspgtragvl aflsdaaval
      781 gdleaarvvr talapyagln imfgslvsam gsadrylgsl dallgtegwe aefaraeamd
      841 ramgahlhva htlaahvaah lttgadgcdv galaaearri atsvgsrrvl rmldaalgep
      901 vgvrarradg ltereievlr lvaqglsnre varslvisen taanhvrsil lktgcenrtr
      961 aaryaatqgl ld
//
LOCUS       WP_285107263             448 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Promicromonospora sp. MEB111].
ACCESSION   WP_285107263
VERSION     WP_285107263.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 448)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..448
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=46284
     Region          137..447
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mpaapgghrt gapwagfslr lritalatav tlacllglam vagrglapll tgavddelrt
       61 alsgaahdvv tgtepasadg levrvldtag gavddapppa ltrdqvralk agtpvtagdr
      121 rqvrwqgsvv tapdgsqrlv vvgtglvgqr aaeasgsrwl lvtalvgtvv agvaiwfavg
      181 salapvarmr qsvrrlapga rlavpdaaag elralagdfn elldrqeatt erlrrftgda
      241 ahelrspvas irlqsevavt npdpalsqev hadvladaer lsalldglla larsdagelp
      301 psddvdlvge vhaavarage qpvpilvnva adqvwaaaar tetglvldnl lrnacryagt
      361 rvvvsvlagr stvrvlvddd gpgvrpehra kvfdrfyrvs ddrartsgga glglalvael
      421 vrrrggraav gespdggarf tvvwprar
//
LOCUS       WP_285107267             393 aa            linear   BCT 25-DEC-2024
DEFINITION  LolA family protein [Promicromonospora sp. MEB111].
ACCESSION   WP_285107267
VERSION     WP_285107267.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Tajima,T., Yokota,N., Matsuyama,S. and Tokuda,H.
  TITLE     Genetic analyses of the in vivo function of LolA, a periplasmic
            chaperone involved in the outer membrane localization of
            Escherichia coli lipoproteins
  JOURNAL   FEBS Lett 439 (1-2), 51-54 (1998)
   PUBMED   9849875
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..393
                     /product="LolA family protein"
                     /calculated_mol_wt=39759
     Region          <94..258
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mrprtkalva agsgiavglg glaltalpag adddpvlpai daeqlvtsal eatppafdgv
       61 aevsnelglp avpgadaldf esvrvfhdga esarvqverp tseltfvknt deawaydsqe
      121 nsarqltwdd adlaaarera gqhaakqgha earmadpaqa ateiieqlrp tsdivvdgta
      181 rvadraayel vltpkptekt llreitvaid eqtrvplrfd vyangrsepv lslgfvefev
      241 gaqdaglfef tppagadvkt tdagdvaqar gehageagep ggpgeslttv gdgwdavlvg
      301 tvpaealgqd vagagpagse gflggagsag ggsaggeqdl agllaqigqp vsgefgsgsy
      361 vriavggaiv tddgrvaaga vpqqvlvdal dqq
//
LOCUS       WP_285107286             411 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285107286
VERSION     WP_285107286.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..411
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=42390
     Region          12..411
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mstaphtpaa glspatvvvs agrpareqgg hinpsvplns tyvsrgvvtp delsyargdn
       61 dawhpfeeal aalegggeag ggaagggaaa patailfssg maaiaaafsl vpdggtlvlp
      121 rhayqagmvl arqiserhgv tlryvdiadt davvaaldga dlllvesptn pmlevadlpa
      181 vlgaaraagv rsvvdntfat plgqrplehg advvlhsvtk ylaghsdvvl galvtrdaal
      241 aatlrehrtl hgaiagpfet wlalrglrtl alrferaqas aaelarrlae hpevaevrhp
      301 slpgdpgher akaqmngfga iigvrprprp gagdaeaagt gpaaverada vvdavrlwlp
      361 atslggvesm lerrrrwgte ahtvpedllr lsvgiedved lwadldaalr a
//
LOCUS       WP_285107320             429 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal-phosphate-dependent aminotransferase family protein
            [Promicromonospora sp. MEB111].
ACCESSION   WP_285107320
VERSION     WP_285107320.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Koper,K., Han,S.W., Kothadia,R., Salamon,H., Yoshikuni,Y. and
            Maeda,H.A.
  TITLE     Multisubstrate specificity shaped the complex evolution of the
            aminotransferase family across the tree of life
  JOURNAL   Proc Natl Acad Sci U S A 121 (26), e2405524121 (2024)
   PUBMED   38885378
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Koper,K., Han,S.W., Pastor,D.C., Yoshikuni,Y. and Maeda,H.A.
  TITLE     Evolutionary origin and functional diversification of
            aminotransferases
  JOURNAL   J Biol Chem 298 (8), 102122 (2022)
   PUBMED   35697072
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..429
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=45326
     Region          9..404
                     /region_name="PucG"
                     /note="Archaeal aspartate aminotransferase or a related
                     aminotransferase, includes purine catabolism protein PucG
                     [Amino acid transport and metabolism, Nucleotide transport
                     and metabolism]; COG0075"
                     /db_xref="CDD:439845"
ORIGIN      
        1 mtqihpparl lmgpgpvdad prvlramaap lvgqfdpfmt dtmteamllw rtvwdtaneq
       61 tllvdgtsra gieaalvsll epgdrvlvpv fgrfghllae isaragaevh tieaewgtvf
      121 rpdqiedavr rvrprllavv hgdtsttmaq pladlgriah ehdallyvda tatlggnpfh
      181 tdewgvdaat aglqkclggp sgsapvtlsp aavaaidrrr hveagirtad dvaphgvpiq
      241 snyldlaqim eywgprrlnh hteatsmlya arecarllva egmatavdrh aqhgaamlag
      301 vlglglevfg dvahkmhnvv avripdgvdg davrgglldd fgieigtsfg plhgvvwrig
      361 tmgfnarrda vlttlaaleh elrragfhap agggvsaala aydgaghggv hdpvhqmvpd
      421 tavakearl
//
LOCUS       WP_285107348             354 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease [unclassified
            Promicromonospora].
ACCESSION   WP_285107348
VERSION     WP_285107348.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 354)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 354)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..354
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35145
     Region          23..353
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 msapapatpt rvtdttvttv adlrtlrrrr qalvvsgmvl vvlvagtaal lmgaagltpg
       61 qaisgvfglg dkgdvfvvqk lrlprieaav vvgvafglag alfqstlrnp laspdilgis
      121 tgaslgavig vlvlglsgma lsglafagag vvalaiwlla wrkglhsirf vlvgvgfayl
      181 gssliawama rsqeheaaav liwtvgsvsd vrgeqltlva agtlvlcaaa avvsrtqgpl
      241 algddnaral gvhvdaarvg alllavalva latsaagpia fvalvapaia rrlvndggaa
      301 lvasaatgaa ltlaadviaq hgllgvaapv givtglvgap yllwllatte krsr
//
LOCUS       WP_285107349             430 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285107349
VERSION     WP_285107349.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..430
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=46947
     Region          1..428
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mnilvagvgy vgtttallla elgwnvigfd tdkskvstls sgtlpfyepg ldkllhtqln
       61 kgnirfisdp vqaiqesqvi ficvgtpsqe dgsadlqyir savtmigtym qeykllimks
      121 tvpvgtqnlv tqwiseaqks plpfdvvsnp eflregnavy dafhpdrivi gtdssaaaqq
      181 vrmlyrdids pylvttpata emikyaanaf latkisymne larlcdqlnv sitdiaagig
      241 ydarigksfl qagigyggsc fpkdvksllh iannhgsslg llqqvvqvne tqhqyfmeqi
      301 kahlgiidkk viavlglafk pgtddlreap slklitqllk dgaliqvhdp varlpeaarq
      361 ahvrqvksvk daihgadavv ictewpeyaa eawqdlayem rntavfdgrn mldgtqmkaw
      421 gyhyygigng
//
LOCUS       WP_285107416             354 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Promicromonospora sp. MEB111].
ACCESSION   WP_285107416
VERSION     WP_285107416.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..354
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35561
     Region          1..352
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 msnrvivvga givgaslayh laargqavtl ldaglpasga tgssfawigr petsdlpsap
       61 lrflaldeyr rlqrelpglr iswsgsltwd gtgddsgdgs gegsgeagrp ggaaadvrai
      121 epglvpgpgt phhapddgal dpvevtellv aaavergael rvgtpaiglv rdgsavtgvr
      181 tgagvlpatt vvvaagagta tlcagigvev pvesspavlv rlratpglvr tivagpelev
      241 rqrpdgtlll playegqtnr aalqdtaeaa rrsllrffpg asdveivsae igwrpmpadg
      301 epivgaepgt sglylavmha gvtlaaaagr laaeeittgv aapelagcrp drfv
//
LOCUS       WP_285107422             172 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285107422
VERSION     WP_285107422.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..172
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19644
     Region          21..145
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 msepkfaacp saltpwyghi lrvryqetds mrvvfhgnyv twfevgrtew irslginyka
       61 leteglllpv tdlqvsykqp avyddqvavy trlqdcspir msfqsvvcrv qrpladelsg
      121 ngwiseptge llvqgsttha wvnedwhltr fdraqpdiwk llqelralpt ss
//
LOCUS       WP_285107571             419 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285107571
VERSION     WP_285107571.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..419
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48629
     Region          1..397
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 maratydqei aiigagisgm tiahelaqkg ytritileqe drvggkchsi eyksktyemg
       61 tliglpsykh tqelmaeygl tdkgpllerg ffnkhgskts qipldqieaf teqfkrlpnl
      121 lsqydclkep gflrlpeelc qpfaswcevh dltviqqvym hyfstfgfgs vdevpaayvl
      181 kflnfdnlls fieithmitw pqganalikr madriddlrl tcsvqymelg sdgrvrvetn
      241 qgtfyfdhvi ytsslhharh llslspaeqq lmeqvtyerf rvyayrvegi pelsgyipdn
      301 mssdrkghmm awyyrwtdee ntdlitvyvm enedmsdqqm retveeelrk lggthirlym
      361 ikqwehfphv nsaalragfy dqldrlqgkq hiyyageimn fptlenciiy akylvnrff
//
LOCUS       WP_285107656             504 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Promicromonospora].
ACCESSION   WP_285107656
VERSION     WP_285107656.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..504
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=53104
     Region          24..>82
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          <101..503
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 mslpsvpsrv wqdeavrsal adwdfgqvsr mvrqlvplrq edvaaltgls qsylsmlecg
       61 drrltdvsrv vqfltglgtp pdlvrlplpg isplpdaaep arattsgqvs sapvvvtpta
      121 pdpalpwtad rmltalrlah vadstadwlp sdangpvsan amsdaagtdt prpasgialn
      181 smiqrwdaeq aeplrratvg trvslelcgh lqgtldelrv mdkgsgsgav adlarahlal
      241 vvrilersty devtgrllaa vaadtatqag wfafdagrtd saraymlagl raahaaaddr
      301 lgagalsyla ihgyssgdpr davraaeagr rriarldaph lsatlltrqa rghaaagege
      361 aarralgeas elcargrged dphwlywmne geihgqagsa hlalgntara vesfghaira
      421 eragerrthg lflsraaqah aragdldaac atgeeavsia etvqsarlre hlrdlsadlr
      481 rggstrrsgm garvlteria alas
//
LOCUS       WP_285107678             481 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285107678
VERSION     WP_285107678.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..481
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52996
     Region          18..366
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkktivfvlt illlfsgfat qsyaslsdtq saaiqalldd agrisgvpgm sisiladdev
       61 fyfssgyadr esglsasent lyelasvska ftgmgillle eqgllsmtdt vqkylpwftl
      121 kyqgkpvdvq sltlnnflhh tsgltngrht qnipqgntpd llqktvemlv daelafppge
      181 qynygtvnyd vlglvieivs gqsyedfmrg qvfqplglhq tyvykedaqa tgqlaqgyrs
      241 sffmttpyna pdysgnkpag yiisctkdma rwmgiqmgiv qdipeifhtv iekshqgdms
      301 vpavnemyya agwsvnanqt iiehpggnpn fgtevaimpi ertavclltn ganinrsmvl
      361 kvkdildgnl tqsyeisgtq lldiilsstt iilcllavlf fllglrrrkt nerqpmtkkr
      421 iivtaillia tialcimcca ldwstiliwq tysvltalis salltasitw fvythrynts
      481 l
//
LOCUS       WP_285107724             721 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Promicromonospora sp. MEB111].
ACCESSION   WP_285107724
VERSION     WP_285107724.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..721
                     /product="PhoX family protein"
                     /calculated_mol_wt=77431
     Region          44..719
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mtiapenrpl ltvhthargk rspvtcrlkc ndaclhpapn esaneyfkdv vssvlsrram
       61 lgtlavaaga vvigaqgaaa psaaaatlpe grfpgaghsq glsfgaidpq pvdvdalvvp
      121 egytwnpiir wgdpilpggr tfdpnnqspe qqakqfgync dyldilpirp gekhrgtrgi
      181 lvsnleytnp eimfppteky wdiaadgsrt knaysraier aahgmavvev rrrgtgkpwd
      241 yqrisvlnrr ihldtefvld gpaagsdllk taadrtgrrv lgtmnncagg ttpwgtvlsg
      301 eenfngyfva agvnptadar ygigastsyg weadeprfaq sagyenesnr fgwiveldpy
      361 dptakpvkht amgrfkhega nvtlsrkgha vaymgddqaf dyvykfvske rvakgdsrwa
      421 rthnktllse gdlfvakftg dspaaqidgs gavpadgafd gtgewlplvq dgrskvpgms
      481 veevliytrl aadkvgatkm drpedveisp vtgriyvact nnsgrtpgna tegateanpr
      541 drkvvngvtt ngnrdghvve iipsgdqtst rftwnlllva gdpavegtyf sgypkdrvsp
      601 iscpdnlafd aegnlwistd gqpsssaiak cdglfkvpva grerghvqqf lsvpagaetc
      661 gplvdsrdgm vyvnvqhpge ngsfeapdsf fpdyvaagat peagdfrgpr ptvvqvyrdr
      721 h
//
LOCUS       WP_285107801             492 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Promicromonospora sp. MEB111].
ACCESSION   WP_285107801
VERSION     WP_285107801.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..492
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52453
     Region          133..473
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mslrrpsvra kvvavvvavt aigllgagll thaiqsqqim ddisedfdqe igelqrlaad
       61 gvdpetgedf hgagrlmsva mernvpgsne mfvsyldgah qqsnppaasr vvveselvqd
      121 vvdgltpqss ttvqreiete igrvwfvvvp vtvpdrqevg ayvmasaldq sleaetavmr
      181 tyaivcsval vllglfawlv vsrllrplrq lsatatrvte tdlsqrvpva tdddlgelag
      241 afntmldrls taietqrqfl ddaghelrtp ltvlrghlev ldpddpadvr etrdllldet
      301 srmgqiveel vllakaersd fvapapvdlg rftddvhdka ralgdrrwvv daradvevsa
      361 dahrltqavl qladnavkft gaddevgigt qvfdgpsgrv vrlwvrdtgp gvppeeadri
      421 fdrfargstt ggvpgsglgl aivraiaqgh ggdvvversd gggarfvmtw paagpgqgaq
      481 paargataee aa
//
LOCUS       WP_285107887              68 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285107887
VERSION     WP_285107887.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 68)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..68
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7915
     Region          2..64
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mkikirlqei ldekgmsqre larlmnlrpn tinhlcsdkv drvyirtles icealnikih
       61 elivedei
//
LOCUS       WP_285107951             215 aa            linear   BCT 25-DEC-2024
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285107951
VERSION     WP_285107951.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..215
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22134
     Region          4..189
                     /region_name="YdeN"
                     /note="Predicted esterase of the alpha/beta hydrolase fold
                     [General function prediction only]; COG3545"
                     /db_xref="CDD:442766"
ORIGIN      
        1 mryvtvpgyg gsgvehwqth werdlpatrf rpaswdtpda rdwadaldrv vadgegpvvl
       61 lahslgclav aswlaevprr dgrgsggrrr dgrepgevag allvavpdpa gpafpagata
      121 ggfravrrrl pvpvtvvvsd ddpyaspawv rglaavwgae avgigpaghv ngasglgvwp
      181 agreilrhlv rprppasats aaatsatadt anavv
//
LOCUS       WP_285107965             316 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Promicromonospora].
ACCESSION   WP_285107965
VERSION     WP_285107965.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..316
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34712
     Region          16..309
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtttagrlla llgllqsrae wtgpelaarl dvtdrtvrnd varlrdlgyp vdsvrgpggr
       61 yrlgvggklp plvlddeeav aiavglraan tvagieessa ralgkleqvl pdrlrsqvaa
      121 lrdatdagpv ntdsnvedpv vdpalltela aairdhqglr fwfreeprev epvrlvawqr
      181 rwylvgrdvg sgrwepfrvd wlelrrpggr rftpveppfd ltefvvreva rtgwavhtri
      241 vvhapahevl drinpavgtv eprddtscll vtggdsietv avwigmlgld ftvtgpqglv
      301 dhlevlsrry dravrg
//
LOCUS       WP_285107994             478 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285107994
VERSION     WP_285107994.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..478
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51706
     Region          16..317
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msrilprstp eaegldpaal rrlvdrldal edvhsvmvlr hgsvvgeaww hphtaarphv
       61 mfsvsksfts tavgiavheg lltlddrvvd llpddapadp gphlgamrvr dlltmttghs
      121 astmegidrt islpgagwar ailaqpvehe pgtrfvyntg atyllsailh rltgqrlldy
      181 ltprllaplg ithatweqdp dgidvggfgl svtteemaaf gqlylqggvw qgqqlvpaew
      241 vaaataaqvp ngphdwpdwn qgygyqfwqc rhgayradga fgqyivvwpe kdlvltmtsg
      301 lsdlqsvldv vwdtllpdga wvapgqavpg aeavpfeqal ptpagapssp lvealrgvtf
      361 eleenqrdvg alalgraadg rtevtftpta gpdrvlrfgh gewvpgswpf rgapadvata
      421 aawtdestlr grlvflgtpf ewrlelrfag ddvavtidqn vafgerellr vkgrarrd
//
LOCUS       WP_285108172             102 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein, partial [Promicromonospora sp.
            MEB111].
ACCESSION   WP_285108172
VERSION     WP_285108172.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..>102
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          12..>79
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mipaaesggg gdryaewdaa yvigalspsd rrtyerhlae caacraavae laglpgllgt
       61 ispahaealv aeapgpaglp dggappgepa pgrpadvvpl tg
//
LOCUS       WP_285108176             889 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Promicromonospora sp. MEB111].
ACCESSION   WP_285108176
VERSION     WP_285108176.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 889)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 889)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 889)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 889)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468444
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..889
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..889
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=88550
     Region          134..414
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
     Region          <304..889
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mdthrvppvg parprvltvg ptirltlaqm rrslgrlaaa glavlistaf vaatlqagtv
       61 vtrttydqva aqyadadlvv fdragtmtpa dvdavravdg vaaadgfrgt yvelarggrt
      121 vrqslvaaps dprltplvla ygvwpdgpdr ialpvdvael fgvgvgdtvs strclragkp
      181 gpgkpglger gaecyggqea vekltvsglv ddpvsayaag ggvavvtpaa lerqlagaga
      241 aaapgmrtvv valdrpgdea avaavrsala aavpsatgvt tpeeyaedvv agisggqniv
      301 ylvfvlalaa vslvvaglvi antfqvlvaq rshtlallrc vgagtgqihr svlleaallg
      361 tvasvagiav gslfvqagll vapafdlgva lprtipltpt aflvplaagl lvtlaaavap
      421 araasrvapl aalrpaagld psgtgrarav fagfatlggl avmaagvalg rsgsidtglf
      481 aavlggsvsl vgiivgsvfw lprvaavfgr lagaggatar lasanalrnp rrtaatstal
      541 ligvtlvsmm ttgaasarlt mndqldarfp vdlrvtstah dadgaaaavp avvtdalagv
      601 dglgavvpvt nasarradgg tpvqvaavdp ddlrsvantp adagrlrpgt ivvpqraael
      661 ydlegagtlv ltgpggrvtl dvvhsgsrsd rayltpqdla alapglapge vwaqvdddrd
      721 aadvvsavqa avsttgetvg vtgtvversa yqqmvdvilg ivvglltvav lialvgvant
      781 lslsviertr enamlraigl srgqlratla vegmviagvg avlgivlglv ygwvgattal
      841 svlgqvplvv pwtevgvvla valvagllas vvparaavrt hpvaalaae
//
LOCUS       WP_285108205             257 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285108205
VERSION     WP_285108205.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..257
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28286
     Region          15..256
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(28..29,31..32,35..36,72,76..77,80..81,114,118,125,
                     128..129,134,150,154..155,157..159,161..162,165..166,
                     169..170,194..195,197..199,201..203,205..206,208..209,213,
                     216..217,223,225)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(153,157,160..161,163..164,208,211..212,214..219,
                     222..224,228,230)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(174..181,196,199..200,203)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mvnigksgtv rlrawlhrld pitkgiwlls tglavmmtms lagqaawfas vllfawtggd
       61 wsgrqwrllf iwllgfgipl ivfqwlvlpg etpilssltg kllteealrd svsltlrsmt
      121 lmassivyat tteprdvvva lvgqlrvpdr iayaaaialr fvplllaeae qmrhaqrlrr
      181 mapargvger lrsarqllla vtqaalrhvh ivstsmeakr fgqggqrtlr rklrirpqgi
      241 glaavsigta vtslywl
//
LOCUS       WP_285108213             580 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 35 protein [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285108213
VERSION     WP_285108213.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 580)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 580)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..580
                     /product="glycoside hydrolase family 35 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65509
     Region          10..322
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
ORIGIN      
        1 mtqltwegqq mllhdrpfri isgamhycri vpeywadrlc klkamgcntv etyvawnlhe
       61 preghfnfng indvagfvrl agemglyviv rptpyvcgew efgglpawll ntpmrlrcsd
      121 prylakvaay ydkliplltp llstnggpii amqveneygs ygndkaylht lrdmliergv
      181 dvllftsdgp hddllqggma egvwatvnfg srsdeafdkl leyqpdaplm cmeywngwfd
      241 hwfeehhths aedavqslde ilargasvnf ymlhggtnfg fmnganhggk yeptvtsydy
      301 daaineagdl tpkfeafrrv igkyvelpke plpsnlpkaa ygevtpfrgv rlwdtldtis
      361 dlhhsicpep mehygqglgf imysttitgp rpesqltiqd vrdralvfid qkligvverw
      421 nptsipvvip eggarldilv enmgrvnygp elidhkgish gvrlnnqfqf hwevrtiple
      481 siaqvqfdvs astldgeqpa fyeaelvieg epadtflyln nwrkgvvfin gfnlgrywev
      541 gpqqslyvpa pilkqgtnqi vvfelhapgk plqfrkepql
//
LOCUS       WP_285108219             784 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285108219
VERSION     WP_285108219.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 784)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 784)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 784)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 784)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..784
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=84683
     Region          14..770
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtrtlpnqla qgderqsfqv kglscancar eceidirrle ngkdaelhyn sgtlkihpsv
       61 nrkqverilr rdgaylveag altgegftra agskgkgsqq seqlhaaghe hshehghdhh
      121 nceghshgsh lhnhangdkh dhsdanhdhg eahghdhshg hshehgsmkr mkwflgissv
      181 lyvstfmldg ripqwslial yliavllsgh ttfmqglrnl frlrfnmdtl mtvaltgavv
      241 mgewkeatlv ailfglneil egygmerarq svasllavap kqanvlrhge tvtipieqlk
      301 vndtvvvrpg ekipsdgtvl egisgvdeaa itgeslpvak evgssvyggs intsgllkvr
      361 vdkayedssl akilhlvrea qdtktptelf idkfaqyytp vimiiaalvm vvppllldgd
      421 wfkwvyqgfa vlivgcpcal ilsspiaivs gitrtarmgi lvkgsvhleq lgkinalafd
      481 ktgtltkgep avmaevvydq grcydvigav eqgslhplak amiryvngkg ltqfvepsha
      541 etvagegiea iiegttylvg serilnrdga afeqaqadae rmkaqgytiv avvehgrplg
      601 vfgladeire esratiqalh dahithtiml tgdhkqsaar vaeavgvsew hagllpeqkv
      661 eqvkelakky rvamvgdgin dapalasaql giamgkgtds avetadivlm qdhlgklpaa
      721 irvsrlvnrv irlniglslg lkiialllti pgwltlwiai lsdmgativv tllgltillg
      781 kdpe
//
LOCUS       WP_285108251             338 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285108251
VERSION     WP_285108251.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..338
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=37789
     Region          <36..338
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrpdrnivli cclllaltfl lihdiwngpl gtvrgvlfiv iymsasilll arirfvarlk
       61 dahqalkrav qgnrntrlla ngepllnevi fsinelieqi dklqvqtirs eaarksllsn
      121 ishdirtplt siigyvdalm ddiadnsaer qaytaivlnk annlkklidh lfdlskldad
      181 eivmkperld laelarecvi efipelrrqq levkasipdv pclivadrvs mnriisnimk
      241 navqygkdgk vvglelteyk qeyelriwdq gtgiveedre kvfdrlyrte rsrsslqggs
      301 glglaiakal ieknggaiwv tsdpgvcttf gitipkhp
//
LOCUS       WP_285108281             396 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase family protein [unclassified
            Promicromonospora].
ACCESSION   WP_285108281
VERSION     WP_285108281.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..396
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=42868
     Region          28..369
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mtrpdeslta svpeanpett gsprrkitgr lvamdglrfg aaaavllyhf tatstvtsyw
       61 gadpdrafpl lnevtrygwl gvelffmisg fvimlsadgr giagfvasrv grlfpaywac
      121 ivltvglqqf wsggrqtdlt etlvnltmvq dlfdvtgvqv vfwtllvelk fyllvlvvla
      181 lgpltrnrvl tfatlwplag waaqelgahw ladwlvpvya pyfavgmllf layrdgfdlv
      241 tsallagglv lcvmrvqeaa grasdlqgvt vdpviavmim lasvvavwat tlrgrtappr
      301 rvatvlgtvg altypvylvh tqfgyavidv lahettrtva lfaagalslg lavaihygie
      361 rptsarlrra vqagllrcsa alrsrglmra wddvrt
//
LOCUS       WP_285108291             379 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: AAA family ATPase [unclassified Promicromonospora].
ACCESSION   WP_285108291
VERSION     WP_285108291.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 379)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..379
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39793
     Region          72..365
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtepafpaqs asrpaeptsd pqagqpgapa apaaqtvqtv pvngpaaagp vdaapapaqp
       61 papsqelrsa laavrtevgk avvgqdaavt slliallcqg hvllegvpgv aktllvrtla
      121 aalkldtkri qftpdlmpgd vtgslvydar taefsfregp vftnlvlade inrtppktqa
      181 slleameerq vsvdgtprpl pdpflviatq npveyegtyp lpeaqldrfl lklvlplper
      241 eqevevlarh aagfdprnla aagvtpvada gvleraraev arvqvsrevl gyavdvcrat
      301 rfspslslgv sprgatallr tarawawlsg rsfvtpddik alahptlrhr vqlraeaele
      361 gvtaegvldt vlasvpvpr
//
LOCUS       WP_285108349             317 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Promicromonospora sp. MEB111].
ACCESSION   WP_285108349
VERSION     WP_285108349.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 317)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..317
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34477
     Region          1..314
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mstpsspada pprrripwtv rarrdrslli mvapavllla vfayvpmlgn vvawqdyspy
       61 vgirespfig wanfarvltn plfldavgnt lvitafqlvf ffpvpivlal llnsvlspgl
      121 rttiqsivyl phffswvivv tifqqifgga gmvatrlrea gytgfdlmtn pdtfllllta
      181 qsvwkdagwg iiiflaalat vdpqlyeasv vdgagrwrrm whvtlpalrp viilllilrl
      241 gdaltvgfeq lilqrgavgt dvaevldtfv yyqgvvngdw afaaaaglvk glvslalvlg
      301 anklahlvge agvyqra
//
LOCUS       WP_285108404             244 aa            linear   BCT 25-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285108404
VERSION     WP_285108404.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..244
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27245
     Region          12..237
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mkgqldktsl eivahrgyaa ifpentmeaf rrsldlgads ieldihhtke sipviihddt
       61 lnrtttgtgr irdltladil eadagikfks efagckvpll eealelcser kaglqlelke
      121 hiteeegral lqmlniynli ertiiisfhs nnlmlvrklh ptielgfltd nhvalepltg
      181 lgraacclqy elvlnkpeli reanelgldl avwtvrslei akqlyalgir rmttdipllk
      241 sdiv
//
LOCUS       WP_285108457             287 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paenibacillus
            sp. UMB4589-SE434].
ACCESSION   WP_285108457
VERSION     WP_285108457.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..287
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31966
     Region          1..284
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mklgvstysl ynaiqngqld vlgalewlke qgaehaeivp lgfdllddsq laedirakae
       61 eiglelsnyc iganfaglde aafeaevkrv qahvdvahrl gvklmrhdva srphamtgte
      121 yfeqdfpqlv eacqrvadya lqygittsve nhgfylqase rvrrlviavn rpnfkttldv
      181 gnficvdeps lyavqqnlpy asmvhlkdfy irpanynpge gwfnslhgqh lrgaivgqgd
      241 lpisdiiqvv knngydgyfs iefegmedcl qatriaiana rrlweqa
//
LOCUS       WP_285108541             967 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Promicromonospora sp. MEB111].
ACCESSION   WP_285108541
VERSION     WP_285108541.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..967
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..967
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=102157
     Region          <2..958
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mpvprarlvg rapelgalea aladvrsggs rtvvvageag igktrlldel tsradgahvi
       61 vgqcadsgsg pvpyaalagl lhgivqavgt etavaaagpa agalaavtpq lfapasdaga
      121 dripevltdl ltalaaerpf vvvledlhws dditravavr lartapsgll lllsyrsddv
      181 grahplrtvm aeldrarlat rldlsrlgad evremardll aeparpgtgl dgapgnltdl
      241 ndlvdladlt dladrsegvp fyveelvgfl gtdlpdslrd illlrywnls rqaqalcrvv
      301 aanprvrydv ldavladaaa dgpgheetar eavdarvlvv tdvgytfrha lvqeavyael
      361 lpgerrrlha ayarvleray ppgarsvakl sriadhwwra gvldqalaaa vaghnaaaad
      421 aasaasvalg eralelweqv pdaeavaglp hhellrtvae slrgstrtar alavaheava
      481 ewpdddpvgl aralsdtali agqagsdegp glieralalv epgrddavrg qllilrarra
      541 mldgrskegm esataayeaa taigsdeira valnlrgvsr mqlgdmdgfa eiergravag
      601 dawqglsryy ingsdalltv gdaagaakia eegvsaarry gasegsrvmi egniveaqid
      661 lgdwaeaaaw yertvplvhd svyavylger rtwlamwrgf veqaqaearr raatwdrfgr
      721 leaqirsrva ttraelallr depdealerv saviapddph ipvydlprla vaaraiarlr
      781 qqgrdvddap yraelarcth wptypvwsav feaelgtgpw taaaelpgpa hlrlhalyre
      841 garlleagdr agarttlgta vteaerigag lvvrqaldls traglldggt glagpacaag
      901 appsdagtds ltarerqvla lvaegltngq iaerlfisak tasvhvsail rklgvatrte
      961 aalrasr
//
LOCUS       WP_285108604             386 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285108604
VERSION     WP_285108604.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..386
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=42173
     Region          10..384
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 msqghhndqf atrlihfgse vckhtgassv piiqastfhh ediynpprhd ysrsgnptre
       61 aledyitvle ggkrgfafas gmaaistafl lfsagdhviv tedvyggtyr llttvlnrln
      121 iestfvdmtd itqvqaairp ntkavymetp snptlritdi aavtawaksk glltlvdntf
      181 mtpyhqrpie lgvdivihsa tkflgghsdv laglivthdq dlghqvkvlq nglgtvlgvq
      241 dswllirgmk tlearmkqse esarrlavwl seredivnvy ypglpnhpgr eiheqqssgy
      301 gavvsfdvgs gerakqvlnk vrlplvavsl gavesilsyp ammshaampp evraergitd
      361 gllrfsvgle hiedlladle qalntn
//
LOCUS       WP_285108627             371 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Promicromonospora sp. MEB111].
ACCESSION   WP_285108627
VERSION     WP_285108627.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. MEB111
  ORGANISM  Promicromonospora sp. MEB111
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 371)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Promicromonospora sp. MEB111"
                     /db_xref="taxon:3040301"
     Protein         1..371
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=39360
     Region          36..369
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mdrapglsvr lkltlsytgf lmlagtlvlg vvwafllrfp psagidtlre llnprvfigg
       61 wgprvfvpaa lvvmtfllvf glvggwflag rmlaplaqvt datrraaggs lahrihlpgr
      121 rdefrelada fdamlarles hvaeqrrfaa nashelrtpl aitqtfldva rrdpdgapgd
      181 lverlhavns raidlteall vlsradqrsf tperidlsll aeeatetllp lagrrgvtie
      241 ttgdvapttg sptlllqltt nlvhnaivhn lpdgaagtvl vrtgaapegv tltventger
      301 ltaglvttla epfqrgsera rarradgdhv gvglglaivr siteahdgtl alepragggl
      361 cvtvrlpaah g
//
LOCUS       WP_285108651             345 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: fatty acid desaturase family protein [unclassified
            Promicromonospora].
ACCESSION   WP_285108651
VERSION     WP_285108651.1
KEYWORDS    RefSeq.
SOURCE      unclassified Promicromonospora
  ORGANISM  unclassified Promicromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="unclassified Promicromonospora"
                     /db_xref="taxon:2647929"
     Protein         1..345
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38444
     Region          2..331
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mtstysslar tvrdagllgr ahryyawvla altvalggiv tgfvllgdsw lqllmagalg
       61 lvltqfafva heashrqvfe sgprndrvgr llanvvvgis yswwmtkhtr hhanpnkmgk
      121 dpdiendtia fteegvrqnr glvrlinryq gwlffplltl eglnlhlisv rsllkgspet
      181 lrsrvrelvt itirlgvyva ilfwalppgm afaflgvqla vfgvymgasf apnhkgmaii
      241 padsridfls kqvltsrnir ggrfmnilmg glnfqiehhl fpsmprphli rtaeivrehc
      301 atlgipytet slarsymivv nylnkvglaa rdpfdcpqyt lmrkv
//
LOCUS       WP_285108673             155 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285108673
VERSION     WP_285108673.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 155)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..155
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17588
     Region          66..>131
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 miksldlkeq vtlealwmmq ltayrieanl igfdkipplm esmeqlaqan ekfygwytdd
       61 rvlagavste meapgelqic rlmvrpdhfr qgiarklmdh vlnmdgihtf tistglknep
      121 avtlyeklgf qykcddevgp gvilrtlemk vpsfm
//
LOCUS       WP_285108710             397 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285108710
VERSION     WP_285108710.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616068
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..397
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=44577
     Region          154..291
                     /region_name="Methyltransf_32"
                     /note="Methyltransferase domain; pfam13679"
                     /db_xref="CDD:379330"
     Site            order(184..190,213..214,239..241)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
ORIGIN      
        1 meqlqqlvqh ilqegtlhsa vfsqvrqape egcvkatikp iqlrgevmvq ityhfankvt
       61 henvtaeraa dklfsmlehn frqallrtte aehhvliskk hkvnirtkqt ksvqadlshn
      121 rkkqyilaeg vpvpfltelg imsdagkvla skydkfkqin rflemvadil phlpsdrtir
      181 iidfgcgksy ltfalyhylh vmcerdvmin gldlkedvia hcealarrlq yeglqfsvgd
      241 iaqydgasav dmvvtlhacd tatdaalnka vrwgasvils vpccqhelfr qvdtpvlepl
      301 lghgilkerf salatdavra klldcvgyqt qllefidmen tpknilirav rapesdvqan
      361 wqqytafrdf lqaapylega lhdliaeqgl qgvrspr
//
LOCUS       WP_285108780             719 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285108780
VERSION     WP_285108780.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 719)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 719)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..719
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..719
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=77885
     Region          40..362
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
     Region          383..709
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mklftthkgv tltltailaa atvfpaygtl haaghtatyq aidkaanstn ipgvivtvkn
       61 gdaswsyasg egniernhkv dadsafrigs ttktfvaavv lqlaaekkls lddtvekwlp
      121 glvqgnghng nkikirqlln qtsglpdylt pelrtklltn pdenytpeqv iaigleqkpv
      181 tgwaysntny aimgliiqka tgetyaeqik kriieplqlk etflpgssvd ipkknargyl
      241 dtgnklvdit llnpsfanag gdmistgedl ttffrallgd klltpemkke mltstsespf
      301 gqyglgihqt klpdgnvvwg hgggipgftn faggtedgqh visininvlg dapnhinqii
      361 aaefakeskk eltekekkik hredvkrvmd evvtnkrvps vvagglqdgg rwsyatgtas
      421 yevpsqvesd fsfrigsitk tftasvilql aeekqlsldd svekwlpgvi kgngydgnni
      481 kirqllnhts glasytdenm rditlpqnpf ryysvddlvg lalakppvya pgtgwnysnv
      541 ntilagkiiq kvtgdtyaeq irkrfieplg ltetfvmens shipgkhatg ynmdrsghly
      601 dltemnqswa naagdmvsnv kdlttffsal lggkllnqem mdqmlttvds plgkvglgif
      661 egktpdgqsy wghaggtfgf etrafgplgg khilvtains vgpdataahi kllnkefsr
//
LOCUS       WP_285108835             232 aa            linear   BCT 25-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285108835
VERSION     WP_285108835.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     BTLCP proteins: a novel family of bacterial transglutaminase-like
            cysteine proteinases
  JOURNAL   Trends Biochem Sci 29 (8), 392-395 (2004)
   PUBMED   15288868
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..232
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=27017
     Region          <16..133
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mraylketel lnyshplirq vihsrqwdrm prkeqilgiy nyvrdeilfg ynraddipas
       61 evlqngygqc ntkgvlfmal lravgvpcrm hgfaidkklq kgamkgwyyq lspreivhsw
      121 vevlyegkwl niegfildip yltklqqkfg hctgsfcgyg vatdhfqnpe iywnendtyv
      181 qkegivrdfg iydspdaffs vhqqglsplk ktiyswvvrh lmnrnvsrir qg
//
LOCUS       WP_285108829             307 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285108829
VERSION     WP_285108829.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 307)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..307
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34976
     Region          1..306
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mkidrliami millenevin agtlakklev snrtiyrdid tlsmaglpif ttkgaaggvg
       61 lmksykidkh lftlrdvqtl stslesykql ydhkdivhvl eklncirreg gqvekesrya
      121 vdlslnqgnr alrpllshve tainkeqyma ldyidmdgnv tsrkiepyqv vlkegswylq
      181 afctlkedyr ifklariskl cvlpeafapr dfsplamdgs dwmsqkwvpv tilislsikd
      241 kvierygeen iisvegnscl atfpiindes gydvllrfgd kceiiepsei reafqnyvrr
      301 ilakyek
//
LOCUS       WP_285108926             358 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285108926
VERSION     WP_285108926.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..358
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40751
     Region          27..356
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mklnwkllls lplcitlaga ttglsflais avyksfyfpt ftvfiryldd vigvmllsvm
       61 ytllwfavyf ilftsllirr ilrvtkavqh iaegdltqri kisakdeigq lehninimae
      121 qlsksieeer raeqtktelv tnvshdlrtp ltsiigylgl veqdkyrdel elrhyisiay
      181 ekskrlhlmi edlfeytrms ggmplhlgrv nlselvgqly vhyrypmeqv glqlrmnnad
      241 qslfmmadsl klvrvfenll snamkygtgg davdlnvsvi adeaqieivn ygtaipqqdl
      301 pyvfdrfyrv dksrgeeqeg sglglaisra ivelhngsiw aesnsfqtrf virlplts
//
LOCUS       WP_285108990             284 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285108990
VERSION     WP_285108990.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..284
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32795
     Region          <81..270
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          185..267
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkidvnqlaa hfahipfqve giyryarnpg vphadytdsl pgfvfpltgk tqfqfngtpy
       61 ifspgkvvhg gpkmklahkm fgntdweyil vlyricssel eessfshqhf elltgqsprl
      121 ielimrlwhv ynqrggismf qtemlfrdvl neallcvdnr qnsyeshilf ervsnyihey
      181 ydqsltiasl aeqnnvnrnr lsyvfrrhag mgpaeyllky rinmaqemlf asdapvqqia
      241 qtvgiadpfy fsrvfkkqlg isptqyrekf innpcqfqqa sili
//
LOCUS       WP_285109057             321 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Paenibacillus
            sp. UMB4589-SE434].
ACCESSION   WP_285109057
VERSION     WP_285109057.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..321
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=34982
     Region          10..318
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mdghpligkk llltgasgft gyhacqrlvd lgievaalvr kpapgltavg advficdmqq
       61 eelvqriver vqpnyvlhla gmnavaaswq ypthalhvnv mgtvhllnal rqvpdarsvi
      121 vtsklkaild ptvppahpys yskalqesvv lawsamygld vmlaapsnli gpgpstgics
      181 llgkytaere rghldaafsl sakhdkrdfl dvrdaiaaye ailchgergk tyrvesgqqr
      241 tleevatlyr rlalvdlplh wredgtscsr slagacqtgs gdtdgsldmt spelkawgwq
      301 prrsfehtva dilnyyraqe r
//
LOCUS       WP_285109092             251 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285109092
VERSION     WP_285109092.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..251
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28530
     Region          31..145
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mpawyeqsfg edyllvykhr dmqgaaeevh rmvnwlqlpq gahifdlccg mgrhsvalae
       61 agyqvtgmdl sevllrearl hdgkgsvtfv rgdmrrvple gpfdavvnlf tsfgyfeeda
      121 dnaqviteia rvlrtgcpfi idflnaayve qhlvrqserv dgntliqetr miedgcvkkn
      181 iklttitqdk qqsveettrh ynervklygl lafrrmiada glmldhvygd yegseydaer
      241 strlilvgrk l
//
LOCUS       WP_285109125             475 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285109125
VERSION     WP_285109125.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..475
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51591
     Region          3..449
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mfdrlqewva ifneywylml ifilivvglm fsirtrfvql saigetfrli tgreretesd
       61 kdkgktgvss fqafamstas rvgtgnlagv aiaislggpg avfwmwviai igsasafves
      121 tlaqiykvrd gnafrggpay ymekalnarw lgivfailit fsfgfvfnsv qantvsaafs
      181 dlfgfspwam gatlavlvil tifggvhria kvsavivpim algyigialf vimlnfdrip
      241 evfssiirna fgfeeavagg igaaimngik rglfsneagm gsapnaaata avshpvkqgl
      301 iqsfgvfvdt llvcsstafi ilfsgiptsg elngiqltqh alaaeiggwa hyfigfavfm
      361 fafssligny yygqsniefi tkskgwmfty rvgvvlvvlf gsvakislvw dmadmfmglm
      421 afinlivifi lgriavaalr dyskqrkegk epqfyadtip glkhvecwer rpses
//
LOCUS       WP_285109207             119 aa            linear   BCT 25-DEC-2024
DEFINITION  HesB/IscA family protein [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285109207
VERSION     WP_285109207.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Lu,H.M., Li,J.D., Zhang,Y.D., Lu,X.L., Xu,C., Huang,Y. and
            Gribskov,M.
  TITLE     The Evolution History of Fe-S Cluster A-Type Assembly Protein
            Reveals Multiple Gene Duplication Events and Essential Protein
            Motifs
  JOURNAL   Genome Biol Evol 12 (3), 160-173 (2020)
   PUBMED   32108236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..119
                     /product="HesB/IscA family protein"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=12693
     Region          1..107
                     /region_name="IscA"
                     /note="Fe-S cluster assembly iron-binding protein IscA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0316"
                     /db_xref="CDD:440085"
ORIGIN      
        1 mitiselaie kikemleqee npnmflrvgv rpggcsgfsy gmgfddeetg ddvhleshgm
       61 kvvvdkesip hltgleidyk esgmsggfti enpnavatcg cgssfrtava egkaekcdd
//
LOCUS       WP_285109221             463 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285109221
VERSION     WP_285109221.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..463
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52398
     Region          133..463
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mkslygrivl fsvvivmisf vvglvvanlv yahglknhye qkmeavgqsm ltlleshdgs
       61 stewstrlqt lselgyqlyl vdgqyngtmy grpfkdltls kdviesvlsg kryrgltekn
      121 wnwfvpavfe nkldmavgfp lswngrsyal farpdmvqql qelrqmlail ftttfvvslv
      181 lialktrylv rplnrlmlat gqlekgrydi hvdmarhdei gelarrftrm sqtlkqvdtm
      241 rkqfvanvsh eiqspltsir glaeqlrdrp lppdeerryl niiaeeserl sslsrqlltl
      301 aalergtetl krqpfrldeq lreviirmep dwsakqield leldvtelsg dsgllhqvwa
      361 nivgnaikft dnegiicvtc kyeeadstvk vwihntgavi ekqdlphifd rfykseaans
      421 rnrsgtglgl aiakriielh ggnitvdsss gqgtgfmvkl pvs
//
LOCUS       WP_285109250             258 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285109250
VERSION     WP_285109250.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..258
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27665
     Region          1..255
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mdikgsvvvi tgassgigal taqlvaeaga ipvlaarstd klaqvsariq gqhecvqldv
       61 tnaeevehvm ariietygri dillnnagfg lferatdltl gqfeammdvn ymgtvrctka
      121 vlpsmlerrs grivnvasma gkigspkssa ysaskhavlg ftnslrmela gtgvtvsavn
      181 pgpidtpffd vadptghyvn nikwfmmppe rvakrilrvm ergtsevdlp wlaaagtkfm
      241 qlfprisnrv agrmlnkk
//
LOCUS       WP_285109255             384 aa            linear   BCT 25-DEC-2024
DEFINITION  CynX/NimT family MFS transporter [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285109255
VERSION     WP_285109255.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..384
                     /product="CynX/NimT family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41226
     Region          2..377
                     /region_name="MFS_NIMT_CynX_like"
                     /note="2-nitroimidazole and cyanate transporters and
                     similar proteins of the Major Facilitator Superfamily of
                     transporters; cd17339"
                     /db_xref="CDD:340897"
     Site            order(12..13,16..17,20,52,101..102,104..106,109,128,
                     131..132,135,209,212..213,216..218,221,248,252,301..302,
                     306,310,327,330..331,334..335,338)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340897"
ORIGIN      
        1 mvaavifvai nqraaitsvg plvglirdhl nmsnavagmi stipllafaf fspfapklgr
       61 kfgievvlla alvvltmgii lrslagvayl fvgtsiigia iavlnvllps likqqfpnri
      121 gtmtgvytis snlmgaiasg isipiaiglg ygwqgalglw gilsfisilv wlpqmkrrsg
      181 gksdreevnd nqqinmwrsp lawqvtlfmg lqsmifyvli twlpeilksq gigsdqsgwv
      241 lsilqlsllp ftfiipvise rmsnqrllvv tmftlflmgt lgllygssnl ivlwiiligs
      301 gggiafglam mffslrtena heaaelsgma qsvgyllaat gplffgflhd vtnswttplf
      361 ilvgstvllf ifglgaasnr yiss
//
LOCUS       WP_285109279             245 aa            linear   BCT 25-DEC-2024
DEFINITION  bleomycin resistance protein [Paenibacillus sp. UMB4589-SE434].
ACCESSION   WP_285109279
VERSION     WP_285109279.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..245
                     /product="bleomycin resistance protein"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=27709
     Region          10..128
                     /region_name="BLMA_like"
                     /note="Bleomycin binding protein (BLMA) and similar
                     proteins; cd08349"
                     /db_xref="CDD:319937"
     Site            order(10..12,42,49..51,53,68..73,78..79,82,126)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319937"
     Site            order(33..34,42,53,55..56,70,115,117,121..123,125)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:319937"
ORIGIN      
        1 mstnriggai pifpcrside qldfyqalgf eltyrqakpn lyasvqhrim elhffvlkql
       61 epsnsysmcy vsvpdvdaiy kefcqnlkkt yqkvpskgfp ritklnnlte drrfnlidpa
      121 gnrlligqkh aspepiqsdq yvvphpsrft kafesayrla yakdepaeaa rvldlvfska
      181 gevsaalryk ayvlradiai smdelnlamt fikeagnlal sdqeikevme ttqrlaelkm
      241 tlgqi
//
LOCUS       WP_285109367             203 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Staphylococcus caprae].
ACCESSION   WP_285109367
VERSION     WP_285109367.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus caprae
  ORGANISM  Staphylococcus caprae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Staphylococcus caprae"
                     /db_xref="taxon:29380"
     Protein         1..203
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=22686
     Region          8..201
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mkpdiksrrk elnltleqvg dlvgvgkstv rkwetgdien mkrdkivkla kalrvspsyi
       61 mgieeeqpql etlpvkkipv vskisaglpi yseenlidyi yfatnklnsd keefglkvsg
      121 dsmdkifqdg divvvekdsi vengqlgvvm ingynatvkr iryngdqiil ipesnnsnhy
      181 pqvygkddev kvigrvvasq klf
//
LOCUS       WP_285109439              72 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Staphylococcus caprae].
ACCESSION   WP_285109439
VERSION     WP_285109439.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus caprae
  ORGANISM  Staphylococcus caprae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 72)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 72)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 72)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..72
                     /organism="Staphylococcus caprae"
                     /db_xref="taxon:29380"
     Protein         1..72
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8146
     Region          8..60
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(10,14,39)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(13,38)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(20..21,32,35,39..40)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mkvvlelklk kvlseknmtq kklseltgir qstisdiirg srtvlnfehi sriasqleis
       61 dirkivelkv ie
//
LOCUS       WP_285109581             452 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Niallia sp.
            SS-2023].
ACCESSION   WP_285109581
VERSION     WP_285109581.1
KEYWORDS    RefSeq.
SOURCE      Niallia sp. SS-2023
  ORGANISM  Niallia sp. SS-2023
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Niallia sp. SS-2023"
                     /db_xref="taxon:3051155"
     Protein         1..452
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50975
     Region          3..449
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 menihiyhtn dlhshfenwp rinelfqkrk nwhteagdsv flfdigdhld lshpyteatq
       61 gkanatllei eqfdavtign negitlpyha ldqlyqdasy dvivanlfhk ngsrpdwcip
      121 hkiyetnkgt rigvigltay fhtlyelldw kltlpfqale eqlgllkdkt diiivlshlg
      181 inddeqmaen ypeidiilga hthhifhqgk linnsllgaa gkygqfaghi eikydphakk
      241 vlakqaevye tsklppaene aeyienlyle gkkalseevi slskqltkqe tagllceavl
      301 awcnadiail neglilddln kgpvsyfdll sicphpinpc nvtlsgaelk evltdmkqps
      361 wetlhvkglg frgtlmgkmi srgvqtktng evitywiggk eldpkaeyiv aipdmftfgd
      421 ffpsiyrape kqyflpefmr nilaealqrm av
//
LOCUS       WP_285109623             261 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Niallia sp.
            SS-2023].
ACCESSION   WP_285109623
VERSION     WP_285109623.1
KEYWORDS    RefSeq.
SOURCE      Niallia sp. SS-2023
  ORGANISM  Niallia sp. SS-2023
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Niallia sp. SS-2023"
                     /db_xref="taxon:3051155"
     Protein         1..261
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29553
     Region          1..260
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mklgiiakpt resfkdanqs qldfielcln egqdvaefhk nrnqlvkwkk qygievasig
       61 rwksirldkq ghviqaelek cfqlidvase lecgnfvsgc nyvdelsyyd ncssaiaffs
      121 alidyakpkg vrissyncrk vnfvhnpevw kiihghlkdl gikfdpshsr yfggdylqet
      181 ldwgdrfnhi hlkgslivng trvddppagl dqtdwksfis llrakgytgg lsiephspiw
      241 tgelgksgvn ytiefmkkli f
//
LOCUS       WP_285109794             489 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Staphylococcus caprae].
ACCESSION   WP_285109794
VERSION     WP_285109794.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus caprae
  ORGANISM  Staphylococcus caprae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Staphylococcus caprae"
                     /db_xref="taxon:29380"
     Protein         1..489
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=57383
     Region          279..472
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mnkrftlkff kylaiflsin liltlttiif viffsfkyiy gdfrnldpdy fnlfsnktep
       61 dnhlknlask tntqiyiinn kekviypknk snisikneis kninyahsip fykggyfvfi
      121 yknkshtsik niddvstskl ldsiatqdfn kyrynlnnnq qisfykntnq rpvlgpdevs
      181 tsndikgyel yivlaifiil diilalitay fvskrltkpl ffytdwiknl sngklfkpee
      241 gkikkrskkl ytelneslsn lndqllndri yqnqinyyke kwlnqishdl kspltsiygy
      301 sklikvadtq khyqnliiek aqymnklies lstnfdvets qmksdkqsfn iqqtinklis
      361 slnyskihvg ylfeaktnfy gnklyferlf mnlidnsiqh nkfnpsieie leknesqlii
      421 nykdngegfd kninledvle rsvttkrdkk nhgvgfsvik eainyhegei qilqcydaih
      481 fkitlkeni
//
LOCUS       WP_285109847            1971 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Proteus mirabilis].
ACCESSION   WP_285109847
VERSION     WP_285109847.1
KEYWORDS    RefSeq.
SOURCE      Proteus mirabilis
  ORGANISM  Proteus mirabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Proteus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1971
                     /organism="Proteus mirabilis"
                     /db_xref="taxon:584"
     Protein         1..1971
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=201842
     Region          345..1971
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mniiffekns nekvqlqpha khtitakagd vyqlidsdtq lspldiqahr ksddlilssk
       61 eqnievvikd fwqecqpgeq qcyatlnvld sngvmgqati tqdgpvlehl vagetgtlsd
      121 nddgiglflw vagsigsala iflanrnhgg dnkgneadit apskpgltae ddgsvsidlp
      181 kdankgdsvd vtfededgns ntvtlekgdn gwtssdpeli pdtdnnqvti pndkikdnsd
      241 vtasakdpsg nksddvtvta kpdpvsdmpv lsipevddgy anaeelkdgl qaevtlpagt
      301 vegaeitltv trpdntteti tytvtkddva agkisidipk davqngqnsv dvsitqgnnp
      361 akpgnkvdfa vdgqipgdtd gdgtvdttpv vtipeatdgv nadelkdgvq tevtvpggsa
      421 agdtltltit kpdgstdtve htltadevta gkadvtipad kvtadgnysv taeitdpagn
      481 tsgqgkptdf mvdtqipgdt dgdgtvdttp vvtipeatdg vnadelkdgv qtevtvpggs
      541 aagdtltlti tkpdgstdtv ehtltadevt agkadvtipa dkvtadgnys vtaeitdpag
      601 ntsgqgkptd fmvdtqipgd tdgdgtvdtt pvvtipeaad gvnadelkdg vqtqvtvpgg
      661 saagdtltlt itkpdgstdt vehtltadev aagkadvtip adkvtadgny svtaeitdpa
      721 gntsgqgkpt dfavdtvaps apvlkaeddg svsvdlptda nkgdtveitf edekgdkhtv
      781 tlekgdngwt sdtpalipds ngdkatipad nvkdnsevtg iakdpsgnes dpstvtsktd
      841 gvadapvlti pevadgyana delkdglqae vtlpagtveg aeitltvtrp dkttetvtht
      901 vtkdeaaagk vsvdipkdav qngqnsvdvs ltqgnnpakp gnkvdfavdg qipgdtdgdg
      961 tvdttpvvti peatdgvnad elkdgvqtev tvpggsaagd tltltitkpd gstdtvehtl
     1021 tadevtagka dvtipadkvt adgnysvtae itdpagntsg qgkptdfmvd tqipgdtdgd
     1081 gtvdttpvvt ipeatdgvna delkdgvqte vtvpggsaag dtltltitkp dgstdtveht
     1141 ltadevtagk advtipadka tpdgnysvka eitdpagnts gegkatdftv dtvapstpvl
     1201 naedngsvsv elpgdankgd tveitfedek gdkqtvtmek gdngwtssdp nlipdsqgnn
     1261 taipsdnvkd nsevtaiakd psgnesapat atsktdvlpt vsisvdttsv ndngdkisad
     1321 asvsgeitev patiedkddt tglvytvald yvaaqdvtvt itltndagha sapdystlag
     1381 sqhdgkialh gdtgkvtydg astvtvvipa gsksvsfivd ptmeanqnaf naegmekvva
     1441 titgtsnnat avtdtvnnag asatgviydg npislrnldg dftlkyslss svaengdfgy
     1501 tigvdsgkkd pklttdyndt iyvgyyqdgs etssysnlan sqdngpdgtk tdgnqsittv
     1561 dlgagddlmv irgnmltntr vyagegndtf tmdgmntalr smyagsylfm esgndtvtik
     1621 rtgvtnagqi ylgsgsdtft qgdandqnnt elsglldlgs gtqdksnmpn eylsvyqdgs
     1681 nlslgndnni davtdvntvt iygsvsgeil ggygsdniti tknltgnvsv gdntdtltag
     1741 wiyggatvsm gdgndtvtvt egaynttisl gagddvfdat agvmgdsvsa tlvngedgnd
     1801 tiklgtigkn ltvdagagdd tviltkdydp spignqgyin ggegtdtlvl sgtitvnmat
     1861 ktdegianfe kvdmtvnsel kvdnssqtik ltasdvlgmn anstiyisgd andkvdlgad
     1921 gagglgtfta tatttkatal dgtehtytly ssasganvyi dnniidnggv i
//
LOCUS       WP_285109868             305 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Niallia sp. SS-2023].
ACCESSION   WP_285109868
VERSION     WP_285109868.1
KEYWORDS    RefSeq.
SOURCE      Niallia sp. SS-2023
  ORGANISM  Niallia sp. SS-2023
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 305)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 305)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Niallia sp. SS-2023"
                     /db_xref="taxon:3051155"
     Protein         1..305
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34636
     Region          2..93
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mihikdlrsg lniykalsse irleiltllq rnqslnlndi aqklqlsnga vtmhikklee
       61 sglidittag gkhgiqkicy lnediltiel qdkgvenfye yeikvghycd yaadptcgla
      121 tkdsiigefd npryfadpdh ihaeivwlkk gyleyripny lkknqqfkei qfifeissea
      181 pfynndwpsd iffslnnvel gywnspgdfg gtkgacnpsw wpphlnqyvl lkllrinksg
      241 tfidgcrisd vtiedvglqd hpdiklkfav tdegtvgglt lygrsfgnye qditarilye
      301 evlpe
//
LOCUS       WP_285110015             527 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Pediococcus sp. AC40].
ACCESSION   WP_285110015
VERSION     WP_285110015.1
KEYWORDS    RefSeq.
SOURCE      Pediococcus sp. AC40
  ORGANISM  Pediococcus sp. AC40
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Pediococcus.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 527)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 527)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Pediococcus sp. AC40"
                     /db_xref="taxon:2962679"
     Protein         1..527
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58886
     Region          1..516
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mnilistfmi lvvvgvsnvl aryipkvsgn yvnllagilt gilpvtnqli apfngeifmv
       61 lilapllffe gqltpllrik kklgsilgta vllatvtmii ltwllhvtls iaaplalaia
      121 aiitptdata fdsviegrki rrvirdtlkt eslfndatgi vllqaamlwl qkgqlvigqn
      181 lldffkmmig gvlvgsitai ilmtireyfm rssnnvrssq tliyllspfa iyffaerlgm
      241 sgviavivsg lihngevnrs rfsdprqvhf glqivtfanr ilnsfvfvvl givlvrilqd
      301 nysmmtksfe wlmvgilvyv illvcrycyg rlfvgdqqrq tallfalggv hgtvtlamtf
      361 sisemltpat fnfvvmvetv aiilsmavst vifkillpqd fdeqirqqql aflregmvka
      421 gikklksidl eeavrdnamy dirdqiqant lgdffkkwre intekrvltn lqsvarrral
      481 myafdaeray lydlakrhvv nsdvvyeiys eillseslvl dpqnqmv
//
LOCUS       WP_285110069             783 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Pediococcus sp. AC40].
ACCESSION   WP_285110069
VERSION     WP_285110069.1
KEYWORDS    RefSeq.
SOURCE      Pediococcus sp. AC40
  ORGANISM  Pediococcus sp. AC40
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Pediococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Pediococcus sp. AC40"
                     /db_xref="taxon:2962679"
     Protein         1..783
                     /product="FtsK/SpoIIIE family DNA translocase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=86668
     Region          25..189
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <314..782
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 makakkrrkt trkrkkqqsl ptqnllglay vlvallgyfg rgflgmlvan mfrifvgsls
       61 plgfvllffy glyllfmgre lrfkgasdrv iglsltmigy llwveyrfas glnlesgfva
      121 ravegiersf leqittndig ggllgavfys gthfllseig sailaivlmt vglvilfgip
      181 fdevlsktgl ailwitqrli egiraltrgv wdwweqldft iskpdvkrtp merkppedga
      241 tkqsvksert rveltteepv idgtrgiehp aepkieistn nqrnprkpkn qekqstanpe
      301 vgfesenkln pnyrlpsstl lteipqadqs seydsikknt qilqdtlnsf gvdasvesvk
      361 mgpsvteyei hpaigvkvsk ivgladdlal alaakdirie apipgkslvg ievpnrtist
      421 vsfrdiiesq pahpddplkv pigrdvsgnl veanlvkmqh lliagatgsg ksvminviit
      481 gllmnarpde vklilidpkk velgiyndip hlltpvvtda rkaakalhkv vaemqhrydl
      541 faemnqrnik synefieekn aadggkrpkm pyivvivdel adlmmvasne vedaiirlaq
      601 laraagihmi iatqrpsvdv vtglikanvp sriafavasg tdsrtiidan gaekllgrgd
      661 mlffpmgknk pervqgafis dhdvkeivdf vkqqqtaeyd dqlnvtdqev aeteatdeld
      721 eyypeavelv temqrastsm lqrkfrigyn raariidqle engvigpqeg skprkvyrtk
      781 deq
//
LOCUS       WP_285110344             445 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Pediococcus sp. AC40].
ACCESSION   WP_285110344
VERSION     WP_285110344.1
KEYWORDS    RefSeq.
SOURCE      Pediococcus sp. AC40
  ORGANISM  Pediococcus sp. AC40
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Pediococcus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Pediococcus sp. AC40"
                     /db_xref="taxon:2962679"
     Protein         1..445
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48589
     Region          1..436
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mekfdvviig agpaglglay dlkqagqava vveenrwggt cpnrgcdpkk vlmaaveakl
       61 rsrhlvgkgl enepeidwps lmrfketfte pvssssrqgl vdagitvldg haefvdqhtl
      121 kvgeqrvess qfviatgqrp grlskienea lmqtstdfla mpelpkrial vgggyiafel
      181 aaianaagae vhvihhndrp lkqfpaksvk qfmeqltkqg vqfhlnidvt aieksaegmt
      241 lrddhqfslp vdqvfvtagr vpnmdtlnle qagvetakng imvddhlktt asniyamgdv
      301 vakaqpkltp vagfeaqyla qllthqssaa iaypviptvv ygvpqlakag mevataqkds
      361 qryevkdldl tnwftyrriq dpdaratvvv drqsqqvvgv vtmsseaehv indltwlinr
      421 ggslselqrq ifaypteasd leylr
//
LOCUS       WP_285110347             147 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Proteus mirabilis].
ACCESSION   WP_285110347
VERSION     WP_285110347.1
KEYWORDS    RefSeq.
SOURCE      Proteus mirabilis
  ORGANISM  Proteus mirabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Proteus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Proteus mirabilis"
                     /db_xref="taxon:584"
     Protein         1..147
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=17327
     Region          38..147
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mrflklpfiy wlllncipfi gfelhsgnik pgvffylgal tiitsgiwlf fclyffikhn
       61 tspnphqtpr qlvttgpyki srnpmylgfl disiglffif gnwgflgaal afyfitdryp
      121 ivqeekilse rfpqawrqyc rhvrrwi
//
LOCUS       WP_285110448             322 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Pediococcus sp. AC40].
ACCESSION   WP_285110448
VERSION     WP_285110448.1
KEYWORDS    RefSeq.
SOURCE      Pediococcus sp. AC40
  ORGANISM  Pediococcus sp. AC40
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Pediococcus.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Pediococcus sp. AC40"
                     /db_xref="taxon:2962679"
     Protein         1..322
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37077
     Region          5..218
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mnkglisviv pvynvedliv tcldaiqeqt yknfeiiiin dgstdntvne inemdiscky
       61 rlintenkgi saarnrgvde svgeyitfid sddvvdpdyl eyllslsrkf nadiascqhi
      121 vefknkksin ksfknpshfm sahdwiqdvl vmhkvdlspw gklyksslfd khifpegllf
      181 edtyaipvlv setkgvavgn evkyhykire ksitrskfks syldlitste vmtekilkef
      241 pdlkrearvr kawasvsvms kilksdnsrd ykelvnkirs dllgysssii fykksnwelk
      301 ialilifini nlynfflslr er
//
LOCUS       WP_285110463             244 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Pediococcus sp. AC40].
ACCESSION   WP_285110463
VERSION     WP_285110463.1
KEYWORDS    RefSeq.
SOURCE      Pediococcus sp. AC40
  ORGANISM  Pediococcus sp. AC40
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Pediococcus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Pediococcus sp. AC40"
                     /db_xref="taxon:2962679"
     Protein         1..244
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=27782
     Region          <1..>232
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mlykesdgnf isksiirsnf ptidldglyt itqtcakdhh iylntfdlnn ivlhvviaiq
       61 rirdgyqtqp qlddfywkss rfakdllkev ensqtnvrfs kddleslglv idgsvsrwti
      121 dmkdsisess lrlirvilay vksiykidlt gpdfinqfai hvsrliqrlr dgksiqnpma
      181 nqmkaqsptv yecavlishk ianyvgvpvp dneiayiamh ignaiakqie dkerlrttil
      241 ipdy
//
LOCUS       WP_285110490             639 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Pediococcus sp. AC40].
ACCESSION   WP_285110490
VERSION     WP_285110490.1
KEYWORDS    RefSeq.
SOURCE      Pediococcus sp. AC40
  ORGANISM  Pediococcus sp. AC40
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Pediococcus.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Pediococcus sp. AC40"
                     /db_xref="taxon:2962679"
     Protein         1..639
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=72009
     Region          8..609
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mhdreaeive flihhgvvhy eqiakatkls krsianyldi iendaqpfnl kltrkpnvgi
       61 ylngqlrnkq dflaalklhs gftskearir ylltklldad rsytlnelad dlyvsrstle
      121 sdfkqireff nehhvkikrg angiairasg eqrerlmaki lktywgqnis viqdgngqia
      181 stlklpdyll nffpadlvqa vlagitdfmv tsrleltdyd lqslaihlii ntddkvtndv
      241 eslgpdllpe tsqllnaikk qrtinfsatg lqrvnrylev ivarqknsyq asdvaqtekq
      301 yyqflldkla elepdevllr dlaihlatav drlkkgivid npytdeikmn lpiafdvaiq
      361 lgeaietqyp vqlhdaelgy lalhfeaffe rchlhapiet vvvssagvga sqllaqrlee
      421 rfnnslkvtr ildlatvmkt nlaekmvvst ipiyglkqpv ilvspllppe diqqinyaii
      481 sltknnhsns ffnlldlqli qidsvkksyv tvleeivgsl tkqnilvnnp kilemlvere
      541 kmastalnav aiphiapnyv qksaialwlv pqgvqwlgnt vyvviflalt reqvaasrev
      601 yqilnrmven tafcqqlaqv ataseamehi qkfiqkegd
//
LOCUS       WP_285110523             855 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Pediococcus sp. AC40].
ACCESSION   WP_285110523
VERSION     WP_285110523.1
KEYWORDS    RefSeq.
SOURCE      Pediococcus sp. AC40
  ORGANISM  Pediococcus sp. AC40
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Pediococcus.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 855)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 855)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 855)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 855)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 855)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 855)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18767243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Pediococcus sp. AC40"
                     /db_xref="taxon:2962679"
     Protein         1..855
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=97692
     Region          1..854
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          1..>135
                     /region_name="AAA_27"
                     /note="AAA domain; pfam13514"
                     /db_xref="CDD:433272"
ORIGIN      
        1 mkikrieiyg fgkwqnvtfd lqndlqvfyg lneagkstlr qfiysvffgf aqgrgsnkyl
       61 kyvpkkgrgs agyggaieid yqnhpyrier vkgknggtvt ikdlldqstv tndflsemlg
      121 pidqhtyerl lgfnqsdldd fndlgnrddl rrhilrmgav gseewiqfek dlkkdadkmh
      181 tassrtreld kkikhyekak qhlqddrdql pdyqsakale dqnraelqei rqqisqlskq
      241 tshqqkllda wsnyqkittl rqrvqkvska dlqldlgqis rladqirkve encqrtqqkl
      301 qnlpplaqka ddldqlmdlq aklpvakvnr deldkaqqqq teltnqlael qennsvdlgs
      361 vepmdsatlk qvkqllqeqa qvaakvnqlr svpsrqtast nkstdgnliw gvgvvlaavd
      421 fflpinaiik lillaviilg ayavvkqvdq paqqadnatd dlqtaetngr kideklrqig
      481 gqtgfdvvpa tewvflqnev vnyqqlgqrl aelkqrqavl rekladfwqt akpilqidea
      541 qpqpslnelt kwvteriqqi qqqqsqvqtq kiltqnlaeq qaelkqlrtk faqfaippld
      601 dhfdewlaql tetqkqavrl rdlektvdpa iqtelqkype ltelqaqqsk ltaelqqlra
      661 qeqalvdert qrigeltglk nqidilneqq alaeeetelk dlidewltlq lgakwvdetl
      721 gvatkgrlpl iiqqaneyfa kitnqryhqi efdnddaihv vdqngqayel gelskgtleq
      781 lyisirfafm qafadtvdlp iiiddafvaf ddqrlaetfg llkqiaqqtq iiyfsakkev
      841 yqlvdqrnvv dlnek
//
LOCUS       WP_285110528             244 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Pediococcus sp. AC40].
ACCESSION   WP_285110528
VERSION     WP_285110528.1
KEYWORDS    RefSeq.
SOURCE      Pediococcus sp. AC40
  ORGANISM  Pediococcus sp. AC40
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Pediococcus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 244)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 244)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 244)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Pediococcus sp. AC40"
                     /db_xref="taxon:2962679"
     Protein         1..244
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=27829
     Region          1..239
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mkvlivddep larqelnyll eenpivdqva eadgvveadq yvanehpdlv fldikledgn
       61 gmalakkwkk mavspyvifa taydqyalda fsseavdyvl kpfeqsrine aldrikklld
      121 rqqrdtanyq qkylnprlsi tneertivik knniiyleaq ggtviihvan lplvtskqpl
      181 rkllaeldpq kflqvhrsyv vnldsvfelq psfnhtyqlt lsngikipvs rsyvnetkrh
      241 lgmk
//
LOCUS       WP_285110530             246 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Pediococcus sp. AC40].
ACCESSION   WP_285110530
VERSION     WP_285110530.1
KEYWORDS    RefSeq.
SOURCE      Pediococcus sp. AC40
  ORGANISM  Pediococcus sp. AC40
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Pediococcus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Pediococcus sp. AC40"
                     /db_xref="taxon:2962679"
     Protein         1..246
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28719
     Region          2..146
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 miyqsfavly dqlfdeeqyq nwfeytkqqv dlnqthewle lacgagrlav klakqrqkvt
       61 gfdlssemla laeqhaysak vplelvqgnm ldlaelptyd viscyadsfc ylaneiellt
      121 aftqvhnhlk eggqfifdvi tpyqtgevyp gymfnyqddq qaflwtsyag edqyhvehdl
      181 tfftkqdpts eafyrteeth fertyelyty vgllqkvgfs vvkyfadfgn apveeqttrw
      241 ffscrr
//
LOCUS       WP_285110633             118 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial [Proteus
            mirabilis].
ACCESSION   WP_285110633
VERSION     WP_285110633.1
KEYWORDS    RefSeq.
SOURCE      Proteus mirabilis
  ORGANISM  Proteus mirabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Proteus.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Proteus mirabilis"
                     /db_xref="taxon:584"
     Protein         <1..>118
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          <1..>118
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 yvsiqteyea tepqhestsi vgldagvtkl atlsdgtvyp pvssfkvnqr klarlqrkls
       61 rkitfsangq kqkrkiqrlh thianirkdy lhkvtseisk nhamiviedl kvsnmsks
//
LOCUS       WP_285111349             461 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Leclercia adecarboxylata].
ACCESSION   WP_285111349
VERSION     WP_285111349.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..461
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50179
     Region          3..448
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 msetrsidyi pdnerhghpf sqftlwfggn lqitaivtga lavvlggdvv wsiigllvgq
       61 vlgatvmsfh alqgprlglp qmiisraqfg vlgaviplvl vcvmyvgfsa sgtvlagqam
      121 akllsvsnva gmilfsaiii viavlgyrvi hklgkvasvv gvlafvylfi allmssdlga
      181 iaqnnhfsmp mfllavslss swqiafcpyv sdysrylprd vsgvktffsv fsgtvlgtqa
      241 smtlgvitaa iagsafkghe vsyivglgks eamamviyfa icfgkitftt lnaygsfmsl
      301 ttivsgfrnq ttlsqrsrvi fvvlmvaisc viallsepaf lkhfthfllf llaffvpwsa
      361 isltdyfiis rkavdipalf dprerygywn mfgisvyavg vliqlpfien plyhgsltwi
      421 fadndvswii gwfctaalyy afrrfdrrvl peqtiypatg s
//
LOCUS       WP_285110852             277 aa            linear   BCT 25-DEC-2024
DEFINITION  dimethyl sulfoxide reductase anchor subunit family protein
            [Leclercia adecarboxylata].
ACCESSION   WP_285110852
VERSION     WP_285110852.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..277
                     /product="dimethyl sulfoxide reductase anchor subunit
                     family protein"
                     /calculated_mol_wt=29942
     Region          1..258
                     /region_name="DmsC"
                     /note="DMSO reductase anchor subunit DmsC [Energy
                     production and conversion]; COG3302"
                     /db_xref="CDD:442531"
ORIGIN      
        1 mhelpllift llvqgsvgmt lfltlsarag srvpevkpql lpgmliacia gglglmvstl
       61 hlgyplnaln alrhvasswl sreivfasly laalglctlv mlvrkqlipl llplaavlgl
      121 idvwcmsaiy ahtsvitwsh fntwlmfyga vgvlgavala wlpmlkarsv arerqsvmrf
      181 aaamvgaiva irllaqpdym ahlasaslsg vitlphqpme iftrlsglrl lswtlsavga
      241 llfavsawrq gkfglmvgsl llvlsevlfr fmffcin
//
LOCUS       WP_285111369            1655 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Leclercia adecarboxylata].
ACCESSION   WP_285111369
VERSION     WP_285111369.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 1655)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1655)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1655)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1655)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1655
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..1655
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=179827
     Region          56..1655
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mkpfrlaals lallttitlv gcddsddkts saapatatas tstpapasap akpdnatlek
       61 laaqsmgktl tlldaseiql dgaaalvltf svpldpsqdf artvhvvdkk sgkvdgawel
      121 apnlkelrlr hlepnrnlvv tverdllaln kntfgsdvek aittrdieps vgfasrgsll
      181 pgkvveglpv malnvnnvdv nfyrvkpesl aafvsqweyr nsltnwesdn llkmadlvyt
      241 grfdlnparn treklllpla dikplqqagv yiavmnqagh ynysnaatlf tlsdiglsah
      301 ryhnrldift qslengaaqs aievqllndk gqtlaqatsd adghatlqtd keaalllark
      361 dgqttlldlt lpaldlaefa isgapgftkq ffmfgprdly rpgetvilng llrdsdgkpl
      421 pdqpvklevl rpdgqvartl vsqpanglyr fdyplesgaq tgmwhvrast gdnqqrmwdf
      481 hvedfmperm alniagqkap vspqdpvafd vtgyylygap angnslqgql flrplreava
      541 alpgfqfgdi aeenlsrsld evqltlndeg rgqvssdsqw kethsplqvi lqasllesgg
      601 rpvtrraeqa vwpaatlpgi rpqfaskavy dyrtdttvnq piveensqag fdivyadasg
      661 akkavsglqv rlirerrdys wnwsesdgwq sqfdqkdlie geqaldlaad etgkvsfpve
      721 wgsyrlevka pdeaissvrf wagyswqdns dgtgaarpdr vtmkldkpay qpgetiklhi
      781 aapaagkgya miessegplw wkeidvpteg ldmtipvdka wkrhdlylst lvvrpgdksk
      841 satpkravgl lhlpmgdesr rlsialdnpq kmrpnqilav kvkasvkega tpqkinvlvs
      901 avdsgvlnit dyvtpdpwqa ffgqkrygad iydiygqvie gqgrlaslrf ggdgdelkrg
      961 gkppvnhvti iaqqaqpvel dangegtvsl pigdfngelr lmaqawtddd fgsseskvvv
     1021 aapvitelnt prflasgdna rltldltnlt drpqtlnval taggnlaleg aqpqpvqlaa
     1081 gerttlfipv ralegygege vaaqvsgltl pgetfapqqk swkigvrpaf paqtvntgtm
     1141 lkpgeswhap eqhlanfspv tlqgqlllsg kpplnlaryi relqaypygc leqtasglfp
     1201 slytsaaqln algikgdsde krraaieigi srllqmqrnd ggfalwdkeg peeywltayv
     1261 tdflvrageq gysvpadavn nannrllryl qdpgmmavry sddiqgskfa iqayaalvla
     1321 rqqkaplgal reiwerraqa ksglplmqlg lalklmgdap rsqqaldlal ktprsetqsw
     1381 madygsplrd nammlsllee ynllpdaqst llnvlsqqaf sqrwlstqes nalflagrsl
     1441 qtlsgawqat ttlaegnvrg dkpqvqnlda drlaalqvtn tgtaplwvrl dssgypqyap
     1501 qpasnvlkie rqilatdgss kslsslksge lvlvwlnvta sqnvpdalvv dllpaglele
     1561 nqnlasssas lqesgsevqn llsqmqqadv qhmefrddrf vaavpvnegq pvtlvylara
     1621 vtpgtyavpv plvesmyvpq wratgaasgp livvp
//
LOCUS       WP_285111527             341 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Leclercia
            adecarboxylata].
ACCESSION   WP_285111527
VERSION     WP_285111527.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..341
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38097
     Region          23..323
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mrtikgpgif lsqyiggqpp fntldglagw aaekgykavq ipcnhkaifd velaaesqty
       61 cdeisgklaq hglviselst hlegqliavn paydeafdnf apqavrgnaa arqawatdiv
      121 kkaaaasarl gltahatfsg slawpfmypw pphnearfqe afselarrwr pildafdeqg
      181 vnlcyeihpg edlhdgvtfe rflalvdnhp rcnilydpsh lllqqmdyla fidhyhtrik
      241 afhvkdaeyr pngrsgvygg yqswinragr frspgdgqid fkgifskltq ydydgwavle
      301 wecclkdgdt garegrefis rhiipvsdra fddfaagelh d
//
LOCUS       WP_285111757             356 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Leclercia adecarboxylata].
ACCESSION   WP_285111757
VERSION     WP_285111757.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..356
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38428
     Region          1..355
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 miktrvvivg aglsglyaay lleqagvdyl llegrervgg rivqapgsqa dlgatwiwpg
       61 iqpalnqlla rlgidifvhq etgdmlferg dntpsrhpgf vsspaaarar ggmsrliaal
      121 kqqieparim tgmqvtqaeq rdeqiavtcl aadkqyvsvq gdhlllalpp mlasaiaflp
      181 alpspllqaw rntgtwmaph akyvalydhg fwknnglsge arssagpmve ihdvsepdem
      241 falfgfigvp faarqalgee qlqklckaql vrlfgaeaaf praeylkdwa gdpftatsrd
      301 ltlpaghavp pawptegrws rvvtgiasew shdfpgyiag aieaaeegvk rilnrs
//
LOCUS       WP_285111998             928 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Leclercia
            adecarboxylata].
ACCESSION   WP_285111998
VERSION     WP_285111998.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..928
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..928
                     /product="class I SAM-dependent DNA methyltransferase"
                     /calculated_mol_wt=103682
     Region          22..913
                     /region_name="YeeA"
                     /note="Type II restriction/modification system,
                     endonuclease and methylase domains [Defense mechanisms];
                     COG1002"
                     /db_xref="CDD:440626"
ORIGIN      
        1 mnaveieqai tdlaeqpfdp iefpyaflea fgnkettikr lragasnksd lggvlqtnni
       61 hilaseegqv tqmlallkas patgkakakf ilatdgkdfe aedlisgqtv acafkdfpdh
      121 fgfflplagi stvrqisena fdiratsrln rlyvellkdn ptwgtaerrh dmnkfmtrli
      181 fcffaedtdi fvgkgrftet vaqmstrdss ntheviatlf rtmntsnkdr aaagiprwan
      241 efpyvngrlf sgsndvprfs kiarsyllhv gsldwtkinp difgsmiqai aedeergelg
      301 mhytsvpnil kvlnplfldd lraqldeagd nprmllnlrk rishirvfdp acgsgnflvi
      361 aykemraiea einkrrsepd rasdipltnf rgielrdfpa eiarlalvia eyqcdvlyrg
      421 lrlalaellp lrnenwitcg nalrldwlri cpptgtgvkl hgddlfgspl dqaeidfene
      481 ggetyicgnp pykgsqtqtd dqkndlkaif dkrttnwksl dyvagwfmka vdygsqtdss
      541 aafvstnsic qgrqvetlws lifaakheis faytsfkwan lashnagvtv ivvgisnhvk
      601 gprkifstte dlgtiikevd ninaylvagk stivaqrsfp lsevsvmdfg smanddggll
      661 fdssessrav ndygadicyf rkawgakefi sgtpraclwl nkdsakkail nswisdriei
      721 trkaranspr aatkkladia yrfgevrqdg seriiivpsv sserreylpc gyldvgsivi
      781 apnlalydsp lwnmaliasr lhlvwvatvc griktdyrys ntlgwntfpv pplteknkad
      841 ltrcaedill arehhfpati adlydpanmp pdlraahern devleriyig rrfkndterl
      901 eklfdlytkm iasaapvkgk krkagnne
//
LOCUS       WP_285111782             672 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein [Leclercia
            adecarboxylata].
ACCESSION   WP_285111782
VERSION     WP_285111782.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 672)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 672)
  AUTHORS   Porat,A., Cho,S.H. and Beckwith,J.
  TITLE     The unusual transmembrane electron transporter DsbD and its
            homologues: a bacterial family of disulfide reductases
  JOURNAL   Res Microbiol 155 (8), 617-622 (2004)
   PUBMED   15380548
REFERENCE   4  (residues 1 to 672)
  AUTHORS   Kimball,R.A., Martin,L. and Saier,M.H. Jr.
  TITLE     Reversing transmembrane electron flow: the DsbD and DsbB protein
            families
  JOURNAL   J Mol Microbiol Biotechnol 5 (3), 133-149 (2003)
   PUBMED   12766342
REFERENCE   5  (residues 1 to 672)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   6  (residues 1 to 672)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   7  (residues 1 to 672)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   8  (residues 1 to 672)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   9  (residues 1 to 672)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12109673
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..672
                     /product="protein-disulfide reductase DsbD family protein"
                     /EC_number="1.8.-.-"
                     /EC_number="1.8.1.8"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=72918
     Region          43..136
                     /region_name="DsbC"
                     /note="Disulphide bond corrector protein DsbC; pfam11412"
                     /db_xref="CDD:463273"
     Region          268..662
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 mktffrslwf llfslsaasa avpgwpikpd nlhaqvhvwh dapaegkvrl lldvtpnegw
       61 ktywrtpgdg gfrpaiawep qtktqwhwpr pvrfdsagfs svgydrrvvf pldvaiderq
      121 rlrgkltlsl csnlcvvnsf pldidlasgp sahfaeawdn amravppdtg pvavksvvad
      181 ndtltvkltt pegwsrpdlf adnpaganls ppqteilgdt ltarfsvsdk qgnpldasrl
      241 qqlpllvsng aqsqqlgvdi spsttlwqiv vvalagglil nlmpcvlpvl giklaslmtl
      301 aessrrqtrl rflataagii fsflvlaavi tglrlsgawi gwgfqfqspw fiatmvlvtw
      361 ifcfslagll eirlpsglst rlataggngi ggsflegafa tllatpctap flgtavtfal
      421 aapvhqlwli flvlgvgmsl pwlvisiapg varwlpkpgp wmaklrlvlv llmlgsclwl
      481 msllvkewga ryvlivgglm vafflfrcaq ampnhkenlr slvfgvlfga glyaflapqp
      541 qgkadsplnw qplseaalse aldarkrvlv ditadwclnc rvnevlvlhr peviaalnrd
      601 dvvllqgnws qpsaeieqfl rrygasgipf naifgpaipq ghvlpsllsk dallttltra
      661 npapspdfte ek
//
LOCUS       WP_285112095             464 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Propionimicrobium lymphophilum].
ACCESSION   WP_285112095
VERSION     WP_285112095.1
KEYWORDS    RefSeq.
SOURCE      Propionimicrobium lymphophilum
  ORGANISM  Propionimicrobium lymphophilum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionimicrobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Propionimicrobium lymphophilum"
                     /db_xref="taxon:33012"
     Protein         1..464
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49539
     Region          10..441
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mtndqdikhe elsqelinrw peshpqpsld rikalcnlla dpqeacpviq itgtngkgst
       61 aimidalira mglrtgrfss phlvdvreri cvdgepiske rfdelyeeie pfvqmvdeqk
      121 iggvkmtffe vitamayaaf adapvdvaim evgmggkwda tsvadakvgv vgpialdhmh
      181 llgdtvaeia eeksgvvkhg gvgvfagqqp eaasvltkrc vevgasmkre gidfglldrq
      241 pgvggqliri dtsggpvsdi flplfgahma hnaalavaav eafqggkpln peiineglgn
      301 vkaparlelv hseptvildt ahnphgvkat laglrevfpd npvicvcamm adkqtgkvle
      361 mlsdevdyli attipdnpra dsaadfadqa qgafgagrvr mserpeeala iamgmadtra
      421 ddavvlvlgs vylaglirpr lidennteka swqvdvissk eelk
//
LOCUS       WP_285112287             533 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Leclercia
            adecarboxylata].
ACCESSION   WP_285112287
VERSION     WP_285112287.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..533
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=58090
     Region          1..525
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtvlsvenlt lsyrtgrewr evvhnvsftl grgellafvg esgsgkttta qaiiglladn
       61 arrdagsirl ngedlsqwsa krldslrgar islvpqdpgn slnpvktvga qvgeilrlhq
      121 kigkaecdnq vlalltkvgl sqpeqrmkqf phqlsggmkq rvliaiaial rpdviiadep
      181 tsaldvtvqk rildlldvlr resgtavlfv thdlalaaqr adrllvfrng evqehgatad
      241 vvrapqhayt rqllsdlngq rltiapvsgr plaspairae giskrfalgk ghqlqaldgv
      301 sfavlrgsth alvgesgsgk ttlarillgf eqadsgqvii ddidattlsh earrqlrqki
      361 qfvyqnpfas ldprqtlfei ieeplknfap vskaeraarv esvtrrvalp pelltrtare
      421 lsggqrqrva iaralilept ilvldeatsa ldvtvqaqil allqqlqqql gltylfithd
      481 latvrriahs vtvlrsgqvv ehgaveslfa spqndytrel idaiphfsqk eya
//
LOCUS       WP_285108095             860 aa            linear   BCT 25-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Paenibacillus sp.
            UMB4589-SE434].
ACCESSION   WP_285108095
VERSION     WP_285108095.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. UMB4589-SE434
  ORGANISM  Paenibacillus sp. UMB4589-SE434
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 860)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     BTLCP proteins: a novel family of bacterial transglutaminase-like
            cysteine proteinases
  JOURNAL   Trends Biochem Sci 29 (8), 392-395 (2004)
   PUBMED   15288868
REFERENCE   2  (residues 1 to 860)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..860
                     /organism="Paenibacillus sp. UMB4589-SE434"
                     /db_xref="taxon:3046314"
     Protein         1..860
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=96950
     Region          <117..212
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mntavtygid qmvleqklai kmewaqhrrq alfgildhhl teeetillkv lyaymplndl
       61 adydgaffld hvrqalkvre elpwgstipd siflnfvlpy rvnnenidds rkviygelae
      121 rvrglsmyda iletnywche ratyigtdmr tvspltlmrt algrcgeqst lavaalrsig
      181 iparqcytpr wahcdsnhaw veawadgrwh flgacepepk ldegwfrsps rramlvntrv
      241 sadyngpeei csdhpwyaei nmldnyapvk qitvqvvnak gapveaevhf qlynyaefys
      301 ivtkktnaag qvtlktglgd lllhvrneqg fgvrkisvtd tdtfevklha steqmlvqew
      361 smvpppvttd meecvvseea krrhearvke gtairaafeg tfyseqqaaa laqqlglaad
      421 rvwvvlekak gnsgqiaafl lqecprygdl plrlleslrd kdladtcqst ladhlysaaa
      481 yadqgvpagl fdpyvlcpri hfemiapyre qllqslseve rheyisdpql lithikdsil
      541 ivqdvdrytg mmtpagvhrm kvtdrmsrei yfvamarslg iparleplnl saqywlneqw
      601 qearfetvha pletsmpars sivfvaaeqh aelaayqqtf tiarledgmy rtlsipfgek
      661 dvygkpyevl sgsyrvttgt rlsdgtvlvr csyftvkpne tvhttlifrq enesvpvlge
      721 vsedtitcis agvmtelpqa giilawldpe repskhllre mrelqlelds cgsavlllar
      781 neeavssiam kglpaaatai rdssyeglkl iqedirmikg sefpivvvld akrhlryvse
      841 gyklgistei vktvrnmkie
//
LOCUS       WP_285112315              88 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Leclercia
            adecarboxylata].
ACCESSION   WP_285112315
VERSION     WP_285112315.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..88
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=9609
     Region          24..83
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mhtafsspss apaaplmpvs daiherfirl pevihlcgls rstiydlisr eafpkqislg
       61 gknvawaqse istwmadria ernrdcda
//
LOCUS       WP_285112321             401 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Leclercia adecarboxylata].
ACCESSION   WP_285112321
VERSION     WP_285112321.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..401
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=46525
     Region          2..386
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 maltdiqikr akpqdkpytl ndgqglslli npdgskgwrf rfrfagkarl msfgsyalvs
       61 laearekrdt arkqvangid pveerkaqkl aqqlstensf eticrewhtn kadrwtvayr
      121 eeiiktfeqd vfpfigkrpi seikplelle vlrriekrga lektrkvrqr cgevyryaii
      181 tgraeynpap dlaialavpk qkhhpflsae elphfirdle gytgsiitrn atkivmltgv
      241 rtqemrfatw eevdleksiw eipaermkmr rphivplstq vidlfkqikp itghypyifi
      301 grnnrskpis kesvsqviel lgykgratgh gfrhtmstil heqgfdstwi emqlahvdkd
      361 tirgtynhaq ylekrlnmlq wysdllypki nfdwnnkrip s
//
LOCUS       WP_285112327             463 aa            linear   BCT 25-DEC-2024
DEFINITION  nucleobase:cation symporter-2 family protein [Leclercia
            adecarboxylata].
ACCESSION   WP_285112327
VERSION     WP_285112327.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10795438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..463
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48459
     Region          29..457
                     /region_name="ncs2"
                     /note="uracil-xanthine permease; TIGR00801"
                     /db_xref="CDD:273276"
ORIGIN      
        1 msvnaveqqd aqpiaqphns eliyrledrp plaqtlfaac qhllamfvav itpallicqa
       61 lglpaqdtqh iismslfasg vasiiqikaw gpvgsgllsi qgtsfnfvap limggtalkt
      121 ggadvptmma alfgtlmlas ctemvisrml hlarriitpl vsgvvvmiig lsliqvglts
      181 igggyaamad htfgapknll lagvvlaiii llnrqrnpyl rvaslviama agylaawamg
      241 mlpqssaatd splivvptpl yyglgidwnl llplmlvfmi tsletigdit atsdvseqpv
      301 sgplymkrlk ggvlanglns fvsgvfntfp nscfgqnngv iqltgvasry vgfvvalmli
      361 vlglfpavsg fvqhipepvl ggatlvmfgt iaasgvrivs replnrraim iialslavgl
      421 gvsqqplilq fapdwvknll ssgiaaggit aivlnlifpp ekn
//
LOCUS       WP_285112385             484 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Propionimicrobium
            lymphophilum].
ACCESSION   WP_285112385
VERSION     WP_285112385.1
KEYWORDS    RefSeq.
SOURCE      Propionimicrobium lymphophilum
  ORGANISM  Propionimicrobium lymphophilum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionimicrobium.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Propionimicrobium lymphophilum"
                     /db_xref="taxon:33012"
     Protein         1..484
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=53241
     Region          11..456
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mskenentvt cikiclepnk aqraqfasfa gsarwaynfa laikvdyqkr wfearkqfve
       61 sgldekaagk kaseqvgrmp nymsiatnew tqlrdevcpw ypevprrvfv ggfqradaaf
      121 knwfdsksgr rsgaavgwpk fksksksres fviasdiqps fvtnlnryik tgeladmdyr
      181 hikvpkcgev rltpgsagql rqlgrtmlae aktgelitri tsgtisrlgd rwyvslvisg
      241 pfvpdaistk rqrrngvvgv dlgsgrfyat tseglsiinp kfvskyeqel aranralakt
      301 akgsaarkka larlrrvhar salardgfsh qvsawltsqf agvavekfdl asmlasakgt
      361 vekpgknvgv karfnahlad vgiastidkl lykgkrdgcr vqvvntldns sttcakcght
      421 cvcgpeqrtf tcpdcgysap rqlnsaqyir qlatvgfdel gldmkakltp dtskrpiafm
      481 tsah
//
LOCUS       WP_285112604             756 aa            linear   BCT 25-DEC-2024
DEFINITION  HelD family protein [Propionimicrobium lymphophilum].
ACCESSION   WP_285112604
VERSION     WP_285112604.1
KEYWORDS    RefSeq.
SOURCE      Propionimicrobium lymphophilum
  ORGANISM  Propionimicrobium lymphophilum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionimicrobium.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 756)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 756)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Propionimicrobium lymphophilum"
                     /db_xref="taxon:33012"
     Protein         1..756
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=83948
     Region          19..738
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 msseidtvng easasdaadi ltkelakeqk hvdrvyeqld vltesarnve aeaeakfktd
       61 rsdwmreedg taiferdafa yqaakrlavl daehdglvfg rldlteeeir yigrlgvrdd
      121 dyeplvidwr apaaepfyra tasnpmevvr rrvlrcrgek vvgieddlld eragddlvvi
      181 gegalmaslk rargphmkdi vatiqaeqde airapyqgvt lisggpgtgk tvvalhraay
      241 llythrkrle qggvlvvgps dlfvnyiarv lpslgenavv lravgdvpgd vlgftsarae
      301 naqaailkgs mrmlpvlraa vneplvsgpe lnrlrvsikg evltleqdel nkirrailln
      361 nklnqakkaa qqalldalwa klpeeiaall didreifdek itdqasytmf lnawwpmlsp
      421 eqvlarladp kflnsiahgh msdeeegvlt dslthargyv pdsgqprpdw smsdmallde
      481 lahmlgpvpa seqddpllfl dsvadaneiv tisdklrddr eidetqprny shvlvdecqd
      541 itpmqwrmlr rrgpqaswtl vgdpaqssyp vqeesdrair dligrapmre frlstnyrsp
      601 teimdlagkv vraaypdavl pnsvretgve plllsvipde lagelkkqim nlsqqvagsi
      661 slitapddyr kfielveqmk lpeevdqrvv vitalqskgl efdativisp ddiveqtpgg
      721 ervlyvaltr ptqrlvtidl sgkhtarwrr tltevn
//
LOCUS       WP_285112711             295 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Propionimicrobium lymphophilum].
ACCESSION   WP_285112711
VERSION     WP_285112711.1
KEYWORDS    RefSeq.
SOURCE      Propionimicrobium lymphophilum
  ORGANISM  Propionimicrobium lymphophilum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionimicrobium.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Propionimicrobium lymphophilum"
                     /db_xref="taxon:33012"
     Protein         1..295
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32991
     Region          19..288
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mpkttselld lldltetspd vfsgsqpdti mqrtyggqvm aqaivaaykt lpedrrmhsm
       61 hafflrpgna hvpitykasr lrdgrtfstr rvdasqekdi fgmsasfhhm eysrlnhqde
      121 lpsptpppek cprlvdfmna aygehpmwhe wdaldvrfag dsagngspkl pkipvhshks
      181 hmrvwiktqd klpddnaihq ailayasdlt llsvttvphs vafmstkiqt asidhamwfh
      241 rqgradewll ydmispsash algygtgrlf qdgkliasca qeglvreven rpils
//
LOCUS       WP_285112776            1209 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Leclercia adecarboxylata].
ACCESSION   WP_285112776
VERSION     WP_285112776.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 1209)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 1209)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13208672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1209
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..1209
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=133166
     Region          410..>446
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Region          <432..>446
                     /region_name="Spore_III_AA"
                     /note="Sporulation stage III, protein AA; cl41941"
                     /db_xref="CDD:477873"
     Site            434..440
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:350691"
     Region          <624..1197
                     /region_name="DNA2"
                     /note="Superfamily I DNA and/or RNA helicase [Replication,
                     recombination and repair]; COG1112"
                     /db_xref="CDD:440729"
ORIGIN      
        1 mktrqyaqks ifdleaifeq srnnvseleq llseltfrnt arartltski eqsltalsdr
       61 sevamsasnp stcnpdsasi qfsqamphsa paaveqlqpk aipdtamreq fdkgqidlgp
      121 lpffspsdka ndarailaaw talealspqg ykrpedmatg drsrvaller gvpwgpnars
      181 kpsyklyfev vlgsialdka tdelvkvfge deersrpdgk kaaigsilid kegyvledkg
      241 vavssfawal kpaldlklgs lgnwpnvepr iiehldrivr rhnedgepip idlnvvhnay
      301 kwlvsqfsvp ehlvepptfa ikvfhhfkak alpepsllns fyledlgeat klletgkaga
      361 glrrymgigr peqkidvlsp isavepfvap slmpqarwps kgghplvllq qaavnaarae
      421 lndapgiigv ngppgtgktt llrdivvgci ldratamcrf nkpqdafstt geklafgsna
      481 flhfyklhas lkgheivvas snnkavenvs kelplkeang rheqiayfrs isdlianpkr
      541 vgyfeaeaeg dipsdpvetw gliaaalgks snrgafqqgf wwnedggflt ylkaarginv
      601 mreikdertg eiidrvmpsv vvnerpstne adaaaawlka rtaflklket vdaeiasiee
      661 mrrdiqalkg aitelqraeq rrpslneave eahqiaescq rehekaksqi eqdkimldsh
      721 lagrpgffsr lfataawksw rstlqmlsst lqqsvlraqe tggalelara ewsntesqlq
      781 qlnqeisskc qavsklkate aearnrmgdr vvderffere heaihltapw lpdeihrlre
      841 dlfaaaltvh ktfidasasr lqhnlgllms gmvagafqss ahrellpdlw sslfmvvptv
      901 sttfasvrtm fgdlppesig wllvdeagqa vpqaavgaim rakrcivvgd plqippvvsl
      961 peklnaeicr ffdidqiews apaastqtla dqasrfkstf vmdvgdrevg lpllvhrrcq
     1021 npmfdvsnsi ayakqmvhav gpkrpgsigs algrsrwvdi ngdaetkwcp degeavirml
     1081 kelaasgitn pdvfiitpfk iveqnmrrrl dretdllraf gvkldewsrd rvgtihtfqg
     1141 readtvilll gapkasqlra rqwaasppni invavsrakq nlyvvgsaas wsgagtslqv
     1201 lqrhlaqla
//
LOCUS       WP_285112831             108 aa            linear   BCT 25-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Propionimicrobium
            lymphophilum].
ACCESSION   WP_285112831
VERSION     WP_285112831.1
KEYWORDS    RefSeq.
SOURCE      Propionimicrobium lymphophilum
  ORGANISM  Propionimicrobium lymphophilum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionimicrobium.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 108)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Propionimicrobium lymphophilum"
                     /db_xref="taxon:33012"
     Protein         1..108
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11893
     Region          4..107
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mdndeilarl nereedlkaq laelakpvdl dgaigfgkri gdgtiqavqa fndsfsaqnl
       61 sdllaqvrra kqklaedtyg kcdecgeeig kerlefrpws skcvkhav
//
LOCUS       WP_285112900             685 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Propionimicrobium lymphophilum].
ACCESSION   WP_285112900
VERSION     WP_285112900.1
KEYWORDS    RefSeq.
SOURCE      Propionimicrobium lymphophilum
  ORGANISM  Propionimicrobium lymphophilum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionimicrobium.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 685)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 685)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 685)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 685)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Propionimicrobium lymphophilum"
                     /db_xref="taxon:33012"
     Protein         1..685
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=74346
     Region          1..>414
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mhafelilvl ftivlvssil dqllsrlslp lvqiamgvvg alvigepfqm tidshlflvi
       61 fiapllydes rrvskralmr nivgilslai glvvasvfav gfalnwisps iplaaglalg
      121 aalgptdava vsalskstkl terqtallsg ealindasgi vsfqfavgaa vtgifsvana
      181 agafaasfgg gllfgvvmgv vvlsilrgvr giglestvfh vtfeiltpfv ifllaegigv
      241 sgilavvaag lmialapnra taytarvslv shgvweviaf ilngivfvfl gshlpsvfth
      301 swedatnpls laglvlvlta ivvtlrfvwv lildwhmmri grllgvhnyr qllkgalttt
      361 lggpkgavtl siamtlpvtl tndagvpird eliflasgti lctlllanfl lpvlsptesk
      421 gqsqertnqv rtmvlsnlve alndnfgtry pmavsmligr ynheiaeltm skdfdaairr
      481 lrlnlllkqr ewlsdllaqg kisnvvfesi gqtidrliqv anhkyssrig lrrvwmrivh
      541 alkeirasrs qhdevttpqq lrdarialsr rsvdylnsle pkpqipheai dyllgdnqrl
      601 lamlqrsaqy deaisgkdhq pakvgirarr tlaeqldlme aealrlelgc vqqlleddli
      661 traeaselrd eiyllqmnls dyssh
//
LOCUS       WP_285113127             475 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Propionimicrobium lymphophilum].
ACCESSION   WP_285113127
VERSION     WP_285113127.1
KEYWORDS    RefSeq.
SOURCE      Propionimicrobium lymphophilum
  ORGANISM  Propionimicrobium lymphophilum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionimicrobium.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Propionimicrobium lymphophilum"
                     /db_xref="taxon:33012"
     Protein         1..475
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50771
     Region          115..467
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mignkirgwv adllaqcrsl pgritqiial siavglllvg atsfftakss iydqmdgela
       61 daaidasiyl qfdldgmagi nstalntanl smvlvrsdgt lrgnsgasvp vktgavelai
      121 artqmgisar tvlgvdgqky rqvavpmtts ndklavviar plsqanavig dmsfnifwvs
      181 alvlvggivv gyfasrslmv plntmakavs rvtetdelvp igihsddeig mlsrnfdtmi
      241 hslsssrerq krliadaghe lrtpltsmrt niellvadqk sgmlppgakd eiladvsaql
      301 aeftslvgdl vqlsrddavn vsrkvldfae vvtdavtrak rrgphitfdv kleplfivge
      361 qdtlgravtn lldnavkfsp reghifvrlh detltiedeg pgiaeedldn ifdrfyrsdk
      421 arntpgtglg lsivkhtiea hggsvwasns nstggakftv vlpaadeeel aelgq
//
LOCUS       WP_285113193             123 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Propionimicrobium lymphophilum].
ACCESSION   WP_285113193
VERSION     WP_285113193.1
KEYWORDS    RefSeq.
SOURCE      Propionimicrobium lymphophilum
  ORGANISM  Propionimicrobium lymphophilum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionimicrobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Propionimicrobium lymphophilum"
                     /db_xref="taxon:33012"
     Protein         1..123
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=13607
     Region          <1..108
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mmialrtftp vvlasiyala iaicassdie irhsplrnrl lvtggewsya fylvhatviy
       61 girgitgvvp wgaatiplwi tiflisllaa gilhllvekp lekklrrwgd qvfcpknhqq
      121 itq
//
LOCUS       WP_285113212             536 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Propionimicrobium lymphophilum].
ACCESSION   WP_285113212
VERSION     WP_285113212.1
KEYWORDS    RefSeq.
SOURCE      Propionimicrobium lymphophilum
  ORGANISM  Propionimicrobium lymphophilum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionimicrobium.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Propionimicrobium lymphophilum"
                     /db_xref="taxon:33012"
     Protein         1..536
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58466
     Region          1..428
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mkltrikven hkrladldie vrdhlvlvga ndvgkssllr cldlllgast aqlysrisse
       61 dfrdsdqpfv iegtltkfsd adkalypdei hidpntnssr lvvrlvatvd enetvsinri
      121 apeggtgrql srdqvlglgw kflsattqir dlqggrkstl ddilqaidlg dekatfedit
      181 anleealcns kvlkdlrdsi seqlskalpd kvaqddlafv pgaaaendvl sdvrlqvskh
      241 geshdlseqs dgtralyaia lydlmsvgan mvgidepeih lhpssqrsla rllkegenqk
      301 iiathsaniv gtfdpdsivv ireggkavqp kagflsgder tavrlwvrnl iealtarrvi
      361 avegisdrii lehianltdr nldrlgvsli eaggvgnmda feklfgkngf riplsvlida
      421 daedrvaksl gvkvedlkrr svsvsqrdle deyvralgpe avwkaieekn lfsdnvlknc
      481 katgpggsrt eddvagfcrn kalykvnaal svlnlftptn arnmssienl lseige
//
LOCUS       WP_285113803             375 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285113803
VERSION     WP_285113803.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..375
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40003
     Region          127..369
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mlgagllsll awwavrrvgv ayaravvapr pgaltrihss tdttvtlead rrtlhrgqfg
       61 lwfgsaghav vgpakahdrt tgtvtrellt vsgdlasarr ghwtahvhpd paslrrchre
      121 iglevaggta pawliepsep grpapvwaih ihglnttrvt vlrsvpatda lgipslvvsf
      181 rgdgeapdap ggvsalgqte wedveaaiay aldhqaqriv lvgwslggai alqlaersvh
      241 raaidrlvlv gpvtdwraai rhtavdqgva gwaaplaira lgdrrmsara glpepivfdr
      301 ldwvrpgrla vpalvihsdg drvvpfsssv mfamanpqlv rlvelppaeh gweynvdpaa
      361 fnraiidflq aprdg
//
LOCUS       WP_285113859             335 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285113859
VERSION     WP_285113859.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..335
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35404
     Region          30..322
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtdvttgtgf pastpaagda arlrsalaav raevgkavvg qdgavtglmi allarghvll
       61 egvpgvaktl lvrslsqals ldtkrvqftp dlmpgdvtgs lvydaqtggf vfregpvftn
      121 illadeinrt ppktqsalle ameerqvsvd gvsrrlpdpf ivaatqnpie yegtyalpea
      181 qldrfllklt levperelev evlrrhaagf nprdlagagv spvlgaaelh aaresaaavg
      241 anpdvlayiv dlaratrnsp svrlgvsprg ttallaaaka wawlsgyesi tpdhvqamlv
      301 pvwrhriqlr peaelegvga dailrsilqq vqvpi
//
LOCUS       WP_285113876             429 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285113876
VERSION     WP_285113876.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..429
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=46781
     Region          176..409
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 matprrtlvp savteflgsa rfnstlalva vitgfsthai raligwpgli galavlvvla
       61 alsfaaqwrl iewhgllpis allfvgwcai stfwsqyqwa tvagvfyqli faflavyial
      121 vrdaiqivrv vgdalrfllt vslslevlsg llidtplrfl giqgniaagg piqglfgsrn
      181 qlsivaliaf vtflvelrtr svrppvaafs itlaglcill ahspviaavs vvvglatlal
      241 yllrkaapqq rpyfqwglai ltlavlvvay iyrtrvidll naradfqvry qlwiqiweli
      301 pvqqtvgwgw vgswptdlyp ftaiqaatgv yhadglnayl dvylqvgiig lllfvalial
      361 afgrswllas nrrsvvyawa plvlvallat svfessilie agwmvlvict vkasqgmswr
      421 lrlphrdqs
//
LOCUS       WP_285113916             625 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285113916
VERSION     WP_285113916.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..625
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=65134
     Region          1..>323
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
     Region          <70..592
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
ORIGIN      
        1 mevglvigvl avltiaaatt igpklgiasp lilvavgilv sllpfvpale lqpewiiagv
       61 lppllysasv smpamnfrre fgaigglsvl lvivssvllg lffawvipgl glawgvalga
      121 ivsptdavat givkragvsp rvvaileges llndatalvl lraaiaaaaa asftlgavtl
      181 sfvysvvvai vfggvvgwln lrvrarvkda tvntvisftv pflasipaea lgasglvaav
      241 vaglvtgsra prvlspehrl sdaqnwrtve lilegliflt mglelfgilq kvqndhsgva
      301 paigvaagal vltilvragf vapllallar rsrrrqnmrp qlqqlqehlt dpealqrgia
      361 arlagtgqra ltpadteade sgagsgmdvp aegdvppdvd aaaavvamdp llgprgegpr
      421 itpkqaerrr rrlirrgipt venltrfgtr lrrviadiey ftgaplgwre gtiviwagmr
      481 gavtvaaaqs lpsttpgrsv lvliaflvaa gslllqggtl glvlkavkps radpaaerde
      541 rrrlmellye agksvpqpkt tertaeafae hksarlarlr aqraalldar ddgtfsadvl
      601 agalsnldad eisidlkgdp teatg
//
LOCUS       WP_285113921             100 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285113921
VERSION     WP_285113921.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 100)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 100)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 100)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..100
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11137
     Region          1..97
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtdyptpdia dvqlvdvlra vadpirlqiv rvladgrphp ksmtewgvdv qkstmahhfk
       61 tlreagvtrt ivsgrtheiq lrrdeldqrf pglveallgd
//
LOCUS       WP_285114107             575 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285114107
VERSION     WP_285114107.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 575)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 575)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..575
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=62308
     Region          22..571
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 melgvyavia vavivgvaaf arrlgvaapi ilvivgvtls flpgvpeiqi ppeiildgll
       61 ppilyaaais vpltdfrrnl apiaglsfvl viitafasgf llytmlpdln laaaialgai
      121 isppdavaat sigrklglpp rvltvlegeg lvndatalvl lrtalaaalg alvtpwagvv
      181 dfvsaviial vvglvvgfvs vwvrsklndp vldtalsvvv pfaafaptea lhgsgvlavv
      241 vtglytghaa prqfsaqari sdqinwrtiq fllengvfll iglelrtlvg dvehpevlsv
      301 wnaiglglia vfaliiirfi livplilglr rraehaersv lrewlmisyy rdhpvryrwq
      361 avrkqraeqr yerhrgdlee yrqeaigwks givlgwagmr gvvtlaaaqs lpgsipyrpq
      421 liliaftvaf vsivlqggtl pwliralslq gadaredrrl lakllddlse aglavlddpe
      481 aaadtatpid pevvervrqs sylraesawe rallsdtpqe srphhvyrtl rlavveaert
      541 rlllerargs ypsrvlteaq slldleetrl rsrar
//
LOCUS       WP_285114137             476 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285114137
VERSION     WP_285114137.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..476
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50107
     Region          6..472
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mseartgteh fvdastqpet rgievisdse rhgrardlff vwaapgvsil nftigatlil
       61 lgleiwqafa vivvasllwv fpgliagsgp aagtsgsvvt ramygiignk lfvafvgwfi
      121 gavflsltwl assfmgadll rriglddpvw vpigvtivvs aitilvaifg hglilriypv
      181 maivlfaifv lvsafilptv nwqytapepl ggvplwsals igftilastp lsfinspdia
      241 rylprstkps hiaaatafgg aipfvvftav gvllatglka safdagidva lfdllpgwlg
      301 pllvigvvvn tialnamtty tssmalqaig frlkripaai ivglvgtalt iylvlsssll
      361 eaanlmlqfl vivsgpamai yavdviqrry vydsvdlfdt grggrywftg gwsipgival
      421 llgglvtalc lstdvwtgpi gqalghvdls vpagmtvsaa vyallsrtrl gkegrl
//
LOCUS       WP_285114262             112 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285114262
VERSION     WP_285114262.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..112
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12651
     Region          1..93
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mfvstfifea kpydddfhrl ndeiaerara ipgflgeeaw tneetglsse vyywesreal
       61 hqligmdthr eakrlhdrwi gayrivisev istygqpgla lehvpaansg la
//
LOCUS       WP_285114333             314 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285114333
VERSION     WP_285114333.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..314
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32951
     Region          8..294
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(37,241,244)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(181,212,239,242..243,246)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mnddsvpral vmgeslvdvv erhgspravh aggsplnvaf glarlgihvt fateygadph
       61 gsliadhlhs agvdtlntsh gnptstatar idpegaahyd fsldwdfapt alppaelvht
      121 gsigalrepg atavrrhvna lgddtlvtfd pnvrpslmpd reqtlksvdw ysrhahlvkl
      181 sdedahwlfp gwthrtvldw ildrgagiav ltrggdgsll rsraaeieie asaahvvdti
      241 gagdaymagl laglmgaepr gqlqrgnvsd ivlrsigela srvaaltvar agampptlde
      301 iqalqtvpaa rggs
//
LOCUS       WP_285114314             446 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285114314
VERSION     WP_285114314.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 446)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..446
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48263
     Region          35..441
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(145,147,296,298,327..329,372)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrklrrvaai aaaaallagv tacsstgsgs nekvtlqywm wddtqvpayq qcaqqftken
       61 pditikisqs awgqywtnls tqiaagsapd vwvdqasyyp qfvqdkqivd iqpmvdkdkv
      121 dlgqyvdgla dlwkvgdary glpkdwdtmg lvynkadlka agideaslsd ltwnpndggt
      181 feqtiakltv dksghngldp afdknnvkvy gflpewadgs qgqngwgnfa ystgwtyadk
      241 npfgtkfnyn dpklaktvqw ladlsdkgya pkldvqstla rsevlanngg alttlgsfnl
      301 asykgktdqf gfaplpvgpe grksaingls daiyagskhk dqawkwvkyl assdcqntva
      361 atgvvfpaik easeksaavr ekdglnakvf ldeqqakdgt fiipisyhgt eisqivqdai
      421 qsvalgqqda ksalgkandq vnglfk
//
LOCUS       WP_285114503             276 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285114503
VERSION     WP_285114503.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..276
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30401
     Region          54..157
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 msdytdanra nwddrasaha drgphgyrvs qyiddreals evvrfdlprl gsveglrvah
       61 lqchigtdtl slarlgarvt gldfsevsia earrlvadte ddvdfvvsdv ydaasvlepg
      121 sfdlvytgvg alcwlpriqp waavvaalla pggslflreg hpilwtmder idddlhlrfp
      181 yfeqtepiew dsdatyvetd rpitatrtye wnhslgeivt alieaglrid llqehdsvpw
      241 ealpgqmvar pdgefalgal dgvaplsftl ratkpa
//
LOCUS       WP_285114592             236 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285114592
VERSION     WP_285114592.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..236
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=24771
     Region          14..99
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 matrsprgfg qyggvarave rvgerwalli vrdllagarr ysdlkaglpr iptnilsdrl
       61 kelqlagvir rvptvrggye ltalgrglep vvlalerwgw aapgdaadgd vftadalgit
      121 lraafrsdva aafppteyll hageasvsav vaggaldvmd vgpdalpqpq grlsvgsted
      181 vlefqvavad ldrllggdvs plevlagrse lverfgstfr fdplpgmgvd aersaa
//
LOCUS       WP_285114606             321 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285114606
VERSION     WP_285114606.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..321
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=35144
     Region          42..302
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mtavlpapra sgsgaapdae tvyrpagpld magtlgllgr gpydptttwd lrgmwrtwrt
       61 pegaatlrih rrsadgsiaa aawgpgaews iaavpellgk sddwsgldvs ghpllrdsrh
      121 rnpgirlart grmleallpa iieqrvtsle ayrswsrllr wygepapgpa pegmrvtptv
      181 qqwrgipswd whragvdprr araiqavlav assleraver aesltaaeta lqtipgvglw
      241 taaetlqrsh ghpdlvsvgd yhlahqvgea ligrrvdddg mlellepyag hrqrvvrlif
      301 asgfrferrg prvtlqdhrw h
//
LOCUS       WP_285114756             212 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285114756
VERSION     WP_285114756.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..212
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /note="Members of this family of hydrolases with an active
                     site Cys residue belong to MEROPS family C26.; Members of
                     this family of hydrolases with an active site Cys residue
                     belong to MEROPS family C26.; Members of this family of
                     hydrolases with an active site Cys residue belong to
                     MEROPS family C26.; Members of this family of hydrolases
                     with an active site Cys residue belong to MEROPS family
                     C26."
                     /calculated_mol_wt=22187
     Region          4..194
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 mtrvlvidny dsfvytlngy lrelgaetev vrnddvtaad lpaklaeyda vlvspgpgkp
       61 adagvsipvv eealrtgqpl lgvclghqai aeafggvvtn aeelmhgkts qvthdgsvlf
      121 dgvaqpftat ryhslavvdg tlpqdldvta rtaggvimal qhreapiygv qfhpesvlte
      181 ggyrmlgnwl evaglpgage aaralnplvk lg
//
LOCUS       WP_285114826             423 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285114826
VERSION     WP_285114826.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..423
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43970
     Region          49..384
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrrqsrfgri alaatagiva lilagctsta gsadlpeqqs ggfskdvekr lssavtdgmk
       61 ladasaafvg vwapwsgswt dalgttkrgg ttpvsadmtf rigqntvpmt ctvllelvdd
      121 gvvslddplt kwlpglvgve gvtmrelcqn tsgigdyiaq lnpkflmnpt rqwpplelas
      181 dgiamerygn pgekygrsat navlvgmalq natnrswpel ykqyvfdklg mtssslpdss
      241 qfsvpgphav gysvgldgag avvcspmrdv skmspsqgwt sggvvsnvhd lkafgqalas
      301 gsllseksrk aqvdavvngq sweryglgvq llgplrgssg avpgylsavy sdpasgltiv
      361 valnnstpgp gfaqllaqrl asivsktpak qkgakvvasl pwseqqavea mtksapcpak
      421 kag
//
LOCUS       WP_285114851             116 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285114851
VERSION     WP_285114851.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 116)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 116)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 116)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..116
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12214
     Region          3..108
                     /region_name="ArsR_Rv2640c_fam"
                     /note="Rv2640c family ArsR-like transcriptional regulator;
                     NF041413"
                     /db_xref="CDD:469304"
ORIGIN      
        1 mamtdllplr dlqaccapit kevisepdal slasamkala dparlrllsm iaahedgeac
       61 vcdlteplgl sqptvshhlk vlsaagfltr tkrgtwayyr iapgsldavs sffgsv
//
LOCUS       WP_285114954             321 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Propionibacterium
            freudenreichii].
ACCESSION   WP_285114954
VERSION     WP_285114954.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..321
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33338
     Region          3..296
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(38,256,259)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(193,226,254,257..258,261)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mavvvcgeal idlipdnsra gttqssywqa hsaggplnta valsrlgmpt rflgrfgidg
       61 fgaqlrshlr angvddslgv qtlagstsls vvsvdssgaa ryvfhlrgta nfgwkpeefp
      121 qldaddwlht gslvatvepg rsalldfvrt tpahlsydln vrptvepdpd aylalidpfv
      181 qvvsqrggvv rasdedllwl agghgeiddl araaverygm dllvvtlgah galatgvgre
      241 tvrvpgfpaa vvdtvgagdt ftagflqgwl rdadlsaall rgcaaasivc trvgadppta
      301 aevdellaag ptrtdpppdt a
//
LOCUS       WP_285114961             134 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285114961
VERSION     WP_285114961.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 134)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..134
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=14630
     Region          6..127
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 mtpaplivsa vavlrdrril mvtargrdvy ylpggkvdag etaeqaaare afeevalels
       61 pdgleelfev rtqahgepdg rqvhmrvfra wtddepvpsn evgsihwtts adavrcppag
      121 vevlrqlver dlid
//
LOCUS       WP_285115003             228 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285115003
VERSION     WP_285115003.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 228)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..228
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24549
     Region          40..140
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mrrtllrrag vlaldylyag ryqlravfdr sapdalvaga ghrapvvllp gifetwrflr
       61 plaqhihgsg hpvhvvtale dnrmevpeaa alvarhlaeh dlhdvvivah skggliakyl
      121 mgmpdsgpri rtavtvatpf agsplarfip ipsmrsllpt apgllrlals ravnaqivsv
      181 wgwfdphvpg gsrlegarni eldvgghfri larpellaiv devlaaad
//
LOCUS       WP_285115017             295 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285115017
VERSION     WP_285115017.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..295
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=32592
     Region          19..286
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mshpepaaap lwhpdapstv vagdnlevla alpdasfrli yldppfntgr sqarrtltsr
       61 psdggagsvi gfkgrsyeri kgdllsyddr fedywgflep rlieawrvla adgtlylhld
      121 yreshyakvl ldalfgresf lneliwaydy gakpknrwpa khdtilvyvk dpsayhfdsa
      181 averepymap glvtpekaql gklptdvwwh tivsptgrek tgyptqkpeg vlrrivqass
      241 regdwvldff agsgttgava salgrrfllv dsnpaaievm rerlgagdaa vrfvg
//
LOCUS       WP_285115071             572 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285115071
VERSION     WP_285115071.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..572
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=61365
     Region          25..556
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msiierrtst sedvveeldw patrlrvrnl rtafrvegal rpvvrgvsfd lrpgecvaiv
       61 gesgsgksvt arslvglagr sasveadelt ihhedvraft agqwqrirgr digfvlqdal
      121 vsldplrpvg reidealrlh gwgsrkarre rvldlltrvg vpfpavrakq rpdqlsgglr
      181 qraliasaia ldpdiviade pttaldvtvq aqvldqlegm kergasvili shdlsvvarl
      241 adqilvmrgg evleqgpaaq vlgdprheyt raliaavpse atrghaltpg aapvaakpap
      301 gavvleatdl vkrfqtsdgt vttavdrvsf alhagetlgi vgesgsgkst tarlalgles
      361 ldggavrllg epwaplaesr rrglrsriav vyqdplssfd prwnverill dalrgesvat
      421 aadrrarvlq llaqvglpen vlprfplkls ggqrqrvaia ralaprpdvi vldeavsald
      481 vtiqaqildl laalqresgv aylfishdlg vishlsdrvi vmkdgvvmee gtpedvferp
      541 ahpytralia aipefdpqga rtvttpeset aa
//
LOCUS       WP_285115158             114 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285115158
VERSION     WP_285115158.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 114)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 114)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..114
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13010
     Region          2..88
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mqtaeldrtf raladptrra ilarltkgea tvatlteqse ltqpaiskhl rvledaglvs
       61 rhrdaqrrlc rleaeplrea trwlsdyref warsfehlda llaelnraea edar
//
LOCUS       WP_285115211             472 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285115211
VERSION     WP_285115211.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..472
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=49381
     Region          20..453
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mtapkktqtp qaaegrpapr isvigtgylg athaaamael gfdvvgvdtd prkveelkeg
       61 rapffepglp elirrnvaag rltfttdlae avavsdvhfi cvgtpqqsgs faanlsyvea
      121 aargvaenlt hdglivgkst vpvgtgarlr aivadvvpag idvevvwnpe flregkaved
      181 tlspdrlvfg gtsaaaeatl rrvyekpiae gtpvlvadlp taelvkvsan aflatkisfi
      241 naiaevcdaa gadvsllada lghdkrigrq flnaglgfgg gclpkdiral mhrsnelgah
      301 gavgllqqvd einmgrrqrv idlalkalgg svlnrrigvl gaafkphtdd vrdspalnva
      361 aalhlrgaqv vvydpqarat aqrlfptlgy adsmeealtg adltvvltew defttadpaa
      421 lrdivsgrsv idgrncldat awsragwsvy amgtvpevap laddlaalap vr
//
LOCUS       WP_285115356             250 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Propionibacterium freudenreichii].
ACCESSION   WP_285115356
VERSION     WP_285115356.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 250)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19271407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..250
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27213
     Region          18..>71
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cl00447"
                     /db_xref="CDD:469772"
     Region          50..217
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mttqapdqpp varfrhevla vvfralaqag trlevmawrr hrapfkdewa lpsgpvnage
       61 tmdqavqrhl aarldltsir yseqlatfsd pgrdpferti asaylvllgq sgpvpggaae
      121 wldtralppm afdhaavvqa girrlrskms ytniafalap deftlkelrd vyvgvlghdv
      181 dvtnlgrvlt rrgqiaptgr rrrsgsgggr partyrfvea ahevtdpfat lrpaetplpg
      241 qaagegkatr
//
LOCUS       WP_285115444             383 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285115444
VERSION     WP_285115444.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..383
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38065
     Region          <237..285
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          <309..359
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mvhvtrhgtp wgvpavgtsl llgaalalsg catgtseldr aqaqvtakek avkeaeatas
       61 tsaqtfcqas etyiraldry gdvlaesapt vgdvrkagsd lakprdaafd gaqaavdaha
      121 elaaarqdla eaqaaleaak sgstgspsaa apsaaspgpt atplvpaatv drvkkaeddf
      181 aaaqesitde tpladasqrf nsaavalefa wlrlfadagc ltgdeaekaq aavasyvtav
      241 qqdlaaagyy sgavdgiygp ettaavealq kahgltvtga mdkataaalq aqlaalggaa
      301 aqrdtattaa lqqtlklagy wtgpidgvws paltdavkal qsdlglpptg vvdavtvnaf
      361 hqalaaakap aptatpspsg ssg
//
LOCUS       WP_285115428             330 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285115428
VERSION     WP_285115428.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..330
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=34532
     Region          2..319
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrvlvtgasg ylggavaqal varcdevrtf qrrpsgvagv qdvlgdltdp grvraavegv
       61 dailhlaakv slagpvadfd rinvegtrtl laearaagvh rfvdvsspsv ahagdslvgd
      121 gagpadpara rgdyartkaa aellaleada pgfavvvvrp hlvwgpgdpq lvgriverar
      181 qrrlpligsg aalidttyid navsallaal draedvhgra yvvtngeprp vaellggict
      241 ssgvpapswh vparvaraag gavegvwrir pgrdeppmtr flaeqlstah wfdqrrtree
      301 lrwsptvtid dglatlarws adqrggyaag
//
LOCUS       WP_285115489             339 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285115489
VERSION     WP_285115489.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..339
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=35709
     Region          1..334
                     /region_name="Tdh"
                     /note="Threonine dehydrogenase or related Zn-dependent
                     dehydrogenase [Amino acid transport and metabolism,
                     General function prediction only]; COG1063"
                     /db_xref="CDD:440683"
ORIGIN      
        1 mraaaitgkg aveivdrpqp hglvdlvvvq ilvapmctef ksrqagdvsd sigheaagvv
       61 vdagsstrva vgdrvvvmpg yacgtcryci agehihcpfq rdvlaeseqp ygtatyaeyv
      121 lkpdwllvpv pddvslvhas aaccllgpsf nasqrmnvaa sdtllvagcg pvglgaiing
      181 vtrnatvlal evnpwradla rqlgatvfdp tapdivdqvl datdgwgvta sietsgvpsn
      241 pallasvsar raglsivawg lditlppivp lgldvhgvwh wkhqtdgwrm ietirkasgl
      301 idtaithrfp ldrvseamdv qdsgrcgkvl lfptevqdl
//
LOCUS       WP_285115492             275 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285115492
VERSION     WP_285115492.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..275
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30033
     Region          7..267
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mslprarfac qtyswqmsad rfrgttrhma qvaadagfag fepevfmlga dwnarrldad
       61 lasvpiqlaa lclvhdwrgp sesdeerrea daaidavagh pgavlnlvvm pgadredlre
      121 rqrnalacmr evaqraadrg vvatfhpnsp agsvfrtpdd yellldelpe plgftpdvgh
      181 iakggmdpia lvrrtsdrir hvhikdihsd ggwaatgegv ldipaivatl ddvgyrgwia
      241 fedesplaer dpdeavrrtg ayvrrslitv teetp
//
LOCUS       WP_285115598             408 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285115598
VERSION     WP_285115598.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..408
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=44069
     Region          9..376
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mddredanpi vvlgggpagm asalslhtag hpviileryr earpagniln lwpppikalr
       61 amgvdttdlg apchttfrsa gghvradiri pesvtaefgg gfigmlrpdl yermlaalpd
      121 gmlrthqevv sihdggqdvv llgladgsti etpvlvgadg idsmvraqlw gasekrdhrl
      181 hiiggytfep vpsaekgeav lthdrevqgs ytsirrgaee gfqwwvleaw dpsreppadl
      241 hahalalagr fggaleelvr ltpaeheqrw pirdrkpltq wskgrvtlag daahatspya
      301 aygagmsicd gyflgqalhg vdladrrave aalvryetpr iphttaqvqq ayalgqafhh
      361 aprplrpvrd flldhtpllq kqvgerspge iiaqldemga gitspalr
//
LOCUS       WP_285115603             306 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285115603
VERSION     WP_285115603.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..306
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34014
     Region          10..295
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtanelpfgl gvslysytdd igvtmtveec iadvadlgat gleilgeghi edypnpstaw
       61 idawfarner lgltptlygs widtrrfpgr gmtadegaqq leldlrlast lgfsfvrpki
      121 gvisedlrvd piwqeavern lqlaadldiv icpeihwptv iksavveeyl efkdrtgseh
      181 fgllidtgvf elspyprrgg sasfrmgdgs arppvvpfvp vsdladvmah tvyfqakfye
      241 vdddlvdhyi pwrdiidvvv dagytgwlss eyeghhepyr apdqlrrqha lirtiaaesa
      301 alpdrn
//
LOCUS       WP_285115654             355 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285115654
VERSION     WP_285115654.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..355
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=36731
     Region          7..349
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mdlrtlldid apivlgpfgg mssveltvav seagglgsfg lyglgpdria avaaelrqrt
       61 srpfnlnlwl pfqgpgerav rdgfdrgefd raiaalfelf aeariepsaw pvaplpdfse
      121 qleaafdaep avlsfvfgvp gpaiveeahs rgilvfgaat tvpearalaa ggvdavvasg
      181 leaaghrpsf laepesslvg slalipqvvd avdvpviaag giadrrgvaa afalgagaaq
      241 vgsaflatrq svappvhrer iraaeahetv ltramsgraa rglpnhavra ieqsggqasf
      301 plqniltgvf rrraaedgra dllslwmgqs aglsrfddaa evfaelaagv pgrrh
//
LOCUS       WP_285115788             621 aa            linear   BCT 25-DEC-2024
DEFINITION  polysaccharide biosynthesis protein [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285115788
VERSION     WP_285115788.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 621)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 621)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 621)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 621)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18500220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..621
                     /product="polysaccharide biosynthesis protein"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=68340
     Region          140..259
                     /region_name="FlaA1"
                     /note="NDP-sugar epimerase, includes UDP-GlcNAc-inverting
                     4,6-dehydratase FlaA1 and capsular polysaccharide
                     biosynthesis protein EpsC [Cell wall/membrane/envelope
                     biogenesis, Posttranslational modification, protein
                     turnover, chaperones]; COG1086"
                     /db_xref="CDD:440703"
     Region          302..581
                     /region_name="Polysacc_synt_2"
                     /note="Polysaccharide biosynthesis protein; pfam02719"
                     /db_xref="CDD:426938"
     Site            order(306,308..311,331..332,358..360,381..383,385,400,423,
                     439,462..465,468..469)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(332,334,338,342,356..359,362,365,383..386,389,393,
                     396,399,469..470,475)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187548"
     Site            order(385,425..427,435,463..464,470..472,475..476,
                     487..489,493,495,530,553,556)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(401,425,435,439)
                     /site_type="active"
                     /db_xref="CDD:187548"
ORIGIN      
        1 malkdwlwtt rvqdetrarg esivarfggq yfadslawiv aivvavvlry dfalhrihwv
       61 pvlvfaiavl llqlvlgwly wvyrgrytyg sfeeataval tvltvallmt iplalvgpaf
      121 glprslalia gpiafglmgv arylkrqyvi rrlkvnpnae rallvgagfm gsimvrrmlt
      181 dpdsqylpvg mldddrskrn lrllgvpvlg evddlqrvat atsatvvlvc varadapfla
      241 risdlaepaa lrvkvlpeld evlegrtrls dvrdvsiedi igrrpvdtdi esiagyltgr
      301 rilvtgaggs igselvrqis kfgpselmml drdetglqha qlnivgngll dsdsliladi
      361 rdgellkdif rrrrpdvvfh aaalkhlpml erypdeawkt nvlgtlnvir asldagveqf
      421 invstdkaar ptsilghskr vaerltawaa essgrdylsv rfgnvlgsrg sliptfkrli
      481 degkpltvth pdatryfmti peacqlvmqa gaigsagevl ildmgqpvsi levahrmiaq
      541 sgrhldivft glrpgeklhe eligegevdr rphhelisha rirpmdparl drgewlrrwe
      601 lghsdtamvg vvdgvsrgae a
//
LOCUS       WP_285115917             394 aa            linear   BCT 25-DEC-2024
DEFINITION  thiolase family protein [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285115917
VERSION     WP_285115917.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 394)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..394
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40147
     Region          1..394
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 maeaylvggv rtpvgrygga lagvraddla alvvaeavrr aaappdalde vilgaanqag
       61 ednrnvarma vllaglpdev pamtvnrlca sgltaviqaa qairagdadl ivaggvesmt
      121 rapwvqakpd kpwsrpgpqf dtsigwrftn prllardkat ytmpetaeev arldgisree
      181 adafaleshr raaaaadggr fdaelidvet psgpvsadeg irrdtgpeal arlkpvvagg
      241 svvtagnasp lndgasaivv asaeaveryg lqprarivaa asagvapevm glgpvpatqk
      301 alaraglgve dldavelnea fasqaiacir rlgldparvn adggaialgh algssgsril
      361 vtllgrmere garrglatmc vgvgqgtsli veav
//
LOCUS       WP_285115952            1138 aa            linear   BCT 25-DEC-2024
DEFINITION  NACHT domain-containing protein [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285115952
VERSION     WP_285115952.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 1138)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 1138)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1138
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..1138
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=123543
     Region          127..1001
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 msilgvlvpv glcavkvalr lasnpaggdw adsladfsdl ygrvsneldr rkldrqaadi
       61 anevtrhlar eieieygsld egdvtaaaea avvalvdslp ldrqdqvsiv aaeysanaly
      121 kvvmrgvdrs swvalhgeav adltqlilrn vshaiaailr krpdlnidml salvnknaef
      181 aalldelsta lidlpmrfse taeasasqre nrqdleflte ylravaeend rldvyglnls
      241 revvhyelta syvtlrlshk stepsagsls rflsrsagas ttgekkssqv vhlsgpagsg
      301 kttllqwlav naargtlpke ygaiaerlpv lirlrnygee rlprvadlar attastlsee
      361 plgwmsrilr ggqgvlllvd gvdefpekra pelatwfedl dsaiprltvv vsgrptaeas
      421 vralaeefgn rwnlfeiqpl grtevqafva hwhravarrs gvgelnseam vvadrlngdp
      481 alrklasspl vcavlcalfh aqhgdlpssr ielyntlatv lvsardsqrg ilvdqdslsg
      541 pqrllvlqal asfmlenrls eipkdragac vrraladipg ghdakttlda llrrsgvlre
      601 pspgvvdfvh rtfleffaar elarrdsleg lahhaddpnw setvvlaasi andtqyrsmc
      661 diilaksdea pgvrsapwav gvmggilaar strvdsvdse llkrlrlnlp prsgddartv
      721 iaageavfge vvasisdpnn evepnvcsav vralgefgge salralaemp srlrlqlvnd
      781 laaiwpwfdp grfaelllqd lkppfatrvv vnssrvfpsl rglsdlfewe avieipdesl
      841 itdcanapiv klniaglell adesartcef vagiaglral rvqgvsnlnl adadlfllns
      901 idlgitrgei dlsilagska ldlvaiaslg ttrmiaprst rivsrvlsls geieispelq
      961 laatqvylkq vpaaalasld lgqtstlhlr diddltsldl vkaqslrhlq iescpalqdi
     1021 edllsidrlg lveirgatsi tnaetlarld eqietfvldv dldallemhy talalkteda
     1081 ddrleargfg rwseakrrpv sgatyedwdp eptfvwrtse edspteeelr sielgdqg
//
LOCUS       WP_285115992             207 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285115992
VERSION     WP_285115992.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..207
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23010
     Region          27..147
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mspdspeqne grdtagsaya erlrrldssw wrrtlnvqap yrwnirrlhl grvldvgsgl
       61 grnlahlgnn gvgvdhnpes vaisrarglt aftsdefpst eyavpgtfds lllahvvehv
      121 dpdfavelvk mylpyvkpgg hvlfitpqer gygsdsthvt ftdfdglhrl adrlgltver
      181 eysfplprfa gkaftynefv llaripg
//
LOCUS       WP_285116041             166 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285116041
VERSION     WP_285116041.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..166
                     /product="metallophosphoesterase family protein"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18204
     Region          2..164
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mklllisdth vpkrarslpa qvltamdaad vvihagdwvd aatldlleer srrlvgvygn
       61 ndgpelrrrl pevarveldg vrfavvhetg patgrelrcd rdfpdtdvlv fghshipwdt
      121 asphglrlln pgsptdrrrq pvctyltaev aegrltdval vpvprp
//
LOCUS       WP_285116169             471 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285116169
VERSION     WP_285116169.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..471
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=51721
     Region          49..414
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mspsrtstvf errrpddavv rhalaparqa vfwtedapgd hyprlrgdvs cdlavvgggy
       61 tglwtallak redpsarvvl vegrrigwaa sgrnggfaea slthgdengr srwpsefdvl
      121 qrlgmqnlde ieatvaelgl daefernggl dvatephqve wlreaagpda tfldrdavqs
      181 lvhspsyeag llrhrdsalv hpaklarala racveagvei ferspvegig dgteletptg
      241 tlrsqrtala tnvfpsllrr nrlatvpvyd yvlmseplsa srresigwmg rqgigdsanq
      301 fhyyrltadd rilfggydav yhyggrvrsa yedrpetfrq lashffttfp qlegltfthr
      361 wagaidtcsr fcaffgsare grvayaagyt glgvaathfg akvmldllag rttertelem
      421 vrsrpipfpp epaaslginl trwsldqadh rsghrnaflr tldavglgfd s
//
LOCUS       WP_285116168             535 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285116168
VERSION     WP_285116168.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..535
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=56378
     Region          10..131
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          221..518
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtsvlptire vlrmepvaga lpevvtgrdr ldapvrwvhv aetaeaarlg sggelllatg
       61 vgwpaedaal rrlgrvliea eiaglvlelg ppmpaapaal vdefaaaglp favlhrearf
      121 vaiteavhsr iiaeqmaalr arddihalft dlslrgspad fiveqaarvl gspvvledts
      181 hrviaaagel geaetrgael sgweqrsraa hrsgdgdwti vpveargmrw grlvglpgep
      241 hpagrtnvle qaavalalsr lsdrdedewt rrshdallaa llgrrfsgdg gitarfeavg
      301 lpivgrpvag aavrlrsgtl pvpatarave aarsagvdav agrhpeqagt lvvavsgrpg
      361 arlddavfqa iaeaagsvrl ddpatvvavg sdargitgll ssleeavela tgaptppear
      421 lgrrpvvqrv qhrpllrlvn algndprmle hteqmlrpli ehdlatggdl vevlraylsh
      481 pgnrtraaaa shlsrsvfyq rialieellg mdldegetva alhaavlarg rtssr
//
LOCUS       WP_285116220             452 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285116220
VERSION     WP_285116220.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..452
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47966
     Region          24..440
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mnsavdlplg madltfaasg ealvrrtvlp sgvrilsehv pgsrsatlgy wvavgsrdes
       61 eggaghpgtl gsthflehll fkgtrtrtal diavsfdsvg gehnamtake ytcyyakvqd
      121 rdlamavevi gdmltsslld paefenergv ileelsmaed dpgdvanerm fqavlgdhpl
      181 grpiggrpdt ihaatrdgvw ehyranyrpq dlvvtaagav dhdllvagve naltsagwdl
      241 dlaatpvsrr gavpaviqrg tplitvqrpt eqanlfvgmp gilatdprrt tmsvlnsvlg
      301 ggmssrlfqe vrerrglaya vysfsgsysd agvfglyagc apakarqvte lmleelrrla
      361 adgvtpdelr ravgqlsgga alaledsdtr msrlgraeit lgefadldes lrrlhlvtad
      421 dvrelaadla grpisiaavg sltddafagl vp
//
LOCUS       WP_285116232             146 aa            linear   BCT 25-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285116232
VERSION     WP_285116232.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..146
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15073
     Region          48..141
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mngfaalgiv lglvavvaag glvwrattgr artlrareav rpgdvgadaf gaqatllqfs
       61 telcspcrst arvlaaaavg sdgvrhveid vtrrpeladr fhllqtpttl ildasgtvra
      121 riggtarpda vhsalrtilr snhvsa
//
LOCUS       WP_285116181             105 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285116181
VERSION     WP_285116181.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 105)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 105)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 105)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..105
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11146
     Region          6..98
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mtsgtlvpvf aalgdetrws vlealgqgda sasaladrlp vsrqaiakhl avleavglve
       61 pvrvgrevry rvlgsqlsat aqrlerigae wdrrlaaike iaetl
//
LOCUS       WP_285116323             281 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285116323
VERSION     WP_285116323.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..281
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=31073
     Region          2..279
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mriavtggsg klgrtvvrel rksgdvvvsl davgergpgf vrvdltdygq tvdaifgvnd
       61 qhdgfdaivh laaipapgil pdvatfhnni rvtynvfqaa rragirnivy assetvlglp
      121 fdvpppyipv dedyparpes tyslvkhlee qmaielvrwd palkivalrf snvmdpedya
      181 afpafdddpw arkwnlwgyi dardgaqair ralewdttgf drfiiaaadt vmsrpndelv
      241 aevfpgvplk rdlgvndtll sidkarrilg yapthswrde v
//
LOCUS       WP_285116413             402 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285116413
VERSION     WP_285116413.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..402
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=43708
     Region          4..379
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 msnpqstrya sldglrgvas lvvlgyhall vvpaisalyi dkvdpsafsp ewwlfktpfr
       61 llfagheavl vffvlsgfvl tlpflsrppt rrstlayygr rivrlyvpvw aslvlalala
      121 lavprnpamg gwmgthhapt vsstwhdpvl lfgtsnlnsp lwsltwevwf sllmpvmfll
      181 irftraarww waaipllmlv saaarfdvir ralpdaglta dllqylpvfg igmllavnrn
      241 rlaaaagrir twwpivagal lltisptlia pngygvgqaf ayllsltgva givvlafasp
      301 vrrplearpv qwagtrsfsi ylvhepilva tallvgangw wwlltaaavi piilltaevf
      361 hrfverpsit lsravgraie grratapvpa avqnggsvsa gp
//
LOCUS       WP_285116438             439 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285116438
VERSION     WP_285116438.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..439
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=46602
     Region          15..365
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mrstdparti ssglrghdna lglirlvlal avlvshtfpl ggfghdpgsg itrgqanlgt
       61 lavagffais gylitksgms advmqfawrr vlrifpafll vlllsalvlg piiwsldghs
      121 laayfarsga spwhylasnw nlhgttwgil dvfqnstpyg qethasving smwtlgyewd
      181 cyvmigllli agvltkarpv vvvvaavffv aqiinlvspg tmgtvfpplg svqfcylayp
      241 favgaafavy srsiplnprf giaagvvlvw tllnggygvi gvpagvyfil wlgsavpgrl
      301 rkigqqndis ygvylyafpv qqtlayfgly klgavpmilg aaiivltlsw lswrfvespa
      361 mslknwgpgr gfaywvqrfr pgkpapvdaa vptatavapa aqatpatptt rtahaslpvt
      421 aeislprrta aaepasppa
//
LOCUS       WP_285116430             443 aa            linear   BCT 25-DEC-2024
DEFINITION  MFS transporter [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285116430
VERSION     WP_285116430.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 443)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 443)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..443
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46844
     Region          4..368
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mnsrrswvvy gigvfaylia vmqrttigva gvaatdrfhv saavlstlav vqlivyagmq
       61 vpvgvlidri gsrvlmlagt almvvgqvav alapsiavai vgrilvgagd atvftslmrl
      121 tnswfrgriv pqlsqwignv gqlgqvlsai pfalllhlsg wtvafltaas lsvvaligil
      181 vavtdrpvga segprpatws dsmrqlrvsl arpgtqlgfw shfvtqssgt vfslmwgipf
      241 lvfalgiqpa easalltvlv gaglisgpil giltarfpmr rsnlvlgiva lmaaawtlvl
      301 lwpgkpplwt vivliaaigi ggpgsligfd fartfnplhs lgsangivnv ggflasfvmm
      361 fligvsldvq ahgadgdaql yqldhfrwaf aiqyvivgig vgflvrarrr trralkedeg
      421 idvaplwval vgtwrrrggr eal
//
LOCUS       WP_285116454             422 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285116454
VERSION     WP_285116454.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..422
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44603
     Region          151..392
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 masggtgsaf gkalgtaavv agglvlatag laawattrva rtvitpvrrr pqnqtirsfd
       61 eglgtvtlrn tadsampgrf glwwggetsf akvgglielg dgsvtreler vefgelragr
      121 arisgyyylq peelglpvts veiatdlgqa pawvfpapdd adsgrwaiqv hgwgasrqeg
      181 lrsvrvfhda gftsllasyr ndgdapesad rryglggtew rdieaavdya vehgarsvvl
      241 mgwsmggavv lqtitrsrsl ehvtgivles pvidwvdtle yqgnllrlpd vmtraamrli
      301 eaewsgpitg qgapidlrsm dfvarasels lpmlilhsdd dgfvpstgsr alaearsdiv
      361 tlvpfdtalh tklwnydeak wtgaiagwla ehvpaaasaa avaapavaav gdpdpiegdp
      421 aa
//
LOCUS       WP_285116477             196 aa            linear   BCT 25-DEC-2024
DEFINITION  HIT family protein [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285116477
VERSION     WP_285116477.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..196
                     /product="HIT family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21272
     Region          58..184
                     /region_name="FHIT"
                     /note="FHIT (fragile histidine family): FHIT proteins,
                     related to the HIT family carry a motif HxHxH/Qxx (x, is a
                     hydrophobic amino acid), On the basis of sequence,
                     substrate specificity, structure, evolution and mechanism,
                     HIT proteins are classified into...; cd01275"
                     /db_xref="CDD:238606"
     Site            order(83,85..86,93,95,141,149,151,155,157)
                     /site_type="active"
                     /note="nucleotide binding site/active site [active]"
                     /db_xref="CDD:238606"
     Site            order(153,155,157..159)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238606"
     Site            155
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238606"
ORIGIN      
        1 marlnlgsyd gagadgadgp vriddpsylv gvpdefqrlw tphrmvyiqq gdpghddcpf
       61 cvaptlsded alivargeha yallnlfpyn sghllvcpyr hiplydqatp eevaeigsit
      121 qtamrvirev skndgfnigm nqgaiagagi ashlhqhivp rwaqdanflp iiaktkalpq
      181 llgevreaia nawpqq
//
LOCUS       WP_285116492             748 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285116492
VERSION     WP_285116492.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 748)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 748)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 748)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 748)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 748)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..748
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..748
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=83115
     Region          28..747
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mvdtttsqsa slrrlvprif sraqpsgavd tlirtvrmhh pkadlslier aysvaerahq
       61 gqkrrsgepy ithpvavaqi iadlgigakt iaaallhdtv edteytldel rdqfgdeiam
      121 lvdgvtkldk vkygdsaqae tvrkmivams kdirvliikl adrlhnartw gfvpaasatr
      181 katetleiya plahrlgiqa ikweledlsf avlypklyae ieslvkqrtp ererlvqqvi
      241 dainddlksa kirgkvvgrp kqyysiyqkm vvrgrefddi ydlvgirvlv ntvrdcyavl
      301 gqiharwtpm pgrfkdyiat pkfnlyqslh ttvigpqgrp veiqirteem hqraefgvaa
      361 hwkykeqttg kssggpakvd ndlawlahis dwqaetadps efldslrfei gakevyvftp
      421 kgrviglpag atpvdfayav htevghrtmg akvngrlvpl esslntgdvv eiftsknpds
      481 gpsqdwlnfv ksprarnkir qwftkerrde aieqgkdaia ramrkqnlpl qklmtqdalv
      541 evasslkhpd vsalyaavge ghistqsvie kivaslqtev esdseleipa kgrrqlrnsd
      601 sgvlvrgapd ilvklakcct pvpgdpivgf itrgqgvsvh qsnchnvqsl lhepermidv
      661 ewapssksvf lvqiqveald rsgllsdvtr vlsehhvnil satvttssdr laisrfvfem
      721 gdtthldrvl navrridavy dvyrvsgg
//
LOCUS       WP_285116674             143 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285116674
VERSION     WP_285116674.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 143)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..143
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15447
     Region          7..143
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04683"
                     /db_xref="CDD:467566"
ORIGIN      
        1 mrptypaavy lcifdgdril lqrrrgtgyr dgelslpagh iepgesataa llreareett
       61 lalaadqvrl alvqhgradg dtyidfffaa elpegatpai gepdkasell wapadalpad
      121 vipvirhgie alvrgetyte ygw
//
LOCUS       WP_285116696             810 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285116696
VERSION     WP_285116696.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..810
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=91238
     Region          13..807
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtdqtlspae rfaasrdrar qplletfrag lrfdldpfqr eacgalergr svlvaaptga
       61 gktivaefav flamreanak vfyttpmkal snqkfqefqd aygpesvgll tgdtninsha
      121 rivvmttevl rnmlyadsdl ltdlayvvmd evhyladrfr gavweeviih lpsevrmvsl
      181 satvsnaeef gdwlqavrgd tdvvvsedrp vpleqhilmr sklidlfdss glaatnrvnp
      241 elvqmarygg rvlssrqmkd vgryhskggr pdtfrmnrad lvallddrnl lpaiffifsr
      301 ngcdaavkqv lragvrltqk herdeireiv eercrtllde dlavlgywew leglergvaa
      361 hhagllpafk evveelfrrk lvkvvfatet lalginmpar tvvleklekf ngearvpitp
      421 geytqltgra grrgidvegh sviqwedgld pqsvaslasr rsyplnssfr ptynmavnli
      481 dqfgrgrtre ilessfaqfq adravvdlar kalqqeqsla gyeeamtchl gdfteyfsir
      541 reltdlerkg srietasnsd rekrqrqlaa lrkrmkdhpc hrcaereqha rwaerwwklk
      601 rdterlrsqi qsrtgavakv fdrvsdvlle lgyltkedge taltvhgrtl kriygerdll
      661 vaeclrrnaw kdldaaglaa macalvfepr reeglahert lprgafrpsl ektttlwsrl
      721 ddleqenrlp gseppstais lamwmwsrgs gldavlsead maagdfvrwt kqtidlldql
      781 slvaqgnvgr varqalesir rgivayssva
//
LOCUS       WP_285116770             411 aa            linear   BCT 25-DEC-2024
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285116770
VERSION     WP_285116770.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..411
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42868
     Region          3..411
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 mtkkivvtgm gassplggta peswaellag tsgarslehd wvakyelpvt faaeakvrpe
       61 evlerpvakr ldpssqfali sameawedag rpdvaperlg vdyatgiggv wtlldawdtl
      121 rergprrvlp mtvpmlmpna asaavsmhfe arafartvas acasstesiv nayehlqagl
      181 adviiaggte saihpitvas fssmqalsrr ndspatasrp ysvdrdgfvm gegaaslvle
      241 teehalarga riyaelaggg vtadsyhita ndpegrgasr avnlalkaag aspddvthin
      301 ahatstpvgd pseyvalrev fgervhgipv satkastghl lggtgaleav fsilairdrq
      361 apptinitem dpaiplqvks tpqplgdgpq lvisnsfgfg ghnavaafrs y
//
LOCUS       WP_285116846             470 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285116846
VERSION     WP_285116846.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..470
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49665
     Region          130..465
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mslrdrrtep giincpllqr daptargppl nwlltlridk ppflitldvl agalvlylli
       61 rptwrrtlag ltaavaggll gwfvvwlctd vldlfgvalt pvttlwtalg fgsvslaian
      121 lfrsrwwrkv iaafsipvfl aaafcginad fgayrngndv lgvvpygalq lhsergevva
      181 gtdwratadp apadpapadp patlpakgev gtvripates rfparkavvy lppvaltanp
      241 palpvlyals gqpgapadmf tagrvaavmd afaakhdgya pivvapdqlg gpgrnpmcvd
      301 srdygdsaty lltdvrnwvr snlrvssdpa gwgvfgysqg atcavqfatg rpdlfgsala
      361 ssselgptlg nealtistgf ggskqayeqa qpsallkaha pyrdsvmvfg agandakysg
      421 fartlyreae qarvhaylls spgtahdwkt vryvlahgfp liapqlglgs
//
LOCUS       WP_285116911             363 aa            linear   BCT 25-DEC-2024
DEFINITION  FUSC family protein [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285116911
VERSION     WP_285116911.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..363
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38493
     Region          20..211
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 martrstgrr lpagialpat irtstrapfl qvvktavamv aawgvaslfv rgelpifati
       61 aallvvqpsv nqsvgraier slgviggvvi ayliglafgt nswivllavv vsvllawalk
      121 ltpgtanqvp itamlvlaig asdpeyalar ivetvigaai gvvvnvaivp pvltaparqa
      181 vaalgnelaa tltrlanalt tghtraelda lliearllrp metkaqsalt aadeslslnp
      241 rqrkhrvile hdqqlfdrlr plinrtlgmt rayhdhydds laaeptihai adelnraahd
      301 lrllvrdpde pivepgteta gvpvltaplt iatpdprhwv ligslvedlr rihveiagdd
      361 eag
//
LOCUS       WP_285117002             250 aa            linear   BCT 25-DEC-2024
DEFINITION  amidohydrolase family protein [Staphylococcus caprae].
ACCESSION   WP_285117002
VERSION     WP_285117002.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus caprae
  ORGANISM  Staphylococcus caprae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Staphylococcus caprae"
                     /db_xref="taxon:29380"
     Protein         1..250
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28880
     Region          3..249
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 meifdahfhi infdypvken ngylppefke kdykvwqedl niiggaivsg sfqefdqeyl
       61 ihaletlkgq fvgttqlpis tpdeviekln elgirgvrfn vkrggsedlk hlksfahrvy
      121 nlvgwhtely ieskklneik eillelplvs idhlgltneg fedlkelveq gvyvkatgfg
      181 rievepiqtm relmdinpdv lmfgtdlpst rakrpfnksd ielikkhfsv eeqqkifykn
      241 amkfyrines
//
LOCUS       WP_285117068             291 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285117068
VERSION     WP_285117068.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..291
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32120
     Region          4..287
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mteplasllt aldltdtgar tsediftgps qwmplgrvfg gqvlaqsiva atrtveddrs
       61 ihsmhgyflr pgdvnfpitf svdrihdgrs fstrrtqayq nglpilsmia syqtedegie
      121 hqdampeglp epeslpstat sledvrhpva qywasqrpfd mrhvtspiyl svegehvaqq
      181 avwfrtigem pddpalhraa layasdytim esvmrrhgia watpglkaas ldhamwwhrp
      241 arvdewllyv qesptagggr glsqgriftr dgvlvasvaq eatirlphgd d
//
LOCUS       WP_285117149             181 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285117149
VERSION     WP_285117149.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..181
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=17976
     Region          <36..169
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mvawalvvac vagwvvvpea ipapaaavvg lvpgstanaa asraegtwew plaehrltaa
       61 yaapatryaa ghrgidlaav agsmvgapaa gvvrfsavvv drpvltldhg dgvlssyepv
      121 rsdlpvgavv argavvgtva sgghcdgsci hvgvrvngey vspmrffgrv ppavllplga
      181 g
//
LOCUS       WP_285117198             363 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285117198
VERSION     WP_285117198.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 363)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 363)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..363
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38668
     Region          36..317
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mnsyatrqpt essvapeeqt taavprmdls elrraaeqit dnvesvidgk heavqtalvv
       61 llaeghllie dvpgvgktml akslaksvdc tvsriqftpd llpsdvtgvs vynqaerrfe
      121 fkpgaifani vigdeinras pktqsallec meerqvtvdg styplaapfi vvatqnpvem
      181 egtyalpeaq rdrfmariam gypdegsela mlttrdtssp lsrirpvvss ddlrammvta
      241 rnvfastpvk qyavdlvrat redrdlrlga spratlqlir aakamaalag rdfvlpddvd
      301 alavpvlghr llptsralgh hhesapviad ivrrivastp vpvgsgaapa gapasglsaa
      361 tgr
//
LOCUS       WP_285117232             476 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Leifsonia sp.
            fls2-241-R2A-40a].
ACCESSION   WP_285117232
VERSION     WP_285117232.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..476
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=53362
     Region          23..473
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 msgersttts sttastdsrd dgpavvwfrd dlrvadnpal saaarsgrpv lcvfvwddet
       61 pdlrvpgaas rwwlhhslaa lteslerlga gltilrgpse rvmtdlleta gaaavfwnrr
      121 yggverhide aiksaardag reatsfaanl lfepwtirtg qgtafsvytp fwraclsape
      181 prkpgpapds lrgaqapstl qtvtlddlgl lpthpdwaag lreawvpgee aaheqlerfl
      241 aedvgdyreq rdvpgvdats rlsprlrwge lsphqvwhat aerrdrstaq gastflsevg
      301 wrefayhtlf ehpdlatvni hreydsfpwp plddsalraw hqgrtgiplv dagmrelwtt
      361 gvmhnrvrmv tasfliknll idwrlgeqwf wdtlvdadpa nnafnwqwia gsgadaapyf
      421 rvfnpelqre kfdahgdyvr rwvpewdtee ypepivdlke trraalaayd avkrsr
//
LOCUS       WP_285117253             270 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285117253
VERSION     WP_285117253.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..270
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27724
     Region          7..244
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mpirlepapt fadrlraadr plygmwscag splvaeicag sgldivlidg ehspvglesi
       61 laqlqaiapy pavpvvrapi gepvilkqll dlgaqnvlvp mvdsvahaee mvravrypph
      121 gvrgvgsala rssrwsripd ylaranelvs ltvqietvda ldaagaiaav dgvdallvgp
      181 adlaasmgll gqqnhpdvis averviaagr asgtpvgvna fdpataerya aagaayvlvg
      241 sdvtllaras eglaerfigg ssdtveptay
//
LOCUS       WP_285117436             445 aa            linear   BCT 25-DEC-2024
DEFINITION  FGGY-family carbohydrate kinase [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285117436
VERSION     WP_285117436.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..445
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=46700
     Region          2..409
                     /region_name="ASKHA_NBD_FGGY_FK"
                     /note="nucleotide-binding domain (NBD) of L-fuculokinase
                     (FK) and similar proteins; cd07773"
                     /db_xref="CDD:466793"
ORIGIN      
        1 mlydpqsper tviaeptpvv ptphgdlrda davvatvlsc idrlleglpp aergavrgig
       61 itslseemvl ldasgrsisp mpawytgvaa eaargegidp sfswsklrwa seqyaaedvr
      121 gvttlnsyia aalgddsdfa iddshasrtg ffdvgaatwq pqlfeatgwp asllpplvpa
      181 gsavstlasp laerwgipgt aaivlgghdh fcgafavgir segqlyvsag tseahclivd
      241 elpqgllpeq vgagrfvdge hfylhrqlps ghlyrqwtgl lgladessra reaeelraep
      301 lgslgttvvp gfgtdvrssv fdlapdagrr tllrallegl acaallvdre lialtgrpit
      361 evvasgipaa spvwqqlran lavaplsvss edeapalgaa llcervatgt egrpsalqrv
      421 padpasaaey galyarfeqk lstlr
//
LOCUS       WP_285117515             440 aa            linear   BCT 25-DEC-2024
DEFINITION  M50 family metallopeptidase [Leifsonia sp. fls2-241-R2A-40a].
ACCESSION   WP_285117515
VERSION     WP_285117515.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia sp. fls2-241-R2A-40a
  ORGANISM  Leifsonia sp. fls2-241-R2A-40a
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Leifsonia sp. fls2-241-R2A-40a"
                     /db_xref="taxon:3040290"
     Protein         1..440
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46063
     Region          2..434
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 mllfvlgvvi iligvavsia lhevghlvpa klfgvkvtqy migfgktlfs frrgeteygv
       61 kaiplggyis migmfppgke ggrgrnattg fmqqmvqdar tastetvavg eeertfyrlp
      121 vwkrivimfg gpfmnlvigv vlfgvllmgf gapqssttva tvsqcvlpag sttktcpada
      181 tqgpaaaagl kpgdtivsid gtkirtwdqs taiirasagr sltmvlsrdg eqrtvqltpv
      241 vnkvaktdan gavvknaagg ietltvgfvg igpvtklvpq pppavlpavg aqtgavvnvf
      301 ahlpqrmvdv wnaafgsaer dpngpisvvg igraagelta ldgvpavdki ytmigmlasl
      361 nialfvfnlv pllpldgghi agalweglrr tfakifrrrd pgpvdmaklm pltfavvivl
      421 ggmsvllmya divkpvnlfg
//
LOCUS       WP_285117689             649 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Lactococcus petauri].
ACCESSION   WP_285117689
VERSION     WP_285117689.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 649)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 649)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 649)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 649)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 649)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..649
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73000
     Region          1..527
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 msavsfiavm ligviaanvi keffpkiset filigvgill sflpefrhfe lepeffmmli
       61 iaplmfnegs ktslkevrkn frgifflsit lavvtvlfva alttnimgsw ifplaicfaa
      121 ivtptdsvav ksiiagkkmp qgvneavefe slfndasglv llslglsvle sghfsiwsgl
      181 gqfafvsigg iligliigtf lvririainl ratnpeatii pisiltpfal yllaehfgts
      241 gvlavvaagl ihnfegdmlk ltstnvqltn ntiweilsgi lnnfvfillg vslfgiwdif
      301 kslgleeavi lffisalvyv lmlfirkfwt nqrgnrsieh ffsndkkerg kdstifalsg
      361 ahgtmtlama fslplntail stenreiiis mativillsl ivptfilpkl lspmkaassd
      421 didsvrndmv dyailhmmqv iedskvrssl tkqlqsqngl qipdhnkssr llenivtwqe
      481 afldssdiqe nfsakaidyf riylensskr amskkirrmf srrsrlrgad qsemqefiav
      541 rnelghledv lyeatmekln rlererfekk vtdfsdieev krvfenrhyr mrneiqeeti
      601 vpnellieaf qleyqyvldq vksetisket snklfkeinn aqvlqlqnq
//
LOCUS       WP_285117845             360 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lactococcus petauri].
ACCESSION   WP_285117845
VERSION     WP_285117845.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..360
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41520
     Region          62..355
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mdiksykkkn gttaykfrvy vgkengkdky vkrsgfttka saraalmqlq neienptsks
       61 emtfrelyne wlvvyekevq nstyykttra fdkhvlpefg dtklsdftpl mlqdyqndla
      121 eklkfarklf gmirkvfnya alygyiqanp alpvtsskik rtaenkkdfy npdelksfmg
      181 fveqtenikk ialfrllaft girkgellal ewndyrkktl dinkavsnsp lglevsatkt
      241 kasirlisld dktcnildql hkiypkttri fesenggils pskprkwlhd ilkdkelqpi
      301 rihgfrhtha sllfdsgmsl kqvqyrlghs dlkttmnvyt hitefakdni gdkfsayidf
//
LOCUS       WP_285117987             644 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Lactococcus petauri].
ACCESSION   WP_285117987
VERSION     WP_285117987.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..644
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=74238
     Region          10..589
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mlvtqreqqi iqeflvkktl tvadmmeatg asrrtiyrdl dkfqltlpnm giylrtsteg
       61 yylegdlarl eqlqelkefs pqerqkaeiv llvtkhhsle elaerfavsl ptvisdlkhl
      121 dkiceenelf lhqddeiwit gkeekirsvl vsilndsmsi sealngdfae gkissfletq
      181 fletakaife knveikavdk skvlmqfflg itllrinqgk tissglwrkp skeaiafvre
      241 iiqelggtsf slteivylas iydvlyfgfg revlfmekfd sqfsykvrql isevsqkmdi
      301 afikddklyg llyahlkete ilpdlsseke nkfikkiead nkkvfkvvqd vlpkifsrkf
      361 sstdtafvtl hfvatlersd lvlpltaaiv tsrgriscef lishlkknfp flkridiiql
      421 seipdlehyd vvfttekeld yiyvsrildq kntddirhql rviqqearke nreeeprhtv
      481 dlsrlfsisn tileefslet lenpphlqav ielivqrlgf sekeglarll lerfeathla
      541 ipdtniallh glhgtvpypl fkiydleeri eviamnqeki svnrvlllla ppevdhymty
      601 llgrisssii enklytkiyd sgnqevveel lktimtesiq kyge
//
LOCUS       WP_285118021             413 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Lactococcus petauri].
ACCESSION   WP_285118021
VERSION     WP_285118021.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         <1..413
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
     Region          95..407
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 dfysalfpke kvgnmkvedi kvgslwsetr knkflwrmry fnivtksedk vsvtltsnsn
       61 qaktkarkil ltkakrkieq selnilnsrl ninsltfssv anlwlndcsr rlkpstlnnr
      121 rkqikrfade fgdqemsqft tfqiqvffns lnlksgtvkg yfltcksifd fakrmeiisk
      181 dptlnvklsl skktledikk qnrklftved lakvlnrmrs sensrtyfia ltieflfltg
      241 lrycelaalk eenydrtrri ikvetnldyt kgvtkhthtt tktlssyrev dlndraieii
      301 eeylkanhdn tyvgyknhgy ifctrsgqph nighlnrsfk yygkatgldk qfschcmrhs
      361 hisllaemgi nqkvvmqrvg hatstitnni ythvtpnmsk elnkkmnrin kis
//
LOCUS       WP_285118105              71 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lactococcus petauri].
ACCESSION   WP_285118105
VERSION     WP_285118105.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 71)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 71)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 71)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..71
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8032
     Region          5..71
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mtktklqimr ekkgltirel tekmsenrqw lgnymakiea ieqgasihcf syygikhlaq
       61 algcsvdelv e
//
LOCUS       WP_285118146             339 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Lactococcus petauri].
ACCESSION   WP_285118146
VERSION     WP_285118146.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..339
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36486
     Region          31..337
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mysktsnknr isiivmllal sllamllslq igsapisvgd lmnmilgrgk dsapllqsil
       61 levrmprill sflvglalga sgtvmqsllq nplassytlg vssgaslgas tvmllginfm
      121 stsismslag fafglvtvfi vllfaqqfsq sldnqtiilv gmvfslfvns fltlmmtfsp
      181 dymqriifwq lgsfsgaswe nvqlltllfv fsfvcllyfh remdilsfgd tfalsqgvev
      241 krtkvilisl stlltgasva mtgvigfvdl iaphiarrlf gathkwvlpg saliggllcv
      301 ladtvarsvf qtrelpigav taligapffc yiffrkgqv
//
LOCUS       WP_285118356             462 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Propionibacterium
            freudenreichii].
ACCESSION   WP_285118356
VERSION     WP_285118356.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..462
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47465
     Region          37..429
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 msdaysslst paghrssste srrsveaplt ltdkpprtlg agaqtamwas fgvtlfgplt
       61 galvtqsvgs lvgglaacal gtlvgalllg gaagigahtg tpsmvglrgl lgrgasvvpt
      121 vlniaqnigw aimeiivits aathivgaaw hwpfvivaga lctlmairpl gsvkilrtvm
      181 lwlvlagsiy lfvmvlrqps haigqdavig fwpgvdlaaa qvvsfaplaa dysrhatsgr
      241 safassatgy glaifayyal gvfavahlgg dlagtnllaa lmvlpaggla iglllldeld
      301 nafanvysst vsvhnlaprl drrvisvavg vvatvlagla gfdqyegfly ligsafvplf
      361 tvavvdffvt rrgrwdttsa apfrwsptla wvigfvayql iypgsipgws dlwaglaqal
      421 gfvapgwlgs tlgsivvsav aaaglgaidt avrrhraeer la
//
LOCUS       WP_285118365             322 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Propionibacterium
            freudenreichii].
ACCESSION   WP_285118365
VERSION     WP_285118365.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..322
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35477
     Region          4..316
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 maarrserlv nlaiallsar rflskaelrr vveayrglsd saferqferd kddlramgvp
       61 vvmgsndvlf dddtgyrisr tdfevppvsf dsdelsalga asrvwqqasa aeqtisalak
      121 lraagadpdv erlaalapri sarepafevc wratlerqlv rfgyrgspev rtvapwsvlw
      181 rrgswyllgl dltregprmf kmsrmnatpe tvggtdayqv pddvdlqala rqvepgepds
      241 rallalrdnk apalrrigtp vappralpeg facfevpytr dsdfvadiaa agpdvvvlep
      301 aelrdqvlaq lravlevshd rs
//
LOCUS       WP_285118427             411 aa            linear   BCT 25-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Lactococcus petauri].
ACCESSION   WP_285118427
VERSION     WP_285118427.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..411
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=42338
     Region          31..382
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mkkklitalm lstvvltaga pfaavkadst dskiaqqdsk ianakneaak aqsqvdsiqs
       61 qvstlkskqt smtkkvnelm aqqkeqsqqi qklsesiker ntaleaqars aqtdgsatny
      121 msavldsksl tdaiqkmtam atvaganksm ieqqqadqka iqtkladnqk kyaeatklqq
      181 eldaqanela tqeaalkvaq ldyqatvtta egkkqdllsq kaaaekaaek aaaaekaaaa
      241 ksvvaqqeka vaaapaasnp apaanntadn snsstlstgn ntggngnssk ptptpdptpi
      301 ptpdpdpdpg hsgtnpypag qctafvwdyf ggnmptymgn agdwvayans gpaagtiavf
      361 ppgnqgaggv ghvavvlsvs gskmtviegn fnggwgttre cstagvsfir p
//
LOCUS       WP_285118461             333 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Lactococcus petauri].
ACCESSION   WP_285118461
VERSION     WP_285118461.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..333
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38201
     Region          1..>115
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkfsiiipvy nsekyiekcv ssithqthqd leilliddgs tdnsgnicde lsksdsrirt
       61 ihqenggtsk srntglkeat gdyvmfmdnd dlwstknglt ainnqllesk advlifdsai
      121 erngnvnyig ksdfsrdkvl kqptevalke liignklvra vwtkvikndl ikkfhlefpv
      181 gmrnedtaft adlitvaqsy dwynyyfyiw iktgvsqtsk rvslqsmkdl eeilvvnfgr
      241 alkienlelk kaflsylsyp yvvllgqvke yqkqdktasl qlirnlkqyk filnidgnpt
      301 vkkikyiyri fgfnvvvyll grvmsrkyrt egi
//
LOCUS       WP_285118620             623 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Propionibacterium
            freudenreichii].
ACCESSION   WP_285118620
VERSION     WP_285118620.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 623)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 623)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 623)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..623
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=65100
     Region          23..617
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mttvtgstsr ttirqqagts lwsridrtdl artlfvaact aalalgldwp sptvpllavi
       61 glvvgcwpvv veawhdirqr rmsmelsmll aiiaagvige wttsllittf vlaaeiledl
      121 smdrgrdalt almsflpttv tlreghttrd ialddvapgq vlvigpgerv rvdgvvdkgr
      181 stldqsritg esmpvdvavg dpvyagsinq vgalevraer vganssygri vtavreaqss
      241 rapvqrmadr faawlvylsi agaivtflvt rdlsatisvi ivagacgiaa gtplavlaai
      301 ariarvgafv kdgahleals vvdtvvfdkt gtltrgvptv tdvrtapgvs tqqllawaga
      361 aeaysehplg raiaahvraa gvapgtaqsf dyqpgrgvsv evdgrmiaag narlvpdapa
      421 saadgvatpv hvsvdghyag tvlladqvrd sarsvvaelr hrglrvmmit gdqpatarav
      481 adelgitevr agllpdeklr aidaeraagh rlamvgdgvn dapalmratv giamgsgtdi
      541 ardsadvvli ssdlndlaat lhiarrarri vmfnfvgtiv vdvigmvlaa fgllgpvlaa
      601 vfhvgsesaf ilnsarlipr rrh
//
LOCUS       WP_285118797             224 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Staphylococcus caprae].
ACCESSION   WP_285118797
VERSION     WP_285118797.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus caprae
  ORGANISM  Staphylococcus caprae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Staphylococcus caprae"
                     /db_xref="taxon:29380"
     Protein         1..224
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26084
     Region          1..66
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mirnrlsell serglkisrv akdvkiarss ltsmaqndse mirydaidkl csylhispse
       61 ffehnpinfe ftfdeepnyk indvfegfev tanithafsi enfdfeilvd vdldnrqkln
      121 fdldvsyket kkitnsqhrf ifmikneden ielkkyvdsl saglknllfk kinqklsgyv
      181 seiivknidn ieelfpkkge kcttlhkeil qtdsrlssdi fkey
//
LOCUS       WP_285118869             382 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Propionibacterium
            freudenreichii].
ACCESSION   WP_285118869
VERSION     WP_285118869.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..382
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42517
     Region          71..371
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 magkrsfgri drqrsgtyra rytgpdmalh kaphtftnks haerwlldeq dlisrdvwea
       61 pevrsakpka ltvgewistv idrranrtrr plaqttvdly rkdyrlrise tlaavlltel
      121 tpamvaawwh glpdtptqna rayallrsam sdalgdelie rdpcrlkeag kptpthtgea
      181 itvpelftyl eavpesrrlp lmiaalcglr sgevrglrrr dvdlkagmlh veqavsrvra
      241 dnhrwewria ppktaagirt valpapvtda lrtwlteapm ngrdgllfpa tdghspmpgt
      301 vlreahlrgr eaigrptlti hdlrrtaatl aaqggattke lmrllghttv svamlyqvad
      361 eerdraraqr ltqqlqegqa gq
//
LOCUS       WP_285118900             340 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Propionibacterium freudenreichii].
ACCESSION   WP_285118900
VERSION     WP_285118900.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 340)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 340)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..340
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=35369
     Region          10..339
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 msapkspgel rvrrtstrmt rqiglatvav sllfvaalvv mvilqsrpae lneparpgev
       61 rihlsaaktv glsigvavaa vvyalvigrv vsrravrpla dalelqrrfv adashelrtp
      121 ltvldarvqm lqrelaegqp agetasalrq dtgrligivn dllavsgdds gegargpgpv
      181 adasqivtss aesmrvlaeq rgvslvidve pdlevrmppa glgrcvtalv dnainhgsgd
      241 hssgdhgsar grvevqlard dgravmtvsd dgpgirgvap drvfdrfaht epvdqpgarq
      301 sfgiglalvq elatrsgggv kvastgpdgt vmeltvplaq
//
LOCUS       WP_285118911             655 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Propionibacterium
            freudenreichii].
ACCESSION   WP_285118911
VERSION     WP_285118911.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 655)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..655
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=67124
     Region          65..645
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mnrlqkwvyg nwsvpvvsgv liiisfavqw lgggvanltv gpqwwlnagt hathanavft
       61 lgdafmiaaa vvagygivvk avrkliarvi gidllvsvat igsviignfw eaaavtflfa
      121 ighaleaatl nktrsalael vaiapdsati vrdgqqqevp aaqvrvgemv lvkngakvpv
      181 dgqvvsgtgv ideasitges ipvekskggq vfagtvsrgg flqvlamgig adttlariih
      241 rveeaqdaka ktqafidrfs gwytpammvl alaaglisgd vvlaltllvi gcpgalvisi
      301 pvaivagigr aasngilikg gefletsaki savavdktgt ltegcpeltd vvildsaler
      361 sevlrwaaaa eagsehplar pildtaqaeg vgphgvpgsv tpvpgkgivs dvdgrrvlig
      421 npplllkygv vddgsaaqaa eslaadgktp mivavddkvi gvvavadqir qdapemiarl
      481 hragvekvvm ltgdtrlvae tigkatgide ihssllpedk lemvaqlqqe gytiamvgdg
      541 vndapalata digvamgaag savavetadi almgdnllkl peaiglakrt vsvmrqniai
      601 alitvmllla gvfaggvtms igmlvheasv lvvianamrl lrnspgstam pksdv
//
LOCUS       WP_285119104             267 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Lactococcus petauri].
ACCESSION   WP_285119104
VERSION     WP_285119104.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..267
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30321
     Region          6..262
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(28..29,31..32,35..36,73,77..78,81..82,112,116,123,
                     126..127,139,155,159..160,162..164,166..167,170..171,
                     174..175,200..201,203..205,207..209,211..212,214..215,219,
                     222..223,229,231)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(158,162,165..166,168..169,214,217..218,220..225,
                     228..230,234,236)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(179..186,202,205..206,209)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mqnmlmgryi pgnsqihrld prskllvmfi fviviffahd wlgylllily tfagvllsgi
       61 sisyflkglr pmiglilftv ifqmlftpge hiifqfwilk isteslinal yiffrfvlii
      121 fmstvltltt ppltladgie tglaplkkik vpvhelglml sislrfiptl mddttmimna
      181 qkargmdfge gnllqkvrsi ipiliplfvs sfrraedlav amesrgyqgg dgrskyrqlk
      241 wskndfilll sifilaalll swntfsr
//
LOCUS       WP_285119177             217 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Lactococcus petauri].
ACCESSION   WP_285119177
VERSION     WP_285119177.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..217
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24391
     Region          2..208
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mkfkaivfdm dgvlvdserf hskvldnffv esgidasdlt pkdfvgsvlk dmwpkvlrde
       61 ftearaaqvh qdfldydaqf pipykelllp gvtdalktfs ekgykmavas ssrrheiaev
      121 ldthdlrqyf efflsgqdef eqskpnpaiy laameklgve psetliieds hygimagkaa
      181 gatvwavkdn yfginqeqad rfietltdak nllaese
//
LOCUS       WP_285119269             370 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Lactococcus petauri].
ACCESSION   WP_285119269
VERSION     WP_285119269.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..370
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41304
     Region          14..357
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mkkiaiiggg iigmtlanyl dtekfditvf dsgkhqatga sagiispwls krrnkqwyal
       61 akdgaaffeq lvkdlslnen iyekcgtlfv rspqalqdle qlalerrata seigevrhlt
      121 keettdmlpl lkpveslyis ggarldgkay lqhlreraqt rgvrviseea qvkkekakwr
      181 visvqeevev delvltpgpa lktlldqlgy takvspqkgq llsfetnfet ekwpvafleg
      241 eadlipfqng rlllgathen eagwdleptq eafeqltkgv qtflkedyfa dtaysyrvgt
      301 raytadfapf fgpivqergl niasglgssg lttgpyiayl laqhlnadns ewdmnhyqke
      361 mnlyvnkkee
//
LOCUS       WP_285119282             650 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC1 kinase family protein [Propionibacterium freudenreichii].
ACCESSION   WP_285119282
VERSION     WP_285119282.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 650)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..650
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..650
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0004672 - protein kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=70015
     Region          116..561
                     /region_name="AarF"
                     /note="Predicted protein kinase regulating ubiquinone
                     biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport
                     and metabolism, Signal transduction mechanisms]; COG0661"
                     /db_xref="CDD:440425"
ORIGIN      
        1 mpapllellv lallavamae vakriitgvs fvrrfvasll vflltlpagt wvmeqtrivt
       61 pdgtlqvswp ifllvmvlcf vwvfaaaltg lvvlemvlps gsmpspiqsa rdirmalrrh
      121 rrylqlgwia mssglwkalr kgpdspgfge alvkmlnrsg vtfiklgqvl strpdvlpga
      181 vmtaltslwd taapapeqni rtmlrsqwgr dpeevlgsfd dtpfaaasia qvhratlkdg
      241 tavvikvqrp gaaeqvvvds dillrftrla eqrfawaram gvdalgrgmt kalkeeldyr
      301 rearntkaia atladnpait tpvvdeeltr ekvlvmspvn gsslaskvdt ldddtrhela
      361 rtlmtatlqg ilvhgifhad lhpgnillld dgriglldfg svgvidaetr qliaallvaf
      421 vaddnsaatt avtaafdvgd evdrmalqrd lgraltllth tgdesaatln efftvmrdyr
      481 itipgdvaga frtltslegt ltalsadygl lagaedamps iitklaapkq lamiaatttm
      541 tsallarrlp arteqitdll argqytlntr mlsdrsdrqw lrsrlddams slfaavavvl
      601 avvfivipgg paitstltgy dlagaaigcv glvlilrlvv rlftrysgrp
//
LOCUS       WP_285119350             645 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Lactococcus petauri].
ACCESSION   WP_285119350
VERSION     WP_285119350.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 645)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 645)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..645
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=74681
     Region          34..627
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mlsynldill fserrfwkld kilevtglks hefqrqlvel nqilqdknqr pleftnnvla
       61 ipeklesfee irfnieeyel tlseekrqfl iyllcfskrs vlaisdfqsl lnvsrntvls
      121 dikklrqqld nenirleysr klgfylqgas kelrkttwrf lqelheesdy yvlskhlnlk
      181 nplfihqvgq qisrliaels vqvihsrylp mliylallqs hlgetdlfqe dvlevealli
      241 gmsdgnfeks gfdflyrigf eimenvmkla avqfedftkt faalrahlvp ayfrlkyhfe
      301 ienvlldkik tdysslfelm dlalsplhea cgeiseaera yfvilfggei ykkkytqslr
      361 aivlcvngis sslimrkrle nmfpsmtfil stavsdldki pafsydiifs tvpvmtdkkl
      421 yvmsafpdse eetrlynrla qdfnlpgfyk pnarailrai epyvdiknna tkkqltriid
      481 rklnnkktes ealgvmlsdl ltkekihftd ekldwrsaie laaqpllnqg eiepsyisai
      541 ikrveefgpy idlgmgialp harpedgvkk lgmsflrceq pvylqddlkh eikifivlaa
      601 idnethlral stltqilsnk delnkmltve tvaeleqifa ekege
//
LOCUS       WP_285119445             431 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Propionibacterium freudenreichii].
ACCESSION   WP_285119445
VERSION     WP_285119445.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..431
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45016
     Region          68..212
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 msfsplaaqa apasadggts stprsvatst ssagvdpasa cgdlvqlapv lssdhtpdgk
       61 qitpkptadg rrvpviivhg wvsydthsda rdhlfsqyvd rtadpaggtg yllaqsqyrs
      121 sligmlqqvp gaevytfdys qvgsrwvtdp qigpklsqai eclsdsyqqk pvlvthsmgg
      181 lvarqalsnn dskgrpisgr vsnvlavgap nngsdsaqmi asaltigsei plaglpirml
      241 wdyigqcseq mdatnttctg iravdafrss ggealrtgsa qlaqlpwwpd nvkvtayvgd
      301 iqmggislfg lnsprlldlg dllvsvdsak agsqrsrqvn ceygiistks aetgpvrlml
      361 agqgnsveqp adllsspcfh eamlhettit gdlqrdltev lgantawhdp atagseqsag
      421 attvsavres r
//
LOCUS       WP_285119446             361 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Lactococcus petauri].
ACCESSION   WP_285119446
VERSION     WP_285119446.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..361
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39903
     Region          5..360
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 msklerisnf lnenevdmtf itnpttlnyl tglaidpher iaglmvfpdk apslftpale
       61 vekakanttg fdifgyedsq npwavvkehl gskniqkiav efsdiplskt kglksqfsgv
      121 efvnltplve rmrliksade iekmkisgdy adkcfeigfe yansdrtetd vvakieyemk
      181 rmgvpqmsfe tivlsgaraa nphgmpedvk iqdnklllfd lgvmkngyas datrtisigk
      241 psdfdadihk ivleaqmaam dfvkpgvsal eidkvardvi tkagygeyfv hrlghgigmd
      301 vhefpsiggs ediiieegmc fsdepgiyip gkvgvriedc lyvtetgcep ltktnkelmi
      361 f
//
LOCUS       WP_285119531             684 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Propionibacterium freudenreichii].
ACCESSION   WP_285119531
VERSION     WP_285119531.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..684
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=75728
     Region          13..609
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mtdlrelpsq plavepahvg lmvkasvqaf gdrpatrvlv gkrwvvasyr eldaramqia
       61 aalmysgvek gdrvgfysrn rpewtqvdla cqfigavsvp iyatdtvdev vhiandcgmv
      121 vafagradea ermgqaserv aslrrvisfd scprtdvtwl eyfapsdrpv pervvsrina
      181 rlnkatgddl fsiiytsgtt gapkgvklah rammselral hrsfpistrd hslcflplsh
      241 alergwtcyl wahgcmntyv vdtrnvgemm rrarptlmva vpklfetvla evhkasavtp
      301 rrkrilqwav svgqhlqfdy rqgrkplllw raqlpladrl vlrkireamg gqktmlvsgg
      361 aplrretelf fgaaglqiln gygmteaapl isynthtayr vgsvgrvmpg griklgdkhe
      421 ilyqgpnvmd gywdneeatr eafltddegt wlrtgdvgri drrgflfvtd rlkdiivteg
      481 gknispqpie ellqadpmfe hvvvlgdnrp fltllvqpsm anlqklaeal hidyghvsel
      541 fnnqnildei kksaealtnn lpkyqqfrdl rmssegfsia nglltptlkv krreverrfr
      601 glidemytki glhhdpksas grdpksasgr dsksasgrds ksasgkdsrs asgrdsgtas
      661 ggdrgrahgq dpratrggds ptar
//
LOCUS       WP_285119550             695 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Lactococcus petauri].
ACCESSION   WP_285119550
VERSION     WP_285119550.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..695
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79615
     Region          458..687
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 matkwknkfa vsiglallll gvnslvftal naeqyifndy fqskyfkqev atleealint
       61 qvnpnipikv taedieeyrm sqpdkysqvs vikedpvfle rlkdakaagd ktaikkledq
      121 qnkklnevek fftddkyvte kvkeqkkeli aqqktdwmpq ykelssdihy qvteinsgky
      181 ldnlsdnktf ataktlfkgn isqinfegqn rfdgqiiilk nsnfnqrasv ksftemknlt
      241 igllcmsils faaflvywkk tkkgedille kvqswdkial dgqiflamil sllyllltre
      301 asltwsflpl lqkfcwaflv lylfaivswg iyhkaqeren wqqtylarsi rllkdaadnf
      361 stgskawfif wsmgavvvgf lltmmwggqg iilylfvlvi yllliliyll rrlvmfnqtv
      421 kiieeiaqgk naevlnvkpk gktvfrrvse nlktineevk tsksqqvkse rlktelitnv
      481 shdlrtplts iitsvdllrn adlsqeeknk yvavidqksk rlkvliddlf eiskmasgni
      541 dlkksridlv qlldqslael sekiedsslk fvtqtdkell alvdgdkmwr vfenlihnil
      601 kysmentrvy isghksengt ielvfknisr eelgensqel sqrfkrgdls rnttgsglgl
      661 aiaqsimeah eghflletdg dlfkvtlsfp slele
//
LOCUS       WP_285119656             457 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Lactococcus petauri].
ACCESSION   WP_285119656
VERSION     WP_285119656.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..457
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=51230
     Region          31..389
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 miqltkftpp tleenlrpvg ltddtmaqrr qklldkmtqd nfdcliiyad lehgsnfeyl
       61 tgflprfeea llvlhkdska ylvlgnenln kadkarlkae avhmphlslp nqpmntqetv
      121 eeilsqcdle htqkiglvgw knftstkedn yqlfdvphfl vhavqslcpk ailenttrlf
      181 igengvrttn nanefahyef gaalagrcml namnqielgk semevarels dlgqahnvvt
      241 imatgerfvk aniypsdkvi kkgdklsltt gykgglqsrg gyavsqasel pdeekdylsa
      301 vaqpyfnavk twleaikigm qgqelynkie evlpqekygw tlnpghlsad eewmsspvyp
      361 qstesiesgm lfqidiipsv sgyggvsces gifladaqlr qeikeaypdi wgrvqerray
      421 iqnelgitlr deilptssat aylrpfmldk tlaftvk
//
LOCUS       WP_285119718             291 aa            linear   BCT 25-DEC-2024
DEFINITION  EamA family transporter [Propionibacterium freudenreichii].
ACCESSION   WP_285119718
VERSION     WP_285119718.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..291
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29570
     Region          7..285
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mspalparst lfgpslvvtg lfcqetgasi avmlfpavgp agivalrlvf saiilcavar
       61 pslrgrrpia wytaiafglv ltgmnlffyl aldrlplgtt vtiellgplt lsvvagrrwm
      121 nlvwaglalv gvvllggsat hldplgvaft lvaaafwagy illskatgrn fagiqglava
      181 mvagsvvtvp ialattgsrl fgphvliagl giallssvap yalemtalrr tpaatfaill
      241 alapavaaaa gffilgqtmt ihdvfgivav icasigavct ppgkpggrqk a
//
LOCUS       WP_285119805             179 aa            linear   BCT 25-DEC-2024
DEFINITION  YagU family protein [Lactococcus petauri].
ACCESSION   WP_285119805
VERSION     WP_285119805.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..179
                     /product="YagU family protein"
                     /calculated_mol_wt=20496
     Region          1..179
                     /region_name="YagU"
                     /note="Uncharacterized membrane protein YagU, involved in
                     acid resistance, DUF1440 family [Function unknown];
                     COG3477"
                     /db_xref="CDD:442700"
ORIGIN      
        1 mfsftipsas lqeiifqsiw cgfisgmisg mvkigweail pprtsernat nppqrmleqf
       61 gvpsslthay vlysrdqkvy wfslilhfsf sivfatlfif iaqywpcial wqgaaygiii
      121 wfvwhivllp vmktipapwk qpfaehfsef fghivwtwsi aaclyylisk dssgiltni
//
LOCUS       WP_285120210             326 aa            linear   BCT 25-DEC-2024
DEFINITION  ribose-phosphate diphosphokinase [Propionibacterium
            freudenreichii].
ACCESSION   WP_285120210
VERSION     WP_285120210.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Sinha,S.C. and Smith,J.L.
  TITLE     The PRT protein family
  JOURNAL   Curr Opin Struct Biol 11 (6), 733-739 (2001)
   PUBMED   11751055
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Becker,M.A., Smith,P.R., Taylor,W., Mustafi,R. and Switzer,R.L.
  TITLE     The genetic and functional basis of purine nucleotide
            feedback-resistant phosphoribosylpyrophosphate synthetase
            superactivity
  JOURNAL   J Clin Invest 96 (5), 2133-2141 (1995)
   PUBMED   7593598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..326
                     /product="ribose-phosphate diphosphokinase"
                     /EC_number="2.7.6.1"
                     /GO_component="GO:0002189 - ribose phosphate
                     diphosphokinase complex [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004749 - ribose phosphate
                     diphosphokinase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0006015 - 5-phosphoribose 1-diphosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009156 - ribonucleoside monophosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009165 - nucleotide biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=35177
     Region          1..310
                     /region_name="PrsA"
                     /note="Phosphoribosylpyrophosphate synthetase [Nucleotide
                     transport and metabolism]; COG0462"
                     /db_xref="CDD:440230"
ORIGIN      
        1 mkdiivfsgs ahepfaeqvc qhlgvrlspv nisrfsndcl qaqlltnvrq rdvyivqplv
       61 pptqdhlmel llmvqaarga sadqitavip hysyarsdkk dasrisvggr lvadmlstag
      121 vdrvltmqlh apqvqsffsv pvdqltamgv laryfqehce nsvvvspdfg naksastfar
      181 llgvpvaags krrlgdnrvv idtivgdvvg khcivmddei atggsilelv rklkdqgavd
      241 asvtcthglf agnaleklsg ekfiteivst dtvpepaehw pelhvlsvtp lfaeaidrih
      301 ngksvskmfe gidpvyappk gqeglf
//
LOCUS       WP_285120299             154 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lactococcus petauri].
ACCESSION   WP_285120299
VERSION     WP_285120299.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..154
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18559
     Region          5..59
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(8,12,37)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(11,36)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(18..19,30,33,37)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mdfynrikkl skeqkksfnk ierdlgyprn tlynyktkep seerlralsr yfgvsedyls
       61 gkiefnsdkt lshydneidv lfddfkekfe diiygielke fdkiyqtedv lnyfsnlqew
      121 vaeevdeldi iintykkrve nrknkekskt vied
//
LOCUS       WP_285120473             223 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein, partial [Propionibacterium freudenreichii].
ACCESSION   WP_285120473
VERSION     WP_285120473.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 223)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..>223
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
     Region          96..>221
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 massnaaksa srreqlraar ereaaaarrk ritvvavavv vaavlvavia maaggvfgkr
       61 sggsgatstv vsvrpphasp gdkgvfsadn vndsapvltv iddfqcpich tyetvfgpvf
      121 eslakkgetr leyrtryfld inlkndssvr aaraaaiadt fgkyqeyhdt vfsnqpakeg
      181 tgytddqlrn afpqaagitg ddlakfqssy dkgemnafvd avd
//
LOCUS       WP_285120555             687 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ParB/RepB/Spo0J family partition protein [Serratia].
ACCESSION   WP_285120555
VERSION     WP_285120555.1
KEYWORDS    RefSeq.
SOURCE      Serratia
  ORGANISM  Serratia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 687)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Serratia"
                     /db_xref="taxon:613"
     Protein         1..687
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=74119
     Region          45..>228
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mstieskapa takatrtaks atkksvvaen ieaalakavr ktatlgqlel dglnvrkkkt
       61 sqasieglaa sirsvgllqn livfemedgq fgvaagerrt lalrwlmgre ddadkttpdg
      121 ivnagyavdv livskemari isltensqre qmhpadqvfa fremsaegra paqiggllgf
      181 stkhvqkclr latmapalld aladdkitld qlqalsated hqrqcdvwin ahgwaaapqh
      241 lreavltdev sakdnsqlaf vgreayesag gtfkfdlftd egfltepall erltreklha
      301 laqqvaeseg wswaegrisa iktwgedael yremaeplpe ftgdeqaeit rlkarfaale
      361 aafeeadvdt dtdvmiaesd avqadierit eqatirswpq amrstggvmv slrggdvvyq
      421 rgivlrasds ttapggddng dgtvttteta sktkekglsa alitclsaer tlavmgalve
      481 nptvalalht htmtvkvfgs ryagsllktd ltpkraellt kaptaegsra drqlgelhaq
      541 weaklppewn tdftwlltwe qadvvallay cvgqsldaiq swpardgkvg geltalehal
      601 dfnlrewwqp tkanyfgris kelmsdalvd agkvaqaasv lkmkkgdaaq laedelsasg
      661 wvpdcllpas deadaaddia hpdnvaa
//
LOCUS       WP_285120722             348 aa            linear   BCT 25-DEC-2024
DEFINITION  lipid II:glycine glycyltransferase FemX [Lactococcus petauri].
ACCESSION   WP_285120722
VERSION     WP_285120722.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Rohrer,S. and Berger-Bachi,B.
  TITLE     FemABX peptidyl transferases: a link between branched-chain cell
            wall peptide formation and beta-lactam resistance in gram-positive
            cocci
  JOURNAL   Antimicrob Agents Chemother 47 (3), 837-846 (2003)
   PUBMED   12604510
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Hegde,S.S. and Shrader,T.E.
  TITLE     FemABX family members are novel nonribosomal peptidyltransferases
            and important pathogen-specific drug targets
  JOURNAL   J Biol Chem 276 (10), 6998-7003 (2001)
   PUBMED   11083873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006395
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..348
                     /product="lipid II:glycine glycyltransferase FemX"
                     /EC_number="2.3.2.-"
                     /calculated_mol_wt=39529
     Region          1..348
                     /region_name="FmhB"
                     /note="Lipid II:glycine glycyltransferase (Peptidoglycan
                     interpeptide bridge formation enzyme) [Cell
                     wall/membrane/envelope biogenesis]; COG2348"
                     /db_xref="CDD:441916"
ORIGIN      
        1 mefleisqeq ftafaaekte sflqtpqmae mlekrgykpi flavkvndqi kmaalmtsvs
       61 vsggaklein fgpignfdqi vyncfiqelk kyaknqqale vkirpavdym vydskgqelq
      121 eanesfisem kklgltyngr hvgyeeqdav aewqyikdls eihseeellk synsnakrnv
      181 kkaiknevtv kiatyeelfe verligntge krhfatkdla yyqelykafg nkieflityk
      241 dgvaiaagvf ievnqeflyl yggsdgaygk lggpflmqht amlhaierqm ktynfygisg
      301 nfdgsdgvlk fkqnfggyit qkvgefsyyp npvkykliqg mkkilgrv
//
LOCUS       WP_285120788             339 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Lactococcus petauri].
ACCESSION   WP_285120788
VERSION     WP_285120788.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..339
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36504
     Region          31..337
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mysktsnknr isiivmllal sllamllslq igsapisvgd lmnmilgrgk dsapllqsil
       61 levrmprill sflvglalga sgtvmqsllq nplassytlg vssgaslgas tvmllginfm
      121 stsismslag fafglvtvfi vllfaqqfsq sldnqtiilv gmvfslfvns fltlmmtfsp
      181 dymqriifwq lgsfsgaswe nvqlltllfv fsfvcllyfh qemdilsfgd tfalsqgvev
      241 krtkvilisl stlltgssva mtgvigfvdl iaphiarrlf gathkwvlps saliggllcv
      301 ladtvarsvf qtrelpigav taligapffc yiffrkgqv
//
LOCUS       WP_285121020             409 aa            linear   BCT 25-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Lactococcus petauri].
ACCESSION   WP_285121020
VERSION     WP_285121020.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..409
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=42123
     Region          31..392
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mkkklitalm lstvvltaga pfaavkadst dskiaqqdsk ianakneaak aqsqidsiqs
       61 qvstlkskqt smtkkvnelm aqqkeqsqqi qklsesiker ntaleaqars aqtdgsatny
      121 msavldsksl tdaiqkmtam atvaganksm ieqqqadqka iqtkladnqk kyaeatklqq
      181 eldaqanela tqeaalkvaq ldyqatvtta egkkqdllsq kaaaekaaqk aaaaekaaaa
      241 ksvvaqqeka vaaapaasnp apaanntadn snsstpstgn ntggngnssk ptptpdptpi
      301 ptpdpdpghs gtnpypagqc tafvwdyfgg nmptymgnag dwvayansgp aagtiavfpp
      361 gnqgaggvgh vavvlsvsgs kmtviegnfn ggwgttrecs tagvsfirp
//
LOCUS       WP_285120891             695 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Lactococcus petauri].
ACCESSION   WP_285120891
VERSION     WP_285120891.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 695)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 695)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..695
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=74740
     Region          2..694
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mrsqnfvitg mtcancvntv skalnnsnki qeatvnlate kakvifddsi sdqdvinive
       61 kvgygaivnd kahqekiaaq arrrnrnlrl slivsviltl plvlamfegv lgthyliflh
      121 npvlqlilat pvqfiigwrf yvgayhalkn gnanmdvlva lgtsvayfss lilavflgqd
      181 nalnfesamv iitlvvlgkv lehnakektn qaitslmssr vkmvhteege rpleevqigd
      241 viqiypgekv pldamilkgk asfdeshltg eslpvvkadd dtlfegavnl dgsikavvvr
      301 dvndstisrm vemmeeaqas kpdiqkfadk isnvfvpivl vislvtfvat waitgtllta
      361 imhavatlvi acpcalglat ptaiisgtgl aaknglllkn analeltnsv ttvffdktgt
      421 ittgefelsq fegndesfki lasleshshh plaqavktee iypvenlkei agrglsgein
      481 grqyyagnak lmeehgydvt sstdtviyla ddvshiatat fkssikqesv qtvaalkkag
      541 iktvmltgdn edsakkiqei vnldevksnl spedkakivq etshsimvgd gindaialas
      601 stvgvamatg sdiameagdv timggkihkl ldlfkisrkt lskikqnyfw afiyniigip
      661 laafgllnpm iaaaamslss vsvilnslll tktki
//
LOCUS       WP_285121081             413 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Lactococcus petauri].
ACCESSION   WP_285121081
VERSION     WP_285121081.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..413
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=47225
     Region          33..60
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          69..94
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          72..326
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          102..128
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(104..105,108..109,111,134,137..138,141..142,
                     144..145,171,174..175,178..179,182)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          132..165
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          170..198
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          203..228
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          236..266
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          271..298
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msysedtidf lhkgdligmh nalsnalkhd neemladlae ylqmmgfide shqvydkilg
       61 dnpestdyli nlaeiaeddg qiddalnyly qipagdenyv aaliqiadly qfegdfetai
      121 skleearels dsplitfala esyyeqgayq eaiqnyakls vreilkqtki styqrigesy
      181 ahlgnfenai sflekslefd ktadtiykia llyseldnqa raisyfkqle dyntdllnye
      241 layaqtlead rqfdeaarva qegllknpns alllhflskl aysqkdqaaa erylmdalnv
      301 aelhdetvfl lanlyfnesd feavirleel leeehllaqw lfaqahkele ndakaealyt
      361 ellstaltdn pdflkdyvdf llqigqneka qtyikqylel vpedeemrgl lfe
//
LOCUS       WP_285121230             404 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Propionibacterium
            freudenreichii].
ACCESSION   WP_285121230
VERSION     WP_285121230.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..404
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43298
     Region          155..391
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtgglppvls dqrratitah lvahsgeltt rvveaiqsrh swftrlgaee rswitvvara
       61 gidnfiswfa ddakadvnpg slfnaapral trkvslhqtv dlvrttvdvv geqinelvpp
      121 qerralelai vyfsrdvafa aaelyaraae lrggwderme aliidavvrg eaddmvvsra
      181 salgwhsqga vmvvvgpsaa gadlesyrha aealglavla srqggrvili gsgeqltdrd
      241 aalalvarle srfgvgniiv gplapdlana nraartalaa arvayawpdc prvassaqll
      301 peralanqdd arealleaiy kpladaggel lhtaasfleh gsleatarsl fihpntvryr
      361 lkriaqttgn sltnprqayv lrlaitlgrl aegqeegana rmhr
//
LOCUS       WP_285121345             373 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Propionibacterium freudenreichii].
ACCESSION   WP_285121345
VERSION     WP_285121345.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..373
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=39332
     Region          1..371
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mltrrsiarr fltgaavvvg vavvtifvvd alvspaifha hlmqadlsnp etvlrhveeg
       61 mrssnmiala vailiavlaa llvslylatr vsaslaplaa aarqvaagdy tarvdagplg
      121 aefdelteav namsqrlasv eqsrtrlfsd lahemrtpia vvqaqlegie dgvvgvedsi
      181 pvlraqaerl trlssdigll sraqehalry efapgevasv vrgcvddmal ryreagvqlt
      241 ldvatharaq ldtarfaqvi tnllanalna tvsagrgrtg drgghvhvgv rrhgnevavq
      301 vrddgvgisp eelphvfdrf arvgpardrs sggfgigltv araimsahhg risadspgpg
      361 rgatftvtvp vlh
//
LOCUS       WP_285121348             358 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lactococcus petauri].
ACCESSION   WP_285121348
VERSION     WP_285121348.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..358
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=40766
     Region          <21..334
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mktierqkvn efeangkttl rkvnkfknfg elaldwfegy rtavtensae tmwssfnvyi
       61 lpalgkykle kittpliqsi inkwvqntnv avkgkrsrpt gyaknvklnl gtirrilqhg
      121 felgvikdnp almvsvgklk eepsdtlkyf dadnlkkfff ylnsladvyv nrwdttlymf
      181 liatglrvne alaltwddfd fdkgivsirk tmtrkvnlqe ktksqssmre ipldeitldm
      241 mlafknrttt efmgkniyni evvfpsnvgg hrarancmkr lkkhyqnagv pdigfhgfrh
      301 tqssillnag adykeiqhrl ghssikitld tyshlapdka ketarigqes lkklgfgs
//
LOCUS       WP_285121351             349 aa            linear   BCT 25-DEC-2024
DEFINITION  lactonase family protein [Propionibacterium freudenreichii].
ACCESSION   WP_285121351
VERSION     WP_285121351.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..349
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=38179
     Region          6..347
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 mstqlcyvsg rrdglittvr fddkaetaev vsrlnlgpkp mplelnrerr llrvatgadp
       61 lrvstlkllp dgscqvlsev ncplsatyls ftpddrmafv vsyhasrlaw apvwdnhlid
      121 dsawhveqvg eqphcvepsp dgrhvyvvel ganrvqgfrv sdgelvadeq igvqfehgtg
      181 prhlvfdasg ehgylieelg ghivhltrdp dsgrltvaer vpysdraddl rpgvhvpsgs
      241 tpslddqtlr hwgaelaldp qrhwivaser rastlnlqal nddgsfgarl dhvptekqpr
      301 gmgligdhhv iagaelgdta tiyrvddqle pvaeveglgg pvwfaslda
//
LOCUS       WP_285121394             853 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Lactococcus petauri].
ACCESSION   WP_285121394
VERSION     WP_285121394.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 853)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 853)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 853)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..853
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..853
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=96336
     Region          <17..>82
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mvgkfvkesg askqahqval vsfgdeatvl qaftpdekql lsalekietr gktnlhsglk
       61 qaeqllqavk degqknifii sdrtpttgek lntgkygnkd iysyqfanaa dnlaqkmkte
      121 qqvsfrtfvf idkiadstka fartffqniq tdgafdfrdv qdmdfvfksk eagkefqsgt
      181 fnygsapagk egrdsqavyh ysdsyfeqsa yayrqeknrp ydprlatmsl nlelaawssi
      241 qeknyllkir naknlleeig fekfkanqhf qerpstdsig aviaqkkltv keedytlial
      301 airgggyeae wasnltlgrs gehqgfreas ekaltfldqy lkehkvtgkv klwingysra
      361 aavtnltaga lnkgrklasg elkaedmyaf cfeapagtlk gtgnregrhd nivnvinvnd
      421 vvtkvgpevy pfeftrygqd sslpdktllp qevyetaksr meaelkklds nliykleefq
      481 akkisildif nglivddpkg krmneslddi irffaverik nrnkyvnahq edirilaaly
      541 fttrvedrek ltkslfknlv tsmmlgsdat kvkkivvdwl rtmglvnhse vrieslaetf
      601 relvfkfmik hpnlsvtlvs nldpvaqahh pdlclawlra qdenyqkeki etpepsktsk
      661 riliagdvdi kvkretgeme eystdevmel stsaaedttv lvqaseatkv dytvqtidnm
      721 dgsvflteef edvelnagek veinlykese nkatelikeg eqlssetrgk eesskyyatn
      781 vrvenenlgf vlgggmtrfa nysplysipr enaefvgwyk gdellssent yqhqvkaeee
      841 lvakfrevks ddq
//
LOCUS       WP_285121591             407 aa            linear   BCT 25-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Lactococcus petauri].
ACCESSION   WP_285121591
VERSION     WP_285121591.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..407
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=41928
     Region          31..390
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mkkklitalm lstvvltaga pfaavkadst dskiaqqdsk ianakneaak aqsqvdsiqs
       61 qvstlkskqt smtkkvnelm aqqkeqsqqi qklsesiker ntaleaqars aqtdgsatny
      121 msavldsksl tdaiqkmtam atvaganksm ieqqqadqka iqtkladnqk kyaeatklqq
      181 eldaqanela tqeaalkvaq ldyqatvtta egkkqdllsq kaaaekaaqk aaaaekaaaa
      241 ksvvaqqeka vaaapaasnp apaanntadd snsstpstgn ntggngnssk ptpeptpept
      301 ptpdpghsgt npypagqcta fvwdyfggnm ptymgnagdw vayansgpaa gtiavfppgn
      361 qgaggvghva vvlsvsgskm tviegnfngg wgttrecsta gvsfirp
//
LOCUS       WP_285121675             264 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Propionibacterium freudenreichii].
ACCESSION   WP_285121675
VERSION     WP_285121675.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..264
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28308
     Region          99..245
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 massnaaksa srreqlraar ereaaaarrk ritvvavavv vaavlvavia maaggvfgkr
       61 sggsgatstv vsvrpphasp gdkgvfsadn vndsapvltv vdyfqcpich tyetvfgpvf
      121 eslakkgeir leyrtryfld inlkndssvr aaraaaiadi fgkyqeyhdt vfsnepakeg
      181 vgytddqlrd afpqaagitg ddlstfqssy dkgemnafvd avdrqaqadg yngtptflan
      241 drkidmprkt npteddimkl vrgv
//
LOCUS       WP_285121686              67 aa            linear   BCT 25-DEC-2024
DEFINITION  integrase catalytic domain-containing protein, partial [Serratia
            nevei].
ACCESSION   WP_285121686
VERSION     WP_285121686.1
KEYWORDS    RefSeq.
SOURCE      Serratia nevei
  ORGANISM  Serratia nevei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Ballandras-Colas,A., Maskell,D.P., Serrao,E., Locke,J., Swuec,P.,
            Jonsson,S.R., Kotecha,A., Cook,N.J., Pye,V.E., Taylor,I.A.,
            Andresdottir,V., Engelman,A.N., Costa,A. and Cherepanov,P.
  TITLE     A supramolecular assembly mediates lentiviral DNA integration
  JOURNAL   Science 355 (6320), 93-95 (2017)
   PUBMED   28059770
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (5), 302-307 (2001)
   PUBMED   11774877
REFERENCE   3  (residues 1 to 67)
  AUTHORS   Dyda,F., Hickman,A.B., Jenkins,T.M., Engelman,A., Craigie,R. and
            Davies,D.R.
  TITLE     Crystal structure of the catalytic domain of HIV-1 integrase:
            similarity to other polynucleotidyl transferases
  JOURNAL   Science 266 (5193), 1981-1986 (1994)
   PUBMED   7801124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10461024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Serratia nevei"
                     /db_xref="taxon:2703794"
     Protein         <1..>67
                     /product="integrase catalytic domain-containing protein"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016893 - endonuclease activity, active
                     with either ribo- or deoxyribonucleic acids and producing
                     5'-phosphomonoesters [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
     Region          6..>66
                     /region_name="rve"
                     /note="Integrase core domain; pfam00665"
                     /db_xref="CDD:459897"
ORIGIN      
        1 dalstgrrik cltcvddftk ecltvtvafg isgvqvscil dsialfrgyp atirtdqgpe
       61 ftcrald
//
LOCUS       WP_285121741             976 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Lactococcus petauri].
ACCESSION   WP_285121741
VERSION     WP_285121741.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..976
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..976
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=101863
     Region          <67..963
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 msksdcgdls lgykyykkir rknkrrknka lhqyfklvly tftlfilspl spvvnwmpsl
       61 gtlsaeasit qqtdgsgitw nlitvgndin tlattalpgs tlyikaandl tlgvtavlpl
      121 nltlvfdmgg halyntgaav itpsvgntit fqnerivstg ttnsttvpsp lgvgtvagvy
      181 nyyyglfsat nisgvsityk nvvqdlgtit twgaggqpfy nigssvnfsg tnyfnynsgq
      241 efmegtginv ldgtttikhs sggnaplwaq saasinvaag atldftgsst grgfiyldnt
      301 ptftinnngt lklnmagass nnfysntgms sitmnygvns sttitapgff dynatggafk
      361 ttigqgasfd ysagntsnaf lgtlaatdsf tlnsakhvrl ntskttgssi lgtdasampf
      421 vlnasspsay aingynstga asllasptsg afgvtgtfhs nladlnkltg qkiptateit
      481 syqnsaqlef nlvspaqanf syvwaanvpg qngiagtllg qlparvseqg tvggvltapt
      541 lsaapkgyyi sgykapngti ystlaaalaa vnnvfgttsn tttpdvymps tndfqvilsa
      601 eeqtfyinyg yaftnfgnvp pfppnaysqk gltgaplais glgaaptgyh ysavmnnkgs
      661 swidqtnpet gaantptpyy vsislaltaa itqqnggmyf gtsslsaapi innqgafdnn
      721 vmamltanae ianytygwan itpgyngnag qiygnlpsqt tsnggfgdti ardtsginsp
      781 gnnyqtfvap pndkalsgys vavrapngit ytsdsnavas stviktttpl ttatqantfk
      841 egaaannfvi tytpiankis whytydpsis nppaapadiv qtgvltgtpl tdpkatapng
      901 yfiegyqypg dakiyptiae lqtahfsgts ditinvllak nfvlpytggs gqfgiilasa
      961 tlaflalafy ifkrkd
//
LOCUS       WP_285121769             215 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Lactococcus petauri].
ACCESSION   WP_285121769
VERSION     WP_285121769.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..215
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24333
     Region          3..208
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 msfntiifdm dgvlidteyh yaqvfdaffd kkgipiahln rrellgrplr dlwpfilged
       61 fdkkdaarlq kefftykkss hfpieeilfp dvkvvlqrls etklkiglat ssshdeiaev
      121 ldthnlrkyf evissgedfp eskphpavyl stmkqlnasa sdvlviedsp ngiaagkaag
      181 atvwairdqr fdsdqsqadr rvehltevle lldfs
//
LOCUS       WP_285122010             206 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Lactococcus
            petauri].
ACCESSION   WP_285122010
VERSION     WP_285122010.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         <1..>206
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
     Region          <6..206
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 etvvtgfyfk lnyfnnslln qfieesmlyr ffvestsydt envshyfiyq fstmddvhfy
       61 ilsllkqvvk mcyfnnkltk aafvllivem sqmtdsclcl hdsdisnnvl akeilnfien
      121 nirtvsleni sqkfhfhpny lsalikketg csysewlikf ridyakkyls qtdlsvqqii
      181 eevgysdkty ffklfkehvn mtpgay
//
LOCUS       WP_285122110             198 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lactococcus petauri].
ACCESSION   WP_285122110
VERSION     WP_285122110.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..198
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=22719
     Region          1..68
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mvvnrlkevl eerkmsfsdl rnllfenkki kvnnsqlsly angkrnprnk klwldisevl
       61 nlklqdivnd ieaylyitqe isetgnekns eiengkrnts lfhelitlid etkaselekv
      121 qrycslaatf eklgadilee gaviyvpsgd ymvkktnpai veqvrvnaal ikldeffeek
      181 rtskpknsge kdwskftk
//
LOCUS       WP_285122200             152 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Lactococcus].
ACCESSION   WP_285122200
VERSION     WP_285122200.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus (lactic streptococci)
  ORGANISM  Lactococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Lactococcus"
                     /db_xref="taxon:1357"
     Protein         1..152
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17490
     Region          8..60
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(9,13,39)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(12,38)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(20..21,32,35,39..40)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mrtidillqn lrkyygvdsl rdlakkiems gdvllnwssg rsspkldqld kiayltnvev
       61 fnllvqdtei siispiwrdn vgrnfienlg rysqekgihk swfdenpcgi sygafryyin
      121 gnnktvnlnk ldelakilgi qtyqllesre nr
//
LOCUS       WP_285122230             148 aa            linear   BCT 25-DEC-2024
DEFINITION  Dps family protein [Lactococcus petauri].
ACCESSION   WP_285122230
VERSION     WP_285122230.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Choi,S.H., Baumler,D.J. and Kaspar,C.W.
  TITLE     Contribution of dps to acid stress tolerance and oxidative stress
            tolerance in Escherichia coli O157:H7
  JOURNAL   Appl Environ Microbiol 66 (9), 3911-3916 (2000)
   PUBMED   10966408
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 148)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   6  (residues 1 to 148)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..148
                     /product="Dps family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16635
     Region          8..147
                     /region_name="DPS"
                     /note="DPS protein, ferritin-like diiron-binding domain;
                     cd01043"
                     /db_xref="CDD:153102"
     Site            order(21..22,26,28..29,40,51,55,58..59)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:153102"
     Site            order(28,40,44,55,59)
                     /site_type="other"
                     /note="DPS ferroxidase diiron center [ion binding]"
                     /db_xref="CDD:153102"
     Site            order(123,130..131)
                     /site_type="active"
                     /note="ion pore [active]"
                     /db_xref="CDD:153102"
ORIGIN      
        1 mskektqevl nqtvadlsqa aalvyqthwy mrgsgfltlh pkmdefmdgl nehldefaer
       61 litiggspvs tlkefdeksk ielqpatwdk smserlhgvl dtykylaklf qegmdiaese
      121 ndavtvdlyt valgdvekti wmleaelg
//
LOCUS       WP_285122309             374 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [Lactococcus].
ACCESSION   WP_285122309
VERSION     WP_285122309.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus (lactic streptococci)
  ORGANISM  Lactococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Lactococcus"
                     /db_xref="taxon:1357"
     Protein         1..374
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43653
     Region          64..372
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mwvetlpngk ykyieryiep ytektkktsi tldkntaqsk kqaltllqek idkltnknni
       61 takitlsely eewfsrykit vkqrsalats kamkkvfvyv pknnlvknmn rqifldffde
      121 iysfgnlsya ytvqikntls nmlnyavere yidknpissi kikrkkdqee nhkqkmdekf
      181 lereeideii iylkknknnl lhariveflw ltglrygelq alqwknyngt sievngtlgi
      241 nnekispktv asnrivdlpq kakdilqetk tanklyfdrv eaddyiflsn rnlplgvqsf
      301 nrilkkaeke cniskplssh ifrhshvsll aelnlplksi mervghsnan ttlkiynhvt
      361 kktreeviea lnni
//
LOCUS       WP_285122461             380 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lactococcus petauri].
ACCESSION   WP_285122461
VERSION     WP_285122461.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..380
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43854
     Region          62..375
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 masiryrqrk gksgvswsye irqgdktlks ksgfktkkea sidglsilre fktgltidkn
       61 sslpalykdw ydlkvknsgr sdetlkkyry ygklieknfe dipvatikps qyqrimnklg
      121 teenvsyntl irvnsvirqt iemvkaddvf ikdfttnvvi qsnfksqtad ekyihsledf
      181 dkiikylkdn ldykksinny ivyflfhtgl rygelvgltw sdidfengyl ktyrryntni
      241 nkfvpsktet sirrvplsst dieileslkk iqesivkslg feneydlvfy hpflihgiph
      301 sttinnhlal vlkqlniqpi itskgarhty gsvllakgys mdvvskllgh kdimmlvrvy
      361 ghaleenisk qiesikklld
//
LOCUS       WP_285122579             325 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Proteus mirabilis].
ACCESSION   WP_285122579
VERSION     WP_285122579.1
KEYWORDS    RefSeq.
SOURCE      Proteus mirabilis
  ORGANISM  Proteus mirabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Proteus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Proteus mirabilis"
                     /db_xref="taxon:584"
     Protein         1..325
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=37894
     Region          2..323
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 milsiqylra iaammvvffh ilaklesssl hdnffyvgaa gvdlffvisg yimvyitekk
       61 etspvyfils rferiypiyl lftlialciy iinpslinss getsvimsff yiplenklml
      121 vqvgwtliye mffyllffis miinyknrit iciliiiafn iifynsrnyq fnflsnqiii
      181 efalgmlsyf ivkviknnyi slcfiffgis fliinnkynv drlvdygipm fslflgvvsi
      241 dvnkknnnyn fkvlkligds sysiylihlf tigvsllifk nitfniyffi lfsfllsvcs
      301 giafhiivek riinffkkvn kklnl
//
LOCUS       WP_285122614             649 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Proteus
            mirabilis].
ACCESSION   WP_285122614
VERSION     WP_285122614.1
KEYWORDS    RefSeq.
SOURCE      Proteus mirabilis
  ORGANISM  Proteus mirabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Proteus.
REFERENCE   1  (residues 1 to 649)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 649)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 649)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 649)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Proteus mirabilis"
                     /db_xref="taxon:584"
     Protein         1..649
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=74162
     Region          44..617
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
     Region          <589..649
                     /region_name="OM_channels"
                     /note="Porin superfamily. These outer membrane channels
                     share a beta-barrel structure that differ in strand and
                     shear number. Classical (gram-negative) porins are
                     non-specific channels for small hydrophillic molecules and
                     form 16 beta-stranded barrels (16,20)...; cl21487"
                     /db_xref="CDD:473880"
ORIGIN      
        1 mkltplcclf lvllpcsvia qttyqqsipd vltvwsspia anpdvltqqq mleqnkvnaa
       61 qalatlpgiv mqksgnrney tlkvrgfdsr qvpvffdgip tyvpydgnld larfttndla
      121 sievnkgyts llqgpnlmgg ainittatpr kpleghiays qgfargadya hnmsarlgar
      181 teygfiqisg sqlqqrftpi pnadennnav gthgrrshsa tddkrgmikv gwtprasdey
      241 tltyvkqdgn knsppnsdpn akgrykywaw pdynkesyyy sgvtqltdsi nlqsrayhdk
      301 fentlymypk kgnrvdyshy ddhstgaalq fgidmeesdl lsfavhwkdd vhraqkekng
      361 dwvrfkdrtw slateyqwvv sndldvvgai sydwrksidt dkkadnnkqn ainweimaky
      421 slanddnirf tisdrsrfpt qkeryttekp kdgsrgiinp nldperalsf dmtyegylne
      481 kwsyqtslyy nrvsdaimah tlyrhgealf qnqnsgrvdy lgldigtkgk mtdwlelgln
      541 ysyihsdpkq vdhieglpkh kaymwltfip veqvrftime eaqswtynri dennklagyt
      601 ktdlrldydv gygisvnasi nnlfdksyqy tqgyiedgrn ywlgaeykf
//
LOCUS       WP_285122677             399 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lactococcus petauri].
ACCESSION   WP_285122677
VERSION     WP_285122677.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..399
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46327
     Region          81..393
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mkvedikvgs lwsetrknkf lwrmryfniv tksedkvsvt ltsnsnqakt karkilltka
       61 krkieqseln ilnsrlnins ltfssvanlw lndcsrrlkp stlnnrrkqi krfadefgdq
      121 emsqfttfqi qvffnslnlk sgtvkgyflt cksifdfakr meiiskdptl nvklslskkt
      181 ledikkqnrk lftvedlakv lnrmrssens rtyfialtie flfltglryc elaalkeeny
      241 drtrriikve tnldytkgvt khthtttktl ssyrevdlnd rgieiieeyl kanhdntyvg
      301 yknhgyifct rsgqphnigh lnrsfkyygk atgldkqfsc hcmrhshisl laemginqkv
      361 vmqrvghats titnniythv tpnmskelnk kmnrinkis
//
LOCUS       WP_285122906             340 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase [Proteus mirabilis].
ACCESSION   WP_285122906
VERSION     WP_285122906.1
KEYWORDS    RefSeq.
SOURCE      Proteus mirabilis
  ORGANISM  Proteus mirabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Proteus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Proteus mirabilis"
                     /db_xref="taxon:584"
     Protein         1..340
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=39446
     Region          2..338
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mqlfnddals vlkalpdnsi dliatdppyf rmkscawdnq wdnveaylsw ldevlvefwr
       61 vlkpngslyl fcgsklasdt ellvrgrfnv lshiiwakps gpwkkqnkes lrtffpster
      121 ilfaehyqkp itakgsefsl kcqelkqnvf kplidyfina rlalqvsake inqatgkqmc
      181 shwfsnsqwq lpseedykkl qilfthiadk heklsplsrq ftelereqvt lqkdyqelik
      241 eygllrrpff vtadvpytdv wdyppvqyyp gkhpcekpsa mmehiirsss regdlvadff
      301 mgsgatlkaa lklnrkvlgv elererfeqt eqeikaltck
//
LOCUS       WP_285123029             379 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lactococcus petauri].
ACCESSION   WP_285123029
VERSION     WP_285123029.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..379
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43843
     Region          63..376
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mwvealengk ykyferyrdp lteklkkvsi tldkntsraq keaqrllqek idkhvkdanv
       61 snitfwelye eyfknwsptv kdsskrglia hdnrikdnip kstparnitr rtiqklvnem
      121 mdegyaysyy ngfkkrfhsi ldfgvrmgyl dkneasyvks pkkvksfeev qekresylel
      181 seikqllkil ritprvdhla nfvefmaytg arygetaalt tkdidlengl vtingtydra
      241 lkikttpktd fsyrtitipd niikiiesql ellelnrsvk gkdfnknnyi ffsvngsaid
      301 ldtlnvvirr aaekakinkh ltshifrhsh vallaelgip lsaamervgh idykttlsiy
      361 shvtksvkvd ivkklnelk
//
LOCUS       WP_285123082             375 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lactococcus petauri].
ACCESSION   WP_285123082
VERSION     WP_285123082.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..375
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44482
     Region          65..371
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mfykklengk yryfekyfdd nqgkwrqvtv tmnsksrvsq seaknklsrk iddclsksqk
       61 kniptiqevy lewrqlrnee iksstqnvee nafkkfirkf gsknitevtp qeiqyfllns
      121 glsgttrnlr ksyyklffey aagvgyvein pmqqvalprs katmeevhrk qnkfltqeem
      181 killnhisky svhkrkgllf eflfltglri gealalrwqn vdvenkllnv hhtlnchgyv
      241 pndrqllspk tiysyrtisi ndrcieiley fhermqkdef lflsnrgrif ntnnltyafk
      301 klceeclgee tenrkynlhm lrhshitllv emnvpiklim ervghsdekm ilqvyshvtk
      361 kmkenldekl nnlsi
//
LOCUS       WP_285123104             172 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lactococcus petauri].
ACCESSION   WP_285123104
VERSION     WP_285123104.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..172
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20329
     Region          13..70
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(17,21,46)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(20,45)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(27..28,39,42,46..47)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mktkdlgnke imsenikrhl nnkrlnikef aeimnfkytt vldwvnakty pridkielma
       61 ryfgvdksdl veeysetpst lyeinkvsek ldeprqkivl etaniqlkeq keeekkntnv
      121 ipikkkrltd eelwdvvehg vasdgseqte yekqfffnll rekldnddsy ed
//
LOCUS       WP_285123270             613 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Prevotella bivia].
ACCESSION   WP_285123270
VERSION     WP_285123270.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 613)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..613
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69729
     Region          6..603
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mqtrchlavl iheqakkfgd kpvltykdfg gsdwktvvws efstrvkevs nallnlkvkp
       61 qetigvfaqn cveylytdfg aygiraisip fyatsseqqi qymiqdasik llfvgeqeqy
      121 dkahrifplc pmleriivfn knvristhdp naiyfedflk lganlprqse vehlwgqvam
      181 ddicnilyts gttgdskgvi ltnkmydaai dangkcvpit dkdrvinflp fthiferaws
      241 ylaltfgael ivntdpkeiq rsmretnpts maavprfwek vyiavkdrmd nasflqrkvf
      301 ynalmvgrrr nvfyksrgkr vplglelkyr fynstilslv rkqlglihpn lfptagayvs
      361 peveefihsi gldmlvgygl teslatvscd hkgkaytigs vgrpisgiei kigkdnevll
      421 kgptitpgyy hrdainasay dkegffhtgd agymkdgely lterikdlfk tsngkyiapq
      481 mvesmllvdk fveqvaiiad qrkfvsaliv pefgllekwa kdhnisfadr eelcanervn
      541 emmkdrietl qqhlaqyeqi krftllahhf smesgeltnt lklkrsvvvk nyadtinamy
      601 eepdlttqlp sie
//
LOCUS       WP_285123486             696 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Lactococcus petauri].
ACCESSION   WP_285123486
VERSION     WP_285123486.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 696)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 696)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 696)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 696)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..696
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78299
     Region          3..496
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mlhtifyvii fllalvisni inkvfpklal pliqvviglc lgflgaskll qvdpefflgf
       61 iiapllfres eeadvkhifk htrtilmlif plvfittigl gylthffyls vplaacfalg
      121 aslaptdaia vaalserfsf pkrvmsiltg egllndasgi isfqiavlal vtgefsltha
      181 sadlvvsaig gvlvgfilvw mksfilrile dvdardvtgy lilelmlpls afliadmlev
      241 sgiiavvvag vmqanglkrt tlfdaqvtkv kntiwnlltf vlnstvflfl gielhqlvfp
      301 liadplystt sllfmvlllt iglfalrfsl lavyyryvsl rrnqsfsayw ndillltfag
      361 skgtvsiatv lllprtvdip hsliiflcaa vtalsfltgl fvlpliaakk vvkvdnmvki
      421 siladvvrel endlkqvtke karlgyniai dsyqdriqkl iieqessnts idfnelqlli
      481 vrleaeglen alrqneismy tyrtyqrylh smeqsvahnl vssiqfasai sirvlhfffs
      541 riirldfsfr ktrpdnatah reitelyfsn telvlqaldn lesvyderli hylqaerlrs
      601 aefvarggyi tgilhraqpn nlkemmrayy lerktifeye srgeltigea kvlrqnvntl
      661 edyslasnhh tllydfiekr rkkvqkttnn elstnk
//
LOCUS       WP_285123509             388 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lactococcus petauri].
ACCESSION   WP_285123509
VERSION     WP_285123509.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..388
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=45949
     Region          71..383
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mftkkqangk iavfekfyde krkkyrqarv tmnnssrqsm searrllaik idsmlkepte
       61 eeillekkks ilvselyeew rvirkkelke ttyftqgqif dvllrdilnr plfeittqdi
      121 hdiifagnrs dttkrnykaf lkqlfdyavd lnyieenivk kiklhkrkit vedvrnsenr
      181 yvdiedlqkl ieyvnsgkmn ksnnhkyyae nqkrylyayi fmfctglrig elqalryinv
      241 eenvariens lnrktfreed rvlttvktvq syrkvilneq alealnyfkn nkldddfifv
      301 nqqgkimvyk tmqqnfkklc eralgkkktp hmlrhgfvsy aseigvneka imsqvghaks
      361 dmtlhythlt knmrnetanv lnkmalkl
//
LOCUS       WP_285123572             457 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Lactococcus petauri].
ACCESSION   WP_285123572
VERSION     WP_285123572.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..457
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=51144
     Region          31..389
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 miqltkftpp tleenlrpvg ltddtmaqrr qklldkmtqd nfdcliiyad lehgsnfeyl
       61 tgflprfeea llvlhkdska ylvlgnenln kadkarlkae avhmphlslp nqpmntqetv
      121 eeilsqcdle htqkiglvgw knftstkedn yqlfdvphfl vhavqslcpk ailenatrlf
      181 igengvrttn nanefahyef gaalagrcml namnqielgk semevarels dlgqahnvvt
      241 imatgerfvk aniypsdkvi kkgdklsltt gykgglqsrg gyavsqasel pdeekdylsa
      301 vaqpyfnavk twleaikigm qgqelynkie evlpqekygw tlnpghlsad eewmsspvyp
      361 qstesiesgm lfqidiipsv sgyggvsces gifladaqlr qeikeaypdi wgrvqerray
      421 iqnelgitlr deilptssat aylrpfmldk asaftvk
//
LOCUS       WP_285123607             649 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Lactococcus petauri].
ACCESSION   WP_285123607
VERSION     WP_285123607.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 649)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 649)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 649)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 649)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 649)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..649
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73099
     Region          1..527
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 msavsfiavm ligviaanvi keffpkiset filigvgill sflpefrhfe lepeffmmli
       61 iaplmfnegs ktslkevrkn frgifflsit lavvtvlfva alttnimgsw ifplaicfaa
      121 ivtptdsvav ksiiagkkmp qgvneavefe slfndasglv llslglsvle sghfsiwrgl
      181 gqfafvsigg iliglivgtf lvririainl ratnpeatii pisiltpfal yllaehfgts
      241 gvlavvaagl ihnfegdmlk ltstnvqltn ntiweilsgi lnnfvfillg vslfgiwdif
      301 kslgleeavi lffisalvyv lmlfirkfwt nqrgnrsieh ffsndkkers kdstifalsg
      361 ahgtmtlama fslplntail stenreiiis mativillsl ivptfilpkl lspmkaassd
      421 didsvrndmv dyailhmmqv iedskvrssl tkqlqsqkgl qipdhnkssr llenivtwqe
      481 afldssdiqe nfsakaidyf riylensskr amskkirrmf srrsrlrgad qsemqefiav
      541 rnelghledv lyeatmekln rlererfekk vtdfsdieev krvfenrhyr mrneiqeeti
      601 vpnellieaf qleyqyvldq vksetisket snklfkeinn aqvlqlqnq
//
LOCUS       WP_285123610             405 aa            linear   BCT 25-DEC-2024
DEFINITION  MDR family MFS transporter [Lactococcus petauri].
ACCESSION   WP_285123610
VERSION     WP_285123610.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023665
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..405
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44979
     Region          11..400
                     /region_name="MFS_MdtH_MDR_like"
                     /note="Multidrug resistance protein MdtH and similar
                     multidrug resistance (MDR) transporters of the Major
                     Facilitator Superfamily; cd17329"
                     /db_xref="CDD:340887"
     Site            order(21..22,25..26,29,60,115..116,118..120,123,143,
                     146..147,150,224,227..228,231..233,236,273,277,326..327,
                     331,335,351,354..355,358..359,362)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mkefwglhpt ikirlvmnfl galcfstvgg smtiyynkym gagitgllli vssimvflvg
       61 lyaghltdlk grrpvmlfst avtavgaala tfsnsgfyfn plttffgfli vnfgfgffnt
      121 asqamivdlt tsenrrtvys iqywiinfai migsglsgwf frdylvwlll vitieeilsf
      181 vvvlfwides fdphqehqkk apniikayff vakdsifmsy lfasvfiami fnqidyylpv
      241 hlsdsfsttr ilglelygqr mltlfllint liivlfmskm nqltknwsrs tgitlgiflq
      301 glgfiiaflg hnlswevtaa vvatlgemil vpfsqalrad lmegdhvgty tgafsvtqpv
      361 asvlsgvlvs lsalygnigm aifmgiiill silpslrair myeas
//
LOCUS       WP_285123642             918 aa            linear   BCT 25-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Lactococcus petauri].
ACCESSION   WP_285123642
VERSION     WP_285123642.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 918)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 918)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 918)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 918)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..918
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..918
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=100437
     Region          2..914
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mefykkakee vieeflvdtk tglnheqilk qrelhgenkl pdeeeesyla tflksfkepi
       61 vivllgaval sfassyyafq fqndskhgme alyeaiaili liiinaflgf yqeisarksl
      121 nalkemnnry vtvlrngqfe kilstelvtg divkasigdf veadvrwiet nelqvieshl
      181 tgeadaiskh tdailettel gdrhnmgfsg ssvsggqglg ivvavgehte lgkiakliqa
      241 venrtsplqn tvhkltktlm qvsagivvft lvvgiiqage lsiasitsvl stsialavas
      301 ipdalpavls ivltigaakm aknkgliksl nsvetlgsts yicsdktgtl tknemtvthf
      361 ytngqyyevs glgytpegei rslsdeeqes sysafiagal lcnesalkev egkfvpfgnp
      421 teialtvlgq kagrtktqll eshelirtlp ftsdrktmsv ivkkgdnyll yikgapdvlv
      481 eksrallidg elnteesekq kfittvndya nealrtlavg yrilskeeae qgqledlekd
      541 iiltgvagii dpareevkas vktlqeasve vvmitgdhen taraiaynlg ivkskeakvi
      601 kgieieemtd eelyavvktt nvyarvspeh kqrivkqlqk hgevvgmtgd gvndapalra
      661 adigiamgia gtevtkdsad lillddkftt iektvengrt iyaniknfir helttnvaev
      721 lslilgllff tvsignvdyt tptltalmvl wvnmvsdavp sfalgydvae sdimnekprd
      781 pkesvlanyt wsrvlirgti mglmvfvafv waakqgmssn eaqtvafltl vygqlwhvfd
      841 arssqtlfrr npfgnprlvl avvfagissf lvtiipffnv vmgtaplsls vyllvlfvpa
      901 lptfilsgik eifkvkiw
//
LOCUS       WP_285123825             524 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Lactococcus petauri].
ACCESSION   WP_285123825
VERSION     WP_285123825.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..524
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60583
     Region          <176..>302
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mlntlhqhlk dprkckifws lifgliwlgt niyvimetpv wnekyitafi lgnicmfiaa
       61 aymvfvyrsv kkigtltesk iqhyykmsmw ilglavllvp fffiihvpdt ahdwdffvif
      121 rdtmqlggrs fthlpmtede llyflrypnn qffgivyntl fapfttnlsr iiattvvaai
      181 ltslsvlggs liikkisnlk maliynlvaf gfipfylyga qlytdtatlp fvifgllfmi
      241 yalqsektsk miiwwiaacl vvffgysikp tvfipmiavf cflvlnrkwk kllimvpvaa
      301 llfvgvhqgv kavianepaf seqandrynl pmihwvtmsf dpinkyggfn pdvlaysqsf
      361 tdvaskkegi khrfienlke mgvpgvlvql wrkimytwfn gdlsnffyty rhsnpfifry
      421 fdwtsfapee gnitgwllik aaqtlywlai vplmwyeifl gifkkhktew fivglsmagl
      481 tgflllwean srylynfapi mlilatmglv dfiqrsrrkn gise
//
LOCUS       WP_285123837             369 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Prevotella bivia].
ACCESSION   WP_285123837
VERSION     WP_285123837.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..369
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41484
     Region          5..369
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mdnkqitvts pllpdlnelq pylediwqrk witnnghyhq elekalaeyl dvpyislftn
       61 gtlplitalq alritgevit tpysfvatth aiwwngckpv fvdidprtgc mdpnkieaai
      121 tprttaimpv pvygkpcdtd aiqeiadkyg lkviydaaha fgvkvngksv lnagdlstls
      181 fhatktyntv eggalvmhda kmkqridylk nfgfanetev vgpginskmd eiraaiglin
      241 lkhvdaaiea rhkvaeqyra alrniegisf wedmpgvqhn ysyfpifvda kkygetrdel
      301 yfrmrennvl grryfyplis tfstyrglps aapanlpvat kmaeeviclp myhllseedv
      361 qrviecikk
//
LOCUS       WP_285123879             203 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Lactococcus petauri].
ACCESSION   WP_285123879
VERSION     WP_285123879.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..203
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23463
     Region          3..192
                     /region_name="HAD_sEH-N_like"
                     /note="N-terminal lipase phosphatase domain of human
                     soluble epoxide hydrolase, Escherichia coli YihX/HAD4
                     alpha-D-glucose 1-phosphate phosphatase, and related
                     domains, may be inactive; cd02603"
                     /db_xref="CDD:319790"
     Site            order(9..13,109..110,148,172..173,176..177)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            143
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mtvkniifdl ggvildldfe rmtqqfyklg ipdfedyftl kkqvdffeal elglitpegf
       61 cdrlreeakv dvdneaieea wnlilkdfss ermnyleris ekyniflfsn tnsihakcfe
      121 krcleqtgrt lesyfkqvfy shslhlrkpd mvafkevles sglqaaetlf iddnlanivg
      181 aqkvglqtih lqkpqtildl eid
//
LOCUS       WP_285123897             278 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Prevotella bivia].
ACCESSION   WP_285123897
VERSION     WP_285123897.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..278
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31062
     Region          20..>278
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mkksillfss lliamiafgq nkkliilhtn dthsqiyeln pnmadtirag rggflrrinl
       61 lkeeraknpd lllfdsgdfs qgspyytmfk gdveiglmnr mhydavtign hefdfgldnm
      121 trlfkmanfp vvcanydftg telakivkpy iiikrngvki gvfglspkle glvakenygs
      181 lkyldpvqta qqmvyalkak kcdliiclsh lgwniegddd qkvmrgtkgl dlvlgghshs
      241 fftqieyvkd lsgrlvgndq ngksgiylgk levnlkkk
//
LOCUS       WP_285124002             937 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Prevotella bivia].
ACCESSION   WP_285124002
VERSION     WP_285124002.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..937
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=106458
     Region          29..424
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          517..935
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mryckvirll fiffalaigs ssiasvcnai klpqgtikgq lsnglsyiik rnahprntte
       61 frlvmrigal qqtdaqggta hflehmafag sksyhgfsmv halegkgmkf grdinaytsf
      121 dktiyslsvp tqsnttkgtr qilgmmrewl dgltfapdyi ekergiilee lkqydthddf
      181 ytlkigdnhy srrmplgsvn dikavskaml hdfytkwyqp rfatvvvvgd idptmverml
      241 kdaftsalnt nhtvlpaysf thkkgwdmht llsplekehk veliiphqgi teksiqhsse
      301 khlgnivvhl lnnrmksrni rvdcsdtwyl adknffsvtf qeadtaallh svtcfanewn
      361 tilqkgfdsd efvaalhdki aaikveerek tsaewcddfi dyiimhdisp tspedieaik
      421 aylstcssqs aqrilscwaq aseqtvlvay tapqeeahel tvqaiqgawq kglakaplsy
      481 tykatktvee tlvstppcla kkalydhkqi rseqsyanig vrdillsngi rillrptkdg
      541 skafsiegfg rggtadlpds vyyqyenaaa yiemggiqkv nrdtlfnyla qnnisldtni
      601 ssywhgfigv aptkkahhlf nlitekvtap einveefket vreemasfgk ttplqerikh
      661 dkdrviinmr dsimgdapsm vrekqtledi kqldiykman yfkslyddth nltlvltgdy
      721 elqpmketvv gvfskwqqrk psssamvyhs mpqqpyrsmv sspdeqqldl hfifagsflp
      781 slhetlilkl mrdviqnrll evlrqrenit yspftdlayh gldghryyfd mmltldrknv
      841 kkaqdllaei vrslqmkpis iaelnrlkls fkatktkvls ddatavwrte lvnkikngem
      901 lsdfnqydai ldsitpkkiq egftkylnpd kfiilgl
//
LOCUS       WP_285124049             372 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lactococcus petauri].
ACCESSION   WP_285124049
VERSION     WP_285124049.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..372
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42902
     Region          58..361
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mplrvyprgk kweyrirdsk gkhvsskggf lnqkeatvag kqaeldflkg trfdnsstvy
       61 dlyqkwynle ilpsnrsqqt klkyqkflkk idkyfgnlva skikysqyqq imneiglsvg
      121 pdylsrlnss irsaiqlarr dllnindftl gvklhaqklp krpedkyiss lsdyhkilty
      181 lrssmdydks impyliyimf ktglrvgeal altweeidfs rkliktfkri dsanhtdtgk
      241 pktpysirei pvgddvldml nklhkeqent nmlelssnli ffdkryglpt nnginkalkt
      301 yltklnitpl ivatgcrhty acvllakkvd iavvaknmgh kniqriidty ghvlnelkee
      361 enratrsale yf
//
LOCUS       WP_285124056             342 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Prevotella bivia].
ACCESSION   WP_285124056
VERSION     WP_285124056.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..342
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40644
     Region          18..329
                     /region_name="WecH"
                     /note="Surface polysaccharide O-acyltransferase WecH [Cell
                     wall/membrane/envelope biogenesis]; COG3274"
                     /db_xref="CDD:442505"
ORIGIN      
        1 mkikdielen isryrgelmg aamlfvilfh vglprddmff glrrmgnigv diflflsgmg
       61 lwfswskhpd tkdfylrrwl rvyptwlima clyyipdftc pnwvhhrghs tniidligdi
      121 sinwdfwlnd eltfwyipat mmlylvtply lkviikhpiy rwspivmlmw cilvqyvtpi
      181 heavghleif wsrvpiyfig inmgaaikrk drmdgaaiwm illmffmala ssifleqvkh
      241 gqfpiflerm lyipltvtsv lmlnrvfrrt pkwfnksvkf igmvsleayl ihdhfvlryl
      301 etfdwtywnt ffatiaitip lawtlhfvve kivitplerl ik
//
LOCUS       WP_285124071             346 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Prevotella
            bivia].
ACCESSION   WP_285124071
VERSION     WP_285124071.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..346
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=38732
     Region          26..344
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mntvltldik qfadnfplkd klrnqtiait gatgllgscm trcllmlnrk hqlklrviai
       61 vrnaekarqm fgeetksfgi ltydfaqhvp fdapehidyl ihfaaptask afveqpietm
      121 ntvffgtnsl ldyarkthls sfvlastlev ygtiyddsia lteekqgyld pmatrssypl
      181 akraaealch nyaseygvsa kvarlaqtfg agvaiednrv faqfakavik qqditlntmg
      241 elsrsycytt davsamlyim lrgeageayn vaneksyisi cdmakmvlhr fypqgklifn
      301 lqeglgfspt tklrlsttki ehlgwqatfs leemfnrlik hlkesm
//
LOCUS       WP_285124321             389 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Prevotella
            bivia].
ACCESSION   WP_285124321
VERSION     WP_285124321.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..389
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=43771
     Region          1..389
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mkkifknihv wlaipigivf viisftggml lfedeitava qadmrtvern gkkalpadkv
       61 maiaqahlat letantakdk qkaegkqakd deepimlksl tiaadptqay kvnlnkkrqa
      121 lyvnqytgev kgkatrletm ttiqslhrnl lqkrpkddsf flgkavigws vlivllifit
      181 gfliwlpska svlknrlsin atkgwrrfwy dlhvaggfya ltflliiait glcysfpwwr
      241 sglyslvgak yekehkekaq agekgdkprt ldahawqkva dqlaktnpny ktievsegea
      301 kvsfdrwgnq hasdnytfdn qtgkitkaer yenqkaekql ggliyslhvc swggwfskil
      361 gllvtligvi lpitgyylwa krtlrkskk
//
LOCUS       WP_285124323             377 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Prevotella bivia].
ACCESSION   WP_285124323
VERSION     WP_285124323.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 377)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..377
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43496
     Region          16..375
                     /region_name="COG1672"
                     /note="Predicted ATPase, archaeal AAA+ ATPase superfamily
                     [General function prediction only]"
                     /db_xref="CDD:441278"
ORIGIN      
        1 mdnpfafgka vegrfftdrq edtkrlranl thgintvlis prrwgktslv kkvmaleenn
       61 pkvkmvmvdv fackseyefc kllatevikq tsskidewve mgknflsnim pkfsfgsdpl
      121 ndfeisfewn qkdetcaeil clpekiaekk gvrivicfde fqqiadfkds lsfqkklrta
      181 wqhqqsvtyc mfgskrhlmm gifadtscpf ykfadmmflq kipkeewvsf icnqfettgk
      241 mispenakhi cditeclssy vqhmawivwy ktdmlvvdkl idqaleelle qnkvffqrdi
      301 esltrlqknf lialadgvat glttkniigk yhlessanvq svkqsmvske fidvvgseis
      361 fndpifkiwi qrnvpli
//
LOCUS       WP_285124351             432 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Prevotella bivia].
ACCESSION   WP_285124351
VERSION     WP_285124351.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..432
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47280
     Region          2..429
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 msyeetvqyl fnstpvfehv gaqaykegls nthlldkhfg hphtqfktih vagtngkgsc
       61 shtlaailqq egyrvglyts phlvdfreri ringemiseq yvidfvaqer sffeplhpsf
      121 felttalafk yfaeqqvdia iievglggrl dctniitpll siitnisldh tqflgdtlak
      181 iayekagiik envpvvvget vpetrpvfea takeksapie faedipffsa httastkgia
      241 ysdtpfgtii gelmgdyqvk nantvlhacv kliqlgiike eqsivkgfan vtattglmgr
      301 wqqladhplt vcdtghnlgg wqylskqiks aakgethivf gmvddkdlda vlallpqnah
      361 fywtqpsshr afpvekvaee alaiglkgtq yptvlaayea akaaaspddf ifiggssyvv
      421 sdllsahtrt nk
//
LOCUS       WP_285124444             785 aa            linear   BCT 25-DEC-2024
DEFINITION  efflux RND transporter permease subunit [Prevotella bivia].
ACCESSION   WP_285124444
VERSION     WP_285124444.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 785)
  AUTHORS   Sandhu,P. and Akhter,Y.
  TITLE     Evolution of structural fitness and multifunctional aspects of
            mycobacterial RND family transporters
  JOURNAL   Arch Microbiol 200 (1), 19-31 (2018)
   PUBMED   28951954
REFERENCE   2  (residues 1 to 785)
  AUTHORS   Hand,N.J., Klein,R., Laskewitz,A. and Pohlschroder,M.
  TITLE     Archaeal and bacterial SecD and SecF homologs exhibit striking
            structural and functional conservation
  JOURNAL   J Bacteriol 188 (4), 1251-1259 (2006)
   PUBMED   16452406
REFERENCE   3  (residues 1 to 785)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
REFERENCE   4  (residues 1 to 785)
  AUTHORS   Arkowitz,R.A. and Wickner,W.
  TITLE     SecD and SecF are required for the proton electrochemical gradient
            stimulation of preprotein translocation
  JOURNAL   EMBO J 13 (4), 954-963 (1994)
   PUBMED   8112309
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..785
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..785
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87631
     Region          7..781
                     /region_name="MMPL"
                     /note="Predicted exporter protein, RND superfamily
                     [General function prediction only]; COG1033"
                     /db_xref="CDD:440656"
ORIGIN      
        1 mkiekinrkf rqtaewilrh rllvtglfal lvafsfvgtk rivmktsfdd yfvsddpmll
       61 ktdefksifg ndyyvavlvk nkdvfskrsl tlirelsnel kdslsyadkv tsltdlefav
      121 gteegmtieq ivpeqipsda aslkeirrka yskpylskkl vskdgtmtwi mvklrpfpad
      181 svwkktsdia pdmvtgkeag riitkakyae lspnaagmpy msyekfvyle gemgrlfaia
      241 flvsivvmli vtrslrgvia plvtsvcalv igfgiigwtg lyidmstami aviltfacsi
      301 aynihlynff ktrfvetgrr kasitdavge tgwgvllsgl ttiaammtfl amsivpmkai
      361 glntslclls vlltclvvtp vllslgrdrk phanmshsfe gyvgdhferf ggfvirnhrr
      421 ivvvslvltl fcgiglfsie pafdvektmg rkveyvkkfl dlcdtelgsm ysydlmitlp
      481 haddakkpen lkrldklati tegylltkrh nsvtdiikdm nctlngskqq fycipddadm
      541 vaqllllyen aggteseywm dydyrrlrlq veiknynsne aekemdalqa earrlfpqah
      601 ismvgnipqf tvmqqyverg qmwsmllsvl vigvilvlvf sswkvglvgm ipnlapaviv
      661 ggmmgwldyp ldmmtaslip milgiavddt ihfinhshva ydrcgdygga irstfrtegl
      721 aivmstvvvs atfagfmssn atqmvnwgil avagmvsall adlfltpilf kylrvfgkek
      781 ktnsq
//
LOCUS       WP_285124451             692 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein [Prevotella bivia].
ACCESSION   WP_285124451
VERSION     WP_285124451.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Porat,A., Cho,S.H. and Beckwith,J.
  TITLE     The unusual transmembrane electron transporter DsbD and its
            homologues: a bacterial family of disulfide reductases
  JOURNAL   Res Microbiol 155 (8), 617-622 (2004)
   PUBMED   15380548
REFERENCE   4  (residues 1 to 692)
  AUTHORS   Kimball,R.A., Martin,L. and Saier,M.H. Jr.
  TITLE     Reversing transmembrane electron flow: the DsbD and DsbB protein
            families
  JOURNAL   J Mol Microbiol Biotechnol 5 (3), 133-149 (2003)
   PUBMED   12766342
REFERENCE   5  (residues 1 to 692)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   6  (residues 1 to 692)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   7  (residues 1 to 692)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   8  (residues 1 to 692)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   9  (residues 1 to 692)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..692
                     /product="protein-disulfide reductase DsbD family protein"
                     /EC_number="1.8.-.-"
                     /EC_number="1.8.1.8"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=75713
     Region          241..685
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 mkttkilsll vmlfvsvlgf aqgqpvhfsv qqkqvsptev dvifsatidk gwhvystglp
       61 adgpisatvt tekavgaepi gkliasgqek nvfdpvfsmk lryfenkvtf iqkykitgkt
      121 yhikgfleyg scddeqcmpp tdvefdykgn gpataptake tvaettageg ktvesaldal
      181 pavaatdtma kamvagdsvv apiaapalsk dveaqwwtpi ikelkafnet tgsqsqslwy
      241 iflmgivggl valltpcvwp iipmtvsffl krakddrkkg irdaitygis iiviymglal
      301 litaifgpqr lnalatnapf niffflmllv fafsffgwfe lalpskwgna vdnkasattg
      361 llsiflmaft lslvsfscta pvvglllvqa vtsgdyiapa vgmfgfalal alpftlfalf
      421 ptwlkqapks gswmnmikvv lgfielafal kffsvadlay gwhlldrevf lslwiaifgl
      481 lglyligmfk fphddvdgkp mpvpaimlgl vslaftiymi pglwgapcka vsafappmnt
      541 qdfnlapttv haaytdyeeg mraaaatgkp vlidftgfgc vncrkmeasv wsdkrvadkl
      601 mkdyilisly vddktplkep ikvkrtdgte rtlrtigdkw shleeskfgy laqpfyvpld
      661 nmgkplngsy sykedipayl dfldkgleny kk
//
LOCUS       WP_285124477             410 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Prevotella bivia].
ACCESSION   WP_285124477
VERSION     WP_285124477.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..410
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45947
     Region          <14..410
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mnttelqktk qrynivgnns glnraldval qvaptdlsvl iigesgvgke iiprvihdns
       61 prkrerylai ncgsipegti dselfghekg sftgaigese gyfgiahkgt ifldevgelp
      121 matqarllrv letgeyirvg gtetkktdvr ivaatnvnvr kavsegkfre dlfyrlntip
      181 iqmpplrdrg ddilllfrlf amqmaekyhl pkvvltdeak qimlhykwpg nvrqlknite
      241 qisilseepe itaekllqfi pldqestqla tisgggshsy esereilyki lyelrgnvsd
      301 lrrdlnsvrk qledntalkt artyvahhtp nvpavaskap ipteetrvet veeaeaeeis
      361 epatlnlndi grqmiekale rnkgnrkkaa qelgisdrtl yrrikqygle
//
LOCUS       WP_285124496             190 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II [Prevotella bivia].
ACCESSION   WP_285124496
VERSION     WP_285124496.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..190
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21369
     Region          4..187
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 mctliidnyd sftynlyhll qsaapknerf dvlkndeitp stllkyhriv aspgpgvpae
       61 agnllhifht ienkvpylgi clghqafaea ygaklyqlsh pihggttkvn inthsplfkq
      121 mksettvvry hswavekenl phelemvsat ndgmimalqh kkyplfgvqf hpesfmtpng
      181 lqmlqnfyai
//
LOCUS       WP_285124517             184 aa            linear   BCT 25-DEC-2024
DEFINITION  UvrB/UvrC motif-containing protein [Prevotella bivia].
ACCESSION   WP_285124517
VERSION     WP_285124517.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10489946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..184
                     /product="UvrB/UvrC motif-containing protein"
                     /calculated_mol_wt=20902
     Region          152..177
                     /region_name="UVR"
                     /note="UvrB/uvrC motif; pfam02151"
                     /db_xref="CDD:308001"
ORIGIN      
        1 mekvkllysg itqlvdssdl ylivlenmek trqiaivcne dierelakrl vehadtstcl
       61 pevmclihpm mnnlhyeili sgitdgnyka flinkddlsy tpirvtdail ialvarleiy
      121 ideqlfrhqs caininterv alpinalntd mlksaldkai asedyesasy irdelnrrnn
      181 rdka
//
LOCUS       WP_285124658             476 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Prevotella bivia].
ACCESSION   WP_285124658
VERSION     WP_285124658.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..476
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55172
     Region          145..464
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtrrhytgnq lfwfvllllm lystcfiifq hnrekdfkvd vlclklqdyn nqiaeammqe
       61 ssnkeltlnh yinehttkfl rvtiidttgn vlydnirkdy tkiknhanrk efylakrkgf
      121 gvdtyrpsqt tglkyfycan yypkqaivvr salpyndela rqlttdrhyi wfaliitiil
      181 aivlyrfthr lgknitalrh famkaesree idpaelssfp ndelgeiseh ivtlftklek
      241 trkeqitikr qltqniahel ktpvasihgy letiltseri ndeqknifln rsfeqckrla
      301 slvddlstln rledapdlhh fqtfnvtevv knieqeaalr lqnnsmrfyn flpkeliing
      361 nqnliysifr nltdnaitya gadttitlsy qngvytfadn gigiseehis rlferfyrid
      421 kgrsrklggt glglaivkna islhggkitv cnvyphglkf eftlspniie eeeqss
//
LOCUS       WP_285124751             255 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Leclercia
            adecarboxylata].
ACCESSION   WP_285124751
VERSION     WP_285124751.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..255
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28770
     Region          19..249
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          162..244
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqhdispilt dlingvsplr qvhfassaeq iphvsprlmi vpegqthdav fsssghvplq
       61 pttclsisfg kqqltiqlqr datvlcqqqv arrgprtgaf llqtlaelqm qpdeqetarl
      121 vvlsllshcr dllgsdihta shsralfeai rtyieehhas altresvaqa fyispnylsh
      181 lfqktgsvgf neyltktrle harqllkgyd lkikeiathc gftdsnyfcr lfrkhtersp
      241 seyrrqyhsh ltakn
//
LOCUS       WP_285124787             445 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Propionibacterium
            freudenreichii].
ACCESSION   WP_285124787
VERSION     WP_285124787.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..445
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48196
     Region          2..444
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mgagfggltv atqlvrrghd vmvleardri ggrvdnarfs sgelveqggq wvfpnhdrml
       61 elideaaaat mpanpgkllv vqqgdvrave qspdehshrt pfaaadlgqg vlrlrrlaer
      121 tvsdpawaga ntawldqpme rwltanlrap saqrdlrgal ravvhgplsd ttlgdvlthv
      181 ragvdmenli atngdigqvr lvdgvlqlae rmaaqlegrv rlstpvvtid qeddavvvvt
      241 segeqirart avlsvppwla kdlvwapqld pwryetvqkt pagaiikchm lferpwwrda
      301 glsgqmaadd gpvrvtfdts dpasergilm gffegaeaat ltkfsasmre rvfrdalvtv
      361 fgeqaatple yldhdwgadp ftkgshgahf apglwsvtgq qlgarfgrvh fagaeyaskf
      421 ngymegavrs gtdtaaqvvm qlhgq
//
LOCUS       WP_285124881             332 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Leclercia adecarboxylata].
ACCESSION   WP_285124881
VERSION     WP_285124881.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..332
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=36668
     Region          <179..271
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mhwqpfrgta ptsmtiysas fpdvsdnwpm kdevtrelna vdralkadpq lmppliekda
       61 sgektikcqh hwsekafatr pavvawrtrl vptalalyai qnplddhlpd gtrmdsrsrq
      121 wfihandaig irsrakvlsv laaqylgndi dnvwvslasg aavpvlealr gaqldgqkvh
      181 ltlvdydpvs lrwaekmaaa eglkvgeqvt ilprdliegl irsdkliqel gegnvelvda
      241 lgifeyfndt davtflkhvl rllkpdgali isnmltsspq idfalrcigw tpifprtlqq
      301 lqdihlaagi paenvtvivp kdgvyavmev rv
//
LOCUS       WP_285125049             881 aa            linear   BCT 25-DEC-2024
DEFINITION  copper-transporting P-type ATPase [Propionibacterium
            freudenreichii].
ACCESSION   WP_285125049
VERSION     WP_285125049.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 881)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 881)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 881)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   4  (residues 1 to 881)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   5  (residues 1 to 881)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   6  (residues 1 to 881)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18340165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..881
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..881
                     /product="copper-transporting P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005375 - copper ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006825 - copper ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=91115
     Region          18..45
                     /region_name="HMBD"
                     /note="Heavy metal binding domain; pfam19335"
                     /db_xref="CDD:437167"
     Region          59..86
                     /region_name="HMBD"
                     /note="Heavy metal binding domain; pfam19335"
                     /db_xref="CDD:437167"
     Region          185..211
                     /region_name="HMBD"
                     /note="Heavy metal binding domain; pfam19335"
                     /db_xref="CDD:437167"
     Region          228..877
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     human copper-transporting ATPases, ATP7A and ATP7B;
                     cd02094"
                     /db_xref="CDD:319783"
     Site            order(530,532,833)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Site            order(574..576,639,655..657,682,722..724,744,747,750,769,
                     772)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319783"
     Site            order(834,862,866)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
ORIGIN      
        1 mseashptit pgtgpgvvyt cpmhpevreg spgrcpicgm nlvpadeqgg spapqahavy
       61 tcpmhpqire atpgrcpicg mnlvpadeva gasdghapmq mdhsagpshp adssstqgnh
      121 pmamttdhtt paatmasgtt pkhdhttpgh dmqghdmhgh dmqghgtpap gapsdqadas
      181 gvtwytcpmh pevrvdhpga cpicgmalep vvttartgtn peltdmrrrf wagvvitvpi
      241 lvlsmvrplf ggfmdavgdq laawlelvla tpvvlwagwp ffvrgaiswr tgklnmftli
      301 smgtgvayvy sliatiapgv fpqtmrtaqg tvepyfeaaa mitvlvllgq vielsarart
      361 sgsiralldl apkkarlvmp dgtehevavd tlqvgdrvrv hpgekvpvdg vvtdgashid
      421 esmvtgepmp varhvgdrvi ggtlntqgsl vvkadklghd svlsgiialv ssaqrsrapi
      481 qglvdkvaaw fvpivlglav iafivwmlvg paprlphaiv vavsvliiac pcalglatpm
      541 avmvgvgraa tagvlirdae aleelskvnt lvvdktgtlt mghptvtqve ttadhdqsev
      601 lrlaagaekg sehplaravl eaaatrtltv pdvsdfhats gagingtveg hhvcigneeh
      661 arpneeltaa aasmrtrgat avfvsvddkp aavlaiedpl kptsrkalaa lvdagvhpvm
      721 vtgdaeatar avadelgide vhagvmpdgk vqvinqlkaa ggvvamagdg indapalaaa
      781 dvgiamgggt dvaiesagit liggdldgiv rachisnatm rtirqnllfa lvyntagipl
      841 aagvlypafg wllspmfsaa amalssvsvi gnslrlravr l
//
LOCUS       WP_285125116             231 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Leclercia adecarboxylata].
ACCESSION   WP_285125116
VERSION     WP_285125116.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 231)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 231)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..231
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25130
     Region          25..98
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlktrlppdn stalelavaa vaatmadpsr vkmlcammdg rawtatelsa vadvapstas
       61 ghltrlmegr litclsqgrh ryyrlaghev aelveqmmgm swgritppet tapesmrhar
      121 tcydhlagtv avqiydfmqa egwlvadgsa ltlsgreafl slgivlnart rrkaccacld
      181 wserrfhlgg eagaallvhm dtkgwiqrva gfrdvsvtps gqraidrhfs r
//
LOCUS       WP_285125262             728 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Leclercia adecarboxylata].
ACCESSION   WP_285125262
VERSION     WP_285125262.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 728)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 728)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 728)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..728
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=78483
     Region          68..728
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mnhtrkmnkt llalaigaia hsavaaeskk eetivvqsaa sdfkpggdql vpafldgqva
       61 nggrmgmlgq qnamdvpfni isytsklved qqahtiadvv andagvqsvq gygnsaesyr
      121 irglkfdgdd mtfgglsgvl prqvvdaqmv drieifkgan slmngaassg vggminlepk
      181 hagatpqakv gvdytsdsqi gttldagrrf gdsdqfgarv nvvhregeap vandrrrttl
      241 lstgldyagd dfrtsmdlgy qkktfhgset gvnisgvdfv peppkndrny sqkwaysnie
      301 nefgmwrsey disdnwtayt glgaqhahee glysgaklvd ksgkatasrl dtnrisdsvs
      361 gmagirgnfa tgfvthkvnv gysamtknek iawkmsaakd npvtniyhnt gvdappstns
      421 ngaggnysdp ltsgrtrtqg wllsdtlgvl ddkllftvga rhqkvvirgy nkvtglenag
      481 dsfdgdrwmp tygvvykpwd eislyanhte alqpgktapn tainygqstg ivhskqnevg
      541 vkadfgrvgg slalfeikmp saildsqtky ygldaeqrnr gielnvfgep tlglrlnasa
      601 twlqaeltkt nngvnqgnda igvpsfygvl gaeydikpvd gltatarvnh sgsqyanlan
      661 skklesyttl dlgmryrfav nndqnqmtvr agienvtden ywssvddsgt ylfqgeprtf
      721 kvsvgyef
//
LOCUS       WP_285125263             657 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Leclercia adecarboxylata].
ACCESSION   WP_285125263
VERSION     WP_285125263.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..657
                     /product="PhoX family protein"
                     /calculated_mol_wt=71931
     Region          26..651
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mgkplksvfk kehrddvsnp sanpvfstva emflsrrrfl qmgavagaaa sfpfllkpen
       61 alaavsqpsa lskavslgft sipvstddtv rvpegyiarp fyrwgdatgi kgnlpafkfd
      121 asnttdeqaa qagmhhdgma wfslpqgeqd pahgllamnh eyidngmlft dgtanwsldk
      181 arkgqnamgv siievkksgs dwevvrpsdf arritvntpm qltgparqqa lmktaadpqg
      241 eqvlgtmqnc angytpwgty ltceenwsdi fvkksernal ekrygisdsd esyrwsevdd
      301 rfnvdktpne pnrfgwvvei dpynpnstpr khtalgrfkh egaavtlaad krvvtymgdd
      361 qkfeyiykfv sdnhynpadr eanmqllsag tlyvarfndd gsgewlplvf gqngldkskg
      421 fdnqgdllik trlaadavga tkmdrpewia vdphnsgsvy ctltnnsdrg kegkapvdaa
      481 npranntfgh imhwheeggd paalrfkwdi lvlagrtdta dekakgsmkg aefgspdgls
      541 fdhqgvlwiq tdvssstink kayegmgnnq mvatipgtne yrrfltgprg ceitgiaftp
      601 dnrtlfiniq hpgeggddit dpanpravsn wpdnnpqgrp rastvvitra dggiigs
//
LOCUS       WP_285125451             607 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Leclercia adecarboxylata].
ACCESSION   WP_285125451
VERSION     WP_285125451.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 607)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 607)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 607)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 607)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..607
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=65820
     Region          43..598
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 msyqsdihpr hsawqklrht lsiishepan llavlllglf swiilapvis vllnallvqs
       61 gdegrtgate gtftayyllr tlssrmsdll lwtpllntla valstvaial vvgivlawlv
      121 nrtdiagrkw fatllivpfm lpswtfalaw stlfknhaig gqpgwleamg iqtpnwmayg
      181 yfpivtimvl hyaplviliv gnalkrmdsq meecaqvlga srrviafkii iplvrpalls
      241 aallifadci gefalpyilg lpvhfdtlst glyraigtrq sgvaaviaav imlmgmltll
      301 ldmkmlreak rfvtlggkgv merrhslgrw rsvatalpla fvllgvaipl ltlflstvmi
      361 lpgrfsadnf tldywighnl dtvalhngil lsaefwhtvw ntlvivgsas lacgvlgllv
      421 gyavlrchfr wvaavlrqlt flpylvpgia faaaflslfa vvrgpvpaly gtplililal
      481 iaekmpyasr sgiaamtqlg keaeeaaria gagwfarlrr ivipiqaapl atgillpfis
      541 gikgvslfvi latpatdvlt twslrlidyn yqqaanavvl mialiswagt vmiqkitgtg
      601 ladglek
//
LOCUS       WP_285125562             341 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase family protein [Leclercia
            adecarboxylata].
ACCESSION   WP_285125562
VERSION     WP_285125562.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..341
                     /product="zinc-dependent alcohol dehydrogenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36471
     Region          5..340
                     /region_name="MDR7"
                     /note="Medium chain dehydrogenases/reductase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cd08276"
                     /db_xref="CDD:176237"
     Site            order(43..45,48,149,153,174..179,197..198,202,217,
                     241..242,244,263..264,288..290)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176237"
ORIGIN      
        1 msrtmqrwvl netgrqnlkl mqaeipqpgp nevlvrvnav slnfrdkvii dggmgngmpm
       61 pftpgsdmag vieavgpgtt rfsqgervis sfnadwidgk lnnnaknphy dtlgyafqgv
      121 laeyvvmsee wlvkapqtlt daeastlvca gltawfalie rgglragetv lvqgtggval
      181 falqiakavg aevfvtsssd eklaaaaalg adhginrkke dwveaiyrmt neqgidhvvd
      241 tvggrnfads vravashgri sligmmdthd tsapgvmlll ksptvqgigv ghrraledlv
      301 ravdwvklkp vidksfsfsk lpealkqldq gafgkivinv g
//
LOCUS       WP_285126050              62 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Propionibacterium
            freudenreichii].
ACCESSION   WP_285126050
VERSION     WP_285126050.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 62)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 62)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 62)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..62
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..62
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=6911
     Region          1..56
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mnendkylsq pqaaryvgms vttiqrriad gtlpayragn ravrvkqsdl drmmkriptm
       61 va
//
LOCUS       WP_285126116             452 aa            linear   BCT 25-DEC-2024
DEFINITION  nitrate/nitrite transporter [Propionibacterium freudenreichii].
ACCESSION   WP_285126116
VERSION     WP_285126116.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 452)
  AUTHORS   Yan,H., Huang,W., Yan,C., Gong,X., Jiang,S., Zhao,Y., Wang,J. and
            Shi,Y.
  TITLE     Structure and mechanism of a nitrate transporter
  JOURNAL   Cell Rep 3 (3), 716-723 (2013)
   PUBMED   23523348
REFERENCE   6  (residues 1 to 452)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   7  (residues 1 to 452)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..452
                     /product="nitrate/nitrite transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48642
     Region          43..440
                     /region_name="MFS_NRT2_like"
                     /note="Plant Nitrate transporter NRT2 family and Bacterial
                     Nitrate/Nitrite transporters of the Major Facilitator
                     Superfamily; cd17341"
                     /db_xref="CDD:340899"
     Site            order(53..54,57..58,61,94,149..150,152..154,157,176,
                     179..180,183,266,269..270,273..275,278,314,318,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340899"
ORIGIN      
        1 mattpagapt spgaalqtsg rvltnwnped aatwspriaw rtlaistysm ilafcvwflv
       61 saiapklnsi gfglttgqly wlaampglsc glirlvymfl ppimgtrklv gwssllylip
      121 mfgwffavqn phtsfwvlmv laftcgiggg tfsgympstg yffpkrlqgt alglqagign
      181 lgmsiiqlvg pilmgfslfg itwlapehta sgnlwvhnaa iffvpwtiva ailaftllkd
      241 vpvkasfrqq idifsnpdtw lmtlmyvmtf glfsgfsaqf gllinstyge tsrfagmaal
      301 pqgvtyaflg pligslvrag wgplcdrfgg aiwtfisgvg lvvtlgwaal flnpsdpgqf
      361 pgflwamlim fffagignag tfkqmpmimp krqaggaigf taaigsfgpf figialsamn
      421 aavwfwicaa fcalcsvicw iryarprapf pg
//
LOCUS       WP_285126651             430 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Propionibacterium freudenreichii].
ACCESSION   WP_285126651
VERSION     WP_285126651.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..430
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44944
     Region          68..212
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 msfsplaaqa apasadggts stprsvatst ssagvdpasa cgdlvqlapv lssdhtpdgk
       61 qitpkptadg rrvpviivhg wvsydthsda rdhlfsqyvd rtadpaggtg yllaqsqyrs
      121 sligmlqqvp gaevytfdys qvgsrwvtdp qigpklsqai eclsdsyqqk pvlvthsmgg
      181 lvarqalsnn dskgrpisgr vsnvlavgap nngsdsaqmi asaltigsei plaglpirml
      241 wdyigqcskq mdatnttctg iravdafrss ggealrtgsa qlaqlpwwpd nvkvtayvgd
      301 iqmggislfg lnsprlldlg dllvsvdsak agsqrsrqvn ceygiistks aetglvrlml
      361 agqgnsveqp adllsspcfh eamlhettit gdlqrdltev lgantawhdp atageqsaga
      421 ttvsavresr
//
LOCUS       WP_285126675             227 aa            linear   BCT 25-DEC-2024
DEFINITION  IMPACT family protein [Propionibacterium freudenreichii].
ACCESSION   WP_285126675
VERSION     WP_285126675.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Park,F., Gajiwala,K., Eroshkina,G., Furlong,E., He,D.,
            Batiyenko,Y., Romero,R., Christopher,J., Badger,J., Hendle,J.,
            Lin,J., Peat,T. and Buchanan,S.
  TITLE     Crystal structure of YIGZ, a conserved hypothetical protein from
            Escherichia coli k12 with a novel fold
  JOURNAL   Proteins 55 (3), 775-777 (2004)
   PUBMED   15103642
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Okamura,K., Hagiwara-Takeuchi,Y., Li,T., Vu,T.H., Hirai,M.,
            Hattori,M., Sakaki,Y., Hoffman,A.R. and Ito,T.
  TITLE     Comparative genome analysis of the mouse imprinted gene impact and
            its nonimprinted human homolog IMPACT: toward the structural basis
            for species-specific imprinting
  JOURNAL   Genome Res 10 (12), 1878-1889 (2000)
   PUBMED   11116084
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..227
                     /product="IMPACT family protein"
                     /calculated_mol_wt=24110
     Region          12..216
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 msqsvesass gdhfvtlrap mrneqeikrs rfiaclypvs ssqqarehia elrkefydar
       61 hrpsafvlga ghteartsdd gepagtagap mlqalvahqt apgrrdlsdv lavvvryfgg
      121 iklgaggltr ayggavseal trasfvvrqr mqlvdvhlpl aeagaieaal rnsslhvvat
      181 rwtstegivq vahvpgeddl treavaaltg glarltdags ewttral
//
LOCUS       WP_285126769             417 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Propionibacterium
            freudenreichii].
ACCESSION   WP_285126769
VERSION     WP_285126769.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..417
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=47319
     Region          60..413
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mrlppatgrv vrnallgilg aqlgaagvlv aadnvrkhra gparfprsav tqaradddlv
       61 svysygedly ndmltairra khtiffetfi wkndpigqdf kqvlieaanr gvavyivydq
      121 fanmvvrpsf frfpdnihvk rhplvqsvaf wnlrnsgrdh rkilvvdsrv afmggynigs
      181 ryartwrdth arfegpsvad fenafvdywn lrpvhllssq rssmpelpdt sqrrwdgsvr
      241 lsrntprwav fpirnmylea idkaqrniwl tsaylipddd lrtalaraaq rgvdvriivp
      301 aqsnhviadw lsrgyytgll rdgirlflfh namvhaktat idghwstigt anidrlslag
      361 nyevnaeits pqvataleri fltdqsncte mdlarwerrs ivakgtewll apwrplf
//
LOCUS       WP_285126846             629 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Propionibacterium freudenreichii].
ACCESSION   WP_285126846
VERSION     WP_285126846.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..629
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69820
     Region          17..615
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mnsvreeils acppsypasf rarvarapha vayrvpqhqe pevwkdltws qvadevdqia
       61 agfialgvqp eqrvaiaamt riewvladlg iacaaaattt vypnsqpdde lfilqdsesv
      121 ivvaenwkql qkvvdqseln aqvhhivlfd ddrpidrada ggdrvvtwda lhalgrdyla
      181 ahptalderl dlmepdtlat lvytsgttgr pkgvriphra wtyqgeamhh mwrgiiddrd
      241 vvylwlplsh vygrdllaaq maigfimpvd gridrivegm gethptimvg vpriyekirs
      301 avitqspang iqgriarwaf avgresrpyr lagkhapwpa rlryavadrl vfsklrdtlg
      361 gsirfmisgs aklstqvqtw fysagllvle gygltetaai aavnlpdkpk fgtvgpvtpg
      421 idariaadge lllsgpivad gyyhlpeeta eafedswfht gdishfdedg yltitdrkkd
      481 lmktsngkyv apqkveaall anvpyisqav avadghpyvi alvtmdhdql mrwgknhghp
      541 nddyatlsql peiresidkf vrkanerldr wetvkrhail dhefaqdtge ltpsmkvkrp
      601 vvlaryekti ddlyeqttvs dltpftggk
//
LOCUS       WP_285126900             247 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Leclercia
            adecarboxylata].
ACCESSION   WP_285126900
VERSION     WP_285126900.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..247
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27566
     Region          11..237
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          156..237
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtytrhvnqt flrqpgvelr stwqstqayk rhshaqlsig ailegqtcct cngepftlyp
       61 gdlivipahm phscnpvaeq prsyhmlyle tdhqpalqvi rsealfrqyl avvdtlsata
      121 idrflallta rptppvplrp tslalqqtlr hslqtppsld alaqrfslrk etlirtfkqd
      181 tgltpgtfln vtriefakar lragddiadv syqsgfadqs hfhktfvsyt aatprqyatg
      241 rsisdnn
//
LOCUS       WP_285126966             629 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Propionibacterium freudenreichii].
ACCESSION   WP_285126966
VERSION     WP_285126966.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..629
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69878
     Region          17..615
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mnsvreeils acppsypasf rarvarapha vayrvpqhqe pevwkdltws qvadevdqia
       61 agfialgvqp eqrvafaamt riewvladlg iacaaaattt vypnsqpdde lfilqdsesv
      121 ivvaenwkql qkvvdqseln aqvhhivlfd ddrpidrada ggdrvvtwda lhalgrdyla
      181 ahptalderl dlmepetlat lvytsgttgr pkgvriphra wtyqgeamhh mwrgiiddrd
      241 vvylwlplsh vygrdllaaq maigfimpvd gridrivegm gethptimvg vpriyekirs
      301 avitqspang iqgriarwaf avgresrpyr lagkhapwpa rlryavadrl vfsklrdtlg
      361 gsirfmisgs aklstqvqtw fysagllvle gygltetaai aavnlpdkpk fgtvgpvtpg
      421 idariaadge lllsgpivad gyyhlpeeta eafedgwfht gdighfdedg yltitdrkkd
      481 lmktsngkyv apqkveaall anvpyisqav avadghpyvi alvtmdhdel mrwgknhghp
      541 nddyatlsql peiresidkf vrkanerldr wetvkryail dhefaqdtge ltpsmkvkrp
      601 vvlaryekti ddryeqttvs dltpftggk
//
LOCUS       WP_285127017             222 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Propionibacterium
            freudenreichii].
ACCESSION   WP_285127017
VERSION     WP_285127017.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..222
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=23945
     Region          <1..201
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mrisivgagn vgrsiareli anghevllie kephaiksdt vpeaewllad acemdslaea
       61 dlqtcdvsia ttgddkanlv htllaktefg vprtvarvnh psnewmfdeq wgvdvavstp
      121 rimsalveea vsvgavvrlm tfkkdsanlv eltlpedspa vgkrvrdlsf pgdgvlvaiv
      181 rdgrsrapeq daavevgdel lftiseeher elshylvpvt kg
//
LOCUS       WP_285127123             623 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Propionibacterium
            freudenreichii].
ACCESSION   WP_285127123
VERSION     WP_285127123.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 623)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 623)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 623)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..623
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64828
     Region          23..617
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mttvtgstsr ttirpqagas lwsridrtdl artlfvaact aalalgldwp sptvpllavi
       61 glvvgcwpvv veawhdirqr rmsmelsmll aiiaagvige wttsllittf vlaaeiledl
      121 smdrgrdalt almsflpttv tlreghttrd ialddvapgq vlvigpgerv pvdgvvdkgr
      181 stldqsritg esmpvdvavg dpvyagsinq vgalevraer vganssygri vtavreaqss
      241 rapvqrmadr faawlvylsi agaivtflvt rdlsatisvi ivagacgiaa gtplavlaai
      301 ariarvgafv kdgahleals vvdtvvfdkt gtltrgvptv tdvrtapgvs tqqllawaga
      361 aeaysehplg raiaahvcaa gvapgtaqsf dyqpgrgvsv evdgrmiaag narlvpdapa
      421 saadgvatpv hvsvdghyag tvlladqvrd sarsvvaelr hrglrvmmit gdqpatarav
      481 adelgitevr agllpdeklr aidaeraagh rlamvgdgvn dapalmratv giamgsgtdi
      541 ardsadvvli ssdlndlaat lhiarrarri vmfnfvgtiv vdvigmvlaa fgllgpvlaa
      601 vfhvgsesaf ilnsarlipg rrh
//
LOCUS       WP_285127151             623 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Propionibacterium
            freudenreichii].
ACCESSION   WP_285127151
VERSION     WP_285127151.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 623)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 623)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 623)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..623
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64866
     Region          23..617
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mttvtgstsr ttirqqagts lwsridrtdl artlfvaact aalalgldwp sptvpllavi
       61 glvvgcwpvv veawhdirqr rmsmelsmll aiiaagvige wttsllittf vlaaeiledl
      121 smdrgrdalt almsflpttv tlreghttrd ialddvapgq vlvigpgerv pvdgvvdkgr
      181 stldqsritg esmpvdvavg dpvyagsinq vgalevraer vganssygri vtavreaqss
      241 rapvqrmadr faawlvylsi agaivtflvt rdlsatisvi ivagacgiaa gtplavlaai
      301 ariarvgafv kdgahleals vvdtvvfdkt gtltrgvptv tdvrtapgvs tqqllawaga
      361 aeaysehplg raiaahvraa gvapgtaqsf dyqpgrgvsv evdgrmiaag narlvpdapa
      421 saadgvstsv hlsvdghyag tvlladqvrd sarsvvaelr hrgmrvmmit gdqpatarav
      481 adelgiaevr agllpdeklr aidaeraagh rlamvgdgvn dapalmratv giamgsgtdi
      541 ardsadvvli spdlndlaat lhiarrarri vlfnfvgtiv vdmvgmvlaa tgllgpvlaa
      601 vvhvgsesaf ilnsarlipg rrh
//
LOCUS       WP_285127259             692 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Propionibacterium
            freudenreichii].
ACCESSION   WP_285127259
VERSION     WP_285127259.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 692)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 692)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..692
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=74503
     Region          19..296
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
     Region          188..511
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
     Region          596..>684
                     /region_name="SPT5"
                     /note="Transcription elongation factor SPT5
                     [Transcription]; COG5164"
                     /db_xref="CDD:444063"
ORIGIN      
        1 mrrmrfplil liviytictv glglipgvdd agnptpamgl fnafyvvsyt gatigfgeip
       61 qpysaaqrmw mtmtiymtvv gwsyslvnil alvqerafqn alrqarftrr iyglrepfyi
      121 vagagetgal vchgldrlgl rfvvvernee rlarmrleef rsdpplivad asqpsvmrda
      181 glvsphcrgv lalteddstn qaiavttrll aprvvvlari rnvetethvg vfggdlvinp
      241 ferfarqlas siiaperyrl reiltglvge pvpdqrqppr ghwimcgygr fghamveelr
      301 stgievtvid eahfdqggvd vrgtgtdses liaagvktad givagnasdt knlaiavtar
      361 elnpgifivt rqnqtantpl fdaflddlsm vpshivaqef larittpllg qylkridqys
      421 ekecavlsdr ltrfgrgrip elwdvvirrg qatavsqrla sghrvtladv ltdpdkrtqr
      481 seaaalmvrr gnksmerpel tmelrpddri lfagstqghg nvslvlqnan algyvqtgqe
      541 gnggvvwrwi tgqrrqseel hdhdavppqe garalaakqr varakaakak aakalsgkpg
      601 grpgrdarga qsgsdgrvna vggrsgqgip vpcgdgptsa gngvpaapaq dtpgappkdd
      661 parqpeadag hgtastgddk gtgpepsase hh
//
LOCUS       WP_285126730             302 aa            linear   BCT 25-DEC-2024
DEFINITION  LysR family transcriptional regulator [Leclercia adecarboxylata].
ACCESSION   WP_285126730
VERSION     WP_285126730.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33430
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="PBP2_CrgA_like_7"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08476"
                     /db_xref="CDD:176165"
     Site            order(100,104,143,157,159,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176165"
     Site            order(101..102,106..107,109..110,113,117,119..125,186,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176165"
ORIGIN      
        1 meslngiaff vqaaearsfs gagrslgvss savgksisrl eerlgvrlfh rstrsitlts
       61 egtlflercr rilseveaae lelsetqqmp sgrlrislpl vsplvmpalt afmfrypave
      121 ldvdfsdrmv dvieegfdvv mrtgeptdsr lmsrplgsyr lqlvaspdyl krhgvpelpa
      181 elchhaclhh rfpstgrlep wplscrpgae elklpttmvc ntsaalldva taglgiaclp
      241 dfmvrqavat gelllvldky idhqgtfrll wpsskylspk irvfidfmvg tlfaemesqk
      301 er
//
LOCUS       WP_285127305             377 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Propionibacterium
            freudenreichii].
ACCESSION   WP_285127305
VERSION     WP_285127305.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..377
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=40577
     Region          128..364
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mttrvveaiq srhswftrlg aeerswitvv aragidnfis wfaddakadv npgslfnaap
       61 raltrkvslh qtvdlvrttv dvvgeqinel vppqerrale laivyfsrdv afaaaelyar
      121 aaelrggwde rmealiidav vrgeaddmvv srasalgwhs qgavmvvvgp saagadlesy
      181 rhaaealgla vlasrqggrv iligsgeqlt drdaalalva rlesrfgvgn iivgplapdl
      241 ananraarta laaarvayaw pdcprvassa qllperalan qddarealle eiykpladag
      301 gellhtaasf lehgsleata rslfihpntv ryrlkriaqt tgnsltnprq ayvlrlaitl
      361 grlaegqeeg anarmhr
//
LOCUS       WP_285127319             266 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-protein kinase family protein [Propionibacterium
            freudenreichii].
ACCESSION   WP_285127319
VERSION     WP_285127319.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..266
                     /product="tyrosine-protein kinase family protein"
                     /calculated_mol_wt=28756
     Region          <18..169
                     /region_name="Mrp"
                     /note="Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG0489"
                     /db_xref="CDD:440255"
ORIGIN      
        1 mttsswsilt saarasprps istaplgllq vlvdstkpen alrptktdgl svlpsfdtpp
       61 npsellgssr maaliqelse dhvvildapp ilpvtdavvl ssladsvlvv vsagrtrveq
      121 lehavdsivr gegkisgivl nrasstklsr lrygdaeygy eysysheyaa drprpdaggt
      181 iassrpdthp hrdsdhratp pddrsdqqaa gqhtpeesse trrmavvnfa eseqwahagv
      241 esghkhqpah eqmgmrrlwr dspkhp
//
LOCUS       WP_285127439             247 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Leclercia
            adecarboxylata].
ACCESSION   WP_285127439
VERSION     WP_285127439.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..247
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27457
     Region          1..237
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          156..237
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mthtrhvnqt frrqpgvelr stwqsaqayk lhshaqlsig ailegqtcct cngepftlyp
       61 gdlivipahm phscnplagq prsyhmlyle tdlqpamqvi rnealfrqyl rvvetlsata
      121 idtllsrlaa gptppaslrs tslalqqtlr hslhkppsld vlarrfslrk etlirtfkqd
      181 tgltpgtfln isriefakar lragddiadv syqsgfadqs hfhktfvsyt aatprqyatg
      241 rsisdnn
//
LOCUS       WP_285127452             231 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Leclercia adecarboxylata].
ACCESSION   WP_285127452
VERSION     WP_285127452.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 231)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 231)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..231
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24779
     Region          27..100
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlktslppdn satlelavaa vaaamadpsr vkmlcalmdg rawtatelsa vadvapstas
       61 ghltrllegr litclsqgrh ryyrlaghdv aalveqmmgl swgritppet tapesmrhar
      121 tcydhlagtv avqiydfmqa agwlvadgsa ltlsgreafl slgialnant rrkaccacld
      181 wserrfhlgg eagaallvhm dtkgwiqrva gfrevtvtas gqraidrhfs r
//
LOCUS       WP_285127761              72 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: transcriptional regulator [Enterobacteriaceae].
ACCESSION   WP_285127761
VERSION     WP_285127761.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008341
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..72
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..72
                     /product="transcriptional regulator"
                     /calculated_mol_wt=7643
     Region          4..63
                     /region_name="YdaS"
                     /note="DNA-binding transcriptional regulator YdaS,
                     prophage-encoded, Cro superfamily [Transcription];
                     COG4197"
                     /db_xref="CDD:443351"
ORIGIN      
        1 mnaldkaiaa vgsatklael lsisamnish wrnrnggqvp qmrvlaifha tgvtphelrp
       61 dlypnptdgl pk
//
LOCUS       WP_285128030             187 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Leclercia
            adecarboxylata].
ACCESSION   WP_285128030
VERSION     WP_285128030.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..187
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19864
     Region          76..137
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 malynfiltl sgvtyetegl edalyasgcd dalicaygrs vyvefdreae sldaaissav
       61 dniesagiga ivgsvdsalv glsdiaemtn msrqaiamlk dgtrgsgdfp cpiqrikgqs
      121 plwdwgdvah wlssngrlkq dselvvnaqv lskwnlvlrn saskdsekia slaaslvarr
      181 ckqavqa
//
LOCUS       WP_285128458             345 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Leclercia adecarboxylata].
ACCESSION   WP_285128458
VERSION     WP_285128458.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..345
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35746
     Region          32..343
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtavvqqtrh swllpasgfl aivalllvia igvsvgelsi plqsvfyait nkigltevpl
       61 nriyesviwd frlsralvaa ccgaglaicg avlqsllkna laepyvlgvs agastgavav
      121 vvlgvgsgtv tlsagafaga faafafvall tngarggser tilagvaasq lfnaitawtv
      181 stsasaqqar dvmfwllgsf sgvrwpefql vlvmvlvgla iclyyarald aftfgddaaa
      241 slgiavpwvr lilfivtalm tativsmags igfvglvvph vmrfffgplh rtlliasala
      301 gailmvladi asrlliapqs lpvgvvtalv gvpffamiiy rsrnk
//
LOCUS       WP_285128603             226 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Leclercia
            adecarboxylata].
ACCESSION   WP_285128603
VERSION     WP_285128603.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..226
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25835
     Region          2..>223
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtrradrlfq ivqilrgrrl ttaahladrl gvsertvyrd irdlslsgvp vegeagsgyr
       61 lmsgfdlppl mltnkeseal mvairllktw ggeslsrele saqekvlail peesrrkaeq
      121 triyapdiam qphsrsgfda ihqaisaqrv lglhyrdesg qlssrnvqpl glffwgehwl
      181 laawcewrdd yrcfrldrcl nitmtdrrfs esadrsladf lrkvkq
//
LOCUS       WP_285128646             657 aa            linear   BCT 25-DEC-2024
DEFINITION  PhoX family protein [Leclercia adecarboxylata].
ACCESSION   WP_285128646
VERSION     WP_285128646.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..657
                     /product="PhoX family protein"
                     /calculated_mol_wt=71788
     Region          26..651
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mgkplksvfk kehrddvsnp sanpvfssva eiflsrrrfl qmgavagaaa sfpfllkpen
       61 alaavsqpsa lskavslgft sipvstedtv rvpegyiarp fyrwgdatgi kgampefkfd
      121 asnttdeqaa qagmhhdgma wfslpqgeen pshgllamnh eyidngmlft dgtaswsldk
      181 arkgqnamgv svievkksgs dwevvrpsgf arritvntpm qltgparqqt lmktaadplg
      241 eqvlgtmqnc angytpwgty ltceenwsdi fvkkgernal ekrygisdsd esyrwsevdd
      301 rfnvdktpne pnrfgwvvei dpynpnstpr khtalgrfkh egaavtlaad krvvtymgdd
      361 qkfeyiykfv sdnqynpadr easmqllttg tlyvarfndd gsgewlplvf gqngldkskg
      421 fesqgdllik trlaadavga tkmdrpewia vdphssgsvy ctltnnsdrg kegkapvdaa
      481 nprannafgh imhwheeggd paalrfkwdi lvlagrtdtt dekakgsmkg aefgspdgls
      541 fdhqgvlwiq tdvssstink kayegmgnnq mvatipgtne yrrfltgprg ceitgiaftp
      601 dnrtlfiniq hpgeggddit dpanpravsn wpdnnpqgrp rastvvitka dggiigs
//
LOCUS       WP_285129282             278 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Leclercia
            adecarboxylata].
ACCESSION   WP_285129282
VERSION     WP_285129282.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..278
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=31878
     Region          3..53
                     /region_name="CAT_RBD"
                     /note="CAT RNA binding domain; smart01061"
                     /db_xref="CDD:215004"
     Region          <60..>275
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mitikkslnn smllvdndqr emilfgkgig fgakpgthid laqvekvflp lsdlksrhfl
       61 sltdtipaaf fdisheilll arrlcgdkln svllftlaeh lhfaversrn gqtllnklsw
      121 evkryypqey svglqaraqv nekfdielpe eeavniafhl inassqddds tahqqvelvn
      181 riadivrykl gksidtqsvn ymrfithlry faervlagki alsetedfyq elmrhrpdam
      241 tvawvirdyv qdkyqltlpk deltwlsihi srlmdgqa
//
LOCUS       WP_285129360             620 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Propionibacterium
            freudenreichii].
ACCESSION   WP_285129360
VERSION     WP_285129360.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 620)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 620)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 620)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 620)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..620
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..620
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64674
     Region          27..614
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mttvtgstsr ttirqqagts lwsrtdlart lfvaactaal algldwpspt vpllaviglv
       61 vgcwpvvvea whdirqrrms melsmllaii aagvigewtt sllittfvla aeiledlsmd
      121 rgrdaltalm sflpttvtlr eghttrdial ddvapgqvlv igpgervpvd gvvdkgrstl
      181 dqsritgesm pvdvavgdpv yagsinqvga levraervga nssygrivta vreaqssrap
      241 vqrmadrfaa wlvylsiaga ivtflvtrdl satisviiva gacgiaagtp lavlaaiari
      301 arvgafvkdg ahlealsvvd tvvfdktgtl trgvptvtdv rtapgvstqq llawagaaea
      361 ysehplgrai aahvraagva pgtaqsfdyq pgrgvsvevd grmisagnar lvpdapasaa
      421 dgvatpvhis vdehyagtil ladqvrdsar svvaelrhrg lrvmmitgdq pataravade
      481 lgitevragl lpdeklraid aeraaghrla mvgdgvndap almratvgia mgsgtdiard
      541 sadvvlissd lndlaatlhi arrarrivmf nfvgtivvdv igmvlaafgl lgpvlaavfh
      601 vgsesafiln sarlipgrrh
//
LOCUS       WP_285129364             713 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Propionibacterium
            freudenreichii].
ACCESSION   WP_285129364
VERSION     WP_285129364.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 713)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 713)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 713)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 713)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..713
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=76824
     Region          40..317
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
     Region          209..532
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
     Region          617..>705
                     /region_name="SPT5"
                     /note="Transcription elongation factor SPT5
                     [Transcription]; COG5164"
                     /db_xref="CDD:444063"
ORIGIN      
        1 mpasstrlkr pggltdvfyl imrrmrfpli lliviytict vglglipgvd dagnptpamg
       61 lfnafyvvsy tgatigfgei pqpysaaqrm wmtmtiymtv vgwsyslvni lalvqerafq
      121 nalrqarftr riyglrepfy ivagagetga lvchgldrlg lrfvvverne erlarmrlee
      181 frsdppliva dasqpsvmrd aglvsphcrg vlalteddst nqaiavttrl laprvvvlar
      241 irnvetethv gvfggdlvin pferfarqla ssiiaperyr lreiltglvg epvpdqrqpp
      301 rghwimcgyg rfghamveel rstgievtvi deahfdqggv dvrgtgtdse sliaagvkta
      361 dgivagnasd tknlaiavta relnpgifiv trqnqtantp lfdaflddls mvpshivaqe
      421 flarittpll gqylkridqy sekecavlsd rltrfgrgri pelwdvvirr gqatavsqrl
      481 asghrvtlad vltdpdkrtq rseaaalmvr rgnksmerpe ltmelrpddr ilfagstqgh
      541 gnvslvlqna nalgyvqtgq egnggvvwrw itgqrrqsee lhdhdavppq egaralaakq
      601 rvarakaaka kaakalsgkp ggrpgrdarg aqsgsdgrvn avggrsgqgi pvpcgdgpts
      661 agngvlaapa qdtpgappkd dparqpeada ghgtastgdd kgtgpepsas ehh
//
LOCUS       WP_285129386             595 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Propionibacterium freudenreichii].
ACCESSION   WP_285129386
VERSION     WP_285129386.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 595)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..595
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66134
     Region          3..581
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mpqhqepevw kdltwsqvad evdqiaagfi algvqpeqrv aiaamtriew vladlgiaca
       61 aaatttvypn sqpddelfil qdsesvivva enwkqlqkvv dqselnaqvh hivlfdddrp
      121 idradaggdr vvtwdalhal grdylaahpt alderldlme pdtlatlvyt sgttgrpkgv
      181 riphrawtyq geamhhmwrg iiddrdvvyl wlplshvygr dllaaqmaig fimpvdgrid
      241 rivegmgeth ptimvgvpri yekirsavit qspangiqgr iarwafavgr esrpyrlagk
      301 hapwparlry avadrlvfsk lrdtlggsir fmisgsakls tqvqtwfysa gllvlegygl
      361 tetaaiaavn lpdkpkfgtv gpvtpgidar iaadgellls gpivadgyyh lpeetaeafe
      421 dswfhtgdig hfdedgylti tdrkkdlmkt sngkyvapqk veaallanvp yisqavavad
      481 ghpyvialvt mdhdqlmrwg knhghpnddy atlsqlpeir esidkfvrka nerldrwetv
      541 kryaildhef aqdtgeltps mkvkrpvvla ryektiddry eqttvsdltp ftggk
//
LOCUS       WP_285129413             342 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein
            [Propionibacterium freudenreichii].
ACCESSION   WP_285129413
VERSION     WP_285129413.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..342
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36985
     Region          15..335
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtsstttnap splnlgayta clhnytleea leilaadglt gaevnvggfi psphcpvdll
       61 igsqtarddy latfeahgmr laglntsgnv lsplpdqgpk haydlrraie lagklgvgei
      121 vcmsgtpgtd pdgkypawvv npwdgtqlev leyqksvldp fwremdlraq dagvqlalel
      181 hphnvvftpv nflefadrid aknvgvnmdp shlmwqgmdi vesirllgsh ikhvhakdtk
      241 lfpgvgtrgv ldssfgpvpa dpalrtptgf dhyvstwpad pawrfvtvge ghdvpwwtef
      301 lkalveidpq mninieheda afgqlegvkl gaknliaaad ar
//
LOCUS       WP_285129567             170 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Leclercia adecarboxylata].
ACCESSION   WP_285129567
VERSION     WP_285129567.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..170
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=19162
     Region          49..160
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mkpfrarirm llppplllvl fllfdlgtsg pnmldlhrlm drpvlsvtal vtgglslylv
       61 iagllrlvcn httinalhpa rtttlitdgc yafsrnpvyl gfvgiqlsva mlsgstlgll
      121 ispllmvlis llhiqpeeee iarrfgeqwk ryreqtprwl twrlrfgrsr
//
LOCUS       WP_285129578             524 aa            linear   BCT 25-DEC-2024
DEFINITION  FGGY-family carbohydrate kinase [Propionibacterium freudenreichii].
ACCESSION   WP_285129578
VERSION     WP_285129578.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..524
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=56478
     Region          11..509
                     /region_name="ASKHA_NBD_FGGY_L-RBK"
                     /note="nucleotide-binding domain (NBD) of ribulokinase
                     (RBK) and similar proteins; cd07781"
                     /db_xref="CDD:466799"
ORIGIN      
        1 migntngsgp yvmgidygte scrvaicdlr grpiaiasta yetthprpgw aeqnpedwwk
       61 alqasthkvl anagipasai agisydattl tlvamdekge elrpaimwmd vrateqaara
      121 adsdsvakly nggghspaia ewfpfkaawl kehepdiyar aahlvdapdw vtykltgewt
      181 tninsaalrm yynraqggwp tdfyetigvg dvfekisdrv ldlgqpvgql glipaqllgl
      241 rpgipvaqgp adawagqigl gvlspgsmal itgsshvltg qtdteihgkg ffgaysdgvm
      301 pgqftveggq vstgsvlkwf kdnfaadvvs aaekvglnpy dvlnekargi rpgsdgliin
      361 eyfqgnrtpy sdskargiiw glslahtpah myhaiqeavc ygtahnlrvm kaggfdveri
      421 vacggatksr dwmqmhadvt dvpitltevg davvlgtcml aavgaglykd lpeasenmvh
      481 eidviepnqa vhdeyqfyvd kycdtypqlq smihdmvdhe aaqk
//
LOCUS       WP_285129588             286 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Propionibacterium
            freudenreichii].
ACCESSION   WP_285129588
VERSION     WP_285129588.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..286
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29980
     Region          56..269
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 msvslsriac vgalatalvl sgcsgssgsg akvasdckpa htfntvsskk ltisapdfas
       61 fvskkdntqs gidvdvinqi aameclstnf lqvdysgaip avqskradva igdyyrttsr
      121 aevvglskam yvdgmglvsk dgvkdiptvi thnvgtvdgy lwvndmkklm gdklkiyksn
      181 vemfadlkag ridvgidsvp aaqfqadqnk daglqvatan pddqvgasvk paqvgipytk
      241 dnadlgkald ddiatlrgng kldqiftdhn vdtsltkldg dylvqs
//
LOCUS       WP_285129582             672 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein [Leclercia
            adecarboxylata].
ACCESSION   WP_285129582
VERSION     WP_285129582.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 672)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 672)
  AUTHORS   Porat,A., Cho,S.H. and Beckwith,J.
  TITLE     The unusual transmembrane electron transporter DsbD and its
            homologues: a bacterial family of disulfide reductases
  JOURNAL   Res Microbiol 155 (8), 617-622 (2004)
   PUBMED   15380548
REFERENCE   4  (residues 1 to 672)
  AUTHORS   Kimball,R.A., Martin,L. and Saier,M.H. Jr.
  TITLE     Reversing transmembrane electron flow: the DsbD and DsbB protein
            families
  JOURNAL   J Mol Microbiol Biotechnol 5 (3), 133-149 (2003)
   PUBMED   12766342
REFERENCE   5  (residues 1 to 672)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   6  (residues 1 to 672)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   7  (residues 1 to 672)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   8  (residues 1 to 672)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   9  (residues 1 to 672)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12109673
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..672
                     /product="protein-disulfide reductase DsbD family protein"
                     /EC_number="1.8.-.-"
                     /EC_number="1.8.1.8"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=72975
     Region          43..136
                     /region_name="DsbC"
                     /note="Disulphide bond corrector protein DsbC; pfam11412"
                     /db_xref="CDD:463273"
     Region          268..662
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 mktffrslwf llfslsaasa avpgwpikpd nlhaqvhvwh dapaegkvrl lldvtpnegw
       61 ktywrtpgdg gfrpaiawep qtktqwhwpr pvrfdsagfs svgydrrvvf plevaiderq
      121 rlrgkltlsl csnlcvvntf pldidlasgp sahfaeawdn amravppdng pvavksvvad
      181 ndsltvklts pegwsqpdlf adnpaganls ppqteilgdt ltarfsvsdk qgnpldasrl
      241 qqlpllisng aqsqqlrvdi spsttlwqiv vvalagglil nlmpcvlpvl giklaslmtl
      301 aessrrqtrl rflataagii fsflvlaavi tglrlsgawi gwgfqfqspw fiatmvlvtw
      361 ifcfslagll eirlpsglst rlataggngi ggsflegafa tllatpctap flgtavtfal
      421 aapvhqlwli flvlgvgmsl pwlvisiapg varwlpkpgp wmgklrlvlv llmlgsclwl
      481 msllvkewga ryvlivgglm vafflfrcaq ampshkenlr slvfgvlfga glyaflapqp
      541 qgkadsplnw qplseaalse aldarkrvlv ditadwclnc rvnevlvlhr peviaalnrd
      601 dvvllqgnws qpsaeieqfl rrygasgipf naifgpaipq ghvlpsllsk dallttltra
      661 npapspdfte ek
//
LOCUS       WP_285129786             395 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Leclercia adecarboxylata].
ACCESSION   WP_285129786
VERSION     WP_285129786.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 395)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 395)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..395
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44970
     Region          1..395
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 miysygfkny fgfkeganvs fhlngrvpkd vshgrdvati lgvkgangag ktnllkalsf
       61 lssfcsysfy skegatinad pyfnndapse fyieflygdy iytyelgvti nkvvyeklfr
      121 kskgtngesk ktrkipvfvr eeneisecls eisqvkvisl kdnaslissa fhykfdeplr
      181 ilnevymffa sfitnvhytg lndfsldtns irfvsefyyk neqafnfikn iiiksdlgis
      241 dveivqgvde sgkkyyfpif ehmvgnkkfs ltiydqssgt kslyvklnhy wralssgsil
      301 ildefdlnch pfilpkllel festetnplg sqfiftshit evleklskyr tylvnkenne
      361 cycyrldeig gdilrhgrai apiynegkig gvpkl
//
LOCUS       WP_285129814             204 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Leclercia
            adecarboxylata].
ACCESSION   WP_285129814
VERSION     WP_285129814.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..204
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23009
     Region          9..180
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mtdsaasnil niyqthaqaf erlrshalme rswlekftal inkqgrmldi gcgngrpiae
       61 fliqqgyqlt gadgaeamla sarqrfpqqh wlqadmrqle lndtfdglia wdsffhltre
      121 dqrrmlpvfs rhahpgsvlm ftsgtsngia mgefegeply haslapeeyh qllvengfrv
      181 vevvfedpec gghsiwlcqk invd
//
LOCUS       WP_285129808             439 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Leclercia].
ACCESSION   WP_285129808
VERSION     WP_285129808.1
KEYWORDS    RefSeq.
SOURCE      Leclercia
  ORGANISM  Leclercia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Leclercia"
                     /db_xref="taxon:83654"
     Protein         1..439
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47637
     Region          35..401
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mqkitslpad dalpgwyhts qprtprpahv gqknarwaiv gagltglaaa rqlalnfpdd
       61 evvlieaqdv gygssgrnag faidvphdig akdyigdvtt anlilklntl gqnylreivk
      121 ehgiacqmte sgkyqaavge kgiaileayr sglekigrha emipgkdlpd higtsyyqqa
      181 lyipgtillq psalvkglad slpsnvtlye ntpitsidyg dkvtlvhdqg sitadtlila
      241 nnafaahfgf lrgrllptfl ygsltrplta eeqaqlggkp vwgvipahpf gstvrrtvdn
      301 rilmrnsfsf hpdgrprekq lkhniethrk sferrfpmls kvdfeyswsg aiclsdnheg
      361 ffgqlapnvy galccnglgi trgtatgkll admiagerne lidflvaspg pnrtppepfl
      421 sigvnsvlkw gqfraglev
//
LOCUS       WP_285129931              99 aa            linear   BCT 25-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Leclercia
            adecarboxylata].
ACCESSION   WP_285129931
VERSION     WP_285129931.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..99
                     /product="type II toxin-antitoxin system RelE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0017148 - negative regulation of
                     translation [Evidence IEA]"
                     /calculated_mol_wt=11665
     Region          2..80
                     /region_name="RelE"
                     /note="mRNA-degrading endonuclease RelE, toxin component
                     of the RelBE toxin-antitoxin system [Defense mechanisms];
                     COG2026"
                     /db_xref="CDD:441629"
ORIGIN      
        1 mkivwsrtak rdlakidkry qtrieekiaa indrnaprpd ikkldmgedy yrlrtgdyrv
       61 ififqgesrd vcyivavkrr tsttylheen tlygctndq
//
LOCUS       WP_285130187             225 aa            linear   BCT 25-DEC-2024
DEFINITION  XRE family transcriptional regulator [Leclercia adecarboxylata].
ACCESSION   WP_285130187
VERSION     WP_285130187.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..225
                     /product="XRE family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=25173
     Region          1..69
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          87..214
                     /region_name="COG2932"
                     /note="Phage repressor protein C, contains Cro/C1-type HTH
                     and peptisase s24 domains [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442176"
ORIGIN      
        1 mktaerinef lkikgwsqae larqlgvtaq svqywttget tprgkrlarl seisglpqsw
       61 flgesesptf pnshqahhrs dsvrfnvlev efscgdgtsv kgdfidvvrs ieldpeyarq
      121 lvgnrpfksi eignargdsm tptiapgdll fldksvtyfd gdgiyafcfd gecyvkrlqk
      181 mgtkivvlsd nsnyhpwsie keafnmlfiq skvissvpfn inrfg
//
LOCUS       WP_285130288              65 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Leclercia
            adecarboxylata].
ACCESSION   WP_285130288
VERSION     WP_285130288.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 65)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..65
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=7238
     Region          1..63
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mgneisslie ekevmsilgi ssrqtilnyt nrhgfpkpvk thpkaylrda fnhwlqnggv
       61 nqkss
//
LOCUS       WP_285130297             238 aa            linear   BCT 25-DEC-2024
DEFINITION  XRE family transcriptional regulator [Leclercia adecarboxylata].
ACCESSION   WP_285130297
VERSION     WP_285130297.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..238
                     /product="XRE family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26621
     Region          1..74
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          105..233
                     /region_name="COG2932"
                     /note="Phage repressor protein C, contains Cro/C1-type HTH
                     and peptisase s24 domains [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442176"
ORIGIN      
        1 mtfserlraa mdyagftqgg laravgmaqs svnkllknad ssrktveiar vlgvrpewls
       61 sgngsmltdg lrdpipayst vretrlkaav wedmsdvqrq efveipllsi nlsagpgcea
      121 ieedeeftls frrhylksrn isednarlvr vtgrsmepml ndgdvvgint kdieirdgkt
      181 yaicqsdllr vkiliatpds viirsinrde ypdevisrdk fhdevrvigk vfwsahsw
//
LOCUS       WP_285130382             659 aa            linear   BCT 25-DEC-2024
DEFINITION  S8 family peptidase [Leclercia adecarboxylata].
ACCESSION   WP_285130382
VERSION     WP_285130382.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10297442
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..659
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=70344
     Region          204..460
                     /region_name="Peptidases_S8_S53"
                     /note="Peptidase domain in the S8 and S53 families;
                     cl10459"
                     /db_xref="CDD:415849"
     Site            order(244,304,422)
                     /site_type="active"
                     /db_xref="CDD:173787"
     Site            order(244,422)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:173787"
     Region          604..650
                     /region_name="ChiC_BD"
                     /note="Chitin-binding domain of chitinase C; cd12215"
                     /db_xref="CDD:213178"
ORIGIN      
        1 mkksilslli caavtcsaya etapqvelaq ngesyvaivv klkpskpllk stgttsastt
       61 tnqltlsdps lvptsmfrpn klrstqsdef aqlnarygfd rylrielpes katdrtyinn
      121 miaeleqnpn vdivypeslp vsldkyhvgn eqnqpllkst vqssvgastv pdfrhlqyyt
      181 kaptdkrqgy ymggvnrdsv nqypgnageg vtiismendi wnvnhinlpt paltqgntky
      241 iddhdtasva imaakdigag vrglswksrv gfsdwkynnl ynmipllkag dvvqigmqtg
      301 ggeitgcttk dcyvpqenvq syydvikalt dkgvyvieaa gngninldhs afkgkfdvht
      361 rdsgaiiaga fcakdgkkas fstygsrvts sswgcwdvvt agygslynaa naqytntfag
      421 tssanpiiag vvaslsgiak angitvtpvq mrqilqdtgt slangesakv gthpdmerav
      481 arilalkdgg ktapaptaaa gadytmvspa sgvstypldg skslnvksfn wsvtkgagtf
      541 wlqeklngsl vnsvnsahaw avipantege vtykltttge dgrtaqdsmt ikvskpaapa
      601 ldvpaynaki ayptkctkvs yngkiwmnqw yvnpgqetpg tggtwgvwrq pgatgnsck
//
LOCUS       WP_285130391             278 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Leclercia
            adecarboxylata].
ACCESSION   WP_285130391
VERSION     WP_285130391.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..278
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31716
     Region          30..278
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          190..273
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mrktptaehl elialndtiv sfsrlfantv ryhhwhqcle ilyveegfgi aivdnrhytm
       61 rpgrlfffpp ftlhkvmvdp qaeanyrrti ihldqhavlk alrdfpqtqq rlqklsqrgg
      121 eawvadmahc hshldhlfsc ypppmnsecv aslliglfam lphddegqpg nsqgiasqvm
      181 fwldehyqqk fsldalagel gksrsyvsrk fhaetgekih dylntlrlrk acesllhsea
      241 svrdiaarvg fsdvtyfisa fkkgigetpl qyrknhaa
//
LOCUS       WP_285129882             728 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor [Leclercia adecarboxylata].
ACCESSION   WP_285129882
VERSION     WP_285129882.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 728)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 728)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 728)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..728
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=78362
     Region          68..728
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mnntrrmnkt llalaigava hsavaaeskk eetivvqsaa sdfkpggdql vpafldgqva
       61 nggrmgmlgq qnamdvpfni isytsklved qqartigdvv andagvqsvq gygnsaesyr
      121 irglkfdgdd mtfgglsgvl prqvvdaqmv drieifkgan slmngaassg vggminlepk
      181 hagatpqakv gvdytsdsqi gttldagrrf gdsdqfgarv nvvhregeap vandrrrttl
      241 lstgldyagd kfrssvdmgy qkktfhgset gvnvagvnfv peppkndrny sqkwaysnie
      301 nefgmwrsey ditdswtayt glgaqhahee glysgaklvd ksgkatasrl dtnrisdsvs
      361 gmagirgnfa tgfvthkvnv gysamtknek iawkmsaakd npvtniyhnt gvdappstns
      421 ngaggnysdp ltsgrtrtqg wllsdtlgvl ddkllftvga rhqkvvirgy nkvtgienag
      481 dsfdgdrwmp tygvvykpwn eislyanhte alqpgktapn tasnygqstg ivhskqnevg
      541 vkadfgrvgg slalfeikmp saildsqtky ygldaeqrnr gvelnvfgep vlglrlnasa
      601 twlqaeltkt nngvnqgnda igvpsfygvl gaeydikpid gltatarvnh sgsqyadlan
      661 skkldsyttl dlgmryrfav nndqnqmtvr agienitden ywssvddggt ylfqgeprtf
      721 kvsvgyef
//
LOCUS       WP_285130566             167 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Propionibacterium freudenreichii].
ACCESSION   WP_285130566
VERSION     WP_285130566.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..167
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=17478
     Region          <32..163
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 migavssgle lfvglvpvsv vgmdgvvvlg slaldaprvg vpvvlehvpa gfpspaqdyf
       61 dgdvdlnehl lmnrpasflv rvtgdsmtgv giydgdeliv drsldpvsgd tviavvddel
      121 tvktlvldaa gpslrpqnpa yptirptsef viwgvvttcl hhlhrvs
//
LOCUS       WP_285130599             208 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Propionibacterium
            freudenreichii].
ACCESSION   WP_285130599
VERSION     WP_285130599.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 208)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..208
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22863
     Region          4..>184
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 maarrserlv nlaiallsar rflskaelrr vveayrglsd saferqferd kddlramgvp
       61 vvmgsndvlf dddtgyrisr tdfevppvsf dsdelsalga asrvwqqasa aeqtisalak
      121 lraagadpdv erlaalapri sarepafevc wratlerqlv rfgyrgspev rtvapwsvlw
      181 rrgaccgvva agtcwawtsr grvpacsr
//
LOCUS       WP_285130645             330 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Leclercia adecarboxylata].
ACCESSION   WP_285130645
VERSION     WP_285130645.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..330
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34693
     Region          23..326
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mprrigyslw glamalavmt llatgfgalr lpvsllwsgs dealrqiwlt irlprvllal
       61 viggslalag cvmqglfrnp ladpgllgis sgaacavalw vvlpislptl lmlyapmlaa
      121 flgalaatvv ifllsqqres slsrlllvgi ainalcgaav gvlswisnda qlrqlslwgm
      181 gslgqaqwst llavtslmip tvlviwrlaa alnllqlgee eahylgvdvr lvqrvlllcs
      241 allvaaavav sgvigfiglv vphlmrmwlg sdhravipgs vlagafllli adtaartlva
      301 paempvgllt silgapwflw lifrrggqhg
//
LOCUS       WP_285130714             264 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Leclercia adecarboxylata].
ACCESSION   WP_285130714
VERSION     WP_285130714.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14398449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..264
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29304
     Region          14..108
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          169..250
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mttqqqfsft trplvpfahd ythgetepwh shtcaqllht lsgvvrveta qgfwivppgr
       61 gvwlpagtqh rllitgnvaa rtlfidpfar adlpsvcqvv qistllreli iaslqlpesy
      121 aagsraeriy elildeirgi svlpfnlpep qssallalcr qiqadpgirw ttarvasqln
      181 isertllrhf rqqtglafse wlrrarlmea lnrlaqgqsv lrvaldlgye shsafsamfr
      241 rtlgvapsdy fqpeslsgsa fska
//
LOCUS       WP_285130880             187 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Leclercia
            adecarboxylata].
ACCESSION   WP_285130880
VERSION     WP_285130880.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..187
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19903
     Region          76..137
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 malynfiltl sgvtyetegl edalyasgcd dalicaygrs vyvefdreae sldaaissav
       61 dniesagiga ivgsvdsalv glsdiaemtn msrqaiamlk dgtrgsgdfp cpiqrikgqs
      121 plwdwgdvah wlssngrlkq dselvvnahv lskwnlvlrn saskdsekia sltaslvarr
      181 ckqavqa
//
LOCUS       WP_285130893              76 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Leclercia
            adecarboxylata].
ACCESSION   WP_285130893
VERSION     WP_285130893.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..76
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8523
     Region          7..61
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(8,12,37)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(11,36)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(18..19,30,33,37..38)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mrmftplrka rlkakmtiqe vassikcdpg nlsrmergiq rpspevaekl aklfdaelte
       61 iqilyperfs sdgcqp
//
LOCUS       WP_285131180             272 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Leclercia
            adecarboxylata].
ACCESSION   WP_285131180
VERSION     WP_285131180.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..272
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=30902
     Region          25..264
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mlelsialpi rvqnggyfis rgvgrhparr ldswevifve kgtltiqeeg svfevhtges
       61 lllwphrlhk giedfpadlr fywlhfevde qslpsarstl lsvqqhgktg dpqamvalfr
      121 qflteqeklq rspaleflll lilqqlslaa gqelppdeag vnlawkarql igtqfhlpis
      181 tstlakelhc nadylgrvfr rvfnltltea ihrqrvraae klllndavsl kevatrcgfn
      241 dagyfrqifr khtgltpgvw krryckehin sa
//
LOCUS       WP_285131219             262 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Leclercia
            adecarboxylata].
ACCESSION   WP_285131219
VERSION     WP_285131219.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..262
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29563
     Region          21..262
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          181..262
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqdfhfqhkh ltaaevsask mhrlhqvklf ypaichithg skviihedsr lvatpdelii
       61 ipantpmeiv nqpaqgifhs dllllspdii aafktrylqs wprsktdslc aplseglafm
      121 wgnllhavrh dfpdelqkhq afglllallh dgvagpllie rnvnlteqvr qfimmspara
      181 wtaqdvasrl avsvptlrrr lreeshsfrq iveevrmava lsqlqstrls vgeiaiqcgy
      241 lsssrftarf rqhygclpkt lr
//
LOCUS       WP_285131306             195 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Leclercia adecarboxylata].
ACCESSION   WP_285131306
VERSION     WP_285131306.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..195
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21697
     Region          25..133
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mtlkyyqdna qtffdgtvnv dmsslyetft qylapgarvl dagcgsgrda kaflgmgyqv
       61 eafdaspamv glarehtglp vqlmtfadvd wkeefdgiwc casllhvpav elpgvmrrla
      121 dalklggvwy vsfkygdger evdgrwftdm deddlntlvs sltaievgdv wltqdkrpdr
      181 keiwvngilr kkdcn
//
LOCUS       WP_285131312             209 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Propionibacterium
            freudenreichii].
ACCESSION   WP_285131312
VERSION     WP_285131312.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..209
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=22607
     Region          11..69
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(29,40,43,47..48)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mssipepwas amkkqnlvdg rsgdrpswsa lartagvhts tviamaegkr etetdvlqkv
       61 akalridvrt vskwagqars vrapysppad anlldseerd tidrlirlla kgkkrntedr
      121 pqrevvqdag tptpvhsapd psrtdnvvdf prdshgdlil pegiaahdtg rksvgrmqne
      181 aqdadaeasq dpgggwddvn qdpdgdder
//
LOCUS       WP_285131315             166 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Leclercia adecarboxylata].
ACCESSION   WP_285131315
VERSION     WP_285131315.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..166
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18472
     Region          82..>144
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mfsqtthydl tgfncgedtl nrflcehlar qhvgrllray llvtddptpk vlgyytlsgs
       61 cfeketlpsk tqqrkvpyvn ipsvtlgrla ihqdlqgqgw gmtlvthamk vvwlasqavg
      121 ihgmfvdaln dkakdfyltl gfiplmgsna dalfyptksi eklfae
//
LOCUS       WP_285131714             637 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Propionibacterium
            freudenreichii].
ACCESSION   WP_285131714
VERSION     WP_285131714.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 637)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..637
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=70734
     Region          11..607
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mptlterqgv llqllsemtd pitnaaladl lgvsprtvry diarvnrltn aplieaargg
       61 hllnlpeyrr lvkrlasvdr agddrerill alvngfdgdl felaqqqmms datvrtlire
      121 lneqlaernl riasvcgvlr legtefdrrr lmgdllsaal sdphgvagrv asvlpdvdle
      181 rvrrvvehnl qlmrpavgdm dlwnlsmnaa iclqryespl egavageptg peavrvserl
      241 vdelaiefpt rllgrndrhy mgvllnalvg trqapgelrd vavgpdleyi vgeairdavs
      301 hfnlkvdmer lqsgltghvr rllgrsgkiv yfrnslresl rtrspvlydv avflahrlst
      361 alrleisdde igllviyigl yiedddselr evravvvcpe yqtlrdwila nlaavfsnrl
      421 hiveivssaa evplvdvdli littgetsss aeavqisall sdidierigk gidavvrsrl
      481 rsrieagies flspelffrd lefasareti lnlcghlqea gvvpggftqs vllresysst
      541 vfaqrfavph amefmasetk iailipkkpi dwgedsrvsm vlllaikndd yesfvafyqa
      601 firalydpdv fsrlraaegy vefcrvlvds lparlgd
//
LOCUS       WP_285131764             254 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Propionibacterium
            freudenreichii].
ACCESSION   WP_285131764
VERSION     WP_285131764.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..254
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27703
     Region          1..218
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mtelgaerpn gdlstrhqvl hlllsegamt apdlacrlsi tptavhrhlt alikggqvve
       61 nqpdqqpsrg rgrpaktfql tdlgrsafnq ayddlamqal rvlvetmgad avtklgekry
      121 vdveqryrgy raahpladpv ealasalndd gyvtkvdeap agaqlcqhhc pvahvaaefp
      181 qlceaetqmf srllgtrvqr latiahgdgv cttnipldiv vidhemvieh tprerkrave
      241 nhratdnnre atsa
//
LOCUS       WP_285131765             321 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Propionibacterium
            freudenreichii].
ACCESSION   WP_285131765
VERSION     WP_285131765.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..321
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33333
     Region          3..296
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(38,256,259)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(193,226,254,257..258,261)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mavvvcgeal idlipdnsra gttqssywqa hsaggplnta valsrlgmpt rflgrfgidg
       61 fgaqlrshlr angvddslgv qtlagstsls vvsvdssgaa ryvfhlhgta nfgwkpeefp
      121 qldaddwlht gslvatvepg rsalldfvrt tpahlsydln vrptvepdpd aylalidpfv
      181 qvvsqrggvv rasdedllwl agghgeiddl araaverygm dllvvtlgah galatgvgre
      241 tvrvpgfpaa vvdtvgagdt ftagflqgwl rdadltaall rgcaaasivc trvgadppta
      301 aevdellaag ptrtdpppdt a
//
LOCUS       WP_285131780             316 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Lactococcus petauri].
ACCESSION   WP_285131780
VERSION     WP_285131780.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..316
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34175
     Region          25..313
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mkirkfsyqv alalvtimvl sflylmlgdq nysfsqiwhe svvlhlrlpr llalmfvgil
       61 lsssgllvqs mtgnpiaeis tlgisggasf alalllvfnl stggwlgtav aslgafialv
      121 tvavltvksk fqpmkvvlvg tsvglfatsl asiltfyskn mqsyflwivg sfsgitplkl
      181 eilmvvtvlf vsmvllfanq ikvlsfgeem atslgisvnr lrllimtmva lasgvtvssv
      241 gvisfvglma phlarrlvgg hflkrffmsn llgvmlllva dvlarnlfkp yefpagsltl
      301 lfgaiffiym mskeek
//
LOCUS       WP_285131849             918 aa            linear   BCT 25-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Lactococcus petauri].
ACCESSION   WP_285131849
VERSION     WP_285131849.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 918)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 918)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 918)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 918)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..918
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..918
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=100499
     Region          2..914
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mefykkakve vieeflvdtk tglnheqilk qrelhgenkl pdeeeesyla tflksfkepi
       61 vivllgaval sfassyyafq fqndskhgme alyeaiaili liiinaflgf yqeisarksl
      121 nalkemnnry vtvlrngqfe kilstelvtg divkasigdf veadvrwiet nelqvieshl
      181 tgeadaiskh tdailettel gdrhnmgfsg ssvsggqglg ivvavgehte lgkiakliqa
      241 venrtsplqn tvhkltktlm qvsagivvft lvvgiiqage lsiasitsvl stsialavas
      301 ipdalpavls ivltigaakm aknkgliksl nsvetlgsts yicsdktgtl tknemtvthf
      361 ytngqyyevs glgytpegei rslsdeeqep sysafiagal lcnesalkev egkfvpfgnp
      421 teialtvlgq kagrtktqll eshelirtlp ftsdrktmsv ivkkgdnyll yikgapdvlv
      481 eksrallidg elnteesekq kfittvndya nealrtlavg yrilskeeae qgqledlekd
      541 iiltgvagii dpareevkas vktlqdasve vvmitgdhen taraiaynlg ivkskeakvi
      601 kgieieemtd eelyevvktt nvyarvspeh kqrivkqlqk hgevvgmtgd gvndapalra
      661 adigiamgia gtevtkdsad lillddkftt iektvengrt iyaniknfir helttnvaev
      721 lslilgllff tvsignvdyt tptltvlmvl wvnmvsdavp sfalgydvae sdimnekprd
      781 pkesvlanyt wsrvlirgti mglmvfvafv waakqgmssn eaqtvafltl vygqlwhvfd
      841 arssqtlfrr npfgnprlvl avvfagissf lvtiipffnv vmgtaplslp vyllvlfvpa
      901 lptfilsgik eifkvkiw
//
LOCUS       WP_285131929              74 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lactococcus petauri].
ACCESSION   WP_285131929
VERSION     WP_285131929.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 74)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..74
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8314
     Region          5..73
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mtktklqimr ekkgltvrel tekmsenrqw lgnymakiea ieqgasihcf sdygikhlaq
       61 vlgcsveelv edeg
//
LOCUS       WP_285131967             251 aa            linear   BCT 25-DEC-2024
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Propionibacterium freudenreichii].
ACCESSION   WP_285131967
VERSION     WP_285131967.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..251
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25656
     Region          1..251
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mtivvaykya pnpqdaevrg dgtvdwsrak savseydpva vqlgrelagd aevvgisvgg
       61 advassmakk namsrgldrg lvvaddaaad wnatrtasal aalvkkvdga dlllagdssv
      121 degakmmsal vagylgwpcf qevsalektd ngyrvtqdqp ggrrvvevtg plvvavaada
      181 vkpkvpgmkd ilaagkktve vvpvadlevs daaiaitase kpaaparkqq ilsdddaaaq
      241 lvaalradsv l
//
LOCUS       WP_285131976             840 aa            linear   BCT 25-DEC-2024
DEFINITION  copper-transporting P-type ATPase [Propionibacterium
            freudenreichii].
ACCESSION   WP_285131976
VERSION     WP_285131976.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 840)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 840)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 840)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   4  (residues 1 to 840)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   5  (residues 1 to 840)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   6  (residues 1 to 840)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18340165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..840
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..840
                     /product="copper-transporting P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005375 - copper ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006825 - copper ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=86842
     Region          18..45
                     /region_name="HMBD"
                     /note="Heavy metal binding domain; pfam19335"
                     /db_xref="CDD:437167"
     Region          144..170
                     /region_name="HMBD"
                     /note="Heavy metal binding domain; pfam19335"
                     /db_xref="CDD:437167"
     Region          187..836
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     human copper-transporting ATPases, ATP7A and ATP7B;
                     cd02094"
                     /db_xref="CDD:319783"
     Site            order(489,491,792)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Site            order(533..535,598,614..616,641,681..683,703,706,709,728,
                     731)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319783"
     Site            order(793,821,825)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
ORIGIN      
        1 mseashptit pgtgpgvvyt cpmhpqirea tpgrcpicgm nlvpadevag asdghapmqm
       61 dhsagpshpa dssstqgnhp mamttdhatp aatmasgttp khdhttpghd mqghdmhghd
      121 mqghgtpapg apsdqadasg vtwytcpmhp evrvdhpgac picgmalepv vttartgtnp
      181 eltdmrrrfw agvvitvpil vlsmvrplfg gfmdavgdql aawlelvlat pvvlwagwpf
      241 fvrgaiswrt gklnmftlis mgtgvayvys liatiapgvf pqtmrtaqgt vepyfeaaam
      301 itvlvllgqv ielsararts gsiralldla pkkarlvmpd gtehevavdt lqvgdrvrvh
      361 pgekvpvdgv vtdgashide smvtgepmpv arhvgdrvig gtlntqgslv vkadklghds
      421 vlsgiialvs saqrsrapiq glvdkvaawf vpivlglavi afivwmlvgp aprlphaivv
      481 avsvliiacp calglatpma vmvgvgraat agvlirdaea leelskvntl vvdktgtltm
      541 ghptvtqvet tadhdqsevl rlaagaekgs ehplaravle aaatrtltvp dvsdfhatsg
      601 agingtvegh hvcigneeha rpneeltaaa asmrtrgata vfvsvddkpa avlaiedplk
      661 ptsrkalaal vdagvhpvmv tgdaeatara vadelgidev hagvmpdgkv qvinqlkaag
      721 gvvamagdgi ndapalaaad vgiamgggtd vaiesagitl iggdldgivr achisnatmr
      781 tirqnllfal vyntagipla agvlypafgw llspmfsaaa malssvsvig nslrlravrl
//
LOCUS       WP_285132135             407 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Propionibacterium
            freudenreichii].
ACCESSION   WP_285132135
VERSION     WP_285132135.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..407
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42581
     Region          3..380
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mmtsgidevl arglragcyp gaiaqvshag tvrragvgsi ashgrdgspi ppaqrepvrp
       61 dlhydlasit kvftaitvls ladegtlamd epiaallpaf rtsperrrit alhllthtsg
      121 lppvwpgwqd agmrarsrea iladimampl rwapgerldy scvgyitama laeqatgqgw
      181 eqlvttrvlr plglahtgfn plrhgvdvad iaptefrpal glrpvgstha pdaagasrpd
      241 saadgvdltm vrgtvhdeta qviggvsgna gmfstladla rlasalssgl pgvlgresfa
      301 mlwddqlprl lgghadaeaa rngyrhgagl cvaqtraagp dapwlrshtg ftgtsvvlnr
      361 agdyaillsn rvhptrqapd lapvrvaltr aaglvepeeq aepggqa
//
LOCUS       WP_285132279            1599 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Propionibacterium freudenreichii].
ACCESSION   WP_285132279
VERSION     WP_285132279.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471668
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1599
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..1599
                     /product="DEAD/DEAH box helicase"
                     /calculated_mol_wt=177064
     Region          3..1575
                     /region_name="COG4889"
                     /note="Predicted helicase [General function prediction
                     only]"
                     /db_xref="CDD:443917"
ORIGIN      
        1 makvrtiqdv ieefgcepsa vvrgtrfeel magyfaadat laatydevfr wpewshnegt
       61 hdtgidlvar eresgewtai qckfydprhr lqkadidsff tasgkrwdgv aftnriiist
      121 tdrwsrhaed althqtipvq rigmadiaes rvdwmfhadd plgftprkav rfglrphqre
      181 aidaiqagfa shdrgqwisa cgtgktftsl klaerrcadn eghltvlfla psislvsqsl
      241 rewlaqsqtp irpfvvcsdt kasrqaedit vhdiplpttd pdrlvaemar ggrrgrqmtv
      301 vfstyqsidv varalkqsga gpfdlvlcde ahrttgvtla gdtgesafik vhdnaylpav
      361 krlymtatpr iygtdvkkka ddaaavltsm ddeamfgpvf hrlgfgqave rgllsdykvm
      421 ilavandaid pgmqaclage ghelslddaa rivgcwngla krttdmdfge hptpmqrava
      481 faanikaska fagalpqvvd qvigddaglq veahhvdgtm naltrgeela wlkapvpege
      541 crilsnarcl aegvdvpald avlflsprns lvdvvqsvgr vmrkapgkdy gyvilpvaid
      601 aseepevalr dnkrfkvvwd vlnalrahdd rfeamintid ldhstggkvs idvfsphggp
      661 adddnrsdgq qpvnpfagtq pllvgsdlwr eailgrivkk cgqreywesw addvvaihan
      721 qvrritgiia aarrdgapva gqfdvflegl ranlnesida aqavdmisqh litrpvfqal
      781 fpagsfaern pvsitmgrma talegyglaa etarldrfyd svgrraaqir tpegrqsvih
      841 qlyeqffrta fpaqasslgv vytpvpvvdf ilraadqvcr dqfgygitdp gvhvqdpftg
      901 tgtfivrllq sgiiapadla rkyagelwan eymllayyia avniettyqa lvaeqqpdrp
      961 vdyvpfpgvt ltdtfqitek gdrvdtslip vnnqrieaql aapikvivgn ppysagqtsa
     1021 ndnnanlsyp tldariaaty aaqstatnkn slydsyiraf rwatdrlgdq gviafvtnng
     1081 wldgntadgi rktfqtefsd iwvynlrgnq rtagetsrre ggkvfgsgsr agvavlvaak
     1141 nphqtgchih yhqvpdyqsr edkldditda tltttgwati tpntdgdwln qrnpafqsfm
     1201 piglkdtrep tprlftmhsr glatsrdawc ynfshkavea nmsrmvdeyn leattctgde
     1261 sklttdptri swsrglkada lrgrthqfhp eriyeslyrp fchqnayfdr plndmvyrle
     1321 sifptpthdn igfyvvgvga vkpfsvlals dvpdlnlfgs eggqffprwt yeradssdqd
     1381 alpapgdavd eygyrrvdni tdqalkgyrd afgpqvskdd ifsyvyavlh sqqyramfaa
     1441 dlkrmlprip laasrddfdr fvaagrtlag lhigyetvep yplseqhsdt ltgpeayrvq
     1501 kmrwkdkttk ktliynthit lddipavase ymlgsrsale wiidryqvkt dkasgiindp
     1561 nqwatehddp ryiidlvkrv trvsvdtvrv vdalpelpl
//
LOCUS       WP_285132216             275 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Propionibacterium freudenreichii].
ACCESSION   WP_285132216
VERSION     WP_285132216.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..275
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29277
     Region          20..263
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(38..39,41..42,45..46,84,88..89,92..93,123,127,134,
                     137..138,143,159,163..164,166..168,170..171,174..175,
                     178..179,199..200,202..204,206..208,210..211,213..214,218,
                     221..222,228,232)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(162,166,169..170,172..173,213,216..217,219..224,
                     227..229,235,237)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(183..190,201,204..205,208)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mtalphaplt gtdqsgasga dwsgalarln pvtrllltvl vaipvlisld wlsatvifvg
       61 elvvflacgv rarmlarrmi pllivaplaa ismalygkpg gdvyfqwwlv visqrslmma
      121 iavvlrifal glaalvlmgg ldltatadgl aqichlparf vlgtlagmrm inlfaadwrt
      181 maqarrargl gdtgrlrrfa tmafallvfa irrgtklata meargfdast aahrtwarps
      241 rmgradavgw lvavvmvala lavsirlgtf tpvtr
//
LOCUS       WP_285132349             368 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Propionibacterium
            freudenreichii].
ACCESSION   WP_285132349
VERSION     WP_285132349.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..368
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37043
     Region          49..365
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtrtaadara daggsadags rthagharta hwlwlgvlvv alavsvvmal gigsvplspg
       61 evvgviarrl rlitgadvtp ladqivwqlr lprvlasiaa gavlavcgai lqtltgnala
      121 dpyllgissg asvgavfvle iglsvglsqs vlmmgaafvg avlgmllvlv latgrggelp
      181 partvlagva vaqvcaaits llimvfggtt aartamewml gsfagarwla agvlagvalv
      241 tlvgamgysr tldafsfgdt saaslginvt rvrwglmift alttamtvaf vgpigfvglt
      301 vphimrllvg prhagllplt alggallllw sdtaarsitg nteipvgvit allgtpvlav
      361 llrrqasq
//
LOCUS       WP_285132473             465 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Propionibacterium freudenreichii].
ACCESSION   WP_285132473
VERSION     WP_285132473.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..465
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49133
     Region          90..460
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mrknwiflgv atlafllvrf aipttaaltp sakgalavav faiivwvtqa vsdalsgfli
       61 illlvissat nlagsfagfs ntslwlivvg fimaaameks glserialsv vrlaggsaik
      121 iywaiagvma vltflvpsit artllmlpii mgigqafgae rgksnivkal ifivamsgtm
      181 msigvltahv gnpatvgliq aatghnvsws ewfkvggppa fvlsalsvvv islmwkpets
      241 rvegardyia gelarlgpik ktewytlavf matlvlwate ppmlstivvg iiavillllp
      301 glgvlnwkea qekvpwnvfm vygaglsmgt alttsgaakw lattmfgpit qlsipvqmii
      361 llwfitilqv fftgggpktn altpiilaha gaiganqtsf glilgmnmnh qyllpvsnmp
      421 navamgtdfi ntrelirtga vmsvlgaafm svmvltywsw lgmvg
//
LOCUS       WP_285132487             366 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Propionibacterium
            freudenreichii].
ACCESSION   WP_285132487
VERSION     WP_285132487.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..366
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=40419
     Region          66..343
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 masiqkrpdg awraryrdrs gkeharhfrr kvdaqrwlde saselvtglw adpqlargkl
       61 etqaaawlas hpewapstra rnrsivglhi lprwggvrlg qittedvqkw vgeltasags
      121 irkitgvlsg imeqavatky lavnpvaava rpkqpmkrrr ylnaieverl ancagvhsdm
      181 iltlaycglr fgemaalhvs svdtqrrrfm ieqsvtevng vlewsapkdh qrrsvpypdf
      241 ladpiaarvn ghhgdrlvfp tpgghamrig narrdwfdpa vqaanlsplt phelrhtaas
      301 lavaagasvl alqrmlghdk psttldvyad lfdedldrla erlatarsea ladflrtnds
      361 pnnppt
//
LOCUS       WP_285132516             370 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Propionibacterium
            freudenreichii].
ACCESSION   WP_285132516
VERSION     WP_285132516.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..370
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41572
     Region          57..356
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msfdgkqysi gryetltlar aaldmarmqv vtrtfippae rkrlrraeqa ekqaqaltvr
       61 qwssewlaql eragrspsti tsyasvlrah ilgpigdkrl tavteddchr lmdavptdav
      121 kfnvartlta mlnaavkiha gnlavspahl pvdrlarslh rddeldsati eqvwaiydrm
      181 dkryriavwl avgcglrlae clglqvrdld ladqdnavlh vrrqwltkra ghpdyappkv
      241 dsvgdesipr tvavmlaehv kryvgdepda pilpspadpr rpisqssfdr lwrdardpva
      301 palhfhslrh vhlslyarda tpqetahrgr hkslavaary qlatrerdre ntqaldrllr
      361 rsphgasqeh
//
LOCUS       WP_285132527             268 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Propionibacterium
            freudenreichii].
ACCESSION   WP_285132527
VERSION     WP_285132527.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 268)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..268
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29214
     Region          1..242
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mptalvtggs sgigyafate larrgydlvl vardpqrlgs aaravrnkfg vqvhelsadl
       61 sdhddiarve qvfadrpidl lvndagfaah ddlldddwsg qvraldlmcl avlvlsgaaa
      121 remvkrgrge iinissmnsl ipadnyaaik awvnsytegl aarldgtgvh anvtitawvk
      181 tefhaaagld rpripdwvwv pvksvvrlal advrrgkvrs vptlrwrfaa wvlqhgplal
      241 prrvshwvqs ehdnnriggp deprpedv
//
LOCUS       WP_285132709             646 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidase U32 family protein [Prevotella bivia].
ACCESSION   WP_285132709
VERSION     WP_285132709.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..646
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=73116
     Region          1..302
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
     Region          448..510
                     /region_name="DUF3656"
                     /note="Collagenase; pfam12392"
                     /db_xref="CDD:463557"
ORIGIN      
        1 mrtiellapa knvecgkaai dhgadavyig aqkfgarqsa gnsvediael cayahrydar
       61 vhvtlntiiy dhelddtikl veelievgvd aflvqdmglf saikkllppy valhastqcd
      121 trtvnkakwl qqqgfnrvvl arelsadeik niheqlpsle leafvhgalc vsysgvcyas
      181 qhcfdrsanr gacsqfcrla fdlvdsdghm iekqahllsl kdmkqidnle tlmrsgacsf
      241 kiegrlkdin yvknvvsays qrldeiiaky pkefcraslg nvvyqftpdl nktfnrgytn
      301 yfvqgrqani fspntpkalg eyvgkvkelr kdsfnvagta tftngdglcf lrmtvvdgie
      361 kttlegfrvn raegnrlypy kmpqglkpgv glyrnqdqaf ekelsgetav rrisvamcle
      421 kykegyvlka eilsshnafp qvevklpfeh qlakkaqcen ivkqltklgt tvyechnmai
      481 gegveqcfip nsvlaelrrm iveqldkmva aqrmqeryrh mavgknrlvv ieanpkqyqg
      541 ftylynisnq valqfyqaqg lkevdmayei ankykidrvk kqresvpdal lmqcrhciry
      601 slgycvkrgg kqpswheply ltlpdkrkfr lefdckncqm nihpae
//
LOCUS       WP_285132932             207 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Prevotella bivia].
ACCESSION   WP_285132932
VERSION     WP_285132932.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..207
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23440
     Region          1..199
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mikaclfdld gvvfdteply tkfwsnvgek ylpsianfai sikgqtlvqi ydkyfygkde
       61 eqkeinkeln afernmsfdy vdgfedfvlk lkaksiktav vtssnlekmr svyqqhpell
      121 tyfdkiltse dfseskpspd cylkaaanfd fdpqecfvfe dsfnglksgr asgarvigva
      181 ttndekaias ycelvirnyi gftlpnd
//
LOCUS       WP_285132941             346 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Prevotella
            bivia].
ACCESSION   WP_285132941
VERSION     WP_285132941.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..346
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=38771
     Region          26..344
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mntvltqdik qfadnfplkd klrnqtiait gatgllgscm trcllmlnrk hqlklrviai
       61 vrnaekarqm fgeetksfgi ltydfaqhvp fdapehidyl ihfaaptask afveqpietm
      121 ntvffgtnsl ldyarkthls sfvlastlev ygtiyddsia lteekqgyld pmatrssypl
      181 akraaealch nyaseygvsa kvarlaqtfg agvaiednrv faqfakavik qqditlnttg
      241 elsrsycytt davsamlyim lrgeageayn vaneksyisi rdmakmvlhr fypqgklifn
      301 lqeglgfspt tklrlsttki ehlgwqatfs leemfdrlik hlkesm
//
LOCUS       WP_285132943             342 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Prevotella bivia].
ACCESSION   WP_285132943
VERSION     WP_285132943.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..342
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40652
     Region          18..329
                     /region_name="WecH"
                     /note="Surface polysaccharide O-acyltransferase WecH [Cell
                     wall/membrane/envelope biogenesis]; COG3274"
                     /db_xref="CDD:442505"
ORIGIN      
        1 mkikdielen isryrgelmg aamlfvilfh vglprddtff glrrmgnigv diflflsgmg
       61 lwfswskhpd tkdfylrrwl rvyptwlima clyyipdftc pnwvhhrghs tniidligdi
      121 sinwdfwlnd eltfwyipat mmlylvtply lkviikhpiy rwspivmlmw cilvqyvtpi
      181 yetvghleif wsrvpiyfig inmgaaikrk drmdgaalwm illmffmala ssifleqvkh
      241 gqfpiflerm lyipltvtsv lilnrvfrrt pkwfnksvkf igmvsleayl ihdhfvlryl
      301 etfdwtywnt ffatiaitip lawtlhfvve kivitplerl ik
//
LOCUS       WP_285133012            1129 aa            linear   BCT 25-DEC-2024
DEFINITION  UvrD-helicase domain-containing protein [Prevotella bivia].
ACCESSION   WP_285133012
VERSION     WP_285133012.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1129)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437585
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1129
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..1129
                     /product="UvrD-helicase domain-containing protein"
                     /EC_number="3.1.11.5"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=130383
     Region          9..1129
                     /region_name="RecB"
                     /note="3#-5# helicase subunit RecB of the DNA repair
                     enzyme RecBCD (exonuclease V) [Replication, recombination
                     and repair]; COG1074"
                     /db_xref="CDD:440692"
ORIGIN      
        1 manndkaltv yrasagsgkt ftltveyisi lvknpedynk mlavtftnka tqemklrils
       61 qlygignglp ssdnyllqvk aktgltetsi rnnalyilek ltheyqnfrv qtidaffqtv
      121 lrnlgkelgl tanlrvdlnt qqveakavdq lidslrendp mlkwideyis snieedrswn
      181 vvkeikefgk tifdelykth ekqldkifkd ekfvtdfikr lrfvcidyek sikekakniv
      241 ekiatsaipi nyfasyaynq vvklskgkie ngdphihtqr iikgekqwas skcskkadke
      301 mlnsfvegvg ltemvanlea sriegwkmyc tsklvllhls klrllhkiak qveddnlenh
      361 rfmlsntqsl lknlmkdndi pfvferigam lkyimidefq dtsrvqwdnf kklllncmae
      421 igshnllvgd vkqsiyrwrq gdwellnnie esikpadgsy vdtssielkt latnyrsean
      481 iiqfnnaffl qamnvyeype dyftpskdkk idklehsqke klklayadva qkspktderg
      541 fvkatfyrkd avytndilae ladnikqlld igysqksiai lvrnkkeiad ivttingtew
      601 gkhiaivsee afrldaslav nilvealrll aqpsdnltra klvrayyqvv npeydfaker
      661 stklvsdvvd iahdehyyeq keefirkhln vslpseyvmd rekllrlsli dlvdklyslf
      721 qlknlsvena yistfydvln dylrdnpadi ddfvkewddn lcgvniqtdd vdgiriltih
      781 kskglefdnv lipfcdwele kkntifwvdg knkvepfsql piipvsfkkd lensffsady
      841 seehfqniid nlnllyvaft ragknlflsg kniadsnrrs nllwhclkal gttlpnakys
      901 estkekdtet kgdepicfef gtllsaheye pnkkkeeeft npftvipqpk dicietfnaa
      961 vsfrqsnksd afvqgeeitd rqkymqvgsv lhnifssikt ladiephlqa leaegviynd
     1021 dissaqlrqq itaalnneqv kswfagewev ynectilqyd katdryyeqr pdrvitkgde
     1081 mvvidykfgn hrneyyeqvh ryiqllqqmg hqkvtgflwy vmrgeilsv
//
LOCUS       WP_285133121             937 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Prevotella bivia].
ACCESSION   WP_285133121
VERSION     WP_285133121.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..937
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=106369
     Region          29..421
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          517..935
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mryckvirll fiffalaigs ssiasvcnai klpqgtikgq lsnglsyiik rnahprntte
       61 frlvmrigal qqtdaqggta hflehmafag sksyhgfsmv halegkgmkf grdinaytsf
      121 dktiyslsvp tqynttkgtr qvlgmmrewl dgltfapdyi ekergiilee lkqydthddf
      181 ytlkigdnhy srrmplgsvn dikavskaml hdfytkwyqp rfatvvvvgd idptmverml
      241 kdaftsalnt nhtvlpaysf thkkgwdmht llsplekehk veliiphqgi teksiqhsse
      301 khlgnivvhl lnnrmksrni rvdcsdtwyl adknffsvtf keadtaallh svtcfanewn
      361 tilqkgfdsd efvaalhdki aaikveerek tsaewcddfi dyiimhdisp tspedieaik
      421 aylatcssqs aqrilscwaq aaeqtvlvay tapqeeahkl tvqaiqgawq kglakaplsy
      481 tykatktvee tlvstppcla kkalydhkqi rseqsyanig vrdillsngi rillrptkdg
      541 skafsiegfg rggtadlpds vyyqyenaaa yiemggiqkv drdtlfnyla qnnisldtni
      601 ssywhgfigv aptkkahhlf nlitekvtap einveefket vqeevasfgk ttplqerikh
      661 dkdrviinmr dsimgdapsm vrekrtledi kqldiykman yfkslyddth nltlvltgdy
      721 elqpmketvv gvfskwqqrk psssamvyhs mpqqpyrsmv sspdeqqldl hfilagsflp
      781 slhetlilkl mrdviqnrll evlrqrenit yspftdlayh gldghryyfd mmltldrknv
      841 kkaqdllaei vcslqmkpis iaelnrlkls fkatktkvls ddatavwrte lvnkikngem
      901 lsdfnqydai ldsitpkkiq egftkylnpd kfiilgl
//
LOCUS       WP_285133152             190 aa            linear   BCT 25-DEC-2024
DEFINITION  anthranilate synthase component II [Prevotella bivia].
ACCESSION   WP_285133152
VERSION     WP_285133152.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Bhagat,A.K., Schlee,S., Straub,K., Nazet,J., Luckner,P.,
            Bruckmann,A. and Sterner,R.
  TITLE     Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate
            Synthase
  JOURNAL   ACS Synth Biol 11 (8), 2846-2856 (2022)
   PUBMED   35816663
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Romero,R.M., Roberts,M.F. and Phillipson,J.D.
  TITLE     Anthranilate synthase in microorganisms and plants
  JOURNAL   Phytochemistry 39 (2), 263-276 (1995)
   PUBMED   7495530
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..190
                     /product="anthranilate synthase component II"
                     /EC_number="4.1.3.27"
                     /GO_function="GO:0004049 - anthranilate synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21368
     Region          4..187
                     /region_name="PabA"
                     /note="Anthranilate/para-aminobenzoate synthase component
                     II (glutamine amidotransferase) [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism]; COG0512"
                     /db_xref="CDD:440278"
ORIGIN      
        1 mctliidnyd sftynlyhll lsaapknerf dvlkndeitp stllkyhriv aspgpgvpae
       61 agnllhifht ienkvpylgi clghqafaea ygaklyqlsh pihggttkvn inthsplfkq
      121 mkseitvary hswavekenl phelemvsat ndgmimalqh kkyplfgvqf hpesfmtpng
      181 lqmlqnfyti
//
LOCUS       WP_285133179             431 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Prevotella bivia].
ACCESSION   WP_285133179
VERSION     WP_285133179.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..431
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47183
     Region          2..429
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 msyeetvqyl fnstpvfehv gaqaykegls nthlldkhfg hphtqfktih vagtngkgsc
       61 shtlaailqq egyrvglyts phlvdfreri ringemiseq yvidfvaqer sffeplhpsf
      121 felttalafk yfaeqqvdia iievglggrl dctniitpll siitnisldh tqflgdtlak
      181 iayekagiik envpvvvget vpetrpvfea takeksapie faedipffsa htttstkgia
      241 ysdtpfgtii gelmgdyqvk nantvlhacv kliqlgiike eqsivkgfan vtattglmgr
      301 wqqladhplt vcdtghnlgg wqylskqiks aakgethivf gmvddkdlda vlallpqnah
      361 fywtqpsshr afpvekvaee alaiglkgtq yptvlaayea akaaaspddf ifiggssyvv
      421 sdllsahtrt d
//
LOCUS       WP_285133200             374 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Prevotella bivia].
ACCESSION   WP_285133200
VERSION     WP_285133200.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 374)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..374
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=43180
     Region          <121..340
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mlfppfpykl issqelkdgy lvdipsfckk nkdnpkcrqf ysslnpkdgl qicpygfvae
       61 chrigdqqvi fsclnvkrks drklmrklqd detiqlsidk ysqirnifeq slltspnesv
      121 dfkeahvqav lnaekealdn amhefrnlnt qlvsqaekls dalnnkfkde tllgslskni
      181 yalsnlmkvr iesynlevga nslenqakip iaiyrkiekv ykcligqcfe rnihislign
      241 synkyeagpm leialfiime naikyspegk dititfkedn nslcvefnnw alkakngeek
      301 rfkergyrgs riieqgkvkg rgigfyllhq iceqykievs yyflkdhfaq dgysyapfiv
      361 klkfkdmilp eier
//
LOCUS       WP_285133357             432 aa            linear   BCT 25-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Prevotella bivia].
ACCESSION   WP_285133357
VERSION     WP_285133357.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..432
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=49585
     Region          46..432
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mflkkitiit siiivsvlfs vteskamilp tdradslivn qlrskgvhfs knnsvallks
       61 gqekfndmfk aieqakssih leyfnfrnds inkelikrla vkakegvevr avfdgfgnas
      121 nnrpmtkayl keirkmgiei ynfkplqfpw fhcifnrdhr kivvidgkia ytggmnvady
      181 yikgtkvvgs whdmhcrieg devntlqkif fkmwylvsgq klqgakyfrg isnahyikgl
      241 ipdtaatagk kmvgiinrep hitkdiiryf yvnaindakd siklinpyft lnhnlmkalk
      301 navkrgvkve illsiksdip ltpdcgfyna hklmkngcti wlykpgfhht kiimidgqfc
      361 tvgsanlnar slrwdreena viidpyttke ldilfenqkk dsfiltpenw kiwrtpwqrl
      421 rgwfahllap ll
//
LOCUS       WP_285133427             114 aa            linear   BCT 25-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Prevotella bivia].
ACCESSION   WP_285133427
VERSION     WP_285133427.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Rengstl,B., Oster,U., Stengel,A. and Nickelsen,J.
  TITLE     An intermediate membrane subfraction in cyanobacteria is involved
            in an assembly network for Photosystem II biogenesis
  JOURNAL   J Biol Chem 286 (24), 21944-21951 (2011)
   PUBMED   21531723
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Komenda,J., Nickelsen,J., Tichy,M., Prasil,O., Eichacker,L.A. and
            Nixon,P.J.
  TITLE     The cyanobacterial homologue of HCF136/YCF48 is a component of an
            early photosystem II assembly complex and is important for both the
            efficient assembly and repair of photosystem II in Synechocystis
            sp. PCC 6803
  JOURNAL   J Biol Chem 283 (33), 22390-22399 (2008)
   PUBMED   18550538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..114
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=12681
     Region          23..>114
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
ORIGIN      
        1 mgqivnfgse mirinfeknr ieystnngns whsrysgsna gefyslcdyg nellactskg
       61 vfysknggns whsrytspva gdfkeitvqg nellaqtskg lyysknggss whrr
//
LOCUS       WP_285133615             346 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Prevotella
            bivia].
ACCESSION   WP_285133615
VERSION     WP_285133615.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..346
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=38721
     Region          26..344
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mntvltqdik qfadnfplkd elrnqtiait gatgllgscm trcllmlnrk hqlelrviai
       61 vrnaekarqm fgeetksfgi ltydfaqhvp fdapehidyl ihfaaptask afveqpietm
      121 ntvffgtnsl ldyarkthls sfvlastlev ygtiyddsna lteekqgyld pmatrssypl
      181 akraaealch nyaseygvsa kvarlaqtfg agvaiednrv faqfakavik qqditlnttg
      241 elsrsycytt davsamlyim lrgeageayn vaneksyisi cdmakmvlhr fypqgklifn
      301 lqeglgfspt tklrlsttki ehlgwqatfs leemfdrlik hlkesm
//
LOCUS       WP_285133679             646 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidase U32 family protein [Prevotella bivia].
ACCESSION   WP_285133679
VERSION     WP_285133679.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..646
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=73058
     Region          1..302
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
     Region          448..507
                     /region_name="DUF3656"
                     /note="Collagenase; pfam12392"
                     /db_xref="CDD:463557"
ORIGIN      
        1 mrtiellapa knvecgkaai dhgadavyig aqkfgarqsa gnsvediael cayahrydar
       61 vhvtlntiiy dhelddtikl veelievgvd aflvqdmglf saikkllppy valhastqcd
      121 trtvnkakwl qqqgfnrvvl arelsadeik niheqlpsle leafvhgalc vsysgvcyas
      181 qhcfdrsanr gacsqfcrla fdlvdsdghm ietqahllsl kdmkqidnle tlmrsgacsf
      241 kiegrlkdin yvknvvsays qrldeiiaky pkefcraslg nvvyqftpdl nktfnrgytn
      301 yfvqgrqani fspntpkalg eyvgkvkelr kdsfnvagta tftngdglcf lrmtvvdgie
      361 kttlegfrvn raegnrlypy kmpqglkpgv glyrnqdqaf ekelsgetav rrisvamcle
      421 kykegyvlka eilsshnafp qvevklpfeh qlakkaqcen ivkqltklgt tvyechnmai
      481 gegveqcfip nsvlaelrrm iveqldkvva aqrmqeryrh mavgenrlvv ieanpkqyqg
      541 ftylynisnq valqfyqaqg lkevdmayei ankykidrvk kqresvpdal lmqcrhciry
      601 slgycvkrgg kqpswheply ltlpdkrkfr lefdckncqm nihpae
//
LOCUS       WP_285133687             197 aa            linear   BCT 25-DEC-2024
DEFINITION  IMPACT family protein [Prevotella bivia].
ACCESSION   WP_285133687
VERSION     WP_285133687.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Park,F., Gajiwala,K., Eroshkina,G., Furlong,E., He,D.,
            Batiyenko,Y., Romero,R., Christopher,J., Badger,J., Hendle,J.,
            Lin,J., Peat,T. and Buchanan,S.
  TITLE     Crystal structure of YIGZ, a conserved hypothetical protein from
            Escherichia coli k12 with a novel fold
  JOURNAL   Proteins 55 (3), 775-777 (2004)
   PUBMED   15103642
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Okamura,K., Hagiwara-Takeuchi,Y., Li,T., Vu,T.H., Hirai,M.,
            Hattori,M., Sakaki,Y., Hoffman,A.R. and Ito,T.
  TITLE     Comparative genome analysis of the mouse imprinted gene impact and
            its nonimprinted human homolog IMPACT: toward the structural basis
            for species-specific imprinting
  JOURNAL   Genome Res 10 (12), 1878-1889 (2000)
   PUBMED   11116084
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..197
                     /product="IMPACT family protein"
                     /calculated_mol_wt=22400
     Region          4..195
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 mcndkyktil enqisegfys ekrskflafa hhvnsaaeal efvkeyrkky ydarhccyay
       61 vvgadrsefr snddgepsst agkpilgqin sneltnilii viryyggvnl gtsglieayr
      121 laaasaivns nieerfveei vkftftypmm ndvmrivkdm eprivsqtfd ntceivlsir
      181 qskadelrtr lkklsfd
//
LOCUS       WP_285133704             230 aa            linear   BCT 25-DEC-2024
DEFINITION  ExbD/TolR family protein [Prevotella bivia].
ACCESSION   WP_285133704
VERSION     WP_285133704.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..230
                     /product="ExbD/TolR family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25747
     Region          15..>92
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD/TolR; pfam02472"
                     /db_xref="CDD:426791"
ORIGIN      
        1 maemvsnnne gggkqkkmtv rvdftpmvdm lmllitffml ctslskpstm eltmpsndkn
       61 tpdvkkneak dshsitiyia dgdkmfygeg kpeydnpswl kpadwtrtkt giryvlqhkq
      121 vgggdtgeia sipyqdlnia mqelerkkqa npkaypdsiy qaeimniktg vingkkigtl
      181 tvvikltdka ayrhlvdild emqisyigtf vidklndqdk sllekkgiql
//
LOCUS       WP_285133706             254 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Prevotella bivia].
ACCESSION   WP_285133706
VERSION     WP_285133706.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..254
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29046
     Region          42..247
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 miprllyrvy alfvflplfl ivslitaivt ivgcklgngh fwgyypgklw scftlrilfl
       61 pvkvegrenl vsgqsyvfvs nhqgsfdifl iygflgrnfk wmmkkgirki afvgeacasa
      121 hhifvdksga skiketydha revlqeemsl vvfpegarsf tghmgifrrg afmladelql
      181 pvcpltings fdvmprtkdw hfprwhrlrl tihkpilpkg kgiefekqtm neayevimsg
      241 ltkeyqgfve npdq
//
LOCUS       WP_285133818             639 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Prevotella bivia].
ACCESSION   WP_285133818
VERSION     WP_285133818.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..639
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=70934
     Region          101..639
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mrryllltic citsvltlfa qhtssatkrk ttttnvqtkt tkriapaakp tvervqntnq
       61 htqkatpkag kkpqrvdrka qpaqrsskkg kktttpikrk aatpkyvtts aikdlqkknq
      121 eiqkeisqne tevkekqkdv eqrlrkimrl dteigqqqqt inhiatdvkg ldnnisilkg
      181 qlkslqvqlt errrrfilsm rymarhrsiq dkmmfifsak slsqmyrrlr fvreyaayqr
      241 aqgeqlkakq aqidhkqvql qqvrvqkstl lykgrqahaq mqskrveqqq vvsslqkdqq
      301 alqaviaqrr qqqqainaqi drlvtieiqk araralaear aqaaaraaaa kkraeemark
      361 raaaikaaqe narriaeaka reakakaeaq aaaaaaekar keaaaraeaa riaaekarqa
      421 aaaetssrke aarrkaeaae rkareaqqka eakaaadrar adqlaneaea nrvaaerkaa
      481 adreraarea eaarkadevd nsmtaadram tgsfannkgr lpmpmsgriv thfgqynvag
      541 mhnirlnsdg inikgapgsp vrsvfmgevs gvfhaggsti vmvrhgfyis vycnlaavnv
      601 htgqkvgtgq tlgtvnstgv lqfqlrnera klnpeqwlr
//
LOCUS       WP_285133883             262 aa            linear   BCT 25-DEC-2024
DEFINITION  RsmE family RNA methyltransferase [Prevotella bivia].
ACCESSION   WP_285133883
VERSION     WP_285133883.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Basturea,G.N., Rudd,K.E. and Deutscher,M.P.
  TITLE     Identification and characterization of RsmE, the founding member of
            a new RNA base methyltransferase family
  JOURNAL   RNA 12 (3), 426-434 (2006)
   PUBMED   16431987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..262
                     /product="RsmE family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=29996
     Region          7..246
                     /region_name="RsmE"
                     /note="16S rRNA U1498 N3-methylase RsmE [Translation,
                     ribosomal structure and biogenesis]; COG1385"
                     /db_xref="CDD:440995"
ORIGIN      
        1 mkearyfyvp nakaqtelpt eealhavrvl rmkegdelfl mdgvgcfyra evvltsakrc
       61 ayviketlpq tktwegrihl aiaptkdmgr iewmvekate lgideitfld crfserkqir
      121 tdriekivis amkqsrkgwk pivnemvsfk efiqtmetna sqqeyslasf ichcyneidk
      181 ndffsviteq enlkddvlil vgpegdfsid evqlaleagf qsvtlgesrl rtetaglnai
      241 amtqlahrkr dnifnnthtr rv
//
LOCUS       WP_285133885             243 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Prevotella bivia].
ACCESSION   WP_285133885
VERSION     WP_285133885.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..243
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27637
     Region          1..242
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mkrkaiimga tsgigrevak lllnkgweig itgrrkeeli kfqqkapnli hfkaidvckd
       61 dapillleli demggidlyv hssgygkqni nldtaiekqt lltngvgftt midavynyfa
      121 ntreeghita itsiagtkgl gaapaysatk rlqwtyleal aqqarmrkla itftdfrpgf
      181 vatdflgndh ypmlmqkkyv akkivqgifq hrrrvtidwr yrllcffwkl tpsfiwermk
      241 irt
//
LOCUS       WP_285133899            1076 aa            linear   BCT 25-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            bivia].
ACCESSION   WP_285133899
VERSION     WP_285133899.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Glenwright,A.J., Pothula,K.R., Bhamidimarri,S.P., Chorev,D.S.,
            Basle,A., Firbank,S.J., Zheng,H., Robinson,C.V., Winterhalter,M.,
            Kleinekathofer,U., Bolam,D.N. and van den Berg,B.
  TITLE     Structural basis for nutrient acquisition by dominant members of
            the human gut microbiota
  JOURNAL   Nature 541 (7637), 407-411 (2017)
   PUBMED   28077872
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Nagano,K., Murakami,Y., Nishikawa,K., Sakakibara,J., Shimozato,K.
            and Yoshimura,F.
  TITLE     Characterization of RagA and RagB in Porphyromonas gingivalis:
            study using gene-deletion mutants
  JOURNAL   J Med Microbiol 56 (Pt 11), 1536-1548 (2007)
   PUBMED   17965357
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   4  (residues 1 to 1076)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11499350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..1076
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=118686
     Region          23..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkitlllv slflmvgtal aqknvsgtvi ssddgqpiig aavkalgasv gtqtdidgkf
       61 sfelpagetk ivvsyvgmvs qtlvggtgmk itlkadnknl devvvvaygt akkqslvgaq
      121 asisskqlen rpvtnvtnal agaapgvqvt tslgqpgssa simirgfgsi nassaplfvv
      181 dgsvyngsla dinpadiesm silkdaasta lygssagngv vlittksgkr nsaeptftft
      241 tsqgisnrgq qpyetvgvne yfplmwqqwy nqyiyeyges keqaalwany emyddlrldr
      301 yqpfagiktg ltfdaatktl gtstdqtqwv dgvpmivgrd gklnpeitgl rwgddldwek
      361 alfrtgyrge ynlsgsysnd kintfmslgh iteqgyrknt eyertsarln ldykvnkfld
      421 lggnisfaha vntapkkasg nysansfafl qgiapfypih ahnagtgeyv ldpitgqpif
      481 dysngrpynd rfnpvyegel dhstttrdml nsrgnatihi lpelklmlnv aydltnsknk
      541 rrynnimgdq pagmlsiedf atsaltfnql leyskkfgnh eitallghes yklhdeslsg
      601 ekknmlvlgi defpnltnit glssytdkyr kegyfarlnw dwmdkynfsa sirrdgtsrf
      661 hpdnrwgtfw avgagwhiar ekfmagaskw lddlkirvsi gqtgndgvss yyayqtlygf
      721 gsnnlygggl rlytyadpsi rweaqtsmdl alefsilrri tgtfeffnke skdlifpypl
      781 pmstgigsqd rnigkvrnlg fefnvnalii nrpdfswkvn vngthyrnki vrlpednrek
      841 gieldyhkyl egksiydyyl nefvgvdpdd giamyrldte lypdakplgt egekatltkd
      901 gqkakkhfcg tsipdlyggf gttltwkgfe lginfayqlg gktydsgyag lmgrrlkagr
      961 amhvdmlnaw kqkgentnip rldagqggmy dgimsdrfli sssalmlkni slgyvlpasw
     1021 mrsiylksgr isvaaenlfl vsarkgmnpm gqysgvpgaa gyaynrtvta tlsltf
//
LOCUS       WP_285133932             938 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Prevotella bivia].
ACCESSION   WP_285133932
VERSION     WP_285133932.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..938
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=105632
     Region          25..465
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          514..938
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mklkqlllls fcfvagmvsa qqmgpistnk nvrqgklsng ltyyilhnew pehvanfyia
       61 qrvgaiqend dqrglahfle hmafngsenf pdstlleftr slgvefgtdl naytsidqtv
      121 yrvcnvptkr qsaldsclli mkdwsngltl adkeidkerg vihqewqlgs spsmriyerv
      181 lpkmypgsky gyrlpiglms vvdnfpykal rdyykkwyrp dnqciivvgd vdvdhteaqi
      241 kklwanvvtp anaakvvdel vpdnkeaiyi vdkdkelqnt svslamkhdv ypdsekndqt
      301 yyidgyaksl igmmlnqrlt ellqkadcpf tsaygydgny ilsktkgafi ldaaakegkg
      361 lealasiyre alrirqfgft ateferakan ylsekesqyt nrnkktnnsy gdelrdhyla
      421 nepipspede yqllkriaem palnvnainm yvkelisdkd snlvvslfeq ekagkqyite
      481 aqlanviknv raekleawvd nvkqepllde tklpkagkiv ketenkvlgy kvltlsngar
      541 vllkktdykd neiqftgysk ggkslygaad fdnlklfdiy lstcglgnft nqelskalag
      601 kevnmnvslt eisqriggsc vpkdvetmmq laylhftdir kdeaelgvik aqletalknk
      661 dlspeavysd sltytitghn prfsplqlst vqkanidril qiwkerfasp gqftymfvgn
      721 fdeatlrpli ekylaclptg kaenfvqysr lvdgkvsnkf trksetpkai afefwrqpas
      781 ytlensvlad aagqvlsmvy lkdiredasa aysvgaggsl skegnksyiq iqaycpmdpt
      841 ksdlavkllh dgfknntmki dtdklqkvkd nmlknadida ksnnhwasvi eeldrfgvdf
      901 htdykkvvna mtpeklanfl kgvyqsgnqi evvmtpak
//
LOCUS       WP_285133961             915 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Prevotella bivia].
ACCESSION   WP_285133961
VERSION     WP_285133961.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 915)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..915
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..915
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=103991
     Region          16..399
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          495..913
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 magvhtaiki pkgtikgrla nglsyiikrn ahprnttefr lvmrigalqq tdaqggtahf
       61 lehmafagsk syhgfsmvha lerkgmkfgr dinaytsfdk tiyslsvptq snttketrqv
      121 lgmmrewldg ltfapdyiek ergiileelk qydthddfyt lkigdnhysr rmplgsvndi
      181 kavskamlhd fytkwyqprf atvvvvgdid ptmvermlkd aftsalntnh tvlpaysfth
      241 kkgwdmhtll spleknhkve liiphqgite ksiqhssekh lgnivvhlln nrmksrnirv
      301 dcsdtwylad knffsvtfqe adtaallhsv tcfanewnti lqkgfdsdef vaalhdkiaa
      361 ikveerekts aewcddfidy iimhdispts pedieaikay lstcssqsaq rilgcwaqaa
      421 eqtvlvayta pqeeahkltv qaiqgawqkg lakaplsyty katktveetl vstppclakk
      481 alydhkqirs eqsyanigvr dillsngiri llrptkdgsk afsiegfgrg gtadlpdsvy
      541 yqyenaaayi emggiqkvdr dtlfnylaqn nisldtniss ywhgfigvap tkkahhlfnl
      601 itekvtapei nveefketvq eevasfgktt plqerikhdk drviinmrds imgdapsmvr
      661 ekrtledikq ldiykmanyf kslyddthnl tlvltgdyel qpmketvvgv fskwqqrkps
      721 ssamvyhsmp qqpyrsmvss pdeqqldlhf ilagsflpsl hetlilklmr dviqnrllev
      781 lrqrenitys pftdlayhgl dghryyfdmm ltldrknvkk aqdllaeivr slqmkpisia
      841 elnrlklsfk atktkvlsdd atavwrtelv nkikngemls dfnqydaild sitpkkiqeg
      901 ftkylnpdkf iilgl
//
LOCUS       WP_285134032             705 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Prevotella
            bivia].
ACCESSION   WP_285134032
VERSION     WP_285134032.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 705)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 705)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 705)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 705)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..705
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=79624
     Region          2..594
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mknydfekrr lvlsavaigi vliyiirlfa lqiasddyrk sadsnaflkk iefpsrglit
       61 drkgkllvyn qpaydimvvm neekghldtl dfckalnitk effiqrmkdi kdrnknpgys
      121 rfsqqlflgq vkdkefsafh erlyrfpgfy iqrrsirayq rpigahilgd vaevnqadve
      181 kdeyyqpgdy igkmgverey ekelrgrkgv qillrdahgq iqgryqdgkf dqkpipgsdi
      241 qlgldadlql lgerlmegkl gaivaiepkt gqilamvssp tfdpremigk lrgktqhtlm
      301 ldpakpllnr aimgqyppgs tfktsqavty ytegiisdst ryachhgfyf kglhlgchah
      361 asplslvpal gtscnayfcw glyhmlsnrk ryknlddamt vwrnymvsmg fgyklgidlp
      421 gekrgmipna qfydhafkvw npltvisisi gqgevnltpl qianlgatia nrgyyitphv
      481 vrkiqgrrld kkyterhrtm gsvksyervv lgmqasvnng tcagaphpgy tlagktgtaq
      541 nrgkdhsvfm gfapvenpki aiavyvengg fgavygvpig almieqying kltpgdmaka
      601 dqiqkrhiay sfkrpltksd slrldsikrv tqikdslkqv kekqmieeik kakeekakld
      661 aekqenkkpq mpndpiirpe tdesvikekg ddhkkdkkpt deekk
//
LOCUS       WP_285134826             668 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Propionibacterium freudenreichii].
ACCESSION   WP_285134826
VERSION     WP_285134826.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..668
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=74224
     Region          13..609
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mtdlrelpsq plavepahvg lmvkasvqaf gdrpatrvlv gkrwvvasyr eldaramqia
       61 aalmysgvek gdrvgfysrn rpewtqvdla cqfigavsvp iyatdtvdev vhiandcgmv
      121 vafagradea ermgqaserv aslrrvisfd scprtdvtwl eyfapsdrpv pervvsrina
      181 rlnkasgddl fsiiytsgtt gapkgvklah rammselral hrsfpistrd hslcflplsh
      241 alergwtcyl wahgcmntyv vdtrkvgemm rrarptlmva vpklfetvla evhkasavtp
      301 rrkrilqwav svgqhlqfdy rqgrkplllw raqlpladrl vlrkireamg gqktmlvsgg
      361 aplrretelf fgaaglqiln gygmteaapl isynthtayr vgsvgrvmpg griklgdkhe
      421 ilyqgpnvmd gywdneeatr eafltddegt wlrtgdlgri drrgflfvtd rlkdiivteg
      481 gknispqpie ellqsdpmfe hvvvlgdnrp fltllvqpsm anlqklaeal hidyghvsel
      541 fnnqnildei kksaealtkn lpkyqqfrdl rmssegfsia nglltptlkv krreverrfr
      601 glidemytki glhhdpksas grdpksasgr dsrsasgrds gtasggdrgr thgqaprstr
      661 ggdsptar
//
LOCUS       WP_285134167             339 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Prevotella
            bivia].
ACCESSION   WP_285134167
VERSION     WP_285134167.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..339
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=38968
     Region          4..307
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mskkvivfga tgnlgapisv ylkqngydvi avghrtsdng ffedmgipyy svdienakqf
       61 dvlptddiya vahfasslps ryeynprdlf esitigtlnv lewmrkigck kivfpqtpsd
      121 masyhncgkm ipedaprefp ltgdhavyti aknaavdlie nyhaeygfsr fvfrfftiye
      181 yhpnayhyrn ykhlmmpfrm lmdraskslp ieiwgnckka kemvyikdfi rlvklaidsd
      241 ieggiynvgn gwqvsleeqi lgiikvfspk dnpspviyvk dkpdplenaf eitkikrdfg
      301 yeplytyilq ledlkhdmet epfaklwgtk edyepkesk
//
LOCUS       WP_285135058             355 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Staphylococcus aureus].
ACCESSION   WP_285135058
VERSION     WP_285135058.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     Protein         1..355
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=38484
     Region          11..353
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mwnknrltqm lsieypiiqa gmagsttpkl vasvsnsggl gtigagyfnt qqledeidyv
       61 rqltsnsfgv nvfvpsqqsf tssqienmna wlkpyrralh leepvvkite eqqfkchidt
      121 iikkqvpvcc ftfgipnesi ikrlkeanik ligtatsvde aianekagid aivaqgseag
      181 ghrgsflkpk nqlpmvgtis lvpqivdvvs ipviaaggim dgrgvlvsiv lgaegvqmgt
      241 afltsqdsna sellrdaiin sketdtvvtk afsgklargi nnrfieemsq yegdipdypi
      301 qneltssirk aaanigdkel thmwsgqspr latthpanti msniinqinq imqyk
//
LOCUS       WP_285135092             296 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Propionibacterium freudenreichii].
ACCESSION   WP_285135092
VERSION     WP_285135092.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 296)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18950610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..296
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=32630
     Region          15..131
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
     Region          141..280
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mtakpavvaa gavvfrgsge qrrvlvehrp hyndwtlpkg kphgdeqlpv tavreveeet
       61 gihvrlglpl pslhydvsag pkqvhfwlgh enrpehphrd detdriawpt lpeaaellty
      121 pdevellara vpladralgt lvvtrhakar prkswqgddw lrplaargtr qsdrlmalld
      181 afgvrrvlss tstrclqtve pyakaigsqi hpvhllseea algrdeeiad lmwqlrvqva
      241 qspedplvvc ghrpvlgamq aglhipiqhl ttaqslvlhi gdeaepvave sypspl
//
LOCUS       WP_285135269             659 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Propionibacterium
            freudenreichii].
ACCESSION   WP_285135269
VERSION     WP_285135269.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..659
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=70162
     Region          386..639
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mttapqhqgp tvadygawss pltpaetvaa gvtlrefgsd gddlywlesa sddvarlsll
       61 rsrdgqivei ttapmnvrtr vyeygggswg arqgtvawsd dtsgqvmats lggltmaitp
      121 vdpnyryaaf vpvpeheciv cvredhsapg epiltiaala wptddvvpha gtvlvegadf
      181 yadptvnedg siawiewnqp amawdasalr agtlvsipel avmhvhtvfd gqhdpgspvs
      241 iqhpkwasdg rllfmsdaag ywnlhmwtpt rgirqlvdea adgdlpmwqq grsafalsgg
      301 wiyyaswdag icslsrvpah ggasealtsv sdvdglasvg gtayalvtrp napaavvsig
      361 aegmriehsp gvlpdpkits vahsltfegk hgqvqswffe phnedfvapa gqlppviltv
      421 hggptgvatd eydpqvqfwt srgfgvlsvn ysgsagfgra yrerlrgqwg iadvddcida
      481 aesllsadla dqskiaimgg saggftvlaa ltrssvfsag icrygiadlv amqeggthkf
      541 eatyndgllg pwpqarkvye erspihhldq lhapmlilqg lddavvppqq adelaaalrq
      601 rslpvsvvmf ageghgfrmp atrtrvlnds lsflsqlfgf rpagtvealt ienlpgaah
//
LOCUS       WP_285135151             283 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein
            [Propionibacterium freudenreichii].
ACCESSION   WP_285135151
VERSION     WP_285135151.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..283
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30784
     Region          17..269
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mvskpppdas gskrlsvsls tsscypehta eafdiaaeag ydgvevmvgl daasadvpyl
       61 arlaaqsgmp vvsvhapcll ltqnvwgpdp wdkvrhscea alalgsdvvv lhpplrwqre
      121 yaagfvagvr disehtgvti avenmypwrt pgrafqaylp swdptdldyd altldvshaa
      181 tsqldalela rmwgprlrhv hltdgvglrr dehlfpgegt qnvwgllqyl ndspfdghiv
      241 levntrkadn haervrelre vadntrlhlg qldaarpgtt pts
//
LOCUS       WP_285135598             266 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285135598
VERSION     WP_285135598.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..266
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27216
     Region          8..242
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mplrlsptfr aalaasdrpl agmwvcsgsa lvaeiaagsg ldwllvdmeh satsldsvla
       61 qlqvaaaypv tpvvrvawnd pvtikrvldv gaqnlivpmi stedearaav aatryppqgi
      121 rgvgsalars arwnrvddyl aeaaehvslt vqiettagva naagiaaveg vdavfvgpsd
      181 lsasmgllgq qshpdvvaav havftacrda gtpvgvnafd pavadaylda gadfvavgad
      241 vallarasea ltarfvtgra aqrdsy
//
LOCUS       WP_285135664             642 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285135664
VERSION     WP_285135664.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..642
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=69299
     Region          10..636
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mttktrqdrl valllrdaew staasladal gvtprsvrsy vtavnarvpg gaaiesgpqg
       61 yragsnaaaa lrsitgsdag tprdrlhtlv rrlldaadgi dvfdtadslh vspatleadl
      121 srvrgllggt eltlersast arlrgtevaq rrllsklahd emdaglfdld alrrtlgers
      181 vgarafgpfk aelvaelgal gyyvneigig dvvmhiaiaa drttrdralg spggdssdaa
      241 aavvtlldrl tlkhigvqlg sgdlrhlatl vltrivapgs pgdddvrarl dpavevavrr
      301 vvenaasefl vdiahddfil rlalhvqnll arareqawsr npltrslkst ypmifevavy
      361 iakglqdglg ipilddeiay iamhvggrle rsrradqllt ativcpgyye mqellrssvd
      421 rslgqaievv gvetridpsw daidtdlvlt tidpprpgdr fvriqpfltd advervqaaa
      481 grirrgrrla rlraeleryf apeafvrgld atdgeagvir rlggllvsqg videdyvlra
      541 vereaissta ftdalavpha mgmtatqtri aigiadpsia wgegrvqvva lvafsetdre
      601 afqtvfeqfv evfserdsvq rivrratsfp afldelvavi dg
//
LOCUS       WP_285135606             115 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285135606
VERSION     WP_285135606.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..115
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12007
     Region          11..98
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mstatltasl thtaalsrlg halsdttrag vllalrqapa ypsdladelg vsrqvmsnql
       61 aclrgcglve avpegrrtry rladthlapa ldellrvvly vepgccager ctcga
//
LOCUS       WP_285135675             215 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285135675
VERSION     WP_285135675.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..215
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=22947
     Region          1..205
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mrvclastsp arlmllrqag iepearaprv deeaviaeve aaegrrlpaa ehvlllarrk
       61 aedvarrlha eepgfdgfvi ggdsmfelgd eilgkpytpe aatarwrqmr grtgvlhsgh
      121 svfrlspgad pteahavaea svtfaadvdd deiaayvssg epllvagaft vdslggafie
      181 rvegdpstvv gmslsttrrl vrelggswtd lwnrs
//
LOCUS       WP_285135705             463 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285135705
VERSION     WP_285135705.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..463
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=49690
     Region          191..436
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mamytnhpvs alptappret tghlllrawc vfvillalgg vglvnaagpv vgavvagasa
       61 vvslviwvvt rppiavrrlp wlafaylawa aasiawsawt aasvltwlll littfqglfv
      121 gavltwrdvv ravasaakwv vglsllfeva vsllvrgpll pgfvvpsarv dptlcwsrdn
      181 lfdggriqgl fgnadllaaa mlvavivfgv rlaagaprrv llmvwtalaa flfvragsat
      241 aviaaafval vlgtvlvmrt arrpgertrw yllyaaigvg fgtalwfgre avfgvlgrga
      301 dllgregiwa dvreragqrp fagwgfstpw ipteplidgw ivdhdqtvvq ahsmwldayl
      361 qlgvvgvill alvflayvwr swffavdspr wdlrddrphs pltllptlvg allvvqgltd
      421 sgplalwgwm fvilfgskik qtpfvghgpg eisasvegge rqr
//
LOCUS       WP_285135696             276 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285135696
VERSION     WP_285135696.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..276
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30488
     Region          3..>140
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mtaprlsvvi paynngrtia etmrsvladr svdlelvvad hastddtleq irrfedderv
       61 tiletpaggg aprnwnrvte sargellklv cgddivmpgt lerqmriled pgvaltacrr
      121 divdakggvl fsgwglrglr rrmtgaravr aavragsnlf gepasvmmrr delasaggwr
      181 gdfpylidqa tycevlmrgd fvpdlntgat frmsasqwsv alvrdqasqa kdfhravhre
      241 hphavssvdv vvgnlratlm ararqisywi lkrrmr
//
LOCUS       WP_285135826             257 aa            linear   BCT 25-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Microbacterium
            sp. lyk4-40-TSB-66].
ACCESSION   WP_285135826
VERSION     WP_285135826.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 257)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..257
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=27452
     Region          20..257
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mpevtthtrn vplgsttlql swaagtdtgr rrevnqdavl aefplfvvad gmgghlggei
       61 asastvdrlr avveggavst kniekalsra vkdivshpet tdegtgttlt gvylethtee
      121 phwvtlnigd srvyvlrdge ivqvttdhsv vqeliaagrl speeaenhpy gnvitravgp
      181 sdsvkpdylr ldvldgdrfv icsdgltkel tdfgirhfle ansdpaaave ammaaaleng
      241 grdnitivvl dvvrrds
//
LOCUS       WP_285135877             309 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285135877
VERSION     WP_285135877.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..309
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33230
     Region          2..296
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mhrvrlevgk avvgqdgtvt glliallsrg hvllegvpgv aktllvrsfs ralgldtrrv
       61 qftpdlmpgd vtgslvydpr aggfdfrpgp vfthvllade inrtppktqa alleameerq
      121 vssdgesral pdpflvaatq npiehegtyt lpeaqldrfl lklvvdlpgr daevdvlrrh
      181 aggfdprrld dagmhavvta deilaaqraa asvavdddll gyvvdlarat rqspsvllgv
      241 sprattglla aakawawlgg ypaitpdhvq tmlvpvwrhr irlrpeaeie gvsvdailts
      301 vlqqtrvpi
//
LOCUS       WP_285135898             112 aa            linear   BCT 25-DEC-2024
DEFINITION  histone-like nucleoid-structuring protein Lsr2 [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285135898
VERSION     WP_285135898.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Gordon,B.R., Li,Y., Wang,L., Sintsova,A., van Bakel,H., Tian,S.,
            Navarre,W.W., Xia,B. and Liu,J.
  TITLE     Lsr2 is a nucleoid-associated protein that targets AT-rich
            sequences and virulence genes in Mycobacterium tuberculosis
  JOURNAL   Proc Natl Acad Sci U S A 107 (11), 5154-5159 (2010)
   PUBMED   20133735
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18741]
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Gordon,B.R., Imperial,R., Wang,L., Navarre,W.W. and Liu,J.
  TITLE     Lsr2 of Mycobacterium represents a novel class of H-NS-like
            proteins
  JOURNAL   J Bacteriol 190 (21), 7052-7059 (2008)
   PUBMED   18776007
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Oshima,T., Ishikawa,S., Kurokawa,K., Aiba,H. and Ogasawara,N.
  TITLE     Escherichia coli histone-like protein H-NS preferentially binds to
            horizontally acquired DNA in association with RNA polymerase
  JOURNAL   DNA Res 13 (4), 141-153 (2006)
   PUBMED   17046956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10570331
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..112
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12151
     Region          1..111
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 makkhitqvi ddldgsvidd gttvqfsfeg rayeidlsvh naekmrdalr pyisagraah
       61 splsaprrtp rgraiptrdl advrswavkn ghaintrgri sssvldayda ah
//
LOCUS       WP_285135946             573 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285135946
VERSION     WP_285135946.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..573
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=61942
     Region          107..545
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mllaiglfta gigtmvflrt tlvnnldeql aqqaagniad svftmtpidg qivfsqiena
       61 pqigsmvvvy gpdgerkafy ngtasktlpq lpstftveqt ysqidrriel hdadsgqhfl
      121 arvgvlqvng ssgvytqmvi qplaqtdriv aayigiyafv alliliatal ltrwlvtlaf
      181 rnlrqvetta mdiaagdfsq rltdivpdte vgrlktaina mlaridgalg qrdatvrqmr
      241 rfigdashel rtplvtmrgy aelyrmgair sdedvaqsme riekeairmg alvedllala
      301 rlderrdvti ipldlrpiar daaldlrvts pqrevtvddt tsrdeivlpt itldplldag
      361 gdpttaasrr raapttsama iagatlsrlr rkprdaaesa stpadgapta aptsptgvvr
      421 tpariapivl gdenkvrqvv anllgnarrf tgddspiglr vgvdvesdmg wieiidhgeg
      481 vpeqirdqif qrfwradtsr tretggsglg lsivasivdl lhgtvevvdt pgggatfrvs
      541 lpladrrdaq ehalietqpl erlpagyrpe pta
//
LOCUS       WP_285135954             188 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285135954
VERSION     WP_285135954.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..188
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=19698
     Region          44..179
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mnrirktlva vaslldprvy lhglrvlhfy gyshvsqvrk ltrgtdvsfa pnvsfrnaer
       61 itigsgtrig eystiwagns tgritfgeka llaprvtlta snygiakgva pmdqpkqedd
      121 ivigagtwlg advvvlagvt igdgaiiaag avvtkdvpen aiaggvpakv iayrrddepa
      181 stpgrvta
//
LOCUS       WP_285135979             404 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285135979
VERSION     WP_285135979.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..404
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=43478
     Region          6..374
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mqqpqlvlls ifagvligaa mvglivaalr ardrsraets idvpegvdam leamddpafv
       61 cdmsstvlal spaaevfgvh tgelvssdel krvarvardt gaavaenlrl rrgaapaear
      121 lvavratpis nrltlvvlrd itererveem rrdfvantsh elktpvgavs llaeaiesas
      181 ddpdqvrhfa armqaevarl salvnrilsl srlqaseelr dvrdvsidev vtaaveahtv
      241 qadsaqvvvv rggtkglwvr gepqilteav gnlianaiay spqgskvgvg ikldvdvvei
      301 avtdrgigip esdqhrvfer fyradqarsr rtggtglgls ivkhavqrhg gevrlwsrpd
      361 rgstftirlp lsetpdldiv rpkqrrkgrk amaaasapvk eett
//
LOCUS       WP_285136097             373 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285136097
VERSION     WP_285136097.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..373
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=39075
     Region          1..358
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mpevlvvgag pvglalaadl dargvdvevv errvdvgggt raigihspal tlleacgatd
       61 giraeavrid rgqaradgrv laeirfeslr arhpyvaalp qhdtmrvlta laptvrngta
      121 vhalrhdgag vraevsgpdg rreiraavvv vasgwagrel vyrhgavrth hypdryvmad
      181 vvasggpvar vhlerggvve sfplpggrrr lvawagsdev gdadaflrea vaartgieid
      241 vagastfgvr ravapalrrg rivvvgdagh evspiggqgm nlglldaltl spllapwvrr
      301 gddaglarwe rdrlssarha arlaflntll graagptaha vrtgalrtll rgpggaaftr
      361 ayamrfdraa rgt
//
LOCUS       WP_285136110             407 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285136110
VERSION     WP_285136110.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..407
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43438
     Region          7..399
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 maqeiirple gllvldfsqf lagpvaalrl adlgarviki erpgvgdigr tlafagrald
       61 gdtvsfhamn rnkesvtadl knpddlayvr elvaradvvi qnfrpgvmer igldyasvke
      121 lnpsivyasa sgygdegpwr drpgqdllaq siaglpwlsg srhdgpvplg lsiadhllsc
      181 hiaqgvtall vrrfrtgkgg lvqsslleav ldlqfellst klnddtiqvq rhgehsahaf
      241 laapygtypt sdghlalamn pipelgrlle lpalealtdp qdawdrqeei egilaarfat
      301 gttahwlgil daadvwcapv ltldellase gfaaidmtqe varrgttvat trsplridgq
      361 vlrsekaapl lgedddrira efpprsagap leavaaagvd gdvgvra
//
LOCUS       WP_285136203             353 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285136203
VERSION     WP_285136203.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..353
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=35201
     Region          8..324
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mgrledllgi dtpvvlgpfg glssvaltaa vsgggglgsf glygyaperv hdtvaalrra
       61 ttgriavnlw wprgdevtpa dvdvapfvaa aaplfaaagv tpplppasfm ptlaaqldav
      121 fdarpdvlsv vfgvpdadtl araaslgirv vgtatsvaea valeaagvda vvatgseagg
      181 hrvsflrdpa hslvgtfalv pqvvdavgip viaaggiadr rgvaaafalg aegvqvgtaf
      241 lrtrqsaatd ghraaitasa dtdtvltram sgrlargipn ramreleasg miapfpaqnw
      301 ltgvfraaat asgdadlvsl wagqaaalar lddaaevltd lragvpaghs gpa
//
LOCUS       WP_285136230             280 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Microbacterium
            sp. lyk4-40-TSB-66].
ACCESSION   WP_285136230
VERSION     WP_285136230.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..280
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30763
     Region          2..278
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrialtgssg klgtvvarel raaghdvigl dihgergpgf vqveltdygq vidalagvnd
       61 qhtgfdavvh lgaipapgir sdiatfhnnm tgtfnvfwaa vrlgirkivy assetvlglp
      121 fdvpppyipv deeyaprpes vyslvktlee rlatelvrwh pdlsitalrf snvmvpadya
      181 efpfdadart rkwnlwgyid ardgaqsiqr alenapngfd tfiiaaadtv mtrpnaelid
      241 evfpgvetrg elgenttlls idkarrllgy dpqhswrdhr
//
LOCUS       WP_285136232             468 aa            linear   BCT 25-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285136232
VERSION     WP_285136232.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..468
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49515
     Region          28..460
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 msdaadsydi avigagpagt aaalraaelg asvvvleagr vggtcvntgc vptrvlakaa
       61 rlmretrsad dygivvdepr vdwsavvsrv hervdavrsi kreaerfada gidlihegra
      121 rfvddhtlel dsgrrvraes ilvcvgghsr rlpipgaela tvpedvlslt elprrvavig
      181 agntgaqlvt vfrsfgaevt lldvaprvlm asdarisnai aeaflsrgvd vhtgidtver
      241 ldehdgairl twreseeaht vdvdvvlmat gwpadvedlg ldragvaver saipvdryfr
      301 tivphilavg dangrdmlvq aaqfegeaaa enavlganrr tphhllpagg ftdpdyagvg
      361 lteeqardrd pscvvatvrf adldravidd resgfltlia drrkelllga havgenavev
      421 iqsvttamaa gidvatlagv rfayptysav ignaarallr adspalle
//
LOCUS       WP_285136259             580 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285136259
VERSION     WP_285136259.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..580
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=62342
     Region          62..187
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mgehggvdtl dfspwsfwqs asddakrsqr erlhalaerg drifahdsfv adtaavdndv
       61 lhlgersyva agayltgelv agsdcsinpy tvirgrvrlg agvrigahts llgfnhsmtp
      121 gtpvfqqplt skgivveddv wigshvvvld gvrvgahsvl aagavvtkdv psgaivggnp
      181 akllrwrvap adgatscprd lvdrlrdfae qsrleaeall arawdaeaga yvdrpgaeps
      241 lrahcdaiev aglllpcapp pltahehrar lasaqrpdgr ipstafgtpf savfaaaesd
      301 gripstgfwv ppgaafadad aayhvlsvgy atdllrgqlp hpiteatrms padivdfces
      361 lpwridpwha ghrvdalgta lhwalrsgrp vlpgaveslf gwlgtradpd tgmwgdpasg
      421 gdllllvngs yrttrgtfaq fgiplphpra tidtvlehaa ddayftaety dacnvldvih
      481 plwltrgalh rfdeaqdlar rvlehalsms spsrgfafrl rdtadegmcs lqgtemwlai
      541 iwyladilge sshlgyrprg vhrpepalri trsglhimgw
//
LOCUS       WP_285136275             201 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285136275
VERSION     WP_285136275.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18527488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..201
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21624
     Region          6..87
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          92..181
                     /region_name="COG3837"
                     /note="Uncharacterized conserved protein, cupin
                     superfamily [Function unknown]"
                     /db_xref="CDD:443048"
ORIGIN      
        1 mdahtttlaa aigsrirrer qsrewtlnrl setaeisrrq lvnveqgevn pslgtllals
       61 ealgiplaal vepptarlvk ihrsgegtel wtgphggrav lligtqppdv vnlwdwrlnp
      121 gerheskahp rgcrevlhvv agtitlevae dryslgpdds itfpgdvgha yangsaepch
      181 fsltvyqpql gantgesnah a
//
LOCUS       WP_285136324             131 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285136324
VERSION     WP_285136324.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 131)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 131)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 131)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..131
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14120
     Region          1..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 madifdviad gtrrdilqll ldratggerg tsvsqivasl gvsqptvskh lkvlreaelv
       61 svremgqhry yslavaplde vddwlvpffs ideenepalp esavhaaevv graaasvkhs
      121 fstalrklpg r
//
LOCUS       WP_285136331            1221 aa            linear   BCT 25-DEC-2024
DEFINITION  TM0106 family RecB-like putative nuclease [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285136331
VERSION     WP_285136331.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03491.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1221
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..1221
                     /product="TM0106 family RecB-like putative nuclease"
                     /calculated_mol_wt=131373
     Region          7..544
                     /region_name="COG2251"
                     /note="Predicted nuclease, RecB family [General function
                     prediction only]"
                     /db_xref="CDD:441852"
     Region          385..1204
                     /region_name="DNA2"
                     /note="Superfamily I DNA and/or RNA helicase [Replication,
                     recombination and repair]; COG1112"
                     /db_xref="CDD:440729"
ORIGIN      
        1 mryierdari vwsasdlkaa aecefawlra idaklgrida vddpvdatle raarlgtahe
       61 lrvldeyrvr lgpavheipa arssdadalg esvrltdaal adpaaevvyq aafatdefvg
      121 fadflvrepe pepgthgtra dgtrpwivqd tklarrarvt almqlaayvd qldrlgvprs
      181 devqlllgdg ststhrvddl lpvfrlrrer lraliadrav glgaagpvig wgdargdlgv
      241 iacgrcatce ievvahrdll lvagmrpvqr drlraggilt idalavavda paamsadtfa
      301 slrtqarlql dspagvpseg dpahaiptfe vvapkslgvl prpdhgdlff dfegdplyte
      361 gvgehwgidy lfgwvdtret ygalwahtfd eeraalerfl dmvalrrsqy pdmhiyhyap
      421 yepthlltma arygvreadv drllrdgvfv dlypvvrral rvgsrsysik kleplymgde
      481 vrtsdvqrgd dsivkyvear alaadgdtaa aqtvlddlad ynrydcvstr rlrdwlvdra
      541 resgavpars aepdeqayep spratalqrw asdaaepgld tpdaqalrla aaaidyypre
      601 ektywathfl rlrepvsvwe etrdvvvvdg grsrvvtdwh iaesgrgser rlvelrgela
      661 pgtrlsvdad pfavydlpap fpietrprwi hgarrvsvre vlddgaiiee iaadgvtwnd
      721 lplaltpaap pragnqqkai dawadavlta aptiphgpaa dilrripprt lsgalapvta
      781 laaarvadtp vsdaaadtgv adtgvgdpvg gepsgddevt aiarsvadld hsylavqgpp
      841 gtgktyvgsh viarlvaerg yrigvvaqsh atiehmldqv iaagvpasrv gkapkdpgie
      901 haftvlpkng vaaftaenaa sgfvvggtaw dfshearipr gsldllvide agqfslasti
      961 avslaaqrll llgdpqqlpq vsqgthpepv dtsalgwiid gaevvppelg yflartrrmh
     1021 pavagpvsql syegrlaahp stalrrlegi epgvhvvpvr htgnstcsve eaaevarlva
     1081 qlvgrewtga eggagdratv qqpralraed iivitpynaq qvsveealaa rgfadvpvgt
     1141 vdrfqgkeav vailtlaass greaprglef lllrnrinva isramqaayv vystallddl
     1201 prtpegvarl safarlvagg d
//
LOCUS       WP_285136396             198 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285136396
VERSION     WP_285136396.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..198
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21607
     Region          6..58
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(15..16,27,31,33..34)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 manvdrlrra ngltvgells ragmtksyyq sragfslpyn tndiealaaa lgvtpeevas
       61 petmtriemr vpadplvarv rrlidsqast edellrhlee idplladnar tllaaashtv
      121 vldeevlrli thwadvptey ltdhtdetva drteaelelr eamraagass iqfralgqms
      181 pdalraiaqs lrsgpstr
//
LOCUS       WP_285136409             470 aa            linear   BCT 25-DEC-2024
DEFINITION  FGGY-family carbohydrate kinase [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285136409
VERSION     WP_285136409.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..470
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48639
     Region          4..437
                     /region_name="ASKHA_NBD_FGGY_FK"
                     /note="nucleotide-binding domain (NBD) of L-fuculokinase
                     (FK) and similar proteins; cd07773"
                     /db_xref="CDD:466793"
ORIGIN      
        1 mtdyvvgidm gststkllva tpegrqvlvv srrspwtnld hgraemtahe aiavvrdlaa
       61 eadvrldady rivalavsgm aeagvlldae gralaplmaw fdprgaaqim atpaefraef
      121 lgrtglpvgp lasiakllhl rdsgiplagt tflnvpeyvv halggprvae yslasrtgll
      181 dqddstpwga aldvlgvdes ilgarvsage avgvlsdeam pagfrgaalt vaghdhlvsa
      241 vavgathtgq lydsmgtaea lvrvlddtlp faarerlala gincvrhvip gkyvllagtk
      301 sgllmrrvlq llgitdatgr aqiddaamal pvdgaladgg levsgarndd gvlkivaqsd
      361 glspaelfaa slrhgndmla ecmavmdrev apptstvltg gwstmasvvr srsallpdvt
      421 vsthdegtay gaalfaafav sadsfevvae sfltsslvad egsllshers
//
LOCUS       WP_285136531             334 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Microbacterium
            sp. lyk4-40-TSB-66].
ACCESSION   WP_285136531
VERSION     WP_285136531.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..334
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37224
     Region          4..316
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 marpvtlftg qwadlpfeev arlagewgyd gleiacwgdh idvarwddea yvqsrldvle
       61 knglkvwtis nhlvgqavcd epiderhhdi vpsrvwgdgd aegvrrraae elkdtarfaa
      121 klgvktvtgf tgssiwkyva mfppasdami ergyadfaar whpildvfee vgvrfalevh
      181 pseiaydywt akktldaigh rpsfgfnfdp shfvwqqlds vafvldfadh ifhvhckest
      241 tnldgrngvl gshlswdnpg rgwtfvstgh gdvpweplfr alnaigydgp tsvewedagm
      301 drliggpeal afvrtlggit pphqlfdaaf srkd
//
LOCUS       WP_285136564             486 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285136564
VERSION     WP_285136564.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..486
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51954
     Region          296..480
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          423..475
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mpgtrtsnev patlsdtaia vashlspghg apsarhitll aesepvtpps lwtdtsaltl
       61 aaqfaararh dslslgigli tryfdgvrll rpaslssrvr sqlyasvgey ccalgwtpva
      121 arfaaeallf adtgalryra isisafaqam ngefraaadq aaraheifda egwpateiar
      181 ahckaeivva ssradaaklr emsarmtaaq pddpfwifta rfadvlarly srdfsgalag
      241 ssellygslr hssprpdrlf lvsvrsdmlv argeydeafa flapfespeg hgicfasqra
      301 tslihlgrer qaiadtdaca adesahslrt lvpllarrav afqrlgsvrr aeqsmesvil
      361 lleragasgl pflmlpdaev rglidivsah rpelratage irrllgrvta ptgvtpppls
      421 tggltptert laamlvtplt ladiarergv slntvksqlr siyvkvgaag raeavelltr
      481 ptsdhr
//
LOCUS       WP_285136604             380 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285136604
VERSION     WP_285136604.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..380
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40831
     Region          15..373
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mtvpvappma aapgpldrvr nlpsltglrw atallifghh lmavnyfggn agvawgvvfe
       61 agktgvtlff ilsgfvlawg yrpqqtarsf wwhrvariyp lhvvgvvlal iaaatlvpei
      121 rtdgaaplva nvllvngwvp dwwqagnpas wslvceaffy lgfpflirpl vrasnriltv
      181 vavaslvlva lapqiaafap gvlssastpl lrlpefvigm tlavmmkrge wmplrlgiav
      241 plavagyals eapmvpgtdi hpglaatvgf yallvaslan adargrstfl arplwqelgr
      301 vsfafylvhl lviasvssgw pdghpelpwr qavplalaaf gialaiawam hklveipaqr
      361 wllrydrsrk astreavaah
//
LOCUS       WP_285136614             561 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285136614
VERSION     WP_285136614.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..561
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=59934
     Region          1..537
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msthpllsir dlavryrtrr geveavrgvs fdveagsvta lvgesgsgks tvaqaaigll
       61 aanghvsggg irlsertdgp telvglserr wrrlrgrcia fipqdpgnsl npvatigwsv
      121 gealrihgwt drakirarvl dllervgidd pearakqyph elsggmrqrv liaaalalrp
      181 eliiadepts aldvtvqrtv ldlldeirte tgtgilfith dlavaadrsd avvvmrrgvv
      241 eeagptaevl aapssaytrt lladapslar vveraapdat tlaapplvtv agltqefrrp
      301 grsplvavdd vsftvargtt halvgesgsg ktttgrsiag lhrptaglir vagtevtgla
      361 ggrarrafhr stqlvyqnpy asldprqsia eilteplrnf gigsraerag raahhlelva
      421 ldpdiaarrp relsggqrqr vaiaralive pelvvldeav saldvtvqaq ilrllarlqa
      481 dlgltyvfis hdlavvrqia dtvsvlqrgr qvehgpaarv fddpqhdytr qllaaipgas
      541 lrghlsttap etrphpeevl r
//
LOCUS       WP_285136650             423 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin-containing monooxygenase [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285136650
VERSION     WP_285136650.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..423
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44719
     Region          1..402
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mvedvdavvv gagqaglats helsarnveh vvleagtpgs swlrwwdsft lvgpnrtisl
       61 pgaaydgddp dgfmsaseis dhlqryagrl kvdvrahtpv rrvtpqgglf lvdteagtlr
      121 artvvlaaga yqrplrpaal dglspdvdvv dvvsyhnper lpegkvlvvg sgqsacqiae
      181 elalagrdvv macgrapwfy rrvgdrdlfd wliaagfyeq rpedlpapaa rrganvqatg
      241 argghdlhfr tlaalgvrlv ghlvgasgst vylasdlvat iaasdagfav vasavarasa
      301 vegrpaprie ppsalatdev teldlrgfga vvvacgfrst yadwvdvpgl ldehgfplhd
      361 dgeirsapgl hvvgshflrr rrssllfgvg ddatatadri aasatlrgrv rkrdsasarr
      421 rhs
//
LOCUS       WP_285136740             401 aa            linear   BCT 25-DEC-2024
DEFINITION  lactonase family protein [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285136740
VERSION     WP_285136740.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..401
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=41394
     Region          1..400
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 mrfwvgayap dtgsaegigi lqagasdapd aggplgmvgt avaasgspsw vaahptasdi
       61 iyaavefdgt vqayrrvget rltplgrpvd agaavchvav spdasflvas cwgdgrvvri
      121 dldaegrpsr piiadeaadp hgsgtssegt vstgarvsga vvpdlaaaar alraaageey
      181 shlipaydda petdaeseea aagdrvsrah qaiflpgglv attdmgfdlv rfwrstpsgl
      241 rlvqevalpq gsgprhgiwh psghlyvvte lscevfvlaa dragrwqvrs gepllgtldt
      301 dtaaelcasr dgstlyagvr gsdtvgvlsv rgageelqlt alaetgthwp rhhvvvadtl
      361 lvagqlahei vslpldartg vpgrvrhrtp spsptrllpm r
//
LOCUS       WP_285136706             120 aa            linear   BCT 25-DEC-2024
DEFINITION  histone-like nucleoid-structuring protein Lsr2 [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285136706
VERSION     WP_285136706.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Gordon,B.R., Li,Y., Wang,L., Sintsova,A., van Bakel,H., Tian,S.,
            Navarre,W.W., Xia,B. and Liu,J.
  TITLE     Lsr2 is a nucleoid-associated protein that targets AT-rich
            sequences and virulence genes in Mycobacterium tuberculosis
  JOURNAL   Proc Natl Acad Sci U S A 107 (11), 5154-5159 (2010)
   PUBMED   20133735
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18741]
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Gordon,B.R., Imperial,R., Wang,L., Navarre,W.W. and Liu,J.
  TITLE     Lsr2 of Mycobacterium represents a novel class of H-NS-like
            proteins
  JOURNAL   J Bacteriol 190 (21), 7052-7059 (2008)
   PUBMED   18776007
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Oshima,T., Ishikawa,S., Kurokawa,K., Aiba,H. and Ogasawara,N.
  TITLE     Escherichia coli histone-like protein H-NS preferentially binds to
            horizontally acquired DNA in association with RNA polymerase
  JOURNAL   DNA Res 13 (4), 141-153 (2006)
   PUBMED   17046956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10570331
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..120
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13371
     Region          1..105
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 maleqifrrl ddldgseldl dstpvsfale gvqysidltr gnteklreal apfiaaarte
       61 gfehahhltr sqrtmkrrai rewarannle vsdrgrisda vldayasqgt nsrqqhygaa
//
LOCUS       WP_285136753             327 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285136753
VERSION     WP_285136753.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..327
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33662
     Region          1..272
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
ORIGIN      
        1 mdgfripvgs wvdagvdwvr dnlsglldvv avvvrflvgg lsdvllaapi ivvivvaaal
       61 afllrswkla vgtvigfali lamgqwvtam qtlalvlvat ivavaisvpl giwsarnptv
      121 ravlkpildf mqtmpafvyl ipaitffsig vvpgvvstvi falppgvrlt elgirgvdse
      181 tveaghafga tpgqilrgiq lplamptima gvnqvimlal smavvagivg adglgkevve
      241 sistvnlpkg veaglsvvvl avyldrltaa lgdragssgs llgvwgrrra araatattas
      301 apqtpdvtsp aereqtptdr tpvpagr
//
LOCUS       WP_285136789             142 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Microbacterium
            sp. lyk4-40-TSB-66].
ACCESSION   WP_285136789
VERSION     WP_285136789.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..142
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15225
     Region          22..117
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mattarivsg pcrawpeesa firevldrig dkwttlvist latgplrysd lqasipgisq
       61 rmltvtlkal erdglltrta faevpprvvy eltdlgrslq davlsmarwa atnhqavaas
      121 rlahertgvg rvkshgstaa dg
//
LOCUS       WP_285136790             226 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285136790
VERSION     WP_285136790.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 226)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..226
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=23092
     Region          1..220
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mptiaiigag tglglaiarv fgakgfdval isrtsaklda lvdqlaaegi taagfpadvl
       61 drpglrsala avkerfgtid vleyspadas agplapvdir eatpenvqpq ieyylygama
      121 atdevlpdll eagagtllft sgagsmypva qygnvtagaa alrnwalnla haiagtgvhv
      181 ayvaigvlia deapapgydv lpaadiapmy wdahetraah eivvrk
//
LOCUS       WP_285136974             241 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285136974
VERSION     WP_285136974.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 241)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..241
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27158
     Region          52..228
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mtrtpapetr dadvrvavst vifsvrrdeh depvlslplv rrtrdpfdgr walpggwlda
       61 aegldvaasr tlaettgltp syleqlyafg avdrsptrvv sivywallrs devdaqvaah
      121 aregdapenv ewfdatdlpa lafdhddive ytlwrlrnkv gysriahgll pdeftladlr
      181 evnetilgkr ldpanfrrqv dtsdtlipte rfrtgshrpa rlyrynrdve ladrgplptr
      241 h
//
LOCUS       WP_285137167             157 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285137167
VERSION     WP_285137167.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..157
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=15897
     Region          <28..146
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 misaslrpla vyaalllalp dplaglgwvw pvervqvvra yeapahaygl ghrgidvasg
       61 evvrspadgh vafagevagr pvvtidhggg lvttlepvvs dvavgdavar aapvgrlaag
      121 ghtapgtlhf gvrldgeyin plrllggvpr avllpcc
//
LOCUS       WP_285137288             318 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285137288
VERSION     WP_285137288.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..318
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=33301
     Region          201..314
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mtadgrttsp prlsaatfar ayfalqavag aawwvavftv plvreatlgd ldpivmaald
       61 vplfvvasal aavlprraag wagaaatawt lavtsvlgvy atvttlagag vilmiaasva
      121 svgawlllvl grvptewlli epfafrparp rrtpvahvia ttgqivvfwg lflavfpvii
      181 raledrwrla lpmpagvava gaviivaasa lglwsaasit vkgdgtplps ampnrlvvag
      241 pyrlirnpma vagiaqgvgv glvlsswivv ayalagslvw nyairpheea dlatafgdey
      301 rayardvrcw vprlrpvr
//
LOCUS       WP_285137329             392 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285137329
VERSION     WP_285137329.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..392
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42357
     Region          78..370
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mrrisgdlat atiqrleetl pwyaemppar rsavglvaqa gitsflqwfe epastpaiaa
       61 difaaaprel lrsvsltqtl qlvrvtvevm eervagrsek vreamlsysr evafaaadvy
      121 araaearglw darlealvvd siltgeadde lpsriaalgw hghgevsvlv gttppqldvd
      181 qvrrtarklg vdvligvqgl rlvlvlgrad lparsgaevt elpftdiakr lepsfgtghl
      241 vlgpavpalv dagqsaraal agfavarawr haprpveadd llperalagd avakqtlvdr
      301 vyrplhahsa dlvatlwsyl dngrsleata relyvhpntv ryrlkrvsev igwdatgpre
      361 alilqtalil gsigtdatrr rgtgkrrpsq pr
//
LOCUS       WP_285137348             409 aa            linear   BCT 25-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285137348
VERSION     WP_285137348.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..409
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43252
     Region          6..409
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mttplapgsg slagvvvldl srvlagpyaa qtladlgatv ikienprdpd vsrgfppylt
       61 hgdeefsayy aqynrgklgv gldlaapggt etlidlvrra dilvenfrpg tmdklgvgyd
      121 vlhaanprlv yvavsgygqt gtrsrrpafd ntaqaaggmw smngypgqpp vrvgvtigdl
      181 satlfavvgt laalrhaert gegqlvdvaq vdsilaltet avvdytvrgv easpagnaha
      241 wvrpyelfdc adgqvffgay tdklwrasca lfgspeaadd peidtmrkrm dadvyarrvk
      301 plvagwlagr tkaeleelag dvipltaikt igevvddpgt aeremivead ygelgtlrmf
      361 gqpiklsatp atpgrvanrf aehsdavltg lagydraria elrasgals
//
LOCUS       WP_285137359             494 aa            linear   BCT 25-DEC-2024
DEFINITION  PucR family transcriptional regulator [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285137359
VERSION     WP_285137359.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..494
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=52031
     Region          181..490
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 maqlttrdll aqterlgvah aagpeegavi arvevttlad lptlpagala vvagdeppap
       61 ylvdvalrqa sarglaglvm ptgfsvteta avlaarggvp vlvslaarap dlavaidrvi
      121 sggaaesmtr aafavekatq aaaagegdav paildaagta lgvrvslred lttswtdada
      181 vfagevpigr lvaetsdpaa tvalpvvasl vsramqrhlq drfapnqsra dlivelmlae
      241 agrvdgfvap aarlglplql shavawmrpq hrtdpglrap rfveaalelf tlqliedrpe
      301 lwhiaflqdd vlvvssedhg agdhqrrlrd visrvqaqar rlvgddwtyt vglgtpqtga
      361 aglrqsaaea rvaadsaiag grldaieltd vtglrrllld fyaspvsrnl lddilhpldv
      421 lgseksitav rtllsylgnr nslaqagrel nlhpnavgyr irrarelldv dlddpdtrfa
      481 velacrvrll gtgr
//
LOCUS       WP_285137384             456 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285137384
VERSION     WP_285137384.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..456
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=51341
     Region          3..453
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mpspslvwfr ddlrltdnpa lraaldrdep ivalyvldee sdgvrligga arwwlhgsla
       61 slaerleerg stlllrrgka aevvpavade vgagavfwnr ryggverdid aglkeklrgd
      121 gitvasfaan llyepwtvrt qtdkpygvys pfaravqkhp aprppmpear kvpgfdghvd
      181 gddlgawgll pttpdwaggl retwepgepa akarlkefld edlgdyskyr defaggatsn
      241 lsprlrwgel spyqvwhdti ehrgsgehak saggflselv wrefawhvty hspdiatvnw
      301 rrnfdafpwp kvnrahletw qqgktgvavv dagmrqlwht gvmhnrvrmv tasfliknll
      361 idwrhgeqwf wdclvdadaa snpfnwqwva gsgadaapyf rvfnpetqrk kfdshdryvr
      421 ewapeylgen ppepmvdlge trkraldaya qvrhgg
//
LOCUS       WP_285137515             827 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285137515
VERSION     WP_285137515.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 827)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 827)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..827
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..827
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=92459
     Region          13..825
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mstsspaerf arasarsthp htadfaemqr felddfqiag chaledgrsv lvaaptgagk
       61 tivgefaihl amlepgdkaf yttpikalsn qkfhelqevy gddevglltg dtninasari
      121 vvmttevlrn mlyadspalr glrfvvmdev hyladrfrga vweeviihlp psvklvslsa
      181 tvsnaeefgd wldtvrgdte vivsetrpvp leqhvlvrgd llplfddrag vataqvnqel
      241 lrirggnagg fennrraqef rsarhaggpr hahqrrgghk pvrasqgpri eridrpevve
      301 llqrshllpa iffifsragc daavqqlrra nvrltsaeer veirqivdel tftlkdedla
      361 vlhfwewrdn lergmaahha gllpafkevv eelfrrklvk vvfatetlal ginmpartvv
      421 leklekfnge arvaitsgey tqltgragrr gidveghavv qftegldpqs vaalasrrty
      481 plnssfrpty nmavnlidqf grararevle ssfaqfqadr svvglarqvk eaeeslagye
      541 qamtcdrgdf reystirrel sdlekinrrd ataprrlrde rqqqiqslrk rmqrhpcqsc
      601 pdreaharwa erywklkrst dktrqqidqr tgtvarvfdr vvevlaaley vrveedgatv
      661 ltpagrtmrr iygerdllva eslrqrlweg ldapslaala cclvyeprrd eagpgerglp
      721 rgafraalda tqtlwqeldd lerdhrlpgs dspasglspa mhawakglpl dsvltladma
      781 agdfvrwakq tidlldqisl vadpklakta rtaldsvrrg ivaytsa
//
LOCUS       WP_285137525             348 aa            linear   BCT 25-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285137525
VERSION     WP_285137525.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..348
                     /product="isopenicillin N synthase family dioxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37370
     Region          1..332
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 masfrvptid isawvgpgsp daraavvaav dhacrtvgfm qvvghgihpa vihdltgald
       61 rffalpleak kryvrpssen rgysppkses lsyslgvdpv trmndffeaf nvgtswreyp
      121 gttatasdya entwpddape fesavsayyd earrvaqtlt rvfaaalrvp ddffdaltgh
      181 sidvlrmnny alppgsielg aeltgmgeht dfglvtvlwa drvaglqvlg qdgswndvsp
      241 aegallvnlg dvaarltndk wlstlhrvkp pvvdgtierr rsaaffhdgd adaviaplph
      301 ftsdeapaly dpvtvrehit aklagsragr knvgaireaa rvaaasra
//
LOCUS       WP_285137552             322 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-methyltransferase [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285137552
VERSION     WP_285137552.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..322
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=35780
     Region          17..318
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 msaatagdal epgaveihha dnlavtpayp dgsfalvyld ppfntgrtrs kavesatwtp
       61 pveeprdaaa peaasepdaa asedpnmltf peeeappppv vqrgfhgrey arlrgdlrty
      121 ddrfddywgf leprlieawr lladdgtlyl hldyrevhya kvmcdalfgr dkflneliwa
      181 ydygaktkrr wptkhetilv yvknpttyff dsdavdrepy mapslvtaek aargklptdv
      241 wwhtivpttg rektgyptqk pegvlrrmvq assrpgdrvl dmfagsgtlg avaaplgrds
      301 vliddnadav avmhkrlepf ar
//
LOCUS       WP_285137654             657 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285137654
VERSION     WP_285137654.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 657)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 657)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 657)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..657
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=70623
     Region          44..344
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mtstidrpaa asaaqsidap prtrsrrlld aawllpplli gllvnalnlg gspqriddeg
       61 tytaqawsig nlgelthyty wydhpplgwi qiaawvgltd gwgrydvavi aareamlvat
      121 aiaavllwyl vrrigfarlt asvsvaifll splavqfhrq vyldniataw llaalllams
      181 rraqligyig aaaalgvavl tketyllalp lvawlmwrga drttrrytls vatavfalmg
      241 lvyvafavvk gevmpatgrv slwdglafql asregsgslf dpnslfsrtv glwwqldavl
      301 ivtalvvavg glivrrlrpw avvllaltaf mfrggylpvp yvimllpfaa ivvagmgqia
      361 leqlrsrtal rriggatlas glvvalvaag plwatqlrgf lladldrplr daeswmtqna
      421 sgdarmlvdd amwvdlvdag farenvvwyy kadtdtdvqe lapdgwrdyd yvittdsmrt
      481 fptefptvrq aiensvvvas fgegaqqvdv rlvdrdqaal aqaaddglya arsiagqqll
      541 rnpdvgvpga aqdlltsgvv dgrilltlgq lsstgridla digqlegdps gvhrrlviss
      601 fagqdargta pgsdavvrfy eslagqlrpv sversdagvv vtfspdeptg llarppa
//
LOCUS       WP_285137697             487 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285137697
VERSION     WP_285137697.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..487
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53547
     Region          26..379
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mvaptaskls sawdtarhaq sgwplfltsl kidglrgwag qavefrypvv avagmngagk
       61 stvlkaaaaa yqaqtnsptm tyyaddffps tpweqvsgvv layavrqgde tssytvrkpt
      121 srwrgaperk rrpvyfldis riqpantlig ygrtaqevis qgtekpltda evaqlnrtlg
      181 rtydyaride nqgkqvgvlt qggvrysnfh qgagedsvld liallnevpn hslviideve
      241 aslhpqaqrg lmteilrlpf dkklqvilst hsqfileqlp dvarifisvd rdserqvlyg
      301 vtadfalnlm dderhyeldi yceddqavyl ieriialgap evlkrarits vgpastvval
      361 stvatkaklp raslcivdge qpagetylrl pggerpervv fqslddshwq avaerlgqpv
      421 gelldakdaa lqienhhawa geiarriggt mrpskvweav vdvwtrdilg eqaakewsep
      481 vlaslan
//
LOCUS       WP_285137702             370 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285137702
VERSION     WP_285137702.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..370
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41358
     Region          90..366
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msaergerid pktrrqlpeg irfrkdrgky qvrvwaigln geqrersfyv etlaeakklr
       61 aetltrrypd ggmtlaqwhs rhwpviagsv rastarayer gwrlrvkpwl ghmkleklta
      121 gvieeaiasw egststrida lavlsrlldg avrahlvpln qarlarrprs esttslrsra
      181 ltaaevpill aaiadahyrr yiaalvytgm raneatalri edvdvaqrti hvrrafsiga
      241 dgrgveltpk shkerdvpip tplvapltda magkhrgdlv ftgprggrin psnlrraidw
      301 ktlratlhre dlrihdlrht latmlfdaga sandvqavlg hssmqmtery srarsdvarr
      361 aataidslfe
//
LOCUS       WP_285137916             661 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285137916
VERSION     WP_285137916.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 661)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 661)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 661)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..661
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..661
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66616
     Region          16..>245
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 msavlsspsi pltpattvar rprgwtlglv aigsvalvlt gwevwagtps eyyasialsm
       61 srswsdflfg avdpagtvtl dkipgsfwip alfvrvfgys awsvilpnaf aavgaalvta
      121 vaarrlagvr agliagavva vtpilvavar snqpeaffvl gisltayaav ravqerragw
      181 vvaagafigl sfqfymleaw avwpalaaay lctrqswarr lghlavagav slaaslwwva
      241 vvslvpagsr pyigstltnd pwemvfgyng lgrfsatads aayesftppf sgdpgvlrlf
      301 niqlagqvaw llpaavlalv vlwvlrfprp lavlltvwfa tfaamfsavs gmhqfytaal
      361 avplglvvat alavarragk twpqvaivgv agatalgigl ayggysvpva vaqaavagva
      421 ialllsrhra rpvttvallv gllltpavws avtvahpnsi npvaggvstm sggfgagmpg
      481 gggrgaagpg ampggggapg gssaqggfgq apgssggrgg tdggggrpsg afgggspqgt
      541 dqggvdttll twltqnaggs tylaatfgaq saaqlivasd ggsflpiggf ngtdavptld
      601 gfvslvqsgq vryvideqrr gsggtgggds sdtttsaqir ewvvqncavd dsapstvyac
      661 g
//
LOCUS       WP_285137941             237 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285137941
VERSION     WP_285137941.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..237
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25882
     Region          1..216
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mfywlmkyvv igpvikavfr pwmvgrrnip aegaailasn hlsfsdsifl plmidrrmaf
       61 laksdyftgk gikgwatrmf ftatgqlpid rsggkaseas lntglgvlgr gellgiypeg
      121 trspdgtlyr grtgiarmal earvpvvpvv mvdtgavmpi gqrlprvgrv givigepldf
      181 srfegmegdr yvlrsvtdei mvalqrlgeq ryedvyastv kdrlataqaa kapasrh
//
LOCUS       WP_285137954             357 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide)
            pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
            [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285137954
VERSION     WP_285137954.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Davies,G.J., Gloster,T.M. and Henrissat,B.
  TITLE     Recent structural insights into the expanding world of
            carbohydrate-active enzymes
  JOURNAL   Curr Opin Struct Biol 15 (6), 637-645 (2005)
   PUBMED   16263268
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   4  (residues 1 to 357)
  AUTHORS   van Heijenoort,J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit
  JOURNAL   Nat Prod Rep 18 (5), 503-519 (2001)
   PUBMED   11699883
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Ha,S., Gross,B. and Walker,S.
  TITLE     E. Coli MurG: a paradigm for a superfamily of glycosyltransferases
  JOURNAL   Curr Drug Targets Infect Disord 1 (2), 201-213 (2001)
   PUBMED   12455415
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..357
                     /product="UDP-N-acetylglucosamine--N-acetylmuramyl-
                     (pentapeptide) pyrophosphoryl-undecaprenol
                     N-acetylglucosamine transferase"
                     /EC_number="2.4.1.227"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0050511 -
                     undecaprenyldiphospho-muramoylpentapeptide
                     beta-N-acetylglucosaminyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051991 -
                     UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-
                     glutamyl-meso-2,
                     6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol
                     4-beta-N-acetylglucosaminlytransferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0030259 - lipid glycosylation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=37136
     Region          1..357
                     /region_name="MurG"
                     /note="UDP-N-acetylglucosamine:LPS N-acetylglucosamine
                     transferase [Cell wall/membrane/envelope biogenesis];
                     COG0707"
                     /db_xref="CDD:440471"
ORIGIN      
        1 mttyllaggg taghvnplla vadglrarda aadvlvlgtr eglearlvpl rgyelltvak
       61 vpfprrpdra aavfptrflr avahvrrlir argvdvvigf ggyaaapayi aarrervpfv
      121 vheanakpgl anvlgarraa avgvafagtp lrgarevgmp lrheivglda aacraeaaah
      181 fgldaarptl lvfggslgal rlntafggaw rdvldagwql lhvtgqgsdl pdpavdgyal
      241 vryvdrmdla faladfvvsr sgaatvsein algipavyvp yavgngeqsl naaasvraga
      301 ailiadadlt pervrseivp llrddsrrta mrdaaartgi rtgtenvial idealag
//
LOCUS       WP_285137997             167 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285137997
VERSION     WP_285137997.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..167
                     /product="metallophosphoesterase family protein"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18102
     Region          4..164
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mvtrlllvad thvpkraral pdavrrtasd vdlivhagdw vtgdlldels algtvcgvwg
       61 nndgedlrsr lpeiaradid gvrvavvhet gaatgrekrm dtafpdtdll vfghshipwd
      121 tvtpnglrll npgsptdrrr qpvctfmtlt laegdvrdvv lheisra
//
LOCUS       WP_285138021             565 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC1 kinase family protein [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285138021
VERSION     WP_285138021.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..565
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0004672 - protein kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=62336
     Region          9..485
                     /region_name="AarF"
                     /note="Predicted protein kinase regulating ubiquinone
                     biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport
                     and metabolism, Signal transduction mechanisms]; COG0661"
                     /db_xref="CDD:440425"
ORIGIN      
        1 mtddalmkar yrritrfaar ylvqawwyel flprfglgwi sargrtrrle riaqrfhvla
       61 vdlgglmikv gqfmssrldv lppsitkqle glqdevpavp faqmraraeh elgmpleraf
      121 asvderplaa aslgqahrav ltdaladetg lravvlkiqr pdidrivdvd lralrkvgvw
      181 lskvalvrdr vdmpslveef avtsleeidy lheaanserf aadfggedgv avpdvvwert
      241 trrvltledv saikindvda lraagidpse vaarfaavmf dqlfddgffh adphpgnvfv
      301 tplssstdag ppawrftfid fgmmgdvppg lrrglrrvli aaasrdgkgl vdgirdvgvl
      361 lpsadtiqle ramtqlfsrf ggmgfaelqe vdprefrafa iefgdvvral pfqlpenfll
      421 ivramsltsg mcssldpafn iwdavepyaq rlireesgnt aqalvrevga vaavtarlpr
      481 radnlisrle egslsvetpr ierrmrdler mvrrvvssvl ftglliggvl lqteqavfgt
      541 ilmvvslapl shallagvva rrnga
//
LOCUS       WP_285138061             234 aa            linear   BCT 25-DEC-2024
DEFINITION  DsbA family protein [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285138061
VERSION     WP_285138061.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 234)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..234
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=23973
     Region          66..214
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mmmaavrkst nwfaigvtaa vlvvvlivag vvwfannqat spgtlpessa vdtetgaiav
       61 gsgaktvdty idfmcpvcnq feqaygptld qlvasdeitl nihpisildr asqgteystr
      121 sasaaycvav ddpanvpafv kalyaqqpse ntaglddatl asiatsvgas daatscisdg
      181 tytrfvtamt qntpvqpgsg giatptiavd gtvlanqtdl tgdpqkdivd rldg
//
LOCUS       WP_285138093             234 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285138093
VERSION     WP_285138093.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..234
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25228
     Region          53..149
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 msrdagrrgg trlgvavrdl rwwvqdyaya lrgqwralvg regpealseg egtpivllpg
       61 iyetwrflep laralhergh pvyvvdelgd nrrpiaeqas rvavllltrg lddvvlvahs
      121 kggligkhvm afhpagsrvr amvavatpfg gsrysrlmpt pslrafasgd atmralaaaa
      181 danarivsiy gtfdphipeg selagarnvr ladgghfril adprviaevv rvae
//
LOCUS       WP_285138269              58 aa            linear   BCT 25-DEC-2024
DEFINITION  YegP family protein [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285138269
VERSION     WP_285138269.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..58
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..58
                     /product="YegP family protein"
                     /calculated_mol_wt=6044
     Region          3..58
                     /region_name="YegP"
                     /note="Uncharacterized conserved protein YegP, UPF0339
                     family [Function unknown]; COG3422"
                     /db_xref="CDD:442648"
ORIGIN      
        1 mtgkyelysd kagkfrfrlk agngqvvavs eayeskasar sgiasvkana dsetvdlt
//
LOCUS       WP_285138307             348 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285138307
VERSION     WP_285138307.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..348
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35000
     Region          42..344
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mttrspvvdv lpdaaslrrp asrrllwllv ltggvvvvsa asiafgtrdv slteiasaft
       61 ggggvgeaav itrvprtvlg llvgaalama gltmqavtrn pladpgilgv sagaslavvt
      121 giaffglsss sgymgfaivg aaaaavfvyt vgslgrggat plklalagaa ttaafgslss
      181 aillprvdll evfrfwqigg iggatwdrvq vvlpvlaiga lvcilcsrgm nslalgddva
      241 tglgehvgrt rlvasagavv lvgaatavag piafvglvvp hvcrmligtd hrwlvpfsal
      301 ggaillvgad vvgrlvarpt evevgiltal igapffiwiv rrqkvrel
//
LOCUS       WP_285138308             358 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285138308
VERSION     WP_285138308.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..358
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=36806
     Region          52..355
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 msaqtlsprg daatasvpdv aalirgrrdr arrrtlvavv lliavlvvyv vtlmvgntfy
       61 tpdqvvrvll gqtvpgasft igelrlpras lgllsglafg magvtfqtml rnplaspdii
      121 gissgasafa vvaiigfsls daavsafalv galatagaiy flsrrgaftg trlvligigv
      181 aamldsvttw vltraanwdl qtamqwltgs lnnaswerll plavtvavvl plmvantrgl
      241 avlrlgddsa aglgvrvert rlllivgavv mlavataasg piafvafmag piaarlvgpg
      301 gsllvpaglv gallvmlsdl lgqfafdnry pvgvitgvlg apyliyllir tnrsggsl
//
LOCUS       WP_285138380             208 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285138380
VERSION     WP_285138380.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12807001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..208
                     /product="helix-turn-helix domain-containing protein"
                     /calculated_mol_wt=22061
     Region          16..91
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          19..189
                     /region_name="PRK09943"
                     /note="HTH-type transcriptional regulator PuuR"
                     /db_xref="CDD:182158"
ORIGIN      
        1 mttmapaidd aptgeellga hlrglrkarg ltltqlaeaa tlshpflsql erglarpsma
       61 slerlaralg tsrveliaas esprtdqdaq psfvaadegv igpyaegtar llatgarrfe
      121 pleftgsnsa pgdhyvheed efltvlegsi visfgiyger tlhvgdsvyc rsgtphrwhs
      181 pdgatyrlli vkdlvhggga ddqsgvea
//
LOCUS       WP_285138323             843 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285138323
VERSION     WP_285138323.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 843)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 843)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 843)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 843)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20665275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..843
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=91006
     Region          2..144
                     /region_name="AAA_16"
                     /note="AAA ATPase domain; pfam13191"
                     /db_xref="CDD:433025"
     Site            29..36
                     /site_type="other"
                     /note="Walker A motif"
                     /db_xref="CDD:99707"
     Site            order(30..37,116,149)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:99707"
     Site            112..117
                     /site_type="other"
                     /note="Walker B motif"
                     /db_xref="CDD:99707"
     Site            163
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:99707"
     Region          <403..840
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          675..842
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          781..837
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mpfvgrarek riaedvigtt ggsgclfige vgigksalar eiagqhgavv vtaspnerlw
       61 pfsglsalaa glggerrnav navlargrdw pehllaeels rtlhlvhdep dvviiddldq
      121 mdgasitvls yvfgrlrgtg lsvvatagaa drrhdfagmr hsrlerlsfe esldlgrvvl
      181 gsgaslavly tvagsvggdp gilsrvrltp cealgddplp lplrlvddds ddrkrggrgv
      241 hdpriaavld llcvgpvfgh drlravaaal gvevdalida glvavhgela riadpalrlr
      301 rlaalsaddr srlhaqaaee hgekypatfl whrshaepda drerllvaav dlaragepsa
      361 avefaerala grvdeasrcr hlvdlgealv mqghdvrgrh ylrragaptd pdvrtraala
      421 wlrattaadq ivddtmlrva aqtddpraae rllcesarlh lwrgeterah elvvlsaerg
      481 iastettlla rlleelgddv lvpvtvdtgl pagaedgdap ieqeilalyt avlreqypav
      541 rrriltllgr rprpqpywrd qlrsllvtte vrggdpvaar eavaawrrew vpgrtselad
      601 vlvlagaaal dplgpgagdl vrhgrdlcrr egtptplpwf avieggsala egrfddavas
      661 leaareavpc edpsllrada dlvealwlsg hradarrilv rleaasvrtp rrwttlavar
      721 sravcrsdrd gaaafreaea iwrtddppie rlrlraarer clpttgrpvl qatprptdrg
      781 rsltpqerdv valvgqglrn rdiaaalfis lrtvelrltg iyrklgvtsr vhlvallhga
      841 slp
//
LOCUS       WP_285138389             386 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285138389
VERSION     WP_285138389.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..386
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=42687
     Region          15..349
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mthtletswr rfrdttrllp ldglravail lvftghveap gpwkavhggv gvtlffvisg
       61 fiittlllre sderpvdfga fyirrafril pmyllvlavy cvlilvlgtq edrraeflna
      121 lpgylmgfpe ivqltntaeh qapfsgawsi giedkfylvw pvvgflllrr rwtaliplll
      181 vsagiltvvg fgtpvarvlq pyvhiilgvl vavglhyrgs fgvlarlfgr wwltwallav
      241 slalvlypdi algtplyvpy gllwavtivs lftappgaat tvlssrpllf igtvsysfyl
      301 thafvlnale klppaipswa qyplglagsl vlawatyrlv espmnrwghr iaarrrarrt
      361 papsasdvrs papiapatrr dsrpdr
//
LOCUS       WP_285138504             121 aa            linear   BCT 25-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Microbacterium sp.
            lyk4-40-TSB-66].
ACCESSION   WP_285138504
VERSION     WP_285138504.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..121
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12002
     Region          19..103
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 mtplvfvgva vaggvgaalr flldtavrra tgerfpwgil avnisgafvl gilsmlpade
       61 awrwivgtgl lggyttfsav avttallaee grtaaatsya avsfagsvva aaaglalgsl
      121 f
//
LOCUS       WP_285138527             231 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Microbacterium sp. lyk4-40-TSB-66].
ACCESSION   WP_285138527
VERSION     WP_285138527.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. lyk4-40-TSB-66
  ORGANISM  Microbacterium sp. lyk4-40-TSB-66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 231)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 231)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 231)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Microbacterium sp. lyk4-40-TSB-66"
                     /db_xref="taxon:3040294"
     Protein         1..231
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=24838
     Region          5..228
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 msvavlvadd eapalhelat llaadprvsv vhtasggaea lrvlergeva vafldihmpg
       61 itgfdlarsl aglrvrpavv fvtadesgal rafdleavdy vlkpvraerl yralgralas
      121 gadpvdetip vtvgsttrlv rradirwvqa ngdysrlytp tcdhlvrvpl sdladrwada
      181 gfvrvhrsyl vhrdavtevr lagsaptvvl aeielpvsrr lipavrdall r
//
LOCUS       WP_285138730             390 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: murein hydrolase activator EnvC family protein
            [Sphingomonas].
ACCESSION   WP_285138730
VERSION     WP_285138730.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..390
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39674
     Region          <95..384
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mlrhgarrhg vlaltalall gatdiagdqr rlaearvgaa aaqaraqale sqagvernaa
       61 aiaqakeram aarvaaaeae vtaararvdl vaglleqqqa klaraqapla hllaamqsma
      121 arpplaavaq pgsvadlahv ravfatvapv iaqrsatvra elaatrrvra qvtvaarala
      181 atttkleser qalakleash rgraealgqv aidesnrala lgeaardivd rmaergeara
      241 tagdlialpg pvsrplgpgv igpviapgty rlpvrgrvag gfgeisdsgv rargitlstv
      301 pyapvaapad gevryagafr gyggivilnh gtgwtslvtg ldgiavkpgq hvaagavlgr
      361 agrggngvep rvtvelrrdg rpmdiaailg
//
LOCUS       WP_285138794             748 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase NtrY-like [Sphingomonas].
ACCESSION   WP_285138794
VERSION     WP_285138794.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 748)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 748)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 748)
  AUTHORS   Machado,H.B., Yates,M.G., Funayama,S., Rigo,L.U., Steffens,M.B.,
            Souza,E.M. and Pedrosa,F.O.
  TITLE     The ntrBC genes of Azospirillum brasilense are part of a
            nifR3-like-ntrB-ntrC operon and are negatively regulated
  JOURNAL   Can J Microbiol 41 (8), 674-684 (1995)
   PUBMED   7553451
REFERENCE   4  (residues 1 to 748)
  AUTHORS   Pawlowski,K., Klosse,U. and de Bruijn,F.J.
  TITLE     Characterization of a novel Azorhizobium caulinodans ORS571
            two-component regulatory system, NtrY/NtrX, involved in nitrogen
            fixation and metabolism
  JOURNAL   Mol Gen Genet 231 (1), 124-138 (1991)
   PUBMED   1661370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20231976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..748
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..748
                     /product="sensor histidine kinase NtrY-like"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=81491
     Region          21..313
                     /region_name="NtrY_N"
                     /note="NtrY N-terminal region; pfam19312"
                     /db_xref="CDD:437144"
     Region          298..724
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mlaplkpaep aegprsrfav tplmevavil gavavaigty vyiasrhdtq gliappvmag
       61 llalnlvpgv lllmllgrrv amrraasspv ggggrlhvrl valfsltasv pilltvvtas
      121 vlfqssaefw isdrarkafg damdiarqsq qqiikrwvdt gramsqdlgr nlpalrenrr
      181 dfhdylvqqt vvrdtvesvl fsydpkqgfk fydffnqpsd ttfrelvtpe miqqasklsr
      241 pevgineqrv wvvtplpegn glmlyigtpv naeflskqhf aaedvfddyr alqgrarslq
      301 lkfnlvlfai allivgiavw ialavadrlv rpvgelvdaa rriaggdlta rvpdpktrde
      361 vgtlanafnq mtgqlerqnt elvtanaqln nrralieavm agvsagvvav grdrqvrian
      421 nsadillgad qdglvgrklg evapeldell dqgrreatvq valhgdmrtl avriaqtgdg
      481 piltfdditq qlldqrraaw sdvarriahe iknpltpiql aaerlqrryg kvigvedptf
      541 grltetivrq vgdlrrmvde fssfarmskp vfreeaiadi caqamflhev ahpevrfqld
      601 qdeppptlvc drrqmsqalt nivknaveai esrpegmtgg kvvmtvgqqg gmvtitvtdn
      661 giglpperdr iiepymttra rgtglglaiv nkiieehagt igfsdnptgg tivsmmfdag
      721 alaaldhgga epelagegql taltrtrt
//
LOCUS       WP_285138846             571 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: PHA/PHB synthase family protein [Sphingomonas].
ACCESSION   WP_285138846
VERSION     WP_285138846.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   4  (residues 1 to 571)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..571
                     /product="PHA/PHB synthase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=63249
     Region          22..570
                     /region_name="PhaC"
                     /note="Poly-beta-hydroxybutyrate synthase [Lipid transport
                     and metabolism]; COG3243"
                     /db_xref="CDD:442475"
ORIGIN      
        1 mtaapatapt lptleelqhw twvmgraqqm mmeaaltppp egmpvvpgfn dpatmgrvrd
       61 fwsdsmalwq rfvdpaaeps qppkpdrrfk aeqwqsplfd wirqsyqmis dhmlrgvdal
      121 egvdpkqkeq irfaarafvd amsptnfpat npevldkive trgenllkgl qnmladigrg
      181 qlthsdstaf evgrnlaatp gkvvkrtply eliqytptte qvaavpilif ppwinrfyil
      241 dlapekslik wlvdqgfsvf lvswksadat mkdviwddyv taqvdaidtv relldveavh
      301 svgycvagtt laatlaylsa kqeadkvasa tfftaqvdfa qagellhfvd deqlkmigtl
      361 spegfldgry laatfnllrg rdliwnyvtn nyllgrdyvp fdllhwngdv tnlpakwhla
      421 yltdlyrdnr lmtpgamsvg gvaldltkva tpayvqagre dhiappesvw kitdaftgpl
      481 rfvlagsghi agvvnppaag kyqywtndqp aktlaefvag atetrgswwp dwaawlhqrd
      541 satvavtgar vpgegalpal deapgryvrq r
//
LOCUS       WP_285138847            1529 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-glutamate dehydrogenase [Sphingomonas zeae].
ACCESSION   WP_285138847
VERSION     WP_285138847.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas zeae
  ORGANISM  Sphingomonas zeae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 1529)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1529
                     /organism="Sphingomonas zeae"
                     /db_xref="taxon:1646122"
     Protein         1..1529
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=163879
     Region          38..1527
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 madaiaarlt qgalpaelqg fgpaevaaaa afvagvaqqr algepsiale pmsgddthrr
       61 mrlaivnddm pflvdsiaam vgadgiaidr vihpvlpvtr daegqlqaig asgksesfiy
      121 lemeradard rrgliddlra vladvraavv dwsglqdala adattlgekn gegaalllwf
      181 lngkltllgh ekwfedgraa palgiartph kvplladisr qraldyfveg gaaplllksn
      241 aistvhrsvp ldlvlvpvie qgrvvglsih aglwtsaala spphevpvlr trlaalqakf
      301 gfdprghtgk althaltalp hdlvtafpae aleqlaltam sladrprpel vlirsvlqrh
      361 lfafvwlprd elttarrvai gdmlgeaang sllnwsiale dgvvaliryt idlrqdgrlp
      421 dtaalserlr kmvrgwmpdv eaalaeqvpa praarlalrw angfptnyrn vsdaaeaaad
      481 ilrlsalede nsrsvrlfpv qagqdrqlki yklngalpls davpvlenfg frvigelptr
      541 lrddadpfvh dfiveteatt epkgaavleg aiaavlegaa endafnrliv dvglspqavv
      601 lfrawfrylr qaglpygltt vvdalrrapk latalierft aahdpkakgd iaaadaaiaa
      661 gldavsaidd drilrsfrdm iaatlrtnaf aeagkealaf kldshkipgl paplpwrevw
      721 vysprvegih lragpvargg lrwsdrrddf rteilglmka qrvknavivp tgakggfypk
      781 qlpspvtdrd gwaaegkesy rvfirallsi tdnivegavv hpdgvrvldg edpyfvvaad
      841 kgtatfsdva nalalergfw lgdafasggs qgydhkamgi takgawvsvq rhfaergvdv
      901 qtqsirvvgc gdmsgdvfgn gmllskaikl vaafdhrhif ldpnpdpats wdelarmfal
      961 prsswadydt slispgggvf prsaktipls deirealgit atsleptali sailkapadl
     1021 lwfggigtyi kaaaennvqv gdpandrlrv daedlrvtai geganlgvtq aariafaerg
     1081 grintdfidn sagvdcsdne vnikialnre miegrlaegd rntllasmtd dvahivledn
     1141 rlqtlglsia eadgagamps yvrvieifes agrldraveg lgsndvllrr gqdgialtrp
     1201 elavllatak ltlqdaiens alalddelrp dlhaafppam reafgeaidq hrlrgeivat
     1261 klanrivnrm gilhpfelae eegaamadia amfvvverlf dlpalwtaie taampeaari
     1321 alfdevarat rsqiadllra mpagtapgaa lerlqpgier laaetpallr deakaqsarv
     1381 vatleeagap adlaaqvvrv seldgavgla dlgqrlslde trlthaftrl gqalgldwaq
     1441 gqaarinpsd pwerlliagl ardfqqqrld flgragatdp eaaveawler naarvgqfka
     1501 vidrarlaaq pnaamlaqia gqarvllgr
//
LOCUS       WP_285138851             478 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Sphingomonas zeae].
ACCESSION   WP_285138851
VERSION     WP_285138851.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas zeae
  ORGANISM  Sphingomonas zeae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 478)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Sphingomonas zeae"
                     /db_xref="taxon:1646122"
     Protein         1..478
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52968
     Region          18..470
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 matgflalla aavaagyair qenrhsdwvi htyhvetvli earrlveqke tarrgymlag
       61 tpafldsfer ahaalvpqiv elrrltadnv hqraplamvv rrlaeldaaq ratnelvrqg
      121 rgaealrlfh adsgllrmqk lravfdlmar eerrllalrd aeqtasrhrf sivaavsill
      181 fllvsilsfl tvrrytrdlq rsrvaladln atleeqvker tadlalanee iqrfayivsh
      241 dlrsplvnvm gftaelsaat gplaelidra eaeaphivte earlaaredl peaigfirts
      301 takmdrlina ilklsregrr vlapemiald qlveqitdsi rhviddrgvt vtierpmpvv
      361 vsdrialeqi lsnlienatk yrhparaaev hvsaqatpgr vivavrdngr gidprdhqrv
      421 fdlfrrsgqq dqpgegigla hvralayrlg gtisvesqlg egatfflslp ptlaiesa
//
LOCUS       WP_285138862             543 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Sphingomonas zeae].
ACCESSION   WP_285138862
VERSION     WP_285138862.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas zeae
  ORGANISM  Sphingomonas zeae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 543)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Sphingomonas zeae"
                     /db_xref="taxon:1646122"
     Protein         1..543
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=57335
     Region          <133..538
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mldeaiirgg waiwsmaprd geppagdilv gaflasearv alidargagd eglraaqalg
       61 aviaatgaam mvavpdsdad tlhaflaagv thilasdasd amvhaelkla erharrtlda
      121 rrrrthadge vgeihrwiad ildrgqpcaa ivvslsrldl inaahgrpag nmllrgvear
      181 mqavaaeafg dqaivarsgg aefvmagvad grrarsiaet letllaqpfq agavpirlgv
      241 rlglseakph edpasllara gealaraqas dgamlrfahp gdvvpldvla adlhhaierg
      301 eidivfqpqv aigtgritgv ealarwrhps lgplgadplf aaaeradlgl alsdhiqqva
      361 lqraarwpak lshlrlsinv taadigragf vrifldrvaa sgfpierltv eitetglire
      421 ldraaqvldt lraegvrvai ddfgtgyssl ayltslpidy lkidralvte vdgsrrdrvv
      481 vrgiiriatq lgmgivaegv etqeqaellg rlgcetyqgf lcaapldena lramvegele
      541 caa
//
LOCUS       WP_285138876             619 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: glycoside hydrolase family 35 protein [Sphingomonas].
ACCESSION   WP_285138876
VERSION     WP_285138876.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 619)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 619)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 619)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 619)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..619
                     /product="glycoside hydrolase family 35 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=68168
     Region          43..352
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
ORIGIN      
        1 mtqrfrpmil aimaatawsp lsaqsatsnd gpakifevkg kgflrngqph qvisgemhyv
       61 riprgywrdr lrkakamgln tittyafwna heprpgvydf sgqndivafi rdaqaegldv
      121 ilrpgpyvca ewelggypaw llkdrklvlr stdpkytaav drwlarlgqe vkplllkngg
      181 pivavqlene ygafgddqay lrgleasykr agfadgvlft snqggdlakg slpnlpsvvn
      241 fgsggaqssv akleayrpdg lrmvgeywag wfdkwgeehh etdgkkeaee maymlkrgys
      301 islymvhggt tfgwmngads htgkdyhpdt tsydydapid eagnprykyg liaaaiaevt
      361 gkpaaptpap tvattfpvsd irrsaslwdn lptpvraaqp ktfeeldqny gyvlyrvavp
      421 agpaqtltlk gmhsyaqvyl nralvgtldr rldqetvelp arakpatldi lventgrvny
      481 shairteqtg ltgavtlaga plsdwqmfrl pmdnlsslkm sakpcsgpcf yeaemtvakp
      541 gdtyldmrga hkgqlwlndh nlgrfwsigp vhtlytpapw lkaganrvlf fdltgdasdr
      601 lstvdkpiyg kvtnhreaq
//
LOCUS       WP_285138910              91 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Sphingomonas].
ACCESSION   WP_285138910
VERSION     WP_285138910.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 91)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..91
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9629
     Region          1..59
                     /region_name="Cro"
                     /note="cl46781"
                     /db_xref="CDD:481121"
ORIGIN      
        1 mtlldylker qervghfagr igepvstiqk iayrqrqpsl plavkierat dglvtaadml
       61 lggddhesgd tisptvpssg nvnqisasvl a
//
LOCUS       WP_285139019             464 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [Sphingomonas].
ACCESSION   WP_285139019
VERSION     WP_285139019.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 464)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..464
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=49710
     Region          125..448
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mpaafgsaaf rfalmlavvv algagallft verqvgyfar easdgmlrae ssvlsaeyaq
       61 lglsgltdai arhrgsdadp pyrylltdka ghrlsgdlpl qaarigqgsv avpedfdgsr
      121 hverlatqvt qlpdglllvv atdsfdvqql rhrlgrftiw sgiaiaafal iggylvgrvf
      181 lrrlatvnra idriidgdga erlpmigfgp efddltrnln rmlerkaaam ealrqvstdi
      241 ahdlrtpltr lhqrlermqv egagdpdsid aaveqtngll atfeallrig sieggvgrrr
      301 fgpvdltell drihaayvpv vedsgqtfia dhsagvtvig dpdllaqlft nlienaivht
      361 psgtrivscl rtvgteavae icdngpgips derekvfrrf yrrdasrste gaglglalvs
      421 aiaaihqakc tipggaeglc vriafrlssa idqvtdapkh hglp
//
LOCUS       WP_285139024             443 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [Sphingomonas].
ACCESSION   WP_285139024
VERSION     WP_285139024.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 443)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 443)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..443
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=46933
     Region          134..441
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mirrlwrstf givvlvalaf aaatlaigav ayevtheale eqldhrvave tralvaease
       61 aglagvaeai rlreetrnea sldyllvdrn grtvaatiap lappepgyqe hfgfrrgdit
      121 gvgqalatpl aggllvvvad rrdldaidst laalfagalg avlalgigaa ilvgwltrrr
      181 lshidataqa iiagdltqrv prdgsdsefd rlaatlnrml drmaalmdnl rqvstdvahd
      241 lrtpltrlcn qldraaagdp gaidsarrqa ddlleifaal lriaevegla erralgtvdl
      301 salledmaet yrpdfeaagh altvdivrgl hiegdrrlla qalsnllent lrhtpagtaa
      361 mlsarllqdg ievtleddgp gvspadagrl fqrfartevs rttdghglgl alvravaigh
      421 ggdaaltrpe sgfgvtlrlp vkv
//
LOCUS       WP_285139030             521 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: Y-family DNA polymerase [Sphingomonas].
ACCESSION   WP_285139030
VERSION     WP_285139030.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..521
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=57263
     Region          12..331
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(15..16,19..20,57,60,114..115,167)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(112,115,185..191,220,244..249,280,306..310,312)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mtrkastprr ylalvfpwlp ierlrarrph lfvardeapi afaesvagai rlaalngeaa
       61 aaglsvgltl adarvrvpev eifphdpaad adwlerlaeg arryspaval dppqglilds
      121 agvdhlfgge rglaedietr marrgitvrl aygdtpeaar alarhagapa pdemgairrl
      181 piaalelded agaaliaagl ksvgdvlarp matiaarfgr eaatalrrlt geedspltpr
      241 avaapigver rfaepvakte hmlgvledla geaaralear heggrrwgar lfrsdgevqa
      301 lrvetgqptr dpavlmrlfr eriealadpl dpgfgydlir ldvglaekld avqlrlegge
      361 graqqgaeav aalidrlgtr lgrervrrih prdshmpeqa elllpatdpa pkaewtrpep
      421 gepplrpihl fdppqpaesl aaetpdgppa rfrwrrkmhd varaegperi agewwrradm
      481 apptrdyyrv edvrgrrfwi frhglysete rprwyvhglf a
//
LOCUS       WP_285139077             139 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [Sphingomonas].
ACCESSION   WP_285139077
VERSION     WP_285139077.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140991
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..139
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15019
     Region          2..127
                     /region_name="HTH_CadR-PbrR-like"
                     /note="Helix-Turn-Helix DNA binding domain of the CadR-
                     and PbrR-like transcription regulators; cd04785"
                     /db_xref="CDD:133412"
     Site            order(3..5,19,36..38)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133412"
     Site            order(50,53,57..58,67,78..79,82,85,89,95,99,102..103,110,
                     115..116,121,123)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133412"
     Site            order(78,113,121)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:133412"
ORIGIN      
        1 mlmigdiakr tgtkvntirf yeeiglmpea artaggrrty gdaevrqlsf irhardlgfs
       61 tdeirslial sanpdqdcke agalarrhla svedriarlm alrdalanat rdceggriad
      121 crvmeaitsp sdlasgarv
//
LOCUS       WP_285139177             109 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [Sphingomonas].
ACCESSION   WP_285139177
VERSION     WP_285139177.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 109)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 109)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 109)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 109)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..109
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11539
     Region          14..91
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdtpdalaal aalshptrld afrllvrhsp dglptgslve asgltqstfs thlavlakag
       61 lvsaekrgrq qvqharldtl rqlmtflakd ccegraelce pliadlscc
//
LOCUS       WP_285139642             356 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Micrococcus luteus].
ACCESSION   WP_285139642
VERSION     WP_285139642.1
KEYWORDS    RefSeq.
SOURCE      Micrococcus luteus
  ORGANISM  Micrococcus luteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Micrococcus.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Micrococcus luteus"
                     /db_xref="taxon:1270"
     Protein         1..356
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=34814
     Region          26..349
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 msvqrtapdd vvarlrrsdr rrlggacagl avavlvlall rvvwgtyqvt vpdlvrilag
       61 etipgasfiv leeklprava avltgaalga agalyrrtlr nplaspdilg vtqgaaaavv
      121 lgmlatagqt gggsdlmraa talvgglaav vavfatarsv ggerfvvagi avaaagqavv
      181 agamlslaqh dvqsatvwia gslngvtwgr iallagvlva alplagvlha rlapadvgpd
      241 lahalgarpr ptsaaalglg avlaavatav vgplafvall atpvargltr glpslpaaal
      301 tgaalvllad lvageavpll tgaalptgvl tgaagaplml wlllrqgrtp ggvrsa
//
LOCUS       WP_285139820             490 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Micrococcus
            luteus].
ACCESSION   WP_285139820
VERSION     WP_285139820.1
KEYWORDS    RefSeq.
SOURCE      Micrococcus luteus
  ORGANISM  Micrococcus luteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Micrococcus.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Micrococcus luteus"
                     /db_xref="taxon:1270"
     Protein         1..490
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51764
     Region          1..450
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mdilgtinda iwtpmayfal avglvftlat kavqfrripd mlreitarpl edegvsplqa
       61 llltlasrvg vgniagvgta vyaggpgaif wmvvvallgs assfaetvla qvfkrridge
      121 hrggapfyve hglklrwlav llaigyvvgy gfifsgvqan niansmdvaf gmpawltavl
      181 ltgvfaltil ggtkriigva qlavpvmaig yilctaaiil anldqvlpti qlvlasafgr
      241 davfggmaga aiawgvrrav fsnvagvgeg tfgsaaasva hpaqqgliqs lsifidtviv
      301 cqatgimlli tqsynvshdg rtmvenlpgv dagvaftqta ldtlvtgwga afvaiallff
      361 aftsmiafyy iaetnltyir grsggwpswa vklgalavta ygsvisadam wtvgdigygl
      421 lgwanmiail allpivikvt rdydrqrrag lqpvfqpeel girgadywte artrdllatv
      481 rtrkdhspva
//
LOCUS       WP_285139850             822 aa            linear   BCT 25-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Micrococcus luteus].
ACCESSION   WP_285139850
VERSION     WP_285139850.1
KEYWORDS    RefSeq.
SOURCE      Micrococcus luteus
  ORGANISM  Micrococcus luteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Micrococcus.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 822)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 822)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 822)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Micrococcus luteus"
                     /db_xref="taxon:1270"
     Protein         1..822
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=83863
     Region          18..820
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mthpasstpa gpqsettrrv dldvtgmtca scvgrverkl gklegvtasv nlpleqatvt
       61 apagvsdeel vaavekagyg atvrrpappa gqaghaahag hahtsdhgee htadhdgvdh
      121 hdhmahgpge dvlkprliga avltvplvli smvpalqfph wgwvafalaa pvalwaawpf
      181 hsaafraarh gsstmdtlvs lgvlvsfsfs avelivapdm tahvggtmae mahhslyfet
      241 aavittflll grwlevrakr eagaalrall dlgaaqatly dpethdertv paqslapgdv
      301 vlirpgekvp tdaevlegts avdaslltge svpvevgpgd altgatlnts grlvaratrv
      361 gsdttlaqmg rlvseaqtgk arvarladri savfvpivlg iavltfavwm lvtgdlpsal
      421 ragvavlvia cpcalglatp vgllagtgra sqlgilirgp evledsrtvd tivldktgtv
      481 tegrmaladv lvldpafvae tgasrsafva etapdqaadv lltlaaaver gsehpiarai
      541 vagaeerglt vpdvadfast agggvsglva lphddgalgs gahdaagpap vrvavgrgsv
      601 letaldggip aehraafeaa eqagatavwv avggrvagvl svrdtvkets adaiarlkel
      661 glrpllvtgd naavatqvaa avgipaedvv agvrpedkvd vvtrlqsega vvamvgdgvn
      721 dapalaaadm giamgsgtdv areaaqitvm gddlhqvvqa ldlsrrtlgi irmnlfwafl
      781 ynvlgipvaa lgllnpmiag gamaassvlv vlnslrltry ar
//
LOCUS       WP_285139908             284 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Listeria
            monocytogenes].
ACCESSION   WP_285139908
VERSION     WP_285139908.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..284
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31461
     Region          12..274
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtnangnlkk cpitissytl gtevsfpkrv kvaaengfdg iglraenyvd alaagltded
       61 mlrildehnm kvteveyitq wgtaedrtae qqkkeqttfh marlfgvkhi ncgllekipe
      121 eqiivalgel cdraeeliig lefmpysgia dlqaawrvae acgrdnaqli cdtwhwaran
      181 qtaesiknvp adrivsiqlc dvhetpykel reeslhdrla pgegygdtvg fakilkehgv
      241 nprvmgvevi sdsmvatgle yaalkvynat kkvldeawpe ispr
//
LOCUS       WP_285139928             612 aa            linear   BCT 25-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Micrococcus luteus].
ACCESSION   WP_285139928
VERSION     WP_285139928.1
KEYWORDS    RefSeq.
SOURCE      Micrococcus luteus
  ORGANISM  Micrococcus luteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Micrococcus.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Micrococcus luteus"
                     /db_xref="taxon:1270"
     Protein         1..612
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64922
     Region          18..612
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mqnqspvhes atelvgmppa dsnitdlivt scadrpdapv yavrngaggw vdvhftaflt
       61 qvravaagli argvqpgdrv glfsptsyaw avldqavwfa gavsvpiyet ssahqvehiv
      121 tdsglrvvav gseelderva eaaghagvdv atfpltdagl aelaeagafv addavehars
      181 latlaspasi vytsgttgrp kgavithgnf vgaainvlhf arevvqwspe tttsrtllfl
      241 plahvlahav qviclyariq vahsgspatl lgdlasfhpt wllavprvfe kveagieaka
      301 qksgtgpiya aakrtaiews tavdeaefgd gpgpsallra rralfdrlvy rkirealgge
      361 viscvsgasa lspelvhffr gagipivegy gltettapat vnipgahrvg tvglpvagvt
      421 vkiaedgeil irgpvvfdgy hgmpqasaea meddffrtgd igaldehgfl ritgrkkdvi
      481 itaggknvyp tpmeetlrqh rliehvvvvg enrpfvgali tldseaftqw aldrelsltp
      541 aeaatdptvl asiqeavdqv nagvsraesi rrfrildhpf tedsghvtqs qklkraqvie
      601 dhaedvealy rr
//
LOCUS       WP_285139946             381 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Micrococcus luteus].
ACCESSION   WP_285139946
VERSION     WP_285139946.1
KEYWORDS    RefSeq.
SOURCE      Micrococcus luteus
  ORGANISM  Micrococcus luteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Micrococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Micrococcus luteus"
                     /db_xref="taxon:1270"
     Protein         1..381
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41952
     Region          22..366
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mtaaspnepg aasvapdekr vpgprfreld glrgiaalav vfshyaaqhn shfpedpspf
       61 hgfewgaagv qlffiisgfv ifmsarrasr psdfaisraa rlyppywisl vfavvllllh
      121 pvpgfpftwg qallnltmvq rwvgvdnvvd vywtlavemq fyviililly ltrcrlsdrv
      181 vlwgsiawsv iswgvvsfta phvgsnpqrd plwvkllnna avaeyaplfv lgmalyiarq
      241 tgrhrgwvaa aavsavgstf vmrgmplale vlvvvllavt vmlrkrtsvl llapiqwygk
      301 isyslyvlha ipgyilihtl wpyvgrnmam lvalavvsvl awalqkygee algkaakrgl
      361 trvrsvvdar tghprslepa r
//
LOCUS       WP_285140074             307 aa            linear   BCT 25-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Micrococcus luteus].
ACCESSION   WP_285140074
VERSION     WP_285140074.1
KEYWORDS    RefSeq.
SOURCE      Micrococcus luteus
  ORGANISM  Micrococcus luteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Micrococcus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Bagautdinov,B. and Kunishima,N.
  TITLE     Crystal structures of shikimate dehydrogenase AroE from Thermus
            thermophilus HB8 and its cofactor and substrate complexes: insights
            into the enzymatic mechanism
  JOURNAL   J Mol Biol 373 (2), 424-438 (2007)
   PUBMED   17825835
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Micrococcus luteus"
                     /db_xref="taxon:1270"
     Protein         1..307
                     /product="shikimate dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30783
     Region          6..280
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 mrpvlraavl grpiahslsp vlhtaayrvl gldvdygrrd lgedevlafa aehlgapgaa
       61 dggaaaargq dwlgcsvtmp lkravvaaag hvsdrvrllg santlvrdhp sapgvvhaen
      121 tdvdgilgal aaagldraar ggtlgvlgng gtataavlaa atlgadavlf gvrdaaraae
      181 vtaladalgl rwatltqadl lrrapglrav vatlppraad alaahvpada alpplldaay
      241 dpwpsvlasa wsrevgpvas glsmllhqgi eqvrlftarp raaagmpepd waavtraaad
      301 algpaag
//
LOCUS       WP_285140251              74 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micrococcus luteus].
ACCESSION   WP_285140251
VERSION     WP_285140251.1
KEYWORDS    RefSeq.
SOURCE      Micrococcus luteus
  ORGANISM  Micrococcus luteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Micrococcus.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 74)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Micrococcus luteus"
                     /db_xref="taxon:1270"
     Protein         1..74
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=8360
     Region          14..67
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mqathsthpp ahflytphtl aerfgvpvat vyswrskgag prgfrvgkfv ryrledveaw
       61 eqeqiekeqa vhng
//
LOCUS       WP_285140290             297 aa            linear   BCT 25-DEC-2024
DEFINITION  tRNA pseudouridine synthase A [Micrococcus luteus].
ACCESSION   WP_285140290
VERSION     WP_285140290.1
KEYWORDS    RefSeq.
SOURCE      Micrococcus luteus
  ORGANISM  Micrococcus luteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Micrococcus.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Hur,S. and Stroud,R.M.
  TITLE     How U38, 39, and 40 of many tRNAs become the targets for
            pseudouridylation by TruA
  JOURNAL   Mol Cell 26 (2), 189-203 (2007)
   PUBMED   17466622
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Foster,P.G., Huang,L., Santi,D.V. and Stroud,R.M.
  TITLE     The structural basis for tRNA recognition and pseudouridine
            formation by pseudouridine synthase I
  JOURNAL   Nat Struct Biol 7 (1), 23-27 (2000)
   PUBMED   10625422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414743
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Micrococcus luteus"
                     /db_xref="taxon:1270"
     Protein         1..297
                     /product="tRNA pseudouridine synthase A"
                     /EC_number="5.4.99.12"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=32175
     Region          20..282
                     /region_name="TruA"
                     /note="tRNA U38,U39,U40 pseudouridine synthase TruA
                     [Translation, ribosomal structure and biogenesis];
                     COG0101"
                     /db_xref="CDD:439871"
ORIGIN      
        1 mseqhrpdap papgdpasvr vrldlaydgg afhgwarqpg ldsvqgaled glerilrrpv
       61 rtvvagrtda gvhargqvah ldltetewag ltrgrpglep aasltrrlgg vlsgwggavv
      121 vhgagrapag fdarfsalwr eyeyriddap aardprtrgf thwhgaaldd rlmaleadav
      181 lglhdflsfc rpragattir evqhlevrrd edgvvrvrir adafchnmvr aivgallqvg
      241 egarepgwla hrvarpards evrlappggl tllavgypde aeelrrraeg trakrtl
//
LOCUS       WP_285140504             907 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Listeria monocytogenes].
ACCESSION   WP_285140504
VERSION     WP_285140504.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 907)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 907)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 907)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 907)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 907)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 907)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 907)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18767243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..907
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..907
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=105757
     Region          1..907
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          1..196
                     /region_name="AAA_27"
                     /note="AAA domain; pfam13514"
                     /db_xref="CDD:433272"
ORIGIN      
        1 mritsidiig ygkwsdahfn nianfqvfyg eneagkstim afihsilfgf ptkqqsiprm
       61 epknggpygg rltledtsfg kviierlkgk atgdvriyyg dgqtageekl peiigeidrn
      121 tyeaifsfdi hglqnihrwk kkeferylla tgttgsdall ktaetlqkkl dslykpsgrn
      181 pvinqqlkrv keaqqafqna kkqnaqyeel inekeqatar qaelqiektt krveldtlet
      241 lgdlwplyqe wkalsnkasq kkeatfppdg iirlehlqlr ekewqnqliq leerkknlis
      301 nndyehsaff akneaeityl ietyaafger eiqlknlkqe infhqvdskq tfrvwtsele
      361 qtmarlkeke qfhkeqqhei qlklkltndt eeklqkkidq iemdmwdnrt fqqakekmqq
      421 kpktfrtktf vsfgvfaval slmivfqsiw svalvfvsal ivgyaimttw kalptnneql
      481 lvfleqkkir qewqqllnem diiasqiael ratenklnet iyqhtmelkq lfsdlgikhn
      541 pdanwayela vykknsekaq lameliskle plaekqevyk arlanlelpg kytdteekit
      601 flrqgllyyr nhltenakla ekleqvtmql dlvkqdllli kkekadllas anakneeefr
      661 maairvkeeq nwrerlvlie aqlepekria lnqyenqati kekelqleet lrqieleqek
      721 ihaslaaqnh aihkleeggt favlmqefys eksklqqiav ewtetklalq ilqdtiqrlq
      781 egklpktlkl aseyfnhltn gnydkvylqd nrlqvesknv vpffpeelsq atkeqlylai
      841 rfalidvihk dfplpiiidd gfvhfdsarm gqmmqllrkr ksenqvifft chqetrkyfs
      901 sedirml
//
LOCUS       WP_285140781             449 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lactococcus petauri].
ACCESSION   WP_285140781
VERSION     WP_285140781.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..449
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=51421
     Region          95..436
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mnnvkisnit qksirdsskk gskkvkfrss fknpltgkrr eflsewytin enyddkgnik
       61 issqlqsivq rdmqnlansi yqdiskvqlt sndnitleki wsewhndrvl kkkvapktla
      121 getgrfnnhi trfiprdsli knirseliqs liddlyplgn hkrvaqsiks dlssiyifav
      181 kknyilpeqn pmlyvtveek glseqleqle nnsienhyle kdelnevlki vrkynqqyar
      241 ilefqvltgm rigevlglks svisfetgla tirrtrathg gasrddyegn vknkqsyrti
      301 klsskallll qeemeinqhh ivgnpnykds dwiftskssn ksdyngiplh ysvinnflns
      361 sqtgkvtktg hikkvginid nqisfnkhis thifrhtfvs hmaeqgvpli avqryighks
      421 gskiteeiyt hitkkmsdti tesidslid
//
LOCUS       WP_285140798             457 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Staphylococcus
            epidermidis].
ACCESSION   WP_285140798
VERSION     WP_285140798.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus epidermidis
  ORGANISM  Staphylococcus epidermidis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Staphylococcus epidermidis"
                     /db_xref="taxon:1282"
     Protein         1..457
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=55277
     Region          1..456
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 maigvilnrv frlnnnplfd yiysnkesin hcyfiiptee feeeakkkaq yyygsiqkfm
       61 yelqrydiep flmsydklid fckkqaidkv vvagdimsyh heeydilhqr krfkqaniqv
      121 islranhyfn prkthnkqge pykvftsfyr kwrpylmird eydyhledis kvvvksqhki
      181 kedyhsygis erdvqnrwse flsqdienyk enreylpevl tsqlsiylay gmidiiqvfn
      241 dllqnydkne qnyetfirel ifrefyyvlm tnypetahva fkekyqqlkw syneenfklw
      301 kdgntgfpii daameelktt gfmhnrmrmv vsqfltkdlf idwiwgesff kqklidydaa
      361 snvhgwqwsa stgtdavpyf rmfnpirqse rfdnnaryik tyiprlnqvd akylhdthkf
      421 eqqikgqgve igkdypkqmi dhkesrqrlm sefkald
//
LOCUS       WP_285140943             215 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Lactococcus petauri].
ACCESSION   WP_285140943
VERSION     WP_285140943.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..215
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24271
     Region          3..208
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 msfntiifdm dgvlidteyh yaqvfdaffd kkgipiahln rrellgrplr dlwpfilged
       61 fdkkdaarlq kefftykkss nfpieemlfp dvkvvlqhls etklkiglat ssshdeiaev
      121 ldthnlrkyf evissgedfp eskphpavyl samkqlnara sdvlviedsp ngiaagkaag
      181 atvwairdqr fdsdqsqadr hvehltevle ilgfs
//
LOCUS       WP_285140989             413 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Lactococcus petauri].
ACCESSION   WP_285140989
VERSION     WP_285140989.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..413
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=47269
     Region          33..60
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          69..94
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          72..326
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          102..128
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(104..105,108..109,111,134,137..138,141..142,
                     144..145,171,174..175,178..179,182)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          132..165
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          170..198
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          203..228
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          236..266
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          271..298
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msysedtidf lhkgdligmh nalsnalkhd neemladlae ylqmmgfide shqvydkilg
       61 dnpestdyli nlaeiaeddg qiddalnyly qipagdenyv aaliqiadly qfegdfetai
      121 skleearels dsplitfala esyyeqgayq eaiqnyvkls vreilqqtki styqrigesy
      181 ahlgnfenai sflekslefd ktadtiykia llyseldnqs raisyfkqle dyntdllnye
      241 layaqtlead rqfdeaarva qegllknpns alllhflskl aysqkdqaaa erylmdalnv
      301 aelhdetvfl lanlyfnesd feavirleel leeehllaqw lfaqahkele ndaqaealyt
      361 ellstaltdn pdflkdyvdf llqigqneka qtyikqylel vpedeemrgl lfe
//
LOCUS       WP_285141007             265 aa            linear   BCT 25-DEC-2024
DEFINITION  TPM domain-containing protein [Lactococcus petauri].
ACCESSION   WP_285141007
VERSION     WP_285141007.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Sirpio,S., Allahverdiyeva,Y., Suorsa,M., Paakkarinen,V.,
            Vainonen,J., Battchikova,N. and Aro,E.M.
  TITLE     TLP18.3, a novel thylakoid lumen protein regulating photosystem II
            repair cycle
  JOURNAL   Biochem J 406 (3), 415-425 (2007)
   PUBMED   17576201
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..265
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28944
     Region          1..>193
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mkkkrilltl fftvitlctl fafakdtsaq qvgiddqaal lsdstqsleq eaqllanqtk
       61 agvfvvttmd dtespkelav nylaqkvgqg nngiilvinm sqrklyiwat gnlkyyitss
      121 riesildvvq pqlsdgnypq aiesfyaqvt hyyeqgipgg rkytvdpqtg avtfhrsfrp
      181 ayiliavila listgafviv lvsryqlkmg ahwnygyqen gklnlskqsd tlvnsfittr
      241 riprnnnssg ggfsggggsg ggrsf
//
LOCUS       WP_285141068             296 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease, partial [Lactococcus petauri].
ACCESSION   WP_285141068
VERSION     WP_285141068.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..>296
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          12..>296
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mnkiiikkvi isnfrsfkns cnsideinnl nmftgknnag ktnilrainl ffnpsnynpq
       61 idmnaikkit ggaskhpkie ikfeenqkgq ksllytivld lnqekdyykl kgkksiskls
      121 sskkisdyla knfkcvylst tdeeiteqay kvvndmilqy ykkrnkairs tienfenqyk
      181 tlistfesni sdleqeiseq faifkssnik iepqlkiesn tnvsdfllen iklelddays
      241 qainakgagi qrtslilltf fllnqiytnt nkiilldepe aflypliige lknsie
//
LOCUS       WP_285141111             318 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Lactococcus
            petauri].
ACCESSION   WP_285141111
VERSION     WP_285141111.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..318
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35329
     Region          1..>313
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mkltilhtnd thsylddmgk rakkineire knlsegnatl ligagdalsg dlyynlyhgk
       61 keaqllnllq ydvmtlgnhe cdggshilsq firdvnfpiv tsninfkhdk liaplveekk
      121 ilpymiktls sgvkigifgl ttletpsygf pssetifndp fmvaremidk lielesdiii
      181 lvshlgddid illakeidgi nvivgghthv pieenivvnd tiivqagayg eflgevnley
      241 tdtgkiklvn kflhkvsena vderlesfls dmkheknkls shklftvkdr idgerivssk
      301 pfstlgnvva daffleai
//
LOCUS       WP_285140281             398 aa            linear   BCT 25-DEC-2024
DEFINITION  HesA/MoeB/ThiF family protein [Micrococcus luteus].
ACCESSION   WP_285140281
VERSION     WP_285140281.1
KEYWORDS    RefSeq.
SOURCE      Micrococcus luteus
  ORGANISM  Micrococcus luteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Micrococcus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Park,J.H., Dorrestein,P.C., Zhai,H., Kinsland,C., McLafferty,F.W.
            and Begley,T.P.
  TITLE     Biosynthesis of the thiazole moiety of thiamin pyrophosphate
            (vitamin B1)
  JOURNAL   Biochemistry 42 (42), 12430-12438 (2003)
   PUBMED   14567704
REFERENCE   3  (residues 1 to 398)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14967496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Micrococcus luteus"
                     /db_xref="taxon:1270"
     Protein         1..398
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40990
     Region          19..257
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
     Region          312..397
                     /region_name="RHOD"
                     /note="Rhodanese Homology Domain (RHOD); an alpha beta
                     fold domain found duplicated in the rhodanese protein. The
                     cysteine containing enzymatically active version of the
                     domain is also found in the Cdc25 class of protein
                     phosphatases and a variety of proteins...; cl00125"
                     /db_xref="CDD:444705"
     Site            362
                     /site_type="active"
                     /note="active site residue [active]"
                     /db_xref="CDD:238089"
ORIGIN      
        1 mtaaldpaar eprdltalsd tqlerfarhl sldgfgpeaq lallrsrvlv vgagglgapv
       61 ltylaaagvg evhvidddmv drsnlhrqvi haeadlgrpk tasaaatmrg lhpevrvveh
      121 rerltaanal ervgavdlvl dgtdnyatry lvadaceiag vpvvwgailr fagqvsvfap
      181 ggplyrdvfp erpepgevps caqagvlgvl pgiigslmaa eaikllsgvg eplvgrllsv
      241 daltmrfrel rlvadpertp vtdlsahaaq aprpddagap gsaeacgaag geitpaalaa
      301 lladaaraas ltlldvredw errlrcveap aavadrhvpl eavlaepaah apgqdrvlvv
      361 ycaagarsar ardavvgadp gaggrvlsla gglaawpa
//
LOCUS       WP_285141413             789 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Lactococcus petauri].
ACCESSION   WP_285141413
VERSION     WP_285141413.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 789)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 789)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 789)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..789
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..789
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=89045
     Region          <33..>134
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mkdldlsisl seaqrqkisf eapddskkkq ysiflmdssr smggrsvkqt kdivgkfvke
       61 sgaskqehqv alvsfgdeat vlqaftpdek qllsalekie trgktnlhsg lkqaeqllqa
      121 vkdegqknif iisdrtpttg eklntgkygn kdiysyqfan aadnlaqkmk teqqvsfrtf
      181 vfidkiadst kafartffqn iqtdgafdfr dvqdmdfvfk skeagkefqs gtfnygsapa
      241 gkegrdsqav yhysdsyfeq sayayrqekn rpydprlatm slnlelaaws siqeknyllk
      301 nrnaknllee igfekfkanq hfqerpstds igaviaqkkl tvkeedytli alairgggye
      361 aewasnltlg rsgehqgfre asekaltfld qylkehkvtg kvklwingys raaavtnlta
      421 galnkgrkla sgelkaedmy afcfeapagt lkgtgnregr hdnivnvinv ndvvtkvgpe
      481 vypfeftryg qdsslpdktl lpqevyetak srmeaelkkl dsnliyklee fqakkisild
      541 ifnglivddp kgkrmnesld diirffaver iknrnkyvna hqedirilae lyfttrvedr
      601 ekltkslfkn lvtsmmlgsd atkvkkivvd wlrtkglvnh sevrieslae tfrelvfkfm
      661 ikhpnlsvtl vsnldpvaqa hhpdlclawl raqdenyqkk kietpepskt skriliagdv
      721 dikvkretge ieeystdevm elstsaaedt tvlvqaseat kvdytvqtid nmdgsvflte
      781 efedvelna
//
LOCUS       WP_285141471             672 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Lactococcus petauri].
ACCESSION   WP_285141471
VERSION     WP_285141471.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 672)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 672)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 672)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 672)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..672
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75657
     Region          5..516
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mlqsilhvii fllalvfsnv inkifpklal plvqvligil fgfggisefl hvdpefflgf
       61 iiapllfres teaevkrivk hrhlilvlif plvfvtalgl ggilhlfyms iplaaclalg
      121 aalaptdaia vgtlstrfvf pqrimnilqg eglfndasgi vsfqiavlal vtgtfslpqa
      181 tlnlilsiig gfaigiglsi fknkileild dvdardvsgy lmlefvmpla afalaevlhv
      241 sgiiavvvag ifqsngfrpt tvfdaqvtrv knsvwetivf mlnssvfifl gielhslvfp
      301 flfdrtysvf wlvfvvlllt falfllrfli llsyylvtvk dkgeifhsyw selllltfsg
      361 tkgtvsiati lllpqladnt nnlliffcas vtglsflvsl ltlpyfavek krtvnnlavi
      421 ailgdvvqel reritekaqn gyhlviadyq nriqkliveq esagitenfn tlqlliirve
      481 iegledalek ekismrtyrt yhryihtleq dlahdlvssi qfaqvvtlra lkvlktrisr
      541 fdfqlsrpkv edmeetrqei snlyldntel vlellenlgt iynaqlvdfl qaerfrqaeh
      601 iaqgnwnyvn gfrvateltn ieelmeayyl erkvifeyeh tgrialneak klrqtvnlle
      661 eyalasdhrs fl
//
LOCUS       WP_285141505             267 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Lactococcus petauri].
ACCESSION   WP_285141505
VERSION     WP_285141505.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..267
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30316
     Region          6..262
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(28..29,31..32,35..36,73,77..78,81..82,112,116,123,
                     126..127,139,155,159..160,162..164,166..167,170..171,
                     174..175,200..201,203..205,207..209,211..212,214..215,219,
                     222..223,229,231)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(158,162,165..166,168..169,214,217..218,220..225,
                     228..230,234,236)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(179..186,202,205..206,209)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mqnmlmgryi pgnslihrld prskllvmfi fviviffahd wlgylllily tfagvllsgi
       61 pisyflkglr pmiglilftv ifqmlftpge hiifqfwilk isteslinal yiffrfvlii
      121 fmstvltltt ppltladgie tglaplkkik vpvhelglml sislrfiptl mddttmimna
      181 qkargmdfge gnllqkvrsi ipiliplfvs sfrraedlav amesrgyqgg dgrskyrqlk
      241 wskndfilll sifilaalll swntfsr
//
LOCUS       WP_285141570             146 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Lactococcus petauri].
ACCESSION   WP_285141570
VERSION     WP_285141570.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 146)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 146)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 146)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..146
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=17093
     Region          <34..137
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mkfhkkidps yteteilvrt ysesiyeeim nmldnsiylk stsgaykvkl gniiyiesnk
       61 nylevyakek ntiknfrvrl tlykikells ddfiqisrty ivnynfldsv eadlihgmva
      121 rvmgfkipis rtylegiysk leeenn
//
LOCUS       WP_285141628             243 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Lactococcus petauri].
ACCESSION   WP_285141628
VERSION     WP_285141628.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..243
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28142
     Region          1..142
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mtasyeefar vydsvmdeel ydlwfefsqr hfpaktqnim elacgtgils irfsqagyev
       61 tgvdlseeml tiadkrarqm eakitfaagd mrelsgettf dvvtcysdsl cympnasevq
      121 rvfdgvynsl naegvfifdv hstyqvdsvf pgysyhende dfaflwdsfv gdyphsvvhe
      181 ltffvkdsdg kfvrkdevhq ertypikeyl irlqkfskve vyadfedgkp deeslrwffv
      241 ckk
//
LOCUS       WP_285141679             215 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Lactococcus petauri].
ACCESSION   WP_285141679
VERSION     WP_285141679.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..215
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24290
     Region          3..208
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 msfntiifdm dgvlidteyh yaqvfdsffd kkgipiahln rrellgrplr dlwpfilged
       61 fdkkdaarlq kefftykkss hfpieemlfp dvkvvlqrls etklkiglat ssshdeiaev
      121 ldthnlrkyf evissgedfp askphpavyl samkqlnara sdvlviedsp ngiaagkaag
      181 atvwairdqr fdsdqsqadr rvehltevle llgfs
//
LOCUS       WP_285141773             524 aa            linear   BCT 25-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Lactococcus petauri].
ACCESSION   WP_285141773
VERSION     WP_285141773.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..524
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60655
     Region          <176..>302
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mlntlhqhlk dprkckifws lifgliwlgt niyvimetpv wnekyitafi lgnicmfiaa
       61 aymvfvyrsv kkidtltesk iqhyykmsmw ilglavllvp fffiihvpdt ahdwdffvif
      121 rdtmqlggrs fthlpmtede llyflrypnn qffgivyntl fapfttnlsr iiattvvaai
      181 ltslsvlggs liikkisnlk maliynlvaf gfipfylyga qlytdtatlp fvifgllfmi
      241 yalqsektsk miiwwiaacl ivffgysikp tvfipmiavf cflvlnrkwk kllimvpvaa
      301 llfvgvhqgv kavianepaf seqandrynl pmihwvtmsf dpinkyggfn pdvlaysqsf
      361 tdvaskkegi khrfienlke mgvpgvlvql wrkimytwfn gdlsnffyty rhsnpfifry
      421 fdwtsfapee gnitgwllik aaqtlywlai vplmwyeifl gifkkhktew fivglsmagl
      481 tgflllwean srylynfapi mlilatmglv dfiqrsrrkn gise
//
LOCUS       WP_285141787             747 aa            linear   BCT 25-DEC-2024
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Serratia ureilytica].
ACCESSION   WP_285141787
VERSION     WP_285141787.1
KEYWORDS    RefSeq.
SOURCE      Serratia ureilytica
  ORGANISM  Serratia ureilytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Serratia ureilytica"
                     /db_xref="taxon:300181"
     Protein         1..747
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81546
     Region          51..>183
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          194..740
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 maitrrtlik gsalavaaml lpistrspaa vvsqdvappd sqhelndwiw idrdgrivig
       61 vsqcevgqgi ytglaevvaa emdadwaqvt vkfvtghday rqvaggeafa qfvaastsmt
      121 kfyqrarlag aqardfflra gakhfalsps qcrtekgwvl ekggkrkvay gdlvryaael
      181 pldpqpalks eaqeresvig kpllrvdtpe kvdgsaiygi didlpemlig vpwmvpdlsg
      241 klvavrnerq irampgvvdl vltrqwsmnn mvgldhdmsl ntvivvaasy wqakkaadll
      301 evdwlpgagk altdsaiaae nlamldgdtl vpavdrgeas alirgveqgs rlhearysap
      361 yvahatlepc natshygegr ietwgpfqgq dmvrnvlakm fglkptdvvv nttylggsfg
      421 rkylpdavmh ataasravgk pvkvvyprei dmrheyyrpa cishyralld engypqalwa
      481 ryagqslfwq mrretvneag gwdesmvecv ystpyriphl kveagiveqp islsylrgvg
      541 svaslffles fiselshkan rdeysyrrhl lqdspealrv ldatataagw qheppsgvsr
      601 gmacniwvgr nnafttyvgl vveiaiqegr lrvlravcai dcgkvinpnl vranveggig
      661 falttclhse lhferggvve gnfdryplla iaempkvevv ildsarapqg cgevstavva
      721 pamasalhka tgktyrtmpf prefssv
//
LOCUS       WP_285141840             339 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator, partial [Lactococcus
            petauri].
ACCESSION   WP_285141840
VERSION     WP_285141840.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401372
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         <1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          60..143
                     /region_name="cupin_Lmo2851-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to Listeria monocytogenes Lmo2851 protein, N-terminal
                     cupin domain; cd06996"
                     /db_xref="CDD:380400"
     Region          255..338
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 miqidkkitr rvipvellnd iareylftln nkeisqrksg nfvfdyptka tndekellsf
       61 skefyiknnq vflskhnrfa dypehdheff efnymlsgsc hqklngkeii lnkgdlilld
      121 pncrhsikal gqndilinii fphksfdinw innlglennt lfnflmnels thskgnyikf
      181 etscnenvev iihqlinkfy tgsyfsneim kfmipilfme ligntpyeln hpqkdraenh
      241 iiaktlqlis eeyfeitleq lanrlhynkn ylsnlikkkt ghtftehlvd ermkrallfi
      301 qtssdsisdi ceqvginnks yfyrlfkdhy ghlptyyrk
//
LOCUS       WP_285141944             232 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Lactococcus petauri].
ACCESSION   WP_285141944
VERSION     WP_285141944.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..>232
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
     Region          3..>217
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 meisiqsaiq emlfdnkarg lskntiifre ktlkvfsvfl yqndilnise ikpihikqyl
       61 vdrlecgyse tsvnahlrai ralfaycvne eymryeeapi hrvkwikerr ivvntftdee
      121 vkmmlrytrk rtfnkikktg kgrtgfctkf vnernyllil vltdtglrin ealnlklehi
      181 ndsqiiikng kgkkdrivhc splvykqylk ytrakdnyls sngiiptenv fv
//
LOCUS       WP_285141937             685 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Lactococcus petauri].
ACCESSION   WP_285141937
VERSION     WP_285141937.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 685)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 685)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 685)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 685)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..685
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77372
     Region          5..516
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mlqsilhvii fllalvfsnv inkifpklal slvqvligil fgfggisefl hvdpefflgf
       61 iiapllfres teaevkrivk hrhlilvlif plvfvtalgl ggilhlfyms iplaaclalg
      121 aalaptdaia vgtlstrfvf pqrimnilqg eglfndasgi vsfqiavlal vtgtfslpqa
      181 tlnlilsiig gfaigiglsi fknkileild dvdardvsgy lmlefvmpla afalaevlhv
      241 sgiiavvvag ifqsngfrpt tvfdaqvtrv knsvwetivf mlnssvfifl gielhslvfp
      301 flfdrtysvf wlvfvvlllt falfllrfli llsyylvtvk dkgeifhsyw selllltfsg
      361 tkgtvsiati lllpqladnt nnlliffcas vtglsflvsl ltlpyfavek krtvnnlavi
      421 ailgdvvqel reritekaqn gyhlviadyq nriqkliveq esagitenfn tlqlliirve
      481 iegledalek ekismrtyrt yhryihtleq dlahdlvssi qfaqvvtlra lkvlktrisr
      541 fdfqlsrpkv edmeetrqei snlyldntel vlellenlgt iynaqlvdfl qaerfrqaeh
      601 iaqgnwnyvn gfrvateltn ieelmeayyl erkvifeyeh tgrialneak klrqtvnlle
      661 eyalasdhrs flydlfefrk rrkgk
//
LOCUS       WP_285141973            1567 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Lactococcus petauri].
ACCESSION   WP_285141973
VERSION     WP_285141973.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471668
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1567
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..1567
                     /product="DEAD/DEAH box helicase"
                     /calculated_mol_wt=177693
     Region          8..1539
                     /region_name="COG4889"
                     /note="Predicted helicase [General function prediction
                     only]"
                     /db_xref="CDD:443917"
ORIGIN      
        1 mvkdffvsfd sliqqindnn vqqrdrgtaf eylvqaylkn epiyknlyse vwmlsevpse
       61 ygiptndigv dlvaqkrtge lvavqakfyd hkiqksdids flselgkdyy segiivstvd
      121 ewgknaeeai nnrsdvsrig lsnlrhsqin weqwsfetpe dvpvksnkep rnyqkevvek
      181 slayfkdydr gqlimapgtg ktftslkvae alakesgkdn fkilylvpsi qlltqtlraw
      241 nndtemsmss mavtsdrnas rraikqdesn lfvkssdigf pattstekvl enyeelknsa
      301 ptellvvyst yqsidvlgka qkeefpdfdl iiadeahrtt gatalgdeds afvkvhndnn
      361 ikgdkrlyqt atpkiygada kskgqemsva issmddeaiy gqviyrlgfg daitrdiltd
      421 yklmvlavde qtiqkdmqks lsnpenglnl ddvgriigvw ngmlkretfs nnvsgspmkr
      481 aiafsqnika skrltdqfet vvneylednd nenrftvhve hadgsmnale knnkldwlad
      541 knlpenqari lsnvrflteg idvpnldaii fmsprksqvd ivqavgriir ksegkdygyi
      601 ilpivipaga tpesildnnk sydvvwqvln alrsvderfe atvnklqlnk nkpeniqvig
      661 vggapddgeg nwkagnqvre eaayqtsfqf dweeiegaiy gkivqkvgdr ryledwskdv
      721 skiaqrhisy intllldnal ikaefdkfla slkhninnsi setqaiemla qhlitkpifd
      781 alfdeysvvr nnpvndamea iltefskygf qkeqkeleaf yesvrlraeg idnaeakqki
      841 ivtlydkffr tgfkstterl givftpievv dfiihsvddv lrkyfgktig skgvhildpf
      901 tgtgtfitrt lqylkglmdk geikledile kyvnelhane iillsyyiaa inieavfdei
      961 ngdeldyepf egivltdtfh stenegtldd dffggnderl krqqevpitv iignppysvg
     1021 qgnandgnqn lvypklnkri eetyakhtka nlkkslydsy iqairwasdr lenngiigfv
     1081 sngsfidkns tsgfrkslkd efnhlyifnl kgdmrsgdwk keggqifgsg sqtpiaisil
     1141 vkdgsdshev hyhdigdyln reqklsilke agsiesfdwt eitpdknndw inqrdenydk
     1201 ylpmdgaifr dkaigvstnr dawvygfska svqanskrli enynsellrl kgisdekekl
     1261 gqlntadnfv kwstglkqkf iknttlqfnp daiivgqyrp ftkkhlqyqp diierpsrfk
     1321 difgesnqii yttgagaska fsviitknvp nlhfldsgqg ffrfdnssnd rlfednsnls
     1381 sdfanklgli eeeifyyvyg vlnqsdyrek yandlqkalp ripllknkek fveigrklad
     1441 lhlnyehqps wqgvtvtgea lgnfkvkkmk hpkkgqidti ifnenitisn ipeqayeyvv
     1501 ngrsaiawim dqyqvktdkk sgivddpnef sdnpryildl llsvitvsmk tvelvgqlpk
     1561 mevlese
//
LOCUS       WP_285142063             542 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Lactococcus petauri].
ACCESSION   WP_285142063
VERSION     WP_285142063.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 542)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..542
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=62882
     Region          8..461
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(22,24,26,30)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(61,64,101,104,146,165,169,201,243,403)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(201,243,318)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          468..538
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; cl02706"
                     /db_xref="CDD:445893"
ORIGIN      
        1 mnqqnwwqei vmyqiyprsf qdsngdgigd ikgiisrldy laelgiggiw lspvyqspnd
       61 dngydisdye simdefgtmr dmerlisead krgikiimdl vvnhtsdehp wfmearkske
      121 nnyhdyyiwr dapsdgslpn dlksifggpa wqwdevaeqy ylhlfskkqp dlnweneklr
      181 qaiyemmnfw idkgiggfrm dvidligkqp nqgitgngpk lhdylkemnq atfgdknllt
      241 vgetwgatpe iakqysnpan kelsmvfqfe higldeaegk tkwdlmplei pklkevfskw
      301 qtelgnegwn slfwnnhdlp rivsrwgndk eyrvesakml aillhmmkgt pyiyqgeeig
      361 mtnkpvndie qiddiesrnm yferleegys kedilhsina kgrdnartpm qwsneksagf
      421 saghpwlain pnyekinvea aledensify tyqklvalrk enpiivwgef klikntaeev
      481 fayirsykge nwlivanfst kenpfsssye vkeevihnys eaidnveeiv lkpyeafvak
      541 lk
//
LOCUS       WP_285142068             595 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 35 protein [Lactococcus petauri].
ACCESSION   WP_285142068
VERSION     WP_285142068.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 595)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 595)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 595)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 595)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..595
                     /product="glycoside hydrolase family 35 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=67568
     Region          9..328
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
ORIGIN      
        1 mktfqikeef mldnkpvkii sgaihyfrip rsqwedslyn lkalgantve tyipwnihep
       61 eegvfdfegm kdirafvkla eslglmvilr psvyicaewe fgglpawllk eseirlrstd
      121 srfmtkveny fkvllpylsp lqitaggpvi mmqveneygs ygmekdylrq tmalmkkygi
      181 nvplftsdga wqaaldagsl ieddvlvtgn fgsrskenaa vlagfmkehg kkwplmcmey
      241 wdgwfnrwge piikrdpqdl adevkamlel gslnlymfhg gtnfgfyngc sardtgnlpq
      301 itsydydall teagkptaky yavqkaikev cpdvwqaqpr vkeianlgsf kvsesvslfk
      361 tkdnmmkalt ssypltleaa gtgygymlys tvlknygket klkiveasdr lqiyldgqhk
      421 htqyqeeigq eilldvaenq eeiqvdclve nlgrvnygfk fnhpsqqkgi rggmmhdihf
      481 hqgytqypld fsveqlsgid fsagknpehp sfyrfnmsle kaadtfidcs nygkgviivn
      541 gknlgrywnq gpvyslycpk dflhegenei lvfeteavei tslnfsnqpv fdtlk
//
LOCUS       WP_285142273             414 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal-phosphate-dependent aminotransferase family protein
            [Serratia ureilytica].
ACCESSION   WP_285142273
VERSION     WP_285142273.1
KEYWORDS    RefSeq.
SOURCE      Serratia ureilytica
  ORGANISM  Serratia ureilytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Koper,K., Han,S.W., Kothadia,R., Salamon,H., Yoshikuni,Y. and
            Maeda,H.A.
  TITLE     Multisubstrate specificity shaped the complex evolution of the
            aminotransferase family across the tree of life
  JOURNAL   Proc Natl Acad Sci U S A 121 (26), e2405524121 (2024)
   PUBMED   38885378
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Koper,K., Han,S.W., Pastor,D.C., Yoshikuni,Y. and Maeda,H.A.
  TITLE     Evolutionary origin and functional diversification of
            aminotransferases
  JOURNAL   J Biol Chem 298 (8), 102122 (2022)
   PUBMED   35697072
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Serratia ureilytica"
                     /db_xref="taxon:300181"
     Protein         1..414
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=45635
     Region          15..410
                     /region_name="PucG"
                     /note="Archaeal aspartate aminotransferase or a related
                     aminotransferase, includes purine catabolism protein PucG
                     [Amino acid transport and metabolism, Nucleotide transport
                     and metabolism]; COG0075"
                     /db_xref="CDD:439845"
ORIGIN      
        1 mlttpqfdqi npparllmgp gpinadprvl ramssqligq ydpamtgymn qvmalyralf
       61 rtenrwtmlv dgtsragiea llvsairpgd kvlvpvfgrf ghllceiarr craevhtiya
      121 pwgevfsadr iedaikrvrp rllltvqgdt sttmlqplhe lgdicrrhgv lfytdatasf
      181 ggnpletdaw gldavsaglq kclggpsgss pvtlspqfee ivrrrkcvee girtaehadg
      241 ddemiysnyf dlgmimdywg perlnhhtea tsmlfaarec arvileegld qaiarhrlhg
      301 aamlagiqgm glavfgdleh rmnnvlgvmi ppqvhgeqvr qmmlndfaie igtsfgplqg
      361 kiwrigtmgy narkdcvlqt laaleavlnr lgfatqqgea lqaawnlyda grpe
//
LOCUS       WP_285142374             235 aa            linear   BCT 25-DEC-2024
DEFINITION  tRNA (adenine(22)-N(1))-methyltransferase [Limosilactobacillus
            reuteri].
ACCESSION   WP_285142374
VERSION     WP_285142374.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus reuteri
  ORGANISM  Limosilactobacillus reuteri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Hori,H.
  TITLE     Methylated nucleosides in tRNA and tRNA methyltransferases
  JOURNAL   Front Genet 5, 144 (2014)
   PUBMED   24904644
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Roovers,M., Kaminska,K.H., Tkaczuk,K.L., Gigot,D., Droogmans,L. and
            Bujnicki,J.M.
  TITLE     The YqfN protein of Bacillus subtilis is the tRNA: m1A22
            methyltransferase (TrmK)
  JOURNAL   Nucleic Acids Res 36 (10), 3252-3262 (2008)
   PUBMED   18420655
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Limosilactobacillus reuteri"
                     /db_xref="taxon:1598"
     Protein         1..235
                     /product="tRNA (adenine(22)-N(1))-methyltransferase"
                     /EC_number="2.1.1.217"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0160105 - tRNA
                     (adenine(22)-N1)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26158
     Region          5..232
                     /region_name="TrmK"
                     /note="tRNA A22 N1-methylase [Translation, ribosomal
                     structure and biogenesis]; COG2384"
                     /db_xref="CDD:441950"
ORIGIN      
        1 mdekhlsarl acvaslvpag arvadigsdh aylpaalvld gkidfaiage vvkgpyenav
       61 heikdhqleg qviprladgl aaiepadkvd titiagmggs liasilekgk dklteikrlv
      121 lqpnvgesql rewlmnnhyq imtekiieed nhiyeiivae psvvpfrysk yeldfgpfll
      181 enkgpifkkk wqeylqreah vidqmqkaqq ppvkkinein eflsqvkeai addnr
//
LOCUS       WP_285142474             158 aa            linear   BCT 25-DEC-2024
DEFINITION  flavodoxin family protein [Limosilactobacillus reuteri].
ACCESSION   WP_285142474
VERSION     WP_285142474.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus reuteri
  ORGANISM  Limosilactobacillus reuteri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Limosilactobacillus reuteri"
                     /db_xref="taxon:1598"
     Protein         1..158
                     /product="flavodoxin family protein"
                     /calculated_mol_wt=17693
     Region          5..158
                     /region_name="FldA"
                     /note="Flavodoxin [Energy production and conversion];
                     COG0716"
                     /db_xref="CDD:440480"
ORIGIN      
        1 makqalilyy sqfentarla skihevtgad ivrikvpddt fpldmeetgr iyqqqlktha
       61 fpklvttlpd lsyydlilvg gpvwnekvss piiallqqlq eftgkiapfs tgwsdtgdyq
      121 edfinnagkl nvtsgyhilt hgspafneks lfswlrkl
//
LOCUS       WP_285142545              78 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Serratia ureilytica].
ACCESSION   WP_285142545
VERSION     WP_285142545.1
KEYWORDS    RefSeq.
SOURCE      Serratia ureilytica
  ORGANISM  Serratia ureilytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Serratia ureilytica"
                     /db_xref="taxon:300181"
     Protein         1..78
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=9023
     Region          25..78
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mntaftpppa ekrlqilrdy gekgdrlvre kerqyitsis rstawklers gqfpqrksig
       61 lkscgwllsd llcwiner
//
LOCUS       WP_285142640             110 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Limosilactobacillus
            reuteri].
ACCESSION   WP_285142640
VERSION     WP_285142640.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus reuteri
  ORGANISM  Limosilactobacillus reuteri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 110)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 110)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Limosilactobacillus reuteri"
                     /db_xref="taxon:1598"
     Protein         1..110
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12750
     Region          3..95
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msstqafide aakiykvlsn strlnilyyl rhydgeadvk tividlhlaq pivskqlgil
       61 yryqlvsrhk egtrvyyald dphviemidd mlkhvkheik gephprnlyk
//
LOCUS       WP_285142669             407 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Serratia ureilytica].
ACCESSION   WP_285142669
VERSION     WP_285142669.1
KEYWORDS    RefSeq.
SOURCE      Serratia ureilytica
  ORGANISM  Serratia ureilytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Serratia ureilytica"
                     /db_xref="taxon:300181"
     Protein         1..407
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=46676
     Region          3..402
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mgkltdiqik awvkvgerfe gradgnglyl cyrdsfatpk wrfryslagk aramwigsyg
       61 elslakaret vrmlsarval gydvagekke rkasaiakie adknarkvsd lateyferqi
      121 lgrwkhpdil rrridkdinp hignlkadev kprhidemlq nivsrgaptv andvlrwtkr
      181 ifnygikrhi levnpaaafe ladaggqeks rerfltddel sqlfsamkka kgfgrqnelt
      241 fklllllccr kmelcsarwe nidlnnaiwh ltgtkngddi diplpenail wlnelkimsc
      301 nsewvlpark mqnrmiphiv estlpvalak lrphlhgidn ftihdfrrta rthlaslgvd
      361 pivaerclnh rikgvegiyn rhqyfderkk alllwqdkli kldmdsd
//
LOCUS       WP_285142801             224 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Limosilactobacillus reuteri].
ACCESSION   WP_285142801
VERSION     WP_285142801.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus reuteri
  ORGANISM  Limosilactobacillus reuteri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Limosilactobacillus reuteri"
                     /db_xref="taxon:1598"
     Protein         1..224
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25822
     Region          1..220
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mlflsflfga svasfitscc yrlgnnhslt ipqrsycdnc hsilrwwhli pifsfiilrg
       61 qcyyckqkis lylpviefls giafttfliy epihdliill fltsliflts tdffshviys
      121 ysllglfpia llsipqnyfy nlifacilvv slllfatftk tlgigdiefl fvicliwgwy
      181 qtliiiqwss limlfiflft rkkklpfipa lslvtilclf iqgc
//
LOCUS       WP_285142919             229 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Serratia ureilytica].
ACCESSION   WP_285142919
VERSION     WP_285142919.1
KEYWORDS    RefSeq.
SOURCE      Serratia ureilytica
  ORGANISM  Serratia ureilytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 229)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Serratia ureilytica"
                     /db_xref="taxon:300181"
     Protein         1..229
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25988
     Region          1..>221
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msraqrlldl mqllrshryp vaghalaqtl gismrtlyrd iatlqqqgae ivgeaglgyv
       61 lrpgfmlppl mfsqaeieal vlgmrwvsrr gdsqlasaag qalakiadvl ptalreelea
      121 ntlliapaqs ppvadelrvl irdsirrerk lhidyldlag qrserllwpf algffdqfqm
      181 lvawcelrqa frhfrldriq aatpleqryp hgrrrllkew rlsegiaeq
//
LOCUS       WP_285143435             353 aa            linear   BCT 25-DEC-2024
DEFINITION  CdaR family transcriptional regulator [Limosilactobacillus
            reuteri].
ACCESSION   WP_285143435
VERSION     WP_285143435.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus reuteri
  ORGANISM  Limosilactobacillus reuteri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20544506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Limosilactobacillus reuteri"
                     /db_xref="taxon:1598"
     Protein         1..353
                     /product="CdaR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=40641
     Region          4..129
                     /region_name="Diacid_rec"
                     /note="Putative sugar diacid recognition; pfam05651"
                     /db_xref="CDD:461704"
     Region          74..345
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mmelkpklaq sivdhmmtqi pyninimnkk gyiiasgnks rintlhvgav daikqrktlp
       61 mdqqygnhgq pgvnmplkfk neiigvvgit gdpnkvtpla sllktavell lqqkqeneqe
      121 heiekvkqrf iyrwlnvsky qdpqldselv eeanrlninl gkqrcviaia gssqiiknlk
      181 ldqetiifsl tnrieliils skhqeayiqq klehqeieyg isnwgnllgr laeqavttlr
      241 lsnifgkpsf ryysqisfvk qvldsdlnli avndqyeall krkdgkelid tirefikcnm
      301 svnqtahnlf vhrntlnnrl lrikklfeld pkntedlfql figyitfyyr qtl
//
LOCUS       WP_285143445             340 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Limosilactobacillus
            reuteri].
ACCESSION   WP_285143445
VERSION     WP_285143445.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus reuteri
  ORGANISM  Limosilactobacillus reuteri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Limosilactobacillus reuteri"
                     /db_xref="taxon:1598"
     Protein         1..340
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39338
     Region          39..322
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkkvnlyifl tlcsfaifll ttpskvkaev vdkqtqhqlq dymkdhhing vmlvngkdgr
       61 pvaiennett nkdqivkadr lfptaslqki vtgtavyqlk qknqldwdts lskyypqidg
      121 skditirelm nhtsglinnd rpfeplrgqk aqiaymlkhl kydhthtwdy qdvdyeilaa
      181 iiskqthlsy ntyirknfak plhlhqikdf sevskkeipq pmdptvdwhr vtvttssdfg
      241 agnlfispnd ywkfvynevl kdpkmineyy qqaqhqevay fggvyfdgdv irangsipgy
      301 nscfvadykt krmimlfsnn idylklkats ddilhnymeh
//
LOCUS       WP_285143833             391 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lelliottia wanjuensis].
ACCESSION   WP_285143833
VERSION     WP_285143833.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..391
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=44957
     Region          2..391
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 maltarqvet arprekeykl aderglfllv kpnggrywrm kyrvagkekk lsigvypdis
       61 laearlkrdd arkvlaeggd psekkqlekl tkkltventf kalalewhhh klaswsesya
      121 esvlealekd ifphvgkrpv aeilplemle vlrmierrga lekmrkvrqy cnqifryaia
      181 tgratinpaa eltgtltppk tehfphlsvs elpefldkla ayhgspitrm atslllltgv
      241 rtielraaew sefdfdnalw tipearmkmr rkhlvplsdq vvailrelqs ltgqyrlvfp
      301 grcdinkpms easinmvlkr igydkratgh gfrhtlstil hehrfntawi emqlahvdkn
      361 sirgtynhal ylddrrvmmq wyadfvdkia d
//
LOCUS       WP_285144027             325 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein [Lelliottia wanjuensis].
ACCESSION   WP_285144027
VERSION     WP_285144027.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..325
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35752
     Region          1..325
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mtktnlvtgf lgsgkttsil hllankdpae kwailvnefg eigidgalla dsgamvkeip
       61 ggcmccvngl pmqvglntll rqgkpdrlii eptglghpkq ildlltapvy epwidlratl
      121 cildprqlld ekvvknenfr dqlasadiiv ankedrasqe srdafdfwwq nfggdrqfvt
      181 atqgkidnal ldqprrnvae lpasaahshi hapqkglaal nlpehqrwrr slnsgqghqa
      241 cgwifdadtc fdtigilewa rlapvdrvkg vmrtqdglvr inrqgadffi etqnvappds
      301 rielisavnt dwnalqasll klrls
//
LOCUS       WP_285144131             253 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Lelliottia wanjuensis].
ACCESSION   WP_285144131
VERSION     WP_285144131.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..253
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29117
     Region          4..217
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mnelisiimp sfnsaktigd tidsivgqsy tnwellitdd cstdetidiv kryakkdsri
       61 klfcnavnsg aavsrnnsie nsagdylafl dsddrwlpnk lndqltfmis yperdftfta
      121 yelidisstk igkivdaqgd nlsfdysdml rkkatlgcst vmfrkmafpd ykmplirtgq
      181 dyalwlkllk tgkkaylink vltqyrilpn sisrnkfkkc krqwqiyrsi eklniyqssv
      241 sfahyawrai frr
//
LOCUS       WP_285144305             437 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Lelliottia
            wanjuensis].
ACCESSION   WP_285144305
VERSION     WP_285144305.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 437)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468625
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..437
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=48856
     Region          32..431
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
     Region          203..433
                     /region_name="RHO_alpha_C_AntDO-like"
                     /note="C-terminal catalytic domain of the oxygenase alpha
                     subunit of Pseudomonas resinovorans strain CA10
                     anthranilate 1,2-dioxygenase and related aromatic ring
                     hydroxylating dioxygenases; cd08879"
                     /db_xref="CDD:176888"
     Site            order(209..210,214,217..218,221,223..224,226,228,336..337,
                     378..380,382..386,397..400,421,424,428)
                     /site_type="other"
                     /note="putative alpha subunit interface [polypeptide
                     binding]"
                     /db_xref="CDD:176888"
     Site            order(218..219,221..222,224..225,229,310..311,313,321,323,
                     328,362,365..366,372..373,376)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176888"
     Site            order(218..219,221..222,224..225,229,310..311,313,321,323,
                     328,362,365..366,372..373)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:176888"
     Site            order(224,229,376)
                     /site_type="other"
                     /note="Fe binding site [ion binding]"
                     /db_xref="CDD:176888"
ORIGIN      
        1 mncdhlitik niditphslp tsaeiaglvq sdrvhtslyt sdslfqleld rifsktwvwv
       61 ahaseipetg sfkttelgtq pvivvrdrkg tvhtllnrcr hraatvcehr sgktnsfvcp
      121 yhgwgyaldg slrgvphpes yadqlekgel glvslrteqy agmifatfne qiepledflg
      181 aakkwmdlfm kqgagypikt gpahrfrfpg nwkiqlentt dgyhfpvvhr sflssvdkqt
      241 eemlnfvdgs gyvedlgngh svmvmipelv dleanldapi perfeelaea lradhdeqqv
      301 rrivravggs gfnlnifpni acsmaffrvl qpvsvnetei hhavitmdgg pdianqarlr
      361 lhehfqgpmg fgtpddseaw ervqrgatag ddlwimlnrg lageyrtddg lrsdvsaetg
      421 mraayqqwkk lmteseq
//
LOCUS       WP_285144460             409 aa            linear   BCT 25-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Lelliottia wanjuensis].
ACCESSION   WP_285144460
VERSION     WP_285144460.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..409
                     /product="metal-dependent hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44738
     Region          4..>65
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
     Region          44..386
                     /region_name="Met_dep_hydrolase_A"
                     /note="Metallo-dependent hydrolases, subgroup A is part of
                     the superfamily of metallo-dependent hydrolases, a large
                     group of proteins that show conservation in their
                     3-dimensional fold (TIM barrel) and in details of their
                     active site. The vast majority of the...; cd01299"
                     /db_xref="CDD:238624"
     Site            order(62,64,228,248,319)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mslllknani fngkdnvita gnillagdki vaissqeipv gsnvqvldlk gkyvmpglid
       61 ahvhitasql dfneanvhkg ymyartfnfl rdmirrgfts vrdaggadmg ikksiddgll
      121 paprlfmscr alsqtgghgd yrhqasemvt cacslcsass iaiicdgvta vrhavreqfr
      181 vgasqikima gggiasptdk idnlqysdee iiaivdearr fnsyvmahay tpaaisrcvk
      241 ygvktiehgn lldeqsakdm hdhqaylvpt laiynafknn mssevpdsvv nkldevrlka
      301 lesirlarlh nvkiglgtdl lgdfhsfeyd eltlrsqves afdtlhsaty inaeildmkd
      361 klgvvaedaf adllvlpknp lddihlfneq ednvlmvikn geivknlla
//
LOCUS       WP_285144497             654 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidase U32 family protein [Lelliottia wanjuensis].
ACCESSION   WP_285144497
VERSION     WP_285144497.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..654
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=72668
     Region          6..307
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
     Region          444..505
                     /region_name="DUF3656"
                     /note="Collagenase; pfam12392"
                     /db_xref="CDD:463557"
ORIGIN      
        1 mrlqshhlel lspardasia reailhgada vyiggpgfga rhnasnslsd iaglvpfahr
       61 ygakvfvtln tilhddelep aqrlitdlyq tgvdalivqd mgvleldipp ielhastqcd
      121 irtvekakfl sdvgftqivl arelnlnqir dihqatdati effihgalcv aysgqcnish
      181 aqtgrsanrg dcsqacrlpy tlkddqgrvv afekhllsmk dndqtanlaq lidagvrsfk
      241 iegrykdmsy vknitahyrq mldaiiedrg dlarasagrt ehffipstdk tfhrgstdyf
      301 vnarkgdiga fdspkfiglp vgevlkvsre hldvkvtepl angdglnvmi kreivgfran
      361 tvektgenqy rvwpnempad lykarpnaal nrnldhnwqq allktsserr iavdielggw
      421 eeqliltmts edgvsvthtl dgqfeeanna dkalnslkdg vaklgqtiyy ardiqvnlpa
      481 alfvpnslln qfrretaeml dearlanypr gsrkavsvpa pvypdthlsf lanvynhkar
      541 afyhrygvql idaayeahee kgdvpvmitk hclrfafnlc pkqakgsiks wkatpmqlvn
      601 gdevltlkfd crpcemhvig kmknhifkmp qpgsvvasvs pdelmktlpk rega
//
LOCUS       WP_285144937             219 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein [Lelliottia wanjuensis].
ACCESSION   WP_285144937
VERSION     WP_285144937.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..219
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=23754
     Region          20..209
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mktlwyelak armkamgirq dalaerlnis qgainhwlng krspslqeig aifellgvsn
       61 aqlnsdgtfn vedevisepv ipqykyplfs svqaggfgev gtytrddavk wipsvkkask
      121 dafwltvtgn smtaptgstp sfpegvlllv dpaediksgd fvvaainggt dvtfkklerd
      181 agtnylvpln psyntlscde tcriigkvvk aqwaddtfk
//
LOCUS       WP_285144818             381 aa            linear   BCT 25-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Lelliottia wanjuensis].
ACCESSION   WP_285144818
VERSION     WP_285144818.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..381
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=41296
     Region          4..380
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mktlatlsvh sgefndqhga vmppiyatst faqpspgeht gyeysrsgnp trhaletaia
       61 elesgtrgya fasglaaist vlelldkdsh ivaiddvygg tyrlienvrk rstglqvswv
      121 kpgdlaalea airpdtkmiw vetptnpllk ladlegiaei arrhniisva dntfaspvih
      181 rplefgfdiv vhsatkylng hsdvvaglav vgdnrelaeq lgylqnavgg vldpfssflt
      241 lrgirtlalr vekhsanala iaqwleqhpq vekvwfpwle shphyqlare qmalpggmis
      301 vvvkgdaqqa taiirklklf tlaeslggve slvsqpysmt hasipleqrl angivpqlir
      361 lsvgiedand liadleqalk n
//
LOCUS       WP_285144889             244 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Lelliottia wanjuensis].
ACCESSION   WP_285144889
VERSION     WP_285144889.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..244
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26927
     Region          41..142
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 maqniydnpa ffegyaqlpr svhgldgape wpalksmlpn ltgksvidlg cgygwfcrsa
       61 remgaaqvmg vdisekmlar alelttdaai tyqrsdlesl qleensldlv ysslalhylp
      121 eldtlfshvq ralkpggslv fsmehpiytc asrqgwltdd ngarfwgvnq yqqegqrvsn
      181 wladgvikyh rtlgttlnal ikagltlrev newgptqaqi dawpalaeea erpmlvliaa
      241 vkpq
//
LOCUS       WP_285145286             525 aa            linear   BCT 25-DEC-2024
DEFINITION  esterase/lipase family protein [Lelliottia wanjuensis].
ACCESSION   WP_285145286
VERSION     WP_285145286.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 525)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..525
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58666
     Region          <173..>228
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mgemtgaena tslttdakek dakaviykip drvipviflp gvmgsnlmik gtnppeslwr
       61 lddngsavgg wwhrgpkdrr rlldpnkvav dqngkidndl sdshfisrrl rgwgevgyls
      121 ygqflpwlqs aldsssntke dlrtkligmn lnleigeepl dadevnlsyk ylypvhvmgy
      181 nwlesivpsa kvllskidei kslyhaksik cekvilvths mgglvarycs elshgrdlil
      241 givhgvlpai gaasayrrmk agmeykgieg kvtaevaggn aaemtavlsq spgplqllpg
      301 ieygrnwfki kdgdevyslp nanpyeeiyk ergrwwslce eklidptidi snkeqlnmaw
      361 asykrlmden iqpvieglsg ryhncthsfy gsetptlgei vwqgntgyld erfarnrrrf
      421 pkdgralndg eeifttrtva tplggggwkt gihqeytiee padfgdgtvp irsakildth
      481 lksrcklave hepayknpda qkytlwailk ivreikktsl kysdd
//
LOCUS       WP_285145321             404 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lelliottia wanjuensis].
ACCESSION   WP_285145321
VERSION     WP_285145321.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..404
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=45826
     Region          2..388
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mklnarqvda akprekaykl adgaglylev vpsgsrywrm kyrfngkekr lafgvypavs
       61 lsqaralrdd akkklaegid psfakkeekl vrdvqlnntf qsvalewhgt kvsrwsegya
      121 sdiieafnkd ifpyigqlpv nevkplvlln vlrrmesrga tekakkvrqr csevfryaiv
      181 tgraeynpaa dltsamsghe skhypfltve elpdffkala gytgsplvvl aarlliltgv
      241 rtgelrgayw sefdlekavw eipaermkmk rphlvplstq aleivqqlkv isgqyplvfp
      301 grndprktms easinqvfkr igytgkvtgh gfrhtmstil heegfntawi etqlahvdkn
      361 tirgtynhal ylegrremmq wygdyldgye hrmnsiltki vsgv
//
LOCUS       WP_285146227             464 aa            linear   BCT 25-DEC-2024
DEFINITION  nucleobase:cation symporter-2 family protein [Lelliottia
            wanjuensis].
ACCESSION   WP_285146227
VERSION     WP_285146227.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10795438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..464
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48613
     Region          30..458
                     /region_name="ncs2"
                     /note="uracil-xanthine permease; TIGR00801"
                     /db_xref="CDD:273276"
ORIGIN      
        1 msvnavespd aqpiaptqhn seliyrledr pplaqtlfaa cqhllamfva vitpallicq
       61 alglpaqdtq hiismslfas gvasiiqika wgpvgsglls iqgtsfnfva plimggtalk
      121 tggadvptmm aalfgtlmla sctemvisri lhlarrvitp lvsgvvvmii glsliqvglt
      181 sigggyaams dhtfgapknl llagvvlaii illnrqrnpy lrvaslviam aagylmawal
      241 gmlpentapt nsplimvptp lyyglgidwn lllplmlvfm itsletigdi tatsdvseqp
      301 vsgplymkrl kggvlangln sfvsavfntf pnscfgqnng viqltgvasr yvgfvvalml
      361 ivlglfpavs gfvqhipepv lggatlvmfg tiaasgvriv sreplnrrai miialslavg
      421 lgvsqqplil qfapdwvknl lssgiaaggi taivlnlvfp pekn
//
LOCUS       WP_285146242             406 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Lelliottia wanjuensis].
ACCESSION   WP_285146242
VERSION     WP_285146242.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..406
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=46471
     Region          130..401
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mtdpvyalep dyprnarmar wllfrllgdl qqgsltvreg nqtfhfgdas aalhaevevl
       61 sptlyrrllt ggslaaaeaw mdgewethql ttllqilaln gktlgrlesg frllgkpver
      121 lrhwarrnhr qqareniaah ydlgntfyaq fldeellyss alftspdqdl taaqqakmar
      181 lcdqlaltpd dhlleigtgw gamaefaarq ygcrvttttl syeqfcwaqa riaraglqdk
      241 vqvllcdyrd ltgefdklvs vemieavgkt flpeffrtcq arlrpggkma iqaitiqdqr
      301 yrsysksvdf iqryifpggf lpsitamsdl mtrhtdfvvr nlfdmgpdya rtlthwrtrf
      361 lhawqdiekl gfderfrrmw lyylgyceag fnartisvvq ltaerv
//
LOCUS       WP_285146398             709 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: putative bifunctional diguanylate
            cyclase/phosphodiesterase [Lelliottia].
ACCESSION   WP_285146398
VERSION     WP_285146398.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia
  ORGANISM  Lelliottia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 709)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 709)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Lelliottia"
                     /db_xref="taxon:1330545"
     Protein         1..709
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=79097
     Region          2..686
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mldvswdpvl iaisflvafi asfvaldsag kisgasrkaa lwwriaggat lgigvwsmhf
       61 igmlsmkmpm amsyhfwltv aslaiaiiaa tsainiavpg nslsltrwfl stlilsagvv
      121 amhytgmaal mlhddiswnm nivalsvaia ivasgaalwl afhlrhrhkg vfinrvaaaf
      181 vmglaicamh ytgmsaanfh hemdnmpggv selglsiwvs sttlvllgim liislvdshf
      241 rthrltenlr qlnkqlelka rfdaltglan rhqmdlslqd clhtsllnkk qfavmfldid
      301 hfklvndawg hqvgdellis vaqritarlt qgvtlarlgg defilllpds dddkisslam
      361 tlleeirrpf ficghtlnit lslgvslypq hgetlhelkf kadaamyhik qegrngwaiy
      421 rpemsksisa epsflqdltq alereqfelw yqptylaelk eihgfeallr whhpeqgvll
      481 psvflsslek tgliipvgvw aieqacrqlr fwteqgfsqw tlsfnlspvq feqqdifevi
      541 sstmqkynle psrlilevte stalknlers ielldafnha gftvsiddfg tgysnllmln
      601 vlpakelkid ksfidsmlen ekskkiveti ihvartmdmv vvaegietee qqltlaslgc
      661 dylqgyyfsr plpaeqvpwl vlqnksdkqi ipigknqiep plnsqknha
//
LOCUS       WP_285146490             319 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Staphylococcus aureus].
ACCESSION   WP_285146490
VERSION     WP_285146490.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     Protein         1..319
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34820
     Region          3..306
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(39,256,259)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(195,226,254,257..258,261)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mrrlfsigea lidfipnitn anlkdvqtft kqiggapcnv actvqklgqq aymitqlgnd
       61 afgdsiieti ssigvdvskv yrtneantal afvslteage rdfsfyrkps admlfepsfv
      121 ndidvnendv vhfcsvdlvd spirdahyql itktlnangt vvfdpnvrlp lwdnaedlrq
      181 tihtflplah ivkvsdeele fitgiqdene aiqslftgnv tvviytkgad gaavylkngi
      241 shyhsgykvk pvdttgagda figavisril atdvlnltql fenegeeila fsnrvaaivt
      301 tkygainslp tlqeveqaf
//
LOCUS       WP_285146651              90 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Lelliottia].
ACCESSION   WP_285146651
VERSION     WP_285146651.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia
  ORGANISM  Lelliottia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 90)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 90)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Lelliottia"
                     /db_xref="taxon:1330545"
     Protein         1..90
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9901
     Region          6..74
                     /region_name="HTH_35"
                     /note="Winged helix-turn-helix DNA-binding; pfam13693"
                     /db_xref="CDD:433408"
ORIGIN      
        1 mnhqnwhtad iiaalkkhgt slaalsrqag lssstlanal srpwpkgell iaqalntspe
       61 viwperyfde qgnpiirqmr vkkrenlsgt
//
LOCUS       WP_285146659             103 aa            linear   BCT 25-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Lelliottia
            wanjuensis].
ACCESSION   WP_285146659
VERSION     WP_285146659.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..103
                     /product="type II toxin-antitoxin system RelE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0017148 - negative regulation of
                     translation [Evidence IEA]"
                     /calculated_mol_wt=12009
     Region          6..84
                     /region_name="RelE"
                     /note="mRNA-degrading endonuclease RelE, toxin component
                     of the RelBE toxin-antitoxin system [Defense mechanisms];
                     COG2026"
                     /db_xref="CDD:441629"
ORIGIN      
        1 mtsqmrviws rpakkdlakl dslsqkriqe klnaianqns phldikkltm pgeyyrlrvg
       61 eyrviflmqg esrnecylia vkrrttttyl heenapygct iyr
//
LOCUS       WP_285146858             475 aa            linear   BCT 25-DEC-2024
DEFINITION  leucyl aminopeptidase family protein [Lelliottia wanjuensis].
ACCESSION   WP_285146858
VERSION     WP_285146858.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Drinkwater,N., Malcolm,T.R. and McGowan,S.
  TITLE     M17 aminopeptidases diversify function by moderating their
            macromolecular assemblies and active site environment
  JOURNAL   Biochimie 166, 38-51 (2019)
   PUBMED   30654132
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Lowther,W.T. and Matthews,B.W.
  TITLE     Metalloaminopeptidases: common functional themes in disparate
            structural surroundings
  JOURNAL   Chem Rev 102 (12), 4581-4608 (2002)
   PUBMED   12475202
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415720
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..475
                     /product="leucyl aminopeptidase family protein"
                     /EC_number="3.4.11.-"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0030145 - manganese ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0019538 - protein metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51312
     Region          <120..470
                     /region_name="PepB"
                     /note="Leucyl aminopeptidase [Amino acid transport and
                     metabolism]; COG0260"
                     /db_xref="CDD:440030"
ORIGIN      
        1 mitcelmttl aeakpethll arpscallpd taliremrkl tsvadtrfgc apfaritllp
       61 dalwqdaltd glvnalrplf aapvsenvvi dvshihdtvl vqvlrflfnq ahklsdlqlk
      121 kkddstlric hvaalclpeq rerlakiiqq qqaiangmia arrladtpsd rctpqyvvde
      181 aqtlcaafpa lrcevldekq iveqglgllh avgkgatcpp rllaihydgt ndgpvrcyvg
      241 kgitfdtggl wlkegagmyt mkydmcgaan vlglmltvae lklpvkimgv lalaenaigp
      301 damqpgtvar acngltvein ntdaegrlvl adaiawasqr hpqahyiidm atltgavvka
      361 lgyelsglmt qnemlrdhlt qaglrsgdev wslpldarlk kqtestiadl cntptnnaai
      421 sasaawllhh fcpptipwah ldisgtalwr eggrsvasgr pipllvehll adies
//
LOCUS       WP_285146876            1649 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Lelliottia wanjuensis].
ACCESSION   WP_285146876
VERSION     WP_285146876.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 1649)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1649)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1649)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   4  (residues 1 to 1649)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1649
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..1649
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=180388
     Region          58..1649
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mtpfrlaals lallttftlv gcdnnddkpq aaapaasatt pktpekpdae klaklasqsa
       61 gkaltlldas evqldgastl vltfsvplnp eqdfartvhv vdkksgkvdg awelapnlke
      121 lrlrhlepnr nlvvtverdl qalnkatfgi dyekaittrd ieptvgfasr gsllpgkvve
      181 glpvmalnvn nvdvnfyrvk peslasfvsq weyrnsltnw esdnllkmae lvytgrfdln
      241 parntrekll lplrdikplq qsgvyiavmn qaghynysna atlftlsdvg lsahryhnrl
      301 diftqsleng aaqsgvevll lndkgqtlaq gtsdadghak letdkeaali larkdgqttl
      361 ldlklpaldl aefdiagepg yskqffmfgp rdlyrpgetv ilngllrdsd gkplpdqpvk
      421 levlrpdgqv artvvaqpen glyrfnypld sgaqtgmwhv rantgdnqqr lwdfhvedfm
      481 permalnltg qktpvstqde vnfdvvgyyl ygapangnsl qgqlflrplr eavsalpgfq
      541 fgdiaeenls rsldevqltl ndqgrgqvst esqwkethsp lqlilqasll esggrpitrr
      601 aeqaiwpadt lpgirpqfas kavydyrtdt tvnqpivden gnasfdivya dasgakkavs
      661 dlqvrlirer rdyywnwses dgwlsqfdqk dlvegeqelt lkadetgkvt fpvewgsyrl
      721 evkapdemvs svrfwagysw qdnsdgtgaa rpdrvmlkld kpsyqpgdti klhiaapaag
      781 kgyamiesse gplwwkeidv pangldmaip vdkawkrhdl ylstlvvrpg dksksatpkr
      841 avgllhlpmg denrrlnial dtpqkmrpnq tlsvkvkasv kegsvpqkvn vlvsavdsgv
      901 lnitdydtpd pwqaffgqkr ygadiydiyg qviegqgrma alrfggdgde lkrggkppvn
      961 hvtiiaqqaq pvaldangeg titlpigdfn gelrvmaqaw teddfgsneg kvivaapvit
     1021 elntprflas gdatrltldl tnltdkpqtl nvaltasglm slegaqpqpv qldpgvrttl
     1081 fipvralegf gdgeimaqvt glqlpgetfa pqqkswkigv rpafpaqtvn tgamlnpges
     1141 wtapaqhitg fspatlqgql llsgkpplnl aryirelqay pygcleqtas glfpslytna
     1201 aqltalgikg dtddkrraai digisrllqm qrddggfalw dkngpeeywl tayvtdflvr
     1261 ageqgysvpa davnnansrl lrylqdpgmm sirysddtqa skfavqayaa lvlarqqkap
     1321 lgalreiwdr raqtgsglpl mqlgmalklm gdaprsqqal dlamktprsd sknwmadygs
     1381 qlrdnalmls lleeykllpd aqntllntls qqafsqrwls tqesnalfla grsiqtisga
     1441 wqattslsdk alssdksqvq nvtgdqlgtl qvtnsgttpl wvrldstgyp eyapqpssnv
     1501 lqierhilat dgstkslssl ksgelvlvwl evkanqnvpd alvvdllpag lelenqnlas
     1561 ssaslqdsgs evqnllnqmq qadiqhmefr ddrfvaavpv nqgqpvtlvy laravtpgty
     1621 evpvpmvesm yvpqwratga asgplivvp
//
LOCUS       WP_285147022             471 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Slackia exigua].
ACCESSION   WP_285147022
VERSION     WP_285147022.1
KEYWORDS    RefSeq.
SOURCE      Slackia exigua
  ORGANISM  Slackia exigua
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Slackia exigua"
                     /db_xref="taxon:84109"
     Protein         1..471
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49399
     Region          1..455
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mdallhivqt ineylsnyvl iflligtglv ftirtrfvqv rffgesmrrv fggfslnggr
       61 hasgmssfqa lataiaaqvg tgnivgacga ilvggpgaif wmwliaflgm stnyaeavla
      121 qktrtvdadg svhggpvyyi rsafkgaggk flagffsvai ilalgfmgsm vqsnsiastv
      181 ntafgiptwa igalivlvag filiggiqri asvaeklvpv maviylvggl valimnahei
      241 lpaiglifec afnpdasigg vtfgiiaals qgakrglfsn eagmgstpha hamanvkdph
      301 dqgvtamvgv fvdtfvvvtm talvvisaly vgdgaltvda tglaaginkt nmaqyafsef
      361 fgtgfgnafv aicllffafs tilswnlfar lnveylfgkk gvmpffvial vfiflgslls
      421 ndlvweladm fnqlmvlpna ialialsgtv aacvngrksk slaeihaede e
//
LOCUS       WP_285147147             509 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Slackia exigua].
ACCESSION   WP_285147147
VERSION     WP_285147147.1
KEYWORDS    RefSeq.
SOURCE      Slackia exigua
  ORGANISM  Slackia exigua
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Slackia exigua"
                     /db_xref="taxon:84109"
     Protein         1..509
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=54589
     Region          1..460
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mdalvavtdt idtymytyfl vflliftgly fsirtkfiqf rgfkdmirnl tehkhvpgkk
       61 svssfqalmv stasrvgtgn iagvataiav ggpgavfwmw vmatissasa fiestlaqiw
      121 kvrgengefr ggpayyiqqa lhsralgvvf aislllcfgl gfnglqtynm ssslqayipn
      181 ytqtaapmal gillavvfaf iifggtrlis ymtsvmvpim aggyilltii lsimnigelp
      241 gifativtea fdfssvvggf agsmvvqgik rglfsneagm gsapnaaasa svshpvkqgl
      301 vqtfsvfidt iiicscsavm imffvndnvd liawggatge aaltnmtlvq aamqngfgaa
      361 glhfmtlaif ffafsslign yfyaegnfky itgskpalyi frilccivif fgaqsnltla
      421 wnladifmgi qaainifvil ilgkwalaal kdyeaqkaqg idpvfvanvi pglpqtecwh
      481 vdashlddav kdekqgnpia etlladeda
//
LOCUS       WP_285147266             480 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Slackia exigua].
ACCESSION   WP_285147266
VERSION     WP_285147266.1
KEYWORDS    RefSeq.
SOURCE      Slackia exigua
  ORGANISM  Slackia exigua
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Slackia exigua"
                     /db_xref="taxon:84109"
     Protein         1..480
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51572
     Region          <347..480
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          421..472
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 msvgarshta ffrpfkligl gfwqawwmca mcspavlpld aaivgldarf aiqiatdvgy
       61 laiivaslsg kisnlramhg alpfaagsfs lgtfmlmlap yltdaslclv vnasacvcvl
      121 fgnalllllw gelwstlatg rvgrhlylsy lfafvlffla hllphpldgl lvctfplasa
      181 liyatcmhep rrtsnrrpip lkslpiasfl gmtvlvsiiy gasqhgipsa ygfgeavsln
      241 pasmlvagtc laafvlnlvi tnpesealql frnvipvmat glaltlllpp dyafagngli
      301 ilgiysldml lmlvstdvsf rtgipvaqtf gvailssrig tllgtfatia laasglwdas
      361 vlrsslivsl fllvvagmli fnqadlekvy rwmpgqddrp feeqlakmld rkcadvaday
      421 gltarerevl vllahgrtvp evceelsiar gtakhhvsni yrkvgvydrr slldvvgtig
//
LOCUS       WP_285147297             237 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor [Slackia
            exigua].
ACCESSION   WP_285147297
VERSION     WP_285147297.1
KEYWORDS    RefSeq.
SOURCE      Slackia exigua
  ORGANISM  Slackia exigua
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 237)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 237)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 237)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Slackia exigua"
                     /db_xref="taxon:84109"
     Protein         1..237
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=26326
     Region          1..233
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mlktiivdde aparselrfl ldeigdvevv aeaagvreav ekmqshpvdv lfldvsmpgv
       61 tglqfaealq rlknppavvf vtaygehale gfkvnavdyl vkpvetdrlr qavkrateyv
      121 tlhvkasqae ripvekggkk ilipidtirf vmarddyayl qtdadryfst vslaqlekrl
      181 eghgffrvhr gylvnldmve evepvqggtl lltlngteek ipvsrrrvsa lkkvlgl
//
LOCUS       WP_285147391             423 aa            linear   BCT 25-DEC-2024
DEFINITION  SufB/SufD family protein [Slackia exigua].
ACCESSION   WP_285147391
VERSION     WP_285147391.1
KEYWORDS    RefSeq.
SOURCE      Slackia exigua
  ORGANISM  Slackia exigua
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Hirabayashi,K., Yuda,E., Tanaka,N., Katayama,S., Iwasaki,K.,
            Matsumoto,T., Kurisu,G., Outten,F.W., Fukuyama,K., Takahashi,Y. and
            Wada,K.
  TITLE     Functional Dynamics Revealed by the Structure of the SufBCD
            Complex, a Novel ATP-binding Cassette (ABC) Protein That Serves as
            a Scaffold for Iron-Sulfur Cluster Biogenesis
  JOURNAL   J Biol Chem 290 (50), 29717-29731 (2015)
   PUBMED   26472926
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Sendra,M., Ollagnier de Choudens,S., Lascoux,D., Sanakis,Y. and
            Fontecave,M.
  TITLE     The SUF iron-sulfur cluster biosynthetic machinery: sulfur transfer
            from the SUFS-SUFE complex to SUFA
  JOURNAL   FEBS Lett 581 (7), 1362-1368 (2007)
   PUBMED   17350000
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Fontecave,M., Choudens,S.O., Py,B. and Barras,F.
  TITLE     Mechanisms of iron-sulfur cluster assembly: the SUF machinery
  JOURNAL   J Biol Inorg Chem 10 (7), 713-721 (2005)
   PUBMED   16211402
  REMARK    Erratum:[J Biol Inorg Chem. 2006 Jan;11(1):128]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10477762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Slackia exigua"
                     /db_xref="taxon:84109"
     Protein         1..423
                     /product="SufB/SufD family protein"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=44394
     Region          170..389
                     /region_name="SUFBD"
                     /note="SUF system FeS cluster assembly, SufBD; pfam01458"
                     /db_xref="CDD:460219"
ORIGIN      
        1 mdaitlqnas pmpaptwhrl smngadietp adliqahdai ievpegesal svtavaltdl
       61 egdafdtavd alsartyatr isaqdlagea dddtdgvrdt aysryqidaa eteraasvaa
      121 afetgmgada rafllqaage vivveapegs egaatvrlng idgavnttav divahegahv
      181 diaiafdtpt egvgaigatl rvfagkdavv rvttiqtadd swqcfddegy vldesakvev
      241 rhtvlgages ytglacdlrg tssdidvdtr ylghgeneld fnyvirhhgq rtmselnang
      301 vlagesvktl rgtidlirgc kgangheset vliaddgahn rtvpvilcse ddvagnhgat
      361 ighirpeqkf ylacrglspd aaeamfaraq ienaeinavd etvrasvvrl gktllgdyeg
      421 veq
//
LOCUS       WP_285147402             285 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Slackia exigua].
ACCESSION   WP_285147402
VERSION     WP_285147402.1
KEYWORDS    RefSeq.
SOURCE      Slackia exigua
  ORGANISM  Slackia exigua
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Slackia exigua"
                     /db_xref="taxon:84109"
     Protein         1..285
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30369
     Region          69..279
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(74..75,77..78,81..82,115,119..120,123..124,142,146,
                     153,156..157,162,177,181..182,184..186,188..189,192..193,
                     196..197,218..219,221..223,225..227,229..230,232..233,237,
                     240..241,247,249)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(180,184,187..188,190..191,232,235..236,238..243,
                     246..248,251,253)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(201..208,220,223..224,227)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mreggaeavc saprmrsalp pwllasedfv pphdrdryis gsmssiamvl sqfrlddgas
       61 apfsptapvk lfvafacilm tslstnfvft livlagvlar lcllpaahlk rvvgvvlvss
      121 altfalmvpa affgqphsav llsvkvlvsv sialtmavtt pynqltsalr tfrvpslfil
      181 tmdlalkniv rlgevalevl talklrsvgr narkgdavgg vsgvvflksk esaevtfdam
      241 rcrgfdgeye thakgparpa vdacwiclva claaafmyfq glmpr
//
LOCUS       WP_285147537             442 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Slackia exigua].
ACCESSION   WP_285147537
VERSION     WP_285147537.1
KEYWORDS    RefSeq.
SOURCE      Slackia exigua
  ORGANISM  Slackia exigua
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Slackia exigua"
                     /db_xref="taxon:84109"
     Protein         1..442
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=47338
     Region          <161..442
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mldrlraqfi vitmalvttv viasfagiva ieyqhgikav healdagigh daqaqdkdge
       61 rmppdddrdd aedrddehgd rdeegylppr iggparqggf ipvavyaisn dgtatmvssr
      121 tnasidesie sevcktvlss sdgygslpve glyykkmtte dgalvafadm asasgwrrta
      181 atmsiigvaa lgallvitvf larwalrpve kawraqkqfv adashelktp ltvmlantsi
      241 llrhpdhtia eesqwlestr iegermqslv gdmltlakve ssgavplcgp vdisemtdgl
      301 ilqfesiafe rsidltcdie gdiivsgdag klekmvatll enackyagad gqvhvvlars
      361 arsglatlai rnsgdaipaa dlphifdrfy rsnearthtd ddmsfglgla iarsiarahh
      421 gdikaestaa dgtvftvtlp lr
//
LOCUS       WP_285147510             343 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Slackia exigua].
ACCESSION   WP_285147510
VERSION     WP_285147510.1
KEYWORDS    RefSeq.
SOURCE      Slackia exigua
  ORGANISM  Slackia exigua
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Slackia exigua"
                     /db_xref="taxon:84109"
     Protein         1..343
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39281
     Region          1..199
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkaisfaipc ynsaaymdtc iesimacvde rddieiiivd dgstkddtav radewqkrhp
       61 svikavhqpn gghgeavntg lanatglyfk vvdsddwldr dslekvldyv rsqigvsept
      121 dlvianyvye kvhegthttm ryrnvfpter qfgwedtkgf rqsqyllmhs viyraqllrd
      181 cglklpkhtf yvdnifvyvp lphvktmyyl dadlyryfig redqsvnqdv mysrrdqqvr
      241 vtramidavd ldadvpsekl hrymcaylsm mmaissvflr mhrtpendaa leslwkylav
      301 rrpqlapkir hslinaalnl pgeagrrvgl agyavarrif kfn
//
LOCUS       WP_285147617             303 aa            linear   BCT 25-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Slackia exigua].
ACCESSION   WP_285147617
VERSION     WP_285147617.1
KEYWORDS    RefSeq.
SOURCE      Slackia exigua
  ORGANISM  Slackia exigua
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Slackia exigua"
                     /db_xref="taxon:84109"
     Protein         1..303
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=31712
     Region          25..299
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mafgrtvfig npaanngaga adiaalesla qanaasfssl efirtagpgd aaararavea
       61 dlvvavggdg tihevvsglm erppadrasl gvipcgngnd fartlgmpvg vaqafpalla
      121 aeerpldvgl cngvpfmqtl sfgldaaial gthdrrvrtg qtgtslfvse gieqllhhrd
      181 eyafeaafdg maergrmmmf avqngrtygg gfdicpeaep sdgmldicya saplglvpal
      241 llflrakggn hvgsrtmtfh rvraldvafd psppaqidge riespryrvq iepaalsvlf
      301 arr
//
LOCUS       WP_285147843             211 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Slackia exigua].
ACCESSION   WP_285147843
VERSION     WP_285147843.1
KEYWORDS    RefSeq.
SOURCE      Slackia exigua
  ORGANISM  Slackia exigua
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Slackia exigua"
                     /db_xref="taxon:84109"
     Protein         1..211
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22786
     Region          <8..206
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(102,106,109..110,112..113,158,161..162,164..169,
                     172..174,178,180)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(123..130,146,149..150,153)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mndgrwtird vistvlisml miviqiainl vcmpndfvsm vlstsfsafa cgvvyvllat
       61 rmgkhgctli yatmagwdlv ttppgdlsaf lskmhapval ilgvlvvfrf fptmaselss
      121 ivrsmrnrsl taparmiahp aasgeyvivp lmlrclqiad qltvsaiarg aerngirssy
      181 ygrpcearda iwlavwmagt alfllvtgak p
//
LOCUS       WP_285147848             106 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Slackia exigua].
ACCESSION   WP_285147848
VERSION     WP_285147848.1
KEYWORDS    RefSeq.
SOURCE      Slackia exigua
  ORGANISM  Slackia exigua
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Slackia exigua"
                     /db_xref="taxon:84109"
     Protein         1..106
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11676
     Region          22..97
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(26..27,29,32,35..36,39..40,43,73,92..93,95..97,
                     99..101)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(27..28,32..34,47..49,58..61,63..64,67..68,70..71,
                     77..79,84..86)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(47,50,92)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mseglegiea getldeemly dladlfkvfa dttrikilya lmetdlcvad lasvvgvsqs
       61 aashqlrllk qahlvkfqrd gkqiiyslsd dhvytmlsqg lthice
//
LOCUS       WP_285147857             852 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Slackia exigua].
ACCESSION   WP_285147857
VERSION     WP_285147857.1
KEYWORDS    RefSeq.
SOURCE      Slackia exigua
  ORGANISM  Slackia exigua
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
REFERENCE   1  (residues 1 to 852)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 852)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..852
                     /organism="Slackia exigua"
                     /db_xref="taxon:84109"
     Protein         1..852
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=91889
     Region          <619..770
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          629..657
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(630,633..634,637..638,640,664,667..668,671..672,
                     674..675,701,704..705,708..709,712)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          662..692
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          700..726
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mpkraiklsv lgkyqsilpv pgqdpaksya vvwngcrqpe ggwgylmemt gkregmllaw
       61 ldagncayac deplaarpar tpdlvlsglv grgdgsvlir stagsdmlpv ggyevsagat
      121 gtllrfrdsy meigpydqgf ydvrtflgvs flayvhlpre rasqagdaat iagiledalp
      181 palplpdvld afalrpydsa svsgferyas eallaagarr irpiaarhdl rlgliwltgl
      241 swihvydeld dqematvlav egalnrlrli glaaraidga gmaslfdega cciedwrcir
      301 sicqsileva rkgdegygls elyghscakg gewdvrmrfa saverlalpf rmgysfdcda
      361 asgifaircs lpdaeafpdr wfvrsshgas gargdgargt wtdvsenrnw arsayavrls
      421 allaacafts svgimkavvn asgpaaretd evelsmsfdr lsfmpvcttg prldeiasee
      481 ltwdapslin lvrpvechvs fdasgtlrlv dpidvdlgar rvdiavddrp ipeeaknllh
      541 adkvcdldif letdeerlak arvreavqda edsplvasal leeildqapv nledgrtply
      601 cqdlagreiv glmtsndger fvnvpdsvyd atlhlsriyr smgdaegsig raealvsmsp
      661 stvrsylelv navveagdfq rseeilrkai avcvsaeerq vvkyrlafal wqngkldhal
      721 alyqtvgsqg pvagaareem relmgemgre evfpererda llrraglrdi ppqeaasriv
      781 gaaivlldan lilpahalvs vlaefsgsdv ifsvarslvs tferahgqgd sdtaadavge
      841 glgdrddsva gg
//
LOCUS       WP_285147919             232 aa            linear   BCT 25-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Slackia exigua].
ACCESSION   WP_285147919
VERSION     WP_285147919.1
KEYWORDS    RefSeq.
SOURCE      Slackia exigua
  ORGANISM  Slackia exigua
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Slackia exigua"
                     /db_xref="taxon:84109"
     Protein         1..232
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24235
     Region          5..211
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(16..17,19..20,23..24,59,63..64,67..68,82,86,93,
                     96..97,109,125,129..130,132..134,136..137,140..141,
                     144..145,170..171,173..175,177..179,181..182,184..185,189,
                     192..193,199,201)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(128,132,135..136,138..139,184,187..188,190..195,
                     198..200,204)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(149..156,172,175..176,179)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mnerrhidar yaiawsfcfs vgvlsthgwr glgafalmla gaciasrvpa rrlfassvpm
       61 lilalfviga hastdplega ryaakaylla lgaialvlac ppdsiaaame rfaapfrrlr
      121 lpvddfcmmt sialgaipdl hiqlarlvaa qasrgaafda gpphtrvlaw grafvalvvv
      181 afrraatlad amearcfgag vrssirlsrs dlaavalava ggaamlacgi fl
//
LOCUS       WP_285148121             470 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Slackia exigua].
ACCESSION   WP_285148121
VERSION     WP_285148121.1
KEYWORDS    RefSeq.
SOURCE      Slackia exigua
  ORGANISM  Slackia exigua
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Slackia exigua"
                     /db_xref="taxon:84109"
     Protein         1..470
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=49925
     Region          184..464
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mnlgipvres grivafavva tmaalvvnli maavgvvmfg gssglnpdep saervaaald
       61 rtggqgstyv laddvadald aqdewamvvd atgevvwsrn vpdalnrqyg lqdvasfsrw
      121 ylddypvttw vyedgimvvg appytiwkyp isfpvdslgt ileflalltl vdfvlavvvg
      181 gafarrrwkr rdeartewia avshdvrtpl svamaeasal adargasved rrraerivgk
      241 vgevsalisd lnaanrlrya mqpvdasdvc iaavvrgvvv damndeesar meassaasar
      301 nrvagetlre saadvpsysr dadgmgavea gahafelave pdaegavvrg sekllrrmva
      361 nlvgnavrhn prgcsiaasv rvkpgifgsp igmrcvieir dggvgfgade lsllnrrpgr
      421 dmpehglglv ivrriahahg grarffnnes ggsacqvvlp aqapscrkrs
//
LOCUS       WP_285148191             300 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Lelliottia wanjuensis].
ACCESSION   WP_285148191
VERSION     WP_285148191.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..300
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34728
     Region          10..288
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mttparsrsa erlvdilmel hlngvvnrrd lmhkfkiter tvyrdlnala pivqhtgngl
       61 yrlihaqqna sgqglhnava nllnadiyfp drgtafwqsl earveenhil ilsndaehtv
      121 qndirrhlta ieksikerhv cqmvykdktr linpyklink kniwylqate ngrlksfsls
      181 qinwldiqke tftpdadtae lleknldpwv sedtfevkif tnniishyft rrdllpdqev
      241 iaesddgvti rcqaahenqi lplifywlpn iqvlepqwlr dklfetlegy mttapaevle
//
LOCUS       WP_285148272             327 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease [Lelliottia].
ACCESSION   WP_285148272
VERSION     WP_285148272.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia
  ORGANISM  Lelliottia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Lelliottia"
                     /db_xref="taxon:1330545"
     Protein         1..327
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33462
     Region          22..325
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mmrtslasvv flalllmgai vhlglgarfi apqavvqafl afdprnfdhn viinlrllrl
       61 aaalttgaal gvagvllqav irnslgephi lglnagaala vvitsalgla lpvgrpliaa
      121 agaailfllv ltlssagrtg ltpmkvtlcg valsafassi taavlildeq tllamrtwla
      181 gdlaglswat tqnaawvtav glalavwisp slnmlalgdr maqglgvslv rmrilaliai
      241 allcgaavsi agpigfiglv vpqiirrlvs vdlrvmvpls accgalvlll adiaartlft
      301 phelatgvmt alvgapvfil maarmfr
//
LOCUS       WP_285148303             410 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein [Lelliottia
            wanjuensis].
ACCESSION   WP_285148303
VERSION     WP_285148303.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Porat,A., Cho,S.H. and Beckwith,J.
  TITLE     The unusual transmembrane electron transporter DsbD and its
            homologues: a bacterial family of disulfide reductases
  JOURNAL   Res Microbiol 155 (8), 617-622 (2004)
   PUBMED   15380548
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Kimball,R.A., Martin,L. and Saier,M.H. Jr.
  TITLE     Reversing transmembrane electron flow: the DsbD and DsbB protein
            families
  JOURNAL   J Mol Microbiol Biotechnol 5 (3), 133-149 (2003)
   PUBMED   12766342
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..410
                     /product="protein-disulfide reductase DsbD family protein"
                     /EC_number="1.8.-.-"
                     /EC_number="1.8.1.8"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=42730
     Region          3..406
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 mltaifaafl ggvilnfmpc vfpvislkal gimrhqgdta sartegfgfl lgviftmmal
       61 aalllalrag gtavgwgfql qsplviavla liilgaalnl lgvfevglsl qrageisvgr
      121 gafvrsaltg alaiivatpc sapfmagavg yalvqppavs laiffalalg faapftlvsl
      181 fpaiarrlpr pgawmdvlkr glafpmlgaf awlvwvlaqq agttalavml asavvvsfaa
      241 wlygiaqrrr ylgksyrvll aftvaffvva iaplpkaint gsaqpatlva envapvkwsp
      301 qsveamrghg kaifvnftas wcitcqvndr tslstqavke amartgavym vadstkfnad
      361 iddainafgq gglplyvvyp adgsapkvlp qvltpsivvn alnqaadkka
//
LOCUS       WP_285148383             371 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Slackia exigua].
ACCESSION   WP_285148383
VERSION     WP_285148383.1
KEYWORDS    RefSeq.
SOURCE      Slackia exigua
  ORGANISM  Slackia exigua
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Slackia exigua"
                     /db_xref="taxon:84109"
     Protein         1..371
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42583
     Region          278..368
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mnqlidrgar mlidattesl hpleqiffel kysptiemaa slhamecpkh fpsqkdrvda
       61 trakmgpdlh sefnciaret lgfapvmdli dhlersdidn ialfldrlad vdpvefaygy
      121 fsglipkrti rallkdpqar ipegealghy fpekslrayf eiqdelrpri asflkaywtd
      181 vfarewdhig aveirrlsee khalaaighr aylagchagi svdddavrlq ksmgftipyr
      241 sikkveivis ayvrphlmmn cfdnvltiyk gvdmaisdre tsfaevekfv kaissvtklk
      301 ilfelnrqeq ttkelaerfd vasssisehl kalreaelvy pqrvqnqvyy rflhenydaq
      361 ltylkdafre r
//
LOCUS       WP_285148412              59 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Slackia exigua].
ACCESSION   WP_285148412
VERSION     WP_285148412.1
KEYWORDS    RefSeq.
SOURCE      Slackia exigua
  ORGANISM  Slackia exigua
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
REFERENCE   1  (residues 1 to 59)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..59
                     /organism="Slackia exigua"
                     /db_xref="taxon:84109"
     Protein         1..59
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=6356
     Region          <14..54
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mcgeaeggtl qrggcsvpyi aenlriadnt vkyhcksicr kpgvrsrqel fdlldgrss
//
LOCUS       WP_285148388             345 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease [Lelliottia].
ACCESSION   WP_285148388
VERSION     WP_285148388.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia
  ORGANISM  Lelliottia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Lelliottia"
                     /db_xref="taxon:1330545"
     Protein         1..345
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36253
     Region          39..342
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mraelrplrw grfstlirpk alawlaglma liaallvlgl thgtlpipts dvaralfype
       61 vlsadaryiv qeirlprllm allcgamlgm agaamqsitr ngladpglig vkegcsvavl
      121 llifqfpals vlwrpvvgma gglltallvv llardisrpr filigigvsw afaagmgvfm
      181 ttadvrdvqt allwlagslh aanwtlvsva agwalpafal llftaraadv allgnhtatg
      241 lgvrisrlal lrvlapvllt aacvscvgsi gfvgliaphm arfllrggqt tllvgsaalg
      301 allvlladni grlaflplql pagivislig gpfflvllwa rrdrf
//
LOCUS       WP_285148436             375 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lelliottia wanjuensis].
ACCESSION   WP_285148436
VERSION     WP_285148436.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..375
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42924
     Region          7..>64
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          189..287
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 msmtfygerl rlarllkgyt lqelgdavav trqsihqyes darapahdir nalaellqvs
       61 pkffeyplag dvkpeqchfr krqttpvgvk ervqsystil eqlvselyeh ldlpenrfnl
      121 idnekipelt apviekiaeg arvrwgltdd apidnminvv enqgaivttf dgvsdkvdal
      181 sinrkypiii rntakesvcr mrfdiahecg hlvmhdgiet gckkteread afasaflfpr
      241 ksfarefptc itsrgtidwk kvynlklrwk msaraiiyra hflgfinaqq yrtanvwfsq
      301 trqtkkekyd dsipmeephi lqesllvlke qlgisfemla eklcvkpill aeisgvdytq
      361 nqnddfdnvv vpfkf
//
LOCUS       WP_285148550             246 aa            linear   BCT 25-DEC-2024
DEFINITION  AcrVA2 family anti-CRISPR protein, partial [Lelliottia wanjuensis].
ACCESSION   WP_285148550
VERSION     WP_285148550.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Koonin,E.V. and Makarova,K.S.
  TITLE     Anti-CRISPRs on the march
  JOURNAL   Science 362 (6411), 156-157 (2018)
   PUBMED   30309933
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Marino,N.D., Zhang,J.Y., Borges,A.L., Sousa,A.A., Leon,L.M.,
            Rauch,B.J., Walton,R.T., Berry,J.D., Joung,J.K., Kleinstiver,B.P.
            and Bondy-Denomy,J.
  TITLE     Discovery of widespread type I and type V CRISPR-Cas inhibitors
  JOURNAL   Science 362 (6411), 240-242 (2018)
   PUBMED   30190308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19225148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..>246
                     /product="AcrVA2 family anti-CRISPR protein"
                     /GO_function="GO:0140721 - nuclease inhibitor activity
                     [Evidence IEA]"
     Region          3..246
                     /region_name="AcrVA2-like"
                     /note="Anti-CRISPR type V subtype A2 and similar proteins;
                     cd22987"
                     /db_xref="CDD:467859"
     Site            order(6,86,106,129..130,132..133)
                     /site_type="other"
                     /note="putative Cas12a binding site [polypeptide binding]"
                     /db_xref="CDD:467859"
     Site            order(33,36,72..74,128,132,135)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467859"
ORIGIN      
        1 mlmkrfpphi vymalaawrt gktllhcdes lfrilgetrq tdalsgemlr rlpfwgfwld
       61 fpadtvfaeg qgalmgafft ladhdnqtda llaltlaqdp lsrehiplgm eylaltnpvs
      121 taisqqdkgi hgfwnavlpv lfwlcsense wgrqgkpvrp aprrvgkhqr fippdkpvqi
      181 fagvragsal rqaprvseas tsverssaph rrlrphirka hwqsywkgkp tqgeeksmll
      241 kwkppq
//
LOCUS       WP_285148741             472 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Slackia exigua].
ACCESSION   WP_285148741
VERSION     WP_285148741.1
KEYWORDS    RefSeq.
SOURCE      Slackia exigua
  ORGANISM  Slackia exigua
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Slackia exigua"
                     /db_xref="taxon:84109"
     Protein         1..472
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49049
     Region          1..452
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mdiirvlnsi datvwgpami vlllgthlfm tvrtgfiqrk lplaikmsvt dddgaegdvs
       61 qfgalatala gtigtgsivg vatavlaggp gavfwmwltg vfgmatkyse vyasvkyrvk
      121 dsggemlgga myawerafkr adgttpwwak lgavlfcvfa viatlgtgsa vqsaamtgii
      181 essfpdlpaw giglaiavsv alvifggvrs iskvceklvp vmavayvggc lvmlawnapy
      241 igdafatiie caftskaafg gavgsgimia lqfgcarglf snesglgtap ivaaaaatkn
      301 parqaliamt gtfwstvvic litgvvvvsa llahpeimaa gsisegaalv saafstlpyv
      361 gtpvlvlgmv sfaystilgw syygnrcity lfgrkairpy qivyvivgfl gaigvgdvvw
      421 tisdignafm avpniimvla lsaliaketr hyvydgnlde acedeiplie sk
//
LOCUS       WP_285148798             409 aa            linear   BCT 25-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Lelliottia wanjuensis].
ACCESSION   WP_285148798
VERSION     WP_285148798.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..409
                     /product="metal-dependent hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44680
     Region          4..>65
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
     Region          44..386
                     /region_name="Met_dep_hydrolase_A"
                     /note="Metallo-dependent hydrolases, subgroup A is part of
                     the superfamily of metallo-dependent hydrolases, a large
                     group of proteins that show conservation in their
                     3-dimensional fold (TIM barrel) and in details of their
                     active site. The vast majority of the...; cd01299"
                     /db_xref="CDD:238624"
     Site            order(62,64,228,248,319)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mslllknani fngkdnvita gnillagdki vaissqaipv gsnvqvldlk gkyvmpglid
       61 ahvhitasql dfneanvhkg ymyartfnfl rdmirrgfts vrdaggadmg ikksiddgll
      121 paprlfmscr alsqtgghgd yrhqasemvt cacslcsass iaiicdgvta vrhavreqfr
      181 vgasqikima gggiasptdk idnlqysdee iiaivdearr fnsyvmahay tpaaisrcvk
      241 ygvktiehgn lldeqsakdm hdhqaylvpt laiynafknn mssevpdsvv nkldevrlka
      301 lesirlarlh nvkiglgtdl lgdfhsfeyd eltlrsqves afdtlhsaty inaeildmkd
      361 klgvvaedaf adllvlpknp lddihlfneq ednvlmvikn geivknlla
//
LOCUS       WP_285149012             437 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Lelliottia
            wanjuensis].
ACCESSION   WP_285149012
VERSION     WP_285149012.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 437)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468625
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..437
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=48772
     Region          32..431
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
     Region          203..433
                     /region_name="RHO_alpha_C_AntDO-like"
                     /note="C-terminal catalytic domain of the oxygenase alpha
                     subunit of Pseudomonas resinovorans strain CA10
                     anthranilate 1,2-dioxygenase and related aromatic ring
                     hydroxylating dioxygenases; cd08879"
                     /db_xref="CDD:176888"
     Site            order(209..210,214,217..218,221,223..224,226,228,336..337,
                     378..380,382..386,397..400,421,424,428)
                     /site_type="other"
                     /note="putative alpha subunit interface [polypeptide
                     binding]"
                     /db_xref="CDD:176888"
     Site            order(218..219,221..222,224..225,229,310..311,313,321,323,
                     328,362,365..366,372..373,376)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176888"
     Site            order(218..219,221..222,224..225,229,310..311,313,321,323,
                     328,362,365..366,372..373)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:176888"
     Site            order(224,229,376)
                     /site_type="other"
                     /note="Fe binding site [ion binding]"
                     /db_xref="CDD:176888"
ORIGIN      
        1 mncdhlitik nidttphslp tsadiaglvq sdrvhtslyt sdslfqleld rifsktwvwv
       61 ahaseipdtg sfkttelgtq pvivvrdrkg tvhtllnrcr hraatvcehr sgktnsfvcp
      121 yhgwgyaldg slrgvphpes yadqlekgel glvslrteqy agmifatfne qiepledflg
      181 aakkwmdlfm kqgagypikt gpahrfrfpg nwkiqlentt dgyhfpvvhr sflssvdkqt
      241 eemlnfvdgs gyvedlgngh svmvmipelv dleanldapi perfealaea lradhdeqqv
      301 rrivravggs gfnlnifpni acsmaffrvl qpvsvnetei hhavitmdgg peianqarlr
      361 lhehfqgpmg fgtpddseaw ervqrgatag ddlwimlnrg lageyrtddg lrsdvsaetg
      421 mraayqqwkk lmteseq
//
LOCUS       WP_285149283             325 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein [Lelliottia wanjuensis].
ACCESSION   WP_285149283
VERSION     WP_285149283.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..325
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35769
     Region          1..325
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mtktnlvtgf lgsgkttsil hllankdpae kwailvnefg eigidgalla dsgamvkeip
       61 ggcmccvngl pmqvglntll rqgkpdrlii eptglghpkq ildlltapvy epwidlratl
      121 cildprqlld ekvvknenfr dqlasadiiv ankedrasqe srdafefwwq nfggdrqfvm
      181 atqgkidnal ldqprrnvae lpasaahshi hapqkglaal slpehqrwrr slnsgqghqa
      241 cgwifdadtc fdtigilewa rlapvdrvkg vmrtqdglvr inrqgadffi etqnvappds
      301 rielisavnt dwnalqasll klrls
//
LOCUS       WP_285149377             385 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal-phosphate-dependent aminotransferase family protein
            [Staphylococcus aureus].
ACCESSION   WP_285149377
VERSION     WP_285149377.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Koper,K., Han,S.W., Kothadia,R., Salamon,H., Yoshikuni,Y. and
            Maeda,H.A.
  TITLE     Multisubstrate specificity shaped the complex evolution of the
            aminotransferase family across the tree of life
  JOURNAL   Proc Natl Acad Sci U S A 121 (26), e2405524121 (2024)
   PUBMED   38885378
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Koper,K., Han,S.W., Pastor,D.C., Yoshikuni,Y. and Maeda,H.A.
  TITLE     Evolutionary origin and functional diversification of
            aminotransferases
  JOURNAL   J Biol Chem 298 (8), 102122 (2022)
   PUBMED   35697072
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     Protein         1..385
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42672
     Region          6..383
                     /region_name="PucG"
                     /note="Archaeal aspartate aminotransferase or a related
                     aminotransferase, includes purine catabolism protein PucG
                     [Amino acid transport and metabolism, Nucleotide transport
                     and metabolism]; COG0075"
                     /db_xref="CDD:439845"
ORIGIN      
        1 myyhqplllt pgptpvpdai mreiqapmvg hrskdfedia qqafqglkpi fgsqndvlil
       61 tssgtsvlea smlnivnped hfvvivsgaf gnrfkqiaqt yyknvhiydv twgeavdvkd
      121 finylstldv evkavfsqyc etsttmlhpi helgnainqf nsniyfvvdg vscigavdvd
      181 inkdkidvlv sgsqkaimlp pglafvaysh rakerfkevt tpkfyldlnk yissqadnst
      241 pftpnvslfr gvnayvetvk aegfnhviar hyairnalrs alkaldltll vndkdasptv
      301 tafkpntnev kiikdelknr fkitiaggqg hlkgqilrig hmgkispfdi lsvvsaleii
      361 ltehrkvnyi gkgiskymev iheai
//
LOCUS       WP_285149619             105 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Lelliottia wanjuensis].
ACCESSION   WP_285149619
VERSION     WP_285149619.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 105)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 105)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 105)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..105
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11281
     Region          8..97
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msdlnllqsq aesaaallkt lshpqrllil cmltgnpgte agelsrlsgl spsatsqhla
       61 rmkseglieg irqarfvrys ikneaifavv qtlkniycpg eedvl
//
LOCUS       WP_285149852             589 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Lelliottia wanjuensis].
ACCESSION   WP_285149852
VERSION     WP_285149852.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 589)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 589)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 589)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 589)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 589)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..589
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=64721
     Region          1..584
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mqalqrkwqs lprgvvvlit alviyiplsf iviqsflsap ffspskewsl esfgfiftdp
       61 dfykalrsgf ilafglvaia iplggvlafl mvrtdlpgrr lieplilvpi fvspmvlgfg
      121 yvvaagpvgf fslwaqslig fvpwniydms sivviaglth vphaylyiss alrsvgsdve
      181 eaariagasp lqvmtavslp mvrpsilyav vllfflglev fglmlvlgdp egnmvlatyl
      241 yqltnklgtp syhlmaavav vlicitiplv mlqrrlmrta nrfvtmkgka sqaralplgk
      301 wrwvagavva fwltvtigvp llgvvlrafi snwgvgvsvw delsintfrt iwqqpnllra
      361 ivnsmaigvf ggalavvcyl figiamhrkp dnttrfldys vlvpravpgl laglaflwvf
      421 lflpmwldna lktgwlsgmp wsqwlrdnli vwlrslrsti fsvwlaytvv wmayglrlis
      481 stllqvapel eeaarstgat rgqitrhvti plsrygligs wllmflifer eystgvylls
      541 pgtetigsml vslwaagaid ivaalsfini llvvvglgia lrfgvklhd
//
LOCUS       WP_285149857             524 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Lelliottia wanjuensis].
ACCESSION   WP_285149857
VERSION     WP_285149857.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 524)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 524)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 524)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..524
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56677
     Region          20..520
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 msvvnvseks iaprpvsqhr papvmvimav vfsllslipp afivyigfdt gwetvkalif
       61 rprvaellsn tlllvlvtvp lcvfvgvmla wlterttlag rrlwsmlava plaipafvqs
      121 yawvsavpsi hglsagvfls vlayypfiyl pvaavlrrld ptledvaasl gtpplrvffr
      181 ivlpqlrlpv wggallvalh llaeyglyam irfdtfttai ydqfqstfsg paanmlagvl
      241 alcclailtl egatrgkary arvgagapre qkrwrlnvlf qvlgqmfafa villafvvpl
      301 avltrwlwlg gienwnqanl wmslqqtlvl aasgaaltll asvpiawlsv rhprplfrml
      361 egcnyftssl pgivvalalv tvtihyarpi yqteitlfla yllmfapral inlragiaqa
      421 pvelenvars lgktpatalw svtlrlaapg aaagaalvfl gvcneltatl llsplgtrtl
      481 stgfwaltse idyvaaapya llmilislpl tgilyvqsqk lagl
//
LOCUS       WP_285149878             217 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lelliottia wanjuensis].
ACCESSION   WP_285149878
VERSION     WP_285149878.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10648172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..217
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24975
     Region          139..194
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 miniilndrd sfyrlgmqtl fsalfpaefd nriafthhln pqsvavadvi vmglshgeis
       61 ichpvlhark qnsliiglye gnappycdpl plcfkniifv nrteplpeik krflrswenc
      121 rilpmiprqw kcqdcrhktl spqqinvanh yyqgataeqi sqilcisikt vfthkrmimg
      181 kfnlhsdyql ftlfnvikal nndtpdflta hrelkra
//
LOCUS       WP_285150095             234 aa            linear   BCT 25-DEC-2024
DEFINITION  XRE family transcriptional regulator [Lelliottia wanjuensis].
ACCESSION   WP_285150095
VERSION     WP_285150095.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..234
                     /product="XRE family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26196
     Region          1..68
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          100..228
                     /region_name="COG2932"
                     /note="Phage repressor protein C, contains Cro/C1-type HTH
                     and peptisase s24 domains [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442176"
ORIGIN      
        1 msgiaerirh llareglkqk dlaeqlstsa qtvnnwikrd sisreaaqqi aerygysldw
       61 llngkgepkq rdggippese wgsvetwddk tpvnddevev pffkdiefac gagrtgdedy
      121 ngyklrfsks tlrrigastd ghgiicfpar gnsmepnipd gttvavnted kkivdgkmya
      181 isedgwkrik llyrtgpetv sirsynsaeh ppeekplgni evigrvfwws vldy
//
LOCUS       WP_285150317             104 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Lelliottia wanjuensis].
ACCESSION   WP_285150317
VERSION     WP_285150317.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..104
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11529
     Region          36..94
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mfilsisdll grvkqpdsis venttmplsi lqphipddpl vdmkyfarag gfslshgydl
       61 lkrgeiaqpi rigrssrwrt syvnawiaer ekqsgtnqsv akea
//
LOCUS       WP_285150367             636 aa            linear   BCT 25-DEC-2024
DEFINITION  BglG family transcription antiterminator [Lelliottia wanjuensis].
ACCESSION   WP_285150367
VERSION     WP_285150367.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..636
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=72367
     Region          14..608
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mrfpnqrlaq lfdllqnetl pqdelaqrls vstrtvradi talnallagh gaqfilsrgn
       61 gyqlkiddaa ryqslqdsrp ralriprtgq ervhylvvrf ltsafslkle dladewfvsr
      121 atlqsdmaev rewfqryslt letrprhgmk lfgsemsira cltdllwela qqdslnplvt
      181 evalnagvpe qlvgilhdtl trhhirltde gelfvrlysa vsvrrisegy plpefnaedv
      241 eenvrdaard iaaaiarlad kvlspseenw lcvhiaarqi qeiapsaina dddealvnyi
      301 lryinthyny nllndaqlha dllthiktmi trvryqimip nplldnikqh ypmawdmtla
      361 avsgwgkytp yviseneigf lvlhigvgle rhynvgyqrq prvllvcdag namarmieav
      421 larkypqvev trtvtlreye laesisedfv istariseka kpvvqiapfp tdyqleqigk
      481 lvlvdrtrpw mlekyfdadh frvidsgmdq qtlfqelcgq lrqegfvdae fldsvverea
      541 ivstmlgdgi alphslglla qktvvytvla pqgikwgdet ahvifllais kseyeeamai
      601 ydifvtflre ramtrlcncr dftefkavam eslsrf
//
LOCUS       WP_285148535             313 aa            linear   BCT 25-DEC-2024
DEFINITION  AcrVA2 family anti-CRISPR protein, partial [Lelliottia wanjuensis].
ACCESSION   WP_285148535
VERSION     WP_285148535.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Koonin,E.V. and Makarova,K.S.
  TITLE     Anti-CRISPRs on the march
  JOURNAL   Science 362 (6411), 156-157 (2018)
   PUBMED   30309933
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Marino,N.D., Zhang,J.Y., Borges,A.L., Sousa,A.A., Leon,L.M.,
            Rauch,B.J., Walton,R.T., Berry,J.D., Joung,J.K., Kleinstiver,B.P.
            and Bondy-Denomy,J.
  TITLE     Discovery of widespread type I and type V CRISPR-Cas inhibitors
  JOURNAL   Science 362 (6411), 240-242 (2018)
   PUBMED   30190308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19225148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..>313
                     /product="AcrVA2 family anti-CRISPR protein"
                     /GO_function="GO:0140721 - nuclease inhibitor activity
                     [Evidence IEA]"
     Region          70..313
                     /region_name="AcrVA2-like"
                     /note="Anti-CRISPR type V subtype A2 and similar proteins;
                     cd22987"
                     /db_xref="CDD:467859"
     Site            order(73,153,173,196..197,199..200)
                     /site_type="other"
                     /note="putative Cas12a binding site [polypeptide binding]"
                     /db_xref="CDD:467859"
     Site            order(100,103,139..141,195,199,202)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467859"
ORIGIN      
        1 mggklhpala fakqvegwsp gifskvdkwr epespapwqf mtfrqcrawi sdwlkhnpap
       61 kegflspvlm krfpphivym alaawrtgkt llhcdeslfr vlgetrqtda lsgemlrrlp
      121 fwgfwldfpa dtvfaegqga lmgafftlad hdnqtdalla ltlaqdplsr ehiplgmeyl
      181 altnpvstai sqqekgihgf wnavlpvlfw lcsensewgr qgkpvrpapr rvgkhqrfip
      241 pdkpvqifag vragsalrqa prvseaspsg drssaphrrl rphirkahwq sywkgkptqg
      301 eeksmllkwk ppq
//
LOCUS       WP_285150400             108 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Lelliottia
            wanjuensis].
ACCESSION   WP_285150400
VERSION     WP_285150400.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..108
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12199
     Region          1..89
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 miavlfeara epahqaryle laaelkplla didgfidier fqslttegki lslswwrdee
       61 airawkqnvf hkaaqaegra sifahyrirv vqlvreygsg dkpeqgsc
//
LOCUS       WP_285150531             324 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lelliottia wanjuensis].
ACCESSION   WP_285150531
VERSION     WP_285150531.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..324
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=37240
     Region          52..324
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 matirklpsg rwnaiirkkg lptktktfet reaaeawaey kdsctqtpsr dtialhtdty
       61 lkevmevngk krgghrtaky llnllsrhfk knvreitsvd veayrvlrlq tcksgsvrle
      121 lqmlkrfmew selhgltefd ktrevfrfik ipkaspnrke ivstqdferl lselqpimqy
      181 icilayetam rrseilqitp smvslnrrvi llskeqtkng ygrnvplstr aievlealie
      241 nkdsesllfs cktnsvtqaf kraitklgln kelcfhslrh tcitryaekg lstiqlqais
      301 ghktihmlsk ychvdgedvv klme
//
LOCUS       WP_285150624             476 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Lelliottia
            wanjuensis].
ACCESSION   WP_285150624
VERSION     WP_285150624.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..476
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51291
     Region          1..448
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mpdffsfine vlwgsvmiyl llgagvwfty rsgfiqfryi rqfgkslkns vnpqpgglts
       61 fqalctslaa rvgsgnlagv alaisaggpg avfwmwvtai igmatsfaec slaqlykerd
      121 kngqfrggpa wymsrglgmr wmgvlfslfl laayglifnt vqansvahal ryafsfpewi
      181 tgvvlavltl lvvvtgikgv arlmqwmvpv mallwvfasl vvtathieqv pgviamifka
      241 afgwreaaag algytisqal tagfqrgmfs neagmgstpn aaaaaaswpp hpaaqgivqm
      301 igvftdtiii ctasamivll agpvphsadm agiqlvqqal vnlsgswgag fvslivmlfa
      361 fssivanyiy aennliflrl dsrnnlwflr lgiagmvlmg svmslplvwq ladvimalma
      421 itnltailll spvvaliard ylrqrkmgvq pvfdptrype iesqiapgsw ddlprq
//
LOCUS       WP_285150701             330 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Lelliottia wanjuensis].
ACCESSION   WP_285150701
VERSION     WP_285150701.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..330
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34807
     Region          23..326
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mprritlslw mlalilalmt llatgfgalr lpvnllwngt dealrqiwft irlprvllal
       61 viggslalag cvmqglfrnp ladpgllgis sgaacavalw vvlpitlpal lmlyapmlaa
      121 flgalaatlv ifllsqqrds slsrlllvgi ainalcgaav gvlswvsnda qlrqlslwgm
      181 gslgsaqwst llavtslmip tvliiwrlag alnllqlgde eahylgvdvs nvqrilllcs
      241 allvasavav sgvigfiglv vphlmrmwlg sdhravipgs vlagafllli adtiartvva
      301 paempvgllt sllgapwflw lifrrggehg
//
LOCUS       WP_285150773             194 aa            linear   BCT 25-DEC-2024
DEFINITION  Maf family protein [Lelliottia wanjuensis].
ACCESSION   WP_285150773
VERSION     WP_285150773.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..194
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=21401
     Region          2..192
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mpnlvlasts pyrrallekl gipfecaapv tdetpqpaes prhlvlrlaq ekaqslaary
       61 pnhliigsdq vcvldgeitg kphteenarl qlmkargsiv tfytglalyn tstghlqtec
      121 epfdvhfrhl seqeiedyvr kerplncags fkseglgial fdkldgrdpn tlvglplial
      181 cqmlrrehcn plsa
//
LOCUS       WP_285150791             589 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Lelliottia
            wanjuensis].
ACCESSION   WP_285150791
VERSION     WP_285150791.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..589
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=65523
     Region          12..137
                     /region_name="GAF_2"
                     /note="GAF domain; cl21515"
                     /db_xref="CDD:473894"
     Region          158..584
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mtssnapsil mqiqptiqqf armlssvlql eveivdntlc rvagtgaygk slgrklskns
       61 rllcyiietk kekvvthsrf dplctdcshk enckekaflg tpviyqdqcv gvislvaltc
      121 eqqerindni qafsdyvrhi ssifvarllq dqagsdniqk lfttmienmd qgvlvvgrdq
      181 kvicanqval kimgathnni mgksihfspl tfegnfrhgh mqhvisiedk keliigqlha
      241 vqdqwlflma fhqshsstdl nhvqegpqie amvgecppmr qlktlmsrva pspssvmiag
      301 esgtgkevva raihklsdrr dqpfiainca aipeqllese lfgyvkgaft galangktgl
      361 iqaanhgtlf ldeigdmqls lqakllrtie sreiqpvgas hplpvdirii satnqnleql
      421 isngkfredl yyrlnvipln lpplrerqed iellihyflh lhtrrlnlvy pgvapdviaf
      481 lkeyqwpgni relsnlieyl vnvvpsgsvi dtsllppnlv ssrrvaeaql pgssttsede
      541 svtvleemer qmirgalsrn snkkqaadel gigiatlyrk ikkyemanl
//
LOCUS       WP_285150807             262 aa            linear   BCT 25-DEC-2024
DEFINITION  anti-sigma factor family protein [Lelliottia wanjuensis].
ACCESSION   WP_285150807
VERSION     WP_285150807.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..262
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29271
     Region          7..>108
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mkslrftppy qddaivawld gemdpndarv faeqlahder lsarteelkt shqdyqrafa
       61 plleeapsaq meerletwla ntpaprpgvs rraliaasvs flligsglgy larpsvalht
      121 enerirdlea qymslysaet lldvdssppl iargivrtae diglkvselq laladaelkm
      181 irmlryesta iaqivwmhad fgpmalcisp leqgdvtdis neqrhgmnva wwrdrdyqfv
      241 ligrnpatql kasarqlqla ll
//
LOCUS       WP_285151552             571 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC1 kinase family protein [Limosilactobacillus fermentum].
ACCESSION   WP_285151552
VERSION     WP_285151552.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus fermentum
  ORGANISM  Limosilactobacillus fermentum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Limosilactobacillus fermentum"
                     /db_xref="taxon:1613"
     Protein         1..571
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0004672 - protein kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=63517
     Region          31..481
                     /region_name="AarF"
                     /note="Predicted protein kinase regulating ubiquinone
                     biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport
                     and metabolism, Signal transduction mechanisms]; COG0661"
                     /db_xref="CDD:440425"
ORIGIN      
        1 mmakqevsat krlrqivnvi sknhflanfy hqtnpeviva aleelgptfi klgqllstrp
       61 dlvspsyisa letlqdqvqe ddfdtvktti eestgqtlae lfadfekrpf asasigqchr
      121 ahlhdgtevv vkvqhpavcq lvevdlalft ravrllkyip egsvvdlpqv veqlgqslrs
      181 eidftieaqa tqrfyelnng rgiflapkaf vdqsssrmlv tqymlgdsik glladpptla
      241 lpdglsltdv rkgvarslve nfiqevfydr ffhadphpgn lfflpvpags tqtttqfqkq
      301 fgdltltinn qtplppyrlv yldfgmmgtl paslaqgiaq vilaittkds yqisqailri
      361 cnqtgpvdeq sfnhqlasfl rpylntglkd ynfsqmifei tslcrrnhlq vkpevtmllr
      421 afgtlegtva kldpsislmd iarpfakqyf kehfnpkhft egqalkllra agattsipir
      481 vatfleqltn geqrlnlhyq gqdrvlakie allnrlltvi vlaaiilass ilvvggtthp
      541 liyklgvsgy llaiiillgl viantwrrfh r
//
LOCUS       WP_285151665             729 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Staphylococcus condimenti].
ACCESSION   WP_285151665
VERSION     WP_285151665.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus condimenti
  ORGANISM  Staphylococcus condimenti
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 729)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 729)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 729)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Staphylococcus condimenti"
                     /db_xref="taxon:70255"
     Protein         1..729
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=83087
     Region          3..727
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mnneypysad evlykaksyl seeeyehvlk syhiayeahq gqfrknglpy imhpiqvagi
       61 ltemhldgpt ivagflhdvi edtpytfddv kamfndevam ivegvtklkk vkyrskeeqq
      121 aenhrklfia iakdvrvilv kladrlhnmr tlkamprekq irisketlei yaplahrlgi
      181 ntikweledi alryidgvqy frivnlmkkk rsereayitn aidrirsemd kmqingding
      241 rpkhiysiyr kmmkqkkqfd qifdllavri ivdsikdcya vlglvhtlwk pmpgrfkdyi
      301 ampkqnmyqs lhttvvgpng dpleiqirtq emheiaehgv aahwaykegk kvtddnsgya
      361 qklswlkdla eadkaandaq efmeslkfdl qsdkvyaftp qsdvielpyg avpidfayav
      421 hsevgnkmig akvngkiepi dyvlqtgdiv eirtskhsyg psrdwlkivk sssakskiks
      481 ffkkqdrssn iekgkfmvea eikdqgfkve dvlteeniea vnqkynfsne ddlfaavgfg
      541 gvtssqivnk ltekqrildk qkalnaaqev tksvpikdhi ttdsgvyveg ienvliklsk
      601 ccnpipgddi vgyitkghgi kvhrtdcpni kseterlidv ewvkskdstq ryqvdlevta
      661 ydrngllnev lqavnatdsn lvkvsgksdv eknaiinlsv mvknvnevfk vverikqlgd
      721 vytvtrvwn
//
LOCUS       WP_285151699             447 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Staphylococcus
            condimenti].
ACCESSION   WP_285151699
VERSION     WP_285151699.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus condimenti
  ORGANISM  Staphylococcus condimenti
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Staphylococcus condimenti"
                     /db_xref="taxon:70255"
     Protein         1..447
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=50548
     Region          10..404
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mknifnplqr lhfyaaifit pllitltlsg iaylffpeve nhlykhefyg qsehkqqqsl
       61 ndaikqiekd hpgyminkvs mmeapynkri tigdmdgnsy yifldnhnqi vaqqnakyty
      121 snmtrsihss lstentviny ldeltacwtv fmilsgiymm frkrlltqns rnlrfqkwhs
      181 ivgiiiavpm lvlvftglpw sgfmgdkink iataypalgq tqiaanppks eeneipwamk
      241 kkqapdssgg ghhggmampm thspgqlsld kvvadaqkeg lkrpyaivyp tsadgsftls
      301 rasnsgvtgf dvspykettm ymdqytgkkl gqvnyqdygi lakwltwgip lheghlfgia
      361 nkiinllvci aflggiifgf iswfkrlgrm ktpqplprri krpmsiglii tlvilgilmp
      421 lfgfsliivf iieallywkd rrkakln
//
LOCUS       WP_285151777             401 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Staphylococcus
            condimenti].
ACCESSION   WP_285151777
VERSION     WP_285151777.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus condimenti
  ORGANISM  Staphylococcus condimenti
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Staphylococcus condimenti"
                     /db_xref="taxon:70255"
     Protein         1..401
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45144
     Region          3..396
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mhipfsppqi sedainsvve tlrsgwittg pktkefedal tkymgtqgtv cmnsataale
       61 mtlrllgigp gdevitsayt ytasasvidh vgakimlvdt qkeslemdyq qledkvtent
      121 kaiipvdiag qlcdyekifd iaerkqalfs tdnevhqkln riaviddgah sfgakkgdir
      181 sgrfadfttf sfhavknltt aeggavtwte dytkygidia krfktsilhg qskdafskmq
      241 kgnweydieq lgykfnmtdi naaigldqle kyeenlkrrk eivkfyeahl npellttlkh
      301 fdndkessch lyltwikgas eekrneiitq laeagiatnv hykplplfta yknygfdikd
      361 fpnayahyqn elslpiypql tneeieyvvk hvnqavsevl i
//
LOCUS       WP_285151764             107 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Staphylococcus
            condimenti].
ACCESSION   WP_285151764
VERSION     WP_285151764.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus condimenti
  ORGANISM  Staphylococcus condimenti
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Staphylococcus condimenti"
                     /db_xref="taxon:70255"
     Protein         1..107
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12299
     Region          9..65
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(12,16,41)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(15,40)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(22..23,34,37,41..42)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mrnndeiiei isqnlsakdm svselsrrvg maksavsrym nktrefplnr aedfaralni
       61 steyllgfdn ksdnedtiaa hfdkddlted emkevedfin ylkskrk
//
LOCUS       WP_285151911              81 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Lactococcus petauri].
ACCESSION   WP_285151911
VERSION     WP_285151911.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 81)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 81)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..81
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8921
     Region          5..81
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mtktklqimr ekkgltveql aekivkvvnd dskdrgniiy vsmvirkyel gnsalnlgia
       61 nknieimaqa lgcsvdelve e
//
LOCUS       WP_285151934             542 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Lactococcus petauri].
ACCESSION   WP_285151934
VERSION     WP_285151934.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus petauri
  ORGANISM  Lactococcus petauri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 542)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Lactococcus petauri"
                     /db_xref="taxon:1940789"
     Protein         1..542
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=62961
     Region          8..461
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(22,24,26,30)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(61,64,101,104,146,165,169,201,243,403)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(201,243,318)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          468..538
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; pfam16657"
                     /db_xref="CDD:435493"
ORIGIN      
        1 mnqqnwwqei vmyqiyprsf qdsngdgigd ikgiisrldy laelgiggiw lspvyqspnd
       61 dngydisdye simdefgtmr dmerlisead krgikiimdl vinhtsdehp wfiearkske
      121 nnyhdyyiwr dapsdgslpn dlksifggpa wqwdevveqy ylhlfskkqp dlnweneklr
      181 qaiyemmnfw idkgiggfrm dvidligkqp nqgitgngpk lhdylkemnq atfgdknllt
      241 vgetwgatpe iakqysnpan kelsmvfqfe higldeaegk tkwdlmplei pklkevfskw
      301 qtelgnegwn slfwnnhdlp rivsrwgndk eyrvesakml aillhmmkgt pyiyqgeeig
      361 mtnkpvndie qiddiesrnm yferleegys kedilhsina kgrdnartpm qwsneksagf
      421 saghpwlain pnyekinvea aledensify tyqklialrk enpiivwgkf ellkdtaeev
      481 fayirsykge nwlivanfst kknqfsssye vkeevihnyp eaidnveeiv lkpyeafvak
      541 lk
//
LOCUS       WP_285152117             112 aa            linear   BCT 25-DEC-2024
DEFINITION  T6SS phospholipase effector Tle1-like catalytic domain-containing
            protein, partial [Serratia ureilytica].
ACCESSION   WP_285152117
VERSION     WP_285152117.1
KEYWORDS    RefSeq.
SOURCE      Serratia ureilytica
  ORGANISM  Serratia ureilytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10561933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Serratia ureilytica"
                     /db_xref="taxon:300181"
     Protein         <1..>112
                     /product="T6SS phospholipase effector Tle1-like catalytic
                     domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          <12..111
                     /region_name="DUF2235"
                     /note="Uncharacterized alpha/beta hydrolase domain
                     (DUF2235); pfam09994"
                     /db_xref="CDD:462937"
ORIGIN      
        1 lksgdvkirl sieflglldt vasvgiania pfaeghmgwa ddtmelpdng likkcthlvs
       61 sheqrlcfpl dsicrsdgty psyatevvyp gmhsdigggy ppgdqgkavg hn
//
LOCUS       WP_285152379             309 aa            linear   BCT 25-DEC-2024
DEFINITION  DHH family phosphoesterase [Sneathia sanguinegens].
ACCESSION   WP_285152379
VERSION     WP_285152379.1
KEYWORDS    RefSeq.
SOURCE      Sneathia sanguinegens
  ORGANISM  Sneathia sanguinegens
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Leptotrichiaceae; Sneathia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Sneathia sanguinegens"
                     /db_xref="taxon:40543"
     Protein         1..309
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=34964
     Region          14..305
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mlnkikeeik kaknivlvgh vnpdgdciga tvafkymies fdssknvkvc inddlpnyve
       61 klpylpkiyk eidgeidlli sldvankerl aidekyikls kktiaidhhi sntkyfdlny
      121 vedissasel tykfldifsi kltkeiatyi ylgiindtgn fkhnnvtaht fmvaseiant
      181 gidlsniyri lfskslkkae lfsksvleat fdkelgfmyy yhgendiytr netngaseym
      241 lgleevkvsl fmqqdgdeik gsfrsksadv nyiaaqfdgg ghklasgfkt kkkldeiiqk
      301 tkeilkcqk
//
LOCUS       WP_285152218             245 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Ligilactobacillus salivarius].
ACCESSION   WP_285152218
VERSION     WP_285152218.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus salivarius
  ORGANISM  Ligilactobacillus salivarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Ligilactobacillus salivarius"
                     /db_xref="taxon:1624"
     Protein         1..245
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28837
     Region          1..236
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mkifiledds lqilrlklil esiqpnlviq tfkesdkllq hitqpdenni ylldielkns
       61 ryggfeasqr irevdnlgti ifitthsefm rktyeyrvaa ldfidkiqtn deikqslvtd
      121 fqlikerqnl neetefiele snseifripv sdiyffeiit dltkrklsvy tksqhfvvkg
      181 nlksietksd sfmrvhrsfv anvnnikrfd skekklyfse ktyclvsrkn vvplknilke
      241 gfvem
//
LOCUS       WP_285152419             124 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Sneathia sanguinegens].
ACCESSION   WP_285152419
VERSION     WP_285152419.1
KEYWORDS    RefSeq.
SOURCE      Sneathia sanguinegens
  ORGANISM  Sneathia sanguinegens
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Leptotrichiaceae; Sneathia.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Sneathia sanguinegens"
                     /db_xref="taxon:40543"
     Protein         1..124
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14450
     Region          39..120
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 meiktiveih nenfekkvdl syfesltniy niytienkgy lilldsvdvy eifeiavrik
       61 eqskgignkl msllpkdkdi llevnekntk alalykrqgf lqiyerkkyy gdfsaiimkk
      121 vcvl
//
LOCUS       WP_285152422             715 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidase U32 family protein [Sneathia sanguinegens].
ACCESSION   WP_285152422
VERSION     WP_285152422.1
KEYWORDS    RefSeq.
SOURCE      Sneathia sanguinegens
  ORGANISM  Sneathia sanguinegens
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Leptotrichiaceae; Sneathia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Sneathia sanguinegens"
                     /db_xref="taxon:40543"
     Protein         1..715
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=82443
     Region          6..279
                     /region_name="RlhA"
                     /note="23S rRNA C2501 and tRNA U34 5'-hydroxylation
                     protein RlhA/YrrN/YrrO, U32 peptidase family [Translation,
                     ribosomal structure and biogenesis]; COG0826"
                     /db_xref="CDD:440588"
     Region          403..476
                     /region_name="DUF3656"
                     /note="Collagenase; pfam12392"
                     /db_xref="CDD:463557"
ORIGIN      
        1 mniigpagny ekleaaikag atevyfglrg fgarrnndnl gfkelldaid yahlrgvkcl
       61 ltlntimkdi elknviknfl piyehgidav ivqdlglisi lkenfkdltl hgstqmtvsn
      121 hieanflksi glsrvvlare lsfeeikkir entdielevf vsgamcisys gncyissfig
      181 grsgnrgmca ytcrkqfkqd dnklrytlsp ndqlltfnei kkleeigina ikiegrkkne
      241 nyvfetvsyy rdvlnninrp slsyklfnrg yskgyfyldd klmnlnyssn fgyllasvkn
      301 nkihlydele tgdgiqfvns nfqtisgefv nkiiqngkkv tkvtkdsyvn ldipkntafi
      361 yknyskklnd eikqkiqntk rtidiqaklk ailgqplslt fsyknfcvev qtitlnelck
      421 ttisendiyn kiselgdttf kltnlelnyd kvsfipfsel keikrqasek lknlilnsyh
      481 kdkvevkyet fpktnekkdf iisalvenee qerackdfgi kkiyhsgydi skeknlntpe
      541 iknvgtlayn feqllrgkkq nitqstnwnm nifnnyslnf makfpnidtv flspelsykq
      601 lkhltsnsik kglviygylk gmyiehdllk ksymqiqgef ydryilrknk lnnvelylyk
      661 pmnlipkldl ienlgidelr ldftfenyeq vlkilnslkk rsgtynpyaf emgvs
//
LOCUS       WP_285152678             622 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Sneathia
            sanguinegens].
ACCESSION   WP_285152678
VERSION     WP_285152678.1
KEYWORDS    RefSeq.
SOURCE      Sneathia sanguinegens
  ORGANISM  Sneathia sanguinegens
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Leptotrichiaceae; Sneathia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Sneathia sanguinegens"
                     /db_xref="taxon:40543"
     Protein         1..622
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=71089
     Region          1..607
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mrenilevke lntylkkdkk elrilkdisf nlkkgkilgi vgesgcgksl tvnsiinlle
       61 nckiegeiky ynkdeeitln klkqygkifr nirgnkismi fqdpmaalnp vytianqite
      121 vllehkdikk sealkeaiel leklgiknak drindyphqf sggqlqriii amamickpdi
      181 liadepttal dvtiqaqilk llkdlkeeyn msiilithdl gviaemadev lvmyagevve
      241 gatayeifkn plhpytrsll qaiptkgnkg kklyvidgiv ppiteftenv crfsnripfl
      301 pkeaheinps lhevekdhfv rctcyksfkl nnrneeilek nkfdevvlev knlkkyynpk
      361 rsifrkkepi kaledinfnv kkgqtigiig esgcgkstla ksimklhdit dgeinidlgk
      421 glqniyklsk gkdllfrkkv qmvfqdpyss lnpskkiyea ldepmrvhkm gdkkkryeki
      481 lealkmvnlp keyldryphe fsggqrqric iaralclepe llildepvsa ldlsvqaqvl
      541 nylieiqqkk sisyifishd lgvvkymcdy iyiinngkfv ekgtteeifn spknaytkkl
      601 lesipdiski ygkdknesnt lv
//
LOCUS       WP_285152695             261 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Sneathia sanguinegens].
ACCESSION   WP_285152695
VERSION     WP_285152695.1
KEYWORDS    RefSeq.
SOURCE      Sneathia sanguinegens
  ORGANISM  Sneathia sanguinegens
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Leptotrichiaceae; Sneathia.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Sneathia sanguinegens"
                     /db_xref="taxon:40543"
     Protein         1..261
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29893
     Region          11..257
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 meqkwtniey ieskenrkyk llkklsqkky rdlnnifiae gekfikeckt ashciiqksr
       61 fdyfekkynl nnfikitiln dklfseissq ensqgilfih skntislnei kgdivilddv
      121 qdpgnigtii rtlvalnyen liltkgscdv ytpkavrasm gsifklniiy atydeikefi
      181 eknsyisfat nlaknsieyt ncklnkdkna yifgnegggv sktlldfcny nviipisdkv
      241 nslnvsvata vflykmrele k
//
LOCUS       WP_285152742             142 aa            linear   BCT 25-DEC-2024
DEFINITION  Dps family protein [Sneathia sanguinegens].
ACCESSION   WP_285152742
VERSION     WP_285152742.1
KEYWORDS    RefSeq.
SOURCE      Sneathia sanguinegens
  ORGANISM  Sneathia sanguinegens
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Leptotrichiaceae; Sneathia.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Choi,S.H., Baumler,D.J. and Kaspar,C.W.
  TITLE     Contribution of dps to acid stress tolerance and oxidative stress
            tolerance in Escherichia coli O157:H7
  JOURNAL   Appl Environ Microbiol 66 (9), 3911-3916 (2000)
   PUBMED   10966408
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 142)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   6  (residues 1 to 142)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Sneathia sanguinegens"
                     /db_xref="taxon:40543"
     Protein         1..142
                     /product="Dps family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16521
     Region          3..139
                     /region_name="DPS"
                     /note="DPS protein, ferritin-like diiron-binding domain;
                     cd01043"
                     /db_xref="CDD:153102"
     Site            order(16..17,21,23..24,35,46,50,53..54)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:153102"
     Site            order(23,35,39,50,54)
                     /site_type="other"
                     /note="DPS ferroxidase diiron center [ion binding]"
                     /db_xref="CDD:153102"
     Site            order(117,124..125)
                     /site_type="active"
                     /note="ion pore [active]"
                     /db_xref="CDD:153102"
ORIGIN      
        1 mektlnlfla dlatlakkvq nfhwnikgks ffsiheqldk mysdlneivd evaerilaln
       61 grplstmksy lenskinege nkditideal kkliedyqyi vdeakqvkik adesddfgts
      121 ammdeyiiry ekllwmlrsi ey
//
LOCUS       WP_285152765             711 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Sneathia sanguinegens].
ACCESSION   WP_285152765
VERSION     WP_285152765.1
KEYWORDS    RefSeq.
SOURCE      Sneathia sanguinegens
  ORGANISM  Sneathia sanguinegens
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Leptotrichiaceae; Sneathia.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 711)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 711)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 711)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 711)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Sneathia sanguinegens"
                     /db_xref="taxon:40543"
     Protein         1..711
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=82749
     Region          2..710
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mdqkeayeil kekclsnkel nmnkiekayi lareahkgqy rksgeeyiih pievsqilvd
       61 lkmdtdtiva gllhdvvedt litlsdieys fgkevsllvd gvtklrnlpk kqgkqienir
      121 kmvvamsqdi rvviikladr lhnmrtikyq spekqieksk ecidvyapia hrigmskiks
      181 eledisfryl npeayyemke lvntkkaeri ritndiieki kleldknnik sevtgrpkhl
      241 ysiykkitek nkkfaelmdl iairviveki decymvlgiv hgkfapvsgr fkdyiarpks
      301 ngyqsihtti eysenqkvei qirtkvmhei aeegvaahwk ykekkikdkn ekyyqavkkm
      361 faqkvtdevl netifvftpk gdvmeldnns taldfafqvh tqigyrtiga kindkivpld
      421 qklengdkve iltskatngp gkdwlnmvnn nsskvkikkw fkdlefenkv kegqeilene
      481 fakiglkfke leedeivyly mkkynipnie nlyykfatns lnlnnfiqkf kpkteeidye
      541 nileeakdna nkyadknenm mgvkisgsdn tmfvfakccn plpgveiggy vtnvkgiiih
      601 nktcqnlkrl ikkdpnreie vywdekllen sncryeysfs irsfnregll ydiiriineh
      661 kldiinmntm ikekngqsya iidirimikn kenfeklkkn llsmkdvidi i
//
LOCUS       WP_285152768             244 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Sneathia sanguinegens].
ACCESSION   WP_285152768
VERSION     WP_285152768.1
KEYWORDS    RefSeq.
SOURCE      Sneathia sanguinegens
  ORGANISM  Sneathia sanguinegens
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Leptotrichiaceae; Sneathia.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Sneathia sanguinegens"
                     /db_xref="taxon:40543"
     Protein         1..244
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=28460
     Region          94..>226
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          111..140
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          143..172
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          175..204
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
ORIGIN      
        1 mtlilekani dpisfyiaqk kakkgsnedi ryvlkvyekl nmndekekyi dlaiknnvqe
       61 vilnkitqyi nenktdelek lipklkskke rdkfegiyly kkgleayens nsnqaidyfk
      121 kaykkgikel ghniaslylk qknineavnw leiskydgne danyelsviy fnnkkyakai
      181 pylieeykkg kkelatsigv cyvnlykyee aivwlekass ngdndakkii ekingfrkes
      241 ynvy
//
LOCUS       WP_285152859             325 aa            linear   BCT 25-DEC-2024
DEFINITION  ribose-phosphate diphosphokinase [Sneathia sanguinegens].
ACCESSION   WP_285152859
VERSION     WP_285152859.1
KEYWORDS    RefSeq.
SOURCE      Sneathia sanguinegens
  ORGANISM  Sneathia sanguinegens
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Leptotrichiaceae; Sneathia.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Sinha,S.C. and Smith,J.L.
  TITLE     The PRT protein family
  JOURNAL   Curr Opin Struct Biol 11 (6), 733-739 (2001)
   PUBMED   11751055
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Becker,M.A., Smith,P.R., Taylor,W., Mustafi,R. and Switzer,R.L.
  TITLE     The genetic and functional basis of purine nucleotide
            feedback-resistant phosphoribosylpyrophosphate synthetase
            superactivity
  JOURNAL   J Clin Invest 96 (5), 2133-2141 (1995)
   PUBMED   7593598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Sneathia sanguinegens"
                     /db_xref="taxon:40543"
     Protein         1..325
                     /product="ribose-phosphate diphosphokinase"
                     /EC_number="2.7.6.1"
                     /GO_component="GO:0002189 - ribose phosphate
                     diphosphokinase complex [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004749 - ribose phosphate
                     diphosphokinase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0006015 - 5-phosphoribose 1-diphosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009156 - ribonucleoside monophosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009165 - nucleotide biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=35769
     Region          3..314
                     /region_name="PrsA"
                     /note="Phosphoribosylpyrophosphate synthetase [Nucleotide
                     transport and metabolism]; COG0462"
                     /db_xref="CDD:440230"
ORIGIN      
        1 mkeheikifa gtssfklank iadklgtklg drdiikfadg effakanctv rgckvfiiqs
       61 tskpvnenim ellvfidslk rasaseiiav mpyygyarqd rkasprepit skliadlltt
      121 agatrvvtmd lhakqiqgff nipvdhmeal pifakyfinq gftnentvvv spdvggvkra
      181 rnlatwlhmp laiidkrrpq anvcevmnii gnvkgkrail iddiidtagt icnaakalke
      241 agatevfaca thavfsgeav qrlknseftk vivtdsiqln ddqlfdklki vsastmfaet
      301 ihriyneepi sdlfalpnni desne
//
LOCUS       WP_285152978             464 aa            linear   BCT 25-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Sneathia
            sanguinegens].
ACCESSION   WP_285152978
VERSION     WP_285152978.1
KEYWORDS    RefSeq.
SOURCE      Sneathia sanguinegens
  ORGANISM  Sneathia sanguinegens
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Leptotrichiaceae; Sneathia.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Sneathia sanguinegens"
                     /db_xref="taxon:40543"
     Protein         1..464
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=50677
     Region          1..443
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mnflnsinai lyypiliill iasglyftfk tgliqlsllk nafsvitetp kkgevssfqa
       61 lmvstasrvg tgnivgvsna iciggygaif wmwiiaiigs ssafiestla qiykkkgkng
      121 syggpsyyiq ngigsktlgl ifaislilty avgfnmlasf nlqdsfrvyt fydpkttpwl
      181 iglflsiiag fcilgggkri ikvtsilvpl mglvfilvsl iiifknytlf psvmkrifld
      241 afnfraifgg isssclvegi krglysneag mgsspnaaas smtthpvkqg lvqmisvfid
      301 tlvicsataf iclssgiepq aniagakyvq mslatifgfy ghifitfsla lfafttllgn
      361 lyyvdsciay clkkdpsknf qiayrilasi fiflgcgmkm dfawnlsdfl mgimclinip
      421 tilylsniaf ralddyksql kkgldpifia kniglddtkl dywk
//
LOCUS       WP_285153011             353 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Sneathia sanguinegens].
ACCESSION   WP_285153011
VERSION     WP_285153011.1
KEYWORDS    RefSeq.
SOURCE      Sneathia sanguinegens
  ORGANISM  Sneathia sanguinegens
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Leptotrichiaceae; Sneathia.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Sneathia sanguinegens"
                     /db_xref="taxon:40543"
     Protein         1..353
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39876
     Region          5..353
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mekirklqky ikenklsglf itspknvfyl tklacdpher llalvikqde ihllvpamey
       61 enakrsvdks idivkyldte dgyalleknt gglsnlglek khltidryer ikkifniqnf
      121 ssidellinl rkyksndele kikkacslad laidiakknl kegiselelk aiiefemkky
      181 akamsfetiv lfgknaadph gesghtklkn gdlalfdlgv yfegyasdet rtiyfgtpna
      241 eaqkiyevvk yanmeaikac kpgvsfasid kiardiikka gygeyfthrl ghglgldvhe
      301 ypdvsektqd lleenmvfti epgiykpgia gvrieddivi tkngcevltk yek
//
LOCUS       WP_285153160             359 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Sneathia sanguinegens].
ACCESSION   WP_285153160
VERSION     WP_285153160.1
KEYWORDS    RefSeq.
SOURCE      Sneathia sanguinegens
  ORGANISM  Sneathia sanguinegens
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Leptotrichiaceae; Sneathia.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Sneathia sanguinegens"
                     /db_xref="taxon:40543"
     Protein         1..359
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=41069
     Region          3..358
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mndkikkifn tlnvdglllt dyfnkryftg ftgttgqali tkekkyfysd fryveqaamq
       61 tkpygfefvr ierraidhii egiekhnikr lgfddlampy aeyqmyskal pnvelvpagn
      121 emlnarqvks ekeieylkka asitdiafke tlkiikegis ekeiaahley iqrlngaedk
      181 sfetivasgy rssmphgvas dkkikrnefi tmdfgcyyng yasdmtrtif fgdkasispe
      241 qqriydlvyq gqtmgiemlk pgvigsnvdl avrkyfkeng dmdkyfghsl ghsfglevhe
      301 ppycskicdd klqenmvmtv epgiyienfc gvrieddili tkdgheritk sprelifig
//
LOCUS       WP_285153254              72 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Sneathia sanguinegens].
ACCESSION   WP_285153254
VERSION     WP_285153254.1
KEYWORDS    RefSeq.
SOURCE      Sneathia sanguinegens
  ORGANISM  Sneathia sanguinegens
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Leptotrichiaceae; Sneathia.
REFERENCE   1  (residues 1 to 72)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 72)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 72)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..72
                     /organism="Sneathia sanguinegens"
                     /db_xref="taxon:40543"
     Protein         1..72
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8099
     Region          5..62
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mkfnynglwk llidknmmkk dlmektgisp stvskmtkge pvnmqilwki ctelgsdige
       61 lvcidkscee dk
//
LOCUS       WP_285153425             341 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Lelliottia
            wanjuensis].
ACCESSION   WP_285153425
VERSION     WP_285153425.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..341
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37810
     Region          8..323
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mrtikgpgif lsqfigaqap fnsldglagw aaskgykalq ipcnhpqifd leqaavsqty
       61 cdeisgklae hglaiselst hlegqlvavn paygeafdhf appevrgnda arqawatakv
      121 kqaaaasakl gltahatfsg slawpffypw pphneqrfre afaelarrwr pvldcfdehg
      181 vdlcfelhpg edlhdgvtfe rflalvdnhp rcnilydpsh malqhmdyla fidiyharik
      241 afhvkdaefr pngrsgvygg yqpwinragr frslsdgqid fkgifskltq ydydgwavle
      301 weccmkdgdv gasegsefir rhiipvsgra fddfaaggan d
//
LOCUS       WP_285153593             670 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein [Lelliottia
            wanjuensis].
ACCESSION   WP_285153593
VERSION     WP_285153593.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 670)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 670)
  AUTHORS   Porat,A., Cho,S.H. and Beckwith,J.
  TITLE     The unusual transmembrane electron transporter DsbD and its
            homologues: a bacterial family of disulfide reductases
  JOURNAL   Res Microbiol 155 (8), 617-622 (2004)
   PUBMED   15380548
REFERENCE   4  (residues 1 to 670)
  AUTHORS   Kimball,R.A., Martin,L. and Saier,M.H. Jr.
  TITLE     Reversing transmembrane electron flow: the DsbD and DsbB protein
            families
  JOURNAL   J Mol Microbiol Biotechnol 5 (3), 133-149 (2003)
   PUBMED   12766342
REFERENCE   5  (residues 1 to 670)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   6  (residues 1 to 670)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   7  (residues 1 to 670)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   8  (residues 1 to 670)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   9  (residues 1 to 670)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12109673
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..670
                     /product="protein-disulfide reductase DsbD family protein"
                     /EC_number="1.8.-.-"
                     /EC_number="1.8.1.8"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=72373
     Region          46..146
                     /region_name="DsbC"
                     /note="Disulphide bond corrector protein DsbC; pfam11412"
                     /db_xref="CDD:463273"
     Region          276..669
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 mhaflrqlli cllwlwlpvs qaadsgwlra adnehasvrl radaqqkgdt rllldvslek
       61 gwktywrspg eggiapaikw qtplemdwrw pvpqrfevag istqgydgkv sfpitlrgam
      121 peklagvltl stcsnvcilt dypfaldlsv padpqfsydf sralgtlpls egltsrltag
      181 fgaekltvta treagwqnpe lfidtlvdtd fgkpvyrvdg qtltatlpvs dgwgdaapdl
      241 rgktlslvla dsgqaqesrv tvgeaqssaa plslgwillm alagglilnv mpcvlpvlam
      301 klgsivqast thrrvvrqqf masaagivts flalalmmta lrlsnqalgw giqfqnpwfi
      361 aamvlvmvgf sasllglfei rlssgfstfl atrggnglvg hfcqgafatl latpctapfl
      421 gtavsvalva plsllwgifl vmgigmslpw lliaawpgla lrlprpgrwm nvvriilglm
      481 mlvsglwlas llavhigqlp tqafsallvi alllatlwrw gwrvalwstl aaivalamtl
      541 vllrtghtgl tkdriawqpl seeaitaala dnkrvfvdvt adwcvtckan kynvllrdev
      601 qdalsapdvv alrgdwsrps etigqflrar qsaavpfnqi ygpgleqgrv lpplldrddv
      661 lqtltdakgk
//
LOCUS       WP_285154262             409 aa            linear   BCT 25-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Lelliottia wanjuensis].
ACCESSION   WP_285154262
VERSION     WP_285154262.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..409
                     /product="metal-dependent hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44770
     Region          3..>65
                     /region_name="metallo-dependent_hydrolases"
                     /note="Superfamily of metallo-dependent hydrolases (also
                     called amidohydrolase superfamily) is a large group of
                     proteins that show conservation in their 3-dimensional
                     fold (TIM barrel) and in details of their active site. The
                     vast majority of the members have a...; cl00281"
                     /db_xref="CDD:469705"
     Region          44..386
                     /region_name="Met_dep_hydrolase_A"
                     /note="Metallo-dependent hydrolases, subgroup A is part of
                     the superfamily of metallo-dependent hydrolases, a large
                     group of proteins that show conservation in their
                     3-dimensional fold (TIM barrel) and in details of their
                     active site. The vast majority of the...; cd01299"
                     /db_xref="CDD:238624"
     Site            order(62,64,228,248,319)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mslllknani fngkdnvita gnillagdki vaissqeipv gsnvqmldlk gkyvmpglid
       61 ahvhitasql dfneanvhkg ymyartfnfl rdmirrgfts vrdaggadmg ikksiddgll
      121 paprlfmscr alsqtgghgd yrhqasemvt cacslcsass iaiicdgvta vrhavreqfr
      181 vgasqikima gggiasptdk idnlqysdee iiaivdearr fnsyvmahay tpaaisrcvk
      241 ygvktiehgn lldeqsakdm hdhqaylvpt laiynafknn mssevpdsvv nkldevrlka
      301 lesirlarlh nvkiglgtdl lgdfhsfeyd eltlrsqves afdtlhsaty inaeildmkd
      361 klgvvaedaf adllvlpknp lddihlfneq ednvlmvikn geivknlla
//
LOCUS       WP_285154364             488 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Lelliottia wanjuensis].
ACCESSION   WP_285154364
VERSION     WP_285154364.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 488)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..488
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=53295
     Region          17..484
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 msesnpilss saqsieayqq aieqssqavm qwlqqsemyq gktvaelrdn islnfgqkgl
       61 gnqaaiarav eyflkdslsv hhpqcvahlh cpslvvsqaa evlinatnqs mdswdqspsa
      121 tiiemklidw lrtrvgyqag dagvftsggt qsnlmglmla rdaffarqgh siqqdglvgd
      181 lrkirvlcse nahfsvqknm allglgyqsv iqvktdecsr mdlndlaaki aqcnasgeqi
      241 laivatagtt dagaidplra iaemaaeqqi wvhvdaawgg allmsdkyrd yldgielvds
      301 itldfhkqff qtiscgafll keerhyelmr yqaaylnsef deeagvpnlv skslqttrrf
      361 dalklwmsle algqeqyaai idhgvtlaqd vaayvqtqds lelvmqpqla svlfrfrpds
      421 alndaaiall nqkigdalld sgranvgvte hngvtclklt llnptvtlgd vkvllslver
      481 taheilak
//
LOCUS       WP_285154490             244 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Lelliottia wanjuensis].
ACCESSION   WP_285154490
VERSION     WP_285154490.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..244
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26877
     Region          26..142
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 maqniydnpa ffegyaqlpr svhgldgape wpalksmlpd ltgksvidlg cgygwfcrsa
       61 remgaaqvig vdisekmlar alelttdaai tyqrsdlesl qleensldlv ysslalhylp
      121 eldtlfshvq ralkpggslv fsmehpiytc asrqgwltdd ngarfwgvnq yqqegqrvsn
      181 wladgvikyh rtlgttlnal ikagltlhev newgptqaqi dgwpalaeea erpmlvliaa
      241 vkpq
//
LOCUS       WP_285154468             254 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Lelliottia wanjuensis].
ACCESSION   WP_285154468
VERSION     WP_285154468.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14398448
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..254
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28194
     Region          14..108
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          176..253
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mtttstfsfa hrplvpfahd yqngdsepwh qhdcaqllhs lsgvvrvdta agcwvvppgr
       61 gvwlpagtph airitgnvaa rtlfidplar adlpascqiv qispllreli vsafdlpeay
      121 spssrheriy elildeirlm pvlpfclpep etdvlrqlcq qirsapellw ssaqaaslts
      181 msertlnrhf qqqtglsfge wtrrarllea lvrlaqgqpv lrvaldlgyg shsaftamfr
      241 rvmgispsdy frna
//
LOCUS       WP_285154621             338 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lelliottia wanjuensis].
ACCESSION   WP_285154621
VERSION     WP_285154621.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..338
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=37831
     Region          88..329
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mahirerrtg rfsrfivgyr vfpsgettka sfhtldeamc hlwraevser qlcpvsvsvt
       61 svprwplrka qwfwlgcqye kveqgittls syrqycknls avpgalqeva igrltplqls
      121 slssdqrkhl rpvlallvsf gwlpvnpigr lskpperkiv lpakaqiram lsaaahreki
      181 aiilgaicgl risevvslry sdisrkeiel crhltttger agtkrkkggr tidmpqelws
      241 lldvdkvgrd iplisgpegk slslnyskrg vlrdllsefg verfhdlrhf aitnalrrgk
      301 avadvakfag hkdpsltlrk yshflvenmg ltgslege
//
LOCUS       WP_285154634             282 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Lelliottia wanjuensis].
ACCESSION   WP_285154634
VERSION     WP_285154634.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..282
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31723
     Region          29..273
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          184..267
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqydisqilt dlingglpiq qvhfanptsp ppelalqvdf prleillegs vqdastgilh
       61 pndvlyvpag gwnfpqwqqp atalsilfgk qqlgfslvqw dgvalrnlak qhvarrgpri
      121 gsfllqtlhe mqmqpqeqqt arlitlslls hctdllgsqi qtasrsealf gavrdyideh
      181 yaspltresv akafyispny lshlfqktga vgfneyltqt rleharqllk gydlkvkeia
      241 hscgfidsny fcrlfrknte rspseyrrqy hsqltgktan pe
//
LOCUS       WP_285154713             201 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Lelliottia
            wanjuensis].
ACCESSION   WP_285154713
VERSION     WP_285154713.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..201
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=22432
     Region          4..180
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 msdaaaknil tiydthagaf aklrsrhlme kgwldkftrl vgeegtildi gcgngvpiae
       61 hfirhgyqlt gvdgapgmla raqqafpeqr wsnldmrqma lneifdglia wdsffhlshd
      121 dqrqmfpifs rhshpgsvlm ftsgtdngia mgefegeply haslspdeyr qrladngftv
      181 ievmfedpec gghsvwlcqr s
//
LOCUS       WP_285155028             263 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Lelliottia wanjuensis].
ACCESSION   WP_285155028
VERSION     WP_285155028.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..263
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27735
     Region          1..236
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mrrnklkali qentpivngw laipssysae ivghqgydav tvdlqhgmid fasalsmlqa
       61 lsatpavplv rvqdndpaqi mrmldagayg iicpmistae qaarfvaacg yppygvrsfg
      121 pargllygga dypqhanqai ltlamietre glanldaild tdgldgvfig pndlsltltg
      181 sasaesqhpe mtaavervvs hcrerqklag ifctsgdaar lrieqgfqfv tpandvmqlg
      241 rasreaiaqa rgtsaptaga sgy
//
LOCUS       WP_285155057             393 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lelliottia wanjuensis].
ACCESSION   WP_285155057
VERSION     WP_285155057.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..393
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=44696
     Region          2..388
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 maltarqidt akpadkdykl adaqglyllv ktsgakywnl kfrfggkekk lsigvypsvt
       61 laqarserdr arrmiaegtd pshakqakkr alrestastf kaiatewfah kartwtaryl
      121 adqqarmenk vypaighrpv seikplevlh clrevesegk letlrktrqi cvqifawaiv
      181 tgratsnpad ylntallspa rqnnrsltae qlpgfvrdvm qsvyfmakgt rllmltglrt
      241 gemrlgrwde vdfdkalwei pkermkkrrp hvvplsrqal allvelkala datrspfilp
      301 salradkprg rrcindfliq tgwheyttah gfrhtfstla hdngfntawi elqlahvdkn
      361 sirgtynhaq ylddrrammq wyadmldspa pqs
//
LOCUS       WP_285155099             694 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Lelliottia wanjuensis].
ACCESSION   WP_285155099
VERSION     WP_285155099.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 694)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 694)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..694
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=75277
     Region          10..681
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mlvsqynqil vvvsfvvail aaytalnmaa rvagsqgiaa rvwlagggva mgigvwamhf
       61 igmlamdism smsyspaitv lsmviaigss mfalwlvsge qlrlrrllpg alvmgtgiva
      121 mhytgmaale vtpgiiwdkt wialsvvial aaslaalwlt frlrheaaqv almrlgaavt
      181 mgiaiagmhy agmkaalfpa stemhhdgin gswlavlvsv valsilgitl lvsmldarlq
      241 artsllassl aeanrelaql alhdtltrlp nrilledrld qaiskadreg thfalmfmdl
      301 dgfkgvnday ghdtgdkllv avterlllpl kgqytlarig gdefvllaev ggpddaasla
      361 salvrtidsp fnvepyelvv tvsigialyp hdgksdrelm fnadaamyht krmgrngyhf
      421 fqpsmntlaq thlqlmndlw laidrdelrl hyqpkfhapa gpilgfeall rwehpkqgll
      481 tpdvflqlae ktgliipign wvineacrql rewhkqghsa wsmavnlstl qfeqptlvqt
      541 vldclarhnl paqslilevt ettamhnpee svrilteltn agvkasiddf gtgyssllyl
      601 kqlpacelki drafvkdlsg ksddativsa ivalaktlnl kvvaegvete aqqqfltelg
      661 cntlqgyllg rpvtaqtvee lcnnleamkt plps
//
LOCUS       WP_285155512              83 aa            linear   BCT 25-DEC-2024
DEFINITION  transcriptional regulator [Lelliottia wanjuensis].
ACCESSION   WP_285155512
VERSION     WP_285155512.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008341
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..83
                     /product="transcriptional regulator"
                     /calculated_mol_wt=8934
     Region          3..62
                     /region_name="YdaS"
                     /note="DNA-binding transcriptional regulator YdaS,
                     prophage-encoded, Cro superfamily [Transcription];
                     COG4197"
                     /db_xref="CDD:443351"
ORIGIN      
        1 mslakairav gtakhlaekl glsenaisqw knkykgiipp drvlevyavt gvtphelrpd
       61 iypnstdalv nknctpaphk dsd
//
LOCUS       WP_285155722             419 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Lelliottia wanjuensis].
ACCESSION   WP_285155722
VERSION     WP_285155722.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..419
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=46653
     Region          168..407
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 minfkkekaq lalmqllfgl ctiafgcviv apnfsvkvlg aagmtallvf ildiknfrkh
       61 dafwiclvlf iigicdlvwy kmykldssaa insyraylev gkiclfgafs ifvfvnkssl
      121 nigsnrihil laialqlmiv iyggyqhlfl etkrvtlsla egadatgaay tiafisfyii
      181 lvvqhssskw keliilghff itflllvate traailtypi iffgllvvkf ykgkhipwkg
      241 ilvflialla gafmmksnli qryddlnrdi iaygnnnsst svgarfamwe tglvaakeny
      301 lwqstdernk kivaavkndk slsgalpftv ghlhnevvet lslkgpsgli lyilfvvsvg
      361 wyalrkansv ilfaflvsli mfgvggvmfy skttpvawml tlimsivlle qnkhrdvik
//
LOCUS       WP_285155969             357 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Ligilactobacillus agilis].
ACCESSION   WP_285155969
VERSION     WP_285155969.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus agilis
  ORGANISM  Ligilactobacillus agilis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Ligilactobacillus agilis"
                     /db_xref="taxon:1601"
     Protein         1..357
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39957
     Region          9..357
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mvkmkdrvek lrlemartsv dcflvtepan ifyfsgftgd dgllliteqn kyvitdarfe
       61 lqlkkqaetw qhvitrnylq aacelvakek lvalgfeaql pywqydylde nltsdlvalp
      121 nllekirsvk dgdeiakika acklagqgyd ylltkfqqst qwterqlate ldyfmksnga
      181 sdksfetiva sglrtawphg tasdklvkkg dlitldygyy lngytsdvtr tfaygsqpae
      241 vrtiyqvvde araltiqaik agvsgkeldr igrdfisqag ygeffnhgmg hgiglsihel
      301 pnvgaryddv lqagqvitie pgiylpnigg vrieddilvt eagyeiltnf grnyqel
//
LOCUS       WP_285155897             381 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Staphylococcus
            aureus].
ACCESSION   WP_285155897
VERSION     WP_285155897.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     Protein         <1..381
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
     Region          50..377
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 ykdpytdkwk rvsvvlnknt kqsqkeamfr leekikekln nkssselktl tfhalldewl
       61 eyhiktsgsk lttlnnikir irnikrysse nlllnkldtk ymqifinkls diysqnqvtr
      121 qlgdmkgaik yavkfynypn eylltnvkip krrktiedie kdeskmynyl emnqvlqird
      181 hilndnklhk rnriliasil evqaltgmri gelqalqekd idllnktini tgtihrikye
      241 egfgykdttk tisskrsisi nsrtveifkk iilenkmlkr wnssyvdrgf ifttkkgnpl
      301 cnnqiagvlk kttkalnmnk kvtthtfrht hitllvemnv slkaimkrvg hvdekttiri
      361 ythvtekmdr eltqklenip s
//
LOCUS       WP_285156047             626 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Ligilactobacillus
            agilis].
ACCESSION   WP_285156047
VERSION     WP_285156047.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus agilis
  ORGANISM  Ligilactobacillus agilis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Ligilactobacillus agilis"
                     /db_xref="taxon:1601"
     Protein         1..626
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=70216
     Region          27..494
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mvkktlkiai vsicglllsl ssvqasspkk vevifthdlh shldsyrlas pkgtedvggv
       61 srlatviktq rqkhpdtlvv dagdfsmgtl yqtlyerqat elnflqelgf dattlgnhef
      121 dygdkalakm ltkakklpll eanidwqksa spkleaefkk yglkkytvvk kgnvkialig
      181 vmgndsiedt pttklkfkdp iksvkqtvae ikrkekvdmi vclshsgtsq tktsedeela
      241 kkvpdldlii sghthtvlnk plrhgqtyiv scgaygrytg lvklkqklnh rwklvdyrli
      301 smtqgipkdq qverqlkadt alinqtylsk lgyhkdqvia ynpynfesvd dhyfkpgehr
      361 lgdfmadsyl yalqqakika dvaivpagvi rdtlvkgpvt indafnlfsl gkgqdklpvy
      421 plvrvyltgk dlkkvaeida slanylnsar lymsglgyey nphralmnkv taaylldkqg
      481 hkkqikdtkl ypvvadmysa hmlgslkkqs ygllnvtprk sngqavtdyq qmvvmkgqre
      541 ykvfeafasy lqsfpkgrqg latipsyynq lhkrkvqkas ynplallskp nrftfaligi
      601 vlglgliviw vakkllrlkr akfkrk
//
LOCUS       WP_285156041             344 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Ligilactobacillus
            agilis].
ACCESSION   WP_285156041
VERSION     WP_285156041.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus agilis
  ORGANISM  Ligilactobacillus agilis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Ligilactobacillus agilis"
                     /db_xref="taxon:1601"
     Protein         1..344
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37797
     Region          33..342
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkkfnlmlil vallvsnpit tkaqtnpnth aiklahklik qkhfagtitl vkngqiiaqi
       61 sngyknyqtk vkntattpym igsvskaita qliallaqnk klaltdrlat yypnlpgask
      121 vtlaellnhr sgldtsyfsl hkhsdsyqty ltalvhqaki dpqninswhy ssynynllag
      181 ivtqvsgqsy atflkqaitt plgihldlmq atalksysyl rggffrqtdy npynaygagq
      241 vamngrdlyy llaaflqskl lapnltatly hkpptaafpy ysagfyhlqs gvyhlhgtql
      301 gdetsvtisp dgqqavlvqs nvtaytkggv nytfdlplfa alnk
//
LOCUS       WP_285156077             485 aa            linear   BCT 25-DEC-2024
DEFINITION  RecQ family ATP-dependent DNA helicase [Ligilactobacillus agilis].
ACCESSION   WP_285156077
VERSION     WP_285156077.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus agilis
  ORGANISM  Ligilactobacillus agilis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Larsen,N.B. and Hickson,I.D.
  TITLE     RecQ Helicases: Conserved Guardians of Genomic Integrity
  JOURNAL   Adv Exp Med Biol 767, 161-184 (2013)
   PUBMED   23161011
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Rezazadeh,S.
  TITLE     RecQ helicases; at the crossroad of genome replication, repair, and
            recombination
  JOURNAL   Mol Biol Rep 39 (4), 4527-4543 (2012)
   PUBMED   21947842
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Bernstein,K.A., Gangloff,S. and Rothstein,R.
  TITLE     The RecQ DNA helicases in DNA repair
  JOURNAL   Annu Rev Genet 44, 393-417 (2010)
   PUBMED   21047263
REFERENCE   5  (residues 1 to 485)
  AUTHORS   Chu,W.K. and Hickson,I.D.
  TITLE     RecQ helicases: multifunctional genome caretakers
  JOURNAL   Nat Rev Cancer 9 (9), 644-654 (2009)
   PUBMED   19657341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Ligilactobacillus agilis"
                     /db_xref="taxon:1601"
     Protein         1..485
                     /product="RecQ family ATP-dependent DNA helicase"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0043138 - 3'-5' DNA helicase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=55110
     Region          1..443
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
ORIGIN      
        1 manleqflkq tyhfssfrpg qkevinalla kqsilailpt gngkslcyqf ygrytnkrvl
       61 ivspllslmq dqvsqmkyqg yqqvialtse qdyltrqkvl anlgayqyif lapeilqnql
      121 vkqalqtlki gllvvdeahc istwgpdfrp dylqlgklqr llgqpltlal tatatpkvke
      181 dicqqlglsk vyqrsvnren iylevlkvas qsqkdqklle lvnylqgpgl iyfsskklad
      241 rlakwlgqrs qlrvaayhag lshldrysiq qqflqgqldl vcatsafgmg vnkediryvi
      301 hyhlpsdlns yvqeigragr dgkqscaill yqagdefiqr qllentlpap leisqyfmsk
      361 aqgqskisse kqrllasfnd qvageqralt ffaarkkerl talkqmatya ktggclrqyi
      421 ltyfaekpgq hndyncchna dywqtlaqlg lkrksrners nawagefeyq tilaqlftny
      481 nksee
//
LOCUS       WP_285156121             465 aa            linear   BCT 25-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Ligilactobacillus
            agilis].
ACCESSION   WP_285156121
VERSION     WP_285156121.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus agilis
  ORGANISM  Ligilactobacillus agilis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Ligilactobacillus agilis"
                     /db_xref="taxon:1601"
     Protein         1..465
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=54947
     Region          11..442
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mvkkkrnkfg ytrqyhisls yqqmelyeka iktqnelyqf alkylyktyg rkhigrplpf
       61 gqginylnnk ikamfineky elnrwnvkkl glsshaadef lktiftnfsq yrkrleqtgq
      121 msavekynlr mnitkdkdgk hknpkhrswy rkgsmnflrn nnsfrtitsq rlpkgntklv
      181 sphhlnvadf geimvfenlk hlnfeeialt kvkrlpdntf rlqitftrek krisqnkvvg
      241 adwnmfnnev frtsenktia ipkeivkkan elevakdklk slrdgeynkr gktalwqkyq
      301 rkqaklsakr aniltetyrk lvhelvdefd tiiiekidaf emrkrswsln kaqntgknkr
      361 lalikpyela kiieslvnkq nktlikvdpy ktsqveygte yeekhelret nkdgkriyvs
      421 aytgkevdrd ynaalnikew glhpekhvkl rdypklkagn lveii
//
LOCUS       WP_285156365             279 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase [Ligilactobacillus agilis].
ACCESSION   WP_285156365
VERSION     WP_285156365.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus agilis
  ORGANISM  Ligilactobacillus agilis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Ligilactobacillus agilis"
                     /db_xref="taxon:1601"
     Protein         1..279
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30838
     Region          3..265
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mallkvsfvs etlhravplv vilptdkiyk anqpkrlvdk pyktlyllhg vlgneedwlt
       61 gtriqrwaea ndlavvmpag ensfyvdnaf tgraysrfia qelveftrks fplspkkedt
      121 figglsmggy galynglkyh dtfgaivals aalmvdesla dlpeqaewfg atkafwqgvf
      181 gpdlkaagqs ecnlkvlinn llaqqvalpa iylaigdddk llaanvdfhe fldqkqvahv
      241 fkvapgshew dfwdrhlkra ldwlpleqas aginsgnvn
//
LOCUS       WP_285156453             285 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Ligilactobacillus agilis].
ACCESSION   WP_285156453
VERSION     WP_285156453.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus agilis
  ORGANISM  Ligilactobacillus agilis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 285)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401372
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Ligilactobacillus agilis"
                     /db_xref="taxon:1601"
     Protein         1..285
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32379
     Region          10..86
                     /region_name="cupin_Lmo2851-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to Listeria monocytogenes Lmo2851 protein, N-terminal
                     cupin domain; cd06996"
                     /db_xref="CDD:380400"
     Region          195..277
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mfnlflaicq nqdiylskhn rfaaypnhkh tffeinyvlq gqakeviagk tvtlnqgdli
       61 lldigtshsi qalgendlli nilfqnnnls vdllkelkgq hnvlvnflla kasskpdyiv
      121 fshqanpkis qlldeiitey yeqaefselv iksylnilis qlirslsikp spkesaqkkl
      181 alqlladias dyqtisltql akrysynrny lsnlfkaeig qtfsavlteq rlmqahkllt
      241 ktnlpvntii eqvgisnrsf fykkylayyh vspkqsrkqa saifd
//
LOCUS       WP_285156201             269 aa            linear   BCT 25-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Ligilactobacillus
            agilis].
ACCESSION   WP_285156201
VERSION     WP_285156201.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus agilis
  ORGANISM  Ligilactobacillus agilis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 269)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Ligilactobacillus agilis"
                     /db_xref="taxon:1601"
     Protein         1..269
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29209
     Region          9..266
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 magykelknl rnrvvvitga sgglgeqlay qaaskgaivv acarrldklq evvancrqis
       61 grlafaytld vsnpnqierv laevetnvgp idvlinnagf glmenllqid eqtiesmfrv
      121 nvlgliylsk ytalrmakrh rgaiiniasm agkiatpkst iysatkfavl gfsnalrlel
      181 kplgimvttv npgpiataff ekadktgnyl ksidkivlqp emvakkvirt igtnkrevnl
      241 pysmeiashl ynafptlgdy laggifnkk
//
LOCUS       WP_285156476             367 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Ligilactobacillus agilis].
ACCESSION   WP_285156476
VERSION     WP_285156476.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus agilis
  ORGANISM  Ligilactobacillus agilis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Ligilactobacillus agilis"
                     /db_xref="taxon:1601"
     Protein         1..367
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=40757
     Region          6..364
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mshltkvqqw laendydiay vsdykniqyf tgfgsdpier vlalfifpdk dpfifapale
       61 veavkevgwk ypvygyldhe npfalikdyi lqtagnpvkw aiekgnltve ryeafkqqfp
      121 sadftgnisp lieheklykt padiellkva gkwadfafev gfnalaqdkt eqdivaeiey
      181 alkkkgilhm sfdtivqsga naadphgapk adkirpnelc lfdlgtvykg fvsdasrtva
      241 fgqidakske iydvcleaql taqaaakpgm taaqldkiar dvidkagygq yfihrlghgm
      301 gqsdhefpsi megnnmelep gmcfsiepgi yipgvagvri edcvyvtdtg vepfthypkd
      361 litlpvk
//
LOCUS       WP_285156490             224 aa            linear   BCT 25-DEC-2024
DEFINITION  prepilin peptidase [Ligilactobacillus agilis].
ACCESSION   WP_285156490
VERSION     WP_285156490.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus agilis
  ORGANISM  Ligilactobacillus agilis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Ligilactobacillus agilis"
                     /db_xref="taxon:1601"
     Protein         1..224
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25174
     Region          1..223
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mylfavfcya tvwasfsscy ayryahsesi fypgsycdyc hhplnfwqli pilgfclqqg
       61 rcyychhkis lhstlveltf glytlslfas kaphlwasls ifcawsllla lsdyltqsvp
      121 afelylgglv lltqklswpp lepgcslcfl vilvgatylq llgsgdliyl gflwasfgiq
      181 fllattclas clalcyfslk kdrptslafi pflttasfil lyfn
//
LOCUS       WP_285156540             529 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Ligilactobacillus agilis].
ACCESSION   WP_285156540
VERSION     WP_285156540.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus agilis
  ORGANISM  Ligilactobacillus agilis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 529)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Ligilactobacillus agilis"
                     /db_xref="taxon:1601"
     Protein         1..529
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=60493
     Region          5..450
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(19,21,23,27)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(58,61,98,101,137,156,160,192,234,392)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(192,234,307)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          457..>494
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; cl02706"
                     /db_xref="CDD:445893"
ORIGIN      
        1 mkwwqkavvy qiyprsfqds ngdgigdlpg iisrldylak lgigaiwlsp vyqspnvdng
       61 ydisdyqaia keygsmedmd llikearkrq irivmdlvvn htsdqhpwfi eakrsktnpy
      121 hdfyvwsdqa ndlgstfggs aweydehlkq yylhlftkqq pdlnwanedl rkaiyqmmnf
      181 wiakgiggfr mdvidligkq paqkitangp klhtylqemn qatfgnsdlm tvgetwgasp
      241 keaklysdpk rqelamvfqf ehmtldqgqs kwdvksldva klkqvlskwq qelsqtgwns
      301 lfwnnhdlpr ivsrwgdegq yrlksaklfa illhlmkgtp yiyqgeeigm tnrkvtaidq
      361 vddiesrnay qellaqglsq kealaainkv grdnartpmq wdaspnagfs qgqpwlavnp
      421 nyqtinvaqa ladpnsifyt yqklielrnn nplvvlgdyq llktspevfa yyrtyqeqkw
      481 lvvanlshke nsieitdeis qvildngakp lvkghnllep ydalvvkla
//
LOCUS       WP_285156675             250 aa            linear   BCT 25-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Ligilactobacillus agilis].
ACCESSION   WP_285156675
VERSION     WP_285156675.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus agilis
  ORGANISM  Ligilactobacillus agilis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Behr,S., Heermann,R. and Jung,K.
  TITLE     Insights into the DNA-binding mechanism of a LytTR-type
            transcription regulator
  JOURNAL   Biosci Rep 36 (2), e00326 (2016)
   PUBMED   27013338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 250)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   6  (residues 1 to 250)
  AUTHORS   Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     A novel type of conserved DNA-binding domain in the transcriptional
            regulators of the AlgR/AgrA/LytR family
  JOURNAL   Nucleic Acids Res 30 (11), 2453-2459 (2002)
   PUBMED   12034833
REFERENCE   7  (residues 1 to 250)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Ligilactobacillus agilis"
                     /db_xref="taxon:1601"
     Protein         1..250
                     /product="LytR/AlgR family response regulator
                     transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28657
     Region          1..248
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mlkvivvddq aeileqvasg ieayvkfenl dvnlalatgd pqavltyvke npndkylffl
       61 didlatesyt gidlaselrk llpyeaivfl tsheelsliv lehrvlpldy ivkqsdftkv
      121 mkavkidlqr tleligqesk vnksyftyvk rgrhyriatt diyyfeampg sphlislyan
      181 nkrlnirrsl sqieeqlnad fyrchrgyli nlarvvalda aekmvyfdee gniacpvatr
      241 rlrdlkrklt
//
LOCUS       WP_285157144             342 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Lelliottia wanjuensis].
ACCESSION   WP_285157144
VERSION     WP_285157144.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..342
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=39264
     Region          1..342
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mnksrilfld ymrifafssv ilghkfyrdl vsvandsnth itiryiaqai yditvggavg
       61 vvvffmisgy iityvlqseg tkefylkrif riypiyifav ltevivkyfn gidipplsvl
      121 vprllligdf fgtplglagv ewtlrievmf yvimglmkfs gvlssgrvac tlmvitcfvl
      181 meskvfptas dfhhglfsty lpilfcgvvv ffmekreisr ftaflclsim lyshfkilev
      241 asprwintny aiigfcifmv swamrdkfsy nywcvllsel tysiylfhdw iwiyfkkiss
      301 aitdnyainn aiimilllsl cyasnkliek rgvkigrlvi sk
//
LOCUS       WP_285157734             339 aa            linear   BCT 25-DEC-2024
DEFINITION  AcrVA2 family anti-CRISPR protein [Lelliottia wanjuensis].
ACCESSION   WP_285157734
VERSION     WP_285157734.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Koonin,E.V. and Makarova,K.S.
  TITLE     Anti-CRISPRs on the march
  JOURNAL   Science 362 (6411), 156-157 (2018)
   PUBMED   30309933
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Marino,N.D., Zhang,J.Y., Borges,A.L., Sousa,A.A., Leon,L.M.,
            Rauch,B.J., Walton,R.T., Berry,J.D., Joung,J.K., Kleinstiver,B.P.
            and Bondy-Denomy,J.
  TITLE     Discovery of widespread type I and type V CRISPR-Cas inhibitors
  JOURNAL   Science 362 (6411), 240-242 (2018)
   PUBMED   30190308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19225148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..339
                     /product="AcrVA2 family anti-CRISPR protein"
                     /GO_function="GO:0140721 - nuclease inhibitor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38354
     Region          70..315
                     /region_name="AcrVA2-like"
                     /note="Anti-CRISPR type V subtype A2 and similar proteins;
                     cd22987"
                     /db_xref="CDD:467859"
     Site            order(73,153,173,196..197,199..200)
                     /site_type="other"
                     /note="putative Cas12a binding site [polypeptide binding]"
                     /db_xref="CDD:467859"
     Site            order(100,103,139..141,195,199,202)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467859"
ORIGIN      
        1 mggklhpala fakqvegwsp gifskvdkwr epespapwqf mtfrqcrawi sdwlkhnpap
       61 kegflspvlm krfpphivym alaawrtgkt llhcdeslfr ilgetrqtda lsgemlrrlp
      121 fwgfwldfpa dtvfaegqga lmgafftlad hdnqtdalla ltlaqdplsr ehiplgmeyl
      181 altnpvstai sqqekgihgf wnavlpvlfw lcsensewgr qgkpvrpapr rvgkhqrfip
      241 pdkpvqifag vragsalrqa prvseaspsg grssaphrrl rphirkahwq sywkgkptqg
      301 eeksmllkwk ppqivngkdd dsleavvrfm ketnkrdke
//
LOCUS       WP_285157694             478 aa            linear   BCT 25-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Lelliottia
            wanjuensis].
ACCESSION   WP_285157694
VERSION     WP_285157694.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..478
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=51920
     Region          4..474
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mktdwlfkha tvmdgsgaaa yiadvavcgn ritgiapait gashnvvdcr grilapgfid
       61 vhthddltvi krpgytekts qgvtsviagn cgisaacavv kdsvpdplgl lgerdefcyp
      121 dfahyrdavn vatpsvnvas lvghttlrnt cmntldgpat aaqitamrhl lrqaleqgal
      181 glstglsyds avnasteeic alaellaeyh giytthlrte ydgitdamee afhigrhagv
      241 pvqishlkca geknwgrste iltrmechqq hqdiscdayp yragsscldl kqvtadfdil
      301 vtwssphpem agkmlkdiaa lwqtglheaa arllpagaiy fqmdeedvrr vlahpatmvg
      361 sdglpcdpnp hprlwgtfpr vlgfyarder lfplttaihk mtglsatrfg lsqrgfireg
      421 ffadlvvfdp dtlrdtatfp vpkqqaegid lvlvngvmtw rhghmtgyra grfldrms
//
LOCUS       WP_285157229             535 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Lelliottia
            wanjuensis].
ACCESSION   WP_285157229
VERSION     WP_285157229.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..535
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=58866
     Region          1..525
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtvlsvenlt lsyrigrqwr evvhnvsftl krgemlafvg esgsgkttta qaiiglladn
       61 arrdsgkivl ngeeisqwsa krlnalrgar islvpqdpgn slnpvktiga qvgevlhihq
      121 kitkdeqenq vlalltkvgl shpeqrmkqy phqlsggmkq rvliaiaial rpdliiadep
      181 tsaldvtvqk rildlldilr resgtavlfv thdlalaaqr adrllvfrhg evqehgatad
      241 vvrapqhayt rqllsdlqgs rltiapvsgq rlasaairaq giskqfslsk nhylqaldnv
      301 sfevprgsth alvgesgsgk ttlarillgf eqadsgrvil ddidatqlsv earrqlrqki
      361 qfvyqnpfas ldprqtlfei ieeplknfgk itrverktrv eavttrvalp lellnrtare
      421 lsggqrqrva iaralilept ilvldeatsa ldvtvqaqil allqqlqqql gltylfithd
      481 latvrriahs vtvlksgqvv ehstvealfs spqnsytrel idaiphfspa tkeya
//
LOCUS       WP_285157579             403 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lelliottia wanjuensis].
ACCESSION   WP_285157579
VERSION     WP_285157579.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..403
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=45500
     Region          2..389
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mklnarqvda akprekaykl adgaglylev vpsgsrywrm kyrfngkekr mafgvypavs
       61 laqaralrde akkklaegid psfakkeekl vrdvqlnntf qsvalewhgt kvsrwsegya
      121 sdiieafnkd ifpyigqqpv neikplvlln vlrrmesrga tekakkvrqr csevfryaiv
      181 tgraeynpaa dltsamsghe skhypfltve elpdffkala gytgsplvvl aarlliltgv
      241 rtgelrgafw sefdlekavw eipaermkmk rphlvplstq aleivqqlkv msgqyplvfp
      301 grndprktms easinqvfkr igykgkvtgh gfrhtmstil heegfisawi etqlahvdkn
      361 airgtynhal ylegrremmq wyadyigsig lsgliiasfn ttv
//
LOCUS       WP_285157770             394 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Lelliottia wanjuensis].
ACCESSION   WP_285157770
VERSION     WP_285157770.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18765941
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..394
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=42776
     Region          110..225
                     /region_name="YfaP"
                     /note="Uncharacterized conserved protein YfaP, DUF2135
                     family [Function unknown]; COG4676"
                     /db_xref="CDD:443712"
     Region          271..>373
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          273..301
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(274,277..278,281..282,284,308,311..312,315..316,
                     318..319,348,351..352,355..356,359)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          306..336
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          347..375
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkgviklsll alsisfsfag yaesntvevl savvkdkkis gaqvviqrng eqsisslsdd
       61 sgnaqignit tdtnesliii kkngystlva kcpcggmsya lsptmkglds mrvvlgwgss
      121 psdldshmvy pgnhiffdhk lgdngnldvd dtdsygpeti tltrrengkp yvyavhdysd
      181 ksdpdtknls nseakvfvyv ggslvrtyyv pkdqsgnlwt vfkvnengai edvnnikgis
      241 vgasdidnvl tpllnsnatl shqnwgaeqi disnalnlkg eesyrrkqye eaisfftesv
      301 nnysengkay gnlglvyqkv grtaeaiwan rkaitlasgk naatiragan ynigkiyege
      361 gqyndalnyy naakkekqnp vydnailrvs skin
//
LOCUS       WP_285157909              64 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Lelliottia wanjuensis].
ACCESSION   WP_285157909
VERSION     WP_285157909.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 64)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 64)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 64)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..64
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..64
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=7207
     Region          5..56
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mknvqlislk elmkiypisr atvyrqikag llpapvqiga rrvawrldei eqhienlqkv
       61 qlag
//
LOCUS       WP_285158346             692 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Lelliottia wanjuensis].
ACCESSION   WP_285158346
VERSION     WP_285158346.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 692)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 692)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 692)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 692)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..692
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75737
     Region          145..679
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mshtlalhpv kkrdavflwv llgwvafall pswsldygll estreeilda yswshfnisw
       61 lwyllpslll vrpfneakre qrsrhyldag wallcmafiv isatvegrgl gfativlfva
      121 lgaimtlalt rlewlggdrf vigslitiva ligifivwps iaifipmftn dagefaplaf
      181 mtvlsqahiv qviinsvlls iavgigctff glvlaiyttr iakrsaiigr ifsilpivtp
      241 pfvvglgvtl mmgrsgyvte lmvdwfgltn tnwlygftgi wlaqvlaftp mafmildgai
      301 ktihpsleea sytlrasrwq tfngvfvpll kpalanafli vivqsladfs nplvlggnfd
      361 vlatqiyfyi tgsqldyqaa stlgafllvf sllvfciqym wigkrsyvtv sgksyrgdvq
      421 plpvtlvwsv vallavwivf nallygsify gsftvnwgvd ytltldnfik lfgqgmsdga
      481 wpslldtlly agiaapitag fglliawvvv rqqfkgkkti efttmlcfav pgtvagvsyi
      541 lafnsapvyl tgtaaiviis mvmrnvpvgi ragiaglgqi dksldeasls lragslrtit
      601 hillpllrpa ilsaliysfv raittvsaiv flvtpdtrva tayilnrved geygvaiayg
      661 silivvmlai iflfdwlige artsrskakn qa
//
LOCUS       WP_285158358             385 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lelliottia wanjuensis].
ACCESSION   WP_285158358
VERSION     WP_285158358.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..385
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44040
     Region          55..363
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mtlrggvwhc hfvtpsgqri rrslgtgdkk qaqelhdrlk seawrvdkig elptrtfeec
       61 cirwirekdh krsldddrtk ieyflrhftg rdvstitaeq vhdavskmvn rkhiqiwesr
      121 rdaairrgke ppayadkpvs qatksqhlsf mrsllkaaad dwgwiksapa iktrkpvskr
      181 irwltrdeae rliecmpesi kpvvifalat glrrsniidl ewqqvdmqrk vawvnpenak
      241 agkaigvaln dtacrvlrdq igkssrwvfa htkaatrpdg tltpavrkmr vddnsawkig
      301 lakagiqdfr fhdlrhtwas wliqygvpls vlqemggwes iemvrryahl apnhltehar
      361 kidaifgnhd tdmtqgenqa glkla
//
LOCUS       WP_285158483             381 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: trans-sulfuration enzyme family protein [Lelliottia].
ACCESSION   WP_285158483
VERSION     WP_285158483.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia
  ORGANISM  Lelliottia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Lelliottia"
                     /db_xref="taxon:1330545"
     Protein         1..381
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=41238
     Region          4..380
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mktlatlsvh sgefndqhga vmppiyatst faqpspgeht gyeysrsgnp trhaletaia
       61 elesgtrgya fasglaaist vlelldkdsh ivaiddvygg tyrlienvrk rstglqvswv
      121 kpgdlaalea airpdtkmiw vetptnpllk ladlagiaei arrhniisva dntfaspvih
      181 rplefgfdiv vhsatkylng hsdvvaglav vgdnrelaeq lgylqnavgg vldpfssflt
      241 lrgirtlalr vekhsanala iaqwleqhpq vekvwfpwle shphyqlare qmalpggmis
      301 vvvkgdaqqa taiirklklf tlaeslggve slvsqpysmt hasipleqrl angivpqlir
      361 lsvgiedand liadleqalk n
//
LOCUS       WP_285158566             360 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lelliottia wanjuensis].
ACCESSION   WP_285158566
VERSION     WP_285158566.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..360
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42109
     Region          67..332
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mafytiekri takgvtryrv tvgvkkggey vhrenktfpr lplarswgal rvadieaggl
       61 ekkepgitlr elltryindd smyksdskks slrsimrssl admlltditm nlyvdyarmr
      121 reaikpstla telsylknvl dlahpfydvr slpgeleaak lylytrniit psdkrnrrpt
      181 reefnllhen ltlafknspl giryhdvfef avyscmrrge icqikwadvd fdnrsvivrd
      241 rkdprkkign hmvvpllgra wdllieqpri sdrifpykpn titeifrrtr drlnipdirf
      301 hdmrreaasr lfelgfsvee taqvtghknl ktlwtvyrem ypqtlhdrfa qlqrerakgd
//
LOCUS       WP_285158692             325 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein [Lelliottia wanjuensis].
ACCESSION   WP_285158692
VERSION     WP_285158692.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..325
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35723
     Region          1..325
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mtktnlvtgf lgsgkttsil hllankdpae kwailvnefg eigidgalla dsgamvkeip
       61 ggcmccvngl pmqvglntll rqgkpdrlii eptglghpkq ildlltapvy epwidlratl
      121 cildprqlld ekavknenfr dqlasadiiv ankedrasqe srnafdfwwq nfggdrqfvt
      181 atqgkidnal ldqprrnvae lpasaahshi hapqkglaal nlpehqrwrr slnsgqghqa
      241 cgwifdadtc fdtigilewa rlapvdrvkg vmrtqdglvr inrqgadffi etqnvappds
      301 rielisavnt dwnalqasll klrls
//
LOCUS       WP_285158764             410 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein [Lelliottia
            wanjuensis].
ACCESSION   WP_285158764
VERSION     WP_285158764.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Porat,A., Cho,S.H. and Beckwith,J.
  TITLE     The unusual transmembrane electron transporter DsbD and its
            homologues: a bacterial family of disulfide reductases
  JOURNAL   Res Microbiol 155 (8), 617-622 (2004)
   PUBMED   15380548
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Kimball,R.A., Martin,L. and Saier,M.H. Jr.
  TITLE     Reversing transmembrane electron flow: the DsbD and DsbB protein
            families
  JOURNAL   J Mol Microbiol Biotechnol 5 (3), 133-149 (2003)
   PUBMED   12766342
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..410
                     /product="protein-disulfide reductase DsbD family protein"
                     /EC_number="1.8.-.-"
                     /EC_number="1.8.1.8"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=42748
     Region          3..406
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 mltaifaafl ggvilnfmpc vfpvislkal gimrhqgdta sartegfgfl lgviftmmal
       61 aalllalrag gtavgwgfql qsplviavla liilgaalnl lgvfevglsl qrageisvgr
      121 gafvrsaltg alaiivatpc sapfmagavg yalvqppavs laiffalalg faapftlvsl
      181 fpaiarrlpr pgawmdvlkr glafpmlgaf awlvwvlaqq agttalavml asavvvsfaa
      241 wlygiaqrrr ylgksyrvll aftvaffvva iaplpkaint gsaqpatlva envapvkwsp
      301 qsveamrghg kaifvnftas wcitcqvndr tslstqavke amartgavym vadstkfnad
      361 iddamnafgq gglplyvvyp adgsapkvlp qvltpsivvn alnqaadkka
//
LOCUS       WP_285158768             207 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Lelliottia wanjuensis].
ACCESSION   WP_285158768
VERSION     WP_285158768.1
KEYWORDS    RefSeq.
SOURCE      Lelliottia wanjuensis
  ORGANISM  Lelliottia wanjuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Lelliottia.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Lelliottia wanjuensis"
                     /db_xref="taxon:3050585"
     Protein         1..207
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23736
     Region          <59..191
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          138..191
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mficqihyqi rnelylagir nsldklashn phwgyqltak dtspqdeahf sifdmteclt
       61 keaflshgia dqprslillk aaqkelmsal vlgsrcsilc vdevhfnmre lidtvmkkkr
      121 ylsvlttrhq titlptspva ltraesmild ylwqgrsgvd iskvlfrsek tisthkrsim
      181 rklnvttdle lrkciqhyen kkmdvvn
//
LOCUS       WP_285159180             101 aa            linear   BCT 25-DEC-2024
DEFINITION  FecCD family ABC transporter permease, partial [Staphylococcus
            capitis].
ACCESSION   WP_285159180
VERSION     WP_285159180.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus capitis
  ORGANISM  Staphylococcus capitis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 101)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Staphylococcus capitis"
                     /db_xref="taxon:29388"
     Protein         <1..101
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          <6..97
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 pkvialmval vgvylaaitv sfvgmigfvg liiphvarll vggkhsrlip ftgilgaill
       61 iladtlsrti iapleipigt tmsliggpff lyllyrqstr r
//
LOCUS       WP_285159223             399 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Klebsiella oxytoca].
ACCESSION   WP_285159223
VERSION     WP_285159223.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella oxytoca
  ORGANISM  Klebsiella oxytoca
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Klebsiella oxytoca"
                     /db_xref="taxon:571"
     Protein         1..399
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=45702
     Region          2..393
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mkltarqvdt akpkekpykl sdggglylev atsgsrywrl kyryagkekr lafgvypevs
       61 laeardkrea akkvlaagnd pgevkkaeki aqklsfentf eaiarewhqv radrwslryr
      121 eeiidtfekd vfpyigkrpi aeikpmelle tlrrmekrga lekmrkvrqr cgevfrhaiv
      181 tgraeynpap dlatalatpk kthfpfltae elphflkdla gytgsiitkt atqiimltgv
      241 rtqelrfarw edinfekrlw eipaevmkmk rphivpmsdq vvalfeslkp itglyplvfi
      301 grndrtkpis kesinqviel lgykgrvtgh gfrhtmstil heegfdsawi etqlahvdkn
      361 airgaynhaq yldgrkemmq wyasfitnls iasvrnias
//
LOCUS       WP_285159278             271 aa            linear   BCT 25-DEC-2024
DEFINITION  ParB/RepB/Spo0J family partition protein [Klebsiella oxytoca].
ACCESSION   WP_285159278
VERSION     WP_285159278.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella oxytoca
  ORGANISM  Klebsiella oxytoca
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Klebsiella oxytoca"
                     /db_xref="taxon:571"
     Protein         1..271
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30314
     Region          24..241
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mtislgqyyk seetgttvkk tflvplseiy iepgynvrel nqdhviefrd afiagefvpp
       61 lavevtengv kvidghhryk galaaceagh eiarleckdf tgseadkiaf mitssqgmpl
      121 spvergfayl rlsnqgwsng eiakkvkrse sdiiqhmqlm ecspyvqklv regrlnyala
      181 ielhrkhgir tdsavakmme kaegsgkqki travaqpqfp akkarrfael fkeaeitgeg
      241 eficlrvpae lheeidslls eireennnev v
//
LOCUS       WP_285159348             629 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Staphylococcus cohnii].
ACCESSION   WP_285159348
VERSION     WP_285159348.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus cohnii
  ORGANISM  Staphylococcus cohnii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus; Staphylococcus cohnii species
            complex.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 629)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10106921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Staphylococcus cohnii"
                     /db_xref="taxon:29382"
     Protein         1..629
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=72793
     Region          435..606
                     /region_name="vWA_norD_type"
                     /note="norD type: Denitrifying bacteria contain both
                     membrane bound and periplasmic nitrate reductases.
                     Denitrification plays a major role in completing the
                     nitrogen cycle by converting nitrate or nitrite to
                     nitrogen gas. The pathway for microbial...; cd01454"
                     /db_xref="CDD:238731"
     Site            order(442,444,446,520,548)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238731"
ORIGIN      
        1 msdrfilfnd eqldakqvmm lqdlarlllk neqtqvkiqk fpyydpinnm litssfwshr
       61 kkdiettglk tdvmlaaygy qlmdetvvne vihndtfkhp kffqqlfkll edkrvlneiv
      121 kqrpstkdai hmrnevrlsy trtqinvykt kktftdllfl ylessflten fydvpqigpq
      181 iddillnmyq ylpnffynds sednlylaer imfqiddiln edmlneyyhl pkkvyaaihe
      241 lnfedlkrtd asntdnasnn dhdeesvsed iesnhqdsas qggaylemel hegensdvvg
      301 dndtaregds gddmtdmqtk kgkgstnqve sdeggsignn sifalkgina nvdvkwnvpe
      361 irpefqneyh dvenevqfet kdliqiikkt idreyqderr nltkgrlqkn llnwfiddqy
      421 klfykkqdls qtfdatftll vdasasmqdk msetikgvvl fhetlkslnv kheilafned
      481 afdaddtkqp niideiiayd qstikregpr imalepqddn rdgvairigs erlmrrahnq
      541 rflivfsdge psaynysqdg ildtyeavet arklgievfn vflsqdpite dveetihniy
      601 gnyaifvegv enlpshlapl lkklllksf
//
LOCUS       WP_285159326             549 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Staphylococcus cohnii].
ACCESSION   WP_285159326
VERSION     WP_285159326.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus cohnii
  ORGANISM  Staphylococcus cohnii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus; Staphylococcus cohnii species
            complex.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 549)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Staphylococcus cohnii"
                     /db_xref="taxon:29382"
     Protein         1..549
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=64205
     Region          7..469
                     /region_name="AmyAc_SI_OligoGlu_DGase"
                     /note="Alpha amylase catalytic domain found in Sucrose
                     isomerases, oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), dextran
                     glucosidase (also called glucan 1,6-alpha-glucosidase),
                     and related proteins; cd11333"
                     /db_xref="CDD:200472"
     Site            order(21,23,25,29)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(60,63,100,103,145,164,168,200,257,411)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(200,257,326)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          476..>517
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; cl02706"
                     /db_xref="CDD:445893"
ORIGIN      
        1 mkrkwwkeai ayqvyprsfn dtnsdgigdl kgviekldyl ddlgidviwl spmykspndd
       61 ngydisdykd imdefgtmdd fdqlldevhq rdmklildlv vnhtsdehqw fiesksskdn
      121 pkrdwyiwrd pkpdgsepnn wesifngstw efdeqtgqyy fhlfskkqpd lnwenqevrn
      181 aifemmnwwf nkgidgfrvd aithikktfe agdlklpegk dyapafevdm nqpgiqtwlq
      241 emkdkslshy dimtvgeang vspenaepwv gettgkfnmi fqfehlslwn sgdvkfdvna
      301 yknvlnewqk klenvgwnal fienhdqprr vstwgddthy wfesatshav vyflqqgtpf
      361 iyqgqeigmt nypfddietf ndvavvneye ivkqqggdvs klldkhkken rdnsrtpmqw
      421 nssnfagfsd vtpwfpvnpn ykninvahqq kdpdsilnfy kaliklkksh dvftygefnl
      481 vdsknnqifa ytrelndqyv livgnltnkk aalsfdasfl eenillhnyk nstidfeniq
      541 pyeafvikl
//
LOCUS       WP_285159775             405 aa            linear   BCT 25-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Staphylococcus cohnii].
ACCESSION   WP_285159775
VERSION     WP_285159775.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus cohnii
  ORGANISM  Staphylococcus cohnii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus; Staphylococcus cohnii species
            complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Staphylococcus cohnii"
                     /db_xref="taxon:29382"
     Protein         1..405
                     /product="metal-dependent hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44034
     Region          2..>64
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
     Region          41..387
                     /region_name="Met_dep_hydrolase_A"
                     /note="Metallo-dependent hydrolases, subgroup A is part of
                     the superfamily of metallo-dependent hydrolases, a large
                     group of proteins that show conservation in their
                     3-dimensional fold (TIM barrel) and in details of their
                     active site. The vast majority of the...; cd01299"
                     /db_xref="CDD:238624"
     Site            order(59,61,226,246,318)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mlikninlid gtgsaiqqnv dvfiqdhrfk tigqnlnhen heiidgtdky llpgmidshv
       61 himeemrplt dklatpfsyt fyraidhlkr tvncgittvr dalgadqgik eavqnglilg
      121 prmqisvnal titgghgdkl tksgitmpsf iedypglptg icdgveevrk kvremlraga
      181 dvikvhatgg vtsptdhpdf tqfsieelkv mveeaqfrgn rkvmahaqgl qgvknciaag
      241 ihsiehgiyl ddeaiekmka qgtflvptll apvsviefad elgmsegsve kskevleaht
      301 tsftkavnag vkiamgtdag vfkhgtnlre lelmvehgmt pmqaivastk taaeclgydn
      361 eigtietdkk adfiivddnp ldrigilknp dnikivgidg eivkr
//
LOCUS       WP_285159774             508 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Staphylococcus cohnii].
ACCESSION   WP_285159774
VERSION     WP_285159774.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus cohnii
  ORGANISM  Staphylococcus cohnii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus; Staphylococcus cohnii species
            complex.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Staphylococcus cohnii"
                     /db_xref="taxon:29382"
     Protein         1..508
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54634
     Region          136..504
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mskdsstkst snfkpfwlit smiilitili lptpeslplm aksalaillf avilwvteav
       61 typvsavmiv gliilligfs pvqnlseslg ypqsngeilk gdslfgtgna lklafsgfst
      121 salalvaaal flatamqitq lhkrlalivl svagnktnri vigtilvaif laffvpsata
      181 ragavipill gmitafgvak qsklagllvi tavqavsiwn igiktaaaqn ivainfindq
      241 lntdiswgqw flyagpwsml msialyfiml kvmppeekel sggksliqqq lkamgpitsk
      301 ewrligisii llilwsteki lhpidsssii llalaimltp kigvmswkea esripwgtii
      361 vfgvgislgn vllkttaaqw lsdqtfgvmg lnhypllvti alialfnili hlgfasatsl
      421 asalipvfis ltttldlgnq sigfvliqqf visfgfllpv sspqsmlayg tetftvkdfl
      481 ktgipitvig ylliilfiat ywhwlgli
//
LOCUS       WP_285159818             404 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Staphylococcus cohnii].
ACCESSION   WP_285159818
VERSION     WP_285159818.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus cohnii
  ORGANISM  Staphylococcus cohnii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus; Staphylococcus cohnii species
            complex.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Staphylococcus cohnii"
                     /db_xref="taxon:29382"
     Protein         1..404
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=47322
     Region          <307..401
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mknetleilq mhaiqllgiq legydmddik aisnhiktpf mnttrkqykn elkhfivhmq
       61 snkiyhykns fnvsflifkf kkyrkiyiig pymdkrpner qcnemllnln ikisklptlk
      121 qyllkipich hvkaqkmcrl airflknrni vyetvdidfs fhaneaflad sklqsdytlq
      181 eieyrynlen qlltavengn veealsilkk mslsvtglrr vkddlsneqy kaylintlcr
      241 kagekagvsl ihideisaky aamidrtldv evleeltyai vkeyaeramk ikanvfspkv
      301 skviqyiern ldsnltleel anyvdlapsy lsrifnqech qslsqfitsl rikkgrdlia
      361 rtkmtvaeva kyvgfreqsy faqcfkkqyg ktplkyrteh kefy
//
LOCUS       WP_285159840             454 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Staphylococcus cohnii].
ACCESSION   WP_285159840
VERSION     WP_285159840.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus cohnii
  ORGANISM  Staphylococcus cohnii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus; Staphylococcus cohnii species
            complex.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Staphylococcus cohnii"
                     /db_xref="taxon:29382"
     Protein         1..454
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52213
     Region          115..452
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mfkslysria iytivillss avlsflltnv iyhnhlkenn dakimrtlkd aisyekqski
       61 qlpkpffehl gqmnyqvmtv sengkkayyg tafrkdnvds kniksvlkgn dyhgisnlpy
      121 npfitgffen ttqntvgvqf qsnghnyavf mrpdigktfs efriflvili tlllvisiiw
      181 visstymiik piqqlkqate rlmegnfdvp idikrndefg tlqyrfdkmr lslkqvddmr
      241 qhfvqnvshe iktplthihh lldqlkftks atereqyide iyqittqlse ltkellllse
      301 idngehlelt dhielnklik qiirheqfat nekdliimsd lanisligne rllnqafqnl
      361 itnaikyseq ggtiditlth dtdhirfnit ddgqgmtpet qsrlferfyk asnhdnsngl
      421 glaiakaife lhngtievss kkyegttftv tink
//
LOCUS       WP_285160007             320 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Klebsiella oxytoca].
ACCESSION   WP_285160007
VERSION     WP_285160007.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella oxytoca
  ORGANISM  Klebsiella oxytoca
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Klebsiella oxytoca"
                     /db_xref="taxon:571"
     Protein         1..320
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=37403
     Region          11..316
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mndisfgllt eqyfyskslr patewsyqkv vrsfegftsf nptkidhltv lkwrhtvlnd
       61 qncatrtwnn kvahmralfn fgikqgllpq aenpfngavv rpgtkkkktl tqtqmdamyr
      121 lmeqyleteg rqgnssmfng rrnallpawf wltvvnvfry tairqnqllh irlgdinlee
      181 rwidlniega knhrehrvpi vsslypslee lvrkageagm esddqvfnvg wfdlmrksky
      241 pevmneyplr affrrlsrec kftitphrfr htvathmmks pernlyavkk llghvsitst
      301 leyidesvds lrdiletelm
//
LOCUS       WP_285160115             636 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Klebsiella oxytoca].
ACCESSION   WP_285160115
VERSION     WP_285160115.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella oxytoca
  ORGANISM  Klebsiella oxytoca
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 636)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 636)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Klebsiella oxytoca"
                     /db_xref="taxon:571"
     Protein         1..636
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71844
     Region          1..488
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mflsklkikg frcfdrefsi slneglsviv gengagksai insirqlfid seserynite
       61 ndfhrpfcnp pkvsdsftin aefsnlgtie kiallpwtgn sdvaklnlyv enkeirgryk
      121 ktlwggdsqn sqfdyelldi iyciylpplr daeskltngr qsrlskllka inrkdlrslk
      181 knggvhllvn kvntfndels nsdlygikaa nqliknhlqn aiglnfgqnt aiqfaesdft
      241 riveslrlif fpnlneedtk lfrnleqnsl gynnllyias ilaeltlgye qdpstcrlll
      301 ieepeahlhp qlqirlldhl kkvsedkdnn vqvivtthst tlassvsvds iihlsksssp
      361 vatrlkdcgl atkskefidr wmdvtksnll fasgvilveg iaeqmllpvl akeiladrdv
      421 gkntlsdlgv svinlngiyf rhfmglycnf tipsektkhe glsipircag ltdldppkki
      481 kklvegkefi ekiiiphdae myegtnhaik lveeinssry arlyvskykt leydlamegn
      541 niaamssvly eiwptdgdik kkikaimdvk ddwskkksyd raiianellq yienselgkg
      601 yfaqsiseki sknevkfetp eyiknailwv cpdetv
//
LOCUS       WP_285160134             475 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Serratia ureilytica].
ACCESSION   WP_285160134
VERSION     WP_285160134.1
KEYWORDS    RefSeq.
SOURCE      Serratia ureilytica
  ORGANISM  Serratia ureilytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 475)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Serratia ureilytica"
                     /db_xref="taxon:300181"
     Protein         1..475
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=51371
     Region          11..473
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mhprlqqdla qfpqildhtr qlaedflagl qqrsvcpple hqqlqpgddr ldengegala
       61 alerfwqryq agisasagpr yfgfvtgggt paavaadwlv svtdqnslls hdtiaatiel
      121 aavtqlksll glpetfsgsl vsgatmanft glaigrqwlg qqrgvdiaqq glaalgpirv
      181 lganphsssv kalsmlgigr ealtivaslp eseamdmaal erqlaagaga gagqptlvla
      241 sagtvntvaf ddlpqllalr erypfwlhvd aafggvaacs plyaprlegw qhadsitvda
      301 hkwlnvpyds aiqftrhldl qmqvfqnhsa yleaptlrpd nylhltpens rrfralplwl
      361 tlkaygrsgi rdivernvel aqalgaalaa edgfhllapv nlnvvcfals hpqgdseaar
      421 drflerlsrh gvarctptry ndqpgiraal vnwmteeqdi rltldslrhc laeta
//
LOCUS       WP_285160238            1049 aa            linear   BCT 25-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Klebsiella oxytoca].
ACCESSION   WP_285160238
VERSION     WP_285160238.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella oxytoca
  ORGANISM  Klebsiella oxytoca
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16109280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Klebsiella oxytoca"
                     /db_xref="taxon:571"
     Protein         1..1049
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=118395
     Region          15..>136
                     /region_name="DEXDc"
                     /note="DEAD-like helicases superfamily; smart00487"
                     /db_xref="CDD:214692"
     Site            45..51
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:350769"
     Region          <238..340
                     /region_name="DEXDc"
                     /note="DEAD-like helicases superfamily; smart00487"
                     /db_xref="CDD:214692"
     Region          <869..925
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            921
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350171"
ORIGIN      
        1 madkhpsiia pltglkdfqq rtvnyvfqqf ygdkqqnrfl vadevglgkt mvargiiaka
       61 iehlqdkvdr idiiyicsna aiaaqnikrl nvsnetqfsh strltllpkq vrslrknrin
      121 fisltpntal dhtrsrgghk eerailyril ydlplakger rerlrmgmln llqatanrpg
      181 wcsavdqlsv ddidrelakd frrqvlddte lyaqlkegce cfadndedge thdselryal
      241 igklrsklas vclsalepdl vildefqrfk alldgddeaa llakalfeqp dvrvlllsat
      301 pykmftldqe seednhyadf irtlqflynd dsqikdiqqy lldhrtalha senaaetkka
      361 lehallqvmc rtervtmtqk ldamtkevsq pamitpadly haaavdgvam evqardvley
      421 wksmpylfnf lknyelrtrm dkalespsda lrklvksakp qlltkakler yqpldaanpr
      481 mrmlfedtld kgmwqllwmp pslpymtpdg vyankgnftk tlvfsawsav pnaiatvcsy
      541 eaerrmigta pkilhsqfkk kvkpllnfak sskdgrlsgm pviawmlpsp tlarhidple
      601 iarqntgepl svkavraiat akcetlietl gnggpgtrad erwywaalal ldaqtetpaw
      661 wqgehywytg psqnepaenf qehidqfagv angsitlgpr pddlaevlcd falaspgtca
      721 lralsridkg lridsaemls aaakiasgfr slynlaesis llrgtgddty wrltlrygid
      781 gniqaildey vhtllesmgl qhepagaqla aiasriqavv slrttqlnid efktnggnyt
      841 wsdlytrcrf alrygqlrdd tdqavahaes vkdafnspfh pfvlastsig qegldfhtwc
      901 havmhwnlps npvdleqreg rvhrykghav rkniaeyygl salhslaesa dpwaqlfala
      961 asqrkagqsd lipywifeeg tsrverrvpi lpyskesikf krlkrelaly rivfgqprqe
     1021 dlmfglkhng desftdltqw lisleppkv
//
LOCUS       WP_285160278             701 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Serratia ureilytica].
ACCESSION   WP_285160278
VERSION     WP_285160278.1
KEYWORDS    RefSeq.
SOURCE      Serratia ureilytica
  ORGANISM  Serratia ureilytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 701)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 701)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Serratia ureilytica"
                     /db_xref="taxon:300181"
     Protein         1..701
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=78186
     Region          14..689
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 msllpeqtnn knpidlysei vddlpglicf gnrlggyfnk qwrdytgaia gehgaadwle
       61 alhpddrerl aaqwrqaiva lssfagearl rersgayrwf mlafnarqdg kalepswylt
      121 atdihpqmlq rqqnvqalsi qqdmldasvd cikvinrdgt lrhmnrsgsl algldpaqke
      181 fgmpwlglls pevrrrgska lrsvkagkna rfaglsvtpq gkkqhwdnil spvsdehgvv
      241 aeilcvsrdv tsqrvmeqrl llaseydelt glpnrrlfkk klkqemkral hgnkslglml
      301 ldldhfklvn dtlghaagdh llrvlgkrls acmnthsfvs rlggdefavv isdveneqdi
      361 friankfllq letpithggk tlhcgmsigg aiypkdarda selmkcadta lyelkeggrg
      421 gvymfdskmm dkararasql nyarqivrdn cirpnyqpkv sladgsivgf eallrwhcpq
      481 ngiqlpatvs eafndyelat kiseamqlkv fadiarwraa gvavrpisln vspieflrdn
      541 yaetflqrll kfhiphhlie levtehafnk hgskyvlral hmlkemgiri alddfgtghs
      601 sfshimdypl dcikldcdfi qrmntepail aivesigilg qklsidiiae gveteqqrqt
      661 lceagfhigq gflfspavgs qqvptllqai lqpaeggman r
//
LOCUS       WP_285160301             512 aa            linear   BCT 25-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Serratia ureilytica].
ACCESSION   WP_285160301
VERSION     WP_285160301.1
KEYWORDS    RefSeq.
SOURCE      Serratia ureilytica
  ORGANISM  Serratia ureilytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Serratia ureilytica"
                     /db_xref="taxon:300181"
     Protein         1..512
                     /product="long-chain-fatty-acid--CoA ligase"
                     /EC_number="6.2.1.3"
                     /GO_function="GO:0004467 - long-chain fatty acid-CoA
                     ligase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55920
     Region          4..512
                     /region_name="FC-FACS_FadD_like"
                     /note="Prokaryotic long-chain fatty acid CoA synthetases
                     similar to Escherichia coli FadD; cd05936"
                     /db_xref="CDD:341259"
     Site            order(169,172..177,179..180)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(172,292..293,314..319,398,410,413,424,505)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(172,214..215,262,264..265,268,292..293,314..319,398,
                     410,413,421..424,486)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(214,264..265,268,292,421..423,480,486)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mlnlatllee sartwperpa viqddiplsy ralnemanrv anllvargvq pgervalacp
       61 nrpefpaiyy gilksgavvv plnillksae fdyyladsaa valfcfegss glplgeealr
      121 aaakaeqcre vfiigdrlpl egerfstaia aqatefasaa tiesdtavvl ytsgttgrak
      181 gaelthanlv lnalgsvrlf dgsetdpdrh lvtlplfhtf gstvqmnagf saaatlvlve
      241 rfdaaqaial mqrhgitffa gvptmywall naldehtdie rlrstlrmav sggaslpvqi
      301 ledfsrrfgv nilegyglse tspvatfnhp hrvtkpgsig qpiwgvevrl ldvngqpidg
      361 vdqvgeiavr gynimkgyln rpeataevle ngwfrtgdla rrdadgfyfi vdrakdmiir
      421 ggfnvyprei eealirhpav slvavigveh pslgeeikav vvlketeepi eeealiawsr
      481 erlaafkypr ivefverlpm tstgkvlkrc lr
//
LOCUS       WP_285160737             267 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Kingella negevensis].
ACCESSION   WP_285160737
VERSION     WP_285160737.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..267
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28854
     Region          45..266
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mkklflatll vtsallagcg dnsapetetp aasaaasqta nletltvgge vsyepyafkd
       61 ekgqaqgfev dvmnaiakaa gmnaqfidap rgaavetlnn gtfmafssam sraayrletm
      121 dmgqpyidfd ralyvldtpk tanlktladf kgkriashks skgnvkkiee mgatpvlsds
      181 fflmlndvaq gkadaaigdk rifqyyqvky petkshiist geekrqfsfs vkkgntellk
      241 kldgglekik adgtldkiie kwfgkqd
//
LOCUS       WP_285160797             403 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Kingella negevensis].
ACCESSION   WP_285160797
VERSION     WP_285160797.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..403
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45389
     Region          2..403
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mivqedhrap vvmtqlwykv gssdemagkt glshalehmm fkgtktvpag eyvkrisalg
       61 gsnnayttte etvyhvtiaa qhlpkvlele adrmanlnfs dtvfnnemkv ireerrqrid
      121 dnpdsmlyae llntawtksp nrtsvigkma dlhklkpndl rqwyrrwyap nnavlvvvgd
      181 vqpenvfaqv eqyfgslker kladhqdise pethekssfa tlkgntkqpm mmlayrvphl
      241 qkmdeklpya ldmltnvldg hsaarlsqrl vrgsqvaqni gtgysllarq sqmwiisvsp
      301 tngvdlaqlk avlkkeiadv ahngvseael nraktiqrtn kiysydeisa ranlmgtles
      361 vglkyddena irqrldevtt adiqaatkll tqerevyvel lpk
//
LOCUS       WP_285160913             343 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Serratia ureilytica].
ACCESSION   WP_285160913
VERSION     WP_285160913.1
KEYWORDS    RefSeq.
SOURCE      Serratia ureilytica
  ORGANISM  Serratia ureilytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Serratia ureilytica"
                     /db_xref="taxon:300181"
     Protein         1..343
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=40928
     Region          7..323
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mkseekmhde weflleeyff tkqlrsatew syrkvaltft rfigetitpa mvtqrevllw
       61 rrhllkeknl svhtwnnkva hlraifnlgi kkalvqhgen pfngtivrsd tkkkriltrs
      121 qltrlylvmq qyeqrekerk pvkggkcaly ptwfwmtvld tfrytgmrnn qmihirlrdv
      181 dieqgwielr legskthrew kvpvvrqlre rikllmmrai ergasqhdll fdvkrfinpr
      241 nthynydekn vlqsfrsfyr rlsresgfdi sshrfrhtla telmkspdrn lklvkdllgh
      301 rnvsttmeyi emdmevagka leqelvlhtd itatrslqsl tqa
//
LOCUS       WP_285160946             266 aa            linear   BCT 25-DEC-2024
DEFINITION  AraC family transcriptional regulator [Serratia ureilytica].
ACCESSION   WP_285160946
VERSION     WP_285160946.1
KEYWORDS    RefSeq.
SOURCE      Serratia ureilytica
  ORGANISM  Serratia ureilytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 266)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 266)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14398439
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Serratia ureilytica"
                     /db_xref="taxon:300181"
     Protein         1..266
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29383
     Region          14..108
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          <141..257
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mlffhdvlpp dqpvrplard yhhgdsepeh yhncaqlihs lsgvvqvttr lgswvvppgr
       61 gvwvpakvvh slritgqvaa rtlfidplar adlpaqcqvv qvspllreli isameiapgy
      121 psggrderim elildelrvl pslplhlpep reasllalcr hiqatlaqpw tleqaaerln
      181 vsgrtlsrrf qretglrfgd wvrrarllaa lnalaigrsg levaldlgyd spsafsamfr
      241 rvlgvapsdy fsraaptltp dsarrr
//
LOCUS       WP_285160997             261 aa            linear   BCT 25-DEC-2024
DEFINITION  ParB/RepB/Spo0J family partition protein [Serratia ureilytica].
ACCESSION   WP_285160997
VERSION     WP_285160997.1
KEYWORDS    RefSeq.
SOURCE      Serratia ureilytica
  ORGANISM  Serratia ureilytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Serratia ureilytica"
                     /db_xref="taxon:300181"
     Protein         1..261
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28586
     Region          46..252
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 maknsteayg asgktnvlnf eperlhlvtd rshplyderi hlpldeamvl nimdqgvlep
       61 iivwkdpetg lscvvdgrqr vrhtleantr lvkegkkpki vpavtkrgsa vrmaqamisa
      121 neirradtpl grakkmadal erghdeedls lmfgvgvqti ratlalldat qavkdavesg
      181 ditvtqarql anltpdeqre kvkaveaata gtkghekarr qrqvigdvkp rmksrkeitk
      241 alegasgdya qalrwvlgde a
//
LOCUS       WP_285161315             295 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: amidohydrolase family protein [Sphingomonas].
ACCESSION   WP_285161315
VERSION     WP_285161315.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..295
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32542
     Region          7..292
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mtdtrppfvd ahfhlwdhgv lrypwldape ttpiaatyri adyraelaaw nlvgavhvda
       61 gadpdqgvde tlwlnqvada gglpdaiiar veldhpavep qlawqaaqpr vkgirhlinw
      121 hptdpgrray dhdltcdprw ragyallgrh glsfdfhgfp aqlsglteva eqhpevpvil
      181 nhlalpiptd gleewragli afaamphaai klsgagfigp rfdpvgfadi vaevierfgt
      241 drvmvatnfp tdrlaadldr tlgayeallt gfsdderrel wgrnanriyr lglnl
//
LOCUS       WP_285161268             439 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Sphingomonas sp.
            UMB7805-LC452B].
ACCESSION   WP_285161268
VERSION     WP_285161268.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. UMB7805-LC452B
  ORGANISM  Sphingomonas sp. UMB7805-LC452B
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 439)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Sphingomonas sp. UMB7805-LC452B"
                     /db_xref="taxon:3046424"
     Protein         1..439
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=46548
     Region          39..438
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mktpfssepa esyrsrsdap sgngrsgdas speppplail liddnpriae slaiaidlag
       61 hrldvalgpe dgfsrlaaqa ydailldlny aagrtdgveg lamldrvlad dpgaciivit
      121 ahsgirlavt amqagardfv mkpwrnaeli akielaarrr paphghaaap dttaeparll
      181 gdspaiaqvr dlirrigptm agvvvtgpsg agrsliaaal hatsnaaarp msridvrdpl
      241 awdrlgsaer gtswllrhpd rldeiaqarl ldrlrpedry iaiadeprai tpalarriaa
      301 veimapalae rqedvpllar hfsriaaerh glapprftpa aeallatahw pdearglaaa
      361 ieralllgen gvieaallap pvsaivapas trasfdldes eramieaali ehhhnvtqaa
      421 qalglsrgal yrrmarhgl
//
LOCUS       WP_285162385             530 aa            linear   BCT 25-DEC-2024
DEFINITION  UvrD-helicase domain-containing protein [Sneathia vaginalis].
ACCESSION   WP_285162385
VERSION     WP_285162385.1
KEYWORDS    RefSeq.
SOURCE      Sneathia vaginalis
  ORGANISM  Sneathia vaginalis
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Leptotrichiaceae; Sneathia.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437585
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Sneathia vaginalis"
                     /db_xref="taxon:187101"
     Protein         1..530
                     /product="UvrD-helicase domain-containing protein"
                     /EC_number="3.1.11.5"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62289
     Region          5..>529
                     /region_name="RecB"
                     /note="3#-5# helicase subunit RecB of the DNA repair
                     enzyme RecBCD (exonuclease V) [Replication, recombination
                     and repair]; COG1074"
                     /db_xref="CDD:440692"
ORIGIN      
        1 mkcdiisasa gtgktytmai kyllalnegv nfenilvitf tkkataeire riiiflkkii
       61 fkepgyedil asmstqidyk nlknayenml knsenikift ndsfinkift kticpryniy
      121 nfeteetnse eylkkllnal vsnkeyfkif ktfynldens keidkyydvi nnilenrpni
      181 ynylddlsnv qrervedfce ikgeiiqyls dktnltklak sflsannite ledfttsglv
      241 sraknefety fkeelvpkla kiyineviip yniaykklak icytldeklk fnyhnftfsd
      301 kafytykyni dpvdvfpnid iimidefqdt dpiqfeiilr lvtyakklfi vgdekqaiys
      361 frggdvslfr nlenilsdrf kdisikrstl ttcyrstnni idyvnnyfkd ipnfnydkvl
      421 ckktggyvkv fnnddlinhl venklytnta ilartnsdld vykkyleknn ihyesiqsir
      481 lyndknvinl mylidylvtt nsyslfkflr sdlvgytleq ikeiingeky
//
LOCUS       WP_285162645             334 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Shewanella goraebulensis].
ACCESSION   WP_285162645
VERSION     WP_285162645.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10106971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..334
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=36831
     Region          93..277
                     /region_name="vWA_BatA_type"
                     /note="VWA BatA type: Von Willebrand factor type A (vWA)
                     domain was originally found in the blood coagulation
                     protein von Willebrand factor (vWF). Typically, the vWA
                     domain is made up of approximately 200 amino acid residues
                     folded into a classic a/b...; cd01467"
                     /db_xref="CDD:238744"
     Site            order(101,103,105,184,212)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238744"
ORIGIN      
        1 mieftypqcf illfapiiiy liaptykekr ssvqvpyfeq lvditgekpq lgavvltrkn
       61 iqklllvlaw fclvvamakp emigaavtqq ksardlmiav dlsgsmdved fylpnqggnq
      121 tnsvdrltav kqvlrefvsq rendrlglil fgdapylqap ftndldtwlt llndtqvgma
      181 gqstafgdai glsisvfghh dtqnrvlivl tdgndtaskv ppveaakvaa asdikiytia
      241 igdpaaadee kvdlavlqsi aditggksfq aidtkalenv yteinqlepe lfesqtfrpr
      301 tsihfipial flslylisll ivtfrfprki ketr
//
LOCUS       WP_285162653             227 aa            linear   BCT 25-DEC-2024
DEFINITION  potassium channel family protein [Mycobacterium tuberculosis].
ACCESSION   WP_285162653
VERSION     WP_285162653.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..227
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=24068
     Region          <1..198
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mrvvvmgcgr vgasvadgls righevaiid rdsaafnrls pqfagervlg qgfdrdvllr
       61 agiqgadafa avssgdnsni isarlaretf gvprvvariy dakraevyer lgiptiatvp
      121 wttdrllnal mqdtetakwr dptgtvavae vvlhedwvgh ratdleqatg ariaflirfg
      181 tgvlsepktv lqagdkvyia aisgraaeaa aiaalppsed fesgarr
//
LOCUS       WP_285162708             644 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Shewanella goraebulensis].
ACCESSION   WP_285162708
VERSION     WP_285162708.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 644)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 644)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 644)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..644
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=69647
     Region          4..500
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mvehitgmla ligvlsllcq wvgwklrlpa ilplllcgll lgpgldilnp daifgdllfp
       61 iislgvavil fegaltlnfk eikdhgrmvt nlvtfgafit waciapaahw llgfewpmal
      121 lfgalvvvtg ptvivpmlrt vrpksnlasi lrwegividp igailavlvy eyiavaaaad
      181 ptthvlsalg mtlllgfglg aiagyligia lrttvfphyl kntavltiml gmfvgsnliq
      241 eesglltvtv mgiwlanmrg vdiadilefk etltvllisa lfillaarln stamldlgwg
      301 gvgvlmvvml varplsiwis gigtslsrsd kwflswvapr givaaaissl faikleaigv
      361 ngassivplv fliiigtvvi qsltagpwak flgvkadssq glllfgaskf srelakvltk
      421 knvkvmladn nwdnirqarm anipvyfgnp asehaenfmd lsgigrvlil spyrqlnplv
      481 sfhfqdllgt qkvyglnnae ggsarhqlse sylkrlclfg esvsyarias ymakgavikv
      541 tnitdnftlq dfkerygeta mpliyltkdq kvkiisgadr elpvgielis llpaeaqekd
      601 viqrnlkeva eresaadeds kqatieqeea qttatselee nepk
//
LOCUS       WP_285162722             784 aa            linear   BCT 25-DEC-2024
DEFINITION  efflux RND transporter permease subunit [Shewanella goraebulensis].
ACCESSION   WP_285162722
VERSION     WP_285162722.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 784)
  AUTHORS   Sandhu,P. and Akhter,Y.
  TITLE     Evolution of structural fitness and multifunctional aspects of
            mycobacterial RND family transporters
  JOURNAL   Arch Microbiol 200 (1), 19-31 (2018)
   PUBMED   28951954
REFERENCE   2  (residues 1 to 784)
  AUTHORS   Hand,N.J., Klein,R., Laskewitz,A. and Pohlschroder,M.
  TITLE     Archaeal and bacterial SecD and SecF homologs exhibit striking
            structural and functional conservation
  JOURNAL   J Bacteriol 188 (4), 1251-1259 (2006)
   PUBMED   16452406
REFERENCE   3  (residues 1 to 784)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
REFERENCE   4  (residues 1 to 784)
  AUTHORS   Arkowitz,R.A. and Wickner,W.
  TITLE     SecD and SecF are required for the proton electrochemical gradient
            stimulation of preprotein translocation
  JOURNAL   EMBO J 13 (4), 954-963 (1994)
   PUBMED   8112309
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..784
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85454
     Region          3..782
                     /region_name="MMPL"
                     /note="Predicted exporter protein, RND superfamily
                     [General function prediction only]; COG1033"
                     /db_xref="CDD:440656"
ORIGIN      
        1 mleklvngfe thlfrnrmwv ilsfvlitvf lgyqasqlqm daafsknipl nheymktytk
       61 hqkdfgganr imvsvedtsg nifnpeyfdt lkkvhdelff ipgversqvk slyspstrft
      121 evvedgfagg pvipadfrnd dyglnvvrdn vekagivgrl vsndyssaml taqlmdfvak
      181 tdeemaeseg aekdittkpl ntiqfakqle qqlrgkyetd tikihiigfa kmagdvaega
      241 qgvllfflia ilitavmvyl fsksliltil plvcslvavt wqlglltvvg fgldpmsilv
      301 pflvfaigvs hgvqminavr rrvldgqntk aasasafrsl lvpggvalls dtvgfltlla
      361 idigiirela isaslgvavi iltnlillpl visyttikpt kedpvkkaki enlwrslsrf
      421 atpkyavivl tctailygfg fqqasnmkig dlqggapalh ldsrynqdtf hitdnysitt
      481 dymtviveat peactyheil neidqfewmv gntpgvesta slasvskrvn agfnegnpkw
      541 qvlprttasl vqavgqvptt sgllngncsv mpvflflkdh kaetievvva kvkqvaeqln
      601 tdtlqfklas gpvgvmaatn eavseaqlpm miyvygavfv lclisfrsik atvavivply
      661 vvstlaqalm twldiglavs tlpvialgvg igvdygiyil stmsgkltqg mavqqayfea
      721 lvergsavif tgltlaigvs twffsalkfq mdmgilltfm flvnmlgaii ilpalsavfw
      781 rkpk
//
LOCUS       WP_285162723             337 aa            linear   BCT 25-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Shewanella
            goraebulensis].
ACCESSION   WP_285162723
VERSION     WP_285162723.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Rengstl,B., Oster,U., Stengel,A. and Nickelsen,J.
  TITLE     An intermediate membrane subfraction in cyanobacteria is involved
            in an assembly network for Photosystem II biogenesis
  JOURNAL   J Biol Chem 286 (24), 21944-21951 (2011)
   PUBMED   21531723
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Komenda,J., Nickelsen,J., Tichy,M., Prasil,O., Eichacker,L.A. and
            Nixon,P.J.
  TITLE     The cyanobacterial homologue of HCF136/YCF48 is a component of an
            early photosystem II assembly complex and is important for both the
            efficient assembly and repair of photosystem II in Synechocystis
            sp. PCC 6803
  JOURNAL   J Biol Chem 283 (33), 22390-22399 (2008)
   PUBMED   18550538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..337
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=37122
     Region          50..221
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          200..334
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
ORIGIN      
        1 msfrtlrhvv alslgyfist apvhaqfdpl svqiqplaes slvldiakag dnlvavgerg
       61 hvlinqqqdw tqinspvisq ltkvfflnek qgwavghdat iihtsdggit wqvqfqstev
      121 ekplmdilff nekdgiavga yglfyrtidg gknwvqefhe ellfpedvsy ladlkaedea
      181 lylseraall phfnrviqls dsqllmvgel glvatssdng qtfsaqafny egsmfnaiev
      241 ndavyvmglr ghvfktdkqf sqwqevelpv kssinnafvt dtgtlylvgn agvvieldss
      301 dnativarrq genivaiesd nqgqvwfags kglfqlk
//
LOCUS       WP_285162632             397 aa            linear   BCT 25-DEC-2024
DEFINITION  cation:proton antiporter [Shewanella goraebulensis].
ACCESSION   WP_285162632
VERSION     WP_285162632.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 397)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..397
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42566
     Region          2..>392
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mylelailav fafsysliag rvetsmisgp mvfvvvgfil gpsvlgwlgg efgnngmrvf
       61 adltlavvlf cdasnsnlsv lkkyisiptr mllyglpgai algvlvgyll fpnltvyeia
      121 alatmlaatd aalgkavvss pivpsklreg lniesglndg icvpilfvfl alaagsvaeg
      181 qvshiaftyl leelgiglmv glsasfiaak likysyqknw itdiwsqniv lslalccfai
      241 sqelhgsgyi aafsggllfg hlmkdvkhkm ilptegigei lalltwmlfg aivigsafes
      301 ftwtmliyal lsltlvrmlp iflalgrkge niptriflgw fgprglasiv fviimlerdl
      361 pggdfmamtv ictvfisliv hgvsakpmsk wistrvk
//
LOCUS       WP_285162778             279 aa            linear   BCT 25-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Shewanella
            goraebulensis].
ACCESSION   WP_285162778
VERSION     WP_285162778.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..279
                     /product="isopenicillin N synthase family dioxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31394
     Region          14..279
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 mkletidyrs encakqfves lretgfgvls nhpiskelve tiykewyeff qaeqkndflf
       61 kpetqdgffp asisetakgh svkdikeyfh vypwgripes lktnilayyk handlaaell
      121 gwieqyapad vaakfsiplp amiaesektl lrvlhyppma gdeelgaira aahedinlit
      181 vlpaanepgl qvqtkddnwv dvpsdfgnii inigdmlqea sggyypstsh rvinpegtdk
      241 tksrislplf lhpnpevvls drytadsylm erlrelgvi
//
LOCUS       WP_285162878             361 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Shewanella goraebulensis].
ACCESSION   WP_285162878
VERSION     WP_285162878.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..361
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41664
     Region          19..345
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 msesaktvnv kpaekkgfln sinhfrgiai ifivmahcyr pagwevetla dkawfnlmmn
       61 gtvffvfisg flfhhvfyhr wdykkymksk tkfvflpyil lslpwifwhl svgtdpamhv
      121 myadiekpvv aaswyvitgr tltaywyipm gmmlfalspw vmhlikrqhl livavplfii
      181 amlihrpesn lnaiqslfyf lpvylfgvwg sahrdklfpf idkywilmll laivlavaqa
      241 hwfgagtlnk aaleltvpdl mlpqkmlltf vilailnkfe hisikplqkl aevsfaiyfi
      301 hpwittpwwm iynspdifgl agsgnilttl ivtmlvivis yfiavaikkl fdkksrylig
      361 w
//
LOCUS       WP_285162880             247 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Shewanella goraebulensis].
ACCESSION   WP_285162880
VERSION     WP_285162880.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..247
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28121
     Region          31..245
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mlgnkqvysw fcgcfiimnv flsqmvfase itvytyqhvp faeqtdtthq gliidiidem
       61 fsraeieykv vfnplkrglt mtkrshnvcv lpivrtqqke sdyrwvgpvl isryglfssk
      121 sqaiplvtlq dakplsigty lgsgiseylt sfryqvqvtn ddalnikkle rnridlwaae
      181 lisaqalmrq skiqlgepel ifhtslrama cnetldkdkh dalvnalntm yqdgfmakln
      241 reygvll
//
LOCUS       WP_285162960             604 aa            linear   BCT 25-DEC-2024
DEFINITION  autotransporter assembly complex protein TamA [Shewanella
            goraebulensis].
ACCESSION   WP_285162960
VERSION     WP_285162960.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..604
                     /product="autotransporter assembly complex protein TamA"
                     /GO_component="GO:0097347 - TAM protein secretion complex
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=68399
     Region          1..604
                     /region_name="TamA"
                     /note="Outer membrane translocation and assembly module
                     TamA [Cell wall/membrane/envelope biogenesis]; COG0729"
                     /db_xref="CDD:440493"
ORIGIN      
        1 mcvalvslas nfawakddwl kieltgtser ltknilahlg espnsavqrr aflftvedsv
       61 taalesmghy hakvdidvte sekgpwklti didegaptii qwidikfsde mlnddsfnrw
      121 lnqltvkpgd tlnhgvysdl ksqlvtlala rgyfdatfar seieinrdfn takihidfqs
      181 gkryligdvv fsgqtvnddl leklipfdpn akystsrlnr lnrnlidtgy fssikvlpli
      241 dnisdsqvpi kvdlaprpth sfevglgadi gnnvenniep rirltwrmpe inrfghtqet
      301 tmewspdrpk flttytiplt hplddqlkfk vgllrdkygv tqdyneenks ydytgelese
      361 krligiirqm rldsgwlfgy slefnqefyn qsdtdydpqy ilagfgigkt trgdntldpk
      421 sgfrqvysve ygdpnlgsei rlakleakfk widtffdrhr fvarldlgan iadsdqidqi
      481 spslryfagg dqsirgysyq elgpyieyen seggtsrqvv ggrylvvgsl eyqyyltdtw
      541 rvasfvdagn afdteqfepv vsvgggihwi spigpikldl gvglketetv drswrihitm
      601 gtel
//
LOCUS       WP_285162899             342 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Shewanella goraebulensis].
ACCESSION   WP_285162899
VERSION     WP_285162899.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   6  (residues 1 to 342)
  AUTHORS   Higgins,C.F., Hyde,S.C., Mimmack,M.M., Gileadi,U., Gill,D.R. and
            Gallagher,M.P.
  TITLE     Binding protein-dependent transport systems
  JOURNAL   J Bioenerg Biomembr 22 (4), 571-592 (1990)
   PUBMED   2229036
REFERENCE   7  (residues 1 to 342)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467926
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..342
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37919
     Region          1..341
                     /region_name="SapB"
                     /note="ABC-type antimicrobial peptide export system,
                     permease component SapB [Defense mechanisms]; COG4168"
                     /db_xref="CDD:443329"
ORIGIN      
        1 mwryflrrin lffatslvmi avlffatgmf pvdkgyalsg iqfptaeqqa qtiedyqleg
       61 nqlsqfvayv tqrlsgnlgi svnsqqsvad elsavlpasf elslfagcla vffgvplgvl
      121 aslsksksvq rsilaitltg ysipvfwlgl tltlwfgvql ewlpisgqin llyeiepvtr
      181 fmlidtllse etyrmsafkd allhiilpav tlavlpftvv iritrqammt vmtqtyiraa
      241 earglntyri llrhalpnal ipvlkafglm lgsfasygiv vevifawpgv gswlingiyq
      301 rdytviqagi lsvslliifl sivielvhtt inpinrkely an
//
LOCUS       WP_285163018             348 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Shewanella goraebulensis].
ACCESSION   WP_285163018
VERSION     WP_285163018.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10106971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..348
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=38795
     Region          82..272
                     /region_name="vWA_BatA_type"
                     /note="VWA BatA type: Von Willebrand factor type A (vWA)
                     domain was originally found in the blood coagulation
                     protein von Willebrand factor (vWF). Typically, the vWA
                     domain is made up of approximately 200 amino acid residues
                     folded into a classic a/b...; cd01467"
                     /db_xref="CDD:238744"
     Site            order(91,93,95,168,196)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238744"
ORIGIN      
        1 mfsitwpwll lllplpfllk qkqvakntgg hlqlpgiget eqqvtisqhk psrkaywlmw
       61 lcllcalirp qwlgepielp segrdvmlav dlsgsmqied mivegktvdr ltlikhvigd
      121 fierrngdrl glilfadhay lqapltqdrr svakfladse iglvgkqtai gesialavrr
      181 fdmvndsnrv lilltdgsnn agniepevaa riaakrnvti ytvgvgaevm errsifgter
      241 vnpsldlded qlqnladmtk ghyfrarnse elaqiyqkid elepvsrdql tyrpkselfy
      301 wplllallms vfislrgqfa nklnlaasnq aslksnissd sskptggl
//
LOCUS       WP_285163060             920 aa            linear   BCT 25-DEC-2024
DEFINITION  S9 family peptidase [Shewanella goraebulensis].
ACCESSION   WP_285163060
VERSION     WP_285163060.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18486225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..920
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=103866
     Region          416..>530
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          654..902
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mtlklhklip ltlltasmsl taaeqatsls lndimhfetl kqpvlsdngr tlaveampdr
       61 gdsralinii eskkqfvidg gsdvkvnsqg syaiamlkps lldketlkks elnsglalln
      121 tatgeqqrfe kvkqaefsdd glflaiwfdv edekeadsdd kdapkinekd igsaiklikl
      181 adnsshdfin vtqfafdrvg knfvvaindn kakqhfikkv nlanntlkql ykstdnqige
      241 lslsddgnwl aftqgnatdd rdereyqlsl lsletfelkd tpqdddwtln qyskvffsed
      301 slrlflgrvp qvdkiislae ieteadlfde tvvtglrnlk vwhgddpkik pheikqyske
      361 vqrtylavlh inanrivqla detipnvlyg eqqryllats dvpyqkmitw agfyqdvylv
      421 dlntgrkqql ltqhptnemp tlspnarfva yyqqgqlfmy diagvrkhti srdisvsfan
      481 edhdypgnap sygfgpwlad gsgiiaydky dvwqfntssf dgymltkgqg retstqlrie
      541 glyedqnapa evtqeqsvli hgynestkad slysvtigvp gltelvdska klkvlarskn
      601 adtivysker ydlypdlyta svtspndavk qtdldkqrdg fnwgsaelvq wsdadgrktd
      661 gvlikptnyq egkqypvmvy fyrfmsdrlh sfphmainhr pnfawyadng yaiflpdirf
      721 evgypgasav kgltsgvqkl idmgiadpda vgiqghswgg yqtafavtqt nifkaavtga
      781 pvsnmtsays girhgsglar qfqyetgqsr iaeslfqspq kyienspvfy veriqtpmmi
      841 mfgdkddavp weqgvelyla mrrtgkdvvf lqyedephhl kkypnkldyt irmkqyfdhy
      901 lkgakapewl ekgeaykeyk
//
LOCUS       WP_285163077             449 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Shewanella
            goraebulensis].
ACCESSION   WP_285163077
VERSION     WP_285163077.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..449
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=49021
     Region          4..439
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mveaklllve ddeslreall dtlllasyec vdvasaedai ialksaefdm visdvqmegi
       61 ggigllnylq qqnnkvpvll mtayatidsa vsaiklgavd ylakpfapev llnqvsrylp
      121 lkqnldqpvv addkslalls iaqrvassda svmimgpsgs gkevlaryvh qnstrseqpf
      181 iaincaaipe nmleatlfgy ekgaftgayq acpgkfeqaq ggtilldeis emelglqakl
      241 lrvlqereve rlggrktisl dvrvlatsnr dlkemvaagg fredlyyrin vfpltwpaln
      301 qrpadilpla rhllvkhakn anisptpald evacrrllty rwpgnvreld nviqralilh
      361 sgdgistndi ildssevdlq qpepkqskta aendglggel kaqehviile tlnqcngsrk
      421 dvaeklgisa rtlrykmakm rdmgiqvpa
//
LOCUS       WP_285163157             502 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Shewanella goraebulensis].
ACCESSION   WP_285163157
VERSION     WP_285163157.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..502
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=56920
     Region          <79..489
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mlsieiiivl fialilllgi vlggyfqqgk fiaeltqtle snnvtqspln fkhtprafkp
       61 lvhnlnlfqq nnpitlerdk ltglsnrvgf krkmfakmpa tegmlvlvdi qqfrfvndlf
      121 gfifgdqllk sfakrikelg nppqfvsrmn gnefllfypk qissfelnsi kqhlqkpfei
      181 eqtpisikvq lgvlelhdhh advslmlrrl dlalkkakvs nkdiafynqd ddkaqyrelm
      241 iinslpkslk qnqlhmvyqp kldissgkce qvealirweh sglgnippte fiplaehtgv
      301 idliskwale qvlkqqvkwl qqginikvav nlstkdlenq hlpidisnll tqykvpaenl
      361 mieitesalm ldlartietl keirelgvki aiddfgtghs slaylrhlpi devkidkafl
      421 ddfncdiqan kivktsiela kslgfdvtve gvetkdvfdt liefgtdtiq geyvskplia
      481 adlelrfsql iqqpfvsipt kh
//
LOCUS       WP_285163197             435 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC1 kinase family protein [Shewanella goraebulensis].
ACCESSION   WP_285163197
VERSION     WP_285163197.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195515
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..435
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48456
     Region          91..341
                     /region_name="ABC1_ADCK3"
                     /note="Activator of bc1 complex (ABC1) kinases, also
                     called aarF domain containing kinase 3; cd13970"
                     /db_xref="CDD:270872"
     Site            order(145..149,151,161,163,222,241..244,284,288..289,291,
                     302..303)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:270872"
ORIGIN      
        1 mtkdvakvps srlsrlskig glasrlagnv lvegakqlsk gqspklqelv ltprnisqva
       61 eklaqlrgaa mkvgqmismd tgdllpaels eimarlrdda kamphkqlve ilkqqwgndw
      121 lmpfaqfelr pfaaasigqv hlaylgsgek lavkiqypgi kdsinsdidn vatllkvaql
      181 vpdhvqfdkl lteakaqlhh eadyeyeanl lkqyqqwvag derfivpkvy eslstdsilv
      241 mefiegeaie nvarldqqtr dniatnllal fldelfefkl vqtdpnfanf myqansgkiv
      301 lldfgatrqi seplsagyrk lmqgamtndk almtqaasei gffqkditie qqqlivdify
      361 qaceplrsea eydfassnla kritdaaksm stkpdewhtp ptdaifvhrk lagiyllasr
      421 ikakvdvkkl flshq
//
LOCUS       WP_285163217             296 aa            linear   BCT 25-DEC-2024
DEFINITION  TolB family protein [Shewanella goraebulensis].
ACCESSION   WP_285163217
VERSION     WP_285163217.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..296
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=33008
     Region          169..>292
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 mksivilitc iavtssffpq qdlyaapyhs alakdkvvef apgiistkan feintvfnka
       61 gdnvifarck ddfshctmmq ssfvsgewqq ptalaisgey ldadpyysad ysqlyfvskr
      121 plegeqeeak evniwrstwk ndqwqqpeyl dinsdaadly psltdkgely fpsfrdngrh
      181 mfvaqpkgng fatpeplssh iygvngnigd savsrdgnti vfsikdreds rgkgdlyisn
      241 rvngkwtian slgdkvntad heftpiispd gnylfftrie ngkgnlyqih lsaldi
//
LOCUS       WP_285163300             491 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Shewanella goraebulensis].
ACCESSION   WP_285163300
VERSION     WP_285163300.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..491
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55192
     Region          45..465
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mdksiaclnt nfqksslvsv lflnsifvla vsllpfnsha fqcdlkpqfe qlrqieqqis
       61 lneldngmiv rqvnrplqst vaiasqfnvg srnetegqtg yahlfehllf kgsenapkds
      121 ypqqmsaiga rfnasthfdy tnyyltipaq alelslfles drfirpvlsq ttvknqqgav
      181 leemattidn qpylrpamef llsqvaespy ahaiigskad visatpiele qfhqryyrpd
      241 amqlslvgkl esdslqtvkq yfadwqapnh sqdtftsiav tpmaikteiv dgrgpwpall
      301 mawhtvgrnh pdyeainllq nhlfqnlksa lasntlenpp qmlsysiplt menhgvtnlv
      361 lvprantsln elqelvaslf nevmqtgine qalcglkaaa inkaqqhytn sqslakflsn
      421 tsvrdkyhpi tqpwqrteav ssadiqrvtk qyfidkavrv dllppwyirw gkalleimpq
      481 gfanslerwa l
//
LOCUS       WP_285163333             358 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Shewanella
            goraebulensis].
ACCESSION   WP_285163333
VERSION     WP_285163333.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..358
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40366
     Region          5..331
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mqtniqrqla mleqiprhpr kitanvltkr lqdrdfdvgl rtvqrelksm sdmglfglel
       61 ddrckpfgws isacwrglnl tlmdqhmala fhtlkhsaaq llppqsvkql tpyferadqv
      121 lasdpdnpwl ywacrvaqlp epspliyseq dsaafklvqy allhkrqiac qiqkvikgqc
      181 ywveyspinp egitisegva llaftvgsvh tkryvqsidl lndirvldtp avtrddfdin
      241 lsgaetqsni idiellvsas asfilrkakl senqtiqllk dgryqvkatv ndskrlrafl
      301 wemadnievv apeklrahft rliakvsmqy qssnidlndi dlididsnat sevvaiag
//
LOCUS       WP_285163373             542 aa            linear   BCT 25-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Shewanella goraebulensis].
ACCESSION   WP_285163373
VERSION     WP_285163373.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Pereira,J. and Lupas,A.N.
  TITLE     The VCBS superfamily forms a third supercluster of beta-propellers
            that includes tachylectin and integrins
  JOURNAL   Bioinformatics 36 (24), 5618-5622 (2021)
   PUBMED   33416871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..542
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=59755
     Region          251..334
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          323..395
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          459..522
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mnlfnrtsln tllvsctgll laahcqsiaa etsftpqfta hhidadfelt qgivsanile
       61 hqgneliavg vddnherwla iygfenealv qldklmlskd iysfdinele pakvsgfnqa
      121 evltqqlffv tdnallqysp aqkkllvstt epdeeldsvd vmpnqgslkk vadiqsisvt
      181 tqadyisrgn fvidinnddi adilisdfre tavllgqang gfiqqslpll pvvelknnga
      241 eyshaklyhs dmnfdqrddi ikvgegslev yyqqedgqfs eiaefisvsq pisgvdwwnk
      301 rdaygenldq sdllyrkver igdvngdgis dlvvrytkss gvldrvndye iylgsnnngq
      361 lsfpreanti ikadgtltgl rfedldndev devivagfdi gltqivsall sgsidqdvhi
      421 fkmndaslfa dkanvskeve lsfsltsgqs gepvvaladi ngdgfkelll sddneeldiy
      481 ygqagsepfk kraeewsvti pvegamlsav dinadgkddl llkfgrqdpe nlqrrfsvli
      541 an
//
LOCUS       WP_285163544             409 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Shewanella goraebulensis].
ACCESSION   WP_285163544
VERSION     WP_285163544.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..409
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=46504
     Region          1..397
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mnnkqlnkii kdgvpgrtai ggglyfrlst sgtcswqvry tinnkrkwft lldsyphlsi
       61 adakhdavll lrdvkhgkdp alekknalqe eivtvhqlfn dwfktdinkr lkhpeiphri
      121 ytkeiapfig elrlkdvtal qvrsiihkvi esnrpatand tlmytkqlfr haaklgvven
      181 npalaftmsd aggaeksrdr aldldeisrm ftvlrsqaht ftrdnylaca llitlgvrkg
      241 eliaaqwqei dfdnevwhlp sersktgiai siplpadvie wlnelkvrsa gsiyvfpsrr
      301 asvrrgyisd dtlnhalakl fgkkvdskkq ptknhfeeqg vnhfvvhdlr rtcrsllayl
      361 gvsshiaerc lnhklkgveg iynrhdylee rrdalnklsh lispivnqk
//
LOCUS       WP_285163565             291 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Mycobacterium tuberculosis].
ACCESSION   WP_285163565
VERSION     WP_285163565.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..291
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31836
     Region          19..277
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtvparptll fadiadvsrr laetgylpdt atatavflad rlgkpllveg pagvgktela
       61 ravaqatgsg lvrlqcyegv dearalyewn hakqilriqa gsgdweatkt dvfseefllq
      121 rplltairrt eptvllidet dkadieiegl llevlsdfav tvpelgtlta trapfvllts
      181 natrelseal krrclylhid fptpelerri llsrvpelpe hfaeelvrii gvlrgmqlkk
      241 vpsiaetidw grtvlalgld tiddavvaat lgvvlkhqsd qqratgelrl n
//
LOCUS       WP_285163728             129 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Shewanella goraebulensis].
ACCESSION   WP_285163728
VERSION     WP_285163728.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..129
                     /product="YybH family protein"
                     /calculated_mol_wt=14269
     Region          1..121
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mtqstttenp vltackngia awqsafnnqd akgcaaqyqq ncimtarpfg vfegreaiea
       61 fwqgimdqgf kdvdytdvtw eaegdngyil tsswtmnkaf gvvhrelwvv eadgkarlas
      121 defevqger
//
LOCUS       WP_285163766             609 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF885 domain-containing protein [Shewanella goraebulensis].
ACCESSION   WP_285163766
VERSION     WP_285163766.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..609
                     /product="DUF885 domain-containing protein"
                     /calculated_mol_wt=69108
     Region          1..606
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
ORIGIN      
        1 mrklilpaii mlavtgckmt tgskaqyylg etqkaetnts tpkqtqsatv edmslkaiid
       61 sawqinldys pqmayslgde akaallpdls petlaeknlr lktllsslkq ldidklsktd
      121 kinaqilqyq lqndvdmyty kdhylpitae sgfhayiasi angrlhsead yqnylaklna
      181 lpkyfaqqtf wlqqgsssgi tpakvtlngf edsisayivd vedsgyykpf tdfpehfsda
      241 qkaelaaegk kvvkekvlpl yqqffdymtq eyipnartsi aakdmpngka fyqnrveyyt
      301 tlnmtadevh qlglqevari raemeqviad vefkgtfaef lhflrtdpqf ypktaeellk
      361 eaayiakkad avlpqyfatl prtpygikpv paeiapkytt grysgsnrdd eagyywvnty
      421 alnkrplyem ealtlheavp ghhlqislnk eltdlpnfrr ysyisafgeg wglyseylgl
      481 eagfyqdpys nfgrltyemw raarlvvdtg mhtkgwsrde aiefmasnta lsmhnvttei
      541 dryiswpgqa lsykigelti krlrdkaese lgerfdirlf hdallqngsv tmdileqkvd
      601 efieeqkaa
//
LOCUS       WP_285163801             377 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Shewanella
            goraebulensis].
ACCESSION   WP_285163801
VERSION     WP_285163801.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..377
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=41900
     Region          1..377
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mkkrllfkas ilagflilss svqsadldkr qselkaiqaq inqqqnslkd ssrqreklis
       61 llkrdeqais saaqkvnltq asltqvntkl geleveqvel dkrritqqkt lskqlssayl
      121 agnhdyskmm lnqqnpatve rmlayyqyln nariaaitnl kttieqleai kdqqvseqqk
      181 lnaliieqkq qaqqlnkeqs qrqqtlaqiq rtltskgael eqmqieeasl krlieqalla
      241 akdnpqmdgl akkrgqlkwp tkghlaskfg srrsgqirwk gvviaapegr sitavapgtv
      301 iyadwlrgfg mvmvvdhgeg ymslyghaqa lliqpgetvq kgesialvgs sggqtesgly
      361 feirhkgqav npakycr
//
LOCUS       WP_285163808             533 aa            linear   BCT 25-DEC-2024
DEFINITION  SLC13 family permease [Shewanella goraebulensis].
ACCESSION   WP_285163808
VERSION     WP_285163808.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..533
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58756
     Region          142..523
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mskeiadnvd pldmnqykme rlpvrsktnf eiwlaksgvw ialaafifll tgspasfltd
       61 fdpsmlsksa aehfhnvglt efswhgqaml aifctavilw itepipnylt slmviialvl
      121 tgvlperqay aqlghpimwl nilsfilasm lvssgaakrf alwficrfgt satpifysfm
      181 vinlalsafi sattakaail mpifmviaav ygarggdnkn nfgrnlvlqn llqinlcaga
      241 fvtgsganll aasliagaig gsfffadwmi vampivicmi vigwllatkv ffplkpeerl
      301 pqieggmerl qeelakmgkv sfreiksivi fvtilffwat dkyhgvsata iafigaiial
      361 cprigvvnwn qvdvpwhlll fsagaytlga gfkqtdlpnl avnfsleyfg ldestpfsvf
      421 yimltgamll sslvfqsktm rtmlfvpiai giaqrfdfpi mslalpvall iehvyvlpfn
      481 skpalllyst dqyslsdsfk fgfsmlmigw atsilmgetw fkwlgyapng vfw
//
LOCUS       WP_285163858             367 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA desaturase [Shewanella goraebulensis].
ACCESSION   WP_285163858
VERSION     WP_285163858.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Los,D.A. and Murata,N.
  TITLE     Structure and expression of fatty acid desaturases
  JOURNAL   Biochim Biophys Acta 1394 (1), 3-15 (1998)
   PUBMED   9767077
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..367
                     /product="acyl-CoA desaturase"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0006636 - unsaturated fatty acid
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=42520
     Region          2..281
                     /region_name="OLE1"
                     /note="Fatty-acid desaturase [Lipid transport and
                     metabolism]; COG1398"
                     /db_xref="CDD:441008"
ORIGIN      
        1 mkkppiiwln tslfaltllg aitlvpwrgm thgfeaiewv afvvlafasg lsitagyhrl
       61 wshkaykahp vmrflfalgg alalqnsalh wssdhrihhk hvdnndkdpy sakkgfwysh
      121 igwmlreyqa sryhdynnvr dlqkdaivmw qhkhylalvv lmniglpafl gwlngdiism
      181 vlmagllrlv vvhhctffin slahiwgsqp ytnkntardn gvialltyge gyhnfhhife
      241 ndyrngikww hydptkwlik smhwvglasd lrvvpqerie saklqmqllr aqdkvahlpn
      301 cdeiianfqa eydlmkqhlv eyyqakksli eakrkqlsyq qlslqveelk arllaqkknw
      361 nnitaay
//
LOCUS       WP_285163945             386 aa            linear   BCT 25-DEC-2024
DEFINITION  Kelch repeat-containing protein [Shewanella goraebulensis].
ACCESSION   WP_285163945
VERSION     WP_285163945.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Shi,X., Xiang,S., Cao,J., Zhu,H., Yang,B., He,Q. and Ying,M.
  TITLE     Kelch-like proteins: Physiological functions and relationships with
            diseases
  JOURNAL   Pharmacol Res 148, 104404 (2019)
   PUBMED   31442578
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Gupta,V.A. and Beggs,A.H.
  TITLE     Kelch proteins: emerging roles in skeletal muscle development and
            diseases
  JOURNAL   Skelet Muscle 4, 11 (2014)
   PUBMED   24959344
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Adams,J., Kelso,R. and Cooley,L.
  TITLE     The kelch repeat superfamily of proteins: propellers of cell
            function
  JOURNAL   Trends Cell Biol 10 (1), 17-24 (2000)
   PUBMED   10603472
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..386
                     /product="Kelch repeat-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=42175
     Region          24..>229
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          99..142
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          146..191
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
ORIGIN      
        1 msrlsqlgav italvsfmps anasypqlpe gvsnnavakv ktakgdylls ftglaegkgy
       61 qavhnkvwgv nlsapnplwq plnpvpfvap lagrlasiav glndkayvfg gytvaknhee
      121 istvdnyqfd vlnnqyqria dmpvavddta asvyqqryiy lfggwhndgn vnlvqiydtk
      181 tntwdqaspm papavfgqav amsgnkivfc ngvkvqanig krrsyqsspv clygevnpqn
      241 hlriswqllp hysvaneqae hdsqanhsla nnlqktpvah yrmaatgvkt gksgqaifma
      301 gsdnpynysg igyngepsep ysqqytfdfd tmqwlkplql etpsmdhrgl ichqgkllrv
      361 ggmleqqqvs kqvlvsplln gqkctq
//
LOCUS       WP_285163948             426 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Shewanella goraebulensis].
ACCESSION   WP_285163948
VERSION     WP_285163948.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..426
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=48811
     Region          8..411
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mavkdkltnt tlemllrkki skpvtqsdgl glsiraspsk vskqnnmnwl fryrigdrts
       61 npetivlgny pdltiakark krdefkswla dgkdpkveva lalektlkpi tvsdaldywi
      121 neyatekrtn slkhrqqfnk wlipelgrlp lgnikkahwi ntirmrskqy pvaagyvlrn
      181 lqqalkfcdk rgyeldrsif didfvdigas kqskrsqrlv eddswqrled likwlgtgkm
      241 mpyyrnltll lisfgcrtqe lrlaetkefn fetrvwtvpa ahnktrdkdq akgesgeikr
      301 pipnelihml knlceqssng yllgelkrse tvsswggkiy kllgheqaws fhdlrrtvat
      361 glndigvaph vveallghsi qgvsgiynrs qylpekldal nkwqerlell rgdtdnvlml
      421 sksvra
//
LOCUS       WP_285164182             242 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Mycobacterium
            tuberculosis].
ACCESSION   WP_285164182
VERSION     WP_285164182.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..242
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25840
     Region          10..238
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mdgrasferd vagigalvdp vrrqlyqfvc sqsmpvsrdq aadavgiprh qakfhldrlt
       61 aeglldteya rltgrsgpga grtaklyrra grdialslpq reyelagrlm aaaivlsatt
      121 geptvevlnr iahdygqamg aaattrppad paaaleltld vlrkygyepr rpagpgddev
      181 elvncpfhal areqtelacn mnhalitgva dalsphspav rlapgparcc vvlkrcsahd
      241 pe
//
LOCUS       WP_285164403             345 aa            linear   BCT 25-DEC-2024
DEFINITION  sulfotransferase family protein [Shewanella goraebulensis].
ACCESSION   WP_285164403
VERSION     WP_285164403.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..345
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=39235
     Region          8..231
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
     Region          <321..345
                     /region_name="SecA"
                     /note="Preprotein translocase subunit SecA (ATPase, RNA
                     helicase) [Intracellular trafficking, secretion, and
                     vesicular transport]; COG0653"
                     /db_xref="CDD:440418"
ORIGIN      
        1 myhfdrpiii lsaprsgstl lfevlsknna lmtiggesha liekipslni ayrgfssnal
       61 nqqdidinlr qhllqrfsde mldsegqran smagtifrfl ektpknslrv dflnvlfpda
      121 lfiylvrdpk enissimqaw qsnkfvtypn lpgwnkrnws lllpekwqtl ngetlesiaa
      181 fqwqeannai inslkkinsa rwcmvsyeql vnqtektier lchfsgieft eelaqicsqa
      241 lphsrytisa pkadkwlany seikkvwpsi ettickinqc lgkhglpvfd sewhyhemge
      301 satgivkesg alndkkdtny knvtrnslcp cgsgkrfkqc hgalr
//
LOCUS       WP_285164541             637 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Shewanella goraebulensis].
ACCESSION   WP_285164541
VERSION     WP_285164541.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 637)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 637)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 637)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..637
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=71475
     Region          <184..607
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mtrisklllt ilsflmmlyv llvisfsqgl etihsdnfhh kitsidvsdv vnanagweal
       61 lflegdivks elhyfavler tdlhlnvvrv kdvfsemmmf snmplllmvl layaipfyik
      121 sriarknnas ldfinnetdk llasfniqlp pskqpntlsq isialnelnk hvkaqniqtq
      181 lsiyqdkltg lidrhayleh lekqlqraee agtrqallfi dldgfkqvnd sfghsfgdei
      241 liqvahrlqt vvrnnqlsrv sesfelelnl srlggdefsi fienipdnlr avevsknvlq
      301 eierdfvlgn kvikigasig iatfpdsasn pntllqmadv amyraktdgr gifrvyspem
      361 gskirrfhyl leemrlaias qsftlsfqpi vnvddcsidy feslvrwnhp iegpispvef
      421 ipiaedsnli lelgnwilfe acrqmsawyn agmnkvrmsv nisgvqlkhv piydwvmdtl
      481 tktglppnal lleitesclf hasnkiiedl enlrkqgvli aiddfgtgfs slstlanlpv
      541 diikidklfi dqatinpkye kilnsisdlg ktlnlkvvae gvevasqfel vknlgihcvq
      601 gylisrpess ydvgsnvikk nlnhialtgt gvctpsk
//
LOCUS       WP_285164542             427 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Shewanella goraebulensis].
ACCESSION   WP_285164542
VERSION     WP_285164542.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..427
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=47493
     Region          200..426
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mfakvsgldk slhknwdnsw gknkeqlall rlinwllklg liffgtelfd ltrppvglty
       61 vfilelvyva ccyrfrfqci nrpsillmtl vldtlfwaiw lfytggatna fvsllllpva
      121 igavtlprwa pwvltllstg myslmmftmp enrirhhgmd msshylgmwf nfvisalvlt
      181 vtvgyiakri rqknaqlsyl reaqlrqekl lalgtvsaqm ahqmatplst lrllvdelae
      241 egvandiepe mqqalircet tlaelrlate sirqqksysl sveklvrdtq eqvqllmpet
      301 qlnieaesea satrvkadts llpailalie ngarasleht stskvsvfvs avepnsvsft
      361 irdygcgmep nqltdlgnni annpkgmgig vllshasfer lggqlslrvh pnggmiasvt
      421 lpvtqne
//
LOCUS       WP_285164586             773 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Shewanella goraebulensis].
ACCESSION   WP_285164586
VERSION     WP_285164586.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 773)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..773
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=87827
     Region          <333..400
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
ORIGIN      
        1 mipvlqrtqa gdvskqyrhs erdkpaktkf lsllclmtfa igfsnsvsat evstvttant
       61 evttqanqvl rnklyrqaly yyfegdyqaa lrqvsinrqr fdadtaksql feaglqvsvg
      121 lhqkatrtls sfeqtlaieq altgnknqan qtssqsqknt spaelklval lqlseqqieq
      181 gqpyqaqqtl qritqvpnsy ieqyhilnql aywpnepaim akiaggvnas asinhdnptd
      241 nqsassslsa yvmlnqalhf ieqkqyqqae tllitiknmp laetetgfwq slftektpse
      301 ltapmtaeni ensqksvtaq esdqqvqqqa indyaqllla qsyvkqgqfq aaftqlkdfp
      361 qqspytesal flyafsaqql qqypislall dllkrqypys lmgwqsaill aaqvreqqsl
      421 eqsltsyqda ealyleqlaq ldafeavlet rfntslimqs altpqglspe alekqpwlek
      481 altdnalknd fttlaslsll eqnltqqqrk sdwlaetidl nkqrrekrls qqqlsdyenl
      541 isqlterkqq lskqiqavdv pvdeitfqqm qlfansteqa wlqriesskq alaniastrd
      601 teddllrltr vegalnwqlq qsfiprlwqh kkllkdidtq lqvlnaqyvr fksvsqsqqg
      661 ateydirqqn lakqieditr dikqasdktq ltiqqklrlf tqnqrqqltq llltsrhema
      721 avlermsqqd itpskaitsd nlnttklmpr qehsplsslt ahfkqvekhy aah
//
LOCUS       WP_285164674             149 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Shewanella goraebulensis].
ACCESSION   WP_285164674
VERSION     WP_285164674.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 149)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 149)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008128
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..149
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16303
     Region          1..149
                     /region_name="CytC556"
                     /note="Cytochrome c556 [Energy production and conversion];
                     COG3909"
                     /db_xref="CDD:443115"
ORIGIN      
        1 mksiifaiaa salliptvna hnfedtddai dyrksgfsli ryqfgdmgam lkgkkdfdln
       61 vfqtraanla alskiphegf idgsdkgnte alakiwnnka dfdekmttfq enaaklniaa
      121 qtgdkkqikq afgntgksck gchdmykkd
//
LOCUS       WP_285164846             875 aa            linear   BCT 25-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Shewanella goraebulensis].
ACCESSION   WP_285164846
VERSION     WP_285164846.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 875)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 875)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 875)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 875)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 875)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14303130
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..875
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..875
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=94674
     Region          92..>484
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          458..674
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
     Region          707..858
                     /region_name="Exop_C"
                     /note="Galactose-binding domain-like; pfam18559"
                     /db_xref="CDD:436577"
ORIGIN      
        1 mkkanrviar kqltlplqii avlvglsacs dddkkaipte vesdkqvvvk vtetneaant
       61 mennidiwpt ldiplakdae learisklme kmtleqkiaq miqpeirdit vedmrkygfg
      121 sylngggayp nddkhatpad wiklaedmyq asiddsvdgi aiptmwgtda vhghnnviga
      181 tlfphniglg aannpdlird iaaitakevm vtgidwvfap tvavvrddrw grtyegysed
      241 privkayshs iveglqgkvg ddflsdqhvi stvkhflgdg gtekgidqgq nmdseqelfd
      301 ihaqgyvggl tagaqtvmas fnswqgkkih gekyllndvl kdkmgfdgfv vgdwnghgqv
      361 dgctnescaq aanagldvfm vptsawkply entiaqvksg eitqarvdda vrrilrvkfr
      421 aglfekpspa nraisgktel igakahrdva rqavreslvl lknnanilpl apnskvlvag
      481 daadnigkqs ggwsitwqgt dnlnedfpga tsiyagieqt vnaaggqawl svdgqfeavn
      541 kpdvaivvfg eepyaegngd idnleyqrgd krdlallnsf ksqgipvvsv fisgrpmwvn
      601 pelnasdafv aawlpgtegd gvaqvlfsnv dgkvnadfvg klsfswpttp qqttvnvnde
      661 nyqplfaygy glkygeksqv sdslsednfa seakleplal feravkapwk liigtestmd
      721 tvsssiqqnd altlrtfdka vqedarlvnf ngtglgfvgl isnfprdlra ysnsnaalsv
      781 likttnkvek pvmlgvacdr dcradvdiag alnssvgdwq tisvdlkcfa nqqvdfgnin
      841 tpfylatdgk aeinfsdlli vpnaaddati tcpvs
//
LOCUS       WP_285164917             675 aa            linear   BCT 25-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Shewanella
            goraebulensis].
ACCESSION   WP_285164917
VERSION     WP_285164917.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 675)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 675)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 675)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   4  (residues 1 to 675)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..675
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73759
     Region          13..643
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mnfikpshks lhlsilsiai lasfnvhaek verdpilniq evivvkgegp taaqssmthw
       61 disreeieas gaqsldlila nvpgiyvrvg gqgaprvdir gfkarhviyl ingvpandae
      121 dgqfdpsvip asqiesvevs vgptsvlygp ggaggvinii trqgdsspsv sgnlefaend
      181 tingnvnlag sgekwqgfas ynrqqtdgfp mssdfedtde qsgdtrlnad ktvdnfyaqg
      241 syfvsdetml tanvnyksgn wgkpstdgtg tskskfervd dfestivqlg fahkfsdrla
      301 lrgygyhnes qvfetvytss dysdidstqd gistvqggnl qliadfdtag lltgsiisek
      361 qtwesvnyea nassasilgs gsgsgsgsgd gsgssddfnk dgwlntlave yqyqndgkyg
      421 vtiggaahsq erddaddtny saqlssfwrv tddsklhagi arkvrfpslr nlyaqssgns
      481 elepeesshv elglnqglay ntslditgyy tdaenyiakd ndgvyqnisn yafkgvdfsv
      541 rneyfddldl tvsysyldae dsdndlmnel eyrpkhqfrf qglyqfdfgm svnlnveyia
      601 dqiyytseki sgetvsvkne mdsytlvdin lvqpllvdnl eayiratnll dvnyyqseal
      661 pqagrqifvg inwqi
//
LOCUS       WP_285165188              57 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Shewanella
            goraebulensis].
ACCESSION   WP_285165188
VERSION     WP_285165188.1
KEYWORDS    RefSeq.
SOURCE      Shewanella goraebulensis
  ORGANISM  Shewanella goraebulensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 57)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 57)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 57)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10601889
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..57
                     /organism="Shewanella goraebulensis"
                     /db_xref="taxon:3050637"
     Protein         1..57
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=6419
     Region          1..57
                     /region_name="HTH_26"
                     /note="Cro/C1-type HTH DNA-binding domain; pfam13443"
                     /db_xref="CDD:433211"
ORIGIN      
        1 marlflnlag varetginkn tlhrlyneta trveldmiet lcrylnvdvg elleiqd
//
LOCUS       WP_285165265             402 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Rhizobium sp. CNPSo
            3968].
ACCESSION   WP_285165265
VERSION     WP_285165265.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3968
  ORGANISM  Rhizobium sp. CNPSo 3968
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Rhizobium sp. CNPSo 3968"
                     /db_xref="taxon:3021408"
     Protein         1..402
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45405
     Region          1..70
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          204..292
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mtvgvknfrg erlkearlar gyyknalgdk igvsavaigr yedgldspqe arleaiasel
       61 kfsvnffvtp gwpeeidlih wrsrssetka areathqrik wlcemyglle seldfptlkl
      121 peltlpadfr litdddiesa asavrrlwgl glapvpdvvl alenagipva alridsdkqd
      181 gfyfyspmld rafvginike ascararfda ahelghivlh grvakedaek penhavierq
      241 ahrfagaflf pqsafrsevg evslnylrsl kkrwgmsiaa mimragdlqm idgeqrqwlf
      301 rnmtyrrwkg hlaepfdaqn empleqprml rrgfevllet gdfarssila slpqpleele
      361 qlaalepnfl atatpvdfqv rrkpgfemtd lesgnviefk rr
//
LOCUS       WP_285165352             384 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Rhizobium sp. CNPSo 3968].
ACCESSION   WP_285165352
VERSION     WP_285165352.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3968
  ORGANISM  Rhizobium sp. CNPSo 3968
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Rhizobium sp. CNPSo 3968"
                     /db_xref="taxon:3021408"
     Protein         1..384
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42384
     Region          15..378
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mdeeeqklkv rpnkaalekl laekqldali cmspenftyv agvhvttven lrprqafvil
       61 kkdgaaelvv csiedslvrs eswvrdvtly tefvqepvda laatlrklkl dhglvgmdld
      121 ylpvssyvrl tealpdlkil nttedvasir svklpdeiav lervarqthq avlegigegk
      181 vgetdkalan riikkmfdag adgtlhlhla sgertphihn hpgdyptqpg qilrldvggl
      241 ygaymsdfar tfstgnpskl qqetyrklcd vqevtiaamk pgvtaeeiff lcksefekrg
      301 lpctlphvgh sfgievherp mirpgdktpl apgmviniep mttdeegscy htedlvlite
      361 rgnriltlgl apkeipilge ftar
//
LOCUS       WP_285165381             237 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Rhizobium sp. CNPSo
            3968].
ACCESSION   WP_285165381
VERSION     WP_285165381.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3968
  ORGANISM  Rhizobium sp. CNPSo 3968
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 237)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Rhizobium sp. CNPSo 3968"
                     /db_xref="taxon:3021408"
     Protein         1..237
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26931
     Region          1..>224
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrkaerlfqi iqilrrstgp vtssqlaiev evarrtiyrd iadligqrvp irgeagigyv
       61 ldqqydmppl mltseeieav vlgsqmvarl gdralttaar dvltkvalav psnlrsfiae
      121 ptvgirpdmv igdlrcdtrp lrsalretrk irleyqalng titsrvvwpv llgydggicl
      181 liawcelkee frhfrsdrmr aiqvledrid lpksklkqkw lqwrqeeqsr rgaiqip
//
LOCUS       WP_285165573             339 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Rhizobium sp. CNPSo
            3968].
ACCESSION   WP_285165573
VERSION     WP_285165573.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3968
  ORGANISM  Rhizobium sp. CNPSo 3968
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Rhizobium sp. CNPSo 3968"
                     /db_xref="taxon:3021408"
     Protein         1..339
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=36620
     Region          87..339
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mlfipfpfav aivllvlfam vagrdderpa nlpfltlilv safqsvlsgl rwgygiqavm
       61 yaaplvaatm pplvyagvfq lvkksvrpsf lrigihclpa vlvlismiiw rdaidivlvl
      121 tfvgyaiail rlmrpgmdal rlaaldevrp ayhailfaaa slllsaaldt vvaldfmwah
      181 gqytpalivg gnlvaliils aaaaaasrsg aakeapeiae apkadagdie tmaavqalms
      241 errlyedhdl tlnrlarkag lsarqiseai nratgknvsq yvnesrvaaa ckllteteks
      301 vieimyavgf qtksnfnref rrvtevtple wrkktlaaa
//
LOCUS       WP_285165599             301 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Rhizobium sp. CNPSo 3968].
ACCESSION   WP_285165599
VERSION     WP_285165599.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3968
  ORGANISM  Rhizobium sp. CNPSo 3968
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Rhizobium sp. CNPSo 3968"
                     /db_xref="taxon:3021408"
     Protein         1..301
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32766
     Region          71..296
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mriliwlcla amlaavliwf vtepampfap ddprlqgngd pargelifaa gdcaschatp
       61 gqkdrlrlgg glalaspfgi frapnissdp vdgigswstv dlanaliggv sprhqhyypv
      121 fpypsltgmr vedirdlray mrtlapvsgr ppahdlffvf rmrrllgfwk llffregqmq
      181 gpvstdpvla rgrylvetlg hcaechssrn rlgairpetr faggidpegt gfvpnitpsr
      241 ignwseadia emlksgntpn hgrvgssmae vvtnmamlpq snrdaiaryi kslpprptph
      301 p
//
LOCUS       WP_285165730             329 aa            linear   BCT 25-DEC-2024
DEFINITION  MDR/zinc-dependent alcohol dehydrogenase-like family protein
            [Rhizobium sp. CNPSo 3968].
ACCESSION   WP_285165730
VERSION     WP_285165730.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3968
  ORGANISM  Rhizobium sp. CNPSo 3968
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Gonzalez-Duarte,R. and Albalat,R.
  TITLE     Merging protein, gene and genomic data: the evolution of the
            MDR-ADH family
  JOURNAL   Heredity (Edinb) 95 (3), 184-197 (2005)
   PUBMED   16121213
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   6  (residues 1 to 329)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169633
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rhizobium sp. CNPSo 3968"
                     /db_xref="taxon:3021408"
     Protein         1..329
                     /product="MDR/zinc-dependent alcohol dehydrogenase-like
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=35796
     Region          17..327
                     /region_name="Zn_ADH9"
                     /note="Alcohol dehydrogenases of the MDR family; cd08269"
                     /db_xref="CDD:176230"
     Site            order(48..50,53,128,132,152..157,175..176,180,207,
                     220..221,223,243..244,268..270)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176230"
     Site            order(48,72..73,128)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176230"
ORIGIN      
        1 mnaitsvwtd amraavvtga gqlrvetmal pepaagqlrv klegcgvcas nlvpwsgpew
       61 mrfptepggl ghegwgtida igddvtgfav gdrvatlgqh ayathdladh ssvvrlpawl
      121 ddrpfpgepl gcalnifkrc dvqpgqsvai vgigflgall tqlcvaagah viaisrrafs
      181 leiakragas etiamkdhwq iieqvrqstr gqfcdrviea vgkqwpldla aeltrergrl
      241 viagyhqdgq rqvnmqlwnw rgldvvnahe rdpavylqgi rdaiaaieag qldpwpflth
      301 rfplerldda lnmtrdrpdg flkalvvys
//
LOCUS       WP_285165763             353 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Rhizobium sp. CNPSo
            3968].
ACCESSION   WP_285165763
VERSION     WP_285165763.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3968
  ORGANISM  Rhizobium sp. CNPSo 3968
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Rhizobium sp. CNPSo 3968"
                     /db_xref="taxon:3021408"
     Protein         1..353
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38690
     Region          3..348
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mgmtrnasds eilqsigfdp alhrkfaagi esgllrdlhv vlaarsqqvf meyygvgsde
       61 nwgtpldsva fdadtlhdlr svtksivsll ygialdkglv pppdaplyeq fpeygdlaed
      121 avraritigh altmtlgmew eedrpytdpl nseiamenap dryrfvlgrp viaepgtrwi
      181 ysggsvalvg tiiergtgkr lpdfaqtalf eplditkfhw ssgydgvasa asglrltapd
      241 llkigmlllq kglwngrriv seewiarslt paistgdgld ygmlwfcgea papafanprp
      301 wragfgnggq rlwlmpdagi aaviysgkyn awdawitptr vwreiilanf lka
//
LOCUS       WP_285165792             240 aa            linear   BCT 25-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Klebsiella oxytoca].
ACCESSION   WP_285165792
VERSION     WP_285165792.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella oxytoca
  ORGANISM  Klebsiella oxytoca
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Klebsiella oxytoca"
                     /db_xref="taxon:571"
     Protein         1..240
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26491
     Region          20..149
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mmnkfspanc pqtyvnqnmm gpnvlrlvee lsrslelwpg mrildlgcgt glssmylate
       61 fgvevvaadl wvraddnarr faaagmdnki tpinldistl pglgifarda fdavvsinaw
      121 hyfardalff eqriapyvkg ggtvaivipg lrssdaetrp eihaliasgi alfttdrwra
      181 iwsgsqhlav nqcrhmasgr qawlewqkcd ndfaatdaai rsdelgqqlr fmqiigrvnk
//
LOCUS       WP_285165875             311 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose 4-epimerase family protein [Rhizobium sp. CNPSo 3968].
ACCESSION   WP_285165875
VERSION     WP_285165875.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3968
  ORGANISM  Rhizobium sp. CNPSo 3968
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142572
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Rhizobium sp. CNPSo 3968"
                     /db_xref="taxon:3021408"
     Protein         1..311
                     /product="UDP-glucose 4-epimerase family protein"
                     /EC_number="5.1.-.-"
                     /GO_function="GO:0016854 - racemase and epimerase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32744
     Region          1..302
                     /region_name="UDP_G4E_4_SDR_e"
                     /note="UDP-glucose 4 epimerase, subgroup 4, extended (e)
                     SDRs; cd05232"
                     /db_xref="CDD:187543"
     Site            order(6,8..11,25..27,62..64,83,106..108,134,138,161..164)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187543"
     Site            order(84,108,134,138)
                     /site_type="active"
                     /db_xref="CDD:187543"
     Site            order(108,134,163,176,186,195)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187543"
ORIGIN      
        1 milvtgatgf vgqalcaels rrrmdyrpvs rnsgpgfaai gaidgqtdws ealagidtvm
       61 hlaarvhvmn esasdplaaf ravnvdatvn larqaagagv krfiflssik vngegtsvgk
      121 pfrasdvplp edaygrskle aeaallaisa etgmevviir pplvygpgvk anfaslmkwa
      181 arpfpwpfga vrnrrslvyv gnlvdfmllc athlsvgnrv flisdgddls igqlisklsl
      241 aagrkawmlp vppsllegfa allgrraaaq rllgslqvdi getrsvtgws ppysveegla
      301 atvadagtka r
//
LOCUS       WP_285166081             394 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Rhizobium sp. CNPSo 3968].
ACCESSION   WP_285166081
VERSION     WP_285166081.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3968
  ORGANISM  Rhizobium sp. CNPSo 3968
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Rhizobium sp. CNPSo 3968"
                     /db_xref="taxon:3021408"
     Protein         1..394
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42173
     Region          15..371
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 meradnptrp vgqssvdlli vgggimglwa avhaerlgir allveaghfg qgasggllga
       61 lmphmpnkws dkklfqfdal vsleeeiavl eaetglsagy rragrliplp kphlrqialg
      121 hsrdaethwr qdehefhwhv ldaapvsgwi dpaagesgfv fdtlaarvap rallnvlrry
      181 lagathvqla egvtvesidp arglatlseg dirfdrcila aghwsfpild rltegrkssl
      241 gqpvkgqaam lkadvdgslp vifrdglyiv phedglvavg stsenhfddp lstdgqlddl
      301 laaarimapv lagaevverw aglrpkavdr dpmvgahpdh rslialtggf kvsfglahrl
      361 aeaavrqaad macsfklpqs ftlashisvi shkt
//
LOCUS       WP_285166084             312 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Rhizobium sp. CNPSo 3968].
ACCESSION   WP_285166084
VERSION     WP_285166084.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3968
  ORGANISM  Rhizobium sp. CNPSo 3968
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Rhizobium sp. CNPSo 3968"
                     /db_xref="taxon:3021408"
     Protein         1..312
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34039
     Region          12..281
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mtiewamshp mfklahisdv hlgplprlsi relaskritg fvnwhrnrrk hlfggtldll
       61 lddirakqad hlavtgdlvn lasgmeiqta aawlktvgdp lrtsvvpgnh dayvpgayek
      121 amrawypyvs gdhapaewqe dqrifpylri rdqvaligcs tavatppfaa sgfysarqar
      181 etvnilraag daglfrvvmi hhppirgats fykrmigirr faavlstgga elvlhghthl
      241 ntlhwlrghm gpvpivgias asqgvgglkp raaynlftia grpgawelka eryslndngn
      301 gvdpegidil at
//
LOCUS       WP_285166096             211 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Rhizobium sp. CNPSo 3968].
ACCESSION   WP_285166096
VERSION     WP_285166096.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3968
  ORGANISM  Rhizobium sp. CNPSo 3968
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Rhizobium sp. CNPSo 3968"
                     /db_xref="taxon:3021408"
     Protein         1..211
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23363
     Region          50..205
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 msefplysad efrrralnqs ggpidlawrd hgdhllnpet iaqvadlklk daavlvpvvd
       61 sgddakvift lrtstlrkhs gqiafpggai dpedaspema avreageeig ladifiepva
      121 rlphylaatg fritpilavv kpgfhlalnp tevedafevp lsflmdpdhh vtdtmlwqgt
      181 erhfyrmpyg qrmiwgitag ivrtlyerly t
//
LOCUS       WP_285166120             383 aa            linear   BCT 25-DEC-2024
DEFINITION  M24 family metallopeptidase [Rhizobium sp. CNPSo 3968].
ACCESSION   WP_285166120
VERSION     WP_285166120.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3968
  ORGANISM  Rhizobium sp. CNPSo 3968
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Rhizobium sp. CNPSo 3968"
                     /db_xref="taxon:3021408"
     Protein         1..383
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42468
     Region          15..381
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 malhfersey darlarllar mqeekldaml lfaqesmywl tgydtfgycf fqalvvkadg
       61 sltlltrsad lrqaqltsvm tdiriwvdrv nadptldlke llsdldllgt rigveydthg
      121 mtgrvarlld qqlasfgqia dasylisglr ltkspaeivh veraaaladn aldaalslik
      181 pgsdeadila amqgaifsgg gdypanefii gsgaeallcr yksgrrklda ddqltlewag
      241 vdahyhaamm rtivignpsh rhrelysacl etlqaietil mpghtfgdvf dmhakimder
      301 glarhrlnac gyslgarfsp swmehemfhm gnpqeiqenm slfvhmiimd sdsgtamtlg
      361 qtylttsqap kalsrhplef lnr
//
LOCUS       WP_285166279             277 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Rhizobium sp.
            CNPSo 3968].
ACCESSION   WP_285166279
VERSION     WP_285166279.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3968
  ORGANISM  Rhizobium sp. CNPSo 3968
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Rhizobium sp. CNPSo 3968"
                     /db_xref="taxon:3021408"
     Protein         1..277
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30114
     Region          2..>230
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkllvtgssg rigraaierl leeghevigi devpssdmrc pfarvdmrdy gqvldavadi
       61 esgidgivhl aaivgakvaa sthifhtnta isynvfqsar iagiknivsa ssetllgvpf
      121 ddppayfpvd dkltskpess yalsklvdes vaaefcrwdp alkmigprfs wvkephqyda
      181 rkacednpgv qkwnlwsyvd rrdcaqaisl alnaslngfh hfviaaddtv larptralra
      241 ayypnvplqg qraehgslvs slvaprrsmi spevqla
//
LOCUS       WP_285166291             240 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Klebsiella oxytoca].
ACCESSION   WP_285166291
VERSION     WP_285166291.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella oxytoca
  ORGANISM  Klebsiella oxytoca
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 240)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Klebsiella oxytoca"
                     /db_xref="taxon:571"
     Protein         1..240
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25633
     Region          <30..98
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlkpveried deslalamaa vasamadasr lkilcalmdg rawtatelst vadispstas
       61 ahlsrlvssg lliclaqgrh ryyrlagsdv agllenmmtm agkravalst atpvnlrvar
      121 tcydhlagev avslydfllr eawiapdgta ltpvgeaqfa rlgimtksgs rrkaccgcld
      181 wserrfhlgg aagaallqhg lqkgwftttp gfrevtitsa gwralhqhfq lakntrsasd
//
LOCUS       WP_285166315             341 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase family protein [Rhizobium sp.
            CNPSo 3968].
ACCESSION   WP_285166315
VERSION     WP_285166315.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3968
  ORGANISM  Rhizobium sp. CNPSo 3968
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Rhizobium sp. CNPSo 3968"
                     /db_xref="taxon:3021408"
     Protein         1..341
                     /product="zinc-dependent alcohol dehydrogenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36177
     Region          5..341
                     /region_name="MDR7"
                     /note="Medium chain dehydrogenases/reductase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cd08276"
                     /db_xref="CDD:176237"
     Site            order(44..46,49,150,154,175..180,198..199,203,242..243,
                     245,264..265,289..291)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176237"
ORIGIN      
        1 mtktmkrwtl dtvavgapln ltetavptpa rgevlvrvka vslnyrdklv reigmglplq
       61 fpfvpasdma gvveavgdgv trfavgdrvi stfhpgwidg kplgdartpp yktlggfypg
      121 vlseyvamse dwlvsspqsl dyaeastlpc agltawfalv ergkikpgdt vlvqgtggva
      181 lfglqiataq gaevfvtssg qeklgrakal gahygidrnk sdwveevyrl tndrgidhii
      241 eiaggpnlgq slkavapqgr isvigvlegf disgpvapll lksptvqgis vghrrsledf
      301 vravdsiglk pvidhryglg eapaafdhld rgpfgkivie l
//
LOCUS       WP_285166364             460 aa            linear   BCT 25-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Rhizobium sp. CNPSo
            3968].
ACCESSION   WP_285166364
VERSION     WP_285166364.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3968
  ORGANISM  Rhizobium sp. CNPSo 3968
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Rhizobium sp. CNPSo 3968"
                     /db_xref="taxon:3021408"
     Protein         1..460
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=49246
     Region          40..451
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mtapfpllsa avaqeadsta pqapddratt tasvppaqea pdpaadlark rdetraqlde
       61 lsktinlssg ktkeledsia sldkstdslr qalidsaarr keldrkiqqt ektltglavk
      121 egkiraslhd rrallaevlg alermgrnpp pallvtpdda lasvrsaill gavvpgmrke
      181 tdkliadltd lsklhadtaa ekasftatmt nsleeerrmd lliaendkhs kenaaqlgae
      241 rkraeelasq atsleglvas lesqigsvrd aaaaaraeea rraqmteqqr eqakalaeng
      301 vpdknritpa ypfsdlkqkl elpvagdtlr qfgdddgtgh tamgltiatg pealvtapad
      361 gtvvyagafr sygqmiildt gdgyhmvlsg mdaiktrpgr fvfageplat mgqkrvasat
      421 alaletdrpt lyiefrkdgk pvdsrpwwts kdtgkarndt
//
LOCUS       WP_285166535             915 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Klebsiella
            oxytoca].
ACCESSION   WP_285166535
VERSION     WP_285166535.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella oxytoca
  ORGANISM  Klebsiella oxytoca
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..915
                     /organism="Klebsiella oxytoca"
                     /db_xref="taxon:571"
     Protein         <1..>915
                     /product="beta strand repeat-containing protein"
     Region          <10..911
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 lyatnqnvat nttnitnlan tpltfvgntg tvtkklgetl tvkggkttag tysdanlntv
       61 vdangnlvvq maenpvftsa iiggtttins sgltitggps vtttgvnags kkvtnvaagt
      121 lsststdgvn gsqlyatnqn vatnttnitn lantpltfag ntgtvtkklg etltvkggkt
      181 tagtysdanl ntvvdangnl vvqmaenpvf tsaiiggttt inssgltitg gpsvtttgvn
      241 agskkvtnva agtlsststd gvngsqlyat nsninniynt gikyfhanst gedsqatgld
      301 svaigmgava gfdndialga gsvtaetvat egvaldgtdy afagvapast vsigsegaer
      361 tltnvaagrl setstdaing sqlhatntal ntlgdravqy dlhedgsvny gditlggdty
      421 nqytneggtt itnvadgsap sdavnfsqlt etnnsiqnly tsgtkyfhan stgadsaavg
      481 vdavaigmga vaahdnsval gagsvtsspv gssgvtlsgt dyvfaganpt stvsvgdtga
      541 ertithvaag rlsesstdav ngsqlyatns avnnifneid glqddallwn gtlnaysash
      601 gdtaenkitr vaagdlnevs tdavngsqly atnqqvegnt tsinnlgdsv eniyntgtky
      661 fhanstgtds salgldsvai gmgaiaantn dvalgagsvs gvtvgtagvt lggtdfafag
      721 atptstvsvg dvgsertitn vaagrlsats tdavngsqly atnttvnnis nemnglkdda
      781 lqwdpsqnaf sashgdttvn ritnvaagel stdstdavng sqlyatnqqv eanttsitnl
      841 gdsveniytt gtkyfhanst gtdssalgld svaigmgaia gnqndvalga nsktaatvgt
      901 agvtlrgtdy afaga
//
LOCUS       WP_285166934             478 aa            linear   BCT 25-DEC-2024
DEFINITION  WS/DGAT/MGAT family O-acyltransferase [Mycobacterium tuberculosis].
ACCESSION   WP_285166934
VERSION     WP_285166934.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Stoveken,T., Kalscheuer,R., Malkus,U., Reichelt,R. and
            Steinbuchel,A.
  TITLE     The wax ester synthase/acyl coenzyme A:diacylglycerol
            acyltransferase from Acinetobacter sp. strain ADP1:
            characterization of a novel type of acyltransferase
  JOURNAL   J Bacteriol 187 (4), 1369-1376 (2005)
   PUBMED   15687201
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Kalscheuer,R. and Steinbuchel,A.
  TITLE     A novel bifunctional wax ester synthase/acyl-CoA:diacylglycerol
            acyltransferase mediates wax ester and triacylglycerol biosynthesis
            in Acinetobacter calcoaceticus ADP1
  JOURNAL   J Biol Chem 278 (10), 8075-8082 (2003)
   PUBMED   12502715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496208
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..478
                     /product="WS/DGAT/MGAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0045017 - glycerolipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=50717
     Region          5..463
                     /region_name="acyl_WS_DGAT"
                     /note="acyltransferase, WS/DGAT/MGAT; TIGR02946"
                     /db_xref="CDD:274360"
ORIGIN      
        1 mdlpmaaada lflwaetptr plhvgalavl sqpdngtgry lrkvfsaava rqqvapwwrr
       61 rphrsltslg qwswrtetev dldyhvrlia lppragtael walvselhag mldrsrplwq
      121 vdlieglpgg rcavyvkvhh aladgvsvmr llqrivtadp hqrqmptlwe vpaqasvakh
      181 taprgssrpl tlakgvlgqa rgvpgmvrvv adttwraaqc rsgpltlaap htplnepiag
      241 arsvagcsfp ierlrqvaeh adatindvvl amcggalray lisrgalpga pliamvpvsl
      301 rdtavidvfg qgpgnkigtl mcslathlas pverlsaira smrdgkaaia grsrnqalam
      361 salgaaplal amalgrvpap lrppnvtisn vpgpqgalyw ngarldalyl lsapvdgaal
      421 nitcsgtneq itfgltgcrr avpalsiltd qlahelellv gvseagpgtr lrriagrr
//
LOCUS       WP_285167405             716 aa            linear   BCT 25-DEC-2024
DEFINITION  RelA/SpoT family protein [Kingella negevensis].
ACCESSION   WP_285167405
VERSION     WP_285167405.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 716)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 716)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
REFERENCE   5  (residues 1 to 716)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..716
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=80348
     Region          19..716
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mpipqpqapy dsltadyreq llrearylsa deqqqlekac afafhahdgq irksgepyit
       61 hpiavatela rwrmdiqals aglmhdvled tsvtkeqmta efgdtiaemv dglsklenlk
      121 ydskeehqae sfrklilamt kdvrviivkl sdrlhnmrtl gakkpasrrr iatetlevya
      181 pianrlglnh vyrelqdlaf famhparygv lqramttfkk nrhdviervl remslrlvgq
      241 nieaqirgre rnlysiyqkm ltkkvkfeel qdiygfrviv nsvsqcytal galhglyqpk
      301 pgkfkdfiai pksngykslh ttlsgpyglp ievqirtrem nmiaevglas hwrdsgsqed
      361 ettrrtnqwl knildlqars enaieflehv kidlfpnesy mltpkgkiit lprgatpidf
      421 ayavhtdvgn hcvgarvnki pvplrtrlkt gdtveiitse yakpnpawln faassrarsa
      481 irsyiknadr sdaialgerl latalgsllp kkvaesdelk ekyfqqladk qlsfedvlyn
      541 vgigrtmpva vameiatmag ehfgdevkls piqvnsheta rvhlgkcclp vagdsiravv
      601 vpeqglmihr dicpvllktd vehqldadwa alpegmekiy qtalvvssed shgllanmas
      661 aisetgcdiv svdtlskaqe gfiefkftlt vrdllhvqav marlhkivqv rkvarv
//
LOCUS       WP_285167431             382 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285167431
VERSION     WP_285167431.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..382
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=40994
     Region          10..364
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 madgaggdrk srsvliagag pvgltvalel arrgfvprii ddgqgpaple esralginar
       61 tltllspsgl terivataqp iahfrirsga kiladvdtrr lpgrfgavha laqgvterll
      121 iealaahgia pewqtavvag kiadlqkpev tlrhadgate tvrpdiliga dgahsavrka
      181 lgagfpgeal eayfyladfr yvrpvdahfa eitlcdpgmv grlpvsadvl ryistledfe
      241 srivhpeava ektwvsqfri nfrhvepmak gnvflagdaa hihspagarg mnlgiedacw
      301 lawliaegre eeysalripa vkqvlkqtyg ltrlitmksp laiaarnlla plllrfgpar
      361 rgllhsvagy dtpkppwidw ae
//
LOCUS       WP_285167527             359 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285167527
VERSION     WP_285167527.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..359
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37713
     Region          17..353
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mpsqeiivig agiigasiaw hlarkgasvt viaakpggea tpssfawina swgnpefyfh
       61 frrrsmaews rlaadlpglp lswcgglcwd lpeaeleaya arqggwgysl rqvdretsaa
      121 lephladppt falhvgeega vepvaaanll ledatrhgat lsygtearrl lrendrivgv
      181 etadgvllad hvvlaagagt aalaasvgid vpietppgli vhsrpaprll nglvmapelh
      241 mrqtmegrii agtdfggtdp gekpqqaade lfakvktmlr ggdeleldfy tvgyrptpkd
      301 gfpiiggvda apglylavlh sgvtlaplvg svaaaeilsg dpdpqlapfr lsrfaptsd
//
LOCUS       WP_285167535             509 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Kingella negevensis].
ACCESSION   WP_285167535
VERSION     WP_285167535.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 509)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 509)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 509)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..509
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56200
     Region          8..501
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mhrhfttlli atipiaflit lvaaplwaml nyqaaaplwa emlhdsyytq kilwttqqaa
       61 ytvlltltlg iptayalarl kffgrklilr llmlpfimpt lvagmgvlal fgehgflwrg
      121 wtdtaallly gnvffnlpvm irtayqgfla vpanrlaaaq tlganawqrf wrvempvlrn
      181 wlaggaclvf lycfsgfgla lllggqqyst ieveiyqlia yelnmesaav lvwlvlgita
      241 iagtlyawis rqtdaaeirf rlpekpktlp ekllllfala vlllccalpl favvfqaaka
      301 gdawrvlwde etlaalwntl rfsgcavala avlgllhaal arrlsvmrsl tflsfmvspv
      361 clsfgvllly pewaatlpml ialyallayp fvtkdilaaw dalpenytka arvfgatpfq
      421 aacsvtlpll lpalrrgltl aaatcigefa aslflsrpew ttlttliyry lgkvgtenhd
      481 ramvltlvlm vlscaaflal dtkekqper
//
LOCUS       WP_285167570             179 aa            linear   BCT 25-DEC-2024
DEFINITION  KdsC family phosphatase [Kingella negevensis].
ACCESSION   WP_285167570
VERSION     WP_285167570.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..179
                     /product="KdsC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=19294
     Region          9..178
                     /region_name="KdsC"
                     /note="3-deoxy-D-manno-octulosonate 8-phosphate
                     phosphatase KdsC and related HAD superfamily phosphatases
                     [Cell wall/membrane/envelope biogenesis, General function
                     prediction only]; COG1778"
                     /db_xref="CDD:441384"
ORIGIN      
        1 mfshyspdil arakrikllv ldvdgvltsa qlfmssngei ikafntldgh gikmlqnsgv
       61 qtaiitarnd eavgarakql githyffgvh dkkvafeqlc eqagvsaeqc amvgddvidl
      121 pvlvrcglpi svanahtfvk khtvlttekn ggfgavrevt dlimqaqntl lpalneylk
//
LOCUS       WP_285167638             251 aa            linear   BCT 25-DEC-2024
DEFINITION  AAA family ATPase [Kingella negevensis].
ACCESSION   WP_285167638
VERSION     WP_285167638.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..251
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27853
     Region          4..243
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mnktfepvfk qlneiilgke pvlkqliaci ladghvlled vpgvgkttla tslaavlglk
       61 yqrvqftndm lpadllgvnv fspnngtfkf hegpvfnqfm ladeinrasp kvqsalleai
      121 eegqvsvdgk tyvlptpflv vatqnpseql gtfplpesql drfmmrlsmg ypveeaekml
      181 yhmgdrrqlv hkvqaiaspe tlhewqtkvk qvtvseavaa yiyrlvaatr rpglfalglr
      241 acihkqlfdk f
//
LOCUS       WP_285167738             529 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285167738
VERSION     WP_285167738.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..529
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56649
     Region          1..511
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 msdhdyiivg sginalvaaa ilgkkgrkvl vferndrigg clrseeitep gfihdvmatt
       61 mvlfltspay gaigkdlear glefahadlp tgvlrpdgsh vifskdrrrn iatfdelslg
      121 dgqtflremd alaadapflf allggalwsg stlrtvvkqg wgrglrklaa wfgnalmpar
      181 sylettyrse dihalwapwv lhcglgpesa ysaemlkvig faielagapv vkggagallt
      241 aferlikdng geirtgadve svtpgpggra ggvklagget lnanagvics vtpnqlyerl
      301 ikdwpsplpp dvktsvaryr ygkgnmqihy alsepprwka daelgkvall hltpgldgvs
      361 raanecergl lpaeptvcig qptsfdpsra pegksilwlq lpeaprhikg daageieipa
      421 gghwtekvre ryadriesll eshienfsgi klarrsyspa dleamnmnlv ggdpyggycg
      481 idqfflwrpf kssvnhrthv aglyhigast hpgpglgggs gfllasslk
//
LOCUS       WP_285167752             612 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285167752
VERSION     WP_285167752.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 612)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 612)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..612
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=67814
     Region          <94..582
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 meetvsgrse qefqdllrrl elaletsqig vwehslnqee ilwdlqmhkl yqtgatdrkv
       61 ssavwlnalh pddveraiae feaataekgf ynsqfriilp egeirylrsr ahfyegpdge
      121 psfigaewdv tadvllnrel tnqkavaear aialeqsrar iehaadhdyl tglpnrryfd
      181 rrlaelradp avktlavlhi dldsfkqind kwghaagdvt lqnaavrisg sitakdmvar
      241 iggdefvvvl vdidgaddlk tiaedilwrl rrdirfhhem lpvgasigaa wsvvgeagnl
      301 laesdialyq akksgrnrve fftpklqsdl qaerqlaeel rlalirheiv pyyqiqvdar
      361 srrivgleal arwwhpekgl lapaaflkva eeygltaeid aailnrvlfd ranwamqglt
      421 ppriavnisg srladpnlie rlqalnipph titfelieti flddpddktl anidaikqmg
      481 ieieiddfgs ghasliglvk lkpkrlkidr qlvtaitvsd eqrrlvgsiv eiaralsvev
      541 iaegvetedh arllaragcd glqgyaigyp spgneiavll tsvlrpdqhp asgnsqgnag
      601 ptgfagrqsa hs
//
LOCUS       WP_285167819             394 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285167819
VERSION     WP_285167819.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..394
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41936
     Region          15..372
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mgradnppgl agqssaelli vgggimglwa avhaerqgve tllvdagrlg qgasggllga
       61 lmphmpdkws ekkqfqfdal vsledeiaal eaatglsagy crsgrliplp kphlrkialg
      121 hsqdaethwh hgerrfhwhv lhaapvegwi dpaagesgfv fdtlaarvap raflkvlasf
      181 ldkakhvrlt egleiqsidp drgtaatqeg tirfrrcils aghrsfpmld gltpgrhspl
      241 gqpvkgqaal lkadveaglp vifrdglyiv phegglvavg stsenrfdnp mstdgqlddl
      301 ltaartmapa vagaevierw aglrpkaidr dpmvgahpdh prlvaltggf kvsfglahrl
      361 aeaavreale iscsfklpeg ftlsnhitva shkt
//
LOCUS       WP_285168164             420 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285168164
VERSION     WP_285168164.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..420
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=47289
     Region          167..377
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mtaidlpyrr vdrpqlaalr lvgtacvafg vflsgfviae papyelwvaf ligtwfilgl
       61 kisrnvapll alfltfnvgg mlsltqmrdl ganshldgpi yvavstflal ssvfyaaiie
      121 dsekrlklif ntwvvaalit aslgilgyfh afpgaeiftr ydramgvfqd pnvfgpylvt
      181 psiylmhgil igdlkkapik alclfvlafg iflsfsraaw glfsfasaml ifcmllqhrs
      241 nafrlrilvm slaaiifmvl llvvalqfhq vsdlfstrtq lvqdydgghl grferhrigf
      301 mlsmerplgi gplvfstlfr edehniwlkt lttygwlgff cwvsmicwti yigfrnflkd
      361 rpwqpyltia wivilghvgi gnvidtdhwr hlymligivw gcgaleqqyq rslarreaas
//
LOCUS       WP_285168177             286 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285168177
VERSION     WP_285168177.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..286
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32214
     Region          68..175
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 memkvqsmlg fakrsrkkva gnsleaifdq yeqgkpdhqn aidalpgwns afpvalnlka
       61 gihhlyadgr idwalrsfgs iegktilevg plegmhtyml hrerparida ieanrlcflr
      121 clvtrqildi ntasfllgdi qawltdhdev ydfavasgvl yhmadpgefl rllarrasav
      181 fiwthfflee ampagdvrrn pfsgkvetrm iegvpvryye rsyqhansna sfcggmkdrh
      241 fwmhrddilt lleklgfsdi likdqdfghs ggpcfsllar kaqaap
//
LOCUS       WP_285168224             311 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Rhizobium sp.
            CNPSo 3464].
ACCESSION   WP_285168224
VERSION     WP_285168224.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..311
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33464
     Region          8..304
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 msrpapprsv rlrrsvlsvp ainrraleki adldcdavif dledsvapek kaearenlra
       61 ffagsppdse ekagkeriir intlssgfga ddlelvlale pdavllpkid epqdvtvvsd
      121 rfaeadapes lriwamietp rgvlnaaaia eagrtagsrl dclvvglndl rketdvlpqp
      181 graylvpwlm qvilavsayg ldaidsvfnd fkdmqavdae caegramgfa gkmlihpnqi
      241 eaanrhfgpd eaaiaeaeai iaafadpaaa glnvvnlggr mverlhlvqa erlvhkarli
      301 aerhrpstss g
//
LOCUS       WP_285168367             308 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Mycobacterium
            tuberculosis].
ACCESSION   WP_285168367
VERSION     WP_285168367.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..308
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=32938
     Region          40..288
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mrsidvvvea vvtfagaagf ahtlaplrrg qqdpcfrvpg dgtiwrtsll ptgpvtaris
       61 ragrdaarcv awgsgaeefv dmapamlgaa ddasdfvplh pavaaahrrl pnlrlgrtgq
      121 vlealipavi eqrvpgaeaf rswrllvsky gtqapgpapp gmrvppsaev wrhipswefh
      181 ranvdpgrar avvgcaqraa slerlvslpa araaealtsl pgvgvwtaae ttqrvfgdad
      241 avsvgdyhip kmigwtlvgr pvddagmlel lepmrphrhr vvrlleasgl areprrgprl
      301 pvqniral
//
LOCUS       WP_285168388             641 aa            linear   BCT 25-DEC-2024
DEFINITION  autotransporter assembly complex protein TamA [Rhizobium sp. CNPSo
            3464].
ACCESSION   WP_285168388
VERSION     WP_285168388.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..641
                     /product="autotransporter assembly complex protein TamA"
                     /GO_component="GO:0097347 - TAM protein secretion complex
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=68037
     Region          59..641
                     /region_name="TamA"
                     /note="Outer membrane translocation and assembly module
                     TamA [Cell wall/membrane/envelope biogenesis]; COG0729"
                     /db_xref="CDD:440493"
ORIGIN      
        1 mhkrtgprks iayrragtvm avaatialgp lhagnafafk lfgmtlwged dttdqvsdpv
       61 hytvdfktdn ldkdlkealt dssmlvsdkk kpvsgdlgvv ikarddrdrl iatlyekary
      121 ggvvtitvng tdidalspnp tfgrskpvav tisvdpgpvf tlgkikllgd argldpagyg
      181 lvpggdagsl tilkagdkiv vdfknqghpl aklikrdvva dhetnrvdva lsvesgpmap
      241 ignvgvsgqk svdpdfikry arinegkpys pdelkkasdr lrklgvfssv tireadklap
      301 dgsipmtiev aegkqryfgv gaqystidgf gvqgywghrn ltgradslri egsvsriget
      361 tdvgqldysa gityvrpatw ypsatftagl kmqslhpday dadtitasgs layelsdqdt
      421 vsgggeisye qdstdaygdq nyltlaiple yvrdtrdnkl dptagyrasi sakpsyeaig
      481 ggvfssfegs isgyqgvgan dnvvfagkls lgsligsnsi edipatrrfy aggggsvrgy
      541 ayqeitpyns ngdalggrsy ataslearik itdtigivpf vdmgsvtdst fpdfsdlrig
      601 agvgvryatp fgpirldvav plkkyengta ygiyagigqa f
//
LOCUS       WP_285168492             561 aa            linear   BCT 25-DEC-2024
DEFINITION  purine-cytosine permease family protein [Mycobacterium
            tuberculosis].
ACCESSION   WP_285168492
VERSION     WP_285168492.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..561
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=60541
     Region          14..490
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mpgvitnses ptaadhdrit atretledyt lrlaprsyrr wppavvgisa lggiayladf
       61 aiganvgitw gtanalcgia ifalvvfvtg lplayyaary nidldlitrg sgfgyygsvv
      121 tnvifatftf iffalegsim aqglklglhi plwagyacst liifplvvyg mkvlsqlqlw
      181 ttplwlilma apfgylvvsh pdsigqffsy agkdghggls fgsvllaagv clsliaqiae
      241 qidylrfmpp rtpenanrww twtllagpgw vafgatkqii glflavylma nipgsstian
      301 qpvhqfmqiy rtfvlgwlal tlavilvvls qikinvtnay sgslawtnsf trltkhypgr
      361 vvflgvnlai alilmeanmf dflntilgcy ancgmawvva vasdigfnky llglspktpe
      421 frrgmlyain pvgfgsllla aglsivtffg glgaalqpys plvaivtalv mppilaaatk
      481 gkyylrrthd gidlpmydeh gnpsaavltc hvchqdferp dmlacqthga hvcslclstd
      541 kqaehvlpgl arahipgdqv p
//
LOCUS       WP_285168547             300 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285168547
VERSION     WP_285168547.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 300)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..300
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=34050
     Region          32..283
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mtiglahael iavltavtgn dprvmtvrsg dalpsgpfel ghrtlqsglr ewvreqtahp
       61 vgyleqlytf adrdrnneil ggrtisisyl glvreqaapg ggrpgwhgwy eyfpwedhrn
      121 grpavmddvv erlnswisdd pakrdqrrrr adftfglnda pwnedlvlqr yellyearlv
      181 leagcaqqsn sgrpmfadhr rilatgmarl rakikyrpvv felmaesftl lqlqrtveal
      241 agltlhkqnf rrlieqqelv eetgateset ggrpaklfrf rraileerel agtklplsrn
//
LOCUS       WP_285168559             420 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285168559
VERSION     WP_285168559.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..420
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44580
     Region          36..405
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 msnpwsggqt idvaiiggga agvaaarrlq slrpdvsvli leakdrvggr awtfrlsslg
       61 depvdlgcgw lhgartngwt eiarqlgltv ettpapwseg grtiggaear saigaffara
      121 eqrgdsgedg sldellepgn rwngcveaig tflngvelaa asihdyvhyd pgpspdwrvr
      181 egygtlisay aqpiptmlst vvqtidhrga eyillqtdrg tlrarmvlvt vatnmiakdq
      241 ikfdpplprk reaasrlplg lanklflsvl spddlpidtr ltgsldqvrt gsyqirpfgt
      301 alieayyggs lardleasge qaalafaree ltkhfgsafg rridavamsa wrgephiggs
      361 ysyaepgasg erivlgetvd drlffageac sptrfstahg aletgfgaae aiaaalkraa
//
LOCUS       WP_285168576             339 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Rhizobium sp. CNPSo
            3464].
ACCESSION   WP_285168576
VERSION     WP_285168576.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..339
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36708
     Region          1..325
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtatgntefa qrfdrafqpv eaavatgrip ggvlgiidrd gnrmvravgs aqkvpitrpm
       61 ladtwfdlas ltkvifttpr ilalaeagti dldaplisll pdlrqydaaa werkvtfrqc
      121 lghqtpfpav eplytygrdp ellrtfilqr ewragppvys dinfillgfa lerltgqtir
      181 dmdagpgfaf satpdqaaat edctwrhrvl sgevhddncs alqgaghagl fgtvdsilnf
      241 avglltgsga sersialmrs plsatrthgw erpydgwsgg slcspgtigh tgftgtglwi
      301 dfdkgrawtl ltnrihptrh fdsgivalrq tvgdlvnka
//
LOCUS       WP_285168700             159 aa            linear   BCT 25-DEC-2024
DEFINITION  SRPBCC family protein [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285168700
VERSION     WP_285168700.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..159
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=17346
     Region          12..151
                     /region_name="SRPBCC_CalC_Aha1-like"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of Micromonospora echinospora CalC, human Aha1, and
                     related proteins; cd07814"
                     /db_xref="CDD:176856"
     Site            order(12,14,16,25..27,29..30,35,45,51,53,55,57,66,68..69,
                     71,74,80,82..83,101..102,104,106,116,118,120,122,131..132,
                     133..138,140..142,145)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mnqavskdtq aivaeevfph apaiiwkalt sgelisrwlm apkgfesvag chftfqttpa
       61 gewdgtihce vlevvpnerl syawrgghaa ndgygskldt vvtftlskae agtrlrlvhs
      121 gfvlpkndta yrnmsegwkk vvkrldmvva eeassqtsh
//
LOCUS       WP_285168704             394 aa            linear   BCT 25-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Rhizobium sp. CNPSo
            3464].
ACCESSION   WP_285168704
VERSION     WP_285168704.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..394
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43261
     Region          11..332
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 makvglrewm alapvfasgk larygddtgg pllrfeadfc akfgvqhalt mssgtgalis
       61 alvaagigpg devlvpaytw iataaaplaa gavpvlvdid qtltmdpadi vrkitpqtka
      121 iipvhmsnmv cdmdsimhia rehnllvied acqavgltyk nkrtgtigdl gaysfnqfkn
      181 mnigeggavv tsdpqlfara rmyhdigslf rghldnanep pmlgvnfkas qiqgamlrvq
      241 lkrldpmigr mrkrydlmte ilsksdrmri gphndvanaa glhvifetpd darqfaeenr
      301 rgvyrlydss rhvytnwqpv lqqrsghpam npynwtdrki eytpdmcaqt ldilkrtcri
      361 slgenypaal maylarrmvr qgptasgkls yatt
//
LOCUS       WP_285168740             326 aa            linear   BCT 25-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285168740
VERSION     WP_285168740.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Pey,A.L., Megarity,C.F. and Timson,D.J.
  TITLE     NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just
            enough mobility, in just the right places
  JOURNAL   Biosci Rep 39 (1) (2019)
   PUBMED   30518535
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..326
                     /product="quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34147
     Region          4..326
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(40..41,45,124,128,131,149,152..154,173..174,178,193,
                     218..219,240..244,264..267,314,316)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(136,233..234,247..252,259..266,269..270)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mrhiaitefg gpeqlvaett edlhpgsgqv lveveaagin yldltqrsga srvhlielpf
       61 vpglegvgrv lelgegiats sglsvgarva wmdargsyas qavvsaerai pipntftvse
      121 gllfqaltah ylvheyrnir agdrvlvhaa agglgqllvq wlkhlgawvv gttssdskae
      181 siralgadav ivygdnydfa devtrltggn gvdlafdglg ektllktiat lgrggtvvai
      241 gaasgpipai nptlltqrgl rlaggsvfay vadpaelqkr asdviaavqa gwlrldeatg
      301 ypldraadah qdienrrakg klylip
//
LOCUS       WP_285168741             164 aa            linear   BCT 25-DEC-2024
DEFINITION  YybH family protein [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285168741
VERSION     WP_285168741.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..164
                     /product="YybH family protein"
                     /calculated_mol_wt=17233
     Region          33..159
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mrnalilaaa illspalptm ssaqtaiate agtsadkqai naiherwagl lqakdaaaie
       61 qlyadnavll apgeaavign aaigarwtrq lqlkdlafsl hpeqvvvsas gdlahdrgty
      121 dfaatlpqgp itdkgkyvlv wqkirgqwkv iadifnsnpt ppan
//
LOCUS       WP_285168745             139 aa            linear   BCT 25-DEC-2024
DEFINITION  type II toxin-antitoxin system tRNA(fMet)-specific endonuclease
            VapC [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285168745
VERSION     WP_285168745.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Lopes,A.P., Lopes,L.M., Fraga,T.R., Chura-Chambi,R.M., Sanson,A.L.,
            Cheng,E., Nakajima,E., Morganti,L. and Martins,E.A.
  TITLE     VapC from the leptospiral VapBC toxin-antitoxin module displays
            ribonuclease activity on the initiator tRNA
  JOURNAL   PLoS One 9 (7), e101678 (2014)
   PUBMED   25047537
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF047863.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     gene            1..139
                     /gene="vapC"
     Protein         1..139
                     /product="type II toxin-antitoxin system
                     tRNA(fMet)-specific endonuclease VapC"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15325
     Region          1..131
                     /region_name="PIN_SF"
                     /note="PIN (PilT N terminus) domain: Superfamily; cl28905"
                     /db_xref="CDD:475124"
ORIGIN      
        1 mlrymldtnl cirllrdrpk glrdrfnena dalcistiil nellygaeks adpvkhrssv
       61 enfaarlvil qfdeaaaaha aniravlerk gqmiggydvl iagharsagl siitgnlref
      121 trvdgliaed wlpenphsn
//
LOCUS       WP_285168860             412 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285168860
VERSION     WP_285168860.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..412
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44526
     Region          14..411
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 msdvtiiggg iigvctaial qnegfsvelv drgiategas ygncgllavg evvpiskpgv
       61 itkipkwlld pesplfvrpk dmitqmpwll rflwsgrrkr vleiakamap lthraeddyk
      121 alfaqvgisd nlvpaenita fnskadyead qfswdlrrqh gfnhrfltge elrslepald
      181 gpiscgvlle gwlqfsdpgl vqqrltkfyv srggklrtas verietdgkk avavhlagge
      241 rlqvrclaic agawsgklvr hlgikvpiaa lqgyhhhlpk pgvtlnravl yanggfvltp
      301 mesglriggt ievagvdprp nferaniiar kavgilpgld isggqqwmgp rpfmpdtlpv
      361 idrapnhdnv ilafghgqvg mtlgattgri vsdliagrtp gldlspyrst rf
//
LOCUS       WP_285168776             417 aa            linear   BCT 25-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Rhizobium sp.
            CNPSo 3464].
ACCESSION   WP_285168776
VERSION     WP_285168776.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..417
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46378
     Region          19..414
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
     Region          173..412
                     /region_name="RHO_alpha_C_GbcA-like"
                     /note="C-terminal catalytic domain of GbcA (glycine
                     betaine catabolism A) from Pseudomonas aeruginosa PAO1 and
                     related aromatic ring hydroxylating dioxygenases; cd08884"
                     /db_xref="CDD:176893"
     Site            order(191..192,196,199..200,203,205..206,210,336..337,
                     374..376,378..382,393..395,397,401,404,408)
                     /site_type="other"
                     /note="putative alpha subunit interface [polypeptide
                     binding]"
                     /db_xref="CDD:176893"
     Site            order(200..201,203..204,206..207,211,307..308,317,319,326,
                     328,358,361..362,368..369,372)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176893"
     Site            order(200..201,203..204,206..207,211,307..308,317,319,326,
                     328,358,361..362,368..369)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:176893"
     Site            order(206,211,372)
                     /site_type="other"
                     /note="Fe binding site [ion binding]"
                     /db_xref="CDD:176893"
ORIGIN      
        1 mlqtfassis slldsradgh slpaglyird dvfeadldvf frkhwicigl dcdvpepgda
       61 tvvdignssl iilrddddqi rvvhnvcrhr garildagst visklvcpyh qwtyeldgtl
      121 ahaphmgidf dksckslrpv nfksiggliy aclsdnpped idrleqvmte rlapydirna
      181 kvayqtdvie ngnwkltmen nrecyhcsan hpelcvsfvd ldfgfdpeal spedleearq
      241 healyaertk sweadgfpsa aveqlvdcat nfrtqrliia gagesqtpda taacskllgs
      301 mtrkdlgdth lwghnswnhf mgdhavvsiv iplsagktlv rtkwlvhkda vegvdydlqk
      361 ltdvwvattd qdselvgrah agaldpaylp gpysrfsett ldkfatwyid rmrangy
//
LOCUS       WP_285168956             415 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285168956
VERSION     WP_285168956.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..415
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45138
     Region          8..414
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mdenrravvv vgagiigvai afelqrrgrq vtlvdkgepg egasfgnmas ialdftassg
       61 pstwakipgw lldpegpvwl rpsyalkmlp wflrfvaagr psrlreieda gmslsrhalg
      121 dfrtmldaig aldlmteegc laiyetesef agdrghielm rrhgfehkvl sgteirdyep
      181 alslkiakav llpdnksird pyqlvlklvd aakalgvtft sgavqtverq angavsvlle
      241 ggrrleandv vlaagvhtrf iasalgepip letergyhtq imkpgiamry siiwphrafm
      301 vtptaggirv ggnvelagld appdfrrpri lvrhaqralp glqvedakdw mghrpalpdt
      361 ipiispssri pgvwyatghg hlgltfsatt arlmadmmtg vtpevdmtpf rinry
//
LOCUS       WP_285169093             533 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285169093
VERSION     WP_285169093.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 533)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 533)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 533)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..533
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56622
     Region          24..514
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mlqkntyaap aaqaaalrlp pltaasggrv phasvialas vvallslvpl gfivwitvdt
       61 gwsdaialif rsrvgelltn tvllevctip lcialavtla wltertnipg sriwswlava
      121 plavpafvhs yawvsllpgm rglwsgvlvs vlayypflyl pvaaqlrrld paiedaaasl
      181 glgpwrvffr ailpqlrlai cggslliglh llaeyglyvm irfdtfstai vdqfqsayns
      241 paanmlggvl vfccllllgi evlvrgnery arvgsgaarp adsrrlgwfv ipaialplaa
      301 avltlgvpfv tlarwlylgg agiwrmdtvg sallqtiala vaggvlatia aipmawlsvr
      361 apgrlqrile achyyvgslp gvvvalalvs itvrlilply qtfatlllay vllflpramv
      421 glrssiaqap veleraamal grtpgqavrq itmrlaapgf aasvalaalg itneltatlm
      481 lspngtetla tkfwsltsei dyvsaapyaf mmvvlslplt lllyaqskrt agq
//
LOCUS       WP_285169247             442 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285169247
VERSION     WP_285169247.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..442
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47478
     Region          16..429
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 msppvgrvas nqdvpksadv vilgggmagv atayelarrg tsvvliekgv iageqssrnw
       61 gwcrqqnrdp relplarlal rrwdnlnael gdetgfrrsg lvyattrkad lnawerwshv
      121 gqefgvdtrm ltgaecatml pgnsrhwngg vhsptdgrae pelavpalar gaqrlgaviv
      181 qncaarelet eagrisgvvt ekgairaaav lvaggawsgm flrhhgirfl qacvkstsfy
      241 tvaapavtdg giamedvtir rrldggytvg lsglgqlqit pygllqardf wrtfqtrrkg
      301 ltfalgrqfm egpeaiarwk adgispferi rtldpqpdah lvergiarlv atypelagir
      361 paecwggmvd stpdaipvis pivsrpglfv ssgysghgfg igpaagmlaa dlirgekpcv
      421 dpkpyryerm idgtdlgkpg ml
//
LOCUS       WP_285169253             487 aa            linear   BCT 25-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285169253
VERSION     WP_285169253.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..487
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=51660
     Region          15..486
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mtlsfdpnsl dlpsghfidg ryvaamggmt mhrpsdgvaf aecpvagkdl vdraveaanr
       61 alktsgwssl rprertkalv rwadlmeeea vtlarleavs strpigqlva gdiaitaeqi
      121 rffaefadke ggdlvptddh slgmimtepy gvvgaitpwn fpismagwkl gpalaagnav
      181 vlkpsemtpf stlymaelsv ragipaglin ivlgdgpttg aaitshpgis kisftgstaa
      241 gaaimeniar sgvkpmtlel ggkspqlvfa dadldqaaea iarnvlanag qacvagsrli
      301 aersiteplt eailrhmhqi kpgptwdeks lyspviserq igridsivra aigvgaeclt
      361 ggsrldrpgy fyaptllagv dqaspavtee ifgpvltlqt feteeealll adhptyglaa
      421 glftrdlsra vrvtrrlqag tvwvnrygrs rdhilptggy knsgigkdlg rdaylanrrs
      481 ksvlini
//
LOCUS       WP_285169353             326 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Rhizobium sp.
            CNPSo 3464].
ACCESSION   WP_285169353
VERSION     WP_285169353.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..326
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=36335
     Region          3..303
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mlilvtgatg kvgqhfiagv lgdprfskar iralchnrlc petervevtq gsiadretva
       61 rtltgvthvv hlatcketpa dvmdvtvkgl fwlleafrts ptarqfilig gdagighfyy
      121 rhetpiteat phraypgcya lskvleevml eqfgiqygln gcclrapwim ekddfrfsls
      181 fgddvfggpd wktlvpqada eryardgtvp llrdadgrpl krnfvhvedl vsamlsaidn
      241 prakgqlfni cmdrpvdyge vaaylartrg lgsidigsqf hsnwmdnska kyllnwspiy
      301 dlemlidsaw gyersegear iiwypg
//
LOCUS       WP_285169416             270 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Rhizobium sp. CNPSo
            3464].
ACCESSION   WP_285169416
VERSION     WP_285169416.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12044921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..270
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30284
     Region          21..166
                     /region_name="Autoind_bind"
                     /note="Autoinducer binding domain; pfam03472"
                     /db_xref="CDD:427319"
     Region          <181..242
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 msynaflihd rsaieraqty ddvcrslyel rerygaanvi ynasrsgnsl gssplmlgtc
       61 dpswvkqycd erlaeidpiv laarrsmlpv ewknvdqssr anryffsqld rfnlgrhgvt
      121 ipleghgger gfiamshhgn eddwhtcyhq hvaeltylgr yihdrmlair egpqargtar
      181 lsrqsaacld llargsdaae iaytlglsvh tvrkhlnram ttlecktkme avlkaarlgf
      241 lpnavgflsa vvmsgamldd ifidrmimwi
//
LOCUS       WP_285169568             278 aa            linear   BCT 25-DEC-2024
DEFINITION  metallophosphoesterase family protein [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285169568
VERSION     WP_285169568.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..278
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31395
     Region          1..251
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mkiiqitdth lspnkphfng nweplakwie acgadliiht gdlsvdgadk dedlifsmdm
       61 mrqvsvpmli vpgnhdvghl pgsyqpvnpe rlarwrrlvg pdywaedvyn wrliglnsll
      121 mgfedaeeqk qfdwlqdlle srgdrrvalf ahkplfvdap degdtgywsv rpaqrrrlyd
      181 liaahdvalf gsghlhwswe grfndtnlvw appgafildk merempgerl igaaihqlge
      241 tvstelvavp gmtayflddv vmevypqaap kaqkepte
//
LOCUS       WP_285169548             485 aa            linear   BCT 25-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Microbacterium sp. zg-B96].
ACCESSION   WP_285169548
VERSION     WP_285169548.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. zg-B96
  ORGANISM  Microbacterium sp. zg-B96
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Microbacterium sp. zg-B96"
                     /db_xref="taxon:3049069"
     Protein         1..485
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=50282
     Region          5..485
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mtkelrrlsi lvlamflamf astsviqvvq adalgenpln rralydtfev qrgsiiasgt
       61 aiassvpsdg lyswqrvytd admwapvtgw inpvlasatg melamnqels gtadsqflsr
      121 ieqivsgqqp rgsnvvlsld aavqraayda lgdlqgavva iepatgrila mvsspsfdtn
      181 plashngeaa eaaytaleed pldpldnrai agalnppgst fklvvasaal atgewtaqst
      241 lpnpptytlp qsssivrnag gdtcgggetv tiadalrlsc nvafaqlavl lgedvireea
      301 ekygfntsft mplvstasty prglsdaeta ltgfgqgdvr atplqmamvs agianegivm
      361 nprmvdsvia adlteqqrfd dtefgravsa diaesmtamm vanvqsgvas gatidgvdva
      421 gktgtaengv ddpytlwftg fapaddprva vavvvenggg lgqsgssnri aapiaakvme
      481 avlsr
//
LOCUS       WP_285169643             330 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: GDP-L-fucose synthase family protein [unclassified
            Microbacterium].
ACCESSION   WP_285169643
VERSION     WP_285169643.1
KEYWORDS    RefSeq.
SOURCE      unclassified Microbacterium
  ORGANISM  unclassified Microbacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="unclassified Microbacterium"
                     /db_xref="taxon:2609290"
     Protein         1..330
                     /product="GDP-L-fucose synthase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35749
     Region          25..322
                     /region_name="GDP_FS_SDR_e"
                     /note="GDP-fucose synthetase, extended (e) SDRs; cd05239"
                     /db_xref="CDD:187550"
     Site            order(28,30..33,54,57..60,80..82,84,104,123..125,154,158,
                     181..182,184)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187550"
     Site            order(101,125,154,158)
                     /site_type="active"
                     /db_xref="CDD:187550"
     Site            order(125,154,183,202,219,227)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187550"
ORIGIN      
        1 mgrsvtasdr ldytpgeldr datfyvaghr glvgsaivrk laasgfgniv gkssaeldlk
       61 nrdavfeymt eikpkyivla aakvggilan stypvdflsd nlriqtnvld aalandverv
      121 aflgssciyp rlaeqpired slltghlept ndayaiakia gilhtqavrr qyglpwisam
      181 ptnlygpndn fspqgshvlp alirrydeaa ssgaptvtnw gtgtprrefl hsddmadavl
      241 hlmehydgpe qvnvgtgtdv tireiaetig tvvgftgate wdttkpdgtp qklldvskla
      301 eagwtakitl eeglertvaw yrdnvdaire
//
LOCUS       WP_285169839             872 aa            linear   BCT 25-DEC-2024
DEFINITION  beta strand repeat-containing protein [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285169839
VERSION     WP_285169839.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..872
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..872
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=85331
     Region          <25..842
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mtsiisslsa sairslstat iaalttddva amgtsqinal tstqiavlst ediavlstkq
       61 mkaispsaiv glgldqlavl ssvqigglst vevraltttq vaglsttqis sltttqiaal
      121 satevgalst ediaalsssq igaissssls klstdnvall stgtiaalkt aqiaaltssq
      181 iaalttkqid vlsstqigal slkqvaalst eavaalsteq iaslksasia glttseiaal
      241 sttqiaaltt tqiaalsate vsalstedia tlsssqigai ssvalsklst dnvallttst
      301 iaalktaqia altssqiaal ttnqvdvlss tqigalslkq vaslstaava alsttqiaal
      361 ktaaivgltt seiaalsttq iaalsttqia alsatevgal ssadiaalss nqigaisssa
      421 lsklttsnva llttsaiaal ktaqiaalts sqiaalttsq idvlsstqmg alslrqvasl
      481 stvavaalst tqiaslksas iaalttsqia alsttqigal tttqiaalsa teasalssad
      541 iaalsssqig alssvalskl stsnvalltt stiaglktaq iaaltssqia alttgqvevl
      601 sstqigalsl kqvaslstaa vaalsttqia alktasiagl ttdeiaalst tqigaltttq
      661 iaalsaaevg alstediaal sssqigalss valsklstdn vallttstia alktaqiaal
      721 tssqiaaltt kqidvlsstq mgalslkqva alstvavaal sttqiaalas asiaalttsq
      781 vavlstaqig alsstqiaal tsaeigalss tdiealsteq ieaistrgik glstsdisvl
      841 sseqlyaitt tqaqaldseq iaaiiaayaa ys
//
LOCUS       WP_285169911             336 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285169911
VERSION     WP_285169911.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..336
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37126
     Region          65..329
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mrpirnteti laslivavft laagfvspaf sqeslpswnd taaksrimaf vkatvtdgge
       61 gyvapedria vfdndgtlwa eqpyyvqlgf mldrvktsap qhpewkekep fksilagdlk
      121 giaksgekgi velgmathag mttdqfasiv tdwfatakhp ktgkpytemt ylpmrelldy
      181 lrangfktyi vsgggvefmr pitekaygip peqvvgstit tefaivddvp vlnrlpeidf
      241 iddgpgkpag inkfigrkpi fvagnsdgdy emmrwttaak spgfamlihh tdgdreyayd
      301 rqsafgkldk aldeagrrnw lvvdmkndwk kifafe
//
LOCUS       WP_285169977             272 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Rhizobium sp.
            CNPSo 3464].
ACCESSION   WP_285169977
VERSION     WP_285169977.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..272
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29527
     Region          5..270
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtrdlkvgcq tftwemlgea wtgtpddllf aisaggyagi eitdtmighy gtkpaefaga
       61 lrdkglqlvs fafgsksgft vadaierdla taqrwidyaa efpgalvsig sativsegpr
      121 edkfaiaaef ysragalgka sgvevavhps shhntllfnr adydqifarl dpelvgwvpd
      181 tghilrghdd ildtmrtyrd rirylhlkdv dthgrwamlg kgvldtsavi dlvsqaprfn
      241 gwlvleeese taaadpaaai kanretmrth gi
//
LOCUS       WP_285169979             272 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Rhizobium sp.
            CNPSo 3464].
ACCESSION   WP_285169979
VERSION     WP_285169979.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..272
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28464
     Region          1..272
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mqvgifaktf pgtdalsvls avrdsgyatt qfnlaccglp smpdtvpepv vatiraaset
       61 agvslaalsg tynmahpdis irqkglsqla viietaaals iplvtlctgt rhpsdqwahh
      121 penrdptawa dmatemskal alaedhgvdl giepeqaniv tsaadakrli aemgserlri
      181 vldpanlfes atplearaiv eravetaagh iamahakdry adgrfatagq givdfpdfia
      241 rlkavgfhgp lvthglsaae aphvaaflke lv
//
LOCUS       WP_285170000             277 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Rhizobium sp.
            CNPSo 3464].
ACCESSION   WP_285170000
VERSION     WP_285170000.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..277
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31974
     Region          20..>163
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mqdmlifqsl wamerrsaky peltleenle kiaaagfdgi sahwsdrdav rriagllrhh
       61 glqaegqcfp ktiddlkpvl eiaaecnvhh lclqpdvrlr rledclplle gwqrlgeeag
      121 idvliethrd rmttdlfftl dlldrfpdlr llgdvshflv grefawpvsd enhalihril
      181 dnswafhgrv asreqvqiei sfphhrpwvd lflgwweygf rswrkragsd dvlaftcelg
      241 pkpyaitgrd gedttdrwee slllmqevra lwartag
//
LOCUS       WP_285170011             280 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285170011
VERSION     WP_285170011.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..280
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31364
     Region          1..191
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 maislilpvh naenfliatl ysinealgag dqlviifdsc tdrsiavfke wrelnassie
       61 yeittsvetl ggvaearnrg ldlvdrpwis fidhddvisp siyrdllasa aradadvarc
      121 gfakcskehv eicypdlspd yyaffgifiw nslfdtrlik angirfvpgy gedyefnlqv
      181 aqyckrqtfv kgplyfwkih glnhhmarrp edfaervigi fnrnhsylvn apnagaafsk
      241 wvyeyithlr gqfgsvavda sieksglsas lsqikslsrv
//
LOCUS       WP_285170069             354 aa            linear   BCT 25-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285170069
VERSION     WP_285170069.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..354
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39081
     Region          30..243
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mlqvpsaasl dlptplsgaa livasersat vavvvpmfna ertigatlas icrqtheald
       61 iiivddgssd ssasiaaaha kqdrririih qsnsgvaaar nngaaatdae flafvdaddl
      121 wapskiglqr ealerggssa glaycwfali dedsrvfsly nrptaegnvl qrmcrknfvg
      181 ngssmlmrrs afekaggfdp slrarkaqgc edllmclrva enyefrvvpq hlvgyrmtnt
      241 nmssdvmqml rsceivldef rekypgygtd ldahladmih wlavrgfvgg rffdgcdllk
      301 rflvleprla issmpnmlnv ycrarlvphw ikarlkrlrs qngkfrplym etir
//
LOCUS       WP_285170102             697 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285170102
VERSION     WP_285170102.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 697)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 697)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 697)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..697
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=77094
     Region          26..678
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mpklaetapr dkrhsslegy irsigrhyva avivmtmlig atyqtveial drhslqqdis
       61 yltgrqfirf qqlanqtrav msasinpdmp eyiiepmved vrkaigdira msgqlnelhd
      121 rlernllekl nprdvasekm rvelagrled fleradrvvs tkledrrqry sfwgpidfaa
      181 ssdsflmrrf selidsshdr sdgsidharl isavllalta talilatavl fmpllkklrn
      241 ehrrtmdfet rlthqahtda ltslnnrssf nealnqsfvs laqtgtgfsm llvdldhfkg
      301 vndssghpag davlrhvaht lkgtfrstdi varlggdefa illpglsdlt plealakrav
      361 taiatefrfd grvlpvsasi ggavvpthaa eeatlmrvad lalyaakakr ntavifdeas
      421 laqrleenql aaalafaadr nefvvhyqqk vnvesgehlg fealvrwhhp rlgilppgrf
      481 lplmegshfi ssmtrcvvni vaqdlkawki aglrpgsvav nlpevllvgg dgydliaaai
      541 ktnelewadf avevtedvfl nrgssqilet itrfrkrgms vslddfgtgf aslvhlrdfp
      601 fdelkidrsf vahlgsdvrs eqivramidl arslgkrcva egietetqrd fllragceig
      661 qgylfakpep asaavdrltv sdrgtpiapl rkrriva
//
LOCUS       WP_285170175             576 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Rhizobium sp. CNPSo
            3464].
ACCESSION   WP_285170175
VERSION     WP_285170175.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..576
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=61652
     Region          25..551
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mapqdrltat lnpagttapp hgsvpllrvd dlsvsygphq vvagvgfklg rgkslalige
       61 sgsgkstiar avlrllpdgg hatgrvefdg qevlglsgsr frplrgraig fvpqdpgnsl
      121 npvrtigvqa meaaalidep nkairkalil etfaqvgldn pqrvydsyph qlsggmlqrv
      181 liglavlprp lllvadepts aldvtiqkri ldllsrlqhe ldislllith dlaiaaerad
      241 tlvvlkdgtv qeagrtatvf sspssayakk lhadvpalnp dryavlrnpg frllrseagk
      301 tpkievsavt ksfavdgkvl tavndvsfsv qagtthalvg esgsgkttti rlllgldepd
      361 tgtisvageq lagrshqslr avwrhlqlvy qnpftsldpt wkveqlvrep ldrfkigtpk
      421 eraeqvreal anvglgdhll srkpgalsgg qrqrvaiars lvlkpdvivl deptsaldvs
      481 vqadivevll slqarlglty vfvshdlalv rqlahtvsvm qrgsivehgt vidifdnpqh
      541 pytaslldsi psgiadpaaq lpqlqtrhil reeria
//
LOCUS       WP_285170229             368 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285170229
VERSION     WP_285170229.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..368
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39521
     Region          3..364
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mntevaiigg glaglnaarl lhaagiefll learttlggr iqtvnesgqp dadgfdlgps
       61 wfwprmqpai atlvaeldlp tfvqnsdgdi vfermsrela krypgldqep etmrlvggsa
      121 alvralardl pearlrcgaq vtkmrltdag vklsirfadg qkeklrasqv iaalpprile
      181 savrfeppqe patielwrqt ptwmaphakf favydrpfwr eagfsgtaqs mvgplaeihd
      241 attstgsaal fgfvgmgaeq raaigeealt racvqqfari fgpeaaqpra tlykdwaadp
      301 ltatsadwfs aghphapddg witgpwkdrl vlagseassi eagylagave astraatdli
      361 nklatnrn
//
LOCUS       WP_285170285              86 aa            linear   BCT 25-DEC-2024
DEFINITION  LexA family protein, partial [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285170285
VERSION     WP_285170285.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         <1..86
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
     Region          12..>85
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 fgkeppagap qftqlqgqyl afiyaytrif krspaeadmr rhfevtapsv hqmvitleka
       61 gliqrqpgva rsiqllvqpe alpilr
//
LOCUS       WP_285170115             317 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Rhizobium sp. CNPSo
            3464].
ACCESSION   WP_285170115
VERSION     WP_285170115.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..317
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34980
     Region          59..317
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          230..315
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkgktvqsgi dpdelsells tpnssikvaa ldnnpvafrc hflsagpvai sdcaydgtll
       61 vkreapsdrm iiflakqgha ifdysrnpih sapghgiile gepskggrif gprhhrnlfi
      121 dkakiaghls rmldrtvsgr idihphidlt sdaglelvnl gdqlyrglyd ggwlrrspla
      181 laslcdavty lilencqhry sselartapa paprqvkwai efmeehiaep islndiataa
      241 kvsvrtlqeg fkqfkntspm ahlhemrmaa ahhdllddhs ertvadiaak wgfrhlgrfa
      301 aeykrrfgcl psqtlks
//
LOCUS       WP_285170437             301 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Rhizobium sp. CNPSo 3464].
ACCESSION   WP_285170437
VERSION     WP_285170437.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..301
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32472
     Region          71..296
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mrilvwlcla aaltataiwf vteptvpftq ndprlegngd pargqlifaa gdcaschasp
       61 gqqdrlrlgg gialaapfgt frapnissdp vdgigrwstv dlanamiggv spqrrhyypv
      121 fpypsytgmr ledikdlray lktlapvsgh ppphdlfllf rirrvlgfwk llffhegqtq
      181 asvggdtvls rggylvetig hcaechssrn ffgaikpetr faggtdpegt gfipnitpsr
      241 ighwseadia ellksgntpd hgrvgssmae vatntamlpq sdrdaiaryi kslparptph
      301 p
//
LOCUS       WP_285171115             337 aa            linear   BCT 25-DEC-2024
DEFINITION  HAD family hydrolase [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285171115
VERSION     WP_285171115.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..337
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37325
     Region          65..329
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mnrahdkiea alasliagla llligglpal aqeplaswnd taaksriidf vkatvtqgge
       61 gyvapedria vfdndgtlwt eqpyyvqfgf mldrvktlap qhpewktkep fksilngdlk
      121 glakggemgi velatathag mttdqfskiv tdwfvkathp ktgkpytdms ylpmrelldy
      181 lrangfktyi vsgggvefmr pvterlygip peqvvgstia teyaivgdvp vlkrlpkidf
      241 vddgrgkpsg inkfigrkpi fvagnsdgdy emlrwvtaak gpgfamlihh tdadreyayd
      301 rqsafgkldk aldeaerrnw lvvdmkkdwk kvftfeq
//
LOCUS       WP_285171119             329 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285171119
VERSION     WP_285171119.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10106971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..329
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=35845
     Region          94..272
                     /region_name="vWA_BatA_type"
                     /note="VWA BatA type: Von Willebrand factor type A (vWA)
                     domain was originally found in the blood coagulation
                     protein von Willebrand factor (vWF). Typically, the vWA
                     domain is made up of approximately 200 amino acid residues
                     folded into a classic a/b...; cd01467"
                     /db_xref="CDD:238744"
     Site            order(101,103,105,179,207)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238744"
ORIGIN      
        1 myqldlpwll lllplplvvh wlfpphhaas psvrlpffee vakaagvtpa rgsvaprrsr
       61 sqvivetiaw gllilalarp qfveppiekl epqrdillal dlsqsmdtrd fpgadgkpea
      121 rvdavrrtvs dfiekrgsdr igliafgdap yplapftmdh slvrtlvagl lpgiagprts
      181 lgdslglair mfektsvpek vlilltdgnd taskmpplka aeiakakgii vhtigigdpk
      241 atgeekldia tlqqiaaktg gryffgsdqp slstiynvld aitpqnqkrl swrprvelfq
      301 wplamafsll sgwylltglv gfarrrvaa
//
LOCUS       WP_285171288             262 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: XRE family transcriptional regulator [unclassified
            Rhizobium].
ACCESSION   WP_285171288
VERSION     WP_285171288.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rhizobium
  ORGANISM  unclassified Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="unclassified Rhizobium"
                     /db_xref="taxon:2613769"
     Protein         1..262
                     /product="XRE family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28441
     Region          1..78
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          117..255
                     /region_name="COG2932"
                     /note="Phage repressor protein C, contains Cro/C1-type HTH
                     and peptisase s24 domains [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442176"
ORIGIN      
        1 mqksmgerlr aareaanyps atkaaealgv slstyrahen gqnefsaeva nryakkfgtt
       61 aaylltgegl rktartapni vmsfdpdeqd hdgfaesgde lsysrehwkp qiegatpevd
      121 vklgagsgiv gevinlpvgs gnvaghkiva ewliptgylr neakaspnht iimevvgdsm
      181 qptympgdrv ivdlsqnqmt tdtvyaisdg ytepqikrlq rvpfthpgqv kiisdnpale
      241 tftveldrlt iigricghia rk
//
LOCUS       WP_285171310             285 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Rhizobium sp.
            CNPSo 4062].
ACCESSION   WP_285171310
VERSION     WP_285171310.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..285
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31254
     Region          42..255
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mgrlvvdlsd rfavsswslh ralgstypyr padqayptgq ptygkgtiel idlpqqcadh
       61 gifrleicsf hlpsplpgyl gdfrkvmeea gvklqtllve dgdlsnpeta qrdaewmagw
      121 idvaaalgae nmrviagktp ptdsaltlae ihlrrlaelt aaagvrlvie nwfdllpapt
      181 evnrildalh gkvglngdfg nwerdgkyed laeimgrael chakgrysaa gldaadyvrc
      241 iklsnaagyh gpftliydss yyhdewtgil eerdcianvf kenaa
//
LOCUS       WP_285171342             341 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285171342
VERSION     WP_285171342.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18827174
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..341
                     /product="ArsR/SmtB family transcription factor"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37680
     Region          12..82
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(16..17,19,22,25..26,29..30,33,63,83..84,86..88,
                     90..92)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(17..18,22..24,37..39,48..51,53..54,57..58,60..61,
                     67..69,74..76)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(37,40,83)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
     Region          124..280
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mtdlvklgld dvvdvlkavg eptrlrllal laagdltvtd lteilgqsqp risrhlkllg
       61 eaglidryqe gawayfrlkq egkavtlars llrhtaekdt vllrdgerls svkrvraera
      121 qayfsrnaae wdelrrlhva dedvdkalid ligpqpidsf ldlgtgtgrm lqllaghyrr
      181 avgidasrdm lavaranldr anitaasvrh gdifnlpleq qdfdlitihq vlhfldqpev
      241 aineaarmlr pggrlviidl aphgleylrd ehahlrlgfs hqaisdwlkl agldvervqd
      301 lhsgreggqa ltvtiwlard prlliasgqg hqsspilagr v
//
LOCUS       WP_285171430             139 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Rhizobium sp.
            CNPSo 4062].
ACCESSION   WP_285171430
VERSION     WP_285171430.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..139
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15730
     Region          28..128
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 maasavvnlr dsidpplrdv dlsnldfsnc pvrdlisqig gkwsvlllet lakrpyrfge
       61 lrrlvpdisq rmltqtlrdl qrdgyvdrev fptkppsvey rmtdlgysly eplalllnwa
      121 eanheavkaa rarfdqspd
//
LOCUS       WP_285171507             548 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Mycobacterium
            tuberculosis].
ACCESSION   WP_285171507
VERSION     WP_285171507.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..548
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=58872
     Region          4..539
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msvpaaplls veglevtfgt dapavcgvdl avrsgqtvav vgesgsgkst taaailgllr
       61 aggritagrv vfdgrditga dakrlrsirg reigyvpqdp mtnlnpvwkv gfqvtealra
      121 ntdgraarrr avellaeagl pdpakqagry phqlsggmcq raliaiglag rprlliadep
      181 tsaldvtvqr qvldhlqglt delgtallli thdlalaaqr aeavvvvrrg vvvesgaaqs
      241 ilqspqheyt rrlvaaapsl tarsrrppes rsrattqagd ilvvseltki yresrgapwr
      301 rvesravdgv sfrlprastl aivgesgsgk stlarmvlgl lqptsgtvvf dgtydvgala
      361 rdqvlafrrr vqpvfqnpys sldpmysvfr aieeplrvhh vgdrrqrqra vrelvdqval
      421 pssilgrrpr elsggqrqrv aiaralalrp evlvcdeavs aldvlvqaqi ldlladlqad
      481 lgltylfish dlavirqiad dvlvmragrv vehasteevf srprheytrq llqaipgaps
      541 aprkvgnl
//
LOCUS       WP_285171580             300 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Rhizobium sp. CNPSo
            4062].
ACCESSION   WP_285171580
VERSION     WP_285171580.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..300
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33671
     Region          53..279
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          195..279
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mlqelidngq vmrtvslprg rhrlhampts agyevredep ydwdgrrrgl tpftvlqhti
       61 sgtgrlryes rnyrvnagdt llvlvphnhr ywlekgerwe yfwismngee alrihrlila
      121 aagpvlklqq atidhladcs lrlvkgattp asasaiayea amalyddvfg shafaadrsv
      181 mqividhina nldkplpvee lakvgglsra hfsrvfaese gvppaefvlq qrmqraakll
      241 tkaafipvke vaimsgfdda nyfskvfrri yginptefrt tgmyasvrsp veetkngrsr
//
LOCUS       WP_285171730             357 aa            linear   BCT 25-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Rhizobium sp. CNPSo
            4062].
ACCESSION   WP_285171730
VERSION     WP_285171730.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..357
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39086
     Region          43..356
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mavtlsnspl ssdqeilqam gfdpglgrkf eagiesgllr dlhvvlaars grvcleyyav
       61 gsdenwgdpl gdvafdadtl hdlrsvtksi agllygiald rgfvpppdas lyeqfpeygd
      121 ltrdparaki tiahaltmtl gmewdedrpy tdplnseiam enapdryrfv lerpliaepg
      181 trwiysggsv alvgaiierg tgrrlpdfar evlfeplgik kfhwnagrdg vaspasglrl
      241 tapdllkigm vflqkgvwsg qrivseewia qslapaistg dglsygrlwf cgedlvpafe
      301 gprpwyagfg nggqrlwlmp dagiaaviys gkynswdawi tptrvwreii lanllka
//
LOCUS       WP_285171768             418 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285171768
VERSION     WP_285171768.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..418
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45258
     Region          1..415
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtgkvivvga giigataalr lveagwdval cdgnapgsea gasygnggwi spasiipmsm
       61 pglwrkvpgf lldrngplti dwrslpqltp wllrflwaga sktrvrrtak llsfllhdgp
      121 erhlelarkt gqeqlvlqkg llyaypdras feaealswel rrengvayve wdeteirqrl
      181 palgphyrfa iyvvngahcr dtggyvagiv eaarrkgvqf hqsavtaild gmtpqvvleg
      241 getlsadriv vaagihsgrl lrplgvripm qsergyhvtv tsgqtpfeip vmpstgrman
      301 tptnmglrls gqvelatvnk ppnweraqvl qrhalasypy laadktpnlr lwmghrpstp
      361 dglpvigpls rhpsltaafg hghvgiaaap ktadlvldal errisdnacp flpsrfgq
//
LOCUS       WP_285171779             443 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285171779
VERSION     WP_285171779.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..443
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=48145
     Region          31..430
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mpgpyvvpvh gdaelpkevd vvvigggiig tsttlelaer glrvalcekg gigqeqssrn
       61 wgwvrisrrd prevplmaea lriwstldkr tgrdtgykra giiftcaddk qyadherwnr
      121 nlegyqlesr misgaefknl fpgtqmelkg alftaadgra epqraapaia eaardngasi
      181 ltecavrgie taggrisgvi terghiacka vvlaggawss lfagmfgldl pqlkvmnsvl
      241 rtkpleggpe qaiwasgfal rkrqdggyti asghenivdi vpssfryagk flpalkkewr
      301 slnfrvsgqf fdearipnrw amdeaspfey crvldpkpst klsnaalanl kkafpvfeka
      361 eitqrwagyi dvtpdavpvi daidsipgfh iatgfsghgf gigpaagrlm adivtgkppv
      421 vdrknfrfsr fhdgskieli sgf
//
LOCUS       WP_285171791             567 aa            linear   BCT 25-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Rhizobium sp. CNPSo
            4062].
ACCESSION   WP_285171791
VERSION     WP_285171791.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..567
                     /product="dipeptide ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=61479
     Region          1..543
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msdpvlsvrd lvvkarlddg trtlidgvsl dlgkgeilgl vgesgsgksl lcrslvrllp
       61 ssllkiesgs irlqgrelte isdaemlevr ggeigmifqn ptshldpvmr igdqiaegir
      121 yhqglkarda raaateileq vgfpdpkrqy dsyshefsgg mrqramigva lscnpkilia
      181 depttaldvt iqaqilrlli dirdkrglsi ilithdlgiv aqtcdriavm rsgrlleqgp
      241 krtilsrpen pytidlinsh pslpdeaatt qpepirpers akplleiddl rvdfrvgggf
      301 lkgsgaktvs avsgvslqim pgetigivge sgsgkstlar ailgltsiss ghvtfdgidl
      361 tqrksaglar lrretamvfq dpfnalnprl tigqtlaevl kvqgkvakae iparigelld
      421 lvglerefad rkprsmsggq cqragiaral avdpkliiad ecvaaldvti qaqiidlfre
      481 ltrrmnltli fiahdlaivr nlcertvvmy rgeiveegrs qeifshpkha ytaaliaaip
      541 didpdkplhs erdaaqagqt qsakrmr
//
LOCUS       WP_285171816             263 aa            linear   BCT 25-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285171816
VERSION     WP_285171816.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..263
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27270
     Region          6..244
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mttdmngfag rlkrrenggm isgwvgipdp mlvnhlaqed fdtivldmqh gmwnmesaan
       61 giayvrlagk paiaripvgd fasasrllda gasaiiapmi nsaddaralv qatkypplge
      121 rswgpslaln hfglpaedyl qsansltati amvetrmald aideilavdg idgifvgpsd
      181 lsialsngar lapdsaaidq alatalarcr ahgkvicafg gdgarageyl klgldlviag
      241 tetaqlraga rtaiqaarkg sds
//
LOCUS       WP_285171820             309 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Rhizobium sp.
            CNPSo 4062].
ACCESSION   WP_285171820
VERSION     WP_285171820.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..309
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34061
     Region          13..300
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 msdgslffgs piwtfnwnpp yqaplrrlaa tgckgfelta wsvdmlsyyt petirelkqi
       61 adgeglvltn fffnlpfsra agaavstvdl egykrgmdva aaigtpivts mtpypfqsev
      121 kpilqrpisq ewgaavepqw dwtgeyeavv egftraceia aaaglkvaie phpyrwvssg
      181 qgmlrliert gaanlglnfd pshlfpagdm phyvvlalgd rifnthfsdn eghtnahwrp
      241 grgkidwkai faalktigys gpitleleda pgashwthfr eatpefddem rrgmnylraa
      301 aaelditis
//
LOCUS       WP_285171901             300 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285171901
VERSION     WP_285171901.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 300)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..300
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=33885
     Region          32..283
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mtiglahael iavltavtgs dprvmtvrsg dalpsgpfel ghrtlqsglr ewvqeqtahp
       61 vgyleqlytf adrdrnndil ggrtisisyl glvreqaapg ggmpgwhgwy eylpwedhrd
      121 grppilddia arltswiged amrsgqrrrr vdfdfglnga awnedlvlqr yellyearlv
      181 teagcdlkhn fgrsmfadhr rilatgmarl rakikyrpvv felmpenftl lqlqktveal
      241 agltlhkqnf rrlieqqelv eetggteset ggrpaklfrf rravleeref agtklplsrn
//
LOCUS       WP_285172190             114 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator, partial
            [Klebsiella].
ACCESSION   WP_285172190
VERSION     WP_285172190.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..>114
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          4..>29
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 marvsiseaa rltgksrttl hrlikagdls tcsgernakm vdtsellrvf gpfeqpkgeh
       61 hsgqvseqrd tasadqseqv irhlkqeieh lntlllskds hidslkqaml llen
//
LOCUS       WP_285172368             232 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285172368
VERSION     WP_285172368.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..232
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25590
     Region          42..186
                     /region_name="YpbQ"
                     /note="Uncharacterized conserved protein YpbQ,
                     isoprenylcysteine carboxyl methyltransferase (ICMT) family
                     [Function unknown]; cl42695"
                     /db_xref="CDD:478404"
     Region          119..231
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mtvtdpepms rkkaisyaig lplallvlif lpagrldwwp gwafiiflvv iygiallimr
       61 rvnpvifrar srfqagtkgw dlilvslill gmiaeiplga ldagrmgwsa mpisivllgy
      121 illaagialg twaqavnrff epgvrlqrer gqhvisdgpy ayvrhpgyvs ailvfaglal
      181 tlgswwalip agwasavlil rtswedally gelegyadys krvrfrllpg iw
//
LOCUS       WP_285172493             487 aa            linear   BCT 25-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285172493
VERSION     WP_285172493.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..487
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=51713
     Region          13..487
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mslsfdpdtl plpighfigg elievpgeid mkrpsdgkpy agcpiagpgm vdravesaka
       61 alkrsnwsgl rprervrvlh awadlieaet etlarieals strlinqlaa gdvavtaeqi
      121 rffaefadke gsdvvptddk tfgmilsepy gvvgaitpwn fpvsmagwkl gpalaagnav
      181 vlkpsemtpf stvylaelav raglpaglfn vvlgdghvtg taltghpdia kvsftgstra
      241 gsaimeniar tgikpvtlel ggkspqivfk dadlskaada iigsvlfnag qacvaatrvi
      301 veasvageft qaliarmadi gpgptwdeat ryspiiserq rdridaivaa aineggrcia
      361 ggkpmdrpgy fyeptlltdl dpsspailee ifgpvltlqt fededeamgl adhpsyglaa
      421 glftsdlsrt irlsrqiqag tvwvnrysrs rdhilptggy krsgigkdlg reaylanrkt
      481 ksvlinl
//
LOCUS       WP_285172540             745 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter permease [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285172540
VERSION     WP_285172540.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 745)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 745)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 745)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 745)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 745)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 745)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 745)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..745
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..745
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79503
     Region          167..719
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mtnskrrldv alifgiaali llpwyriegg ffglgwlsgf pgdpstapgi lqivsygrww
       61 laiaaglfml ggiarfissp msrgalmala galgfaflsm qglaitssgw swsicetifg
      121 aladgqpamg agaiilgivf vlffslglae rgamkgdafv vsaitmlivl vaifvfypvg
      181 smfvgafqaf dgsfdpsgft tniqdpsiws lscivggdrc gvawrtlwla iltasgstll
      241 glcfalvatr trfpfkkglr lltilpiitp pfvvglaltl lfgragvvtq aaasifgtep
      301 srwlygltgi wiaqvlsftp isflvligvv egvspsmeea sqtlranrwr tfwrvslplm
      361 kpglanafli gfiesmadfg npmvlggshg vlsteiffsv vgaqndpsra avlamillvf
      421 tlsaflaqrl wlqgksfatv tgkgdsgahs alprglsitv halvipwmif tvvvyvmilf
      481 ggfvrtwgld ntltvehyvk afsiglrddg glawtgvawn sfwttmeial isapltaavg
      541 lltaylivrq kfvgrglfef almmsfaipg tvigisyima fnlpplemtg talilvacfv
      601 frnmpvgvrg gvaamsqldk sldeasltlr adslrtirkv ilpllrpait aalvysfvra
      661 itsisavifl vsaqynmsta yivglvenge ygvaiayssa livvmisvia gfqllvgerr
      721 lrrvnrvait ppptapasla qekta
//
LOCUS       WP_285172650             173 aa            linear   BCT 25-DEC-2024
DEFINITION  c-type cytochrome [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285172650
VERSION     WP_285172650.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 173)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 173)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 173)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..173
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18702
     Region          <48..129
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mgyaregrqy rtdpplgaal delrlmpngi sgappeiyfa lgkpyektay dlsqgkrlys
       61 rfgcgachge grggtgpsfl dgwwlygpem vsiaasirdg rphgmpafrd kmtideiwql
      121 agyvqtigay kakttapsrn ddkqtrpaen rapaailfde gpagpnavqe psh
//
LOCUS       WP_285172717             757 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase NtrY-like [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285172717
VERSION     WP_285172717.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 757)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 757)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 757)
  AUTHORS   Machado,H.B., Yates,M.G., Funayama,S., Rigo,L.U., Steffens,M.B.,
            Souza,E.M. and Pedrosa,F.O.
  TITLE     The ntrBC genes of Azospirillum brasilense are part of a
            nifR3-like-ntrB-ntrC operon and are negatively regulated
  JOURNAL   Can J Microbiol 41 (8), 674-684 (1995)
   PUBMED   7553451
REFERENCE   4  (residues 1 to 757)
  AUTHORS   Pawlowski,K., Klosse,U. and de Bruijn,F.J.
  TITLE     Characterization of a novel Azorhizobium caulinodans ORS571
            two-component regulatory system, NtrY/NtrX, involved in nitrogen
            fixation and metabolism
  JOURNAL   Mol Gen Genet 231 (1), 124-138 (1991)
   PUBMED   1661370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20231976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..757
                     /product="sensor histidine kinase NtrY-like"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=82947
     Region          25..306
                     /region_name="NtrY_N"
                     /note="NtrY N-terminal region; pfam19312"
                     /db_xref="CDD:437144"
     Region          295..743
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mmqdavspaa sdetvvkvtd rrasfalpgl ilaggallca iatllmllgl tpvaptssvv
       61 ftsvvinglf vlglialiar evarlmkars rgraaarlhi rivvlfsiva itpailvaiv
      121 asltlnvgld rwfgvrtqqi isssqnvaqa ylmenasylq gqtvsmandl ernrslfnld
      181 rtgfadlmtr qargrgllga flvrrdgsai vqaeikterp lpaipkdald ssangqptli
      241 ppgvtnlvga vikldeipga flytvravdp rvmnamrmve dntveykame egrmslqiaf
      301 avlyigfali vllaaiwtai aiadrivrpi rllisaadnv asgnmnvlvp vrsadgdvgs
      361 lsrtfnkmis eirtqrdeil eakdevddrr rfieavlsgv taavigvehd rritivntsa
      421 edlltlksde ligknlsdis pevdqvvtea ttrhrsdfrk qislvrggtv rtlsvqvtre
      481 esrdanesyv itldditdlv iaqrstawad varriaheik npltpiqlsa erirrrfgkn
      541 iadadrpvfd qctdtiirqv gdigrmvdef ssfarmpkpt meptdlrdil rdavflremg
      601 nthvqfgrel gderlegmfd armlgqafgn liknaveaie gvpsdqapeq pkilvrssld
      661 pdrdrftvdv idngrglpve nrhsilepym tmrekgtglg laivkkiied hggqielhda
      721 padfdqgrga mirvhlprre qaavahtend kesvygi
//
LOCUS       WP_285172730             103 aa            linear   BCT 25-DEC-2024
DEFINITION  FtsB family cell division protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285172730
VERSION     WP_285172730.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..103
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=12040
     Region          13..100
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 mwtkyhkkrr fgrlilpait iafvsyfgyh cihgdyglka teifekrrid rakeladlva
       61 krehlekeva llsdgsldkd mldqyaryql tyskaneivi fnk
//
LOCUS       WP_285172783             483 aa            linear   BCT 25-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285172783
VERSION     WP_285172783.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..483
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=54615
     Region          6..464
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mttsktkpil lwfrkdlrld dnhalqaaat sgrpvipiyi lelegngggp lgdaqewwlh
       61 hslaalqvaf grldsklilr qgdalavldn liaetgaeai vwnrrydpag iaadtqikka
      121 lrgngieats fagqllhepi rlrtgtgnhy ktytpfwraf eqsgeppfpi eppeklpaps
      181 hwpksdrlda wsllptkpnw aiafpqmwtp geaaaqeklk gfidgavdvy avdrdfpdkp
      241 atsllsphla fgeispariw hatrglpdni atdnvvrfrk elvwrefcyh qlfhfpklrt
      301 enwndryddf pwltdakllr swqrgqtgyp ivdagmrqlw rhgwmhnrvr miaasflikd
      361 llidwrdgea wfrdtlvdad paantanwqw vagsgadasp ffrifnpvlq gekfdpdggy
      421 vrtfvpelan ldrkyihrpf eapddvlkra gvelgkhypr pivdhamarr ralaahaslk
      481 dng
//
LOCUS       WP_285172846             522 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285172846
VERSION     WP_285172846.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..522
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55521
     Region          1..522
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 msydaiivga ghnglaaavh laskgwkvav iegnaepgga vktrevtlpg frhdlcamnl
       61 smfagsaffa qyknellaeg lgfvpaadcf asvfrdnayl gvstdlekta gaiadispqd
      121 aaawrtmlst fgtdaphifg llgspmpsma aakvvwkawr dkgtgwvydt armlfasprd
      181 fldarfqntk lktmmaawgl hldfapdvag galfpylesm anqafgmvig kggadtiika
      241 maavlkskgg elmlgtrvdk ittsggkatg vvladgrrye akravianvh pqilfgklle
      301 qdpsrrefdg kvsrfragpg tmmihlalsg lpewtagqal qnfayvhiap dlemmsrvya
      361 eaiggllpte palvigqpta idpsrapagq hvlwiqvrvl paefhsdaag qisgagwdei
      421 kdayaervld iveryapglr gkilgrsvfs pvdlerenpn lvggdnlsgs hhldqnflfr
      481 pvagysrykt pvaslymcga stwpgagtga gsgfmlgkml ak
//
LOCUS       WP_285172848             529 aa            linear   BCT 25-DEC-2024
DEFINITION  phytoene desaturase family protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285172848
VERSION     WP_285172848.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..529
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56807
     Region          1..512
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mgdhdyiivg sginalvaaa mlgkkghkvl vlerndrigg clrteeitep gfihdvmatt
       61 mvlfltspay gaigkdlear glefahadlp tgvlrpdgsh vifskdrqrn iaafdklspg
      121 dgqtfsrdme alasdapflf sllggalwsg stlktvakqg wsrglrklaa wfgealtpar
      181 gyletsyrse dihalwapwv lhcglgpesa ysaemlkvig falelggapi vkggaekllt
      241 aferlitdng geirvsadve aiipdanrsa dgvrlanget lkakagvics vtpnqlyerl
      301 mmdwpdplpp evksgvasyr ygkgdmqlhy alsepprwka naelgkvall hltsgldgvs
      361 raanecergl lpaeptvcvg qpvaldptra pegksilwlq lpeaprhikg daageietpr
      421 dgrwteevre ryadrieall sshienfsgi klarrayspa dleamnmnlv ggdpyggycg
      481 idqlfiwrpf kssvnhrthi sglyhigasv hpgaglgggs gfllasslk
//
LOCUS       WP_285172862             143 aa            linear   BCT 25-DEC-2024
DEFINITION  acyl-CoA thioesterase [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285172862
VERSION     WP_285172862.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..143
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15823
     Region          1..135
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mafrtirplr fgdcdpsgia yfpsylnilv gvledyfasi gfswrklidd rrigvptvrl
       61 dltfikpglq gddlefllsv hgvgrssldl qhqvsanglv lwtakhrvva tsldthtsle
      121 wpediraalt shlettdahh pat
//
LOCUS       WP_285172949             420 aa            linear   BCT 25-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285172949
VERSION     WP_285172949.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..420
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44546
     Region          36..403
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mpieswrgge vdvtvigaga agvaaarqlq llrpdlsill leasdrvggr arsihpfgad
       61 aaaldlgcgw lhgartnawt diaeevgltv drtpapwsdg ghrleqndpd akaaaaavnd
      121 ffervygyeg dtdadlsaml spddpwneri yavgafmtgg eldkssvidl grydpgpgpd
      181 wrvrqgygmv vatyglrvpt vvgaevsrid hsgaehivls takgelraka vivtvstnvl
      241 aaeriafwpp lpekieaasr lplglanklf lrtaeprmfp edahvmgsqh srrtgayqlk
      301 pfgmpvieay faadlaldle regvdamfdf sveqlkrtfg advgrklspl aasawagepf
      361 fggsysyatp gasdlrgvla ashdgrlffa geacskarys tahgayetga aaaeavaksl
//
LOCUS       WP_285172955             522 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Rhizobium sp. CNPSo
            4062].
ACCESSION   WP_285172955
VERSION     WP_285172955.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 522)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..522
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=56572
     Region          11..511
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mtvynsakgg aqilvveddp iqrrllknai erhghvahla engrlglefl krgndqinvi
       61 vldlmmpemn gieflgalnd mgidlpvivq tgqggidtvv qamragafdf vvkpvsperi
      121 aasianalkl dqreakarag rksrsssitf ddivsaspam mrvidlahra aqsnipvvle
      181 gesgvgkelv araiqaasdr agkpfvtvnc gaiphnlves ilfghekgaf tgaaerhvgk
      241 fmeadggtlf ldeigdlple vqvkllravq qgeietvgar vaqkvnvrli satnkdliee
      301 vkagrfredl yyrlnvfpit mpalrrrked iphlarafad rfaleqkldh plgisndala
      361 lltaydwpgn irqlenavfr avvlsegpel ldtdfpqiaa qlpgyfaaeh ptlvvdnsha
      421 ssadllaaer servsygvsh gsaattplas adasdnvivs tntsgdvrkl adveeelirf
      481 alkfyrgqms qvarklgigr stlyrklkdy gidpddpqkn aa
//
LOCUS       WP_285173005             478 aa            linear   BCT 25-DEC-2024
DEFINITION  WS/DGAT/MGAT family O-acyltransferase [Mycobacterium tuberculosis].
ACCESSION   WP_285173005
VERSION     WP_285173005.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Stoveken,T., Kalscheuer,R., Malkus,U., Reichelt,R. and
            Steinbuchel,A.
  TITLE     The wax ester synthase/acyl coenzyme A:diacylglycerol
            acyltransferase from Acinetobacter sp. strain ADP1:
            characterization of a novel type of acyltransferase
  JOURNAL   J Bacteriol 187 (4), 1369-1376 (2005)
   PUBMED   15687201
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Kalscheuer,R. and Steinbuchel,A.
  TITLE     A novel bifunctional wax ester synthase/acyl-CoA:diacylglycerol
            acyltransferase mediates wax ester and triacylglycerol biosynthesis
            in Acinetobacter calcoaceticus ADP1
  JOURNAL   J Biol Chem 278 (10), 8075-8082 (2003)
   PUBMED   12502715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496208
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..478
                     /product="WS/DGAT/MGAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0045017 - glycerolipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=50672
     Region          5..463
                     /region_name="acyl_WS_DGAT"
                     /note="acyltransferase, WS/DGAT/MGAT; TIGR02946"
                     /db_xref="CDD:274360"
ORIGIN      
        1 mdlpmaaada lflwaetptr plhvgalavl sqpdngtgry lrkvfsaava rqqvapwwrr
       61 rphrsltslg qwswrtetev dldyhvrlsa lppragtael walvselhag mldrsrplwq
      121 vdlieglpgg rcavyvkvhh aladgvsvmr llqrivtadp hqrqmptlwe vpaqasvakh
      181 taprgssrpl tlakgvlgqa rgvpgmvrvv adttwraaqc rsgpltlaap htplnepiag
      241 arsvagcsfp ierlrqvaeh adatindvvl amcggalray lisrgalpga pliamvpvsl
      301 rdtavidvfg qgpgnkigtl mcslathlas pverlsaira smrdgkaaia grsrnqalam
      361 salgaaplal amalghvpap lrppnvtisn vpgpqgalyw ngarldalyl lsapvdgaal
      421 nitcsgtneq itfgltgcrr avpalsiltd qlahelellv gvseagpgtr lrriagrr
//
LOCUS       WP_285173035             480 aa            linear   BCT 25-DEC-2024
DEFINITION  vWA domain-containing protein [Mycobacterium tuberculosis].
ACCESSION   WP_285173035
VERSION     WP_285173035.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466432
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..480
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=52443
     Region          18..478
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 maarriraar plaphglpgh lvgfvealrg sgisvgpset vdagrvmatl glgdrevlre
       61 giacavlrrp dhrdtydamf dlwfpaalga ravittedes agsgglppdd veamrqllld
      121 llannqdlag kderlvemia riveaygkys ssrgpsfssy qalkamalde legkllagll
      181 apygdeptat qeqiakalaa qkiaqlrrmv daetkrrtae qlgrehvqmy gipqlsenve
      241 flrasgeqlr qmrrvvapla rtlatrlaar rrraragsid lrktlrksms tggvpidlvl
      301 hkprparpel vvlcdvsgsv agfshftlll vhalrqqfsr vrvfafidst devthmfgpe
      361 sdlaiaiqri treagvyard ghsdygnafv sfmqgfpnvl sprssllvlg dgrtnyrnpa
      421 tdvladmvta srhahwlnpe pkhlwgsgds avpryqevit mhecrsakql atvidqlppv
//
LOCUS       WP_285173212             603 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-dependent nuclease [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285173212
VERSION     WP_285173212.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..603
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=66668
     Region          1..468
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mrltkfriln yrnimdsswv tttdvtafvg qneagksnlf ealyclnpyv dgaayndaed
       61 wpvdnwkgrk dakgkrvcea ffsltsediq slfaaahtpe ksaetetept iakpltlpas
      121 ldlfacrnyg qptlfvvvga delgldvtkv sawakahlpk fvlihdynfs gtqveldqlk
      181 qrwdavgrsn rhllstedqt ilivldlaqi diddfvqkgt sadgrtirqf dkraasaylt
      241 qqfqrlwtqk kvkfdididg ptlnifaede sigfpvrmhr rstgfrwyvs fawkfthasd
      301 gefencilll eepgvhlhys gqrdllkvfd dlaekntily tthlasmvdq anpervrive
      361 tqdnhlainh gvvsaqaapm avieaslglt adlagmlgnr kvliveggtd alilnklssi
      421 lsaggktgls eqvymwpaat stkapmyaaf aigqrwnagv lldsdeagls akkkisemgl
      481 kelasnegyd frvmmlgeas gikktdvaie dlfpddffre cvnrayglgi rdgdlpvdgs
      541 tliskrvekv lssrygktld kklvlgemlk vfdiwktvad lpaetvaaae klfkainaaf
      601 sat
//
LOCUS       WP_285173318             281 aa            linear   BCT 25-DEC-2024
DEFINITION  protein-L-isoaspartate O-methyltransferase family protein
            [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285173318
VERSION     WP_285173318.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Edwin,R.K., Challa,N., Sharma,R., Satyamoorthy,K., Parsa,K. and
            Misra,P.
  TITLE     PIMT/TGS1: An evolving metabolic molecular switch with conserved
            methyl transferase activity
  JOURNAL   Drug Discov Today 27 (8), 2386-2393 (2022)
   PUBMED   35462043
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Furuchi,T., Sakurako,K., Katane,M., Sekine,M. and Homma,H.
  TITLE     The role of protein L-isoaspartyl/D-aspartyl O-methyltransferase
            (PIMT) in intracellular signal transduction
  JOURNAL   Chem Biodivers 7 (6), 1337-1348 (2010)
   PUBMED   20564550
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Kagan,R.M., McFadden,H.J., McFadden,P.N., O'Connor,C. and Clarke,S.
  TITLE     Molecular phylogenetics of a protein repair methyltransferase
  JOURNAL   Comp Biochem Physiol B Biochem Mol Biol 117 (3), 379-385 (1997)
   PUBMED   9253175
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..281
                     /product="protein-L-isoaspartate O-methyltransferase
                     family protein"
                     /EC_number="2.1.1.77"
                     /GO_function="GO:0004719 - protein-L-isoaspartate
                     (D-aspartate) O-methyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0030091 - protein repair [Evidence IEA]"
                     /GO_process="GO:0036211 - protein modification process
                     [Evidence IEA]"
                     /calculated_mol_wt=30170
     Region          27..232
                     /region_name="Pcm"
                     /note="Protein-L-isoaspartate O-methyltransferase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2518"
                     /db_xref="CDD:442008"
ORIGIN      
        1 mtadrrasld eirdfhaklm aaasnssder lerafrlvrr eafmgpgpwq iragrhylet
       61 pnadptflyq nvlvaldksk ginngepflh aaflgavapq pgetvvhigt gtgyytails
      121 tlvapggqvh aveidetlas rtrdnlasfe nasvicadat elelpqgdli yvsagvvapp
      181 iswlqalrlg griivpwqan dkvglavlit raeqgfgara lmpayfipci gasdpmqttk
      241 tpnggearsi qsvwltqdra pdetavaiyr dvwfsnaglg v
//
LOCUS       WP_285173361             185 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: YceD family protein [unclassified Rhizobium].
ACCESSION   WP_285173361
VERSION     WP_285173361.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rhizobium
  ORGANISM  unclassified Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Yang,J., Suzuki,M. and McCarty,D.R.
  TITLE     Essential role of conserved DUF177A protein in plastid 23S rRNA
            accumulation and plant embryogenesis
  JOURNAL   J Exp Bot 67 (18), 5447-5460 (2016)
   PUBMED   27574185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="unclassified Rhizobium"
                     /db_xref="taxon:2613769"
     Protein         1..185
                     /product="YceD family protein"
                     /calculated_mol_wt=20155
     Region          9..185
                     /region_name="YceD"
                     /note="23S rRNA accumulation protein YceD (essential in
                     plants, uncharacterized in bacteria) [Translation,
                     ribosomal structure and biogenesis]; COG1399"
                     /db_xref="CDD:441009"
ORIGIN      
        1 mkrhdsdetp fsypvkvghi sanpvdvhve addrelagla alwdvlsvgk leadlkisrw
       61 krdgvrikgn vkakivqacv vtlepvesdi dedfehifvp edsklaraps vdagemildp
      121 dgpdlpetft gdtidagaav aefaalaidp yprkpgvefd ahiedtgedd rkpspfavlk
      181 dwkke
//
LOCUS       WP_285173472              83 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Klebsiella
            aerogenes].
ACCESSION   WP_285173472
VERSION     WP_285173472.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella aerogenes
  ORGANISM  Klebsiella aerogenes
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10648172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Klebsiella aerogenes"
                     /db_xref="taxon:548"
     Protein         <1..>83
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          32..80
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 gkvpvtfvpr titiidfval ingsycsvpe aavslsrkqh qvlscianqm ttedileklk
       61 islktfychk hnimmilnlk rin
//
LOCUS       WP_285173630             517 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285173630
VERSION     WP_285173630.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 517)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 517)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 517)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..517
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55232
     Region          154..468
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrvlsdisvg avafvnrvgr swlsrtsgdg evrgqelail rrlalvssva lfavpaglsl
       61 vtspavalpa gvatvcaafl fsavgsials rqrpalrpae avvvehrdlm lesafglvll
      121 ldpqgnvtta ggrdrtefls wmhnplgrgf veqihisdri vflqaidvlr qgrdahsadl
      181 rlersavvgg ddqfvhvrme ltarrdgegr laaivsqlrd isqdqqlred aarkaaeaes
      241 andaksrfla avshelrtpl nailgfsdil sgeyfgklen drqreyvgli rqsgahllsv
      301 vntmldmski eagryellle sfaiedtiat ceamlglqak ekgltltsri qrglgeivad
      361 qraiqqilin lvgnaikftd aggaitidaa ladgmlklsi gdtgigiase rlaslgqpfv
      421 qiqndytrry agtglglslv kglvglhggn fsiasapgeg tvitilipfd gsgavtmqqp
      481 vdvnrpvdfp prlkhtveid egrnkelmng pakakia
//
LOCUS       WP_285173669             483 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285173669
VERSION     WP_285173669.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 483)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..483
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=53038
     Region          180..463
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mnlersrslr wglikrlivl qafllvlffv llvawlwiin peledaneea vrvvaqqitr
       61 nddgqlqvae tqevaelkrr ypelwfmird skgilfqyge ipaaaldesf pwtidrarve
      121 agngahatve nretsvgklq ivaatergfn ndglnvwinm rvdvakgpng eihwlnvlpa
      181 laflifigvf pilavtgvat llvtpravgr slsglvetat qaqaidfdsr sarlerskvp
      241 teiiplvdaf nhalskldeg ynrhnrflad aahelrtpia iartradllp eaeisqqvrn
      301 didrlsrvah qllemqaiga velraekkdl nmlveniaad lapiamdagy dfdfepssee
      361 alfviqtsti emavvnlirn aidhaggkgs iivrvsadga idvcdegpgi plaerdrvfe
      421 pfrrinasss gaglglnlvk kaaelhggrv sfpdtgcgfc vrlqigsipp tvvvadmgwr
      481 qkp
//
LOCUS       WP_285173699             379 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285173699
VERSION     WP_285173699.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..379
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40019
     Region          8..351
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mrdagsnagk sahmlvslqv lralaassvv lahalheaei latatgsvav dgsawnlgfg
       61 vdiffvlsgf imthtaasef grsgaplhff lrrcarvvpl ywlltsimll galaapsllv
      121 vpvgsishvl asyffipsgr gvgeirpvla lgwtlnyeml fyvlfalall lpirlgivwl
      181 salmvgmalv gnlvdpshvq iafwtspiil eflfgvyval ifrsgvrigk giafglvaig
      241 llgfvhvstl wndaalpqfl rsglpaallv laaaigpalp hrrpvlwsaa lgdasyslyl
      301 ahpfilrpmr aiwaqmigga lppglfagfs tlaavllala lfrgvekplt rsvqdvvlgs
      361 arrkrisaga lptadtesa
//
LOCUS       WP_285173737             139 aa            linear   BCT 25-DEC-2024
DEFINITION  NUDIX hydrolase [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285173737
VERSION     WP_285173737.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 139)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..139
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15200
     Region          6..128
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 mtktiriaaa lvlrpdgktl lvrkrgttaf mqpggklepr etpetalire lfeelgltae
       61 tkdltflggf qaaaanepdh tvvadifrlq vgniaitaaa eieeirwvsp qdpgnitmap
      121 ltehhvlpfh rqqshprcd
//
LOCUS       WP_285173738             326 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285173738
VERSION     WP_285173738.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..326
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34245
     Region          20..323
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mirfslalaa tlflaapsgy aaglkfiris gdadnpaida amwspcaapp tevriralav
       61 patpdcpiag eelpliiish gyggwylghh dtaealadag fivvainhph anhadmsqan
      121 glgvlierpa dikrtvdfml daspdagkin pqqigfygfs lggytglvva ganpdfsklp
      181 rrcsdpkaag cppaghaqpp rqpssqslth dpriravvva dplsivfpta dsvkdvkvpl
      241 qlwgselggg ggaapenvat larllpekpd frvvpnavhl sfltpcpelr pssdacidap
      301 gfdrvafhkq fntavvaffr khltkp
//
LOCUS       WP_285173796             903 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285173796
VERSION     WP_285173796.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 903)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 903)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..903
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..903
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=99128
     Region          1..894
                     /region_name="PRK10490"
                     /note="sensor protein KdpD; Provisional"
                     /db_xref="CDD:236701"
ORIGIN      
        1 madesrdmlg rpspdallek araetrgrlk iflgaapgvg ktyemlmsgr akiadgvdvv
       61 vgvvethgrr etqalldgfe ivprvnvdyk graleemdld ailkrrpelv lvdelahtna
      121 ygsrhpkryl dvkelldrgi dvyttlniqh veslndvvsq itrirvretv pdsiidmadd
      181 veiidltpdd likrlhdgkv yvsktaeral tnyftpgnlt alrelalrrt aqrvddqllt
      241 hmqahaiqgp waagervlvs idhhprsaal vryaarmaar lrapwaavyv etnrsislse
      301 aqrdtiaatl rlaeqlggea itlpgrevae ellrhsasnn vthivigspk igswrdwsrr
      361 svsydlirra gdisvhvisg seadgeaakr gvkvapsppp fqfrgyvlat lyvaialgfc
      421 vildqvldvr nlalvflmav lvsavtqglr palyscflga lafnffflpp rytltisdpe
      481 svlafffflg vaviasnlta tvqrqaaaar qrarttedly lfskklagtg tlddvlwata
      541 fqlasmlklr vvlllpehgt iavragyppd dtlddadiaa arwawehnha agrgadtlpg
      601 akrlyvplrt grtavgvigl dsdrrdgpll tpeqqrllda ladqaalaie rvqlvadvdr
      661 aklaveadrl rsalltsish dlktplaail gaagtlrdyl etlphedrvd llstvidese
      721 rlnrfianll dmtkiesgam epnyalhyag divgsalrra ekilahhrvd vqmpvdlpmv
      781 kvdpvlfeqv lfnlldnaak yapegsairl eawadidniv frvmdegpgi ppadlervfd
      841 tfyrvrkgdq vragtglgls icrgfieamg gtiaagnrtd rqgavftirl pkptdvlkld
      901 elk
//
LOCUS       WP_285174035             443 aa            linear   BCT 25-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285174035
VERSION     WP_285174035.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..443
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47139
     Region          8..436
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 msqaplnpsl sqvlsrldql tnwerkprge mrvglepmld lmqrlgnphr sfravhvagt
       61 kgkgsvsall eagllragwr igrygsphvd rvnervsilg qeveddalat aitqvldsye
      121 dakraataae datwfdvita aafvvfrdag lswvvvevgl ggrldstnvv fgevaivtni
      181 glehteilgs treaiarekv gilkpgatlv ttlaagdvag qvlqqradel gckvlrtdlp
      241 edatiaetni alvglafdhl grqgesvreg gekgqpigaw llekavidka clpgrmerfd
      301 vslspvlakg rqslpmimdg ahvpfnieav lrditrsssv sgecvaival asdkdapgfl
      361 dvlsryaaya vfteasgsgr ahpaieleal grslgmscea epdphraldr atvkaaergg
      421 wmlvtgslyl vgalrstvvr naq
//
LOCUS       WP_285174077             420 aa            linear   BCT 25-DEC-2024
DEFINITION  O-antigen ligase family protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285174077
VERSION     WP_285174077.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..420
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=46841
     Region          168..401
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 msainlpssr vaqpqlaamr lvgtasvavg vflsgfviae papyelwlaf ligtwfilgl
       61 kisrsvapll alfllfnigg mlsitqmhdl aasdhlagpi yiavstflal ssvfyaaite
      121 dnekrlklif stwvvaalit aslgilgyfh avpgfdiftr ydramgafqd pnvfgpylva
      181 pslylmhgll igdlkkapik giclfvlafg iflsfsraaw alfafasvml ifcmllkhrs
      241 ntfrlrilvm slaaiilmvv llvgalqfpq vsdlfstrlq lvqsydgghl grferhsigf
      301 qmsmerpfgi gplvfgqifr edehntwlkt lttygwlgfv twvsmicwti yigfrnllre
      361 rpwqpylmia wivilghvgi gnvidtdhwr hfylligivw gcgaleqkyq rdlnkrkaas
//
LOCUS       WP_285174088             752 aa            linear   BCT 25-DEC-2024
DEFINITION  GumC family protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285174088
VERSION     WP_285174088.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..752
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=80669
     Region          2..686
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 msgvnstqqd vdidlaqlfr avwqrrvrvv aitlagacaa laiakvmspe yrsearilie
       61 qrapafaatt ssndagagpl ldelniasqv qilqsadlvk qvitnlklyd rpefaagnng
      121 safsdilikl hlkqaaadka peermldafn srlqvyqins srvigisfts rnpdlaasvp
      181 namaqvylsm qsgakldsns eatrwlepei aklrdkvsea ekkvadyrsa ngllqtsqnn
      241 nfatqqladi stqlaqvrgd kanaearaqa vrsalssgrs tdtladvags qtiqrlkatq
      301 snlesqisdl sttlmdghpr lkslraqlvd irqqidretq rilasienea kvaqlreqql
      361 laqsntlkad saragedevg lnalereata erqlletyla ryreaasrvd knsspadari
      421 vstavepvdp sfpkvgpivv vatlatfilt aivimlaelf sgralrpvgl vrkedaaale
      481 taqrtqpvte papvrpvara ssvetpasml svpveeipvr aadtvtapeq aialdtaiap
      541 dhgpkqvaqt aaeeeedfsi qsvadylids gsrlaiaisp tgdngstatv mlartiadag
      601 srivlvdmtg tgcpsrlmae hdelpgvtdl lcgeaafgdt ihpdrlsdah lvpqgmsdla
      661 ramrgadrls lildalgsay divlvecgaa evsgvarltr sketeiilsm pepdesqfia
      721 amtefqkagy ehiilmsgwr eehdpdtrrd aa
//
LOCUS       WP_285174103             125 aa            linear   BCT 25-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Rhizobium sp.
            CNPSo 4062].
ACCESSION   WP_285174103
VERSION     WP_285174103.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..125
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=13872
     Region          17..104
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mstnkasrfa atpeppyyiv sfasirtagd ngygamgerm eemalaqdgc lglesargad
       61 gfgitnsfwr dgesilawkn vvahlaaqkl grerwyeqyk vriarveray dfqlregdaf
      121 aehld
//
LOCUS       WP_285174121             172 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Rhizobium sp.
            CNPSo 4062].
ACCESSION   WP_285174121
VERSION     WP_285174121.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..172
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19080
     Region          6..109
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mdierrsgcp inltmevlgd rwslvvirdi mfgnrrhfre llnrseegia snilaarlkr
       61 lvslglitkl ddpshsqkai ysltepaiql vpmiamigaw grrhlpased lsiraellek
      121 ggpalwddfm ndlrnihiad piggangsvt spvlmgltna flevrakmer ke
//
LOCUS       WP_285174125            1151 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285174125
VERSION     WP_285174125.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 1151)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1151)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 1151)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 1151)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 1151)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 1151)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 1151)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20693118
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1151
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..1151
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=128373
     Region          1..208
                     /region_name="AAA_27"
                     /note="AAA domain; pfam13514"
                     /db_xref="CDD:433272"
     Region          <273..>810
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          583..1148
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
ORIGIN      
        1 mrftrldilr ygaltdraid frpdarlhvi ygpneagkss alsaisdllf gfptaaeqsf
       61 lhepgalrig adisardgar lsfrrrrgrk gtllapddke talaedalap flgnlsrdvf
      121 erafgldsqr lrqgasamlr sggeigsllf saasgltgls rlrqsleaea dgiyaarrsk
      181 drgfyqaldr yedarkaerd nelksgdwkk llaeaaelet elerlqaerr gtresldrlk
      241 rlktlqplls eidaethald glsdlaaipd gfadkleqrl rdkeaseael rrarqavlra
      301 eedlsriqvd eallrmstdi tqlfadtgny raqrhdlprv dqelagydtt laqltrrlgl
      361 aeaelerrqp sdidrarlse lveqgrqlar qmqslaeqad gerrqlaale kdslngrlid
      421 prpyidqlea lgsdlsalar ldgletqirr teadlhetag rlqppigdid ilfsvplpev
      481 teitghrdai daarskvrda tgklqtydeq laeierilad aertgpvvtr eqiaaaresr
      541 daqwsfiqqr wtngaapepk ilagltvsva eadrladaal sdadrvarha dyrlrqarll
      601 rereeasgrl kgcekalkda qaafaalfep cgvdaldpsa mlewrravel lrrerkalrd
      661 lvdqrdenal aedrvlpalq diveatgykn grlppaaiae glrkhlrlls erwsesrtre
      721 geigaarerl arfgdqqqsl erqhtdwrga fakavellgl ppdttldman aalkawqelp
      781 dvlaerenrl rrvsgmrrdm adferrlatl aansgyeldh lppdaaveal htrvnamrge
      841 lkkrdgleee rqrgeglvvr qeaalaaiat dldhltadld gvedlpglls rlhersrlta
      901 rlaesrdrfr lqadgkaede lraelagfer vaadlemerl teedqrqfai hgelsarlae
      961 nrrqrqalet gasaeyavfe klsaeqeakd larqwvvlki aarmlagsme ayrekqadpv
     1021 isragelfsq ltggrfsrlv eahdesdalq llaeraager vpldglsegt gdqlylalrl
     1081 afledysarn epaplivddi fqtfddervs aglqvlaata drfqtilfth ersvvdiaks
     1141 eigrdldliq l
//
LOCUS       WP_285174202              67 aa            linear   BCT 25-DEC-2024
DEFINITION  transcriptional regulator [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285174202
VERSION     WP_285174202.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008341
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..67
                     /product="transcriptional regulator"
                     /calculated_mol_wt=6885
     Region          12..62
                     /region_name="YdaS"
                     /note="DNA-binding transcriptional regulator YdaS,
                     prophage-encoded, Cro superfamily [Transcription];
                     COG4197"
                     /db_xref="CDD:443351"
ORIGIN      
        1 menvcdiakl kaggpaalak alggvtsqav sqwkkvpaer vldveritgi srhelrpdvf
       61 gsaetaa
//
LOCUS       WP_285174344             404 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [unclassified Rhizobium].
ACCESSION   WP_285174344
VERSION     WP_285174344.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rhizobium
  ORGANISM  unclassified Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 404)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="unclassified Rhizobium"
                     /db_xref="taxon:2613769"
     Protein         1..404
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43296
     Region          29..403
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(138,140,259,261,291..293,336)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mkrslifaaa laasslpgig aqaqdaavtl twqmwgapnd aelwqqladl vnkqypdikv
       61 klqlsgwtdy wtrlpvlaas gqvadivsmq smrlpnfssi ltplddyvkg sdvkvadfet
      121 simsglsqdg klyalpydvg pwmvfynrdk faaaglkepa kdwtfddfka dakaltkdga
      181 ygygtqafdf iagpvalgad yfnadnefdl tnagfvdafs kyadltakdk lspvfasaad
      241 asaasgrfas gnvamyidgp wslitgqanv nfkigiaplp rgsgssrfit agsgwgisat
      301 sqhkdaafka lqvltspkaa eilgaagral parlaqqtaw ydgaaknvsg trdtlqyifa
      361 httpfrinek wnqfenlvmq yvplaltgds kpdgvlsdiq sqlp
//
LOCUS       WP_285174436             341 aa            linear   BCT 25-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase family protein [Rhizobium sp.
            CNPSo 4062].
ACCESSION   WP_285174436
VERSION     WP_285174436.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..341
                     /product="zinc-dependent alcohol dehydrogenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36235
     Region          5..341
                     /region_name="MDR7"
                     /note="Medium chain dehydrogenases/reductase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cd08276"
                     /db_xref="CDD:176237"
     Site            order(44..46,49,150,154,175..180,198..199,203,218,
                     242..243,245,264..265,289..291)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176237"
ORIGIN      
        1 mtktmkrwtl dkiavgapln ltetaipspa rgevlvrvka vslnyrdklv retgmglpiq
       61 fpfvpasdma gvieavgdgv trfatgdrvi stfhpgwidg kplgdartpp yktlggfypg
      121 vlseyiampe dwfvsapksl dyaeastlpc agltawfalv ergkvkpgds vlvqgtggva
      181 lfglqiaaaq gaevfvtssg reklerakal gahhgidrsk sdwveevyrl tndrgidhii
      241 eiaggpnfgq slkavaphgr isvigvlegf disgpvapll lksptvqgig vghrrsledf
      301 vhavdsiglk pvidhryalg eaaaafdhld rgpfgkivie l
//
LOCUS       WP_285174468             415 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285174468
VERSION     WP_285174468.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..415
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45915
     Region          1..412
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtkdaivlga givgvstaih lqrrgrqvvl vdrqppgqgt sfgnagliqr egvvpygfpq
       61 qfglllryaf nnridahyhl ralpaqiafl arywwnsntk rhemisraya pliehsvseh
      121 ndlieashae elirkngwve lfrsnekrda efaeaerlnr efgigydals naeittmeph
      181 lrgnfsgalr wrdpwsvldp hgltatyrry fesiggrvtt gdavslgmag sawrmvtaeg
      241 sieaedvvva lgpwadivtk rfgyafplgv krgyhmhyaa egnailnnwt ldaergylla
      301 pmsrgirltt gaefalrdap ktpvqldrae avarttfplg erldpepwmg arpctpdmmp
      361 iigkaprhng lwfafghahh gltlgpvtgr vlaelitgek pfidisayap grfap
//
LOCUS       WP_285174507             432 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285174507
VERSION     WP_285174507.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..432
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47567
     Region          1..>66
                     /region_name="PLN00093"
                     /note="geranylgeranyl diphosphate reductase; Provisional"
                     /db_xref="CDD:177713"
     Region          35..399
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtlqetwqsp iapglsfyqa tvgprtsypk ldgsrradva iigggytglq aaynlakgga
       61 evvlidanrf gdgasgrngg qlgtgqrwwp eemeekigye rskalfdlae dakrhlldfs
      121 aehgididfl pgqmnvthkr sykrdymdna eiaatrygyp hmtfmdqaet qerlgsqfyl
      181 ygvrdmgtgh ihplklligl arvaaeagaa lfemtkakgf rqaegktiie tdggeitadr
      241 vliacngyig nlepvtashv mpirsfigat qpldrfpqvl pgneavadsr fvvryfrksk
      301 dgrllfggre aytadnprdi tqhirrqite iypalgdini dyawggsvgi tmprqpfvre
      361 vmpgvtsigg ysghgvmlsn ycgklyaktv lgnadelhlf kelnippfpg garmrapllf
      421 lalswfalrd rf
//
LOCUS       WP_285174611             518 aa            linear   BCT 25-DEC-2024
DEFINITION  formate dehydrogenase beta subunit [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285174611
VERSION     WP_285174611.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11555116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..518
                     /product="formate dehydrogenase beta subunit"
                     /GO_component="GO:0009326 - formate dehydrogenase complex
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=54575
     Region          3..94
                     /region_name="TRX_Fd_FDH_beta"
                     /note="TRX-like [2Fe-2S] Ferredoxin (Fd) family,
                     NAD-dependent formate dehydrogenase (FDH) beta subunit;
                     composed of proteins similar to the beta subunit of
                     NAD-linked FDH of Ralstonia eutropha, a soluble enzyme
                     that catalyzes the irreversible oxidation of...; cd03063"
                     /db_xref="CDD:239361"
     Site            order(4,6,40..42)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239361"
     Region          100..508
                     /region_name="NuoF"
                     /note="NADH:ubiquinone oxidoreductase, NADH-binding 51 kD
                     subunit (chain F) [Energy production and conversion];
                     COG1894"
                     /db_xref="CDD:441498"
ORIGIN      
        1 mtltiyiprd aaalslgaek vaksvaqeia krgldarivr ngsrgmfwle plveveidgk
       61 rigygpvkak dvsalfdagl aeggehplcl gevenlpflk eqtrltfarc gitdplslqd
      121 yeahgglkgl rraidmaagd ivkevtdsgl rgrggagfpt gikwktvlda pgtrkyivcn
      181 adegdsgtfa drmimegdpf vliegmaiag latgatkgfv ytrseyphai aamikaveia
      241 rkagilgasv lgsgkafdme irtgagayvc geetallnsl egkrgivrak pplpahkglf
      301 gcptvinnvi slasvpiimd kgaafyrdfg mgrsrgtipl qiagnvkhgg lyetafglsl
      361 gdivdriggg tatgrpvkav qvggplgayf pralfdtpfd yeafaakdgl ighagivvfd
      421 dtadmlkqar famefcaves cgkctpcrig strgvetadk iaqgiepekn rvlladlcnt
      481 mkfgslcalg gftpypvmsa mthfpedfsp aplieaae
//
LOCUS       WP_285174559              84 aa            linear   BCT 25-DEC-2024
DEFINITION  sensor histidine kinase [Kingella negevensis].
ACCESSION   WP_285174559
VERSION     WP_285174559.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 84)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 84)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 84)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 84)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 84)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..84
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=8941
     Region          <2..83
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 msaeelsdki liciedngng tpeserkrvl npfyrilgsv evgtglglsi aetiakrygg
       61 sialkesvnf etglrveitf pkaa
//
LOCUS       WP_285174628             264 aa            linear   BCT 25-DEC-2024
DEFINITION  FAD binding domain-containing protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285174628
VERSION     WP_285174628.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..264
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=27393
     Region          1..263
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 myatnyhras svdeavklls ntdegkyvsg gmtliatmkq rlaspsdlvd lrhipsikgi
       61 rvdgrrvtig aatthaevas saairavcpa lcdlagmigd phvrhmgtig gsianndpaa
      121 dypsamlaln ativtdrrqi aaddffqglf etalegaelv tsiafdaper agyakfpnpa
      181 sryamtgvfv akgaggvrva vtgagadgvf rhaeleqala anwlpdavtg vtvdpsslls
      241 dlhataeyra nlvkvmakra vaag
//
LOCUS       WP_285174691             259 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Kingella negevensis].
ACCESSION   WP_285174691
VERSION     WP_285174691.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..259
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=29206
     Region          121..232
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
ORIGIN      
        1 mqtktllltl iafslsacnt iaqnsslktq tptpvyeeek peasipyptp shqeeyeqla
       61 mqvakleqkv eqlqtrvhql ekrpvaqqpt kkqskpqtqr taaqptitls dplvnlleta
      121 qqqykkgdyr aatqtlhdad sggdgshtaq qamylllqsh qklnncqsvi nigqryatrf
      181 sdsntaaeal ysvgecqwki qqqdiakdtw rnlqrsypns saakraqtkl tkypkmerrr
      241 ladkskkqpe npqikkvip
//
LOCUS       WP_285174776              95 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: BolA family protein [unclassified Rhizobium].
ACCESSION   WP_285174776
VERSION     WP_285174776.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rhizobium
  ORGANISM  unclassified Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="unclassified Rhizobium"
                     /db_xref="taxon:2613769"
     Protein         1..95
                     /product="BolA family protein"
                     /calculated_mol_wt=10376
     Region          4..95
                     /region_name="BolA"
                     /note="DNA-binding global transcriptional regulator BolA,
                     affects cell shape, cell division and biofilm formation
                     [Transcription, Signal transduction mechanisms]; COG0271"
                     /db_xref="CDD:440041"
ORIGIN      
        1 mettlqsrie rkltdafape rlavineshl haghqpnmtg tgethiriri vsakfsgmpr
       61 larhrainel lkpeldaglh alavepaapg eavrw
//
LOCUS       WP_285174819             267 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: lysophospholipid acyltransferase family protein
            [unclassified Rhizobium].
ACCESSION   WP_285174819
VERSION     WP_285174819.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rhizobium
  ORGANISM  unclassified Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="unclassified Rhizobium"
                     /db_xref="taxon:2613769"
     Protein         1..267
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30352
     Region          27..236
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 miilrsilfn tafyanliir mivlapiyfl mprkaayaip kawaksstwl mekivgttfe
       61 ieglenipkg sfifapkhqs fwdtfallpy lddpvyilkr elmwiplfgw yagkqrmipv
      121 drgargkvmf dvlkrtreel atgrqliiyp egtrrppgae pvykygiarm yrdlgipvva
      181 vamhpglfwp rrtfrkypgh ikvrilppie pgmdpdaffa rlieeteras dellvetvan
      241 npnlplppta vqrlaeiaka kpvtaav
//
LOCUS       WP_285174851             229 aa            linear   BCT 25-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Rhizobium sp. CNPSo
            4062].
ACCESSION   WP_285174851
VERSION     WP_285174851.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..229
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=24676
     Region          12..216
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mlssatnlnr gprdvmqiir derdiergla alleldprlr pvaaeagtlp lrlrepgfeg
       61 lahiivsqvv srasadaiwg kmiagmgqvt akgyvrlepe awrtfglsri khetlhrvae
      121 avaaggldlh alsaespeka laeltsikgi gpwtaevylm fcgghadvfp agdvalqaav
      181 gmafghevrp lakaiareaa vwapwrsvaa rlfwayyavk trrdalpiv
//
LOCUS       WP_285174957             399 aa            linear   BCT 25-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Kingella negevensis].
ACCESSION   WP_285174957
VERSION     WP_285174957.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..399
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=45911
     Region          2..396
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mkltdkqcan agvpekgtkq lsdgggmyle irangckywk mkytspitkr qtilhlgtyp
       61 emnlkaarta hmkarfeien gndpkdqkqa akkkaasnre ntfehiartw htdrskqadk
      121 wsedhaarvl rslelhifpy igslpiaeim pmqvleqlkr ieyagkndta hkvydvvnqv
      181 fsyavrlric lfnptaelrt elaavkqksf phitdpiqig ellrkidgyl glpqtrtllk
      241 ispylftrpv eirtmkwsei dfqaalweks gedmkngldf ivplpkqaie lleslkpftg
      301 hyeyvfynia knqplseaaa skamqrlgys gimtphgfrh mastrlnemn fnkdwieaql
      361 ahkdpnttra tynkaqyldh rrqmlqewad yldtlrhqp
//
LOCUS       WP_285174976             668 aa            linear   BCT 25-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Kingella
            negevensis].
ACCESSION   WP_285174976
VERSION     WP_285174976.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Shan,L., Mathews,I.I. and Khosla,C.
  TITLE     Structural and mechanistic analysis of two prolyl endopeptidases:
            role of interdomain dynamics in catalysis and specificity
  JOURNAL   Proc Natl Acad Sci U S A 102 (10), 3599-3604 (2005)
   PUBMED   15738423
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Polgar,L.
  TITLE     The prolyl oligopeptidase family
  JOURNAL   Cell Mol Life Sci 59 (2), 349-362 (2002)
   PUBMED   11915948
REFERENCE   3  (residues 1 to 668)
  AUTHORS   Polgar,L.
  TITLE     A potential processing enzyme in prokaryotes: oligopeptidase B, a
            new type of serine peptidase
  JOURNAL   Proteins 28 (3), 375-379 (1997)
   PUBMED   9223183
REFERENCE   4  (residues 1 to 668)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 668)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..668
                     /product="prolyl oligopeptidase family serine peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=74482
     Region          2..664
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mqdtyqylen lhspetqkfh qsahaetlvq fcqsknfhkt kqqiteqlqd erqipfcqeh
       61 rarmyhfhqs adlpkgvyrv csaasyragi pdweilfsva dfdeilgddv yldgvshyve
      121 rpelalisls sqgsdsayti efnlktgeiv sggfhfplgk nhvawrdens vwvcpawder
      181 qlttsgyprq vwlmqrgqsf deatpvyemd adgvmvsawr yldaqgapld lieantsffq
      241 kdyfyvnadl aavklslprd cevvgylagq lflhlksdwq rskqkyvsgs liavklnkge
      301 lgeafclfap tssqalelie ttrkfviasl ldnvsgslka wkwengawve qalprfpnga
      361 ieladqpwgg dtvylaasdf vtpltlfald lnvmeltvlr rqpkqfdaqg ivvtqnfats
      421 adgtripyyh vgktqspdtp tlvyvyggfa vpelphymga igrhwlergg afvlanvrgg
      481 gefthwhtaa qrenkhksvd dllsvindlv ehgyssakki aiqggsnggl vvasafcrqp
      541 enlgamicev pltdmlryte lyagaswide ygnpadpkmr eylaafspyh qlsgslnypp
      601 afittslsdd rvhpahalkf yaklrdnpna kawlfapekg ghtgngtqae taeelaavla
      661 flqqmivl
//
LOCUS       WP_285175024             157 aa            linear   BCT 25-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285175024
VERSION     WP_285175024.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..157
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17372
     Region          55..154
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mqeaieitks kgvicrdims eltdwftdpa vieacagave slpmfgcvea ntvagfvslr
       61 ahppaameiv viatrrrhhr sgvgkrllaa aetfarssdc klltvktlap rgrdepqyek
      121 trafydrngf iraeifptlw resdpclffv kpltsin
//
LOCUS       WP_285175089             310 aa            linear   BCT 25-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Rhizobium sp.
            CNPSo 4062].
ACCESSION   WP_285175089
VERSION     WP_285175089.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..310
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34950
     Region          56..296
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mpltlslntn plvnrfaepa dlietvardl rirdlqlthe finpswqapv irrltrdmqa
       61 alkrtgvrvt sgmtgpygrl nhfghpdkdv rryyvdwfkt faditadlgg hsvgtqfaif
      121 tykdyddpvr reelieiaie cwdevaehar aaglsyifwe pmsigrefge tidaclslqd
      181 rltkapfaip mwmmadidhg dvtssnpddy dpyawaravp kvspiihikq slmdkgghrp
      241 ftaefnakgr iqpepllkaf aeggakdnei clelsfkere pndrqviaqi aesiafwaph
      301 idtgagdlhi
//
LOCUS       WP_285175128             308 aa            linear   BCT 25-DEC-2024
DEFINITION  CobW family GTP-binding protein [Kingella negevensis].
ACCESSION   WP_285175128
VERSION     WP_285175128.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..308
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34163
     Region          3..308
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mqtptkihlf tgflgtgktt airsliaqkp shekwllivn efgevgidga vlsnngipvt
       61 eltggclccs agaelgdtmr qvlaefqptr ilieasglah aagvidelkt lefaqkleia
      121 aaftlidprh faddnyfrnp lyydqigvsd vlvaskidlc naeelarfre ratnlfppka
      181 lvvetdnaam qlswldtevv aksryrlktq pentlgfqsq gftfaaecqf dvdkisqffq
      241 qlpnladglv rakgvfqvdg twvwlnwsdg hwgatqvawr rdnrfeliak sfdvdeierc
      301 lrlafqaa
//
LOCUS       WP_285175166             139 aa            linear   BCT 25-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285175166
VERSION     WP_285175166.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..139
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=13720
     Region          6..135
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mshvltssvl sdegvmtlln aaisaatamg qpqcivivdq sgvtlgcfrm rgsrfqslks
       61 atakaqtaas iggashslpe harvplaiat hggmtglrgg lpirvggtlv ggigvgsgsg
      121 eqdeqiaraa lkaigadld
//
LOCUS       WP_285175344             612 aa            linear   BCT 25-DEC-2024
DEFINITION  DUF262 domain-containing protein [Kingella negevensis].
ACCESSION   WP_285175344
VERSION     WP_285175344.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..612
                     /product="DUF262 domain-containing protein"
                     /calculated_mol_wt=72496
     Region          6..515
                     /region_name="GmrSD"
                     /note="DNAse/DNA nickase specific for phosphorothioated or
                     glycosylated phage DNA, GmrSD/DndB/SspE family, contains
                     DUF262 and HNH nuclease domains [Defense mechanisms];
                     COG1479"
                     /db_xref="CDD:441088"
     Region          492..604
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 msqeltlsif qllhqdryii piyqrnyawt dkeispllsd myqafqrqse hyyigslvvy
       61 rrenallevi dgqqrlttft llahqlrnqf sgslnladkp nisfehrqdf aahlhqpnql
      121 pehfqaalka ikqnwlpeys vkfaqfildn vyiirtempp ktdlnhyfei mntrgeqlek
      181 heilkvrlls rlndchatsr tqeafsqiwd acsdmnrymv lgfkpaarka ifgnnyqefq
      241 lnsdsikqaf sakesdvstt ilqlienkfe asqsdgkdeq qetserfhsv idfpnflmhv
      301 lrifveketg dvenaknivl derklletik veewdkkkic qfaktlcqcr ylfdryvikt
      361 dsnkddhwsl ltikpynkss yqfdntfsiq neqnsivmll amfhvslpsl vyknwlyavl
      421 rwlyfraaep tvadyqrfle dlsdryyfgy ygndkkvaff dlitqenfrl pehltypkif
      481 ketgiqipnf ifnrldyllw knekynqykd kfrfafrtsv ehfypqnpde qhqrlsdnvl
      541 hsfgnlcllp sninskftnn lpaakkanfs nmdnpsfklm lmfeladkwn ediikqhene
      601 mlavlnqrfq aa
//
LOCUS       WP_285175467             157 aa            linear   BCT 25-DEC-2024
DEFINITION  methyltransferase family protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285175467
VERSION     WP_285175467.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..157
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=17106
     Region          66..157
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mavesdsagv rfpppfiylg alllglaaer fvtlrsvgid wrlliatgap lfvagaavml
       61 aaagvfrrlg tnvrpsqptt liatngpyrw trnpmylgma liyaglaigf dapialallp
      121 lvliaiqtqv iareerylea kfgddyrryk aevrrwl
//
LOCUS       WP_285175430             308 aa            linear   BCT 25-DEC-2024
DEFINITION  carbohydrate kinase family protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285175430
VERSION     WP_285175430.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..308
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32370
     Region          1..265
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(34,246,249)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(186,217,244,247..248,251)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 milccgeali dmlprdttlg ekgfapyagg aifntaialg rlgiptgfft giaddmmgei
       61 lrdtlsaskv dfsycaitpr pstiafvklv ngqatyafyd egtagrmite adlpalgddc
      121 ealhfgaisl ipdpcgatye almkrehqsr visldpnirp gfikdqaahm grisrmaams
      181 dilkfsdedl ewfgiagnhd elaahwlnqg aklvvvtkga egatgytksl kvsvpservt
      241 vvdtvgagdt fdagilaslk mnnlltkaqv aslnekalqd alalgakaaa vtvsraganp
      301 pwaseigl
//
LOCUS       WP_285175507             113 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285175507
VERSION     WP_285175507.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 113)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 113)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 113)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..113
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12504
     Region          2..86
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdtlsatlsa ladptrrail arlasgeasv selaepfdms lvavskhlkv lekagliskg
       61 reaqwrpcrl epkplrqvdd wlenyrqfwn dnldrleaya allqkggknd psn
//
LOCUS       WP_285175525             150 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: SRPBCC family protein [unclassified Rhizobium].
ACCESSION   WP_285175525
VERSION     WP_285175525.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rhizobium
  ORGANISM  unclassified Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10141965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="unclassified Rhizobium"
                     /db_xref="taxon:2613769"
     Protein         1..150
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=15510
     Region          1..145
                     /region_name="CoxG"
                     /note="Carbon monoxide dehydrogenase subunit G (CoxG);
                     cd05018"
                     /db_xref="CDD:176853"
     Site            order(3,5,7,16..18,20..21,26,30,36,42,44,46,48,50,55,59,
                     63..65,68,74,76,78,90..92,94,96,105,107,109,111,125..129,
                     131..133,135..137,140)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176853"
ORIGIN      
        1 mdmtgeeria aprdavwaal ndpeilkqci pgcqslekvs pteltatvkl kigpvsasfn
       61 gevklsnina pesytisgeg kggiagfakg gadvilkedg netilqyeak aqvggkiaql
      121 gsrlvdssak klaqqffadf taaingqana
//
LOCUS       WP_285175562             324 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285175562
VERSION     WP_285175562.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..324
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34564
     Region          6..323
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mrflkigill afglaassar aagltsiqvp atadnpalsa fvwspcatpp eevklgpmtv
       61 vavrncpiaa rklplivish ghgggslnhh dvaetladag flvvalnhpg dnfsdlsrsg
      121 disimfqrpr dikrlidfll agwpqaekid pdrigffgfs rggytglvla gavpdfhdat
      181 vpcpepapic geirrneipa eplardlrik afvladplsf fstkeslkav dapiqlwgse
      241 hggdgvlpen vaslavnlpd kpdfhvvpgs ahfaflapcs pglarsqpem ctdqaafdrt
      301 afhrsldani leffrqnlap erks
//
LOCUS       WP_285175588             472 aa            linear   BCT 25-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285175588
VERSION     WP_285175588.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 472)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..472
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=52057
     Region          5..468
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mdweqfrqws ekaanwgady raslrdrpvr akaapgeiaa hiadsppesg etmedifkdf
       61 enilvpgmth wqhprffayf panaapvsvv aeylvsaiaa qcmlwqtsps ateletkvvd
      121 wlrqalglpe tftgviqdsa statlaavlv mreraldwqg nksglaanka vriystdqvh
      181 tsidraiwis gvgdenlvri psggpnkamd pkaladaier draagllpag viacvggtsv
      241 gacddiaavv evahahglyv hvdaawagsa micpefrtlw qgveradsvv fnphkwlgaq
      301 fdcsvqfvre petlvrtlai qpeylrthgh dgiinysews vplgrrfral klwfllryhg
      361 leglrtmirn hvawsqnlak rlaaepdfei vtepflslfs fdhkapegvd qeshtqrlln
      421 ainndgriyl tqtrvsgrlv irfqagqfea taddidtafd viveiarsls sa
//
LOCUS       WP_285175608             259 aa            linear   BCT 25-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Kingella negevensis].
ACCESSION   WP_285175608
VERSION     WP_285175608.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..259
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=29188
     Region          121..232
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
ORIGIN      
        1 mqtktllptl iafslsacnt iapnsslktq tptpvyeeek peapipyptp shqeeyeqla
       61 mqvakleqkv eqlqtrvrql ekrpvaqqpt kkqskpqtqr taaqptitls dplvnlleta
      121 qqqykkgdyr aatqtlhdad sggdgshtaq qamylllqsh qklnncqsvi nigqryatrf
      181 sdsntaaeal ysvgecqwki qqqdiakdtw rnlqrsypns saakraqtkl tkypkmerrr
      241 ladkskkqpe npqikkvip
//
LOCUS       WP_285175644             290 aa            linear   BCT 25-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Kingella negevensis].
ACCESSION   WP_285175644
VERSION     WP_285175644.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Dwyer,M.A. and Hellinga,H.W.
  TITLE     Periplasmic binding proteins: a versatile superfamily for protein
            engineering
  JOURNAL   Curr Opin Struct Biol 14 (4), 495-504 (2004)
   PUBMED   15313245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..290
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=31244
     Region          67..290
                     /region_name="HisJ"
                     /note="ABC-type amino acid transport/signal transduction
                     system, periplasmic component/domain [Amino acid transport
                     and metabolism, Signal transduction mechanisms]; COG0834"
                     /db_xref="CDD:440596"
ORIGIN      
        1 mktfkklllv samstvlaac ggseqassss taqpaqaeaq kasapannvp vaadnyvspl
       61 panaptvnva tvgktlpfsf sdnagqligm dvdvirkige eagfkvqfhk kpwvnmlgsv
      121 etgesdlais gisytderek kyaisnsyaf npsslmfire dlngkvkdln slegltvgvl
      181 geskqdsqit aankaksivr ynstyllftg mlkkevdvia qdslllnqla ktnteyktfs
      241 vnyenesdps ahlvilvnkd kaqlrddink alakikedgt lakieekwlk
//
LOCUS       WP_285175663             103 aa            linear   BCT 25-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Kingella negevensis].
ACCESSION   WP_285175663
VERSION     WP_285175663.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 103)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 103)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 103)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..103
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11494
     Region          11..95
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlktapilqp tptlnetaql fkalsnpqrl ailldlnddv rslkelvest gqpptqlath
       61 leklrqmgiv dhtrfmrilq yriisptvls vlktlqpenk iva
//
LOCUS       WP_285175711             347 aa            linear   BCT 25-DEC-2024
DEFINITION  acyltransferase family protein [Kingella negevensis].
ACCESSION   WP_285175711
VERSION     WP_285175711.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..347
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=39921
     Region          11..347
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mctkiftqpe kpnrslqldg lrgvlacavi thhfcynfnw reggkwgatd vliqnlgavs
       61 vclfflmsay lhigkiqhsp kikwrdffia rikriyplyi avfllvaavt lsykpltaqn
      121 lpeflrfilq wllfqnvsfq gfqahlaiag vqwtlvyewa vytilplvhm iyqrnfsfqa
      181 aawvaigvva wiigwhsqtr yywlfvlaip aailaqpirf vmqkqplvvh almialtvca
      241 faytqpyswa qrlvlmvwfg fvangysfan vlnyrgltkl gdlsyaiyll hglvifmwfg
      301 awkmfvfkqg nflgyvlhlp lifsvaigaa ylgnryvemp fsrkrkk
//
LOCUS       WP_285175851             150 aa            linear   BCT 25-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Rhizobium sp.
            CNPSo 4062].
ACCESSION   WP_285175851
VERSION     WP_285175851.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..150
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16522
     Region          4..108
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mvarkslkgd ycpsarsldv igdwwslliv rdafdgltrf gefqkslgia knilterlrt
       61 lvasgilelv ptseggtrme yrltamgkdl fpvmvalrqf gerhlfapae ehsvlvdrat
      121 gqpvqleira qdgrsigpde avivkvpeek
//
LOCUS       WP_285175948             534 aa            linear   BCT 25-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Kingella negevensis].
ACCESSION   WP_285175948
VERSION     WP_285175948.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..534
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=58556
     Region          7..530
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mslnspvlvi ddetdirdlm emtlmkmglh vdtaagvkea iskldtkrys lvltdmrmpd
       61 gfglevvehi tkknldvpva vitafgnadq avqalkvgaf dylqkpitls qlrtlvksai
      121 kvqdenvdik pviqakaapk apaktqpete istfdfdvpd lpaaapapaa pkrtapvqaa
      181 kpialaaeap vlpvtmpnep llkteadlpr llgsspqiet vrglirklap anvpvyisge
      241 sgsgkeqaar sihelsprrd kpfiavncga ipenlmesef fgykkgsftg adqdrlgffq
      301 hahggtlfld evadlplamq vkllraiqek avrrigdaqe vkvdvrivsa thknlaalve
      361 sgafrqdlfy rlnvvtlnmp alremhedla nliqhllrkh hsgeismtsa areallryny
      421 pgnfreleni leravalssg nmidvddlqi niaplnaeaa dipegsnqhq vinglpnfhm
      481 gstqiqdyld diekqileya lrltqgnrtq aakvlgisfr smryrlerln idve
//
LOCUS       WP_285176020             438 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [unclassified Rhizobium].
ACCESSION   WP_285176020
VERSION     WP_285176020.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rhizobium
  ORGANISM  unclassified Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 438)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="unclassified Rhizobium"
                     /db_xref="taxon:2613769"
     Protein         1..438
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47801
     Region          24..425
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(135,137,263,265,300..302,352)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mklktlllga csalmfagla saetltiatv nngdmvrmqk ltddfkaknp gidlqwvtle
       61 envlrqkvtt diatkagqyd vltigtyevp iwsklgwlas ldklsadkny dvddllpair
      121 sglttdgkly aapfygessm vmyrkdlfek aglkmpdapt wdfvadaark itdkdhevyg
      181 iclrgkagwg enmafltams nsfgarwfde kwkaqfdqpe wkdtldfyvk lmkdagppga
      241 ssngfnenla lfqsgkcgmw idatvaasfv sdpkeskvad kvgfalapdk glgkrgnwlw
      301 awnlaipass kkteaaekfi swatskdytn lvaqkegwln appgtrtsly anadyqkaap
      361 fakmtldsin sadpthptvk pvpyvgvqfv aipefqgigt avgqqfsaal agqisvdqal
      421 kaaqqltere mkkagypk
//
LOCUS       WP_285176047             438 aa            linear   BCT 25-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Rhizobium sp. CNPSo
            4062].
ACCESSION   WP_285176047
VERSION     WP_285176047.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 438)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..438
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47737
     Region          52..428
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(141,144,278,280,315..317,358)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrnwraglaa gtmallagta vfaadlpgkf pgvtidakli ggqqyeplya riseweketg
       61 akvnilskkn hfeldkeiks dmasgsiswc vgsnhssfap qypdlytdls kllpkeeiaq
      121 fvdstiqast idgrlimlpr aqfdvsalyy qkslykdeak ktafkakygy dlappktwke
      181 vsdqavffsn ppnffgtqfp gkeeaingrf yemlvaegge ylgkdgkpaf nseagvrald
      241 wfvnmykaka vpagttnylw ddlgagfasg sialdldwpg watyfndpks skiagnvgvv
      301 vqpvgssgkh tgwsghhgfs vtescahkda aaslvwfltn ddsqkleaan gtlptrkavw
      361 ewdiqqaasd pykkevlstf qeamkyafpv prtpqwieis nvvypelqaa ilgdksskea
      421 ldaaaqkatd vlkdagal
//
LOCUS       WP_285176132             393 aa            linear   BCT 25-DEC-2024
DEFINITION  ATP-binding protein [Mycobacterium tuberculosis].
ACCESSION   WP_285176132
VERSION     WP_285176132.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..393
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=42741
     Region          30..>376
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mpsratvqef sdsypfchng frpimmpkiv svqhstrrhl tsfvgrkael ndvrrllsdk
       61 rlvtltgpdg mgksrlalqi gaqiahefty grwdcdlatv tdrdcvsism lnalglpvqp
      121 glsaidtlvg vindarvllv ldhcehllda caaiidsllr scprltiltt steaiglage
      181 ltwrvpplsl tnnaielfvd rarrvrsdfa inadtavtvg eicrrldgvp laielaaart
      241 dtlspveila glndrfrlva gaagnavrpe qtlcatvqws hallsgpera llhrlavfag
      301 gfdldgaqav gandedfegy qtlgrfaelv dkafvvvenn rgragyrlly svrqyalekl
      361 sesgeadavl aryrkhlkqp nqvvragsgg vry
//
LOCUS       WP_285176107             216 aa            linear   BCT 25-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Mycobacterium tuberculosis].
ACCESSION   WP_285176107
VERSION     WP_285176107.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 216)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13031065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..216
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23096
     Region          67..205
                     /region_name="SpoU-like"
                     /note="SAM-dependent rRNA or tRNA methylase related to
                     SpoU; cd18096"
                     /db_xref="CDD:349969"
     Site            order(140,142,162..165,168,182..183,185,191..192,194,197)
                     /site_type="other"
                     /note="putative SAM binding site [chemical binding]"
                     /db_xref="CDD:349969"
ORIGIN      
        1 msalgpgpte wgaptggvgp wagdlpddpr ydpvllrdgd arnvvdayry wtreaiiadi
       61 dtrrhplhva ienfghdani gsvvrtanaf avhtvhivgr rrwnrrgamv tdryqrlchh
      121 dsttgllefa agagltvvav dnvpgaarle qtalprecll lfgregpgit ddaragaavt
      181 vsiaqfgstr sinagvaagi amhawirqha dlgraw
//
LOCUS       WP_285176133             472 aa            linear   BCT 25-DEC-2024
DEFINITION  WS/DGAT/MGAT family O-acyltransferase [Mycobacterium tuberculosis].
ACCESSION   WP_285176133
VERSION     WP_285176133.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Stoveken,T., Kalscheuer,R., Malkus,U., Reichelt,R. and
            Steinbuchel,A.
  TITLE     The wax ester synthase/acyl coenzyme A:diacylglycerol
            acyltransferase from Acinetobacter sp. strain ADP1:
            characterization of a novel type of acyltransferase
  JOURNAL   J Bacteriol 187 (4), 1369-1376 (2005)
   PUBMED   15687201
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Kalscheuer,R. and Steinbuchel,A.
  TITLE     A novel bifunctional wax ester synthase/acyl-CoA:diacylglycerol
            acyltransferase mediates wax ester and triacylglycerol biosynthesis
            in Acinetobacter calcoaceticus ADP1
  JOURNAL   J Biol Chem 278 (10), 8075-8082 (2003)
   PUBMED   12502715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496208
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..472
                     /product="WS/DGAT/MGAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0045017 - glycerolipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=50086
     Region          5..457
                     /region_name="acyl_WS_DGAT"
                     /note="acyltransferase, WS/DGAT/MGAT; TIGR02946"
                     /db_xref="CDD:274360"
ORIGIN      
        1 mdlpmaaada lflwaetptr plhvgalavl sqpdngtgry lrkvfsaava rqqvapwwrr
       61 rphrsltslg qwswrtetev dldyhvrlsa lppragtael walvselhag mldrsrplwq
      121 vdlieglpgg rcavyvkvhh aladgvsvmr llqrivtadp hqrqmptlwe vpaqasvakh
      181 taprgssrpl tlakgvlgqa rgvpgmvrvv adttwraaqc rsgpltlaap htplnepiag
      241 arsvaerlrq vaehadatin dvvlamcgga lraylisrga lpgapliamv pvslrdtavi
      301 dvfgqgpgnk igtlmcslat hlaspverls airasmrdgk aaiagrsrnq alamsalgaa
      361 plalamalgr vpaplrppnv tisnvpgpqg alywngarld alyllsapvd gaalnitcsg
      421 tneqitfglt gcrravpals iltdqlahel ellvgvseag pgtrlrriag rr
//
LOCUS       WP_285176157             333 aa            linear   BCT 25-DEC-2024
DEFINITION  MULTISPECIES: 2-hydroxyacid dehydrogenase [unclassified Rhizobium].
ACCESSION   WP_285176157
VERSION     WP_285176157.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rhizobium
  ORGANISM  unclassified Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="unclassified Rhizobium"
                     /db_xref="taxon:2613769"
     Protein         1..333
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=36749
     Region          7..322
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(13..14,16,56..58,79,107..108,111..112,114..115,118,
                     122,124,132,136,138,140..146,148..152,170..171,174..175,
                     275..276,283,292..298,300..303,305)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(57,80..82,105,246,296,299)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240626"
     Site            order(81..82,109,160..164,182..184,187,216..218,222..223,
                     244..246,270..271,296,298..299)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 mttkkkpkvy vtrklpdave trmrelfdae lniddrprtk delmeavrsv dvlvptvtdr
       61 idaevieeag pqmkliasfs ngtdhidvea aarrgitvtn tpnvltedta dmtmalilaa
      121 prrlaegarv ltdnpgewag wsptwmlgrr ihgkrigivg mgrigtavar rakafglsih
      181 yhnrkrvnpa tedeleatyw dsldqmlarv divsvncpst patyhlisar rlallqptsy
      241 ivntargdvi detalikilr egkiagagld vfenepavnp klvklanegk vvilphmssa
      301 tlegridmgd kviinirtfi dghrppnrvl pfr
//
LOCUS       WP_285176220             259 aa            linear   BCT 25-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Mycobacterium
            tuberculosis].
ACCESSION   WP_285176220
VERSION     WP_285176220.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..259
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28297
     Region          4..209
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mepvygtvir larlswriqg lkitvtgvdn lptsggavva inhtsyldft faglpayqqg
       61 lgrkvrfmak qevfdhkitg pimrslrhip vdrqdgsasy daavrmlkag elvgvypeat
      121 isrsfeikef ktgaarmaie agvpivphiv wgaqriwtkd rpkklfrpkv pvtivvgeri
      181 eptlptaeln gllhsrmqhl leraqelyga hpagefwvph rlgggapsla eaarldaqea
      241 avraarraqr ahpagapeq
//
LOCUS       WP_285176306             246 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Rhizobium sp. CNPSo
            4062].
ACCESSION   WP_285176306
VERSION     WP_285176306.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12044921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..246
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28075
     Region          21..165
                     /region_name="Autoind_bind"
                     /note="Autoinducer binding domain; pfam03472"
                     /db_xref="CDD:427319"
     Region          <185..246
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mnihsliqll vvieecklak dvvaelelvl rsykfdfygv lkqtrpnvdv anfilagrwp
       61 dqwpltyvrk rymlvdpvar yasraqrpfr wsdavaaqks dplrrrmeqm madarangla
      121 dgylfpihgr ngllgsmtig geavdlspte isvfdavark vfwrllefrd eapyferaga
      181 adlkltkrem evlnhladgm tsieisrllv isnhtvdwym nsiqeklkar nrqhivaiaf
      241 rnglip
//
LOCUS       WP_285176497             137 aa            linear   BCT 25-DEC-2024
DEFINITION  MerR family transcriptional regulator [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285176497
VERSION     WP_285176497.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140991
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..137
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15618
     Region          2..127
                     /region_name="HTH_CadR-PbrR-like"
                     /note="Helix-Turn-Helix DNA binding domain of the CadR-
                     and PbrR-like transcription regulators; cd04785"
                     /db_xref="CDD:133412"
     Site            order(3..5,19,36..38)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133412"
     Site            order(50,53,57..58,67,78..79,82,85,89,95,99,102..103,110,
                     115..116,121,123)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133412"
     Site            order(78,113,121)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:133412"
ORIGIN      
        1 mltigdlsrr tgvkvptiry yeqmglisep ersegnqrry skadlerlaf irhgrdlglt
       61 idaikelisl sqhpdrpcvg adriakehld dvrtkiarlk kleheleriv shcdghsied
      121 cyviralsdh glceheh
//
LOCUS       WP_285176516             457 aa            linear   BCT 25-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Rhizobium sp.
            CNPSo 4062].
ACCESSION   WP_285176516
VERSION     WP_285176516.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..457
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=49726
     Region          18..416
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msaftaaepa aaatqnvsly raiwrwhffa gllvipfmln laitgslylf kdqiadtfys
       61 hrylvaetgp mlqpqqiada alaafpgtra tsyheasapn rsasitvskg gqstivyvnp
      121 ydgsilgsvg sqqefgwvvk rihsleyfgk wtnriieiva gfalvlvvtg iylwwprqqs
      181 ggvltvrgnp srrvfwrdlh avtgalagil ifflafsgmp wsgywganvn awltannlgt
      241 paavwdevpk sakvtqdivs ragwvvenap vplsdiaaaq sakpigldka vdimhglgmv
      301 agsdlaipsd etgvytashy fgdlgkertv hidqysgkpl idisfdqypa lgkaiewgin
      361 vhqgqewglf nqllmlatcl aivlccgtaa tmwwkrrpsg rlgvppmpsr ksvyvglwli
      421 aivfgvafpl tgaaivamll ldqfvvrfvp plrrffs
//
LOCUS       WP_285176536             291 aa            linear   BCT 25-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285176536
VERSION     WP_285176536.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Niehaus,T.D., Elbadawi-Sidhu,M., de Crecy-Lagard,V., Fiehn,O. and
            Hanson,A.D.
  TITLE     Discovery of a widespread prokaryotic 5-oxoprolinase that was
            hiding in plain sight
  JOURNAL   J Biol Chem 292 (39), 16360-16367 (2017)
   PUBMED   28830929
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Fan,C., Li,Z., Yin,H. and Xiang,S.
  TITLE     Structure and function of allophanate hydrolase
  JOURNAL   J Biol Chem 288 (29), 21422-21432 (2013)
   PUBMED   23754281
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Wang,L., Grau,R., Perego,M. and Hoch,J.A.
  TITLE     A novel histidine kinase inhibitor regulating development in
            Bacillus subtilis
  JOURNAL   Genes Dev 11 (19), 2569-2579 (1997)
   PUBMED   9334321
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005226
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..291
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=32816
     Region          1..254
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 mptrftfggd ehlfvecsde msleaffksl smakgvresa ingvteicpa nasfqikfdp
       61 diikpddllr evkaiegaae kaepvittri veipvfyndp wthetlmrfr erhqeptgtd
      121 ldyaaringy davkdfisah agspwfvsmv gfvaglpfmy qmverrrqie vpkylrprtd
      181 tprltvghgg cfgciysvrg aggyqmfgit pmpifdptqs tsylrdfmvf frpgdivkfr
      241 pidrdgydqa vedvdkgrfa ppirevsfdl rqyqadidgy naklegalhg h
//
LOCUS       WP_285176565             243 aa            linear   BCT 25-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Rhizobium sp. CNPSo
            4062].
ACCESSION   WP_285176565
VERSION     WP_285176565.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12044921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..243
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27101
     Region          19..165
                     /region_name="Autoind_bind"
                     /note="Autoinducer binding domain; pfam03472"
                     /db_xref="CDD:427319"
     Region          <177..241
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mltgsrqshc lseiaqandi delrqflfkf cslyglanaa fhvtqiaalp qqnpllllty
       61 ppewvdtyia hdyfsidpvv qagrngflpf dwstldlksp qsisffreae afdvgryglt
      121 lvvrgphger slftvtsnlk sgdwehlrns iigdlqviay ylheqslivs glreqsigrr
      181 lskretecle llahgllpkq itsilgises avrlylssgr rklhvsttnq aiakaislel
      241 iks
//
LOCUS       WP_285176597            1008 aa            linear   BCT 25-DEC-2024
DEFINITION  alpha-mannosidase [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285176597
VERSION     WP_285176597.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..1008
                     /product="alpha-mannosidase"
                     /calculated_mol_wt=112218
     Region          240..1007
                     /region_name="MngB"
                     /note="Alpha-mannosidase [Carbohydrate transport and
                     metabolism]; COG0383"
                     /db_xref="CDD:440152"
ORIGIN      
        1 msltiaqrld rlkvrttela hwrdrqslai dgwtfdgepi ahhqdwphrn gtvrfaakat
       61 apqdwpleqi rlqldlgges lltlrypdge tetfgldpyh qefptkgrdf qiatesvarf
      121 pfgepnrapk lnrarliwld epvhrlhlll qqigeaadil dgheavphli daaeralrsl
      181 dwpsdtsayi srtasaamqq kiwelpelqd spaglseaqs asaaaaydel laqlkelqkr
      241 fpqngelllt ghahidlawl wpygetrrkm rrtfntalsl mersddfrfn qstaqyyaqi
      301 eeddpeller ikkkvaegkw etvggmwvep dtnmptgesl arqvlygqry fekhfglrhs
      361 vcwlpdcfgf sgalpqilql ggidsfftik vnwsesnhip sdlfwwkgld gskvlthtfd
      421 npmqgyngfv qpdcfvptwk nfrgktqhdt sllavgygdg gggvtpemve revqlrdfpa
      481 ipkarwgtvk gfyekahrta aqkelpvwdg eiylelhrat ltsqsgvkrk hrqaeralit
      541 aetlaslahm lgadkpqsle adwrvvlkne fhdilpgssi revyadaere ldgvignara
      601 eqasalktlw ahlpagavvd alvivnpsls prpltatlsd gtvlasadsv aplsvavfdr
      661 kslkpagglk adthhleneh lsvvigkdga vsslvhkatg reaiegsanq lwvypadkpr
      721 nwdawdvdad yaekgihldq pesitlveeg phraairvin ryrnstvtql yvltanarrl
      781 diettidwhd rrtllrtlnp vavrsrtatf ecafgiverq thtntsweqa mfeaaahrfv
      841 dlsepgfgva llnnakyghs argnvigmsl vrspiypdpl adegeqsfty almphedawy
      901 dggvlseaid lnqplvsmea sglaagtlsp lgvegtpvaf sglkpaeege glilrlyepa
      961 grrgrlsltl psgwqvsgpl nileepiers gpadimpfei rtwklhra
//
LOCUS       WP_285176604             472 aa            linear   BCT 25-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Rhizobium sp. CNPSo
            4062].
ACCESSION   WP_285176604
VERSION     WP_285176604.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..472
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=50924
     Region          1..435
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mkiavigtgy vglvsgtcfa ewgnrvvcvd knadkiaalr qgrmpiyepd ldelvernya
       61 agrldfscdi akavegaaiv fialaalpqp gqadadlsfi yhaarelaal isadsivvir
      121 stvpvgtgda vhriigsart pgtfavasnp eflregvavr dflapdrivl gveeewackr
      181 lvelydvpie rqntpviitm rrtaelikha anaflatkit fineladlce emgsdvgela
      241 lgmgldkrig asllaagpgy ggscfpksal allqaaqdhg valriveetl avnemrkrrm
      301 arkvtkalgg didgrtiavl gltfrpdtdd mrdapsvpli etlqrlgari raydpagien
      361 aakvlnsvdf cedpyecarn adavvvmtew dairkidlaq lkqnlrqpvl idlrnaldte
      421 aarrigfhvc aigksasths slrdiakrrn rqravkaatp klvpihdtge ti
//
LOCUS       WP_285176654             265 aa            linear   BCT 25-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285176654
VERSION     WP_285176654.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..265
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29525
     Region          14..215
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mplplhaarh gslriaahrg fsrrfpenti lafqegvnag aneceidlml trddqivvih
       61 drtldrttsg fgfvadhdlq hilsldagak fdprfagthv ptladtllwa kqtdtrlaie
      121 mkepersnrl idlmigtlre ldafeyvais sfdhldllrv keleprlqte ailhhrpvdi
      181 vasmrvggid gvslelnrfh rtdaealqqa giavrlslpl peklamfwqg grdllpmirs
      241 cvkdrlvdal igddvdflrm lgtsa
//
LOCUS       WP_285176659             194 aa            linear   BCT 25-DEC-2024
DEFINITION  IMPACT family protein [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285176659
VERSION     WP_285176659.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Park,F., Gajiwala,K., Eroshkina,G., Furlong,E., He,D.,
            Batiyenko,Y., Romero,R., Christopher,J., Badger,J., Hendle,J.,
            Lin,J., Peat,T. and Buchanan,S.
  TITLE     Crystal structure of YIGZ, a conserved hypothetical protein from
            Escherichia coli k12 with a novel fold
  JOURNAL   Proteins 55 (3), 775-777 (2004)
   PUBMED   15103642
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Okamura,K., Hagiwara-Takeuchi,Y., Li,T., Vu,T.H., Hirai,M.,
            Hattori,M., Sakaki,Y., Hoffman,A.R. and Ito,T.
  TITLE     Comparative genome analysis of the mouse imprinted gene impact and
            its nonimprinted human homolog IMPACT: toward the structural basis
            for species-specific imprinting
  JOURNAL   Genome Res 10 (12), 1878-1889 (2000)
   PUBMED   11116084
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..194
                     /product="IMPACT family protein"
                     /calculated_mol_wt=20385
     Region          1..192
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 mfelvasata nqeikrsrfv ataapiadte aakafvaqhs vadanhncwa wrigqnyrfs
       61 ddgepsgtag kpilqaidgf eldmvavvvt rwfggtllga gglirayggt aalclqgaek
      121 retlptvtat ievqfshlal vkakllaeag vqlveerfte sgavlslaia aslveqvvdn
      181 irdltsgrat akld
//
LOCUS       WP_285176731             953 aa            linear   BCT 25-DEC-2024
DEFINITION  M16 family metallopeptidase [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285176731
VERSION     WP_285176731.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 953)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..953
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..953
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=102647
     Region          40..481
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          529..951
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 msrqnppgrl slklfvattl allvtvaapa haetpvaswp qatsdlpveq girfgtlpng
       61 mryavmhnat pagqvairfr igagslqerd dqqglahfle hmafkgsahv pegemirtlq
      121 rlglafgadt nastsygetv yaldlpeanp etvstglmlm retaseltld agafdrergv
      181 ilseeklrdt pqyrggtgfl aqllpgqrvp erppigktdi isnapvdllr dfyrtyyrpd
      241 rttlivvgdi daaaieadir nrfgnwaaaa papadpdlgt lqnhgervgt vivpggatrv
      301 qlawtrpyda spdrtakrra qlvediglav lnrrlsvlaq qpnppfvsaq agaqdllksa
      361 hvamvaadsd pakwqgalaa idqeqrriaq fgadqseidr eiaeyrstlq aaasgaatra
      421 spdiasslnw svgenmvfts paddlalfda amkdlhagev nnalqhvfag ngpqlvlqip
      481 qmpeggdsav ekayadsrvv avkaleqtas vawpytdfgk pgdiverrtv ddlgvtmvrf
      541 angvrltvkp tkyradevlv raevghgrla lpndrplpiw aapalplsgv kaisyddiqk
      601 afaakvvsid faiqdaafky egttqprdlq tqlqlltayv sdpayrpdvf krvqqaylnm
      661 lpqlqatpgs vvgrdlsgll hsgdprwsfp drtqlldakp edfegllqpa lskgpvevii
      721 agdvgvddai rltaqtfgal pvrgdgekqg dgsgvhfpap ttdpvvrlhd grsdsagaav
      781 ampigdflsd lpraaaanva gailqnrlvd qfriaegaty spqgevdlsr sipgygfayl
      841 yvettpakvd hffelvdkia adlghgdvsp deltrakvpi ieavkrsqqt ngywvqnlrd
      901 aqadprrldr irrsisgyea vtaedvraia ttylkpntsw rlkilpangs avr
//
LOCUS       WP_285176810             329 aa            linear   BCT 25-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Rhizobium sp.
            CNPSo 4062].
ACCESSION   WP_285176810
VERSION     WP_285176810.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..329
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=36268
     Region          3..320
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mgralvtggc gfvgrhlvrr llaegldvvc vdslvagtga lhpelwqrlq rsrftfceed
       61 crtffarppe hfdyvfhlaa lvggrltlet raldvaedla vdaelwqwas rakpgsviff
      121 sssaaypvsl qtianhrlls edminfdaav gvpdlsygwa kltgeylmkl yverygrrai
      181 ayrpfsgyge dqdlaypfpa icrrllaekg apevfvwgsg hqcrdfihis dcidfiwqtk
      241 ellpdgasln lstgtatsfi alaeaisrqi gwqpavtgrs nhpegvfyrc gdtalqrsyg
      301 ltpsvgleeg iartlaylqa erasyalam
//
LOCUS       WP_285176949             718 aa            linear   BCT 25-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Klebsiella aerogenes].
ACCESSION   WP_285176949
VERSION     WP_285176949.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella aerogenes
  ORGANISM  Klebsiella aerogenes
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 718)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 718)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 718)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Klebsiella aerogenes"
                     /db_xref="taxon:548"
     Protein         1..718
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=79354
     Region          109..718
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 miplpgwrni psakilsilv flaglglvvs vislfylsqh lvsiktneid khrsmlsveg
       61 avqtsvnrvl slvldnsiwd davkqtytph ldahwlydsw gsgfkinnly dgtfildeny
      121 rilwgafrse pftesdigff gsglqtlieq hadalrrgkn afagitrtra giafvgigli
      181 rptigrlpiy dktrrylvit rhinptmlet lgntfqinrl httqfageys vplrteggkt
      241 laylswqprl pgaeaaraas nsirliaila aslillfiml sslglyklar geqqarknal
      301 idwlsllpnr ralierlnam gkcgknemqs vvfidldgfk dvndnyghdt gdaliahiar
      361 elrdrvpaga mlarmggdef amtmsgehav nqasafalav lellktpval sarkiyisas
      421 igiasgvptq csstelfrra dmamyhakks gkgraawydd tlnetrqhql hiengiregl
      481 ekgefdvwyq pivnaetlvm egveallrwp rrpegplapd afipiaessg liyalgqfal
      541 sqacydlqtm gdlllsvnis paqfrdpefe trviqtlgrc qfparrlqle vtesyvlenp
      601 erarvaienl kslgiavald dfgigyssig ylrscrfdsl kidkslagvv dvdpqaaelv
      661 rgtvrianal gitvvaegve tqqqlallrr agcdrlqgyy fsqpmpidsl lqlrqqqg
//
LOCUS       WP_285176965             341 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285176965
VERSION     WP_285176965.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Rhizobium sp. CNPSo 4062"
                     /db_xref="taxon:3021410"
     Protein         1..341
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=39028
     Region          169..288
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mlspfeqvyr krdydfvayn darfqysghw qerpdqtlnl gfgrgssihw ngpgrdvlfl
       61 vmrhpwsgti svdedpsrte nlcslctytd ailansltiv gkpvisqgee liiygafvpr
      121 talndsqset ssfdeerfrs vqtdqvdrwi rniietgqdi eeitlkrrda ylmrwretep
      181 yvnrgakvld igcgnflpgm leyfekadft ytgldiderv idgnigktqg rlnfnflras
      241 neklpcldde fdfvfsshsl ehssdlessf neimrvlkpg gwlffavpld vdnapehlwi
      301 ispeiwkrlp svagfslrnv higdiypeig ydmvvvaqkp k
//
LOCUS       WP_285176970             347 aa            linear   BCT 25-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Rhizobium sp. CNPSo 4062].
ACCESSION   WP_285176970
VERSION     WP_285176970.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 4062
  ORGANISM  Rhizobium sp. CNPSo 4062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
           